data_9JLW
# 
_entry.id   9JLW 
# 
_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   9JLW         pdb_00009jlw 10.2210/pdb9jlw/pdb 
WWPDB D_1300051236 ?            ?                   
# 
_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                        9JLW 
_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' 57252.250 2   ? E256Q/D352N ? ? 
2 branched    syn 
;alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
;
1153.001  1   ? ?           ? ? 
3 branched    syn 
;alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose
;
990.860   1   ? ?           ? ? 
4 non-polymer syn GLYCEROL 92.094    2   ? ?           ? ? 
5 water       nat water 18.015    345 ? ?           ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLNGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLNGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 GLYCEROL GOL 
5 water    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   LEU n 
1 5   PHE n 
1 6   LEU n 
1 7   VAL n 
1 8   PHE n 
1 9   TRP n 
1 10  TRP n 
1 11  HIS n 
1 12  MET n 
1 13  HIS n 
1 14  GLN n 
1 15  PRO n 
1 16  LEU n 
1 17  TYR n 
1 18  ARG n 
1 19  GLU n 
1 20  PRO n 
1 21  TYR n 
1 22  THR n 
1 23  GLY n 
1 24  GLU n 
1 25  TYR n 
1 26  LEU n 
1 27  LEU n 
1 28  PRO n 
1 29  TRP n 
1 30  THR n 
1 31  PHE n 
1 32  PHE n 
1 33  HIS n 
1 34  ALA n 
1 35  VAL n 
1 36  LYS n 
1 37  ASP n 
1 38  TYR n 
1 39  TYR n 
1 40  ASP n 
1 41  MET n 
1 42  PRO n 
1 43  ALA n 
1 44  TYR n 
1 45  LEU n 
1 46  LYS n 
1 47  ASP n 
1 48  PHE n 
1 49  GLU n 
1 50  ILE n 
1 51  LYS n 
1 52  LEU n 
1 53  ASN n 
1 54  PHE n 
1 55  ASN n 
1 56  LEU n 
1 57  THR n 
1 58  PRO n 
1 59  VAL n 
1 60  LEU n 
1 61  ILE n 
1 62  ASP n 
1 63  GLN n 
1 64  ILE n 
1 65  GLN n 
1 66  GLU n 
1 67  TYR n 
1 68  ALA n 
1 69  GLN n 
1 70  GLY n 
1 71  LYS n 
1 72  ALA n 
1 73  LYS n 
1 74  ASP n 
1 75  VAL n 
1 76  PHE n 
1 77  LEU n 
1 78  GLU n 
1 79  ALA n 
1 80  ILE n 
1 81  ARG n 
1 82  LYS n 
1 83  ASP n 
1 84  PRO n 
1 85  ASP n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  LYS n 
1 90  GLU n 
1 91  GLU n 
1 92  VAL n 
1 93  GLU n 
1 94  LYS n 
1 95  LEU n 
1 96  ILE n 
1 97  GLU n 
1 98  PHE n 
1 99  THR n 
1 100 LYS n 
1 101 LEU n 
1 102 ASN n 
1 103 TYR n 
1 104 GLU n 
1 105 LYS n 
1 106 PRO n 
1 107 ILE n 
1 108 TYR n 
1 109 ARG n 
1 110 PHE n 
1 111 GLU n 
1 112 ARG n 
1 113 ILE n 
1 114 ARG n 
1 115 GLU n 
1 116 LEU n 
1 117 MET n 
1 118 ASN n 
1 119 LYS n 
1 120 GLU n 
1 121 LYS n 
1 122 LEU n 
1 123 ASN n 
1 124 ARG n 
1 125 GLU n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 ASP n 
1 130 LEU n 
1 131 GLN n 
1 132 THR n 
1 133 LEU n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 ALA n 
1 138 TRP n 
1 139 CYS n 
1 140 GLY n 
1 141 ARG n 
1 142 THR n 
1 143 LEU n 
1 144 ARG n 
1 145 LYS n 
1 146 ASP n 
1 147 LEU n 
1 148 LYS n 
1 149 ASP n 
1 150 LEU n 
1 151 LEU n 
1 152 ASN n 
1 153 LYS n 
1 154 GLY n 
1 155 ARG n 
1 156 ASN n 
1 157 TYR n 
1 158 THR n 
1 159 GLN n 
1 160 GLU n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 TYR n 
1 165 VAL n 
1 166 LEU n 
1 167 ASN n 
1 168 LYS n 
1 169 TYR n 
1 170 PHE n 
1 171 GLU n 
1 172 ILE n 
1 173 ILE n 
1 174 LYS n 
1 175 LYS n 
1 176 THR n 
1 177 LEU n 
1 178 SER n 
1 179 ILE n 
1 180 TYR n 
1 181 ARG n 
1 182 GLU n 
1 183 ILE n 
1 184 LYS n 
1 185 GLU n 
1 186 GLU n 
1 187 GLY n 
1 188 LYS n 
1 189 GLY n 
1 190 SER n 
1 191 VAL n 
1 192 SER n 
1 193 THR n 
1 194 SER n 
1 195 PRO n 
1 196 TYR n 
1 197 TYR n 
1 198 HIS n 
1 199 PRO n 
1 200 LEU n 
1 201 ILE n 
1 202 PRO n 
1 203 ILE n 
1 204 LEU n 
1 205 LEU n 
1 206 ASN n 
1 207 PRO n 
1 208 ASN n 
1 209 CYS n 
1 210 VAL n 
1 211 TYR n 
1 212 GLU n 
1 213 THR n 
1 214 THR n 
1 215 PRO n 
1 216 ASN n 
1 217 VAL n 
1 218 LYS n 
1 219 ILE n 
1 220 PRO n 
1 221 ASP n 
1 222 PHE n 
1 223 ALA n 
1 224 VAL n 
1 225 SER n 
1 226 PHE n 
1 227 ARG n 
1 228 GLU n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 HIS n 
1 234 VAL n 
1 235 GLU n 
1 236 LEU n 
1 237 ALA n 
1 238 LYS n 
1 239 GLU n 
1 240 LYS n 
1 241 TYR n 
1 242 PHE n 
1 243 GLU n 
1 244 ILE n 
1 245 PHE n 
1 246 GLY n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 VAL n 
1 251 TYR n 
1 252 MET n 
1 253 TRP n 
1 254 PRO n 
1 255 PRO n 
1 256 GLU n 
1 257 ALA n 
1 258 SER n 
1 259 VAL n 
1 260 SER n 
1 261 ASN n 
1 262 GLU n 
1 263 ALA n 
1 264 LEU n 
1 265 GLU n 
1 266 LEU n 
1 267 TYR n 
1 268 TYR n 
1 269 GLU n 
1 270 LYS n 
1 271 GLY n 
1 272 ILE n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 ALA n 
1 277 THR n 
1 278 ASP n 
1 279 GLU n 
1 280 VAL n 
1 281 ILE n 
1 282 LEU n 
1 283 LYS n 
1 284 ASN n 
1 285 SER n 
1 286 VAL n 
1 287 GLU n 
1 288 ARG n 
1 289 ALA n 
1 290 SER n 
1 291 PRO n 
1 292 TYR n 
1 293 LEU n 
1 294 ARG n 
1 295 TYR n 
1 296 TYR n 
1 297 PHE n 
1 298 ARG n 
1 299 GLU n 
1 300 LEU n 
1 301 ILE n 
1 302 SER n 
1 303 VAL n 
1 304 PHE n 
1 305 PHE n 
1 306 ARG n 
1 307 ASP n 
1 308 LYS n 
1 309 THR n 
1 310 LEU n 
1 311 SER n 
1 312 ASP n 
1 313 LEU n 
1 314 ILE n 
1 315 GLY n 
1 316 PHE n 
1 317 SER n 
1 318 TYR n 
1 319 HIS n 
1 320 ALA n 
1 321 TRP n 
1 322 ASN n 
1 323 ALA n 
1 324 GLU n 
1 325 ASP n 
1 326 ALA n 
1 327 VAL n 
1 328 ARG n 
1 329 ASP n 
1 330 PHE n 
1 331 ILE n 
1 332 GLY n 
1 333 ARG n 
1 334 LEU n 
1 335 LYS n 
1 336 LYS n 
1 337 ILE n 
1 338 HIS n 
1 339 GLU n 
1 340 SER n 
1 341 VAL n 
1 342 ASP n 
1 343 PHE n 
1 344 GLN n 
1 345 PRO n 
1 346 VAL n 
1 347 VAL n 
1 348 PHE n 
1 349 VAL n 
1 350 VAL n 
1 351 LEU n 
1 352 ASN n 
1 353 GLY n 
1 354 GLU n 
1 355 ASN n 
1 356 CYS n 
1 357 TRP n 
1 358 GLU n 
1 359 TYR n 
1 360 TYR n 
1 361 GLU n 
1 362 GLU n 
1 363 ASN n 
1 364 GLY n 
1 365 ILE n 
1 366 PRO n 
1 367 PHE n 
1 368 LEU n 
1 369 GLU n 
1 370 LYS n 
1 371 LEU n 
1 372 TYR n 
1 373 SER n 
1 374 THR n 
1 375 LEU n 
1 376 GLU n 
1 377 LYS n 
1 378 GLU n 
1 379 GLU n 
1 380 TRP n 
1 381 ILE n 
1 382 GLU n 
1 383 THR n 
1 384 LEU n 
1 385 THR n 
1 386 LEU n 
1 387 GLU n 
1 388 GLU n 
1 389 ALA n 
1 390 MET n 
1 391 ARG n 
1 392 LYS n 
1 393 GLU n 
1 394 ASP n 
1 395 VAL n 
1 396 LYS n 
1 397 THR n 
1 398 GLU n 
1 399 VAL n 
1 400 ILE n 
1 401 GLU n 
1 402 SER n 
1 403 VAL n 
1 404 LYS n 
1 405 ALA n 
1 406 GLY n 
1 407 THR n 
1 408 TRP n 
1 409 PHE n 
1 410 ASP n 
1 411 GLY n 
1 412 ASN n 
1 413 PHE n 
1 414 LEU n 
1 415 LYS n 
1 416 TRP n 
1 417 ILE n 
1 418 GLY n 
1 419 ASN n 
1 420 LYS n 
1 421 GLU n 
1 422 LYS n 
1 423 ASN n 
1 424 GLU n 
1 425 TYR n 
1 426 TRP n 
1 427 LYS n 
1 428 ILE n 
1 429 LEU n 
1 430 ILE n 
1 431 GLU n 
1 432 ALA n 
1 433 LYS n 
1 434 LYS n 
1 435 LYS n 
1 436 ALA n 
1 437 LYS n 
1 438 ASN n 
1 439 ASP n 
1 440 TYR n 
1 441 ILE n 
1 442 LEU n 
1 443 VAL n 
1 444 ALA n 
1 445 GLU n 
1 446 GLY n 
1 447 SER n 
1 448 ASP n 
1 449 TRP n 
1 450 PHE n 
1 451 TRP n 
1 452 TRP n 
1 453 GLN n 
1 454 GLY n 
1 455 GLU n 
1 456 GLU n 
1 457 LYS n 
1 458 ALA n 
1 459 PRO n 
1 460 PHE n 
1 461 VAL n 
1 462 GLU n 
1 463 VAL n 
1 464 PHE n 
1 465 ASP n 
1 466 LYS n 
1 467 LEU n 
1 468 PHE n 
1 469 ARG n 
1 470 SER n 
1 471 PHE n 
1 472 VAL n 
1 473 ARG n 
1 474 ARG n 
1 475 ALA n 
1 476 GLN n 
1 477 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   477 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 aq_720 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Aquifex aeolicus VF5' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     224324 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
2 oligosaccharide 
3 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 DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROH 'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,7,6/[a2122h-1a_1-5]/1-1-1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1_e4-f1_f4-g1' 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]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}}}}}' 
LINUCS                      PDB-CARE   ?     
4 3 DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROH 'Glycam Condensed Sequence' GMML       1.0   
5 3 'WURCS=2.0/1,6,5/[a2122h-1a_1-5]/1-1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1_e4-f1' WURCS                       PDB2Glycan 1.1.0 
6 3 '[][a-D-Glcp]{[(4+1)][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 ? 
5  2 6 GLC C1 O1 5 GLC O4 HO4 sing ? 
6  2 7 GLC C1 O1 6 GLC O4 HO4 sing ? 
7  3 2 GLC C1 O1 1 GLC O4 HO4 sing ? 
8  3 3 GLC C1 O1 2 GLC O4 HO4 sing ? 
9  3 4 GLC C1 O1 3 GLC O4 HO4 sing ? 
10 3 5 GLC C1 O1 4 GLC O4 HO4 sing ? 
11 3 6 GLC C1 O1 5 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  
GOL non-polymer                   . GLYCEROL              'GLYCERIN; PROPANE-1,2,3-TRIOL'       'C3 H8 O3'       92.094  
HIS 'L-peptide linking'           y HISTIDINE             ?                                     'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER                 ?                                     'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE            ?                                     'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE               ?                                     'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                ?                                     'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'           y METHIONINE            ?                                     'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking'           y PHENYLALANINE         ?                                     'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'           y PROLINE               ?                                     'C5 H9 N O2'     115.130 
SER 'L-peptide linking'           y SERINE                ?                                     'C3 H7 N O3'     105.093 
THR 'L-peptide linking'           y THREONINE             ?                                     'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'           y TRYPTOPHAN            ?                                     'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'           y TYROSINE              ?                                     'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'           y VALINE                ?                                     'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
GLC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpa            
GLC 'COMMON NAME'                         GMML     1.0 a-D-glucopyranose 
GLC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-D-Glcp          
GLC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  HIS 11  11  11  HIS HIS A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 TRP 253 253 253 TRP TRP A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 GLU 256 256 256 GLU GLU A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 VAL 259 259 259 VAL VAL A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 ASN 261 261 261 ASN ASN A . n 
A 1 262 GLU 262 262 262 GLU GLU A . n 
A 1 263 ALA 263 263 263 ALA ALA A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 TYR 268 268 268 TYR TYR A . n 
A 1 269 GLU 269 269 269 GLU GLU A . n 
A 1 270 LYS 270 270 270 LYS LYS A . n 
A 1 271 GLY 271 271 271 GLY GLY A . n 
A 1 272 ILE 272 272 272 ILE ILE A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 MET 274 274 274 MET MET A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 ALA 276 276 276 ALA ALA A . n 
A 1 277 THR 277 277 277 THR THR A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 VAL 280 280 280 VAL VAL A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 LYS 283 283 283 LYS LYS A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 VAL 286 286 286 VAL VAL A . n 
A 1 287 GLU 287 287 287 GLU GLU A . n 
A 1 288 ARG 288 288 288 ARG ARG A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 SER 290 290 290 SER SER A . n 
A 1 291 PRO 291 291 291 PRO PRO A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 TYR 295 295 295 TYR TYR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 PHE 297 297 297 PHE PHE A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ILE 301 301 301 ILE ILE A . n 
A 1 302 SER 302 302 302 SER SER A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 PHE 304 304 304 PHE PHE A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 ARG 306 306 306 ARG ARG A . n 
A 1 307 ASP 307 307 307 ASP ASP A . n 
A 1 308 LYS 308 308 308 LYS LYS A . n 
A 1 309 THR 309 309 309 THR THR A . n 
A 1 310 LEU 310 310 310 LEU LEU A . n 
A 1 311 SER 311 311 311 SER SER A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 LEU 313 313 313 LEU LEU A . n 
A 1 314 ILE 314 314 314 ILE ILE A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 PHE 316 316 316 PHE PHE A . n 
A 1 317 SER 317 317 317 SER SER A . n 
A 1 318 TYR 318 318 318 TYR TYR A . n 
A 1 319 HIS 319 319 319 HIS HIS A . n 
A 1 320 ALA 320 320 320 ALA ALA A . n 
A 1 321 TRP 321 321 321 TRP TRP A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 GLU 324 324 324 GLU GLU A . n 
A 1 325 ASP 325 325 325 ASP ASP A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 VAL 327 327 327 VAL VAL A . n 
A 1 328 ARG 328 328 328 ARG ARG A . n 
A 1 329 ASP 329 329 329 ASP ASP A . n 
A 1 330 PHE 330 330 330 PHE PHE A . n 
A 1 331 ILE 331 331 331 ILE ILE A . n 
A 1 332 GLY 332 332 332 GLY GLY A . n 
A 1 333 ARG 333 333 333 ARG ARG A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 HIS 338 338 338 HIS HIS A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 SER 340 340 340 SER SER A . n 
A 1 341 VAL 341 341 341 VAL VAL A . n 
A 1 342 ASP 342 342 342 ASP ASP A . n 
A 1 343 PHE 343 343 343 PHE PHE A . n 
A 1 344 GLN 344 344 344 GLN GLN A . n 
A 1 345 PRO 345 345 345 PRO PRO A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 VAL 347 347 347 VAL VAL A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 LEU 351 351 351 LEU LEU A . n 
A 1 352 ASN 352 352 352 ASN ASN A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 CYS 356 356 356 CYS CYS A . n 
A 1 357 TRP 357 357 357 TRP TRP A . n 
A 1 358 GLU 358 358 358 GLU GLU A . n 
A 1 359 TYR 359 359 359 TYR TYR A . n 
A 1 360 TYR 360 360 360 TYR TYR A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 PRO 366 366 366 PRO PRO A . n 
A 1 367 PHE 367 367 367 PHE PHE A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 TYR 372 372 372 TYR TYR A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 TRP 380 380 380 TRP TRP A . n 
A 1 381 ILE 381 381 381 ILE ILE A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 MET 390 390 390 MET MET A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 ASP 394 394 394 ASP ASP A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ILE 400 400 400 ILE ILE A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 SER 402 402 402 SER SER A . n 
A 1 403 VAL 403 403 403 VAL VAL A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 ALA 405 405 405 ALA ALA A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 TRP 408 408 408 TRP TRP A . n 
A 1 409 PHE 409 409 409 PHE PHE A . n 
A 1 410 ASP 410 410 410 ASP ASP A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 ASN 412 412 412 ASN ASN A . n 
A 1 413 PHE 413 413 413 PHE PHE A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 TRP 416 416 416 TRP TRP A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 GLY 418 418 418 GLY GLY A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 TYR 425 425 425 TYR TYR A . n 
A 1 426 TRP 426 426 426 TRP TRP A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 LYS 437 437 437 LYS LYS A . n 
A 1 438 ASN 438 438 438 ASN ASN A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 LEU 442 442 442 LEU LEU A . n 
A 1 443 VAL 443 443 443 VAL VAL A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 SER 447 447 447 SER SER A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 TRP 449 449 449 TRP TRP A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 TRP 451 451 451 TRP TRP A . n 
A 1 452 TRP 452 452 452 TRP TRP A . n 
A 1 453 GLN 453 453 453 GLN GLN A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 GLU 456 456 456 GLU GLU A . n 
A 1 457 LYS 457 457 457 LYS LYS A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 PRO 459 459 459 PRO PRO A . n 
A 1 460 PHE 460 460 460 PHE PHE A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 GLU 462 462 462 GLU GLU A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 PHE 464 464 464 PHE PHE A . n 
A 1 465 ASP 465 465 465 ASP ASP A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 LEU 467 467 467 LEU LEU A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 PHE 471 471 471 PHE PHE A . n 
A 1 472 VAL 472 472 472 VAL VAL A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 ARG 474 474 474 ARG ARG A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 GLN 476 476 476 GLN GLN A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   LYS 2   2   2   LYS LYS B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   PHE 5   5   5   PHE PHE B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  TRP 10  10  10  TRP TRP B . n 
B 1 11  HIS 11  11  11  HIS HIS B . n 
B 1 12  MET 12  12  12  MET MET B . n 
B 1 13  HIS 13  13  13  HIS HIS B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ARG 18  18  18  ARG ARG B . n 
B 1 19  GLU 19  19  19  GLU GLU B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  TYR 25  25  25  TYR TYR B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  THR 30  30  30  THR THR B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  ASP 37  37  37  ASP ASP B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  MET 41  41  41  MET MET B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  PHE 54  54  54  PHE PHE B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 LYS 105 105 105 LYS LYS B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 TYR 108 108 108 TYR TYR B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 PHE 110 110 110 PHE PHE B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 ASN 123 123 123 ASN ASN B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 TRP 138 138 138 TRP TRP B . n 
B 1 139 CYS 139 139 139 CYS CYS B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 GLN 159 159 159 GLN GLN B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 TYR 180 180 180 TYR TYR B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 LYS 184 184 184 LYS LYS B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 LYS 188 188 188 LYS LYS B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 SER 194 194 194 SER SER B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 TYR 196 196 196 TYR TYR B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 HIS 198 198 198 HIS HIS B . n 
B 1 199 PRO 199 199 199 PRO PRO B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 ASN 208 208 208 ASN ASN B . n 
B 1 209 CYS 209 209 209 CYS CYS B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 PRO 215 215 215 PRO PRO B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 PHE 226 226 226 PHE PHE B . n 
B 1 227 ARG 227 227 227 ARG ARG B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 LYS 232 232 232 LYS LYS B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 VAL 234 234 234 VAL VAL B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 PHE 242 242 242 PHE PHE B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 PHE 245 245 245 PHE PHE B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 HIS 248 248 248 HIS HIS B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 TYR 251 251 251 TYR TYR B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 TRP 253 253 253 TRP TRP B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 GLU 256 256 256 GLU GLU B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 SER 258 258 258 SER SER B . n 
B 1 259 VAL 259 259 259 VAL VAL B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 ASN 261 261 261 ASN ASN B . n 
B 1 262 GLU 262 262 262 GLU GLU B . n 
B 1 263 ALA 263 263 263 ALA ALA B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 GLU 265 265 265 GLU GLU B . n 
B 1 266 LEU 266 266 266 LEU LEU B . n 
B 1 267 TYR 267 267 267 TYR TYR B . n 
B 1 268 TYR 268 268 268 TYR TYR B . n 
B 1 269 GLU 269 269 269 GLU GLU B . n 
B 1 270 LYS 270 270 270 LYS LYS B . n 
B 1 271 GLY 271 271 271 GLY GLY B . n 
B 1 272 ILE 272 272 272 ILE ILE B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 MET 274 274 274 MET MET B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 ALA 276 276 276 ALA ALA B . n 
B 1 277 THR 277 277 277 THR THR B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 VAL 280 280 280 VAL VAL B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 ASN 284 284 284 ASN ASN B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 VAL 286 286 286 VAL VAL B . n 
B 1 287 GLU 287 287 287 GLU GLU B . n 
B 1 288 ARG 288 288 288 ARG ARG B . n 
B 1 289 ALA 289 289 289 ALA ALA B . n 
B 1 290 SER 290 290 290 SER SER B . n 
B 1 291 PRO 291 291 291 PRO PRO B . n 
B 1 292 TYR 292 292 292 TYR TYR B . n 
B 1 293 LEU 293 293 293 LEU LEU B . n 
B 1 294 ARG 294 294 294 ARG ARG B . n 
B 1 295 TYR 295 295 295 TYR TYR B . n 
B 1 296 TYR 296 296 296 TYR TYR B . n 
B 1 297 PHE 297 297 297 PHE PHE B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLU 299 299 299 GLU GLU B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 ILE 301 301 301 ILE ILE B . n 
B 1 302 SER 302 302 302 SER SER B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 PHE 304 304 304 PHE PHE B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 ARG 306 306 306 ARG ARG B . n 
B 1 307 ASP 307 307 307 ASP ASP B . n 
B 1 308 LYS 308 308 308 LYS LYS B . n 
B 1 309 THR 309 309 309 THR THR B . n 
B 1 310 LEU 310 310 310 LEU LEU B . n 
B 1 311 SER 311 311 311 SER SER B . n 
B 1 312 ASP 312 312 312 ASP ASP B . n 
B 1 313 LEU 313 313 313 LEU LEU B . n 
B 1 314 ILE 314 314 314 ILE ILE B . n 
B 1 315 GLY 315 315 315 GLY GLY B . n 
B 1 316 PHE 316 316 316 PHE PHE B . n 
B 1 317 SER 317 317 317 SER SER B . n 
B 1 318 TYR 318 318 318 TYR TYR B . n 
B 1 319 HIS 319 319 319 HIS HIS B . n 
B 1 320 ALA 320 320 320 ALA ALA B . n 
B 1 321 TRP 321 321 321 TRP TRP B . n 
B 1 322 ASN 322 322 322 ASN ASN B . n 
B 1 323 ALA 323 323 323 ALA ALA B . n 
B 1 324 GLU 324 324 324 GLU GLU B . n 
B 1 325 ASP 325 325 325 ASP ASP B . n 
B 1 326 ALA 326 326 326 ALA ALA B . n 
B 1 327 VAL 327 327 327 VAL VAL B . n 
B 1 328 ARG 328 328 328 ARG ARG B . n 
B 1 329 ASP 329 329 329 ASP ASP B . n 
B 1 330 PHE 330 330 330 PHE PHE B . n 
B 1 331 ILE 331 331 331 ILE ILE B . n 
B 1 332 GLY 332 332 332 GLY GLY B . n 
B 1 333 ARG 333 333 333 ARG ARG B . n 
B 1 334 LEU 334 334 334 LEU LEU B . n 
B 1 335 LYS 335 335 335 LYS LYS B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 ILE 337 337 337 ILE ILE B . n 
B 1 338 HIS 338 338 338 HIS HIS B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 SER 340 340 340 SER SER B . n 
B 1 341 VAL 341 341 341 VAL VAL B . n 
B 1 342 ASP 342 342 342 ASP ASP B . n 
B 1 343 PHE 343 343 343 PHE PHE B . n 
B 1 344 GLN 344 344 344 GLN GLN B . n 
B 1 345 PRO 345 345 345 PRO PRO B . n 
B 1 346 VAL 346 346 346 VAL VAL B . n 
B 1 347 VAL 347 347 347 VAL VAL B . n 
B 1 348 PHE 348 348 348 PHE PHE B . n 
B 1 349 VAL 349 349 349 VAL VAL B . n 
B 1 350 VAL 350 350 350 VAL VAL B . n 
B 1 351 LEU 351 351 351 LEU LEU B . n 
B 1 352 ASN 352 352 352 ASN ASN B . n 
B 1 353 GLY 353 353 353 GLY GLY B . n 
B 1 354 GLU 354 354 354 GLU GLU B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 CYS 356 356 356 CYS CYS B . n 
B 1 357 TRP 357 357 357 TRP TRP B . n 
B 1 358 GLU 358 358 358 GLU GLU B . n 
B 1 359 TYR 359 359 359 TYR TYR B . n 
B 1 360 TYR 360 360 360 TYR TYR B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 ILE 365 365 365 ILE ILE B . n 
B 1 366 PRO 366 366 366 PRO PRO B . n 
B 1 367 PHE 367 367 367 PHE PHE B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 GLU 369 369 369 GLU GLU B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 TYR 372 372 372 TYR TYR B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 GLU 378 378 378 GLU GLU B . n 
B 1 379 GLU 379 379 379 GLU GLU B . n 
B 1 380 TRP 380 380 380 TRP TRP B . n 
B 1 381 ILE 381 381 381 ILE ILE B . n 
B 1 382 GLU 382 382 382 GLU GLU B . n 
B 1 383 THR 383 383 383 THR THR B . n 
B 1 384 LEU 384 384 384 LEU LEU B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLU 387 387 387 GLU GLU B . n 
B 1 388 GLU 388 388 388 GLU GLU B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 MET 390 390 390 MET MET B . n 
B 1 391 ARG 391 391 391 ARG ARG B . n 
B 1 392 LYS 392 392 392 LYS LYS B . n 
B 1 393 GLU 393 393 393 GLU GLU B . n 
B 1 394 ASP 394 394 394 ASP ASP B . n 
B 1 395 VAL 395 395 395 VAL VAL B . n 
B 1 396 LYS 396 396 396 LYS LYS B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 VAL 399 399 399 VAL VAL B . n 
B 1 400 ILE 400 400 400 ILE ILE B . n 
B 1 401 GLU 401 401 401 GLU GLU B . n 
B 1 402 SER 402 402 402 SER SER B . n 
B 1 403 VAL 403 403 403 VAL VAL B . n 
B 1 404 LYS 404 404 404 LYS LYS B . n 
B 1 405 ALA 405 405 405 ALA ALA B . n 
B 1 406 GLY 406 406 406 GLY GLY B . n 
B 1 407 THR 407 407 407 THR THR B . n 
B 1 408 TRP 408 408 408 TRP TRP B . n 
B 1 409 PHE 409 409 409 PHE PHE B . n 
B 1 410 ASP 410 410 410 ASP ASP B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 ASN 412 412 412 ASN ASN B . n 
B 1 413 PHE 413 413 413 PHE PHE B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 LYS 415 415 415 LYS LYS B . n 
B 1 416 TRP 416 416 416 TRP TRP B . n 
B 1 417 ILE 417 417 417 ILE ILE B . n 
B 1 418 GLY 418 418 418 GLY GLY B . n 
B 1 419 ASN 419 419 419 ASN ASN B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 LYS 422 422 422 LYS LYS B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 TYR 425 425 425 TYR TYR B . n 
B 1 426 TRP 426 426 426 TRP TRP B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 ILE 428 428 428 ILE ILE B . n 
B 1 429 LEU 429 429 429 LEU LEU B . n 
B 1 430 ILE 430 430 430 ILE ILE B . n 
B 1 431 GLU 431 431 431 GLU GLU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 LYS 433 433 433 LYS LYS B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 LYS 435 435 435 LYS LYS B . n 
B 1 436 ALA 436 436 436 ALA ALA B . n 
B 1 437 LYS 437 437 437 LYS LYS B . n 
B 1 438 ASN 438 438 438 ASN ASN B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 TYR 440 440 440 TYR TYR B . n 
B 1 441 ILE 441 441 441 ILE ILE B . n 
B 1 442 LEU 442 442 442 LEU LEU B . n 
B 1 443 VAL 443 443 443 VAL VAL B . n 
B 1 444 ALA 444 444 444 ALA ALA B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 GLY 446 446 446 GLY GLY B . n 
B 1 447 SER 447 447 447 SER SER B . n 
B 1 448 ASP 448 448 448 ASP ASP B . n 
B 1 449 TRP 449 449 449 TRP TRP B . n 
B 1 450 PHE 450 450 450 PHE PHE B . n 
B 1 451 TRP 451 451 451 TRP TRP B . n 
B 1 452 TRP 452 452 452 TRP TRP B . n 
B 1 453 GLN 453 453 453 GLN GLN B . n 
B 1 454 GLY 454 454 454 GLY GLY B . n 
B 1 455 GLU 455 455 455 GLU GLU B . n 
B 1 456 GLU 456 456 456 GLU GLU B . n 
B 1 457 LYS 457 457 457 LYS LYS B . n 
B 1 458 ALA 458 458 458 ALA ALA B . n 
B 1 459 PRO 459 459 459 PRO PRO B . n 
B 1 460 PHE 460 460 460 PHE PHE B . n 
B 1 461 VAL 461 461 461 VAL VAL B . n 
B 1 462 GLU 462 462 462 GLU GLU B . n 
B 1 463 VAL 463 463 463 VAL VAL B . n 
B 1 464 PHE 464 464 464 PHE PHE B . n 
B 1 465 ASP 465 465 465 ASP ASP B . n 
B 1 466 LYS 466 466 466 LYS LYS B . n 
B 1 467 LEU 467 467 467 LEU LEU B . n 
B 1 468 PHE 468 468 468 PHE PHE B . n 
B 1 469 ARG 469 469 469 ARG ARG B . n 
B 1 470 SER 470 470 470 SER SER B . n 
B 1 471 PHE 471 471 471 PHE PHE B . n 
B 1 472 VAL 472 472 472 VAL VAL B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 ARG 474 474 474 ARG ARG B . n 
B 1 475 ALA 475 475 475 ALA ALA B . n 
B 1 476 GLN 476 476 476 GLN GLN B . n 
B 1 477 GLU 477 477 477 GLU GLU B . n 
# 
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 
C 2 GLC 1 C GLC 1 A GLC 491 n 
C 2 GLC 2 C GLC 2 A GLC 492 n 
C 2 GLC 3 C GLC 3 A GLC 493 n 
C 2 GLC 4 C GLC 4 A GLC 494 n 
C 2 GLC 5 C GLC 5 A GLC 495 n 
C 2 GLC 6 C GLC 6 A GLC 496 n 
C 2 GLC 7 C GLC 7 A GLC 497 n 
D 3 GLC 1 D GLC 1 B GLC 491 n 
D 3 GLC 2 D GLC 2 B GLC 492 n 
D 3 GLC 3 D GLC 3 B GLC 493 n 
D 3 GLC 4 D GLC 4 B GLC 494 n 
D 3 GLC 5 D GLC 5 B GLC 495 n 
D 3 GLC 6 D GLC 6 B GLC 496 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 
E 4 GOL 1   501 501 GOL GOL A . 
F 4 GOL 1   501 501 GOL GOL B . 
G 5 HOH 1   601 28  HOH HOH A . 
G 5 HOH 2   602 309 HOH HOH A . 
G 5 HOH 3   603 218 HOH HOH A . 
G 5 HOH 4   604 149 HOH HOH A . 
G 5 HOH 5   605 209 HOH HOH A . 
G 5 HOH 6   606 237 HOH HOH A . 
G 5 HOH 7   607 257 HOH HOH A . 
G 5 HOH 8   608 114 HOH HOH A . 
G 5 HOH 9   609 228 HOH HOH A . 
G 5 HOH 10  610 244 HOH HOH A . 
G 5 HOH 11  611 155 HOH HOH A . 
G 5 HOH 12  612 14  HOH HOH A . 
G 5 HOH 13  613 89  HOH HOH A . 
G 5 HOH 14  614 199 HOH HOH A . 
G 5 HOH 15  615 232 HOH HOH A . 
G 5 HOH 16  616 45  HOH HOH A . 
G 5 HOH 17  617 118 HOH HOH A . 
G 5 HOH 18  618 116 HOH HOH A . 
G 5 HOH 19  619 179 HOH HOH A . 
G 5 HOH 20  620 17  HOH HOH A . 
G 5 HOH 21  621 197 HOH HOH A . 
G 5 HOH 22  622 205 HOH HOH A . 
G 5 HOH 23  623 59  HOH HOH A . 
G 5 HOH 24  624 277 HOH HOH A . 
G 5 HOH 25  625 31  HOH HOH A . 
G 5 HOH 26  626 65  HOH HOH A . 
G 5 HOH 27  627 75  HOH HOH A . 
G 5 HOH 28  628 43  HOH HOH A . 
G 5 HOH 29  629 38  HOH HOH A . 
G 5 HOH 30  630 34  HOH HOH A . 
G 5 HOH 31  631 206 HOH HOH A . 
G 5 HOH 32  632 153 HOH HOH A . 
G 5 HOH 33  633 22  HOH HOH A . 
G 5 HOH 34  634 83  HOH HOH A . 
G 5 HOH 35  635 187 HOH HOH A . 
G 5 HOH 36  636 39  HOH HOH A . 
G 5 HOH 37  637 37  HOH HOH A . 
G 5 HOH 38  638 11  HOH HOH A . 
G 5 HOH 39  639 1   HOH HOH A . 
G 5 HOH 40  640 77  HOH HOH A . 
G 5 HOH 41  641 245 HOH HOH A . 
G 5 HOH 42  642 151 HOH HOH A . 
G 5 HOH 43  643 29  HOH HOH A . 
G 5 HOH 44  644 322 HOH HOH A . 
G 5 HOH 45  645 50  HOH HOH A . 
G 5 HOH 46  646 35  HOH HOH A . 
G 5 HOH 47  647 46  HOH HOH A . 
G 5 HOH 48  648 208 HOH HOH A . 
G 5 HOH 49  649 2   HOH HOH A . 
G 5 HOH 50  650 8   HOH HOH A . 
G 5 HOH 51  651 68  HOH HOH A . 
G 5 HOH 52  652 54  HOH HOH A . 
G 5 HOH 53  653 57  HOH HOH A . 
G 5 HOH 54  654 178 HOH HOH A . 
G 5 HOH 55  655 298 HOH HOH A . 
G 5 HOH 56  656 16  HOH HOH A . 
G 5 HOH 57  657 101 HOH HOH A . 
G 5 HOH 58  658 105 HOH HOH A . 
G 5 HOH 59  659 138 HOH HOH A . 
G 5 HOH 60  660 251 HOH HOH A . 
G 5 HOH 61  661 36  HOH HOH A . 
G 5 HOH 62  662 158 HOH HOH A . 
G 5 HOH 63  663 224 HOH HOH A . 
G 5 HOH 64  664 24  HOH HOH A . 
G 5 HOH 65  665 85  HOH HOH A . 
G 5 HOH 66  666 262 HOH HOH A . 
G 5 HOH 67  667 98  HOH HOH A . 
G 5 HOH 68  668 92  HOH HOH A . 
G 5 HOH 69  669 140 HOH HOH A . 
G 5 HOH 70  670 120 HOH HOH A . 
G 5 HOH 71  671 119 HOH HOH A . 
G 5 HOH 72  672 207 HOH HOH A . 
G 5 HOH 73  673 82  HOH HOH A . 
G 5 HOH 74  674 80  HOH HOH A . 
G 5 HOH 75  675 344 HOH HOH A . 
G 5 HOH 76  676 324 HOH HOH A . 
G 5 HOH 77  677 72  HOH HOH A . 
G 5 HOH 78  678 302 HOH HOH A . 
G 5 HOH 79  679 227 HOH HOH A . 
G 5 HOH 80  680 86  HOH HOH A . 
G 5 HOH 81  681 91  HOH HOH A . 
G 5 HOH 82  682 23  HOH HOH A . 
G 5 HOH 83  683 180 HOH HOH A . 
G 5 HOH 84  684 100 HOH HOH A . 
G 5 HOH 85  685 339 HOH HOH A . 
G 5 HOH 86  686 128 HOH HOH A . 
G 5 HOH 87  687 219 HOH HOH A . 
G 5 HOH 88  688 182 HOH HOH A . 
G 5 HOH 89  689 247 HOH HOH A . 
G 5 HOH 90  690 285 HOH HOH A . 
G 5 HOH 91  691 3   HOH HOH A . 
G 5 HOH 92  692 6   HOH HOH A . 
G 5 HOH 93  693 51  HOH HOH A . 
G 5 HOH 94  694 106 HOH HOH A . 
G 5 HOH 95  695 30  HOH HOH A . 
G 5 HOH 96  696 133 HOH HOH A . 
G 5 HOH 97  697 307 HOH HOH A . 
G 5 HOH 98  698 115 HOH HOH A . 
G 5 HOH 99  699 47  HOH HOH A . 
G 5 HOH 100 700 146 HOH HOH A . 
G 5 HOH 101 701 64  HOH HOH A . 
G 5 HOH 102 702 184 HOH HOH A . 
G 5 HOH 103 703 152 HOH HOH A . 
G 5 HOH 104 704 269 HOH HOH A . 
G 5 HOH 105 705 99  HOH HOH A . 
G 5 HOH 106 706 40  HOH HOH A . 
G 5 HOH 107 707 314 HOH HOH A . 
G 5 HOH 108 708 143 HOH HOH A . 
G 5 HOH 109 709 160 HOH HOH A . 
G 5 HOH 110 710 10  HOH HOH A . 
G 5 HOH 111 711 62  HOH HOH A . 
G 5 HOH 112 712 172 HOH HOH A . 
G 5 HOH 113 713 170 HOH HOH A . 
G 5 HOH 114 714 147 HOH HOH A . 
G 5 HOH 115 715 234 HOH HOH A . 
G 5 HOH 116 716 258 HOH HOH A . 
G 5 HOH 117 717 73  HOH HOH A . 
G 5 HOH 118 718 87  HOH HOH A . 
G 5 HOH 119 719 342 HOH HOH A . 
G 5 HOH 120 720 233 HOH HOH A . 
G 5 HOH 121 721 121 HOH HOH A . 
G 5 HOH 122 722 93  HOH HOH A . 
G 5 HOH 123 723 183 HOH HOH A . 
G 5 HOH 124 724 290 HOH HOH A . 
G 5 HOH 125 725 67  HOH HOH A . 
G 5 HOH 126 726 222 HOH HOH A . 
G 5 HOH 127 727 159 HOH HOH A . 
G 5 HOH 128 728 13  HOH HOH A . 
G 5 HOH 129 729 330 HOH HOH A . 
G 5 HOH 130 730 144 HOH HOH A . 
G 5 HOH 131 731 81  HOH HOH A . 
G 5 HOH 132 732 299 HOH HOH A . 
G 5 HOH 133 733 236 HOH HOH A . 
G 5 HOH 134 734 328 HOH HOH A . 
G 5 HOH 135 735 201 HOH HOH A . 
G 5 HOH 136 736 132 HOH HOH A . 
G 5 HOH 137 737 26  HOH HOH A . 
G 5 HOH 138 738 161 HOH HOH A . 
G 5 HOH 139 739 213 HOH HOH A . 
G 5 HOH 140 740 226 HOH HOH A . 
G 5 HOH 141 741 53  HOH HOH A . 
G 5 HOH 142 742 265 HOH HOH A . 
G 5 HOH 143 743 294 HOH HOH A . 
G 5 HOH 144 744 323 HOH HOH A . 
G 5 HOH 145 745 292 HOH HOH A . 
G 5 HOH 146 746 112 HOH HOH A . 
G 5 HOH 147 747 194 HOH HOH A . 
G 5 HOH 148 748 297 HOH HOH A . 
G 5 HOH 149 749 283 HOH HOH A . 
G 5 HOH 150 750 48  HOH HOH A . 
G 5 HOH 151 751 286 HOH HOH A . 
G 5 HOH 152 752 163 HOH HOH A . 
G 5 HOH 153 753 240 HOH HOH A . 
G 5 HOH 154 754 231 HOH HOH A . 
G 5 HOH 155 755 19  HOH HOH A . 
G 5 HOH 156 756 193 HOH HOH A . 
G 5 HOH 157 757 69  HOH HOH A . 
G 5 HOH 158 758 319 HOH HOH A . 
G 5 HOH 159 759 320 HOH HOH A . 
G 5 HOH 160 760 267 HOH HOH A . 
G 5 HOH 161 761 142 HOH HOH A . 
G 5 HOH 162 762 156 HOH HOH A . 
G 5 HOH 163 763 171 HOH HOH A . 
G 5 HOH 164 764 191 HOH HOH A . 
G 5 HOH 165 765 281 HOH HOH A . 
G 5 HOH 166 766 131 HOH HOH A . 
G 5 HOH 167 767 148 HOH HOH A . 
G 5 HOH 168 768 263 HOH HOH A . 
G 5 HOH 169 769 202 HOH HOH A . 
G 5 HOH 170 770 301 HOH HOH A . 
G 5 HOH 171 771 235 HOH HOH A . 
G 5 HOH 172 772 346 HOH HOH A . 
G 5 HOH 173 773 88  HOH HOH A . 
G 5 HOH 174 774 266 HOH HOH A . 
G 5 HOH 175 775 293 HOH HOH A . 
G 5 HOH 176 776 279 HOH HOH A . 
G 5 HOH 177 777 239 HOH HOH A . 
G 5 HOH 178 778 254 HOH HOH A . 
G 5 HOH 179 779 326 HOH HOH A . 
G 5 HOH 180 780 230 HOH HOH A . 
G 5 HOH 181 781 125 HOH HOH A . 
G 5 HOH 182 782 311 HOH HOH A . 
G 5 HOH 183 783 296 HOH HOH A . 
G 5 HOH 184 784 168 HOH HOH A . 
G 5 HOH 185 785 274 HOH HOH A . 
G 5 HOH 186 786 211 HOH HOH A . 
G 5 HOH 187 787 192 HOH HOH A . 
G 5 HOH 188 788 340 HOH HOH A . 
G 5 HOH 189 789 229 HOH HOH A . 
G 5 HOH 190 790 337 HOH HOH A . 
H 5 HOH 1   601 223 HOH HOH B . 
H 5 HOH 2   602 4   HOH HOH B . 
H 5 HOH 3   603 273 HOH HOH B . 
H 5 HOH 4   604 129 HOH HOH B . 
H 5 HOH 5   605 5   HOH HOH B . 
H 5 HOH 6   606 214 HOH HOH B . 
H 5 HOH 7   607 280 HOH HOH B . 
H 5 HOH 8   608 329 HOH HOH B . 
H 5 HOH 9   609 95  HOH HOH B . 
H 5 HOH 10  610 189 HOH HOH B . 
H 5 HOH 11  611 289 HOH HOH B . 
H 5 HOH 12  612 117 HOH HOH B . 
H 5 HOH 13  613 111 HOH HOH B . 
H 5 HOH 14  614 304 HOH HOH B . 
H 5 HOH 15  615 33  HOH HOH B . 
H 5 HOH 16  616 78  HOH HOH B . 
H 5 HOH 17  617 287 HOH HOH B . 
H 5 HOH 18  618 135 HOH HOH B . 
H 5 HOH 19  619 56  HOH HOH B . 
H 5 HOH 20  620 27  HOH HOH B . 
H 5 HOH 21  621 313 HOH HOH B . 
H 5 HOH 22  622 200 HOH HOH B . 
H 5 HOH 23  623 310 HOH HOH B . 
H 5 HOH 24  624 108 HOH HOH B . 
H 5 HOH 25  625 55  HOH HOH B . 
H 5 HOH 26  626 123 HOH HOH B . 
H 5 HOH 27  627 44  HOH HOH B . 
H 5 HOH 28  628 341 HOH HOH B . 
H 5 HOH 29  629 164 HOH HOH B . 
H 5 HOH 30  630 71  HOH HOH B . 
H 5 HOH 31  631 252 HOH HOH B . 
H 5 HOH 32  632 295 HOH HOH B . 
H 5 HOH 33  633 49  HOH HOH B . 
H 5 HOH 34  634 110 HOH HOH B . 
H 5 HOH 35  635 174 HOH HOH B . 
H 5 HOH 36  636 225 HOH HOH B . 
H 5 HOH 37  637 261 HOH HOH B . 
H 5 HOH 38  638 25  HOH HOH B . 
H 5 HOH 39  639 306 HOH HOH B . 
H 5 HOH 40  640 42  HOH HOH B . 
H 5 HOH 41  641 70  HOH HOH B . 
H 5 HOH 42  642 268 HOH HOH B . 
H 5 HOH 43  643 18  HOH HOH B . 
H 5 HOH 44  644 333 HOH HOH B . 
H 5 HOH 45  645 210 HOH HOH B . 
H 5 HOH 46  646 325 HOH HOH B . 
H 5 HOH 47  647 343 HOH HOH B . 
H 5 HOH 48  648 107 HOH HOH B . 
H 5 HOH 49  649 66  HOH HOH B . 
H 5 HOH 50  650 41  HOH HOH B . 
H 5 HOH 51  651 63  HOH HOH B . 
H 5 HOH 52  652 76  HOH HOH B . 
H 5 HOH 53  653 181 HOH HOH B . 
H 5 HOH 54  654 271 HOH HOH B . 
H 5 HOH 55  655 124 HOH HOH B . 
H 5 HOH 56  656 102 HOH HOH B . 
H 5 HOH 57  657 126 HOH HOH B . 
H 5 HOH 58  658 127 HOH HOH B . 
H 5 HOH 59  659 109 HOH HOH B . 
H 5 HOH 60  660 104 HOH HOH B . 
H 5 HOH 61  661 20  HOH HOH B . 
H 5 HOH 62  662 21  HOH HOH B . 
H 5 HOH 63  663 173 HOH HOH B . 
H 5 HOH 64  664 334 HOH HOH B . 
H 5 HOH 65  665 253 HOH HOH B . 
H 5 HOH 66  666 221 HOH HOH B . 
H 5 HOH 67  667 7   HOH HOH B . 
H 5 HOH 68  668 272 HOH HOH B . 
H 5 HOH 69  669 79  HOH HOH B . 
H 5 HOH 70  670 278 HOH HOH B . 
H 5 HOH 71  671 154 HOH HOH B . 
H 5 HOH 72  672 122 HOH HOH B . 
H 5 HOH 73  673 137 HOH HOH B . 
H 5 HOH 74  674 220 HOH HOH B . 
H 5 HOH 75  675 186 HOH HOH B . 
H 5 HOH 76  676 321 HOH HOH B . 
H 5 HOH 77  677 284 HOH HOH B . 
H 5 HOH 78  678 96  HOH HOH B . 
H 5 HOH 79  679 15  HOH HOH B . 
H 5 HOH 80  680 238 HOH HOH B . 
H 5 HOH 81  681 52  HOH HOH B . 
H 5 HOH 82  682 162 HOH HOH B . 
H 5 HOH 83  683 204 HOH HOH B . 
H 5 HOH 84  684 61  HOH HOH B . 
H 5 HOH 85  685 84  HOH HOH B . 
H 5 HOH 86  686 215 HOH HOH B . 
H 5 HOH 87  687 275 HOH HOH B . 
H 5 HOH 88  688 241 HOH HOH B . 
H 5 HOH 89  689 291 HOH HOH B . 
H 5 HOH 90  690 196 HOH HOH B . 
H 5 HOH 91  691 58  HOH HOH B . 
H 5 HOH 92  692 176 HOH HOH B . 
H 5 HOH 93  693 248 HOH HOH B . 
H 5 HOH 94  694 316 HOH HOH B . 
H 5 HOH 95  695 12  HOH HOH B . 
H 5 HOH 96  696 166 HOH HOH B . 
H 5 HOH 97  697 336 HOH HOH B . 
H 5 HOH 98  698 216 HOH HOH B . 
H 5 HOH 99  699 165 HOH HOH B . 
H 5 HOH 100 700 318 HOH HOH B . 
H 5 HOH 101 701 141 HOH HOH B . 
H 5 HOH 102 702 169 HOH HOH B . 
H 5 HOH 103 703 331 HOH HOH B . 
H 5 HOH 104 704 305 HOH HOH B . 
H 5 HOH 105 705 327 HOH HOH B . 
H 5 HOH 106 706 270 HOH HOH B . 
H 5 HOH 107 707 242 HOH HOH B . 
H 5 HOH 108 708 90  HOH HOH B . 
H 5 HOH 109 709 188 HOH HOH B . 
H 5 HOH 110 710 139 HOH HOH B . 
H 5 HOH 111 711 145 HOH HOH B . 
H 5 HOH 112 712 345 HOH HOH B . 
H 5 HOH 113 713 150 HOH HOH B . 
H 5 HOH 114 714 338 HOH HOH B . 
H 5 HOH 115 715 97  HOH HOH B . 
H 5 HOH 116 716 130 HOH HOH B . 
H 5 HOH 117 717 243 HOH HOH B . 
H 5 HOH 118 718 335 HOH HOH B . 
H 5 HOH 119 719 195 HOH HOH B . 
H 5 HOH 120 720 94  HOH HOH B . 
H 5 HOH 121 721 217 HOH HOH B . 
H 5 HOH 122 722 259 HOH HOH B . 
H 5 HOH 123 723 185 HOH HOH B . 
H 5 HOH 124 724 134 HOH HOH B . 
H 5 HOH 125 725 212 HOH HOH B . 
H 5 HOH 126 726 312 HOH HOH B . 
H 5 HOH 127 727 303 HOH HOH B . 
H 5 HOH 128 728 175 HOH HOH B . 
H 5 HOH 129 729 246 HOH HOH B . 
H 5 HOH 130 730 60  HOH HOH B . 
H 5 HOH 131 731 167 HOH HOH B . 
H 5 HOH 132 732 332 HOH HOH B . 
H 5 HOH 133 733 177 HOH HOH B . 
H 5 HOH 134 734 9   HOH HOH B . 
H 5 HOH 135 735 260 HOH HOH B . 
H 5 HOH 136 736 113 HOH HOH B . 
H 5 HOH 137 737 264 HOH HOH B . 
H 5 HOH 138 738 32  HOH HOH B . 
H 5 HOH 139 739 276 HOH HOH B . 
H 5 HOH 140 740 249 HOH HOH B . 
H 5 HOH 141 741 255 HOH HOH B . 
H 5 HOH 142 742 315 HOH HOH B . 
H 5 HOH 143 743 190 HOH HOH B . 
H 5 HOH 144 744 250 HOH HOH B . 
H 5 HOH 145 745 103 HOH HOH B . 
H 5 HOH 146 746 300 HOH HOH B . 
H 5 HOH 147 747 308 HOH HOH B . 
H 5 HOH 148 748 282 HOH HOH B . 
H 5 HOH 149 749 317 HOH HOH B . 
H 5 HOH 150 750 157 HOH HOH B . 
H 5 HOH 151 751 288 HOH HOH B . 
H 5 HOH 152 752 256 HOH HOH B . 
H 5 HOH 153 753 136 HOH HOH B . 
H 5 HOH 154 754 198 HOH HOH B . 
H 5 HOH 155 755 203 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   94.48 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JLW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.420 
_cell.length_a_esd                 ? 
_cell.length_b                     41.150 
_cell.length_b_esd                 ? 
_cell.length_c                     193.210 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JLW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                3 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 2 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                   9JLW 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.14 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Sodium citrate, pH 4.2, 20% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            338 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2023-11-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97918 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97918 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JLW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               64.21 
_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                                     70504 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.223 
_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                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.95 
_reflns_shell.d_res_low                                     2.00 
_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                             5134 
_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                               1.653 
_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                                  0.459 
_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                                  1.398 
_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                                 9JLW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.950 
_refine.ls_d_res_low                             59.718 
_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                     70478 
_refine.ls_number_reflns_R_free                  3508 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.00 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1968 
_refine.ls_R_factor_R_free                       0.2328 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1949 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.44 
_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                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.950 
_refine_hist.d_res_low                        59.718 
_refine_hist.number_atoms_solvent             345 
_refine_hist.number_atoms_total               8590 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8245 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006 ? 8480  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.810 ? 11488 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 4.833 ? 5051  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.047 ? 1233  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 1424  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.9500 1.9767 . . 131 2663 99.00  . . . . 0.2680 . . . . . . . . . . . 0.3264 
'X-RAY DIFFRACTION' 1.9767 2.0050 . . 122 2623 99.00  . . . . 0.2484 . . . . . . . . . . . 0.3087 
'X-RAY DIFFRACTION' 2.0050 2.0349 . . 127 2647 99.00  . . . . 0.2380 . . . . . . . . . . . 0.3066 
'X-RAY DIFFRACTION' 2.0349 2.0667 . . 149 2696 99.00  . . . . 0.2277 . . . . . . . . . . . 0.2876 
'X-RAY DIFFRACTION' 2.0667 2.1006 . . 130 2633 99.00  . . . . 0.2180 . . . . . . . . . . . 0.2520 
'X-RAY DIFFRACTION' 2.1006 2.1368 . . 147 2629 99.00  . . . . 0.2117 . . . . . . . . . . . 0.2471 
'X-RAY DIFFRACTION' 2.1368 2.1757 . . 137 2692 99.00  . . . . 0.2117 . . . . . . . . . . . 0.2725 
'X-RAY DIFFRACTION' 2.1757 2.2175 . . 162 2571 99.00  . . . . 0.2015 . . . . . . . . . . . 0.2779 
'X-RAY DIFFRACTION' 2.2175 2.2628 . . 144 2692 99.00  . . . . 0.2045 . . . . . . . . . . . 0.2629 
'X-RAY DIFFRACTION' 2.2628 2.3120 . . 137 2685 99.00  . . . . 0.1985 . . . . . . . . . . . 0.2556 
'X-RAY DIFFRACTION' 2.3120 2.3658 . . 134 2650 99.00  . . . . 0.1958 . . . . . . . . . . . 0.2622 
'X-RAY DIFFRACTION' 2.3658 2.4249 . . 112 2704 99.00  . . . . 0.2009 . . . . . . . . . . . 0.2741 
'X-RAY DIFFRACTION' 2.4249 2.4905 . . 142 2644 99.00  . . . . 0.1977 . . . . . . . . . . . 0.2728 
'X-RAY DIFFRACTION' 2.4905 2.5638 . . 127 2770 99.00  . . . . 0.1949 . . . . . . . . . . . 0.2378 
'X-RAY DIFFRACTION' 2.5638 2.6465 . . 135 2638 99.00  . . . . 0.1905 . . . . . . . . . . . 0.2481 
'X-RAY DIFFRACTION' 2.6465 2.7411 . . 124 2714 99.00  . . . . 0.1860 . . . . . . . . . . . 0.2286 
'X-RAY DIFFRACTION' 2.7411 2.8509 . . 124 2676 100.00 . . . . 0.1875 . . . . . . . . . . . 0.2335 
'X-RAY DIFFRACTION' 2.8509 2.9806 . . 170 2663 99.00  . . . . 0.1890 . . . . . . . . . . . 0.2155 
'X-RAY DIFFRACTION' 2.9806 3.1378 . . 160 2676 99.00  . . . . 0.1889 . . . . . . . . . . . 0.2131 
'X-RAY DIFFRACTION' 3.1378 3.3343 . . 132 2694 99.00  . . . . 0.1925 . . . . . . . . . . . 0.2312 
'X-RAY DIFFRACTION' 3.3343 3.5917 . . 158 2681 99.00  . . . . 0.1838 . . . . . . . . . . . 0.2241 
'X-RAY DIFFRACTION' 3.5917 3.9531 . . 172 2673 99.00  . . . . 0.1734 . . . . . . . . . . . 0.2152 
'X-RAY DIFFRACTION' 3.9531 4.5250 . . 151 2725 99.00  . . . . 0.1684 . . . . . . . . . . . 0.1843 
'X-RAY DIFFRACTION' 4.5250 5.7003 . . 165 2742 99.00  . . . . 0.1900 . . . . . . . . . . . 0.2228 
'X-RAY DIFFRACTION' 5.7003 59.718 . . 116 2789 96.00  . . . . 0.2187 . . . . . . . . . . . 0.2257 
# 
_struct.entry_id                     9JLW 
_struct.title                        
'Crystal structure of GH57 family amylopullulanase from Aquifex aeolicus mutant D352N in complex with maltoheptaose' 
_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        9JLW 
_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 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
_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 9JLW A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9JLW B 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 9JLW ASN A 352 ? UNP O66934 ASP 352 'engineered mutation' 352 1 
2 9JLW ASN B 352 ? UNP O66934 ASP 352 'engineered mutation' 352 2 
# 
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 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,G 
2 1 B,D,F,H 
# 
_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  ? ASP A 37  ? PRO A 28  ASP A 37  1 ? 10 
HELX_P HELX_P2  AA2 TYR A 39  ? TYR A 44  ? TYR A 39  TYR A 44  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 45  ? ASP A 47  ? LEU A 45  ASP A 47  5 ? 3  
HELX_P HELX_P4  AA4 THR A 57  ? GLN A 69  ? THR A 57  GLN A 69  1 ? 13 
HELX_P HELX_P5  AA5 VAL A 75  ? LYS A 82  ? VAL A 75  LYS A 82  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 83  ? LEU A 87  ? ASP A 83  LEU A 87  5 ? 5  
HELX_P HELX_P7  AA7 GLU A 88  ? TYR A 103 ? GLU A 88  TYR A 103 1 ? 16 
HELX_P HELX_P8  AA8 LYS A 105 ? ARG A 109 ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P9  AA9 PHE A 110 ? ASN A 118 ? PHE A 110 ASN A 118 1 ? 9  
HELX_P HELX_P10 AB1 ASN A 123 ? TRP A 138 ? ASN A 123 TRP A 138 1 ? 16 
HELX_P HELX_P11 AB2 GLY A 140 ? LEU A 147 ? GLY A 140 LEU A 147 1 ? 8  
HELX_P HELX_P12 AB3 LEU A 147 ? GLY A 154 ? LEU A 147 GLY A 154 1 ? 8  
HELX_P HELX_P13 AB4 THR A 158 ? LYS A 175 ? THR A 158 LYS A 175 1 ? 18 
HELX_P HELX_P14 AB5 LYS A 175 ? GLU A 186 ? LYS A 175 GLU A 186 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 207 ? THR A 213 ? PRO A 207 THR A 213 5 ? 7  
HELX_P HELX_P17 AB8 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P18 AB9 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P19 AC1 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P20 AC2 ASP A 278 ? VAL A 286 ? ASP A 278 VAL A 286 1 ? 9  
HELX_P HELX_P21 AC3 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P22 AC4 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P23 AC5 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P24 AC6 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P25 AC7 GLY A 364 ? GLU A 378 ? GLY A 364 GLU A 378 1 ? 15 
HELX_P HELX_P26 AC8 THR A 385 ? LYS A 392 ? THR A 385 LYS A 392 1 ? 8  
HELX_P HELX_P27 AC9 ASN A 419 ? LYS A 435 ? ASN A 419 LYS A 435 1 ? 17 
HELX_P HELX_P28 AD1 ASP A 439 ? GLU A 445 ? ASP A 439 GLU A 445 1 ? 7  
HELX_P HELX_P29 AD2 GLY A 446 ? GLN A 453 ? GLY A 446 GLN A 453 1 ? 8  
HELX_P HELX_P30 AD3 PHE A 460 ? GLN A 476 ? PHE A 460 GLN A 476 1 ? 17 
HELX_P HELX_P31 AD4 PRO B 28  ? ASP B 37  ? PRO B 28  ASP B 37  1 ? 10 
HELX_P HELX_P32 AD5 TYR B 39  ? TYR B 44  ? TYR B 39  TYR B 44  1 ? 6  
HELX_P HELX_P33 AD6 LEU B 45  ? ASP B 47  ? LEU B 45  ASP B 47  5 ? 3  
HELX_P HELX_P34 AD7 THR B 57  ? GLN B 69  ? THR B 57  GLN B 69  1 ? 13 
HELX_P HELX_P35 AD8 VAL B 75  ? LYS B 82  ? VAL B 75  LYS B 82  1 ? 8  
HELX_P HELX_P36 AD9 ASP B 83  ? LEU B 87  ? ASP B 83  LEU B 87  5 ? 5  
HELX_P HELX_P37 AE1 GLU B 88  ? TYR B 103 ? GLU B 88  TYR B 103 1 ? 16 
HELX_P HELX_P38 AE2 LYS B 105 ? ARG B 109 ? LYS B 105 ARG B 109 5 ? 5  
HELX_P HELX_P39 AE3 PHE B 110 ? ASN B 118 ? PHE B 110 ASN B 118 1 ? 9  
HELX_P HELX_P40 AE4 ASN B 123 ? TRP B 138 ? ASN B 123 TRP B 138 1 ? 16 
HELX_P HELX_P41 AE5 ARG B 141 ? LYS B 145 ? ARG B 141 LYS B 145 5 ? 5  
HELX_P HELX_P42 AE6 LEU B 147 ? GLY B 154 ? LEU B 147 GLY B 154 1 ? 8  
HELX_P HELX_P43 AE7 THR B 158 ? LYS B 175 ? THR B 158 LYS B 175 1 ? 18 
HELX_P HELX_P44 AE8 LYS B 175 ? GLU B 186 ? LYS B 175 GLU B 186 1 ? 12 
HELX_P HELX_P45 AE9 LEU B 200 ? ASN B 206 ? LEU B 200 ASN B 206 1 ? 7  
HELX_P HELX_P46 AF1 PRO B 207 ? THR B 213 ? PRO B 207 THR B 213 5 ? 7  
HELX_P HELX_P47 AF2 PHE B 226 ? GLY B 246 ? PHE B 226 GLY B 246 1 ? 21 
HELX_P HELX_P48 AF3 PRO B 254 ? SER B 258 ? PRO B 254 SER B 258 5 ? 5  
HELX_P HELX_P49 AF4 SER B 260 ? LYS B 270 ? SER B 260 LYS B 270 1 ? 11 
HELX_P HELX_P50 AF5 ASP B 278 ? VAL B 286 ? ASP B 278 VAL B 286 1 ? 9  
HELX_P HELX_P51 AF6 ASP B 307 ? SER B 317 ? ASP B 307 SER B 317 1 ? 11 
HELX_P HELX_P52 AF7 TYR B 318 ? TRP B 321 ? TYR B 318 TRP B 321 5 ? 4  
HELX_P HELX_P53 AF8 ASN B 322 ? VAL B 341 ? ASN B 322 VAL B 341 1 ? 20 
HELX_P HELX_P54 AF9 CYS B 356 ? ASN B 363 ? CYS B 356 ASN B 363 5 ? 8  
HELX_P HELX_P55 AG1 GLY B 364 ? GLU B 376 ? GLY B 364 GLU B 376 1 ? 13 
HELX_P HELX_P56 AG2 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P57 AG3 ASN B 419 ? LYS B 434 ? ASN B 419 LYS B 434 1 ? 16 
HELX_P HELX_P58 AG4 ASP B 439 ? GLU B 445 ? ASP B 439 GLU B 445 1 ? 7  
HELX_P HELX_P59 AG5 GLY B 446 ? GLN B 453 ? GLY B 446 GLN B 453 1 ? 8  
HELX_P HELX_P60 AG6 PHE B 460 ? GLN B 476 ? PHE B 460 GLN B 476 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 1 C GLC 2 1_555 ? ? ? ? ? ? ? 1.433 ? ? 
covale2  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 2 C GLC 3 1_555 ? ? ? ? ? ? ? 1.451 ? ? 
covale3  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 3 C GLC 4 1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale4  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 4 C GLC 5 1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale5  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 5 C GLC 6 1_555 ? ? ? ? ? ? ? 1.446 ? ? 
covale6  covale both ? C GLC . O4 ? ? ? 1_555 C GLC . C1 ? ? C GLC 6 C GLC 7 1_555 ? ? ? ? ? ? ? 1.454 ? ? 
covale7  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 1 D GLC 2 1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale8  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 2 D GLC 3 1_555 ? ? ? ? ? ? ? 1.449 ? ? 
covale9  covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 3 D GLC 4 1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale10 covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 4 D GLC 5 1_555 ? ? ? ? ? ? ? 1.438 ? ? 
covale11 covale both ? D GLC . O4 ? ? ? 1_555 D GLC . C1 ? ? D GLC 5 D GLC 6 1_555 ? ? ? ? ? ? ? 1.443 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA1 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA1 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA1 4 VAL A 346 ? ASN A 352 ? VAL A 346 ASN A 352 
AA2 1 VAL A 191 ? SER A 192 ? VAL A 191 SER A 192 
AA2 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA2 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA2 4 ILE A 381 ? THR A 383 ? ILE A 381 THR A 383 
AA3 1 GLU A 24  ? TYR A 25  ? GLU A 24  TYR A 25  
AA3 2 LYS A 73  ? ASP A 74  ? LYS A 73  ASP A 74  
AA4 1 TYR A 251 ? MET A 252 ? TYR A 251 MET A 252 
AA4 2 MET A 274 ? THR A 277 ? MET A 274 THR A 277 
AA4 3 ILE A 301 ? PHE A 305 ? ILE A 301 PHE A 305 
AA4 4 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 5 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
AA5 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA5 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA5 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA5 4 VAL B 346 ? ASN B 352 ? VAL B 346 ASN B 352 
AA6 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA6 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA6 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA6 4 ILE B 381 ? THR B 383 ? ILE B 381 THR B 383 
AA7 1 GLU B 24  ? TYR B 25  ? GLU B 24  TYR B 25  
AA7 2 LYS B 73  ? ASP B 74  ? LYS B 73  ASP B 74  
AA8 1 TYR B 251 ? MET B 252 ? TYR B 251 MET B 252 
AA8 2 MET B 274 ? THR B 277 ? MET B 274 THR B 277 
AA8 3 ILE B 301 ? PHE B 305 ? ILE B 301 PHE B 305 
AA8 4 ARG B 294 ? PHE B 297 ? ARG B 294 PHE B 297 
AA8 5 THR B 397 ? ILE B 400 ? THR B 397 ILE B 400 
# 
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 MET A 252 ? N MET A 252 O MET A 274 ? O MET A 274 
AA4 2 3 N THR A 277 ? N THR A 277 O PHE A 304 ? O PHE A 304 
AA4 3 4 O VAL A 303 ? O VAL A 303 N TYR A 295 ? N TYR A 295 
AA4 4 5 N TYR A 296 ? N TYR A 296 O 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 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA5 3 4 N PHE B 5   ? N PHE B 5   O VAL B 347 ? O VAL B 347 
AA6 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA6 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA6 3 4 N LEU B 4   ? N LEU B 4   O GLU B 382 ? O GLU B 382 
AA7 1 2 N TYR B 25  ? N TYR B 25  O LYS B 73  ? O LYS B 73  
AA8 1 2 N MET B 252 ? N MET B 252 O MET B 274 ? O MET B 274 
AA8 2 3 N LEU B 275 ? N LEU B 275 O SER B 302 ? O SER B 302 
AA8 3 4 O VAL B 303 ? O VAL B 303 N TYR B 295 ? N TYR B 295 
AA8 4 5 N TYR B 296 ? N TYR B 296 O ILE B 400 ? O ILE B 400 
# 
_pdbx_entry_details.entry_id                   9JLW 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 A GLU 361 ? ? O A HOH 601 ? ? 1.85 
2 1 O   A HOH 760 ? ? O A HOH 771 ? ? 2.17 
3 1 O   A HOH 751 ? ? O A HOH 768 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C A GLN 453 ? ? O A GLN 453 ? ? 1.086 1.229 -0.143 0.019 N 
2 1 C B ASN 352 ? ? O B ASN 352 ? ? 1.079 1.229 -0.150 0.019 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 206 ? ? -160.11 90.64   
2 1 ALA A 257 ? ? 56.14   17.06   
3 1 ASP A 410 ? ? 59.03   14.68   
4 1 GLU A 456 ? ? -6.94   134.91  
5 1 ASN B 206 ? ? -165.02 94.25   
6 1 THR B 277 ? ? -149.94 -159.99 
7 1 ARG B 288 ? ? -109.36 78.68   
8 1 ASP B 394 ? ? -92.57  57.42   
9 1 GLN B 453 ? ? -102.25 74.06   
# 
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 -8.9127  11.7590 71.9797 0.1253 ? -0.0118 ? -0.0046 ? 0.1271 ? 0.0049  ? 0.1516 ? 0.4304 ? 
-0.0237 ? 0.1600  ? 0.2405 ? -0.3696 ? 0.3365 ? 0.0068  ? -0.0061 ? -0.0766 ? -0.0414 ? 0.0080  ? 0.0106  ? -0.0073 ? 0.0366  ? 
-0.0001 ? 
2  'X-RAY DIFFRACTION' ? refined -22.9651 24.9773 81.9788 0.1470 ? 0.0061  ? 0.0175  ? 0.1582 ? 0.0072  ? 0.1917 ? 0.7058 ? 0.1542 
? -0.4129 ? 0.4710 ? -0.2821 ? 0.3661 ? 0.0311  ? -0.0487 ? 0.1929  ? 0.0079  ? 0.0216  ? 0.1037  ? -0.1498 ? -0.0585 ? 0.0003  ? 
3  'X-RAY DIFFRACTION' ? refined 4.5874   11.7754 66.1464 0.1641 ? -0.0145 ? -0.0002 ? 0.1343 ? -0.0216 ? 0.1897 ? 0.5711 ? 0.1040 
? -0.1782 ? 0.1673 ? -0.1717 ? 0.4573 ? -0.0261 ? 0.0485  ? -0.0776 ? -0.0596 ? 0.0142  ? -0.0447 ? 0.0500  ? 0.0650  ? 0.0000  ? 
4  'X-RAY DIFFRACTION' ? refined -5.1357  20.7874 52.2785 0.1697 ? -0.0138 ? -0.0003 ? 0.1670 ? 0.0247  ? 0.1498 ? 0.7821 ? 0.5494 
? 0.0613  ? 0.5353 ? -0.1070 ? 0.6288 ? 0.0153  ? 0.1076  ? 0.0681  ? -0.0573 ? 0.0459  ? -0.0363 ? -0.0531 ? 0.0505  ? 0.0005  ? 
5  'X-RAY DIFFRACTION' ? refined 14.8157  18.2325 75.5637 0.2000 ? -0.0174 ? 0.0081  ? 0.1801 ? -0.0139 ? 0.2139 ? 0.4890 ? 0.0275 
? 0.0594  ? 0.3149 ? -0.0609 ? 0.2352 ? 0.0079  ? -0.0439 ? 0.0874  ? -0.0407 ? 0.0369  ? -0.0761 ? -0.1826 ? 0.2316  ? -0.0000 ? 
6  'X-RAY DIFFRACTION' ? refined 4.4751   14.5727 86.1836 0.1748 ? 0.0022  ? -0.0093 ? 0.1609 ? 0.0136  ? 0.1482 ? 0.3551 ? 0.0109 
? 0.0569  ? 0.0497 ? 0.0772  ? 0.0189 ? -0.0648 ? -0.2141 ? -0.0110 ? 0.1281  ? 0.0536  ? -0.0085 ? -0.2897 ? 0.1058  ? 0.0002  ? 
7  'X-RAY DIFFRACTION' ? refined -22.9198 33.4033 27.2332 0.2091 ? 0.0091  ? 0.0058  ? 0.2090 ? -0.0069 ? 0.1527 ? 0.4464 ? 
-0.0717 ? 0.0296  ? 0.2761 ? 0.1647  ? 0.1759 ? 0.1234  ? 0.0611  ? -0.0573 ? -0.1207 ? -0.0327 ? -0.1579 ? 0.0591  ? 0.1055  ? 
0.0000  ? 
8  'X-RAY DIFFRACTION' ? refined -18.3874 30.1671 9.9643  0.3108 ? 0.0565  ? -0.0112 ? 0.3175 ? 0.0035  ? 0.1548 ? 0.1123 ? 
-0.0886 ? -0.1428 ? 0.0926 ? 0.0516  ? 0.0689 ? 0.0464  ? 0.3282  ? -0.1703 ? -0.2490 ? -0.1054 ? 0.1855  ? 0.2307  ? -0.0797 ? 
0.0007  ? 
9  'X-RAY DIFFRACTION' ? refined -12.7667 38.9709 16.6410 0.2270 ? 0.0268  ? 0.0208  ? 0.2837 ? 0.0340  ? 0.2572 ? 0.6747 ? 0.0206 
? -0.5087 ? 0.1641 ? -0.0815 ? 0.9049 ? 0.0705  ? 0.1129  ? 0.0494  ? -0.0444 ? -0.0444 ? -0.0490 ? 0.0128  ? 0.1607  ? -0.0001 ? 
10 'X-RAY DIFFRACTION' ? refined -45.5781 29.4726 24.6609 0.2843 ? -0.0252 ? -0.0421 ? 0.2660 ? 0.0049  ? 0.2855 ? 0.1997 ? 0.0588 
? -0.3138 ? 0.2304 ? -0.0246 ? 0.7484 ? -0.0030 ? 0.1534  ? -0.1816 ? -0.1400 ? 0.0357  ? 0.2416  ? 0.1705  ? -0.3042 ? 0.0007  ? 
11 'X-RAY DIFFRACTION' ? refined -40.0457 27.6301 34.9225 0.2490 ? -0.0103 ? -0.0135 ? 0.2555 ? 0.0199  ? 0.2485 ? 0.1592 ? 0.2062 
? -0.1625 ? 0.2588 ? -0.0355 ? 0.2852 ? -0.0782 ? 0.0767  ? -0.1466 ? 0.1729  ? 0.0571  ? -0.1102 ? 0.2034  ? 0.0053  ? 0.0001  ? 
12 'X-RAY DIFFRACTION' ? refined -31.5177 43.2283 41.5874 0.2224 ? -0.0115 ? 0.0140  ? 0.1863 ? -0.0287 ? 0.2335 ? 0.4928 ? 
-0.2904 ? 0.2946  ? 0.4987 ? -0.3452 ? 0.8947 ? 0.0677  ? -0.0921 ? 0.1554  ? 0.0088  ? -0.0112 ? 0.0754  ? -0.1491 ? -0.0142 ? 
-0.0001 ? 
13 'X-RAY DIFFRACTION' ? refined -21.2601 37.4835 44.5464 0.1976 ? -0.0314 ? -0.0075 ? 0.2417 ? -0.0352 ? 0.2237 ? 0.5455 ? 
-0.3834 ? 0.1264  ? 0.3133 ? 0.1185  ? 0.4291 ? 0.0329  ? 0.0009  ? 0.0630  ? 0.0002  ? 0.1142  ? -0.0492 ? 0.1432  ? 0.1263  ? 
0.0000  ? 
14 'X-RAY DIFFRACTION' ? refined -46.3237 38.3224 23.3162 0.2545 ? -0.0016 ? -0.0261 ? 0.3058 ? 0.0250  ? 0.2383 ? 0.1152 ? 
-0.2260 ? 0.1538  ? 0.2843 ? -0.1370 ? 0.1374 ? 0.0470  ? 0.0049  ? 0.0379  ? -0.1260 ? 0.0358  ? 0.1014  ? -0.0315 ? -0.4213 ? 
-0.0001 ? 
15 'X-RAY DIFFRACTION' ? refined -37.6137 34.5178 11.2922 0.3193 ? 0.0313  ? -0.0152 ? 0.2569 ? 0.0287  ? 0.1797 ? 0.3107 ? 
-0.1163 ? -0.2003 ? 0.0658 ? 0.0209  ? 0.2200 ? 0.1180  ? 0.2411  ? 0.0764  ? -0.1239 ? -0.0163 ? -0.1510 ? -0.0306 ? -0.2466 ? 
0.0002  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 81 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 82 through 158 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 159 through 322 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 323 through 396 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 57 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 58 through 88 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 89 through 200 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 201 through 245 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 246 through 278 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 279 through 360 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 361 through 396 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 397 through 435 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 436 through 477 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 B MET 1 ? B MET 1 
# 
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 
GOL C1   C N N 161 
GOL O1   O N N 162 
GOL C2   C N N 163 
GOL O2   O N N 164 
GOL C3   C N N 165 
GOL O3   O N N 166 
GOL H11  H N N 167 
GOL H12  H N N 168 
GOL HO1  H N N 169 
GOL H2   H N N 170 
GOL HO2  H N N 171 
GOL H31  H N N 172 
GOL H32  H N N 173 
GOL HO3  H N N 174 
HIS N    N N N 175 
HIS CA   C N S 176 
HIS C    C N N 177 
HIS O    O N N 178 
HIS CB   C N N 179 
HIS CG   C Y N 180 
HIS ND1  N Y N 181 
HIS CD2  C Y N 182 
HIS CE1  C Y N 183 
HIS NE2  N Y N 184 
HIS OXT  O N N 185 
HIS H    H N N 186 
HIS H2   H N N 187 
HIS HA   H N N 188 
HIS HB2  H N N 189 
HIS HB3  H N N 190 
HIS HD1  H N N 191 
HIS HD2  H N N 192 
HIS HE1  H N N 193 
HIS HE2  H N N 194 
HIS HXT  H N N 195 
HOH O    O N N 196 
HOH H1   H N N 197 
HOH H2   H N N 198 
ILE N    N N N 199 
ILE CA   C N S 200 
ILE C    C N N 201 
ILE O    O N N 202 
ILE CB   C N S 203 
ILE CG1  C N N 204 
ILE CG2  C N N 205 
ILE CD1  C N N 206 
ILE OXT  O N N 207 
ILE H    H N N 208 
ILE H2   H N N 209 
ILE HA   H N N 210 
ILE HB   H N N 211 
ILE HG12 H N N 212 
ILE HG13 H N N 213 
ILE HG21 H N N 214 
ILE HG22 H N N 215 
ILE HG23 H N N 216 
ILE HD11 H N N 217 
ILE HD12 H N N 218 
ILE HD13 H N N 219 
ILE HXT  H N N 220 
LEU N    N N N 221 
LEU CA   C N S 222 
LEU C    C N N 223 
LEU O    O N N 224 
LEU CB   C N N 225 
LEU CG   C N N 226 
LEU CD1  C N N 227 
LEU CD2  C N N 228 
LEU OXT  O N N 229 
LEU H    H N N 230 
LEU H2   H N N 231 
LEU HA   H N N 232 
LEU HB2  H N N 233 
LEU HB3  H N N 234 
LEU HG   H N N 235 
LEU HD11 H N N 236 
LEU HD12 H N N 237 
LEU HD13 H N N 238 
LEU HD21 H N N 239 
LEU HD22 H N N 240 
LEU HD23 H N N 241 
LEU HXT  H N N 242 
LYS N    N N N 243 
LYS CA   C N S 244 
LYS C    C N N 245 
LYS O    O N N 246 
LYS CB   C N N 247 
LYS CG   C N N 248 
LYS CD   C N N 249 
LYS CE   C N N 250 
LYS NZ   N N N 251 
LYS OXT  O N N 252 
LYS H    H N N 253 
LYS H2   H N N 254 
LYS HA   H N N 255 
LYS HB2  H N N 256 
LYS HB3  H N N 257 
LYS HG2  H N N 258 
LYS HG3  H N N 259 
LYS HD2  H N N 260 
LYS HD3  H N N 261 
LYS HE2  H N N 262 
LYS HE3  H N N 263 
LYS HZ1  H N N 264 
LYS HZ2  H N N 265 
LYS HZ3  H N N 266 
LYS HXT  H N N 267 
MET N    N N N 268 
MET CA   C N S 269 
MET C    C N N 270 
MET O    O N N 271 
MET CB   C N N 272 
MET CG   C N N 273 
MET SD   S N N 274 
MET CE   C N N 275 
MET OXT  O N N 276 
MET H    H N N 277 
MET H2   H N N 278 
MET HA   H N N 279 
MET HB2  H N N 280 
MET HB3  H N N 281 
MET HG2  H N N 282 
MET HG3  H N N 283 
MET HE1  H N N 284 
MET HE2  H N N 285 
MET HE3  H N N 286 
MET HXT  H N N 287 
PHE N    N N N 288 
PHE CA   C N S 289 
PHE C    C N N 290 
PHE O    O N N 291 
PHE CB   C N N 292 
PHE CG   C Y N 293 
PHE CD1  C Y N 294 
PHE CD2  C Y N 295 
PHE CE1  C Y N 296 
PHE CE2  C Y N 297 
PHE CZ   C Y N 298 
PHE OXT  O N N 299 
PHE H    H N N 300 
PHE H2   H N N 301 
PHE HA   H N N 302 
PHE HB2  H N N 303 
PHE HB3  H N N 304 
PHE HD1  H N N 305 
PHE HD2  H N N 306 
PHE HE1  H N N 307 
PHE HE2  H N N 308 
PHE HZ   H N N 309 
PHE HXT  H N N 310 
PRO N    N N N 311 
PRO CA   C N S 312 
PRO C    C N N 313 
PRO O    O N N 314 
PRO CB   C N N 315 
PRO CG   C N N 316 
PRO CD   C N N 317 
PRO OXT  O N N 318 
PRO H    H N N 319 
PRO HA   H N N 320 
PRO HB2  H N N 321 
PRO HB3  H N N 322 
PRO HG2  H N N 323 
PRO HG3  H N N 324 
PRO HD2  H N N 325 
PRO HD3  H N N 326 
PRO HXT  H N N 327 
SER N    N N N 328 
SER CA   C N S 329 
SER C    C N N 330 
SER O    O N N 331 
SER CB   C N N 332 
SER OG   O N N 333 
SER OXT  O N N 334 
SER H    H N N 335 
SER H2   H N N 336 
SER HA   H N N 337 
SER HB2  H N N 338 
SER HB3  H N N 339 
SER HG   H N N 340 
SER HXT  H N N 341 
THR N    N N N 342 
THR CA   C N S 343 
THR C    C N N 344 
THR O    O N N 345 
THR CB   C N R 346 
THR OG1  O N N 347 
THR CG2  C N N 348 
THR OXT  O N N 349 
THR H    H N N 350 
THR H2   H N N 351 
THR HA   H N N 352 
THR HB   H N N 353 
THR HG1  H N N 354 
THR HG21 H N N 355 
THR HG22 H N N 356 
THR HG23 H N N 357 
THR HXT  H N N 358 
TRP N    N N N 359 
TRP CA   C N S 360 
TRP C    C N N 361 
TRP O    O N N 362 
TRP CB   C N N 363 
TRP CG   C Y N 364 
TRP CD1  C Y N 365 
TRP CD2  C Y N 366 
TRP NE1  N Y N 367 
TRP CE2  C Y N 368 
TRP CE3  C Y N 369 
TRP CZ2  C Y N 370 
TRP CZ3  C Y N 371 
TRP CH2  C Y N 372 
TRP OXT  O N N 373 
TRP H    H N N 374 
TRP H2   H N N 375 
TRP HA   H N N 376 
TRP HB2  H N N 377 
TRP HB3  H N N 378 
TRP HD1  H N N 379 
TRP HE1  H N N 380 
TRP HE3  H N N 381 
TRP HZ2  H N N 382 
TRP HZ3  H N N 383 
TRP HH2  H N N 384 
TRP HXT  H N N 385 
TYR N    N N N 386 
TYR CA   C N S 387 
TYR C    C N N 388 
TYR O    O N N 389 
TYR CB   C N N 390 
TYR CG   C Y N 391 
TYR CD1  C Y N 392 
TYR CD2  C Y N 393 
TYR CE1  C Y N 394 
TYR CE2  C Y N 395 
TYR CZ   C Y N 396 
TYR OH   O N N 397 
TYR OXT  O N N 398 
TYR H    H N N 399 
TYR H2   H N N 400 
TYR HA   H N N 401 
TYR HB2  H N N 402 
TYR HB3  H N N 403 
TYR HD1  H N N 404 
TYR HD2  H N N 405 
TYR HE1  H N N 406 
TYR HE2  H N N 407 
TYR HH   H N N 408 
TYR HXT  H N N 409 
VAL N    N N N 410 
VAL CA   C N S 411 
VAL C    C N N 412 
VAL O    O N N 413 
VAL CB   C N N 414 
VAL CG1  C N N 415 
VAL CG2  C N N 416 
VAL OXT  O N N 417 
VAL H    H N N 418 
VAL H2   H N N 419 
VAL HA   H N N 420 
VAL HB   H N N 421 
VAL HG11 H N N 422 
VAL HG12 H N N 423 
VAL HG13 H N N 424 
VAL HG21 H N N 425 
VAL HG22 H N N 426 
VAL HG23 H N N 427 
VAL HXT  H N N 428 
# 
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 
GOL C1  O1   sing N N 153 
GOL C1  C2   sing N N 154 
GOL C1  H11  sing N N 155 
GOL C1  H12  sing N N 156 
GOL O1  HO1  sing N N 157 
GOL C2  O2   sing N N 158 
GOL C2  C3   sing N N 159 
GOL C2  H2   sing N N 160 
GOL O2  HO2  sing N N 161 
GOL C3  O3   sing N N 162 
GOL C3  H31  sing N N 163 
GOL C3  H32  sing N N 164 
GOL O3  HO3  sing N N 165 
HIS N   CA   sing N N 166 
HIS N   H    sing N N 167 
HIS N   H2   sing N N 168 
HIS CA  C    sing N N 169 
HIS CA  CB   sing N N 170 
HIS CA  HA   sing N N 171 
HIS C   O    doub N N 172 
HIS C   OXT  sing N N 173 
HIS CB  CG   sing N N 174 
HIS CB  HB2  sing N N 175 
HIS CB  HB3  sing N N 176 
HIS CG  ND1  sing Y N 177 
HIS CG  CD2  doub Y N 178 
HIS ND1 CE1  doub Y N 179 
HIS ND1 HD1  sing N N 180 
HIS CD2 NE2  sing Y N 181 
HIS CD2 HD2  sing N N 182 
HIS CE1 NE2  sing Y N 183 
HIS CE1 HE1  sing N N 184 
HIS NE2 HE2  sing N N 185 
HIS OXT HXT  sing N N 186 
HOH O   H1   sing N N 187 
HOH O   H2   sing N N 188 
ILE N   CA   sing N N 189 
ILE N   H    sing N N 190 
ILE N   H2   sing N N 191 
ILE CA  C    sing N N 192 
ILE CA  CB   sing N N 193 
ILE CA  HA   sing N N 194 
ILE C   O    doub N N 195 
ILE C   OXT  sing N N 196 
ILE CB  CG1  sing N N 197 
ILE CB  CG2  sing N N 198 
ILE CB  HB   sing N N 199 
ILE CG1 CD1  sing N N 200 
ILE CG1 HG12 sing N N 201 
ILE CG1 HG13 sing N N 202 
ILE CG2 HG21 sing N N 203 
ILE CG2 HG22 sing N N 204 
ILE CG2 HG23 sing N N 205 
ILE CD1 HD11 sing N N 206 
ILE CD1 HD12 sing N N 207 
ILE CD1 HD13 sing N N 208 
ILE OXT HXT  sing N N 209 
LEU N   CA   sing N N 210 
LEU N   H    sing N N 211 
LEU N   H2   sing N N 212 
LEU CA  C    sing N N 213 
LEU CA  CB   sing N N 214 
LEU CA  HA   sing N N 215 
LEU C   O    doub N N 216 
LEU C   OXT  sing N N 217 
LEU CB  CG   sing N N 218 
LEU CB  HB2  sing N N 219 
LEU CB  HB3  sing N N 220 
LEU CG  CD1  sing N N 221 
LEU CG  CD2  sing N N 222 
LEU CG  HG   sing N N 223 
LEU CD1 HD11 sing N N 224 
LEU CD1 HD12 sing N N 225 
LEU CD1 HD13 sing N N 226 
LEU CD2 HD21 sing N N 227 
LEU CD2 HD22 sing N N 228 
LEU CD2 HD23 sing N N 229 
LEU OXT HXT  sing N N 230 
LYS N   CA   sing N N 231 
LYS N   H    sing N N 232 
LYS N   H2   sing N N 233 
LYS CA  C    sing N N 234 
LYS CA  CB   sing N N 235 
LYS CA  HA   sing N N 236 
LYS C   O    doub N N 237 
LYS C   OXT  sing N N 238 
LYS CB  CG   sing N N 239 
LYS CB  HB2  sing N N 240 
LYS CB  HB3  sing N N 241 
LYS CG  CD   sing N N 242 
LYS CG  HG2  sing N N 243 
LYS CG  HG3  sing N N 244 
LYS CD  CE   sing N N 245 
LYS CD  HD2  sing N N 246 
LYS CD  HD3  sing N N 247 
LYS CE  NZ   sing N N 248 
LYS CE  HE2  sing N N 249 
LYS CE  HE3  sing N N 250 
LYS NZ  HZ1  sing N N 251 
LYS NZ  HZ2  sing N N 252 
LYS NZ  HZ3  sing N N 253 
LYS OXT HXT  sing N N 254 
MET N   CA   sing N N 255 
MET N   H    sing N N 256 
MET N   H2   sing N N 257 
MET CA  C    sing N N 258 
MET CA  CB   sing N N 259 
MET CA  HA   sing N N 260 
MET C   O    doub N N 261 
MET C   OXT  sing N N 262 
MET CB  CG   sing N N 263 
MET CB  HB2  sing N N 264 
MET CB  HB3  sing N N 265 
MET CG  SD   sing N N 266 
MET CG  HG2  sing N N 267 
MET CG  HG3  sing N N 268 
MET SD  CE   sing N N 269 
MET CE  HE1  sing N N 270 
MET CE  HE2  sing N N 271 
MET CE  HE3  sing N N 272 
MET OXT HXT  sing N N 273 
PHE N   CA   sing N N 274 
PHE N   H    sing N N 275 
PHE N   H2   sing N N 276 
PHE CA  C    sing N N 277 
PHE CA  CB   sing N N 278 
PHE CA  HA   sing N N 279 
PHE C   O    doub N N 280 
PHE C   OXT  sing N N 281 
PHE CB  CG   sing N N 282 
PHE CB  HB2  sing N N 283 
PHE CB  HB3  sing N N 284 
PHE CG  CD1  doub Y N 285 
PHE CG  CD2  sing Y N 286 
PHE CD1 CE1  sing Y N 287 
PHE CD1 HD1  sing N N 288 
PHE CD2 CE2  doub Y N 289 
PHE CD2 HD2  sing N N 290 
PHE CE1 CZ   doub Y N 291 
PHE CE1 HE1  sing N N 292 
PHE CE2 CZ   sing Y N 293 
PHE CE2 HE2  sing N N 294 
PHE CZ  HZ   sing N N 295 
PHE OXT HXT  sing N N 296 
PRO N   CA   sing N N 297 
PRO N   CD   sing N N 298 
PRO N   H    sing N N 299 
PRO CA  C    sing N N 300 
PRO CA  CB   sing N N 301 
PRO CA  HA   sing N N 302 
PRO C   O    doub N N 303 
PRO C   OXT  sing N N 304 
PRO CB  CG   sing N N 305 
PRO CB  HB2  sing N N 306 
PRO CB  HB3  sing N N 307 
PRO CG  CD   sing N N 308 
PRO CG  HG2  sing N N 309 
PRO CG  HG3  sing N N 310 
PRO CD  HD2  sing N N 311 
PRO CD  HD3  sing N N 312 
PRO OXT HXT  sing N N 313 
SER N   CA   sing N N 314 
SER N   H    sing N N 315 
SER N   H2   sing N N 316 
SER CA  C    sing N N 317 
SER CA  CB   sing N N 318 
SER CA  HA   sing N N 319 
SER C   O    doub N N 320 
SER C   OXT  sing N N 321 
SER CB  OG   sing N N 322 
SER CB  HB2  sing N N 323 
SER CB  HB3  sing N N 324 
SER OG  HG   sing N N 325 
SER OXT HXT  sing N N 326 
THR N   CA   sing N N 327 
THR N   H    sing N N 328 
THR N   H2   sing N N 329 
THR CA  C    sing N N 330 
THR CA  CB   sing N N 331 
THR CA  HA   sing N N 332 
THR C   O    doub N N 333 
THR C   OXT  sing N N 334 
THR CB  OG1  sing N N 335 
THR CB  CG2  sing N N 336 
THR CB  HB   sing N N 337 
THR OG1 HG1  sing N N 338 
THR CG2 HG21 sing N N 339 
THR CG2 HG22 sing N N 340 
THR CG2 HG23 sing N N 341 
THR OXT HXT  sing N N 342 
TRP N   CA   sing N N 343 
TRP N   H    sing N N 344 
TRP N   H2   sing N N 345 
TRP CA  C    sing N N 346 
TRP CA  CB   sing N N 347 
TRP CA  HA   sing N N 348 
TRP C   O    doub N N 349 
TRP C   OXT  sing N N 350 
TRP CB  CG   sing N N 351 
TRP CB  HB2  sing N N 352 
TRP CB  HB3  sing N N 353 
TRP CG  CD1  doub Y N 354 
TRP CG  CD2  sing Y N 355 
TRP CD1 NE1  sing Y N 356 
TRP CD1 HD1  sing N N 357 
TRP CD2 CE2  doub Y N 358 
TRP CD2 CE3  sing Y N 359 
TRP NE1 CE2  sing Y N 360 
TRP NE1 HE1  sing N N 361 
TRP CE2 CZ2  sing Y N 362 
TRP CE3 CZ3  doub Y N 363 
TRP CE3 HE3  sing N N 364 
TRP CZ2 CH2  doub Y N 365 
TRP CZ2 HZ2  sing N N 366 
TRP CZ3 CH2  sing Y N 367 
TRP CZ3 HZ3  sing N N 368 
TRP CH2 HH2  sing N N 369 
TRP OXT HXT  sing N N 370 
TYR N   CA   sing N N 371 
TYR N   H    sing N N 372 
TYR N   H2   sing N N 373 
TYR CA  C    sing N N 374 
TYR CA  CB   sing N N 375 
TYR CA  HA   sing N N 376 
TYR C   O    doub N N 377 
TYR C   OXT  sing N N 378 
TYR CB  CG   sing N N 379 
TYR CB  HB2  sing N N 380 
TYR CB  HB3  sing N N 381 
TYR CG  CD1  doub Y N 382 
TYR CG  CD2  sing Y N 383 
TYR CD1 CE1  sing Y N 384 
TYR CD1 HD1  sing N N 385 
TYR CD2 CE2  doub Y N 386 
TYR CD2 HD2  sing N N 387 
TYR CE1 CZ   doub Y N 388 
TYR CE1 HE1  sing N N 389 
TYR CE2 CZ   sing Y N 390 
TYR CE2 HE2  sing N N 391 
TYR CZ  OH   sing N N 392 
TYR OH  HH   sing N N 393 
TYR OXT HXT  sing N N 394 
VAL N   CA   sing N N 395 
VAL N   H    sing N N 396 
VAL N   H2   sing N N 397 
VAL CA  C    sing N N 398 
VAL CA  CB   sing N N 399 
VAL CA  HA   sing N N 400 
VAL C   O    doub N N 401 
VAL C   OXT  sing N N 402 
VAL CB  CG1  sing N N 403 
VAL CB  CG2  sing N N 404 
VAL CB  HB   sing N N 405 
VAL CG1 HG11 sing N N 406 
VAL CG1 HG12 sing N N 407 
VAL CG1 HG13 sing N N 408 
VAL CG2 HG21 sing N N 409 
VAL CG2 HG22 sing N N 410 
VAL CG2 HG23 sing N N 411 
VAL OXT HXT  sing N N 412 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 GLC 1 n 
2 GLC 2 n 
2 GLC 3 n 
2 GLC 4 n 
2 GLC 5 n 
2 GLC 6 n 
2 GLC 7 n 
3 GLC 1 n 
3 GLC 2 n 
3 GLC 3 n 
3 GLC 4 n 
3 GLC 5 n 
3 GLC 6 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                    9JLW 
_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]   0.016281 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001277 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024301 
_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]   0.005192 
_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 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LYS A 1 2   ? -0.609  17.463 35.875  1.00 34.95  ? 2   LYS A N   1 
ATOM   2    C CA  . LYS A 1 2   ? 0.205   17.749 37.054  1.00 39.23  ? 2   LYS A CA  1 
ATOM   3    C C   . LYS A 1 2   ? -0.677  17.984 38.278  1.00 32.87  ? 2   LYS A C   1 
ATOM   4    O O   . LYS A 1 2   ? -1.537  18.861 38.273  1.00 35.59  ? 2   LYS A O   1 
ATOM   5    C CB  . LYS A 1 2   ? 1.104   18.968 36.812  1.00 42.83  ? 2   LYS A CB  1 
ATOM   6    C CG  . LYS A 1 2   ? 2.146   19.198 37.900  1.00 43.16  ? 2   LYS A CG  1 
ATOM   7    C CD  . LYS A 1 2   ? 3.074   20.357 37.553  1.00 50.11  ? 2   LYS A CD  1 
ATOM   8    C CE  . LYS A 1 2   ? 2.383   21.702 37.741  1.00 54.41  ? 2   LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 2   ? 3.282   22.852 37.404  1.00 53.78  ? 2   LYS A NZ  1 
ATOM   10   N N   . LYS A 1 3   ? -0.461  17.197 39.324  1.00 27.13  ? 3   LYS A N   1 
ATOM   11   C CA  . LYS A 1 3   ? -1.236  17.315 40.549  1.00 25.37  ? 3   LYS A CA  1 
ATOM   12   C C   . LYS A 1 3   ? -0.375  17.896 41.662  1.00 24.62  ? 3   LYS A C   1 
ATOM   13   O O   . LYS A 1 3   ? 0.860   17.835 41.630  1.00 22.69  ? 3   LYS A O   1 
ATOM   14   C CB  . LYS A 1 3   ? -1.793  15.957 41.004  1.00 24.26  ? 3   LYS A CB  1 
ATOM   15   C CG  . LYS A 1 3   ? -2.569  15.206 39.928  1.00 36.87  ? 3   LYS A CG  1 
ATOM   16   C CD  . LYS A 1 3   ? -4.049  15.541 39.971  1.00 44.69  ? 3   LYS A CD  1 
ATOM   17   C CE  . LYS A 1 3   ? -4.898  14.274 39.993  1.00 50.97  ? 3   LYS A CE  1 
ATOM   18   N NZ  . LYS A 1 3   ? -6.360  14.566 40.064  1.00 55.68  ? 3   LYS A NZ  1 
ATOM   19   N N   . LEU A 1 4   ? -1.050  18.470 42.645  1.00 24.01  ? 4   LEU A N   1 
ATOM   20   C CA  . LEU A 1 4   ? -0.448  18.789 43.928  1.00 22.03  ? 4   LEU A CA  1 
ATOM   21   C C   . LEU A 1 4   ? -0.925  17.742 44.919  1.00 19.63  ? 4   LEU A C   1 
ATOM   22   O O   . LEU A 1 4   ? -2.132  17.497 45.032  1.00 24.20  ? 4   LEU A O   1 
ATOM   23   C CB  . LEU A 1 4   ? -0.837  20.190 44.392  1.00 20.19  ? 4   LEU A CB  1 
ATOM   24   C CG  . LEU A 1 4   ? -0.263  20.613 45.747  1.00 25.14  ? 4   LEU A CG  1 
ATOM   25   C CD1 . LEU A 1 4   ? 0.008   22.129 45.753  1.00 23.07  ? 4   LEU A CD1 1 
ATOM   26   C CD2 . LEU A 1 4   ? -1.207  20.222 46.898  1.00 22.21  ? 4   LEU A CD2 1 
ATOM   27   N N   . PHE A 1 5   ? 0.010   17.106 45.611  1.00 19.39  ? 5   PHE A N   1 
ATOM   28   C CA  . PHE A 1 5   ? -0.329  16.068 46.574  1.00 22.80  ? 5   PHE A CA  1 
ATOM   29   C C   . PHE A 1 5   ? -0.385  16.682 47.964  1.00 21.51  ? 5   PHE A C   1 
ATOM   30   O O   . PHE A 1 5   ? 0.586   17.287 48.421  1.00 25.13  ? 5   PHE A O   1 
ATOM   31   C CB  . PHE A 1 5   ? 0.671   14.913 46.516  1.00 20.58  ? 5   PHE A CB  1 
ATOM   32   C CG  . PHE A 1 5   ? 0.663   14.181 45.194  1.00 24.67  ? 5   PHE A CG  1 
ATOM   33   C CD1 . PHE A 1 5   ? -0.528  13.738 44.640  1.00 27.48  ? 5   PHE A CD1 1 
ATOM   34   C CD2 . PHE A 1 5   ? 1.844   13.963 44.497  1.00 28.48  ? 5   PHE A CD2 1 
ATOM   35   C CE1 . PHE A 1 5   ? -0.543  13.085 43.413  1.00 28.90  ? 5   PHE A CE1 1 
ATOM   36   C CE2 . PHE A 1 5   ? 1.838   13.303 43.282  1.00 32.43  ? 5   PHE A CE2 1 
ATOM   37   C CZ  . PHE A 1 5   ? 0.646   12.867 42.733  1.00 29.34  ? 5   PHE A CZ  1 
ATOM   38   N N   . LEU A 1 6   ? -1.523  16.527 48.626  1.00 18.09  ? 6   LEU A N   1 
ATOM   39   C CA  . LEU A 1 6   ? -1.766  17.119 49.928  1.00 15.04  ? 6   LEU A CA  1 
ATOM   40   C C   . LEU A 1 6   ? -1.948  16.009 50.955  1.00 19.94  ? 6   LEU A C   1 
ATOM   41   O O   . LEU A 1 6   ? -2.705  15.060 50.722  1.00 20.78  ? 6   LEU A O   1 
ATOM   42   C CB  . LEU A 1 6   ? -3.001  18.023 49.875  1.00 19.06  ? 6   LEU A CB  1 
ATOM   43   C CG  . LEU A 1 6   ? -3.385  18.819 51.115  1.00 15.36  ? 6   LEU A CG  1 
ATOM   44   C CD1 . LEU A 1 6   ? -2.217  19.616 51.654  1.00 26.76  ? 6   LEU A CD1 1 
ATOM   45   C CD2 . LEU A 1 6   ? -4.591  19.726 50.766  1.00 20.92  ? 6   LEU A CD2 1 
ATOM   46   N N   . VAL A 1 7   ? -1.258  16.123 52.086  1.00 17.39  ? 7   VAL A N   1 
ATOM   47   C CA  . VAL A 1 7   ? -1.286  15.093 53.120  1.00 20.59  ? 7   VAL A CA  1 
ATOM   48   C C   . VAL A 1 7   ? -1.615  15.761 54.452  1.00 19.11  ? 7   VAL A C   1 
ATOM   49   O O   . VAL A 1 7   ? -0.778  16.478 55.014  1.00 23.93  ? 7   VAL A O   1 
ATOM   50   C CB  . VAL A 1 7   ? 0.037   14.323 53.212  1.00 22.88  ? 7   VAL A CB  1 
ATOM   51   C CG1 . VAL A 1 7   ? -0.097  13.170 54.187  1.00 24.16  ? 7   VAL A CG1 1 
ATOM   52   C CG2 . VAL A 1 7   ? 0.448   13.812 51.850  1.00 22.31  ? 7   VAL A CG2 1 
ATOM   53   N N   . PHE A 1 8   ? -2.836  15.547 54.940  1.00 17.93  ? 8   PHE A N   1 
ATOM   54   C CA  . PHE A 1 8   ? -3.216  16.000 56.272  1.00 18.36  ? 8   PHE A CA  1 
ATOM   55   C C   . PHE A 1 8   ? -2.783  14.931 57.266  1.00 18.58  ? 8   PHE A C   1 
ATOM   56   O O   . PHE A 1 8   ? -2.994  13.740 57.029  1.00 18.84  ? 8   PHE A O   1 
ATOM   57   C CB  . PHE A 1 8   ? -4.732  16.238 56.374  1.00 18.01  ? 8   PHE A CB  1 
ATOM   58   C CG  . PHE A 1 8   ? -5.201  17.494 55.695  1.00 19.41  ? 8   PHE A CG  1 
ATOM   59   C CD1 . PHE A 1 8   ? -5.162  18.716 56.359  1.00 20.73  ? 8   PHE A CD1 1 
ATOM   60   C CD2 . PHE A 1 8   ? -5.674  17.461 54.388  1.00 22.69  ? 8   PHE A CD2 1 
ATOM   61   C CE1 . PHE A 1 8   ? -5.592  19.887 55.727  1.00 25.67  ? 8   PHE A CE1 1 
ATOM   62   C CE2 . PHE A 1 8   ? -6.103  18.623 53.751  1.00 20.80  ? 8   PHE A CE2 1 
ATOM   63   C CZ  . PHE A 1 8   ? -6.054  19.838 54.417  1.00 16.76  ? 8   PHE A CZ  1 
ATOM   64   N N   . TRP A 1 9   ? -2.168  15.347 58.365  1.00 17.11  ? 9   TRP A N   1 
ATOM   65   C CA  . TRP A 1 9   ? -1.767  14.406 59.415  1.00 24.47  ? 9   TRP A CA  1 
ATOM   66   C C   . TRP A 1 9   ? -2.095  15.069 60.752  1.00 20.28  ? 9   TRP A C   1 
ATOM   67   O O   . TRP A 1 9   ? -1.375  15.968 61.201  1.00 13.91  ? 9   TRP A O   1 
ATOM   68   C CB  . TRP A 1 9   ? -0.289  14.034 59.282  1.00 23.52  ? 9   TRP A CB  1 
ATOM   69   C CG  . TRP A 1 9   ? 0.166   12.797 60.037  1.00 18.78  ? 9   TRP A CG  1 
ATOM   70   C CD1 . TRP A 1 9   ? -0.546  12.071 60.943  1.00 15.85  ? 9   TRP A CD1 1 
ATOM   71   C CD2 . TRP A 1 9   ? 1.460   12.175 59.953  1.00 17.67  ? 9   TRP A CD2 1 
ATOM   72   N NE1 . TRP A 1 9   ? 0.232   11.036 61.436  1.00 15.10  ? 9   TRP A NE1 1 
ATOM   73   C CE2 . TRP A 1 9   ? 1.464   11.088 60.843  1.00 14.88  ? 9   TRP A CE2 1 
ATOM   74   C CE3 . TRP A 1 9   ? 2.622   12.448 59.219  1.00 19.56  ? 9   TRP A CE3 1 
ATOM   75   C CZ2 . TRP A 1 9   ? 2.573   10.249 60.993  1.00 20.61  ? 9   TRP A CZ2 1 
ATOM   76   C CZ3 . TRP A 1 9   ? 3.719   11.624 59.377  1.00 19.80  ? 9   TRP A CZ3 1 
ATOM   77   C CH2 . TRP A 1 9   ? 3.690   10.543 60.263  1.00 23.84  ? 9   TRP A CH2 1 
ATOM   78   N N   . TRP A 1 10  ? -3.210  14.640 61.356  1.00 17.87  ? 10  TRP A N   1 
ATOM   79   C CA  . TRP A 1 10  ? -3.723  15.190 62.609  1.00 15.67  ? 10  TRP A CA  1 
ATOM   80   C C   . TRP A 1 10  ? -3.162  14.386 63.784  1.00 18.26  ? 10  TRP A C   1 
ATOM   81   O O   . TRP A 1 10  ? -3.393  13.175 63.879  1.00 19.56  ? 10  TRP A O   1 
ATOM   82   C CB  . TRP A 1 10  ? -5.256  15.138 62.639  1.00 12.76  ? 10  TRP A CB  1 
ATOM   83   C CG  . TRP A 1 10  ? -5.936  15.866 61.506  1.00 16.01  ? 10  TRP A CG  1 
ATOM   84   C CD1 . TRP A 1 10  ? -6.575  15.312 60.432  1.00 15.96  ? 10  TRP A CD1 1 
ATOM   85   C CD2 . TRP A 1 10  ? -6.003  17.283 61.328  1.00 11.80  ? 10  TRP A CD2 1 
ATOM   86   N NE1 . TRP A 1 10  ? -7.060  16.306 59.610  1.00 23.07  ? 10  TRP A NE1 1 
ATOM   87   C CE2 . TRP A 1 10  ? -6.711  17.526 60.135  1.00 17.02  ? 10  TRP A CE2 1 
ATOM   88   C CE3 . TRP A 1 10  ? -5.540  18.370 62.071  1.00 15.31  ? 10  TRP A CE3 1 
ATOM   89   C CZ2 . TRP A 1 10  ? -6.971  18.817 59.668  1.00 19.16  ? 10  TRP A CZ2 1 
ATOM   90   C CZ3 . TRP A 1 10  ? -5.800  19.662 61.602  1.00 23.63  ? 10  TRP A CZ3 1 
ATOM   91   C CH2 . TRP A 1 10  ? -6.513  19.870 60.419  1.00 19.53  ? 10  TRP A CH2 1 
ATOM   92   N N   . HIS A 1 11  ? -2.487  15.061 64.707  1.00 14.95  ? 11  HIS A N   1 
ATOM   93   C CA  . HIS A 1 11  ? -1.849  14.400 65.839  1.00 14.81  ? 11  HIS A CA  1 
ATOM   94   C C   . HIS A 1 11  ? -2.731  14.530 67.080  1.00 19.27  ? 11  HIS A C   1 
ATOM   95   O O   . HIS A 1 11  ? -3.117  15.641 67.458  1.00 21.28  ? 11  HIS A O   1 
ATOM   96   C CB  . HIS A 1 11  ? -0.461  14.995 66.085  1.00 14.53  ? 11  HIS A CB  1 
ATOM   97   C CG  . HIS A 1 11  ? 0.104   14.678 67.433  1.00 19.70  ? 11  HIS A CG  1 
ATOM   98   N ND1 . HIS A 1 11  ? 0.400   13.394 67.835  1.00 19.13  ? 11  HIS A ND1 1 
ATOM   99   C CD2 . HIS A 1 11  ? 0.432   15.483 68.471  1.00 21.20  ? 11  HIS A CD2 1 
ATOM   100  C CE1 . HIS A 1 11  ? 0.889   13.421 69.061  1.00 21.48  ? 11  HIS A CE1 1 
ATOM   101  N NE2 . HIS A 1 11  ? 0.912   14.675 69.474  1.00 21.32  ? 11  HIS A NE2 1 
ATOM   102  N N   . MET A 1 12  ? -3.058  13.393 67.703  1.00 16.28  ? 12  MET A N   1 
ATOM   103  C CA  . MET A 1 12  ? -3.936  13.352 68.867  1.00 17.12  ? 12  MET A CA  1 
ATOM   104  C C   . MET A 1 12  ? -3.179  12.764 70.046  1.00 17.59  ? 12  MET A C   1 
ATOM   105  O O   . MET A 1 12  ? -2.651  11.652 69.952  1.00 21.06  ? 12  MET A O   1 
ATOM   106  C CB  . MET A 1 12  ? -5.193  12.509 68.594  1.00 14.17  ? 12  MET A CB  1 
ATOM   107  C CG  . MET A 1 12  ? -5.875  12.770 67.248  1.00 19.07  ? 12  MET A CG  1 
ATOM   108  S SD  . MET A 1 12  ? -6.577  14.420 67.144  1.00 19.94  ? 12  MET A SD  1 
ATOM   109  C CE  . MET A 1 12  ? -7.713  14.256 65.760  1.00 19.67  ? 12  MET A CE  1 
ATOM   110  N N   . HIS A 1 13  ? -3.168  13.485 71.162  1.00 16.80  ? 13  HIS A N   1 
ATOM   111  C CA  . HIS A 1 13  ? -2.408  13.059 72.324  1.00 19.06  ? 13  HIS A CA  1 
ATOM   112  C C   . HIS A 1 13  ? -2.993  13.683 73.577  1.00 13.91  ? 13  HIS A C   1 
ATOM   113  O O   . HIS A 1 13  ? -3.458  14.824 73.553  1.00 16.68  ? 13  HIS A O   1 
ATOM   114  C CB  . HIS A 1 13  ? -0.930  13.465 72.189  1.00 18.10  ? 13  HIS A CB  1 
ATOM   115  C CG  . HIS A 1 13  ? -0.151  13.345 73.464  1.00 21.51  ? 13  HIS A CG  1 
ATOM   116  N ND1 . HIS A 1 13  ? 0.018   12.144 74.125  1.00 18.24  ? 13  HIS A ND1 1 
ATOM   117  C CD2 . HIS A 1 13  ? 0.509   14.275 74.195  1.00 17.30  ? 13  HIS A CD2 1 
ATOM   118  C CE1 . HIS A 1 13  ? 0.741   12.345 75.213  1.00 20.29  ? 13  HIS A CE1 1 
ATOM   119  N NE2 . HIS A 1 13  ? 1.055   13.629 75.275  1.00 18.26  ? 13  HIS A NE2 1 
ATOM   120  N N   . GLN A 1 14  ? -2.934  12.937 74.680  1.00 14.81  ? 14  GLN A N   1 
ATOM   121  C CA  . GLN A 1 14  ? -3.165  13.479 76.012  1.00 11.47  ? 14  GLN A CA  1 
ATOM   122  C C   . GLN A 1 14  ? -2.193  12.753 76.926  1.00 14.14  ? 14  GLN A C   1 
ATOM   123  O O   . GLN A 1 14  ? -2.023  11.532 76.796  1.00 18.29  ? 14  GLN A O   1 
ATOM   124  C CB  . GLN A 1 14  ? -4.592  13.279 76.545  1.00 11.13  ? 14  GLN A CB  1 
ATOM   125  C CG  . GLN A 1 14  ? -5.653  13.984 75.748  1.00 12.75  ? 14  GLN A CG  1 
ATOM   126  C CD  . GLN A 1 14  ? -5.608  15.483 75.919  1.00 17.16  ? 14  GLN A CD  1 
ATOM   127  O OE1 . GLN A 1 14  ? -5.108  16.008 76.931  1.00 16.09  ? 14  GLN A OE1 1 
ATOM   128  N NE2 . GLN A 1 14  ? -6.148  16.190 74.931  1.00 15.82  ? 14  GLN A NE2 1 
ATOM   129  N N   . PRO A 1 15  ? -1.545  13.464 77.846  1.00 17.01  ? 15  PRO A N   1 
ATOM   130  C CA  . PRO A 1 15  ? -0.755  12.781 78.876  1.00 19.19  ? 15  PRO A CA  1 
ATOM   131  C C   . PRO A 1 15  ? -1.671  11.991 79.795  1.00 16.28  ? 15  PRO A C   1 
ATOM   132  O O   . PRO A 1 15  ? -2.891  12.158 79.783  1.00 17.67  ? 15  PRO A O   1 
ATOM   133  C CB  . PRO A 1 15  ? -0.051  13.917 79.619  1.00 13.08  ? 15  PRO A CB  1 
ATOM   134  C CG  . PRO A 1 15  ? -0.942  15.123 79.411  1.00 18.06  ? 15  PRO A CG  1 
ATOM   135  C CD  . PRO A 1 15  ? -1.560  14.929 78.020  1.00 17.47  ? 15  PRO A CD  1 
ATOM   136  N N   . LEU A 1 16  ? -1.068  11.119 80.609  1.00 14.38  ? 16  LEU A N   1 
ATOM   137  C CA  . LEU A 1 16  ? -1.853  10.276 81.508  1.00 20.65  ? 16  LEU A CA  1 
ATOM   138  C C   . LEU A 1 16  ? -2.356  11.122 82.672  1.00 24.05  ? 16  LEU A C   1 
ATOM   139  O O   . LEU A 1 16  ? -1.563  11.584 83.499  1.00 20.52  ? 16  LEU A O   1 
ATOM   140  C CB  . LEU A 1 16  ? -1.020  9.090  82.003  1.00 17.05  ? 16  LEU A CB  1 
ATOM   141  C CG  . LEU A 1 16  ? -1.765  8.114  82.920  1.00 20.68  ? 16  LEU A CG  1 
ATOM   142  C CD1 . LEU A 1 16  ? -2.980  7.536  82.193  1.00 21.93  ? 16  LEU A CD1 1 
ATOM   143  C CD2 . LEU A 1 16  ? -0.836  6.996  83.410  1.00 20.92  ? 16  LEU A CD2 1 
ATOM   144  N N   . TYR A 1 17  ? -3.677  11.336 82.743  1.00 21.87  ? 17  TYR A N   1 
ATOM   145  C CA  . TYR A 1 17  ? -4.253  12.146 83.810  1.00 17.77  ? 17  TYR A CA  1 
ATOM   146  C C   . TYR A 1 17  ? -4.615  11.325 85.032  1.00 23.89  ? 17  TYR A C   1 
ATOM   147  O O   . TYR A 1 17  ? -5.125  11.881 86.013  1.00 25.09  ? 17  TYR A O   1 
ATOM   148  C CB  . TYR A 1 17  ? -5.506  12.886 83.323  1.00 18.88  ? 17  TYR A CB  1 
ATOM   149  C CG  . TYR A 1 17  ? -5.242  13.917 82.262  1.00 16.51  ? 17  TYR A CG  1 
ATOM   150  C CD1 . TYR A 1 17  ? -4.524  15.078 82.552  1.00 17.75  ? 17  TYR A CD1 1 
ATOM   151  C CD2 . TYR A 1 17  ? -5.713  13.739 80.965  1.00 14.76  ? 17  TYR A CD2 1 
ATOM   152  C CE1 . TYR A 1 17  ? -4.283  16.034 81.571  1.00 17.32  ? 17  TYR A CE1 1 
ATOM   153  C CE2 . TYR A 1 17  ? -5.470  14.674 79.986  1.00 19.32  ? 17  TYR A CE2 1 
ATOM   154  C CZ  . TYR A 1 17  ? -4.754  15.816 80.285  1.00 17.45  ? 17  TYR A CZ  1 
ATOM   155  O OH  . TYR A 1 17  ? -4.520  16.730 79.290  1.00 22.58  ? 17  TYR A OH  1 
ATOM   156  N N   . ARG A 1 18  ? -4.367  10.026 84.992  1.00 22.86  ? 18  ARG A N   1 
ATOM   157  C CA  . ARG A 1 18  ? -4.832  9.106  86.020  1.00 23.43  ? 18  ARG A CA  1 
ATOM   158  C C   . ARG A 1 18  ? -3.791  9.029  87.131  1.00 22.65  ? 18  ARG A C   1 
ATOM   159  O O   . ARG A 1 18  ? -2.670  8.560  86.911  1.00 23.93  ? 18  ARG A O   1 
ATOM   160  C CB  . ARG A 1 18  ? -5.096  7.742  85.393  1.00 26.40  ? 18  ARG A CB  1 
ATOM   161  C CG  . ARG A 1 18  ? -5.623  6.683  86.348  1.00 28.64  ? 18  ARG A CG  1 
ATOM   162  C CD  . ARG A 1 18  ? -5.567  5.338  85.634  1.00 34.73  ? 18  ARG A CD  1 
ATOM   163  N NE  . ARG A 1 18  ? -6.344  4.315  86.314  1.00 34.44  ? 18  ARG A NE  1 
ATOM   164  C CZ  . ARG A 1 18  ? -5.874  3.567  87.304  1.00 34.64  ? 18  ARG A CZ  1 
ATOM   165  N NH1 . ARG A 1 18  ? -4.625  3.729  87.733  1.00 35.15  ? 18  ARG A NH1 1 
ATOM   166  N NH2 . ARG A 1 18  ? -6.652  2.656  87.863  1.00 35.29  ? 18  ARG A NH2 1 
ATOM   167  N N   . GLU A 1 19  ? -4.162  9.498  88.313  1.00 20.12  ? 19  GLU A N   1 
ATOM   168  C CA  . GLU A 1 19  ? -3.265  9.463  89.460  1.00 18.70  ? 19  GLU A CA  1 
ATOM   169  C C   . GLU A 1 19  ? -2.986  8.013  89.858  1.00 23.64  ? 19  GLU A C   1 
ATOM   170  O O   . GLU A 1 19  ? -3.929  7.241  90.072  1.00 22.52  ? 19  GLU A O   1 
ATOM   171  C CB  . GLU A 1 19  ? -3.879  10.239 90.623  1.00 24.31  ? 19  GLU A CB  1 
ATOM   172  C CG  . GLU A 1 19  ? -2.857  10.911 91.532  1.00 35.00  ? 19  GLU A CG  1 
ATOM   173  C CD  . GLU A 1 19  ? -2.458  10.032 92.702  1.00 43.43  ? 19  GLU A CD  1 
ATOM   174  O OE1 . GLU A 1 19  ? -3.141  9.015  92.931  1.00 41.33  ? 19  GLU A OE1 1 
ATOM   175  O OE2 . GLU A 1 19  ? -1.467  10.358 93.390  1.00 47.93  ? 19  GLU A OE2 1 
ATOM   176  N N   . PRO A 1 20  ? -1.717  7.612  89.983  1.00 26.41  ? 20  PRO A N   1 
ATOM   177  C CA  . PRO A 1 20  ? -1.405  6.178  90.120  1.00 32.24  ? 20  PRO A CA  1 
ATOM   178  C C   . PRO A 1 20  ? -1.839  5.560  91.433  1.00 32.66  ? 20  PRO A C   1 
ATOM   179  O O   . PRO A 1 20  ? -1.966  4.335  91.497  1.00 31.46  ? 20  PRO A O   1 
ATOM   180  C CB  . PRO A 1 20  ? 0.124   6.134  89.975  1.00 32.34  ? 20  PRO A CB  1 
ATOM   181  C CG  . PRO A 1 20  ? 0.584   7.512  90.361  1.00 24.55  ? 20  PRO A CG  1 
ATOM   182  C CD  . PRO A 1 20  ? -0.500  8.443  89.907  1.00 24.55  ? 20  PRO A CD  1 
ATOM   183  N N   . TYR A 1 21  ? -2.058  6.345  92.485  1.00 26.15  ? 21  TYR A N   1 
ATOM   184  C CA  . TYR A 1 21  ? -2.426  5.732  93.755  1.00 26.23  ? 21  TYR A CA  1 
ATOM   185  C C   . TYR A 1 21  ? -3.939  5.636  93.935  1.00 31.26  ? 21  TYR A C   1 
ATOM   186  O O   . TYR A 1 21  ? -4.450  4.603  94.375  1.00 33.22  ? 21  TYR A O   1 
ATOM   187  C CB  . TYR A 1 21  ? -1.787  6.511  94.902  1.00 27.16  ? 21  TYR A CB  1 
ATOM   188  C CG  . TYR A 1 21  ? -0.269  6.460  94.886  1.00 36.35  ? 21  TYR A CG  1 
ATOM   189  C CD1 . TYR A 1 21  ? 0.415   5.347  95.372  1.00 38.55  ? 21  TYR A CD1 1 
ATOM   190  C CD2 . TYR A 1 21  ? 0.482   7.518  94.373  1.00 36.32  ? 21  TYR A CD2 1 
ATOM   191  C CE1 . TYR A 1 21  ? 1.806   5.295  95.359  1.00 37.29  ? 21  TYR A CE1 1 
ATOM   192  C CE2 . TYR A 1 21  ? 1.874   7.475  94.359  1.00 33.29  ? 21  TYR A CE2 1 
ATOM   193  C CZ  . TYR A 1 21  ? 2.527   6.361  94.853  1.00 36.69  ? 21  TYR A CZ  1 
ATOM   194  O OH  . TYR A 1 21  ? 3.908   6.303  94.843  1.00 40.05  ? 21  TYR A OH  1 
ATOM   195  N N   . THR A 1 22  ? -4.668  6.704  93.612  1.00 30.82  ? 22  THR A N   1 
ATOM   196  C CA  . THR A 1 22  ? -6.121  6.697  93.731  1.00 29.77  ? 22  THR A CA  1 
ATOM   197  C C   . THR A 1 22  ? -6.812  6.184  92.477  1.00 30.59  ? 22  THR A C   1 
ATOM   198  O O   . THR A 1 22  ? -7.976  5.769  92.549  1.00 23.60  ? 22  THR A O   1 
ATOM   199  C CB  . THR A 1 22  ? -6.634  8.110  94.046  1.00 30.79  ? 22  THR A CB  1 
ATOM   200  O OG1 . THR A 1 22  ? -6.372  8.987  92.939  1.00 25.24  ? 22  THR A OG1 1 
ATOM   201  C CG2 . THR A 1 22  ? -5.946  8.664  95.277  1.00 26.55  ? 22  THR A CG2 1 
ATOM   202  N N   . GLY A 1 23  ? -6.128  6.205  91.335  1.00 24.81  ? 23  GLY A N   1 
ATOM   203  C CA  . GLY A 1 23  ? -6.766  5.861  90.082  1.00 25.92  ? 23  GLY A CA  1 
ATOM   204  C C   . GLY A 1 23  ? -7.715  6.906  89.547  1.00 31.39  ? 23  GLY A C   1 
ATOM   205  O O   . GLY A 1 23  ? -8.444  6.630  88.593  1.00 38.08  ? 23  GLY A O   1 
ATOM   206  N N   . GLU A 1 24  ? -7.736  8.097  90.132  1.00 24.26  ? 24  GLU A N   1 
ATOM   207  C CA  . GLU A 1 24  ? -8.648  9.151  89.707  1.00 20.98  ? 24  GLU A CA  1 
ATOM   208  C C   . GLU A 1 24  ? -8.060  9.929  88.537  1.00 26.92  ? 24  GLU A C   1 
ATOM   209  O O   . GLU A 1 24  ? -6.865  10.252 88.528  1.00 23.29  ? 24  GLU A O   1 
ATOM   210  C CB  . GLU A 1 24  ? -8.934  10.104 90.866  1.00 23.55  ? 24  GLU A CB  1 
ATOM   211  C CG  . GLU A 1 24  ? -9.474  9.402  92.108  1.00 31.89  ? 24  GLU A CG  1 
ATOM   212  C CD  . GLU A 1 24  ? -9.846  10.377 93.212  1.00 49.51  ? 24  GLU A CD  1 
ATOM   213  O OE1 . GLU A 1 24  ? -9.172  11.424 93.338  1.00 48.92  ? 24  GLU A OE1 1 
ATOM   214  O OE2 . GLU A 1 24  ? -10.822 10.100 93.947  1.00 60.51  ? 24  GLU A OE2 1 
ATOM   215  N N   . TYR A 1 25  ? -8.900  10.226 87.545  1.00 22.67  ? 25  TYR A N   1 
ATOM   216  C CA  . TYR A 1 25  ? -8.501  11.151 86.488  1.00 21.80  ? 25  TYR A CA  1 
ATOM   217  C C   . TYR A 1 25  ? -8.653  12.569 87.021  1.00 20.37  ? 25  TYR A C   1 
ATOM   218  O O   . TYR A 1 25  ? -9.773  13.034 87.267  1.00 21.74  ? 25  TYR A O   1 
ATOM   219  C CB  . TYR A 1 25  ? -9.321  10.934 85.226  1.00 20.40  ? 25  TYR A CB  1 
ATOM   220  C CG  . TYR A 1 25  ? -8.808  9.801  84.371  1.00 21.94  ? 25  TYR A CG  1 
ATOM   221  C CD1 . TYR A 1 25  ? -8.988  8.480  84.759  1.00 26.05  ? 25  TYR A CD1 1 
ATOM   222  C CD2 . TYR A 1 25  ? -8.133  10.051 83.174  1.00 26.29  ? 25  TYR A CD2 1 
ATOM   223  C CE1 . TYR A 1 25  ? -8.532  7.434  83.983  1.00 23.23  ? 25  TYR A CE1 1 
ATOM   224  C CE2 . TYR A 1 25  ? -7.667  9.009  82.390  1.00 25.74  ? 25  TYR A CE2 1 
ATOM   225  C CZ  . TYR A 1 25  ? -7.870  7.705  82.799  1.00 26.94  ? 25  TYR A CZ  1 
ATOM   226  O OH  . TYR A 1 25  ? -7.411  6.664  82.029  1.00 30.91  ? 25  TYR A OH  1 
ATOM   227  N N   . LEU A 1 26  ? -7.520  13.243 87.216  1.00 18.84  ? 26  LEU A N   1 
ATOM   228  C CA  . LEU A 1 26  ? -7.474  14.510 87.934  1.00 18.30  ? 26  LEU A CA  1 
ATOM   229  C C   . LEU A 1 26  ? -7.857  15.700 87.068  1.00 18.33  ? 26  LEU A C   1 
ATOM   230  O O   . LEU A 1 26  ? -8.150  16.769 87.609  1.00 22.80  ? 26  LEU A O   1 
ATOM   231  C CB  . LEU A 1 26  ? -6.067  14.725 88.515  1.00 20.71  ? 26  LEU A CB  1 
ATOM   232  C CG  . LEU A 1 26  ? -5.593  13.703 89.553  1.00 22.16  ? 26  LEU A CG  1 
ATOM   233  C CD1 . LEU A 1 26  ? -4.383  14.217 90.338  1.00 24.01  ? 26  LEU A CD1 1 
ATOM   234  C CD2 . LEU A 1 26  ? -6.722  13.309 90.510  1.00 24.50  ? 26  LEU A CD2 1 
ATOM   235  N N   . LEU A 1 27  ? -7.826  15.553 85.753  1.00 16.66  ? 27  LEU A N   1 
ATOM   236  C CA  . LEU A 1 27  ? -8.329  16.537 84.807  1.00 15.61  ? 27  LEU A CA  1 
ATOM   237  C C   . LEU A 1 27  ? -9.185  15.806 83.789  1.00 17.03  ? 27  LEU A C   1 
ATOM   238  O O   . LEU A 1 27  ? -8.984  14.611 83.554  1.00 21.36  ? 27  LEU A O   1 
ATOM   239  C CB  . LEU A 1 27  ? -7.199  17.294 84.083  1.00 14.12  ? 27  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 27  ? -6.287  18.188 84.930  1.00 20.36  ? 27  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 27  ? -5.061  18.618 84.126  1.00 21.84  ? 27  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 27  ? -7.031  19.401 85.438  1.00 22.77  ? 27  LEU A CD2 1 
ATOM   243  N N   . PRO A 1 28  ? -10.161 16.490 83.194  1.00 20.23  ? 28  PRO A N   1 
ATOM   244  C CA  . PRO A 1 28  ? -11.117 15.828 82.288  1.00 23.27  ? 28  PRO A CA  1 
ATOM   245  C C   . PRO A 1 28  ? -10.794 15.991 80.812  1.00 22.80  ? 28  PRO A C   1 
ATOM   246  O O   . PRO A 1 28  ? -11.672 15.719 79.984  1.00 22.05  ? 28  PRO A O   1 
ATOM   247  C CB  . PRO A 1 28  ? -12.420 16.557 82.623  1.00 20.83  ? 28  PRO A CB  1 
ATOM   248  C CG  . PRO A 1 28  ? -11.954 17.986 82.906  1.00 25.90  ? 28  PRO A CG  1 
ATOM   249  C CD  . PRO A 1 28  ? -10.580 17.861 83.545  1.00 23.95  ? 28  PRO A CD  1 
ATOM   250  N N   . TRP A 1 29  ? -9.579  16.419 80.479  1.00 14.44  ? 29  TRP A N   1 
ATOM   251  C CA  . TRP A 1 29  ? -9.299  16.834 79.109  1.00 17.36  ? 29  TRP A CA  1 
ATOM   252  C C   . TRP A 1 29  ? -9.376  15.675 78.129  1.00 17.79  ? 29  TRP A C   1 
ATOM   253  O O   . TRP A 1 29  ? -9.739  15.878 76.963  1.00 21.22  ? 29  TRP A O   1 
ATOM   254  C CB  . TRP A 1 29  ? -7.930  17.495 79.028  1.00 18.25  ? 29  TRP A CB  1 
ATOM   255  C CG  . TRP A 1 29  ? -7.785  18.771 79.824  1.00 25.57  ? 29  TRP A CG  1 
ATOM   256  C CD1 . TRP A 1 29  ? -6.798  19.063 80.721  1.00 24.65  ? 29  TRP A CD1 1 
ATOM   257  C CD2 . TRP A 1 29  ? -8.621  19.938 79.755  1.00 24.08  ? 29  TRP A CD2 1 
ATOM   258  N NE1 . TRP A 1 29  ? -6.971  20.332 81.222  1.00 26.20  ? 29  TRP A NE1 1 
ATOM   259  C CE2 . TRP A 1 29  ? -8.079  20.893 80.642  1.00 24.11  ? 29  TRP A CE2 1 
ATOM   260  C CE3 . TRP A 1 29  ? -9.762  20.272 79.019  1.00 21.23  ? 29  TRP A CE3 1 
ATOM   261  C CZ2 . TRP A 1 29  ? -8.646  22.154 80.821  1.00 24.22  ? 29  TRP A CZ2 1 
ATOM   262  C CZ3 . TRP A 1 29  ? -10.322 21.522 79.196  1.00 19.20  ? 29  TRP A CZ3 1 
ATOM   263  C CH2 . TRP A 1 29  ? -9.764  22.449 80.090  1.00 22.06  ? 29  TRP A CH2 1 
ATOM   264  N N   . THR A 1 30  ? -9.028  14.458 78.557  1.00 14.54  ? 30  THR A N   1 
ATOM   265  C CA  . THR A 1 30  ? -9.188  13.327 77.648  1.00 13.18  ? 30  THR A CA  1 
ATOM   266  C C   . THR A 1 30  ? -10.661 13.105 77.318  1.00 18.87  ? 30  THR A C   1 
ATOM   267  O O   . THR A 1 30  ? -11.023 12.915 76.151  1.00 22.56  ? 30  THR A O   1 
ATOM   268  C CB  . THR A 1 30  ? -8.548  12.071 78.238  1.00 16.23  ? 30  THR A CB  1 
ATOM   269  O OG1 . THR A 1 30  ? -7.129  12.252 78.307  1.00 18.18  ? 30  THR A OG1 1 
ATOM   270  C CG2 . THR A 1 30  ? -8.838  10.850 77.347  1.00 20.57  ? 30  THR A CG2 1 
ATOM   271  N N   . PHE A 1 31  ? -11.530 13.175 78.328  1.00 21.86  ? 31  PHE A N   1 
ATOM   272  C CA  . PHE A 1 31  ? -12.963 13.045 78.091  1.00 19.46  ? 31  PHE A CA  1 
ATOM   273  C C   . PHE A 1 31  ? -13.459 14.106 77.120  1.00 16.92  ? 31  PHE A C   1 
ATOM   274  O O   . PHE A 1 31  ? -14.140 13.798 76.135  1.00 21.75  ? 31  PHE A O   1 
ATOM   275  C CB  . PHE A 1 31  ? -13.726 13.149 79.416  1.00 16.48  ? 31  PHE A CB  1 
ATOM   276  C CG  . PHE A 1 31  ? -15.227 13.154 79.254  1.00 15.58  ? 31  PHE A CG  1 
ATOM   277  C CD1 . PHE A 1 31  ? -15.925 11.972 79.066  1.00 17.57  ? 31  PHE A CD1 1 
ATOM   278  C CD2 . PHE A 1 31  ? -15.937 14.338 79.293  1.00 23.14  ? 31  PHE A CD2 1 
ATOM   279  C CE1 . PHE A 1 31  ? -17.304 11.977 78.920  1.00 22.55  ? 31  PHE A CE1 1 
ATOM   280  C CE2 . PHE A 1 31  ? -17.310 14.337 79.141  1.00 25.55  ? 31  PHE A CE2 1 
ATOM   281  C CZ  . PHE A 1 31  ? -17.988 13.157 78.964  1.00 21.90  ? 31  PHE A CZ  1 
ATOM   282  N N   . PHE A 1 32  ? -13.132 15.373 77.383  1.00 21.97  ? 32  PHE A N   1 
ATOM   283  C CA  . PHE A 1 32  ? -13.703 16.449 76.582  1.00 18.06  ? 32  PHE A CA  1 
ATOM   284  C C   . PHE A 1 32  ? -13.168 16.430 75.159  1.00 18.22  ? 32  PHE A C   1 
ATOM   285  O O   . PHE A 1 32  ? -13.926 16.660 74.210  1.00 18.76  ? 32  PHE A O   1 
ATOM   286  C CB  . PHE A 1 32  ? -13.453 17.795 77.261  1.00 21.87  ? 32  PHE A CB  1 
ATOM   287  C CG  . PHE A 1 32  ? -14.387 18.071 78.413  1.00 24.96  ? 32  PHE A CG  1 
ATOM   288  C CD1 . PHE A 1 32  ? -15.760 17.970 78.246  1.00 24.56  ? 32  PHE A CD1 1 
ATOM   289  C CD2 . PHE A 1 32  ? -13.893 18.408 79.662  1.00 24.06  ? 32  PHE A CD2 1 
ATOM   290  C CE1 . PHE A 1 32  ? -16.620 18.211 79.290  1.00 18.58  ? 32  PHE A CE1 1 
ATOM   291  C CE2 . PHE A 1 32  ? -14.750 18.661 80.709  1.00 24.84  ? 32  PHE A CE2 1 
ATOM   292  C CZ  . PHE A 1 32  ? -16.114 18.562 80.525  1.00 21.44  ? 32  PHE A CZ  1 
ATOM   293  N N   . HIS A 1 33  ? -11.872 16.146 74.971  1.00 15.37  ? 33  HIS A N   1 
ATOM   294  C CA  . HIS A 1 33  ? -11.395 16.059 73.598  1.00 18.37  ? 33  HIS A CA  1 
ATOM   295  C C   . HIS A 1 33  ? -11.849 14.770 72.915  1.00 18.94  ? 33  HIS A C   1 
ATOM   296  O O   . HIS A 1 33  ? -11.970 14.743 71.689  1.00 19.02  ? 33  HIS A O   1 
ATOM   297  C CB  . HIS A 1 33  ? -9.865  16.247 73.551  1.00 12.54  ? 33  HIS A CB  1 
ATOM   298  C CG  . HIS A 1 33  ? -9.458  17.684 73.696  1.00 15.27  ? 33  HIS A CG  1 
ATOM   299  N ND1 . HIS A 1 33  ? -9.781  18.644 72.754  1.00 20.62  ? 33  HIS A ND1 1 
ATOM   300  C CD2 . HIS A 1 33  ? -8.859  18.348 74.715  1.00 17.31  ? 33  HIS A CD2 1 
ATOM   301  C CE1 . HIS A 1 33  ? -9.349  19.826 73.163  1.00 16.13  ? 33  HIS A CE1 1 
ATOM   302  N NE2 . HIS A 1 33  ? -8.789  19.673 74.349  1.00 15.65  ? 33  HIS A NE2 1 
ATOM   303  N N   . ALA A 1 34  ? -12.159 13.721 73.676  1.00 15.82  ? 34  ALA A N   1 
ATOM   304  C CA  . ALA A 1 34  ? -12.746 12.533 73.053  1.00 19.87  ? 34  ALA A CA  1 
ATOM   305  C C   . ALA A 1 34  ? -14.170 12.802 72.547  1.00 17.39  ? 34  ALA A C   1 
ATOM   306  O O   . ALA A 1 34  ? -14.511 12.438 71.414  1.00 18.85  ? 34  ALA A O   1 
ATOM   307  C CB  . ALA A 1 34  ? -12.720 11.359 74.036  1.00 16.96  ? 34  ALA A CB  1 
ATOM   308  N N   . VAL A 1 35  ? -15.010 13.461 73.342  1.00 17.46  ? 35  VAL A N   1 
ATOM   309  C CA  . VAL A 1 35  ? -16.383 13.679 72.879  1.00 20.13  ? 35  VAL A CA  1 
ATOM   310  C C   . VAL A 1 35  ? -16.443 14.750 71.797  1.00 24.23  ? 35  VAL A C   1 
ATOM   311  O O   . VAL A 1 35  ? -17.346 14.727 70.952  1.00 24.00  ? 35  VAL A O   1 
ATOM   312  C CB  . VAL A 1 35  ? -17.330 14.022 74.047  1.00 14.26  ? 35  VAL A CB  1 
ATOM   313  C CG1 . VAL A 1 35  ? -17.222 12.964 75.143  1.00 18.17  ? 35  VAL A CG1 1 
ATOM   314  C CG2 . VAL A 1 35  ? -17.073 15.443 74.581  1.00 18.91  ? 35  VAL A CG2 1 
ATOM   315  N N   . LYS A 1 36  ? -15.482 15.678 71.773  1.00 20.17  ? 36  LYS A N   1 
ATOM   316  C CA  . LYS A 1 36  ? -15.525 16.789 70.830  1.00 18.46  ? 36  LYS A CA  1 
ATOM   317  C C   . LYS A 1 36  ? -14.738 16.508 69.554  1.00 20.10  ? 36  LYS A C   1 
ATOM   318  O O   . LYS A 1 36  ? -15.223 16.813 68.458  1.00 17.27  ? 36  LYS A O   1 
ATOM   319  C CB  . LYS A 1 36  ? -14.999 18.077 71.495  1.00 20.24  ? 36  LYS A CB  1 
ATOM   320  C CG  . LYS A 1 36  ? -15.110 19.366 70.612  1.00 16.43  ? 36  LYS A CG  1 
ATOM   321  C CD  . LYS A 1 36  ? -14.733 20.674 71.350  1.00 16.03  ? 36  LYS A CD  1 
ATOM   322  C CE  . LYS A 1 36  ? -13.223 20.932 71.359  1.00 17.10  ? 36  LYS A CE  1 
ATOM   323  N NZ  . LYS A 1 36  ? -12.694 21.220 69.987  1.00 15.05  ? 36  LYS A NZ  1 
ATOM   324  N N   . ASP A 1 37  ? -13.528 15.935 69.667  1.00 20.65  ? 37  ASP A N   1 
ATOM   325  C CA  . ASP A 1 37  ? -12.588 15.890 68.544  1.00 21.22  ? 37  ASP A CA  1 
ATOM   326  C C   . ASP A 1 37  ? -12.131 14.494 68.132  1.00 15.18  ? 37  ASP A C   1 
ATOM   327  O O   . ASP A 1 37  ? -11.980 14.237 66.938  1.00 19.55  ? 37  ASP A O   1 
ATOM   328  C CB  . ASP A 1 37  ? -11.345 16.739 68.877  1.00 18.79  ? 37  ASP A CB  1 
ATOM   329  C CG  . ASP A 1 37  ? -11.703 18.084 69.483  1.00 19.57  ? 37  ASP A CG  1 
ATOM   330  O OD1 . ASP A 1 37  ? -12.325 18.922 68.781  1.00 18.58  ? 37  ASP A OD1 1 
ATOM   331  O OD2 . ASP A 1 37  ? -11.366 18.304 70.662  1.00 21.77  ? 37  ASP A OD2 1 
ATOM   332  N N   . TYR A 1 38  ? -11.926 13.568 69.068  1.00 13.55  ? 38  TYR A N   1 
ATOM   333  C CA  . TYR A 1 38  ? -11.230 12.334 68.703  1.00 11.36  ? 38  TYR A CA  1 
ATOM   334  C C   . TYR A 1 38  ? -12.088 11.393 67.862  1.00 16.16  ? 38  TYR A C   1 
ATOM   335  O O   . TYR A 1 38  ? -11.553 10.644 67.033  1.00 16.51  ? 38  TYR A O   1 
ATOM   336  C CB  . TYR A 1 38  ? -10.727 11.635 69.963  1.00 17.04  ? 38  TYR A CB  1 
ATOM   337  C CG  . TYR A 1 38  ? -9.591  12.388 70.638  1.00 19.79  ? 38  TYR A CG  1 
ATOM   338  C CD1 . TYR A 1 38  ? -8.699  13.147 69.898  1.00 19.48  ? 38  TYR A CD1 1 
ATOM   339  C CD2 . TYR A 1 38  ? -9.429  12.350 72.020  1.00 18.90  ? 38  TYR A CD2 1 
ATOM   340  C CE1 . TYR A 1 38  ? -7.661  13.836 70.520  1.00 24.42  ? 38  TYR A CE1 1 
ATOM   341  C CE2 . TYR A 1 38  ? -8.415  13.045 72.644  1.00 19.58  ? 38  TYR A CE2 1 
ATOM   342  C CZ  . TYR A 1 38  ? -7.529  13.773 71.895  1.00 18.75  ? 38  TYR A CZ  1 
ATOM   343  O OH  . TYR A 1 38  ? -6.516  14.449 72.530  1.00 22.31  ? 38  TYR A OH  1 
ATOM   344  N N   . TYR A 1 39  ? -13.406 11.383 68.076  1.00 16.28  ? 39  TYR A N   1 
ATOM   345  C CA  . TYR A 1 39  ? -14.290 10.705 67.140  1.00 13.12  ? 39  TYR A CA  1 
ATOM   346  C C   . TYR A 1 39  ? -14.551 11.557 65.901  1.00 16.67  ? 39  TYR A C   1 
ATOM   347  O O   . TYR A 1 39  ? -14.525 11.047 64.775  1.00 15.62  ? 39  TYR A O   1 
ATOM   348  C CB  . TYR A 1 39  ? -15.615 10.358 67.833  1.00 16.98  ? 39  TYR A CB  1 
ATOM   349  C CG  . TYR A 1 39  ? -16.619 9.701  66.909  1.00 19.21  ? 39  TYR A CG  1 
ATOM   350  C CD1 . TYR A 1 39  ? -16.537 8.341  66.620  1.00 17.14  ? 39  TYR A CD1 1 
ATOM   351  C CD2 . TYR A 1 39  ? -17.644 10.441 66.316  1.00 21.57  ? 39  TYR A CD2 1 
ATOM   352  C CE1 . TYR A 1 39  ? -17.439 7.726  65.770  1.00 21.87  ? 39  TYR A CE1 1 
ATOM   353  C CE2 . TYR A 1 39  ? -18.558 9.832  65.471  1.00 24.66  ? 39  TYR A CE2 1 
ATOM   354  C CZ  . TYR A 1 39  ? -18.451 8.479  65.199  1.00 25.80  ? 39  TYR A CZ  1 
ATOM   355  O OH  . TYR A 1 39  ? -19.359 7.873  64.358  1.00 32.98  ? 39  TYR A OH  1 
ATOM   356  N N   . ASP A 1 40  ? -14.784 12.861 66.085  1.00 13.93  ? 40  ASP A N   1 
ATOM   357  C CA  . ASP A 1 40  ? -15.391 13.655 65.025  1.00 15.73  ? 40  ASP A CA  1 
ATOM   358  C C   . ASP A 1 40  ? -14.395 14.030 63.931  1.00 15.02  ? 40  ASP A C   1 
ATOM   359  O O   . ASP A 1 40  ? -14.778 14.101 62.756  1.00 18.75  ? 40  ASP A O   1 
ATOM   360  C CB  . ASP A 1 40  ? -16.076 14.882 65.640  1.00 20.66  ? 40  ASP A CB  1 
ATOM   361  C CG  . ASP A 1 40  ? -17.480 14.546 66.190  1.00 25.90  ? 40  ASP A CG  1 
ATOM   362  O OD1 . ASP A 1 40  ? -18.395 14.366 65.364  1.00 21.58  ? 40  ASP A OD1 1 
ATOM   363  O OD2 . ASP A 1 40  ? -17.665 14.420 67.435  1.00 22.70  ? 40  ASP A OD2 1 
ATOM   364  N N   . MET A 1 41  ? -13.117 14.214 64.266  1.00 15.93  ? 41  MET A N   1 
ATOM   365  C CA  . MET A 1 41  ? -12.143 14.513 63.220  1.00 15.51  ? 41  MET A CA  1 
ATOM   366  C C   . MET A 1 41  ? -12.072 13.402 62.178  1.00 18.84  ? 41  MET A C   1 
ATOM   367  O O   . MET A 1 41  ? -12.281 13.697 60.989  1.00 16.91  ? 41  MET A O   1 
ATOM   368  C CB  . MET A 1 41  ? -10.787 14.843 63.854  1.00 10.89  ? 41  MET A CB  1 
ATOM   369  C CG  . MET A 1 41  ? -10.735 16.271 64.442  1.00 14.45  ? 41  MET A CG  1 
ATOM   370  S SD  . MET A 1 41  ? -10.756 17.566 63.170  1.00 16.06  ? 41  MET A SD  1 
ATOM   371  C CE  . MET A 1 41  ? -9.017  17.554 62.692  1.00 16.04  ? 41  MET A CE  1 
ATOM   372  N N   . PRO A 1 42  ? -11.861 12.126 62.529  1.00 18.94  ? 42  PRO A N   1 
ATOM   373  C CA  . PRO A 1 42  ? -11.965 11.075 61.492  1.00 17.78  ? 42  PRO A CA  1 
ATOM   374  C C   . PRO A 1 42  ? -13.372 10.888 60.925  1.00 13.79  ? 42  PRO A C   1 
ATOM   375  O O   . PRO A 1 42  ? -13.504 10.473 59.764  1.00 20.02  ? 42  PRO A O   1 
ATOM   376  C CB  . PRO A 1 42  ? -11.476 9.812  62.214  1.00 19.44  ? 42  PRO A CB  1 
ATOM   377  C CG  . PRO A 1 42  ? -11.684 10.093 63.661  1.00 16.74  ? 42  PRO A CG  1 
ATOM   378  C CD  . PRO A 1 42  ? -11.477 11.574 63.840  1.00 15.99  ? 42  PRO A CD  1 
ATOM   379  N N   . ALA A 1 43  ? -14.423 11.181 61.695  1.00 11.87  ? 43  ALA A N   1 
ATOM   380  C CA  . ALA A 1 43  ? -15.796 11.053 61.199  1.00 19.30  ? 43  ALA A CA  1 
ATOM   381  C C   . ALA A 1 43  ? -16.129 12.024 60.059  1.00 26.06  ? 43  ALA A C   1 
ATOM   382  O O   . ALA A 1 43  ? -17.137 11.810 59.371  1.00 26.40  ? 43  ALA A O   1 
ATOM   383  C CB  . ALA A 1 43  ? -16.804 11.246 62.347  1.00 19.71  ? 43  ALA A CB  1 
ATOM   384  N N   . TYR A 1 44  ? -15.323 13.070 59.826  1.00 22.47  ? 44  TYR A N   1 
ATOM   385  C CA  . TYR A 1 44  ? -15.496 13.867 58.606  1.00 18.24  ? 44  TYR A CA  1 
ATOM   386  C C   . TYR A 1 44  ? -15.359 13.008 57.350  1.00 22.46  ? 44  TYR A C   1 
ATOM   387  O O   . TYR A 1 44  ? -15.964 13.318 56.313  1.00 20.16  ? 44  TYR A O   1 
ATOM   388  C CB  . TYR A 1 44  ? -14.474 15.005 58.539  1.00 17.65  ? 44  TYR A CB  1 
ATOM   389  C CG  . TYR A 1 44  ? -14.837 16.256 59.311  1.00 17.27  ? 44  TYR A CG  1 
ATOM   390  C CD1 . TYR A 1 44  ? -15.588 17.276 58.720  1.00 19.88  ? 44  TYR A CD1 1 
ATOM   391  C CD2 . TYR A 1 44  ? -14.423 16.423 60.624  1.00 12.41  ? 44  TYR A CD2 1 
ATOM   392  C CE1 . TYR A 1 44  ? -15.918 18.423 59.426  1.00 18.15  ? 44  TYR A CE1 1 
ATOM   393  C CE2 . TYR A 1 44  ? -14.747 17.561 61.341  1.00 19.95  ? 44  TYR A CE2 1 
ATOM   394  C CZ  . TYR A 1 44  ? -15.485 18.564 60.733  1.00 21.94  ? 44  TYR A CZ  1 
ATOM   395  O OH  . TYR A 1 44  ? -15.807 19.686 61.459  1.00 28.25  ? 44  TYR A OH  1 
ATOM   396  N N   . LEU A 1 45  ? -14.565 11.934 57.415  1.00 21.94  ? 45  LEU A N   1 
ATOM   397  C CA  . LEU A 1 45  ? -14.356 11.083 56.249  1.00 19.05  ? 45  LEU A CA  1 
ATOM   398  C C   . LEU A 1 45  ? -15.619 10.345 55.824  1.00 22.34  ? 45  LEU A C   1 
ATOM   399  O O   . LEU A 1 45  ? -15.654 9.794  54.715  1.00 22.81  ? 45  LEU A O   1 
ATOM   400  C CB  . LEU A 1 45  ? -13.230 10.087 56.526  1.00 21.00  ? 45  LEU A CB  1 
ATOM   401  C CG  . LEU A 1 45  ? -11.861 10.755 56.753  1.00 21.70  ? 45  LEU A CG  1 
ATOM   402  C CD1 . LEU A 1 45  ? -10.884 9.771  57.348  1.00 17.80  ? 45  LEU A CD1 1 
ATOM   403  C CD2 . LEU A 1 45  ? -11.319 11.308 55.449  1.00 17.62  ? 45  LEU A CD2 1 
ATOM   404  N N   . LYS A 1 46  ? -16.651 10.318 56.661  1.00 24.44  ? 46  LYS A N   1 
ATOM   405  C CA  . LYS A 1 46  ? -17.916 9.724  56.247  1.00 30.26  ? 46  LYS A CA  1 
ATOM   406  C C   . LYS A 1 46  ? -18.706 10.627 55.313  1.00 32.45  ? 46  LYS A C   1 
ATOM   407  O O   . LYS A 1 46  ? -19.558 10.132 54.563  1.00 28.28  ? 46  LYS A O   1 
ATOM   408  C CB  . LYS A 1 46  ? -18.766 9.393  57.472  1.00 27.20  ? 46  LYS A CB  1 
ATOM   409  C CG  . LYS A 1 46  ? -17.977 8.695  58.556  1.00 37.92  ? 46  LYS A CG  1 
ATOM   410  C CD  . LYS A 1 46  ? -18.840 7.721  59.315  1.00 46.83  ? 46  LYS A CD  1 
ATOM   411  C CE  . LYS A 1 46  ? -19.950 8.442  60.024  1.00 50.00  ? 46  LYS A CE  1 
ATOM   412  N NZ  . LYS A 1 46  ? -20.292 7.754  61.296  1.00 54.06  ? 46  LYS A NZ  1 
ATOM   413  N N   . ASP A 1 47  ? -18.445 11.936 55.341  1.00 28.81  ? 47  ASP A N   1 
ATOM   414  C CA  . ASP A 1 47  ? -19.202 12.891 54.550  1.00 28.73  ? 47  ASP A CA  1 
ATOM   415  C C   . ASP A 1 47  ? -18.417 13.505 53.398  1.00 29.94  ? 47  ASP A C   1 
ATOM   416  O O   . ASP A 1 47  ? -19.032 14.082 52.499  1.00 32.49  ? 47  ASP A O   1 
ATOM   417  C CB  . ASP A 1 47  ? -19.734 14.016 55.455  1.00 32.52  ? 47  ASP A CB  1 
ATOM   418  C CG  . ASP A 1 47  ? -20.681 13.494 56.538  1.00 39.39  ? 47  ASP A CG  1 
ATOM   419  O OD1 . ASP A 1 47  ? -21.385 12.488 56.282  1.00 35.37  ? 47  ASP A OD1 1 
ATOM   420  O OD2 . ASP A 1 47  ? -20.716 14.071 57.643  1.00 38.41  ? 47  ASP A OD2 1 
ATOM   421  N N   . PHE A 1 48  ? -17.086 13.396 53.397  1.00 28.12  ? 48  PHE A N   1 
ATOM   422  C CA  . PHE A 1 48  ? -16.259 13.998 52.358  1.00 24.85  ? 48  PHE A CA  1 
ATOM   423  C C   . PHE A 1 48  ? -15.315 12.953 51.787  1.00 21.14  ? 48  PHE A C   1 
ATOM   424  O O   . PHE A 1 48  ? -14.660 12.230 52.544  1.00 23.18  ? 48  PHE A O   1 
ATOM   425  C CB  . PHE A 1 48  ? -15.477 15.194 52.915  1.00 22.36  ? 48  PHE A CB  1 
ATOM   426  C CG  . PHE A 1 48  ? -16.357 16.252 53.510  1.00 24.54  ? 48  PHE A CG  1 
ATOM   427  C CD1 . PHE A 1 48  ? -16.905 17.241 52.706  1.00 24.92  ? 48  PHE A CD1 1 
ATOM   428  C CD2 . PHE A 1 48  ? -16.671 16.233 54.858  1.00 22.09  ? 48  PHE A CD2 1 
ATOM   429  C CE1 . PHE A 1 48  ? -17.748 18.214 53.242  1.00 32.34  ? 48  PHE A CE1 1 
ATOM   430  C CE2 . PHE A 1 48  ? -17.509 17.194 55.410  1.00 28.65  ? 48  PHE A CE2 1 
ATOM   431  C CZ  . PHE A 1 48  ? -18.050 18.192 54.600  1.00 36.14  ? 48  PHE A CZ  1 
ATOM   432  N N   . GLU A 1 49  ? -15.235 12.885 50.451  1.00 17.68  ? 49  GLU A N   1 
ATOM   433  C CA  . GLU A 1 49  ? -14.393 11.894 49.776  1.00 29.44  ? 49  GLU A CA  1 
ATOM   434  C C   . GLU A 1 49  ? -12.999 12.489 49.596  1.00 33.87  ? 49  GLU A C   1 
ATOM   435  O O   . GLU A 1 49  ? -12.604 12.960 48.525  1.00 34.33  ? 49  GLU A O   1 
ATOM   436  C CB  . GLU A 1 49  ? -15.007 11.454 48.452  1.00 28.82  ? 49  GLU A CB  1 
ATOM   437  C CG  . GLU A 1 49  ? -16.150 10.447 48.618  1.00 46.29  ? 49  GLU A CG  1 
ATOM   438  C CD  . GLU A 1 49  ? -15.672 9.010  48.841  1.00 59.71  ? 49  GLU A CD  1 
ATOM   439  O OE1 . GLU A 1 49  ? -14.727 8.570  48.147  1.00 62.46  ? 49  GLU A OE1 1 
ATOM   440  O OE2 . GLU A 1 49  ? -16.250 8.317  49.711  1.00 64.61  ? 49  GLU A OE2 1 
ATOM   441  N N   . ILE A 1 50  ? -12.253 12.481 50.696  1.00 33.32  ? 50  ILE A N   1 
ATOM   442  C CA  . ILE A 1 50  ? -10.859 12.894 50.735  1.00 26.42  ? 50  ILE A CA  1 
ATOM   443  C C   . ILE A 1 50  ? -10.130 11.899 51.623  1.00 24.67  ? 50  ILE A C   1 
ATOM   444  O O   . ILE A 1 50  ? -10.748 11.090 52.317  1.00 26.36  ? 50  ILE A O   1 
ATOM   445  C CB  . ILE A 1 50  ? -10.689 14.319 51.289  1.00 23.43  ? 50  ILE A CB  1 
ATOM   446  C CG1 . ILE A 1 50  ? -11.328 14.398 52.678  1.00 24.70  ? 50  ILE A CG1 1 
ATOM   447  C CG2 . ILE A 1 50  ? -11.326 15.343 50.356  1.00 25.94  ? 50  ILE A CG2 1 
ATOM   448  C CD1 . ILE A 1 50  ? -11.022 15.657 53.424  1.00 24.96  ? 50  ILE A CD1 1 
ATOM   449  N N   . LYS A 1 51  ? -8.800  11.979 51.601  1.00 21.08  ? 51  LYS A N   1 
ATOM   450  C CA  . LYS A 1 51  ? -7.947  11.262 52.541  1.00 18.14  ? 51  LYS A CA  1 
ATOM   451  C C   . LYS A 1 51  ? -7.534  12.192 53.676  1.00 19.77  ? 51  LYS A C   1 
ATOM   452  O O   . LYS A 1 51  ? -7.157  13.348 53.434  1.00 21.84  ? 51  LYS A O   1 
ATOM   453  C CB  . LYS A 1 51  ? -6.697  10.725 51.841  1.00 13.85  ? 51  LYS A CB  1 
ATOM   454  C CG  . LYS A 1 51  ? -6.990  10.028 50.514  1.00 23.95  ? 51  LYS A CG  1 
ATOM   455  C CD  . LYS A 1 51  ? -7.777  8.732  50.729  1.00 26.35  ? 51  LYS A CD  1 
ATOM   456  C CE  . LYS A 1 51  ? -7.855  7.936  49.422  1.00 27.50  ? 51  LYS A CE  1 
ATOM   457  N NZ  . LYS A 1 51  ? -8.722  6.753  49.562  1.00 38.99  ? 51  LYS A NZ  1 
ATOM   458  N N   . LEU A 1 52  ? -7.597  11.679 54.913  1.00 16.51  ? 52  LEU A N   1 
ATOM   459  C CA  . LEU A 1 52  ? -7.098  12.357 56.112  1.00 17.94  ? 52  LEU A CA  1 
ATOM   460  C C   . LEU A 1 52  ? -6.402  11.319 56.985  1.00 22.14  ? 52  LEU A C   1 
ATOM   461  O O   . LEU A 1 52  ? -6.945  10.229 57.191  1.00 22.64  ? 52  LEU A O   1 
ATOM   462  C CB  . LEU A 1 52  ? -8.215  13.032 56.919  1.00 24.16  ? 52  LEU A CB  1 
ATOM   463  C CG  . LEU A 1 52  ? -9.051  14.176 56.325  1.00 21.79  ? 52  LEU A CG  1 
ATOM   464  C CD1 . LEU A 1 52  ? -10.247 14.464 57.229  1.00 19.10  ? 52  LEU A CD1 1 
ATOM   465  C CD2 . LEU A 1 52  ? -8.230  15.450 56.069  1.00 15.89  ? 52  LEU A CD2 1 
ATOM   466  N N   . ASN A 1 53  ? -5.203  11.658 57.492  1.00 19.26  ? 53  ASN A N   1 
ATOM   467  C CA  . ASN A 1 53  ? -4.388  10.778 58.328  1.00 19.59  ? 53  ASN A CA  1 
ATOM   468  C C   . ASN A 1 53  ? -4.338  11.268 59.774  1.00 20.11  ? 53  ASN A C   1 
ATOM   469  O O   . ASN A 1 53  ? -4.473  12.460 60.050  1.00 17.69  ? 53  ASN A O   1 
ATOM   470  C CB  . ASN A 1 53  ? -2.952  10.688 57.791  1.00 19.12  ? 53  ASN A CB  1 
ATOM   471  C CG  . ASN A 1 53  ? -2.914  10.383 56.316  1.00 21.08  ? 53  ASN A CG  1 
ATOM   472  O OD1 . ASN A 1 53  ? -3.116  9.236  55.903  1.00 17.67  ? 53  ASN A OD1 1 
ATOM   473  N ND2 . ASN A 1 53  ? -2.691  11.415 55.501  1.00 17.68  ? 53  ASN A ND2 1 
ATOM   474  N N   . PHE A 1 54  ? -4.104  10.336 60.693  1.00 19.16  ? 54  PHE A N   1 
ATOM   475  C CA  . PHE A 1 54  ? -4.185  10.622 62.116  1.00 15.15  ? 54  PHE A CA  1 
ATOM   476  C C   . PHE A 1 54  ? -3.049  9.930  62.838  1.00 16.46  ? 54  PHE A C   1 
ATOM   477  O O   . PHE A 1 54  ? -2.627  8.836  62.461  1.00 20.02  ? 54  PHE A O   1 
ATOM   478  C CB  . PHE A 1 54  ? -5.536  10.165 62.702  1.00 20.01  ? 54  PHE A CB  1 
ATOM   479  C CG  . PHE A 1 54  ? -6.709  10.800 62.034  1.00 17.71  ? 54  PHE A CG  1 
ATOM   480  C CD1 . PHE A 1 54  ? -7.250  10.248 60.869  1.00 16.82  ? 54  PHE A CD1 1 
ATOM   481  C CD2 . PHE A 1 54  ? -7.247  11.969 62.529  1.00 20.01  ? 54  PHE A CD2 1 
ATOM   482  C CE1 . PHE A 1 54  ? -8.319  10.859 60.239  1.00 19.26  ? 54  PHE A CE1 1 
ATOM   483  C CE2 . PHE A 1 54  ? -8.319  12.575 61.909  1.00 19.65  ? 54  PHE A CE2 1 
ATOM   484  C CZ  . PHE A 1 54  ? -8.849  12.027 60.761  1.00 16.78  ? 54  PHE A CZ  1 
ATOM   485  N N   . ASN A 1 55  ? -2.569  10.574 63.890  1.00 19.50  ? 55  ASN A N   1 
ATOM   486  C CA  . ASN A 1 55  ? -1.643  9.963  64.827  1.00 24.88  ? 55  ASN A CA  1 
ATOM   487  C C   . ASN A 1 55  ? -2.346  9.798  66.158  1.00 21.90  ? 55  ASN A C   1 
ATOM   488  O O   . ASN A 1 55  ? -2.959  10.741 66.645  1.00 19.03  ? 55  ASN A O   1 
ATOM   489  C CB  . ASN A 1 55  ? -0.388  10.810 65.035  1.00 20.74  ? 55  ASN A CB  1 
ATOM   490  C CG  . ASN A 1 55  ? 0.616   10.103 65.903  1.00 21.33  ? 55  ASN A CG  1 
ATOM   491  O OD1 . ASN A 1 55  ? 1.126   9.064  65.510  1.00 18.01  ? 55  ASN A OD1 1 
ATOM   492  N ND2 . ASN A 1 55  ? 0.893   10.645 67.098  1.00 13.27  ? 55  ASN A ND2 1 
ATOM   493  N N   . LEU A 1 56  ? -2.226  8.615  66.757  1.00 23.20  ? 56  LEU A N   1 
ATOM   494  C CA  . LEU A 1 56  ? -2.801  8.359  68.069  1.00 23.48  ? 56  LEU A CA  1 
ATOM   495  C C   . LEU A 1 56  ? -1.694  7.869  68.982  1.00 23.15  ? 56  LEU A C   1 
ATOM   496  O O   . LEU A 1 56  ? -1.110  6.816  68.728  1.00 22.61  ? 56  LEU A O   1 
ATOM   497  C CB  . LEU A 1 56  ? -3.924  7.327  67.990  1.00 19.60  ? 56  LEU A CB  1 
ATOM   498  C CG  . LEU A 1 56  ? -5.082  7.740  67.086  1.00 23.09  ? 56  LEU A CG  1 
ATOM   499  C CD1 . LEU A 1 56  ? -5.947  6.517  66.730  1.00 25.61  ? 56  LEU A CD1 1 
ATOM   500  C CD2 . LEU A 1 56  ? -5.922  8.849  67.740  1.00 16.87  ? 56  LEU A CD2 1 
ATOM   501  N N   . THR A 1 57  ? -1.401  8.623  70.035  1.00 19.70  ? 57  THR A N   1 
ATOM   502  C CA  . THR A 1 57  ? -0.400  8.135  70.960  1.00 15.95  ? 57  THR A CA  1 
ATOM   503  C C   . THR A 1 57  ? -0.970  6.973  71.779  1.00 14.14  ? 57  THR A C   1 
ATOM   504  O O   . THR A 1 57  ? -2.174  6.910  72.042  1.00 15.00  ? 57  THR A O   1 
ATOM   505  C CB  . THR A 1 57  ? 0.111   9.253  71.880  1.00 15.73  ? 57  THR A CB  1 
ATOM   506  O OG1 . THR A 1 57  ? -0.933  9.706  72.757  1.00 17.17  ? 57  THR A OG1 1 
ATOM   507  C CG2 . THR A 1 57  ? 0.659   10.434 71.042  1.00 14.33  ? 57  THR A CG2 1 
ATOM   508  N N   . PRO A 1 58  ? -0.115  6.041  72.193  1.00 17.42  ? 58  PRO A N   1 
ATOM   509  C CA  . PRO A 1 58  ? -0.601  4.898  72.978  1.00 20.97  ? 58  PRO A CA  1 
ATOM   510  C C   . PRO A 1 58  ? -1.177  5.299  74.325  1.00 24.26  ? 58  PRO A C   1 
ATOM   511  O O   . PRO A 1 58  ? -2.212  4.757  74.727  1.00 25.24  ? 58  PRO A O   1 
ATOM   512  C CB  . PRO A 1 58  ? 0.655   4.026  73.118  1.00 21.52  ? 58  PRO A CB  1 
ATOM   513  C CG  . PRO A 1 58  ? 1.564   4.467  71.959  1.00 17.84  ? 58  PRO A CG  1 
ATOM   514  C CD  . PRO A 1 58  ? 1.315   5.930  71.855  1.00 14.16  ? 58  PRO A CD  1 
ATOM   515  N N   . VAL A 1 59  ? -0.546  6.250  75.025  1.00 16.58  ? 59  VAL A N   1 
ATOM   516  C CA  . VAL A 1 59  ? -1.105  6.746  76.282  1.00 17.53  ? 59  VAL A CA  1 
ATOM   517  C C   . VAL A 1 59  ? -2.514  7.303  76.071  1.00 18.39  ? 59  VAL A C   1 
ATOM   518  O O   . VAL A 1 59  ? -3.403  7.106  76.903  1.00 19.15  ? 59  VAL A O   1 
ATOM   519  C CB  . VAL A 1 59  ? -0.158  7.785  76.924  1.00 20.67  ? 59  VAL A CB  1 
ATOM   520  C CG1 . VAL A 1 59  ? 0.065   9.001  76.005  1.00 24.93  ? 59  VAL A CG1 1 
ATOM   521  C CG2 . VAL A 1 59  ? -0.649  8.213  78.317  1.00 17.53  ? 59  VAL A CG2 1 
ATOM   522  N N   . LEU A 1 60  ? -2.749  8.008  74.964  1.00 21.54  ? 60  LEU A N   1 
ATOM   523  C CA  . LEU A 1 60  ? -4.112  8.481  74.722  1.00 25.36  ? 60  LEU A CA  1 
ATOM   524  C C   . LEU A 1 60  ? -5.059  7.317  74.474  1.00 18.60  ? 60  LEU A C   1 
ATOM   525  O O   . LEU A 1 60  ? -6.178  7.301  75.002  1.00 20.44  ? 60  LEU A O   1 
ATOM   526  C CB  . LEU A 1 60  ? -4.154  9.452  73.545  1.00 22.16  ? 60  LEU A CB  1 
ATOM   527  C CG  . LEU A 1 60  ? -5.548  9.785  73.025  1.00 21.03  ? 60  LEU A CG  1 
ATOM   528  C CD1 . LEU A 1 60  ? -6.429  10.389 74.130  1.00 20.47  ? 60  LEU A CD1 1 
ATOM   529  C CD2 . LEU A 1 60  ? -5.433  10.746 71.856  1.00 19.96  ? 60  LEU A CD2 1 
ATOM   530  N N   . ILE A 1 61  ? -4.639  6.349  73.651  1.00 22.51  ? 61  ILE A N   1 
ATOM   531  C CA  . ILE A 1 61  ? -5.468  5.172  73.391  1.00 20.61  ? 61  ILE A CA  1 
ATOM   532  C C   . ILE A 1 61  ? -5.859  4.496  74.696  1.00 19.57  ? 61  ILE A C   1 
ATOM   533  O O   . ILE A 1 61  ? -7.022  4.121  74.891  1.00 20.33  ? 61  ILE A O   1 
ATOM   534  C CB  . ILE A 1 61  ? -4.745  4.195  72.443  1.00 23.69  ? 61  ILE A CB  1 
ATOM   535  C CG1 . ILE A 1 61  ? -4.570  4.807  71.054  1.00 20.20  ? 61  ILE A CG1 1 
ATOM   536  C CG2 . ILE A 1 61  ? -5.548  2.891  72.292  1.00 23.44  ? 61  ILE A CG2 1 
ATOM   537  C CD1 . ILE A 1 61  ? -3.723  3.961  70.141  1.00 28.75  ? 61  ILE A CD1 1 
ATOM   538  N N   . ASP A 1 62  ? -4.903  4.355  75.619  1.00 21.29  ? 62  ASP A N   1 
ATOM   539  C CA  . ASP A 1 62  ? -5.190  3.737  76.915  1.00 25.42  ? 62  ASP A CA  1 
ATOM   540  C C   . ASP A 1 62  ? -6.350  4.432  77.622  1.00 23.70  ? 62  ASP A C   1 
ATOM   541  O O   . ASP A 1 62  ? -7.250  3.779  78.163  1.00 25.22  ? 62  ASP A O   1 
ATOM   542  C CB  . ASP A 1 62  ? -3.949  3.780  77.814  1.00 26.11  ? 62  ASP A CB  1 
ATOM   543  C CG  . ASP A 1 62  ? -2.908  2.751  77.431  1.00 30.44  ? 62  ASP A CG  1 
ATOM   544  O OD1 . ASP A 1 62  ? -3.281  1.730  76.820  1.00 28.94  ? 62  ASP A OD1 1 
ATOM   545  O OD2 . ASP A 1 62  ? -1.714  2.975  77.736  1.00 27.10  ? 62  ASP A OD2 1 
ATOM   546  N N   . GLN A 1 63  ? -6.324  5.763  77.657  1.00 23.99  ? 63  GLN A N   1 
ATOM   547  C CA  . GLN A 1 63  ? -7.351  6.496  78.385  1.00 18.98  ? 63  GLN A CA  1 
ATOM   548  C C   . GLN A 1 63  ? -8.692  6.426  77.678  1.00 19.61  ? 63  GLN A C   1 
ATOM   549  O O   . GLN A 1 63  ? -9.733  6.291  78.326  1.00 20.10  ? 63  GLN A O   1 
ATOM   550  C CB  . GLN A 1 63  ? -6.929  7.947  78.555  1.00 16.91  ? 63  GLN A CB  1 
ATOM   551  C CG  . GLN A 1 63  ? -5.584  8.124  79.183  1.00 20.89  ? 63  GLN A CG  1 
ATOM   552  C CD  . GLN A 1 63  ? -5.222  9.585  79.245  1.00 24.13  ? 63  GLN A CD  1 
ATOM   553  O OE1 . GLN A 1 63  ? -5.908  10.370 79.903  1.00 22.62  ? 63  GLN A OE1 1 
ATOM   554  N NE2 . GLN A 1 63  ? -4.171  9.971  78.534  1.00 19.41  ? 63  GLN A NE2 1 
ATOM   555  N N   . ILE A 1 64  ? -8.691  6.547  76.351  1.00 26.87  ? 64  ILE A N   1 
ATOM   556  C CA  . ILE A 1 64  ? -9.916  6.358  75.582  1.00 19.00  ? 64  ILE A CA  1 
ATOM   557  C C   . ILE A 1 64  ? -10.546 5.010  75.914  1.00 25.90  ? 64  ILE A C   1 
ATOM   558  O O   . ILE A 1 64  ? -11.768 4.902  76.103  1.00 22.25  ? 64  ILE A O   1 
ATOM   559  C CB  . ILE A 1 64  ? -9.614  6.487  74.077  1.00 22.43  ? 64  ILE A CB  1 
ATOM   560  C CG1 . ILE A 1 64  ? -9.341  7.943  73.704  1.00 20.88  ? 64  ILE A CG1 1 
ATOM   561  C CG2 . ILE A 1 64  ? -10.756 5.911  73.254  1.00 28.02  ? 64  ILE A CG2 1 
ATOM   562  C CD1 . ILE A 1 64  ? -9.160  8.161  72.231  1.00 19.98  ? 64  ILE A CD1 1 
ATOM   563  N N   . GLN A 1 65  ? -9.718  3.960  75.996  1.00 19.85  ? 65  GLN A N   1 
ATOM   564  C CA  . GLN A 1 65  ? -10.240 2.637  76.325  1.00 23.65  ? 65  GLN A CA  1 
ATOM   565  C C   . GLN A 1 65  ? -10.837 2.619  77.724  1.00 24.03  ? 65  GLN A C   1 
ATOM   566  O O   . GLN A 1 65  ? -11.897 2.020  77.950  1.00 23.39  ? 65  GLN A O   1 
ATOM   567  C CB  . GLN A 1 65  ? -9.138  1.585  76.221  1.00 21.71  ? 65  GLN A CB  1 
ATOM   568  C CG  . GLN A 1 65  ? -8.750  1.233  74.792  1.00 24.47  ? 65  GLN A CG  1 
ATOM   569  C CD  . GLN A 1 65  ? -7.649  0.205  74.752  1.00 27.91  ? 65  GLN A CD  1 
ATOM   570  O OE1 . GLN A 1 65  ? -6.591  0.397  75.343  1.00 34.18  ? 65  GLN A OE1 1 
ATOM   571  N NE2 . GLN A 1 65  ? -7.903  -0.913 74.076  1.00 28.89  ? 65  GLN A NE2 1 
ATOM   572  N N   . GLU A 1 66  ? -10.166 3.260  78.681  1.00 21.47  ? 66  GLU A N   1 
ATOM   573  C CA  . GLU A 1 66  ? -10.665 3.227  80.048  1.00 21.90  ? 66  GLU A CA  1 
ATOM   574  C C   . GLU A 1 66  ? -11.997 3.962  80.166  1.00 23.81  ? 66  GLU A C   1 
ATOM   575  O O   . GLU A 1 66  ? -12.884 3.519  80.900  1.00 26.85  ? 66  GLU A O   1 
ATOM   576  C CB  . GLU A 1 66  ? -9.635  3.804  81.016  1.00 22.39  ? 66  GLU A CB  1 
ATOM   577  C CG  . GLU A 1 66  ? -9.848  3.311  82.442  1.00 36.06  ? 66  GLU A CG  1 
ATOM   578  C CD  . GLU A 1 66  ? -8.868  3.902  83.437  1.00 50.85  ? 66  GLU A CD  1 
ATOM   579  O OE1 . GLU A 1 66  ? -9.236  4.022  84.628  1.00 55.06  ? 66  GLU A OE1 1 
ATOM   580  O OE2 . GLU A 1 66  ? -7.734  4.241  83.033  1.00 52.90  ? 66  GLU A OE2 1 
ATOM   581  N N   . TYR A 1 67  ? -12.166 5.072  79.441  1.00 19.80  ? 67  TYR A N   1 
ATOM   582  C CA  . TYR A 1 67  ? -13.464 5.742  79.443  1.00 23.56  ? 67  TYR A CA  1 
ATOM   583  C C   . TYR A 1 67  ? -14.524 4.907  78.731  1.00 27.38  ? 67  TYR A C   1 
ATOM   584  O O   . TYR A 1 67  ? -15.660 4.811  79.204  1.00 26.48  ? 67  TYR A O   1 
ATOM   585  C CB  . TYR A 1 67  ? -13.370 7.115  78.790  1.00 20.72  ? 67  TYR A CB  1 
ATOM   586  C CG  . TYR A 1 67  ? -12.845 8.232  79.676  1.00 20.35  ? 67  TYR A CG  1 
ATOM   587  C CD1 . TYR A 1 67  ? -13.707 9.010  80.456  1.00 17.20  ? 67  TYR A CD1 1 
ATOM   588  C CD2 . TYR A 1 67  ? -11.490 8.539  79.694  1.00 20.09  ? 67  TYR A CD2 1 
ATOM   589  C CE1 . TYR A 1 67  ? -13.208 10.069 81.259  1.00 14.02  ? 67  TYR A CE1 1 
ATOM   590  C CE2 . TYR A 1 67  ? -10.980 9.581  80.482  1.00 21.65  ? 67  TYR A CE2 1 
ATOM   591  C CZ  . TYR A 1 67  ? -11.833 10.338 81.250  1.00 16.55  ? 67  TYR A CZ  1 
ATOM   592  O OH  . TYR A 1 67  ? -11.311 11.354 82.008  1.00 18.11  ? 67  TYR A OH  1 
ATOM   593  N N   . ALA A 1 68  ? -14.186 4.318  77.580  1.00 20.83  ? 68  ALA A N   1 
ATOM   594  C CA  . ALA A 1 68  ? -15.179 3.533  76.848  1.00 19.12  ? 68  ALA A CA  1 
ATOM   595  C C   . ALA A 1 68  ? -15.661 2.339  77.662  1.00 22.65  ? 68  ALA A C   1 
ATOM   596  O O   . ALA A 1 68  ? -16.843 1.977  77.591  1.00 25.52  ? 68  ALA A O   1 
ATOM   597  C CB  . ALA A 1 68  ? -14.609 3.065  75.512  1.00 22.61  ? 68  ALA A CB  1 
ATOM   598  N N   . GLN A 1 69  ? -14.781 1.746  78.461  1.00 21.31  ? 69  GLN A N   1 
ATOM   599  C CA  . GLN A 1 69  ? -15.122 0.636  79.339  1.00 30.92  ? 69  GLN A CA  1 
ATOM   600  C C   . GLN A 1 69  ? -15.814 1.082  80.621  1.00 35.45  ? 69  GLN A C   1 
ATOM   601  O O   . GLN A 1 69  ? -16.186 0.223  81.427  1.00 35.02  ? 69  GLN A O   1 
ATOM   602  C CB  . GLN A 1 69  ? -13.864 -0.163 79.694  1.00 30.02  ? 69  GLN A CB  1 
ATOM   603  C CG  . GLN A 1 69  ? -13.201 -0.853 78.511  1.00 36.31  ? 69  GLN A CG  1 
ATOM   604  C CD  . GLN A 1 69  ? -11.755 -1.221 78.787  1.00 46.49  ? 69  GLN A CD  1 
ATOM   605  O OE1 . GLN A 1 69  ? -11.234 -0.964 79.872  1.00 52.58  ? 69  GLN A OE1 1 
ATOM   606  N NE2 . GLN A 1 69  ? -11.095 -1.815 77.798  1.00 43.72  ? 69  GLN A NE2 1 
ATOM   607  N N   . GLY A 1 70  ? -15.979 2.386  80.835  1.00 27.56  ? 70  GLY A N   1 
ATOM   608  C CA  . GLY A 1 70  ? -16.589 2.868  82.056  1.00 26.23  ? 70  GLY A CA  1 
ATOM   609  C C   . GLY A 1 70  ? -15.771 2.659  83.311  1.00 31.93  ? 70  GLY A C   1 
ATOM   610  O O   . GLY A 1 70  ? -16.341 2.581  84.406  1.00 29.21  ? 70  GLY A O   1 
ATOM   611  N N   . LYS A 1 71  ? -14.445 2.574  83.190  1.00 33.57  ? 71  LYS A N   1 
ATOM   612  C CA  . LYS A 1 71  ? -13.567 2.401  84.341  1.00 37.81  ? 71  LYS A CA  1 
ATOM   613  C C   . LYS A 1 71  ? -12.863 3.687  84.760  1.00 32.05  ? 71  LYS A C   1 
ATOM   614  O O   . LYS A 1 71  ? -12.174 3.690  85.786  1.00 34.31  ? 71  LYS A O   1 
ATOM   615  C CB  . LYS A 1 71  ? -12.502 1.329  84.059  1.00 41.75  ? 71  LYS A CB  1 
ATOM   616  C CG  . LYS A 1 71  ? -13.033 -0.041 83.664  1.00 45.59  ? 71  LYS A CG  1 
ATOM   617  C CD  . LYS A 1 71  ? -11.875 -0.951 83.247  1.00 47.71  ? 71  LYS A CD  1 
ATOM   618  C CE  . LYS A 1 71  ? -12.347 -2.331 82.790  1.00 45.85  ? 71  LYS A CE  1 
ATOM   619  N NZ  . LYS A 1 71  ? -11.189 -3.258 82.605  1.00 45.95  ? 71  LYS A NZ  1 
ATOM   620  N N   . ALA A 1 72  ? -13.007 4.765  83.994  1.00 24.23  ? 72  ALA A N   1 
ATOM   621  C CA  . ALA A 1 72  ? -12.328 6.026  84.283  1.00 25.55  ? 72  ALA A CA  1 
ATOM   622  C C   . ALA A 1 72  ? -13.036 6.781  85.412  1.00 24.52  ? 72  ALA A C   1 
ATOM   623  O O   . ALA A 1 72  ? -14.177 7.217  85.252  1.00 27.27  ? 72  ALA A O   1 
ATOM   624  C CB  . ALA A 1 72  ? -12.278 6.883  83.017  1.00 23.86  ? 72  ALA A CB  1 
ATOM   625  N N   . LYS A 1 73  ? -12.355 6.951  86.545  1.00 27.25  ? 73  LYS A N   1 
ATOM   626  C CA  . LYS A 1 73  ? -12.880 7.730  87.672  1.00 28.30  ? 73  LYS A CA  1 
ATOM   627  C C   . LYS A 1 73  ? -12.442 9.181  87.498  1.00 27.91  ? 73  LYS A C   1 
ATOM   628  O O   . LYS A 1 73  ? -11.402 9.610  88.000  1.00 24.92  ? 73  LYS A O   1 
ATOM   629  C CB  . LYS A 1 73  ? -12.399 7.147  88.997  1.00 29.94  ? 73  LYS A CB  1 
ATOM   630  C CG  . LYS A 1 73  ? -12.863 5.716  89.238  1.00 37.02  ? 73  LYS A CG  1 
ATOM   631  C CD  . LYS A 1 73  ? -12.193 5.078  90.457  1.00 44.25  ? 73  LYS A CD  1 
ATOM   632  C CE  . LYS A 1 73  ? -10.762 4.637  90.151  1.00 48.37  ? 73  LYS A CE  1 
ATOM   633  N NZ  . LYS A 1 73  ? -10.695 3.545  89.135  1.00 51.59  ? 73  LYS A NZ  1 
ATOM   634  N N   . ASP A 1 74  ? -13.266 9.958  86.800  1.00 26.72  ? 74  ASP A N   1 
ATOM   635  C CA  . ASP A 1 74  ? -12.939 11.322 86.394  1.00 25.19  ? 74  ASP A CA  1 
ATOM   636  C C   . ASP A 1 74  ? -13.539 12.290 87.405  1.00 25.65  ? 74  ASP A C   1 
ATOM   637  O O   . ASP A 1 74  ? -14.755 12.475 87.437  1.00 32.27  ? 74  ASP A O   1 
ATOM   638  C CB  . ASP A 1 74  ? -13.473 11.573 84.984  1.00 22.34  ? 74  ASP A CB  1 
ATOM   639  C CG  . ASP A 1 74  ? -13.076 12.923 84.422  1.00 25.71  ? 74  ASP A CG  1 
ATOM   640  O OD1 . ASP A 1 74  ? -13.246 13.962 85.108  1.00 21.45  ? 74  ASP A OD1 1 
ATOM   641  O OD2 . ASP A 1 74  ? -12.609 12.939 83.260  1.00 30.67  ? 74  ASP A OD2 1 
ATOM   642  N N   . VAL A 1 75  ? -12.687 12.938 88.203  1.00 19.50  ? 75  VAL A N   1 
ATOM   643  C CA  . VAL A 1 75  ? -13.190 13.736 89.322  1.00 26.74  ? 75  VAL A CA  1 
ATOM   644  C C   . VAL A 1 75  ? -14.037 14.904 88.828  1.00 27.32  ? 75  VAL A C   1 
ATOM   645  O O   . VAL A 1 75  ? -15.113 15.176 89.374  1.00 28.19  ? 75  VAL A O   1 
ATOM   646  C CB  . VAL A 1 75  ? -12.037 14.217 90.224  1.00 31.73  ? 75  VAL A CB  1 
ATOM   647  C CG1 . VAL A 1 75  ? -11.378 13.027 90.911  1.00 30.82  ? 75  VAL A CG1 1 
ATOM   648  C CG2 . VAL A 1 75  ? -11.020 15.017 89.441  1.00 33.40  ? 75  VAL A CG2 1 
ATOM   649  N N   . PHE A 1 76  ? -13.582 15.607 87.792  1.00 18.77  ? 76  PHE A N   1 
ATOM   650  C CA  . PHE A 1 76  ? -14.378 16.726 87.308  1.00 27.55  ? 76  PHE A CA  1 
ATOM   651  C C   . PHE A 1 76  ? -15.693 16.258 86.696  1.00 28.57  ? 76  PHE A C   1 
ATOM   652  O O   . PHE A 1 76  ? -16.717 16.939 86.826  1.00 32.02  ? 76  PHE A O   1 
ATOM   653  C CB  . PHE A 1 76  ? -13.594 17.555 86.300  1.00 31.48  ? 76  PHE A CB  1 
ATOM   654  C CG  . PHE A 1 76  ? -14.318 18.781 85.901  1.00 40.88  ? 76  PHE A CG  1 
ATOM   655  C CD1 . PHE A 1 76  ? -14.328 19.883 86.738  1.00 43.66  ? 76  PHE A CD1 1 
ATOM   656  C CD2 . PHE A 1 76  ? -15.054 18.815 84.728  1.00 42.55  ? 76  PHE A CD2 1 
ATOM   657  C CE1 . PHE A 1 76  ? -15.031 21.011 86.396  1.00 48.59  ? 76  PHE A CE1 1 
ATOM   658  C CE2 . PHE A 1 76  ? -15.759 19.946 84.377  1.00 46.92  ? 76  PHE A CE2 1 
ATOM   659  C CZ  . PHE A 1 76  ? -15.752 21.043 85.214  1.00 48.73  ? 76  PHE A CZ  1 
ATOM   660  N N   . LEU A 1 77  ? -15.689 15.100 86.038  1.00 27.85  ? 77  LEU A N   1 
ATOM   661  C CA  . LEU A 1 77  ? -16.914 14.587 85.431  1.00 28.59  ? 77  LEU A CA  1 
ATOM   662  C C   . LEU A 1 77  ? -17.938 14.169 86.483  1.00 27.16  ? 77  LEU A C   1 
ATOM   663  O O   . LEU A 1 77  ? -19.145 14.322 86.263  1.00 22.89  ? 77  LEU A O   1 
ATOM   664  C CB  . LEU A 1 77  ? -16.570 13.421 84.510  1.00 26.69  ? 77  LEU A CB  1 
ATOM   665  C CG  . LEU A 1 77  ? -17.644 12.892 83.565  1.00 32.61  ? 77  LEU A CG  1 
ATOM   666  C CD1 . LEU A 1 77  ? -18.175 14.003 82.649  1.00 32.71  ? 77  LEU A CD1 1 
ATOM   667  C CD2 . LEU A 1 77  ? -17.057 11.750 82.761  1.00 27.58  ? 77  LEU A CD2 1 
ATOM   668  N N   . GLU A 1 78  ? -17.497 13.648 87.633  1.00 28.27  ? 78  GLU A N   1 
ATOM   669  C CA  . GLU A 1 78  ? -18.475 13.310 88.662  1.00 25.72  ? 78  GLU A CA  1 
ATOM   670  C C   . GLU A 1 78  ? -19.154 14.560 89.208  1.00 26.06  ? 78  GLU A C   1 
ATOM   671  O O   . GLU A 1 78  ? -20.329 14.517 89.578  1.00 28.63  ? 78  GLU A O   1 
ATOM   672  C CB  . GLU A 1 78  ? -17.846 12.496 89.794  1.00 33.09  ? 78  GLU A CB  1 
ATOM   673  C CG  . GLU A 1 78  ? -16.702 11.564 89.390  1.00 48.12  ? 78  GLU A CG  1 
ATOM   674  C CD  . GLU A 1 78  ? -17.089 10.472 88.375  1.00 60.89  ? 78  GLU A CD  1 
ATOM   675  O OE1 . GLU A 1 78  ? -17.933 9.604  88.701  1.00 63.40  ? 78  GLU A OE1 1 
ATOM   676  O OE2 . GLU A 1 78  ? -16.536 10.474 87.249  1.00 62.26  ? 78  GLU A OE2 1 
ATOM   677  N N   . ALA A 1 79  ? -18.447 15.684 89.231  1.00 25.33  ? 79  ALA A N   1 
ATOM   678  C CA  . ALA A 1 79  ? -19.084 16.931 89.643  1.00 29.01  ? 79  ALA A CA  1 
ATOM   679  C C   . ALA A 1 79  ? -20.098 17.414 88.612  1.00 33.89  ? 79  ALA A C   1 
ATOM   680  O O   . ALA A 1 79  ? -21.028 18.157 88.952  1.00 36.62  ? 79  ALA A O   1 
ATOM   681  C CB  . ALA A 1 79  ? -18.025 18.007 89.883  1.00 22.82  ? 79  ALA A CB  1 
ATOM   682  N N   . ILE A 1 80  ? -19.915 17.030 87.352  1.00 30.66  ? 80  ILE A N   1 
ATOM   683  C CA  . ILE A 1 80  ? -20.876 17.365 86.305  1.00 27.18  ? 80  ILE A CA  1 
ATOM   684  C C   . ILE A 1 80  ? -22.104 16.469 86.405  1.00 25.49  ? 80  ILE A C   1 
ATOM   685  O O   . ILE A 1 80  ? -23.244 16.932 86.275  1.00 24.72  ? 80  ILE A O   1 
ATOM   686  C CB  . ILE A 1 80  ? -20.209 17.240 84.921  1.00 31.63  ? 80  ILE A CB  1 
ATOM   687  C CG1 . ILE A 1 80  ? -19.193 18.365 84.688  1.00 36.40  ? 80  ILE A CG1 1 
ATOM   688  C CG2 . ILE A 1 80  ? -21.256 17.181 83.809  1.00 25.42  ? 80  ILE A CG2 1 
ATOM   689  C CD1 . ILE A 1 80  ? -19.820 19.682 84.336  1.00 42.21  ? 80  ILE A CD1 1 
ATOM   690  N N   . ARG A 1 81  ? -21.890 15.175 86.645  1.00 30.41  ? 81  ARG A N   1 
ATOM   691  C CA  . ARG A 1 81  ? -22.975 14.204 86.579  1.00 27.96  ? 81  ARG A CA  1 
ATOM   692  C C   . ARG A 1 81  ? -23.909 14.280 87.782  1.00 25.50  ? 81  ARG A C   1 
ATOM   693  O O   . ARG A 1 81  ? -25.108 14.009 87.645  1.00 21.66  ? 81  ARG A O   1 
ATOM   694  C CB  . ARG A 1 81  ? -22.392 12.796 86.454  1.00 33.53  ? 81  ARG A CB  1 
ATOM   695  C CG  . ARG A 1 81  ? -23.386 11.677 86.728  1.00 46.48  ? 81  ARG A CG  1 
ATOM   696  C CD  . ARG A 1 81  ? -22.729 10.316 86.659  1.00 52.12  ? 81  ARG A CD  1 
ATOM   697  N NE  . ARG A 1 81  ? -22.488 9.896  85.281  1.00 59.70  ? 81  ARG A NE  1 
ATOM   698  C CZ  . ARG A 1 81  ? -23.440 9.512  84.432  1.00 62.67  ? 81  ARG A CZ  1 
ATOM   699  N NH1 . ARG A 1 81  ? -24.716 9.494  84.810  1.00 63.78  ? 81  ARG A NH1 1 
ATOM   700  N NH2 . ARG A 1 81  ? -23.112 9.144  83.198  1.00 60.07  ? 81  ARG A NH2 1 
ATOM   701  N N   . LYS A 1 82  ? -23.400 14.651 88.956  1.00 24.27  ? 82  LYS A N   1 
ATOM   702  C CA  . LYS A 1 82  ? -24.217 14.619 90.165  1.00 25.49  ? 82  LYS A CA  1 
ATOM   703  C C   . LYS A 1 82  ? -25.368 15.626 90.124  1.00 27.14  ? 82  LYS A C   1 
ATOM   704  O O   . LYS A 1 82  ? -25.276 16.703 89.524  1.00 24.18  ? 82  LYS A O   1 
ATOM   705  C CB  . LYS A 1 82  ? -23.343 14.886 91.391  1.00 33.09  ? 82  LYS A CB  1 
ATOM   706  C CG  . LYS A 1 82  ? -22.654 13.627 91.907  1.00 41.45  ? 82  LYS A CG  1 
ATOM   707  C CD  . LYS A 1 82  ? -22.136 13.799 93.330  1.00 45.64  ? 82  LYS A CD  1 
ATOM   708  C CE  . LYS A 1 82  ? -20.776 14.453 93.353  1.00 46.99  ? 82  LYS A CE  1 
ATOM   709  N NZ  . LYS A 1 82  ? -20.200 14.445 94.729  1.00 51.71  ? 82  LYS A NZ  1 
ATOM   710  N N   . ASP A 1 83  ? -26.472 15.259 90.770  1.00 22.02  ? 83  ASP A N   1 
ATOM   711  C CA  . ASP A 1 83  ? -27.480 16.254 91.096  1.00 23.65  ? 83  ASP A CA  1 
ATOM   712  C C   . ASP A 1 83  ? -26.818 17.364 91.910  1.00 24.41  ? 83  ASP A C   1 
ATOM   713  O O   . ASP A 1 83  ? -26.013 17.075 92.800  1.00 22.52  ? 83  ASP A O   1 
ATOM   714  C CB  . ASP A 1 83  ? -28.628 15.615 91.879  1.00 26.38  ? 83  ASP A CB  1 
ATOM   715  C CG  . ASP A 1 83  ? -29.827 16.534 92.024  1.00 32.95  ? 83  ASP A CG  1 
ATOM   716  O OD1 . ASP A 1 83  ? -29.695 17.576 92.700  1.00 33.41  ? 83  ASP A OD1 1 
ATOM   717  O OD2 . ASP A 1 83  ? -30.901 16.212 91.462  1.00 32.24  ? 83  ASP A OD2 1 
ATOM   718  N N   . PRO A 1 84  ? -27.089 18.638 91.604  1.00 27.89  ? 84  PRO A N   1 
ATOM   719  C CA  . PRO A 1 84  ? -26.381 19.728 92.303  1.00 28.41  ? 84  PRO A CA  1 
ATOM   720  C C   . PRO A 1 84  ? -26.544 19.719 93.816  1.00 31.38  ? 84  PRO A C   1 
ATOM   721  O O   . PRO A 1 84  ? -25.658 20.234 94.516  1.00 25.20  ? 84  PRO A O   1 
ATOM   722  C CB  . PRO A 1 84  ? -26.996 20.990 91.684  1.00 29.39  ? 84  PRO A CB  1 
ATOM   723  C CG  . PRO A 1 84  ? -27.424 20.555 90.320  1.00 27.00  ? 84  PRO A CG  1 
ATOM   724  C CD  . PRO A 1 84  ? -27.879 19.135 90.463  1.00 25.04  ? 84  PRO A CD  1 
ATOM   725  N N   . ASP A 1 85  ? -27.664 19.193 94.331  1.00 28.32  ? 85  ASP A N   1 
ATOM   726  C CA  . ASP A 1 85  ? -27.858 19.017 95.771  1.00 25.78  ? 85  ASP A CA  1 
ATOM   727  C C   . ASP A 1 85  ? -26.836 18.071 96.377  1.00 25.01  ? 85  ASP A C   1 
ATOM   728  O O   . ASP A 1 85  ? -26.628 18.092 97.596  1.00 24.46  ? 85  ASP A O   1 
ATOM   729  C CB  . ASP A 1 85  ? -29.251 18.456 96.063  1.00 23.27  ? 85  ASP A CB  1 
ATOM   730  C CG  . ASP A 1 85  ? -30.358 19.459 95.793  1.00 38.04  ? 85  ASP A CG  1 
ATOM   731  O OD1 . ASP A 1 85  ? -30.083 20.682 95.795  1.00 43.32  ? 85  ASP A OD1 1 
ATOM   732  O OD2 . ASP A 1 85  ? -31.512 19.022 95.598  1.00 43.39  ? 85  ASP A OD2 1 
ATOM   733  N N   . ASP A 1 86  ? -26.223 17.225 95.557  1.00 23.80  ? 86  ASP A N   1 
ATOM   734  C CA  . ASP A 1 86  ? -25.228 16.271 96.014  1.00 27.93  ? 86  ASP A CA  1 
ATOM   735  C C   . ASP A 1 86  ? -23.808 16.803 95.910  1.00 23.45  ? 86  ASP A C   1 
ATOM   736  O O   . ASP A 1 86  ? -22.887 16.156 96.414  1.00 29.82  ? 86  ASP A O   1 
ATOM   737  C CB  . ASP A 1 86  ? -25.352 14.969 95.218  1.00 26.65  ? 86  ASP A CB  1 
ATOM   738  C CG  . ASP A 1 86  ? -26.674 14.270 95.450  1.00 34.97  ? 86  ASP A CG  1 
ATOM   739  O OD1 . ASP A 1 86  ? -27.265 14.456 96.532  1.00 36.94  ? 86  ASP A OD1 1 
ATOM   740  O OD2 . ASP A 1 86  ? -27.128 13.535 94.549  1.00 40.74  ? 86  ASP A OD2 1 
ATOM   741  N N   . LEU A 1 87  ? -23.619 17.973 95.307  1.00 20.10  ? 87  LEU A N   1 
ATOM   742  C CA  . LEU A 1 87  ? -22.286 18.518 95.098  1.00 23.26  ? 87  LEU A CA  1 
ATOM   743  C C   . LEU A 1 87  ? -21.612 18.917 96.408  1.00 26.09  ? 87  LEU A C   1 
ATOM   744  O O   . LEU A 1 87  ? -22.211 19.559 97.275  1.00 25.84  ? 87  LEU A O   1 
ATOM   745  C CB  . LEU A 1 87  ? -22.355 19.739 94.182  1.00 28.07  ? 87  LEU A CB  1 
ATOM   746  C CG  . LEU A 1 87  ? -22.566 19.413 92.705  1.00 27.93  ? 87  LEU A CG  1 
ATOM   747  C CD1 . LEU A 1 87  ? -22.819 20.691 91.900  1.00 25.90  ? 87  LEU A CD1 1 
ATOM   748  C CD2 . LEU A 1 87  ? -21.377 18.630 92.160  1.00 21.95  ? 87  LEU A CD2 1 
ATOM   749  N N   . GLU A 1 88  ? -20.338 18.567 96.526  1.00 24.07  ? 88  GLU A N   1 
ATOM   750  C CA  . GLU A 1 88  ? -19.506 19.111 97.585  1.00 25.36  ? 88  GLU A CA  1 
ATOM   751  C C   . GLU A 1 88  ? -19.141 20.553 97.274  1.00 26.34  ? 88  GLU A C   1 
ATOM   752  O O   . GLU A 1 88  ? -19.082 20.962 96.109  1.00 22.36  ? 88  GLU A O   1 
ATOM   753  C CB  . GLU A 1 88  ? -18.246 18.259 97.751  1.00 25.20  ? 88  GLU A CB  1 
ATOM   754  C CG  . GLU A 1 88  ? -18.568 16.803 97.964  1.00 26.43  ? 88  GLU A CG  1 
ATOM   755  C CD  . GLU A 1 88  ? -17.395 15.881 97.680  1.00 40.08  ? 88  GLU A CD  1 
ATOM   756  O OE1 . GLU A 1 88  ? -16.368 16.372 97.165  1.00 36.54  ? 88  GLU A OE1 1 
ATOM   757  O OE2 . GLU A 1 88  ? -17.502 14.666 97.979  1.00 48.25  ? 88  GLU A OE2 1 
ATOM   758  N N   . LYS A 1 89  ? -18.911 21.336 98.335  1.00 22.22  ? 89  LYS A N   1 
ATOM   759  C CA  . LYS A 1 89  ? -18.456 22.707 98.145  1.00 25.72  ? 89  LYS A CA  1 
ATOM   760  C C   . LYS A 1 89  ? -17.233 22.765 97.227  1.00 27.32  ? 89  LYS A C   1 
ATOM   761  O O   . LYS A 1 89  ? -17.136 23.659 96.375  1.00 24.34  ? 89  LYS A O   1 
ATOM   762  C CB  . LYS A 1 89  ? -18.157 23.357 99.501  1.00 26.48  ? 89  LYS A CB  1 
ATOM   763  C CG  . LYS A 1 89  ? -19.393 23.524 100.388 1.00 32.52  ? 89  LYS A CG  1 
ATOM   764  C CD  . LYS A 1 89  ? -19.038 23.837 101.855 1.00 36.24  ? 89  LYS A CD  1 
ATOM   765  C CE  . LYS A 1 89  ? -20.246 23.639 102.778 1.00 36.51  ? 89  LYS A CE  1 
ATOM   766  N NZ  . LYS A 1 89  ? -20.128 24.391 104.063 1.00 47.12  ? 89  LYS A NZ  1 
ATOM   767  N N   . GLU A 1 90  ? -16.298 21.809 97.366  1.00 22.17  ? 90  GLU A N   1 
ATOM   768  C CA  . GLU A 1 90  ? -15.126 21.792 96.485  1.00 26.99  ? 90  GLU A CA  1 
ATOM   769  C C   . GLU A 1 90  ? -15.523 21.527 95.037  1.00 28.39  ? 90  GLU A C   1 
ATOM   770  O O   . GLU A 1 90  ? -14.866 22.007 94.105  1.00 23.81  ? 90  GLU A O   1 
ATOM   771  C CB  . GLU A 1 90  ? -14.111 20.721 96.895  1.00 35.39  ? 90  GLU A CB  1 
ATOM   772  C CG  . GLU A 1 90  ? -13.739 20.623 98.340  1.00 48.26  ? 90  GLU A CG  1 
ATOM   773  C CD  . GLU A 1 90  ? -12.695 19.540 98.564  1.00 58.75  ? 90  GLU A CD  1 
ATOM   774  O OE1 . GLU A 1 90  ? -11.863 19.695 99.483  1.00 62.08  ? 90  GLU A OE1 1 
ATOM   775  O OE2 . GLU A 1 90  ? -12.701 18.538 97.813  1.00 61.98  ? 90  GLU A OE2 1 
ATOM   776  N N   . GLU A 1 91  ? -16.559 20.718 94.826  1.00 22.69  ? 91  GLU A N   1 
ATOM   777  C CA  . GLU A 1 91  ? -16.945 20.393 93.460  1.00 23.13  ? 91  GLU A CA  1 
ATOM   778  C C   . GLU A 1 91  ? -17.586 21.591 92.773  1.00 22.53  ? 91  GLU A C   1 
ATOM   779  O O   . GLU A 1 91  ? -17.342 21.833 91.585  1.00 26.78  ? 91  GLU A O   1 
ATOM   780  C CB  . GLU A 1 91  ? -17.873 19.187 93.463  1.00 27.64  ? 91  GLU A CB  1 
ATOM   781  C CG  . GLU A 1 91  ? -17.165 17.916 93.891  1.00 27.37  ? 91  GLU A CG  1 
ATOM   782  C CD  . GLU A 1 91  ? -18.099 16.741 93.973  1.00 32.53  ? 91  GLU A CD  1 
ATOM   783  O OE1 . GLU A 1 91  ? -19.140 16.870 94.646  1.00 25.97  ? 91  GLU A OE1 1 
ATOM   784  O OE2 . GLU A 1 91  ? -17.799 15.693 93.356  1.00 32.11  ? 91  GLU A OE2 1 
ATOM   785  N N   . VAL A 1 92  ? -18.394 22.359 93.507  1.00 24.54  ? 92  VAL A N   1 
ATOM   786  C CA  . VAL A 1 92  ? -18.933 23.604 92.968  1.00 25.42  ? 92  VAL A CA  1 
ATOM   787  C C   . VAL A 1 92  ? -17.804 24.564 92.597  1.00 28.09  ? 92  VAL A C   1 
ATOM   788  O O   . VAL A 1 92  ? -17.810 25.156 91.514  1.00 33.96  ? 92  VAL A O   1 
ATOM   789  C CB  . VAL A 1 92  ? -19.919 24.237 93.968  1.00 29.02  ? 92  VAL A CB  1 
ATOM   790  C CG1 . VAL A 1 92  ? -20.505 25.509 93.397  1.00 26.87  ? 92  VAL A CG1 1 
ATOM   791  C CG2 . VAL A 1 92  ? -21.033 23.244 94.315  1.00 23.49  ? 92  VAL A CG2 1 
ATOM   792  N N   . GLU A 1 93  ? -16.821 24.739 93.486  1.00 26.72  ? 93  GLU A N   1 
ATOM   793  C CA  . GLU A 1 93  ? -15.698 25.617 93.158  1.00 28.54  ? 93  GLU A CA  1 
ATOM   794  C C   . GLU A 1 93  ? -14.958 25.119 91.924  1.00 24.87  ? 93  GLU A C   1 
ATOM   795  O O   . GLU A 1 93  ? -14.603 25.909 91.042  1.00 28.28  ? 93  GLU A O   1 
ATOM   796  C CB  . GLU A 1 93  ? -14.739 25.725 94.341  1.00 27.20  ? 93  GLU A CB  1 
ATOM   797  C CG  . GLU A 1 93  ? -15.306 26.477 95.515  1.00 40.08  ? 93  GLU A CG  1 
ATOM   798  C CD  . GLU A 1 93  ? -14.585 26.161 96.807  1.00 48.37  ? 93  GLU A CD  1 
ATOM   799  O OE1 . GLU A 1 93  ? -13.583 25.410 96.766  1.00 51.76  ? 93  GLU A OE1 1 
ATOM   800  O OE2 . GLU A 1 93  ? -15.022 26.663 97.861  1.00 50.18  ? 93  GLU A OE2 1 
ATOM   801  N N   . LYS A 1 94  ? -14.732 23.809 91.838  1.00 24.98  ? 94  LYS A N   1 
ATOM   802  C CA  . LYS A 1 94  ? -14.048 23.246 90.676  1.00 32.35  ? 94  LYS A CA  1 
ATOM   803  C C   . LYS A 1 94  ? -14.841 23.496 89.397  1.00 27.84  ? 94  LYS A C   1 
ATOM   804  O O   . LYS A 1 94  ? -14.268 23.791 88.342  1.00 25.74  ? 94  LYS A O   1 
ATOM   805  C CB  . LYS A 1 94  ? -13.819 21.746 90.879  1.00 39.56  ? 94  LYS A CB  1 
ATOM   806  C CG  . LYS A 1 94  ? -12.501 21.357 91.563  1.00 45.36  ? 94  LYS A CG  1 
ATOM   807  C CD  . LYS A 1 94  ? -12.187 22.216 92.787  1.00 54.02  ? 94  LYS A CD  1 
ATOM   808  C CE  . LYS A 1 94  ? -11.754 21.370 93.992  1.00 56.35  ? 94  LYS A CE  1 
ATOM   809  N NZ  . LYS A 1 94  ? -11.493 22.216 95.201  1.00 55.19  ? 94  LYS A NZ  1 
ATOM   810  N N   . LEU A 1 95  ? -16.167 23.381 89.479  1.00 25.53  ? 95  LEU A N   1 
ATOM   811  C CA  . LEU A 1 95  ? -17.027 23.635 88.328  1.00 26.30  ? 95  LEU A CA  1 
ATOM   812  C C   . LEU A 1 95  ? -16.959 25.097 87.896  1.00 23.62  ? 95  LEU A C   1 
ATOM   813  O O   . LEU A 1 95  ? -16.905 25.405 86.697  1.00 22.20  ? 95  LEU A O   1 
ATOM   814  C CB  . LEU A 1 95  ? -18.464 23.236 88.688  1.00 23.41  ? 95  LEU A CB  1 
ATOM   815  C CG  . LEU A 1 95  ? -19.595 23.555 87.721  1.00 41.11  ? 95  LEU A CG  1 
ATOM   816  C CD1 . LEU A 1 95  ? -19.343 22.918 86.358  1.00 42.52  ? 95  LEU A CD1 1 
ATOM   817  C CD2 . LEU A 1 95  ? -20.940 23.092 88.307  1.00 46.02  ? 95  LEU A CD2 1 
ATOM   818  N N   . ILE A 1 96  ? -16.991 26.012 88.864  1.00 21.38  ? 96  ILE A N   1 
ATOM   819  C CA  . ILE A 1 96  ? -16.908 27.434 88.559  1.00 27.16  ? 96  ILE A CA  1 
ATOM   820  C C   . ILE A 1 96  ? -15.532 27.778 87.995  1.00 26.25  ? 96  ILE A C   1 
ATOM   821  O O   . ILE A 1 96  ? -15.418 28.510 87.003  1.00 26.51  ? 96  ILE A O   1 
ATOM   822  C CB  . ILE A 1 96  ? -17.239 28.256 89.821  1.00 25.17  ? 96  ILE A CB  1 
ATOM   823  C CG1 . ILE A 1 96  ? -18.728 28.107 90.185  1.00 24.70  ? 96  ILE A CG1 1 
ATOM   824  C CG2 . ILE A 1 96  ? -16.870 29.726 89.631  1.00 26.25  ? 96  ILE A CG2 1 
ATOM   825  C CD1 . ILE A 1 96  ? -19.097 28.779 91.494  1.00 25.90  ? 96  ILE A CD1 1 
ATOM   826  N N   . GLU A 1 97  ? -14.467 27.261 88.613  1.00 26.23  ? 97  GLU A N   1 
ATOM   827  C CA  . GLU A 1 97  ? -13.124 27.558 88.121  1.00 26.80  ? 97  GLU A CA  1 
ATOM   828  C C   . GLU A 1 97  ? -12.960 27.068 86.690  1.00 22.71  ? 97  GLU A C   1 
ATOM   829  O O   . GLU A 1 97  ? -12.412 27.780 85.840  1.00 21.27  ? 97  GLU A O   1 
ATOM   830  C CB  . GLU A 1 97  ? -12.063 26.929 89.031  1.00 32.32  ? 97  GLU A CB  1 
ATOM   831  C CG  . GLU A 1 97  ? -11.970 27.542 90.441  1.00 45.22  ? 97  GLU A CG  1 
ATOM   832  C CD  . GLU A 1 97  ? -11.510 26.536 91.509  1.00 57.03  ? 97  GLU A CD  1 
ATOM   833  O OE1 . GLU A 1 97  ? -11.086 26.970 92.605  1.00 59.86  ? 97  GLU A OE1 1 
ATOM   834  O OE2 . GLU A 1 97  ? -11.575 25.310 91.258  1.00 60.47  ? 97  GLU A OE2 1 
ATOM   835  N N   . PHE A 1 98  ? -13.461 25.859 86.401  1.00 25.59  ? 98  PHE A N   1 
ATOM   836  C CA  . PHE A 1 98  ? -13.358 25.302 85.054  1.00 22.47  ? 98  PHE A CA  1 
ATOM   837  C C   . PHE A 1 98  ? -14.114 26.145 84.032  1.00 25.26  ? 98  PHE A C   1 
ATOM   838  O O   . PHE A 1 98  ? -13.610 26.390 82.933  1.00 23.22  ? 98  PHE A O   1 
ATOM   839  C CB  . PHE A 1 98  ? -13.886 23.873 85.044  1.00 21.83  ? 98  PHE A CB  1 
ATOM   840  C CG  . PHE A 1 98  ? -13.622 23.131 83.766  1.00 23.76  ? 98  PHE A CG  1 
ATOM   841  C CD1 . PHE A 1 98  ? -12.378 22.570 83.524  1.00 23.59  ? 98  PHE A CD1 1 
ATOM   842  C CD2 . PHE A 1 98  ? -14.615 22.979 82.812  1.00 24.60  ? 98  PHE A CD2 1 
ATOM   843  C CE1 . PHE A 1 98  ? -12.132 21.870 82.356  1.00 22.88  ? 98  PHE A CE1 1 
ATOM   844  C CE2 . PHE A 1 98  ? -14.376 22.281 81.639  1.00 25.45  ? 98  PHE A CE2 1 
ATOM   845  C CZ  . PHE A 1 98  ? -13.133 21.724 81.411  1.00 22.47  ? 98  PHE A CZ  1 
ATOM   846  N N   . THR A 1 99  ? -15.344 26.559 84.362  1.00 22.03  ? 99  THR A N   1 
ATOM   847  C CA  . THR A 1 99  ? -16.085 27.475 83.497  1.00 21.58  ? 99  THR A CA  1 
ATOM   848  C C   . THR A 1 99  ? -15.288 28.746 83.236  1.00 21.98  ? 99  THR A C   1 
ATOM   849  O O   . THR A 1 99  ? -15.169 29.203 82.091  1.00 22.49  ? 99  THR A O   1 
ATOM   850  C CB  . THR A 1 99  ? -17.432 27.827 84.137  1.00 23.94  ? 99  THR A CB  1 
ATOM   851  O OG1 . THR A 1 99  ? -18.152 26.631 84.457  1.00 22.76  ? 99  THR A OG1 1 
ATOM   852  C CG2 . THR A 1 99  ? -18.263 28.675 83.193  1.00 25.89  ? 99  THR A CG2 1 
ATOM   853  N N   . LYS A 1 100 ? -14.743 29.337 84.301  1.00 21.72  ? 100 LYS A N   1 
ATOM   854  C CA  . LYS A 1 100 ? -13.997 30.582 84.173  1.00 23.13  ? 100 LYS A CA  1 
ATOM   855  C C   . LYS A 1 100 ? -12.784 30.413 83.274  1.00 31.32  ? 100 LYS A C   1 
ATOM   856  O O   . LYS A 1 100 ? -12.409 31.348 82.558  1.00 29.81  ? 100 LYS A O   1 
ATOM   857  C CB  . LYS A 1 100 ? -13.545 31.066 85.550  1.00 28.91  ? 100 LYS A CB  1 
ATOM   858  C CG  . LYS A 1 100 ? -14.535 31.971 86.268  1.00 39.36  ? 100 LYS A CG  1 
ATOM   859  C CD  . LYS A 1 100 ? -13.985 32.474 87.609  1.00 48.98  ? 100 LYS A CD  1 
ATOM   860  C CE  . LYS A 1 100 ? -12.451 32.439 87.679  1.00 58.14  ? 100 LYS A CE  1 
ATOM   861  N NZ  . LYS A 1 100 ? -11.768 33.342 86.696  1.00 61.90  ? 100 LYS A NZ  1 
ATOM   862  N N   . LEU A 1 101 ? -12.154 29.236 83.313  1.00 27.43  ? 101 LEU A N   1 
ATOM   863  C CA  . LEU A 1 101 ? -10.996 28.978 82.465  1.00 29.31  ? 101 LEU A CA  1 
ATOM   864  C C   . LEU A 1 101 ? -11.384 28.984 80.993  1.00 28.53  ? 101 LEU A C   1 
ATOM   865  O O   . LEU A 1 101 ? -10.626 29.467 80.144  1.00 27.38  ? 101 LEU A O   1 
ATOM   866  C CB  . LEU A 1 101 ? -10.367 27.637 82.847  1.00 26.65  ? 101 LEU A CB  1 
ATOM   867  C CG  . LEU A 1 101 ? -9.211  27.122 81.987  1.00 34.07  ? 101 LEU A CG  1 
ATOM   868  C CD1 . LEU A 1 101 ? -7.964  27.985 82.194  1.00 37.48  ? 101 LEU A CD1 1 
ATOM   869  C CD2 . LEU A 1 101 ? -8.925  25.658 82.285  1.00 31.15  ? 101 LEU A CD2 1 
ATOM   870  N N   . ASN A 1 102 ? -12.561 28.457 80.670  1.00 19.32  ? 102 ASN A N   1 
ATOM   871  C CA  . ASN A 1 102 ? -12.984 28.310 79.284  1.00 23.45  ? 102 ASN A CA  1 
ATOM   872  C C   . ASN A 1 102 ? -13.916 29.428 78.819  1.00 22.27  ? 102 ASN A C   1 
ATOM   873  O O   . ASN A 1 102 ? -14.360 29.404 77.665  1.00 18.74  ? 102 ASN A O   1 
ATOM   874  C CB  . ASN A 1 102 ? -13.658 26.948 79.096  1.00 23.76  ? 102 ASN A CB  1 
ATOM   875  C CG  . ASN A 1 102 ? -12.691 25.786 79.286  1.00 23.76  ? 102 ASN A CG  1 
ATOM   876  O OD1 . ASN A 1 102 ? -11.772 25.599 78.493  1.00 30.79  ? 102 ASN A OD1 1 
ATOM   877  N ND2 . ASN A 1 102 ? -12.893 25.009 80.336  1.00 21.00  ? 102 ASN A ND2 1 
ATOM   878  N N   . TYR A 1 103 ? -14.154 30.431 79.668  1.00 26.00  ? 103 TYR A N   1 
ATOM   879  C CA  . TYR A 1 103 ? -15.278 31.354 79.497  1.00 31.82  ? 103 TYR A CA  1 
ATOM   880  C C   . TYR A 1 103 ? -15.213 32.124 78.177  1.00 27.98  ? 103 TYR A C   1 
ATOM   881  O O   . TYR A 1 103 ? -16.252 32.413 77.572  1.00 24.68  ? 103 TYR A O   1 
ATOM   882  C CB  . TYR A 1 103 ? -15.315 32.327 80.683  1.00 28.21  ? 103 TYR A CB  1 
ATOM   883  C CG  . TYR A 1 103 ? -16.434 33.331 80.658  1.00 34.72  ? 103 TYR A CG  1 
ATOM   884  C CD1 . TYR A 1 103 ? -17.680 33.012 81.170  1.00 36.88  ? 103 TYR A CD1 1 
ATOM   885  C CD2 . TYR A 1 103 ? -16.239 34.609 80.148  1.00 35.04  ? 103 TYR A CD2 1 
ATOM   886  C CE1 . TYR A 1 103 ? -18.712 33.934 81.165  1.00 36.93  ? 103 TYR A CE1 1 
ATOM   887  C CE2 . TYR A 1 103 ? -17.262 35.534 80.137  1.00 39.14  ? 103 TYR A CE2 1 
ATOM   888  C CZ  . TYR A 1 103 ? -18.496 35.187 80.648  1.00 39.87  ? 103 TYR A CZ  1 
ATOM   889  O OH  . TYR A 1 103 ? -19.519 36.096 80.648  1.00 47.50  ? 103 TYR A OH  1 
ATOM   890  N N   . GLU A 1 104 ? -14.015 32.496 77.728  1.00 22.76  ? 104 GLU A N   1 
ATOM   891  C CA  . GLU A 1 104 ? -13.899 33.339 76.542  1.00 27.06  ? 104 GLU A CA  1 
ATOM   892  C C   . GLU A 1 104 ? -13.753 32.538 75.254  1.00 30.04  ? 104 GLU A C   1 
ATOM   893  O O   . GLU A 1 104 ? -13.605 33.142 74.185  1.00 26.32  ? 104 GLU A O   1 
ATOM   894  C CB  . GLU A 1 104 ? -12.717 34.308 76.685  1.00 29.89  ? 104 GLU A CB  1 
ATOM   895  C CG  . GLU A 1 104 ? -12.839 35.279 77.862  1.00 35.13  ? 104 GLU A CG  1 
ATOM   896  C CD  . GLU A 1 104 ? -13.887 36.360 77.626  1.00 43.92  ? 104 GLU A CD  1 
ATOM   897  O OE1 . GLU A 1 104 ? -14.281 36.562 76.458  1.00 45.73  ? 104 GLU A OE1 1 
ATOM   898  O OE2 . GLU A 1 104 ? -14.319 37.006 78.609  1.00 47.50  ? 104 GLU A OE2 1 
ATOM   899  N N   . LYS A 1 105 ? -13.802 31.207 75.326  1.00 23.38  ? 105 LYS A N   1 
ATOM   900  C CA  . LYS A 1 105 ? -13.706 30.391 74.123  1.00 20.20  ? 105 LYS A CA  1 
ATOM   901  C C   . LYS A 1 105 ? -15.007 30.465 73.328  1.00 21.66  ? 105 LYS A C   1 
ATOM   902  O O   . LYS A 1 105 ? -16.092 30.489 73.911  1.00 22.84  ? 105 LYS A O   1 
ATOM   903  C CB  . LYS A 1 105 ? -13.383 28.939 74.482  1.00 19.39  ? 105 LYS A CB  1 
ATOM   904  C CG  . LYS A 1 105 ? -11.976 28.776 75.036  1.00 20.49  ? 105 LYS A CG  1 
ATOM   905  C CD  . LYS A 1 105 ? -11.756 27.449 75.720  1.00 22.70  ? 105 LYS A CD  1 
ATOM   906  C CE  . LYS A 1 105 ? -10.292 27.320 76.163  1.00 22.99  ? 105 LYS A CE  1 
ATOM   907  N NZ  . LYS A 1 105 ? -9.971  25.908 76.490  1.00 21.20  ? 105 LYS A NZ  1 
ATOM   908  N N   . PRO A 1 106 ? -14.926 30.521 71.999  1.00 26.18  ? 106 PRO A N   1 
ATOM   909  C CA  . PRO A 1 106 ? -16.159 30.572 71.189  1.00 17.93  ? 106 PRO A CA  1 
ATOM   910  C C   . PRO A 1 106 ? -17.125 29.428 71.461  1.00 26.33  ? 106 PRO A C   1 
ATOM   911  O O   . PRO A 1 106 ? -18.343 29.642 71.451  1.00 28.78  ? 106 PRO A O   1 
ATOM   912  C CB  . PRO A 1 106 ? -15.624 30.535 69.750  1.00 25.27  ? 106 PRO A CB  1 
ATOM   913  C CG  . PRO A 1 106 ? -14.237 31.134 69.848  1.00 24.39  ? 106 PRO A CG  1 
ATOM   914  C CD  . PRO A 1 106 ? -13.705 30.745 71.199  1.00 26.17  ? 106 PRO A CD  1 
ATOM   915  N N   . ILE A 1 107 ? -16.624 28.216 71.724  1.00 21.42  ? 107 ILE A N   1 
ATOM   916  C CA  . ILE A 1 107 ? -17.525 27.109 72.005  1.00 22.69  ? 107 ILE A CA  1 
ATOM   917  C C   . ILE A 1 107 ? -18.275 27.305 73.311  1.00 23.81  ? 107 ILE A C   1 
ATOM   918  O O   . ILE A 1 107 ? -19.285 26.631 73.538  1.00 19.74  ? 107 ILE A O   1 
ATOM   919  C CB  . ILE A 1 107 ? -16.778 25.758 72.023  1.00 25.04  ? 107 ILE A CB  1 
ATOM   920  C CG1 . ILE A 1 107 ? -15.647 25.757 73.056  1.00 23.21  ? 107 ILE A CG1 1 
ATOM   921  C CG2 . ILE A 1 107 ? -16.252 25.428 70.637  1.00 25.11  ? 107 ILE A CG2 1 
ATOM   922  C CD1 . ILE A 1 107 ? -15.129 24.360 73.390  1.00 23.53  ? 107 ILE A CD1 1 
ATOM   923  N N   . TYR A 1 108 ? -17.811 28.210 74.181  1.00 22.99  ? 108 TYR A N   1 
ATOM   924  C CA  . TYR A 1 108 ? -18.510 28.530 75.418  1.00 22.24  ? 108 TYR A CA  1 
ATOM   925  C C   . TYR A 1 108 ? -19.439 29.727 75.274  1.00 24.00  ? 108 TYR A C   1 
ATOM   926  O O   . TYR A 1 108 ? -19.949 30.231 76.279  1.00 23.68  ? 108 TYR A O   1 
ATOM   927  C CB  . TYR A 1 108 ? -17.508 28.776 76.554  1.00 22.18  ? 108 TYR A CB  1 
ATOM   928  C CG  . TYR A 1 108 ? -17.187 27.525 77.359  1.00 20.79  ? 108 TYR A CG  1 
ATOM   929  C CD1 . TYR A 1 108 ? -16.400 26.513 76.823  1.00 25.62  ? 108 TYR A CD1 1 
ATOM   930  C CD2 . TYR A 1 108 ? -17.691 27.349 78.651  1.00 29.15  ? 108 TYR A CD2 1 
ATOM   931  C CE1 . TYR A 1 108 ? -16.112 25.346 77.550  1.00 18.24  ? 108 TYR A CE1 1 
ATOM   932  C CE2 . TYR A 1 108 ? -17.406 26.188 79.389  1.00 25.42  ? 108 TYR A CE2 1 
ATOM   933  C CZ  . TYR A 1 108 ? -16.610 25.205 78.829  1.00 21.62  ? 108 TYR A CZ  1 
ATOM   934  O OH  . TYR A 1 108 ? -16.319 24.069 79.542  1.00 23.98  ? 108 TYR A OH  1 
ATOM   935  N N   . ARG A 1 109 ? -19.708 30.180 74.051  1.00 20.90  ? 109 ARG A N   1 
ATOM   936  C CA  . ARG A 1 109 ? -20.555 31.354 73.879  1.00 28.20  ? 109 ARG A CA  1 
ATOM   937  C C   . ARG A 1 109 ? -22.018 30.922 73.967  1.00 31.79  ? 109 ARG A C   1 
ATOM   938  O O   . ARG A 1 109 ? -22.704 30.704 72.965  1.00 31.98  ? 109 ARG A O   1 
ATOM   939  C CB  . ARG A 1 109 ? -20.243 32.062 72.570  1.00 34.52  ? 109 ARG A CB  1 
ATOM   940  C CG  . ARG A 1 109 ? -20.563 33.541 72.602  1.00 45.96  ? 109 ARG A CG  1 
ATOM   941  C CD  . ARG A 1 109 ? -20.101 34.218 71.321  1.00 54.94  ? 109 ARG A CD  1 
ATOM   942  N NE  . ARG A 1 109 ? -18.647 34.180 71.169  1.00 54.09  ? 109 ARG A NE  1 
ATOM   943  C CZ  . ARG A 1 109 ? -18.023 34.083 70.000  1.00 48.81  ? 109 ARG A CZ  1 
ATOM   944  N NH1 . ARG A 1 109 ? -18.728 34.007 68.880  1.00 51.15  ? 109 ARG A NH1 1 
ATOM   945  N NH2 . ARG A 1 109 ? -16.698 34.065 69.949  1.00 41.77  ? 109 ARG A NH2 1 
ATOM   946  N N   . PHE A 1 110 ? -22.489 30.781 75.206  1.00 25.48  ? 110 PHE A N   1 
ATOM   947  C CA  . PHE A 1 110 ? -23.906 30.638 75.528  1.00 23.61  ? 110 PHE A CA  1 
ATOM   948  C C   . PHE A 1 110 ? -24.286 31.796 76.432  1.00 26.56  ? 110 PHE A C   1 
ATOM   949  O O   . PHE A 1 110 ? -23.627 32.016 77.451  1.00 30.32  ? 110 PHE A O   1 
ATOM   950  C CB  . PHE A 1 110 ? -24.203 29.331 76.275  1.00 21.65  ? 110 PHE A CB  1 
ATOM   951  C CG  . PHE A 1 110 ? -23.862 28.092 75.522  1.00 23.24  ? 110 PHE A CG  1 
ATOM   952  C CD1 . PHE A 1 110 ? -22.576 27.594 75.528  1.00 30.02  ? 110 PHE A CD1 1 
ATOM   953  C CD2 . PHE A 1 110 ? -24.848 27.389 74.846  1.00 26.33  ? 110 PHE A CD2 1 
ATOM   954  C CE1 . PHE A 1 110 ? -22.270 26.427 74.846  1.00 37.27  ? 110 PHE A CE1 1 
ATOM   955  C CE2 . PHE A 1 110 ? -24.557 26.229 74.173  1.00 26.33  ? 110 PHE A CE2 1 
ATOM   956  C CZ  . PHE A 1 110 ? -23.262 25.747 74.166  1.00 33.82  ? 110 PHE A CZ  1 
ATOM   957  N N   . GLU A 1 111 ? -25.347 32.524 76.072  1.00 33.04  ? 111 GLU A N   1 
ATOM   958  C CA  . GLU A 1 111 ? -25.764 33.660 76.889  1.00 33.41  ? 111 GLU A CA  1 
ATOM   959  C C   . GLU A 1 111 ? -26.021 33.233 78.330  1.00 29.64  ? 111 GLU A C   1 
ATOM   960  O O   . GLU A 1 111 ? -25.718 33.975 79.270  1.00 29.52  ? 111 GLU A O   1 
ATOM   961  C CB  . GLU A 1 111 ? -27.009 34.311 76.286  1.00 38.18  ? 111 GLU A CB  1 
ATOM   962  C CG  . GLU A 1 111 ? -27.621 35.432 77.124  1.00 47.29  ? 111 GLU A CG  1 
ATOM   963  C CD  . GLU A 1 111 ? -26.836 36.734 77.050  1.00 59.26  ? 111 GLU A CD  1 
ATOM   964  O OE1 . GLU A 1 111 ? -26.486 37.164 75.929  1.00 62.73  ? 111 GLU A OE1 1 
ATOM   965  O OE2 . GLU A 1 111 ? -26.576 37.331 78.120  1.00 63.36  ? 111 GLU A OE2 1 
ATOM   966  N N   . ARG A 1 112 ? -26.551 32.023 78.525  1.00 18.58  ? 112 ARG A N   1 
ATOM   967  C CA  . ARG A 1 112 ? -26.835 31.572 79.885  1.00 26.83  ? 112 ARG A CA  1 
ATOM   968  C C   . ARG A 1 112 ? -25.570 31.463 80.727  1.00 29.86  ? 112 ARG A C   1 
ATOM   969  O O   . ARG A 1 112 ? -25.622 31.666 81.946  1.00 29.49  ? 112 ARG A O   1 
ATOM   970  C CB  . ARG A 1 112 ? -27.574 30.237 79.853  1.00 22.57  ? 112 ARG A CB  1 
ATOM   971  C CG  . ARG A 1 112 ? -27.908 29.678 81.226  1.00 27.73  ? 112 ARG A CG  1 
ATOM   972  C CD  . ARG A 1 112 ? -28.793 30.618 82.027  1.00 29.28  ? 112 ARG A CD  1 
ATOM   973  N NE  . ARG A 1 112 ? -29.439 29.908 83.129  1.00 34.77  ? 112 ARG A NE  1 
ATOM   974  C CZ  . ARG A 1 112 ? -30.116 30.500 84.108  1.00 30.70  ? 112 ARG A CZ  1 
ATOM   975  N NH1 . ARG A 1 112 ? -30.232 31.820 84.130  1.00 29.45  ? 112 ARG A NH1 1 
ATOM   976  N NH2 . ARG A 1 112 ? -30.668 29.769 85.069  1.00 26.17  ? 112 ARG A NH2 1 
ATOM   977  N N   . ILE A 1 113 ? -24.424 31.161 80.105  1.00 27.70  ? 113 ILE A N   1 
ATOM   978  C CA  . ILE A 1 113 ? -23.176 31.105 80.859  1.00 26.31  ? 113 ILE A CA  1 
ATOM   979  C C   . ILE A 1 113 ? -22.794 32.492 81.364  1.00 28.53  ? 113 ILE A C   1 
ATOM   980  O O   . ILE A 1 113 ? -22.335 32.646 82.503  1.00 31.87  ? 113 ILE A O   1 
ATOM   981  C CB  . ILE A 1 113 ? -22.049 30.489 80.009  1.00 25.05  ? 113 ILE A CB  1 
ATOM   982  C CG1 . ILE A 1 113 ? -22.263 28.991 79.834  1.00 26.73  ? 113 ILE A CG1 1 
ATOM   983  C CG2 . ILE A 1 113 ? -20.689 30.746 80.663  1.00 27.29  ? 113 ILE A CG2 1 
ATOM   984  C CD1 . ILE A 1 113 ? -21.173 28.316 79.031  1.00 27.99  ? 113 ILE A CD1 1 
ATOM   985  N N   . ARG A 1 114 ? -22.958 33.520 80.522  1.00 26.52  ? 114 ARG A N   1 
ATOM   986  C CA  . ARG A 1 114 ? -22.716 34.890 80.966  1.00 28.42  ? 114 ARG A CA  1 
ATOM   987  C C   . ARG A 1 114 ? -23.591 35.242 82.163  1.00 33.06  ? 114 ARG A C   1 
ATOM   988  O O   . ARG A 1 114 ? -23.134 35.906 83.100  1.00 37.88  ? 114 ARG A O   1 
ATOM   989  C CB  . ARG A 1 114 ? -22.978 35.874 79.823  1.00 32.13  ? 114 ARG A CB  1 
ATOM   990  C CG  . ARG A 1 114 ? -22.458 35.434 78.462  1.00 41.52  ? 114 ARG A CG  1 
ATOM   991  C CD  . ARG A 1 114 ? -22.183 36.627 77.552  1.00 51.18  ? 114 ARG A CD  1 
ATOM   992  N NE  . ARG A 1 114 ? -23.152 36.735 76.462  1.00 60.25  ? 114 ARG A NE  1 
ATOM   993  C CZ  . ARG A 1 114 ? -23.060 36.075 75.311  1.00 62.61  ? 114 ARG A CZ  1 
ATOM   994  N NH1 . ARG A 1 114 ? -22.044 35.253 75.094  1.00 61.21  ? 114 ARG A NH1 1 
ATOM   995  N NH2 . ARG A 1 114 ? -23.988 36.233 74.375  1.00 66.59  ? 114 ARG A NH2 1 
ATOM   996  N N   . GLU A 1 115 ? -24.851 34.797 82.156  1.00 35.88  ? 115 GLU A N   1 
ATOM   997  C CA  . GLU A 1 115 ? -25.751 35.111 83.264  1.00 35.77  ? 115 GLU A CA  1 
ATOM   998  C C   . GLU A 1 115 ? -25.311 34.423 84.551  1.00 33.51  ? 115 GLU A C   1 
ATOM   999  O O   . GLU A 1 115 ? -25.276 35.045 85.619  1.00 31.64  ? 115 GLU A O   1 
ATOM   1000 C CB  . GLU A 1 115 ? -27.185 34.708 82.917  1.00 41.34  ? 115 GLU A CB  1 
ATOM   1001 C CG  . GLU A 1 115 ? -27.771 35.373 81.696  1.00 43.62  ? 115 GLU A CG  1 
ATOM   1002 C CD  . GLU A 1 115 ? -29.106 34.759 81.311  1.00 51.91  ? 115 GLU A CD  1 
ATOM   1003 O OE1 . GLU A 1 115 ? -29.665 34.007 82.136  1.00 52.30  ? 115 GLU A OE1 1 
ATOM   1004 O OE2 . GLU A 1 115 ? -29.591 35.018 80.187  1.00 55.06  ? 115 GLU A OE2 1 
ATOM   1005 N N   . LEU A 1 116 ? -24.965 33.136 84.466  1.00 30.98  ? 116 LEU A N   1 
ATOM   1006 C CA  . LEU A 1 116 ? -24.598 32.376 85.657  1.00 33.54  ? 116 LEU A CA  1 
ATOM   1007 C C   . LEU A 1 116 ? -23.332 32.917 86.308  1.00 35.44  ? 116 LEU A C   1 
ATOM   1008 O O   . LEU A 1 116 ? -23.237 32.986 87.539  1.00 34.55  ? 116 LEU A O   1 
ATOM   1009 C CB  . LEU A 1 116 ? -24.413 30.902 85.296  1.00 32.35  ? 116 LEU A CB  1 
ATOM   1010 C CG  . LEU A 1 116 ? -25.660 30.195 84.759  1.00 34.17  ? 116 LEU A CG  1 
ATOM   1011 C CD1 . LEU A 1 116 ? -25.345 28.770 84.261  1.00 31.45  ? 116 LEU A CD1 1 
ATOM   1012 C CD2 . LEU A 1 116 ? -26.752 30.182 85.821  1.00 32.13  ? 116 LEU A CD2 1 
ATOM   1013 N N   . MET A 1 117 ? -22.335 33.277 85.504  1.00 37.70  ? 117 MET A N   1 
ATOM   1014 C CA  . MET A 1 117 ? -21.088 33.788 86.062  1.00 42.95  ? 117 MET A CA  1 
ATOM   1015 C C   . MET A 1 117 ? -21.203 35.221 86.563  1.00 41.90  ? 117 MET A C   1 
ATOM   1016 O O   . MET A 1 117 ? -20.258 35.722 87.180  1.00 41.25  ? 117 MET A O   1 
ATOM   1017 C CB  . MET A 1 117 ? -19.967 33.676 85.026  1.00 37.79  ? 117 MET A CB  1 
ATOM   1018 C CG  . MET A 1 117 ? -19.698 32.236 84.567  1.00 40.47  ? 117 MET A CG  1 
ATOM   1019 S SD  . MET A 1 117 ? -18.915 31.204 85.835  1.00 42.53  ? 117 MET A SD  1 
ATOM   1020 C CE  . MET A 1 117 ? -20.347 30.428 86.578  1.00 42.75  ? 117 MET A CE  1 
ATOM   1021 N N   . ASN A 1 118 ? -22.327 35.888 86.322  1.00 38.04  ? 118 ASN A N   1 
ATOM   1022 C CA  . ASN A 1 118 ? -22.559 37.227 86.844  1.00 46.25  ? 118 ASN A CA  1 
ATOM   1023 C C   . ASN A 1 118 ? -23.501 37.220 88.041  1.00 49.86  ? 118 ASN A C   1 
ATOM   1024 O O   . ASN A 1 118 ? -23.924 38.290 88.492  1.00 53.23  ? 118 ASN A O   1 
ATOM   1025 C CB  . ASN A 1 118 ? -23.105 38.143 85.747  1.00 53.37  ? 118 ASN A CB  1 
ATOM   1026 C CG  . ASN A 1 118 ? -22.025 38.611 84.780  1.00 61.72  ? 118 ASN A CG  1 
ATOM   1027 O OD1 . ASN A 1 118 ? -22.218 39.580 84.046  1.00 67.40  ? 118 ASN A OD1 1 
ATOM   1028 N ND2 . ASN A 1 118 ? -20.894 37.921 84.766  1.00 64.55  ? 118 ASN A ND2 1 
ATOM   1029 N N   . LYS A 1 119 ? -23.843 36.040 88.557  1.00 49.12  ? 119 LYS A N   1 
ATOM   1030 C CA  . LYS A 1 119 ? -24.714 35.897 89.715  1.00 50.81  ? 119 LYS A CA  1 
ATOM   1031 C C   . LYS A 1 119 ? -23.881 35.684 90.970  1.00 50.08  ? 119 LYS A C   1 
ATOM   1032 O O   . LYS A 1 119 ? -22.843 35.017 90.937  1.00 46.24  ? 119 LYS A O   1 
ATOM   1033 C CB  . LYS A 1 119 ? -25.687 34.728 89.538  1.00 49.94  ? 119 LYS A CB  1 
ATOM   1034 C CG  . LYS A 1 119 ? -26.570 34.860 88.318  1.00 53.88  ? 119 LYS A CG  1 
ATOM   1035 C CD  . LYS A 1 119 ? -27.687 33.838 88.283  1.00 56.74  ? 119 LYS A CD  1 
ATOM   1036 C CE  . LYS A 1 119 ? -29.000 34.502 87.904  1.00 58.65  ? 119 LYS A CE  1 
ATOM   1037 N NZ  . LYS A 1 119 ? -30.178 33.878 88.561  1.00 60.35  ? 119 LYS A NZ  1 
ATOM   1038 N N   . GLU A 1 120 ? -24.354 36.249 92.080  1.00 51.30  ? 120 GLU A N   1 
ATOM   1039 C CA  . GLU A 1 120 ? -23.620 36.144 93.334  1.00 54.75  ? 120 GLU A CA  1 
ATOM   1040 C C   . GLU A 1 120 ? -23.614 34.707 93.840  1.00 50.72  ? 120 GLU A C   1 
ATOM   1041 O O   . GLU A 1 120 ? -22.555 34.152 94.158  1.00 46.73  ? 120 GLU A O   1 
ATOM   1042 C CB  . GLU A 1 120 ? -24.229 37.097 94.365  1.00 59.90  ? 120 GLU A CB  1 
ATOM   1043 C CG  . GLU A 1 120 ? -24.719 38.420 93.762  1.00 63.74  ? 120 GLU A CG  1 
ATOM   1044 C CD  . GLU A 1 120 ? -25.373 39.339 94.785  1.00 69.26  ? 120 GLU A CD  1 
ATOM   1045 O OE1 . GLU A 1 120 ? -24.884 39.403 95.933  1.00 69.76  ? 120 GLU A OE1 1 
ATOM   1046 O OE2 . GLU A 1 120 ? -26.377 40.004 94.439  1.00 72.37  ? 120 GLU A OE2 1 
ATOM   1047 N N   . LYS A 1 121 ? -24.788 34.085 93.902  1.00 50.89  ? 121 LYS A N   1 
ATOM   1048 C CA  . LYS A 1 121 ? -24.944 32.697 94.307  1.00 49.60  ? 121 LYS A CA  1 
ATOM   1049 C C   . LYS A 1 121 ? -25.801 31.983 93.271  1.00 45.54  ? 121 LYS A C   1 
ATOM   1050 O O   . LYS A 1 121 ? -26.579 32.608 92.545  1.00 42.82  ? 121 LYS A O   1 
ATOM   1051 C CB  . LYS A 1 121 ? -25.588 32.589 95.700  1.00 53.32  ? 121 LYS A CB  1 
ATOM   1052 C CG  . LYS A 1 121 ? -24.951 31.556 96.613  1.00 54.67  ? 121 LYS A CG  1 
ATOM   1053 C CD  . LYS A 1 121 ? -25.631 31.535 97.976  1.00 60.76  ? 121 LYS A CD  1 
ATOM   1054 C CE  . LYS A 1 121 ? -27.147 31.467 97.838  1.00 67.68  ? 121 LYS A CE  1 
ATOM   1055 N NZ  . LYS A 1 121 ? -27.609 30.161 97.278  1.00 73.24  ? 121 LYS A NZ  1 
ATOM   1056 N N   . LEU A 1 122 ? -25.657 30.662 93.197  1.00 41.65  ? 122 LEU A N   1 
ATOM   1057 C CA  . LEU A 1 122 ? -26.416 29.866 92.239  1.00 36.74  ? 122 LEU A CA  1 
ATOM   1058 C C   . LEU A 1 122 ? -27.243 28.824 92.973  1.00 36.20  ? 122 LEU A C   1 
ATOM   1059 O O   . LEU A 1 122 ? -26.731 28.125 93.856  1.00 30.26  ? 122 LEU A O   1 
ATOM   1060 C CB  . LEU A 1 122 ? -25.491 29.189 91.227  1.00 42.10  ? 122 LEU A CB  1 
ATOM   1061 C CG  . LEU A 1 122 ? -24.464 30.115 90.576  1.00 44.35  ? 122 LEU A CG  1 
ATOM   1062 C CD1 . LEU A 1 122 ? -23.192 29.334 90.282  1.00 47.51  ? 122 LEU A CD1 1 
ATOM   1063 C CD2 . LEU A 1 122 ? -25.022 30.767 89.321  1.00 43.03  ? 122 LEU A CD2 1 
ATOM   1064 N N   . ASN A 1 123 ? -28.518 28.726 92.608  1.00 30.80  ? 123 ASN A N   1 
ATOM   1065 C CA  . ASN A 1 123 ? -29.400 27.724 93.189  1.00 31.22  ? 123 ASN A CA  1 
ATOM   1066 C C   . ASN A 1 123 ? -29.260 26.422 92.401  1.00 29.46  ? 123 ASN A C   1 
ATOM   1067 O O   . ASN A 1 123 ? -28.393 26.285 91.532  1.00 29.32  ? 123 ASN A O   1 
ATOM   1068 C CB  . ASN A 1 123 ? -30.838 28.241 93.233  1.00 30.69  ? 123 ASN A CB  1 
ATOM   1069 C CG  . ASN A 1 123 ? -31.360 28.675 91.869  1.00 32.16  ? 123 ASN A CG  1 
ATOM   1070 O OD1 . ASN A 1 123 ? -30.900 28.208 90.828  1.00 28.94  ? 123 ASN A OD1 1 
ATOM   1071 N ND2 . ASN A 1 123 ? -32.347 29.566 91.876  1.00 35.09  ? 123 ASN A ND2 1 
ATOM   1072 N N   . ARG A 1 124 ? -30.122 25.447 92.696  1.00 31.58  ? 124 ARG A N   1 
ATOM   1073 C CA  . ARG A 1 124 ? -29.998 24.133 92.073  1.00 29.14  ? 124 ARG A CA  1 
ATOM   1074 C C   . ARG A 1 124 ? -30.254 24.189 90.569  1.00 30.66  ? 124 ARG A C   1 
ATOM   1075 O O   . ARG A 1 124 ? -29.522 23.567 89.790  1.00 28.15  ? 124 ARG A O   1 
ATOM   1076 C CB  . ARG A 1 124 ? -30.955 23.146 92.740  1.00 30.06  ? 124 ARG A CB  1 
ATOM   1077 C CG  . ARG A 1 124 ? -30.866 21.741 92.177  1.00 27.44  ? 124 ARG A CG  1 
ATOM   1078 C CD  . ARG A 1 124 ? -31.929 20.833 92.773  1.00 34.27  ? 124 ARG A CD  1 
ATOM   1079 N NE  . ARG A 1 124 ? -31.874 19.505 92.172  1.00 32.33  ? 124 ARG A NE  1 
ATOM   1080 C CZ  . ARG A 1 124 ? -32.460 19.182 91.023  1.00 37.24  ? 124 ARG A CZ  1 
ATOM   1081 N NH1 . ARG A 1 124 ? -33.155 20.088 90.349  1.00 36.51  ? 124 ARG A NH1 1 
ATOM   1082 N NH2 . ARG A 1 124 ? -32.352 17.948 90.549  1.00 37.75  ? 124 ARG A NH2 1 
ATOM   1083 N N   . GLU A 1 125 ? -31.295 24.912 90.145  1.00 29.09  ? 125 GLU A N   1 
ATOM   1084 C CA  . GLU A 1 125 ? -31.563 25.081 88.715  1.00 32.08  ? 125 GLU A CA  1 
ATOM   1085 C C   . GLU A 1 125 ? -30.377 25.705 87.989  1.00 27.11  ? 125 GLU A C   1 
ATOM   1086 O O   . GLU A 1 125 ? -30.050 25.322 86.857  1.00 24.24  ? 125 GLU A O   1 
ATOM   1087 C CB  . GLU A 1 125 ? -32.809 25.947 88.518  1.00 32.89  ? 125 GLU A CB  1 
ATOM   1088 C CG  . GLU A 1 125 ? -34.045 25.437 89.256  1.00 47.46  ? 125 GLU A CG  1 
ATOM   1089 C CD  . GLU A 1 125 ? -35.349 25.779 88.548  1.00 57.57  ? 125 GLU A CD  1 
ATOM   1090 O OE1 . GLU A 1 125 ? -36.365 25.101 88.820  1.00 59.96  ? 125 GLU A OE1 1 
ATOM   1091 O OE2 . GLU A 1 125 ? -35.361 26.727 87.729  1.00 61.69  ? 125 GLU A OE2 1 
ATOM   1092 N N   . GLU A 1 126 ? -29.745 26.700 88.606  1.00 26.63  ? 126 GLU A N   1 
ATOM   1093 C CA  . GLU A 1 126 ? -28.656 27.388 87.931  1.00 28.96  ? 126 GLU A CA  1 
ATOM   1094 C C   . GLU A 1 126 ? -27.408 26.517 87.858  1.00 19.38  ? 126 GLU A C   1 
ATOM   1095 O O   . GLU A 1 126 ? -26.674 26.575 86.864  1.00 22.46  ? 126 GLU A O   1 
ATOM   1096 C CB  . GLU A 1 126 ? -28.372 28.717 88.634  1.00 28.53  ? 126 GLU A CB  1 
ATOM   1097 C CG  . GLU A 1 126 ? -29.417 29.786 88.303  1.00 24.73  ? 126 GLU A CG  1 
ATOM   1098 C CD  . GLU A 1 126 ? -29.633 30.761 89.439  1.00 30.76  ? 126 GLU A CD  1 
ATOM   1099 O OE1 . GLU A 1 126 ? -29.012 30.567 90.507  1.00 32.95  ? 126 GLU A OE1 1 
ATOM   1100 O OE2 . GLU A 1 126 ? -30.432 31.714 89.267  1.00 32.96  ? 126 GLU A OE2 1 
ATOM   1101 N N   . LEU A 1 127 ? -27.157 25.691 88.879  1.00 23.80  ? 127 LEU A N   1 
ATOM   1102 C CA  . LEU A 1 127 ? -26.017 24.777 88.809  1.00 26.78  ? 127 LEU A CA  1 
ATOM   1103 C C   . LEU A 1 127 ? -26.223 23.704 87.741  1.00 24.62  ? 127 LEU A C   1 
ATOM   1104 O O   . LEU A 1 127 ? -25.268 23.317 87.057  1.00 24.03  ? 127 LEU A O   1 
ATOM   1105 C CB  . LEU A 1 127 ? -25.762 24.142 90.177  1.00 23.59  ? 127 LEU A CB  1 
ATOM   1106 C CG  . LEU A 1 127 ? -25.221 25.117 91.228  1.00 21.05  ? 127 LEU A CG  1 
ATOM   1107 C CD1 . LEU A 1 127 ? -25.320 24.519 92.615  1.00 27.49  ? 127 LEU A CD1 1 
ATOM   1108 C CD2 . LEU A 1 127 ? -23.780 25.498 90.895  1.00 24.66  ? 127 LEU A CD2 1 
ATOM   1109 N N   . LEU A 1 128 ? -27.460 23.215 87.576  1.00 24.35  ? 128 LEU A N   1 
ATOM   1110 C CA  . LEU A 1 128 ? -27.744 22.225 86.534  1.00 21.39  ? 128 LEU A CA  1 
ATOM   1111 C C   . LEU A 1 128 ? -27.451 22.783 85.149  1.00 19.60  ? 128 LEU A C   1 
ATOM   1112 O O   . LEU A 1 128 ? -26.951 22.071 84.269  1.00 25.26  ? 128 LEU A O   1 
ATOM   1113 C CB  . LEU A 1 128 ? -29.209 21.776 86.603  1.00 22.66  ? 128 LEU A CB  1 
ATOM   1114 C CG  . LEU A 1 128 ? -29.537 20.428 87.243  1.00 27.88  ? 128 LEU A CG  1 
ATOM   1115 C CD1 . LEU A 1 128 ? -31.047 20.279 87.366  1.00 28.58  ? 128 LEU A CD1 1 
ATOM   1116 C CD2 . LEU A 1 128 ? -28.926 19.255 86.458  1.00 24.17  ? 128 LEU A CD2 1 
ATOM   1117 N N   . ASP A 1 129 ? -27.780 24.053 84.929  1.00 17.11  ? 129 ASP A N   1 
ATOM   1118 C CA  . ASP A 1 129 ? -27.426 24.687 83.668  1.00 19.15  ? 129 ASP A CA  1 
ATOM   1119 C C   . ASP A 1 129 ? -25.914 24.808 83.522  1.00 21.69  ? 129 ASP A C   1 
ATOM   1120 O O   . ASP A 1 129 ? -25.368 24.555 82.444  1.00 27.71  ? 129 ASP A O   1 
ATOM   1121 C CB  . ASP A 1 129 ? -28.084 26.059 83.573  1.00 19.66  ? 129 ASP A CB  1 
ATOM   1122 C CG  . ASP A 1 129 ? -29.560 25.971 83.231  1.00 27.39  ? 129 ASP A CG  1 
ATOM   1123 O OD1 . ASP A 1 129 ? -30.107 24.846 83.297  1.00 28.03  ? 129 ASP A OD1 1 
ATOM   1124 O OD2 . ASP A 1 129 ? -30.170 27.020 82.898  1.00 27.27  ? 129 ASP A OD2 1 
ATOM   1125 N N   . LEU A 1 130 ? -25.221 25.175 84.603  1.00 16.66  ? 130 LEU A N   1 
ATOM   1126 C CA  . LEU A 1 130 ? -23.770 25.307 84.534  1.00 23.03  ? 130 LEU A CA  1 
ATOM   1127 C C   . LEU A 1 130 ? -23.112 23.967 84.231  1.00 25.14  ? 130 LEU A C   1 
ATOM   1128 O O   . LEU A 1 130 ? -22.195 23.887 83.402  1.00 19.50  ? 130 LEU A O   1 
ATOM   1129 C CB  . LEU A 1 130 ? -23.246 25.895 85.845  1.00 28.80  ? 130 LEU A CB  1 
ATOM   1130 C CG  . LEU A 1 130 ? -21.762 26.259 85.893  1.00 29.23  ? 130 LEU A CG  1 
ATOM   1131 C CD1 . LEU A 1 130 ? -21.494 27.409 84.947  1.00 27.61  ? 130 LEU A CD1 1 
ATOM   1132 C CD2 . LEU A 1 130 ? -21.383 26.618 87.313  1.00 26.59  ? 130 LEU A CD2 1 
ATOM   1133 N N   . GLN A 1 131 ? -23.563 22.907 84.909  1.00 24.14  ? 131 GLN A N   1 
ATOM   1134 C CA  . GLN A 1 131 ? -23.116 21.553 84.607  1.00 16.04  ? 131 GLN A CA  1 
ATOM   1135 C C   . GLN A 1 131 ? -23.387 21.191 83.152  1.00 19.27  ? 131 GLN A C   1 
ATOM   1136 O O   . GLN A 1 131 ? -22.493 20.717 82.437  1.00 21.09  ? 131 GLN A O   1 
ATOM   1137 C CB  . GLN A 1 131 ? -23.829 20.554 85.524  1.00 14.65  ? 131 GLN A CB  1 
ATOM   1138 C CG  . GLN A 1 131 ? -23.379 20.568 86.971  1.00 19.22  ? 131 GLN A CG  1 
ATOM   1139 C CD  . GLN A 1 131 ? -24.258 19.692 87.863  1.00 22.59  ? 131 GLN A CD  1 
ATOM   1140 O OE1 . GLN A 1 131 ? -25.487 19.691 87.743  1.00 22.65  ? 131 GLN A OE1 1 
ATOM   1141 N NE2 . GLN A 1 131 ? -23.625 18.933 88.751  1.00 22.58  ? 131 GLN A NE2 1 
ATOM   1142 N N   . THR A 1 132 ? -24.631 21.372 82.704  1.00 18.74  ? 132 THR A N   1 
ATOM   1143 C CA  . THR A 1 132 ? -25.017 20.866 81.389  1.00 14.96  ? 132 THR A CA  1 
ATOM   1144 C C   . THR A 1 132 ? -24.398 21.698 80.273  1.00 12.92  ? 132 THR A C   1 
ATOM   1145 O O   . THR A 1 132 ? -24.038 21.167 79.218  1.00 20.95  ? 132 THR A O   1 
ATOM   1146 C CB  . THR A 1 132 ? -26.546 20.838 81.270  1.00 17.53  ? 132 THR A CB  1 
ATOM   1147 O OG1 . THR A 1 132 ? -27.107 20.237 82.447  1.00 22.17  ? 132 THR A OG1 1 
ATOM   1148 C CG2 . THR A 1 132 ? -26.970 20.026 80.070  1.00 19.62  ? 132 THR A CG2 1 
ATOM   1149 N N   . LEU A 1 133 ? -24.290 23.012 80.477  1.00 21.31  ? 133 LEU A N   1 
ATOM   1150 C CA  . LEU A 1 133 ? -23.704 23.863 79.454  1.00 20.27  ? 133 LEU A CA  1 
ATOM   1151 C C   . LEU A 1 133 ? -22.202 23.632 79.323  1.00 25.12  ? 133 LEU A C   1 
ATOM   1152 O O   . LEU A 1 133 ? -21.647 23.835 78.239  1.00 20.55  ? 133 LEU A O   1 
ATOM   1153 C CB  . LEU A 1 133 ? -24.011 25.333 79.758  1.00 18.63  ? 133 LEU A CB  1 
ATOM   1154 C CG  . LEU A 1 133 ? -25.439 25.763 79.403  1.00 20.36  ? 133 LEU A CG  1 
ATOM   1155 C CD1 . LEU A 1 133 ? -25.808 27.053 80.116  1.00 23.55  ? 133 LEU A CD1 1 
ATOM   1156 C CD2 . LEU A 1 133 ? -25.571 25.922 77.898  1.00 26.51  ? 133 LEU A CD2 1 
ATOM   1157 N N   . ASN A 1 134 ? -21.528 23.208 80.405  1.00 25.74  ? 134 ASN A N   1 
ATOM   1158 C CA  . ASN A 1 134 ? -20.120 22.813 80.294  1.00 24.30  ? 134 ASN A CA  1 
ATOM   1159 C C   . ASN A 1 134 ? -19.970 21.552 79.445  1.00 24.45  ? 134 ASN A C   1 
ATOM   1160 O O   . ASN A 1 134 ? -19.049 21.454 78.618  1.00 22.13  ? 134 ASN A O   1 
ATOM   1161 C CB  . ASN A 1 134 ? -19.511 22.600 81.687  1.00 19.50  ? 134 ASN A CB  1 
ATOM   1162 C CG  . ASN A 1 134 ? -18.821 23.848 82.229  1.00 23.51  ? 134 ASN A CG  1 
ATOM   1163 O OD1 . ASN A 1 134 ? -17.655 24.135 81.891  1.00 25.39  ? 134 ASN A OD1 1 
ATOM   1164 N ND2 . ASN A 1 134 ? -19.529 24.594 83.078  1.00 20.04  ? 134 ASN A ND2 1 
ATOM   1165 N N   . LEU A 1 135 ? -20.863 20.573 79.641  1.00 20.35  ? 135 LEU A N   1 
ATOM   1166 C CA  . LEU A 1 135 ? -20.923 19.414 78.755  1.00 20.47  ? 135 LEU A CA  1 
ATOM   1167 C C   . LEU A 1 135 ? -21.163 19.834 77.307  1.00 19.91  ? 135 LEU A C   1 
ATOM   1168 O O   . LEU A 1 135 ? -20.406 19.456 76.403  1.00 20.27  ? 135 LEU A O   1 
ATOM   1169 C CB  . LEU A 1 135 ? -22.034 18.464 79.207  1.00 23.25  ? 135 LEU A CB  1 
ATOM   1170 C CG  . LEU A 1 135 ? -21.745 17.382 80.240  1.00 28.63  ? 135 LEU A CG  1 
ATOM   1171 C CD1 . LEU A 1 135 ? -22.965 16.483 80.384  1.00 27.54  ? 135 LEU A CD1 1 
ATOM   1172 C CD2 . LEU A 1 135 ? -20.533 16.572 79.828  1.00 28.81  ? 135 LEU A CD2 1 
ATOM   1173 N N   . LEU A 1 136 ? -22.212 20.632 77.075  1.00 19.68  ? 136 LEU A N   1 
ATOM   1174 C CA  . LEU A 1 136 ? -22.660 20.929 75.714  1.00 13.85  ? 136 LEU A CA  1 
ATOM   1175 C C   . LEU A 1 136 ? -21.662 21.784 74.944  1.00 21.77  ? 136 LEU A C   1 
ATOM   1176 O O   . LEU A 1 136 ? -21.626 21.734 73.707  1.00 21.65  ? 136 LEU A O   1 
ATOM   1177 C CB  . LEU A 1 136 ? -24.021 21.618 75.761  1.00 12.45  ? 136 LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 136 ? -25.166 20.645 76.030  1.00 22.88  ? 136 LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 136 ? -26.453 21.415 76.264  1.00 22.10  ? 136 LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 136 ? -25.320 19.666 74.863  1.00 21.94  ? 136 LEU A CD2 1 
ATOM   1181 N N   . ALA A 1 137 ? -20.873 22.598 75.643  1.00 24.32  ? 137 ALA A N   1 
ATOM   1182 C CA  . ALA A 1 137 ? -19.859 23.403 74.976  1.00 22.30  ? 137 ALA A CA  1 
ATOM   1183 C C   . ALA A 1 137 ? -18.783 22.548 74.316  1.00 18.25  ? 137 ALA A C   1 
ATOM   1184 O O   . ALA A 1 137 ? -18.103 23.018 73.395  1.00 18.80  ? 137 ALA A O   1 
ATOM   1185 C CB  . ALA A 1 137 ? -19.208 24.352 75.982  1.00 22.17  ? 137 ALA A CB  1 
ATOM   1186 N N   . TRP A 1 138 ? -18.586 21.322 74.787  1.00 16.92  ? 138 TRP A N   1 
ATOM   1187 C CA  . TRP A 1 138 ? -17.624 20.417 74.182  1.00 19.97  ? 138 TRP A CA  1 
ATOM   1188 C C   . TRP A 1 138 ? -18.286 19.456 73.206  1.00 17.78  ? 138 TRP A C   1 
ATOM   1189 O O   . TRP A 1 138 ? -17.677 18.452 72.821  1.00 21.48  ? 138 TRP A O   1 
ATOM   1190 C CB  . TRP A 1 138 ? -16.864 19.664 75.272  1.00 20.74  ? 138 TRP A CB  1 
ATOM   1191 C CG  . TRP A 1 138 ? -16.061 20.596 76.108  1.00 20.93  ? 138 TRP A CG  1 
ATOM   1192 C CD1 . TRP A 1 138 ? -16.455 21.217 77.256  1.00 20.18  ? 138 TRP A CD1 1 
ATOM   1193 C CD2 . TRP A 1 138 ? -14.726 21.044 75.845  1.00 19.98  ? 138 TRP A CD2 1 
ATOM   1194 N NE1 . TRP A 1 138 ? -15.439 22.008 77.740  1.00 25.12  ? 138 TRP A NE1 1 
ATOM   1195 C CE2 . TRP A 1 138 ? -14.366 21.922 76.893  1.00 22.31  ? 138 TRP A CE2 1 
ATOM   1196 C CE3 . TRP A 1 138 ? -13.803 20.785 74.836  1.00 22.45  ? 138 TRP A CE3 1 
ATOM   1197 C CZ2 . TRP A 1 138 ? -13.125 22.548 76.950  1.00 22.95  ? 138 TRP A CZ2 1 
ATOM   1198 C CZ3 . TRP A 1 138 ? -12.563 21.405 74.895  1.00 26.73  ? 138 TRP A CZ3 1 
ATOM   1199 C CH2 . TRP A 1 138 ? -12.236 22.273 75.947  1.00 25.56  ? 138 TRP A CH2 1 
ATOM   1200 N N   . CYS A 1 139 ? -19.505 19.766 72.771  1.00 18.69  ? 139 CYS A N   1 
ATOM   1201 C CA  . CYS A 1 139 ? -20.222 18.886 71.858  1.00 20.01  ? 139 CYS A CA  1 
ATOM   1202 C C   . CYS A 1 139 ? -19.529 18.829 70.501  1.00 22.77  ? 139 CYS A C   1 
ATOM   1203 O O   . CYS A 1 139 ? -19.206 19.865 69.910  1.00 22.30  ? 139 CYS A O   1 
ATOM   1204 C CB  . CYS A 1 139 ? -21.663 19.360 71.687  1.00 16.64  ? 139 CYS A CB  1 
ATOM   1205 S SG  . CYS A 1 139 ? -22.752 18.150 70.896  1.00 25.45  ? 139 CYS A SG  1 
ATOM   1206 N N   . GLY A 1 140 ? -19.320 17.609 69.997  1.00 21.87  ? 140 GLY A N   1 
ATOM   1207 C CA  . GLY A 1 140 ? -18.696 17.446 68.701  1.00 23.12  ? 140 GLY A CA  1 
ATOM   1208 C C   . GLY A 1 140 ? -19.674 17.577 67.542  1.00 19.69  ? 140 GLY A C   1 
ATOM   1209 O O   . GLY A 1 140 ? -20.890 17.707 67.712  1.00 18.26  ? 140 GLY A O   1 
ATOM   1210 N N   . ARG A 1 141 ? -19.110 17.537 66.330  1.00 19.47  ? 141 ARG A N   1 
ATOM   1211 C CA  . ARG A 1 141 ? -19.905 17.787 65.126  1.00 23.66  ? 141 ARG A CA  1 
ATOM   1212 C C   . ARG A 1 141 ? -21.085 16.823 64.997  1.00 25.32  ? 141 ARG A C   1 
ATOM   1213 O O   . ARG A 1 141 ? -22.199 17.242 64.656  1.00 20.50  ? 141 ARG A O   1 
ATOM   1214 C CB  . ARG A 1 141 ? -19.015 17.713 63.883  1.00 13.10  ? 141 ARG A CB  1 
ATOM   1215 C CG  . ARG A 1 141 ? -19.805 17.881 62.584  1.00 16.52  ? 141 ARG A CG  1 
ATOM   1216 C CD  . ARG A 1 141 ? -18.895 17.895 61.348  1.00 22.74  ? 141 ARG A CD  1 
ATOM   1217 N NE  . ARG A 1 141 ? -18.737 16.532 60.888  1.00 40.49  ? 141 ARG A NE  1 
ATOM   1218 C CZ  . ARG A 1 141 ? -19.178 16.079 59.729  1.00 30.51  ? 141 ARG A CZ  1 
ATOM   1219 N NH1 . ARG A 1 141 ? -19.782 16.896 58.877  1.00 32.62  ? 141 ARG A NH1 1 
ATOM   1220 N NH2 . ARG A 1 141 ? -18.985 14.813 59.423  1.00 34.44  ? 141 ARG A NH2 1 
ATOM   1221 N N   . THR A 1 142 ? -20.864 15.531 65.265  1.00 20.25  ? 142 THR A N   1 
ATOM   1222 C CA  . THR A 1 142 ? -21.918 14.536 65.081  1.00 22.31  ? 142 THR A CA  1 
ATOM   1223 C C   . THR A 1 142 ? -23.096 14.799 66.009  1.00 23.69  ? 142 THR A C   1 
ATOM   1224 O O   . THR A 1 142 ? -24.249 14.867 65.569  1.00 26.46  ? 142 THR A O   1 
ATOM   1225 C CB  . THR A 1 142 ? -21.366 13.133 65.325  1.00 23.74  ? 142 THR A CB  1 
ATOM   1226 O OG1 . THR A 1 142 ? -20.381 12.838 64.332  1.00 19.43  ? 142 THR A OG1 1 
ATOM   1227 C CG2 . THR A 1 142 ? -22.501 12.088 65.270  1.00 17.93  ? 142 THR A CG2 1 
ATOM   1228 N N   . LEU A 1 143 ? -22.832 14.940 67.301  1.00 21.42  ? 143 LEU A N   1 
ATOM   1229 C CA  . LEU A 1 143 ? -23.929 15.171 68.228  1.00 25.50  ? 143 LEU A CA  1 
ATOM   1230 C C   . LEU A 1 143 ? -24.444 16.607 68.192  1.00 29.62  ? 143 LEU A C   1 
ATOM   1231 O O   . LEU A 1 143 ? -25.562 16.858 68.666  1.00 25.02  ? 143 LEU A O   1 
ATOM   1232 C CB  . LEU A 1 143 ? -23.501 14.797 69.643  1.00 19.34  ? 143 LEU A CB  1 
ATOM   1233 C CG  . LEU A 1 143 ? -23.252 13.304 69.873  1.00 22.65  ? 143 LEU A CG  1 
ATOM   1234 C CD1 . LEU A 1 143 ? -22.921 13.049 71.338  1.00 17.33  ? 143 LEU A CD1 1 
ATOM   1235 C CD2 . LEU A 1 143 ? -24.474 12.486 69.436  1.00 24.76  ? 143 LEU A CD2 1 
ATOM   1236 N N   . ARG A 1 144 ? -23.669 17.553 67.641  1.00 25.12  ? 144 ARG A N   1 
ATOM   1237 C CA  . ARG A 1 144 ? -24.217 18.886 67.394  1.00 25.01  ? 144 ARG A CA  1 
ATOM   1238 C C   . ARG A 1 144 ? -25.394 18.815 66.440  1.00 30.10  ? 144 ARG A C   1 
ATOM   1239 O O   . ARG A 1 144 ? -26.348 19.593 66.565  1.00 30.62  ? 144 ARG A O   1 
ATOM   1240 C CB  . ARG A 1 144 ? -23.144 19.826 66.837  1.00 25.38  ? 144 ARG A CB  1 
ATOM   1241 C CG  . ARG A 1 144 ? -22.413 20.652 67.915  1.00 29.69  ? 144 ARG A CG  1 
ATOM   1242 C CD  . ARG A 1 144 ? -21.262 21.462 67.338  1.00 34.00  ? 144 ARG A CD  1 
ATOM   1243 N NE  . ARG A 1 144 ? -20.440 22.090 68.373  1.00 34.86  ? 144 ARG A NE  1 
ATOM   1244 C CZ  . ARG A 1 144 ? -20.634 23.323 68.829  1.00 38.93  ? 144 ARG A CZ  1 
ATOM   1245 N NH1 . ARG A 1 144 ? -21.624 24.062 68.341  1.00 37.64  ? 144 ARG A NH1 1 
ATOM   1246 N NH2 . ARG A 1 144 ? -19.841 23.821 69.771  1.00 35.69  ? 144 ARG A NH2 1 
ATOM   1247 N N   . LYS A 1 145 ? -25.349 17.889 65.486  1.00 33.75  ? 145 LYS A N   1 
ATOM   1248 C CA  . LYS A 1 145 ? -26.506 17.665 64.634  1.00 36.77  ? 145 LYS A CA  1 
ATOM   1249 C C   . LYS A 1 145 ? -27.586 16.886 65.376  1.00 33.26  ? 145 LYS A C   1 
ATOM   1250 O O   . LYS A 1 145 ? -28.769 17.230 65.290  1.00 33.98  ? 145 LYS A O   1 
ATOM   1251 C CB  . LYS A 1 145 ? -26.080 16.935 63.358  1.00 40.14  ? 145 LYS A CB  1 
ATOM   1252 C CG  . LYS A 1 145 ? -25.318 17.812 62.358  1.00 47.45  ? 145 LYS A CG  1 
ATOM   1253 C CD  . LYS A 1 145 ? -23.937 17.240 62.033  1.00 51.55  ? 145 LYS A CD  1 
ATOM   1254 C CE  . LYS A 1 145 ? -23.406 17.726 60.679  1.00 55.43  ? 145 LYS A CE  1 
ATOM   1255 N NZ  . LYS A 1 145 ? -22.813 19.108 60.704  1.00 54.12  ? 145 LYS A NZ  1 
ATOM   1256 N N   . ASP A 1 146 ? -27.199 15.863 66.140  1.00 33.67  ? 146 ASP A N   1 
ATOM   1257 C CA  . ASP A 1 146 ? -28.197 15.002 66.770  1.00 31.74  ? 146 ASP A CA  1 
ATOM   1258 C C   . ASP A 1 146 ? -28.880 15.687 67.950  1.00 34.96  ? 146 ASP A C   1 
ATOM   1259 O O   . ASP A 1 146 ? -30.088 15.519 68.154  1.00 40.33  ? 146 ASP A O   1 
ATOM   1260 C CB  . ASP A 1 146 ? -27.554 13.687 67.207  1.00 35.08  ? 146 ASP A CB  1 
ATOM   1261 C CG  . ASP A 1 146 ? -26.954 12.913 66.042  1.00 39.28  ? 146 ASP A CG  1 
ATOM   1262 O OD1 . ASP A 1 146 ? -27.180 13.296 64.875  1.00 43.29  ? 146 ASP A OD1 1 
ATOM   1263 O OD2 . ASP A 1 146 ? -26.251 11.917 66.292  1.00 43.50  ? 146 ASP A OD2 1 
ATOM   1264 N N   . LEU A 1 147 ? -28.137 16.453 68.747  1.00 30.56  ? 147 LEU A N   1 
ATOM   1265 C CA  . LEU A 1 147 ? -28.681 17.087 69.942  1.00 28.70  ? 147 LEU A CA  1 
ATOM   1266 C C   . LEU A 1 147 ? -29.038 18.550 69.715  1.00 27.84  ? 147 LEU A C   1 
ATOM   1267 O O   . LEU A 1 147 ? -29.065 19.328 70.674  1.00 32.24  ? 147 LEU A O   1 
ATOM   1268 C CB  . LEU A 1 147 ? -27.697 16.972 71.111  1.00 29.24  ? 147 LEU A CB  1 
ATOM   1269 C CG  . LEU A 1 147 ? -27.180 15.578 71.481  1.00 33.66  ? 147 LEU A CG  1 
ATOM   1270 C CD1 . LEU A 1 147 ? -25.997 15.634 72.451  1.00 29.83  ? 147 LEU A CD1 1 
ATOM   1271 C CD2 . LEU A 1 147 ? -28.300 14.734 72.050  1.00 37.22  ? 147 LEU A CD2 1 
ATOM   1272 N N   . LYS A 1 148 ? -29.319 18.944 68.468  1.00 21.25  ? 148 LYS A N   1 
ATOM   1273 C CA  . LYS A 1 148 ? -29.453 20.366 68.167  1.00 29.74  ? 148 LYS A CA  1 
ATOM   1274 C C   . LYS A 1 148 ? -30.530 21.038 69.024  1.00 34.22  ? 148 LYS A C   1 
ATOM   1275 O O   . LYS A 1 148 ? -30.359 22.196 69.431  1.00 32.98  ? 148 LYS A O   1 
ATOM   1276 C CB  . LYS A 1 148 ? -29.730 20.556 66.671  1.00 32.25  ? 148 LYS A CB  1 
ATOM   1277 C CG  . LYS A 1 148 ? -31.199 20.726 66.296  1.00 40.31  ? 148 LYS A CG  1 
ATOM   1278 C CD  . LYS A 1 148 ? -31.397 20.841 64.784  1.00 49.24  ? 148 LYS A CD  1 
ATOM   1279 C CE  . LYS A 1 148 ? -30.352 21.753 64.148  1.00 57.95  ? 148 LYS A CE  1 
ATOM   1280 N NZ  . LYS A 1 148 ? -30.283 23.091 64.797  1.00 60.06  ? 148 LYS A NZ  1 
ATOM   1281 N N   . ASP A 1 149 ? -31.615 20.320 69.355  1.00 31.62  ? 149 ASP A N   1 
ATOM   1282 C CA  . ASP A 1 149 ? -32.723 20.946 70.075  1.00 37.32  ? 149 ASP A CA  1 
ATOM   1283 C C   . ASP A 1 149 ? -32.357 21.245 71.529  1.00 38.35  ? 149 ASP A C   1 
ATOM   1284 O O   . ASP A 1 149 ? -32.745 22.289 72.065  1.00 38.31  ? 149 ASP A O   1 
ATOM   1285 C CB  . ASP A 1 149 ? -33.971 20.065 69.993  1.00 37.31  ? 149 ASP A CB  1 
ATOM   1286 C CG  . ASP A 1 149 ? -34.429 19.834 68.556  1.00 40.05  ? 149 ASP A CG  1 
ATOM   1287 O OD1 . ASP A 1 149 ? -34.372 20.781 67.742  1.00 44.64  ? 149 ASP A OD1 1 
ATOM   1288 O OD2 . ASP A 1 149 ? -34.829 18.697 68.235  1.00 43.75  ? 149 ASP A OD2 1 
ATOM   1289 N N   . LEU A 1 150 ? -31.612 20.350 72.186  1.00 33.46  ? 150 LEU A N   1 
ATOM   1290 C CA  . LEU A 1 150 ? -31.108 20.670 73.522  1.00 32.48  ? 150 LEU A CA  1 
ATOM   1291 C C   . LEU A 1 150 ? -30.068 21.782 73.465  1.00 28.48  ? 150 LEU A C   1 
ATOM   1292 O O   . LEU A 1 150 ? -30.017 22.641 74.354  1.00 25.47  ? 150 LEU A O   1 
ATOM   1293 C CB  . LEU A 1 150 ? -30.511 19.426 74.185  1.00 31.24  ? 150 LEU A CB  1 
ATOM   1294 C CG  . LEU A 1 150 ? -31.473 18.268 74.440  1.00 35.87  ? 150 LEU A CG  1 
ATOM   1295 C CD1 . LEU A 1 150 ? -30.704 17.050 74.938  1.00 32.34  ? 150 LEU A CD1 1 
ATOM   1296 C CD2 . LEU A 1 150 ? -32.586 18.673 75.412  1.00 34.02  ? 150 LEU A CD2 1 
ATOM   1297 N N   . LEU A 1 151 ? -29.221 21.776 72.431  1.00 31.76  ? 151 LEU A N   1 
ATOM   1298 C CA  . LEU A 1 151 ? -28.204 22.815 72.291  1.00 33.10  ? 151 LEU A CA  1 
ATOM   1299 C C   . LEU A 1 151 ? -28.839 24.194 72.156  1.00 36.25  ? 151 LEU A C   1 
ATOM   1300 O O   . LEU A 1 151 ? -28.438 25.140 72.844  1.00 39.14  ? 151 LEU A O   1 
ATOM   1301 C CB  . LEU A 1 151 ? -27.316 22.523 71.084  1.00 38.71  ? 151 LEU A CB  1 
ATOM   1302 C CG  . LEU A 1 151 ? -26.052 21.687 71.266  1.00 38.81  ? 151 LEU A CG  1 
ATOM   1303 C CD1 . LEU A 1 151 ? -25.508 21.318 69.893  1.00 39.60  ? 151 LEU A CD1 1 
ATOM   1304 C CD2 . LEU A 1 151 ? -24.992 22.428 72.087  1.00 34.21  ? 151 LEU A CD2 1 
ATOM   1305 N N   . ASN A 1 152 ? -29.834 24.327 71.270  1.00 37.85  ? 152 ASN A N   1 
ATOM   1306 C CA  . ASN A 1 152 ? -30.519 25.603 71.062  1.00 40.12  ? 152 ASN A CA  1 
ATOM   1307 C C   . ASN A 1 152 ? -31.407 25.988 72.235  1.00 37.69  ? 152 ASN A C   1 
ATOM   1308 O O   . ASN A 1 152 ? -31.831 27.147 72.326  1.00 36.10  ? 152 ASN A O   1 
ATOM   1309 C CB  . ASN A 1 152 ? -31.370 25.558 69.790  1.00 42.14  ? 152 ASN A CB  1 
ATOM   1310 C CG  . ASN A 1 152 ? -30.536 25.466 68.526  1.00 44.29  ? 152 ASN A CG  1 
ATOM   1311 O OD1 . ASN A 1 152 ? -29.313 25.629 68.552  1.00 43.98  ? 152 ASN A OD1 1 
ATOM   1312 N ND2 . ASN A 1 152 ? -31.199 25.209 67.405  1.00 44.15  ? 152 ASN A ND2 1 
ATOM   1313 N N   . LYS A 1 153 ? -31.733 25.030 73.101  1.00 36.62  ? 153 LYS A N   1 
ATOM   1314 C CA  . LYS A 1 153 ? -32.423 25.338 74.347  1.00 37.55  ? 153 LYS A CA  1 
ATOM   1315 C C   . LYS A 1 153 ? -31.652 26.388 75.138  1.00 39.49  ? 153 LYS A C   1 
ATOM   1316 O O   . LYS A 1 153 ? -32.210 27.409 75.558  1.00 39.52  ? 153 LYS A O   1 
ATOM   1317 C CB  . LYS A 1 153 ? -32.582 24.052 75.160  1.00 36.71  ? 153 LYS A CB  1 
ATOM   1318 C CG  . LYS A 1 153 ? -33.681 24.062 76.179  1.00 40.31  ? 153 LYS A CG  1 
ATOM   1319 C CD  . LYS A 1 153 ? -33.623 22.823 77.062  1.00 27.02  ? 153 LYS A CD  1 
ATOM   1320 C CE  . LYS A 1 153 ? -34.374 23.102 78.347  1.00 26.33  ? 153 LYS A CE  1 
ATOM   1321 N NZ  . LYS A 1 153 ? -34.615 21.879 79.151  1.00 37.44  ? 153 LYS A NZ  1 
ATOM   1322 N N   . GLY A 1 154 ? -30.356 26.144 75.349  1.00 30.87  ? 154 GLY A N   1 
ATOM   1323 C CA  . GLY A 1 154 ? -29.458 27.117 75.924  1.00 30.33  ? 154 GLY A CA  1 
ATOM   1324 C C   . GLY A 1 154 ? -29.556 27.321 77.416  1.00 29.00  ? 154 GLY A C   1 
ATOM   1325 O O   . GLY A 1 154 ? -28.691 27.998 77.979  1.00 29.21  ? 154 GLY A O   1 
ATOM   1326 N N   . ARG A 1 155 ? -30.559 26.755 78.085  1.00 32.71  ? 155 ARG A N   1 
ATOM   1327 C CA  . ARG A 1 155 ? -30.834 27.077 79.483  1.00 29.54  ? 155 ARG A CA  1 
ATOM   1328 C C   . ARG A 1 155 ? -31.887 26.106 79.994  1.00 25.37  ? 155 ARG A C   1 
ATOM   1329 O O   . ARG A 1 155 ? -32.468 25.345 79.221  1.00 28.64  ? 155 ARG A O   1 
ATOM   1330 C CB  . ARG A 1 155 ? -31.315 28.526 79.639  1.00 29.93  ? 155 ARG A CB  1 
ATOM   1331 C CG  . ARG A 1 155 ? -32.626 28.817 78.903  1.00 37.56  ? 155 ARG A CG  1 
ATOM   1332 C CD  . ARG A 1 155 ? -33.073 30.265 79.079  1.00 37.50  ? 155 ARG A CD  1 
ATOM   1333 N NE  . ARG A 1 155 ? -32.091 31.209 78.549  1.00 37.47  ? 155 ARG A NE  1 
ATOM   1334 C CZ  . ARG A 1 155 ? -31.428 32.088 79.295  1.00 36.49  ? 155 ARG A CZ  1 
ATOM   1335 N NH1 . ARG A 1 155 ? -30.550 32.909 78.732  1.00 41.28  ? 155 ARG A NH1 1 
ATOM   1336 N NH2 . ARG A 1 155 ? -31.646 32.149 80.605  1.00 35.51  ? 155 ARG A NH2 1 
ATOM   1337 N N   . ASN A 1 156 ? -32.135 26.157 81.308  1.00 25.80  ? 156 ASN A N   1 
ATOM   1338 C CA  . ASN A 1 156 ? -33.222 25.418 81.968  1.00 30.58  ? 156 ASN A CA  1 
ATOM   1339 C C   . ASN A 1 156 ? -33.118 23.906 81.750  1.00 28.02  ? 156 ASN A C   1 
ATOM   1340 O O   . ASN A 1 156 ? -34.100 23.234 81.418  1.00 23.17  ? 156 ASN A O   1 
ATOM   1341 C CB  . ASN A 1 156 ? -34.599 25.918 81.518  1.00 30.24  ? 156 ASN A CB  1 
ATOM   1342 C CG  . ASN A 1 156 ? -34.744 27.422 81.608  1.00 38.35  ? 156 ASN A CG  1 
ATOM   1343 O OD1 . ASN A 1 156 ? -34.208 28.060 82.519  1.00 42.24  ? 156 ASN A OD1 1 
ATOM   1344 N ND2 . ASN A 1 156 ? -35.481 27.999 80.663  1.00 33.49  ? 156 ASN A ND2 1 
ATOM   1345 N N   . TYR A 1 157 ? -31.926 23.367 81.972  1.00 19.82  ? 157 TYR A N   1 
ATOM   1346 C CA  . TYR A 1 157 ? -31.681 21.951 81.752  1.00 22.61  ? 157 TYR A CA  1 
ATOM   1347 C C   . TYR A 1 157 ? -32.111 21.132 82.965  1.00 22.65  ? 157 TYR A C   1 
ATOM   1348 O O   . TYR A 1 157 ? -31.995 21.567 84.115  1.00 29.70  ? 157 TYR A O   1 
ATOM   1349 C CB  . TYR A 1 157 ? -30.193 21.715 81.440  1.00 20.12  ? 157 TYR A CB  1 
ATOM   1350 C CG  . TYR A 1 157 ? -29.800 22.264 80.084  1.00 21.56  ? 157 TYR A CG  1 
ATOM   1351 C CD1 . TYR A 1 157 ? -30.189 21.611 78.916  1.00 25.08  ? 157 TYR A CD1 1 
ATOM   1352 C CD2 . TYR A 1 157 ? -29.081 23.449 79.961  1.00 16.95  ? 157 TYR A CD2 1 
ATOM   1353 C CE1 . TYR A 1 157 ? -29.855 22.107 77.667  1.00 20.74  ? 157 TYR A CE1 1 
ATOM   1354 C CE2 . TYR A 1 157 ? -28.747 23.960 78.703  1.00 19.85  ? 157 TYR A CE2 1 
ATOM   1355 C CZ  . TYR A 1 157 ? -29.139 23.281 77.565  1.00 22.32  ? 157 TYR A CZ  1 
ATOM   1356 O OH  . TYR A 1 157 ? -28.808 23.756 76.313  1.00 23.42  ? 157 TYR A OH  1 
ATOM   1357 N N   . THR A 1 158 ? -32.608 19.934 82.703  1.00 18.42  ? 158 THR A N   1 
ATOM   1358 C CA  . THR A 1 158 ? -32.957 19.016 83.776  1.00 17.40  ? 158 THR A CA  1 
ATOM   1359 C C   . THR A 1 158 ? -31.882 17.956 83.933  1.00 18.65  ? 158 THR A C   1 
ATOM   1360 O O   . THR A 1 158 ? -31.101 17.696 83.017  1.00 22.98  ? 158 THR A O   1 
ATOM   1361 C CB  . THR A 1 158 ? -34.306 18.333 83.524  1.00 20.66  ? 158 THR A CB  1 
ATOM   1362 O OG1 . THR A 1 158 ? -34.160 17.335 82.500  1.00 21.05  ? 158 THR A OG1 1 
ATOM   1363 C CG2 . THR A 1 158 ? -35.383 19.353 83.128  1.00 22.52  ? 158 THR A CG2 1 
ATOM   1364 N N   . GLN A 1 159 ? -31.852 17.348 85.126  1.00 20.16  ? 159 GLN A N   1 
ATOM   1365 C CA  . GLN A 1 159 ? -30.984 16.199 85.364  1.00 24.26  ? 159 GLN A CA  1 
ATOM   1366 C C   . GLN A 1 159 ? -31.143 15.147 84.272  1.00 26.81  ? 159 GLN A C   1 
ATOM   1367 O O   . GLN A 1 159 ? -30.152 14.568 83.809  1.00 25.18  ? 159 GLN A O   1 
ATOM   1368 C CB  . GLN A 1 159 ? -31.284 15.592 86.741  1.00 23.29  ? 159 GLN A CB  1 
ATOM   1369 C CG  . GLN A 1 159 ? -30.375 14.430 87.126  1.00 26.13  ? 159 GLN A CG  1 
ATOM   1370 C CD  . GLN A 1 159 ? -28.936 14.854 87.378  1.00 27.04  ? 159 GLN A CD  1 
ATOM   1371 O OE1 . GLN A 1 159 ? -28.656 16.018 87.661  1.00 24.53  ? 159 GLN A OE1 1 
ATOM   1372 N NE2 . GLN A 1 159 ? -28.012 13.892 87.289  1.00 25.07  ? 159 GLN A NE2 1 
ATOM   1373 N N   . GLU A 1 160 ? -32.378 14.910 83.821  1.00 19.69  ? 160 GLU A N   1 
ATOM   1374 C CA  . GLU A 1 160 ? -32.603 13.868 82.819  1.00 23.15  ? 160 GLU A CA  1 
ATOM   1375 C C   . GLU A 1 160 ? -31.963 14.231 81.488  1.00 17.54  ? 160 GLU A C   1 
ATOM   1376 O O   . GLU A 1 160 ? -31.350 13.379 80.830  1.00 25.18  ? 160 GLU A O   1 
ATOM   1377 C CB  . GLU A 1 160 ? -34.101 13.613 82.640  1.00 25.23  ? 160 GLU A CB  1 
ATOM   1378 C CG  . GLU A 1 160 ? -34.472 12.844 81.372  1.00 32.35  ? 160 GLU A CG  1 
ATOM   1379 C CD  . GLU A 1 160 ? -33.887 11.450 81.338  1.00 50.35  ? 160 GLU A CD  1 
ATOM   1380 O OE1 . GLU A 1 160 ? -33.725 10.842 82.421  1.00 56.56  ? 160 GLU A OE1 1 
ATOM   1381 O OE2 . GLU A 1 160 ? -33.592 10.961 80.223  1.00 57.45  ? 160 GLU A OE2 1 
ATOM   1382 N N   . GLU A 1 161 ? -32.104 15.485 81.079  1.00 16.49  ? 161 GLU A N   1 
ATOM   1383 C CA  . GLU A 1 161 ? -31.477 15.954 79.854  1.00 18.79  ? 161 GLU A CA  1 
ATOM   1384 C C   . GLU A 1 161 ? -29.960 15.905 79.960  1.00 19.97  ? 161 GLU A C   1 
ATOM   1385 O O   . GLU A 1 161 ? -29.277 15.563 78.986  1.00 23.45  ? 161 GLU A O   1 
ATOM   1386 C CB  . GLU A 1 161 ? -31.962 17.372 79.546  1.00 20.25  ? 161 GLU A CB  1 
ATOM   1387 C CG  . GLU A 1 161 ? -33.458 17.414 79.165  1.00 24.26  ? 161 GLU A CG  1 
ATOM   1388 C CD  . GLU A 1 161 ? -34.024 18.822 79.133  1.00 29.59  ? 161 GLU A CD  1 
ATOM   1389 O OE1 . GLU A 1 161 ? -33.281 19.779 79.451  1.00 25.66  ? 161 GLU A OE1 1 
ATOM   1390 O OE2 . GLU A 1 161 ? -35.220 18.969 78.804  1.00 33.51  ? 161 GLU A OE2 1 
ATOM   1391 N N   . LYS A 1 162 ? -29.409 16.248 81.129  1.00 21.01  ? 162 LYS A N   1 
ATOM   1392 C CA  . LYS A 1 162 ? -27.959 16.185 81.308  1.00 21.57  ? 162 LYS A CA  1 
ATOM   1393 C C   . LYS A 1 162 ? -27.448 14.748 81.199  1.00 24.12  ? 162 LYS A C   1 
ATOM   1394 O O   . LYS A 1 162 ? -26.422 14.488 80.546  1.00 21.64  ? 162 LYS A O   1 
ATOM   1395 C CB  . LYS A 1 162 ? -27.584 16.804 82.655  1.00 20.91  ? 162 LYS A CB  1 
ATOM   1396 C CG  . LYS A 1 162 ? -26.111 16.761 82.997  1.00 17.47  ? 162 LYS A CG  1 
ATOM   1397 C CD  . LYS A 1 162 ? -25.837 17.373 84.373  1.00 19.03  ? 162 LYS A CD  1 
ATOM   1398 C CE  . LYS A 1 162 ? -26.389 16.545 85.503  1.00 24.24  ? 162 LYS A CE  1 
ATOM   1399 N NZ  . LYS A 1 162 ? -25.933 17.029 86.859  1.00 20.20  ? 162 LYS A NZ  1 
ATOM   1400 N N   . GLU A 1 163 ? -28.152 13.804 81.831  1.00 17.08  ? 163 GLU A N   1 
ATOM   1401 C CA  . GLU A 1 163 ? -27.779 12.396 81.747  1.00 23.73  ? 163 GLU A CA  1 
ATOM   1402 C C   . GLU A 1 163 ? -27.971 11.846 80.337  1.00 23.78  ? 163 GLU A C   1 
ATOM   1403 O O   . GLU A 1 163 ? -27.211 10.972 79.909  1.00 23.54  ? 163 GLU A O   1 
ATOM   1404 C CB  . GLU A 1 163 ? -28.593 11.571 82.751  1.00 27.34  ? 163 GLU A CB  1 
ATOM   1405 C CG  . GLU A 1 163 ? -28.121 11.699 84.210  1.00 30.36  ? 163 GLU A CG  1 
ATOM   1406 C CD  . GLU A 1 163 ? -29.083 11.042 85.193  1.00 41.24  ? 163 GLU A CD  1 
ATOM   1407 O OE1 . GLU A 1 163 ? -28.857 11.144 86.423  1.00 42.74  ? 163 GLU A OE1 1 
ATOM   1408 O OE2 . GLU A 1 163 ? -30.069 10.426 84.734  1.00 41.32  ? 163 GLU A OE2 1 
ATOM   1409 N N   . TYR A 1 164 ? -28.965 12.344 79.604  1.00 23.10  ? 164 TYR A N   1 
ATOM   1410 C CA  . TYR A 1 164 ? -29.108 11.950 78.203  1.00 26.81  ? 164 TYR A CA  1 
ATOM   1411 C C   . TYR A 1 164 ? -27.879 12.355 77.399  1.00 26.93  ? 164 TYR A C   1 
ATOM   1412 O O   . TYR A 1 164 ? -27.314 11.549 76.644  1.00 24.37  ? 164 TYR A O   1 
ATOM   1413 C CB  . TYR A 1 164 ? -30.372 12.570 77.611  1.00 23.43  ? 164 TYR A CB  1 
ATOM   1414 C CG  . TYR A 1 164 ? -30.624 12.128 76.193  1.00 29.37  ? 164 TYR A CG  1 
ATOM   1415 C CD1 . TYR A 1 164 ? -31.079 10.843 75.919  1.00 36.14  ? 164 TYR A CD1 1 
ATOM   1416 C CD2 . TYR A 1 164 ? -30.372 12.978 75.123  1.00 29.12  ? 164 TYR A CD2 1 
ATOM   1417 C CE1 . TYR A 1 164 ? -31.300 10.427 74.627  1.00 36.60  ? 164 TYR A CE1 1 
ATOM   1418 C CE2 . TYR A 1 164 ? -30.591 12.567 73.819  1.00 31.12  ? 164 TYR A CE2 1 
ATOM   1419 C CZ  . TYR A 1 164 ? -31.054 11.293 73.580  1.00 37.92  ? 164 TYR A CZ  1 
ATOM   1420 O OH  . TYR A 1 164 ? -31.274 10.877 72.287  1.00 41.11  ? 164 TYR A OH  1 
ATOM   1421 N N   . VAL A 1 165 ? -27.444 13.605 77.565  1.00 19.88  ? 165 VAL A N   1 
ATOM   1422 C CA  . VAL A 1 165 ? -26.244 14.090 76.885  1.00 18.21  ? 165 VAL A CA  1 
ATOM   1423 C C   . VAL A 1 165 ? -25.035 13.240 77.261  1.00 15.47  ? 165 VAL A C   1 
ATOM   1424 O O   . VAL A 1 165 ? -24.259 12.818 76.397  1.00 23.73  ? 165 VAL A O   1 
ATOM   1425 C CB  . VAL A 1 165 ? -26.019 15.573 77.213  1.00 17.58  ? 165 VAL A CB  1 
ATOM   1426 C CG1 . VAL A 1 165 ? -24.623 16.006 76.776  1.00 16.30  ? 165 VAL A CG1 1 
ATOM   1427 C CG2 . VAL A 1 165 ? -27.090 16.451 76.529  1.00 17.33  ? 165 VAL A CG2 1 
ATOM   1428 N N   . LEU A 1 166 ? -24.837 13.010 78.566  1.00 14.33  ? 166 LEU A N   1 
ATOM   1429 C CA  . LEU A 1 166 ? -23.735 12.168 79.027  1.00 20.52  ? 166 LEU A CA  1 
ATOM   1430 C C   . LEU A 1 166 ? -23.757 10.794 78.364  1.00 23.65  ? 166 LEU A C   1 
ATOM   1431 O O   . LEU A 1 166 ? -22.706 10.277 77.960  1.00 25.20  ? 166 LEU A O   1 
ATOM   1432 C CB  . LEU A 1 166 ? -23.795 12.017 80.550  1.00 22.33  ? 166 LEU A CB  1 
ATOM   1433 C CG  . LEU A 1 166 ? -22.981 13.011 81.368  1.00 31.84  ? 166 LEU A CG  1 
ATOM   1434 C CD1 . LEU A 1 166 ? -23.136 12.700 82.851  1.00 37.92  ? 166 LEU A CD1 1 
ATOM   1435 C CD2 . LEU A 1 166 ? -21.511 12.997 80.952  1.00 26.30  ? 166 LEU A CD2 1 
ATOM   1436 N N   . ASN A 1 167 ? -24.941 10.178 78.273  1.00 18.00  ? 167 ASN A N   1 
ATOM   1437 C CA  . ASN A 1 167 ? -25.080 8.874  77.624  1.00 22.86  ? 167 ASN A CA  1 
ATOM   1438 C C   . ASN A 1 167 ? -24.648 8.937  76.172  1.00 20.42  ? 167 ASN A C   1 
ATOM   1439 O O   . ASN A 1 167 ? -23.941 8.047  75.682  1.00 26.83  ? 167 ASN A O   1 
ATOM   1440 C CB  . ASN A 1 167 ? -26.527 8.391  77.699  1.00 26.02  ? 167 ASN A CB  1 
ATOM   1441 C CG  . ASN A 1 167 ? -26.849 7.721  79.016  1.00 44.26  ? 167 ASN A CG  1 
ATOM   1442 O OD1 . ASN A 1 167 ? -25.957 7.211  79.698  1.00 46.13  ? 167 ASN A OD1 1 
ATOM   1443 N ND2 . ASN A 1 167 ? -28.127 7.714  79.384  1.00 53.51  ? 167 ASN A ND2 1 
ATOM   1444 N N   . LYS A 1 168 ? -25.085 9.972  75.455  1.00 17.36  ? 168 LYS A N   1 
ATOM   1445 C CA  . LYS A 1 168 ? -24.690 10.081 74.060  1.00 19.20  ? 168 LYS A CA  1 
ATOM   1446 C C   . LYS A 1 168 ? -23.190 10.307 73.928  1.00 16.70  ? 168 LYS A C   1 
ATOM   1447 O O   . LYS A 1 168 ? -22.575 9.802  72.987  1.00 20.34  ? 168 LYS A O   1 
ATOM   1448 C CB  . LYS A 1 168 ? -25.470 11.201 73.373  1.00 21.37  ? 168 LYS A CB  1 
ATOM   1449 C CG  . LYS A 1 168 ? -26.981 11.012 73.434  1.00 26.17  ? 168 LYS A CG  1 
ATOM   1450 C CD  . LYS A 1 168 ? -27.411 9.682  72.844  1.00 30.97  ? 168 LYS A CD  1 
ATOM   1451 C CE  . LYS A 1 168 ? -27.277 9.685  71.339  1.00 39.56  ? 168 LYS A CE  1 
ATOM   1452 N NZ  . LYS A 1 168 ? -27.964 8.515  70.713  1.00 41.79  ? 168 LYS A NZ  1 
ATOM   1453 N N   . TYR A 1 169 ? -22.590 11.052 74.858  1.00 16.81  ? 169 TYR A N   1 
ATOM   1454 C CA  . TYR A 1 169 ? -21.151 11.289 74.801  1.00 15.42  ? 169 TYR A CA  1 
ATOM   1455 C C   . TYR A 1 169 ? -20.375 9.994  74.967  1.00 17.94  ? 169 TYR A C   1 
ATOM   1456 O O   . TYR A 1 169 ? -19.394 9.755  74.256  1.00 21.90  ? 169 TYR A O   1 
ATOM   1457 C CB  . TYR A 1 169 ? -20.733 12.287 75.880  1.00 16.96  ? 169 TYR A CB  1 
ATOM   1458 C CG  . TYR A 1 169 ? -20.944 13.747 75.531  1.00 15.80  ? 169 TYR A CG  1 
ATOM   1459 C CD1 . TYR A 1 169 ? -21.757 14.126 74.476  1.00 19.05  ? 169 TYR A CD1 1 
ATOM   1460 C CD2 . TYR A 1 169 ? -20.322 14.745 76.270  1.00 18.35  ? 169 TYR A CD2 1 
ATOM   1461 C CE1 . TYR A 1 169 ? -21.950 15.472 74.161  1.00 23.65  ? 169 TYR A CE1 1 
ATOM   1462 C CE2 . TYR A 1 169 ? -20.501 16.100 75.956  1.00 14.57  ? 169 TYR A CE2 1 
ATOM   1463 C CZ  . TYR A 1 169 ? -21.322 16.452 74.912  1.00 21.21  ? 169 TYR A CZ  1 
ATOM   1464 O OH  . TYR A 1 169 ? -21.504 17.789 74.608  1.00 20.29  ? 169 TYR A OH  1 
ATOM   1465 N N   . PHE A 1 170 ? -20.794 9.144  75.914  1.00 17.93  ? 170 PHE A N   1 
ATOM   1466 C CA  . PHE A 1 170 ? -20.104 7.877  76.116  1.00 18.00  ? 170 PHE A CA  1 
ATOM   1467 C C   . PHE A 1 170 ? -20.311 6.932  74.938  1.00 22.09  ? 170 PHE A C   1 
ATOM   1468 O O   . PHE A 1 170 ? -19.411 6.144  74.612  1.00 17.74  ? 170 PHE A O   1 
ATOM   1469 C CB  . PHE A 1 170 ? -20.545 7.247  77.442  1.00 16.55  ? 170 PHE A CB  1 
ATOM   1470 C CG  . PHE A 1 170 ? -19.725 7.720  78.604  1.00 19.40  ? 170 PHE A CG  1 
ATOM   1471 C CD1 . PHE A 1 170 ? -18.433 7.251  78.789  1.00 19.62  ? 170 PHE A CD1 1 
ATOM   1472 C CD2 . PHE A 1 170 ? -20.209 8.705  79.461  1.00 27.27  ? 170 PHE A CD2 1 
ATOM   1473 C CE1 . PHE A 1 170 ? -17.643 7.725  79.847  1.00 22.90  ? 170 PHE A CE1 1 
ATOM   1474 C CE2 . PHE A 1 170 ? -19.430 9.177  80.511  1.00 27.99  ? 170 PHE A CE2 1 
ATOM   1475 C CZ  . PHE A 1 170 ? -18.146 8.681  80.705  1.00 28.68  ? 170 PHE A CZ  1 
ATOM   1476 N N   . GLU A 1 171 ? -21.465 7.017  74.278  1.00 18.29  ? 171 GLU A N   1 
ATOM   1477 C CA  . GLU A 1 171 ? -21.655 6.304  73.018  1.00 27.92  ? 171 GLU A CA  1 
ATOM   1478 C C   . GLU A 1 171 ? -20.603 6.714  71.993  1.00 28.29  ? 171 GLU A C   1 
ATOM   1479 O O   . GLU A 1 171 ? -20.046 5.860  71.286  1.00 27.23  ? 171 GLU A O   1 
ATOM   1480 C CB  . GLU A 1 171 ? -23.062 6.568  72.476  1.00 27.42  ? 171 GLU A CB  1 
ATOM   1481 C CG  . GLU A 1 171 ? -24.169 5.977  73.347  1.00 38.69  ? 171 GLU A CG  1 
ATOM   1482 C CD  . GLU A 1 171 ? -25.562 6.179  72.762  1.00 45.50  ? 171 GLU A CD  1 
ATOM   1483 O OE1 . GLU A 1 171 ? -25.668 6.660  71.613  1.00 45.17  ? 171 GLU A OE1 1 
ATOM   1484 O OE2 . GLU A 1 171 ? -26.552 5.860  73.457  1.00 51.57  ? 171 GLU A OE2 1 
ATOM   1485 N N   . ILE A 1 172 ? -20.317 8.019  71.906  1.00 20.62  ? 172 ILE A N   1 
ATOM   1486 C CA  . ILE A 1 172 ? -19.297 8.515  70.985  1.00 21.91  ? 172 ILE A CA  1 
ATOM   1487 C C   . ILE A 1 172 ? -17.931 7.931  71.341  1.00 21.70  ? 172 ILE A C   1 
ATOM   1488 O O   . ILE A 1 172 ? -17.206 7.423  70.474  1.00 20.99  ? 172 ILE A O   1 
ATOM   1489 C CB  . ILE A 1 172 ? -19.279 10.059 70.988  1.00 24.93  ? 172 ILE A CB  1 
ATOM   1490 C CG1 . ILE A 1 172 ? -20.507 10.646 70.276  1.00 26.26  ? 172 ILE A CG1 1 
ATOM   1491 C CG2 . ILE A 1 172 ? -18.007 10.609 70.352  1.00 23.51  ? 172 ILE A CG2 1 
ATOM   1492 C CD1 . ILE A 1 172 ? -20.599 10.348 68.786  1.00 24.02  ? 172 ILE A CD1 1 
ATOM   1493 N N   . ILE A 1 173 ? -17.560 7.994  72.625  1.00 22.00  ? 173 ILE A N   1 
ATOM   1494 C CA  . ILE A 1 173 ? -16.274 7.451  73.056  1.00 19.76  ? 173 ILE A CA  1 
ATOM   1495 C C   . ILE A 1 173 ? -16.176 5.963  72.729  1.00 24.71  ? 173 ILE A C   1 
ATOM   1496 O O   . ILE A 1 173 ? -15.132 5.483  72.266  1.00 29.90  ? 173 ILE A O   1 
ATOM   1497 C CB  . ILE A 1 173 ? -16.049 7.733  74.555  1.00 23.16  ? 173 ILE A CB  1 
ATOM   1498 C CG1 . ILE A 1 173 ? -15.943 9.251  74.780  1.00 16.55  ? 173 ILE A CG1 1 
ATOM   1499 C CG2 . ILE A 1 173 ? -14.782 7.002  75.051  1.00 19.78  ? 173 ILE A CG2 1 
ATOM   1500 C CD1 . ILE A 1 173 ? -15.989 9.712  76.255  1.00 19.54  ? 173 ILE A CD1 1 
ATOM   1501 N N   . LYS A 1 174 ? -17.261 5.213  72.934  1.00 22.29  ? 174 LYS A N   1 
ATOM   1502 C CA  . LYS A 1 174 ? -17.237 3.773  72.676  1.00 21.93  ? 174 LYS A CA  1 
ATOM   1503 C C   . LYS A 1 174 ? -17.048 3.434  71.200  1.00 23.27  ? 174 LYS A C   1 
ATOM   1504 O O   . LYS A 1 174 ? -16.602 2.323  70.891  1.00 24.31  ? 174 LYS A O   1 
ATOM   1505 C CB  . LYS A 1 174 ? -18.527 3.114  73.181  1.00 24.50  ? 174 LYS A CB  1 
ATOM   1506 C CG  . LYS A 1 174 ? -18.655 3.107  74.704  1.00 28.81  ? 174 LYS A CG  1 
ATOM   1507 C CD  . LYS A 1 174 ? -19.850 2.280  75.163  1.00 35.93  ? 174 LYS A CD  1 
ATOM   1508 C CE  . LYS A 1 174 ? -20.418 2.804  76.476  1.00 38.70  ? 174 LYS A CE  1 
ATOM   1509 N NZ  . LYS A 1 174 ? -19.522 2.549  77.637  1.00 43.42  ? 174 LYS A NZ  1 
ATOM   1510 N N   . LYS A 1 175 ? -17.378 4.353  70.291  1.00 20.23  ? 175 LYS A N   1 
ATOM   1511 C CA  . LYS A 1 175 ? -17.219 4.161  68.852  1.00 22.40  ? 175 LYS A CA  1 
ATOM   1512 C C   . LYS A 1 175 ? -15.903 4.717  68.308  1.00 26.27  ? 175 LYS A C   1 
ATOM   1513 O O   . LYS A 1 175 ? -15.662 4.621  67.099  1.00 26.41  ? 175 LYS A O   1 
ATOM   1514 C CB  . LYS A 1 175 ? -18.382 4.828  68.105  1.00 25.50  ? 175 LYS A CB  1 
ATOM   1515 C CG  . LYS A 1 175 ? -19.739 4.155  68.325  1.00 29.29  ? 175 LYS A CG  1 
ATOM   1516 C CD  . LYS A 1 175 ? -20.872 5.160  68.229  1.00 32.52  ? 175 LYS A CD  1 
ATOM   1517 C CE  . LYS A 1 175 ? -21.250 5.441  66.791  1.00 45.87  ? 175 LYS A CE  1 
ATOM   1518 N NZ  . LYS A 1 175 ? -22.709 5.190  66.542  1.00 52.12  ? 175 LYS A NZ  1 
ATOM   1519 N N   . THR A 1 176 ? -15.053 5.296  69.159  1.00 20.95  ? 176 THR A N   1 
ATOM   1520 C CA  . THR A 1 176 ? -13.931 6.096  68.669  1.00 21.77  ? 176 THR A CA  1 
ATOM   1521 C C   . THR A 1 176 ? -12.833 5.220  68.064  1.00 24.85  ? 176 THR A C   1 
ATOM   1522 O O   . THR A 1 176 ? -12.383 5.464  66.940  1.00 23.63  ? 176 THR A O   1 
ATOM   1523 C CB  . THR A 1 176 ? -13.386 6.975  69.798  1.00 27.99  ? 176 THR A CB  1 
ATOM   1524 O OG1 . THR A 1 176 ? -14.366 7.962  70.142  1.00 21.84  ? 176 THR A OG1 1 
ATOM   1525 C CG2 . THR A 1 176 ? -12.094 7.696  69.371  1.00 20.20  ? 176 THR A CG2 1 
ATOM   1526 N N   . LEU A 1 177 ? -12.391 4.188  68.781  1.00 18.21  ? 177 LEU A N   1 
ATOM   1527 C CA  . LEU A 1 177 ? -11.386 3.310  68.187  1.00 24.45  ? 177 LEU A CA  1 
ATOM   1528 C C   . LEU A 1 177 ? -11.942 2.577  66.966  1.00 26.44  ? 177 LEU A C   1 
ATOM   1529 O O   . LEU A 1 177 ? -11.205 2.331  66.003  1.00 22.19  ? 177 LEU A O   1 
ATOM   1530 C CB  . LEU A 1 177 ? -10.862 2.322  69.234  1.00 26.14  ? 177 LEU A CB  1 
ATOM   1531 C CG  . LEU A 1 177 ? -10.101 2.947  70.412  1.00 26.12  ? 177 LEU A CG  1 
ATOM   1532 C CD1 . LEU A 1 177 ? -9.493  1.870  71.290  1.00 24.38  ? 177 LEU A CD1 1 
ATOM   1533 C CD2 . LEU A 1 177 ? -9.017  3.917  69.936  1.00 35.84  ? 177 LEU A CD2 1 
ATOM   1534 N N   . SER A 1 178 ? -13.240 2.247  66.970  1.00 19.26  ? 178 SER A N   1 
ATOM   1535 C CA  . SER A 1 178 ? -13.845 1.623  65.795  1.00 17.03  ? 178 SER A CA  1 
ATOM   1536 C C   . SER A 1 178 ? -13.786 2.522  64.569  1.00 20.48  ? 178 SER A C   1 
ATOM   1537 O O   . SER A 1 178 ? -13.640 2.022  63.442  1.00 17.35  ? 178 SER A O   1 
ATOM   1538 C CB  . SER A 1 178 ? -15.304 1.244  66.072  1.00 25.98  ? 178 SER A CB  1 
ATOM   1539 O OG  . SER A 1 178 ? -15.368 0.162  66.971  1.00 30.48  ? 178 SER A OG  1 
ATOM   1540 N N   . ILE A 1 179 ? -13.962 3.845  64.742  1.00 18.76  ? 179 ILE A N   1 
ATOM   1541 C CA  . ILE A 1 179 ? -13.961 4.677  63.538  1.00 22.72  ? 179 ILE A CA  1 
ATOM   1542 C C   . ILE A 1 179 ? -12.550 4.747  62.956  1.00 24.14  ? 179 ILE A C   1 
ATOM   1543 O O   . ILE A 1 179 ? -12.380 4.770  61.726  1.00 21.95  ? 179 ILE A O   1 
ATOM   1544 C CB  . ILE A 1 179 ? -14.558 6.084  63.784  1.00 26.40  ? 179 ILE A CB  1 
ATOM   1545 C CG1 . ILE A 1 179 ? -14.848 6.779  62.446  1.00 30.92  ? 179 ILE A CG1 1 
ATOM   1546 C CG2 . ILE A 1 179 ? -13.648 6.996  64.607  1.00 21.52  ? 179 ILE A CG2 1 
ATOM   1547 C CD1 . ILE A 1 179 ? -16.130 7.589  62.432  1.00 35.01  ? 179 ILE A CD1 1 
ATOM   1548 N N   . TYR A 1 180 ? -11.522 4.741  63.806  1.00 22.81  ? 180 TYR A N   1 
ATOM   1549 C CA  . TYR A 1 180 ? -10.157 4.743  63.286  1.00 22.98  ? 180 TYR A CA  1 
ATOM   1550 C C   . TYR A 1 180 ? -9.863  3.459  62.520  1.00 22.25  ? 180 TYR A C   1 
ATOM   1551 O O   . TYR A 1 180 ? -9.295  3.511  61.423  1.00 21.28  ? 180 TYR A O   1 
ATOM   1552 C CB  . TYR A 1 180 ? -9.149  4.964  64.412  1.00 25.55  ? 180 TYR A CB  1 
ATOM   1553 C CG  . TYR A 1 180 ? -9.086  6.417  64.847  1.00 24.69  ? 180 TYR A CG  1 
ATOM   1554 C CD1 . TYR A 1 180 ? -8.391  7.377  64.093  1.00 18.30  ? 180 TYR A CD1 1 
ATOM   1555 C CD2 . TYR A 1 180 ? -9.738  6.834  65.992  1.00 16.77  ? 180 TYR A CD2 1 
ATOM   1556 C CE1 . TYR A 1 180 ? -8.351  8.702  64.489  1.00 15.21  ? 180 TYR A CE1 1 
ATOM   1557 C CE2 . TYR A 1 180 ? -9.699  8.151  66.396  1.00 15.48  ? 180 TYR A CE2 1 
ATOM   1558 C CZ  . TYR A 1 180 ? -9.014  9.079  65.647  1.00 18.88  ? 180 TYR A CZ  1 
ATOM   1559 O OH  . TYR A 1 180 ? -9.007  10.379 66.073  1.00 22.95  ? 180 TYR A OH  1 
ATOM   1560 N N   . ARG A 1 181 ? -10.293 2.300  63.046  1.00 24.77  ? 181 ARG A N   1 
ATOM   1561 C CA  . ARG A 1 181 ? -10.123 1.046  62.310  1.00 21.38  ? 181 ARG A CA  1 
ATOM   1562 C C   . ARG A 1 181 ? -10.859 1.088  60.977  1.00 26.02  ? 181 ARG A C   1 
ATOM   1563 O O   . ARG A 1 181 ? -10.339 0.616  59.958  1.00 23.26  ? 181 ARG A O   1 
ATOM   1564 C CB  . ARG A 1 181 ? -10.619 -0.148 63.135  1.00 21.05  ? 181 ARG A CB  1 
ATOM   1565 C CG  . ARG A 1 181 ? -9.940  -0.376 64.487  1.00 20.96  ? 181 ARG A CG  1 
ATOM   1566 C CD  . ARG A 1 181 ? -10.423 -1.699 65.116  1.00 28.13  ? 181 ARG A CD  1 
ATOM   1567 N NE  . ARG A 1 181 ? -9.969  -1.823 66.497  1.00 38.96  ? 181 ARG A NE  1 
ATOM   1568 C CZ  . ARG A 1 181 ? -10.741 -1.643 67.560  1.00 42.94  ? 181 ARG A CZ  1 
ATOM   1569 N NH1 . ARG A 1 181 ? -12.023 -1.345 67.413  1.00 39.22  ? 181 ARG A NH1 1 
ATOM   1570 N NH2 . ARG A 1 181 ? -10.226 -1.764 68.774  1.00 46.50  ? 181 ARG A NH2 1 
ATOM   1571 N N   . GLU A 1 182 ? -12.073 1.654  60.966  1.00 25.90  ? 182 GLU A N   1 
ATOM   1572 C CA  . GLU A 1 182 ? -12.878 1.690  59.747  1.00 30.93  ? 182 GLU A CA  1 
ATOM   1573 C C   . GLU A 1 182 ? -12.236 2.546  58.655  1.00 27.54  ? 182 GLU A C   1 
ATOM   1574 O O   . GLU A 1 182 ? -12.128 2.108  57.502  1.00 24.25  ? 182 GLU A O   1 
ATOM   1575 C CB  . GLU A 1 182 ? -14.283 2.203  60.049  1.00 31.04  ? 182 GLU A CB  1 
ATOM   1576 C CG  . GLU A 1 182 ? -15.163 2.199  58.817  1.00 39.69  ? 182 GLU A CG  1 
ATOM   1577 C CD  . GLU A 1 182 ? -16.594 2.613  59.100  1.00 46.15  ? 182 GLU A CD  1 
ATOM   1578 O OE1 . GLU A 1 182 ? -16.854 3.210  60.174  1.00 50.25  ? 182 GLU A OE1 1 
ATOM   1579 O OE2 . GLU A 1 182 ? -17.458 2.339  58.242  1.00 40.45  ? 182 GLU A OE2 1 
ATOM   1580 N N   . ILE A 1 183 ? -11.843 3.786  58.978  1.00 24.26  ? 183 ILE A N   1 
ATOM   1581 C CA  . ILE A 1 183 ? -11.269 4.636  57.934  1.00 22.88  ? 183 ILE A CA  1 
ATOM   1582 C C   . ILE A 1 183 ? -9.936  4.060  57.475  1.00 24.29  ? 183 ILE A C   1 
ATOM   1583 O O   . ILE A 1 183 ? -9.535  4.241  56.316  1.00 25.33  ? 183 ILE A O   1 
ATOM   1584 C CB  . ILE A 1 183 ? -11.129 6.098  58.410  1.00 23.33  ? 183 ILE A CB  1 
ATOM   1585 C CG1 . ILE A 1 183 ? -10.105 6.224  59.541  1.00 28.54  ? 183 ILE A CG1 1 
ATOM   1586 C CG2 . ILE A 1 183 ? -12.477 6.620  58.875  1.00 26.55  ? 183 ILE A CG2 1 
ATOM   1587 C CD1 . ILE A 1 183 ? -8.774  6.821  59.125  1.00 26.02  ? 183 ILE A CD1 1 
ATOM   1588 N N   . LYS A 1 184 ? -9.244  3.348  58.364  1.00 21.76  ? 184 LYS A N   1 
ATOM   1589 C CA  . LYS A 1 184 ? -8.001  2.685  57.987  1.00 27.89  ? 184 LYS A CA  1 
ATOM   1590 C C   . LYS A 1 184 ? -8.266  1.516  57.050  1.00 28.31  ? 184 LYS A C   1 
ATOM   1591 O O   . LYS A 1 184 ? -7.580  1.359  56.033  1.00 30.91  ? 184 LYS A O   1 
ATOM   1592 C CB  . LYS A 1 184 ? -7.262  2.216  59.243  1.00 27.29  ? 184 LYS A CB  1 
ATOM   1593 C CG  . LYS A 1 184 ? -5.927  1.533  58.970  1.00 29.51  ? 184 LYS A CG  1 
ATOM   1594 C CD  . LYS A 1 184 ? -5.283  1.045  60.260  1.00 31.18  ? 184 LYS A CD  1 
ATOM   1595 C CE  . LYS A 1 184 ? -4.016  0.264  59.973  1.00 30.86  ? 184 LYS A CE  1 
ATOM   1596 N NZ  . LYS A 1 184 ? -4.279  -0.817 58.986  1.00 31.35  ? 184 LYS A NZ  1 
ATOM   1597 N N   . GLU A 1 185 ? -9.264  0.687  57.377  1.00 18.37  ? 185 GLU A N   1 
ATOM   1598 C CA  . GLU A 1 185 ? -9.592  -0.455 56.535  1.00 24.04  ? 185 GLU A CA  1 
ATOM   1599 C C   . GLU A 1 185 ? -10.110 -0.007 55.175  1.00 25.88  ? 185 GLU A C   1 
ATOM   1600 O O   . GLU A 1 185 ? -9.800  -0.627 54.155  1.00 26.70  ? 185 GLU A O   1 
ATOM   1601 C CB  . GLU A 1 185 ? -10.629 -1.333 57.241  1.00 25.13  ? 185 GLU A CB  1 
ATOM   1602 C CG  . GLU A 1 185 ? -10.905 -2.657 56.566  1.00 32.54  ? 185 GLU A CG  1 
ATOM   1603 C CD  . GLU A 1 185 ? -11.371 -3.724 57.549  1.00 36.26  ? 185 GLU A CD  1 
ATOM   1604 O OE1 . GLU A 1 185 ? -11.398 -3.453 58.771  1.00 36.03  ? 185 GLU A OE1 1 
ATOM   1605 O OE2 . GLU A 1 185 ? -11.718 -4.830 57.101  1.00 43.67  ? 185 GLU A OE2 1 
ATOM   1606 N N   . GLU A 1 186 ? -10.898 1.068  55.137  1.00 25.86  ? 186 GLU A N   1 
ATOM   1607 C CA  . GLU A 1 186 ? -11.494 1.514  53.882  1.00 28.59  ? 186 GLU A CA  1 
ATOM   1608 C C   . GLU A 1 186 ? -10.532 2.304  53.012  1.00 30.16  ? 186 GLU A C   1 
ATOM   1609 O O   . GLU A 1 186 ? -10.889 2.649  51.879  1.00 31.79  ? 186 GLU A O   1 
ATOM   1610 C CB  . GLU A 1 186 ? -12.748 2.354  54.160  1.00 32.92  ? 186 GLU A CB  1 
ATOM   1611 C CG  . GLU A 1 186 ? -13.829 1.567  54.878  1.00 36.18  ? 186 GLU A CG  1 
ATOM   1612 C CD  . GLU A 1 186 ? -15.049 2.394  55.167  1.00 38.25  ? 186 GLU A CD  1 
ATOM   1613 O OE1 . GLU A 1 186 ? -14.884 3.609  55.387  1.00 42.16  ? 186 GLU A OE1 1 
ATOM   1614 O OE2 . GLU A 1 186 ? -16.166 1.827  55.179  1.00 38.15  ? 186 GLU A OE2 1 
ATOM   1615 N N   . GLY A 1 187 ? -9.328  2.591  53.497  1.00 27.11  ? 187 GLY A N   1 
ATOM   1616 C CA  . GLY A 1 187 ? -8.398  3.351  52.697  1.00 26.45  ? 187 GLY A CA  1 
ATOM   1617 C C   . GLY A 1 187 ? -8.672  4.830  52.686  1.00 24.12  ? 187 GLY A C   1 
ATOM   1618 O O   . GLY A 1 187 ? -8.223  5.527  51.773  1.00 26.97  ? 187 GLY A O   1 
ATOM   1619 N N   . LYS A 1 188 ? -9.417  5.337  53.664  1.00 23.57  ? 188 LYS A N   1 
ATOM   1620 C CA  . LYS A 1 188 ? -9.690  6.767  53.706  1.00 29.52  ? 188 LYS A CA  1 
ATOM   1621 C C   . LYS A 1 188 ? -8.581  7.534  54.407  1.00 24.87  ? 188 LYS A C   1 
ATOM   1622 O O   . LYS A 1 188 ? -8.494  8.753  54.252  1.00 21.71  ? 188 LYS A O   1 
ATOM   1623 C CB  . LYS A 1 188 ? -11.029 7.037  54.397  1.00 29.42  ? 188 LYS A CB  1 
ATOM   1624 C CG  . LYS A 1 188 ? -12.254 6.439  53.693  1.00 30.73  ? 188 LYS A CG  1 
ATOM   1625 C CD  . LYS A 1 188 ? -13.478 6.535  54.608  1.00 38.83  ? 188 LYS A CD  1 
ATOM   1626 C CE  . LYS A 1 188 ? -14.782 6.448  53.833  1.00 40.32  ? 188 LYS A CE  1 
ATOM   1627 N NZ  . LYS A 1 188 ? -14.873 5.173  53.094  1.00 43.80  ? 188 LYS A NZ  1 
ATOM   1628 N N   . GLY A 1 189 ? -7.755  6.848  55.184  1.00 25.07  ? 189 GLY A N   1 
ATOM   1629 C CA  . GLY A 1 189 ? -6.573  7.454  55.765  1.00 29.56  ? 189 GLY A CA  1 
ATOM   1630 C C   . GLY A 1 189 ? -5.704  6.417  56.437  1.00 26.56  ? 189 GLY A C   1 
ATOM   1631 O O   . GLY A 1 189 ? -6.131  5.286  56.682  1.00 25.37  ? 189 GLY A O   1 
ATOM   1632 N N   . SER A 1 190 ? -4.473  6.823  56.734  1.00 24.98  ? 190 SER A N   1 
ATOM   1633 C CA  . SER A 1 190 ? -3.537  5.996  57.481  1.00 21.07  ? 190 SER A CA  1 
ATOM   1634 C C   . SER A 1 190 ? -3.552  6.413  58.946  1.00 20.41  ? 190 SER A C   1 
ATOM   1635 O O   . SER A 1 190 ? -3.851  7.562  59.280  1.00 19.19  ? 190 SER A O   1 
ATOM   1636 C CB  . SER A 1 190 ? -2.110  6.118  56.925  1.00 17.61  ? 190 SER A CB  1 
ATOM   1637 O OG  . SER A 1 190 ? -2.019  5.571  55.617  1.00 22.02  ? 190 SER A OG  1 
ATOM   1638 N N   . VAL A 1 191 ? -3.231  5.470  59.828  1.00 19.46  ? 191 VAL A N   1 
ATOM   1639 C CA  . VAL A 1 191 ? -3.149  5.762  61.253  1.00 18.65  ? 191 VAL A CA  1 
ATOM   1640 C C   . VAL A 1 191 ? -1.740  5.449  61.729  1.00 19.39  ? 191 VAL A C   1 
ATOM   1641 O O   . VAL A 1 191 ? -1.207  4.363  61.455  1.00 22.07  ? 191 VAL A O   1 
ATOM   1642 C CB  . VAL A 1 191 ? -4.190  4.978  62.071  1.00 18.92  ? 191 VAL A CB  1 
ATOM   1643 C CG1 . VAL A 1 191 ? -4.109  5.403  63.542  1.00 21.69  ? 191 VAL A CG1 1 
ATOM   1644 C CG2 . VAL A 1 191 ? -5.590  5.227  61.526  1.00 19.19  ? 191 VAL A CG2 1 
ATOM   1645 N N   . SER A 1 192 ? -1.145  6.399  62.443  1.00 16.93  ? 192 SER A N   1 
ATOM   1646 C CA  . SER A 1 192 ? 0.187   6.273  63.003  1.00 18.14  ? 192 SER A CA  1 
ATOM   1647 C C   . SER A 1 192 ? 0.096   6.310  64.525  1.00 17.65  ? 192 SER A C   1 
ATOM   1648 O O   . SER A 1 192 ? -0.970  6.539  65.105  1.00 18.15  ? 192 SER A O   1 
ATOM   1649 C CB  . SER A 1 192 ? 1.098   7.405  62.500  1.00 19.90  ? 192 SER A CB  1 
ATOM   1650 O OG  . SER A 1 192 ? 0.696   8.656  63.055  1.00 18.39  ? 192 SER A OG  1 
ATOM   1651 N N   . THR A 1 193 ? 1.230   6.067  65.173  1.00 20.00  ? 193 THR A N   1 
ATOM   1652 C CA  . THR A 1 193 ? 1.363   6.283  66.606  1.00 21.98  ? 193 THR A CA  1 
ATOM   1653 C C   . THR A 1 193 ? 2.715   6.954  66.864  1.00 24.53  ? 193 THR A C   1 
ATOM   1654 O O   . THR A 1 193 ? 3.495   7.208  65.937  1.00 21.80  ? 193 THR A O   1 
ATOM   1655 C CB  . THR A 1 193 ? 1.170   4.970  67.384  1.00 22.40  ? 193 THR A CB  1 
ATOM   1656 O OG1 . THR A 1 193 ? 0.976   5.264  68.772  1.00 23.25  ? 193 THR A OG1 1 
ATOM   1657 C CG2 . THR A 1 193 ? 2.355   4.020  67.202  1.00 21.77  ? 193 THR A CG2 1 
ATOM   1658 N N   . SER A 1 194 ? 2.968   7.290  68.125  1.00 22.73  ? 194 SER A N   1 
ATOM   1659 C CA  . SER A 1 194 ? 4.202   7.885  68.612  1.00 23.60  ? 194 SER A CA  1 
ATOM   1660 C C   . SER A 1 194 ? 4.765   6.992  69.707  1.00 20.60  ? 194 SER A C   1 
ATOM   1661 O O   . SER A 1 194 ? 4.028   6.196  70.296  1.00 18.98  ? 194 SER A O   1 
ATOM   1662 C CB  . SER A 1 194 ? 3.957   9.292  69.185  1.00 16.93  ? 194 SER A CB  1 
ATOM   1663 O OG  . SER A 1 194 ? 3.381   10.172 68.229  1.00 20.88  ? 194 SER A OG  1 
ATOM   1664 N N   . PRO A 1 195 ? 6.055   7.101  70.021  1.00 17.53  ? 195 PRO A N   1 
ATOM   1665 C CA  . PRO A 1 195 ? 6.574   6.405  71.205  1.00 20.31  ? 195 PRO A CA  1 
ATOM   1666 C C   . PRO A 1 195 ? 5.683   6.677  72.416  1.00 17.35  ? 195 PRO A C   1 
ATOM   1667 O O   . PRO A 1 195 ? 5.147   7.772  72.583  1.00 22.87  ? 195 PRO A O   1 
ATOM   1668 C CB  . PRO A 1 195 ? 7.973   6.998  71.382  1.00 26.30  ? 195 PRO A CB  1 
ATOM   1669 C CG  . PRO A 1 195 ? 8.372   7.406  70.002  1.00 34.99  ? 195 PRO A CG  1 
ATOM   1670 C CD  . PRO A 1 195 ? 7.115   7.834  69.303  1.00 24.87  ? 195 PRO A CD  1 
ATOM   1671 N N   . TYR A 1 196 ? 5.573   5.664  73.281  1.00 20.58  ? 196 TYR A N   1 
ATOM   1672 C CA  . TYR A 1 196 ? 4.383   5.432  74.100  1.00 19.80  ? 196 TYR A CA  1 
ATOM   1673 C C   . TYR A 1 196 ? 3.897   6.676  74.834  1.00 20.37  ? 196 TYR A C   1 
ATOM   1674 O O   . TYR A 1 196 ? 2.739   7.088  74.683  1.00 21.43  ? 196 TYR A O   1 
ATOM   1675 C CB  . TYR A 1 196 ? 4.658   4.311  75.107  1.00 18.83  ? 196 TYR A CB  1 
ATOM   1676 C CG  . TYR A 1 196 ? 3.398   3.603  75.547  1.00 19.21  ? 196 TYR A CG  1 
ATOM   1677 C CD1 . TYR A 1 196 ? 2.473   4.225  76.377  1.00 15.68  ? 196 TYR A CD1 1 
ATOM   1678 C CD2 . TYR A 1 196 ? 3.130   2.300  75.117  1.00 23.74  ? 196 TYR A CD2 1 
ATOM   1679 C CE1 . TYR A 1 196 ? 1.308   3.561  76.782  1.00 20.50  ? 196 TYR A CE1 1 
ATOM   1680 C CE2 . TYR A 1 196 ? 1.984   1.637  75.499  1.00 22.22  ? 196 TYR A CE2 1 
ATOM   1681 C CZ  . TYR A 1 196 ? 1.077   2.260  76.334  1.00 25.53  ? 196 TYR A CZ  1 
ATOM   1682 O OH  . TYR A 1 196 ? -0.052  1.556  76.708  1.00 23.56  ? 196 TYR A OH  1 
ATOM   1683 N N   . TYR A 1 197 ? 4.738   7.260  75.685  1.00 18.70  ? 197 TYR A N   1 
ATOM   1684 C CA  . TYR A 1 197 ? 4.276   8.377  76.501  1.00 21.47  ? 197 TYR A CA  1 
ATOM   1685 C C   . TYR A 1 197 ? 4.689   9.727  75.926  1.00 17.78  ? 197 TYR A C   1 
ATOM   1686 O O   . TYR A 1 197 ? 4.778   10.712 76.662  1.00 13.64  ? 197 TYR A O   1 
ATOM   1687 C CB  . TYR A 1 197 ? 4.751   8.204  77.942  1.00 18.77  ? 197 TYR A CB  1 
ATOM   1688 C CG  . TYR A 1 197 ? 4.089   7.014  78.594  1.00 17.83  ? 197 TYR A CG  1 
ATOM   1689 C CD1 . TYR A 1 197 ? 2.752   7.063  78.966  1.00 17.67  ? 197 TYR A CD1 1 
ATOM   1690 C CD2 . TYR A 1 197 ? 4.778   5.824  78.786  1.00 21.40  ? 197 TYR A CD2 1 
ATOM   1691 C CE1 . TYR A 1 197 ? 2.131   5.979  79.536  1.00 17.99  ? 197 TYR A CE1 1 
ATOM   1692 C CE2 . TYR A 1 197 ? 4.163   4.725  79.366  1.00 20.68  ? 197 TYR A CE2 1 
ATOM   1693 C CZ  . TYR A 1 197 ? 2.837   4.817  79.740  1.00 21.49  ? 197 TYR A CZ  1 
ATOM   1694 O OH  . TYR A 1 197 ? 2.202   3.743  80.303  1.00 31.08  ? 197 TYR A OH  1 
ATOM   1695 N N   . HIS A 1 198 ? 4.911   9.795  74.613  1.00 15.52  ? 198 HIS A N   1 
ATOM   1696 C CA  . HIS A 1 198 ? 5.181   11.054 73.931  1.00 15.92  ? 198 HIS A CA  1 
ATOM   1697 C C   . HIS A 1 198 ? 6.428   11.748 74.499  1.00 22.86  ? 198 HIS A C   1 
ATOM   1698 O O   . HIS A 1 198 ? 6.378   12.945 74.807  1.00 18.78  ? 198 HIS A O   1 
ATOM   1699 C CB  . HIS A 1 198 ? 3.947   11.962 74.049  1.00 17.06  ? 198 HIS A CB  1 
ATOM   1700 C CG  . HIS A 1 198 ? 3.898   13.091 73.053  1.00 16.94  ? 198 HIS A CG  1 
ATOM   1701 N ND1 . HIS A 1 198 ? 4.342   14.361 73.349  1.00 20.85  ? 198 HIS A ND1 1 
ATOM   1702 C CD2 . HIS A 1 198 ? 3.430   13.143 71.782  1.00 18.81  ? 198 HIS A CD2 1 
ATOM   1703 C CE1 . HIS A 1 198 ? 4.153   15.149 72.302  1.00 20.04  ? 198 HIS A CE1 1 
ATOM   1704 N NE2 . HIS A 1 198 ? 3.596   14.434 71.338  1.00 18.30  ? 198 HIS A NE2 1 
ATOM   1705 N N   . PRO A 1 199 ? 7.552   11.054 74.662  1.00 23.96  ? 199 PRO A N   1 
ATOM   1706 C CA  . PRO A 1 199 ? 8.753   11.707 75.184  1.00 23.20  ? 199 PRO A CA  1 
ATOM   1707 C C   . PRO A 1 199 ? 9.553   12.393 74.080  1.00 23.78  ? 199 PRO A C   1 
ATOM   1708 O O   . PRO A 1 199 ? 9.294   12.231 72.886  1.00 24.47  ? 199 PRO A O   1 
ATOM   1709 C CB  . PRO A 1 199 ? 9.539   10.528 75.769  1.00 22.92  ? 199 PRO A CB  1 
ATOM   1710 C CG  . PRO A 1 199 ? 9.253   9.418  74.846  1.00 20.12  ? 199 PRO A CG  1 
ATOM   1711 C CD  . PRO A 1 199 ? 7.819   9.631  74.366  1.00 25.98  ? 199 PRO A CD  1 
ATOM   1712 N N   . LEU A 1 200 ? 10.572  13.138 74.509  1.00 25.79  ? 200 LEU A N   1 
ATOM   1713 C CA  . LEU A 1 200 ? 11.563  13.696 73.590  1.00 16.91  ? 200 LEU A CA  1 
ATOM   1714 C C   . LEU A 1 200 ? 12.640  12.643 73.379  1.00 19.91  ? 200 LEU A C   1 
ATOM   1715 O O   . LEU A 1 200 ? 13.630  12.580 74.110  1.00 20.29  ? 200 LEU A O   1 
ATOM   1716 C CB  . LEU A 1 200 ? 12.136  14.997 74.133  1.00 22.74  ? 200 LEU A CB  1 
ATOM   1717 C CG  . LEU A 1 200 ? 11.166  16.182 74.192  1.00 30.56  ? 200 LEU A CG  1 
ATOM   1718 C CD1 . LEU A 1 200 ? 11.799  17.301 74.976  1.00 37.48  ? 200 LEU A CD1 1 
ATOM   1719 C CD2 . LEU A 1 200 ? 10.792  16.674 72.803  1.00 35.34  ? 200 LEU A CD2 1 
ATOM   1720 N N   . ILE A 1 201 ? 12.449  11.821 72.344  1.00 25.51  ? 201 ILE A N   1 
ATOM   1721 C CA  . ILE A 1 201 ? 13.405  10.750 72.044  1.00 25.05  ? 201 ILE A CA  1 
ATOM   1722 C C   . ILE A 1 201 ? 14.840  11.263 71.896  1.00 26.45  ? 201 ILE A C   1 
ATOM   1723 O O   . ILE A 1 201 ? 15.752  10.632 72.446  1.00 20.17  ? 201 ILE A O   1 
ATOM   1724 C CB  . ILE A 1 201 ? 12.937  9.946  70.825  1.00 24.30  ? 201 ILE A CB  1 
ATOM   1725 C CG1 . ILE A 1 201 ? 11.627  9.221  71.126  1.00 21.98  ? 201 ILE A CG1 1 
ATOM   1726 C CG2 . ILE A 1 201 ? 13.985  8.934  70.428  1.00 20.90  ? 201 ILE A CG2 1 
ATOM   1727 C CD1 . ILE A 1 201 ? 11.805  8.030  72.036  1.00 17.43  ? 201 ILE A CD1 1 
ATOM   1728 N N   . PRO A 1 202 ? 15.114  12.357 71.171  1.00 20.71  ? 202 PRO A N   1 
ATOM   1729 C CA  . PRO A 1 202 ? 16.525  12.773 71.006  1.00 19.97  ? 202 PRO A CA  1 
ATOM   1730 C C   . PRO A 1 202 ? 17.217  13.095 72.316  1.00 22.14  ? 202 PRO A C   1 
ATOM   1731 O O   . PRO A 1 202 ? 18.430  12.864 72.447  1.00 17.97  ? 202 PRO A O   1 
ATOM   1732 C CB  . PRO A 1 202 ? 16.423  14.015 70.107  1.00 17.61  ? 202 PRO A CB  1 
ATOM   1733 C CG  . PRO A 1 202 ? 15.177  13.782 69.314  1.00 18.51  ? 202 PRO A CG  1 
ATOM   1734 C CD  . PRO A 1 202 ? 14.224  13.144 70.294  1.00 19.53  ? 202 PRO A CD  1 
ATOM   1735 N N   . ILE A 1 203 ? 16.478  13.603 73.301  1.00 18.04  ? 203 ILE A N   1 
ATOM   1736 C CA  . ILE A 1 203 ? 17.090  13.911 74.584  1.00 20.78  ? 203 ILE A CA  1 
ATOM   1737 C C   . ILE A 1 203 ? 17.354  12.633 75.369  1.00 21.60  ? 203 ILE A C   1 
ATOM   1738 O O   . ILE A 1 203 ? 18.442  12.460 75.935  1.00 23.38  ? 203 ILE A O   1 
ATOM   1739 C CB  . ILE A 1 203 ? 16.214  14.906 75.358  1.00 25.05  ? 203 ILE A CB  1 
ATOM   1740 C CG1 . ILE A 1 203 ? 16.341  16.295 74.719  1.00 28.06  ? 203 ILE A CG1 1 
ATOM   1741 C CG2 . ILE A 1 203 ? 16.621  14.961 76.828  1.00 17.03  ? 203 ILE A CG2 1 
ATOM   1742 C CD1 . ILE A 1 203 ? 15.544  17.359 75.435  1.00 30.75  ? 203 ILE A CD1 1 
ATOM   1743 N N   . LEU A 1 204 ? 16.376  11.710 75.393  1.00 17.47  ? 204 LEU A N   1 
ATOM   1744 C CA  . LEU A 1 204 ? 16.578  10.402 76.013  1.00 21.60  ? 204 LEU A CA  1 
ATOM   1745 C C   . LEU A 1 204 ? 17.815  9.699  75.455  1.00 20.64  ? 204 LEU A C   1 
ATOM   1746 O O   . LEU A 1 204 ? 18.593  9.101  76.203  1.00 18.99  ? 204 LEU A O   1 
ATOM   1747 C CB  . LEU A 1 204 ? 15.343  9.526  75.805  1.00 20.01  ? 204 LEU A CB  1 
ATOM   1748 C CG  . LEU A 1 204 ? 14.016  9.974  76.453  1.00 18.58  ? 204 LEU A CG  1 
ATOM   1749 C CD1 . LEU A 1 204 ? 13.030  8.817  76.536  1.00 21.16  ? 204 LEU A CD1 1 
ATOM   1750 C CD2 . LEU A 1 204 ? 14.277  10.520 77.829  1.00 18.41  ? 204 LEU A CD2 1 
ATOM   1751 N N   . LEU A 1 205 ? 18.002  9.747  74.138  1.00 19.93  ? 205 LEU A N   1 
ATOM   1752 C CA  . LEU A 1 205 ? 19.166  9.100  73.541  1.00 25.03  ? 205 LEU A CA  1 
ATOM   1753 C C   . LEU A 1 205 ? 20.450  9.851  73.866  1.00 24.31  ? 205 LEU A C   1 
ATOM   1754 O O   . LEU A 1 205 ? 21.486  9.234  74.153  1.00 25.25  ? 205 LEU A O   1 
ATOM   1755 C CB  . LEU A 1 205 ? 18.980  8.994  72.031  1.00 22.98  ? 205 LEU A CB  1 
ATOM   1756 C CG  . LEU A 1 205 ? 17.861  8.046  71.620  1.00 23.47  ? 205 LEU A CG  1 
ATOM   1757 C CD1 . LEU A 1 205 ? 17.707  8.078  70.111  1.00 22.67  ? 205 LEU A CD1 1 
ATOM   1758 C CD2 . LEU A 1 205 ? 18.220  6.662  72.097  1.00 21.93  ? 205 LEU A CD2 1 
ATOM   1759 N N   . ASN A 1 206 ? 20.405  11.170 73.828  1.00 17.88  ? 206 ASN A N   1 
ATOM   1760 C CA  . ASN A 1 206 ? 21.641  11.923 73.968  1.00 16.87  ? 206 ASN A CA  1 
ATOM   1761 C C   . ASN A 1 206 ? 21.318  13.353 74.385  1.00 19.71  ? 206 ASN A C   1 
ATOM   1762 O O   . ASN A 1 206 ? 21.129  14.232 73.527  1.00 21.51  ? 206 ASN A O   1 
ATOM   1763 C CB  . ASN A 1 206 ? 22.427  11.882 72.653  1.00 20.39  ? 206 ASN A CB  1 
ATOM   1764 C CG  . ASN A 1 206 ? 23.680  12.726 72.694  1.00 28.43  ? 206 ASN A CG  1 
ATOM   1765 O OD1 . ASN A 1 206 ? 24.165  13.093 73.769  1.00 27.45  ? 206 ASN A OD1 1 
ATOM   1766 N ND2 . ASN A 1 206 ? 24.201  13.061 71.518  1.00 27.03  ? 206 ASN A ND2 1 
ATOM   1767 N N   . PRO A 1 207 ? 21.264  13.620 75.693  1.00 21.89  ? 207 PRO A N   1 
ATOM   1768 C CA  . PRO A 1 207 ? 20.856  14.957 76.167  1.00 21.10  ? 207 PRO A CA  1 
ATOM   1769 C C   . PRO A 1 207 ? 21.699  16.093 75.615  1.00 29.48  ? 207 PRO A C   1 
ATOM   1770 O O   . PRO A 1 207 ? 21.232  17.240 75.594  1.00 25.34  ? 207 PRO A O   1 
ATOM   1771 C CB  . PRO A 1 207 ? 21.007  14.849 77.688  1.00 24.83  ? 207 PRO A CB  1 
ATOM   1772 C CG  . PRO A 1 207 ? 20.879  13.373 77.978  1.00 30.72  ? 207 PRO A CG  1 
ATOM   1773 C CD  . PRO A 1 207 ? 21.477  12.668 76.798  1.00 28.53  ? 207 PRO A CD  1 
ATOM   1774 N N   . ASN A 1 208 ? 22.919  15.814 75.164  1.00 27.11  ? 208 ASN A N   1 
ATOM   1775 C CA  . ASN A 1 208 ? 23.772  16.855 74.614  1.00 27.93  ? 208 ASN A CA  1 
ATOM   1776 C C   . ASN A 1 208 ? 23.350  17.314 73.227  1.00 27.77  ? 208 ASN A C   1 
ATOM   1777 O O   . ASN A 1 208 ? 23.896  18.310 72.739  1.00 22.81  ? 208 ASN A O   1 
ATOM   1778 C CB  . ASN A 1 208 ? 25.213  16.366 74.583  1.00 26.37  ? 208 ASN A CB  1 
ATOM   1779 C CG  . ASN A 1 208 ? 25.760  16.147 75.963  1.00 28.18  ? 208 ASN A CG  1 
ATOM   1780 O OD1 . ASN A 1 208 ? 25.455  16.908 76.885  1.00 28.99  ? 208 ASN A OD1 1 
ATOM   1781 N ND2 . ASN A 1 208 ? 26.560  15.102 76.127  1.00 32.97  ? 208 ASN A ND2 1 
ATOM   1782 N N   . CYS A 1 209 ? 22.402  16.631 72.580  1.00 27.90  ? 209 CYS A N   1 
ATOM   1783 C CA  . CYS A 1 209 ? 21.942  17.086 71.274  1.00 30.03  ? 209 CYS A CA  1 
ATOM   1784 C C   . CYS A 1 209 ? 21.272  18.456 71.332  1.00 30.48  ? 209 CYS A C   1 
ATOM   1785 O O   . CYS A 1 209 ? 21.098  19.081 70.281  1.00 23.66  ? 209 CYS A O   1 
ATOM   1786 C CB  . CYS A 1 209 ? 20.977  16.064 70.666  1.00 27.44  ? 209 CYS A CB  1 
ATOM   1787 S SG  . CYS A 1 209 ? 19.349  16.072 71.438  1.00 29.22  ? 209 CYS A SG  1 
ATOM   1788 N N   . VAL A 1 210 ? 20.911  18.941 72.525  1.00 29.25  ? 210 VAL A N   1 
ATOM   1789 C CA  . VAL A 1 210 ? 20.316  20.269 72.646  1.00 24.79  ? 210 VAL A CA  1 
ATOM   1790 C C   . VAL A 1 210 ? 21.305  21.355 72.257  1.00 20.72  ? 210 VAL A C   1 
ATOM   1791 O O   . VAL A 1 210 ? 20.905  22.434 71.805  1.00 19.24  ? 210 VAL A O   1 
ATOM   1792 C CB  . VAL A 1 210 ? 19.774  20.489 74.073  1.00 30.48  ? 210 VAL A CB  1 
ATOM   1793 C CG1 . VAL A 1 210 ? 18.758  19.382 74.436  1.00 24.96  ? 210 VAL A CG1 1 
ATOM   1794 C CG2 . VAL A 1 210 ? 20.909  20.555 75.092  1.00 30.64  ? 210 VAL A CG2 1 
ATOM   1795 N N   . TYR A 1 211 ? 22.603  21.106 72.431  1.00 21.69  ? 211 TYR A N   1 
ATOM   1796 C CA  . TYR A 1 211 ? 23.626  22.076 72.061  1.00 24.61  ? 211 TYR A CA  1 
ATOM   1797 C C   . TYR A 1 211 ? 23.817  22.208 70.563  1.00 26.61  ? 211 TYR A C   1 
ATOM   1798 O O   . TYR A 1 211 ? 24.620  23.041 70.138  1.00 31.53  ? 211 TYR A O   1 
ATOM   1799 C CB  . TYR A 1 211 ? 24.959  21.701 72.696  1.00 23.66  ? 211 TYR A CB  1 
ATOM   1800 C CG  . TYR A 1 211 ? 24.867  21.571 74.173  1.00 25.57  ? 211 TYR A CG  1 
ATOM   1801 C CD1 . TYR A 1 211 ? 24.410  22.624 74.953  1.00 29.97  ? 211 TYR A CD1 1 
ATOM   1802 C CD2 . TYR A 1 211 ? 25.205  20.388 74.795  1.00 30.78  ? 211 TYR A CD2 1 
ATOM   1803 C CE1 . TYR A 1 211 ? 24.305  22.502 76.318  1.00 32.59  ? 211 TYR A CE1 1 
ATOM   1804 C CE2 . TYR A 1 211 ? 25.115  20.256 76.153  1.00 33.65  ? 211 TYR A CE2 1 
ATOM   1805 C CZ  . TYR A 1 211 ? 24.661  21.310 76.910  1.00 37.49  ? 211 TYR A CZ  1 
ATOM   1806 O OH  . TYR A 1 211 ? 24.582  21.170 78.269  1.00 42.60  ? 211 TYR A OH  1 
ATOM   1807 N N   . GLU A 1 212 ? 23.146  21.399 69.747  1.00 24.71  ? 212 GLU A N   1 
ATOM   1808 C CA  . GLU A 1 212 ? 23.232  21.618 68.310  1.00 28.81  ? 212 GLU A CA  1 
ATOM   1809 C C   . GLU A 1 212 ? 22.563  22.929 67.903  1.00 31.27  ? 212 GLU A C   1 
ATOM   1810 O O   . GLU A 1 212 ? 22.972  23.544 66.914  1.00 33.48  ? 212 GLU A O   1 
ATOM   1811 C CB  . GLU A 1 212 ? 22.614  20.440 67.562  1.00 29.95  ? 212 GLU A CB  1 
ATOM   1812 C CG  . GLU A 1 212 ? 23.303  19.122 67.844  1.00 32.39  ? 212 GLU A CG  1 
ATOM   1813 C CD  . GLU A 1 212 ? 22.736  17.993 67.019  1.00 41.01  ? 212 GLU A CD  1 
ATOM   1814 O OE1 . GLU A 1 212 ? 22.897  16.822 67.423  1.00 46.13  ? 212 GLU A OE1 1 
ATOM   1815 O OE2 . GLU A 1 212 ? 22.123  18.280 65.972  1.00 40.57  ? 212 GLU A OE2 1 
ATOM   1816 N N   . THR A 1 213 ? 21.559  23.385 68.662  1.00 30.44  ? 213 THR A N   1 
ATOM   1817 C CA  . THR A 1 213 ? 20.830  24.606 68.330  1.00 31.54  ? 213 THR A CA  1 
ATOM   1818 C C   . THR A 1 213 ? 20.914  25.709 69.377  1.00 31.46  ? 213 THR A C   1 
ATOM   1819 O O   . THR A 1 213 ? 20.798  26.882 69.014  1.00 32.63  ? 213 THR A O   1 
ATOM   1820 C CB  . THR A 1 213 ? 19.343  24.302 68.083  1.00 28.12  ? 213 THR A CB  1 
ATOM   1821 O OG1 . THR A 1 213 ? 18.802  23.564 69.196  1.00 33.76  ? 213 THR A OG1 1 
ATOM   1822 C CG2 . THR A 1 213 ? 19.187  23.505 66.823  1.00 24.84  ? 213 THR A CG2 1 
ATOM   1823 N N   . THR A 1 214 ? 21.067  25.377 70.658  1.00 30.87  ? 214 THR A N   1 
ATOM   1824 C CA  . THR A 1 214 ? 21.123  26.367 71.737  1.00 28.12  ? 214 THR A CA  1 
ATOM   1825 C C   . THR A 1 214 ? 22.378  26.107 72.558  1.00 28.02  ? 214 THR A C   1 
ATOM   1826 O O   . THR A 1 214 ? 22.314  25.520 73.649  1.00 28.50  ? 214 THR A O   1 
ATOM   1827 C CB  . THR A 1 214 ? 19.873  26.314 72.621  1.00 30.21  ? 214 THR A CB  1 
ATOM   1828 O OG1 . THR A 1 214 ? 19.745  25.009 73.197  1.00 25.49  ? 214 THR A OG1 1 
ATOM   1829 C CG2 . THR A 1 214 ? 18.610  26.627 71.812  1.00 23.02  ? 214 THR A CG2 1 
ATOM   1830 N N   . PRO A 1 215 ? 23.542  26.539 72.066  1.00 26.49  ? 215 PRO A N   1 
ATOM   1831 C CA  . PRO A 1 215 ? 24.797  26.252 72.781  1.00 27.89  ? 215 PRO A CA  1 
ATOM   1832 C C   . PRO A 1 215 ? 24.876  26.849 74.181  1.00 28.78  ? 215 PRO A C   1 
ATOM   1833 O O   . PRO A 1 215 ? 25.656  26.348 74.998  1.00 32.22  ? 215 PRO A O   1 
ATOM   1834 C CB  . PRO A 1 215 ? 25.874  26.854 71.862  1.00 32.42  ? 215 PRO A CB  1 
ATOM   1835 C CG  . PRO A 1 215 ? 25.143  27.799 70.954  1.00 34.36  ? 215 PRO A CG  1 
ATOM   1836 C CD  . PRO A 1 215 ? 23.776  27.224 70.782  1.00 31.81  ? 215 PRO A CD  1 
ATOM   1837 N N   . ASN A 1 216 ? 24.110  27.889 74.498  1.00 24.47  ? 216 ASN A N   1 
ATOM   1838 C CA  . ASN A 1 216 ? 24.279  28.566 75.780  1.00 36.18  ? 216 ASN A CA  1 
ATOM   1839 C C   . ASN A 1 216 ? 23.342  28.053 76.866  1.00 39.60  ? 216 ASN A C   1 
ATOM   1840 O O   . ASN A 1 216 ? 23.284  28.644 77.950  1.00 43.77  ? 216 ASN A O   1 
ATOM   1841 C CB  . ASN A 1 216 ? 24.091  30.073 75.608  1.00 42.72  ? 216 ASN A CB  1 
ATOM   1842 C CG  . ASN A 1 216 ? 25.267  30.718 74.918  1.00 53.44  ? 216 ASN A CG  1 
ATOM   1843 O OD1 . ASN A 1 216 ? 26.423  30.409 75.220  1.00 59.20  ? 216 ASN A OD1 1 
ATOM   1844 N ND2 . ASN A 1 216 ? 24.986  31.605 73.973  1.00 58.59  ? 216 ASN A ND2 1 
ATOM   1845 N N   . VAL A 1 217 ? 22.626  26.978 76.615  1.00 34.80  ? 217 VAL A N   1 
ATOM   1846 C CA  . VAL A 1 217 ? 21.629  26.511 77.568  1.00 33.91  ? 217 VAL A CA  1 
ATOM   1847 C C   . VAL A 1 217 ? 22.305  25.694 78.664  1.00 25.87  ? 217 VAL A C   1 
ATOM   1848 O O   . VAL A 1 217 ? 23.308  25.011 78.426  1.00 32.33  ? 217 VAL A O   1 
ATOM   1849 C CB  . VAL A 1 217 ? 20.528  25.718 76.836  1.00 36.36  ? 217 VAL A CB  1 
ATOM   1850 C CG1 . VAL A 1 217 ? 20.929  24.258 76.598  1.00 29.97  ? 217 VAL A CG1 1 
ATOM   1851 C CG2 . VAL A 1 217 ? 19.256  25.792 77.607  1.00 36.87  ? 217 VAL A CG2 1 
ATOM   1852 N N   . LYS A 1 218 ? 21.783  25.803 79.886  1.00 28.00  ? 218 LYS A N   1 
ATOM   1853 C CA  . LYS A 1 218 ? 22.212  24.972 81.007  1.00 27.49  ? 218 LYS A CA  1 
ATOM   1854 C C   . LYS A 1 218 ? 21.329  23.731 81.083  1.00 28.40  ? 218 LYS A C   1 
ATOM   1855 O O   . LYS A 1 218 ? 20.105  23.834 80.987  1.00 26.59  ? 218 LYS A O   1 
ATOM   1856 C CB  . LYS A 1 218 ? 22.109  25.730 82.331  1.00 25.56  ? 218 LYS A CB  1 
ATOM   1857 C CG  . LYS A 1 218 ? 22.930  26.989 82.436  1.00 36.41  ? 218 LYS A CG  1 
ATOM   1858 C CD  . LYS A 1 218 ? 22.931  27.490 83.876  1.00 44.49  ? 218 LYS A CD  1 
ATOM   1859 C CE  . LYS A 1 218 ? 22.336  28.885 83.973  1.00 54.79  ? 218 LYS A CE  1 
ATOM   1860 N NZ  . LYS A 1 218 ? 21.775  29.184 85.330  1.00 60.64  ? 218 LYS A NZ  1 
ATOM   1861 N N   . ILE A 1 219 ? 21.940  22.566 81.263  1.00 19.74  ? 219 ILE A N   1 
ATOM   1862 C CA  . ILE A 1 219 ? 21.147  21.359 81.507  1.00 24.18  ? 219 ILE A CA  1 
ATOM   1863 C C   . ILE A 1 219 ? 21.701  20.643 82.735  1.00 24.69  ? 219 ILE A C   1 
ATOM   1864 O O   . ILE A 1 219 ? 22.882  20.811 83.073  1.00 29.21  ? 219 ILE A O   1 
ATOM   1865 C CB  . ILE A 1 219 ? 21.126  20.423 80.286  1.00 21.34  ? 219 ILE A CB  1 
ATOM   1866 C CG1 . ILE A 1 219 ? 22.506  19.801 80.062  1.00 29.91  ? 219 ILE A CG1 1 
ATOM   1867 C CG2 . ILE A 1 219 ? 20.583  21.135 79.028  1.00 22.89  ? 219 ILE A CG2 1 
ATOM   1868 C CD1 . ILE A 1 219 ? 22.483  18.596 79.109  1.00 33.00  ? 219 ILE A CD1 1 
ATOM   1869 N N   . PRO A 1 220 ? 20.902  19.853 83.444  1.00 23.76  ? 220 PRO A N   1 
ATOM   1870 C CA  . PRO A 1 220 ? 21.426  19.151 84.621  1.00 25.13  ? 220 PRO A CA  1 
ATOM   1871 C C   . PRO A 1 220 ? 22.429  18.077 84.231  1.00 24.06  ? 220 PRO A C   1 
ATOM   1872 O O   . PRO A 1 220 ? 22.620  17.741 83.055  1.00 20.19  ? 220 PRO A O   1 
ATOM   1873 C CB  . PRO A 1 220 ? 20.177  18.533 85.257  1.00 27.30  ? 220 PRO A CB  1 
ATOM   1874 C CG  . PRO A 1 220 ? 19.195  18.445 84.161  1.00 31.15  ? 220 PRO A CG  1 
ATOM   1875 C CD  . PRO A 1 220 ? 19.455  19.621 83.265  1.00 23.59  ? 220 PRO A CD  1 
ATOM   1876 N N   . ASP A 1 221 ? 23.062  17.521 85.261  1.00 24.19  ? 221 ASP A N   1 
ATOM   1877 C CA  . ASP A 1 221 ? 24.017  16.422 85.118  1.00 25.87  ? 221 ASP A CA  1 
ATOM   1878 C C   . ASP A 1 221 ? 23.261  15.116 84.876  1.00 24.55  ? 221 ASP A C   1 
ATOM   1879 O O   . ASP A 1 221 ? 22.666  14.555 85.800  1.00 24.97  ? 221 ASP A O   1 
ATOM   1880 C CB  . ASP A 1 221 ? 24.889  16.327 86.366  1.00 20.70  ? 221 ASP A CB  1 
ATOM   1881 C CG  . ASP A 1 221 ? 25.985  15.288 86.239  1.00 29.05  ? 221 ASP A CG  1 
ATOM   1882 O OD1 . ASP A 1 221 ? 26.636  15.238 85.181  1.00 28.30  ? 221 ASP A OD1 1 
ATOM   1883 O OD2 . ASP A 1 221 ? 26.209  14.529 87.207  1.00 36.09  ? 221 ASP A OD2 1 
ATOM   1884 N N   . PHE A 1 222 ? 23.301  14.615 83.640  1.00 21.06  ? 222 PHE A N   1 
ATOM   1885 C CA  . PHE A 1 222 ? 22.581  13.393 83.279  1.00 22.63  ? 222 PHE A CA  1 
ATOM   1886 C C   . PHE A 1 222 ? 23.401  12.179 83.703  1.00 24.48  ? 222 PHE A C   1 
ATOM   1887 O O   . PHE A 1 222 ? 24.096  11.538 82.910  1.00 26.04  ? 222 PHE A O   1 
ATOM   1888 C CB  . PHE A 1 222 ? 22.277  13.372 81.788  1.00 24.90  ? 222 PHE A CB  1 
ATOM   1889 C CG  . PHE A 1 222 ? 20.983  14.044 81.434  1.00 24.14  ? 222 PHE A CG  1 
ATOM   1890 C CD1 . PHE A 1 222 ? 20.927  15.426 81.276  1.00 25.09  ? 222 PHE A CD1 1 
ATOM   1891 C CD2 . PHE A 1 222 ? 19.830  13.305 81.271  1.00 26.11  ? 222 PHE A CD2 1 
ATOM   1892 C CE1 . PHE A 1 222 ? 19.735  16.056 80.962  1.00 25.11  ? 222 PHE A CE1 1 
ATOM   1893 C CE2 . PHE A 1 222 ? 18.635  13.922 80.952  1.00 24.47  ? 222 PHE A CE2 1 
ATOM   1894 C CZ  . PHE A 1 222 ? 18.588  15.304 80.798  1.00 20.67  ? 222 PHE A CZ  1 
ATOM   1895 N N   . ALA A 1 223 ? 23.283  11.841 84.986  1.00 23.24  ? 223 ALA A N   1 
ATOM   1896 C CA  . ALA A 1 223 ? 24.091  10.801 85.604  1.00 31.52  ? 223 ALA A CA  1 
ATOM   1897 C C   . ALA A 1 223 ? 23.552  9.392  85.381  1.00 32.12  ? 223 ALA A C   1 
ATOM   1898 O O   . ALA A 1 223 ? 24.093  8.451  85.971  1.00 35.19  ? 223 ALA A O   1 
ATOM   1899 C CB  . ALA A 1 223 ? 24.212  11.068 87.109  1.00 35.95  ? 223 ALA A CB  1 
ATOM   1900 N N   . VAL A 1 224 ? 22.497  9.218  84.579  1.00 30.27  ? 224 VAL A N   1 
ATOM   1901 C CA  . VAL A 1 224 ? 22.027  7.902  84.160  1.00 21.58  ? 224 VAL A CA  1 
ATOM   1902 C C   . VAL A 1 224 ? 21.712  7.947  82.672  1.00 23.13  ? 224 VAL A C   1 
ATOM   1903 O O   . VAL A 1 224 ? 21.579  9.015  82.070  1.00 27.82  ? 224 VAL A O   1 
ATOM   1904 C CB  . VAL A 1 224 ? 20.775  7.420  84.924  1.00 30.89  ? 224 VAL A CB  1 
ATOM   1905 C CG1 . VAL A 1 224 ? 21.160  6.810  86.244  1.00 38.34  ? 224 VAL A CG1 1 
ATOM   1906 C CG2 . VAL A 1 224 ? 19.791  8.553  85.083  1.00 26.87  ? 224 VAL A CG2 1 
ATOM   1907 N N   . SER A 1 225 ? 21.543  6.760  82.098  1.00 23.83  ? 225 SER A N   1 
ATOM   1908 C CA  . SER A 1 225 ? 21.222  6.598  80.687  1.00 24.06  ? 225 SER A CA  1 
ATOM   1909 C C   . SER A 1 225 ? 19.728  6.337  80.517  1.00 26.32  ? 225 SER A C   1 
ATOM   1910 O O   . SER A 1 225 ? 19.169  5.441  81.153  1.00 21.47  ? 225 SER A O   1 
ATOM   1911 C CB  . SER A 1 225 ? 22.019  5.441  80.085  1.00 27.89  ? 225 SER A CB  1 
ATOM   1912 O OG  . SER A 1 225 ? 21.613  5.207  78.753  1.00 29.33  ? 225 SER A OG  1 
ATOM   1913 N N   . PHE A 1 226 ? 19.100  7.108  79.639  1.00 23.32  ? 226 PHE A N   1 
ATOM   1914 C CA  . PHE A 1 226 ? 17.727  6.895  79.220  1.00 20.69  ? 226 PHE A CA  1 
ATOM   1915 C C   . PHE A 1 226 ? 17.654  6.219  77.853  1.00 18.81  ? 226 PHE A C   1 
ATOM   1916 O O   . PHE A 1 226 ? 16.567  6.119  77.285  1.00 20.88  ? 226 PHE A O   1 
ATOM   1917 C CB  . PHE A 1 226 ? 16.978  8.231  79.187  1.00 21.32  ? 226 PHE A CB  1 
ATOM   1918 C CG  . PHE A 1 226 ? 16.758  8.854  80.544  1.00 25.22  ? 226 PHE A CG  1 
ATOM   1919 C CD1 . PHE A 1 226 ? 15.643  8.530  81.303  1.00 24.19  ? 226 PHE A CD1 1 
ATOM   1920 C CD2 . PHE A 1 226 ? 17.659  9.790  81.051  1.00 24.29  ? 226 PHE A CD2 1 
ATOM   1921 C CE1 . PHE A 1 226 ? 15.426  9.129  82.555  1.00 22.06  ? 226 PHE A CE1 1 
ATOM   1922 C CE2 . PHE A 1 226 ? 17.455  10.374 82.293  1.00 26.10  ? 226 PHE A CE2 1 
ATOM   1923 C CZ  . PHE A 1 226 ? 16.341  10.046 83.045  1.00 25.36  ? 226 PHE A CZ  1 
ATOM   1924 N N   . ARG A 1 227 ? 18.788  5.743  77.319  1.00 20.53  ? 227 ARG A N   1 
ATOM   1925 C CA  . ARG A 1 227 ? 18.792  5.198  75.959  1.00 23.01  ? 227 ARG A CA  1 
ATOM   1926 C C   . ARG A 1 227 ? 17.904  3.962  75.842  1.00 24.73  ? 227 ARG A C   1 
ATOM   1927 O O   . ARG A 1 227 ? 17.197  3.791  74.843  1.00 21.17  ? 227 ARG A O   1 
ATOM   1928 C CB  . ARG A 1 227 ? 20.219  4.871  75.523  1.00 26.51  ? 227 ARG A CB  1 
ATOM   1929 C CG  . ARG A 1 227 ? 21.117  6.096  75.435  1.00 29.03  ? 227 ARG A CG  1 
ATOM   1930 C CD  . ARG A 1 227 ? 22.539  5.710  75.075  1.00 37.85  ? 227 ARG A CD  1 
ATOM   1931 N NE  . ARG A 1 227 ? 22.613  5.060  73.769  1.00 38.65  ? 227 ARG A NE  1 
ATOM   1932 C CZ  . ARG A 1 227 ? 22.517  5.705  72.609  1.00 43.94  ? 227 ARG A CZ  1 
ATOM   1933 N NH1 . ARG A 1 227 ? 22.330  7.025  72.584  1.00 39.12  ? 227 ARG A NH1 1 
ATOM   1934 N NH2 . ARG A 1 227 ? 22.602  5.031  71.471  1.00 44.86  ? 227 ARG A NH2 1 
ATOM   1935 N N   . GLU A 1 228 ? 17.930  3.089  76.850  1.00 19.77  ? 228 GLU A N   1 
ATOM   1936 C CA  . GLU A 1 228 ? 17.076  1.904  76.818  1.00 27.40  ? 228 GLU A CA  1 
ATOM   1937 C C   . GLU A 1 228 ? 15.594  2.266  76.945  1.00 24.49  ? 228 GLU A C   1 
ATOM   1938 O O   . GLU A 1 228 ? 14.739  1.646  76.297  1.00 27.16  ? 228 GLU A O   1 
ATOM   1939 C CB  . GLU A 1 228 ? 17.504  0.932  77.919  1.00 28.47  ? 228 GLU A CB  1 
ATOM   1940 C CG  . GLU A 1 228 ? 17.601  -0.500 77.451  1.00 47.74  ? 228 GLU A CG  1 
ATOM   1941 C CD  . GLU A 1 228 ? 16.242  -1.090 77.145  1.00 61.64  ? 228 GLU A CD  1 
ATOM   1942 O OE1 . GLU A 1 228 ? 15.390  -1.077 78.054  1.00 66.16  ? 228 GLU A OE1 1 
ATOM   1943 O OE2 . GLU A 1 228 ? 16.022  -1.562 76.006  1.00 65.53  ? 228 GLU A OE2 1 
ATOM   1944 N N   . ASP A 1 229 ? 15.260  3.244  77.791  1.00 24.91  ? 229 ASP A N   1 
ATOM   1945 C CA  . ASP A 1 229 ? 13.869  3.686  77.875  1.00 20.95  ? 229 ASP A CA  1 
ATOM   1946 C C   . ASP A 1 229 ? 13.390  4.256  76.540  1.00 21.05  ? 229 ASP A C   1 
ATOM   1947 O O   . ASP A 1 229 ? 12.210  4.126  76.196  1.00 20.23  ? 229 ASP A O   1 
ATOM   1948 C CB  . ASP A 1 229 ? 13.700  4.729  78.987  1.00 19.49  ? 229 ASP A CB  1 
ATOM   1949 C CG  . ASP A 1 229 ? 13.752  4.119  80.385  1.00 22.37  ? 229 ASP A CG  1 
ATOM   1950 O OD1 . ASP A 1 229 ? 13.747  2.877  80.504  1.00 24.78  ? 229 ASP A OD1 1 
ATOM   1951 O OD2 . ASP A 1 229 ? 13.797  4.887  81.371  1.00 22.97  ? 229 ASP A OD2 1 
ATOM   1952 N N   . ALA A 1 230 ? 14.287  4.875  75.773  1.00 24.47  ? 230 ALA A N   1 
ATOM   1953 C CA  . ALA A 1 230 ? 13.909  5.375  74.453  1.00 27.86  ? 230 ALA A CA  1 
ATOM   1954 C C   . ALA A 1 230 ? 13.473  4.230  73.542  1.00 20.36  ? 230 ALA A C   1 
ATOM   1955 O O   . ALA A 1 230 ? 12.422  4.306  72.893  1.00 22.43  ? 230 ALA A O   1 
ATOM   1956 C CB  . ALA A 1 230 ? 15.067  6.160  73.836  1.00 24.68  ? 230 ALA A CB  1 
ATOM   1957 N N   . SER A 1 231 ? 14.255  3.142  73.507  1.00 20.85  ? 231 SER A N   1 
ATOM   1958 C CA  . SER A 1 231 ? 13.820  1.933  72.802  1.00 24.87  ? 231 SER A CA  1 
ATOM   1959 C C   . SER A 1 231 ? 12.477  1.432  73.323  1.00 26.02  ? 231 SER A C   1 
ATOM   1960 O O   . SER A 1 231 ? 11.621  1.006  72.540  1.00 26.56  ? 231 SER A O   1 
ATOM   1961 C CB  . SER A 1 231 ? 14.864  0.824  72.940  1.00 26.37  ? 231 SER A CB  1 
ATOM   1962 O OG  . SER A 1 231 ? 15.826  0.897  71.907  1.00 41.44  ? 231 SER A OG  1 
ATOM   1963 N N   . LYS A 1 232 ? 12.284  1.466  74.645  1.00 25.47  ? 232 LYS A N   1 
ATOM   1964 C CA  . LYS A 1 232 ? 11.056  0.950  75.253  1.00 21.82  ? 232 LYS A CA  1 
ATOM   1965 C C   . LYS A 1 232 ? 9.815   1.703  74.775  1.00 24.50  ? 232 LYS A C   1 
ATOM   1966 O O   . LYS A 1 232 ? 8.823   1.083  74.376  1.00 27.74  ? 232 LYS A O   1 
ATOM   1967 C CB  . LYS A 1 232 ? 11.170  1.018  76.773  1.00 23.94  ? 232 LYS A CB  1 
ATOM   1968 C CG  . LYS A 1 232 ? 10.472  -0.119 77.504  1.00 40.10  ? 232 LYS A CG  1 
ATOM   1969 C CD  . LYS A 1 232 ? 11.124  -0.367 78.854  1.00 48.64  ? 232 LYS A CD  1 
ATOM   1970 C CE  . LYS A 1 232 ? 12.465  -1.047 78.683  1.00 51.25  ? 232 LYS A CE  1 
ATOM   1971 N NZ  . LYS A 1 232 ? 13.403  -0.783 79.817  1.00 54.77  ? 232 LYS A NZ  1 
ATOM   1972 N N   . HIS A 1 233 ? 9.831   3.044  74.852  1.00 25.81  ? 233 HIS A N   1 
ATOM   1973 C CA  . HIS A 1 233 ? 8.703   3.833  74.351  1.00 24.73  ? 233 HIS A CA  1 
ATOM   1974 C C   . HIS A 1 233 ? 8.302   3.403  72.945  1.00 23.55  ? 233 HIS A C   1 
ATOM   1975 O O   . HIS A 1 233 ? 7.113   3.285  72.636  1.00 17.57  ? 233 HIS A O   1 
ATOM   1976 C CB  . HIS A 1 233 ? 9.046   5.327  74.334  1.00 26.22  ? 233 HIS A CB  1 
ATOM   1977 C CG  . HIS A 1 233 ? 9.030   5.976  75.680  1.00 21.10  ? 233 HIS A CG  1 
ATOM   1978 N ND1 . HIS A 1 233 ? 7.866   6.344  76.312  1.00 18.28  ? 233 HIS A ND1 1 
ATOM   1979 C CD2 . HIS A 1 233 ? 10.039  6.334  76.508  1.00 19.66  ? 233 HIS A CD2 1 
ATOM   1980 C CE1 . HIS A 1 233 ? 8.155   6.896  77.478  1.00 17.75  ? 233 HIS A CE1 1 
ATOM   1981 N NE2 . HIS A 1 233 ? 9.470   6.901  77.621  1.00 19.19  ? 233 HIS A NE2 1 
ATOM   1982 N N   . VAL A 1 234 ? 9.286   3.171  72.076  1.00 20.18  ? 234 VAL A N   1 
ATOM   1983 C CA  . VAL A 1 234 ? 8.987   2.831  70.688  1.00 20.15  ? 234 VAL A CA  1 
ATOM   1984 C C   . VAL A 1 234 ? 8.437   1.419  70.585  1.00 21.18  ? 234 VAL A C   1 
ATOM   1985 O O   . VAL A 1 234 ? 7.471   1.173  69.853  1.00 19.24  ? 234 VAL A O   1 
ATOM   1986 C CB  . VAL A 1 234 ? 10.233  3.007  69.805  1.00 20.18  ? 234 VAL A CB  1 
ATOM   1987 C CG1 . VAL A 1 234 ? 9.892   2.725  68.340  1.00 22.44  ? 234 VAL A CG1 1 
ATOM   1988 C CG2 . VAL A 1 234 ? 10.783  4.410  69.959  1.00 24.17  ? 234 VAL A CG2 1 
ATOM   1989 N N   . GLU A 1 235 ? 9.055   0.466  71.295  1.00 21.75  ? 235 GLU A N   1 
ATOM   1990 C CA  . GLU A 1 235 ? 8.630   -0.929 71.219  1.00 27.39  ? 235 GLU A CA  1 
ATOM   1991 C C   . GLU A 1 235 ? 7.226   -1.118 71.792  1.00 23.26  ? 235 GLU A C   1 
ATOM   1992 O O   . GLU A 1 235 ? 6.384   -1.783 71.184  1.00 21.86  ? 235 GLU A O   1 
ATOM   1993 C CB  . GLU A 1 235 ? 9.639   -1.817 71.953  1.00 34.92  ? 235 GLU A CB  1 
ATOM   1994 C CG  . GLU A 1 235 ? 9.696   -3.247 71.447  1.00 48.06  ? 235 GLU A CG  1 
ATOM   1995 C CD  . GLU A 1 235 ? 9.973   -3.324 69.960  1.00 56.21  ? 235 GLU A CD  1 
ATOM   1996 O OE1 . GLU A 1 235 ? 11.101  -2.983 69.537  1.00 61.59  ? 235 GLU A OE1 1 
ATOM   1997 O OE2 . GLU A 1 235 ? 9.059   -3.722 69.214  1.00 60.40  ? 235 GLU A OE2 1 
ATOM   1998 N N   . LEU A 1 236 ? 6.957   -0.547 72.969  1.00 23.94  ? 236 LEU A N   1 
ATOM   1999 C CA  . LEU A 1 236 ? 5.626   -0.687 73.560  1.00 23.58  ? 236 LEU A CA  1 
ATOM   2000 C C   . LEU A 1 236 ? 4.561   0.032  72.729  1.00 20.68  ? 236 LEU A C   1 
ATOM   2001 O O   . LEU A 1 236 ? 3.406   -0.402 72.694  1.00 18.93  ? 236 LEU A O   1 
ATOM   2002 C CB  . LEU A 1 236 ? 5.631   -0.157 74.991  1.00 23.64  ? 236 LEU A CB  1 
ATOM   2003 C CG  . LEU A 1 236 ? 6.577   -0.811 76.006  1.00 27.53  ? 236 LEU A CG  1 
ATOM   2004 C CD1 . LEU A 1 236 ? 6.517   -0.046 77.322  1.00 31.75  ? 236 LEU A CD1 1 
ATOM   2005 C CD2 . LEU A 1 236 ? 6.244   -2.285 76.219  1.00 25.01  ? 236 LEU A CD2 1 
ATOM   2006 N N   . ALA A 1 237 ? 4.931   1.122  72.058  1.00 22.46  ? 237 ALA A N   1 
ATOM   2007 C CA  . ALA A 1 237 ? 4.006   1.798  71.154  1.00 20.13  ? 237 ALA A CA  1 
ATOM   2008 C C   . ALA A 1 237 ? 3.643   0.901  69.979  1.00 21.41  ? 237 ALA A C   1 
ATOM   2009 O O   . ALA A 1 237 ? 2.486   0.876  69.546  1.00 20.90  ? 237 ALA A O   1 
ATOM   2010 C CB  . ALA A 1 237 ? 4.626   3.099  70.647  1.00 18.21  ? 237 ALA A CB  1 
ATOM   2011 N N   . LYS A 1 238 ? 4.630   0.178  69.434  1.00 20.56  ? 238 LYS A N   1 
ATOM   2012 C CA  . LYS A 1 238 ? 4.331   -0.794 68.387  1.00 20.11  ? 238 LYS A CA  1 
ATOM   2013 C C   . LYS A 1 238 ? 3.404   -1.885 68.902  1.00 23.94  ? 238 LYS A C   1 
ATOM   2014 O O   . LYS A 1 238 ? 2.506   -2.338 68.183  1.00 24.12  ? 238 LYS A O   1 
ATOM   2015 C CB  . LYS A 1 238 ? 5.618   -1.417 67.854  1.00 21.60  ? 238 LYS A CB  1 
ATOM   2016 C CG  . LYS A 1 238 ? 6.542   -0.439 67.128  1.00 21.01  ? 238 LYS A CG  1 
ATOM   2017 C CD  . LYS A 1 238 ? 7.914   -1.065 66.884  1.00 25.11  ? 238 LYS A CD  1 
ATOM   2018 C CE  . LYS A 1 238 ? 7.803   -2.344 66.109  1.00 24.51  ? 238 LYS A CE  1 
ATOM   2019 N NZ  . LYS A 1 238 ? 9.155   -2.932 65.787  1.00 25.78  ? 238 LYS A NZ  1 
ATOM   2020 N N   . GLU A 1 239 ? 3.629   -2.343 70.140  1.00 20.02  ? 239 GLU A N   1 
ATOM   2021 C CA  . GLU A 1 239 ? 2.774   -3.378 70.715  1.00 24.20  ? 239 GLU A CA  1 
ATOM   2022 C C   . GLU A 1 239 ? 1.351   -2.863 70.868  1.00 25.97  ? 239 GLU A C   1 
ATOM   2023 O O   . GLU A 1 239 ? 0.387   -3.566 70.535  1.00 28.29  ? 239 GLU A O   1 
ATOM   2024 C CB  . GLU A 1 239 ? 3.299   -3.814 72.082  1.00 22.24  ? 239 GLU A CB  1 
ATOM   2025 C CG  . GLU A 1 239 ? 4.639   -4.502 72.126  1.00 32.86  ? 239 GLU A CG  1 
ATOM   2026 C CD  . GLU A 1 239 ? 4.922   -5.055 73.518  1.00 55.18  ? 239 GLU A CD  1 
ATOM   2027 O OE1 . GLU A 1 239 ? 6.061   -5.499 73.782  1.00 62.44  ? 239 GLU A OE1 1 
ATOM   2028 O OE2 . GLU A 1 239 ? 3.987   -5.025 74.358  1.00 63.81  ? 239 GLU A OE2 1 
ATOM   2029 N N   . LYS A 1 240 ? 1.191   -1.641 71.387  1.00 29.74  ? 240 LYS A N   1 
ATOM   2030 C CA  . LYS A 1 240 ? -0.144  -1.093 71.628  1.00 26.17  ? 240 LYS A CA  1 
ATOM   2031 C C   . LYS A 1 240 ? -0.900  -0.920 70.314  1.00 27.60  ? 240 LYS A C   1 
ATOM   2032 O O   . LYS A 1 240 ? -2.072  -1.305 70.201  1.00 23.21  ? 240 LYS A O   1 
ATOM   2033 C CB  . LYS A 1 240 ? -0.025  0.233  72.381  1.00 19.70  ? 240 LYS A CB  1 
ATOM   2034 C CG  . LYS A 1 240 ? -1.360  0.847  72.795  1.00 18.77  ? 240 LYS A CG  1 
ATOM   2035 C CD  . LYS A 1 240 ? -2.061  -0.047 73.788  1.00 16.52  ? 240 LYS A CD  1 
ATOM   2036 C CE  . LYS A 1 240 ? -3.496  0.423  73.974  1.00 26.02  ? 240 LYS A CE  1 
ATOM   2037 N NZ  . LYS A 1 240 ? -4.146  -0.324 75.085  1.00 26.65  ? 240 LYS A NZ  1 
ATOM   2038 N N   . TYR A 1 241 ? -0.234  -0.348 69.306  1.00 24.08  ? 241 TYR A N   1 
ATOM   2039 C CA  . TYR A 1 241 ? -0.838  -0.186 67.988  1.00 24.24  ? 241 TYR A CA  1 
ATOM   2040 C C   . TYR A 1 241 ? -1.231  -1.534 67.399  1.00 22.47  ? 241 TYR A C   1 
ATOM   2041 O O   . TYR A 1 241 ? -2.312  -1.675 66.814  1.00 23.00  ? 241 TYR A O   1 
ATOM   2042 C CB  . TYR A 1 241 ? 0.140   0.554  67.072  1.00 24.52  ? 241 TYR A CB  1 
ATOM   2043 C CG  . TYR A 1 241 ? -0.373  0.888  65.686  1.00 23.10  ? 241 TYR A CG  1 
ATOM   2044 C CD1 . TYR A 1 241 ? -0.372  -0.075 64.678  1.00 23.51  ? 241 TYR A CD1 1 
ATOM   2045 C CD2 . TYR A 1 241 ? -0.822  2.168  65.374  1.00 21.02  ? 241 TYR A CD2 1 
ATOM   2046 C CE1 . TYR A 1 241 ? -0.818  0.215  63.418  1.00 23.72  ? 241 TYR A CE1 1 
ATOM   2047 C CE2 . TYR A 1 241 ? -1.279  2.470  64.101  1.00 18.55  ? 241 TYR A CE2 1 
ATOM   2048 C CZ  . TYR A 1 241 ? -1.276  1.475  63.131  1.00 18.62  ? 241 TYR A CZ  1 
ATOM   2049 O OH  . TYR A 1 241 ? -1.714  1.735  61.859  1.00 22.26  ? 241 TYR A OH  1 
ATOM   2050 N N   . PHE A 1 242 ? -0.360  -2.535 67.557  1.00 19.11  ? 242 PHE A N   1 
ATOM   2051 C CA  . PHE A 1 242 ? -0.668  -3.899 67.144  1.00 23.55  ? 242 PHE A CA  1 
ATOM   2052 C C   . PHE A 1 242 ? -1.934  -4.413 67.817  1.00 26.31  ? 242 PHE A C   1 
ATOM   2053 O O   . PHE A 1 242 ? -2.773  -5.049 67.170  1.00 25.34  ? 242 PHE A O   1 
ATOM   2054 C CB  . PHE A 1 242 ? 0.522   -4.800 67.467  1.00 29.64  ? 242 PHE A CB  1 
ATOM   2055 C CG  . PHE A 1 242 ? 0.318   -6.241 67.108  1.00 39.02  ? 242 PHE A CG  1 
ATOM   2056 C CD1 . PHE A 1 242 ? -0.027  -6.611 65.818  1.00 43.44  ? 242 PHE A CD1 1 
ATOM   2057 C CD2 . PHE A 1 242 ? 0.506   -7.232 68.061  1.00 48.59  ? 242 PHE A CD2 1 
ATOM   2058 C CE1 . PHE A 1 242 ? -0.202  -7.939 65.483  1.00 48.96  ? 242 PHE A CE1 1 
ATOM   2059 C CE2 . PHE A 1 242 ? 0.337   -8.566 67.736  1.00 57.13  ? 242 PHE A CE2 1 
ATOM   2060 C CZ  . PHE A 1 242 ? -0.017  -8.919 66.444  1.00 55.40  ? 242 PHE A CZ  1 
ATOM   2061 N N   . GLU A 1 243 ? -2.083  -4.154 69.120  1.00 27.62  ? 243 GLU A N   1 
ATOM   2062 C CA  . GLU A 1 243 ? -3.272  -4.584 69.850  1.00 29.63  ? 243 GLU A CA  1 
ATOM   2063 C C   . GLU A 1 243 ? -4.539  -4.006 69.233  1.00 29.82  ? 243 GLU A C   1 
ATOM   2064 O O   . GLU A 1 243 ? -5.542  -4.711 69.084  1.00 27.36  ? 243 GLU A O   1 
ATOM   2065 C CB  . GLU A 1 243 ? -3.153  -4.172 71.320  1.00 35.53  ? 243 GLU A CB  1 
ATOM   2066 C CG  . GLU A 1 243 ? -4.479  -3.873 72.022  1.00 44.97  ? 243 GLU A CG  1 
ATOM   2067 C CD  . GLU A 1 243 ? -4.307  -3.509 73.500  1.00 57.85  ? 243 GLU A CD  1 
ATOM   2068 O OE1 . GLU A 1 243 ? -3.176  -3.648 74.028  1.00 67.34  ? 243 GLU A OE1 1 
ATOM   2069 O OE2 . GLU A 1 243 ? -5.302  -3.092 74.133  1.00 53.53  ? 243 GLU A OE2 1 
ATOM   2070 N N   . ILE A 1 244 ? -4.504  -2.734 68.829  1.00 26.54  ? 244 ILE A N   1 
ATOM   2071 C CA  . ILE A 1 244 ? -5.704  -2.047 68.366  1.00 20.40  ? 244 ILE A CA  1 
ATOM   2072 C C   . ILE A 1 244 ? -5.986  -2.358 66.898  1.00 24.32  ? 244 ILE A C   1 
ATOM   2073 O O   . ILE A 1 244 ? -7.125  -2.661 66.523  1.00 22.74  ? 244 ILE A O   1 
ATOM   2074 C CB  . ILE A 1 244 ? -5.558  -0.534 68.610  1.00 23.72  ? 244 ILE A CB  1 
ATOM   2075 C CG1 . ILE A 1 244 ? -5.329  -0.258 70.098  1.00 21.71  ? 244 ILE A CG1 1 
ATOM   2076 C CG2 . ILE A 1 244 ? -6.775  0.219  68.055  1.00 22.93  ? 244 ILE A CG2 1 
ATOM   2077 C CD1 . ILE A 1 244 ? -6.426  -0.821 71.035  1.00 24.36  ? 244 ILE A CD1 1 
ATOM   2078 N N   . PHE A 1 245 ? -4.965  -2.293 66.043  1.00 20.93  ? 245 PHE A N   1 
ATOM   2079 C CA  . PHE A 1 245 ? -5.160  -2.406 64.603  1.00 20.16  ? 245 PHE A CA  1 
ATOM   2080 C C   . PHE A 1 245 ? -4.703  -3.741 64.018  1.00 24.20  ? 245 PHE A C   1 
ATOM   2081 O O   . PHE A 1 245 ? -4.908  -3.974 62.824  1.00 27.08  ? 245 PHE A O   1 
ATOM   2082 C CB  . PHE A 1 245 ? -4.447  -1.250 63.892  1.00 21.38  ? 245 PHE A CB  1 
ATOM   2083 C CG  . PHE A 1 245 ? -4.952  0.114  64.292  1.00 24.58  ? 245 PHE A CG  1 
ATOM   2084 C CD1 . PHE A 1 245 ? -6.161  0.583  63.815  1.00 23.22  ? 245 PHE A CD1 1 
ATOM   2085 C CD2 . PHE A 1 245 ? -4.212  0.928  65.151  1.00 25.79  ? 245 PHE A CD2 1 
ATOM   2086 C CE1 . PHE A 1 245 ? -6.629  1.839  64.172  1.00 21.75  ? 245 PHE A CE1 1 
ATOM   2087 C CE2 . PHE A 1 245 ? -4.678  2.195  65.515  1.00 26.39  ? 245 PHE A CE2 1 
ATOM   2088 C CZ  . PHE A 1 245 ? -5.892  2.644  65.030  1.00 17.16  ? 245 PHE A CZ  1 
ATOM   2089 N N   . GLY A 1 246 ? -4.113  -4.629 64.818  1.00 24.23  ? 246 GLY A N   1 
ATOM   2090 C CA  . GLY A 1 246 ? -3.726  -5.943 64.328  1.00 25.95  ? 246 GLY A CA  1 
ATOM   2091 C C   . GLY A 1 246 ? -2.492  -5.968 63.457  1.00 34.41  ? 246 GLY A C   1 
ATOM   2092 O O   . GLY A 1 246 ? -2.144  -7.023 62.914  1.00 30.57  ? 246 GLY A O   1 
ATOM   2093 N N   . GLU A 1 247 ? -1.815  -4.835 63.317  1.00 34.34  ? 247 GLU A N   1 
ATOM   2094 C CA  . GLU A 1 247 ? -0.643  -4.712 62.469  1.00 40.45  ? 247 GLU A CA  1 
ATOM   2095 C C   . GLU A 1 247 ? 0.366   -3.839 63.204  1.00 30.24  ? 247 GLU A C   1 
ATOM   2096 O O   . GLU A 1 247 ? -0.009  -3.039 64.061  1.00 22.30  ? 247 GLU A O   1 
ATOM   2097 C CB  . GLU A 1 247 ? -1.044  -4.127 61.096  1.00 43.39  ? 247 GLU A CB  1 
ATOM   2098 C CG  . GLU A 1 247 ? 0.011   -3.313 60.381  1.00 55.12  ? 247 GLU A CG  1 
ATOM   2099 C CD  . GLU A 1 247 ? -0.594  -2.262 59.476  1.00 61.36  ? 247 GLU A CD  1 
ATOM   2100 O OE1 . GLU A 1 247 ? -1.808  -2.348 59.204  1.00 63.49  ? 247 GLU A OE1 1 
ATOM   2101 O OE2 . GLU A 1 247 ? 0.140   -1.347 59.039  1.00 64.81  ? 247 GLU A OE2 1 
ATOM   2102 N N   . HIS A 1 248 ? 1.648   -4.042 62.915  1.00 23.98  ? 248 HIS A N   1 
ATOM   2103 C CA  . HIS A 1 248 ? 2.633   -3.152 63.504  1.00 27.00  ? 248 HIS A CA  1 
ATOM   2104 C C   . HIS A 1 248 ? 2.659   -1.831 62.734  1.00 26.27  ? 248 HIS A C   1 
ATOM   2105 O O   . HIS A 1 248 ? 2.528   -1.825 61.508  1.00 28.02  ? 248 HIS A O   1 
ATOM   2106 C CB  . HIS A 1 248 ? 4.017   -3.802 63.496  1.00 32.61  ? 248 HIS A CB  1 
ATOM   2107 C CG  . HIS A 1 248 ? 4.159   -4.912 64.489  1.00 41.83  ? 248 HIS A CG  1 
ATOM   2108 N ND1 . HIS A 1 248 ? 4.181   -6.242 64.122  1.00 45.06  ? 248 HIS A ND1 1 
ATOM   2109 C CD2 . HIS A 1 248 ? 4.258   -4.893 65.838  1.00 42.38  ? 248 HIS A CD2 1 
ATOM   2110 C CE1 . HIS A 1 248 ? 4.301   -6.992 65.204  1.00 45.90  ? 248 HIS A CE1 1 
ATOM   2111 N NE2 . HIS A 1 248 ? 4.348   -6.198 66.258  1.00 44.81  ? 248 HIS A NE2 1 
ATOM   2112 N N   . PRO A 1 249 ? 2.819   -0.703 63.419  1.00 22.78  ? 249 PRO A N   1 
ATOM   2113 C CA  . PRO A 1 249 ? 2.819   0.585  62.712  1.00 26.93  ? 249 PRO A CA  1 
ATOM   2114 C C   . PRO A 1 249 ? 4.068   0.734  61.852  1.00 28.17  ? 249 PRO A C   1 
ATOM   2115 O O   . PRO A 1 249 ? 5.187   0.491  62.303  1.00 27.03  ? 249 PRO A O   1 
ATOM   2116 C CB  . PRO A 1 249 ? 2.793   1.615  63.850  1.00 27.74  ? 249 PRO A CB  1 
ATOM   2117 C CG  . PRO A 1 249 ? 3.493   0.922  64.973  1.00 25.19  ? 249 PRO A CG  1 
ATOM   2118 C CD  . PRO A 1 249 ? 3.104   -0.548 64.857  1.00 26.50  ? 249 PRO A CD  1 
ATOM   2119 N N   . VAL A 1 250 ? 3.865   1.151  60.608  1.00 29.51  ? 250 VAL A N   1 
ATOM   2120 C CA  . VAL A 1 250 ? 4.976   1.450  59.714  1.00 30.99  ? 250 VAL A CA  1 
ATOM   2121 C C   . VAL A 1 250 ? 5.293   2.948  59.673  1.00 25.87  ? 250 VAL A C   1 
ATOM   2122 O O   . VAL A 1 250 ? 6.399   3.323  59.249  1.00 20.39  ? 250 VAL A O   1 
ATOM   2123 C CB  . VAL A 1 250 ? 4.681   0.883  58.303  1.00 32.30  ? 250 VAL A CB  1 
ATOM   2124 C CG1 . VAL A 1 250 ? 3.386   1.413  57.775  1.00 37.34  ? 250 VAL A CG1 1 
ATOM   2125 C CG2 . VAL A 1 250 ? 5.782   1.158  57.337  1.00 36.33  ? 250 VAL A CG2 1 
ATOM   2126 N N   . TYR A 1 251 ? 4.370   3.806  60.119  1.00 20.27  ? 251 TYR A N   1 
ATOM   2127 C CA  . TYR A 1 251 ? 4.588   5.246  60.222  1.00 25.05  ? 251 TYR A CA  1 
ATOM   2128 C C   . TYR A 1 251 ? 4.541   5.678  61.678  1.00 23.95  ? 251 TYR A C   1 
ATOM   2129 O O   . TYR A 1 251 ? 3.773   5.125  62.475  1.00 24.71  ? 251 TYR A O   1 
ATOM   2130 C CB  . TYR A 1 251 ? 3.534   6.038  59.431  1.00 33.66  ? 251 TYR A CB  1 
ATOM   2131 C CG  . TYR A 1 251 ? 3.103   5.319  58.190  1.00 38.52  ? 251 TYR A CG  1 
ATOM   2132 C CD1 . TYR A 1 251 ? 3.977   5.189  57.123  1.00 42.49  ? 251 TYR A CD1 1 
ATOM   2133 C CD2 . TYR A 1 251 ? 1.843   4.730  58.093  1.00 42.20  ? 251 TYR A CD2 1 
ATOM   2134 C CE1 . TYR A 1 251 ? 3.618   4.514  55.989  1.00 48.83  ? 251 TYR A CE1 1 
ATOM   2135 C CE2 . TYR A 1 251 ? 1.465   4.046  56.939  1.00 42.99  ? 251 TYR A CE2 1 
ATOM   2136 C CZ  . TYR A 1 251 ? 2.368   3.948  55.896  1.00 50.04  ? 251 TYR A CZ  1 
ATOM   2137 O OH  . TYR A 1 251 ? 2.057   3.275  54.744  1.00 59.74  ? 251 TYR A OH  1 
ATOM   2138 N N   . MET A 1 252 ? 5.374   6.663  62.029  1.00 18.03  ? 252 MET A N   1 
ATOM   2139 C CA  . MET A 1 252 ? 5.311   7.255  63.352  1.00 17.77  ? 252 MET A CA  1 
ATOM   2140 C C   . MET A 1 252 ? 5.439   8.766  63.242  1.00 22.97  ? 252 MET A C   1 
ATOM   2141 O O   . MET A 1 252 ? 6.162   9.291  62.386  1.00 18.29  ? 252 MET A O   1 
ATOM   2142 C CB  . MET A 1 252 ? 6.399   6.709  64.290  1.00 25.95  ? 252 MET A CB  1 
ATOM   2143 C CG  . MET A 1 252 ? 6.042   5.364  64.912  1.00 28.84  ? 252 MET A CG  1 
ATOM   2144 S SD  . MET A 1 252 ? 7.059   4.927  66.332  1.00 25.50  ? 252 MET A SD  1 
ATOM   2145 C CE  . MET A 1 252 ? 6.302   3.397  66.880  1.00 24.61  ? 252 MET A CE  1 
ATOM   2146 N N   . TRP A 1 253 ? 4.713   9.456  64.114  1.00 21.42  ? 253 TRP A N   1 
ATOM   2147 C CA  . TRP A 1 253 ? 4.919   10.870 64.346  1.00 17.13  ? 253 TRP A CA  1 
ATOM   2148 C C   . TRP A 1 253 ? 5.837   11.024 65.540  1.00 19.42  ? 253 TRP A C   1 
ATOM   2149 O O   . TRP A 1 253 ? 5.431   10.685 66.665  1.00 18.88  ? 253 TRP A O   1 
ATOM   2150 C CB  . TRP A 1 253 ? 3.592   11.581 64.600  1.00 21.86  ? 253 TRP A CB  1 
ATOM   2151 C CG  . TRP A 1 253 ? 3.803   12.954 65.059  1.00 18.41  ? 253 TRP A CG  1 
ATOM   2152 C CD1 . TRP A 1 253 ? 3.526   13.455 66.297  1.00 23.59  ? 253 TRP A CD1 1 
ATOM   2153 C CD2 . TRP A 1 253 ? 4.362   14.031 64.301  1.00 21.50  ? 253 TRP A CD2 1 
ATOM   2154 N NE1 . TRP A 1 253 ? 3.877   14.777 66.359  1.00 25.90  ? 253 TRP A NE1 1 
ATOM   2155 C CE2 . TRP A 1 253 ? 4.393   15.159 65.147  1.00 27.89  ? 253 TRP A CE2 1 
ATOM   2156 C CE3 . TRP A 1 253 ? 4.838   14.153 62.990  1.00 21.76  ? 253 TRP A CE3 1 
ATOM   2157 C CZ2 . TRP A 1 253 ? 4.876   16.403 64.723  1.00 23.27  ? 253 TRP A CZ2 1 
ATOM   2158 C CZ3 . TRP A 1 253 ? 5.324   15.383 62.571  1.00 21.30  ? 253 TRP A CZ3 1 
ATOM   2159 C CH2 . TRP A 1 253 ? 5.346   16.493 63.438  1.00 18.80  ? 253 TRP A CH2 1 
ATOM   2160 N N   . PRO A 1 254 ? 7.062   11.518 65.364  1.00 17.05  ? 254 PRO A N   1 
ATOM   2161 C CA  . PRO A 1 254 ? 7.926   11.765 66.504  1.00 18.12  ? 254 PRO A CA  1 
ATOM   2162 C C   . PRO A 1 254 ? 7.362   12.896 67.347  1.00 18.46  ? 254 PRO A C   1 
ATOM   2163 O O   . PRO A 1 254 ? 7.003   13.953 66.816  1.00 19.55  ? 254 PRO A O   1 
ATOM   2164 C CB  . PRO A 1 254 ? 9.274   12.147 65.862  1.00 22.54  ? 254 PRO A CB  1 
ATOM   2165 C CG  . PRO A 1 254 ? 8.921   12.687 64.516  1.00 26.61  ? 254 PRO A CG  1 
ATOM   2166 C CD  . PRO A 1 254 ? 7.666   11.942 64.085  1.00 22.53  ? 254 PRO A CD  1 
ATOM   2167 N N   . PRO A 1 255 ? 7.231   12.687 68.651  1.00 20.14  ? 255 PRO A N   1 
ATOM   2168 C CA  . PRO A 1 255 ? 6.680   13.721 69.531  1.00 19.22  ? 255 PRO A CA  1 
ATOM   2169 C C   . PRO A 1 255 ? 7.377   15.057 69.343  1.00 18.48  ? 255 PRO A C   1 
ATOM   2170 O O   . PRO A 1 255 ? 8.605   15.132 69.314  1.00 18.32  ? 255 PRO A O   1 
ATOM   2171 C CB  . PRO A 1 255 ? 6.924   13.152 70.929  1.00 21.27  ? 255 PRO A CB  1 
ATOM   2172 C CG  . PRO A 1 255 ? 6.948   11.687 70.725  1.00 20.20  ? 255 PRO A CG  1 
ATOM   2173 C CD  . PRO A 1 255 ? 7.576   11.458 69.384  1.00 20.67  ? 255 PRO A CD  1 
ATOM   2174 N N   . GLU A 1 256 ? 6.568   16.115 69.200  1.00 22.35  ? 256 GLU A N   1 
ATOM   2175 C CA  . GLU A 1 256 ? 7.041   17.481 68.940  1.00 19.85  ? 256 GLU A CA  1 
ATOM   2176 C C   . GLU A 1 256 ? 7.880   17.569 67.674  1.00 19.75  ? 256 GLU A C   1 
ATOM   2177 O O   . GLU A 1 256 ? 8.795   18.383 67.603  1.00 17.10  ? 256 GLU A O   1 
ATOM   2178 C CB  . GLU A 1 256 ? 7.850   18.044 70.112  1.00 23.42  ? 256 GLU A CB  1 
ATOM   2179 C CG  . GLU A 1 256 ? 7.238   17.785 71.465  1.00 25.23  ? 256 GLU A CG  1 
ATOM   2180 C CD  . GLU A 1 256 ? 5.993   18.606 71.685  1.00 22.68  ? 256 GLU A CD  1 
ATOM   2181 O OE1 . GLU A 1 256 ? 5.799   19.629 70.986  1.00 22.79  ? 256 GLU A OE1 1 
ATOM   2182 O OE2 . GLU A 1 256 ? 5.205   18.229 72.567  1.00 24.48  ? 256 GLU A OE2 1 
ATOM   2183 N N   . ALA A 1 257 ? 7.603   16.718 66.681  1.00 18.82  ? 257 ALA A N   1 
ATOM   2184 C CA  . ALA A 1 257 ? 8.405   16.651 65.452  1.00 21.41  ? 257 ALA A CA  1 
ATOM   2185 C C   . ALA A 1 257 ? 9.884   16.390 65.742  1.00 22.26  ? 257 ALA A C   1 
ATOM   2186 O O   . ALA A 1 257 ? 10.742  16.615 64.875  1.00 20.76  ? 257 ALA A O   1 
ATOM   2187 C CB  . ALA A 1 257 ? 8.261   17.930 64.610  1.00 16.88  ? 257 ALA A CB  1 
ATOM   2188 N N   . SER A 1 258 ? 10.213  15.919 66.949  1.00 20.91  ? 258 SER A N   1 
ATOM   2189 C CA  . SER A 1 258 ? 11.606  15.915 67.381  1.00 16.60  ? 258 SER A CA  1 
ATOM   2190 C C   . SER A 1 258 ? 12.375  14.798 66.691  1.00 20.84  ? 258 SER A C   1 
ATOM   2191 O O   . SER A 1 258 ? 12.011  13.623 66.796  1.00 17.93  ? 258 SER A O   1 
ATOM   2192 C CB  . SER A 1 258 ? 11.704  15.765 68.894  1.00 24.98  ? 258 SER A CB  1 
ATOM   2193 O OG  . SER A 1 258 ? 12.995  16.152 69.327  1.00 33.06  ? 258 SER A OG  1 
ATOM   2194 N N   . VAL A 1 259 ? 13.460  15.171 66.002  1.00 21.34  ? 259 VAL A N   1 
ATOM   2195 C CA  . VAL A 1 259 ? 14.376  14.218 65.400  1.00 16.78  ? 259 VAL A CA  1 
ATOM   2196 C C   . VAL A 1 259 ? 15.810  14.619 65.713  1.00 20.79  ? 259 VAL A C   1 
ATOM   2197 O O   . VAL A 1 259 ? 16.110  15.756 66.091  1.00 20.74  ? 259 VAL A O   1 
ATOM   2198 C CB  . VAL A 1 259 ? 14.185  14.094 63.866  1.00 22.40  ? 259 VAL A CB  1 
ATOM   2199 C CG1 . VAL A 1 259 ? 12.796  13.559 63.536  1.00 18.08  ? 259 VAL A CG1 1 
ATOM   2200 C CG2 . VAL A 1 259 ? 14.435  15.432 63.190  1.00 23.67  ? 259 VAL A CG2 1 
ATOM   2201 N N   . SER A 1 260 ? 16.689  13.636 65.576  1.00 26.70  ? 260 SER A N   1 
ATOM   2202 C CA  . SER A 1 260 ? 18.131  13.797 65.592  1.00 26.85  ? 260 SER A CA  1 
ATOM   2203 C C   . SER A 1 260 ? 18.669  12.622 64.786  1.00 24.01  ? 260 SER A C   1 
ATOM   2204 O O   . SER A 1 260 ? 17.913  11.721 64.410  1.00 23.30  ? 260 SER A O   1 
ATOM   2205 C CB  . SER A 1 260 ? 18.692  13.820 67.021  1.00 23.84  ? 260 SER A CB  1 
ATOM   2206 O OG  . SER A 1 260 ? 18.601  12.537 67.642  1.00 25.23  ? 260 SER A OG  1 
ATOM   2207 N N   . ASN A 1 261 ? 19.978  12.634 64.512  1.00 18.97  ? 261 ASN A N   1 
ATOM   2208 C CA  . ASN A 1 261 ? 20.576  11.511 63.792  1.00 20.80  ? 261 ASN A CA  1 
ATOM   2209 C C   . ASN A 1 261 ? 20.375  10.202 64.550  1.00 20.01  ? 261 ASN A C   1 
ATOM   2210 O O   . ASN A 1 261 ? 20.054  9.167  63.952  1.00 19.54  ? 261 ASN A O   1 
ATOM   2211 C CB  . ASN A 1 261 ? 22.070  11.758 63.557  1.00 21.83  ? 261 ASN A CB  1 
ATOM   2212 C CG  . ASN A 1 261 ? 22.335  12.875 62.574  1.00 23.41  ? 261 ASN A CG  1 
ATOM   2213 O OD1 . ASN A 1 261 ? 21.444  13.302 61.840  1.00 20.96  ? 261 ASN A OD1 1 
ATOM   2214 N ND2 . ASN A 1 261 ? 23.571  13.360 62.556  1.00 26.28  ? 261 ASN A ND2 1 
ATOM   2215 N N   . GLU A 1 262 ? 20.576  10.227 65.867  1.00 20.52  ? 262 GLU A N   1 
ATOM   2216 C CA  . GLU A 1 262 ? 20.392  9.021  66.670  1.00 20.84  ? 262 GLU A CA  1 
ATOM   2217 C C   . GLU A 1 262 ? 18.929  8.609  66.730  1.00 21.36  ? 262 GLU A C   1 
ATOM   2218 O O   . GLU A 1 262 ? 18.614  7.411  66.699  1.00 21.98  ? 262 GLU A O   1 
ATOM   2219 C CB  . GLU A 1 262 ? 20.938  9.240  68.080  1.00 22.75  ? 262 GLU A CB  1 
ATOM   2220 C CG  . GLU A 1 262 ? 22.459  9.271  68.118  1.00 25.17  ? 262 GLU A CG  1 
ATOM   2221 C CD  . GLU A 1 262 ? 23.014  9.464  69.524  1.00 40.07  ? 262 GLU A CD  1 
ATOM   2222 O OE1 . GLU A 1 262 ? 22.652  8.675  70.426  1.00 44.31  ? 262 GLU A OE1 1 
ATOM   2223 O OE2 . GLU A 1 262 ? 23.816  10.404 69.724  1.00 41.37  ? 262 GLU A OE2 1 
ATOM   2224 N N   . ALA A 1 263 ? 18.017  9.578  66.838  1.00 22.25  ? 263 ALA A N   1 
ATOM   2225 C CA  . ALA A 1 263 ? 16.600  9.224  66.909  1.00 23.69  ? 263 ALA A CA  1 
ATOM   2226 C C   . ALA A 1 263 ? 16.149  8.549  65.625  1.00 21.78  ? 263 ALA A C   1 
ATOM   2227 O O   . ALA A 1 263 ? 15.461  7.523  65.662  1.00 19.38  ? 263 ALA A O   1 
ATOM   2228 C CB  . ALA A 1 263 ? 15.749  10.461 67.198  1.00 15.77  ? 263 ALA A CB  1 
ATOM   2229 N N   . LEU A 1 264 ? 16.564  9.092  64.477  1.00 24.04  ? 264 LEU A N   1 
ATOM   2230 C CA  . LEU A 1 264 ? 16.200  8.496  63.196  1.00 24.70  ? 264 LEU A CA  1 
ATOM   2231 C C   . LEU A 1 264 ? 16.765  7.083  63.058  1.00 25.55  ? 264 LEU A C   1 
ATOM   2232 O O   . LEU A 1 264 ? 16.125  6.207  62.467  1.00 23.35  ? 264 LEU A O   1 
ATOM   2233 C CB  . LEU A 1 264 ? 16.685  9.389  62.056  1.00 21.19  ? 264 LEU A CB  1 
ATOM   2234 C CG  . LEU A 1 264 ? 15.923  10.704 61.851  1.00 26.82  ? 264 LEU A CG  1 
ATOM   2235 C CD1 . LEU A 1 264 ? 16.752  11.667 61.029  1.00 28.95  ? 264 LEU A CD1 1 
ATOM   2236 C CD2 . LEU A 1 264 ? 14.585  10.448 61.175  1.00 23.21  ? 264 LEU A CD2 1 
ATOM   2237 N N   . GLU A 1 265 ? 17.973  6.851  63.576  1.00 19.57  ? 265 GLU A N   1 
ATOM   2238 C CA  . GLU A 1 265 ? 18.542  5.508  63.563  1.00 21.63  ? 265 GLU A CA  1 
ATOM   2239 C C   . GLU A 1 265 ? 17.721  4.555  64.417  1.00 24.02  ? 265 GLU A C   1 
ATOM   2240 O O   . GLU A 1 265 ? 17.503  3.402  64.032  1.00 27.37  ? 265 GLU A O   1 
ATOM   2241 C CB  . GLU A 1 265 ? 19.989  5.543  64.058  1.00 21.18  ? 265 GLU A CB  1 
ATOM   2242 C CG  . GLU A 1 265 ? 20.953  6.190  63.089  1.00 27.04  ? 265 GLU A CG  1 
ATOM   2243 C CD  . GLU A 1 265 ? 21.312  5.290  61.917  1.00 37.69  ? 265 GLU A CD  1 
ATOM   2244 O OE1 . GLU A 1 265 ? 21.013  4.071  61.964  1.00 40.48  ? 265 GLU A OE1 1 
ATOM   2245 O OE2 . GLU A 1 265 ? 21.902  5.807  60.944  1.00 44.49  ? 265 GLU A OE2 1 
ATOM   2246 N N   . LEU A 1 266 ? 17.274  5.017  65.584  1.00 23.52  ? 266 LEU A N   1 
ATOM   2247 C CA  . LEU A 1 266 ? 16.454  4.178  66.453  1.00 20.20  ? 266 LEU A CA  1 
ATOM   2248 C C   . LEU A 1 266 ? 15.118  3.834  65.801  1.00 18.87  ? 266 LEU A C   1 
ATOM   2249 O O   . LEU A 1 266 ? 14.679  2.680  65.839  1.00 22.26  ? 266 LEU A O   1 
ATOM   2250 C CB  . LEU A 1 266 ? 16.230  4.878  67.793  1.00 19.73  ? 266 LEU A CB  1 
ATOM   2251 C CG  . LEU A 1 266 ? 15.240  4.178  68.718  1.00 22.47  ? 266 LEU A CG  1 
ATOM   2252 C CD1 . LEU A 1 266 ? 15.809  2.832  69.161  1.00 28.21  ? 266 LEU A CD1 1 
ATOM   2253 C CD2 . LEU A 1 266 ? 14.926  5.062  69.916  1.00 19.80  ? 266 LEU A CD2 1 
ATOM   2254 N N   . TYR A 1 267 ? 14.435  4.833  65.232  1.00 22.79  ? 267 TYR A N   1 
ATOM   2255 C CA  . TYR A 1 267 ? 13.191  4.554  64.516  1.00 21.93  ? 267 TYR A CA  1 
ATOM   2256 C C   . TYR A 1 267 ? 13.420  3.534  63.404  1.00 24.83  ? 267 TYR A C   1 
ATOM   2257 O O   . TYR A 1 267 ? 12.584  2.655  63.165  1.00 26.15  ? 267 TYR A O   1 
ATOM   2258 C CB  . TYR A 1 267 ? 12.617  5.850  63.937  1.00 22.66  ? 267 TYR A CB  1 
ATOM   2259 C CG  . TYR A 1 267 ? 11.946  6.746  64.954  1.00 21.07  ? 267 TYR A CG  1 
ATOM   2260 C CD1 . TYR A 1 267 ? 10.859  6.286  65.697  1.00 25.81  ? 267 TYR A CD1 1 
ATOM   2261 C CD2 . TYR A 1 267 ? 12.387  8.050  65.167  1.00 21.90  ? 267 TYR A CD2 1 
ATOM   2262 C CE1 . TYR A 1 267 ? 10.221  7.102  66.636  1.00 19.98  ? 267 TYR A CE1 1 
ATOM   2263 C CE2 . TYR A 1 267 ? 11.762  8.878  66.114  1.00 23.57  ? 267 TYR A CE2 1 
ATOM   2264 C CZ  . TYR A 1 267 ? 10.675  8.388  66.840  1.00 17.28  ? 267 TYR A CZ  1 
ATOM   2265 O OH  . TYR A 1 267 ? 10.035  9.170  67.776  1.00 19.11  ? 267 TYR A OH  1 
ATOM   2266 N N   . TYR A 1 268 ? 14.555  3.633  62.718  1.00 20.85  ? 268 TYR A N   1 
ATOM   2267 C CA  . TYR A 1 268 ? 14.853  2.689  61.648  1.00 21.54  ? 268 TYR A CA  1 
ATOM   2268 C C   . TYR A 1 268 ? 15.088  1.286  62.193  1.00 26.32  ? 268 TYR A C   1 
ATOM   2269 O O   . TYR A 1 268 ? 14.563  0.306  61.651  1.00 21.19  ? 268 TYR A O   1 
ATOM   2270 C CB  . TYR A 1 268 ? 16.076  3.158  60.864  1.00 21.28  ? 268 TYR A CB  1 
ATOM   2271 C CG  . TYR A 1 268 ? 16.710  2.057  60.054  1.00 26.32  ? 268 TYR A CG  1 
ATOM   2272 C CD1 . TYR A 1 268 ? 16.046  1.495  58.973  1.00 29.58  ? 268 TYR A CD1 1 
ATOM   2273 C CD2 . TYR A 1 268 ? 17.978  1.586  60.365  1.00 24.61  ? 268 TYR A CD2 1 
ATOM   2274 C CE1 . TYR A 1 268 ? 16.626  0.482  58.225  1.00 32.67  ? 268 TYR A CE1 1 
ATOM   2275 C CE2 . TYR A 1 268 ? 18.567  0.585  59.627  1.00 32.26  ? 268 TYR A CE2 1 
ATOM   2276 C CZ  . TYR A 1 268 ? 17.888  0.034  58.559  1.00 33.82  ? 268 TYR A CZ  1 
ATOM   2277 O OH  . TYR A 1 268 ? 18.479  -0.969 57.827  1.00 36.44  ? 268 TYR A OH  1 
ATOM   2278 N N   . GLU A 1 269 ? 15.881  1.167  63.258  1.00 24.32  ? 269 GLU A N   1 
ATOM   2279 C CA  . GLU A 1 269 ? 16.132  -0.150 63.833  1.00 27.91  ? 269 GLU A CA  1 
ATOM   2280 C C   . GLU A 1 269 ? 14.851  -0.789 64.350  1.00 28.44  ? 269 GLU A C   1 
ATOM   2281 O O   . GLU A 1 269 ? 14.745  -2.019 64.375  1.00 30.68  ? 269 GLU A O   1 
ATOM   2282 C CB  . GLU A 1 269 ? 17.167  -0.044 64.954  1.00 29.81  ? 269 GLU A CB  1 
ATOM   2283 C CG  . GLU A 1 269 ? 18.545  0.361  64.463  1.00 38.31  ? 269 GLU A CG  1 
ATOM   2284 C CD  . GLU A 1 269 ? 19.462  0.796  65.591  1.00 52.88  ? 269 GLU A CD  1 
ATOM   2285 O OE1 . GLU A 1 269 ? 18.970  0.978  66.727  1.00 54.99  ? 269 GLU A OE1 1 
ATOM   2286 O OE2 . GLU A 1 269 ? 20.680  0.952  65.339  1.00 58.57  ? 269 GLU A OE2 1 
ATOM   2287 N N   . LYS A 1 270 ? 13.870  0.020  64.758  1.00 21.71  ? 270 LYS A N   1 
ATOM   2288 C CA  . LYS A 1 270 ? 12.597  -0.486 65.253  1.00 22.51  ? 270 LYS A CA  1 
ATOM   2289 C C   . LYS A 1 270 ? 11.577  -0.710 64.135  1.00 26.06  ? 270 LYS A C   1 
ATOM   2290 O O   . LYS A 1 270 ? 10.378  -0.859 64.417  1.00 24.01  ? 270 LYS A O   1 
ATOM   2291 C CB  . LYS A 1 270 ? 12.024  0.468  66.308  1.00 28.58  ? 270 LYS A CB  1 
ATOM   2292 C CG  . LYS A 1 270 ? 12.843  0.540  67.608  1.00 31.24  ? 270 LYS A CG  1 
ATOM   2293 C CD  . LYS A 1 270 ? 13.085  -0.843 68.170  1.00 38.06  ? 270 LYS A CD  1 
ATOM   2294 C CE  . LYS A 1 270 ? 13.820  -0.795 69.498  1.00 44.09  ? 270 LYS A CE  1 
ATOM   2295 N NZ  . LYS A 1 270 ? 14.811  -1.909 69.608  1.00 49.51  ? 270 LYS A NZ  1 
ATOM   2296 N N   . GLY A 1 271 ? 12.023  -0.718 62.878  1.00 23.77  ? 271 GLY A N   1 
ATOM   2297 C CA  . GLY A 1 271 ? 11.158  -1.067 61.768  1.00 29.76  ? 271 GLY A CA  1 
ATOM   2298 C C   . GLY A 1 271 ? 10.281  0.041  61.225  1.00 26.29  ? 271 GLY A C   1 
ATOM   2299 O O   . GLY A 1 271 ? 9.412   -0.242 60.397  1.00 24.80  ? 271 GLY A O   1 
ATOM   2300 N N   . ILE A 1 272 ? 10.471  1.289  61.655  1.00 18.84  ? 272 ILE A N   1 
ATOM   2301 C CA  . ILE A 1 272 ? 9.651   2.395  61.171  1.00 18.48  ? 272 ILE A CA  1 
ATOM   2302 C C   . ILE A 1 272 ? 10.150  2.788  59.787  1.00 23.84  ? 272 ILE A C   1 
ATOM   2303 O O   . ILE A 1 272 ? 11.354  2.965  59.577  1.00 23.51  ? 272 ILE A O   1 
ATOM   2304 C CB  . ILE A 1 272 ? 9.705   3.588  62.149  1.00 22.61  ? 272 ILE A CB  1 
ATOM   2305 C CG1 . ILE A 1 272 ? 9.389   3.147  63.586  1.00 23.40  ? 272 ILE A CG1 1 
ATOM   2306 C CG2 . ILE A 1 272 ? 8.783   4.730  61.699  1.00 20.34  ? 272 ILE A CG2 1 
ATOM   2307 C CD1 . ILE A 1 272 ? 8.077   2.390  63.724  1.00 31.50  ? 272 ILE A CD1 1 
ATOM   2308 N N   . ASN A 1 273 ? 9.231   2.915  58.831  1.00 22.73  ? 273 ASN A N   1 
ATOM   2309 C CA  . ASN A 1 273 ? 9.637   3.214  57.467  1.00 25.54  ? 273 ASN A CA  1 
ATOM   2310 C C   . ASN A 1 273 ? 9.471   4.680  57.092  1.00 26.56  ? 273 ASN A C   1 
ATOM   2311 O O   . ASN A 1 273 ? 10.156  5.145  56.178  1.00 25.97  ? 273 ASN A O   1 
ATOM   2312 C CB  . ASN A 1 273 ? 8.852   2.351  56.473  1.00 38.19  ? 273 ASN A CB  1 
ATOM   2313 C CG  . ASN A 1 273 ? 9.476   0.997  56.267  1.00 52.05  ? 273 ASN A CG  1 
ATOM   2314 O OD1 . ASN A 1 273 ? 9.220   0.058  57.021  1.00 55.11  ? 273 ASN A OD1 1 
ATOM   2315 N ND2 . ASN A 1 273 ? 10.318  0.888  55.250  1.00 60.46  ? 273 ASN A ND2 1 
ATOM   2316 N N   . MET A 1 274 ? 8.589   5.418  57.761  1.00 19.98  ? 274 MET A N   1 
ATOM   2317 C CA  . MET A 1 274 ? 8.406   6.819  57.420  1.00 23.95  ? 274 MET A CA  1 
ATOM   2318 C C   . MET A 1 274 ? 7.987   7.609  58.652  1.00 26.82  ? 274 MET A C   1 
ATOM   2319 O O   . MET A 1 274 ? 7.238   7.114  59.500  1.00 27.15  ? 274 MET A O   1 
ATOM   2320 C CB  . MET A 1 274 ? 7.370   6.987  56.303  1.00 25.12  ? 274 MET A CB  1 
ATOM   2321 C CG  . MET A 1 274 ? 7.330   8.380  55.720  1.00 39.04  ? 274 MET A CG  1 
ATOM   2322 S SD  . MET A 1 274 ? 5.928   9.269  56.391  1.00 57.66  ? 274 MET A SD  1 
ATOM   2323 C CE  . MET A 1 274 ? 4.632   8.528  55.395  1.00 49.97  ? 274 MET A CE  1 
ATOM   2324 N N   . LEU A 1 275 ? 8.483   8.833  58.746  1.00 23.91  ? 275 LEU A N   1 
ATOM   2325 C CA  . LEU A 1 275 ? 7.990   9.791  59.718  1.00 24.69  ? 275 LEU A CA  1 
ATOM   2326 C C   . LEU A 1 275 ? 7.951   11.157 59.050  1.00 25.06  ? 275 LEU A C   1 
ATOM   2327 O O   . LEU A 1 275 ? 8.354   11.316 57.893  1.00 20.39  ? 275 LEU A O   1 
ATOM   2328 C CB  . LEU A 1 275 ? 8.860   9.791  60.976  1.00 31.81  ? 275 LEU A CB  1 
ATOM   2329 C CG  . LEU A 1 275 ? 10.373  9.847  60.759  1.00 36.86  ? 275 LEU A CG  1 
ATOM   2330 C CD1 . LEU A 1 275 ? 10.851  11.294 60.685  1.00 40.00  ? 275 LEU A CD1 1 
ATOM   2331 C CD2 . LEU A 1 275 ? 11.090  9.099  61.874  1.00 33.44  ? 275 LEU A CD2 1 
ATOM   2332 N N   . ALA A 1 276 ? 7.455   12.148 59.781  1.00 21.39  ? 276 ALA A N   1 
ATOM   2333 C CA  . ALA A 1 276 ? 7.562   13.535 59.365  1.00 21.76  ? 276 ALA A CA  1 
ATOM   2334 C C   . ALA A 1 276 ? 8.173   14.337 60.501  1.00 25.22  ? 276 ALA A C   1 
ATOM   2335 O O   . ALA A 1 276 ? 8.131   13.933 61.664  1.00 25.29  ? 276 ALA A O   1 
ATOM   2336 C CB  . ALA A 1 276 ? 6.199   14.133 58.970  1.00 16.00  ? 276 ALA A CB  1 
ATOM   2337 N N   . THR A 1 277 ? 8.777   15.467 60.147  1.00 21.51  ? 277 THR A N   1 
ATOM   2338 C CA  . THR A 1 277 ? 9.273   16.421 61.126  1.00 23.83  ? 277 THR A CA  1 
ATOM   2339 C C   . THR A 1 277 ? 8.997   17.815 60.576  1.00 23.56  ? 277 THR A C   1 
ATOM   2340 O O   . THR A 1 277 ? 8.245   17.976 59.605  1.00 20.32  ? 277 THR A O   1 
ATOM   2341 C CB  . THR A 1 277 ? 10.759  16.182 61.439  1.00 24.41  ? 277 THR A CB  1 
ATOM   2342 O OG1 . THR A 1 277 ? 11.198  17.099 62.451  1.00 22.96  ? 277 THR A OG1 1 
ATOM   2343 C CG2 . THR A 1 277 ? 11.590  16.400 60.215  1.00 20.75  ? 277 THR A CG2 1 
ATOM   2344 N N   . ASP A 1 278 ? 9.624   18.829 61.181  1.00 17.83  ? 278 ASP A N   1 
ATOM   2345 C CA  . ASP A 1 278 ? 9.306   20.223 60.893  1.00 17.50  ? 278 ASP A CA  1 
ATOM   2346 C C   . ASP A 1 278 ? 10.225  20.827 59.838  1.00 19.53  ? 278 ASP A C   1 
ATOM   2347 O O   . ASP A 1 278 ? 11.371  20.413 59.665  1.00 24.99  ? 278 ASP A O   1 
ATOM   2348 C CB  . ASP A 1 278 ? 9.384   21.083 62.160  1.00 17.89  ? 278 ASP A CB  1 
ATOM   2349 C CG  . ASP A 1 278 ? 8.846   22.491 61.938  1.00 24.23  ? 278 ASP A CG  1 
ATOM   2350 O OD1 . ASP A 1 278 ? 7.669   22.637 61.531  1.00 27.69  ? 278 ASP A OD1 1 
ATOM   2351 O OD2 . ASP A 1 278 ? 9.601   23.453 62.142  1.00 31.43  ? 278 ASP A OD2 1 
ATOM   2352 N N   . GLU A 1 279 ? 9.695   21.847 59.161  1.00 26.31  ? 279 GLU A N   1 
ATOM   2353 C CA  . GLU A 1 279 ? 10.422  22.585 58.133  1.00 28.03  ? 279 GLU A CA  1 
ATOM   2354 C C   . GLU A 1 279 ? 11.641  23.322 58.690  1.00 26.44  ? 279 GLU A C   1 
ATOM   2355 O O   . GLU A 1 279 ? 12.635  23.502 57.975  1.00 27.89  ? 279 GLU A O   1 
ATOM   2356 C CB  . GLU A 1 279 ? 9.461   23.574 57.461  1.00 27.13  ? 279 GLU A CB  1 
ATOM   2357 C CG  . GLU A 1 279 ? 10.031  24.259 56.254  1.00 30.45  ? 279 GLU A CG  1 
ATOM   2358 C CD  . GLU A 1 279 ? 8.995   24.997 55.422  1.00 36.83  ? 279 GLU A CD  1 
ATOM   2359 O OE1 . GLU A 1 279 ? 7.791   24.913 55.738  1.00 34.87  ? 279 GLU A OE1 1 
ATOM   2360 O OE2 . GLU A 1 279 ? 9.398   25.677 54.449  1.00 38.86  ? 279 GLU A OE2 1 
ATOM   2361 N N   . VAL A 1 280 ? 11.584  23.781 59.944  1.00 23.69  ? 280 VAL A N   1 
ATOM   2362 C CA  . VAL A 1 280 ? 12.754  24.427 60.534  1.00 22.24  ? 280 VAL A CA  1 
ATOM   2363 C C   . VAL A 1 280 ? 13.910  23.440 60.656  1.00 24.06  ? 280 VAL A C   1 
ATOM   2364 O O   . VAL A 1 280 ? 15.080  23.826 60.549  1.00 19.96  ? 280 VAL A O   1 
ATOM   2365 C CB  . VAL A 1 280 ? 12.382  25.058 61.893  1.00 23.78  ? 280 VAL A CB  1 
ATOM   2366 C CG1 . VAL A 1 280 ? 13.617  25.568 62.626  1.00 27.45  ? 280 VAL A CG1 1 
ATOM   2367 C CG2 . VAL A 1 280 ? 11.386  26.195 61.690  1.00 27.75  ? 280 VAL A CG2 1 
ATOM   2368 N N   . ILE A 1 281 ? 13.609  22.153 60.858  1.00 23.10  ? 281 ILE A N   1 
ATOM   2369 C CA  . ILE A 1 281 ? 14.673  21.151 60.930  1.00 21.36  ? 281 ILE A CA  1 
ATOM   2370 C C   . ILE A 1 281 ? 15.371  21.034 59.592  1.00 26.40  ? 281 ILE A C   1 
ATOM   2371 O O   . ILE A 1 281 ? 16.611  20.993 59.513  1.00 25.43  ? 281 ILE A O   1 
ATOM   2372 C CB  . ILE A 1 281 ? 14.126  19.780 61.376  1.00 20.48  ? 281 ILE A CB  1 
ATOM   2373 C CG1 . ILE A 1 281 ? 13.324  19.894 62.673  1.00 28.27  ? 281 ILE A CG1 1 
ATOM   2374 C CG2 . ILE A 1 281 ? 15.276  18.787 61.507  1.00 17.63  ? 281 ILE A CG2 1 
ATOM   2375 C CD1 . ILE A 1 281 ? 13.960  20.767 63.715  1.00 31.54  ? 281 ILE A CD1 1 
ATOM   2376 N N   . LEU A 1 282 ? 14.586  20.977 58.518  1.00 23.95  ? 282 LEU A N   1 
ATOM   2377 C CA  . LEU A 1 282 ? 15.155  20.933 57.180  1.00 27.24  ? 282 LEU A CA  1 
ATOM   2378 C C   . LEU A 1 282 ? 16.070  22.126 56.937  1.00 26.55  ? 282 LEU A C   1 
ATOM   2379 O O   . LEU A 1 282 ? 17.221  21.961 56.523  1.00 24.85  ? 282 LEU A O   1 
ATOM   2380 C CB  . LEU A 1 282 ? 14.037  20.884 56.138  1.00 28.35  ? 282 LEU A CB  1 
ATOM   2381 C CG  . LEU A 1 282 ? 14.489  20.601 54.700  1.00 30.50  ? 282 LEU A CG  1 
ATOM   2382 C CD1 . LEU A 1 282 ? 15.379  19.379 54.663  1.00 27.74  ? 282 LEU A CD1 1 
ATOM   2383 C CD2 . LEU A 1 282 ? 13.304  20.423 53.754  1.00 29.36  ? 282 LEU A CD2 1 
ATOM   2384 N N   . LYS A 1 283 ? 15.581  23.342 57.197  1.00 24.67  ? 283 LYS A N   1 
ATOM   2385 C CA  . LYS A 1 283 ? 16.402  24.513 56.903  1.00 31.07  ? 283 LYS A CA  1 
ATOM   2386 C C   . LYS A 1 283 ? 17.636  24.585 57.792  1.00 22.12  ? 283 LYS A C   1 
ATOM   2387 O O   . LYS A 1 283 ? 18.682  25.087 57.358  1.00 26.33  ? 283 LYS A O   1 
ATOM   2388 C CB  . LYS A 1 283 ? 15.567  25.788 57.029  1.00 42.07  ? 283 LYS A CB  1 
ATOM   2389 C CG  . LYS A 1 283 ? 14.317  25.758 56.149  1.00 52.94  ? 283 LYS A CG  1 
ATOM   2390 C CD  . LYS A 1 283 ? 14.692  25.664 54.665  1.00 59.79  ? 283 LYS A CD  1 
ATOM   2391 C CE  . LYS A 1 283 ? 13.499  25.336 53.790  1.00 59.29  ? 283 LYS A CE  1 
ATOM   2392 N NZ  . LYS A 1 283 ? 12.410  24.752 54.588  1.00 60.06  ? 283 LYS A NZ  1 
ATOM   2393 N N   . ASN A 1 284 ? 17.562  24.075 59.021  1.00 19.82  ? 284 ASN A N   1 
ATOM   2394 C CA  . ASN A 1 284 ? 18.755  23.998 59.855  1.00 22.91  ? 284 ASN A CA  1 
ATOM   2395 C C   . ASN A 1 284 ? 19.741  22.938 59.377  1.00 24.10  ? 284 ASN A C   1 
ATOM   2396 O O   . ASN A 1 284 ? 20.926  23.015 59.718  1.00 21.69  ? 284 ASN A O   1 
ATOM   2397 C CB  . ASN A 1 284 ? 18.367  23.705 61.301  1.00 29.39  ? 284 ASN A CB  1 
ATOM   2398 C CG  . ASN A 1 284 ? 17.761  24.911 61.998  1.00 31.37  ? 284 ASN A CG  1 
ATOM   2399 O OD1 . ASN A 1 284 ? 17.697  26.007 61.435  1.00 30.31  ? 284 ASN A OD1 1 
ATOM   2400 N ND2 . ASN A 1 284 ? 17.298  24.712 63.225  1.00 28.32  ? 284 ASN A ND2 1 
ATOM   2401 N N   . SER A 1 285 ? 19.292  21.953 58.603  1.00 22.76  ? 285 SER A N   1 
ATOM   2402 C CA  . SER A 1 285 ? 20.110  20.784 58.295  1.00 24.79  ? 285 SER A CA  1 
ATOM   2403 C C   . SER A 1 285 ? 20.643  20.753 56.873  1.00 29.16  ? 285 SER A C   1 
ATOM   2404 O O   . SER A 1 285 ? 21.668  20.109 56.631  1.00 31.51  ? 285 SER A O   1 
ATOM   2405 C CB  . SER A 1 285 ? 19.311  19.496 58.527  1.00 24.55  ? 285 SER A CB  1 
ATOM   2406 O OG  . SER A 1 285 ? 18.659  19.488 59.788  1.00 27.03  ? 285 SER A OG  1 
ATOM   2407 N N   . VAL A 1 286 ? 19.963  21.391 55.921  1.00 25.96  ? 286 VAL A N   1 
ATOM   2408 C CA  . VAL A 1 286 ? 20.362  21.377 54.516  1.00 30.59  ? 286 VAL A CA  1 
ATOM   2409 C C   . VAL A 1 286 ? 20.414  22.816 54.019  1.00 36.35  ? 286 VAL A C   1 
ATOM   2410 O O   . VAL A 1 286 ? 19.490  23.601 54.266  1.00 36.49  ? 286 VAL A O   1 
ATOM   2411 C CB  . VAL A 1 286 ? 19.397  20.538 53.647  1.00 29.14  ? 286 VAL A CB  1 
ATOM   2412 C CG1 . VAL A 1 286 ? 20.001  20.293 52.264  1.00 33.13  ? 286 VAL A CG1 1 
ATOM   2413 C CG2 . VAL A 1 286 ? 19.050  19.219 54.332  1.00 32.67  ? 286 VAL A CG2 1 
ATOM   2414 N N   . GLU A 1 287 ? 21.496  23.162 53.308  1.00 30.76  ? 287 GLU A N   1 
ATOM   2415 C CA  . GLU A 1 287 ? 21.685  24.541 52.865  1.00 30.49  ? 287 GLU A CA  1 
ATOM   2416 C C   . GLU A 1 287 ? 20.513  25.025 52.017  1.00 33.38  ? 287 GLU A C   1 
ATOM   2417 O O   . GLU A 1 287 ? 19.918  26.073 52.299  1.00 35.41  ? 287 GLU A O   1 
ATOM   2418 C CB  . GLU A 1 287 ? 22.999  24.667 52.096  1.00 31.00  ? 287 GLU A CB  1 
ATOM   2419 C CG  . GLU A 1 287 ? 24.177  24.864 53.008  1.00 35.76  ? 287 GLU A CG  1 
ATOM   2420 C CD  . GLU A 1 287 ? 25.488  25.045 52.267  1.00 44.69  ? 287 GLU A CD  1 
ATOM   2421 O OE1 . GLU A 1 287 ? 25.488  25.053 51.012  1.00 43.68  ? 287 GLU A OE1 1 
ATOM   2422 O OE2 . GLU A 1 287 ? 26.520  25.180 52.955  1.00 44.20  ? 287 GLU A OE2 1 
ATOM   2423 N N   . ARG A 1 288 ? 20.165  24.277 50.974  1.00 30.26  ? 288 ARG A N   1 
ATOM   2424 C CA  . ARG A 1 288 ? 19.049  24.623 50.097  1.00 29.15  ? 288 ARG A CA  1 
ATOM   2425 C C   . ARG A 1 288 ? 18.185  23.385 49.954  1.00 26.86  ? 288 ARG A C   1 
ATOM   2426 O O   . ARG A 1 288 ? 18.630  22.383 49.386  1.00 33.67  ? 288 ARG A O   1 
ATOM   2427 C CB  . ARG A 1 288 ? 19.539  25.104 48.730  1.00 33.99  ? 288 ARG A CB  1 
ATOM   2428 C CG  . ARG A 1 288 ? 18.420  25.509 47.794  1.00 32.67  ? 288 ARG A CG  1 
ATOM   2429 C CD  . ARG A 1 288 ? 18.566  24.840 46.442  1.00 34.09  ? 288 ARG A CD  1 
ATOM   2430 N NE  . ARG A 1 288 ? 19.827  25.176 45.810  1.00 40.51  ? 288 ARG A NE  1 
ATOM   2431 C CZ  . ARG A 1 288 ? 20.531  24.342 45.056  1.00 34.28  ? 288 ARG A CZ  1 
ATOM   2432 N NH1 . ARG A 1 288 ? 21.670  24.742 44.525  1.00 25.01  ? 288 ARG A NH1 1 
ATOM   2433 N NH2 . ARG A 1 288 ? 20.097  23.108 44.843  1.00 38.25  ? 288 ARG A NH2 1 
ATOM   2434 N N   . ALA A 1 289 ? 16.956  23.444 50.460  1.00 28.83  ? 289 ALA A N   1 
ATOM   2435 C CA  . ALA A 1 289 ? 16.129  22.247 50.508  1.00 29.53  ? 289 ALA A CA  1 
ATOM   2436 C C   . ALA A 1 289 ? 14.656  22.606 50.404  1.00 28.30  ? 289 ALA A C   1 
ATOM   2437 O O   . ALA A 1 289 ? 14.157  23.454 51.149  1.00 31.45  ? 289 ALA A O   1 
ATOM   2438 C CB  . ALA A 1 289 ? 16.393  21.456 51.793  1.00 36.43  ? 289 ALA A CB  1 
ATOM   2439 N N   . SER A 1 290 ? 13.972  21.953 49.478  1.00 27.03  ? 290 SER A N   1 
ATOM   2440 C CA  . SER A 1 290 ? 12.539  22.171 49.384  1.00 29.29  ? 290 SER A CA  1 
ATOM   2441 C C   . SER A 1 290 ? 11.797  21.163 50.258  1.00 29.20  ? 290 SER A C   1 
ATOM   2442 O O   . SER A 1 290 ? 12.155  19.975 50.286  1.00 24.88  ? 290 SER A O   1 
ATOM   2443 C CB  . SER A 1 290 ? 12.071  22.037 47.941  1.00 27.21  ? 290 SER A CB  1 
ATOM   2444 O OG  . SER A 1 290 ? 10.665  21.931 47.873  1.00 25.41  ? 290 SER A OG  1 
ATOM   2445 N N   . PRO A 1 291 ? 10.757  21.604 50.965  1.00 30.03  ? 291 PRO A N   1 
ATOM   2446 C CA  . PRO A 1 291 ? 9.966   20.683 51.781  1.00 24.48  ? 291 PRO A CA  1 
ATOM   2447 C C   . PRO A 1 291 ? 8.907   19.915 51.006  1.00 21.14  ? 291 PRO A C   1 
ATOM   2448 O O   . PRO A 1 291 ? 8.060   19.265 51.628  1.00 25.76  ? 291 PRO A O   1 
ATOM   2449 C CB  . PRO A 1 291 ? 9.317   21.638 52.792  1.00 27.19  ? 291 PRO A CB  1 
ATOM   2450 C CG  . PRO A 1 291 ? 9.039   22.855 51.966  1.00 22.75  ? 291 PRO A CG  1 
ATOM   2451 C CD  . PRO A 1 291 ? 10.186  22.960 50.975  1.00 22.37  ? 291 PRO A CD  1 
ATOM   2452 N N   . TYR A 1 292 ? 8.906   19.992 49.673  1.00 20.21  ? 292 TYR A N   1 
ATOM   2453 C CA  . TYR A 1 292 ? 7.881   19.343 48.859  1.00 20.98  ? 292 TYR A CA  1 
ATOM   2454 C C   . TYR A 1 292 ? 8.354   18.026 48.261  1.00 20.65  ? 292 TYR A C   1 
ATOM   2455 O O   . TYR A 1 292 ? 7.660   17.450 47.412  1.00 24.53  ? 292 TYR A O   1 
ATOM   2456 C CB  . TYR A 1 292 ? 7.399   20.293 47.752  1.00 23.16  ? 292 TYR A CB  1 
ATOM   2457 C CG  . TYR A 1 292 ? 6.895   21.613 48.296  1.00 27.92  ? 292 TYR A CG  1 
ATOM   2458 C CD1 . TYR A 1 292 ? 6.093   21.649 49.424  1.00 21.49  ? 292 TYR A CD1 1 
ATOM   2459 C CD2 . TYR A 1 292 ? 7.234   22.814 47.694  1.00 31.25  ? 292 TYR A CD2 1 
ATOM   2460 C CE1 . TYR A 1 292 ? 5.643   22.838 49.939  1.00 29.92  ? 292 TYR A CE1 1 
ATOM   2461 C CE2 . TYR A 1 292 ? 6.776   24.020 48.202  1.00 32.85  ? 292 TYR A CE2 1 
ATOM   2462 C CZ  . TYR A 1 292 ? 5.985   24.022 49.328  1.00 30.07  ? 292 TYR A CZ  1 
ATOM   2463 O OH  . TYR A 1 292 ? 5.529   25.208 49.854  1.00 32.88  ? 292 TYR A OH  1 
ATOM   2464 N N   . LEU A 1 293 ? 9.508   17.534 48.695  1.00 23.32  ? 293 LEU A N   1 
ATOM   2465 C CA  . LEU A 1 293 ? 10.097  16.289 48.235  1.00 23.43  ? 293 LEU A CA  1 
ATOM   2466 C C   . LEU A 1 293 ? 9.958   15.220 49.317  1.00 23.45  ? 293 LEU A C   1 
ATOM   2467 O O   . LEU A 1 293 ? 9.799   15.523 50.505  1.00 23.36  ? 293 LEU A O   1 
ATOM   2468 C CB  . LEU A 1 293 ? 11.591  16.491 47.898  1.00 23.05  ? 293 LEU A CB  1 
ATOM   2469 C CG  . LEU A 1 293 ? 12.040  17.234 46.634  1.00 33.28  ? 293 LEU A CG  1 
ATOM   2470 C CD1 . LEU A 1 293 ? 11.646  18.695 46.647  1.00 37.32  ? 293 LEU A CD1 1 
ATOM   2471 C CD2 . LEU A 1 293 ? 13.555  17.100 46.458  1.00 34.03  ? 293 LEU A CD2 1 
ATOM   2472 N N   . ARG A 1 294 ? 10.016  13.954 48.902  1.00 20.71  ? 294 ARG A N   1 
ATOM   2473 C CA  . ARG A 1 294 ? 10.179  12.866 49.857  1.00 20.94  ? 294 ARG A CA  1 
ATOM   2474 C C   . ARG A 1 294 ? 11.670  12.686 50.125  1.00 21.90  ? 294 ARG A C   1 
ATOM   2475 O O   . ARG A 1 294 ? 12.474  12.602 49.189  1.00 21.64  ? 294 ARG A O   1 
ATOM   2476 C CB  . ARG A 1 294 ? 9.547   11.565 49.345  1.00 21.79  ? 294 ARG A CB  1 
ATOM   2477 C CG  . ARG A 1 294 ? 9.680   10.384 50.321  1.00 24.96  ? 294 ARG A CG  1 
ATOM   2478 C CD  . ARG A 1 294 ? 8.814   9.180  49.912  1.00 23.04  ? 294 ARG A CD  1 
ATOM   2479 N NE  . ARG A 1 294 ? 9.242   8.628  48.633  1.00 22.51  ? 294 ARG A NE  1 
ATOM   2480 C CZ  . ARG A 1 294 ? 8.448   8.427  47.582  1.00 27.81  ? 294 ARG A CZ  1 
ATOM   2481 N NH1 . ARG A 1 294 ? 7.149   8.715  47.645  1.00 24.88  ? 294 ARG A NH1 1 
ATOM   2482 N NH2 . ARG A 1 294 ? 8.961   7.929  46.459  1.00 24.86  ? 294 ARG A NH2 1 
ATOM   2483 N N   . TYR A 1 295 ? 12.048  12.678 51.396  1.00 24.93  ? 295 TYR A N   1 
ATOM   2484 C CA  . TYR A 1 295 ? 13.455  12.569 51.755  1.00 25.95  ? 295 TYR A CA  1 
ATOM   2485 C C   . TYR A 1 295 ? 13.758  11.191 52.324  1.00 23.74  ? 295 TYR A C   1 
ATOM   2486 O O   . TYR A 1 295 ? 12.932  10.577 53.010  1.00 23.57  ? 295 TYR A O   1 
ATOM   2487 C CB  . TYR A 1 295 ? 13.878  13.636 52.768  1.00 24.92  ? 295 TYR A CB  1 
ATOM   2488 C CG  . TYR A 1 295 ? 13.997  15.020 52.162  1.00 24.50  ? 295 TYR A CG  1 
ATOM   2489 C CD1 . TYR A 1 295 ? 12.874  15.798 51.974  1.00 19.73  ? 295 TYR A CD1 1 
ATOM   2490 C CD2 . TYR A 1 295 ? 15.232  15.540 51.762  1.00 24.72  ? 295 TYR A CD2 1 
ATOM   2491 C CE1 . TYR A 1 295 ? 12.956  17.064 51.406  1.00 23.10  ? 295 TYR A CE1 1 
ATOM   2492 C CE2 . TYR A 1 295 ? 15.323  16.819 51.195  1.00 19.21  ? 295 TYR A CE2 1 
ATOM   2493 C CZ  . TYR A 1 295 ? 14.179  17.571 51.023  1.00 20.28  ? 295 TYR A CZ  1 
ATOM   2494 O OH  . TYR A 1 295 ? 14.240  18.836 50.465  1.00 24.92  ? 295 TYR A OH  1 
ATOM   2495 N N   . TYR A 1 296 ? 14.974  10.728 52.038  1.00 17.44  ? 296 TYR A N   1 
ATOM   2496 C CA  . TYR A 1 296 ? 15.486  9.461  52.544  1.00 21.10  ? 296 TYR A CA  1 
ATOM   2497 C C   . TYR A 1 296 ? 16.679  9.760  53.447  1.00 27.38  ? 296 TYR A C   1 
ATOM   2498 O O   . TYR A 1 296 ? 17.727  10.212 52.969  1.00 26.47  ? 296 TYR A O   1 
ATOM   2499 C CB  . TYR A 1 296 ? 15.883  8.531  51.394  1.00 24.88  ? 296 TYR A CB  1 
ATOM   2500 C CG  . TYR A 1 296 ? 14.789  8.251  50.384  1.00 33.57  ? 296 TYR A CG  1 
ATOM   2501 C CD1 . TYR A 1 296 ? 13.472  8.045  50.792  1.00 35.12  ? 296 TYR A CD1 1 
ATOM   2502 C CD2 . TYR A 1 296 ? 15.069  8.155  49.019  1.00 38.53  ? 296 TYR A CD2 1 
ATOM   2503 C CE1 . TYR A 1 296 ? 12.477  7.740  49.879  1.00 35.74  ? 296 TYR A CE1 1 
ATOM   2504 C CE2 . TYR A 1 296 ? 14.073  7.876  48.098  1.00 34.84  ? 296 TYR A CE2 1 
ATOM   2505 C CZ  . TYR A 1 296 ? 12.783  7.674  48.541  1.00 34.30  ? 296 TYR A CZ  1 
ATOM   2506 O OH  . TYR A 1 296 ? 11.786  7.397  47.634  1.00 33.59  ? 296 TYR A OH  1 
ATOM   2507 N N   . PHE A 1 297 ? 16.527  9.513  54.747  1.00 23.30  ? 297 PHE A N   1 
ATOM   2508 C CA  . PHE A 1 297 ? 17.639  9.701  55.677  1.00 22.63  ? 297 PHE A CA  1 
ATOM   2509 C C   . PHE A 1 297 ? 18.581  8.509  55.536  1.00 23.85  ? 297 PHE A C   1 
ATOM   2510 O O   . PHE A 1 297 ? 18.246  7.386  55.938  1.00 23.94  ? 297 PHE A O   1 
ATOM   2511 C CB  . PHE A 1 297 ? 17.131  9.867  57.110  1.00 25.61  ? 297 PHE A CB  1 
ATOM   2512 C CG  . PHE A 1 297 ? 18.229  9.961  58.149  1.00 25.75  ? 297 PHE A CG  1 
ATOM   2513 C CD1 . PHE A 1 297 ? 18.925  11.153 58.344  1.00 27.70  ? 297 PHE A CD1 1 
ATOM   2514 C CD2 . PHE A 1 297 ? 18.568  8.859  58.924  1.00 21.87  ? 297 PHE A CD2 1 
ATOM   2515 C CE1 . PHE A 1 297 ? 19.946  11.240 59.305  1.00 23.42  ? 297 PHE A CE1 1 
ATOM   2516 C CE2 . PHE A 1 297 ? 19.588  8.939  59.877  1.00 20.00  ? 297 PHE A CE2 1 
ATOM   2517 C CZ  . PHE A 1 297 ? 20.275  10.132 60.065  1.00 19.72  ? 297 PHE A CZ  1 
ATOM   2518 N N   . ARG A 1 298 ? 19.738  8.742  54.896  1.00 23.82  ? 298 ARG A N   1 
ATOM   2519 C CA  . ARG A 1 298 ? 20.795  7.741  54.728  1.00 23.37  ? 298 ARG A CA  1 
ATOM   2520 C C   . ARG A 1 298 ? 20.310  6.494  53.990  1.00 26.05  ? 298 ARG A C   1 
ATOM   2521 O O   . ARG A 1 298 ? 20.923  5.439  54.092  1.00 24.80  ? 298 ARG A O   1 
ATOM   2522 C CB  . ARG A 1 298 ? 21.422  7.361  56.080  1.00 23.81  ? 298 ARG A CB  1 
ATOM   2523 C CG  . ARG A 1 298 ? 22.235  8.503  56.709  1.00 23.07  ? 298 ARG A CG  1 
ATOM   2524 C CD  . ARG A 1 298 ? 22.718  8.258  58.155  1.00 28.10  ? 298 ARG A CD  1 
ATOM   2525 N NE  . ARG A 1 298 ? 23.202  9.515  58.741  1.00 27.06  ? 298 ARG A NE  1 
ATOM   2526 C CZ  . ARG A 1 298 ? 23.648  9.685  59.988  1.00 27.91  ? 298 ARG A CZ  1 
ATOM   2527 N NH1 . ARG A 1 298 ? 23.707  8.672  60.842  1.00 28.64  ? 298 ARG A NH1 1 
ATOM   2528 N NH2 . ARG A 1 298 ? 24.040  10.897 60.383  1.00 27.13  ? 298 ARG A NH2 1 
ATOM   2529 N N   . GLU A 1 299 ? 19.222  6.617  53.221  1.00 31.19  ? 299 GLU A N   1 
ATOM   2530 C CA  . GLU A 1 299 ? 18.556  5.485  52.551  1.00 25.41  ? 299 GLU A CA  1 
ATOM   2531 C C   . GLU A 1 299 ? 18.037  4.460  53.557  1.00 24.48  ? 299 GLU A C   1 
ATOM   2532 O O   . GLU A 1 299 ? 17.827  3.295  53.216  1.00 25.72  ? 299 GLU A O   1 
ATOM   2533 C CB  . GLU A 1 299 ? 19.467  4.797  51.518  1.00 29.60  ? 299 GLU A CB  1 
ATOM   2534 C CG  . GLU A 1 299 ? 19.961  5.700  50.397  1.00 32.03  ? 299 GLU A CG  1 
ATOM   2535 C CD  . GLU A 1 299 ? 18.904  5.979  49.333  1.00 34.89  ? 299 GLU A CD  1 
ATOM   2536 O OE1 . GLU A 1 299 ? 17.695  5.975  49.649  1.00 34.87  ? 299 GLU A OE1 1 
ATOM   2537 O OE2 . GLU A 1 299 ? 19.286  6.205  48.165  1.00 40.89  ? 299 GLU A OE2 1 
ATOM   2538 N N   . LEU A 1 300 ? 17.817  4.892  54.802  1.00 19.46  ? 300 LEU A N   1 
ATOM   2539 C CA  . LEU A 1 300 ? 17.313  4.060  55.889  1.00 24.46  ? 300 LEU A CA  1 
ATOM   2540 C C   . LEU A 1 300 ? 15.813  4.220  56.124  1.00 29.26  ? 300 LEU A C   1 
ATOM   2541 O O   . LEU A 1 300 ? 15.122  3.231  56.403  1.00 28.90  ? 300 LEU A O   1 
ATOM   2542 C CB  . LEU A 1 300 ? 18.053  4.387  57.195  1.00 26.34  ? 300 LEU A CB  1 
ATOM   2543 C CG  . LEU A 1 300 ? 19.430  3.786  57.542  1.00 36.53  ? 300 LEU A CG  1 
ATOM   2544 C CD1 . LEU A 1 300 ? 20.322  3.636  56.342  1.00 47.00  ? 300 LEU A CD1 1 
ATOM   2545 C CD2 . LEU A 1 300 ? 20.137  4.606  58.621  1.00 32.18  ? 300 LEU A CD2 1 
ATOM   2546 N N   . ILE A 1 301 ? 15.299  5.444  56.055  1.00 18.26  ? 301 ILE A N   1 
ATOM   2547 C CA  . ILE A 1 301 ? 13.931  5.725  56.481  1.00 19.73  ? 301 ILE A CA  1 
ATOM   2548 C C   . ILE A 1 301 ? 13.472  6.971  55.734  1.00 24.27  ? 301 ILE A C   1 
ATOM   2549 O O   . ILE A 1 301 ? 14.264  7.881  55.475  1.00 24.21  ? 301 ILE A O   1 
ATOM   2550 C CB  . ILE A 1 301 ? 13.851  5.899  58.016  1.00 26.92  ? 301 ILE A CB  1 
ATOM   2551 C CG1 . ILE A 1 301 ? 12.419  6.186  58.475  1.00 24.18  ? 301 ILE A CG1 1 
ATOM   2552 C CG2 . ILE A 1 301 ? 14.794  7.004  58.494  1.00 27.57  ? 301 ILE A CG2 1 
ATOM   2553 C CD1 . ILE A 1 301 ? 12.269  6.208  59.990  1.00 20.32  ? 301 ILE A CD1 1 
ATOM   2554 N N   . SER A 1 302 ? 12.198  6.995  55.358  1.00 22.50  ? 302 SER A N   1 
ATOM   2555 C CA  . SER A 1 302 ? 11.673  8.123  54.599  1.00 23.47  ? 302 SER A CA  1 
ATOM   2556 C C   . SER A 1 302 ? 11.226  9.236  55.534  1.00 23.18  ? 302 SER A C   1 
ATOM   2557 O O   . SER A 1 302 ? 10.643  8.986  56.594  1.00 24.07  ? 302 SER A O   1 
ATOM   2558 C CB  . SER A 1 302 ? 10.512  7.672  53.714  1.00 28.11  ? 302 SER A CB  1 
ATOM   2559 O OG  . SER A 1 302 ? 10.939  6.624  52.861  1.00 30.01  ? 302 SER A OG  1 
ATOM   2560 N N   . VAL A 1 303 ? 11.495  10.471 55.136  1.00 20.11  ? 303 VAL A N   1 
ATOM   2561 C CA  . VAL A 1 303 ? 11.157  11.636 55.948  1.00 23.28  ? 303 VAL A CA  1 
ATOM   2562 C C   . VAL A 1 303 ? 10.459  12.668 55.075  1.00 24.40  ? 303 VAL A C   1 
ATOM   2563 O O   . VAL A 1 303 ? 10.959  13.024 54.001  1.00 26.87  ? 303 VAL A O   1 
ATOM   2564 C CB  . VAL A 1 303 ? 12.404  12.255 56.611  1.00 24.63  ? 303 VAL A CB  1 
ATOM   2565 C CG1 . VAL A 1 303 ? 12.000  13.440 57.493  1.00 24.74  ? 303 VAL A CG1 1 
ATOM   2566 C CG2 . VAL A 1 303 ? 13.152  11.211 57.418  1.00 21.25  ? 303 VAL A CG2 1 
ATOM   2567 N N   . PHE A 1 304 ? 9.308   13.150 55.536  1.00 17.64  ? 304 PHE A N   1 
ATOM   2568 C CA  . PHE A 1 304 ? 8.702   14.348 54.985  1.00 20.29  ? 304 PHE A CA  1 
ATOM   2569 C C   . PHE A 1 304 ? 8.846   15.487 55.990  1.00 23.59  ? 304 PHE A C   1 
ATOM   2570 O O   . PHE A 1 304 ? 8.759   15.281 57.204  1.00 23.65  ? 304 PHE A O   1 
ATOM   2571 C CB  . PHE A 1 304 ? 7.232   14.122 54.656  1.00 21.78  ? 304 PHE A CB  1 
ATOM   2572 C CG  . PHE A 1 304 ? 7.009   13.318 53.404  1.00 21.05  ? 304 PHE A CG  1 
ATOM   2573 C CD1 . PHE A 1 304 ? 7.062   13.930 52.151  1.00 20.31  ? 304 PHE A CD1 1 
ATOM   2574 C CD2 . PHE A 1 304 ? 6.741   11.963 53.479  1.00 17.78  ? 304 PHE A CD2 1 
ATOM   2575 C CE1 . PHE A 1 304 ? 6.845   13.197 50.999  1.00 21.49  ? 304 PHE A CE1 1 
ATOM   2576 C CE2 . PHE A 1 304 ? 6.509   11.219 52.319  1.00 18.43  ? 304 PHE A CE2 1 
ATOM   2577 C CZ  . PHE A 1 304 ? 6.569   11.841 51.081  1.00 20.14  ? 304 PHE A CZ  1 
ATOM   2578 N N   . PHE A 1 305 ? 9.079   16.688 55.487  1.00 17.25  ? 305 PHE A N   1 
ATOM   2579 C CA  . PHE A 1 305 ? 9.125   17.875 56.327  1.00 14.21  ? 305 PHE A CA  1 
ATOM   2580 C C   . PHE A 1 305 ? 7.839   18.642 56.087  1.00 19.89  ? 305 PHE A C   1 
ATOM   2581 O O   . PHE A 1 305 ? 7.541   19.022 54.948  1.00 22.20  ? 305 PHE A O   1 
ATOM   2582 C CB  . PHE A 1 305 ? 10.365  18.710 56.016  1.00 15.09  ? 305 PHE A CB  1 
ATOM   2583 C CG  . PHE A 1 305 ? 11.650  17.946 56.218  1.00 22.95  ? 305 PHE A CG  1 
ATOM   2584 C CD1 . PHE A 1 305 ? 12.133  17.095 55.227  1.00 29.22  ? 305 PHE A CD1 1 
ATOM   2585 C CD2 . PHE A 1 305 ? 12.350  18.040 57.408  1.00 22.52  ? 305 PHE A CD2 1 
ATOM   2586 C CE1 . PHE A 1 305 ? 13.301  16.369 55.417  1.00 26.14  ? 305 PHE A CE1 1 
ATOM   2587 C CE2 . PHE A 1 305 ? 13.532  17.327 57.597  1.00 22.33  ? 305 PHE A CE2 1 
ATOM   2588 C CZ  . PHE A 1 305 ? 13.997  16.486 56.604  1.00 25.87  ? 305 PHE A CZ  1 
ATOM   2589 N N   . ARG A 1 306 ? 7.056   18.827 57.144  1.00 21.03  ? 306 ARG A N   1 
ATOM   2590 C CA  . ARG A 1 306 ? 5.749   19.442 56.973  1.00 24.99  ? 306 ARG A CA  1 
ATOM   2591 C C   . ARG A 1 306 ? 5.892   20.881 56.478  1.00 24.98  ? 306 ARG A C   1 
ATOM   2592 O O   . ARG A 1 306 ? 6.910   21.549 56.704  1.00 23.08  ? 306 ARG A O   1 
ATOM   2593 C CB  . ARG A 1 306 ? 4.981   19.414 58.291  1.00 26.72  ? 306 ARG A CB  1 
ATOM   2594 C CG  . ARG A 1 306 ? 5.564   20.325 59.330  1.00 25.41  ? 306 ARG A CG  1 
ATOM   2595 C CD  . ARG A 1 306 ? 4.703   20.476 60.568  1.00 29.09  ? 306 ARG A CD  1 
ATOM   2596 N NE  . ARG A 1 306 ? 5.193   21.638 61.289  1.00 25.98  ? 306 ARG A NE  1 
ATOM   2597 C CZ  . ARG A 1 306 ? 4.499   22.379 62.144  1.00 23.01  ? 306 ARG A CZ  1 
ATOM   2598 N NH1 . ARG A 1 306 ? 3.229   22.111 62.452  1.00 18.71  ? 306 ARG A NH1 1 
ATOM   2599 N NH2 . ARG A 1 306 ? 5.108   23.412 62.687  1.00 21.84  ? 306 ARG A NH2 1 
ATOM   2600 N N   . ASP A 1 307 ? 4.860   21.351 55.775  1.00 20.94  ? 307 ASP A N   1 
ATOM   2601 C CA  . ASP A 1 307 ? 4.744   22.762 55.412  1.00 19.02  ? 307 ASP A CA  1 
ATOM   2602 C C   . ASP A 1 307 ? 4.371   23.540 56.664  1.00 17.98  ? 307 ASP A C   1 
ATOM   2603 O O   . ASP A 1 307 ? 3.211   23.540 57.082  1.00 18.79  ? 307 ASP A O   1 
ATOM   2604 C CB  . ASP A 1 307 ? 3.699   22.952 54.314  1.00 16.56  ? 307 ASP A CB  1 
ATOM   2605 C CG  . ASP A 1 307 ? 3.767   24.331 53.672  1.00 29.59  ? 307 ASP A CG  1 
ATOM   2606 O OD1 . ASP A 1 307 ? 3.759   25.345 54.407  1.00 30.76  ? 307 ASP A OD1 1 
ATOM   2607 O OD2 . ASP A 1 307 ? 3.829   24.400 52.429  1.00 33.91  ? 307 ASP A OD2 1 
ATOM   2608 N N   . LYS A 1 308 ? 5.352   24.232 57.258  1.00 20.08  ? 308 LYS A N   1 
ATOM   2609 C CA  . LYS A 1 308 ? 5.128   24.929 58.526  1.00 22.35  ? 308 LYS A CA  1 
ATOM   2610 C C   . LYS A 1 308 ? 4.075   26.031 58.397  1.00 22.38  ? 308 LYS A C   1 
ATOM   2611 O O   . LYS A 1 308 ? 3.241   26.215 59.294  1.00 19.07  ? 308 LYS A O   1 
ATOM   2612 C CB  . LYS A 1 308 ? 6.452   25.518 59.030  1.00 24.02  ? 308 LYS A CB  1 
ATOM   2613 C CG  . LYS A 1 308 ? 6.381   26.396 60.299  1.00 21.41  ? 308 LYS A CG  1 
ATOM   2614 C CD  . LYS A 1 308 ? 7.803   26.835 60.697  1.00 26.29  ? 308 LYS A CD  1 
ATOM   2615 C CE  . LYS A 1 308 ? 7.906   27.508 62.064  1.00 30.13  ? 308 LYS A CE  1 
ATOM   2616 N NZ  . LYS A 1 308 ? 6.620   27.789 62.735  1.00 28.08  ? 308 LYS A NZ  1 
ATOM   2617 N N   . THR A 1 309 ? 4.120   26.804 57.309  1.00 25.37  ? 309 THR A N   1 
ATOM   2618 C CA  . THR A 1 309 ? 3.192   27.924 57.162  1.00 22.89  ? 309 THR A CA  1 
ATOM   2619 C C   . THR A 1 309 ? 1.747   27.443 57.133  1.00 21.27  ? 309 THR A C   1 
ATOM   2620 O O   . THR A 1 309 ? 0.909   27.910 57.911  1.00 21.90  ? 309 THR A O   1 
ATOM   2621 C CB  . THR A 1 309 ? 3.505   28.711 55.891  1.00 27.49  ? 309 THR A CB  1 
ATOM   2622 O OG1 . THR A 1 309 ? 4.867   29.157 55.924  1.00 29.84  ? 309 THR A OG1 1 
ATOM   2623 C CG2 . THR A 1 309 ? 2.583   29.917 55.776  1.00 22.72  ? 309 THR A CG2 1 
ATOM   2624 N N   . LEU A 1 310 ? 1.439   26.510 56.229  1.00 20.50  ? 310 LEU A N   1 
ATOM   2625 C CA  . LEU A 1 310 ? 0.081   25.988 56.115  1.00 20.03  ? 310 LEU A CA  1 
ATOM   2626 C C   . LEU A 1 310 ? -0.352  25.289 57.395  1.00 23.71  ? 310 LEU A C   1 
ATOM   2627 O O   . LEU A 1 310 ? -1.523  25.371 57.785  1.00 24.81  ? 310 LEU A O   1 
ATOM   2628 C CB  . LEU A 1 310 ? -0.011  25.026 54.929  1.00 22.12  ? 310 LEU A CB  1 
ATOM   2629 C CG  . LEU A 1 310 ? 0.237   25.634 53.542  1.00 27.43  ? 310 LEU A CG  1 
ATOM   2630 C CD1 . LEU A 1 310 ? 0.348   24.523 52.514  1.00 27.55  ? 310 LEU A CD1 1 
ATOM   2631 C CD2 . LEU A 1 310 ? -0.893  26.586 53.164  1.00 24.86  ? 310 LEU A CD2 1 
ATOM   2632 N N   . SER A 1 311 ? 0.568   24.560 58.043  1.00 19.11  ? 311 SER A N   1 
ATOM   2633 C CA  . SER A 1 311 ? 0.227   23.905 59.300  1.00 18.33  ? 311 SER A CA  1 
ATOM   2634 C C   . SER A 1 311 ? -0.084  24.934 60.376  1.00 20.72  ? 311 SER A C   1 
ATOM   2635 O O   . SER A 1 311 ? -1.056  24.783 61.126  1.00 19.75  ? 311 SER A O   1 
ATOM   2636 C CB  . SER A 1 311 ? 1.366   22.987 59.748  1.00 19.04  ? 311 SER A CB  1 
ATOM   2637 O OG  . SER A 1 311 ? 1.692   22.044 58.746  1.00 21.87  ? 311 SER A OG  1 
ATOM   2638 N N   . ASP A 1 312 ? 0.719   26.002 60.444  1.00 15.56  ? 312 ASP A N   1 
ATOM   2639 C CA  . ASP A 1 312 ? 0.485   27.068 61.414  1.00 20.23  ? 312 ASP A CA  1 
ATOM   2640 C C   . ASP A 1 312 ? -0.777  27.868 61.104  1.00 21.20  ? 312 ASP A C   1 
ATOM   2641 O O   . ASP A 1 312 ? -1.404  28.400 62.027  1.00 21.58  ? 312 ASP A O   1 
ATOM   2642 C CB  . ASP A 1 312 ? 1.677   28.032 61.460  1.00 22.04  ? 312 ASP A CB  1 
ATOM   2643 C CG  . ASP A 1 312 ? 2.860   27.490 62.243  1.00 29.65  ? 312 ASP A CG  1 
ATOM   2644 O OD1 . ASP A 1 312 ? 2.725   26.477 62.963  1.00 33.17  ? 312 ASP A OD1 1 
ATOM   2645 O OD2 . ASP A 1 312 ? 3.947   28.086 62.121  1.00 32.34  ? 312 ASP A OD2 1 
ATOM   2646 N N   . LEU A 1 313 ? -1.127  28.016 59.823  1.00 21.06  ? 313 LEU A N   1 
ATOM   2647 C CA  . LEU A 1 313 ? -2.322  28.774 59.473  1.00 16.59  ? 313 LEU A CA  1 
ATOM   2648 C C   . LEU A 1 313 ? -3.556  28.133 60.090  1.00 19.86  ? 313 LEU A C   1 
ATOM   2649 O O   . LEU A 1 313 ? -4.372  28.806 60.729  1.00 17.83  ? 313 LEU A O   1 
ATOM   2650 C CB  . LEU A 1 313 ? -2.453  28.882 57.951  1.00 15.15  ? 313 LEU A CB  1 
ATOM   2651 C CG  . LEU A 1 313 ? -1.472  29.917 57.374  1.00 22.49  ? 313 LEU A CG  1 
ATOM   2652 C CD1 . LEU A 1 313 ? -1.350  29.841 55.847  1.00 21.89  ? 313 LEU A CD1 1 
ATOM   2653 C CD2 . LEU A 1 313 ? -1.850  31.333 57.832  1.00 19.11  ? 313 LEU A CD2 1 
ATOM   2654 N N   . ILE A 1 314 ? -3.677  26.812 59.960  1.00 22.01  ? 314 ILE A N   1 
ATOM   2655 C CA  . ILE A 1 314 ? -4.824  26.127 60.540  1.00 23.22  ? 314 ILE A CA  1 
ATOM   2656 C C   . ILE A 1 314 ? -4.709  26.102 62.058  1.00 21.20  ? 314 ILE A C   1 
ATOM   2657 O O   . ILE A 1 314 ? -5.675  26.401 62.783  1.00 17.92  ? 314 ILE A O   1 
ATOM   2658 C CB  . ILE A 1 314 ? -4.928  24.714 59.939  1.00 18.91  ? 314 ILE A CB  1 
ATOM   2659 C CG1 . ILE A 1 314 ? -5.232  24.818 58.442  1.00 24.40  ? 314 ILE A CG1 1 
ATOM   2660 C CG2 . ILE A 1 314 ? -5.972  23.884 60.691  1.00 15.62  ? 314 ILE A CG2 1 
ATOM   2661 C CD1 . ILE A 1 314 ? -5.361  23.463 57.737  1.00 32.65  ? 314 ILE A CD1 1 
ATOM   2662 N N   . GLY A 1 315 ? -3.515  25.797 62.562  1.00 15.85  ? 315 GLY A N   1 
ATOM   2663 C CA  . GLY A 1 315 ? -3.346  25.599 63.987  1.00 19.66  ? 315 GLY A CA  1 
ATOM   2664 C C   . GLY A 1 315 ? -3.451  26.868 64.802  1.00 23.28  ? 315 GLY A C   1 
ATOM   2665 O O   . GLY A 1 315 ? -3.795  26.802 65.986  1.00 21.56  ? 315 GLY A O   1 
ATOM   2666 N N   . PHE A 1 316 ? -3.176  28.024 64.200  1.00 22.15  ? 316 PHE A N   1 
ATOM   2667 C CA  . PHE A 1 316 ? -3.066  29.239 65.001  1.00 20.14  ? 316 PHE A CA  1 
ATOM   2668 C C   . PHE A 1 316 ? -3.699  30.475 64.390  1.00 24.26  ? 316 PHE A C   1 
ATOM   2669 O O   . PHE A 1 316 ? -4.001  31.405 65.143  1.00 24.37  ? 316 PHE A O   1 
ATOM   2670 C CB  . PHE A 1 316 ? -1.593  29.550 65.290  1.00 24.57  ? 316 PHE A CB  1 
ATOM   2671 C CG  . PHE A 1 316 ? -0.901  28.508 66.109  1.00 31.30  ? 316 PHE A CG  1 
ATOM   2672 C CD1 . PHE A 1 316 ? -1.119  28.427 67.476  1.00 34.83  ? 316 PHE A CD1 1 
ATOM   2673 C CD2 . PHE A 1 316 ? -0.031  27.609 65.521  1.00 36.27  ? 316 PHE A CD2 1 
ATOM   2674 C CE1 . PHE A 1 316 ? -0.482  27.461 68.235  1.00 36.77  ? 316 PHE A CE1 1 
ATOM   2675 C CE2 . PHE A 1 316 ? 0.610   26.646 66.275  1.00 42.22  ? 316 PHE A CE2 1 
ATOM   2676 C CZ  . PHE A 1 316 ? 0.380   26.572 67.634  1.00 40.12  ? 316 PHE A CZ  1 
ATOM   2677 N N   . SER A 1 317 ? -3.881  30.551 63.071  1.00 20.06  ? 317 SER A N   1 
ATOM   2678 C CA  . SER A 1 317 ? -4.338  31.769 62.415  1.00 17.46  ? 317 SER A CA  1 
ATOM   2679 C C   . SER A 1 317 ? -5.829  31.764 62.105  1.00 18.99  ? 317 SER A C   1 
ATOM   2680 O O   . SER A 1 317 ? -6.514  32.737 62.406  1.00 18.80  ? 317 SER A O   1 
ATOM   2681 C CB  . SER A 1 317 ? -3.563  31.996 61.108  1.00 21.06  ? 317 SER A CB  1 
ATOM   2682 O OG  . SER A 1 317 ? -2.167  32.044 61.359  1.00 25.79  ? 317 SER A OG  1 
ATOM   2683 N N   . TYR A 1 318 ? -6.336  30.701 61.471  1.00 25.18  ? 318 TYR A N   1 
ATOM   2684 C CA  . TYR A 1 318 ? -7.647  30.772 60.833  1.00 26.94  ? 318 TYR A CA  1 
ATOM   2685 C C   . TYR A 1 318 ? -8.799  30.867 61.826  1.00 23.48  ? 318 TYR A C   1 
ATOM   2686 O O   . TYR A 1 318 ? -9.918  31.198 61.413  1.00 24.89  ? 318 TYR A O   1 
ATOM   2687 C CB  . TYR A 1 318 ? -7.849  29.562 59.918  1.00 17.63  ? 318 TYR A CB  1 
ATOM   2688 C CG  . TYR A 1 318 ? -7.064  29.645 58.620  1.00 18.66  ? 318 TYR A CG  1 
ATOM   2689 C CD1 . TYR A 1 318 ? -6.612  30.865 58.127  1.00 16.66  ? 318 TYR A CD1 1 
ATOM   2690 C CD2 . TYR A 1 318 ? -6.803  28.506 57.882  1.00 23.14  ? 318 TYR A CD2 1 
ATOM   2691 C CE1 . TYR A 1 318 ? -5.904  30.937 56.924  1.00 19.82  ? 318 TYR A CE1 1 
ATOM   2692 C CE2 . TYR A 1 318 ? -6.104  28.560 56.693  1.00 18.82  ? 318 TYR A CE2 1 
ATOM   2693 C CZ  . TYR A 1 318 ? -5.662  29.769 56.212  1.00 22.38  ? 318 TYR A CZ  1 
ATOM   2694 O OH  . TYR A 1 318 ? -4.965  29.790 55.015  1.00 21.12  ? 318 TYR A OH  1 
ATOM   2695 N N   . HIS A 1 319 ? -8.568  30.568 63.105  1.00 22.26  ? 319 HIS A N   1 
ATOM   2696 C CA  . HIS A 1 319 ? -9.594  30.843 64.103  1.00 20.06  ? 319 HIS A CA  1 
ATOM   2697 C C   . HIS A 1 319 ? -10.006 32.317 64.066  1.00 24.85  ? 319 HIS A C   1 
ATOM   2698 O O   . HIS A 1 319 ? -11.176 32.643 64.312  1.00 22.38  ? 319 HIS A O   1 
ATOM   2699 C CB  . HIS A 1 319 ? -9.097  30.454 65.495  1.00 13.58  ? 319 HIS A CB  1 
ATOM   2700 C CG  . HIS A 1 319 ? -8.161  31.457 66.092  1.00 22.84  ? 319 HIS A CG  1 
ATOM   2701 N ND1 . HIS A 1 319 ? -8.596  32.512 66.867  1.00 23.63  ? 319 HIS A ND1 1 
ATOM   2702 C CD2 . HIS A 1 319 ? -6.815  31.586 65.999  1.00 23.30  ? 319 HIS A CD2 1 
ATOM   2703 C CE1 . HIS A 1 319 ? -7.556  33.241 67.232  1.00 28.89  ? 319 HIS A CE1 1 
ATOM   2704 N NE2 . HIS A 1 319 ? -6.462  32.697 66.725  1.00 24.21  ? 319 HIS A NE2 1 
ATOM   2705 N N   . ALA A 1 320 ? -9.080  33.218 63.719  1.00 20.70  ? 320 ALA A N   1 
ATOM   2706 C CA  . ALA A 1 320 ? -9.394  34.645 63.692  1.00 24.90  ? 320 ALA A CA  1 
ATOM   2707 C C   . ALA A 1 320 ? -9.941  35.122 62.345  1.00 24.12  ? 320 ALA A C   1 
ATOM   2708 O O   . ALA A 1 320 ? -10.098 36.334 62.152  1.00 24.44  ? 320 ALA A O   1 
ATOM   2709 C CB  . ALA A 1 320 ? -8.155  35.484 64.075  1.00 18.12  ? 320 ALA A CB  1 
ATOM   2710 N N   . TRP A 1 321 ? -10.215 34.217 61.408  1.00 21.48  ? 321 TRP A N   1 
ATOM   2711 C CA  . TRP A 1 321 ? -10.750 34.594 60.108  1.00 21.01  ? 321 TRP A CA  1 
ATOM   2712 C C   . TRP A 1 321 ? -12.191 34.135 59.964  1.00 24.40  ? 321 TRP A C   1 
ATOM   2713 O O   . TRP A 1 321 ? -12.658 33.238 60.665  1.00 23.60  ? 321 TRP A O   1 
ATOM   2714 C CB  . TRP A 1 321 ? -9.966  33.971 58.950  1.00 21.81  ? 321 TRP A CB  1 
ATOM   2715 C CG  . TRP A 1 321 ? -8.518  34.317 58.798  1.00 24.15  ? 321 TRP A CG  1 
ATOM   2716 C CD1 . TRP A 1 321 ? -7.575  34.394 59.778  1.00 17.14  ? 321 TRP A CD1 1 
ATOM   2717 C CD2 . TRP A 1 321 ? -7.835  34.550 57.559  1.00 23.23  ? 321 TRP A CD2 1 
ATOM   2718 N NE1 . TRP A 1 321 ? -6.348  34.684 59.224  1.00 22.53  ? 321 TRP A NE1 1 
ATOM   2719 C CE2 . TRP A 1 321 ? -6.485  34.791 57.863  1.00 26.31  ? 321 TRP A CE2 1 
ATOM   2720 C CE3 . TRP A 1 321 ? -8.244  34.597 56.220  1.00 30.87  ? 321 TRP A CE3 1 
ATOM   2721 C CZ2 . TRP A 1 321 ? -5.531  35.076 56.874  1.00 27.16  ? 321 TRP A CZ2 1 
ATOM   2722 C CZ3 . TRP A 1 321 ? -7.295  34.881 55.239  1.00 30.06  ? 321 TRP A CZ3 1 
ATOM   2723 C CH2 . TRP A 1 321 ? -5.957  35.118 55.575  1.00 26.52  ? 321 TRP A CH2 1 
ATOM   2724 N N   . ASN A 1 322 ? -12.876 34.740 59.000  1.00 23.31  ? 322 ASN A N   1 
ATOM   2725 C CA  . ASN A 1 322 ? -14.116 34.176 58.495  1.00 30.16  ? 322 ASN A CA  1 
ATOM   2726 C C   . ASN A 1 322 ? -13.808 32.879 57.737  1.00 30.83  ? 322 ASN A C   1 
ATOM   2727 O O   . ASN A 1 322 ? -12.756 32.743 57.109  1.00 28.58  ? 322 ASN A O   1 
ATOM   2728 C CB  . ASN A 1 322 ? -14.805 35.224 57.612  1.00 38.89  ? 322 ASN A CB  1 
ATOM   2729 C CG  . ASN A 1 322 ? -15.704 34.627 56.563  1.00 43.08  ? 322 ASN A CG  1 
ATOM   2730 O OD1 . ASN A 1 322 ? -15.234 34.137 55.537  1.00 45.83  ? 322 ASN A OD1 1 
ATOM   2731 N ND2 . ASN A 1 322 ? -17.012 34.701 56.791  1.00 38.54  ? 322 ASN A ND2 1 
ATOM   2732 N N   . ALA A 1 323 ? -14.734 31.916 57.803  1.00 28.60  ? 323 ALA A N   1 
ATOM   2733 C CA  . ALA A 1 323 ? -14.449 30.568 57.301  1.00 26.11  ? 323 ALA A CA  1 
ATOM   2734 C C   . ALA A 1 323 ? -14.196 30.556 55.793  1.00 22.17  ? 323 ALA A C   1 
ATOM   2735 O O   . ALA A 1 323 ? -13.254 29.911 55.315  1.00 20.30  ? 323 ALA A O   1 
ATOM   2736 C CB  . ALA A 1 323 ? -15.600 29.621 57.655  1.00 27.31  ? 323 ALA A CB  1 
ATOM   2737 N N   . GLU A 1 324 ? -15.037 31.250 55.017  1.00 28.67  ? 324 GLU A N   1 
ATOM   2738 C CA  . GLU A 1 324 ? -14.860 31.244 53.564  1.00 31.24  ? 324 GLU A CA  1 
ATOM   2739 C C   . GLU A 1 324 ? -13.532 31.881 53.155  1.00 31.36  ? 324 GLU A C   1 
ATOM   2740 O O   . GLU A 1 324 ? -12.850 31.384 52.251  1.00 26.24  ? 324 GLU A O   1 
ATOM   2741 C CB  . GLU A 1 324 ? -16.032 31.958 52.885  1.00 37.19  ? 324 GLU A CB  1 
ATOM   2742 C CG  . GLU A 1 324 ? -17.392 31.280 53.079  1.00 48.84  ? 324 GLU A CG  1 
ATOM   2743 C CD  . GLU A 1 324 ? -18.164 31.818 54.279  1.00 60.27  ? 324 GLU A CD  1 
ATOM   2744 O OE1 . GLU A 1 324 ? -19.397 31.609 54.336  1.00 64.00  ? 324 GLU A OE1 1 
ATOM   2745 O OE2 . GLU A 1 324 ? -17.541 32.445 55.168  1.00 61.97  ? 324 GLU A OE2 1 
ATOM   2746 N N   . ASP A 1 325 ? -13.146 32.978 53.812  1.00 24.66  ? 325 ASP A N   1 
ATOM   2747 C CA  . ASP A 1 325 ? -11.897 33.648 53.466  1.00 27.76  ? 325 ASP A CA  1 
ATOM   2748 C C   . ASP A 1 325 ? -10.688 32.794 53.833  1.00 25.88  ? 325 ASP A C   1 
ATOM   2749 O O   . ASP A 1 325 ? -9.690  32.762 53.098  1.00 23.30  ? 325 ASP A O   1 
ATOM   2750 C CB  . ASP A 1 325 ? -11.823 35.009 54.165  1.00 38.20  ? 325 ASP A CB  1 
ATOM   2751 C CG  . ASP A 1 325 ? -12.910 35.975 53.700  1.00 52.10  ? 325 ASP A CG  1 
ATOM   2752 O OD1 . ASP A 1 325 ? -13.328 35.901 52.520  1.00 54.80  ? 325 ASP A OD1 1 
ATOM   2753 O OD2 . ASP A 1 325 ? -13.343 36.820 54.516  1.00 55.13  ? 325 ASP A OD2 1 
ATOM   2754 N N   . ALA A 1 326 ? -10.750 32.116 54.980  1.00 22.12  ? 326 ALA A N   1 
ATOM   2755 C CA  . ALA A 1 326 ? -9.675  31.215 55.374  1.00 19.60  ? 326 ALA A CA  1 
ATOM   2756 C C   . ALA A 1 326 ? -9.440  30.145 54.320  1.00 24.17  ? 326 ALA A C   1 
ATOM   2757 O O   . ALA A 1 326 ? -8.288  29.835 53.982  1.00 19.33  ? 326 ALA A O   1 
ATOM   2758 C CB  . ALA A 1 326 ? -10.009 30.561 56.714  1.00 21.61  ? 326 ALA A CB  1 
ATOM   2759 N N   . VAL A 1 327 ? -10.521 29.544 53.812  1.00 22.89  ? 327 VAL A N   1 
ATOM   2760 C CA  . VAL A 1 327 ? -10.385 28.480 52.827  1.00 23.29  ? 327 VAL A CA  1 
ATOM   2761 C C   . VAL A 1 327 ? -9.888  29.046 51.508  1.00 27.17  ? 327 VAL A C   1 
ATOM   2762 O O   . VAL A 1 327 ? -9.090  28.412 50.803  1.00 27.08  ? 327 VAL A O   1 
ATOM   2763 C CB  . VAL A 1 327 ? -11.724 27.743 52.657  1.00 27.91  ? 327 VAL A CB  1 
ATOM   2764 C CG1 . VAL A 1 327 ? -11.680 26.808 51.437  1.00 21.03  ? 327 VAL A CG1 1 
ATOM   2765 C CG2 . VAL A 1 327 ? -12.062 26.973 53.947  1.00 29.06  ? 327 VAL A CG2 1 
ATOM   2766 N N   . ARG A 1 328 ? -10.350 30.251 51.153  1.00 21.95  ? 328 ARG A N   1 
ATOM   2767 C CA  . ARG A 1 328 ? -9.847  30.897 49.947  1.00 27.92  ? 328 ARG A CA  1 
ATOM   2768 C C   . ARG A 1 328 ? -8.349  31.123 50.056  1.00 26.26  ? 328 ARG A C   1 
ATOM   2769 O O   . ARG A 1 328 ? -7.607  30.875 49.103  1.00 28.77  ? 328 ARG A O   1 
ATOM   2770 C CB  . ARG A 1 328 ? -10.578 32.221 49.698  1.00 22.82  ? 328 ARG A CB  1 
ATOM   2771 C CG  . ARG A 1 328 ? -10.016 33.042 48.521  1.00 32.30  ? 328 ARG A CG  1 
ATOM   2772 C CD  . ARG A 1 328 ? -10.787 34.351 48.282  1.00 40.56  ? 328 ARG A CD  1 
ATOM   2773 N NE  . ARG A 1 328 ? -10.418 35.402 49.230  1.00 47.83  ? 328 ARG A NE  1 
ATOM   2774 C CZ  . ARG A 1 328 ? -11.257 35.948 50.104  1.00 52.56  ? 328 ARG A CZ  1 
ATOM   2775 N NH1 . ARG A 1 328 ? -12.521 35.541 50.153  1.00 55.21  ? 328 ARG A NH1 1 
ATOM   2776 N NH2 . ARG A 1 328 ? -10.836 36.898 50.930  1.00 53.61  ? 328 ARG A NH2 1 
ATOM   2777 N N   . ASP A 1 329 ? -7.888  31.560 51.230  1.00 28.92  ? 329 ASP A N   1 
ATOM   2778 C CA  . ASP A 1 329 ? -6.462  31.776 51.451  1.00 28.38  ? 329 ASP A CA  1 
ATOM   2779 C C   . ASP A 1 329 ? -5.684  30.469 51.340  1.00 25.82  ? 329 ASP A C   1 
ATOM   2780 O O   . ASP A 1 329 ? -4.678  30.386 50.621  1.00 24.36  ? 329 ASP A O   1 
ATOM   2781 C CB  . ASP A 1 329 ? -6.254  32.417 52.826  1.00 25.49  ? 329 ASP A CB  1 
ATOM   2782 C CG  . ASP A 1 329 ? -4.797  32.687 53.126  1.00 25.95  ? 329 ASP A CG  1 
ATOM   2783 O OD1 . ASP A 1 329 ? -4.284  33.708 52.630  1.00 27.84  ? 329 ASP A OD1 1 
ATOM   2784 O OD2 . ASP A 1 329 ? -4.173  31.887 53.850  1.00 24.11  ? 329 ASP A OD2 1 
ATOM   2785 N N   . PHE A 1 330 ? -6.138  29.434 52.053  1.00 23.04  ? 330 PHE A N   1 
ATOM   2786 C CA  . PHE A 1 330 ? -5.479  28.130 52.014  1.00 24.19  ? 330 PHE A CA  1 
ATOM   2787 C C   . PHE A 1 330 ? -5.396  27.596 50.587  1.00 26.40  ? 330 PHE A C   1 
ATOM   2788 O O   . PHE A 1 330 ? -4.320  27.212 50.114  1.00 22.69  ? 330 PHE A O   1 
ATOM   2789 C CB  . PHE A 1 330 ? -6.237  27.160 52.924  1.00 19.90  ? 330 PHE A CB  1 
ATOM   2790 C CG  . PHE A 1 330 ? -5.473  25.908 53.283  1.00 25.06  ? 330 PHE A CG  1 
ATOM   2791 C CD1 . PHE A 1 330 ? -4.537  25.916 54.305  1.00 24.28  ? 330 PHE A CD1 1 
ATOM   2792 C CD2 . PHE A 1 330 ? -5.724  24.712 52.620  1.00 22.45  ? 330 PHE A CD2 1 
ATOM   2793 C CE1 . PHE A 1 330 ? -3.847  24.758 54.642  1.00 28.40  ? 330 PHE A CE1 1 
ATOM   2794 C CE2 . PHE A 1 330 ? -5.032  23.548 52.951  1.00 28.30  ? 330 PHE A CE2 1 
ATOM   2795 C CZ  . PHE A 1 330 ? -4.099  23.570 53.960  1.00 25.51  ? 330 PHE A CZ  1 
ATOM   2796 N N   . ILE A 1 331 ? -6.525  27.594 49.876  1.00 25.70  ? 331 ILE A N   1 
ATOM   2797 C CA  . ILE A 1 331 ? -6.543  27.104 48.502  1.00 27.61  ? 331 ILE A CA  1 
ATOM   2798 C C   . ILE A 1 331 ? -5.634  27.949 47.621  1.00 29.56  ? 331 ILE A C   1 
ATOM   2799 O O   . ILE A 1 331 ? -4.931  27.425 46.745  1.00 28.85  ? 331 ILE A O   1 
ATOM   2800 C CB  . ILE A 1 331 ? -7.989  27.072 47.967  1.00 30.90  ? 331 ILE A CB  1 
ATOM   2801 C CG1 . ILE A 1 331 ? -8.823  26.071 48.762  1.00 33.16  ? 331 ILE A CG1 1 
ATOM   2802 C CG2 . ILE A 1 331 ? -8.012  26.725 46.485  1.00 30.08  ? 331 ILE A CG2 1 
ATOM   2803 C CD1 . ILE A 1 331 ? -8.307  24.651 48.694  1.00 34.52  ? 331 ILE A CD1 1 
ATOM   2804 N N   . GLY A 1 332 ? -5.628  29.270 47.841  1.00 25.60  ? 332 GLY A N   1 
ATOM   2805 C CA  . GLY A 1 332 ? -4.782  30.138 47.039  1.00 22.74  ? 332 GLY A CA  1 
ATOM   2806 C C   . GLY A 1 332 ? -3.304  29.833 47.208  1.00 25.48  ? 332 GLY A C   1 
ATOM   2807 O O   . GLY A 1 332 ? -2.536  29.872 46.244  1.00 30.91  ? 332 GLY A O   1 
ATOM   2808 N N   . ARG A 1 333 ? -2.885  29.525 48.435  1.00 24.71  ? 333 ARG A N   1 
ATOM   2809 C CA  . ARG A 1 333 ? -1.486  29.168 48.651  1.00 25.74  ? 333 ARG A CA  1 
ATOM   2810 C C   . ARG A 1 333 ? -1.142  27.853 47.961  1.00 22.54  ? 333 ARG A C   1 
ATOM   2811 O O   . ARG A 1 333 ? -0.097  27.745 47.314  1.00 25.06  ? 333 ARG A O   1 
ATOM   2812 C CB  . ARG A 1 333 ? -1.182  29.114 50.150  1.00 21.67  ? 333 ARG A CB  1 
ATOM   2813 C CG  . ARG A 1 333 ? -1.279  30.481 50.835  1.00 21.76  ? 333 ARG A CG  1 
ATOM   2814 C CD  . ARG A 1 333 ? -1.398  30.301 52.347  1.00 25.53  ? 333 ARG A CD  1 
ATOM   2815 N NE  . ARG A 1 333 ? -1.442  31.568 53.066  1.00 28.08  ? 333 ARG A NE  1 
ATOM   2816 C CZ  . ARG A 1 333 ? -0.368  32.281 53.395  1.00 31.44  ? 333 ARG A CZ  1 
ATOM   2817 N NH1 . ARG A 1 333 ? 0.850   31.863 53.058  1.00 28.66  ? 333 ARG A NH1 1 
ATOM   2818 N NH2 . ARG A 1 333 ? -0.513  33.418 54.062  1.00 30.45  ? 333 ARG A NH2 1 
ATOM   2819 N N   . LEU A 1 334 ? -2.027  26.848 48.051  1.00 23.78  ? 334 LEU A N   1 
ATOM   2820 C CA  . LEU A 1 334 ? -1.782  25.590 47.345  1.00 23.98  ? 334 LEU A CA  1 
ATOM   2821 C C   . LEU A 1 334 ? -1.682  25.807 45.837  1.00 26.19  ? 334 LEU A C   1 
ATOM   2822 O O   . LEU A 1 334 ? -0.861  25.170 45.163  1.00 23.62  ? 334 LEU A O   1 
ATOM   2823 C CB  . LEU A 1 334 ? -2.891  24.589 47.658  1.00 22.49  ? 334 LEU A CB  1 
ATOM   2824 C CG  . LEU A 1 334 ? -2.990  24.160 49.118  1.00 25.40  ? 334 LEU A CG  1 
ATOM   2825 C CD1 . LEU A 1 334 ? -4.265  23.353 49.306  1.00 21.28  ? 334 LEU A CD1 1 
ATOM   2826 C CD2 . LEU A 1 334 ? -1.752  23.361 49.526  1.00 24.37  ? 334 LEU A CD2 1 
ATOM   2827 N N   . LYS A 1 335 ? -2.502  26.707 45.288  1.00 27.21  ? 335 LYS A N   1 
ATOM   2828 C CA  . LYS A 1 335 ? -2.389  27.013 43.864  1.00 26.90  ? 335 LYS A CA  1 
ATOM   2829 C C   . LYS A 1 335 ? -1.035  27.635 43.527  1.00 25.49  ? 335 LYS A C   1 
ATOM   2830 O O   . LYS A 1 335 ? -0.472  27.350 42.465  1.00 25.28  ? 335 LYS A O   1 
ATOM   2831 C CB  . LYS A 1 335 ? -3.537  27.923 43.416  1.00 32.80  ? 335 LYS A CB  1 
ATOM   2832 C CG  . LYS A 1 335 ? -3.721  27.934 41.900  1.00 41.53  ? 335 LYS A CG  1 
ATOM   2833 C CD  . LYS A 1 335 ? -5.001  28.647 41.474  1.00 44.41  ? 335 LYS A CD  1 
ATOM   2834 C CE  . LYS A 1 335 ? -4.711  30.068 40.997  1.00 51.12  ? 335 LYS A CE  1 
ATOM   2835 N NZ  . LYS A 1 335 ? -4.227  30.138 39.583  1.00 54.64  ? 335 LYS A NZ  1 
ATOM   2836 N N   . LYS A 1 336 ? -0.497  28.466 44.423  1.00 20.85  ? 336 LYS A N   1 
ATOM   2837 C CA  . LYS A 1 336 ? 0.818   29.071 44.183  1.00 22.41  ? 336 LYS A CA  1 
ATOM   2838 C C   . LYS A 1 336 ? 1.930   28.027 44.223  1.00 29.36  ? 336 LYS A C   1 
ATOM   2839 O O   . LYS A 1 336 ? 2.864   28.068 43.413  1.00 34.27  ? 336 LYS A O   1 
ATOM   2840 C CB  . LYS A 1 336 ? 1.103   30.195 45.202  1.00 28.72  ? 336 LYS A CB  1 
ATOM   2841 C CG  . LYS A 1 336 ? 2.594   30.629 45.277  1.00 46.72  ? 336 LYS A CG  1 
ATOM   2842 C CD  . LYS A 1 336 ? 3.032   31.151 46.668  1.00 56.44  ? 336 LYS A CD  1 
ATOM   2843 C CE  . LYS A 1 336 ? 4.464   30.720 47.002  1.00 60.72  ? 336 LYS A CE  1 
ATOM   2844 N NZ  . LYS A 1 336 ? 4.687   30.652 48.483  1.00 63.56  ? 336 LYS A NZ  1 
ATOM   2845 N N   . ILE A 1 337 ? 1.850   27.085 45.162  1.00 28.55  ? 337 ILE A N   1 
ATOM   2846 C CA  . ILE A 1 337 ? 2.793   25.968 45.172  1.00 24.08  ? 337 ILE A CA  1 
ATOM   2847 C C   . ILE A 1 337 ? 2.650   25.148 43.892  1.00 29.21  ? 337 ILE A C   1 
ATOM   2848 O O   . ILE A 1 337 ? 3.646   24.783 43.253  1.00 30.12  ? 337 ILE A O   1 
ATOM   2849 C CB  . ILE A 1 337 ? 2.575   25.105 46.434  1.00 23.52  ? 337 ILE A CB  1 
ATOM   2850 C CG1 . ILE A 1 337 ? 2.842   25.928 47.694  1.00 26.55  ? 337 ILE A CG1 1 
ATOM   2851 C CG2 . ILE A 1 337 ? 3.435   23.843 46.403  1.00 24.34  ? 337 ILE A CG2 1 
ATOM   2852 C CD1 . ILE A 1 337 ? 2.318   25.269 48.950  1.00 26.18  ? 337 ILE A CD1 1 
ATOM   2853 N N   . HIS A 1 338 ? 1.405   24.867 43.488  1.00 27.08  ? 338 HIS A N   1 
ATOM   2854 C CA  . HIS A 1 338 ? 1.156   24.069 42.288  1.00 28.00  ? 338 HIS A CA  1 
ATOM   2855 C C   . HIS A 1 338 ? 1.783   24.699 41.051  1.00 32.44  ? 338 HIS A C   1 
ATOM   2856 O O   . HIS A 1 338 ? 2.300   23.988 40.180  1.00 28.62  ? 338 HIS A O   1 
ATOM   2857 C CB  . HIS A 1 338 ? -0.345  23.905 42.074  1.00 29.19  ? 338 HIS A CB  1 
ATOM   2858 C CG  . HIS A 1 338 ? -0.702  23.080 40.873  1.00 31.60  ? 338 HIS A CG  1 
ATOM   2859 N ND1 . HIS A 1 338 ? -1.325  23.611 39.765  1.00 34.03  ? 338 HIS A ND1 1 
ATOM   2860 C CD2 . HIS A 1 338 ? -0.539  21.759 40.617  1.00 31.28  ? 338 HIS A CD2 1 
ATOM   2861 C CE1 . HIS A 1 338 ? -1.534  22.653 38.878  1.00 32.40  ? 338 HIS A CE1 1 
ATOM   2862 N NE2 . HIS A 1 338 ? -1.061  21.520 39.368  1.00 33.80  ? 338 HIS A NE2 1 
ATOM   2863 N N   . GLU A 1 339 ? 1.723   26.029 40.945  1.00 30.78  ? 339 GLU A N   1 
ATOM   2864 C CA  . GLU A 1 339 ? 2.217   26.728 39.765  1.00 34.12  ? 339 GLU A CA  1 
ATOM   2865 C C   . GLU A 1 339 ? 3.716   26.981 39.812  1.00 32.70  ? 339 GLU A C   1 
ATOM   2866 O O   . GLU A 1 339 ? 4.316   27.250 38.766  1.00 32.52  ? 339 GLU A O   1 
ATOM   2867 C CB  . GLU A 1 339 ? 1.496   28.071 39.600  1.00 34.83  ? 339 GLU A CB  1 
ATOM   2868 C CG  . GLU A 1 339 ? -0.019  27.987 39.458  1.00 39.66  ? 339 GLU A CG  1 
ATOM   2869 C CD  . GLU A 1 339 ? -0.697  29.317 39.745  1.00 50.51  ? 339 GLU A CD  1 
ATOM   2870 O OE1 . GLU A 1 339 ? -1.903  29.456 39.440  1.00 55.45  ? 339 GLU A OE1 1 
ATOM   2871 O OE2 . GLU A 1 339 ? -0.023  30.225 40.281  1.00 53.95  ? 339 GLU A OE2 1 
ATOM   2872 N N   . SER A 1 340 ? 4.331   26.902 40.988  1.00 34.25  ? 340 SER A N   1 
ATOM   2873 C CA  . SER A 1 340 ? 5.714   27.323 41.152  1.00 34.87  ? 340 SER A CA  1 
ATOM   2874 C C   . SER A 1 340 ? 6.713   26.206 40.895  1.00 37.35  ? 340 SER A C   1 
ATOM   2875 O O   . SER A 1 340 ? 7.919   26.472 40.849  1.00 35.26  ? 340 SER A O   1 
ATOM   2876 C CB  . SER A 1 340 ? 5.930   27.891 42.559  1.00 37.11  ? 340 SER A CB  1 
ATOM   2877 O OG  . SER A 1 340 ? 6.254   26.862 43.477  1.00 38.56  ? 340 SER A OG  1 
ATOM   2878 N N   . VAL A 1 341 ? 6.253   24.970 40.737  1.00 41.83  ? 341 VAL A N   1 
ATOM   2879 C CA  . VAL A 1 341 ? 7.145   23.857 40.461  1.00 41.48  ? 341 VAL A CA  1 
ATOM   2880 C C   . VAL A 1 341 ? 6.614   23.071 39.274  1.00 42.02  ? 341 VAL A C   1 
ATOM   2881 O O   . VAL A 1 341 ? 5.404   22.990 39.026  1.00 35.22  ? 341 VAL A O   1 
ATOM   2882 C CB  . VAL A 1 341 ? 7.336   22.930 41.682  1.00 40.10  ? 341 VAL A CB  1 
ATOM   2883 C CG1 . VAL A 1 341 ? 8.173   23.627 42.748  1.00 42.76  ? 341 VAL A CG1 1 
ATOM   2884 C CG2 . VAL A 1 341 ? 5.990   22.492 42.237  1.00 33.66  ? 341 VAL A CG2 1 
ATOM   2885 N N   . ASP A 1 342 ? 7.551   22.497 38.536  1.00 43.25  ? 342 ASP A N   1 
ATOM   2886 C CA  . ASP A 1 342 ? 7.251   21.703 37.359  1.00 46.27  ? 342 ASP A CA  1 
ATOM   2887 C C   . ASP A 1 342 ? 6.901   20.267 37.722  1.00 45.10  ? 342 ASP A C   1 
ATOM   2888 O O   . ASP A 1 342 ? 6.235   19.580 36.941  1.00 48.66  ? 342 ASP A O   1 
ATOM   2889 C CB  . ASP A 1 342 ? 8.476   21.698 36.461  1.00 57.39  ? 342 ASP A CB  1 
ATOM   2890 C CG  . ASP A 1 342 ? 9.703   21.207 37.216  1.00 64.16  ? 342 ASP A CG  1 
ATOM   2891 O OD1 . ASP A 1 342 ? 9.818   19.979 37.387  1.00 67.50  ? 342 ASP A OD1 1 
ATOM   2892 O OD2 . ASP A 1 342 ? 10.484  22.032 37.743  1.00 64.52  ? 342 ASP A OD2 1 
ATOM   2893 N N   . PHE A 1 343 ? 7.390   19.783 38.867  1.00 39.23  ? 343 PHE A N   1 
ATOM   2894 C CA  . PHE A 1 343 ? 7.118   18.436 39.338  1.00 31.10  ? 343 PHE A CA  1 
ATOM   2895 C C   . PHE A 1 343 ? 5.871   18.437 40.223  1.00 27.12  ? 343 PHE A C   1 
ATOM   2896 O O   . PHE A 1 343 ? 5.216   19.463 40.413  1.00 28.54  ? 343 PHE A O   1 
ATOM   2897 C CB  . PHE A 1 343 ? 8.320   17.865 40.091  1.00 32.13  ? 343 PHE A CB  1 
ATOM   2898 C CG  . PHE A 1 343 ? 8.809   18.740 41.217  1.00 34.22  ? 343 PHE A CG  1 
ATOM   2899 C CD1 . PHE A 1 343 ? 9.679   19.796 40.965  1.00 35.10  ? 343 PHE A CD1 1 
ATOM   2900 C CD2 . PHE A 1 343 ? 8.403   18.512 42.521  1.00 34.82  ? 343 PHE A CD2 1 
ATOM   2901 C CE1 . PHE A 1 343 ? 10.133  20.603 41.993  1.00 32.57  ? 343 PHE A CE1 1 
ATOM   2902 C CE2 . PHE A 1 343 ? 8.856   19.317 43.555  1.00 34.25  ? 343 PHE A CE2 1 
ATOM   2903 C CZ  . PHE A 1 343 ? 9.718   20.365 43.287  1.00 31.89  ? 343 PHE A CZ  1 
ATOM   2904 N N   . GLN A 1 344 ? 5.531   17.268 40.766  1.00 23.86  ? 344 GLN A N   1 
ATOM   2905 C CA  . GLN A 1 344 ? 4.333   17.144 41.585  1.00 22.77  ? 344 GLN A CA  1 
ATOM   2906 C C   . GLN A 1 344 ? 4.714   17.279 43.050  1.00 24.72  ? 344 GLN A C   1 
ATOM   2907 O O   . GLN A 1 344 ? 5.232   16.323 43.642  1.00 23.47  ? 344 GLN A O   1 
ATOM   2908 C CB  . GLN A 1 344 ? 3.631   15.810 41.319  1.00 27.71  ? 344 GLN A CB  1 
ATOM   2909 C CG  . GLN A 1 344 ? 3.240   15.641 39.849  1.00 29.15  ? 344 GLN A CG  1 
ATOM   2910 C CD  . GLN A 1 344 ? 2.294   14.493 39.625  1.00 31.57  ? 344 GLN A CD  1 
ATOM   2911 O OE1 . GLN A 1 344 ? 1.134   14.690 39.251  1.00 33.22  ? 344 GLN A OE1 1 
ATOM   2912 N NE2 . GLN A 1 344 ? 2.778   13.275 39.864  1.00 32.68  ? 344 GLN A NE2 1 
ATOM   2913 N N   . PRO A 1 345 ? 4.489   18.430 43.674  1.00 28.34  ? 345 PRO A N   1 
ATOM   2914 C CA  . PRO A 1 345 ? 4.934   18.620 45.057  1.00 23.15  ? 345 PRO A CA  1 
ATOM   2915 C C   . PRO A 1 345 ? 4.092   17.817 46.038  1.00 25.42  ? 345 PRO A C   1 
ATOM   2916 O O   . PRO A 1 345 ? 2.887   17.622 45.845  1.00 29.42  ? 345 PRO A O   1 
ATOM   2917 C CB  . PRO A 1 345 ? 4.753   20.127 45.276  1.00 19.56  ? 345 PRO A CB  1 
ATOM   2918 C CG  . PRO A 1 345 ? 3.622   20.496 44.370  1.00 27.76  ? 345 PRO A CG  1 
ATOM   2919 C CD  . PRO A 1 345 ? 3.772   19.606 43.150  1.00 31.07  ? 345 PRO A CD  1 
ATOM   2920 N N   . VAL A 1 346 ? 4.741   17.339 47.099  1.00 22.33  ? 346 VAL A N   1 
ATOM   2921 C CA  . VAL A 1 346 ? 4.047   16.714 48.223  1.00 26.66  ? 346 VAL A CA  1 
ATOM   2922 C C   . VAL A 1 346 ? 3.974   17.727 49.363  1.00 23.24  ? 346 VAL A C   1 
ATOM   2923 O O   . VAL A 1 346 ? 5.007   18.170 49.873  1.00 21.06  ? 346 VAL A O   1 
ATOM   2924 C CB  . VAL A 1 346 ? 4.747   15.424 48.679  1.00 23.92  ? 346 VAL A CB  1 
ATOM   2925 C CG1 . VAL A 1 346 ? 3.958   14.787 49.818  1.00 27.42  ? 346 VAL A CG1 1 
ATOM   2926 C CG2 . VAL A 1 346 ? 4.896   14.430 47.504  1.00 19.52  ? 346 VAL A CG2 1 
ATOM   2927 N N   . VAL A 1 347 ? 2.763   18.080 49.787  1.00 19.00  ? 347 VAL A N   1 
ATOM   2928 C CA  . VAL A 1 347 ? 2.571   19.137 50.776  1.00 23.87  ? 347 VAL A CA  1 
ATOM   2929 C C   . VAL A 1 347 ? 2.003   18.513 52.048  1.00 25.11  ? 347 VAL A C   1 
ATOM   2930 O O   . VAL A 1 347 ? 0.857   18.040 52.059  1.00 19.98  ? 347 VAL A O   1 
ATOM   2931 C CB  . VAL A 1 347 ? 1.655   20.251 50.253  1.00 23.01  ? 347 VAL A CB  1 
ATOM   2932 C CG1 . VAL A 1 347 ? 1.514   21.343 51.316  1.00 22.57  ? 347 VAL A CG1 1 
ATOM   2933 C CG2 . VAL A 1 347 ? 2.193   20.831 48.926  1.00 19.24  ? 347 VAL A CG2 1 
ATOM   2934 N N   . PHE A 1 348 ? 2.787   18.549 53.130  1.00 23.53  ? 348 PHE A N   1 
ATOM   2935 C CA  . PHE A 1 348 ? 2.416   17.917 54.395  1.00 26.32  ? 348 PHE A CA  1 
ATOM   2936 C C   . PHE A 1 348 ? 1.895   18.962 55.382  1.00 23.36  ? 348 PHE A C   1 
ATOM   2937 O O   . PHE A 1 348 ? 2.604   19.915 55.737  1.00 16.07  ? 348 PHE A O   1 
ATOM   2938 C CB  . PHE A 1 348 ? 3.601   17.162 54.993  1.00 30.14  ? 348 PHE A CB  1 
ATOM   2939 C CG  . PHE A 1 348 ? 3.560   15.664 54.774  1.00 26.68  ? 348 PHE A CG  1 
ATOM   2940 C CD1 . PHE A 1 348 ? 3.826   15.120 53.518  1.00 23.90  ? 348 PHE A CD1 1 
ATOM   2941 C CD2 . PHE A 1 348 ? 3.293   14.807 55.829  1.00 21.34  ? 348 PHE A CD2 1 
ATOM   2942 C CE1 . PHE A 1 348 ? 3.800   13.745 53.321  1.00 29.44  ? 348 PHE A CE1 1 
ATOM   2943 C CE2 . PHE A 1 348 ? 3.278   13.428 55.645  1.00 33.47  ? 348 PHE A CE2 1 
ATOM   2944 C CZ  . PHE A 1 348 ? 3.529   12.897 54.384  1.00 36.34  ? 348 PHE A CZ  1 
ATOM   2945 N N   . VAL A 1 349 ? 0.657   18.782 55.814  1.00 19.77  ? 349 VAL A N   1 
ATOM   2946 C CA  . VAL A 1 349 ? 0.022   19.636 56.809  1.00 22.01  ? 349 VAL A CA  1 
ATOM   2947 C C   . VAL A 1 349 ? -0.081  18.796 58.074  1.00 24.64  ? 349 VAL A C   1 
ATOM   2948 O O   . VAL A 1 349 ? -0.848  17.823 58.118  1.00 21.74  ? 349 VAL A O   1 
ATOM   2949 C CB  . VAL A 1 349 ? -1.353  20.132 56.338  1.00 17.88  ? 349 VAL A CB  1 
ATOM   2950 C CG1 . VAL A 1 349 ? -2.001  21.011 57.392  1.00 18.38  ? 349 VAL A CG1 1 
ATOM   2951 C CG2 . VAL A 1 349 ? -1.215  20.888 55.000  1.00 21.94  ? 349 VAL A CG2 1 
ATOM   2952 N N   . VAL A 1 350 ? 0.732   19.124 59.080  1.00 15.96  ? 350 VAL A N   1 
ATOM   2953 C CA  . VAL A 1 350 ? 0.834   18.308 60.288  1.00 17.05  ? 350 VAL A CA  1 
ATOM   2954 C C   . VAL A 1 350 ? 0.691   19.212 61.496  1.00 19.43  ? 350 VAL A C   1 
ATOM   2955 O O   . VAL A 1 350 ? 1.513   20.115 61.698  1.00 17.28  ? 350 VAL A O   1 
ATOM   2956 C CB  . VAL A 1 350 ? 2.163   17.538 60.368  1.00 14.60  ? 350 VAL A CB  1 
ATOM   2957 C CG1 . VAL A 1 350 ? 2.195   16.688 61.641  1.00 13.26  ? 350 VAL A CG1 1 
ATOM   2958 C CG2 . VAL A 1 350 ? 2.369   16.667 59.113  1.00 17.41  ? 350 VAL A CG2 1 
ATOM   2959 N N   . LEU A 1 351 ? -0.322  18.944 62.321  1.00 23.46  ? 351 LEU A N   1 
ATOM   2960 C CA  . LEU A 1 351 ? -0.535  19.711 63.543  1.00 26.03  ? 351 LEU A CA  1 
ATOM   2961 C C   . LEU A 1 351 ? -1.413  18.883 64.474  1.00 22.30  ? 351 LEU A C   1 
ATOM   2962 O O   . LEU A 1 351 ? -1.955  17.851 64.082  1.00 20.76  ? 351 LEU A O   1 
ATOM   2963 C CB  . LEU A 1 351 ? -1.166  21.076 63.235  1.00 22.92  ? 351 LEU A CB  1 
ATOM   2964 C CG  . LEU A 1 351 ? -2.556  21.046 62.598  1.00 22.91  ? 351 LEU A CG  1 
ATOM   2965 C CD1 . LEU A 1 351 ? -3.349  22.204 63.146  1.00 24.87  ? 351 LEU A CD1 1 
ATOM   2966 C CD2 . LEU A 1 351 ? -2.498  21.118 61.079  1.00 17.48  ? 351 LEU A CD2 1 
ATOM   2967 N N   . ASN A 1 352 ? -1.571  19.324 65.708  1.00 15.42  ? 352 ASN A N   1 
ATOM   2968 C CA  . ASN A 1 352 ? -2.484  18.719 66.625  1.00 16.09  ? 352 ASN A CA  1 
ATOM   2969 C C   . ASN A 1 352 ? -3.916  18.735 66.044  1.00 18.90  ? 352 ASN A C   1 
ATOM   2970 O O   . ASN A 1 352 ? -4.332  19.647 65.426  1.00 18.81  ? 352 ASN A O   1 
ATOM   2971 C CB  . ASN A 1 352 ? -2.500  19.361 67.961  1.00 19.00  ? 352 ASN A CB  1 
ATOM   2972 C CG  . ASN A 1 352 ? -1.545  18.771 68.866  1.00 27.00  ? 352 ASN A CG  1 
ATOM   2973 O OD1 . ASN A 1 352 ? -1.904  17.869 69.627  1.00 25.83  ? 352 ASN A OD1 1 
ATOM   2974 N ND2 . ASN A 1 352 ? -0.396  19.203 68.818  1.00 31.72  ? 352 ASN A ND2 1 
ATOM   2975 N N   . GLY A 1 353 ? -4.655  17.678 66.250  1.00 19.48  ? 353 GLY A N   1 
ATOM   2976 C CA  . GLY A 1 353 ? -5.973  17.562 65.674  1.00 16.32  ? 353 GLY A CA  1 
ATOM   2977 C C   . GLY A 1 353 ? -7.109  17.942 66.585  1.00 15.74  ? 353 GLY A C   1 
ATOM   2978 O O   . GLY A 1 353 ? -8.261  17.892 66.152  1.00 19.55  ? 353 GLY A O   1 
ATOM   2979 N N   . GLU A 1 354 ? -6.835  18.311 67.840  1.00 15.77  ? 354 GLU A N   1 
ATOM   2980 C CA  . GLU A 1 354 ? -7.904  18.534 68.804  1.00 19.78  ? 354 GLU A CA  1 
ATOM   2981 C C   . GLU A 1 354 ? -7.843  19.879 69.525  1.00 18.88  ? 354 GLU A C   1 
ATOM   2982 O O   . GLU A 1 354 ? -8.792  20.204 70.246  1.00 16.87  ? 354 GLU A O   1 
ATOM   2983 C CB  . GLU A 1 354 ? -7.923  17.402 69.853  1.00 17.39  ? 354 GLU A CB  1 
ATOM   2984 C CG  . GLU A 1 354 ? -6.867  17.513 70.961  1.00 13.18  ? 354 GLU A CG  1 
ATOM   2985 C CD  . GLU A 1 354 ? -5.486  16.953 70.542  1.00 26.77  ? 354 GLU A CD  1 
ATOM   2986 O OE1 . GLU A 1 354 ? -4.995  15.971 71.157  1.00 24.04  ? 354 GLU A OE1 1 
ATOM   2987 O OE2 . GLU A 1 354 ? -4.886  17.500 69.601  1.00 23.31  ? 354 GLU A OE2 1 
ATOM   2988 N N   . ASN A 1 355 ? -6.789  20.678 69.351  1.00 18.97  ? 355 ASN A N   1 
ATOM   2989 C CA  . ASN A 1 355 ? -6.596  21.827 70.227  1.00 22.84  ? 355 ASN A CA  1 
ATOM   2990 C C   . ASN A 1 355 ? -7.003  23.166 69.612  1.00 25.61  ? 355 ASN A C   1 
ATOM   2991 O O   . ASN A 1 355 ? -7.266  24.115 70.358  1.00 19.90  ? 355 ASN A O   1 
ATOM   2992 C CB  . ASN A 1 355 ? -5.130  21.904 70.671  1.00 21.34  ? 355 ASN A CB  1 
ATOM   2993 C CG  . ASN A 1 355 ? -4.772  20.817 71.669  1.00 21.63  ? 355 ASN A CG  1 
ATOM   2994 O OD1 . ASN A 1 355 ? -5.629  20.347 72.419  1.00 22.68  ? 355 ASN A OD1 1 
ATOM   2995 N ND2 . ASN A 1 355 ? -3.510  20.403 71.673  1.00 21.44  ? 355 ASN A ND2 1 
ATOM   2996 N N   . CYS A 1 356 ? -7.047  23.280 68.289  1.00 22.26  ? 356 CYS A N   1 
ATOM   2997 C CA  . CYS A 1 356 ? -7.322  24.584 67.706  1.00 22.25  ? 356 CYS A CA  1 
ATOM   2998 C C   . CYS A 1 356 ? -8.811  24.861 67.533  1.00 24.11  ? 356 CYS A C   1 
ATOM   2999 O O   . CYS A 1 356 ? -9.202  26.032 67.465  1.00 20.05  ? 356 CYS A O   1 
ATOM   3000 C CB  . CYS A 1 356 ? -6.611  24.717 66.356  1.00 20.80  ? 356 CYS A CB  1 
ATOM   3001 S SG  . CYS A 1 356 ? -6.959  23.364 65.207  1.00 18.12  ? 356 CYS A SG  1 
ATOM   3002 N N   . TRP A 1 357 ? -9.652  23.822 67.481  1.00 19.34  ? 357 TRP A N   1 
ATOM   3003 C CA  . TRP A 1 357 ? -11.032 24.018 67.034  1.00 19.31  ? 357 TRP A CA  1 
ATOM   3004 C C   . TRP A 1 357 ? -11.871 24.814 68.031  1.00 18.24  ? 357 TRP A C   1 
ATOM   3005 O O   . TRP A 1 357 ? -12.780 25.544 67.613  1.00 17.82  ? 357 TRP A O   1 
ATOM   3006 C CB  . TRP A 1 357 ? -11.665 22.659 66.732  1.00 19.21  ? 357 TRP A CB  1 
ATOM   3007 C CG  . TRP A 1 357 ? -10.752 21.808 65.879  1.00 22.15  ? 357 TRP A CG  1 
ATOM   3008 C CD1 . TRP A 1 357 ? -10.236 20.572 66.183  1.00 21.02  ? 357 TRP A CD1 1 
ATOM   3009 C CD2 . TRP A 1 357 ? -10.253 22.144 64.578  1.00 17.33  ? 357 TRP A CD2 1 
ATOM   3010 N NE1 . TRP A 1 357 ? -9.444  20.123 65.145  1.00 20.47  ? 357 TRP A NE1 1 
ATOM   3011 C CE2 . TRP A 1 357 ? -9.438  21.070 64.150  1.00 20.41  ? 357 TRP A CE2 1 
ATOM   3012 C CE3 . TRP A 1 357 ? -10.404 23.259 63.737  1.00 19.45  ? 357 TRP A CE3 1 
ATOM   3013 C CZ2 . TRP A 1 357 ? -8.782  21.075 62.912  1.00 18.58  ? 357 TRP A CZ2 1 
ATOM   3014 C CZ3 . TRP A 1 357 ? -9.756  23.259 62.506  1.00 22.36  ? 357 TRP A CZ3 1 
ATOM   3015 C CH2 . TRP A 1 357 ? -8.952  22.175 62.109  1.00 23.31  ? 357 TRP A CH2 1 
ATOM   3016 N N   . GLU A 1 358 ? -11.572 24.724 69.331  1.00 18.97  ? 358 GLU A N   1 
ATOM   3017 C CA  . GLU A 1 358 ? -12.361 25.434 70.342  1.00 19.37  ? 358 GLU A CA  1 
ATOM   3018 C C   . GLU A 1 358 ? -12.268 26.951 70.235  1.00 22.42  ? 358 GLU A C   1 
ATOM   3019 O O   . GLU A 1 358 ? -13.107 27.645 70.823  1.00 25.16  ? 358 GLU A O   1 
ATOM   3020 C CB  . GLU A 1 358 ? -11.943 25.009 71.754  1.00 16.48  ? 358 GLU A CB  1 
ATOM   3021 C CG  . GLU A 1 358 ? -10.489 25.298 72.077  1.00 14.99  ? 358 GLU A CG  1 
ATOM   3022 C CD  . GLU A 1 358 ? -9.978  24.370 73.171  1.00 28.94  ? 358 GLU A CD  1 
ATOM   3023 O OE1 . GLU A 1 358 ? -9.675  24.859 74.286  1.00 31.21  ? 358 GLU A OE1 1 
ATOM   3024 O OE2 . GLU A 1 358 ? -9.905  23.147 72.917  1.00 26.82  ? 358 GLU A OE2 1 
ATOM   3025 N N   . TYR A 1 359 ? -11.281 27.482 69.516  1.00 18.56  ? 359 TYR A N   1 
ATOM   3026 C CA  . TYR A 1 359 ? -11.172 28.915 69.276  1.00 28.87  ? 359 TYR A CA  1 
ATOM   3027 C C   . TYR A 1 359 ? -11.790 29.347 67.952  1.00 27.82  ? 359 TYR A C   1 
ATOM   3028 O O   . TYR A 1 359 ? -11.883 30.554 67.700  1.00 21.90  ? 359 TYR A O   1 
ATOM   3029 C CB  . TYR A 1 359 ? -9.697  29.363 69.330  1.00 24.47  ? 359 TYR A CB  1 
ATOM   3030 C CG  . TYR A 1 359 ? -9.030  28.978 70.634  1.00 29.31  ? 359 TYR A CG  1 
ATOM   3031 C CD1 . TYR A 1 359 ? -9.215  29.742 71.785  1.00 29.76  ? 359 TYR A CD1 1 
ATOM   3032 C CD2 . TYR A 1 359 ? -8.253  27.824 70.727  1.00 30.75  ? 359 TYR A CD2 1 
ATOM   3033 C CE1 . TYR A 1 359 ? -8.621  29.385 72.987  1.00 33.21  ? 359 TYR A CE1 1 
ATOM   3034 C CE2 . TYR A 1 359 ? -7.655  27.460 71.926  1.00 37.14  ? 359 TYR A CE2 1 
ATOM   3035 C CZ  . TYR A 1 359 ? -7.845  28.242 73.051  1.00 38.52  ? 359 TYR A CZ  1 
ATOM   3036 O OH  . TYR A 1 359 ? -7.251  27.878 74.240  1.00 44.31  ? 359 TYR A OH  1 
ATOM   3037 N N   . TYR A 1 360 ? -12.209 28.403 67.112  1.00 23.77  ? 360 TYR A N   1 
ATOM   3038 C CA  . TYR A 1 360 ? -12.945 28.728 65.896  1.00 19.77  ? 360 TYR A CA  1 
ATOM   3039 C C   . TYR A 1 360 ? -14.426 28.871 66.214  1.00 22.91  ? 360 TYR A C   1 
ATOM   3040 O O   . TYR A 1 360 ? -14.941 28.230 67.133  1.00 20.34  ? 360 TYR A O   1 
ATOM   3041 C CB  . TYR A 1 360 ? -12.823 27.625 64.846  1.00 21.72  ? 360 TYR A CB  1 
ATOM   3042 C CG  . TYR A 1 360 ? -11.545 27.489 64.055  1.00 16.76  ? 360 TYR A CG  1 
ATOM   3043 C CD1 . TYR A 1 360 ? -10.382 27.001 64.637  1.00 21.04  ? 360 TYR A CD1 1 
ATOM   3044 C CD2 . TYR A 1 360 ? -11.541 27.736 62.697  1.00 19.90  ? 360 TYR A CD2 1 
ATOM   3045 C CE1 . TYR A 1 360 ? -9.236  26.821 63.889  1.00 17.87  ? 360 TYR A CE1 1 
ATOM   3046 C CE2 . TYR A 1 360 ? -10.408 27.563 61.942  1.00 22.92  ? 360 TYR A CE2 1 
ATOM   3047 C CZ  . TYR A 1 360 ? -9.263  27.116 62.537  1.00 19.38  ? 360 TYR A CZ  1 
ATOM   3048 O OH  . TYR A 1 360 ? -8.154  26.964 61.755  1.00 19.44  ? 360 TYR A OH  1 
ATOM   3049 N N   . GLU A 1 361 ? -15.122 29.675 65.411  1.00 28.24  ? 361 GLU A N   1 
ATOM   3050 C CA  . GLU A 1 361 ? -16.578 29.711 65.507  1.00 31.66  ? 361 GLU A CA  1 
ATOM   3051 C C   . GLU A 1 361 ? -17.160 28.333 65.216  1.00 24.66  ? 361 GLU A C   1 
ATOM   3052 O O   . GLU A 1 361 ? -16.737 27.647 64.283  1.00 21.07  ? 361 GLU A O   1 
ATOM   3053 C CB  . GLU A 1 361 ? -17.176 30.731 64.532  1.00 39.32  ? 361 GLU A CB  1 
ATOM   3054 C CG  . GLU A 1 361 ? -16.391 32.021 64.379  1.00 54.37  ? 361 GLU A CG  1 
ATOM   3055 C CD  . GLU A 1 361 ? -15.321 31.922 63.308  1.00 65.61  ? 361 GLU A CD  1 
ATOM   3056 O OE1 . GLU A 1 361 ? -14.340 31.190 63.538  1.00 61.56  ? 361 GLU A OE1 1 
ATOM   3057 O OE2 . GLU A 1 361 ? -15.462 32.571 62.243  1.00 70.44  ? 361 GLU A OE2 1 
ATOM   3058 N N   . GLU A 1 362 ? -18.140 27.942 66.030  1.00 25.06  ? 362 GLU A N   1 
ATOM   3059 C CA  . GLU A 1 362 ? -18.846 26.680 65.866  1.00 32.07  ? 362 GLU A CA  1 
ATOM   3060 C C   . GLU A 1 362 ? -17.861 25.513 65.818  1.00 23.70  ? 362 GLU A C   1 
ATOM   3061 O O   . GLU A 1 362 ? -17.996 24.594 65.011  1.00 21.84  ? 362 GLU A O   1 
ATOM   3062 C CB  . GLU A 1 362 ? -19.735 26.705 64.623  1.00 40.60  ? 362 GLU A CB  1 
ATOM   3063 C CG  . GLU A 1 362 ? -20.828 27.768 64.656  1.00 52.56  ? 362 GLU A CG  1 
ATOM   3064 C CD  . GLU A 1 362 ? -22.150 27.219 65.145  1.00 63.11  ? 362 GLU A CD  1 
ATOM   3065 O OE1 . GLU A 1 362 ? -22.652 27.706 66.184  1.00 66.32  ? 362 GLU A OE1 1 
ATOM   3066 O OE2 . GLU A 1 362 ? -22.682 26.294 64.489  1.00 68.81  ? 362 GLU A OE2 1 
ATOM   3067 N N   . ASN A 1 363 ? -16.840 25.576 66.674  1.00 22.86  ? 363 ASN A N   1 
ATOM   3068 C CA  . ASN A 1 363 ? -15.925 24.452 66.895  1.00 22.13  ? 363 ASN A CA  1 
ATOM   3069 C C   . ASN A 1 363 ? -15.227 24.021 65.602  1.00 23.33  ? 363 ASN A C   1 
ATOM   3070 O O   . ASN A 1 363 ? -14.974 22.828 65.375  1.00 24.36  ? 363 ASN A O   1 
ATOM   3071 C CB  . ASN A 1 363 ? -16.670 23.275 67.531  1.00 22.46  ? 363 ASN A CB  1 
ATOM   3072 C CG  . ASN A 1 363 ? -15.740 22.224 68.063  1.00 24.11  ? 363 ASN A CG  1 
ATOM   3073 O OD1 . ASN A 1 363 ? -14.664 22.537 68.570  1.00 25.55  ? 363 ASN A OD1 1 
ATOM   3074 N ND2 . ASN A 1 363 ? -16.133 20.965 67.929  1.00 21.73  ? 363 ASN A ND2 1 
ATOM   3075 N N   . GLY A 1 364 ? -14.933 24.986 64.734  1.00 22.34  ? 364 GLY A N   1 
ATOM   3076 C CA  . GLY A 1 364 ? -14.239 24.737 63.487  1.00 21.02  ? 364 GLY A CA  1 
ATOM   3077 C C   . GLY A 1 364 ? -15.046 24.036 62.424  1.00 20.19  ? 364 GLY A C   1 
ATOM   3078 O O   . GLY A 1 364 ? -14.500 23.718 61.364  1.00 21.73  ? 364 GLY A O   1 
ATOM   3079 N N   . ILE A 1 365 ? -16.333 23.800 62.656  1.00 19.49  ? 365 ILE A N   1 
ATOM   3080 C CA  . ILE A 1 365 ? -17.117 22.967 61.754  1.00 18.61  ? 365 ILE A CA  1 
ATOM   3081 C C   . ILE A 1 365 ? -17.357 23.713 60.441  1.00 24.94  ? 365 ILE A C   1 
ATOM   3082 O O   . ILE A 1 365 ? -17.139 23.128 59.368  1.00 23.22  ? 365 ILE A O   1 
ATOM   3083 C CB  . ILE A 1 365 ? -18.410 22.501 62.451  1.00 22.89  ? 365 ILE A CB  1 
ATOM   3084 C CG1 . ILE A 1 365 ? -18.062 21.404 63.469  1.00 21.37  ? 365 ILE A CG1 1 
ATOM   3085 C CG2 . ILE A 1 365 ? -19.438 21.993 61.441  1.00 20.64  ? 365 ILE A CG2 1 
ATOM   3086 C CD1 . ILE A 1 365 ? -19.037 21.289 64.642  1.00 22.54  ? 365 ILE A CD1 1 
ATOM   3087 N N   . PRO A 1 366 ? -17.744 25.001 60.447  1.00 25.10  ? 366 PRO A N   1 
ATOM   3088 C CA  . PRO A 1 366 ? -17.869 25.700 59.155  1.00 21.41  ? 366 PRO A CA  1 
ATOM   3089 C C   . PRO A 1 366 ? -16.570 25.719 58.374  1.00 23.09  ? 366 PRO A C   1 
ATOM   3090 O O   . PRO A 1 366 ? -16.577 25.474 57.157  1.00 20.19  ? 366 PRO A O   1 
ATOM   3091 C CB  . PRO A 1 366 ? -18.331 27.105 59.567  1.00 25.83  ? 366 PRO A CB  1 
ATOM   3092 C CG  . PRO A 1 366 ? -19.054 26.882 60.828  1.00 25.78  ? 366 PRO A CG  1 
ATOM   3093 C CD  . PRO A 1 366 ? -18.264 25.833 61.545  1.00 25.48  ? 366 PRO A CD  1 
ATOM   3094 N N   . PHE A 1 367 ? -15.440 25.934 59.053  1.00 25.40  ? 367 PHE A N   1 
ATOM   3095 C CA  . PHE A 1 367 ? -14.163 25.958 58.353  1.00 27.57  ? 367 PHE A CA  1 
ATOM   3096 C C   . PHE A 1 367 ? -13.861 24.603 57.715  1.00 21.46  ? 367 PHE A C   1 
ATOM   3097 O O   . PHE A 1 367 ? -13.604 24.521 56.509  1.00 22.52  ? 367 PHE A O   1 
ATOM   3098 C CB  . PHE A 1 367 ? -13.037 26.380 59.297  1.00 28.58  ? 367 PHE A CB  1 
ATOM   3099 C CG  . PHE A 1 367 ? -11.667 26.206 58.702  1.00 26.27  ? 367 PHE A CG  1 
ATOM   3100 C CD1 . PHE A 1 367 ? -11.188 27.107 57.754  1.00 22.65  ? 367 PHE A CD1 1 
ATOM   3101 C CD2 . PHE A 1 367 ? -10.864 25.125 59.071  1.00 20.06  ? 367 PHE A CD2 1 
ATOM   3102 C CE1 . PHE A 1 367 ? -9.930  26.940 57.190  1.00 26.77  ? 367 PHE A CE1 1 
ATOM   3103 C CE2 . PHE A 1 367 ? -9.607  24.954 58.510  1.00 19.38  ? 367 PHE A CE2 1 
ATOM   3104 C CZ  . PHE A 1 367 ? -9.138  25.853 57.567  1.00 21.13  ? 367 PHE A CZ  1 
ATOM   3105 N N   . LEU A 1 368 ? -13.917 23.524 58.501  1.00 16.63  ? 368 LEU A N   1 
ATOM   3106 C CA  . LEU A 1 368 ? -13.528 22.213 57.987  1.00 19.62  ? 368 LEU A CA  1 
ATOM   3107 C C   . LEU A 1 368 ? -14.510 21.698 56.936  1.00 21.03  ? 368 LEU A C   1 
ATOM   3108 O O   . LEU A 1 368 ? -14.093 21.065 55.963  1.00 18.20  ? 368 LEU A O   1 
ATOM   3109 C CB  . LEU A 1 368 ? -13.391 21.205 59.138  1.00 19.77  ? 368 LEU A CB  1 
ATOM   3110 C CG  . LEU A 1 368 ? -12.111 21.289 59.992  1.00 20.15  ? 368 LEU A CG  1 
ATOM   3111 C CD1 . LEU A 1 368 ? -12.037 20.144 61.025  1.00 17.80  ? 368 LEU A CD1 1 
ATOM   3112 C CD2 . LEU A 1 368 ? -10.824 21.326 59.147  1.00 19.86  ? 368 LEU A CD2 1 
ATOM   3113 N N   . GLU A 1 369 ? -15.817 21.939 57.110  1.00 22.51  ? 369 GLU A N   1 
ATOM   3114 C CA  . GLU A 1 369 ? -16.770 21.505 56.088  1.00 20.96  ? 369 GLU A CA  1 
ATOM   3115 C C   . GLU A 1 369 ? -16.549 22.260 54.780  1.00 22.63  ? 369 GLU A C   1 
ATOM   3116 O O   . GLU A 1 369 ? -16.621 21.667 53.699  1.00 22.84  ? 369 GLU A O   1 
ATOM   3117 C CB  . GLU A 1 369 ? -18.210 21.681 56.588  1.00 22.20  ? 369 GLU A CB  1 
ATOM   3118 C CG  . GLU A 1 369 ? -18.535 20.778 57.775  1.00 21.94  ? 369 GLU A CG  1 
ATOM   3119 C CD  . GLU A 1 369 ? -20.013 20.736 58.120  1.00 25.48  ? 369 GLU A CD  1 
ATOM   3120 O OE1 . GLU A 1 369 ? -20.759 21.650 57.722  1.00 24.09  ? 369 GLU A OE1 1 
ATOM   3121 O OE2 . GLU A 1 369 ? -20.431 19.772 58.793  1.00 26.70  ? 369 GLU A OE2 1 
ATOM   3122 N N   . LYS A 1 370 ? -16.249 23.559 54.857  1.00 21.05  ? 370 LYS A N   1 
ATOM   3123 C CA  . LYS A 1 370 ? -15.962 24.325 53.643  1.00 24.29  ? 370 LYS A CA  1 
ATOM   3124 C C   . LYS A 1 370 ? -14.608 23.942 53.057  1.00 27.38  ? 370 LYS A C   1 
ATOM   3125 O O   . LYS A 1 370 ? -14.452 23.870 51.830  1.00 23.08  ? 370 LYS A O   1 
ATOM   3126 C CB  . LYS A 1 370 ? -16.005 25.825 53.931  1.00 33.00  ? 370 LYS A CB  1 
ATOM   3127 C CG  . LYS A 1 370 ? -17.403 26.390 54.127  1.00 42.83  ? 370 LYS A CG  1 
ATOM   3128 C CD  . LYS A 1 370 ? -17.372 27.911 54.320  1.00 48.59  ? 370 LYS A CD  1 
ATOM   3129 C CE  . LYS A 1 370 ? -18.384 28.366 55.378  1.00 51.58  ? 370 LYS A CE  1 
ATOM   3130 N NZ  . LYS A 1 370 ? -19.801 28.218 54.931  1.00 51.71  ? 370 LYS A NZ  1 
ATOM   3131 N N   . LEU A 1 371 ? -13.614 23.692 53.915  1.00 23.90  ? 371 LEU A N   1 
ATOM   3132 C CA  . LEU A 1 371 ? -12.300 23.293 53.416  1.00 25.79  ? 371 LEU A CA  1 
ATOM   3133 C C   . LEU A 1 371 ? -12.370 21.933 52.734  1.00 28.48  ? 371 LEU A C   1 
ATOM   3134 O O   . LEU A 1 371 ? -11.883 21.761 51.610  1.00 21.57  ? 371 LEU A O   1 
ATOM   3135 C CB  . LEU A 1 371 ? -11.286 23.269 54.559  1.00 23.31  ? 371 LEU A CB  1 
ATOM   3136 C CG  . LEU A 1 371 ? -9.943  22.604 54.239  1.00 24.09  ? 371 LEU A CG  1 
ATOM   3137 C CD1 . LEU A 1 371 ? -9.183  23.403 53.176  1.00 21.52  ? 371 LEU A CD1 1 
ATOM   3138 C CD2 . LEU A 1 371 ? -9.097  22.445 55.495  1.00 21.32  ? 371 LEU A CD2 1 
ATOM   3139 N N   . TYR A 1 372 ? -12.984 20.953 53.397  1.00 25.22  ? 372 TYR A N   1 
ATOM   3140 C CA  . TYR A 1 372 ? -13.002 19.604 52.847  1.00 21.55  ? 372 TYR A CA  1 
ATOM   3141 C C   . TYR A 1 372 ? -13.901 19.513 51.612  1.00 26.72  ? 372 TYR A C   1 
ATOM   3142 O O   . TYR A 1 372 ? -13.594 18.775 50.669  1.00 23.02  ? 372 TYR A O   1 
ATOM   3143 C CB  . TYR A 1 372 ? -13.453 18.623 53.917  1.00 17.90  ? 372 TYR A CB  1 
ATOM   3144 C CG  . TYR A 1 372 ? -12.479 18.411 55.065  1.00 18.78  ? 372 TYR A CG  1 
ATOM   3145 C CD1 . TYR A 1 372 ? -11.103 18.695 54.939  1.00 19.63  ? 372 TYR A CD1 1 
ATOM   3146 C CD2 . TYR A 1 372 ? -12.936 17.911 56.270  1.00 17.90  ? 372 TYR A CD2 1 
ATOM   3147 C CE1 . TYR A 1 372 ? -10.228 18.467 56.005  1.00 17.51  ? 372 TYR A CE1 1 
ATOM   3148 C CE2 . TYR A 1 372 ? -12.082 17.684 57.321  1.00 18.43  ? 372 TYR A CE2 1 
ATOM   3149 C CZ  . TYR A 1 372 ? -10.738 17.961 57.189  1.00 20.22  ? 372 TYR A CZ  1 
ATOM   3150 O OH  . TYR A 1 372 ? -9.946  17.715 58.269  1.00 21.46  ? 372 TYR A OH  1 
ATOM   3151 N N   . SER A 1 373 ? -15.010 20.258 51.596  1.00 24.35  ? 373 SER A N   1 
ATOM   3152 C CA  . SER A 1 373 ? -15.871 20.276 50.415  1.00 26.49  ? 373 SER A CA  1 
ATOM   3153 C C   . SER A 1 373 ? -15.181 20.933 49.230  1.00 32.89  ? 373 SER A C   1 
ATOM   3154 O O   . SER A 1 373 ? -15.409 20.545 48.078  1.00 32.72  ? 373 SER A O   1 
ATOM   3155 C CB  . SER A 1 373 ? -17.168 21.019 50.724  1.00 25.78  ? 373 SER A CB  1 
ATOM   3156 O OG  . SER A 1 373 ? -17.823 21.374 49.527  1.00 33.11  ? 373 SER A OG  1 
ATOM   3157 N N   . THR A 1 374 ? -14.353 21.939 49.495  1.00 26.03  ? 374 THR A N   1 
ATOM   3158 C CA  . THR A 1 374 ? -13.615 22.599 48.427  1.00 28.99  ? 374 THR A CA  1 
ATOM   3159 C C   . THR A 1 374 ? -12.504 21.699 47.910  1.00 27.74  ? 374 THR A C   1 
ATOM   3160 O O   . THR A 1 374 ? -12.322 21.554 46.697  1.00 30.88  ? 374 THR A O   1 
ATOM   3161 C CB  . THR A 1 374 ? -13.035 23.922 48.939  1.00 25.61  ? 374 THR A CB  1 
ATOM   3162 O OG1 . THR A 1 374 ? -14.090 24.748 49.441  1.00 23.78  ? 374 THR A OG1 1 
ATOM   3163 C CG2 . THR A 1 374 ? -12.279 24.650 47.840  1.00 30.16  ? 374 THR A CG2 1 
ATOM   3164 N N   . LEU A 1 375 ? -11.745 21.093 48.826  1.00 24.45  ? 375 LEU A N   1 
ATOM   3165 C CA  . LEU A 1 375 ? -10.629 20.239 48.429  1.00 23.39  ? 375 LEU A CA  1 
ATOM   3166 C C   . LEU A 1 375 ? -11.101 19.110 47.534  1.00 21.38  ? 375 LEU A C   1 
ATOM   3167 O O   . LEU A 1 375 ? -10.498 18.833 46.491  1.00 30.13  ? 375 LEU A O   1 
ATOM   3168 C CB  . LEU A 1 375 ? -9.935  19.665 49.666  1.00 23.52  ? 375 LEU A CB  1 
ATOM   3169 C CG  . LEU A 1 375 ? -9.067  20.642 50.450  1.00 24.16  ? 375 LEU A CG  1 
ATOM   3170 C CD1 . LEU A 1 375 ? -8.571  19.973 51.724  1.00 24.73  ? 375 LEU A CD1 1 
ATOM   3171 C CD2 . LEU A 1 375 ? -7.913  21.124 49.585  1.00 27.76  ? 375 LEU A CD2 1 
ATOM   3172 N N   . GLU A 1 376 ? -12.201 18.470 47.918  1.00 24.38  ? 376 GLU A N   1 
ATOM   3173 C CA  . GLU A 1 376 ? -12.721 17.311 47.219  1.00 25.55  ? 376 GLU A CA  1 
ATOM   3174 C C   . GLU A 1 376 ? -13.177 17.642 45.802  1.00 28.57  ? 376 GLU A C   1 
ATOM   3175 O O   . GLU A 1 376 ? -13.265 16.737 44.968  1.00 31.44  ? 376 GLU A O   1 
ATOM   3176 C CB  . GLU A 1 376 ? -13.828 16.730 48.094  1.00 31.02  ? 376 GLU A CB  1 
ATOM   3177 C CG  . GLU A 1 376 ? -15.056 16.197 47.444  1.00 40.78  ? 376 GLU A CG  1 
ATOM   3178 C CD  . GLU A 1 376 ? -16.085 15.819 48.497  1.00 42.96  ? 376 GLU A CD  1 
ATOM   3179 O OE1 . GLU A 1 376 ? -17.037 16.604 48.709  1.00 40.60  ? 376 GLU A OE1 1 
ATOM   3180 O OE2 . GLU A 1 376 ? -15.926 14.752 49.128  1.00 45.43  ? 376 GLU A OE2 1 
ATOM   3181 N N   . LYS A 1 377 ? -13.420 18.914 45.492  1.00 26.16  ? 377 LYS A N   1 
ATOM   3182 C CA  . LYS A 1 377 ? -13.824 19.306 44.148  1.00 29.13  ? 377 LYS A CA  1 
ATOM   3183 C C   . LYS A 1 377 ? -12.690 19.916 43.333  1.00 33.39  ? 377 LYS A C   1 
ATOM   3184 O O   . LYS A 1 377 ? -12.893 20.217 42.151  1.00 36.17  ? 377 LYS A O   1 
ATOM   3185 C CB  . LYS A 1 377 ? -15.004 20.283 44.217  1.00 28.13  ? 377 LYS A CB  1 
ATOM   3186 C CG  . LYS A 1 377 ? -16.281 19.640 44.742  1.00 30.38  ? 377 LYS A CG  1 
ATOM   3187 C CD  . LYS A 1 377 ? -17.326 20.670 45.159  1.00 31.95  ? 377 LYS A CD  1 
ATOM   3188 C CE  . LYS A 1 377 ? -18.198 20.137 46.308  1.00 38.48  ? 377 LYS A CE  1 
ATOM   3189 N NZ  . LYS A 1 377 ? -19.618 19.944 45.901  1.00 44.26  ? 377 LYS A NZ  1 
ATOM   3190 N N   . GLU A 1 378 ? -11.504 20.095 43.915  1.00 26.67  ? 378 GLU A N   1 
ATOM   3191 C CA  . GLU A 1 378 ? -10.362 20.642 43.178  1.00 36.25  ? 378 GLU A CA  1 
ATOM   3192 C C   . GLU A 1 378 ? -9.668  19.507 42.436  1.00 34.74  ? 378 GLU A C   1 
ATOM   3193 O O   . GLU A 1 378 ? -8.968  18.689 43.035  1.00 36.30  ? 378 GLU A O   1 
ATOM   3194 C CB  . GLU A 1 378 ? -9.389  21.370 44.103  1.00 42.45  ? 378 GLU A CB  1 
ATOM   3195 C CG  . GLU A 1 378 ? -9.953  22.608 44.796  1.00 49.63  ? 378 GLU A CG  1 
ATOM   3196 C CD  . GLU A 1 378 ? -10.181 23.781 43.853  1.00 62.32  ? 378 GLU A CD  1 
ATOM   3197 O OE1 . GLU A 1 378 ? -9.805  23.692 42.662  1.00 66.65  ? 378 GLU A OE1 1 
ATOM   3198 O OE2 . GLU A 1 378 ? -10.758 24.794 44.305  1.00 67.08  ? 378 GLU A OE2 1 
ATOM   3199 N N   . GLU A 1 379 ? -9.857  19.484 41.114  1.00 44.56  ? 379 GLU A N   1 
ATOM   3200 C CA  . GLU A 1 379 ? -9.265  18.491 40.214  1.00 50.36  ? 379 GLU A CA  1 
ATOM   3201 C C   . GLU A 1 379 ? -7.761  18.298 40.408  1.00 43.63  ? 379 GLU A C   1 
ATOM   3202 O O   . GLU A 1 379 ? -7.253  17.170 40.417  1.00 44.39  ? 379 GLU A O   1 
ATOM   3203 C CB  . GLU A 1 379 ? -9.555  18.930 38.776  1.00 60.49  ? 379 GLU A CB  1 
ATOM   3204 C CG  . GLU A 1 379 ? -8.882  18.120 37.685  1.00 71.89  ? 379 GLU A CG  1 
ATOM   3205 C CD  . GLU A 1 379 ? -9.621  18.222 36.361  1.00 78.86  ? 379 GLU A CD  1 
ATOM   3206 O OE1 . GLU A 1 379 ? -9.916  17.168 35.760  1.00 80.77  ? 379 GLU A OE1 1 
ATOM   3207 O OE2 . GLU A 1 379 ? -9.908  19.359 35.924  1.00 82.55  ? 379 GLU A OE2 1 
ATOM   3208 N N   . TRP A 1 380 ? -7.032  19.396 40.536  1.00 35.88  ? 380 TRP A N   1 
ATOM   3209 C CA  . TRP A 1 380 ? -5.578  19.365 40.529  1.00 33.11  ? 380 TRP A CA  1 
ATOM   3210 C C   . TRP A 1 380 ? -4.984  19.036 41.895  1.00 33.36  ? 380 TRP A C   1 
ATOM   3211 O O   . TRP A 1 380 ? -3.754  18.921 42.000  1.00 30.62  ? 380 TRP A O   1 
ATOM   3212 C CB  . TRP A 1 380 ? -5.047  20.713 40.040  1.00 31.46  ? 380 TRP A CB  1 
ATOM   3213 C CG  . TRP A 1 380 ? -5.672  21.854 40.762  1.00 28.78  ? 380 TRP A CG  1 
ATOM   3214 C CD1 . TRP A 1 380 ? -6.889  22.411 40.515  1.00 32.92  ? 380 TRP A CD1 1 
ATOM   3215 C CD2 . TRP A 1 380 ? -5.122  22.570 41.877  1.00 30.75  ? 380 TRP A CD2 1 
ATOM   3216 N NE1 . TRP A 1 380 ? -7.124  23.442 41.391  1.00 35.64  ? 380 TRP A NE1 1 
ATOM   3217 C CE2 . TRP A 1 380 ? -6.055  23.556 42.240  1.00 30.96  ? 380 TRP A CE2 1 
ATOM   3218 C CE3 . TRP A 1 380 ? -3.922  22.481 42.591  1.00 29.44  ? 380 TRP A CE3 1 
ATOM   3219 C CZ2 . TRP A 1 380 ? -5.832  24.441 43.292  1.00 26.75  ? 380 TRP A CZ2 1 
ATOM   3220 C CZ3 . TRP A 1 380 ? -3.704  23.363 43.637  1.00 22.68  ? 380 TRP A CZ3 1 
ATOM   3221 C CH2 . TRP A 1 380 ? -4.650  24.323 43.979  1.00 23.33  ? 380 TRP A CH2 1 
ATOM   3222 N N   . ILE A 1 381 ? -5.818  18.878 42.929  1.00 23.52  ? 381 ILE A N   1 
ATOM   3223 C CA  . ILE A 1 381 ? -5.380  18.466 44.259  1.00 25.21  ? 381 ILE A CA  1 
ATOM   3224 C C   . ILE A 1 381 ? -5.745  17.002 44.461  1.00 28.53  ? 381 ILE A C   1 
ATOM   3225 O O   . ILE A 1 381 ? -6.890  16.602 44.217  1.00 33.24  ? 381 ILE A O   1 
ATOM   3226 C CB  . ILE A 1 381 ? -6.024  19.333 45.356  1.00 21.10  ? 381 ILE A CB  1 
ATOM   3227 C CG1 . ILE A 1 381 ? -5.576  20.784 45.246  1.00 26.72  ? 381 ILE A CG1 1 
ATOM   3228 C CG2 . ILE A 1 381 ? -5.670  18.799 46.740  1.00 22.18  ? 381 ILE A CG2 1 
ATOM   3229 C CD1 . ILE A 1 381 ? -6.142  21.661 46.349  1.00 28.34  ? 381 ILE A CD1 1 
ATOM   3230 N N   . GLU A 1 382 ? -4.788  16.206 44.926  1.00 26.04  ? 382 GLU A N   1 
ATOM   3231 C CA  . GLU A 1 382 ? -5.047  14.832 45.349  1.00 21.85  ? 382 GLU A CA  1 
ATOM   3232 C C   . GLU A 1 382 ? -4.565  14.685 46.786  1.00 22.53  ? 382 GLU A C   1 
ATOM   3233 O O   . GLU A 1 382 ? -3.355  14.678 47.043  1.00 21.54  ? 382 GLU A O   1 
ATOM   3234 C CB  . GLU A 1 382 ? -4.358  13.828 44.418  1.00 28.52  ? 382 GLU A CB  1 
ATOM   3235 C CG  . GLU A 1 382 ? -4.527  12.365 44.831  1.00 38.81  ? 382 GLU A CG  1 
ATOM   3236 C CD  . GLU A 1 382 ? -3.842  11.385 43.873  1.00 54.42  ? 382 GLU A CD  1 
ATOM   3237 O OE1 . GLU A 1 382 ? -3.687  11.726 42.678  1.00 57.66  ? 382 GLU A OE1 1 
ATOM   3238 O OE2 . GLU A 1 382 ? -3.454  10.275 44.312  1.00 57.94  ? 382 GLU A OE2 1 
ATOM   3239 N N   . THR A 1 383 ? -5.503  14.595 47.726  1.00 21.19  ? 383 THR A N   1 
ATOM   3240 C CA  . THR A 1 383 ? -5.144  14.226 49.087  1.00 22.45  ? 383 THR A CA  1 
ATOM   3241 C C   . THR A 1 383 ? -4.709  12.765 49.137  1.00 23.00  ? 383 THR A C   1 
ATOM   3242 O O   . THR A 1 383 ? -5.170  11.923 48.360  1.00 25.07  ? 383 THR A O   1 
ATOM   3243 C CB  . THR A 1 383 ? -6.310  14.468 50.047  1.00 23.77  ? 383 THR A CB  1 
ATOM   3244 O OG1 . THR A 1 383 ? -7.455  13.719 49.609  1.00 26.89  ? 383 THR A OG1 1 
ATOM   3245 C CG2 . THR A 1 383 ? -6.650  15.960 50.102  1.00 22.51  ? 383 THR A CG2 1 
ATOM   3246 N N   . LEU A 1 384 ? -3.773  12.475 50.036  1.00 18.12  ? 384 LEU A N   1 
ATOM   3247 C CA  . LEU A 1 384 ? -3.097  11.189 50.078  1.00 19.88  ? 384 LEU A CA  1 
ATOM   3248 C C   . LEU A 1 384 ? -3.106  10.626 51.491  1.00 21.16  ? 384 LEU A C   1 
ATOM   3249 O O   . LEU A 1 384 ? -2.930  11.370 52.461  1.00 19.66  ? 384 LEU A O   1 
ATOM   3250 C CB  . LEU A 1 384 ? -1.648  11.324 49.596  1.00 19.74  ? 384 LEU A CB  1 
ATOM   3251 C CG  . LEU A 1 384 ? -1.375  11.824 48.178  1.00 22.46  ? 384 LEU A CG  1 
ATOM   3252 C CD1 . LEU A 1 384 ? 0.108   11.709 47.900  1.00 20.87  ? 384 LEU A CD1 1 
ATOM   3253 C CD2 . LEU A 1 384 ? -2.166  11.028 47.148  1.00 21.00  ? 384 LEU A CD2 1 
ATOM   3254 N N   . THR A 1 385 ? -3.321  9.313  51.605  1.00 17.26  ? 385 THR A N   1 
ATOM   3255 C CA  . THR A 1 385 ? -2.980  8.634  52.846  1.00 15.35  ? 385 THR A CA  1 
ATOM   3256 C C   . THR A 1 385 ? -1.468  8.655  53.023  1.00 15.10  ? 385 THR A C   1 
ATOM   3257 O O   . THR A 1 385 ? -0.716  8.877  52.073  1.00 17.75  ? 385 THR A O   1 
ATOM   3258 C CB  . THR A 1 385 ? -3.463  7.173  52.856  1.00 16.38  ? 385 THR A CB  1 
ATOM   3259 O OG1 . THR A 1 385 ? -2.638  6.401  51.976  1.00 22.41  ? 385 THR A OG1 1 
ATOM   3260 C CG2 . THR A 1 385 ? -4.932  7.043  52.405  1.00 16.49  ? 385 THR A CG2 1 
ATOM   3261 N N   . LEU A 1 386 ? -1.019  8.417  54.262  1.00 16.56  ? 386 LEU A N   1 
ATOM   3262 C CA  . LEU A 1 386 ? 0.418   8.305  54.491  1.00 21.38  ? 386 LEU A CA  1 
ATOM   3263 C C   . LEU A 1 386 ? 1.020   7.195  53.631  1.00 23.56  ? 386 LEU A C   1 
ATOM   3264 O O   . LEU A 1 386 ? 2.135   7.340  53.119  1.00 20.81  ? 386 LEU A O   1 
ATOM   3265 C CB  . LEU A 1 386 ? 0.717   8.056  55.970  1.00 18.36  ? 386 LEU A CB  1 
ATOM   3266 C CG  . LEU A 1 386 ? 0.211   9.039  57.034  1.00 20.66  ? 386 LEU A CG  1 
ATOM   3267 C CD1 . LEU A 1 386 ? 0.588   8.566  58.425  1.00 21.20  ? 386 LEU A CD1 1 
ATOM   3268 C CD2 . LEU A 1 386 ? 0.776   10.431 56.792  1.00 20.34  ? 386 LEU A CD2 1 
ATOM   3269 N N   . GLU A 1 387 ? 0.305   6.077  53.474  1.00 25.56  ? 387 GLU A N   1 
ATOM   3270 C CA  . GLU A 1 387 ? 0.816   4.975  52.659  1.00 26.33  ? 387 GLU A CA  1 
ATOM   3271 C C   . GLU A 1 387 ? 1.041   5.413  51.220  1.00 19.71  ? 387 GLU A C   1 
ATOM   3272 O O   . GLU A 1 387 ? 2.066   5.086  50.607  1.00 23.86  ? 387 GLU A O   1 
ATOM   3273 C CB  . GLU A 1 387 ? -0.146  3.785  52.695  1.00 32.78  ? 387 GLU A CB  1 
ATOM   3274 C CG  . GLU A 1 387 ? 0.397   2.553  51.980  1.00 39.22  ? 387 GLU A CG  1 
ATOM   3275 C CD  . GLU A 1 387 ? -0.680  1.540  51.633  1.00 53.44  ? 387 GLU A CD  1 
ATOM   3276 O OE1 . GLU A 1 387 ? -0.362  0.333  51.574  1.00 60.27  ? 387 GLU A OE1 1 
ATOM   3277 O OE2 . GLU A 1 387 ? -1.841  1.949  51.413  1.00 58.39  ? 387 GLU A OE2 1 
ATOM   3278 N N   . GLU A 1 388 ? 0.078   6.140  50.660  1.00 19.67  ? 388 GLU A N   1 
ATOM   3279 C CA  . GLU A 1 388 ? 0.214   6.622  49.292  1.00 22.77  ? 388 GLU A CA  1 
ATOM   3280 C C   . GLU A 1 388 ? 1.367   7.609  49.173  1.00 23.95  ? 388 GLU A C   1 
ATOM   3281 O O   . GLU A 1 388 ? 2.154   7.539  48.225  1.00 27.88  ? 388 GLU A O   1 
ATOM   3282 C CB  . GLU A 1 388 ? -1.101  7.252  48.832  1.00 23.84  ? 388 GLU A CB  1 
ATOM   3283 C CG  . GLU A 1 388 ? -2.205  6.222  48.553  1.00 25.16  ? 388 GLU A CG  1 
ATOM   3284 C CD  . GLU A 1 388 ? -3.582  6.858  48.435  1.00 30.70  ? 388 GLU A CD  1 
ATOM   3285 O OE1 . GLU A 1 388 ? -3.773  7.965  48.962  1.00 26.69  ? 388 GLU A OE1 1 
ATOM   3286 O OE2 . GLU A 1 388 ? -4.478  6.245  47.815  1.00 36.97  ? 388 GLU A OE2 1 
ATOM   3287 N N   . ALA A 1 389 ? 1.493   8.535  50.130  1.00 27.02  ? 389 ALA A N   1 
ATOM   3288 C CA  . ALA A 1 389 ? 2.612   9.474  50.089  1.00 18.55  ? 389 ALA A CA  1 
ATOM   3289 C C   . ALA A 1 389 ? 3.947   8.753  50.204  1.00 22.78  ? 389 ALA A C   1 
ATOM   3290 O O   . ALA A 1 389 ? 4.933   9.160  49.577  1.00 28.65  ? 389 ALA A O   1 
ATOM   3291 C CB  . ALA A 1 389 ? 2.486   10.507 51.209  1.00 15.54  ? 389 ALA A CB  1 
ATOM   3292 N N   . MET A 1 390 ? 4.000   7.688  51.009  1.00 27.53  ? 390 MET A N   1 
ATOM   3293 C CA  . MET A 1 390 ? 5.228   6.915  51.154  1.00 28.43  ? 390 MET A CA  1 
ATOM   3294 C C   . MET A 1 390 ? 5.588   6.189  49.862  1.00 33.21  ? 390 MET A C   1 
ATOM   3295 O O   . MET A 1 390 ? 6.763   6.151  49.478  1.00 33.12  ? 390 MET A O   1 
ATOM   3296 C CB  . MET A 1 390 ? 5.089   5.925  52.310  1.00 26.22  ? 390 MET A CB  1 
ATOM   3297 C CG  . MET A 1 390 ? 6.313   5.037  52.500  1.00 37.46  ? 390 MET A CG  1 
ATOM   3298 S SD  . MET A 1 390 ? 6.276   3.983  53.976  1.00 45.39  ? 390 MET A SD  1 
ATOM   3299 C CE  . MET A 1 390 ? 5.296   2.594  53.403  1.00 45.94  ? 390 MET A CE  1 
ATOM   3300 N N   . ARG A 1 391 ? 4.601   5.617  49.172  1.00 26.50  ? 391 ARG A N   1 
ATOM   3301 C CA  . ARG A 1 391 ? 4.867   4.784  48.002  1.00 33.41  ? 391 ARG A CA  1 
ATOM   3302 C C   . ARG A 1 391 ? 4.695   5.528  46.680  1.00 34.08  ? 391 ARG A C   1 
ATOM   3303 O O   . ARG A 1 391 ? 4.859   4.921  45.615  1.00 35.49  ? 391 ARG A O   1 
ATOM   3304 C CB  . ARG A 1 391 ? 3.964   3.538  48.022  1.00 33.02  ? 391 ARG A CB  1 
ATOM   3305 C CG  . ARG A 1 391 ? 4.002   2.764  49.345  1.00 39.06  ? 391 ARG A CG  1 
ATOM   3306 C CD  . ARG A 1 391 ? 3.349   1.390  49.248  1.00 48.64  ? 391 ARG A CD  1 
ATOM   3307 N NE  . ARG A 1 391 ? 4.165   0.360  49.892  1.00 61.39  ? 391 ARG A NE  1 
ATOM   3308 C CZ  . ARG A 1 391 ? 3.796   -0.339 50.964  1.00 67.89  ? 391 ARG A CZ  1 
ATOM   3309 N NH1 . ARG A 1 391 ? 2.612   -0.130 51.528  1.00 67.50  ? 391 ARG A NH1 1 
ATOM   3310 N NH2 . ARG A 1 391 ? 4.615   -1.253 51.472  1.00 69.11  ? 391 ARG A NH2 1 
ATOM   3311 N N   . LYS A 1 392 ? 4.405   6.823  46.719  1.00 27.77  ? 392 LYS A N   1 
ATOM   3312 C CA  . LYS A 1 392 ? 4.139   7.577  45.499  1.00 31.89  ? 392 LYS A CA  1 
ATOM   3313 C C   . LYS A 1 392 ? 5.369   7.597  44.600  1.00 35.07  ? 392 LYS A C   1 
ATOM   3314 O O   . LYS A 1 392 ? 6.446   8.032  45.017  1.00 32.06  ? 392 LYS A O   1 
ATOM   3315 C CB  . LYS A 1 392 ? 3.716   8.999  45.858  1.00 33.23  ? 392 LYS A CB  1 
ATOM   3316 C CG  . LYS A 1 392 ? 2.959   9.711  44.752  1.00 41.34  ? 392 LYS A CG  1 
ATOM   3317 C CD  . LYS A 1 392 ? 1.562   9.147  44.586  1.00 48.26  ? 392 LYS A CD  1 
ATOM   3318 C CE  . LYS A 1 392 ? 0.588   10.233 44.203  1.00 57.02  ? 392 LYS A CE  1 
ATOM   3319 N NZ  . LYS A 1 392 ? -0.702  9.653  43.743  1.00 63.04  ? 392 LYS A NZ  1 
ATOM   3320 N N   . GLU A 1 393 ? 5.208   7.121  43.364  1.00 38.90  ? 393 GLU A N   1 
ATOM   3321 C CA  . GLU A 1 393 ? 6.323   7.051  42.425  1.00 41.51  ? 393 GLU A CA  1 
ATOM   3322 C C   . GLU A 1 393 ? 6.568   8.371  41.699  1.00 35.83  ? 393 GLU A C   1 
ATOM   3323 O O   . GLU A 1 393 ? 7.723   8.734  41.452  1.00 39.15  ? 393 GLU A O   1 
ATOM   3324 C CB  . GLU A 1 393 ? 6.081   5.933  41.408  1.00 43.11  ? 393 GLU A CB  1 
ATOM   3325 C CG  . GLU A 1 393 ? 7.219   5.724  40.424  1.00 53.70  ? 393 GLU A CG  1 
ATOM   3326 C CD  . GLU A 1 393 ? 6.807   4.907  39.208  1.00 63.50  ? 393 GLU A CD  1 
ATOM   3327 O OE1 . GLU A 1 393 ? 7.508   4.979  38.175  1.00 66.94  ? 393 GLU A OE1 1 
ATOM   3328 O OE2 . GLU A 1 393 ? 5.783   4.190  39.285  1.00 65.91  ? 393 GLU A OE2 1 
ATOM   3329 N N   . ASP A 1 394 ? 5.511   9.109  41.366  1.00 31.06  ? 394 ASP A N   1 
ATOM   3330 C CA  . ASP A 1 394 ? 5.645   10.304 40.530  1.00 35.70  ? 394 ASP A CA  1 
ATOM   3331 C C   . ASP A 1 394 ? 5.891   11.562 41.363  1.00 35.44  ? 394 ASP A C   1 
ATOM   3332 O O   . ASP A 1 394 ? 5.212   12.577 41.217  1.00 39.04  ? 394 ASP A O   1 
ATOM   3333 C CB  . ASP A 1 394 ? 4.412   10.462 39.649  1.00 38.26  ? 394 ASP A CB  1 
ATOM   3334 C CG  . ASP A 1 394 ? 3.113   10.272 40.416  1.00 46.22  ? 394 ASP A CG  1 
ATOM   3335 O OD1 . ASP A 1 394 ? 3.164   10.036 41.645  1.00 47.82  ? 394 ASP A OD1 1 
ATOM   3336 O OD2 . ASP A 1 394 ? 2.037   10.375 39.789  1.00 48.08  ? 394 ASP A OD2 1 
ATOM   3337 N N   . VAL A 1 395 ? 6.885   11.498 42.248  1.00 35.25  ? 395 VAL A N   1 
ATOM   3338 C CA  . VAL A 1 395 ? 7.259   12.622 43.095  1.00 36.29  ? 395 VAL A CA  1 
ATOM   3339 C C   . VAL A 1 395 ? 8.772   12.764 43.062  1.00 36.66  ? 395 VAL A C   1 
ATOM   3340 O O   . VAL A 1 395 ? 9.491   11.876 42.602  1.00 32.21  ? 395 VAL A O   1 
ATOM   3341 C CB  . VAL A 1 395 ? 6.761   12.459 44.551  1.00 33.88  ? 395 VAL A CB  1 
ATOM   3342 C CG1 . VAL A 1 395 ? 5.242   12.416 44.579  1.00 30.01  ? 395 VAL A CG1 1 
ATOM   3343 C CG2 . VAL A 1 395 ? 7.359   11.222 45.198  1.00 34.33  ? 395 VAL A CG2 1 
ATOM   3344 N N   . LYS A 1 396 ? 9.250   13.903 43.553  1.00 35.97  ? 396 LYS A N   1 
ATOM   3345 C CA  . LYS A 1 396 ? 10.678  14.171 43.601  1.00 34.84  ? 396 LYS A CA  1 
ATOM   3346 C C   . LYS A 1 396 ? 11.255  13.742 44.946  1.00 34.87  ? 396 LYS A C   1 
ATOM   3347 O O   . LYS A 1 396 ? 10.605  13.853 45.993  1.00 25.49  ? 396 LYS A O   1 
ATOM   3348 C CB  . LYS A 1 396 ? 10.967  15.653 43.357  1.00 41.34  ? 396 LYS A CB  1 
ATOM   3349 C CG  . LYS A 1 396 ? 10.900  16.054 41.892  1.00 48.55  ? 396 LYS A CG  1 
ATOM   3350 C CD  . LYS A 1 396 ? 12.095  16.902 41.498  1.00 50.49  ? 396 LYS A CD  1 
ATOM   3351 C CE  . LYS A 1 396 ? 12.036  17.309 40.033  1.00 51.91  ? 396 LYS A CE  1 
ATOM   3352 N NZ  . LYS A 1 396 ? 12.300  16.167 39.116  1.00 54.23  ? 396 LYS A NZ  1 
ATOM   3353 N N   . THR A 1 397 ? 12.502  13.271 44.908  1.00 19.96  ? 397 THR A N   1 
ATOM   3354 C CA  . THR A 1 397 ? 13.094  12.619 46.063  1.00 24.27  ? 397 THR A CA  1 
ATOM   3355 C C   . THR A 1 397 ? 14.537  13.087 46.252  1.00 32.57  ? 397 THR A C   1 
ATOM   3356 O O   . THR A 1 397 ? 15.198  13.545 45.312  1.00 32.51  ? 397 THR A O   1 
ATOM   3357 C CB  . THR A 1 397 ? 13.028  11.095 45.899  1.00 34.65  ? 397 THR A CB  1 
ATOM   3358 O OG1 . THR A 1 397 ? 13.015  10.478 47.186  1.00 48.25  ? 397 THR A OG1 1 
ATOM   3359 C CG2 . THR A 1 397 ? 14.225  10.591 45.109  1.00 27.78  ? 397 THR A CG2 1 
ATOM   3360 N N   . GLU A 1 398 ? 15.027  12.949 47.488  1.00 29.35  ? 398 GLU A N   1 
ATOM   3361 C CA  . GLU A 1 398 ? 16.354  13.431 47.844  1.00 29.92  ? 398 GLU A CA  1 
ATOM   3362 C C   . GLU A 1 398 ? 16.879  12.660 49.052  1.00 30.72  ? 398 GLU A C   1 
ATOM   3363 O O   . GLU A 1 398 ? 16.125  12.354 49.981  1.00 26.06  ? 398 GLU A O   1 
ATOM   3364 C CB  . GLU A 1 398 ? 16.325  14.933 48.144  1.00 27.85  ? 398 GLU A CB  1 
ATOM   3365 C CG  . GLU A 1 398 ? 17.702  15.562 48.339  1.00 29.08  ? 398 GLU A CG  1 
ATOM   3366 C CD  . GLU A 1 398 ? 17.638  17.044 48.690  1.00 34.02  ? 398 GLU A CD  1 
ATOM   3367 O OE1 . GLU A 1 398 ? 18.457  17.494 49.519  1.00 36.36  ? 398 GLU A OE1 1 
ATOM   3368 O OE2 . GLU A 1 398 ? 16.776  17.760 48.131  1.00 36.05  ? 398 GLU A OE2 1 
ATOM   3369 N N   . VAL A 1 399 ? 18.169  12.352 49.030  1.00 25.77  ? 399 VAL A N   1 
ATOM   3370 C CA  . VAL A 1 399 ? 18.840  11.713 50.158  1.00 22.27  ? 399 VAL A CA  1 
ATOM   3371 C C   . VAL A 1 399 ? 19.452  12.803 51.026  1.00 28.81  ? 399 VAL A C   1 
ATOM   3372 O O   . VAL A 1 399 ? 20.046  13.758 50.513  1.00 25.54  ? 399 VAL A O   1 
ATOM   3373 C CB  . VAL A 1 399 ? 19.923  10.726 49.674  1.00 30.84  ? 399 VAL A CB  1 
ATOM   3374 C CG1 . VAL A 1 399 ? 20.745  10.211 50.853  1.00 28.34  ? 399 VAL A CG1 1 
ATOM   3375 C CG2 . VAL A 1 399 ? 19.302  9.554  48.891  1.00 33.63  ? 399 VAL A CG2 1 
ATOM   3376 N N   . ILE A 1 400 ? 19.317  12.671 52.342  1.00 30.81  ? 400 ILE A N   1 
ATOM   3377 C CA  . ILE A 1 400 ? 20.062  13.525 53.259  1.00 30.92  ? 400 ILE A CA  1 
ATOM   3378 C C   . ILE A 1 400 ? 20.786  12.639 54.262  1.00 29.39  ? 400 ILE A C   1 
ATOM   3379 O O   . ILE A 1 400 ? 20.334  11.536 54.594  1.00 26.96  ? 400 ILE A O   1 
ATOM   3380 C CB  . ILE A 1 400 ? 19.169  14.561 53.971  1.00 33.12  ? 400 ILE A CB  1 
ATOM   3381 C CG1 . ILE A 1 400 ? 17.961  13.894 54.614  1.00 34.39  ? 400 ILE A CG1 1 
ATOM   3382 C CG2 . ILE A 1 400 ? 18.698  15.619 52.986  1.00 37.89  ? 400 ILE A CG2 1 
ATOM   3383 C CD1 . ILE A 1 400 ? 17.063  14.890 55.285  1.00 34.64  ? 400 ILE A CD1 1 
ATOM   3384 N N   . GLU A 1 401 ? 21.932  13.132 54.735  1.00 26.16  ? 401 GLU A N   1 
ATOM   3385 C CA  . GLU A 1 401 ? 22.839  12.341 55.553  1.00 26.71  ? 401 GLU A CA  1 
ATOM   3386 C C   . GLU A 1 401 ? 22.862  12.740 57.020  1.00 27.58  ? 401 GLU A C   1 
ATOM   3387 O O   . GLU A 1 401 ? 23.349  11.962 57.847  1.00 26.27  ? 401 GLU A O   1 
ATOM   3388 C CB  . GLU A 1 401 ? 24.268  12.435 54.997  1.00 32.43  ? 401 GLU A CB  1 
ATOM   3389 C CG  . GLU A 1 401 ? 24.405  11.930 53.566  1.00 41.69  ? 401 GLU A CG  1 
ATOM   3390 C CD  . GLU A 1 401 ? 24.192  10.429 53.449  1.00 51.64  ? 401 GLU A CD  1 
ATOM   3391 O OE1 . GLU A 1 401 ? 23.762  9.969  52.370  1.00 55.91  ? 401 GLU A OE1 1 
ATOM   3392 O OE2 . GLU A 1 401 ? 24.452  9.708  54.435  1.00 55.38  ? 401 GLU A OE2 1 
ATOM   3393 N N   . SER A 1 402 ? 22.359  13.919 57.363  1.00 25.56  ? 402 SER A N   1 
ATOM   3394 C CA  . SER A 1 402 ? 22.493  14.401 58.728  1.00 26.16  ? 402 SER A CA  1 
ATOM   3395 C C   . SER A 1 402 ? 21.419  15.442 58.980  1.00 26.86  ? 402 SER A C   1 
ATOM   3396 O O   . SER A 1 402 ? 21.039  16.194 58.078  1.00 28.80  ? 402 SER A O   1 
ATOM   3397 C CB  . SER A 1 402 ? 23.889  14.998 58.974  1.00 28.70  ? 402 SER A CB  1 
ATOM   3398 O OG  . SER A 1 402 ? 24.127  15.206 60.360  1.00 31.38  ? 402 SER A OG  1 
ATOM   3399 N N   . VAL A 1 403 ? 20.934  15.474 60.214  1.00 23.34  ? 403 VAL A N   1 
ATOM   3400 C CA  . VAL A 1 403 ? 19.991  16.495 60.637  1.00 25.30  ? 403 VAL A CA  1 
ATOM   3401 C C   . VAL A 1 403 ? 20.540  17.151 61.891  1.00 23.80  ? 403 VAL A C   1 
ATOM   3402 O O   . VAL A 1 403 ? 21.295  16.544 62.658  1.00 24.10  ? 403 VAL A O   1 
ATOM   3403 C CB  . VAL A 1 403 ? 18.573  15.932 60.881  1.00 25.22  ? 403 VAL A CB  1 
ATOM   3404 C CG1 . VAL A 1 403 ? 17.979  15.414 59.577  1.00 28.00  ? 403 VAL A CG1 1 
ATOM   3405 C CG2 . VAL A 1 403 ? 18.603  14.835 61.937  1.00 26.24  ? 403 VAL A CG2 1 
ATOM   3406 N N   . LYS A 1 404 ? 20.200  18.419 62.068  1.00 19.14  ? 404 LYS A N   1 
ATOM   3407 C CA  . LYS A 1 404 ? 20.492  19.111 63.312  1.00 20.09  ? 404 LYS A CA  1 
ATOM   3408 C C   . LYS A 1 404 ? 19.300  18.892 64.238  1.00 28.24  ? 404 LYS A C   1 
ATOM   3409 O O   . LYS A 1 404 ? 18.160  19.184 63.859  1.00 31.16  ? 404 LYS A O   1 
ATOM   3410 C CB  . LYS A 1 404 ? 20.752  20.596 63.056  1.00 24.88  ? 404 LYS A CB  1 
ATOM   3411 C CG  . LYS A 1 404 ? 21.175  21.360 64.303  1.00 32.17  ? 404 LYS A CG  1 
ATOM   3412 C CD  . LYS A 1 404 ? 21.608  22.781 63.989  1.00 42.69  ? 404 LYS A CD  1 
ATOM   3413 C CE  . LYS A 1 404 ? 23.061  22.826 63.535  1.00 48.01  ? 404 LYS A CE  1 
ATOM   3414 N NZ  . LYS A 1 404 ? 23.148  22.913 62.056  1.00 51.68  ? 404 LYS A NZ  1 
ATOM   3415 N N   . ALA A 1 405 ? 19.552  18.343 65.430  1.00 21.47  ? 405 ALA A N   1 
ATOM   3416 C CA  . ALA A 1 405 ? 18.456  17.947 66.304  1.00 22.71  ? 405 ALA A CA  1 
ATOM   3417 C C   . ALA A 1 405 ? 17.587  19.145 66.661  1.00 19.95  ? 405 ALA A C   1 
ATOM   3418 O O   . ALA A 1 405 ? 18.079  20.262 66.828  1.00 21.78  ? 405 ALA A O   1 
ATOM   3419 C CB  . ALA A 1 405 ? 18.995  17.294 67.581  1.00 25.22  ? 405 ALA A CB  1 
ATOM   3420 N N   . GLY A 1 406 ? 16.287  18.907 66.785  1.00 19.12  ? 406 GLY A N   1 
ATOM   3421 C CA  . GLY A 1 406 ? 15.387  19.964 67.200  1.00 23.90  ? 406 GLY A CA  1 
ATOM   3422 C C   . GLY A 1 406 ? 13.964  19.454 67.272  1.00 23.07  ? 406 GLY A C   1 
ATOM   3423 O O   . GLY A 1 406 ? 13.697  18.256 67.147  1.00 21.33  ? 406 GLY A O   1 
ATOM   3424 N N   . THR A 1 407 ? 13.054  20.393 67.505  1.00 18.29  ? 407 THR A N   1 
ATOM   3425 C CA  . THR A 1 407 ? 11.618  20.144 67.540  1.00 18.04  ? 407 THR A CA  1 
ATOM   3426 C C   . THR A 1 407 ? 10.923  21.183 66.663  1.00 18.99  ? 407 THR A C   1 
ATOM   3427 O O   . THR A 1 407 ? 11.561  22.067 66.093  1.00 17.23  ? 407 THR A O   1 
ATOM   3428 C CB  . THR A 1 407 ? 11.060  20.233 68.965  1.00 19.51  ? 407 THR A CB  1 
ATOM   3429 O OG1 . THR A 1 407 ? 10.910  21.613 69.299  1.00 21.27  ? 407 THR A OG1 1 
ATOM   3430 C CG2 . THR A 1 407 ? 11.993  19.551 69.995  1.00 16.63  ? 407 THR A CG2 1 
ATOM   3431 N N   . TRP A 1 408 ? 9.590   21.110 66.585  1.00 17.18  ? 408 TRP A N   1 
ATOM   3432 C CA  . TRP A 1 408 ? 8.882   22.142 65.840  1.00 18.77  ? 408 TRP A CA  1 
ATOM   3433 C C   . TRP A 1 408 ? 8.685   23.415 66.657  1.00 22.87  ? 408 TRP A C   1 
ATOM   3434 O O   . TRP A 1 408 ? 8.097   24.379 66.153  1.00 21.41  ? 408 TRP A O   1 
ATOM   3435 C CB  . TRP A 1 408 ? 7.545   21.606 65.319  1.00 17.75  ? 408 TRP A CB  1 
ATOM   3436 C CG  . TRP A 1 408 ? 6.605   21.073 66.349  1.00 20.49  ? 408 TRP A CG  1 
ATOM   3437 C CD1 . TRP A 1 408 ? 6.757   21.086 67.717  1.00 22.34  ? 408 TRP A CD1 1 
ATOM   3438 C CD2 . TRP A 1 408 ? 5.336   20.457 66.091  1.00 17.67  ? 408 TRP A CD2 1 
ATOM   3439 N NE1 . TRP A 1 408 ? 5.657   20.512 68.315  1.00 21.48  ? 408 TRP A NE1 1 
ATOM   3440 C CE2 . TRP A 1 408 ? 4.773   20.115 67.339  1.00 21.36  ? 408 TRP A CE2 1 
ATOM   3441 C CE3 . TRP A 1 408 ? 4.623   20.161 64.921  1.00 16.22  ? 408 TRP A CE3 1 
ATOM   3442 C CZ2 . TRP A 1 408 ? 3.528   19.481 67.448  1.00 17.75  ? 408 TRP A CZ2 1 
ATOM   3443 C CZ3 . TRP A 1 408 ? 3.382   19.538 65.030  1.00 20.31  ? 408 TRP A CZ3 1 
ATOM   3444 C CH2 . TRP A 1 408 ? 2.849   19.211 66.287  1.00 19.57  ? 408 TRP A CH2 1 
ATOM   3445 N N   . PHE A 1 409 ? 9.180   23.453 67.897  1.00 18.41  ? 409 PHE A N   1 
ATOM   3446 C CA  . PHE A 1 409 ? 9.228   24.694 68.668  1.00 20.45  ? 409 PHE A CA  1 
ATOM   3447 C C   . PHE A 1 409 ? 10.577  25.359 68.407  1.00 25.71  ? 409 PHE A C   1 
ATOM   3448 O O   . PHE A 1 409 ? 11.582  25.059 69.054  1.00 23.45  ? 409 PHE A O   1 
ATOM   3449 C CB  . PHE A 1 409 ? 9.009   24.423 70.152  1.00 28.09  ? 409 PHE A CB  1 
ATOM   3450 C CG  . PHE A 1 409 ? 9.235   25.632 71.016  1.00 41.22  ? 409 PHE A CG  1 
ATOM   3451 C CD1 . PHE A 1 409 ? 8.246   26.590 71.160  1.00 43.27  ? 409 PHE A CD1 1 
ATOM   3452 C CD2 . PHE A 1 409 ? 10.451  25.823 71.666  1.00 48.56  ? 409 PHE A CD2 1 
ATOM   3453 C CE1 . PHE A 1 409 ? 8.455   27.711 71.941  1.00 46.24  ? 409 PHE A CE1 1 
ATOM   3454 C CE2 . PHE A 1 409 ? 10.666  26.946 72.448  1.00 50.25  ? 409 PHE A CE2 1 
ATOM   3455 C CZ  . PHE A 1 409 ? 9.668   27.888 72.585  1.00 50.01  ? 409 PHE A CZ  1 
ATOM   3456 N N   . ASP A 1 410 ? 10.602  26.270 67.428  1.00 24.12  ? 410 ASP A N   1 
ATOM   3457 C CA  . ASP A 1 410 ? 11.781  27.056 67.058  1.00 32.36  ? 410 ASP A CA  1 
ATOM   3458 C C   . ASP A 1 410 ? 12.965  26.199 66.638  1.00 36.93  ? 410 ASP A C   1 
ATOM   3459 O O   . ASP A 1 410 ? 14.100  26.705 66.569  1.00 36.19  ? 410 ASP A O   1 
ATOM   3460 C CB  . ASP A 1 410 ? 12.220  27.990 68.192  1.00 39.09  ? 410 ASP A CB  1 
ATOM   3461 C CG  . ASP A 1 410 ? 11.165  29.011 68.547  1.00 51.58  ? 410 ASP A CG  1 
ATOM   3462 O OD1 . ASP A 1 410 ? 10.356  29.365 67.659  1.00 54.56  ? 410 ASP A OD1 1 
ATOM   3463 O OD2 . ASP A 1 410 ? 11.151  29.465 69.711  1.00 55.04  ? 410 ASP A OD2 1 
ATOM   3464 N N   . GLY A 1 411 ? 12.739  24.916 66.361  1.00 28.33  ? 411 GLY A N   1 
ATOM   3465 C CA  . GLY A 1 411 ? 13.827  24.022 66.026  1.00 23.91  ? 411 GLY A CA  1 
ATOM   3466 C C   . GLY A 1 411 ? 14.732  23.664 67.179  1.00 23.25  ? 411 GLY A C   1 
ATOM   3467 O O   . GLY A 1 411 ? 15.862  23.226 66.942  1.00 28.43  ? 411 GLY A O   1 
ATOM   3468 N N   . ASN A 1 412 ? 14.284  23.851 68.425  1.00 22.06  ? 412 ASN A N   1 
ATOM   3469 C CA  . ASN A 1 412 ? 15.140  23.628 69.583  1.00 25.67  ? 412 ASN A CA  1 
ATOM   3470 C C   . ASN A 1 412 ? 14.307  23.036 70.720  1.00 25.54  ? 412 ASN A C   1 
ATOM   3471 O O   . ASN A 1 412 ? 13.114  22.754 70.571  1.00 20.24  ? 412 ASN A O   1 
ATOM   3472 C CB  . ASN A 1 412 ? 15.875  24.923 69.993  1.00 24.57  ? 412 ASN A CB  1 
ATOM   3473 C CG  . ASN A 1 412 ? 14.945  26.000 70.550  1.00 26.26  ? 412 ASN A CG  1 
ATOM   3474 O OD1 . ASN A 1 412 ? 14.132  25.751 71.442  1.00 25.50  ? 412 ASN A OD1 1 
ATOM   3475 N ND2 . ASN A 1 412 ? 15.088  27.216 70.038  1.00 24.69  ? 412 ASN A ND2 1 
ATOM   3476 N N   . PHE A 1 413 ? 14.954  22.837 71.867  1.00 23.78  ? 413 PHE A N   1 
ATOM   3477 C CA  . PHE A 1 413 ? 14.383  22.071 72.966  1.00 21.27  ? 413 PHE A CA  1 
ATOM   3478 C C   . PHE A 1 413 ? 13.988  22.940 74.155  1.00 22.19  ? 413 PHE A C   1 
ATOM   3479 O O   . PHE A 1 413 ? 13.655  22.403 75.217  1.00 17.52  ? 413 PHE A O   1 
ATOM   3480 C CB  . PHE A 1 413 ? 15.377  20.986 73.395  1.00 17.33  ? 413 PHE A CB  1 
ATOM   3481 C CG  . PHE A 1 413 ? 15.555  19.893 72.355  1.00 21.36  ? 413 PHE A CG  1 
ATOM   3482 C CD1 . PHE A 1 413 ? 14.653  18.841 72.272  1.00 20.44  ? 413 PHE A CD1 1 
ATOM   3483 C CD2 . PHE A 1 413 ? 16.605  19.943 71.447  1.00 20.92  ? 413 PHE A CD2 1 
ATOM   3484 C CE1 . PHE A 1 413 ? 14.803  17.849 71.308  1.00 23.91  ? 413 PHE A CE1 1 
ATOM   3485 C CE2 . PHE A 1 413 ? 16.772  18.953 70.486  1.00 24.33  ? 413 PHE A CE2 1 
ATOM   3486 C CZ  . PHE A 1 413 ? 15.877  17.908 70.410  1.00 24.09  ? 413 PHE A CZ  1 
ATOM   3487 N N   . LEU A 1 414 ? 14.008  24.269 73.999  1.00 17.89  ? 414 LEU A N   1 
ATOM   3488 C CA  . LEU A 1 414 ? 13.826  25.174 75.129  1.00 18.69  ? 414 LEU A CA  1 
ATOM   3489 C C   . LEU A 1 414 ? 12.431  25.094 75.758  1.00 19.53  ? 414 LEU A C   1 
ATOM   3490 O O   . LEU A 1 414 ? 12.249  25.583 76.878  1.00 24.69  ? 414 LEU A O   1 
ATOM   3491 C CB  . LEU A 1 414 ? 14.136  26.604 74.684  1.00 20.91  ? 414 LEU A CB  1 
ATOM   3492 C CG  . LEU A 1 414 ? 15.560  26.792 74.156  1.00 28.77  ? 414 LEU A CG  1 
ATOM   3493 C CD1 . LEU A 1 414 ? 15.851  28.261 73.881  1.00 29.99  ? 414 LEU A CD1 1 
ATOM   3494 C CD2 . LEU A 1 414 ? 16.580  26.215 75.135  1.00 25.10  ? 414 LEU A CD2 1 
ATOM   3495 N N   . LYS A 1 415 ? 11.455  24.467 75.102  1.00 23.25  ? 415 LYS A N   1 
ATOM   3496 C CA  . LYS A 1 415 ? 10.152  24.309 75.746  1.00 28.43  ? 415 LYS A CA  1 
ATOM   3497 C C   . LYS A 1 415 ? 10.156  23.255 76.843  1.00 26.72  ? 415 LYS A C   1 
ATOM   3498 O O   . LYS A 1 415 ? 9.191   23.185 77.616  1.00 25.28  ? 415 LYS A O   1 
ATOM   3499 C CB  . LYS A 1 415 ? 9.075   23.948 74.723  1.00 27.64  ? 415 LYS A CB  1 
ATOM   3500 C CG  . LYS A 1 415 ? 8.189   25.115 74.328  1.00 42.61  ? 415 LYS A CG  1 
ATOM   3501 C CD  . LYS A 1 415 ? 7.669   25.882 75.542  1.00 52.11  ? 415 LYS A CD  1 
ATOM   3502 C CE  . LYS A 1 415 ? 6.357   25.292 76.039  1.00 57.27  ? 415 LYS A CE  1 
ATOM   3503 N NZ  . LYS A 1 415 ? 5.692   26.156 77.056  1.00 59.71  ? 415 LYS A NZ  1 
ATOM   3504 N N   . TRP A 1 416 ? 11.202  22.435 76.932  1.00 22.86  ? 416 TRP A N   1 
ATOM   3505 C CA  . TRP A 1 416 ? 11.207  21.300 77.846  1.00 17.67  ? 416 TRP A CA  1 
ATOM   3506 C C   . TRP A 1 416 ? 12.449  21.209 78.717  1.00 24.02  ? 416 TRP A C   1 
ATOM   3507 O O   . TRP A 1 416 ? 12.493  20.360 79.617  1.00 20.53  ? 416 TRP A O   1 
ATOM   3508 C CB  . TRP A 1 416 ? 11.064  19.990 77.060  1.00 18.25  ? 416 TRP A CB  1 
ATOM   3509 C CG  . TRP A 1 416 ? 9.868   19.982 76.149  1.00 22.63  ? 416 TRP A CG  1 
ATOM   3510 C CD1 . TRP A 1 416 ? 8.618   19.527 76.443  1.00 19.11  ? 416 TRP A CD1 1 
ATOM   3511 C CD2 . TRP A 1 416 ? 9.815   20.455 74.796  1.00 21.22  ? 416 TRP A CD2 1 
ATOM   3512 N NE1 . TRP A 1 416 ? 7.786   19.684 75.356  1.00 21.71  ? 416 TRP A NE1 1 
ATOM   3513 C CE2 . TRP A 1 416 ? 8.499   20.253 74.333  1.00 23.76  ? 416 TRP A CE2 1 
ATOM   3514 C CE3 . TRP A 1 416 ? 10.756  21.022 73.930  1.00 17.50  ? 416 TRP A CE3 1 
ATOM   3515 C CZ2 . TRP A 1 416 ? 8.094   20.618 73.047  1.00 25.76  ? 416 TRP A CZ2 1 
ATOM   3516 C CZ3 . TRP A 1 416 ? 10.357  21.375 72.647  1.00 27.82  ? 416 TRP A CZ3 1 
ATOM   3517 C CH2 . TRP A 1 416 ? 9.039   21.164 72.215  1.00 26.18  ? 416 TRP A CH2 1 
ATOM   3518 N N   . ILE A 1 417 ? 13.459  22.038 78.475  1.00 21.13  ? 417 ILE A N   1 
ATOM   3519 C CA  . ILE A 1 417 ? 14.703  21.977 79.225  1.00 24.76  ? 417 ILE A CA  1 
ATOM   3520 C C   . ILE A 1 417 ? 15.378  23.329 79.054  1.00 29.89  ? 417 ILE A C   1 
ATOM   3521 O O   . ILE A 1 417 ? 15.131  24.039 78.075  1.00 28.31  ? 417 ILE A O   1 
ATOM   3522 C CB  . ILE A 1 417 ? 15.580  20.795 78.729  1.00 21.66  ? 417 ILE A CB  1 
ATOM   3523 C CG1 . ILE A 1 417 ? 16.769  20.538 79.667  1.00 21.61  ? 417 ILE A CG1 1 
ATOM   3524 C CG2 . ILE A 1 417 ? 16.028  21.016 77.276  1.00 19.58  ? 417 ILE A CG2 1 
ATOM   3525 C CD1 . ILE A 1 417 ? 17.313  19.122 79.589  1.00 20.61  ? 417 ILE A CD1 1 
ATOM   3526 N N   . GLY A 1 418 ? 16.183  23.718 80.038  1.00 29.05  ? 418 GLY A N   1 
ATOM   3527 C CA  . GLY A 1 418 ? 17.012  24.904 79.917  1.00 29.84  ? 418 GLY A CA  1 
ATOM   3528 C C   . GLY A 1 418 ? 16.757  26.019 80.910  1.00 34.20  ? 418 GLY A C   1 
ATOM   3529 O O   . GLY A 1 418 ? 17.587  26.936 80.997  1.00 46.66  ? 418 GLY A O   1 
ATOM   3530 N N   . ASN A 1 419 ? 15.659  26.029 81.655  1.00 35.74  ? 419 ASN A N   1 
ATOM   3531 C CA  . ASN A 1 419 ? 15.504  26.991 82.736  1.00 33.93  ? 419 ASN A CA  1 
ATOM   3532 C C   . ASN A 1 419 ? 15.478  26.252 84.070  1.00 33.75  ? 419 ASN A C   1 
ATOM   3533 O O   . ASN A 1 419 ? 15.400  25.020 84.120  1.00 34.46  ? 419 ASN A O   1 
ATOM   3534 C CB  . ASN A 1 419 ? 14.250  27.862 82.538  1.00 35.24  ? 419 ASN A CB  1 
ATOM   3535 C CG  . ASN A 1 419 ? 12.941  27.081 82.635  1.00 33.42  ? 419 ASN A CG  1 
ATOM   3536 O OD1 . ASN A 1 419 ? 12.838  26.074 83.329  1.00 32.84  ? 419 ASN A OD1 1 
ATOM   3537 N ND2 . ASN A 1 419 ? 11.918  27.577 81.946  1.00 34.71  ? 419 ASN A ND2 1 
ATOM   3538 N N   . LYS A 1 420 ? 15.530  27.026 85.158  1.00 31.98  ? 420 LYS A N   1 
ATOM   3539 C CA  . LYS A 1 420 ? 15.662  26.428 86.484  1.00 33.99  ? 420 LYS A CA  1 
ATOM   3540 C C   . LYS A 1 420 ? 14.533  25.450 86.772  1.00 35.74  ? 420 LYS A C   1 
ATOM   3541 O O   . LYS A 1 420 ? 14.767  24.358 87.305  1.00 32.85  ? 420 LYS A O   1 
ATOM   3542 C CB  . LYS A 1 420 ? 15.703  27.517 87.554  1.00 41.41  ? 420 LYS A CB  1 
ATOM   3543 C CG  . LYS A 1 420 ? 15.986  26.973 88.946  1.00 49.95  ? 420 LYS A CG  1 
ATOM   3544 C CD  . LYS A 1 420 ? 15.632  27.977 90.033  1.00 54.62  ? 420 LYS A CD  1 
ATOM   3545 C CE  . LYS A 1 420 ? 15.642  27.326 91.410  1.00 58.67  ? 420 LYS A CE  1 
ATOM   3546 N NZ  . LYS A 1 420 ? 15.093  25.942 91.376  1.00 61.86  ? 420 LYS A NZ  1 
ATOM   3547 N N   . GLU A 1 421 ? 13.303  25.813 86.405  1.00 31.09  ? 421 GLU A N   1 
ATOM   3548 C CA  . GLU A 1 421 ? 12.154  24.994 86.767  1.00 31.50  ? 421 GLU A CA  1 
ATOM   3549 C C   . GLU A 1 421 ? 12.096  23.715 85.932  1.00 25.94  ? 421 GLU A C   1 
ATOM   3550 O O   . GLU A 1 421 ? 11.877  22.621 86.467  1.00 22.35  ? 421 GLU A O   1 
ATOM   3551 C CB  . GLU A 1 421 ? 10.874  25.811 86.609  1.00 36.36  ? 421 GLU A CB  1 
ATOM   3552 C CG  . GLU A 1 421 ? 10.600  26.748 87.772  1.00 46.62  ? 421 GLU A CG  1 
ATOM   3553 C CD  . GLU A 1 421 ? 11.281  28.103 87.609  1.00 61.70  ? 421 GLU A CD  1 
ATOM   3554 O OE1 . GLU A 1 421 ? 11.812  28.384 86.508  1.00 64.73  ? 421 GLU A OE1 1 
ATOM   3555 O OE2 . GLU A 1 421 ? 11.282  28.889 88.584  1.00 68.31  ? 421 GLU A OE2 1 
ATOM   3556 N N   . LYS A 1 422 ? 12.293  23.828 84.616  1.00 27.67  ? 422 LYS A N   1 
ATOM   3557 C CA  . LYS A 1 422 ? 12.272  22.631 83.780  1.00 24.44  ? 422 LYS A CA  1 
ATOM   3558 C C   . LYS A 1 422 ? 13.441  21.711 84.113  1.00 25.25  ? 422 LYS A C   1 
ATOM   3559 O O   . LYS A 1 422 ? 13.287  20.483 84.128  1.00 23.51  ? 422 LYS A O   1 
ATOM   3560 C CB  . LYS A 1 422 ? 12.277  23.024 82.303  1.00 26.76  ? 422 LYS A CB  1 
ATOM   3561 C CG  . LYS A 1 422 ? 10.999  23.728 81.837  1.00 22.88  ? 422 LYS A CG  1 
ATOM   3562 C CD  . LYS A 1 422 ? 11.100  24.136 80.375  1.00 19.75  ? 422 LYS A CD  1 
ATOM   3563 C CE  . LYS A 1 422 ? 10.006  25.138 80.002  1.00 24.43  ? 422 LYS A CE  1 
ATOM   3564 N NZ  . LYS A 1 422 ? 8.637   24.604 80.307  1.00 19.19  ? 422 LYS A NZ  1 
ATOM   3565 N N   . ASN A 1 423 ? 14.616  22.288 84.407  1.00 21.96  ? 423 ASN A N   1 
ATOM   3566 C CA  . ASN A 1 423 ? 15.775  21.482 84.785  1.00 22.87  ? 423 ASN A CA  1 
ATOM   3567 C C   . ASN A 1 423 ? 15.548  20.748 86.092  1.00 27.42  ? 423 ASN A C   1 
ATOM   3568 O O   . ASN A 1 423 ? 16.075  19.643 86.275  1.00 24.19  ? 423 ASN A O   1 
ATOM   3569 C CB  . ASN A 1 423 ? 17.019  22.358 84.898  1.00 18.00  ? 423 ASN A CB  1 
ATOM   3570 C CG  . ASN A 1 423 ? 17.574  22.739 83.546  1.00 32.55  ? 423 ASN A CG  1 
ATOM   3571 O OD1 . ASN A 1 423 ? 17.059  22.311 82.493  1.00 17.74  ? 423 ASN A OD1 1 
ATOM   3572 N ND2 . ASN A 1 423 ? 18.613  23.555 83.553  1.00 28.67  ? 423 ASN A ND2 1 
ATOM   3573 N N   . GLU A 1 424 ? 14.782  21.343 87.011  1.00 28.47  ? 424 GLU A N   1 
ATOM   3574 C CA  . GLU A 1 424 ? 14.458  20.644 88.248  1.00 28.69  ? 424 GLU A CA  1 
ATOM   3575 C C   . GLU A 1 424 ? 13.694  19.352 87.964  1.00 26.08  ? 424 GLU A C   1 
ATOM   3576 O O   . GLU A 1 424 ? 13.962  18.317 88.585  1.00 19.56  ? 424 GLU A O   1 
ATOM   3577 C CB  . GLU A 1 424 ? 13.662  21.558 89.181  1.00 29.56  ? 424 GLU A CB  1 
ATOM   3578 C CG  . GLU A 1 424 ? 13.175  20.873 90.464  1.00 34.47  ? 424 GLU A CG  1 
ATOM   3579 C CD  . GLU A 1 424 ? 14.316  20.375 91.343  1.00 45.61  ? 424 GLU A CD  1 
ATOM   3580 O OE1 . GLU A 1 424 ? 15.368  21.052 91.409  1.00 49.42  ? 424 GLU A OE1 1 
ATOM   3581 O OE2 . GLU A 1 424 ? 14.163  19.300 91.967  1.00 48.78  ? 424 GLU A OE2 1 
ATOM   3582 N N   . TYR A 1 425 ? 12.744  19.387 87.025  1.00 26.40  ? 425 TYR A N   1 
ATOM   3583 C CA  . TYR A 1 425 ? 12.050  18.155 86.664  1.00 24.06  ? 425 TYR A CA  1 
ATOM   3584 C C   . TYR A 1 425 ? 13.027  17.122 86.123  1.00 20.01  ? 425 TYR A C   1 
ATOM   3585 O O   . TYR A 1 425 ? 12.936  15.937 86.454  1.00 19.71  ? 425 TYR A O   1 
ATOM   3586 C CB  . TYR A 1 425 ? 10.951  18.430 85.640  1.00 24.39  ? 425 TYR A CB  1 
ATOM   3587 C CG  . TYR A 1 425 ? 9.577   18.707 86.235  1.00 24.16  ? 425 TYR A CG  1 
ATOM   3588 C CD1 . TYR A 1 425 ? 9.435   19.162 87.542  1.00 22.10  ? 425 TYR A CD1 1 
ATOM   3589 C CD2 . TYR A 1 425 ? 8.428   18.533 85.480  1.00 23.10  ? 425 TYR A CD2 1 
ATOM   3590 C CE1 . TYR A 1 425 ? 8.167   19.416 88.086  1.00 18.04  ? 425 TYR A CE1 1 
ATOM   3591 C CE2 . TYR A 1 425 ? 7.164   18.799 86.011  1.00 22.96  ? 425 TYR A CE2 1 
ATOM   3592 C CZ  . TYR A 1 425 ? 7.049   19.241 87.304  1.00 20.87  ? 425 TYR A CZ  1 
ATOM   3593 O OH  . TYR A 1 425 ? 5.804   19.498 87.823  1.00 27.23  ? 425 TYR A OH  1 
ATOM   3594 N N   . TRP A 1 426 ? 13.978  17.550 85.293  1.00 18.75  ? 426 TRP A N   1 
ATOM   3595 C CA  . TRP A 1 426 ? 14.939  16.584 84.778  1.00 18.20  ? 426 TRP A CA  1 
ATOM   3596 C C   . TRP A 1 426 ? 15.795  16.016 85.900  1.00 20.44  ? 426 TRP A C   1 
ATOM   3597 O O   . TRP A 1 426 ? 16.053  14.807 85.935  1.00 18.21  ? 426 TRP A O   1 
ATOM   3598 C CB  . TRP A 1 426 ? 15.797  17.216 83.690  1.00 23.11  ? 426 TRP A CB  1 
ATOM   3599 C CG  . TRP A 1 426 ? 15.062  17.346 82.392  1.00 20.36  ? 426 TRP A CG  1 
ATOM   3600 C CD1 . TRP A 1 426 ? 14.554  18.496 81.851  1.00 23.51  ? 426 TRP A CD1 1 
ATOM   3601 C CD2 . TRP A 1 426 ? 14.748  16.296 81.471  1.00 24.21  ? 426 TRP A CD2 1 
ATOM   3602 N NE1 . TRP A 1 426 ? 13.948  18.224 80.647  1.00 19.08  ? 426 TRP A NE1 1 
ATOM   3603 C CE2 . TRP A 1 426 ? 14.058  16.882 80.389  1.00 22.15  ? 426 TRP A CE2 1 
ATOM   3604 C CE3 . TRP A 1 426 ? 14.999  14.923 81.446  1.00 26.64  ? 426 TRP A CE3 1 
ATOM   3605 C CZ2 . TRP A 1 426 ? 13.607  16.143 79.306  1.00 24.06  ? 426 TRP A CZ2 1 
ATOM   3606 C CZ3 . TRP A 1 426 ? 14.546  14.187 80.370  1.00 24.80  ? 426 TRP A CZ3 1 
ATOM   3607 C CH2 . TRP A 1 426 ? 13.860  14.797 79.314  1.00 22.67  ? 426 TRP A CH2 1 
ATOM   3608 N N   . LYS A 1 427 ? 16.226  16.867 86.842  1.00 22.63  ? 427 LYS A N   1 
ATOM   3609 C CA  . LYS A 1 427 ? 16.957  16.369 88.002  1.00 24.17  ? 427 LYS A CA  1 
ATOM   3610 C C   . LYS A 1 427 ? 16.134  15.345 88.769  1.00 18.92  ? 427 LYS A C   1 
ATOM   3611 O O   . LYS A 1 427 ? 16.657  14.307 89.183  1.00 19.92  ? 427 LYS A O   1 
ATOM   3612 C CB  . LYS A 1 427 ? 17.356  17.525 88.927  1.00 27.30  ? 427 LYS A CB  1 
ATOM   3613 C CG  . LYS A 1 427 ? 18.466  18.402 88.393  1.00 33.60  ? 427 LYS A CG  1 
ATOM   3614 C CD  . LYS A 1 427 ? 18.415  19.799 89.017  1.00 38.13  ? 427 LYS A CD  1 
ATOM   3615 C CE  . LYS A 1 427 ? 19.549  20.009 90.016  1.00 45.15  ? 427 LYS A CE  1 
ATOM   3616 N NZ  . LYS A 1 427 ? 19.866  21.457 90.249  1.00 47.37  ? 427 LYS A NZ  1 
ATOM   3617 N N   . ILE A 1 428 ? 14.842  15.625 88.974  1.00 20.14  ? 428 ILE A N   1 
ATOM   3618 C CA  . ILE A 1 428 ? 13.979  14.689 89.694  1.00 20.09  ? 428 ILE A CA  1 
ATOM   3619 C C   . ILE A 1 428 ? 13.902  13.365 88.951  1.00 22.87  ? 428 ILE A C   1 
ATOM   3620 O O   . ILE A 1 428 ? 14.024  12.292 89.553  1.00 20.70  ? 428 ILE A O   1 
ATOM   3621 C CB  . ILE A 1 428 ? 12.584  15.305 89.912  1.00 23.27  ? 428 ILE A CB  1 
ATOM   3622 C CG1 . ILE A 1 428 ? 12.658  16.389 90.987  1.00 22.74  ? 428 ILE A CG1 1 
ATOM   3623 C CG2 . ILE A 1 428 ? 11.546  14.224 90.269  1.00 15.96  ? 428 ILE A CG2 1 
ATOM   3624 C CD1 . ILE A 1 428 ? 11.608  17.452 90.853  1.00 21.50  ? 428 ILE A CD1 1 
ATOM   3625 N N   . LEU A 1 429 ? 13.723  13.425 87.627  1.00 18.70  ? 429 LEU A N   1 
ATOM   3626 C CA  . LEU A 1 429 ? 13.658  12.221 86.806  1.00 16.84  ? 429 LEU A CA  1 
ATOM   3627 C C   . LEU A 1 429 ? 14.973  11.458 86.811  1.00 21.25  ? 429 LEU A C   1 
ATOM   3628 O O   . LEU A 1 429 ? 14.981  10.221 86.873  1.00 24.23  ? 429 LEU A O   1 
ATOM   3629 C CB  . LEU A 1 429 ? 13.268  12.598 85.376  1.00 21.47  ? 429 LEU A CB  1 
ATOM   3630 C CG  . LEU A 1 429 ? 12.963  11.432 84.428  1.00 26.61  ? 429 LEU A CG  1 
ATOM   3631 C CD1 . LEU A 1 429 ? 11.651  10.764 84.812  1.00 24.80  ? 429 LEU A CD1 1 
ATOM   3632 C CD2 . LEU A 1 429 ? 12.924  11.908 82.974  1.00 27.52  ? 429 LEU A CD2 1 
ATOM   3633 N N   . ILE A 1 430 ? 16.103  12.175 86.732  1.00 21.68  ? 430 ILE A N   1 
ATOM   3634 C CA  . ILE A 1 430 ? 17.408  11.513 86.715  1.00 21.92  ? 430 ILE A CA  1 
ATOM   3635 C C   . ILE A 1 430 ? 17.628  10.726 88.007  1.00 28.47  ? 430 ILE A C   1 
ATOM   3636 O O   . ILE A 1 430 ? 18.030  9.556  87.980  1.00 28.27  ? 430 ILE A O   1 
ATOM   3637 C CB  . ILE A 1 430 ? 18.525  12.549 86.492  1.00 23.92  ? 430 ILE A CB  1 
ATOM   3638 C CG1 . ILE A 1 430 ? 18.532  13.006 85.031  1.00 18.94  ? 430 ILE A CG1 1 
ATOM   3639 C CG2 . ILE A 1 430 ? 19.893  11.991 86.905  1.00 30.67  ? 430 ILE A CG2 1 
ATOM   3640 C CD1 . ILE A 1 430 ? 18.983  14.440 84.887  1.00 17.43  ? 430 ILE A CD1 1 
ATOM   3641 N N   . GLU A 1 431 ? 17.372  11.360 89.159  1.00 32.10  ? 431 GLU A N   1 
ATOM   3642 C CA  . GLU A 1 431 ? 17.537  10.668 90.435  1.00 26.63  ? 431 GLU A CA  1 
ATOM   3643 C C   . GLU A 1 431 ? 16.549  9.515  90.559  1.00 24.01  ? 431 GLU A C   1 
ATOM   3644 O O   . GLU A 1 431 ? 16.902  8.436  91.053  1.00 28.72  ? 431 GLU A O   1 
ATOM   3645 C CB  . GLU A 1 431 ? 17.359  11.646 91.600  1.00 32.93  ? 431 GLU A CB  1 
ATOM   3646 C CG  . GLU A 1 431 ? 18.642  11.944 92.363  1.00 47.23  ? 431 GLU A CG  1 
ATOM   3647 C CD  . GLU A 1 431 ? 19.238  10.706 93.023  1.00 54.35  ? 431 GLU A CD  1 
ATOM   3648 O OE1 . GLU A 1 431 ? 20.391  10.354 92.697  1.00 54.24  ? 431 GLU A OE1 1 
ATOM   3649 O OE2 . GLU A 1 431 ? 18.552  10.085 93.864  1.00 56.28  ? 431 GLU A OE2 1 
ATOM   3650 N N   . ALA A 1 432 ? 15.298  9.728  90.126  1.00 17.51  ? 432 ALA A N   1 
ATOM   3651 C CA  . ALA A 1 432 ? 14.310  8.655  90.183  1.00 22.98  ? 432 ALA A CA  1 
ATOM   3652 C C   . ALA A 1 432 ? 14.700  7.487  89.285  1.00 31.89  ? 432 ALA A C   1 
ATOM   3653 O O   . ALA A 1 432 ? 14.461  6.323  89.631  1.00 34.21  ? 432 ALA A O   1 
ATOM   3654 C CB  . ALA A 1 432 ? 12.936  9.187  89.790  1.00 19.27  ? 432 ALA A CB  1 
ATOM   3655 N N   . LYS A 1 433 ? 15.287  7.781  88.116  1.00 27.97  ? 433 LYS A N   1 
ATOM   3656 C CA  . LYS A 1 433 ? 15.680  6.724  87.189  1.00 27.29  ? 433 LYS A CA  1 
ATOM   3657 C C   . LYS A 1 433 ? 16.710  5.787  87.817  1.00 28.09  ? 433 LYS A C   1 
ATOM   3658 O O   . LYS A 1 433 ? 16.725  4.587  87.514  1.00 33.19  ? 433 LYS A O   1 
ATOM   3659 C CB  . LYS A 1 433 ? 16.212  7.354  85.893  1.00 23.28  ? 433 LYS A CB  1 
ATOM   3660 C CG  . LYS A 1 433 ? 16.833  6.380  84.899  1.00 26.31  ? 433 LYS A CG  1 
ATOM   3661 C CD  . LYS A 1 433 ? 15.786  5.427  84.316  1.00 22.58  ? 433 LYS A CD  1 
ATOM   3662 C CE  . LYS A 1 433 ? 16.398  4.480  83.296  1.00 25.16  ? 433 LYS A CE  1 
ATOM   3663 N NZ  . LYS A 1 433 ? 15.364  3.498  82.842  1.00 29.52  ? 433 LYS A NZ  1 
ATOM   3664 N N   . LYS A 1 434 ? 17.561  6.308  88.706  1.00 27.45  ? 434 LYS A N   1 
ATOM   3665 C CA  . LYS A 1 434 ? 18.532  5.464  89.400  1.00 32.73  ? 434 LYS A CA  1 
ATOM   3666 C C   . LYS A 1 434 ? 17.850  4.405  90.256  1.00 35.05  ? 434 LYS A C   1 
ATOM   3667 O O   . LYS A 1 434 ? 18.382  3.300  90.415  1.00 34.19  ? 434 LYS A O   1 
ATOM   3668 C CB  . LYS A 1 434 ? 19.449  6.321  90.274  1.00 37.43  ? 434 LYS A CB  1 
ATOM   3669 C CG  . LYS A 1 434 ? 20.325  7.292  89.508  1.00 39.32  ? 434 LYS A CG  1 
ATOM   3670 C CD  . LYS A 1 434 ? 21.078  8.222  90.439  1.00 37.71  ? 434 LYS A CD  1 
ATOM   3671 C CE  . LYS A 1 434 ? 22.187  8.942  89.709  1.00 39.87  ? 434 LYS A CE  1 
ATOM   3672 N NZ  . LYS A 1 434 ? 22.600  10.187 90.424  1.00 49.69  ? 434 LYS A NZ  1 
ATOM   3673 N N   . LYS A 1 435 ? 16.677  4.722  90.811  1.00 29.47  ? 435 LYS A N   1 
ATOM   3674 C CA  . LYS A 1 435 ? 15.946  3.843  91.715  1.00 31.22  ? 435 LYS A CA  1 
ATOM   3675 C C   . LYS A 1 435 ? 14.645  3.324  91.108  1.00 36.02  ? 435 LYS A C   1 
ATOM   3676 O O   . LYS A 1 435 ? 13.782  2.819  91.835  1.00 34.56  ? 435 LYS A O   1 
ATOM   3677 C CB  . LYS A 1 435 ? 15.658  4.574  93.026  1.00 38.81  ? 435 LYS A CB  1 
ATOM   3678 C CG  . LYS A 1 435 ? 16.789  5.489  93.486  1.00 48.73  ? 435 LYS A CG  1 
ATOM   3679 C CD  . LYS A 1 435 ? 16.402  6.268  94.734  1.00 51.12  ? 435 LYS A CD  1 
ATOM   3680 C CE  . LYS A 1 435 ? 17.485  7.258  95.122  1.00 54.75  ? 435 LYS A CE  1 
ATOM   3681 N NZ  . LYS A 1 435 ? 17.022  8.250  96.136  1.00 57.91  ? 435 LYS A NZ  1 
ATOM   3682 N N   . ALA A 1 436 ? 14.493  3.423  89.790  1.00 30.37  ? 436 ALA A N   1 
ATOM   3683 C CA  . ALA A 1 436 ? 13.256  3.018  89.141  1.00 31.54  ? 436 ALA A CA  1 
ATOM   3684 C C   . ALA A 1 436 ? 13.094  1.499  89.157  1.00 34.86  ? 436 ALA A C   1 
ATOM   3685 O O   . ALA A 1 436 ? 14.061  0.749  88.985  1.00 30.07  ? 436 ALA A O   1 
ATOM   3686 C CB  . ALA A 1 436 ? 13.222  3.537  87.704  1.00 27.77  ? 436 ALA A CB  1 
ATOM   3687 N N   . LYS A 1 437 ? 11.852  1.052  89.367  1.00 29.42  ? 437 LYS A N   1 
ATOM   3688 C CA  . LYS A 1 437 ? 11.532  -0.368 89.425  1.00 30.19  ? 437 LYS A CA  1 
ATOM   3689 C C   . LYS A 1 437 ? 10.393  -0.795 88.510  1.00 32.14  ? 437 LYS A C   1 
ATOM   3690 O O   . LYS A 1 437 ? 10.129  -2.000 88.414  1.00 29.42  ? 437 LYS A O   1 
ATOM   3691 C CB  . LYS A 1 437 ? 11.189  -0.776 90.865  1.00 29.57  ? 437 LYS A CB  1 
ATOM   3692 C CG  . LYS A 1 437 ? 12.358  -0.631 91.814  1.00 29.87  ? 437 LYS A CG  1 
ATOM   3693 C CD  . LYS A 1 437 ? 11.913  -0.518 93.255  1.00 36.82  ? 437 LYS A CD  1 
ATOM   3694 C CE  . LYS A 1 437 ? 13.079  -0.105 94.146  1.00 43.62  ? 437 LYS A CE  1 
ATOM   3695 N NZ  . LYS A 1 437 ? 13.397  1.355  94.024  1.00 44.05  ? 437 LYS A NZ  1 
ATOM   3696 N N   . ASN A 1 438 ? 9.718   0.132  87.829  1.00 32.23  ? 438 ASN A N   1 
ATOM   3697 C CA  . ASN A 1 438 ? 8.577   -0.217 86.993  1.00 33.10  ? 438 ASN A CA  1 
ATOM   3698 C C   . ASN A 1 438 ? 8.411   0.851  85.917  1.00 32.88  ? 438 ASN A C   1 
ATOM   3699 O O   . ASN A 1 438 ? 9.105   1.874  85.914  1.00 28.44  ? 438 ASN A O   1 
ATOM   3700 C CB  . ASN A 1 438 ? 7.304   -0.367 87.831  1.00 29.08  ? 438 ASN A CB  1 
ATOM   3701 C CG  . ASN A 1 438 ? 6.992   0.880  88.637  1.00 31.64  ? 438 ASN A CG  1 
ATOM   3702 O OD1 . ASN A 1 438 ? 6.689   1.926  88.071  1.00 35.44  ? 438 ASN A OD1 1 
ATOM   3703 N ND2 . ASN A 1 438 ? 7.052   0.773  89.964  1.00 29.36  ? 438 ASN A ND2 1 
ATOM   3704 N N   . ASP A 1 439 ? 7.458   0.617  85.011  1.00 29.17  ? 439 ASP A N   1 
ATOM   3705 C CA  . ASP A 1 439 ? 7.305   1.457  83.830  1.00 30.66  ? 439 ASP A CA  1 
ATOM   3706 C C   . ASP A 1 439 ? 6.671   2.817  84.123  1.00 30.35  ? 439 ASP A C   1 
ATOM   3707 O O   . ASP A 1 439 ? 6.468   3.591  83.183  1.00 26.42  ? 439 ASP A O   1 
ATOM   3708 C CB  . ASP A 1 439 ? 6.491   0.720  82.755  1.00 30.73  ? 439 ASP A CB  1 
ATOM   3709 C CG  . ASP A 1 439 ? 7.336   -0.285 81.965  1.00 38.55  ? 439 ASP A CG  1 
ATOM   3710 O OD1 . ASP A 1 439 ? 8.559   -0.365 82.204  1.00 39.25  ? 439 ASP A OD1 1 
ATOM   3711 O OD2 . ASP A 1 439 ? 6.777   -1.007 81.115  1.00 42.89  ? 439 ASP A OD2 1 
ATOM   3712 N N   . TYR A 1 440 ? 6.361   3.149  85.384  1.00 24.67  ? 440 TYR A N   1 
ATOM   3713 C CA  . TYR A 1 440 ? 5.903   4.509  85.650  1.00 20.42  ? 440 TYR A CA  1 
ATOM   3714 C C   . TYR A 1 440 ? 7.008   5.519  85.420  1.00 16.70  ? 440 TYR A C   1 
ATOM   3715 O O   . TYR A 1 440 ? 6.721   6.706  85.248  1.00 23.61  ? 440 TYR A O   1 
ATOM   3716 C CB  . TYR A 1 440 ? 5.346   4.641  87.064  1.00 22.88  ? 440 TYR A CB  1 
ATOM   3717 C CG  . TYR A 1 440 ? 3.862   4.358  87.093  1.00 28.72  ? 440 TYR A CG  1 
ATOM   3718 C CD1 . TYR A 1 440 ? 2.960   5.257  86.543  1.00 23.29  ? 440 TYR A CD1 1 
ATOM   3719 C CD2 . TYR A 1 440 ? 3.371   3.162  87.607  1.00 27.35  ? 440 TYR A CD2 1 
ATOM   3720 C CE1 . TYR A 1 440 ? 1.591   4.994  86.544  1.00 27.17  ? 440 TYR A CE1 1 
ATOM   3721 C CE2 . TYR A 1 440 ? 2.015   2.896  87.628  1.00 28.14  ? 440 TYR A CE2 1 
ATOM   3722 C CZ  . TYR A 1 440 ? 1.130   3.812  87.090  1.00 32.65  ? 440 TYR A CZ  1 
ATOM   3723 O OH  . TYR A 1 440 ? -0.220  3.542  87.093  1.00 40.16  ? 440 TYR A OH  1 
ATOM   3724 N N   . ILE A 1 441 ? 8.260   5.062  85.386  1.00 17.29  ? 441 ILE A N   1 
ATOM   3725 C CA  . ILE A 1 441 ? 9.341   5.940  84.974  1.00 15.74  ? 441 ILE A CA  1 
ATOM   3726 C C   . ILE A 1 441 ? 9.152   6.371  83.522  1.00 20.99  ? 441 ILE A C   1 
ATOM   3727 O O   . ILE A 1 441 ? 9.512   7.497  83.158  1.00 24.25  ? 441 ILE A O   1 
ATOM   3728 C CB  . ILE A 1 441 ? 10.713  5.270  85.228  1.00 18.11  ? 441 ILE A CB  1 
ATOM   3729 C CG1 . ILE A 1 441 ? 11.803  6.334  85.336  1.00 22.32  ? 441 ILE A CG1 1 
ATOM   3730 C CG2 . ILE A 1 441 ? 11.062  4.257  84.139  1.00 21.82  ? 441 ILE A CG2 1 
ATOM   3731 C CD1 . ILE A 1 441 ? 11.608  7.269  86.518  1.00 23.87  ? 441 ILE A CD1 1 
ATOM   3732 N N   . LEU A 1 442 ? 8.551   5.519  82.676  1.00 17.19  ? 442 LEU A N   1 
ATOM   3733 C CA  . LEU A 1 442 ? 8.316   5.945  81.295  1.00 16.54  ? 442 LEU A CA  1 
ATOM   3734 C C   . LEU A 1 442 ? 7.213   6.988  81.224  1.00 17.55  ? 442 LEU A C   1 
ATOM   3735 O O   . LEU A 1 442 ? 7.256   7.891  80.379  1.00 22.52  ? 442 LEU A O   1 
ATOM   3736 C CB  . LEU A 1 442 ? 7.949   4.756  80.408  1.00 15.36  ? 442 LEU A CB  1 
ATOM   3737 C CG  . LEU A 1 442 ? 8.906   3.563  80.345  1.00 21.86  ? 442 LEU A CG  1 
ATOM   3738 C CD1 . LEU A 1 442 ? 8.285   2.460  79.492  1.00 25.39  ? 442 LEU A CD1 1 
ATOM   3739 C CD2 . LEU A 1 442 ? 10.235  3.967  79.783  1.00 14.86  ? 442 LEU A CD2 1 
ATOM   3740 N N   . VAL A 1 443 ? 6.185   6.851  82.064  1.00 17.40  ? 443 VAL A N   1 
ATOM   3741 C CA  . VAL A 1 443 ? 5.112   7.840  82.077  1.00 13.67  ? 443 VAL A CA  1 
ATOM   3742 C C   . VAL A 1 443 ? 5.678   9.221  82.381  1.00 17.27  ? 443 VAL A C   1 
ATOM   3743 O O   . VAL A 1 443 ? 5.329   10.220 81.733  1.00 23.13  ? 443 VAL A O   1 
ATOM   3744 C CB  . VAL A 1 443 ? 4.031   7.458  83.108  1.00 13.54  ? 443 VAL A CB  1 
ATOM   3745 C CG1 . VAL A 1 443 ? 2.924   8.498  83.075  1.00 17.10  ? 443 VAL A CG1 1 
ATOM   3746 C CG2 . VAL A 1 443 ? 3.484   6.061  82.857  1.00 14.39  ? 443 VAL A CG2 1 
ATOM   3747 N N   . ALA A 1 444 ? 6.536   9.293  83.402  1.00 20.11  ? 444 ALA A N   1 
ATOM   3748 C CA  . ALA A 1 444 ? 7.194   10.529 83.801  1.00 20.56  ? 444 ALA A CA  1 
ATOM   3749 C C   . ALA A 1 444 ? 8.119   11.071 82.727  1.00 21.56  ? 444 ALA A C   1 
ATOM   3750 O O   . ALA A 1 444 ? 8.473   12.252 82.782  1.00 23.83  ? 444 ALA A O   1 
ATOM   3751 C CB  . ALA A 1 444 ? 7.997   10.314 85.084  1.00 16.30  ? 444 ALA A CB  1 
ATOM   3752 N N   . GLU A 1 445 ? 8.525   10.252 81.759  1.00 17.53  ? 445 GLU A N   1 
ATOM   3753 C CA  . GLU A 1 445 ? 9.357   10.792 80.687  1.00 21.52  ? 445 GLU A CA  1 
ATOM   3754 C C   . GLU A 1 445 ? 8.554   11.481 79.588  1.00 16.55  ? 445 GLU A C   1 
ATOM   3755 O O   . GLU A 1 445 ? 9.160   11.999 78.652  1.00 17.83  ? 445 GLU A O   1 
ATOM   3756 C CB  . GLU A 1 445 ? 10.233  9.689  80.085  1.00 22.45  ? 445 GLU A CB  1 
ATOM   3757 C CG  . GLU A 1 445 ? 11.261  9.177  81.079  1.00 20.96  ? 445 GLU A CG  1 
ATOM   3758 C CD  . GLU A 1 445 ? 11.811  7.800  80.741  1.00 21.61  ? 445 GLU A CD  1 
ATOM   3759 O OE1 . GLU A 1 445 ? 11.499  7.262  79.665  1.00 22.71  ? 445 GLU A OE1 1 
ATOM   3760 O OE2 . GLU A 1 445 ? 12.583  7.262  81.556  1.00 24.92  ? 445 GLU A OE2 1 
ATOM   3761 N N   . GLY A 1 446 ? 7.227   11.525 79.690  1.00 16.39  ? 446 GLY A N   1 
ATOM   3762 C CA  . GLY A 1 446 ? 6.438   12.232 78.689  1.00 17.61  ? 446 GLY A CA  1 
ATOM   3763 C C   . GLY A 1 446 ? 6.749   13.723 78.639  1.00 18.84  ? 446 GLY A C   1 
ATOM   3764 O O   . GLY A 1 446 ? 7.016   14.365 79.658  1.00 22.12  ? 446 GLY A O   1 
ATOM   3765 N N   . SER A 1 447 ? 6.685   14.282 77.427  1.00 20.66  ? 447 SER A N   1 
ATOM   3766 C CA  . SER A 1 447 ? 7.066   15.682 77.217  1.00 18.17  ? 447 SER A CA  1 
ATOM   3767 C C   . SER A 1 447 ? 6.182   16.652 77.995  1.00 25.52  ? 447 SER A C   1 
ATOM   3768 O O   . SER A 1 447 ? 6.656   17.719 78.416  1.00 20.13  ? 447 SER A O   1 
ATOM   3769 C CB  . SER A 1 447 ? 7.002   16.011 75.728  1.00 13.74  ? 447 SER A CB  1 
ATOM   3770 O OG  . SER A 1 447 ? 5.649   15.887 75.261  1.00 16.19  ? 447 SER A OG  1 
ATOM   3771 N N   . ASP A 1 448 ? 4.908   16.290 78.211  1.00 17.26  ? 448 ASP A N   1 
ATOM   3772 C CA  . ASP A 1 448 ? 3.927   17.236 78.746  1.00 13.68  ? 448 ASP A CA  1 
ATOM   3773 C C   . ASP A 1 448 ? 4.315   17.774 80.118  1.00 13.64  ? 448 ASP A C   1 
ATOM   3774 O O   . ASP A 1 448 ? 4.124   18.967 80.399  1.00 16.96  ? 448 ASP A O   1 
ATOM   3775 C CB  . ASP A 1 448 ? 2.551   16.575 78.813  1.00 18.74  ? 448 ASP A CB  1 
ATOM   3776 C CG  . ASP A 1 448 ? 2.133   15.975 77.478  1.00 18.99  ? 448 ASP A CG  1 
ATOM   3777 O OD1 . ASP A 1 448 ? 2.621   14.885 77.130  1.00 19.95  ? 448 ASP A OD1 1 
ATOM   3778 O OD2 . ASP A 1 448 ? 1.318   16.598 76.775  1.00 18.55  ? 448 ASP A OD2 1 
ATOM   3779 N N   . TRP A 1 449 ? 4.830   16.916 81.003  1.00 15.80  ? 449 TRP A N   1 
ATOM   3780 C CA  . TRP A 1 449 ? 5.176   17.383 82.344  1.00 14.14  ? 449 TRP A CA  1 
ATOM   3781 C C   . TRP A 1 449 ? 6.215   18.504 82.277  1.00 16.36  ? 449 TRP A C   1 
ATOM   3782 O O   . TRP A 1 449 ? 6.172   19.469 83.057  1.00 16.39  ? 449 TRP A O   1 
ATOM   3783 C CB  . TRP A 1 449 ? 5.686   16.202 83.178  1.00 16.35  ? 449 TRP A CB  1 
ATOM   3784 C CG  . TRP A 1 449 ? 4.924   14.939 82.913  1.00 18.56  ? 449 TRP A CG  1 
ATOM   3785 C CD1 . TRP A 1 449 ? 5.408   13.771 82.374  1.00 17.90  ? 449 TRP A CD1 1 
ATOM   3786 C CD2 . TRP A 1 449 ? 3.529   14.718 83.169  1.00 21.13  ? 449 TRP A CD2 1 
ATOM   3787 N NE1 . TRP A 1 449 ? 4.391   12.834 82.287  1.00 18.02  ? 449 TRP A NE1 1 
ATOM   3788 C CE2 . TRP A 1 449 ? 3.231   13.393 82.765  1.00 18.88  ? 449 TRP A CE2 1 
ATOM   3789 C CE3 . TRP A 1 449 ? 2.501   15.519 83.692  1.00 15.21  ? 449 TRP A CE3 1 
ATOM   3790 C CZ2 . TRP A 1 449 ? 1.943   12.850 82.867  1.00 18.80  ? 449 TRP A CZ2 1 
ATOM   3791 C CZ3 . TRP A 1 449 ? 1.215   14.971 83.812  1.00 13.08  ? 449 TRP A CZ3 1 
ATOM   3792 C CH2 . TRP A 1 449 ? 0.952   13.645 83.398  1.00 14.43  ? 449 TRP A CH2 1 
ATOM   3793 N N   . PHE A 1 450 ? 7.154   18.394 81.339  1.00 18.77  ? 450 PHE A N   1 
ATOM   3794 C CA  . PHE A 1 450 ? 8.198   19.401 81.186  1.00 16.49  ? 450 PHE A CA  1 
ATOM   3795 C C   . PHE A 1 450 ? 7.692   20.626 80.431  1.00 20.32  ? 450 PHE A C   1 
ATOM   3796 O O   . PHE A 1 450 ? 8.168   21.744 80.674  1.00 17.61  ? 450 PHE A O   1 
ATOM   3797 C CB  . PHE A 1 450 ? 9.394   18.777 80.471  1.00 17.50  ? 450 PHE A CB  1 
ATOM   3798 C CG  . PHE A 1 450 ? 9.949   17.557 81.176  1.00 21.45  ? 450 PHE A CG  1 
ATOM   3799 C CD1 . PHE A 1 450 ? 9.401   16.302 80.960  1.00 19.83  ? 450 PHE A CD1 1 
ATOM   3800 C CD2 . PHE A 1 450 ? 10.998  17.676 82.063  1.00 18.30  ? 450 PHE A CD2 1 
ATOM   3801 C CE1 . PHE A 1 450 ? 9.886   15.192 81.623  1.00 21.48  ? 450 PHE A CE1 1 
ATOM   3802 C CE2 . PHE A 1 450 ? 11.506  16.554 82.725  1.00 21.64  ? 450 PHE A CE2 1 
ATOM   3803 C CZ  . PHE A 1 450 ? 10.941  15.316 82.501  1.00 20.27  ? 450 PHE A CZ  1 
ATOM   3804 N N   . TRP A 1 451 ? 6.727   20.428 79.534  1.00 21.53  ? 451 TRP A N   1 
ATOM   3805 C CA  . TRP A 1 451 ? 6.095   21.537 78.820  1.00 21.27  ? 451 TRP A CA  1 
ATOM   3806 C C   . TRP A 1 451 ? 5.456   22.535 79.783  1.00 26.51  ? 451 TRP A C   1 
ATOM   3807 O O   . TRP A 1 451 ? 5.621   23.754 79.636  1.00 22.47  ? 451 TRP A O   1 
ATOM   3808 C CB  . TRP A 1 451 ? 5.042   20.966 77.879  1.00 19.67  ? 451 TRP A CB  1 
ATOM   3809 C CG  . TRP A 1 451 ? 4.720   21.785 76.696  1.00 24.49  ? 451 TRP A CG  1 
ATOM   3810 C CD1 . TRP A 1 451 ? 5.282   21.686 75.454  1.00 28.14  ? 451 TRP A CD1 1 
ATOM   3811 C CD2 . TRP A 1 451 ? 3.731   22.806 76.610  1.00 32.97  ? 451 TRP A CD2 1 
ATOM   3812 N NE1 . TRP A 1 451 ? 4.711   22.597 74.606  1.00 37.05  ? 451 TRP A NE1 1 
ATOM   3813 C CE2 . TRP A 1 451 ? 3.756   23.301 75.291  1.00 37.42  ? 451 TRP A CE2 1 
ATOM   3814 C CE3 . TRP A 1 451 ? 2.832   23.358 77.522  1.00 39.31  ? 451 TRP A CE3 1 
ATOM   3815 C CZ2 . TRP A 1 451 ? 2.915   24.325 74.862  1.00 35.44  ? 451 TRP A CZ2 1 
ATOM   3816 C CZ3 . TRP A 1 451 ? 1.999   24.372 77.097  1.00 43.52  ? 451 TRP A CZ3 1 
ATOM   3817 C CH2 . TRP A 1 451 ? 2.046   24.845 75.776  1.00 43.32  ? 451 TRP A CH2 1 
ATOM   3818 N N   . TRP A 1 452 ? 4.713   22.036 80.771  1.00 23.77  ? 452 TRP A N   1 
ATOM   3819 C CA  . TRP A 1 452 ? 3.982   22.918 81.669  1.00 23.63  ? 452 TRP A CA  1 
ATOM   3820 C C   . TRP A 1 452 ? 4.849   23.473 82.789  1.00 27.85  ? 452 TRP A C   1 
ATOM   3821 O O   . TRP A 1 452 ? 4.542   24.542 83.324  1.00 27.86  ? 452 TRP A O   1 
ATOM   3822 C CB  . TRP A 1 452 ? 2.764   22.165 82.235  1.00 19.94  ? 452 TRP A CB  1 
ATOM   3823 C CG  . TRP A 1 452 ? 1.775   21.878 81.163  1.00 20.54  ? 452 TRP A CG  1 
ATOM   3824 C CD1 . TRP A 1 452 ? 1.523   20.673 80.574  1.00 18.23  ? 452 TRP A CD1 1 
ATOM   3825 C CD2 . TRP A 1 452 ? 0.915   22.828 80.515  1.00 16.58  ? 452 TRP A CD2 1 
ATOM   3826 N NE1 . TRP A 1 452 ? 0.564   20.814 79.608  1.00 18.39  ? 452 TRP A NE1 1 
ATOM   3827 C CE2 . TRP A 1 452 ? 0.179   22.125 79.544  1.00 18.56  ? 452 TRP A CE2 1 
ATOM   3828 C CE3 . TRP A 1 452 ? 0.707   24.204 80.657  1.00 22.40  ? 452 TRP A CE3 1 
ATOM   3829 C CZ2 . TRP A 1 452 ? -0.764  22.747 78.726  1.00 24.10  ? 452 TRP A CZ2 1 
ATOM   3830 C CZ3 . TRP A 1 452 ? -0.221  24.823 79.840  1.00 25.56  ? 452 TRP A CZ3 1 
ATOM   3831 C CH2 . TRP A 1 452 ? -0.950  24.096 78.891  1.00 27.85  ? 452 TRP A CH2 1 
ATOM   3832 N N   . GLN A 1 453 ? 5.900   22.826 83.138  1.00 26.83  ? 453 GLN A N   1 
ATOM   3833 C CA  . GLN A 1 453 ? 6.729   23.241 84.157  1.00 30.33  ? 453 GLN A CA  1 
ATOM   3834 C C   . GLN A 1 453 ? 7.423   24.563 83.888  1.00 27.91  ? 453 GLN A C   1 
ATOM   3835 O O   . GLN A 1 453 ? 7.892   24.838 82.948  1.00 27.53  ? 453 GLN A O   1 
ATOM   3836 C CB  . GLN A 1 453 ? 7.669   22.127 84.536  1.00 28.06  ? 453 GLN A CB  1 
ATOM   3837 C CG  . GLN A 1 453 ? 8.684   22.446 85.557  1.00 33.20  ? 453 GLN A CG  1 
ATOM   3838 C CD  . GLN A 1 453 ? 8.161   22.544 87.021  1.00 37.94  ? 453 GLN A CD  1 
ATOM   3839 O OE1 . GLN A 1 453 ? 7.024   22.525 87.298  1.00 27.91  ? 453 GLN A OE1 1 
ATOM   3840 N NE2 . GLN A 1 453 ? 9.117   22.662 87.931  1.00 34.09  ? 453 GLN A NE2 1 
ATOM   3841 N N   . GLY A 1 454 ? 7.383   25.356 84.875  1.00 36.36  ? 454 GLY A N   1 
ATOM   3842 C CA  . GLY A 1 454 ? 8.037   26.629 84.923  1.00 43.46  ? 454 GLY A CA  1 
ATOM   3843 C C   . GLY A 1 454 ? 7.639   27.591 83.924  1.00 55.59  ? 454 GLY A C   1 
ATOM   3844 O O   . GLY A 1 454 ? 8.398   28.257 83.326  1.00 55.96  ? 454 GLY A O   1 
ATOM   3845 N N   . GLU A 1 455 ? 6.359   27.617 83.786  1.00 66.38  ? 455 GLU A N   1 
ATOM   3846 C CA  . GLU A 1 455 ? 5.719   28.465 82.923  1.00 74.05  ? 455 GLU A CA  1 
ATOM   3847 C C   . GLU A 1 455 ? 4.575   28.776 83.727  1.00 82.52  ? 455 GLU A C   1 
ATOM   3848 O O   . GLU A 1 455 ? 3.914   27.915 84.331  1.00 83.10  ? 455 GLU A O   1 
ATOM   3849 C CB  . GLU A 1 455 ? 5.030   27.815 81.796  1.00 73.44  ? 455 GLU A CB  1 
ATOM   3850 C CG  . GLU A 1 455 ? 5.791   26.952 80.922  1.00 72.81  ? 455 GLU A CG  1 
ATOM   3851 C CD  . GLU A 1 455 ? 6.517   27.682 79.874  1.00 71.38  ? 455 GLU A CD  1 
ATOM   3852 O OE1 . GLU A 1 455 ? 7.376   27.031 79.328  1.00 65.70  ? 455 GLU A OE1 1 
ATOM   3853 O OE2 . GLU A 1 455 ? 6.142   28.845 79.564  1.00 73.81  ? 455 GLU A OE2 1 
ATOM   3854 N N   . GLU A 1 456 ? 4.399   30.064 83.668  1.00 88.60  ? 456 GLU A N   1 
ATOM   3855 C CA  . GLU A 1 456 ? 3.355   30.843 84.164  1.00 95.45  ? 456 GLU A CA  1 
ATOM   3856 C C   . GLU A 1 456 ? 2.156   30.013 84.746  1.00 98.03  ? 456 GLU A C   1 
ATOM   3857 O O   . GLU A 1 456 ? 1.662   29.064 84.148  1.00 98.14  ? 456 GLU A O   1 
ATOM   3858 C CB  . GLU A 1 456 ? 3.056   31.745 82.945  1.00 97.44  ? 456 GLU A CB  1 
ATOM   3859 C CG  . GLU A 1 456 ? 1.785   32.495 82.903  1.00 100.17 ? 456 GLU A CG  1 
ATOM   3860 C CD  . GLU A 1 456 ? 0.629   31.563 82.949  1.00 102.78 ? 456 GLU A CD  1 
ATOM   3861 O OE1 . GLU A 1 456 ? 0.398   30.904 81.899  1.00 102.82 ? 456 GLU A OE1 1 
ATOM   3862 O OE2 . GLU A 1 456 ? -0.002  31.482 84.076  1.00 103.66 ? 456 GLU A OE2 1 
ATOM   3863 N N   . LYS A 1 457 ? 1.685   30.439 85.914  1.00 97.30  ? 457 LYS A N   1 
ATOM   3864 C CA  . LYS A 1 457 ? 0.666   29.745 86.646  1.00 93.20  ? 457 LYS A CA  1 
ATOM   3865 C C   . LYS A 1 457 ? -0.814  29.997 86.513  1.00 90.31  ? 457 LYS A C   1 
ATOM   3866 O O   . LYS A 1 457 ? -1.350  30.864 87.100  1.00 91.67  ? 457 LYS A O   1 
ATOM   3867 C CB  . LYS A 1 457 ? 1.024   29.830 88.070  1.00 91.32  ? 457 LYS A CB  1 
ATOM   3868 C CG  . LYS A 1 457 ? 2.399   29.242 88.308  1.00 89.65  ? 457 LYS A CG  1 
ATOM   3869 C CD  . LYS A 1 457 ? 2.515   27.814 87.844  1.00 89.17  ? 457 LYS A CD  1 
ATOM   3870 C CE  . LYS A 1 457 ? 1.292   26.994 88.148  1.00 89.97  ? 457 LYS A CE  1 
ATOM   3871 N NZ  . LYS A 1 457 ? 1.168   25.777 87.276  1.00 88.96  ? 457 LYS A NZ  1 
ATOM   3872 N N   . ALA A 1 458 ? -1.451  29.147 85.781  1.00 84.89  ? 458 ALA A N   1 
ATOM   3873 C CA  . ALA A 1 458 ? -2.830  29.238 85.566  1.00 81.40  ? 458 ALA A CA  1 
ATOM   3874 C C   . ALA A 1 458 ? -3.559  28.084 86.190  1.00 77.22  ? 458 ALA A C   1 
ATOM   3875 O O   . ALA A 1 458 ? -2.943  27.199 86.712  1.00 76.54  ? 458 ALA A O   1 
ATOM   3876 C CB  . ALA A 1 458 ? -3.038  29.308 84.100  1.00 81.11  ? 458 ALA A CB  1 
ATOM   3877 N N   . PRO A 1 459 ? -4.933  28.170 86.180  1.00 73.29  ? 459 PRO A N   1 
ATOM   3878 C CA  . PRO A 1 459 ? -5.589  27.052 86.841  1.00 69.77  ? 459 PRO A CA  1 
ATOM   3879 C C   . PRO A 1 459 ? -5.168  25.712 86.398  1.00 65.26  ? 459 PRO A C   1 
ATOM   3880 O O   . PRO A 1 459 ? -4.847  25.439 85.275  1.00 65.49  ? 459 PRO A O   1 
ATOM   3881 C CB  . PRO A 1 459 ? -7.127  27.310 86.656  1.00 71.12  ? 459 PRO A CB  1 
ATOM   3882 C CG  . PRO A 1 459 ? -7.259  28.507 85.846  1.00 71.31  ? 459 PRO A CG  1 
ATOM   3883 C CD  . PRO A 1 459 ? -5.989  29.251 85.936  1.00 72.38  ? 459 PRO A CD  1 
ATOM   3884 N N   . PHE A 1 460 ? -5.101  24.860 87.372  1.00 60.60  ? 460 PHE A N   1 
ATOM   3885 C CA  . PHE A 1 460 ? -4.955  23.415 87.183  1.00 54.17  ? 460 PHE A CA  1 
ATOM   3886 C C   . PHE A 1 460 ? -3.595  22.993 86.640  1.00 49.87  ? 460 PHE A C   1 
ATOM   3887 O O   . PHE A 1 460 ? -3.378  21.797 86.445  1.00 49.52  ? 460 PHE A O   1 
ATOM   3888 C CB  . PHE A 1 460 ? -6.052  22.838 86.280  1.00 51.49  ? 460 PHE A CB  1 
ATOM   3889 C CG  . PHE A 1 460 ? -7.434  23.309 86.629  1.00 54.31  ? 460 PHE A CG  1 
ATOM   3890 C CD1 . PHE A 1 460 ? -8.078  22.823 87.752  1.00 56.78  ? 460 PHE A CD1 1 
ATOM   3891 C CD2 . PHE A 1 460 ? -8.081  24.250 85.846  1.00 58.10  ? 460 PHE A CD2 1 
ATOM   3892 C CE1 . PHE A 1 460 ? -9.349  23.260 88.085  1.00 60.40  ? 460 PHE A CE1 1 
ATOM   3893 C CE2 . PHE A 1 460 ? -9.349  24.696 86.176  1.00 60.74  ? 460 PHE A CE2 1 
ATOM   3894 C CZ  . PHE A 1 460 ? -9.985  24.197 87.295  1.00 60.75  ? 460 PHE A CZ  1 
ATOM   3895 N N   . VAL A 1 461 ? -2.670  23.922 86.388  1.00 45.98  ? 461 VAL A N   1 
ATOM   3896 C CA  . VAL A 1 461 ? -1.336  23.488 86.004  1.00 43.01  ? 461 VAL A CA  1 
ATOM   3897 C C   . VAL A 1 461 ? -0.614  22.860 87.189  1.00 39.44  ? 461 VAL A C   1 
ATOM   3898 O O   . VAL A 1 461 ? 0.303   22.053 87.000  1.00 37.68  ? 461 VAL A O   1 
ATOM   3899 C CB  . VAL A 1 461 ? -0.529  24.655 85.398  1.00 49.22  ? 461 VAL A CB  1 
ATOM   3900 C CG1 . VAL A 1 461 ? 0.761   24.151 84.764  1.00 50.19  ? 461 VAL A CG1 1 
ATOM   3901 C CG2 . VAL A 1 461 ? -1.372  25.403 84.376  1.00 49.51  ? 461 VAL A CG2 1 
ATOM   3902 N N   . GLU A 1 462 ? -1.020  23.198 88.418  1.00 28.68  ? 462 GLU A N   1 
ATOM   3903 C CA  . GLU A 1 462 ? -0.546  22.475 89.591  1.00 26.52  ? 462 GLU A CA  1 
ATOM   3904 C C   . GLU A 1 462 ? -0.918  20.998 89.542  1.00 26.16  ? 462 GLU A C   1 
ATOM   3905 O O   . GLU A 1 462 ? -0.244  20.176 90.172  1.00 31.55  ? 462 GLU A O   1 
ATOM   3906 C CB  . GLU A 1 462 ? -1.108  23.098 90.866  1.00 36.37  ? 462 GLU A CB  1 
ATOM   3907 C CG  . GLU A 1 462 ? -0.416  24.378 91.277  1.00 49.84  ? 462 GLU A CG  1 
ATOM   3908 C CD  . GLU A 1 462 ? -1.222  25.168 92.287  1.00 61.10  ? 462 GLU A CD  1 
ATOM   3909 O OE1 . GLU A 1 462 ? -1.872  24.535 93.150  1.00 65.76  ? 462 GLU A OE1 1 
ATOM   3910 O OE2 . GLU A 1 462 ? -1.212  26.418 92.209  1.00 63.74  ? 462 GLU A OE2 1 
ATOM   3911 N N   . VAL A 1 463 ? -1.986  20.645 88.825  1.00 27.38  ? 463 VAL A N   1 
ATOM   3912 C CA  . VAL A 1 463 ? -2.368  19.241 88.721  1.00 24.66  ? 463 VAL A CA  1 
ATOM   3913 C C   . VAL A 1 463 ? -1.322  18.465 87.931  1.00 22.08  ? 463 VAL A C   1 
ATOM   3914 O O   . VAL A 1 463 ? -1.014  17.313 88.250  1.00 22.15  ? 463 VAL A O   1 
ATOM   3915 C CB  . VAL A 1 463 ? -3.767  19.112 88.095  1.00 21.21  ? 463 VAL A CB  1 
ATOM   3916 C CG1 . VAL A 1 463 ? -4.131  17.644 87.907  1.00 20.23  ? 463 VAL A CG1 1 
ATOM   3917 C CG2 . VAL A 1 463 ? -4.802  19.843 88.965  1.00 19.52  ? 463 VAL A CG2 1 
ATOM   3918 N N   . PHE A 1 464 ? -0.763  19.083 86.882  1.00 19.91  ? 464 PHE A N   1 
ATOM   3919 C CA  . PHE A 1 464 ? 0.317   18.441 86.137  1.00 23.19  ? 464 PHE A CA  1 
ATOM   3920 C C   . PHE A 1 464 ? 1.519   18.172 87.031  1.00 17.08  ? 464 PHE A C   1 
ATOM   3921 O O   . PHE A 1 464 ? 2.194   17.148 86.889  1.00 22.07  ? 464 PHE A O   1 
ATOM   3922 C CB  . PHE A 1 464 ? 0.718   19.308 84.939  1.00 21.70  ? 464 PHE A CB  1 
ATOM   3923 C CG  . PHE A 1 464 ? -0.273  19.263 83.810  1.00 21.74  ? 464 PHE A CG  1 
ATOM   3924 C CD1 . PHE A 1 464 ? -1.342  20.150 83.773  1.00 28.16  ? 464 PHE A CD1 1 
ATOM   3925 C CD2 . PHE A 1 464 ? -0.155  18.319 82.806  1.00 20.91  ? 464 PHE A CD2 1 
ATOM   3926 C CE1 . PHE A 1 464 ? -2.267  20.109 82.740  1.00 27.92  ? 464 PHE A CE1 1 
ATOM   3927 C CE2 . PHE A 1 464 ? -1.076  18.271 81.769  1.00 24.34  ? 464 PHE A CE2 1 
ATOM   3928 C CZ  . PHE A 1 464 ? -2.135  19.168 81.739  1.00 20.61  ? 464 PHE A CZ  1 
ATOM   3929 N N   . ASP A 1 465 ? 1.817   19.089 87.948  1.00 19.85  ? 465 ASP A N   1 
ATOM   3930 C CA  . ASP A 1 465 ? 2.951   18.863 88.832  1.00 16.50  ? 465 ASP A CA  1 
ATOM   3931 C C   . ASP A 1 465 ? 2.658   17.731 89.805  1.00 21.90  ? 465 ASP A C   1 
ATOM   3932 O O   . ASP A 1 465 ? 3.539   16.918 90.110  1.00 18.61  ? 465 ASP A O   1 
ATOM   3933 C CB  . ASP A 1 465 ? 3.307   20.149 89.574  1.00 19.83  ? 465 ASP A CB  1 
ATOM   3934 C CG  . ASP A 1 465 ? 4.320   19.919 90.668  1.00 21.95  ? 465 ASP A CG  1 
ATOM   3935 O OD1 . ASP A 1 465 ? 5.535   19.787 90.353  1.00 22.88  ? 465 ASP A OD1 1 
ATOM   3936 O OD2 . ASP A 1 465 ? 3.896   19.840 91.839  1.00 25.37  ? 465 ASP A OD2 1 
ATOM   3937 N N   . LYS A 1 466 ? 1.414   17.663 90.292  1.00 17.25  ? 466 LYS A N   1 
ATOM   3938 C CA  . LYS A 1 466 ? 0.993   16.568 91.161  1.00 21.46  ? 466 LYS A CA  1 
ATOM   3939 C C   . LYS A 1 466 ? 1.114   15.229 90.446  1.00 20.46  ? 466 LYS A C   1 
ATOM   3940 O O   . LYS A 1 466 ? 1.546   14.229 91.035  1.00 22.70  ? 466 LYS A O   1 
ATOM   3941 C CB  . LYS A 1 466 ? -0.458  16.810 91.613  1.00 28.88  ? 466 LYS A CB  1 
ATOM   3942 C CG  . LYS A 1 466 ? -1.199  15.563 92.105  1.00 39.98  ? 466 LYS A CG  1 
ATOM   3943 C CD  . LYS A 1 466 ? -0.908  15.293 93.563  1.00 50.50  ? 466 LYS A CD  1 
ATOM   3944 C CE  . LYS A 1 466 ? -1.230  13.861 93.958  1.00 58.84  ? 466 LYS A CE  1 
ATOM   3945 N NZ  . LYS A 1 466 ? -0.410  13.415 95.131  1.00 61.94  ? 466 LYS A NZ  1 
ATOM   3946 N N   . LEU A 1 467 ? 0.725   15.193 89.171  1.00 18.37  ? 467 LEU A N   1 
ATOM   3947 C CA  . LEU A 1 467 ? 0.772   13.955 88.404  1.00 15.03  ? 467 LEU A CA  1 
ATOM   3948 C C   . LEU A 1 467 ? 2.212   13.529 88.138  1.00 19.43  ? 467 LEU A C   1 
ATOM   3949 O O   . LEU A 1 467 ? 2.574   12.361 88.339  1.00 19.38  ? 467 LEU A O   1 
ATOM   3950 C CB  . LEU A 1 467 ? 0.021   14.131 87.085  1.00 13.37  ? 467 LEU A CB  1 
ATOM   3951 C CG  . LEU A 1 467 ? -1.512  14.084 87.152  1.00 19.89  ? 467 LEU A CG  1 
ATOM   3952 C CD1 . LEU A 1 467 ? -2.138  14.689 85.886  1.00 16.46  ? 467 LEU A CD1 1 
ATOM   3953 C CD2 . LEU A 1 467 ? -1.962  12.655 87.338  1.00 22.45  ? 467 LEU A CD2 1 
ATOM   3954 N N   . PHE A 1 468 ? 3.045   14.462 87.674  1.00 18.58  ? 468 PHE A N   1 
ATOM   3955 C CA  . PHE A 1 468 ? 4.441   14.126 87.399  1.00 17.32  ? 468 PHE A CA  1 
ATOM   3956 C C   . PHE A 1 468 ? 5.098   13.532 88.634  1.00 21.06  ? 468 PHE A C   1 
ATOM   3957 O O   . PHE A 1 468 ? 5.634   12.418 88.592  1.00 19.69  ? 468 PHE A O   1 
ATOM   3958 C CB  . PHE A 1 468 ? 5.200   15.363 86.934  1.00 19.19  ? 468 PHE A CB  1 
ATOM   3959 C CG  . PHE A 1 468 ? 6.695   15.166 86.841  1.00 22.68  ? 468 PHE A CG  1 
ATOM   3960 C CD1 . PHE A 1 468 ? 7.253   14.462 85.783  1.00 23.09  ? 468 PHE A CD1 1 
ATOM   3961 C CD2 . PHE A 1 468 ? 7.539   15.684 87.810  1.00 13.86  ? 468 PHE A CD2 1 
ATOM   3962 C CE1 . PHE A 1 468 ? 8.629   14.291 85.683  1.00 21.34  ? 468 PHE A CE1 1 
ATOM   3963 C CE2 . PHE A 1 468 ? 8.923   15.517 87.713  1.00 22.65  ? 468 PHE A CE2 1 
ATOM   3964 C CZ  . PHE A 1 468 ? 9.465   14.815 86.649  1.00 20.18  ? 468 PHE A CZ  1 
ATOM   3965 N N   . ARG A 1 469 ? 5.006   14.237 89.764  1.00 22.69  ? 469 ARG A N   1 
ATOM   3966 C CA  . ARG A 1 469 ? 5.687   13.784 90.972  1.00 23.80  ? 469 ARG A CA  1 
ATOM   3967 C C   . ARG A 1 469 ? 5.088   12.495 91.526  1.00 28.05  ? 469 ARG A C   1 
ATOM   3968 O O   . ARG A 1 469 ? 5.801   11.708 92.160  1.00 24.70  ? 469 ARG A O   1 
ATOM   3969 C CB  . ARG A 1 469 ? 5.659   14.893 92.024  1.00 19.77  ? 469 ARG A CB  1 
ATOM   3970 C CG  . ARG A 1 469 ? 6.414   16.129 91.585  1.00 20.58  ? 469 ARG A CG  1 
ATOM   3971 C CD  . ARG A 1 469 ? 6.356   17.229 92.636  1.00 23.85  ? 469 ARG A CD  1 
ATOM   3972 N NE  . ARG A 1 469 ? 7.100   18.436 92.258  1.00 23.05  ? 469 ARG A NE  1 
ATOM   3973 C CZ  . ARG A 1 469 ? 8.358   18.685 92.619  1.00 25.51  ? 469 ARG A CZ  1 
ATOM   3974 N NH1 . ARG A 1 469 ? 9.028   17.805 93.359  1.00 19.13  ? 469 ARG A NH1 1 
ATOM   3975 N NH2 . ARG A 1 469 ? 8.943   19.822 92.247  1.00 24.40  ? 469 ARG A NH2 1 
ATOM   3976 N N   . SER A 1 470 ? 3.790   12.261 91.302  1.00 24.33  ? 470 SER A N   1 
ATOM   3977 C CA  . SER A 1 470 ? 3.187   10.994 91.705  1.00 24.73  ? 470 SER A CA  1 
ATOM   3978 C C   . SER A 1 470 ? 3.726   9.839  90.880  1.00 18.40  ? 470 SER A C   1 
ATOM   3979 O O   . SER A 1 470 ? 3.976   8.750  91.414  1.00 20.78  ? 470 SER A O   1 
ATOM   3980 C CB  . SER A 1 470 ? 1.666   11.059 91.561  1.00 25.46  ? 470 SER A CB  1 
ATOM   3981 O OG  . SER A 1 470 ? 1.086   11.826 92.593  1.00 31.06  ? 470 SER A OG  1 
ATOM   3982 N N   . PHE A 1 471 ? 3.848   10.035 89.565  1.00 18.32  ? 471 PHE A N   1 
ATOM   3983 C CA  . PHE A 1 471 ? 4.403   8.993  88.703  1.00 18.56  ? 471 PHE A CA  1 
ATOM   3984 C C   . PHE A 1 471 ? 5.863   8.710  89.064  1.00 22.71  ? 471 PHE A C   1 
ATOM   3985 O O   . PHE A 1 471 ? 6.302   7.550  89.067  1.00 22.20  ? 471 PHE A O   1 
ATOM   3986 C CB  . PHE A 1 471 ? 4.281   9.404  87.230  1.00 20.26  ? 471 PHE A CB  1 
ATOM   3987 C CG  . PHE A 1 471 ? 2.854   9.462  86.718  1.00 26.85  ? 471 PHE A CG  1 
ATOM   3988 C CD1 . PHE A 1 471 ? 1.954   8.448  87.006  1.00 30.50  ? 471 PHE A CD1 1 
ATOM   3989 C CD2 . PHE A 1 471 ? 2.416   10.540 85.959  1.00 19.34  ? 471 PHE A CD2 1 
ATOM   3990 C CE1 . PHE A 1 471 ? 0.646   8.503  86.537  1.00 30.79  ? 471 PHE A CE1 1 
ATOM   3991 C CE2 . PHE A 1 471 ? 1.113   10.607 85.488  1.00 19.91  ? 471 PHE A CE2 1 
ATOM   3992 C CZ  . PHE A 1 471 ? 0.223   9.591  85.780  1.00 22.05  ? 471 PHE A CZ  1 
ATOM   3993 N N   . VAL A 1 472 ? 6.622   9.757  89.391  1.00 24.78  ? 472 VAL A N   1 
ATOM   3994 C CA  . VAL A 1 472 ? 8.021   9.567  89.757  1.00 25.52  ? 472 VAL A CA  1 
ATOM   3995 C C   . VAL A 1 472 ? 8.122   8.795  91.067  1.00 25.57  ? 472 VAL A C   1 
ATOM   3996 O O   . VAL A 1 472 ? 8.944   7.881  91.200  1.00 24.64  ? 472 VAL A O   1 
ATOM   3997 C CB  . VAL A 1 472 ? 8.744   10.926 89.817  1.00 30.32  ? 472 VAL A CB  1 
ATOM   3998 C CG1 . VAL A 1 472 ? 9.921   10.869 90.772  1.00 36.32  ? 472 VAL A CG1 1 
ATOM   3999 C CG2 . VAL A 1 472 ? 9.221   11.318 88.422  1.00 26.70  ? 472 VAL A CG2 1 
ATOM   4000 N N   . ARG A 1 473 ? 7.249   9.110  92.035  1.00 24.27  ? 473 ARG A N   1 
ATOM   4001 C CA  . ARG A 1 473 ? 7.230   8.369  93.295  1.00 28.66  ? 473 ARG A CA  1 
ATOM   4002 C C   . ARG A 1 473 ? 6.812   6.920  93.076  1.00 28.52  ? 473 ARG A C   1 
ATOM   4003 O O   . ARG A 1 473 ? 7.456   5.991  93.580  1.00 34.81  ? 473 ARG A O   1 
ATOM   4004 C CB  . ARG A 1 473 ? 6.296   9.054  94.291  1.00 33.36  ? 473 ARG A CB  1 
ATOM   4005 C CG  . ARG A 1 473 ? 6.547   8.649  95.731  1.00 43.27  ? 473 ARG A CG  1 
ATOM   4006 C CD  . ARG A 1 473 ? 5.263   8.580  96.549  1.00 49.55  ? 473 ARG A CD  1 
ATOM   4007 N NE  . ARG A 1 473 ? 5.536   8.272  97.953  1.00 55.80  ? 473 ARG A NE  1 
ATOM   4008 C CZ  . ARG A 1 473 ? 5.150   9.028  98.975  1.00 60.06  ? 473 ARG A CZ  1 
ATOM   4009 N NH1 . ARG A 1 473 ? 4.462   10.140 98.754  1.00 58.49  ? 473 ARG A NH1 1 
ATOM   4010 N NH2 . ARG A 1 473 ? 5.447   8.670  100.219 1.00 62.20  ? 473 ARG A NH2 1 
ATOM   4011 N N   . ARG A 1 474 ? 5.744   6.710  92.312  1.00 28.11  ? 474 ARG A N   1 
ATOM   4012 C CA  . ARG A 1 474 ? 5.269   5.355  92.055  1.00 29.37  ? 474 ARG A CA  1 
ATOM   4013 C C   . ARG A 1 474 ? 6.310   4.520  91.301  1.00 28.59  ? 474 ARG A C   1 
ATOM   4014 O O   . ARG A 1 474 ? 6.451   3.316  91.550  1.00 31.48  ? 474 ARG A O   1 
ATOM   4015 C CB  . ARG A 1 474 ? 3.951   5.417  91.280  1.00 31.64  ? 474 ARG A CB  1 
ATOM   4016 C CG  . ARG A 1 474 ? 3.444   4.056  90.843  1.00 38.50  ? 474 ARG A CG  1 
ATOM   4017 C CD  . ARG A 1 474 ? 2.707   3.334  91.957  1.00 47.34  ? 474 ARG A CD  1 
ATOM   4018 N NE  . ARG A 1 474 ? 1.895   2.249  91.413  1.00 55.96  ? 474 ARG A NE  1 
ATOM   4019 C CZ  . ARG A 1 474 ? 2.293   0.982  91.330  1.00 60.34  ? 474 ARG A CZ  1 
ATOM   4020 N NH1 . ARG A 1 474 ? 3.497   0.629  91.770  1.00 58.50  ? 474 ARG A NH1 1 
ATOM   4021 N NH2 . ARG A 1 474 ? 1.486   0.064  90.806  1.00 59.33  ? 474 ARG A NH2 1 
ATOM   4022 N N   . ALA A 1 475 ? 7.055   5.146  90.385  1.00 31.54  ? 475 ALA A N   1 
ATOM   4023 C CA  . ALA A 1 475 ? 8.087   4.445  89.621  1.00 25.15  ? 475 ALA A CA  1 
ATOM   4024 C C   . ALA A 1 475 ? 9.139   3.779  90.498  1.00 30.49  ? 475 ALA A C   1 
ATOM   4025 O O   . ALA A 1 475 ? 9.805   2.845  90.043  1.00 35.09  ? 475 ALA A O   1 
ATOM   4026 C CB  . ALA A 1 475 ? 8.779   5.412  88.661  1.00 18.76  ? 475 ALA A CB  1 
ATOM   4027 N N   . GLN A 1 476 ? 9.318   4.236  91.733  1.00 32.03  ? 476 GLN A N   1 
ATOM   4028 C CA  . GLN A 1 476 ? 10.366  3.722  92.600  1.00 34.43  ? 476 GLN A CA  1 
ATOM   4029 C C   . GLN A 1 476 ? 9.851   2.700  93.607  1.00 40.31  ? 476 GLN A C   1 
ATOM   4030 O O   . GLN A 1 476 ? 10.626  2.245  94.453  1.00 44.79  ? 476 GLN A O   1 
ATOM   4031 C CB  . GLN A 1 476 ? 11.066  4.881  93.314  1.00 28.54  ? 476 GLN A CB  1 
ATOM   4032 C CG  . GLN A 1 476 ? 11.629  5.918  92.342  1.00 33.02  ? 476 GLN A CG  1 
ATOM   4033 C CD  . GLN A 1 476 ? 12.098  7.191  93.021  1.00 37.26  ? 476 GLN A CD  1 
ATOM   4034 O OE1 . GLN A 1 476 ? 13.165  7.217  93.641  1.00 48.66  ? 476 GLN A OE1 1 
ATOM   4035 N NE2 . GLN A 1 476 ? 11.317  8.263  92.891  1.00 26.37  ? 476 GLN A NE2 1 
ATOM   4036 N N   . GLU A 1 477 ? 8.580   2.312  93.518  1.00 38.04  ? 477 GLU A N   1 
ATOM   4037 C CA  . GLU A 1 477 ? 7.985   1.335  94.434  1.00 40.67  ? 477 GLU A CA  1 
ATOM   4038 C C   . GLU A 1 477 ? 7.634   0.035  93.718  1.00 42.25  ? 477 GLU A C   1 
ATOM   4039 O O   . GLU A 1 477 ? 7.415   0.024  92.507  1.00 40.57  ? 477 GLU A O   1 
ATOM   4040 C CB  . GLU A 1 477 ? 6.731   1.912  95.100  1.00 40.06  ? 477 GLU A CB  1 
ATOM   4041 C CG  . GLU A 1 477 ? 7.037   2.904  96.207  1.00 50.06  ? 477 GLU A CG  1 
ATOM   4042 C CD  . GLU A 1 477 ? 5.906   3.883  96.448  1.00 57.96  ? 477 GLU A CD  1 
ATOM   4043 O OE1 . GLU A 1 477 ? 4.764   3.592  96.022  1.00 59.21  ? 477 GLU A OE1 1 
ATOM   4044 O OE2 . GLU A 1 477 ? 6.163   4.946  97.059  1.00 59.95  ? 477 GLU A OE2 1 
ATOM   4045 N N   . LYS B 1 2   ? -25.610 38.585 60.184  1.00 35.87  ? 2   LYS B N   1 
ATOM   4046 C CA  . LYS B 1 2   ? -26.569 38.829 59.109  1.00 38.83  ? 2   LYS B CA  1 
ATOM   4047 C C   . LYS B 1 2   ? -25.845 39.037 57.776  1.00 30.63  ? 2   LYS B C   1 
ATOM   4048 O O   . LYS B 1 2   ? -25.041 39.945 57.633  1.00 37.25  ? 2   LYS B O   1 
ATOM   4049 C CB  . LYS B 1 2   ? -27.448 40.044 59.435  1.00 47.30  ? 2   LYS B CB  1 
ATOM   4050 C CG  . LYS B 1 2   ? -28.250 40.596 58.254  1.00 53.29  ? 2   LYS B CG  1 
ATOM   4051 C CD  . LYS B 1 2   ? -29.159 41.767 58.659  1.00 56.46  ? 2   LYS B CD  1 
ATOM   4052 C CE  . LYS B 1 2   ? -28.363 43.002 59.095  1.00 55.91  ? 2   LYS B CE  1 
ATOM   4053 N NZ  . LYS B 1 2   ? -29.118 43.808 60.103  1.00 56.95  ? 2   LYS B NZ  1 
ATOM   4054 N N   . LYS B 1 3   ? -26.139 38.186 56.803  1.00 30.03  ? 3   LYS B N   1 
ATOM   4055 C CA  . LYS B 1 3   ? -25.528 38.261 55.488  1.00 28.52  ? 3   LYS B CA  1 
ATOM   4056 C C   . LYS B 1 3   ? -26.528 38.808 54.480  1.00 26.67  ? 3   LYS B C   1 
ATOM   4057 O O   . LYS B 1 3   ? -27.744 38.772 54.688  1.00 28.40  ? 3   LYS B O   1 
ATOM   4058 C CB  . LYS B 1 3   ? -25.027 36.884 55.027  1.00 32.44  ? 3   LYS B CB  1 
ATOM   4059 C CG  . LYS B 1 3   ? -24.123 36.166 56.020  1.00 36.09  ? 3   LYS B CG  1 
ATOM   4060 C CD  . LYS B 1 3   ? -22.705 36.050 55.479  1.00 38.61  ? 3   LYS B CD  1 
ATOM   4061 C CE  . LYS B 1 3   ? -21.752 35.480 56.510  1.00 41.71  ? 3   LYS B CE  1 
ATOM   4062 N NZ  . LYS B 1 3   ? -21.236 36.539 57.415  1.00 48.49  ? 3   LYS B NZ  1 
ATOM   4063 N N   . LEU B 1 4   ? -25.993 39.343 53.393  1.00 23.75  ? 4   LEU B N   1 
ATOM   4064 C CA  . LEU B 1 4   ? -26.754 39.593 52.178  1.00 25.80  ? 4   LEU B CA  1 
ATOM   4065 C C   . LEU B 1 4   ? -26.379 38.500 51.187  1.00 28.84  ? 4   LEU B C   1 
ATOM   4066 O O   . LEU B 1 4   ? -25.193 38.287 50.922  1.00 28.71  ? 4   LEU B O   1 
ATOM   4067 C CB  . LEU B 1 4   ? -26.440 40.976 51.593  1.00 21.21  ? 4   LEU B CB  1 
ATOM   4068 C CG  . LEU B 1 4   ? -27.199 41.394 50.321  1.00 24.56  ? 4   LEU B CG  1 
ATOM   4069 C CD1 . LEU B 1 4   ? -27.461 42.890 50.309  1.00 20.85  ? 4   LEU B CD1 1 
ATOM   4070 C CD2 . LEU B 1 4   ? -26.474 40.977 49.024  1.00 28.81  ? 4   LEU B CD2 1 
ATOM   4071 N N   . PHE B 1 5   ? -27.379 37.809 50.650  1.00 25.06  ? 5   PHE B N   1 
ATOM   4072 C CA  . PHE B 1 5   ? -27.157 36.752 49.671  1.00 23.53  ? 5   PHE B CA  1 
ATOM   4073 C C   . PHE B 1 5   ? -27.310 37.322 48.267  1.00 24.68  ? 5   PHE B C   1 
ATOM   4074 O O   . PHE B 1 5   ? -28.386 37.808 47.901  1.00 22.26  ? 5   PHE B O   1 
ATOM   4075 C CB  . PHE B 1 5   ? -28.126 35.591 49.885  1.00 20.53  ? 5   PHE B CB  1 
ATOM   4076 C CG  . PHE B 1 5   ? -27.970 34.920 51.219  1.00 19.40  ? 5   PHE B CG  1 
ATOM   4077 C CD1 . PHE B 1 5   ? -26.747 34.426 51.614  1.00 23.20  ? 5   PHE B CD1 1 
ATOM   4078 C CD2 . PHE B 1 5   ? -29.055 34.791 52.080  1.00 26.85  ? 5   PHE B CD2 1 
ATOM   4079 C CE1 . PHE B 1 5   ? -26.595 33.802 52.851  1.00 31.97  ? 5   PHE B CE1 1 
ATOM   4080 C CE2 . PHE B 1 5   ? -28.915 34.177 53.308  1.00 32.21  ? 5   PHE B CE2 1 
ATOM   4081 C CZ  . PHE B 1 5   ? -27.683 33.678 53.696  1.00 37.19  ? 5   PHE B CZ  1 
ATOM   4082 N N   . LEU B 1 6   ? -26.246 37.232 47.482  1.00 22.98  ? 6   LEU B N   1 
ATOM   4083 C CA  . LEU B 1 6   ? -26.192 37.822 46.153  1.00 27.70  ? 6   LEU B CA  1 
ATOM   4084 C C   . LEU B 1 6   ? -26.140 36.702 45.126  1.00 25.63  ? 6   LEU B C   1 
ATOM   4085 O O   . LEU B 1 6   ? -25.322 35.784 45.245  1.00 25.41  ? 6   LEU B O   1 
ATOM   4086 C CB  . LEU B 1 6   ? -24.976 38.737 46.016  1.00 21.53  ? 6   LEU B CB  1 
ATOM   4087 C CG  . LEU B 1 6   ? -24.844 39.541 44.718  1.00 20.90  ? 6   LEU B CG  1 
ATOM   4088 C CD1 . LEU B 1 6   ? -26.060 40.432 44.463  1.00 18.96  ? 6   LEU B CD1 1 
ATOM   4089 C CD2 . LEU B 1 6   ? -23.574 40.386 44.770  1.00 26.13  ? 6   LEU B CD2 1 
ATOM   4090 N N   . VAL B 1 7   ? -27.005 36.781 44.121  1.00 19.04  ? 7   VAL B N   1 
ATOM   4091 C CA  . VAL B 1 7   ? -27.149 35.725 43.123  1.00 22.78  ? 7   VAL B CA  1 
ATOM   4092 C C   . VAL B 1 7   ? -27.022 36.361 41.744  1.00 19.02  ? 7   VAL B C   1 
ATOM   4093 O O   . VAL B 1 7   ? -27.918 37.092 41.304  1.00 24.48  ? 7   VAL B O   1 
ATOM   4094 C CB  . VAL B 1 7   ? -28.479 34.971 43.264  1.00 21.68  ? 7   VAL B CB  1 
ATOM   4095 C CG1 . VAL B 1 7   ? -28.524 33.778 42.302  1.00 24.90  ? 7   VAL B CG1 1 
ATOM   4096 C CG2 . VAL B 1 7   ? -28.671 34.500 44.701  1.00 21.86  ? 7   VAL B CG2 1 
ATOM   4097 N N   . PHE B 1 8   ? -25.895 36.123 41.085  1.00 16.00  ? 8   PHE B N   1 
ATOM   4098 C CA  . PHE B 1 8   ? -25.709 36.486 39.689  1.00 17.97  ? 8   PHE B CA  1 
ATOM   4099 C C   . PHE B 1 8   ? -26.228 35.360 38.807  1.00 22.68  ? 8   PHE B C   1 
ATOM   4100 O O   . PHE B 1 8   ? -25.913 34.188 39.040  1.00 22.74  ? 8   PHE B O   1 
ATOM   4101 C CB  . PHE B 1 8   ? -24.229 36.719 39.379  1.00 22.38  ? 8   PHE B CB  1 
ATOM   4102 C CG  . PHE B 1 8   ? -23.692 38.006 39.910  1.00 28.97  ? 8   PHE B CG  1 
ATOM   4103 C CD1 . PHE B 1 8   ? -23.926 39.193 39.240  1.00 25.86  ? 8   PHE B CD1 1 
ATOM   4104 C CD2 . PHE B 1 8   ? -22.949 38.029 41.082  1.00 26.49  ? 8   PHE B CD2 1 
ATOM   4105 C CE1 . PHE B 1 8   ? -23.432 40.387 39.725  1.00 29.04  ? 8   PHE B CE1 1 
ATOM   4106 C CE2 . PHE B 1 8   ? -22.452 39.215 41.569  1.00 27.91  ? 8   PHE B CE2 1 
ATOM   4107 C CZ  . PHE B 1 8   ? -22.693 40.398 40.892  1.00 30.84  ? 8   PHE B CZ  1 
ATOM   4108 N N   . TRP B 1 9   ? -26.980 35.719 37.771  1.00 19.66  ? 9   TRP B N   1 
ATOM   4109 C CA  . TRP B 1 9   ? -27.524 34.744 36.830  1.00 23.45  ? 9   TRP B CA  1 
ATOM   4110 C C   . TRP B 1 9   ? -27.393 35.377 35.453  1.00 21.44  ? 9   TRP B C   1 
ATOM   4111 O O   . TRP B 1 9   ? -28.214 36.216 35.066  1.00 21.16  ? 9   TRP B O   1 
ATOM   4112 C CB  . TRP B 1 9   ? -28.964 34.390 37.163  1.00 24.54  ? 9   TRP B CB  1 
ATOM   4113 C CG  . TRP B 1 9   ? -29.500 33.124 36.538  1.00 16.60  ? 9   TRP B CG  1 
ATOM   4114 C CD1 . TRP B 1 9   ? -28.891 32.309 35.620  1.00 18.85  ? 9   TRP B CD1 1 
ATOM   4115 C CD2 . TRP B 1 9   ? -30.775 32.557 36.792  1.00 16.73  ? 9   TRP B CD2 1 
ATOM   4116 N NE1 . TRP B 1 9   ? -29.724 31.253 35.290  1.00 15.35  ? 9   TRP B NE1 1 
ATOM   4117 C CE2 . TRP B 1 9   ? -30.889 31.389 35.998  1.00 21.70  ? 9   TRP B CE2 1 
ATOM   4118 C CE3 . TRP B 1 9   ? -31.846 32.923 37.612  1.00 17.68  ? 9   TRP B CE3 1 
ATOM   4119 C CZ2 . TRP B 1 9   ? -32.030 30.584 36.017  1.00 27.39  ? 9   TRP B CZ2 1 
ATOM   4120 C CZ3 . TRP B 1 9   ? -32.976 32.124 37.626  1.00 27.44  ? 9   TRP B CZ3 1 
ATOM   4121 C CH2 . TRP B 1 9   ? -33.061 30.967 36.832  1.00 27.65  ? 9   TRP B CH2 1 
ATOM   4122 N N   . TRP B 1 10  ? -26.340 34.983 34.746  1.00 17.91  ? 10  TRP B N   1 
ATOM   4123 C CA  . TRP B 1 10  ? -25.985 35.508 33.434  1.00 18.77  ? 10  TRP B CA  1 
ATOM   4124 C C   . TRP B 1 10  ? -26.667 34.681 32.354  1.00 19.87  ? 10  TRP B C   1 
ATOM   4125 O O   . TRP B 1 10  ? -26.424 33.476 32.250  1.00 21.32  ? 10  TRP B O   1 
ATOM   4126 C CB  . TRP B 1 10  ? -24.469 35.455 33.230  1.00 18.18  ? 10  TRP B CB  1 
ATOM   4127 C CG  . TRP B 1 10  ? -23.673 36.242 34.234  1.00 24.08  ? 10  TRP B CG  1 
ATOM   4128 C CD1 . TRP B 1 10  ? -22.889 35.749 35.241  1.00 23.28  ? 10  TRP B CD1 1 
ATOM   4129 C CD2 . TRP B 1 10  ? -23.589 37.659 34.315  1.00 23.01  ? 10  TRP B CD2 1 
ATOM   4130 N NE1 . TRP B 1 10  ? -22.323 36.782 35.950  1.00 21.02  ? 10  TRP B NE1 1 
ATOM   4131 C CE2 . TRP B 1 10  ? -22.737 37.968 35.399  1.00 23.69  ? 10  TRP B CE2 1 
ATOM   4132 C CE3 . TRP B 1 10  ? -24.154 38.705 33.572  1.00 20.37  ? 10  TRP B CE3 1 
ATOM   4133 C CZ2 . TRP B 1 10  ? -22.421 39.282 35.755  1.00 23.52  ? 10  TRP B CZ2 1 
ATOM   4134 C CZ3 . TRP B 1 10  ? -23.844 40.015 33.931  1.00 24.75  ? 10  TRP B CZ3 1 
ATOM   4135 C CH2 . TRP B 1 10  ? -22.987 40.292 35.015  1.00 20.61  ? 10  TRP B CH2 1 
ATOM   4136 N N   . HIS B 1 11  ? -27.465 35.336 31.518  1.00 17.51  ? 11  HIS B N   1 
ATOM   4137 C CA  . HIS B 1 11  ? -28.276 34.659 30.518  1.00 22.68  ? 11  HIS B CA  1 
ATOM   4138 C C   . HIS B 1 11  ? -27.603 34.754 29.155  1.00 25.15  ? 11  HIS B C   1 
ATOM   4139 O O   . HIS B 1 11  ? -27.275 35.850 28.698  1.00 24.40  ? 11  HIS B O   1 
ATOM   4140 C CB  . HIS B 1 11  ? -29.671 35.279 30.480  1.00 19.66  ? 11  HIS B CB  1 
ATOM   4141 C CG  . HIS B 1 11  ? -30.466 34.921 29.271  1.00 24.50  ? 11  HIS B CG  1 
ATOM   4142 N ND1 . HIS B 1 11  ? -30.832 33.626 28.976  1.00 21.34  ? 11  HIS B ND1 1 
ATOM   4143 C CD2 . HIS B 1 11  ? -30.983 35.696 28.286  1.00 24.13  ? 11  HIS B CD2 1 
ATOM   4144 C CE1 . HIS B 1 11  ? -31.532 33.615 27.857  1.00 18.34  ? 11  HIS B CE1 1 
ATOM   4145 N NE2 . HIS B 1 11  ? -31.636 34.858 27.417  1.00 21.83  ? 11  HIS B NE2 1 
ATOM   4146 N N   . MET B 1 12  ? -27.404 33.606 28.510  1.00 24.52  ? 12  MET B N   1 
ATOM   4147 C CA  . MET B 1 12  ? -26.689 33.525 27.244  1.00 21.07  ? 12  MET B CA  1 
ATOM   4148 C C   . MET B 1 12  ? -27.620 32.948 26.190  1.00 22.93  ? 12  MET B C   1 
ATOM   4149 O O   . MET B 1 12  ? -28.152 31.850 26.369  1.00 22.51  ? 12  MET B O   1 
ATOM   4150 C CB  . MET B 1 12  ? -25.439 32.643 27.375  1.00 17.34  ? 12  MET B CB  1 
ATOM   4151 C CG  . MET B 1 12  ? -24.538 32.974 28.568  1.00 20.07  ? 12  MET B CG  1 
ATOM   4152 S SD  . MET B 1 12  ? -23.923 34.669 28.536  1.00 22.14  ? 12  MET B SD  1 
ATOM   4153 C CE  . MET B 1 12  ? -22.581 34.576 29.741  1.00 21.30  ? 12  MET B CE  1 
ATOM   4154 N N   . HIS B 1 13  ? -27.802 33.676 25.090  1.00 23.23  ? 13  HIS B N   1 
ATOM   4155 C CA  . HIS B 1 13  ? -28.741 33.243 24.070  1.00 20.07  ? 13  HIS B CA  1 
ATOM   4156 C C   . HIS B 1 13  ? -28.337 33.814 22.724  1.00 25.41  ? 13  HIS B C   1 
ATOM   4157 O O   . HIS B 1 13  ? -27.840 34.943 22.639  1.00 22.58  ? 13  HIS B O   1 
ATOM   4158 C CB  . HIS B 1 13  ? -30.175 33.690 24.383  1.00 15.08  ? 13  HIS B CB  1 
ATOM   4159 C CG  . HIS B 1 13  ? -31.125 33.490 23.244  1.00 19.33  ? 13  HIS B CG  1 
ATOM   4160 N ND1 . HIS B 1 13  ? -31.404 32.247 22.717  1.00 20.75  ? 13  HIS B ND1 1 
ATOM   4161 C CD2 . HIS B 1 13  ? -31.849 34.376 22.518  1.00 22.22  ? 13  HIS B CD2 1 
ATOM   4162 C CE1 . HIS B 1 13  ? -32.258 32.376 21.715  1.00 19.30  ? 13  HIS B CE1 1 
ATOM   4163 N NE2 . HIS B 1 13  ? -32.543 33.657 21.575  1.00 18.14  ? 13  HIS B NE2 1 
ATOM   4164 N N   . GLN B 1 14  ? -28.595 33.033 21.669  1.00 22.77  ? 14  GLN B N   1 
ATOM   4165 C CA  . GLN B 1 14  ? -28.554 33.523 20.297  1.00 21.70  ? 14  GLN B CA  1 
ATOM   4166 C C   . GLN B 1 14  ? -29.656 32.798 19.534  1.00 24.15  ? 14  GLN B C   1 
ATOM   4167 O O   . GLN B 1 14  ? -29.788 31.571 19.677  1.00 23.57  ? 14  GLN B O   1 
ATOM   4168 C CB  . GLN B 1 14  ? -27.205 33.291 19.606  1.00 17.51  ? 14  GLN B CB  1 
ATOM   4169 C CG  . GLN B 1 14  ? -26.050 34.069 20.186  1.00 15.70  ? 14  GLN B CG  1 
ATOM   4170 C CD  . GLN B 1 14  ? -26.164 35.581 19.985  1.00 29.41  ? 14  GLN B CD  1 
ATOM   4171 O OE1 . GLN B 1 14  ? -26.834 36.066 19.054  1.00 24.27  ? 14  GLN B OE1 1 
ATOM   4172 N NE2 . GLN B 1 14  ? -25.507 36.336 20.870  1.00 23.77  ? 14  GLN B NE2 1 
ATOM   4173 N N   . PRO B 1 15  ? -30.455 33.503 18.742  1.00 21.26  ? 15  PRO B N   1 
ATOM   4174 C CA  . PRO B 1 15  ? -31.392 32.817 17.840  1.00 26.65  ? 15  PRO B CA  1 
ATOM   4175 C C   . PRO B 1 15  ? -30.626 32.046 16.768  1.00 31.03  ? 15  PRO B C   1 
ATOM   4176 O O   . PRO B 1 15  ? -29.419 32.215 16.580  1.00 26.86  ? 15  PRO B O   1 
ATOM   4177 C CB  . PRO B 1 15  ? -32.219 33.958 17.236  1.00 20.87  ? 15  PRO B CB  1 
ATOM   4178 C CG  . PRO B 1 15  ? -31.307 35.159 17.317  1.00 23.90  ? 15  PRO B CG  1 
ATOM   4179 C CD  . PRO B 1 15  ? -30.478 34.968 18.582  1.00 15.12  ? 15  PRO B CD  1 
ATOM   4180 N N   . LEU B 1 16  ? -31.345 31.185 16.046  1.00 27.57  ? 16  LEU B N   1 
ATOM   4181 C CA  . LEU B 1 16  ? -30.698 30.353 15.030  1.00 29.38  ? 16  LEU B CA  1 
ATOM   4182 C C   . LEU B 1 16  ? -30.374 31.192 13.797  1.00 29.62  ? 16  LEU B C   1 
ATOM   4183 O O   . LEU B 1 16  ? -31.279 31.627 13.080  1.00 27.12  ? 16  LEU B O   1 
ATOM   4184 C CB  . LEU B 1 16  ? -31.588 29.172 14.662  1.00 26.10  ? 16  LEU B CB  1 
ATOM   4185 C CG  . LEU B 1 16  ? -30.910 28.099 13.811  1.00 24.52  ? 16  LEU B CG  1 
ATOM   4186 C CD1 . LEU B 1 16  ? -29.655 27.581 14.519  1.00 22.43  ? 16  LEU B CD1 1 
ATOM   4187 C CD2 . LEU B 1 16  ? -31.867 26.949 13.486  1.00 22.92  ? 16  LEU B CD2 1 
ATOM   4188 N N   . TYR B 1 17  ? -29.082 31.408 13.537  1.00 30.88  ? 17  TYR B N   1 
ATOM   4189 C CA  . TYR B 1 17  ? -28.625 32.178 12.384  1.00 25.00  ? 17  TYR B CA  1 
ATOM   4190 C C   . TYR B 1 17  ? -28.425 31.310 11.151  1.00 30.31  ? 17  TYR B C   1 
ATOM   4191 O O   . TYR B 1 17  ? -28.114 31.834 10.076  1.00 27.67  ? 17  TYR B O   1 
ATOM   4192 C CB  . TYR B 1 17  ? -27.313 32.916 12.717  1.00 27.38  ? 17  TYR B CB  1 
ATOM   4193 C CG  . TYR B 1 17  ? -27.450 33.977 13.800  1.00 28.84  ? 17  TYR B CG  1 
ATOM   4194 C CD1 . TYR B 1 17  ? -28.325 35.049 13.641  1.00 20.73  ? 17  TYR B CD1 1 
ATOM   4195 C CD2 . TYR B 1 17  ? -26.706 33.905 14.982  1.00 27.34  ? 17  TYR B CD2 1 
ATOM   4196 C CE1 . TYR B 1 17  ? -28.453 36.021 14.626  1.00 26.51  ? 17  TYR B CE1 1 
ATOM   4197 C CE2 . TYR B 1 17  ? -26.823 34.879 15.969  1.00 19.57  ? 17  TYR B CE2 1 
ATOM   4198 C CZ  . TYR B 1 17  ? -27.711 35.926 15.787  1.00 22.29  ? 17  TYR B CZ  1 
ATOM   4199 O OH  . TYR B 1 17  ? -27.857 36.888 16.755  1.00 22.01  ? 17  TYR B OH  1 
ATOM   4200 N N   . ARG B 1 18  ? -28.600 30.001 11.287  1.00 29.26  ? 18  ARG B N   1 
ATOM   4201 C CA  . ARG B 1 18  ? -28.320 29.045 10.226  1.00 28.78  ? 18  ARG B CA  1 
ATOM   4202 C C   . ARG B 1 18  ? -29.548 28.941 9.331   1.00 31.13  ? 18  ARG B C   1 
ATOM   4203 O O   . ARG B 1 18  ? -30.584 28.404 9.740   1.00 30.51  ? 18  ARG B O   1 
ATOM   4204 C CB  . ARG B 1 18  ? -27.949 27.691 10.827  1.00 25.70  ? 18  ARG B CB  1 
ATOM   4205 C CG  . ARG B 1 18  ? -27.356 26.689 9.856   1.00 29.25  ? 18  ARG B CG  1 
ATOM   4206 C CD  . ARG B 1 18  ? -27.320 25.303 10.492  1.00 32.18  ? 18  ARG B CD  1 
ATOM   4207 N NE  . ARG B 1 18  ? -26.639 24.323 9.657   1.00 32.50  ? 18  ARG B NE  1 
ATOM   4208 C CZ  . ARG B 1 18  ? -27.241 23.564 8.747   1.00 33.79  ? 18  ARG B CZ  1 
ATOM   4209 N NH1 . ARG B 1 18  ? -28.550 23.663 8.552   1.00 37.04  ? 18  ARG B NH1 1 
ATOM   4210 N NH2 . ARG B 1 18  ? -26.530 22.704 8.031   1.00 38.72  ? 18  ARG B NH2 1 
ATOM   4211 N N   . GLU B 1 19  ? -29.433 29.460 8.120   1.00 30.20  ? 19  GLU B N   1 
ATOM   4212 C CA  . GLU B 1 19  ? -30.514 29.341 7.149   1.00 32.55  ? 19  GLU B CA  1 
ATOM   4213 C C   . GLU B 1 19  ? -30.633 27.896 6.669   1.00 35.03  ? 19  GLU B C   1 
ATOM   4214 O O   . GLU B 1 19  ? -29.626 27.293 6.280   1.00 37.22  ? 19  GLU B O   1 
ATOM   4215 C CB  . GLU B 1 19  ? -30.251 30.276 5.979   1.00 39.43  ? 19  GLU B CB  1 
ATOM   4216 C CG  . GLU B 1 19  ? -31.487 30.637 5.189   1.00 46.93  ? 19  GLU B CG  1 
ATOM   4217 C CD  . GLU B 1 19  ? -31.865 29.554 4.204   1.00 49.19  ? 19  GLU B CD  1 
ATOM   4218 O OE1 . GLU B 1 19  ? -30.988 29.125 3.429   1.00 49.10  ? 19  GLU B OE1 1 
ATOM   4219 O OE2 . GLU B 1 19  ? -33.036 29.122 4.220   1.00 51.57  ? 19  GLU B OE2 1 
ATOM   4220 N N   . PRO B 1 20  ? -31.835 27.314 6.661   1.00 33.53  ? 20  PRO B N   1 
ATOM   4221 C CA  . PRO B 1 20  ? -31.945 25.865 6.394   1.00 36.55  ? 20  PRO B CA  1 
ATOM   4222 C C   . PRO B 1 20  ? -31.642 25.455 4.960   1.00 34.91  ? 20  PRO B C   1 
ATOM   4223 O O   . PRO B 1 20  ? -31.223 24.312 4.740   1.00 40.90  ? 20  PRO B O   1 
ATOM   4224 C CB  . PRO B 1 20  ? -33.402 25.548 6.762   1.00 37.73  ? 20  PRO B CB  1 
ATOM   4225 C CG  . PRO B 1 20  ? -34.124 26.877 6.646   1.00 34.87  ? 20  PRO B CG  1 
ATOM   4226 C CD  . PRO B 1 20  ? -33.118 27.909 7.074   1.00 34.32  ? 20  PRO B CD  1 
ATOM   4227 N N   . TYR B 1 21  ? -31.842 26.325 3.973   1.00 30.97  ? 21  TYR B N   1 
ATOM   4228 C CA  . TYR B 1 21  ? -31.625 25.895 2.595   1.00 33.78  ? 21  TYR B CA  1 
ATOM   4229 C C   . TYR B 1 21  ? -30.167 26.044 2.167   1.00 36.22  ? 21  TYR B C   1 
ATOM   4230 O O   . TYR B 1 21  ? -29.583 25.099 1.624   1.00 33.78  ? 21  TYR B O   1 
ATOM   4231 C CB  . TYR B 1 21  ? -32.560 26.662 1.662   1.00 36.58  ? 21  TYR B CB  1 
ATOM   4232 C CG  . TYR B 1 21  ? -34.009 26.308 1.915   1.00 38.29  ? 21  TYR B CG  1 
ATOM   4233 C CD1 . TYR B 1 21  ? -34.575 25.168 1.356   1.00 38.99  ? 21  TYR B CD1 1 
ATOM   4234 C CD2 . TYR B 1 21  ? -34.799 27.089 2.756   1.00 39.66  ? 21  TYR B CD2 1 
ATOM   4235 C CE1 . TYR B 1 21  ? -35.899 24.833 1.601   1.00 42.30  ? 21  TYR B CE1 1 
ATOM   4236 C CE2 . TYR B 1 21  ? -36.117 26.761 3.008   1.00 42.22  ? 21  TYR B CE2 1 
ATOM   4237 C CZ  . TYR B 1 21  ? -36.663 25.633 2.428   1.00 41.95  ? 21  TYR B CZ  1 
ATOM   4238 O OH  . TYR B 1 21  ? -37.978 25.312 2.681   1.00 44.44  ? 21  TYR B OH  1 
ATOM   4239 N N   . THR B 1 22  ? -29.562 27.210 2.411   1.00 34.56  ? 22  THR B N   1 
ATOM   4240 C CA  . THR B 1 22  ? -28.134 27.359 2.150   1.00 34.99  ? 22  THR B CA  1 
ATOM   4241 C C   . THR B 1 22  ? -27.283 26.573 3.141   1.00 37.19  ? 22  THR B C   1 
ATOM   4242 O O   . THR B 1 22  ? -26.140 26.226 2.819   1.00 33.82  ? 22  THR B O   1 
ATOM   4243 C CB  . THR B 1 22  ? -27.736 28.837 2.184   1.00 34.14  ? 22  THR B CB  1 
ATOM   4244 O OG1 . THR B 1 22  ? -28.204 29.436 3.403   1.00 39.35  ? 22  THR B OG1 1 
ATOM   4245 C CG2 . THR B 1 22  ? -28.331 29.586 0.987   1.00 36.34  ? 22  THR B CG2 1 
ATOM   4246 N N   . GLY B 1 23  ? -27.815 26.274 4.327   1.00 33.86  ? 23  GLY B N   1 
ATOM   4247 C CA  . GLY B 1 23  ? -27.026 25.645 5.365   1.00 35.77  ? 23  GLY B CA  1 
ATOM   4248 C C   . GLY B 1 23  ? -25.999 26.557 5.992   1.00 40.99  ? 23  GLY B C   1 
ATOM   4249 O O   . GLY B 1 23  ? -25.130 26.080 6.728   1.00 46.08  ? 23  GLY B O   1 
ATOM   4250 N N   . GLU B 1 24  ? -26.085 27.857 5.734   1.00 36.24  ? 24  GLU B N   1 
ATOM   4251 C CA  . GLU B 1 24  ? -25.056 28.814 6.106   1.00 32.30  ? 24  GLU B CA  1 
ATOM   4252 C C   . GLU B 1 24  ? -25.548 29.704 7.236   1.00 34.71  ? 24  GLU B C   1 
ATOM   4253 O O   . GLU B 1 24  ? -26.731 30.076 7.288   1.00 31.63  ? 24  GLU B O   1 
ATOM   4254 C CB  . GLU B 1 24  ? -24.645 29.677 4.904   1.00 30.37  ? 24  GLU B CB  1 
ATOM   4255 C CG  . GLU B 1 24  ? -23.852 28.927 3.836   1.00 34.62  ? 24  GLU B CG  1 
ATOM   4256 C CD  . GLU B 1 24  ? -23.378 29.834 2.713   1.00 41.41  ? 24  GLU B CD  1 
ATOM   4257 O OE1 . GLU B 1 24  ? -24.152 30.718 2.290   1.00 40.30  ? 24  GLU B OE1 1 
ATOM   4258 O OE2 . GLU B 1 24  ? -22.228 29.662 2.253   1.00 43.22  ? 24  GLU B OE2 1 
ATOM   4259 N N   . TYR B 1 25  ? -24.638 30.032 8.146   1.00 28.63  ? 25  TYR B N   1 
ATOM   4260 C CA  . TYR B 1 25  ? -24.922 30.992 9.203   1.00 28.49  ? 25  TYR B CA  1 
ATOM   4261 C C   . TYR B 1 25  ? -24.857 32.386 8.599   1.00 27.91  ? 25  TYR B C   1 
ATOM   4262 O O   . TYR B 1 25  ? -23.783 32.842 8.189   1.00 30.14  ? 25  TYR B O   1 
ATOM   4263 C CB  . TYR B 1 25  ? -23.925 30.843 10.343  1.00 32.27  ? 25  TYR B CB  1 
ATOM   4264 C CG  . TYR B 1 25  ? -24.253 29.724 11.296  1.00 37.84  ? 25  TYR B CG  1 
ATOM   4265 C CD1 . TYR B 1 25  ? -24.111 28.391 10.912  1.00 40.41  ? 25  TYR B CD1 1 
ATOM   4266 C CD2 . TYR B 1 25  ? -24.692 29.995 12.589  1.00 34.60  ? 25  TYR B CD2 1 
ATOM   4267 C CE1 . TYR B 1 25  ? -24.401 27.363 11.788  1.00 35.70  ? 25  TYR B CE1 1 
ATOM   4268 C CE2 . TYR B 1 25  ? -24.987 28.971 13.469  1.00 30.51  ? 25  TYR B CE2 1 
ATOM   4269 C CZ  . TYR B 1 25  ? -24.836 27.660 13.065  1.00 29.69  ? 25  TYR B CZ  1 
ATOM   4270 O OH  . TYR B 1 25  ? -25.127 26.640 13.936  1.00 33.30  ? 25  TYR B OH  1 
ATOM   4271 N N   . LEU B 1 26  ? -26.009 33.065 8.537   1.00 31.06  ? 26  LEU B N   1 
ATOM   4272 C CA  . LEU B 1 26  ? -26.108 34.339 7.831   1.00 28.73  ? 26  LEU B CA  1 
ATOM   4273 C C   . LEU B 1 26  ? -25.603 35.517 8.653   1.00 33.38  ? 26  LEU B C   1 
ATOM   4274 O O   . LEU B 1 26  ? -25.385 36.598 8.092   1.00 30.19  ? 26  LEU B O   1 
ATOM   4275 C CB  . LEU B 1 26  ? -27.559 34.600 7.418   1.00 27.84  ? 26  LEU B CB  1 
ATOM   4276 C CG  . LEU B 1 26  ? -28.284 33.525 6.607   1.00 31.25  ? 26  LEU B CG  1 
ATOM   4277 C CD1 . LEU B 1 26  ? -29.577 34.084 6.037   1.00 35.95  ? 26  LEU B CD1 1 
ATOM   4278 C CD2 . LEU B 1 26  ? -27.397 32.962 5.504   1.00 31.59  ? 26  LEU B CD2 1 
ATOM   4279 N N   . LEU B 1 27  ? -25.434 35.342 9.960   1.00 31.19  ? 27  LEU B N   1 
ATOM   4280 C CA  . LEU B 1 27  ? -24.872 36.356 10.829  1.00 30.48  ? 27  LEU B CA  1 
ATOM   4281 C C   . LEU B 1 27  ? -23.825 35.706 11.721  1.00 30.02  ? 27  LEU B C   1 
ATOM   4282 O O   . LEU B 1 27  ? -23.984 34.544 12.113  1.00 32.42  ? 27  LEU B O   1 
ATOM   4283 C CB  . LEU B 1 27  ? -25.953 37.017 11.693  1.00 34.95  ? 27  LEU B CB  1 
ATOM   4284 C CG  . LEU B 1 27  ? -26.845 38.037 10.991  1.00 36.88  ? 27  LEU B CG  1 
ATOM   4285 C CD1 . LEU B 1 27  ? -27.899 38.576 11.952  1.00 35.39  ? 27  LEU B CD1 1 
ATOM   4286 C CD2 . LEU B 1 27  ? -26.014 39.169 10.402  1.00 36.83  ? 27  LEU B CD2 1 
ATOM   4287 N N   . PRO B 1 28  ? -22.748 36.421 12.046  1.00 27.89  ? 28  PRO B N   1 
ATOM   4288 C CA  . PRO B 1 28  ? -21.636 35.836 12.813  1.00 28.34  ? 28  PRO B CA  1 
ATOM   4289 C C   . PRO B 1 28  ? -21.713 36.036 14.321  1.00 28.43  ? 28  PRO B C   1 
ATOM   4290 O O   . PRO B 1 28  ? -20.715 35.791 15.009  1.00 25.75  ? 28  PRO B O   1 
ATOM   4291 C CB  . PRO B 1 28  ? -20.433 36.601 12.248  1.00 32.99  ? 28  PRO B CB  1 
ATOM   4292 C CG  . PRO B 1 28  ? -20.995 38.001 12.024  1.00 33.39  ? 28  PRO B CG  1 
ATOM   4293 C CD  . PRO B 1 28  ? -22.467 37.815 11.651  1.00 34.12  ? 28  PRO B CD  1 
ATOM   4294 N N   . TRP B 1 29  ? -22.857 36.463 14.849  1.00 21.58  ? 29  TRP B N   1 
ATOM   4295 C CA  . TRP B 1 29  ? -22.897 36.933 16.230  1.00 24.42  ? 29  TRP B CA  1 
ATOM   4296 C C   . TRP B 1 29  ? -22.659 35.796 17.218  1.00 28.57  ? 29  TRP B C   1 
ATOM   4297 O O   . TRP B 1 29  ? -22.007 35.990 18.254  1.00 25.63  ? 29  TRP B O   1 
ATOM   4298 C CB  . TRP B 1 29  ? -24.234 37.609 16.507  1.00 24.04  ? 29  TRP B CB  1 
ATOM   4299 C CG  . TRP B 1 29  ? -24.491 38.860 15.727  1.00 27.88  ? 29  TRP B CG  1 
ATOM   4300 C CD1 . TRP B 1 29  ? -25.581 39.119 14.946  1.00 32.08  ? 29  TRP B CD1 1 
ATOM   4301 C CD2 . TRP B 1 29  ? -23.672 40.040 15.679  1.00 31.86  ? 29  TRP B CD2 1 
ATOM   4302 N NE1 . TRP B 1 29  ? -25.493 40.383 14.410  1.00 32.33  ? 29  TRP B NE1 1 
ATOM   4303 C CE2 . TRP B 1 29  ? -24.332 40.971 14.844  1.00 33.88  ? 29  TRP B CE2 1 
ATOM   4304 C CE3 . TRP B 1 29  ? -22.455 40.406 16.264  1.00 32.19  ? 29  TRP B CE3 1 
ATOM   4305 C CZ2 . TRP B 1 29  ? -23.810 42.236 14.574  1.00 29.33  ? 29  TRP B CZ2 1 
ATOM   4306 C CZ3 . TRP B 1 29  ? -21.937 41.666 15.991  1.00 35.72  ? 29  TRP B CZ3 1 
ATOM   4307 C CH2 . TRP B 1 29  ? -22.617 42.566 15.156  1.00 32.55  ? 29  TRP B CH2 1 
ATOM   4308 N N   . THR B 1 30  ? -23.172 34.600 16.921  1.00 28.97  ? 30  THR B N   1 
ATOM   4309 C CA  . THR B 1 30  ? -22.879 33.475 17.799  1.00 28.50  ? 30  THR B CA  1 
ATOM   4310 C C   . THR B 1 30  ? -21.382 33.219 17.860  1.00 28.95  ? 30  THR B C   1 
ATOM   4311 O O   . THR B 1 30  ? -20.830 32.995 18.945  1.00 29.94  ? 30  THR B O   1 
ATOM   4312 C CB  . THR B 1 30  ? -23.628 32.225 17.345  1.00 32.06  ? 30  THR B CB  1 
ATOM   4313 O OG1 . THR B 1 30  ? -25.040 32.473 17.380  1.00 28.99  ? 30  THR B OG1 1 
ATOM   4314 C CG2 . THR B 1 30  ? -23.309 31.055 18.282  1.00 34.90  ? 30  THR B CG2 1 
ATOM   4315 N N   . PHE B 1 31  ? -20.695 33.289 16.712  1.00 24.12  ? 31  PHE B N   1 
ATOM   4316 C CA  . PHE B 1 31  ? -19.247 33.077 16.719  1.00 25.53  ? 31  PHE B CA  1 
ATOM   4317 C C   . PHE B 1 31  ? -18.546 34.130 17.573  1.00 26.23  ? 31  PHE B C   1 
ATOM   4318 O O   . PHE B 1 31  ? -17.655 33.812 18.376  1.00 23.27  ? 31  PHE B O   1 
ATOM   4319 C CB  . PHE B 1 31  ? -18.695 33.103 15.294  1.00 27.89  ? 31  PHE B CB  1 
ATOM   4320 C CG  . PHE B 1 31  ? -17.181 33.095 15.232  1.00 29.54  ? 31  PHE B CG  1 
ATOM   4321 C CD1 . PHE B 1 31  ? -16.480 31.899 15.313  1.00 21.68  ? 31  PHE B CD1 1 
ATOM   4322 C CD2 . PHE B 1 31  ? -16.466 34.281 15.122  1.00 27.57  ? 31  PHE B CD2 1 
ATOM   4323 C CE1 . PHE B 1 31  ? -15.087 31.884 15.262  1.00 24.16  ? 31  PHE B CE1 1 
ATOM   4324 C CE2 . PHE B 1 31  ? -15.063 34.270 15.074  1.00 24.34  ? 31  PHE B CE2 1 
ATOM   4325 C CZ  . PHE B 1 31  ? -14.383 33.068 15.144  1.00 25.80  ? 31  PHE B CZ  1 
ATOM   4326 N N   . PHE B 1 32  ? -18.952 35.394 17.423  1.00 24.37  ? 32  PHE B N   1 
ATOM   4327 C CA  . PHE B 1 32  ? -18.217 36.479 18.060  1.00 18.86  ? 32  PHE B CA  1 
ATOM   4328 C C   . PHE B 1 32  ? -18.490 36.531 19.558  1.00 21.08  ? 32  PHE B C   1 
ATOM   4329 O O   . PHE B 1 32  ? -17.565 36.730 20.353  1.00 23.31  ? 32  PHE B O   1 
ATOM   4330 C CB  . PHE B 1 32  ? -18.551 37.800 17.365  1.00 21.34  ? 32  PHE B CB  1 
ATOM   4331 C CG  . PHE B 1 32  ? -17.756 38.024 16.091  1.00 30.69  ? 32  PHE B CG  1 
ATOM   4332 C CD1 . PHE B 1 32  ? -16.367 38.022 16.120  1.00 29.18  ? 32  PHE B CD1 1 
ATOM   4333 C CD2 . PHE B 1 32  ? -18.392 38.202 14.871  1.00 33.19  ? 32  PHE B CD2 1 
ATOM   4334 C CE1 . PHE B 1 32  ? -15.624 38.207 14.957  1.00 30.65  ? 32  PHE B CE1 1 
ATOM   4335 C CE2 . PHE B 1 32  ? -17.656 38.392 13.710  1.00 35.30  ? 32  PHE B CE2 1 
ATOM   4336 C CZ  . PHE B 1 32  ? -16.266 38.395 13.753  1.00 31.71  ? 32  PHE B CZ  1 
ATOM   4337 N N   . HIS B 1 33  ? -19.737 36.315 19.969  1.00 19.86  ? 33  HIS B N   1 
ATOM   4338 C CA  . HIS B 1 33  ? -20.023 36.256 21.400  1.00 23.35  ? 33  HIS B CA  1 
ATOM   4339 C C   . HIS B 1 33  ? -19.449 35.001 22.053  1.00 23.94  ? 33  HIS B C   1 
ATOM   4340 O O   . HIS B 1 33  ? -19.164 35.009 23.261  1.00 22.84  ? 33  HIS B O   1 
ATOM   4341 C CB  . HIS B 1 33  ? -21.530 36.371 21.611  1.00 18.97  ? 33  HIS B CB  1 
ATOM   4342 C CG  . HIS B 1 33  ? -22.023 37.772 21.436  1.00 22.16  ? 33  HIS B CG  1 
ATOM   4343 N ND1 . HIS B 1 33  ? -21.593 38.808 22.238  1.00 22.95  ? 33  HIS B ND1 1 
ATOM   4344 C CD2 . HIS B 1 33  ? -22.827 38.328 20.502  1.00 23.35  ? 33  HIS B CD2 1 
ATOM   4345 C CE1 . HIS B 1 33  ? -22.148 39.937 21.832  1.00 24.05  ? 33  HIS B CE1 1 
ATOM   4346 N NE2 . HIS B 1 33  ? -22.899 39.672 20.777  1.00 24.74  ? 33  HIS B NE2 1 
ATOM   4347 N N   . ALA B 1 34  ? -19.245 33.940 21.284  1.00 20.13  ? 34  ALA B N   1 
ATOM   4348 C CA  . ALA B 1 34  ? -18.621 32.751 21.853  1.00 23.88  ? 34  ALA B CA  1 
ATOM   4349 C C   . ALA B 1 34  ? -17.133 32.982 22.103  1.00 25.61  ? 34  ALA B C   1 
ATOM   4350 O O   . ALA B 1 34  ? -16.614 32.612 23.164  1.00 26.10  ? 34  ALA B O   1 
ATOM   4351 C CB  . ALA B 1 34  ? -18.841 31.551 20.935  1.00 19.58  ? 34  ALA B CB  1 
ATOM   4352 N N   . VAL B 1 35  ? -16.432 33.603 21.149  1.00 22.30  ? 35  VAL B N   1 
ATOM   4353 C CA  . VAL B 1 35  ? -15.001 33.822 21.353  1.00 22.13  ? 35  VAL B CA  1 
ATOM   4354 C C   . VAL B 1 35  ? -14.761 34.880 22.420  1.00 25.21  ? 35  VAL B C   1 
ATOM   4355 O O   . VAL B 1 35  ? -13.768 34.810 23.158  1.00 25.82  ? 35  VAL B O   1 
ATOM   4356 C CB  . VAL B 1 35  ? -14.301 34.187 20.028  1.00 27.89  ? 35  VAL B CB  1 
ATOM   4357 C CG1 . VAL B 1 35  ? -14.536 33.110 18.989  1.00 28.68  ? 35  VAL B CG1 1 
ATOM   4358 C CG2 . VAL B 1 35  ? -14.761 35.543 19.517  1.00 29.05  ? 35  VAL B CG2 1 
ATOM   4359 N N   . LYS B 1 36  ? -15.665 35.856 22.545  1.00 21.78  ? 36  LYS B N   1 
ATOM   4360 C CA  . LYS B 1 36  ? -15.473 36.969 23.465  1.00 23.96  ? 36  LYS B CA  1 
ATOM   4361 C C   . LYS B 1 36  ? -16.074 36.718 24.848  1.00 27.47  ? 36  LYS B C   1 
ATOM   4362 O O   . LYS B 1 36  ? -15.463 37.088 25.860  1.00 23.54  ? 36  LYS B O   1 
ATOM   4363 C CB  . LYS B 1 36  ? -16.074 38.251 22.867  1.00 23.24  ? 36  LYS B CB  1 
ATOM   4364 C CG  . LYS B 1 36  ? -15.796 39.506 23.689  1.00 25.53  ? 36  LYS B CG  1 
ATOM   4365 C CD  . LYS B 1 36  ? -16.155 40.800 22.942  1.00 25.45  ? 36  LYS B CD  1 
ATOM   4366 C CE  . LYS B 1 36  ? -17.632 41.189 23.115  1.00 18.15  ? 36  LYS B CE  1 
ATOM   4367 N NZ  . LYS B 1 36  ? -18.090 41.299 24.535  1.00 23.51  ? 36  LYS B NZ  1 
ATOM   4368 N N   . ASP B 1 37  ? -17.265 36.100 24.919  1.00 27.78  ? 37  ASP B N   1 
ATOM   4369 C CA  . ASP B 1 37  ? -18.049 36.105 26.154  1.00 26.62  ? 37  ASP B CA  1 
ATOM   4370 C C   . ASP B 1 37  ? -18.444 34.728 26.675  1.00 23.84  ? 37  ASP B C   1 
ATOM   4371 O O   . ASP B 1 37  ? -18.387 34.509 27.878  1.00 18.08  ? 37  ASP B O   1 
ATOM   4372 C CB  . ASP B 1 37  ? -19.319 36.940 25.962  1.00 24.39  ? 37  ASP B CB  1 
ATOM   4373 C CG  . ASP B 1 37  ? -19.039 38.350 25.452  1.00 27.59  ? 37  ASP B CG  1 
ATOM   4374 O OD1 . ASP B 1 37  ? -18.333 39.134 26.146  1.00 21.43  ? 37  ASP B OD1 1 
ATOM   4375 O OD2 . ASP B 1 37  ? -19.550 38.671 24.353  1.00 27.81  ? 37  ASP B OD2 1 
ATOM   4376 N N   . TYR B 1 38  ? -18.859 33.784 25.816  1.00 26.24  ? 38  TYR B N   1 
ATOM   4377 C CA  . TYR B 1 38  ? -19.497 32.574 26.342  1.00 22.58  ? 38  TYR B CA  1 
ATOM   4378 C C   . TYR B 1 38  ? -18.512 31.675 27.094  1.00 22.77  ? 38  TYR B C   1 
ATOM   4379 O O   . TYR B 1 38  ? -18.912 30.973 28.031  1.00 23.15  ? 38  TYR B O   1 
ATOM   4380 C CB  . TYR B 1 38  ? -20.197 31.805 25.217  1.00 20.98  ? 38  TYR B CB  1 
ATOM   4381 C CG  . TYR B 1 38  ? -21.408 32.555 24.648  1.00 20.70  ? 38  TYR B CG  1 
ATOM   4382 C CD1 . TYR B 1 38  ? -22.231 33.302 25.471  1.00 21.69  ? 38  TYR B CD1 1 
ATOM   4383 C CD2 . TYR B 1 38  ? -21.697 32.533 23.291  1.00 21.77  ? 38  TYR B CD2 1 
ATOM   4384 C CE1 . TYR B 1 38  ? -23.322 34.002 24.967  1.00 25.57  ? 38  TYR B CE1 1 
ATOM   4385 C CE2 . TYR B 1 38  ? -22.793 33.230 22.771  1.00 21.30  ? 38  TYR B CE2 1 
ATOM   4386 C CZ  . TYR B 1 38  ? -23.602 33.962 23.619  1.00 24.52  ? 38  TYR B CZ  1 
ATOM   4387 O OH  . TYR B 1 38  ? -24.696 34.656 23.134  1.00 19.15  ? 38  TYR B OH  1 
ATOM   4388 N N   . TYR B 1 39  ? -17.228 31.704 26.733  1.00 21.94  ? 39  TYR B N   1 
ATOM   4389 C CA  . TYR B 1 39  ? -16.229 30.983 27.518  1.00 22.93  ? 39  TYR B CA  1 
ATOM   4390 C C   . TYR B 1 39  ? -15.667 31.845 28.646  1.00 24.42  ? 39  TYR B C   1 
ATOM   4391 O O   . TYR B 1 39  ? -15.502 31.363 29.777  1.00 21.05  ? 39  TYR B O   1 
ATOM   4392 C CB  . TYR B 1 39  ? -15.094 30.499 26.607  1.00 19.96  ? 39  TYR B CB  1 
ATOM   4393 C CG  . TYR B 1 39  ? -13.909 29.911 27.355  1.00 23.70  ? 39  TYR B CG  1 
ATOM   4394 C CD1 . TYR B 1 39  ? -13.860 28.554 27.661  1.00 28.12  ? 39  TYR B CD1 1 
ATOM   4395 C CD2 . TYR B 1 39  ? -12.842 30.714 27.760  1.00 24.67  ? 39  TYR B CD2 1 
ATOM   4396 C CE1 . TYR B 1 39  ? -12.789 28.010 28.342  1.00 30.19  ? 39  TYR B CE1 1 
ATOM   4397 C CE2 . TYR B 1 39  ? -11.757 30.175 28.447  1.00 26.18  ? 39  TYR B CE2 1 
ATOM   4398 C CZ  . TYR B 1 39  ? -11.741 28.825 28.735  1.00 32.40  ? 39  TYR B CZ  1 
ATOM   4399 O OH  . TYR B 1 39  ? -10.678 28.287 29.424  1.00 34.35  ? 39  TYR B OH  1 
ATOM   4400 N N   . ASP B 1 40  ? -15.383 33.121 28.356  1.00 22.29  ? 40  ASP B N   1 
ATOM   4401 C CA  . ASP B 1 40  ? -14.698 33.982 29.315  1.00 21.48  ? 40  ASP B CA  1 
ATOM   4402 C C   . ASP B 1 40  ? -15.570 34.359 30.508  1.00 25.53  ? 40  ASP B C   1 
ATOM   4403 O O   . ASP B 1 40  ? -15.039 34.564 31.604  1.00 28.21  ? 40  ASP B O   1 
ATOM   4404 C CB  . ASP B 1 40  ? -14.196 35.239 28.617  1.00 23.15  ? 40  ASP B CB  1 
ATOM   4405 C CG  . ASP B 1 40  ? -12.874 35.012 27.916  1.00 28.36  ? 40  ASP B CG  1 
ATOM   4406 O OD1 . ASP B 1 40  ? -11.841 34.942 28.621  1.00 29.85  ? 40  ASP B OD1 1 
ATOM   4407 O OD2 . ASP B 1 40  ? -12.872 34.883 26.669  1.00 25.19  ? 40  ASP B OD2 1 
ATOM   4408 N N   . MET B 1 41  ? -16.892 34.468 30.333  1.00 24.35  ? 41  MET B N   1 
ATOM   4409 C CA  . MET B 1 41  ? -17.730 34.819 31.480  1.00 21.92  ? 41  MET B CA  1 
ATOM   4410 C C   . MET B 1 41  ? -17.662 33.779 32.597  1.00 22.64  ? 41  MET B C   1 
ATOM   4411 O O   . MET B 1 41  ? -17.346 34.163 33.734  1.00 25.69  ? 41  MET B O   1 
ATOM   4412 C CB  . MET B 1 41  ? -19.159 35.100 31.007  1.00 20.22  ? 41  MET B CB  1 
ATOM   4413 C CG  . MET B 1 41  ? -19.342 36.525 30.446  1.00 23.47  ? 41  MET B CG  1 
ATOM   4414 S SD  . MET B 1 41  ? -19.030 37.865 31.647  1.00 23.31  ? 41  MET B SD  1 
ATOM   4415 C CE  . MET B 1 41  ? -20.592 37.880 32.529  1.00 20.39  ? 41  MET B CE  1 
ATOM   4416 N N   . PRO B 1 42  ? -17.895 32.474 32.369  1.00 22.51  ? 42  PRO B N   1 
ATOM   4417 C CA  . PRO B 1 42  ? -17.631 31.508 33.454  1.00 23.76  ? 42  PRO B CA  1 
ATOM   4418 C C   . PRO B 1 42  ? -16.151 31.343 33.773  1.00 24.39  ? 42  PRO B C   1 
ATOM   4419 O O   . PRO B 1 42  ? -15.821 30.925 34.891  1.00 24.29  ? 42  PRO B O   1 
ATOM   4420 C CB  . PRO B 1 42  ? -18.244 30.198 32.931  1.00 26.92  ? 42  PRO B CB  1 
ATOM   4421 C CG  . PRO B 1 42  ? -18.223 30.332 31.454  1.00 23.35  ? 42  PRO B CG  1 
ATOM   4422 C CD  . PRO B 1 42  ? -18.422 31.801 31.162  1.00 21.55  ? 42  PRO B CD  1 
ATOM   4423 N N   . ALA B 1 43  ? -15.244 31.672 32.846  1.00 21.80  ? 43  ALA B N   1 
ATOM   4424 C CA  . ALA B 1 43  ? -13.821 31.507 33.142  1.00 22.25  ? 43  ALA B CA  1 
ATOM   4425 C C   . ALA B 1 43  ? -13.349 32.422 34.268  1.00 26.15  ? 43  ALA B C   1 
ATOM   4426 O O   . ALA B 1 43  ? -12.306 32.141 34.873  1.00 28.95  ? 43  ALA B O   1 
ATOM   4427 C CB  . ALA B 1 43  ? -12.973 31.732 31.889  1.00 17.31  ? 43  ALA B CB  1 
ATOM   4428 N N   . TYR B 1 44  ? -14.100 33.486 34.576  1.00 20.51  ? 44  TYR B N   1 
ATOM   4429 C CA  . TYR B 1 44  ? -13.773 34.340 35.720  1.00 23.75  ? 44  TYR B CA  1 
ATOM   4430 C C   . TYR B 1 44  ? -13.713 33.540 37.016  1.00 25.32  ? 44  TYR B C   1 
ATOM   4431 O O   . TYR B 1 44  ? -13.021 33.941 37.963  1.00 24.51  ? 44  TYR B O   1 
ATOM   4432 C CB  . TYR B 1 44  ? -14.820 35.461 35.867  1.00 24.52  ? 44  TYR B CB  1 
ATOM   4433 C CG  . TYR B 1 44  ? -14.581 36.691 35.016  1.00 28.06  ? 44  TYR B CG  1 
ATOM   4434 C CD1 . TYR B 1 44  ? -13.798 37.739 35.484  1.00 30.39  ? 44  TYR B CD1 1 
ATOM   4435 C CD2 . TYR B 1 44  ? -15.145 36.806 33.750  1.00 25.47  ? 44  TYR B CD2 1 
ATOM   4436 C CE1 . TYR B 1 44  ? -13.570 38.859 34.711  1.00 26.93  ? 44  TYR B CE1 1 
ATOM   4437 C CE2 . TYR B 1 44  ? -14.921 37.921 32.965  1.00 27.82  ? 44  TYR B CE2 1 
ATOM   4438 C CZ  . TYR B 1 44  ? -14.135 38.951 33.456  1.00 30.03  ? 44  TYR B CZ  1 
ATOM   4439 O OH  . TYR B 1 44  ? -13.895 40.080 32.699  1.00 28.68  ? 44  TYR B OH  1 
ATOM   4440 N N   . LEU B 1 45  ? -14.458 32.432 37.090  1.00 24.86  ? 45  LEU B N   1 
ATOM   4441 C CA  . LEU B 1 45  ? -14.495 31.605 38.292  1.00 28.01  ? 45  LEU B CA  1 
ATOM   4442 C C   . LEU B 1 45  ? -13.174 30.886 38.544  1.00 28.89  ? 45  LEU B C   1 
ATOM   4443 O O   . LEU B 1 45  ? -12.968 30.368 39.646  1.00 28.20  ? 45  LEU B O   1 
ATOM   4444 C CB  . LEU B 1 45  ? -15.646 30.593 38.202  1.00 21.96  ? 45  LEU B CB  1 
ATOM   4445 C CG  . LEU B 1 45  ? -17.077 31.161 38.244  1.00 25.66  ? 45  LEU B CG  1 
ATOM   4446 C CD1 . LEU B 1 45  ? -18.116 30.150 37.782  1.00 20.17  ? 45  LEU B CD1 1 
ATOM   4447 C CD2 . LEU B 1 45  ? -17.433 31.709 39.633  1.00 23.31  ? 45  LEU B CD2 1 
ATOM   4448 N N   . LYS B 1 46  ? -12.272 30.841 37.565  1.00 26.64  ? 46  LYS B N   1 
ATOM   4449 C CA  . LYS B 1 46  ? -10.944 30.317 37.846  1.00 26.66  ? 46  LYS B CA  1 
ATOM   4450 C C   . LYS B 1 46  ? -10.089 31.301 38.631  1.00 33.23  ? 46  LYS B C   1 
ATOM   4451 O O   . LYS B 1 46  ? -9.155  30.872 39.317  1.00 32.66  ? 46  LYS B O   1 
ATOM   4452 C CB  . LYS B 1 46  ? -10.239 29.940 36.545  1.00 28.18  ? 46  LYS B CB  1 
ATOM   4453 C CG  . LYS B 1 46  ? -11.101 29.106 35.626  1.00 39.59  ? 46  LYS B CG  1 
ATOM   4454 C CD  . LYS B 1 46  ? -10.460 28.921 34.274  1.00 49.14  ? 46  LYS B CD  1 
ATOM   4455 C CE  . LYS B 1 46  ? -10.805 27.554 33.699  1.00 56.26  ? 46  LYS B CE  1 
ATOM   4456 N NZ  . LYS B 1 46  ? -9.850  27.163 32.617  1.00 57.28  ? 46  LYS B NZ  1 
ATOM   4457 N N   . ASP B 1 47  ? -10.400 32.601 38.569  1.00 33.27  ? 47  ASP B N   1 
ATOM   4458 C CA  . ASP B 1 47  ? -9.565  33.633 39.173  1.00 34.53  ? 47  ASP B CA  1 
ATOM   4459 C C   . ASP B 1 47  ? -10.166 34.281 40.413  1.00 36.43  ? 47  ASP B C   1 
ATOM   4460 O O   . ASP B 1 47  ? -9.421  34.892 41.190  1.00 33.03  ? 47  ASP B O   1 
ATOM   4461 C CB  . ASP B 1 47  ? -9.260  34.741 38.154  1.00 33.13  ? 47  ASP B CB  1 
ATOM   4462 C CG  . ASP B 1 47  ? -8.256  34.306 37.100  1.00 38.22  ? 47  ASP B CG  1 
ATOM   4463 O OD1 . ASP B 1 47  ? -7.589  33.270 37.297  1.00 41.39  ? 47  ASP B OD1 1 
ATOM   4464 O OD2 . ASP B 1 47  ? -8.134  35.007 36.075  1.00 41.42  ? 47  ASP B OD2 1 
ATOM   4465 N N   . PHE B 1 48  ? -11.482 34.191 40.605  1.00 32.99  ? 48  PHE B N   1 
ATOM   4466 C CA  . PHE B 1 48  ? -12.156 34.772 41.759  1.00 32.96  ? 48  PHE B CA  1 
ATOM   4467 C C   . PHE B 1 48  ? -13.052 33.712 42.378  1.00 32.27  ? 48  PHE B C   1 
ATOM   4468 O O   . PHE B 1 48  ? -13.852 33.087 41.675  1.00 30.95  ? 48  PHE B O   1 
ATOM   4469 C CB  . PHE B 1 48  ? -12.967 36.010 41.352  1.00 37.23  ? 48  PHE B CB  1 
ATOM   4470 C CG  . PHE B 1 48  ? -12.173 37.013 40.558  1.00 34.35  ? 48  PHE B CG  1 
ATOM   4471 C CD1 . PHE B 1 48  ? -12.068 36.901 39.179  1.00 33.33  ? 48  PHE B CD1 1 
ATOM   4472 C CD2 . PHE B 1 48  ? -11.510 38.050 41.188  1.00 30.51  ? 48  PHE B CD2 1 
ATOM   4473 C CE1 . PHE B 1 48  ? -11.325 37.813 38.446  1.00 30.72  ? 48  PHE B CE1 1 
ATOM   4474 C CE2 . PHE B 1 48  ? -10.762 38.968 40.453  1.00 25.45  ? 48  PHE B CE2 1 
ATOM   4475 C CZ  . PHE B 1 48  ? -10.675 38.844 39.082  1.00 24.25  ? 48  PHE B CZ  1 
ATOM   4476 N N   . GLU B 1 49  ? -12.908 33.487 43.682  1.00 32.38  ? 49  GLU B N   1 
ATOM   4477 C CA  . GLU B 1 49  ? -13.625 32.386 44.325  1.00 39.28  ? 49  GLU B CA  1 
ATOM   4478 C C   . GLU B 1 49  ? -14.957 32.906 44.868  1.00 39.98  ? 49  GLU B C   1 
ATOM   4479 O O   . GLU B 1 49  ? -15.162 33.106 46.066  1.00 41.80  ? 49  GLU B O   1 
ATOM   4480 C CB  . GLU B 1 49  ? -12.773 31.728 45.406  1.00 50.56  ? 49  GLU B CB  1 
ATOM   4481 C CG  . GLU B 1 49  ? -13.330 30.365 45.872  1.00 61.03  ? 49  GLU B CG  1 
ATOM   4482 C CD  . GLU B 1 49  ? -12.281 29.256 45.946  1.00 67.86  ? 49  GLU B CD  1 
ATOM   4483 O OE1 . GLU B 1 49  ? -11.442 29.285 46.873  1.00 69.42  ? 49  GLU B OE1 1 
ATOM   4484 O OE2 . GLU B 1 49  ? -12.304 28.347 45.085  1.00 69.44  ? 49  GLU B OE2 1 
ATOM   4485 N N   . ILE B 1 50  ? -15.868 33.140 43.927  1.00 35.79  ? 50  ILE B N   1 
ATOM   4486 C CA  . ILE B 1 50  ? -17.253 33.484 44.215  1.00 30.18  ? 50  ILE B CA  1 
ATOM   4487 C C   . ILE B 1 50  ? -18.134 32.501 43.462  1.00 27.61  ? 50  ILE B C   1 
ATOM   4488 O O   . ILE B 1 50  ? -17.631 31.580 42.812  1.00 31.69  ? 50  ILE B O   1 
ATOM   4489 C CB  . ILE B 1 50  ? -17.563 34.941 43.822  1.00 25.80  ? 50  ILE B CB  1 
ATOM   4490 C CG1 . ILE B 1 50  ? -17.231 35.179 42.349  1.00 28.46  ? 50  ILE B CG1 1 
ATOM   4491 C CG2 . ILE B 1 50  ? -16.780 35.905 44.692  1.00 27.28  ? 50  ILE B CG2 1 
ATOM   4492 C CD1 . ILE B 1 50  ? -17.825 36.461 41.819  1.00 30.26  ? 50  ILE B CD1 1 
ATOM   4493 N N   . LYS B 1 51  ? -19.446 32.661 43.570  1.00 24.69  ? 51  LYS B N   1 
ATOM   4494 C CA  . LYS B 1 51  ? -20.406 31.857 42.825  1.00 22.23  ? 51  LYS B CA  1 
ATOM   4495 C C   . LYS B 1 51  ? -21.022 32.711 41.726  1.00 22.43  ? 51  LYS B C   1 
ATOM   4496 O O   . LYS B 1 51  ? -21.422 33.853 41.975  1.00 20.68  ? 51  LYS B O   1 
ATOM   4497 C CB  . LYS B 1 51  ? -21.505 31.307 43.738  1.00 24.65  ? 51  LYS B CB  1 
ATOM   4498 C CG  . LYS B 1 51  ? -21.017 30.739 45.067  1.00 31.01  ? 51  LYS B CG  1 
ATOM   4499 C CD  . LYS B 1 51  ? -20.147 29.509 44.865  1.00 27.87  ? 51  LYS B CD  1 
ATOM   4500 C CE  . LYS B 1 51  ? -19.847 28.838 46.201  1.00 31.61  ? 51  LYS B CE  1 
ATOM   4501 N NZ  . LYS B 1 51  ? -18.811 27.776 46.066  1.00 45.47  ? 51  LYS B NZ  1 
ATOM   4502 N N   . LEU B 1 52  ? -21.095 32.155 40.518  1.00 19.96  ? 52  LEU B N   1 
ATOM   4503 C CA  . LEU B 1 52  ? -21.714 32.807 39.371  1.00 24.13  ? 52  LEU B CA  1 
ATOM   4504 C C   . LEU B 1 52  ? -22.565 31.769 38.663  1.00 26.74  ? 52  LEU B C   1 
ATOM   4505 O O   . LEU B 1 52  ? -22.136 30.628 38.486  1.00 24.49  ? 52  LEU B O   1 
ATOM   4506 C CB  . LEU B 1 52  ? -20.680 33.379 38.395  1.00 23.38  ? 52  LEU B CB  1 
ATOM   4507 C CG  . LEU B 1 52  ? -19.742 34.472 38.913  1.00 24.20  ? 52  LEU B CG  1 
ATOM   4508 C CD1 . LEU B 1 52  ? -18.742 34.874 37.826  1.00 22.53  ? 52  LEU B CD1 1 
ATOM   4509 C CD2 . LEU B 1 52  ? -20.542 35.685 39.391  1.00 21.37  ? 52  LEU B CD2 1 
ATOM   4510 N N   . ASN B 1 53  ? -23.777 32.152 38.284  1.00 21.53  ? 53  ASN B N   1 
ATOM   4511 C CA  . ASN B 1 53  ? -24.699 31.211 37.670  1.00 18.55  ? 53  ASN B CA  1 
ATOM   4512 C C   . ASN B 1 53  ? -24.977 31.626 36.235  1.00 21.38  ? 53  ASN B C   1 
ATOM   4513 O O   . ASN B 1 53  ? -24.812 32.788 35.858  1.00 23.52  ? 53  ASN B O   1 
ATOM   4514 C CB  . ASN B 1 53  ? -25.972 31.109 38.489  1.00 23.69  ? 53  ASN B CB  1 
ATOM   4515 C CG  . ASN B 1 53  ? -25.676 30.810 39.947  1.00 25.69  ? 53  ASN B CG  1 
ATOM   4516 O OD1 . ASN B 1 53  ? -25.270 29.696 40.284  1.00 22.36  ? 53  ASN B OD1 1 
ATOM   4517 N ND2 . ASN B 1 53  ? -25.827 31.813 40.809  1.00 20.48  ? 53  ASN B ND2 1 
ATOM   4518 N N   . PHE B 1 54  ? -25.346 30.649 35.417  1.00 19.13  ? 54  PHE B N   1 
ATOM   4519 C CA  . PHE B 1 54  ? -25.466 30.892 33.991  1.00 21.65  ? 54  PHE B CA  1 
ATOM   4520 C C   . PHE B 1 54  ? -26.679 30.170 33.447  1.00 19.94  ? 54  PHE B C   1 
ATOM   4521 O O   . PHE B 1 54  ? -27.035 29.082 33.901  1.00 26.55  ? 54  PHE B O   1 
ATOM   4522 C CB  . PHE B 1 54  ? -24.205 30.437 33.242  1.00 19.03  ? 54  PHE B CB  1 
ATOM   4523 C CG  . PHE B 1 54  ? -22.969 31.138 33.689  1.00 24.24  ? 54  PHE B CG  1 
ATOM   4524 C CD1 . PHE B 1 54  ? -22.241 30.668 34.767  1.00 16.78  ? 54  PHE B CD1 1 
ATOM   4525 C CD2 . PHE B 1 54  ? -22.534 32.279 33.036  1.00 23.34  ? 54  PHE B CD2 1 
ATOM   4526 C CE1 . PHE B 1 54  ? -21.116 31.315 35.184  1.00 21.41  ? 54  PHE B CE1 1 
ATOM   4527 C CE2 . PHE B 1 54  ? -21.402 32.923 33.440  1.00 17.94  ? 54  PHE B CE2 1 
ATOM   4528 C CZ  . PHE B 1 54  ? -20.689 32.446 34.517  1.00 22.62  ? 54  PHE B CZ  1 
ATOM   4529 N N   . ASN B 1 55  ? -27.302 30.798 32.453  1.00 19.18  ? 55  ASN B N   1 
ATOM   4530 C CA  . ASN B 1 55  ? -28.359 30.196 31.662  1.00 22.98  ? 55  ASN B CA  1 
ATOM   4531 C C   . ASN B 1 55  ? -27.856 30.044 30.235  1.00 27.30  ? 55  ASN B C   1 
ATOM   4532 O O   . ASN B 1 55  ? -27.270 30.979 29.683  1.00 24.80  ? 55  ASN B O   1 
ATOM   4533 C CB  . ASN B 1 55  ? -29.625 31.054 31.676  1.00 21.82  ? 55  ASN B CB  1 
ATOM   4534 C CG  . ASN B 1 55  ? -30.764 30.388 30.951  1.00 19.47  ? 55  ASN B CG  1 
ATOM   4535 O OD1 . ASN B 1 55  ? -31.355 29.455 31.465  1.00 22.74  ? 55  ASN B OD1 1 
ATOM   4536 N ND2 . ASN B 1 55  ? -31.074 30.857 29.747  1.00 22.23  ? 55  ASN B ND2 1 
ATOM   4537 N N   . LEU B 1 56  ? -28.083 28.873 29.641  1.00 25.43  ? 56  LEU B N   1 
ATOM   4538 C CA  . LEU B 1 56  ? -27.693 28.621 28.256  1.00 23.13  ? 56  LEU B CA  1 
ATOM   4539 C C   . LEU B 1 56  ? -28.911 28.098 27.511  1.00 18.19  ? 56  LEU B C   1 
ATOM   4540 O O   . LEU B 1 56  ? -29.414 27.016 27.829  1.00 24.94  ? 56  LEU B O   1 
ATOM   4541 C CB  . LEU B 1 56  ? -26.542 27.614 28.172  1.00 23.99  ? 56  LEU B CB  1 
ATOM   4542 C CG  . LEU B 1 56  ? -25.200 27.905 28.849  1.00 26.55  ? 56  LEU B CG  1 
ATOM   4543 C CD1 . LEU B 1 56  ? -24.366 26.615 28.962  1.00 27.77  ? 56  LEU B CD1 1 
ATOM   4544 C CD2 . LEU B 1 56  ? -24.431 28.969 28.074  1.00 26.12  ? 56  LEU B CD2 1 
ATOM   4545 N N   . THR B 1 57  ? -29.380 28.845 26.510  1.00 22.06  ? 57  THR B N   1 
ATOM   4546 C CA  . THR B 1 57  ? -30.544 28.383 25.773  1.00 27.43  ? 57  THR B CA  1 
ATOM   4547 C C   . THR B 1 57  ? -30.146 27.212 24.879  1.00 23.38  ? 57  THR B C   1 
ATOM   4548 O O   . THR B 1 57  ? -29.013 27.147 24.397  1.00 21.46  ? 57  THR B O   1 
ATOM   4549 C CB  . THR B 1 57  ? -31.163 29.506 24.937  1.00 23.17  ? 57  THR B CB  1 
ATOM   4550 O OG1 . THR B 1 57  ? -30.298 29.841 23.840  1.00 23.08  ? 57  THR B OG1 1 
ATOM   4551 C CG2 . THR B 1 57  ? -31.399 30.734 25.822  1.00 16.31  ? 57  THR B CG2 1 
ATOM   4552 N N   . PRO B 1 58  ? -31.053 26.261 24.665  1.00 20.36  ? 58  PRO B N   1 
ATOM   4553 C CA  . PRO B 1 58  ? -30.699 25.107 23.830  1.00 22.27  ? 58  PRO B CA  1 
ATOM   4554 C C   . PRO B 1 58  ? -30.356 25.485 22.403  1.00 27.97  ? 58  PRO B C   1 
ATOM   4555 O O   . PRO B 1 58  ? -29.505 24.827 21.796  1.00 25.21  ? 58  PRO B O   1 
ATOM   4556 C CB  . PRO B 1 58  ? -31.947 24.227 23.905  1.00 24.84  ? 58  PRO B CB  1 
ATOM   4557 C CG  . PRO B 1 58  ? -32.634 24.657 25.197  1.00 26.20  ? 58  PRO B CG  1 
ATOM   4558 C CD  . PRO B 1 58  ? -32.390 26.131 25.265  1.00 19.69  ? 58  PRO B CD  1 
ATOM   4559 N N   . VAL B 1 59  ? -30.983 26.529 21.845  1.00 21.77  ? 59  VAL B N   1 
ATOM   4560 C CA  . VAL B 1 59  ? -30.654 26.897 20.473  1.00 25.10  ? 59  VAL B CA  1 
ATOM   4561 C C   . VAL B 1 59  ? -29.244 27.473 20.406  1.00 21.55  ? 59  VAL B C   1 
ATOM   4562 O O   . VAL B 1 59  ? -28.547 27.311 19.398  1.00 26.23  ? 59  VAL B O   1 
ATOM   4563 C CB  . VAL B 1 59  ? -31.706 27.865 19.891  1.00 22.06  ? 59  VAL B CB  1 
ATOM   4564 C CG1 . VAL B 1 59  ? -31.784 29.135 20.717  1.00 20.86  ? 59  VAL B CG1 1 
ATOM   4565 C CG2 . VAL B 1 59  ? -31.390 28.191 18.421  1.00 23.49  ? 59  VAL B CG2 1 
ATOM   4566 N N   . LEU B 1 60  ? -28.792 28.147 21.465  1.00 21.47  ? 60  LEU B N   1 
ATOM   4567 C CA  . LEU B 1 60  ? -27.413 28.623 21.472  1.00 23.60  ? 60  LEU B CA  1 
ATOM   4568 C C   . LEU B 1 60  ? -26.441 27.459 21.616  1.00 18.85  ? 60  LEU B C   1 
ATOM   4569 O O   . LEU B 1 60  ? -25.411 27.415 20.933  1.00 23.63  ? 60  LEU B O   1 
ATOM   4570 C CB  . LEU B 1 60  ? -27.203 29.645 22.594  1.00 22.78  ? 60  LEU B CB  1 
ATOM   4571 C CG  . LEU B 1 60  ? -25.728 29.878 22.953  1.00 22.41  ? 60  LEU B CG  1 
ATOM   4572 C CD1 . LEU B 1 60  ? -25.006 30.573 21.817  1.00 20.41  ? 60  LEU B CD1 1 
ATOM   4573 C CD2 . LEU B 1 60  ? -25.576 30.661 24.276  1.00 20.97  ? 60  LEU B CD2 1 
ATOM   4574 N N   . ILE B 1 61  ? -26.757 26.502 22.494  1.00 23.27  ? 61  ILE B N   1 
ATOM   4575 C CA  . ILE B 1 61  ? -25.916 25.320 22.633  1.00 24.43  ? 61  ILE B CA  1 
ATOM   4576 C C   . ILE B 1 61  ? -25.738 24.625 21.286  1.00 27.09  ? 61  ILE B C   1 
ATOM   4577 O O   . ILE B 1 61  ? -24.630 24.205 20.936  1.00 25.95  ? 61  ILE B O   1 
ATOM   4578 C CB  . ILE B 1 61  ? -26.500 24.366 23.693  1.00 23.44  ? 61  ILE B CB  1 
ATOM   4579 C CG1 . ILE B 1 61  ? -26.439 25.006 25.082  1.00 18.44  ? 61  ILE B CG1 1 
ATOM   4580 C CG2 . ILE B 1 61  ? -25.726 23.062 23.719  1.00 26.93  ? 61  ILE B CG2 1 
ATOM   4581 C CD1 . ILE B 1 61  ? -27.115 24.192 26.147  1.00 19.79  ? 61  ILE B CD1 1 
ATOM   4582 N N   . ASP B 1 62  ? -26.815 24.504 20.507  1.00 21.42  ? 62  ASP B N   1 
ATOM   4583 C CA  . ASP B 1 62  ? -26.707 23.838 19.205  1.00 33.63  ? 62  ASP B CA  1 
ATOM   4584 C C   . ASP B 1 62  ? -25.644 24.497 18.337  1.00 33.20  ? 62  ASP B C   1 
ATOM   4585 O O   . ASP B 1 62  ? -24.774 23.820 17.767  1.00 27.21  ? 62  ASP B O   1 
ATOM   4586 C CB  . ASP B 1 62  ? -28.047 23.863 18.469  1.00 32.03  ? 62  ASP B CB  1 
ATOM   4587 C CG  . ASP B 1 62  ? -29.052 22.904 19.046  1.00 35.34  ? 62  ASP B CG  1 
ATOM   4588 O OD1 . ASP B 1 62  ? -28.643 21.867 19.609  1.00 37.07  ? 62  ASP B OD1 1 
ATOM   4589 O OD2 . ASP B 1 62  ? -30.257 23.193 18.932  1.00 34.61  ? 62  ASP B OD2 1 
ATOM   4590 N N   . GLN B 1 63  ? -25.704 25.825 18.225  1.00 29.58  ? 63  GLN B N   1 
ATOM   4591 C CA  . GLN B 1 63  ? -24.781 26.550 17.360  1.00 23.14  ? 63  GLN B CA  1 
ATOM   4592 C C   . GLN B 1 63  ? -23.354 26.491 17.893  1.00 24.79  ? 63  GLN B C   1 
ATOM   4593 O O   . GLN B 1 63  ? -22.402 26.341 17.120  1.00 28.45  ? 63  GLN B O   1 
ATOM   4594 C CB  . GLN B 1 63  ? -25.252 27.999 17.203  1.00 21.68  ? 63  GLN B CB  1 
ATOM   4595 C CG  . GLN B 1 63  ? -26.712 28.097 16.833  1.00 19.84  ? 63  GLN B CG  1 
ATOM   4596 C CD  . GLN B 1 63  ? -27.251 29.520 16.846  1.00 36.19  ? 63  GLN B CD  1 
ATOM   4597 O OE1 . GLN B 1 63  ? -26.960 30.315 15.950  1.00 35.45  ? 63  GLN B OE1 1 
ATOM   4598 N NE2 . GLN B 1 63  ? -28.054 29.842 17.861  1.00 31.19  ? 63  GLN B NE2 1 
ATOM   4599 N N   . ILE B 1 64  ? -23.177 26.609 19.207  1.00 28.96  ? 64  ILE B N   1 
ATOM   4600 C CA  . ILE B 1 64  ? -21.837 26.465 19.764  1.00 24.67  ? 64  ILE B CA  1 
ATOM   4601 C C   . ILE B 1 64  ? -21.258 25.103 19.387  1.00 25.19  ? 64  ILE B C   1 
ATOM   4602 O O   . ILE B 1 64  ? -20.088 24.998 18.993  1.00 26.15  ? 64  ILE B O   1 
ATOM   4603 C CB  . ILE B 1 64  ? -21.864 26.690 21.288  1.00 25.79  ? 64  ILE B CB  1 
ATOM   4604 C CG1 . ILE B 1 64  ? -21.947 28.192 21.602  1.00 26.55  ? 64  ILE B CG1 1 
ATOM   4605 C CG2 . ILE B 1 64  ? -20.635 26.045 21.957  1.00 31.13  ? 64  ILE B CG2 1 
ATOM   4606 C CD1 . ILE B 1 64  ? -22.147 28.511 23.076  1.00 23.11  ? 64  ILE B CD1 1 
ATOM   4607 N N   . GLN B 1 65  ? -22.083 24.048 19.442  1.00 20.43  ? 65  GLN B N   1 
ATOM   4608 C CA  . GLN B 1 65  ? -21.605 22.717 19.074  1.00 28.61  ? 65  GLN B CA  1 
ATOM   4609 C C   . GLN B 1 65  ? -21.228 22.639 17.601  1.00 31.49  ? 65  GLN B C   1 
ATOM   4610 O O   . GLN B 1 65  ? -20.179 22.080 17.255  1.00 30.15  ? 65  GLN B O   1 
ATOM   4611 C CB  . GLN B 1 65  ? -22.662 21.668 19.396  1.00 31.37  ? 65  GLN B CB  1 
ATOM   4612 C CG  . GLN B 1 65  ? -22.741 21.295 20.868  1.00 31.91  ? 65  GLN B CG  1 
ATOM   4613 C CD  . GLN B 1 65  ? -23.835 20.278 21.141  1.00 36.66  ? 65  GLN B CD  1 
ATOM   4614 O OE1 . GLN B 1 65  ? -24.975 20.451 20.722  1.00 29.65  ? 65  GLN B OE1 1 
ATOM   4615 N NE2 . GLN B 1 65  ? -23.486 19.204 21.835  1.00 45.64  ? 65  GLN B NE2 1 
ATOM   4616 N N   . GLU B 1 66  ? -22.074 23.181 16.719  1.00 33.74  ? 66  GLU B N   1 
ATOM   4617 C CA  . GLU B 1 66  ? -21.760 23.160 15.293  1.00 34.18  ? 66  GLU B CA  1 
ATOM   4618 C C   . GLU B 1 66  ? -20.449 23.889 15.004  1.00 32.06  ? 66  GLU B C   1 
ATOM   4619 O O   . GLU B 1 66  ? -19.627 23.408 14.213  1.00 29.57  ? 66  GLU B O   1 
ATOM   4620 C CB  . GLU B 1 66  ? -22.911 23.766 14.488  1.00 34.78  ? 66  GLU B CB  1 
ATOM   4621 C CG  . GLU B 1 66  ? -22.911 23.362 13.017  1.00 39.75  ? 66  GLU B CG  1 
ATOM   4622 C CD  . GLU B 1 66  ? -24.164 23.813 12.272  1.00 44.07  ? 66  GLU B CD  1 
ATOM   4623 O OE1 . GLU B 1 66  ? -25.099 24.336 12.918  1.00 41.45  ? 66  GLU B OE1 1 
ATOM   4624 O OE2 . GLU B 1 66  ? -24.207 23.647 11.032  1.00 46.43  ? 66  GLU B OE2 1 
ATOM   4625 N N   . TYR B 1 67  ? -20.223 25.041 15.648  1.00 22.19  ? 67  TYR B N   1 
ATOM   4626 C CA  . TYR B 1 67  ? -18.968 25.760 15.439  1.00 24.33  ? 67  TYR B CA  1 
ATOM   4627 C C   . TYR B 1 67  ? -17.793 24.960 15.987  1.00 33.93  ? 67  TYR B C   1 
ATOM   4628 O O   . TYR B 1 67  ? -16.723 24.893 15.368  1.00 36.35  ? 67  TYR B O   1 
ATOM   4629 C CB  . TYR B 1 67  ? -19.022 27.136 16.110  1.00 21.73  ? 67  TYR B CB  1 
ATOM   4630 C CG  . TYR B 1 67  ? -19.645 28.247 15.285  1.00 26.79  ? 67  TYR B CG  1 
ATOM   4631 C CD1 . TYR B 1 67  ? -18.890 28.964 14.359  1.00 24.82  ? 67  TYR B CD1 1 
ATOM   4632 C CD2 . TYR B 1 67  ? -20.981 28.599 15.456  1.00 27.61  ? 67  TYR B CD2 1 
ATOM   4633 C CE1 . TYR B 1 67  ? -19.461 30.003 13.613  1.00 26.96  ? 67  TYR B CE1 1 
ATOM   4634 C CE2 . TYR B 1 67  ? -21.559 29.633 14.716  1.00 24.84  ? 67  TYR B CE2 1 
ATOM   4635 C CZ  . TYR B 1 67  ? -20.796 30.329 13.794  1.00 25.90  ? 67  TYR B CZ  1 
ATOM   4636 O OH  . TYR B 1 67  ? -21.373 31.362 13.062  1.00 23.05  ? 67  TYR B OH  1 
ATOM   4637 N N   . ALA B 1 68  ? -17.987 24.348 17.155  1.00 35.37  ? 68  ALA B N   1 
ATOM   4638 C CA  . ALA B 1 68  ? -16.948 23.550 17.793  1.00 31.13  ? 68  ALA B CA  1 
ATOM   4639 C C   . ALA B 1 68  ? -16.540 22.371 16.919  1.00 32.52  ? 68  ALA B C   1 
ATOM   4640 O O   . ALA B 1 68  ? -15.344 22.093 16.748  1.00 34.71  ? 68  ALA B O   1 
ATOM   4641 C CB  . ALA B 1 68  ? -17.454 23.064 19.152  1.00 30.56  ? 68  ALA B CB  1 
ATOM   4642 N N   . GLN B 1 69  ? -17.518 21.672 16.348  1.00 23.11  ? 69  GLN B N   1 
ATOM   4643 C CA  . GLN B 1 69  ? -17.221 20.532 15.492  1.00 31.56  ? 69  GLN B CA  1 
ATOM   4644 C C   . GLN B 1 69  ? -16.694 20.951 14.127  1.00 41.58  ? 69  GLN B C   1 
ATOM   4645 O O   . GLN B 1 69  ? -16.279 20.084 13.351  1.00 46.21  ? 69  GLN B O   1 
ATOM   4646 C CB  . GLN B 1 69  ? -18.471 19.665 15.328  1.00 29.15  ? 69  GLN B CB  1 
ATOM   4647 C CG  . GLN B 1 69  ? -18.924 18.982 16.616  1.00 38.06  ? 69  GLN B CG  1 
ATOM   4648 C CD  . GLN B 1 69  ? -20.371 18.496 16.555  1.00 45.50  ? 69  GLN B CD  1 
ATOM   4649 O OE1 . GLN B 1 69  ? -21.002 18.511 15.496  1.00 52.68  ? 69  GLN B OE1 1 
ATOM   4650 N NE2 . GLN B 1 69  ? -20.902 18.071 17.699  1.00 42.83  ? 69  GLN B NE2 1 
ATOM   4651 N N   . GLY B 1 70  ? -16.698 22.246 13.820  1.00 41.29  ? 70  GLY B N   1 
ATOM   4652 C CA  . GLY B 1 70  ? -16.199 22.719 12.546  1.00 39.54  ? 70  GLY B CA  1 
ATOM   4653 C C   . GLY B 1 70  ? -17.156 22.560 11.391  1.00 39.35  ? 70  GLY B C   1 
ATOM   4654 O O   . GLY B 1 70  ? -16.712 22.456 10.244  1.00 40.06  ? 70  GLY B O   1 
ATOM   4655 N N   . LYS B 1 71  ? -18.463 22.532 11.652  1.00 40.36  ? 71  LYS B N   1 
ATOM   4656 C CA  . LYS B 1 71  ? -19.461 22.371 10.605  1.00 38.82  ? 71  LYS B CA  1 
ATOM   4657 C C   . LYS B 1 71  ? -20.210 23.656 10.275  1.00 35.09  ? 71  LYS B C   1 
ATOM   4658 O O   . LYS B 1 71  ? -21.005 23.660 9.329   1.00 33.20  ? 71  LYS B O   1 
ATOM   4659 C CB  . LYS B 1 71  ? -20.473 21.289 10.984  1.00 43.80  ? 71  LYS B CB  1 
ATOM   4660 C CG  . LYS B 1 71  ? -19.857 19.933 11.272  1.00 48.49  ? 71  LYS B CG  1 
ATOM   4661 C CD  . LYS B 1 71  ? -20.727 19.130 12.235  1.00 53.42  ? 71  LYS B CD  1 
ATOM   4662 C CE  . LYS B 1 71  ? -21.346 17.910 11.558  1.00 56.80  ? 71  LYS B CE  1 
ATOM   4663 N NZ  . LYS B 1 71  ? -22.715 17.624 12.077  1.00 57.02  ? 71  LYS B NZ  1 
ATOM   4664 N N   . ALA B 1 72  ? -19.996 24.729 11.034  1.00 31.60  ? 72  ALA B N   1 
ATOM   4665 C CA  . ALA B 1 72  ? -20.713 25.979 10.804  1.00 32.23  ? 72  ALA B CA  1 
ATOM   4666 C C   . ALA B 1 72  ? -20.148 26.677 9.572   1.00 39.53  ? 72  ALA B C   1 
ATOM   4667 O O   . ALA B 1 72  ? -18.971 27.058 9.547   1.00 40.85  ? 72  ALA B O   1 
ATOM   4668 C CB  . ALA B 1 72  ? -20.617 26.884 12.031  1.00 28.56  ? 72  ALA B CB  1 
ATOM   4669 N N   . LYS B 1 73  ? -20.980 26.843 8.546   1.00 39.53  ? 73  LYS B N   1 
ATOM   4670 C CA  . LYS B 1 73  ? -20.584 27.592 7.353   1.00 41.35  ? 73  LYS B CA  1 
ATOM   4671 C C   . LYS B 1 73  ? -21.055 29.030 7.537   1.00 36.42  ? 73  LYS B C   1 
ATOM   4672 O O   . LYS B 1 73  ? -22.163 29.397 7.155   1.00 36.41  ? 73  LYS B O   1 
ATOM   4673 C CB  . LYS B 1 73  ? -21.164 26.954 6.095   1.00 43.58  ? 73  LYS B CB  1 
ATOM   4674 C CG  . LYS B 1 73  ? -20.819 25.478 5.948   1.00 46.51  ? 73  LYS B CG  1 
ATOM   4675 C CD  . LYS B 1 73  ? -21.486 24.844 4.724   1.00 54.14  ? 73  LYS B CD  1 
ATOM   4676 C CE  . LYS B 1 73  ? -22.994 24.675 4.910   1.00 57.81  ? 73  LYS B CE  1 
ATOM   4677 N NZ  . LYS B 1 73  ? -23.366 23.653 5.940   1.00 56.37  ? 73  LYS B NZ  1 
ATOM   4678 N N   . ASP B 1 74  ? -20.191 29.854 8.130   1.00 29.78  ? 74  ASP B N   1 
ATOM   4679 C CA  . ASP B 1 74  ? -20.516 31.235 8.471   1.00 27.90  ? 74  ASP B CA  1 
ATOM   4680 C C   . ASP B 1 74  ? -20.067 32.167 7.346   1.00 32.43  ? 74  ASP B C   1 
ATOM   4681 O O   . ASP B 1 74  ? -18.869 32.256 7.046   1.00 34.62  ? 74  ASP B O   1 
ATOM   4682 C CB  . ASP B 1 74  ? -19.850 31.604 9.797   1.00 25.86  ? 74  ASP B CB  1 
ATOM   4683 C CG  . ASP B 1 74  ? -20.307 32.947 10.343  1.00 33.74  ? 74  ASP B CG  1 
ATOM   4684 O OD1 . ASP B 1 74  ? -20.402 33.926 9.562   1.00 32.29  ? 74  ASP B OD1 1 
ATOM   4685 O OD2 . ASP B 1 74  ? -20.555 33.021 11.569  1.00 34.47  ? 74  ASP B OD2 1 
ATOM   4686 N N   . VAL B 1 75  ? -21.021 32.889 6.751   1.00 33.01  ? 75  VAL B N   1 
ATOM   4687 C CA  . VAL B 1 75  ? -20.730 33.673 5.553   1.00 35.35  ? 75  VAL B CA  1 
ATOM   4688 C C   . VAL B 1 75  ? -19.861 34.883 5.883   1.00 34.51  ? 75  VAL B C   1 
ATOM   4689 O O   . VAL B 1 75  ? -18.996 35.268 5.090   1.00 35.60  ? 75  VAL B O   1 
ATOM   4690 C CB  . VAL B 1 75  ? -22.037 34.078 4.842   1.00 45.25  ? 75  VAL B CB  1 
ATOM   4691 C CG1 . VAL B 1 75  ? -22.921 32.861 4.640   1.00 50.17  ? 75  VAL B CG1 1 
ATOM   4692 C CG2 . VAL B 1 75  ? -22.789 35.156 5.609   1.00 47.30  ? 75  VAL B CG2 1 
ATOM   4693 N N   . PHE B 1 76  ? -20.069 35.505 7.048   1.00 35.49  ? 76  PHE B N   1 
ATOM   4694 C CA  . PHE B 1 76  ? -19.200 36.606 7.456   1.00 32.91  ? 76  PHE B CA  1 
ATOM   4695 C C   . PHE B 1 76  ? -17.806 36.107 7.822   1.00 29.98  ? 76  PHE B C   1 
ATOM   4696 O O   . PHE B 1 76  ? -16.806 36.781 7.546   1.00 26.30  ? 76  PHE B O   1 
ATOM   4697 C CB  . PHE B 1 76  ? -19.819 37.361 8.628   1.00 39.30  ? 76  PHE B CB  1 
ATOM   4698 C CG  . PHE B 1 76  ? -20.794 38.423 8.208   1.00 48.37  ? 76  PHE B CG  1 
ATOM   4699 C CD1 . PHE B 1 76  ? -22.116 38.098 7.924   1.00 45.96  ? 76  PHE B CD1 1 
ATOM   4700 C CD2 . PHE B 1 76  ? -20.386 39.743 8.077   1.00 47.50  ? 76  PHE B CD2 1 
ATOM   4701 C CE1 . PHE B 1 76  ? -23.015 39.066 7.528   1.00 42.93  ? 76  PHE B CE1 1 
ATOM   4702 C CE2 . PHE B 1 76  ? -21.279 40.720 7.679   1.00 45.58  ? 76  PHE B CE2 1 
ATOM   4703 C CZ  . PHE B 1 76  ? -22.598 40.382 7.408   1.00 44.01  ? 76  PHE B CZ  1 
ATOM   4704 N N   . LEU B 1 77  ? -17.722 34.930 8.445   1.00 31.39  ? 77  LEU B N   1 
ATOM   4705 C CA  . LEU B 1 77  ? -16.426 34.337 8.757   1.00 37.19  ? 77  LEU B CA  1 
ATOM   4706 C C   . LEU B 1 77  ? -15.677 33.927 7.495   1.00 40.66  ? 77  LEU B C   1 
ATOM   4707 O O   . LEU B 1 77  ? -14.442 33.922 7.488   1.00 35.22  ? 77  LEU B O   1 
ATOM   4708 C CB  . LEU B 1 77  ? -16.616 33.131 9.683   1.00 40.68  ? 77  LEU B CB  1 
ATOM   4709 C CG  . LEU B 1 77  ? -15.569 32.810 10.755  1.00 39.97  ? 77  LEU B CG  1 
ATOM   4710 C CD1 . LEU B 1 77  ? -15.058 34.076 11.434  1.00 42.89  ? 77  LEU B CD1 1 
ATOM   4711 C CD2 . LEU B 1 77  ? -16.155 31.841 11.784  1.00 26.79  ? 77  LEU B CD2 1 
ATOM   4712 N N   . GLU B 1 78  ? -16.398 33.570 6.426   1.00 41.27  ? 78  GLU B N   1 
ATOM   4713 C CA  . GLU B 1 78  ? -15.727 33.246 5.171   1.00 46.13  ? 78  GLU B CA  1 
ATOM   4714 C C   . GLU B 1 78  ? -15.094 34.488 4.556   1.00 43.55  ? 78  GLU B C   1 
ATOM   4715 O O   . GLU B 1 78  ? -14.015 34.413 3.959   1.00 43.30  ? 78  GLU B O   1 
ATOM   4716 C CB  . GLU B 1 78  ? -16.712 32.611 4.189   1.00 50.93  ? 78  GLU B CB  1 
ATOM   4717 C CG  . GLU B 1 78  ? -17.158 31.206 4.559   1.00 57.26  ? 78  GLU B CG  1 
ATOM   4718 C CD  . GLU B 1 78  ? -16.060 30.176 4.393   1.00 64.51  ? 78  GLU B CD  1 
ATOM   4719 O OE1 . GLU B 1 78  ? -15.226 30.337 3.475   1.00 66.10  ? 78  GLU B OE1 1 
ATOM   4720 O OE2 . GLU B 1 78  ? -16.031 29.206 5.182   1.00 65.64  ? 78  GLU B OE2 1 
ATOM   4721 N N   . ALA B 1 79  ? -15.760 35.638 4.691   1.00 40.71  ? 79  ALA B N   1 
ATOM   4722 C CA  . ALA B 1 79  ? -15.201 36.892 4.205   1.00 36.49  ? 79  ALA B CA  1 
ATOM   4723 C C   . ALA B 1 79  ? -14.027 37.352 5.056   1.00 40.30  ? 79  ALA B C   1 
ATOM   4724 O O   . ALA B 1 79  ? -13.171 38.107 4.576   1.00 39.89  ? 79  ALA B O   1 
ATOM   4725 C CB  . ALA B 1 79  ? -16.285 37.967 4.171   1.00 30.23  ? 79  ALA B CB  1 
ATOM   4726 N N   . ILE B 1 80  ? -13.975 36.917 6.318   1.00 33.85  ? 80  ILE B N   1 
ATOM   4727 C CA  . ILE B 1 80  ? -12.834 37.209 7.178   1.00 32.54  ? 80  ILE B CA  1 
ATOM   4728 C C   . ILE B 1 80  ? -11.661 36.294 6.847   1.00 37.13  ? 80  ILE B C   1 
ATOM   4729 O O   . ILE B 1 80  ? -10.518 36.744 6.707   1.00 34.97  ? 80  ILE B O   1 
ATOM   4730 C CB  . ILE B 1 80  ? -13.241 37.068 8.657   1.00 33.57  ? 80  ILE B CB  1 
ATOM   4731 C CG1 . ILE B 1 80  ? -14.314 38.095 9.037   1.00 36.52  ? 80  ILE B CG1 1 
ATOM   4732 C CG2 . ILE B 1 80  ? -12.010 37.154 9.553   1.00 38.20  ? 80  ILE B CG2 1 
ATOM   4733 C CD1 . ILE B 1 80  ? -13.767 39.379 9.600   1.00 44.25  ? 80  ILE B CD1 1 
ATOM   4734 N N   . ARG B 1 81  ? -11.931 34.991 6.727   1.00 39.16  ? 81  ARG B N   1 
ATOM   4735 C CA  . ARG B 1 81  ? -10.857 34.014 6.596   1.00 36.05  ? 81  ARG B CA  1 
ATOM   4736 C C   . ARG B 1 81  ? -10.128 34.157 5.269   1.00 34.10  ? 81  ARG B C   1 
ATOM   4737 O O   . ARG B 1 81  ? -8.899  34.027 5.215   1.00 36.36  ? 81  ARG B O   1 
ATOM   4738 C CB  . ARG B 1 81  ? -11.417 32.598 6.741   1.00 40.38  ? 81  ARG B CB  1 
ATOM   4739 C CG  . ARG B 1 81  ? -10.344 31.510 6.807   1.00 48.57  ? 81  ARG B CG  1 
ATOM   4740 C CD  . ARG B 1 81  ? -10.925 30.123 6.581   1.00 51.90  ? 81  ARG B CD  1 
ATOM   4741 N NE  . ARG B 1 81  ? -11.626 29.626 7.763   1.00 52.71  ? 81  ARG B NE  1 
ATOM   4742 C CZ  . ARG B 1 81  ? -11.033 29.004 8.780   1.00 55.21  ? 81  ARG B CZ  1 
ATOM   4743 N NH1 . ARG B 1 81  ? -9.723  28.798 8.759   1.00 54.87  ? 81  ARG B NH1 1 
ATOM   4744 N NH2 . ARG B 1 81  ? -11.749 28.589 9.820   1.00 53.34  ? 81  ARG B NH2 1 
ATOM   4745 N N   . LYS B 1 82  ? -10.862 34.438 4.195   1.00 35.21  ? 82  LYS B N   1 
ATOM   4746 C CA  . LYS B 1 82  ? -10.303 34.348 2.852   1.00 39.76  ? 82  LYS B CA  1 
ATOM   4747 C C   . LYS B 1 82  ? -9.196  35.368 2.632   1.00 45.19  ? 82  LYS B C   1 
ATOM   4748 O O   . LYS B 1 82  ? -9.192  36.459 3.213   1.00 42.32  ? 82  LYS B O   1 
ATOM   4749 C CB  . LYS B 1 82  ? -11.390 34.561 1.808   1.00 43.87  ? 82  LYS B CB  1 
ATOM   4750 C CG  . LYS B 1 82  ? -12.177 33.312 1.512   1.00 51.39  ? 82  LYS B CG  1 
ATOM   4751 C CD  . LYS B 1 82  ? -13.449 33.668 0.792   1.00 55.20  ? 82  LYS B CD  1 
ATOM   4752 C CE  . LYS B 1 82  ? -13.262 33.422 -0.680  1.00 58.66  ? 82  LYS B CE  1 
ATOM   4753 N NZ  . LYS B 1 82  ? -14.389 33.921 -1.523  1.00 64.45  ? 82  LYS B NZ  1 
ATOM   4754 N N   . ASP B 1 83  ? -8.241  34.989 1.788   1.00 43.52  ? 83  ASP B N   1 
ATOM   4755 C CA  . ASP B 1 83  ? -7.308  35.959 1.247   1.00 38.19  ? 83  ASP B CA  1 
ATOM   4756 C C   . ASP B 1 83  ? -8.112  37.040 0.537   1.00 35.00  ? 83  ASP B C   1 
ATOM   4757 O O   . ASP B 1 83  ? -9.024  36.713 -0.238  1.00 34.32  ? 83  ASP B O   1 
ATOM   4758 C CB  . ASP B 1 83  ? -6.331  35.295 0.274   1.00 39.96  ? 83  ASP B CB  1 
ATOM   4759 C CG  . ASP B 1 83  ? -5.024  36.066 0.131   1.00 42.17  ? 83  ASP B CG  1 
ATOM   4760 O OD1 . ASP B 1 83  ? -5.031  37.186 -0.436  1.00 35.09  ? 83  ASP B OD1 1 
ATOM   4761 O OD2 . ASP B 1 83  ? -3.984  35.547 0.599   1.00 44.08  ? 83  ASP B OD2 1 
ATOM   4762 N N   . PRO B 1 84  ? -7.841  38.320 0.797   1.00 32.12  ? 84  PRO B N   1 
ATOM   4763 C CA  . PRO B 1 84  ? -8.571  39.384 0.094   1.00 29.77  ? 84  PRO B CA  1 
ATOM   4764 C C   . PRO B 1 84  ? -8.569  39.220 -1.412  1.00 34.28  ? 84  PRO B C   1 
ATOM   4765 O O   . PRO B 1 84  ? -9.552  39.594 -2.063  1.00 37.03  ? 84  PRO B O   1 
ATOM   4766 C CB  . PRO B 1 84  ? -7.826  40.654 0.523   1.00 29.43  ? 84  PRO B CB  1 
ATOM   4767 C CG  . PRO B 1 84  ? -7.259  40.316 1.849   1.00 29.41  ? 84  PRO B CG  1 
ATOM   4768 C CD  . PRO B 1 84  ? -6.892  38.857 1.785   1.00 31.96  ? 84  PRO B CD  1 
ATOM   4769 N N   . ASP B 1 85  ? -7.502  38.654 -1.991  1.00 33.88  ? 85  ASP B N   1 
ATOM   4770 C CA  . ASP B 1 85  ? -7.484  38.432 -3.432  1.00 35.51  ? 85  ASP B CA  1 
ATOM   4771 C C   . ASP B 1 85  ? -8.562  37.450 -3.870  1.00 39.16  ? 85  ASP B C   1 
ATOM   4772 O O   . ASP B 1 85  ? -8.922  37.428 -5.051  1.00 39.70  ? 85  ASP B O   1 
ATOM   4773 C CB  . ASP B 1 85  ? -6.106  37.934 -3.879  1.00 39.87  ? 85  ASP B CB  1 
ATOM   4774 C CG  . ASP B 1 85  ? -5.039  39.025 -3.837  1.00 42.96  ? 85  ASP B CG  1 
ATOM   4775 O OD1 . ASP B 1 85  ? -5.390  40.223 -3.935  1.00 43.92  ? 85  ASP B OD1 1 
ATOM   4776 O OD2 . ASP B 1 85  ? -3.843  38.685 -3.709  1.00 43.01  ? 85  ASP B OD2 1 
ATOM   4777 N N   . ASP B 1 86  ? -9.092  36.648 -2.947  1.00 39.73  ? 86  ASP B N   1 
ATOM   4778 C CA  . ASP B 1 86  ? -10.147 35.689 -3.241  1.00 41.28  ? 86  ASP B CA  1 
ATOM   4779 C C   . ASP B 1 86  ? -11.537 36.197 -2.871  1.00 39.05  ? 86  ASP B C   1 
ATOM   4780 O O   . ASP B 1 86  ? -12.515 35.460 -3.039  1.00 39.30  ? 86  ASP B O   1 
ATOM   4781 C CB  . ASP B 1 86  ? -9.876  34.364 -2.513  1.00 45.05  ? 86  ASP B CB  1 
ATOM   4782 C CG  . ASP B 1 86  ? -8.557  33.733 -2.920  1.00 46.24  ? 86  ASP B CG  1 
ATOM   4783 O OD1 . ASP B 1 86  ? -8.055  34.070 -4.011  1.00 44.85  ? 86  ASP B OD1 1 
ATOM   4784 O OD2 . ASP B 1 86  ? -8.023  32.903 -2.149  1.00 48.16  ? 86  ASP B OD2 1 
ATOM   4785 N N   . LEU B 1 87  ? -11.652 37.432 -2.385  1.00 32.70  ? 87  LEU B N   1 
ATOM   4786 C CA  . LEU B 1 87  ? -12.943 37.969 -1.968  1.00 30.15  ? 87  LEU B CA  1 
ATOM   4787 C C   . LEU B 1 87  ? -13.779 38.365 -3.177  1.00 34.53  ? 87  LEU B C   1 
ATOM   4788 O O   . LEU B 1 87  ? -13.282 39.014 -4.106  1.00 34.32  ? 87  LEU B O   1 
ATOM   4789 C CB  . LEU B 1 87  ? -12.757 39.184 -1.054  1.00 32.55  ? 87  LEU B CB  1 
ATOM   4790 C CG  . LEU B 1 87  ? -12.363 38.954 0.405   1.00 39.20  ? 87  LEU B CG  1 
ATOM   4791 C CD1 . LEU B 1 87  ? -12.094 40.294 1.102   1.00 39.34  ? 87  LEU B CD1 1 
ATOM   4792 C CD2 . LEU B 1 87  ? -13.430 38.150 1.159   1.00 34.94  ? 87  LEU B CD2 1 
ATOM   4793 N N   . GLU B 1 88  ? -15.048 37.965 -3.168  1.00 33.67  ? 88  GLU B N   1 
ATOM   4794 C CA  . GLU B 1 88  ? -16.020 38.553 -4.071  1.00 36.09  ? 88  GLU B CA  1 
ATOM   4795 C C   . GLU B 1 88  ? -16.357 39.974 -3.618  1.00 37.41  ? 88  GLU B C   1 
ATOM   4796 O O   . GLU B 1 88  ? -16.136 40.358 -2.464  1.00 32.32  ? 88  GLU B O   1 
ATOM   4797 C CB  . GLU B 1 88  ? -17.287 37.695 -4.125  1.00 37.32  ? 88  GLU B CB  1 
ATOM   4798 C CG  . GLU B 1 88  ? -17.047 36.275 -4.619  1.00 40.56  ? 88  GLU B CG  1 
ATOM   4799 C CD  . GLU B 1 88  ? -18.074 35.278 -4.097  1.00 47.47  ? 88  GLU B CD  1 
ATOM   4800 O OE1 . GLU B 1 88  ? -18.717 35.561 -3.058  1.00 46.33  ? 88  GLU B OE1 1 
ATOM   4801 O OE2 . GLU B 1 88  ? -18.235 34.206 -4.728  1.00 47.89  ? 88  GLU B OE2 1 
ATOM   4802 N N   . LYS B 1 89  ? -16.905 40.764 -4.545  1.00 40.29  ? 89  LYS B N   1 
ATOM   4803 C CA  . LYS B 1 89  ? -17.280 42.133 -4.203  1.00 47.26  ? 89  LYS B CA  1 
ATOM   4804 C C   . LYS B 1 89  ? -18.355 42.168 -3.118  1.00 47.16  ? 89  LYS B C   1 
ATOM   4805 O O   . LYS B 1 89  ? -18.358 43.076 -2.278  1.00 43.22  ? 89  LYS B O   1 
ATOM   4806 C CB  . LYS B 1 89  ? -17.747 42.880 -5.459  1.00 51.11  ? 89  LYS B CB  1 
ATOM   4807 C CG  . LYS B 1 89  ? -18.515 44.170 -5.187  1.00 54.84  ? 89  LYS B CG  1 
ATOM   4808 C CD  . LYS B 1 89  ? -17.588 45.301 -4.748  1.00 60.12  ? 89  LYS B CD  1 
ATOM   4809 C CE  . LYS B 1 89  ? -18.310 46.295 -3.845  1.00 63.21  ? 89  LYS B CE  1 
ATOM   4810 N NZ  . LYS B 1 89  ? -17.378 47.019 -2.931  1.00 62.90  ? 89  LYS B NZ  1 
ATOM   4811 N N   . GLU B 1 90  ? -19.266 41.188 -3.110  1.00 45.26  ? 90  GLU B N   1 
ATOM   4812 C CA  . GLU B 1 90  ? -20.291 41.140 -2.070  1.00 40.28  ? 90  GLU B CA  1 
ATOM   4813 C C   . GLU B 1 90  ? -19.670 41.002 -0.686  1.00 35.35  ? 90  GLU B C   1 
ATOM   4814 O O   . GLU B 1 90  ? -20.184 41.564 0.289   1.00 32.71  ? 90  GLU B O   1 
ATOM   4815 C CB  . GLU B 1 90  ? -21.256 39.979 -2.344  1.00 38.38  ? 90  GLU B CB  1 
ATOM   4816 C CG  . GLU B 1 90  ? -22.644 40.154 -1.762  1.00 44.29  ? 90  GLU B CG  1 
ATOM   4817 C CD  . GLU B 1 90  ? -22.716 39.746 -0.308  1.00 56.87  ? 90  GLU B CD  1 
ATOM   4818 O OE1 . GLU B 1 90  ? -21.780 39.059 0.160   1.00 61.19  ? 90  GLU B OE1 1 
ATOM   4819 O OE2 . GLU B 1 90  ? -23.706 40.109 0.367   1.00 63.77  ? 90  GLU B OE2 1 
ATOM   4820 N N   . GLU B 1 91  ? -18.550 40.281 -0.592  1.00 28.59  ? 91  GLU B N   1 
ATOM   4821 C CA  . GLU B 1 91  ? -17.921 39.993 0.689   1.00 34.99  ? 91  GLU B CA  1 
ATOM   4822 C C   . GLU B 1 91  ? -17.108 41.172 1.210   1.00 37.05  ? 91  GLU B C   1 
ATOM   4823 O O   . GLU B 1 91  ? -17.077 41.407 2.423   1.00 36.13  ? 91  GLU B O   1 
ATOM   4824 C CB  . GLU B 1 91  ? -17.037 38.760 0.560   1.00 37.74  ? 91  GLU B CB  1 
ATOM   4825 C CG  . GLU B 1 91  ? -17.784 37.519 0.146   1.00 41.49  ? 91  GLU B CG  1 
ATOM   4826 C CD  . GLU B 1 91  ? -16.841 36.386 -0.168  1.00 45.30  ? 91  GLU B CD  1 
ATOM   4827 O OE1 . GLU B 1 91  ? -16.805 35.408 0.611   1.00 48.44  ? 91  GLU B OE1 1 
ATOM   4828 O OE2 . GLU B 1 91  ? -16.127 36.479 -1.186  1.00 43.31  ? 91  GLU B OE2 1 
ATOM   4829 N N   . VAL B 1 92  ? -16.428 41.911 0.324   1.00 35.84  ? 92  VAL B N   1 
ATOM   4830 C CA  . VAL B 1 92  ? -15.781 43.148 0.761   1.00 38.00  ? 92  VAL B CA  1 
ATOM   4831 C C   . VAL B 1 92  ? -16.832 44.140 1.253   1.00 43.18  ? 92  VAL B C   1 
ATOM   4832 O O   . VAL B 1 92  ? -16.566 44.948 2.155   1.00 37.47  ? 92  VAL B O   1 
ATOM   4833 C CB  . VAL B 1 92  ? -14.904 43.750 -0.366  1.00 34.04  ? 92  VAL B CB  1 
ATOM   4834 C CG1 . VAL B 1 92  ? -14.091 42.669 -1.079  1.00 28.22  ? 92  VAL B CG1 1 
ATOM   4835 C CG2 . VAL B 1 92  ? -15.745 44.515 -1.365  1.00 41.30  ? 92  VAL B CG2 1 
ATOM   4836 N N   . GLU B 1 93  ? -18.043 44.078 0.688   1.00 47.26  ? 93  GLU B N   1 
ATOM   4837 C CA  . GLU B 1 93  ? -19.151 44.907 1.153   1.00 48.82  ? 93  GLU B CA  1 
ATOM   4838 C C   . GLU B 1 93  ? -19.586 44.496 2.556   1.00 42.45  ? 93  GLU B C   1 
ATOM   4839 O O   . GLU B 1 93  ? -19.760 45.346 3.439   1.00 43.89  ? 93  GLU B O   1 
ATOM   4840 C CB  . GLU B 1 93  ? -20.317 44.802 0.165   1.00 53.53  ? 93  GLU B CB  1 
ATOM   4841 C CG  . GLU B 1 93  ? -21.435 45.812 0.373   1.00 64.14  ? 93  GLU B CG  1 
ATOM   4842 C CD  . GLU B 1 93  ? -22.715 45.434 -0.366  1.00 71.52  ? 93  GLU B CD  1 
ATOM   4843 O OE1 . GLU B 1 93  ? -23.757 45.245 0.300   1.00 71.59  ? 93  GLU B OE1 1 
ATOM   4844 O OE2 . GLU B 1 93  ? -22.676 45.325 -1.613  1.00 73.14  ? 93  GLU B OE2 1 
ATOM   4845 N N   . LYS B 1 94  ? -19.763 43.190 2.777   1.00 35.95  ? 94  LYS B N   1 
ATOM   4846 C CA  . LYS B 1 94  ? -20.139 42.690 4.097   1.00 34.66  ? 94  LYS B CA  1 
ATOM   4847 C C   . LYS B 1 94  ? -19.118 43.083 5.157   1.00 30.90  ? 94  LYS B C   1 
ATOM   4848 O O   . LYS B 1 94  ? -19.486 43.462 6.275   1.00 30.82  ? 94  LYS B O   1 
ATOM   4849 C CB  . LYS B 1 94  ? -20.283 41.168 4.056   1.00 44.83  ? 94  LYS B CB  1 
ATOM   4850 C CG  . LYS B 1 94  ? -21.595 40.665 3.496   1.00 53.38  ? 94  LYS B CG  1 
ATOM   4851 C CD  . LYS B 1 94  ? -21.785 39.187 3.817   1.00 58.35  ? 94  LYS B CD  1 
ATOM   4852 C CE  . LYS B 1 94  ? -23.077 38.669 3.215   1.00 60.99  ? 94  LYS B CE  1 
ATOM   4853 N NZ  . LYS B 1 94  ? -23.943 39.791 2.755   1.00 64.75  ? 94  LYS B NZ  1 
ATOM   4854 N N   . LEU B 1 95  ? -17.825 42.971 4.831   1.00 35.51  ? 95  LEU B N   1 
ATOM   4855 C CA  . LEU B 1 95  ? -16.778 43.303 5.793   1.00 33.16  ? 95  LEU B CA  1 
ATOM   4856 C C   . LEU B 1 95  ? -16.836 44.773 6.189   1.00 31.57  ? 95  LEU B C   1 
ATOM   4857 O O   . LEU B 1 95  ? -16.746 45.111 7.375   1.00 27.77  ? 95  LEU B O   1 
ATOM   4858 C CB  . LEU B 1 95  ? -15.408 42.968 5.205   1.00 38.25  ? 95  LEU B CB  1 
ATOM   4859 C CG  . LEU B 1 95  ? -14.266 42.705 6.187   1.00 40.91  ? 95  LEU B CG  1 
ATOM   4860 C CD1 . LEU B 1 95  ? -14.343 41.268 6.682   1.00 42.22  ? 95  LEU B CD1 1 
ATOM   4861 C CD2 . LEU B 1 95  ? -12.918 42.982 5.527   1.00 38.22  ? 95  LEU B CD2 1 
ATOM   4862 N N   . ILE B 1 96  ? -16.994 45.662 5.209   1.00 32.51  ? 96  ILE B N   1 
ATOM   4863 C CA  . ILE B 1 96  ? -17.014 47.092 5.499   1.00 31.78  ? 96  ILE B CA  1 
ATOM   4864 C C   . ILE B 1 96  ? -18.238 47.455 6.338   1.00 34.60  ? 96  ILE B C   1 
ATOM   4865 O O   . ILE B 1 96  ? -18.124 48.161 7.347   1.00 33.96  ? 96  ILE B O   1 
ATOM   4866 C CB  . ILE B 1 96  ? -16.938 47.894 4.187   1.00 34.56  ? 96  ILE B CB  1 
ATOM   4867 C CG1 . ILE B 1 96  ? -15.537 47.737 3.583   1.00 33.93  ? 96  ILE B CG1 1 
ATOM   4868 C CG2 . ILE B 1 96  ? -17.246 49.371 4.424   1.00 40.77  ? 96  ILE B CG2 1 
ATOM   4869 C CD1 . ILE B 1 96  ? -15.373 48.297 2.187   1.00 37.68  ? 96  ILE B CD1 1 
ATOM   4870 N N   . GLU B 1 97  ? -19.418 46.943 5.961   1.00 34.00  ? 97  GLU B N   1 
ATOM   4871 C CA  . GLU B 1 97  ? -20.643 47.252 6.704   1.00 33.98  ? 97  GLU B CA  1 
ATOM   4872 C C   . GLU B 1 97  ? -20.569 46.755 8.139   1.00 30.78  ? 97  GLU B C   1 
ATOM   4873 O O   . GLU B 1 97  ? -21.082 47.404 9.060   1.00 30.46  ? 97  GLU B O   1 
ATOM   4874 C CB  . GLU B 1 97  ? -21.854 46.621 6.024   1.00 40.93  ? 97  GLU B CB  1 
ATOM   4875 C CG  . GLU B 1 97  ? -22.340 47.325 4.787   1.00 55.90  ? 97  GLU B CG  1 
ATOM   4876 C CD  . GLU B 1 97  ? -23.446 46.545 4.103   1.00 66.29  ? 97  GLU B CD  1 
ATOM   4877 O OE1 . GLU B 1 97  ? -23.237 46.083 2.961   1.00 69.49  ? 97  GLU B OE1 1 
ATOM   4878 O OE2 . GLU B 1 97  ? -24.522 46.381 4.717   1.00 69.91  ? 97  GLU B OE2 1 
ATOM   4879 N N   . PHE B 1 98  ? -19.978 45.578 8.343   1.00 26.74  ? 98  PHE B N   1 
ATOM   4880 C CA  . PHE B 1 98  ? -19.852 45.059 9.698   1.00 26.92  ? 98  PHE B CA  1 
ATOM   4881 C C   . PHE B 1 98  ? -18.927 45.941 10.523  1.00 29.11  ? 98  PHE B C   1 
ATOM   4882 O O   . PHE B 1 98  ? -19.206 46.224 11.697  1.00 32.46  ? 98  PHE B O   1 
ATOM   4883 C CB  . PHE B 1 98  ? -19.346 43.618 9.656   1.00 23.11  ? 98  PHE B CB  1 
ATOM   4884 C CG  . PHE B 1 98  ? -19.399 42.917 10.975  1.00 22.41  ? 98  PHE B CG  1 
ATOM   4885 C CD1 . PHE B 1 98  ? -20.570 42.312 11.409  1.00 29.86  ? 98  PHE B CD1 1 
ATOM   4886 C CD2 . PHE B 1 98  ? -18.277 42.842 11.776  1.00 30.66  ? 98  PHE B CD2 1 
ATOM   4887 C CE1 . PHE B 1 98  ? -20.622 41.662 12.624  1.00 28.45  ? 98  PHE B CE1 1 
ATOM   4888 C CE2 . PHE B 1 98  ? -18.317 42.181 12.995  1.00 33.30  ? 98  PHE B CE2 1 
ATOM   4889 C CZ  . PHE B 1 98  ? -19.487 41.593 13.419  1.00 29.12  ? 98  PHE B CZ  1 
ATOM   4890 N N   . THR B 1 99  ? -17.818 46.389 9.917   1.00 26.98  ? 99  THR B N   1 
ATOM   4891 C CA  . THR B 1 99  ? -16.945 47.349 10.584  1.00 31.19  ? 99  THR B CA  1 
ATOM   4892 C C   . THR B 1 99  ? -17.699 48.632 10.916  1.00 33.52  ? 99  THR B C   1 
ATOM   4893 O O   . THR B 1 99  ? -17.580 49.160 12.029  1.00 32.70  ? 99  THR B O   1 
ATOM   4894 C CB  . THR B 1 99  ? -15.719 47.653 9.713   1.00 33.47  ? 99  THR B CB  1 
ATOM   4895 O OG1 . THR B 1 99  ? -15.067 46.431 9.330   1.00 33.66  ? 99  THR B OG1 1 
ATOM   4896 C CG2 . THR B 1 99  ? -14.731 48.525 10.475  1.00 29.49  ? 99  THR B CG2 1 
ATOM   4897 N N   . LYS B 1 100 ? -18.497 49.138 9.966   1.00 35.76  ? 100 LYS B N   1 
ATOM   4898 C CA  . LYS B 1 100 ? -19.271 50.354 10.207  1.00 35.23  ? 100 LYS B CA  1 
ATOM   4899 C C   . LYS B 1 100 ? -20.263 50.166 11.350  1.00 32.50  ? 100 LYS B C   1 
ATOM   4900 O O   . LYS B 1 100 ? -20.447 51.070 12.176  1.00 32.63  ? 100 LYS B O   1 
ATOM   4901 C CB  . LYS B 1 100 ? -20.005 50.778 8.931   1.00 37.12  ? 100 LYS B CB  1 
ATOM   4902 C CG  . LYS B 1 100 ? -19.106 51.002 7.731   1.00 42.21  ? 100 LYS B CG  1 
ATOM   4903 C CD  . LYS B 1 100 ? -19.377 52.316 7.027   1.00 52.47  ? 100 LYS B CD  1 
ATOM   4904 C CE  . LYS B 1 100 ? -18.317 52.571 5.968   1.00 56.07  ? 100 LYS B CE  1 
ATOM   4905 N NZ  . LYS B 1 100 ? -17.656 53.890 6.149   1.00 59.91  ? 100 LYS B NZ  1 
ATOM   4906 N N   . LEU B 1 101 ? -20.915 49.001 11.420  1.00 28.46  ? 101 LEU B N   1 
ATOM   4907 C CA  . LEU B 1 101 ? -21.912 48.792 12.468  1.00 35.06  ? 101 LEU B CA  1 
ATOM   4908 C C   . LEU B 1 101 ? -21.275 48.833 13.852  1.00 34.98  ? 101 LEU B C   1 
ATOM   4909 O O   . LEU B 1 101 ? -21.885 49.320 14.813  1.00 36.45  ? 101 LEU B O   1 
ATOM   4910 C CB  . LEU B 1 101 ? -22.646 47.469 12.247  1.00 37.93  ? 101 LEU B CB  1 
ATOM   4911 C CG  . LEU B 1 101 ? -23.637 47.046 13.343  1.00 41.45  ? 101 LEU B CG  1 
ATOM   4912 C CD1 . LEU B 1 101 ? -24.890 47.908 13.318  1.00 39.83  ? 101 LEU B CD1 1 
ATOM   4913 C CD2 . LEU B 1 101 ? -23.989 45.563 13.231  1.00 37.34  ? 101 LEU B CD2 1 
ATOM   4914 N N   . ASN B 1 102 ? -20.040 48.352 13.972  1.00 32.08  ? 102 ASN B N   1 
ATOM   4915 C CA  . ASN B 1 102 ? -19.370 48.255 15.262  1.00 29.51  ? 102 ASN B CA  1 
ATOM   4916 C C   . ASN B 1 102 ? -18.368 49.380 15.499  1.00 29.48  ? 102 ASN B C   1 
ATOM   4917 O O   . ASN B 1 102 ? -17.684 49.376 16.529  1.00 31.95  ? 102 ASN B O   1 
ATOM   4918 C CB  . ASN B 1 102 ? -18.666 46.899 15.388  1.00 32.17  ? 102 ASN B CB  1 
ATOM   4919 C CG  . ASN B 1 102 ? -19.632 45.711 15.366  1.00 31.07  ? 102 ASN B CG  1 
ATOM   4920 O OD1 . ASN B 1 102 ? -20.449 45.547 16.261  1.00 31.86  ? 102 ASN B OD1 1 
ATOM   4921 N ND2 . ASN B 1 102 ? -19.511 44.864 14.349  1.00 33.48  ? 102 ASN B ND2 1 
ATOM   4922 N N   . TYR B 1 103 ? -18.299 50.356 14.591  1.00 31.48  ? 103 TYR B N   1 
ATOM   4923 C CA  . TYR B 1 103 ? -17.156 51.270 14.524  1.00 35.14  ? 103 TYR B CA  1 
ATOM   4924 C C   . TYR B 1 103 ? -16.958 52.055 15.819  1.00 32.23  ? 103 TYR B C   1 
ATOM   4925 O O   . TYR B 1 103 ? -15.818 52.271 16.250  1.00 33.01  ? 103 TYR B O   1 
ATOM   4926 C CB  . TYR B 1 103 ? -17.336 52.225 13.338  1.00 39.90  ? 103 TYR B CB  1 
ATOM   4927 C CG  . TYR B 1 103 ? -16.207 53.206 13.116  1.00 40.13  ? 103 TYR B CG  1 
ATOM   4928 C CD1 . TYR B 1 103 ? -15.074 52.841 12.400  1.00 38.96  ? 103 TYR B CD1 1 
ATOM   4929 C CD2 . TYR B 1 103 ? -16.282 54.507 13.608  1.00 36.40  ? 103 TYR B CD2 1 
ATOM   4930 C CE1 . TYR B 1 103 ? -14.048 53.736 12.182  1.00 40.68  ? 103 TYR B CE1 1 
ATOM   4931 C CE2 . TYR B 1 103 ? -15.255 55.409 13.402  1.00 39.49  ? 103 TYR B CE2 1 
ATOM   4932 C CZ  . TYR B 1 103 ? -14.141 55.020 12.682  1.00 45.37  ? 103 TYR B CZ  1 
ATOM   4933 O OH  . TYR B 1 103 ? -13.114 55.916 12.471  1.00 51.15  ? 103 TYR B OH  1 
ATOM   4934 N N   . GLU B 1 104 ? -18.044 52.491 16.452  1.00 33.15  ? 104 GLU B N   1 
ATOM   4935 C CA  . GLU B 1 104 ? -17.945 53.376 17.607  1.00 37.96  ? 104 GLU B CA  1 
ATOM   4936 C C   . GLU B 1 104 ? -17.840 52.631 18.931  1.00 34.28  ? 104 GLU B C   1 
ATOM   4937 O O   . GLU B 1 104 ? -17.741 53.277 19.977  1.00 39.11  ? 104 GLU B O   1 
ATOM   4938 C CB  . GLU B 1 104 ? -19.147 54.330 17.652  1.00 44.90  ? 104 GLU B CB  1 
ATOM   4939 C CG  . GLU B 1 104 ? -19.257 55.275 16.455  1.00 52.96  ? 104 GLU B CG  1 
ATOM   4940 C CD  . GLU B 1 104 ? -18.171 56.343 16.432  1.00 60.72  ? 104 GLU B CD  1 
ATOM   4941 O OE1 . GLU B 1 104 ? -17.540 56.584 17.483  1.00 62.23  ? 104 GLU B OE1 1 
ATOM   4942 O OE2 . GLU B 1 104 ? -17.949 56.945 15.357  1.00 62.40  ? 104 GLU B OE2 1 
ATOM   4943 N N   . LYS B 1 105 ? -17.851 51.304 18.919  1.00 31.94  ? 105 LYS B N   1 
ATOM   4944 C CA  . LYS B 1 105 ? -17.776 50.559 20.166  1.00 30.27  ? 105 LYS B CA  1 
ATOM   4945 C C   . LYS B 1 105 ? -16.370 50.656 20.751  1.00 34.35  ? 105 LYS B C   1 
ATOM   4946 O O   . LYS B 1 105 ? -15.383 50.683 20.003  1.00 32.21  ? 105 LYS B O   1 
ATOM   4947 C CB  . LYS B 1 105 ? -18.147 49.094 19.948  1.00 28.72  ? 105 LYS B CB  1 
ATOM   4948 C CG  . LYS B 1 105 ? -19.647 48.849 19.872  1.00 31.89  ? 105 LYS B CG  1 
ATOM   4949 C CD  . LYS B 1 105 ? -19.960 47.565 19.130  1.00 30.80  ? 105 LYS B CD  1 
ATOM   4950 C CE  . LYS B 1 105 ? -21.451 47.435 18.856  1.00 26.31  ? 105 LYS B CE  1 
ATOM   4951 N NZ  . LYS B 1 105 ? -21.770 46.093 18.261  1.00 27.59  ? 105 LYS B NZ  1 
ATOM   4952 N N   . PRO B 1 106 ? -16.245 50.710 22.081  1.00 31.56  ? 106 PRO B N   1 
ATOM   4953 C CA  . PRO B 1 106 ? -14.904 50.739 22.693  1.00 30.97  ? 106 PRO B CA  1 
ATOM   4954 C C   . PRO B 1 106 ? -14.012 49.580 22.275  1.00 30.88  ? 106 PRO B C   1 
ATOM   4955 O O   . PRO B 1 106 ? -12.799 49.769 22.130  1.00 34.57  ? 106 PRO B O   1 
ATOM   4956 C CB  . PRO B 1 106 ? -15.216 50.704 24.197  1.00 35.81  ? 106 PRO B CB  1 
ATOM   4957 C CG  . PRO B 1 106 ? -16.594 51.303 24.310  1.00 32.11  ? 106 PRO B CG  1 
ATOM   4958 C CD  . PRO B 1 106 ? -17.323 50.882 23.075  1.00 30.39  ? 106 PRO B CD  1 
ATOM   4959 N N   . ILE B 1 107 ? -14.572 48.385 22.060  1.00 28.25  ? 107 ILE B N   1 
ATOM   4960 C CA  . ILE B 1 107 ? -13.746 47.243 21.678  1.00 29.47  ? 107 ILE B CA  1 
ATOM   4961 C C   . ILE B 1 107 ? -13.199 47.364 20.265  1.00 30.57  ? 107 ILE B C   1 
ATOM   4962 O O   . ILE B 1 107 ? -12.290 46.611 19.895  1.00 25.00  ? 107 ILE B O   1 
ATOM   4963 C CB  . ILE B 1 107 ? -14.517 45.910 21.814  1.00 32.59  ? 107 ILE B CB  1 
ATOM   4964 C CG1 . ILE B 1 107 ? -15.665 45.839 20.804  1.00 29.00  ? 107 ILE B CG1 1 
ATOM   4965 C CG2 . ILE B 1 107 ? -15.012 45.722 23.252  1.00 29.92  ? 107 ILE B CG2 1 
ATOM   4966 C CD1 . ILE B 1 107 ? -16.297 44.456 20.690  1.00 28.40  ? 107 ILE B CD1 1 
ATOM   4967 N N   . TYR B 1 108 ? -13.719 48.302 19.469  1.00 36.59  ? 108 TYR B N   1 
ATOM   4968 C CA  . TYR B 1 108 ? -13.240 48.545 18.116  1.00 29.69  ? 108 TYR B CA  1 
ATOM   4969 C C   . TYR B 1 108 ? -12.269 49.721 18.036  1.00 35.45  ? 108 TYR B C   1 
ATOM   4970 O O   . TYR B 1 108 ? -11.997 50.218 16.936  1.00 32.28  ? 108 TYR B O   1 
ATOM   4971 C CB  . TYR B 1 108 ? -14.427 48.763 17.176  1.00 31.10  ? 108 TYR B CB  1 
ATOM   4972 C CG  . TYR B 1 108 ? -14.864 47.474 16.523  1.00 29.91  ? 108 TYR B CG  1 
ATOM   4973 C CD1 . TYR B 1 108 ? -15.492 46.480 17.262  1.00 24.39  ? 108 TYR B CD1 1 
ATOM   4974 C CD2 . TYR B 1 108 ? -14.604 47.230 15.181  1.00 33.38  ? 108 TYR B CD2 1 
ATOM   4975 C CE1 . TYR B 1 108 ? -15.871 45.278 16.670  1.00 25.20  ? 108 TYR B CE1 1 
ATOM   4976 C CE2 . TYR B 1 108 ? -14.972 46.040 14.583  1.00 31.38  ? 108 TYR B CE2 1 
ATOM   4977 C CZ  . TYR B 1 108 ? -15.606 45.069 15.327  1.00 28.80  ? 108 TYR B CZ  1 
ATOM   4978 O OH  . TYR B 1 108 ? -15.974 43.889 14.723  1.00 29.36  ? 108 TYR B OH  1 
ATOM   4979 N N   . ARG B 1 109 ? -11.717 50.157 19.172  1.00 35.29  ? 109 ARG B N   1 
ATOM   4980 C CA  . ARG B 1 109 ? -10.894 51.367 19.221  1.00 41.03  ? 109 ARG B CA  1 
ATOM   4981 C C   . ARG B 1 109 ? -9.452  51.038 18.828  1.00 37.92  ? 109 ARG B C   1 
ATOM   4982 O O   . ARG B 1 109 ? -8.539  50.961 19.652  1.00 40.44  ? 109 ARG B O   1 
ATOM   4983 C CB  . ARG B 1 109 ? -10.963 52.001 20.602  1.00 45.96  ? 109 ARG B CB  1 
ATOM   4984 C CG  . ARG B 1 109 ? -10.901 53.510 20.581  1.00 55.62  ? 109 ARG B CG  1 
ATOM   4985 C CD  . ARG B 1 109 ? -11.738 54.098 21.698  1.00 59.59  ? 109 ARG B CD  1 
ATOM   4986 N NE  . ARG B 1 109 ? -11.202 53.747 23.009  1.00 59.91  ? 109 ARG B NE  1 
ATOM   4987 C CZ  . ARG B 1 109 ? -11.893 53.814 24.141  1.00 62.45  ? 109 ARG B CZ  1 
ATOM   4988 N NH1 . ARG B 1 109 ? -13.159 54.218 24.131  1.00 61.24  ? 109 ARG B NH1 1 
ATOM   4989 N NH2 . ARG B 1 109 ? -11.314 53.474 25.286  1.00 65.54  ? 109 ARG B NH2 1 
ATOM   4990 N N   . PHE B 1 110 ? -9.261  50.836 17.528  1.00 35.76  ? 110 PHE B N   1 
ATOM   4991 C CA  . PHE B 1 110 ? -7.946  50.635 16.935  1.00 32.78  ? 110 PHE B CA  1 
ATOM   4992 C C   . PHE B 1 110 ? -7.700  51.768 15.954  1.00 33.48  ? 110 PHE B C   1 
ATOM   4993 O O   . PHE B 1 110 ? -8.526  52.009 15.070  1.00 34.34  ? 110 PHE B O   1 
ATOM   4994 C CB  . PHE B 1 110 ? -7.841  49.296 16.196  1.00 30.51  ? 110 PHE B CB  1 
ATOM   4995 C CG  . PHE B 1 110 ? -7.977  48.086 17.075  1.00 34.67  ? 110 PHE B CG  1 
ATOM   4996 C CD1 . PHE B 1 110 ? -6.869  47.535 17.695  1.00 35.21  ? 110 PHE B CD1 1 
ATOM   4997 C CD2 . PHE B 1 110 ? -9.206  47.471 17.241  1.00 41.69  ? 110 PHE B CD2 1 
ATOM   4998 C CE1 . PHE B 1 110 ? -6.982  46.408 18.485  1.00 34.01  ? 110 PHE B CE1 1 
ATOM   4999 C CE2 . PHE B 1 110 ? -9.328  46.342 18.036  1.00 41.77  ? 110 PHE B CE2 1 
ATOM   5000 C CZ  . PHE B 1 110 ? -8.214  45.812 18.658  1.00 39.26  ? 110 PHE B CZ  1 
ATOM   5001 N N   . GLU B 1 111 ? -6.569  52.456 16.105  1.00 34.51  ? 111 GLU B N   1 
ATOM   5002 C CA  . GLU B 1 111 ? -6.280  53.573 15.212  1.00 36.59  ? 111 GLU B CA  1 
ATOM   5003 C C   . GLU B 1 111 ? -6.253  53.132 13.751  1.00 32.69  ? 111 GLU B C   1 
ATOM   5004 O O   . GLU B 1 111 ? -6.606  53.909 12.858  1.00 35.81  ? 111 GLU B O   1 
ATOM   5005 C CB  . GLU B 1 111 ? -4.958  54.226 15.610  1.00 42.82  ? 111 GLU B CB  1 
ATOM   5006 C CG  . GLU B 1 111 ? -4.499  55.337 14.682  1.00 50.57  ? 111 GLU B CG  1 
ATOM   5007 C CD  . GLU B 1 111 ? -3.003  55.295 14.461  1.00 63.48  ? 111 GLU B CD  1 
ATOM   5008 O OE1 . GLU B 1 111 ? -2.544  55.698 13.370  1.00 68.87  ? 111 GLU B OE1 1 
ATOM   5009 O OE2 . GLU B 1 111 ? -2.286  54.845 15.382  1.00 67.37  ? 111 GLU B OE2 1 
ATOM   5010 N N   . ARG B 1 112 ? -5.863  51.886 13.492  1.00 33.72  ? 112 ARG B N   1 
ATOM   5011 C CA  . ARG B 1 112 ? -5.798  51.409 12.115  1.00 31.47  ? 112 ARG B CA  1 
ATOM   5012 C C   . ARG B 1 112 ? -7.192  51.261 11.507  1.00 31.77  ? 112 ARG B C   1 
ATOM   5013 O O   . ARG B 1 112 ? -7.375  51.510 10.311  1.00 34.00  ? 112 ARG B O   1 
ATOM   5014 C CB  . ARG B 1 112 ? -5.027  50.092 12.062  1.00 30.99  ? 112 ARG B CB  1 
ATOM   5015 C CG  . ARG B 1 112 ? -4.925  49.475 10.680  1.00 35.62  ? 112 ARG B CG  1 
ATOM   5016 C CD  . ARG B 1 112 ? -4.200  50.374 9.706   1.00 38.74  ? 112 ARG B CD  1 
ATOM   5017 N NE  . ARG B 1 112 ? -3.643  49.589 8.608   1.00 41.50  ? 112 ARG B NE  1 
ATOM   5018 C CZ  . ARG B 1 112 ? -3.241  50.095 7.448   1.00 41.95  ? 112 ARG B CZ  1 
ATOM   5019 N NH1 . ARG B 1 112 ? -3.329  51.401 7.222   1.00 38.04  ? 112 ARG B NH1 1 
ATOM   5020 N NH2 . ARG B 1 112 ? -2.751  49.289 6.514   1.00 43.49  ? 112 ARG B NH2 1 
ATOM   5021 N N   . ILE B 1 113 ? -8.192  50.867 12.306  1.00 33.04  ? 113 ILE B N   1 
ATOM   5022 C CA  . ILE B 1 113 ? -9.560  50.817 11.785  1.00 29.88  ? 113 ILE B CA  1 
ATOM   5023 C C   . ILE B 1 113 ? -10.020 52.213 11.388  1.00 35.36  ? 113 ILE B C   1 
ATOM   5024 O O   . ILE B 1 113 ? -10.681 52.395 10.358  1.00 34.92  ? 113 ILE B O   1 
ATOM   5025 C CB  . ILE B 1 113 ? -10.513 50.168 12.807  1.00 28.73  ? 113 ILE B CB  1 
ATOM   5026 C CG1 . ILE B 1 113 ? -10.280 48.656 12.864  1.00 28.72  ? 113 ILE B CG1 1 
ATOM   5027 C CG2 . ILE B 1 113 ? -11.978 50.468 12.451  1.00 26.62  ? 113 ILE B CG2 1 
ATOM   5028 C CD1 . ILE B 1 113 ? -11.111 47.942 13.929  1.00 30.94  ? 113 ILE B CD1 1 
ATOM   5029 N N   . ARG B 1 114 ? -9.655  53.223 12.187  1.00 38.67  ? 114 ARG B N   1 
ATOM   5030 C CA  . ARG B 1 114 ? -9.955  54.605 11.825  1.00 39.77  ? 114 ARG B CA  1 
ATOM   5031 C C   . ARG B 1 114 ? -9.330  54.958 10.483  1.00 39.17  ? 114 ARG B C   1 
ATOM   5032 O O   . ARG B 1 114 ? -9.963  55.620 9.652   1.00 35.33  ? 114 ARG B O   1 
ATOM   5033 C CB  . ARG B 1 114 ? -9.450  55.561 12.908  1.00 49.19  ? 114 ARG B CB  1 
ATOM   5034 C CG  . ARG B 1 114 ? -9.310  54.930 14.286  1.00 60.34  ? 114 ARG B CG  1 
ATOM   5035 C CD  . ARG B 1 114 ? -9.454  55.943 15.412  1.00 68.84  ? 114 ARG B CD  1 
ATOM   5036 N NE  . ARG B 1 114 ? -10.858 56.240 15.675  1.00 73.28  ? 114 ARG B NE  1 
ATOM   5037 C CZ  . ARG B 1 114 ? -11.667 55.469 16.395  1.00 70.31  ? 114 ARG B CZ  1 
ATOM   5038 N NH1 . ARG B 1 114 ? -11.211 54.346 16.939  1.00 64.56  ? 114 ARG B NH1 1 
ATOM   5039 N NH2 . ARG B 1 114 ? -12.934 55.821 16.570  1.00 70.33  ? 114 ARG B NH2 1 
ATOM   5040 N N   . GLU B 1 115 ? -8.084  54.525 10.257  1.00 39.25  ? 115 GLU B N   1 
ATOM   5041 C CA  . GLU B 1 115 ? -7.423  54.768 8.978   1.00 39.15  ? 115 GLU B CA  1 
ATOM   5042 C C   . GLU B 1 115 ? -8.169  54.085 7.842   1.00 37.28  ? 115 GLU B C   1 
ATOM   5043 O O   . GLU B 1 115 ? -8.397  54.682 6.786   1.00 37.30  ? 115 GLU B O   1 
ATOM   5044 C CB  . GLU B 1 115 ? -5.973  54.272 9.021   1.00 40.18  ? 115 GLU B CB  1 
ATOM   5045 C CG  . GLU B 1 115 ? -5.041  55.033 9.953   1.00 44.04  ? 115 GLU B CG  1 
ATOM   5046 C CD  . GLU B 1 115 ? -3.600  54.503 9.917   1.00 48.73  ? 115 GLU B CD  1 
ATOM   5047 O OE1 . GLU B 1 115 ? -2.825  54.827 10.838  1.00 49.62  ? 115 GLU B OE1 1 
ATOM   5048 O OE2 . GLU B 1 115 ? -3.236  53.770 8.971   1.00 48.92  ? 115 GLU B OE2 1 
ATOM   5049 N N   . LEU B 1 116 ? -8.559  52.823 8.045   1.00 38.02  ? 116 LEU B N   1 
ATOM   5050 C CA  . LEU B 1 116 ? -9.110  52.031 6.951   1.00 35.78  ? 116 LEU B CA  1 
ATOM   5051 C C   . LEU B 1 116 ? -10.472 52.551 6.520   1.00 33.55  ? 116 LEU B C   1 
ATOM   5052 O O   . LEU B 1 116 ? -10.784 52.561 5.325   1.00 34.56  ? 116 LEU B O   1 
ATOM   5053 C CB  . LEU B 1 116 ? -9.206  50.563 7.360   1.00 34.74  ? 116 LEU B CB  1 
ATOM   5054 C CG  . LEU B 1 116 ? -7.859  49.910 7.673   1.00 34.57  ? 116 LEU B CG  1 
ATOM   5055 C CD1 . LEU B 1 116 ? -8.029  48.508 8.229   1.00 35.32  ? 116 LEU B CD1 1 
ATOM   5056 C CD2 . LEU B 1 116 ? -7.001  49.910 6.436   1.00 35.44  ? 116 LEU B CD2 1 
ATOM   5057 N N   . MET B 1 117 ? -11.292 52.986 7.476   1.00 37.00  ? 117 MET B N   1 
ATOM   5058 C CA  . MET B 1 117 ? -12.637 53.457 7.167   1.00 40.55  ? 117 MET B CA  1 
ATOM   5059 C C   . MET B 1 117 ? -12.637 54.831 6.509   1.00 48.63  ? 117 MET B C   1 
ATOM   5060 O O   . MET B 1 117 ? -13.626 55.192 5.864   1.00 51.82  ? 117 MET B O   1 
ATOM   5061 C CB  . MET B 1 117 ? -13.488 53.478 8.440   1.00 35.01  ? 117 MET B CB  1 
ATOM   5062 C CG  . MET B 1 117 ? -13.795 52.094 8.984   1.00 35.97  ? 117 MET B CG  1 
ATOM   5063 S SD  . MET B 1 117 ? -14.935 51.138 7.961   1.00 48.09  ? 117 MET B SD  1 
ATOM   5064 C CE  . MET B 1 117 ? -13.840 49.937 7.226   1.00 46.43  ? 117 MET B CE  1 
ATOM   5065 N N   . ASN B 1 118 ? -11.556 55.596 6.648   1.00 52.55  ? 118 ASN B N   1 
ATOM   5066 C CA  . ASN B 1 118 ? -11.424 56.887 5.988   1.00 58.01  ? 118 ASN B CA  1 
ATOM   5067 C C   . ASN B 1 118 ? -10.839 56.775 4.587   1.00 55.25  ? 118 ASN B C   1 
ATOM   5068 O O   . ASN B 1 118 ? -10.514 57.800 3.982   1.00 54.02  ? 118 ASN B O   1 
ATOM   5069 C CB  . ASN B 1 118 ? -10.561 57.831 6.828   1.00 63.36  ? 118 ASN B CB  1 
ATOM   5070 C CG  . ASN B 1 118 ? -11.349 58.531 7.913   1.00 67.74  ? 118 ASN B CG  1 
ATOM   5071 O OD1 . ASN B 1 118 ? -12.572 58.664 7.824   1.00 69.94  ? 118 ASN B OD1 1 
ATOM   5072 N ND2 . ASN B 1 118 ? -10.650 58.987 8.948   1.00 67.27  ? 118 ASN B ND2 1 
ATOM   5073 N N   . LYS B 1 119 ? -10.694 55.563 4.063   1.00 55.53  ? 119 LYS B N   1 
ATOM   5074 C CA  . LYS B 1 119 ? -10.159 55.343 2.729   1.00 54.48  ? 119 LYS B CA  1 
ATOM   5075 C C   . LYS B 1 119 ? -11.288 55.135 1.728   1.00 54.23  ? 119 LYS B C   1 
ATOM   5076 O O   . LYS B 1 119 ? -12.337 54.574 2.052   1.00 53.62  ? 119 LYS B O   1 
ATOM   5077 C CB  . LYS B 1 119 ? -9.219  54.136 2.711   1.00 51.16  ? 119 LYS B CB  1 
ATOM   5078 C CG  . LYS B 1 119 ? -7.925  54.340 3.481   1.00 51.34  ? 119 LYS B CG  1 
ATOM   5079 C CD  . LYS B 1 119 ? -6.869  53.336 3.049   1.00 53.51  ? 119 LYS B CD  1 
ATOM   5080 C CE  . LYS B 1 119 ? -5.794  53.156 4.113   1.00 58.23  ? 119 LYS B CE  1 
ATOM   5081 N NZ  . LYS B 1 119 ? -5.089  54.429 4.451   1.00 61.30  ? 119 LYS B NZ  1 
ATOM   5082 N N   . GLU B 1 120 ? -11.061 55.602 0.500   1.00 57.20  ? 120 GLU B N   1 
ATOM   5083 C CA  . GLU B 1 120 ? -12.008 55.355 -0.581  1.00 60.44  ? 120 GLU B CA  1 
ATOM   5084 C C   . GLU B 1 120 ? -11.894 53.925 -1.103  1.00 61.87  ? 120 GLU B C   1 
ATOM   5085 O O   . GLU B 1 120 ? -12.910 53.278 -1.379  1.00 67.08  ? 120 GLU B O   1 
ATOM   5086 C CB  . GLU B 1 120 ? -11.781 56.364 -1.710  1.00 60.60  ? 120 GLU B CB  1 
ATOM   5087 C CG  . GLU B 1 120 ? -12.542 56.064 -2.991  1.00 64.31  ? 120 GLU B CG  1 
ATOM   5088 C CD  . GLU B 1 120 ? -11.931 56.743 -4.209  1.00 71.82  ? 120 GLU B CD  1 
ATOM   5089 O OE1 . GLU B 1 120 ? -11.004 57.566 -4.036  1.00 73.03  ? 120 GLU B OE1 1 
ATOM   5090 O OE2 . GLU B 1 120 ? -12.377 56.455 -5.341  1.00 73.22  ? 120 GLU B OE2 1 
ATOM   5091 N N   . LYS B 1 121 ? -10.672 53.413 -1.227  1.00 55.58  ? 121 LYS B N   1 
ATOM   5092 C CA  . LYS B 1 121 ? -10.422 52.085 -1.762  1.00 54.24  ? 121 LYS B CA  1 
ATOM   5093 C C   . LYS B 1 121 ? -9.412  51.370 -0.873  1.00 52.06  ? 121 LYS B C   1 
ATOM   5094 O O   . LYS B 1 121 ? -8.522  51.996 -0.289  1.00 48.93  ? 121 LYS B O   1 
ATOM   5095 C CB  . LYS B 1 121 ? -9.914  52.167 -3.215  1.00 57.90  ? 121 LYS B CB  1 
ATOM   5096 C CG  . LYS B 1 121 ? -9.601  50.833 -3.876  1.00 63.76  ? 121 LYS B CG  1 
ATOM   5097 C CD  . LYS B 1 121 ? -8.596  51.010 -5.009  1.00 69.10  ? 121 LYS B CD  1 
ATOM   5098 C CE  . LYS B 1 121 ? -8.305  49.691 -5.723  1.00 69.47  ? 121 LYS B CE  1 
ATOM   5099 N NZ  . LYS B 1 121 ? -7.818  48.632 -4.792  1.00 67.52  ? 121 LYS B NZ  1 
ATOM   5100 N N   . LEU B 1 122 ? -9.567  50.055 -0.756  1.00 51.24  ? 122 LEU B N   1 
ATOM   5101 C CA  . LEU B 1 122 ? -8.720  49.241 0.105   1.00 45.14  ? 122 LEU B CA  1 
ATOM   5102 C C   . LEU B 1 122 ? -8.034  48.171 -0.728  1.00 42.87  ? 122 LEU B C   1 
ATOM   5103 O O   . LEU B 1 122 ? -8.698  47.414 -1.443  1.00 37.22  ? 122 LEU B O   1 
ATOM   5104 C CB  . LEU B 1 122 ? -9.532  48.592 1.229   1.00 44.81  ? 122 LEU B CB  1 
ATOM   5105 C CG  . LEU B 1 122 ? -10.425 49.536 2.037   1.00 46.33  ? 122 LEU B CG  1 
ATOM   5106 C CD1 . LEU B 1 122 ? -11.732 48.842 2.363   1.00 47.94  ? 122 LEU B CD1 1 
ATOM   5107 C CD2 . LEU B 1 122 ? -9.730  50.016 3.302   1.00 45.67  ? 122 LEU B CD2 1 
ATOM   5108 N N   . ASN B 1 123 ? -6.710  48.106 -0.629  1.00 44.42  ? 123 ASN B N   1 
ATOM   5109 C CA  . ASN B 1 123 ? -5.951  47.072 -1.316  1.00 48.64  ? 123 ASN B CA  1 
ATOM   5110 C C   . ASN B 1 123 ? -5.951  45.798 -0.468  1.00 46.47  ? 123 ASN B C   1 
ATOM   5111 O O   . ASN B 1 123 ? -6.630  45.700 0.559   1.00 39.84  ? 123 ASN B O   1 
ATOM   5112 C CB  . ASN B 1 123 ? -4.542  47.570 -1.627  1.00 51.05  ? 123 ASN B CB  1 
ATOM   5113 C CG  . ASN B 1 123 ? -3.863  48.206 -0.425  1.00 53.71  ? 123 ASN B CG  1 
ATOM   5114 O OD1 . ASN B 1 123 ? -4.022  47.750 0.712   1.00 50.82  ? 123 ASN B OD1 1 
ATOM   5115 N ND2 . ASN B 1 123 ? -3.092  49.263 -0.674  1.00 51.79  ? 123 ASN B ND2 1 
ATOM   5116 N N   . ARG B 1 124 ? -5.173  44.800 -0.896  1.00 45.33  ? 124 ARG B N   1 
ATOM   5117 C CA  . ARG B 1 124 ? -5.139  43.526 -0.186  1.00 47.28  ? 124 ARG B CA  1 
ATOM   5118 C C   . ARG B 1 124 ? -4.567  43.671 1.222   1.00 45.73  ? 124 ARG B C   1 
ATOM   5119 O O   . ARG B 1 124 ? -5.009  42.982 2.147   1.00 44.47  ? 124 ARG B O   1 
ATOM   5120 C CB  . ARG B 1 124 ? -4.339  42.504 -0.998  1.00 46.41  ? 124 ARG B CB  1 
ATOM   5121 C CG  . ARG B 1 124 ? -4.201  41.153 -0.320  1.00 46.63  ? 124 ARG B CG  1 
ATOM   5122 C CD  . ARG B 1 124 ? -3.169  40.293 -1.007  1.00 45.82  ? 124 ARG B CD  1 
ATOM   5123 N NE  . ARG B 1 124 ? -2.860  39.102 -0.226  1.00 42.68  ? 124 ARG B NE  1 
ATOM   5124 C CZ  . ARG B 1 124 ? -1.952  39.053 0.742   1.00 37.98  ? 124 ARG B CZ  1 
ATOM   5125 N NH1 . ARG B 1 124 ? -1.253  40.136 1.066   1.00 39.23  ? 124 ARG B NH1 1 
ATOM   5126 N NH2 . ARG B 1 124 ? -1.749  37.919 1.391   1.00 35.68  ? 124 ARG B NH2 1 
ATOM   5127 N N   . GLU B 1 125 ? -3.607  44.577 1.408   1.00 47.37  ? 125 GLU B N   1 
ATOM   5128 C CA  . GLU B 1 125 ? -3.017  44.811 2.727   1.00 48.58  ? 125 GLU B CA  1 
ATOM   5129 C C   . GLU B 1 125 ? -4.028  45.371 3.692   1.00 43.39  ? 125 GLU B C   1 
ATOM   5130 O O   . GLU B 1 125 ? -4.189  44.865 4.808   1.00 39.95  ? 125 GLU B O   1 
ATOM   5131 C CB  . GLU B 1 125 ? -1.852  45.784 2.614   1.00 59.31  ? 125 GLU B CB  1 
ATOM   5132 C CG  . GLU B 1 125 ? -0.605  45.050 2.323   1.00 71.84  ? 125 GLU B CG  1 
ATOM   5133 C CD  . GLU B 1 125 ? -0.842  44.009 1.235   1.00 81.44  ? 125 GLU B CD  1 
ATOM   5134 O OE1 . GLU B 1 125 ? -0.335  42.879 1.347   1.00 83.64  ? 125 GLU B OE1 1 
ATOM   5135 O OE2 . GLU B 1 125 ? -1.542  44.331 0.244   1.00 83.80  ? 125 GLU B OE2 1 
ATOM   5136 N N   . GLU B 1 126 ? -4.663  46.462 3.289   1.00 37.47  ? 126 GLU B N   1 
ATOM   5137 C CA  . GLU B 1 126 ? -5.653  47.107 4.129   1.00 34.05  ? 126 GLU B CA  1 
ATOM   5138 C C   . GLU B 1 126 ? -6.817  46.167 4.418   1.00 30.63  ? 126 GLU B C   1 
ATOM   5139 O O   . GLU B 1 126 ? -7.340  46.134 5.541   1.00 31.67  ? 126 GLU B O   1 
ATOM   5140 C CB  . GLU B 1 126 ? -6.102  48.397 3.445   1.00 39.14  ? 126 GLU B CB  1 
ATOM   5141 C CG  . GLU B 1 126 ? -5.004  49.450 3.476   1.00 39.78  ? 126 GLU B CG  1 
ATOM   5142 C CD  . GLU B 1 126 ? -4.990  50.358 2.261   1.00 46.44  ? 126 GLU B CD  1 
ATOM   5143 O OE1 . GLU B 1 126 ? -5.897  50.258 1.404   1.00 46.54  ? 126 GLU B OE1 1 
ATOM   5144 O OE2 . GLU B 1 126 ? -4.054  51.181 2.171   1.00 50.52  ? 126 GLU B OE2 1 
ATOM   5145 N N   . LEU B 1 127 ? -7.208  45.357 3.428   1.00 27.87  ? 127 LEU B N   1 
ATOM   5146 C CA  . LEU B 1 127 ? -8.273  44.387 3.662   1.00 27.92  ? 127 LEU B CA  1 
ATOM   5147 C C   . LEU B 1 127 ? -7.846  43.320 4.661   1.00 27.75  ? 127 LEU B C   1 
ATOM   5148 O O   . LEU B 1 127 ? -8.667  42.873 5.474   1.00 31.46  ? 127 LEU B O   1 
ATOM   5149 C CB  . LEU B 1 127 ? -8.720  43.748 2.343   1.00 30.61  ? 127 LEU B CB  1 
ATOM   5150 C CG  . LEU B 1 127 ? -9.603  44.632 1.451   1.00 36.14  ? 127 LEU B CG  1 
ATOM   5151 C CD1 . LEU B 1 127 ? -9.927  43.921 0.141   1.00 35.47  ? 127 LEU B CD1 1 
ATOM   5152 C CD2 . LEU B 1 127 ? -10.887 45.065 2.172   1.00 37.15  ? 127 LEU B CD2 1 
ATOM   5153 N N   . LEU B 1 128 ? -6.568  42.924 4.640   1.00 28.08  ? 128 LEU B N   1 
ATOM   5154 C CA  . LEU B 1 128 ? -6.060  41.980 5.635   1.00 33.68  ? 128 LEU B CA  1 
ATOM   5155 C C   . LEU B 1 128 ? -6.105  42.575 7.034   1.00 31.33  ? 128 LEU B C   1 
ATOM   5156 O O   . LEU B 1 128 ? -6.442  41.879 8.003   1.00 27.76  ? 128 LEU B O   1 
ATOM   5157 C CB  . LEU B 1 128 ? -4.627  41.564 5.293   1.00 37.14  ? 128 LEU B CB  1 
ATOM   5158 C CG  . LEU B 1 128 ? -4.432  40.245 4.545   1.00 37.55  ? 128 LEU B CG  1 
ATOM   5159 C CD1 . LEU B 1 128 ? -2.938  39.994 4.276   1.00 39.92  ? 128 LEU B CD1 1 
ATOM   5160 C CD2 . LEU B 1 128 ? -5.045  39.095 5.314   1.00 37.01  ? 128 LEU B CD2 1 
ATOM   5161 N N   . ASP B 1 129 ? -5.740  43.854 7.159   1.00 32.58  ? 129 ASP B N   1 
ATOM   5162 C CA  . ASP B 1 129 ? -5.824  44.544 8.440   1.00 31.44  ? 129 ASP B CA  1 
ATOM   5163 C C   . ASP B 1 129 ? -7.269  44.691 8.893   1.00 31.84  ? 129 ASP B C   1 
ATOM   5164 O O   . ASP B 1 129 ? -7.560  44.619 10.092  1.00 32.40  ? 129 ASP B O   1 
ATOM   5165 C CB  . ASP B 1 129 ? -5.167  45.918 8.337   1.00 34.50  ? 129 ASP B CB  1 
ATOM   5166 C CG  . ASP B 1 129 ? -3.665  45.850 8.408   1.00 34.81  ? 129 ASP B CG  1 
ATOM   5167 O OD1 . ASP B 1 129 ? -3.124  44.732 8.283   1.00 35.66  ? 129 ASP B OD1 1 
ATOM   5168 O OD2 . ASP B 1 129 ? -3.028  46.913 8.590   1.00 33.59  ? 129 ASP B OD2 1 
ATOM   5169 N N   . LEU B 1 130 ? -8.186  44.894 7.949   1.00 34.41  ? 130 LEU B N   1 
ATOM   5170 C CA  . LEU B 1 130 ? -9.593  45.043 8.306   1.00 35.07  ? 130 LEU B CA  1 
ATOM   5171 C C   . LEU B 1 130 ? -10.193 43.715 8.758   1.00 37.74  ? 130 LEU B C   1 
ATOM   5172 O O   . LEU B 1 130 ? -10.934 43.667 9.751   1.00 30.20  ? 130 LEU B O   1 
ATOM   5173 C CB  . LEU B 1 130 ? -10.364 45.619 7.122   1.00 33.07  ? 130 LEU B CB  1 
ATOM   5174 C CG  . LEU B 1 130 ? -11.772 46.126 7.425   1.00 39.36  ? 130 LEU B CG  1 
ATOM   5175 C CD1 . LEU B 1 130 ? -11.725 47.258 8.450   1.00 43.41  ? 130 LEU B CD1 1 
ATOM   5176 C CD2 . LEU B 1 130 ? -12.460 46.565 6.143   1.00 40.14  ? 130 LEU B CD2 1 
ATOM   5177 N N   . GLN B 1 131 ? -9.871  42.626 8.050   1.00 34.32  ? 131 GLN B N   1 
ATOM   5178 C CA  . GLN B 1 131 ? -10.296 41.296 8.483   1.00 30.04  ? 131 GLN B CA  1 
ATOM   5179 C C   . GLN B 1 131 ? -9.748  40.963 9.867   1.00 30.55  ? 131 GLN B C   1 
ATOM   5180 O O   . GLN B 1 131 ? -10.489 40.515 10.752  1.00 27.84  ? 131 GLN B O   1 
ATOM   5181 C CB  . GLN B 1 131 ? -9.834  40.244 7.474   1.00 22.62  ? 131 GLN B CB  1 
ATOM   5182 C CG  . GLN B 1 131 ? -10.459 40.338 6.109   1.00 22.82  ? 131 GLN B CG  1 
ATOM   5183 C CD  . GLN B 1 131 ? -9.733  39.481 5.107   1.00 32.77  ? 131 GLN B CD  1 
ATOM   5184 O OE1 . GLN B 1 131 ? -8.501  39.497 5.041   1.00 34.41  ? 131 GLN B OE1 1 
ATOM   5185 N NE2 . GLN B 1 131 ? -10.488 38.709 4.326   1.00 37.27  ? 131 GLN B NE2 1 
ATOM   5186 N N   . THR B 1 132 ? -8.444  41.188 10.073  1.00 30.57  ? 132 THR B N   1 
ATOM   5187 C CA  . THR B 1 132 ? -7.793  40.745 11.304  1.00 29.64  ? 132 THR B CA  1 
ATOM   5188 C C   . THR B 1 132 ? -8.197  41.600 12.502  1.00 28.44  ? 132 THR B C   1 
ATOM   5189 O O   . THR B 1 132 ? -8.354  41.080 13.613  1.00 34.18  ? 132 THR B O   1 
ATOM   5190 C CB  . THR B 1 132 ? -6.275  40.761 11.134  1.00 31.53  ? 132 THR B CB  1 
ATOM   5191 O OG1 . THR B 1 132 ? -5.914  40.030 9.949   1.00 28.50  ? 132 THR B OG1 1 
ATOM   5192 C CG2 . THR B 1 132 ? -5.596  40.116 12.360  1.00 29.24  ? 132 THR B CG2 1 
ATOM   5193 N N   . LEU B 1 133 ? -8.349  42.913 12.308  1.00 24.44  ? 133 LEU B N   1 
ATOM   5194 C CA  . LEU B 1 133 ? -8.775  43.777 13.409  1.00 27.27  ? 133 LEU B CA  1 
ATOM   5195 C C   . LEU B 1 133 ? -10.240 43.570 13.772  1.00 27.13  ? 133 LEU B C   1 
ATOM   5196 O O   . LEU B 1 133 ? -10.621 43.802 14.928  1.00 31.58  ? 133 LEU B O   1 
ATOM   5197 C CB  . LEU B 1 133 ? -8.509  45.249 13.066  1.00 29.18  ? 133 LEU B CB  1 
ATOM   5198 C CG  . LEU B 1 133 ? -7.022  45.627 13.131  1.00 27.79  ? 133 LEU B CG  1 
ATOM   5199 C CD1 . LEU B 1 133 ? -6.726  46.921 12.384  1.00 29.78  ? 133 LEU B CD1 1 
ATOM   5200 C CD2 . LEU B 1 133 ? -6.547  45.721 14.569  1.00 25.60  ? 133 LEU B CD2 1 
ATOM   5201 N N   . ASN B 1 134 ? -11.070 43.120 12.823  1.00 24.82  ? 134 ASN B N   1 
ATOM   5202 C CA  . ASN B 1 134 ? -12.420 42.708 13.182  1.00 27.86  ? 134 ASN B CA  1 
ATOM   5203 C C   . ASN B 1 134 ? -12.391 41.496 14.108  1.00 31.58  ? 134 ASN B C   1 
ATOM   5204 O O   . ASN B 1 134 ? -13.166 41.431 15.070  1.00 35.84  ? 134 ASN B O   1 
ATOM   5205 C CB  . ASN B 1 134 ? -13.246 42.416 11.926  1.00 28.15  ? 134 ASN B CB  1 
ATOM   5206 C CG  . ASN B 1 134 ? -13.983 43.650 11.412  1.00 29.55  ? 134 ASN B CG  1 
ATOM   5207 O OD1 . ASN B 1 134 ? -15.105 43.944 11.838  1.00 28.59  ? 134 ASN B OD1 1 
ATOM   5208 N ND2 . ASN B 1 134 ? -13.358 44.372 10.498  1.00 25.34  ? 134 ASN B ND2 1 
ATOM   5209 N N   . LEU B 1 135 ? -11.500 40.531 13.849  1.00 24.02  ? 135 LEU B N   1 
ATOM   5210 C CA  . LEU B 1 135 ? -11.371 39.400 14.767  1.00 27.25  ? 135 LEU B CA  1 
ATOM   5211 C C   . LEU B 1 135 ? -10.857 39.852 16.131  1.00 28.76  ? 135 LEU B C   1 
ATOM   5212 O O   . LEU B 1 135 ? -11.436 39.512 17.171  1.00 29.11  ? 135 LEU B O   1 
ATOM   5213 C CB  . LEU B 1 135 ? -10.447 38.337 14.175  1.00 28.82  ? 135 LEU B CB  1 
ATOM   5214 C CG  . LEU B 1 135 ? -10.951 37.603 12.934  1.00 28.95  ? 135 LEU B CG  1 
ATOM   5215 C CD1 . LEU B 1 135 ? -9.852  36.727 12.350  1.00 28.16  ? 135 LEU B CD1 1 
ATOM   5216 C CD2 . LEU B 1 135 ? -12.155 36.772 13.286  1.00 31.51  ? 135 LEU B CD2 1 
ATOM   5217 N N   . LEU B 1 136 ? -9.763  40.625 16.142  1.00 23.32  ? 136 LEU B N   1 
ATOM   5218 C CA  . LEU B 1 136 ? -9.106  40.982 17.395  1.00 25.67  ? 136 LEU B CA  1 
ATOM   5219 C C   . LEU B 1 136 ? -10.002 41.828 18.284  1.00 31.07  ? 136 LEU B C   1 
ATOM   5220 O O   . LEU B 1 136 ? -9.906  41.744 19.516  1.00 30.09  ? 136 LEU B O   1 
ATOM   5221 C CB  . LEU B 1 136 ? -7.795  41.718 17.110  1.00 21.97  ? 136 LEU B CB  1 
ATOM   5222 C CG  . LEU B 1 136 ? -6.665  40.846 16.556  1.00 29.41  ? 136 LEU B CG  1 
ATOM   5223 C CD1 . LEU B 1 136 ? -5.440  41.698 16.194  1.00 27.11  ? 136 LEU B CD1 1 
ATOM   5224 C CD2 . LEU B 1 136 ? -6.298  39.747 17.548  1.00 28.49  ? 136 LEU B CD2 1 
ATOM   5225 N N   . ALA B 1 137 ? -10.870 42.651 17.680  1.00 27.37  ? 137 ALA B N   1 
ATOM   5226 C CA  . ALA B 1 137 ? -11.810 43.457 18.451  1.00 26.57  ? 137 ALA B CA  1 
ATOM   5227 C C   . ALA B 1 137 ? -12.657 42.598 19.381  1.00 24.13  ? 137 ALA B C   1 
ATOM   5228 O O   . ALA B 1 137 ? -13.004 43.034 20.485  1.00 29.75  ? 137 ALA B O   1 
ATOM   5229 C CB  . ALA B 1 137 ? -12.710 44.254 17.507  1.00 23.53  ? 137 ALA B CB  1 
ATOM   5230 N N   . TRP B 1 138 ? -12.986 41.377 18.969  1.00 22.39  ? 138 TRP B N   1 
ATOM   5231 C CA  . TRP B 1 138 ? -13.807 40.491 19.785  1.00 24.54  ? 138 TRP B CA  1 
ATOM   5232 C C   . TRP B 1 138 ? -12.978 39.522 20.633  1.00 29.16  ? 138 TRP B C   1 
ATOM   5233 O O   . TRP B 1 138 ? -13.514 38.511 21.101  1.00 31.16  ? 138 TRP B O   1 
ATOM   5234 C CB  . TRP B 1 138 ? -14.785 39.725 18.899  1.00 27.10  ? 138 TRP B CB  1 
ATOM   5235 C CG  . TRP B 1 138 ? -15.713 40.635 18.176  1.00 27.90  ? 138 TRP B CG  1 
ATOM   5236 C CD1 . TRP B 1 138 ? -15.476 41.275 17.000  1.00 27.15  ? 138 TRP B CD1 1 
ATOM   5237 C CD2 . TRP B 1 138 ? -17.024 41.023 18.590  1.00 25.52  ? 138 TRP B CD2 1 
ATOM   5238 N NE1 . TRP B 1 138 ? -16.560 42.033 16.646  1.00 24.42  ? 138 TRP B NE1 1 
ATOM   5239 C CE2 . TRP B 1 138 ? -17.526 41.900 17.610  1.00 25.99  ? 138 TRP B CE2 1 
ATOM   5240 C CE3 . TRP B 1 138 ? -17.826 40.710 19.695  1.00 23.59  ? 138 TRP B CE3 1 
ATOM   5241 C CZ2 . TRP B 1 138 ? -18.798 42.470 17.696  1.00 25.41  ? 138 TRP B CZ2 1 
ATOM   5242 C CZ3 . TRP B 1 138 ? -19.076 41.275 19.786  1.00 21.95  ? 138 TRP B CZ3 1 
ATOM   5243 C CH2 . TRP B 1 138 ? -19.558 42.145 18.790  1.00 24.14  ? 138 TRP B CH2 1 
ATOM   5244 N N   . CYS B 1 139 ? -11.693 39.815 20.847  1.00 25.35  ? 139 CYS B N   1 
ATOM   5245 C CA  . CYS B 1 139 ? -10.859 38.974 21.702  1.00 23.33  ? 139 CYS B CA  1 
ATOM   5246 C C   . CYS B 1 139 ? -11.381 38.994 23.131  1.00 28.45  ? 139 CYS B C   1 
ATOM   5247 O O   . CYS B 1 139 ? -11.637 40.062 23.700  1.00 29.03  ? 139 CYS B O   1 
ATOM   5248 C CB  . CYS B 1 139 ? -9.403  39.461 21.671  1.00 24.72  ? 139 CYS B CB  1 
ATOM   5249 S SG  . CYS B 1 139 ? -8.218  38.463 22.632  1.00 33.44  ? 139 CYS B SG  1 
ATOM   5250 N N   . GLY B 1 140 ? -11.522 37.817 23.713  1.00 27.08  ? 140 GLY B N   1 
ATOM   5251 C CA  . GLY B 1 140 ? -11.965 37.729 25.081  1.00 27.40  ? 140 GLY B CA  1 
ATOM   5252 C C   . GLY B 1 140 ? -10.829 37.877 26.067  1.00 27.90  ? 140 GLY B C   1 
ATOM   5253 O O   . GLY B 1 140 ? -9.648  37.920 25.714  1.00 31.60  ? 140 GLY B O   1 
ATOM   5254 N N   . ARG B 1 141 ? -11.214 37.929 27.339  1.00 22.00  ? 141 ARG B N   1 
ATOM   5255 C CA  . ARG B 1 141 ? -10.245 38.118 28.414  1.00 20.19  ? 141 ARG B CA  1 
ATOM   5256 C C   . ARG B 1 141 ? -9.121  37.083 28.352  1.00 24.50  ? 141 ARG B C   1 
ATOM   5257 O O   . ARG B 1 141 ? -7.936  37.430 28.465  1.00 22.35  ? 141 ARG B O   1 
ATOM   5258 C CB  . ARG B 1 141 ? -10.986 38.053 29.755  1.00 21.81  ? 141 ARG B CB  1 
ATOM   5259 C CG  . ARG B 1 141 ? -10.112 38.162 30.992  1.00 27.23  ? 141 ARG B CG  1 
ATOM   5260 C CD  . ARG B 1 141 ? -10.997 38.303 32.226  1.00 26.79  ? 141 ARG B CD  1 
ATOM   5261 N NE  . ARG B 1 141 ? -10.244 38.164 33.468  1.00 32.02  ? 141 ARG B NE  1 
ATOM   5262 C CZ  . ARG B 1 141 ? -10.103 37.022 34.131  1.00 25.49  ? 141 ARG B CZ  1 
ATOM   5263 N NH1 . ARG B 1 141 ? -10.671 35.914 33.680  1.00 24.94  ? 141 ARG B NH1 1 
ATOM   5264 N NH2 . ARG B 1 141 ? -9.411  36.992 35.258  1.00 24.31  ? 141 ARG B NH2 1 
ATOM   5265 N N   . THR B 1 142 ? -9.474  35.810 28.160  1.00 25.11  ? 142 THR B N   1 
ATOM   5266 C CA  . THR B 1 142 ? -8.476  34.742 28.180  1.00 32.52  ? 142 THR B CA  1 
ATOM   5267 C C   . THR B 1 142 ? -7.411  34.952 27.112  1.00 39.38  ? 142 THR B C   1 
ATOM   5268 O O   . THR B 1 142 ? -6.208  34.849 27.391  1.00 42.86  ? 142 THR B O   1 
ATOM   5269 C CB  . THR B 1 142 ? -9.147  33.376 27.993  1.00 38.34  ? 142 THR B CB  1 
ATOM   5270 O OG1 . THR B 1 142 ? -9.967  33.077 29.130  1.00 38.23  ? 142 THR B OG1 1 
ATOM   5271 C CG2 . THR B 1 142 ? -8.097  32.275 27.831  1.00 43.82  ? 142 THR B CG2 1 
ATOM   5272 N N   . LEU B 1 143 ? -7.833  35.252 25.881  1.00 31.52  ? 143 LEU B N   1 
ATOM   5273 C CA  . LEU B 1 143 ? -6.873  35.264 24.788  1.00 32.16  ? 143 LEU B CA  1 
ATOM   5274 C C   . LEU B 1 143 ? -6.006  36.521 24.758  1.00 34.84  ? 143 LEU B C   1 
ATOM   5275 O O   . LEU B 1 143 ? -5.130  36.637 23.891  1.00 27.86  ? 143 LEU B O   1 
ATOM   5276 C CB  . LEU B 1 143 ? -7.589  35.008 23.460  1.00 33.42  ? 143 LEU B CB  1 
ATOM   5277 C CG  . LEU B 1 143 ? -7.752  33.493 23.192  1.00 27.22  ? 143 LEU B CG  1 
ATOM   5278 C CD1 . LEU B 1 143 ? -8.397  33.287 21.860  1.00 27.55  ? 143 LEU B CD1 1 
ATOM   5279 C CD2 . LEU B 1 143 ? -6.442  32.645 23.264  1.00 28.23  ? 143 LEU B CD2 1 
ATOM   5280 N N   . ARG B 1 144 ? -6.168  37.423 25.727  1.00 34.79  ? 144 ARG B N   1 
ATOM   5281 C CA  . ARG B 1 144 ? -5.370  38.644 25.707  1.00 38.81  ? 144 ARG B CA  1 
ATOM   5282 C C   . ARG B 1 144 ? -3.874  38.383 25.917  1.00 38.09  ? 144 ARG B C   1 
ATOM   5283 O O   . ARG B 1 144 ? -3.053  39.126 25.354  1.00 37.24  ? 144 ARG B O   1 
ATOM   5284 C CB  . ARG B 1 144 ? -5.885  39.641 26.746  1.00 45.88  ? 144 ARG B CB  1 
ATOM   5285 C CG  . ARG B 1 144 ? -6.942  40.588 26.203  1.00 50.87  ? 144 ARG B CG  1 
ATOM   5286 C CD  . ARG B 1 144 ? -8.047  40.803 27.215  1.00 52.48  ? 144 ARG B CD  1 
ATOM   5287 N NE  . ARG B 1 144 ? -7.583  41.485 28.424  1.00 52.29  ? 144 ARG B NE  1 
ATOM   5288 C CZ  . ARG B 1 144 ? -7.253  40.866 29.554  1.00 50.19  ? 144 ARG B CZ  1 
ATOM   5289 N NH1 . ARG B 1 144 ? -7.316  39.543 29.629  1.00 45.30  ? 144 ARG B NH1 1 
ATOM   5290 N NH2 . ARG B 1 144 ? -6.849  41.567 30.608  1.00 50.60  ? 144 ARG B NH2 1 
ATOM   5291 N N   . LYS B 1 145 ? -3.480  37.369 26.719  1.00 34.97  ? 145 LYS B N   1 
ATOM   5292 C CA  . LYS B 1 145 ? -2.046  37.084 26.858  1.00 36.64  ? 145 LYS B CA  1 
ATOM   5293 C C   . LYS B 1 145 ? -1.476  36.460 25.593  1.00 33.41  ? 145 LYS B C   1 
ATOM   5294 O O   . LYS B 1 145 ? -0.431  36.882 25.094  1.00 40.08  ? 145 LYS B O   1 
ATOM   5295 C CB  . LYS B 1 145 ? -1.780  36.203 28.095  1.00 44.47  ? 145 LYS B CB  1 
ATOM   5296 C CG  . LYS B 1 145 ? -1.838  34.661 27.978  1.00 57.01  ? 145 LYS B CG  1 
ATOM   5297 C CD  . LYS B 1 145 ? -3.048  34.095 27.513  1.00 58.55  ? 145 LYS B CD  1 
ATOM   5298 C CE  . LYS B 1 145 ? -3.000  32.491 27.708  1.00 60.90  ? 145 LYS B CE  1 
ATOM   5299 N NZ  . LYS B 1 145 ? -4.089  32.091 26.771  1.00 60.72  ? 145 LYS B NZ  1 
ATOM   5300 N N   . ASP B 1 146 ? -2.151  35.463 25.042  1.00 35.96  ? 146 ASP B N   1 
ATOM   5301 C CA  . ASP B 1 146 ? -1.602  34.758 23.881  1.00 36.48  ? 146 ASP B CA  1 
ATOM   5302 C C   . ASP B 1 146 ? -1.545  35.646 22.649  1.00 36.78  ? 146 ASP B C   1 
ATOM   5303 O O   . ASP B 1 146 ? -0.671  35.449 21.802  1.00 37.02  ? 146 ASP B O   1 
ATOM   5304 C CB  . ASP B 1 146 ? -2.423  33.513 23.547  1.00 43.41  ? 146 ASP B CB  1 
ATOM   5305 C CG  . ASP B 1 146 ? -2.042  32.319 24.400  1.00 54.49  ? 146 ASP B CG  1 
ATOM   5306 O OD1 . ASP B 1 146 ? -1.073  32.415 25.184  1.00 55.05  ? 146 ASP B OD1 1 
ATOM   5307 O OD2 . ASP B 1 146 ? -2.740  31.289 24.302  1.00 57.06  ? 146 ASP B OD2 1 
ATOM   5308 N N   . LEU B 1 147 ? -2.490  36.577 22.493  1.00 36.11  ? 147 LEU B N   1 
ATOM   5309 C CA  . LEU B 1 147 ? -2.562  37.430 21.310  1.00 31.23  ? 147 LEU B CA  1 
ATOM   5310 C C   . LEU B 1 147 ? -1.975  38.812 21.553  1.00 32.79  ? 147 LEU B C   1 
ATOM   5311 O O   . LEU B 1 147 ? -2.142  39.704 20.709  1.00 38.88  ? 147 LEU B O   1 
ATOM   5312 C CB  . LEU B 1 147 ? -4.020  37.563 20.838  1.00 27.99  ? 147 LEU B CB  1 
ATOM   5313 C CG  . LEU B 1 147 ? -4.738  36.262 20.473  1.00 29.62  ? 147 LEU B CG  1 
ATOM   5314 C CD1 . LEU B 1 147 ? -6.146  36.539 19.955  1.00 27.66  ? 147 LEU B CD1 1 
ATOM   5315 C CD2 . LEU B 1 147 ? -3.929  35.440 19.465  1.00 38.66  ? 147 LEU B CD2 1 
ATOM   5316 N N   . LYS B 1 148 ? -1.299  39.020 22.693  1.00 26.37  ? 148 LYS B N   1 
ATOM   5317 C CA  . LYS B 1 148 ? -0.813  40.360 23.000  1.00 31.13  ? 148 LYS B CA  1 
ATOM   5318 C C   . LYS B 1 148 ? 0.141   40.855 21.923  1.00 34.51  ? 148 LYS B C   1 
ATOM   5319 O O   . LYS B 1 148 ? 0.149   42.048 21.602  1.00 32.71  ? 148 LYS B O   1 
ATOM   5320 C CB  . LYS B 1 148 ? -0.127  40.393 24.369  1.00 37.33  ? 148 LYS B CB  1 
ATOM   5321 C CG  . LYS B 1 148 ? 0.390   41.785 24.763  1.00 36.55  ? 148 LYS B CG  1 
ATOM   5322 C CD  . LYS B 1 148 ? 1.030   41.797 26.156  1.00 36.79  ? 148 LYS B CD  1 
ATOM   5323 C CE  . LYS B 1 148 ? -0.021  41.853 27.270  1.00 42.05  ? 148 LYS B CE  1 
ATOM   5324 N NZ  . LYS B 1 148 ? 0.579   41.545 28.616  1.00 46.03  ? 148 LYS B NZ  1 
ATOM   5325 N N   . ASP B 1 149 ? 0.937   39.956 21.344  1.00 32.56  ? 149 ASP B N   1 
ATOM   5326 C CA  . ASP B 1 149 ? 1.825   40.351 20.257  1.00 34.38  ? 149 ASP B CA  1 
ATOM   5327 C C   . ASP B 1 149 ? 1.037   40.967 19.106  1.00 36.46  ? 149 ASP B C   1 
ATOM   5328 O O   . ASP B 1 149 ? 1.366   42.058 18.625  1.00 37.08  ? 149 ASP B O   1 
ATOM   5329 C CB  . ASP B 1 149 ? 2.627   39.146 19.773  1.00 37.42  ? 149 ASP B CB  1 
ATOM   5330 C CG  . ASP B 1 149 ? 3.531   39.490 18.615  1.00 48.07  ? 149 ASP B CG  1 
ATOM   5331 O OD1 . ASP B 1 149 ? 4.327   40.437 18.770  1.00 54.43  ? 149 ASP B OD1 1 
ATOM   5332 O OD2 . ASP B 1 149 ? 3.434   38.840 17.552  1.00 52.16  ? 149 ASP B OD2 1 
ATOM   5333 N N   . LEU B 1 150 ? -0.024  40.287 18.662  1.00 31.29  ? 150 LEU B N   1 
ATOM   5334 C CA  . LEU B 1 150 ? -0.806  40.787 17.537  1.00 33.28  ? 150 LEU B CA  1 
ATOM   5335 C C   . LEU B 1 150 ? -1.623  42.007 17.926  1.00 37.96  ? 150 LEU B C   1 
ATOM   5336 O O   . LEU B 1 150 ? -1.848  42.891 17.092  1.00 39.92  ? 150 LEU B O   1 
ATOM   5337 C CB  . LEU B 1 150 ? -1.708  39.677 16.997  1.00 33.97  ? 150 LEU B CB  1 
ATOM   5338 C CG  . LEU B 1 150 ? -0.939  38.541 16.320  1.00 33.80  ? 150 LEU B CG  1 
ATOM   5339 C CD1 . LEU B 1 150 ? -1.865  37.421 15.874  1.00 30.47  ? 150 LEU B CD1 1 
ATOM   5340 C CD2 . LEU B 1 150 ? -0.143  39.088 15.140  1.00 29.99  ? 150 LEU B CD2 1 
ATOM   5341 N N   . LEU B 1 151 ? -2.073  42.074 19.182  1.00 39.55  ? 151 LEU B N   1 
ATOM   5342 C CA  . LEU B 1 151 ? -2.762  43.269 19.654  1.00 38.30  ? 151 LEU B CA  1 
ATOM   5343 C C   . LEU B 1 151 ? -1.815  44.467 19.698  1.00 40.46  ? 151 LEU B C   1 
ATOM   5344 O O   . LEU B 1 151 ? -2.199  45.582 19.323  1.00 36.59  ? 151 LEU B O   1 
ATOM   5345 C CB  . LEU B 1 151 ? -3.388  43.006 21.027  1.00 34.96  ? 151 LEU B CB  1 
ATOM   5346 C CG  . LEU B 1 151 ? -4.691  42.188 21.070  1.00 32.30  ? 151 LEU B CG  1 
ATOM   5347 C CD1 . LEU B 1 151 ? -4.953  41.582 22.453  1.00 25.67  ? 151 LEU B CD1 1 
ATOM   5348 C CD2 . LEU B 1 151 ? -5.876  43.041 20.655  1.00 35.68  ? 151 LEU B CD2 1 
ATOM   5349 N N   . ASN B 1 152 ? -0.566  44.251 20.133  1.00 37.90  ? 152 ASN B N   1 
ATOM   5350 C CA  . ASN B 1 152 ? 0.426   45.323 20.147  1.00 37.02  ? 152 ASN B CA  1 
ATOM   5351 C C   . ASN B 1 152 ? 0.755   45.803 18.739  1.00 43.69  ? 152 ASN B C   1 
ATOM   5352 O O   . ASN B 1 152 ? 1.032   46.992 18.535  1.00 46.74  ? 152 ASN B O   1 
ATOM   5353 C CB  . ASN B 1 152 ? 1.712   44.853 20.833  1.00 36.30  ? 152 ASN B CB  1 
ATOM   5354 C CG  . ASN B 1 152 ? 1.688   45.027 22.340  1.00 33.65  ? 152 ASN B CG  1 
ATOM   5355 O OD1 . ASN B 1 152 ? 0.671   45.372 22.922  1.00 36.70  ? 152 ASN B OD1 1 
ATOM   5356 N ND2 . ASN B 1 152 ? 2.837   44.786 22.980  1.00 35.93  ? 152 ASN B ND2 1 
ATOM   5357 N N   . LYS B 1 153 ? 0.758   44.890 17.763  1.00 39.19  ? 153 LYS B N   1 
ATOM   5358 C CA  . LYS B 1 153 ? 1.103   45.254 16.390  1.00 38.67  ? 153 LYS B CA  1 
ATOM   5359 C C   . LYS B 1 153 ? 0.153   46.316 15.839  1.00 39.45  ? 153 LYS B C   1 
ATOM   5360 O O   . LYS B 1 153 ? 0.591   47.352 15.328  1.00 42.87  ? 153 LYS B O   1 
ATOM   5361 C CB  . LYS B 1 153 ? 1.091   44.005 15.508  1.00 35.89  ? 153 LYS B CB  1 
ATOM   5362 C CG  . LYS B 1 153 ? 1.829   44.151 14.190  1.00 37.59  ? 153 LYS B CG  1 
ATOM   5363 C CD  . LYS B 1 153 ? 1.865   42.832 13.434  1.00 33.81  ? 153 LYS B CD  1 
ATOM   5364 C CE  . LYS B 1 153 ? 2.777   42.911 12.218  1.00 36.91  ? 153 LYS B CE  1 
ATOM   5365 N NZ  . LYS B 1 153 ? 2.911   41.576 11.556  1.00 42.99  ? 153 LYS B NZ  1 
ATOM   5366 N N   . GLY B 1 154 ? -1.156  46.076 15.940  1.00 35.75  ? 154 GLY B N   1 
ATOM   5367 C CA  . GLY B 1 154 ? -2.150  47.046 15.531  1.00 36.87  ? 154 GLY B CA  1 
ATOM   5368 C C   . GLY B 1 154 ? -2.363  47.190 14.037  1.00 35.59  ? 154 GLY B C   1 
ATOM   5369 O O   . GLY B 1 154 ? -3.354  47.811 13.632  1.00 29.75  ? 154 GLY B O   1 
ATOM   5370 N N   . ARG B 1 155 ? -1.485  46.638 13.200  1.00 33.48  ? 155 ARG B N   1 
ATOM   5371 C CA  . ARG B 1 155 ? -1.572  46.876 11.763  1.00 34.97  ? 155 ARG B CA  1 
ATOM   5372 C C   . ARG B 1 155 ? -0.649  45.907 11.037  1.00 38.43  ? 155 ARG B C   1 
ATOM   5373 O O   . ARG B 1 155 ? 0.186   45.233 11.646  1.00 40.43  ? 155 ARG B O   1 
ATOM   5374 C CB  . ARG B 1 155 ? -1.204  48.322 11.411  1.00 34.96  ? 155 ARG B CB  1 
ATOM   5375 C CG  . ARG B 1 155 ? 0.248   48.682 11.752  1.00 39.54  ? 155 ARG B CG  1 
ATOM   5376 C CD  . ARG B 1 155 ? 0.594   50.109 11.356  1.00 42.73  ? 155 ARG B CD  1 
ATOM   5377 N NE  . ARG B 1 155 ? -0.181  51.077 12.124  1.00 50.10  ? 155 ARG B NE  1 
ATOM   5378 C CZ  . ARG B 1 155 ? -1.079  51.900 11.596  1.00 53.53  ? 155 ARG B CZ  1 
ATOM   5379 N NH1 . ARG B 1 155 ? -1.304  51.879 10.289  1.00 59.56  ? 155 ARG B NH1 1 
ATOM   5380 N NH2 . ARG B 1 155 ? -1.748  52.744 12.373  1.00 50.06  ? 155 ARG B NH2 1 
ATOM   5381 N N   . ASN B 1 156 ? -0.809  45.862 9.713   1.00 37.11  ? 156 ASN B N   1 
ATOM   5382 C CA  . ASN B 1 156 ? 0.089   45.127 8.821   1.00 40.29  ? 156 ASN B CA  1 
ATOM   5383 C C   . ASN B 1 156 ? 0.094   43.633 9.142   1.00 38.39  ? 156 ASN B C   1 
ATOM   5384 O O   . ASN B 1 156 ? 1.142   43.016 9.332   1.00 39.57  ? 156 ASN B O   1 
ATOM   5385 C CB  . ASN B 1 156 ? 1.505   45.706 8.872   1.00 46.31  ? 156 ASN B CB  1 
ATOM   5386 C CG  . ASN B 1 156 ? 1.535   47.192 8.571   1.00 49.42  ? 156 ASN B CG  1 
ATOM   5387 O OD1 . ASN B 1 156 ? 0.724   47.693 7.790   1.00 51.39  ? 156 ASN B OD1 1 
ATOM   5388 N ND2 . ASN B 1 156 ? 2.470   47.906 9.194   1.00 49.87  ? 156 ASN B ND2 1 
ATOM   5389 N N   . TYR B 1 157 ? -1.094  43.045 9.188   1.00 34.20  ? 157 TYR B N   1 
ATOM   5390 C CA  . TYR B 1 157 ? -1.220  41.632 9.499   1.00 34.19  ? 157 TYR B CA  1 
ATOM   5391 C C   . TYR B 1 157 ? -1.078  40.787 8.237   1.00 37.31  ? 157 TYR B C   1 
ATOM   5392 O O   . TYR B 1 157 ? -1.496  41.193 7.146   1.00 35.33  ? 157 TYR B O   1 
ATOM   5393 C CB  . TYR B 1 157 ? -2.560  41.359 10.174  1.00 33.96  ? 157 TYR B CB  1 
ATOM   5394 C CG  . TYR B 1 157 ? -2.713  42.089 11.488  1.00 33.21  ? 157 TYR B CG  1 
ATOM   5395 C CD1 . TYR B 1 157 ? -2.136  41.587 12.647  1.00 30.12  ? 157 TYR B CD1 1 
ATOM   5396 C CD2 . TYR B 1 157 ? -3.411  43.288 11.568  1.00 33.62  ? 157 TYR B CD2 1 
ATOM   5397 C CE1 . TYR B 1 157 ? -2.258  42.243 13.849  1.00 27.31  ? 157 TYR B CE1 1 
ATOM   5398 C CE2 . TYR B 1 157 ? -3.542  43.959 12.778  1.00 29.97  ? 157 TYR B CE2 1 
ATOM   5399 C CZ  . TYR B 1 157 ? -2.962  43.424 13.914  1.00 29.81  ? 157 TYR B CZ  1 
ATOM   5400 O OH  . TYR B 1 157 ? -3.075  44.067 15.124  1.00 27.89  ? 157 TYR B OH  1 
ATOM   5401 N N   . THR B 1 158 ? -0.476  39.613 8.395   1.00 31.28  ? 158 THR B N   1 
ATOM   5402 C CA  . THR B 1 158 ? -0.356  38.644 7.317   1.00 35.13  ? 158 THR B CA  1 
ATOM   5403 C C   . THR B 1 158 ? -1.525  37.662 7.357   1.00 34.80  ? 158 THR B C   1 
ATOM   5404 O O   . THR B 1 158 ? -2.267  37.575 8.340   1.00 40.26  ? 158 THR B O   1 
ATOM   5405 C CB  . THR B 1 158 ? 0.972   37.898 7.421   1.00 32.91  ? 158 THR B CB  1 
ATOM   5406 O OG1 . THR B 1 158 ? 0.897   36.948 8.488   1.00 37.87  ? 158 THR B OG1 1 
ATOM   5407 C CG2 . THR B 1 158 ? 2.091   38.866 7.721   1.00 32.88  ? 158 THR B CG2 1 
ATOM   5408 N N   . GLN B 1 159 ? -1.698  36.922 6.261   1.00 29.77  ? 159 GLN B N   1 
ATOM   5409 C CA  . GLN B 1 159 ? -2.726  35.886 6.240   1.00 34.97  ? 159 GLN B CA  1 
ATOM   5410 C C   . GLN B 1 159 ? -2.441  34.803 7.279   1.00 39.32  ? 159 GLN B C   1 
ATOM   5411 O O   . GLN B 1 159 ? -3.375  34.243 7.869   1.00 37.50  ? 159 GLN B O   1 
ATOM   5412 C CB  . GLN B 1 159 ? -2.834  35.292 4.831   1.00 37.37  ? 159 GLN B CB  1 
ATOM   5413 C CG  . GLN B 1 159 ? -3.745  34.072 4.702   1.00 30.12  ? 159 GLN B CG  1 
ATOM   5414 C CD  . GLN B 1 159 ? -5.237  34.409 4.751   1.00 30.45  ? 159 GLN B CD  1 
ATOM   5415 O OE1 . GLN B 1 159 ? -5.665  35.494 4.350   1.00 29.83  ? 159 GLN B OE1 1 
ATOM   5416 N NE2 . GLN B 1 159 ? -6.031  33.472 5.244   1.00 26.83  ? 159 GLN B NE2 1 
ATOM   5417 N N   . GLU B 1 160 ? -1.160  34.520 7.546   1.00 31.36  ? 160 GLU B N   1 
ATOM   5418 C CA  . GLU B 1 160 ? -0.818  33.511 8.545   1.00 33.05  ? 160 GLU B CA  1 
ATOM   5419 C C   . GLU B 1 160 ? -1.207  33.961 9.948   1.00 32.59  ? 160 GLU B C   1 
ATOM   5420 O O   . GLU B 1 160 ? -1.721  33.161 10.738  1.00 32.78  ? 160 GLU B O   1 
ATOM   5421 C CB  . GLU B 1 160 ? 0.675   33.187 8.484   1.00 40.26  ? 160 GLU B CB  1 
ATOM   5422 C CG  . GLU B 1 160 ? 1.204   32.482 9.727   1.00 49.94  ? 160 GLU B CG  1 
ATOM   5423 C CD  . GLU B 1 160 ? 2.666   32.073 9.601   1.00 57.78  ? 160 GLU B CD  1 
ATOM   5424 O OE1 . GLU B 1 160 ? 2.967   30.874 9.786   1.00 58.72  ? 160 GLU B OE1 1 
ATOM   5425 O OE2 . GLU B 1 160 ? 3.514   32.948 9.322   1.00 60.89  ? 160 GLU B OE2 1 
ATOM   5426 N N   . GLU B 1 161 ? -0.967  35.235 10.281  1.00 30.10  ? 161 GLU B N   1 
ATOM   5427 C CA  . GLU B 1 161 ? -1.330  35.727 11.607  1.00 30.36  ? 161 GLU B CA  1 
ATOM   5428 C C   . GLU B 1 161 ? -2.843  35.736 11.786  1.00 31.99  ? 161 GLU B C   1 
ATOM   5429 O O   . GLU B 1 161 ? -3.347  35.385 12.858  1.00 34.22  ? 161 GLU B O   1 
ATOM   5430 C CB  . GLU B 1 161 ? -0.757  37.128 11.835  1.00 30.69  ? 161 GLU B CB  1 
ATOM   5431 C CG  . GLU B 1 161 ? 0.761   37.173 11.997  1.00 31.73  ? 161 GLU B CG  1 
ATOM   5432 C CD  . GLU B 1 161 ? 1.328   38.581 11.840  1.00 42.04  ? 161 GLU B CD  1 
ATOM   5433 O OE1 . GLU B 1 161 ? 0.581   39.486 11.397  1.00 42.84  ? 161 GLU B OE1 1 
ATOM   5434 O OE2 . GLU B 1 161 ? 2.527   38.780 12.145  1.00 44.64  ? 161 GLU B OE2 1 
ATOM   5435 N N   . LYS B 1 162 ? -3.583  36.134 10.747  1.00 31.02  ? 162 LYS B N   1 
ATOM   5436 C CA  . LYS B 1 162 ? -5.042  36.119 10.829  1.00 31.27  ? 162 LYS B CA  1 
ATOM   5437 C C   . LYS B 1 162 ? -5.568  34.703 11.032  1.00 33.56  ? 162 LYS B C   1 
ATOM   5438 O O   . LYS B 1 162 ? -6.549  34.497 11.752  1.00 27.62  ? 162 LYS B O   1 
ATOM   5439 C CB  . LYS B 1 162 ? -5.652  36.744 9.572   1.00 29.01  ? 162 LYS B CB  1 
ATOM   5440 C CG  . LYS B 1 162 ? -7.191  36.674 9.515   1.00 24.19  ? 162 LYS B CG  1 
ATOM   5441 C CD  . LYS B 1 162 ? -7.720  37.187 8.186   1.00 28.42  ? 162 LYS B CD  1 
ATOM   5442 C CE  . LYS B 1 162 ? -7.260  36.302 7.039   1.00 35.13  ? 162 LYS B CE  1 
ATOM   5443 N NZ  . LYS B 1 162 ? -7.893  36.653 5.736   1.00 32.53  ? 162 LYS B NZ  1 
ATOM   5444 N N   . GLU B 1 163 ? -4.921  33.710 10.411  1.00 34.68  ? 163 GLU B N   1 
ATOM   5445 C CA  . GLU B 1 163 ? -5.346  32.323 10.593  1.00 31.34  ? 163 GLU B CA  1 
ATOM   5446 C C   . GLU B 1 163 ? -4.983  31.797 11.976  1.00 33.00  ? 163 GLU B C   1 
ATOM   5447 O O   . GLU B 1 163 ? -5.678  30.919 12.509  1.00 32.89  ? 163 GLU B O   1 
ATOM   5448 C CB  . GLU B 1 163 ? -4.735  31.441 9.505   1.00 32.94  ? 163 GLU B CB  1 
ATOM   5449 C CG  . GLU B 1 163 ? -5.434  31.578 8.168   1.00 36.78  ? 163 GLU B CG  1 
ATOM   5450 C CD  . GLU B 1 163 ? -4.642  30.996 7.012   1.00 46.86  ? 163 GLU B CD  1 
ATOM   5451 O OE1 . GLU B 1 163 ? -3.494  30.543 7.228   1.00 51.99  ? 163 GLU B OE1 1 
ATOM   5452 O OE2 . GLU B 1 163 ? -5.176  30.987 5.886   1.00 47.20  ? 163 GLU B OE2 1 
ATOM   5453 N N   . TYR B 1 164 ? -3.906  32.313 12.569  1.00 28.47  ? 164 TYR B N   1 
ATOM   5454 C CA  . TYR B 1 164 ? -3.570  31.939 13.936  1.00 35.30  ? 164 TYR B CA  1 
ATOM   5455 C C   . TYR B 1 164 ? -4.659  32.382 14.899  1.00 33.99  ? 164 TYR B C   1 
ATOM   5456 O O   . TYR B 1 164 ? -5.051  31.631 15.799  1.00 34.10  ? 164 TYR B O   1 
ATOM   5457 C CB  . TYR B 1 164 ? -2.232  32.551 14.343  1.00 36.83  ? 164 TYR B CB  1 
ATOM   5458 C CG  . TYR B 1 164 ? -1.859  32.241 15.776  1.00 42.46  ? 164 TYR B CG  1 
ATOM   5459 C CD1 . TYR B 1 164 ? -1.415  30.972 16.137  1.00 40.06  ? 164 TYR B CD1 1 
ATOM   5460 C CD2 . TYR B 1 164 ? -1.957  33.210 16.771  1.00 45.17  ? 164 TYR B CD2 1 
ATOM   5461 C CE1 . TYR B 1 164 ? -1.074  30.678 17.445  1.00 38.64  ? 164 TYR B CE1 1 
ATOM   5462 C CE2 . TYR B 1 164 ? -1.614  32.922 18.086  1.00 42.86  ? 164 TYR B CE2 1 
ATOM   5463 C CZ  . TYR B 1 164 ? -1.175  31.652 18.412  1.00 40.58  ? 164 TYR B CZ  1 
ATOM   5464 O OH  . TYR B 1 164 ? -0.834  31.343 19.708  1.00 48.38  ? 164 TYR B OH  1 
ATOM   5465 N N   . VAL B 1 165 ? -5.156  33.606 14.727  1.00 32.59  ? 165 VAL B N   1 
ATOM   5466 C CA  . VAL B 1 165 ? -6.221  34.098 15.588  1.00 29.59  ? 165 VAL B CA  1 
ATOM   5467 C C   . VAL B 1 165 ? -7.445  33.199 15.470  1.00 30.83  ? 165 VAL B C   1 
ATOM   5468 O O   . VAL B 1 165 ? -8.029  32.785 16.478  1.00 31.68  ? 165 VAL B O   1 
ATOM   5469 C CB  . VAL B 1 165 ? -6.543  35.565 15.249  1.00 29.01  ? 165 VAL B CB  1 
ATOM   5470 C CG1 . VAL B 1 165 ? -7.780  36.044 16.001  1.00 27.47  ? 165 VAL B CG1 1 
ATOM   5471 C CG2 . VAL B 1 165 ? -5.339  36.435 15.566  1.00 27.30  ? 165 VAL B CG2 1 
ATOM   5472 N N   . LEU B 1 166 ? -7.836  32.863 14.234  1.00 28.87  ? 166 LEU B N   1 
ATOM   5473 C CA  . LEU B 1 166 ? -8.991  31.992 14.031  1.00 31.68  ? 166 LEU B CA  1 
ATOM   5474 C C   . LEU B 1 166 ? -8.781  30.635 14.692  1.00 34.30  ? 166 LEU B C   1 
ATOM   5475 O O   . LEU B 1 166 ? -9.729  30.047 15.225  1.00 36.74  ? 166 LEU B O   1 
ATOM   5476 C CB  . LEU B 1 166 ? -9.270  31.809 12.539  1.00 31.96  ? 166 LEU B CB  1 
ATOM   5477 C CG  . LEU B 1 166 ? -9.967  32.945 11.786  1.00 34.48  ? 166 LEU B CG  1 
ATOM   5478 C CD1 . LEU B 1 166 ? -10.212 32.519 10.347  1.00 38.60  ? 166 LEU B CD1 1 
ATOM   5479 C CD2 . LEU B 1 166 ? -11.259 33.332 12.471  1.00 28.00  ? 166 LEU B CD2 1 
ATOM   5480 N N   . ASN B 1 167 ? -7.546  30.122 14.658  1.00 33.40  ? 167 ASN B N   1 
ATOM   5481 C CA  . ASN B 1 167 ? -7.244  28.843 15.297  1.00 34.72  ? 167 ASN B CA  1 
ATOM   5482 C C   . ASN B 1 167 ? -7.446  28.920 16.806  1.00 33.73  ? 167 ASN B C   1 
ATOM   5483 O O   . ASN B 1 167 ? -8.053  28.027 17.406  1.00 31.25  ? 167 ASN B O   1 
ATOM   5484 C CB  . ASN B 1 167 ? -5.809  28.414 14.981  1.00 40.44  ? 167 ASN B CB  1 
ATOM   5485 C CG  . ASN B 1 167 ? -5.606  28.055 13.522  1.00 48.44  ? 167 ASN B CG  1 
ATOM   5486 O OD1 . ASN B 1 167 ? -6.554  27.708 12.813  1.00 51.24  ? 167 ASN B OD1 1 
ATOM   5487 N ND2 . ASN B 1 167 ? -4.363  28.142 13.063  1.00 47.72  ? 167 ASN B ND2 1 
ATOM   5488 N N   . LYS B 1 168 ? -6.919  29.978 17.441  1.00 25.29  ? 168 LYS B N   1 
ATOM   5489 C CA  . LYS B 1 168 ? -7.111  30.167 18.877  1.00 23.19  ? 168 LYS B CA  1 
ATOM   5490 C C   . LYS B 1 168 ? -8.569  30.470 19.211  1.00 27.31  ? 168 LYS B C   1 
ATOM   5491 O O   . LYS B 1 168 ? -9.045  30.131 20.301  1.00 26.71  ? 168 LYS B O   1 
ATOM   5492 C CB  . LYS B 1 168 ? -6.214  31.299 19.381  1.00 29.32  ? 168 LYS B CB  1 
ATOM   5493 C CG  . LYS B 1 168 ? -4.727  31.116 19.062  1.00 33.91  ? 168 LYS B CG  1 
ATOM   5494 C CD  . LYS B 1 168 ? -4.162  29.852 19.712  1.00 34.46  ? 168 LYS B CD  1 
ATOM   5495 C CE  . LYS B 1 168 ? -4.080  29.995 21.224  1.00 37.55  ? 168 LYS B CE  1 
ATOM   5496 N NZ  . LYS B 1 168 ? -3.666  28.736 21.921  1.00 38.87  ? 168 LYS B NZ  1 
ATOM   5497 N N   . TYR B 1 169 ? -9.284  31.113 18.296  1.00 24.98  ? 169 TYR B N   1 
ATOM   5498 C CA  . TYR B 1 169 ? -10.690 31.407 18.554  1.00 29.51  ? 169 TYR B CA  1 
ATOM   5499 C C   . TYR B 1 169 ? -11.524 30.133 18.533  1.00 28.40  ? 169 TYR B C   1 
ATOM   5500 O O   . TYR B 1 169 ? -12.427 29.956 19.359  1.00 25.65  ? 169 TYR B O   1 
ATOM   5501 C CB  . TYR B 1 169 ? -11.200 32.417 17.530  1.00 25.90  ? 169 TYR B CB  1 
ATOM   5502 C CG  . TYR B 1 169 ? -10.886 33.853 17.879  1.00 25.85  ? 169 TYR B CG  1 
ATOM   5503 C CD1 . TYR B 1 169 ? -10.065 34.173 18.951  1.00 26.82  ? 169 TYR B CD1 1 
ATOM   5504 C CD2 . TYR B 1 169 ? -11.420 34.892 17.134  1.00 27.65  ? 169 TYR B CD2 1 
ATOM   5505 C CE1 . TYR B 1 169 ? -9.781  35.502 19.262  1.00 28.17  ? 169 TYR B CE1 1 
ATOM   5506 C CE2 . TYR B 1 169 ? -11.150 36.203 17.436  1.00 26.06  ? 169 TYR B CE2 1 
ATOM   5507 C CZ  . TYR B 1 169 ? -10.335 36.506 18.494  1.00 23.64  ? 169 TYR B CZ  1 
ATOM   5508 O OH  . TYR B 1 169 ? -10.089 37.828 18.768  1.00 27.99  ? 169 TYR B OH  1 
ATOM   5509 N N   . PHE B 1 170 ? -11.219 29.219 17.612  1.00 29.42  ? 170 PHE B N   1 
ATOM   5510 C CA  . PHE B 1 170 ? -11.939 27.955 17.593  1.00 30.07  ? 170 PHE B CA  1 
ATOM   5511 C C   . PHE B 1 170 ? -11.529 27.061 18.759  1.00 30.13  ? 170 PHE B C   1 
ATOM   5512 O O   . PHE B 1 170 ? -12.350 26.281 19.255  1.00 26.37  ? 170 PHE B O   1 
ATOM   5513 C CB  . PHE B 1 170 ? -11.732 27.260 16.247  1.00 31.14  ? 170 PHE B CB  1 
ATOM   5514 C CG  . PHE B 1 170 ? -12.665 27.755 15.177  1.00 32.14  ? 170 PHE B CG  1 
ATOM   5515 C CD1 . PHE B 1 170 ? -13.982 27.300 15.116  1.00 32.92  ? 170 PHE B CD1 1 
ATOM   5516 C CD2 . PHE B 1 170 ? -12.246 28.700 14.257  1.00 32.11  ? 170 PHE B CD2 1 
ATOM   5517 C CE1 . PHE B 1 170 ? -14.861 27.774 14.132  1.00 34.16  ? 170 PHE B CE1 1 
ATOM   5518 C CE2 . PHE B 1 170 ? -13.111 29.177 13.278  1.00 36.05  ? 170 PHE B CE2 1 
ATOM   5519 C CZ  . PHE B 1 170 ? -14.423 28.711 13.215  1.00 36.06  ? 170 PHE B CZ  1 
ATOM   5520 N N   . GLU B 1 171 ? -10.289 27.180 19.232  1.00 29.73  ? 171 GLU B N   1 
ATOM   5521 C CA  . GLU B 1 171 ? -9.908  26.492 20.464  1.00 33.26  ? 171 GLU B CA  1 
ATOM   5522 C C   . GLU B 1 171 ? -10.816 26.898 21.621  1.00 30.28  ? 171 GLU B C   1 
ATOM   5523 O O   . GLU B 1 171 ? -11.284 26.048 22.387  1.00 31.87  ? 171 GLU B O   1 
ATOM   5524 C CB  . GLU B 1 171 ? -8.449  26.787 20.805  1.00 38.38  ? 171 GLU B CB  1 
ATOM   5525 C CG  . GLU B 1 171 ? -7.479  26.336 19.738  1.00 51.19  ? 171 GLU B CG  1 
ATOM   5526 C CD  . GLU B 1 171 ? -6.135  25.913 20.296  1.00 57.51  ? 171 GLU B CD  1 
ATOM   5527 O OE1 . GLU B 1 171 ? -5.671  26.543 21.272  1.00 51.55  ? 171 GLU B OE1 1 
ATOM   5528 O OE2 . GLU B 1 171 ? -5.540  24.958 19.746  1.00 62.34  ? 171 GLU B OE2 1 
ATOM   5529 N N   . ILE B 1 172 ? -11.066 28.203 21.763  1.00 24.51  ? 172 ILE B N   1 
ATOM   5530 C CA  . ILE B 1 172 ? -11.942 28.699 22.821  1.00 26.86  ? 172 ILE B CA  1 
ATOM   5531 C C   . ILE B 1 172 ? -13.342 28.123 22.667  1.00 25.66  ? 172 ILE B C   1 
ATOM   5532 O O   . ILE B 1 172 ? -13.968 27.699 23.649  1.00 24.88  ? 172 ILE B O   1 
ATOM   5533 C CB  . ILE B 1 172 ? -11.964 30.238 22.815  1.00 30.59  ? 172 ILE B CB  1 
ATOM   5534 C CG1 . ILE B 1 172 ? -10.591 30.804 23.182  1.00 37.75  ? 172 ILE B CG1 1 
ATOM   5535 C CG2 . ILE B 1 172 ? -13.037 30.761 23.761  1.00 25.48  ? 172 ILE B CG2 1 
ATOM   5536 C CD1 . ILE B 1 172 ? -10.144 30.507 24.606  1.00 37.83  ? 172 ILE B CD1 1 
ATOM   5537 N N   . ILE B 1 173 ? -13.854 28.097 21.434  1.00 23.98  ? 173 ILE B N   1 
ATOM   5538 C CA  . ILE B 1 173 ? -15.189 27.561 21.196  1.00 25.26  ? 173 ILE B CA  1 
ATOM   5539 C C   . ILE B 1 173 ? -15.240 26.091 21.577  1.00 26.71  ? 173 ILE B C   1 
ATOM   5540 O O   . ILE B 1 173 ? -16.169 25.641 22.256  1.00 24.21  ? 173 ILE B O   1 
ATOM   5541 C CB  . ILE B 1 173 ? -15.607 27.775 19.731  1.00 28.50  ? 173 ILE B CB  1 
ATOM   5542 C CG1 . ILE B 1 173 ? -15.673 29.274 19.417  1.00 35.11  ? 173 ILE B CG1 1 
ATOM   5543 C CG2 . ILE B 1 173 ? -16.948 27.104 19.479  1.00 27.39  ? 173 ILE B CG2 1 
ATOM   5544 C CD1 . ILE B 1 173 ? -16.175 29.609 18.021  1.00 36.37  ? 173 ILE B CD1 1 
ATOM   5545 N N   . LYS B 1 174 ? -14.229 25.324 21.164  1.00 27.58  ? 174 LYS B N   1 
ATOM   5546 C CA  . LYS B 1 174 ? -14.194 23.899 21.479  1.00 33.77  ? 174 LYS B CA  1 
ATOM   5547 C C   . LYS B 1 174 ? -14.165 23.627 22.978  1.00 31.52  ? 174 LYS B C   1 
ATOM   5548 O O   . LYS B 1 174 ? -14.580 22.547 23.403  1.00 30.64  ? 174 LYS B O   1 
ATOM   5549 C CB  . LYS B 1 174 ? -12.980 23.245 20.820  1.00 36.11  ? 174 LYS B CB  1 
ATOM   5550 C CG  . LYS B 1 174 ? -13.290 22.503 19.538  1.00 48.98  ? 174 LYS B CG  1 
ATOM   5551 C CD  . LYS B 1 174 ? -14.480 21.565 19.704  1.00 57.19  ? 174 LYS B CD  1 
ATOM   5552 C CE  . LYS B 1 174 ? -14.193 20.340 20.572  1.00 57.40  ? 174 LYS B CE  1 
ATOM   5553 N NZ  . LYS B 1 174 ? -15.447 19.541 20.757  1.00 54.03  ? 174 LYS B NZ  1 
ATOM   5554 N N   . LYS B 1 175 ? -13.689 24.574 23.785  1.00 32.11  ? 175 LYS B N   1 
ATOM   5555 C CA  . LYS B 1 175 ? -13.573 24.396 25.228  1.00 30.50  ? 175 LYS B CA  1 
ATOM   5556 C C   . LYS B 1 175 ? -14.749 24.986 25.994  1.00 33.78  ? 175 LYS B C   1 
ATOM   5557 O O   . LYS B 1 175 ? -14.745 24.975 27.229  1.00 30.49  ? 175 LYS B O   1 
ATOM   5558 C CB  . LYS B 1 175 ? -12.267 25.018 25.726  1.00 34.44  ? 175 LYS B CB  1 
ATOM   5559 C CG  . LYS B 1 175 ? -10.992 24.323 25.230  1.00 36.90  ? 175 LYS B CG  1 
ATOM   5560 C CD  . LYS B 1 175 ? -9.762  25.161 25.565  1.00 40.75  ? 175 LYS B CD  1 
ATOM   5561 C CE  . LYS B 1 175 ? -8.486  24.324 25.619  1.00 48.29  ? 175 LYS B CE  1 
ATOM   5562 N NZ  . LYS B 1 175 ? -7.726  24.344 24.330  1.00 49.02  ? 175 LYS B NZ  1 
ATOM   5563 N N   . THR B 1 176 ? -15.767 25.484 25.295  1.00 31.84  ? 176 THR B N   1 
ATOM   5564 C CA  . THR B 1 176 ? -16.763 26.322 25.950  1.00 26.52  ? 176 THR B CA  1 
ATOM   5565 C C   . THR B 1 176 ? -17.745 25.500 26.778  1.00 28.29  ? 176 THR B C   1 
ATOM   5566 O O   . THR B 1 176 ? -17.970 25.799 27.956  1.00 30.19  ? 176 THR B O   1 
ATOM   5567 C CB  . THR B 1 176 ? -17.487 27.163 24.900  1.00 23.47  ? 176 THR B CB  1 
ATOM   5568 O OG1 . THR B 1 176 ? -16.594 28.180 24.422  1.00 23.90  ? 176 THR B OG1 1 
ATOM   5569 C CG2 . THR B 1 176 ? -18.731 27.826 25.495  1.00 19.23  ? 176 THR B CG2 1 
ATOM   5570 N N   . LEU B 1 177 ? -18.341 24.461 26.187  1.00 20.18  ? 177 LEU B N   1 
ATOM   5571 C CA  . LEU B 1 177 ? -19.295 23.666 26.944  1.00 29.84  ? 177 LEU B CA  1 
ATOM   5572 C C   . LEU B 1 177 ? -18.607 22.911 28.074  1.00 27.36  ? 177 LEU B C   1 
ATOM   5573 O O   . LEU B 1 177 ? -19.225 22.651 29.112  1.00 23.30  ? 177 LEU B O   1 
ATOM   5574 C CB  . LEU B 1 177 ? -20.059 22.725 26.012  1.00 31.16  ? 177 LEU B CB  1 
ATOM   5575 C CG  . LEU B 1 177 ? -21.027 23.483 25.089  1.00 30.73  ? 177 LEU B CG  1 
ATOM   5576 C CD1 . LEU B 1 177 ? -21.657 22.545 24.084  1.00 37.48  ? 177 LEU B CD1 1 
ATOM   5577 C CD2 . LEU B 1 177 ? -22.130 24.238 25.857  1.00 27.23  ? 177 LEU B CD2 1 
ATOM   5578 N N   . SER B 1 178 ? -17.321 22.593 27.897  1.00 22.91  ? 178 SER B N   1 
ATOM   5579 C CA  . SER B 1 178 ? -16.549 21.975 28.971  1.00 23.49  ? 178 SER B CA  1 
ATOM   5580 C C   . SER B 1 178 ? -16.465 22.882 30.196  1.00 24.03  ? 178 SER B C   1 
ATOM   5581 O O   . SER B 1 178 ? -16.577 22.405 31.328  1.00 30.03  ? 178 SER B O   1 
ATOM   5582 C CB  . SER B 1 178 ? -15.131 21.632 28.487  1.00 24.95  ? 178 SER B CB  1 
ATOM   5583 O OG  . SER B 1 178 ? -15.162 20.711 27.413  1.00 32.48  ? 178 SER B OG  1 
ATOM   5584 N N   . ILE B 1 179 ? -16.231 24.185 29.999  1.00 29.40  ? 179 ILE B N   1 
ATOM   5585 C CA  . ILE B 1 179 ? -16.028 25.012 31.185  1.00 30.36  ? 179 ILE B CA  1 
ATOM   5586 C C   . ILE B 1 179 ? -17.328 25.161 31.967  1.00 29.47  ? 179 ILE B C   1 
ATOM   5587 O O   . ILE B 1 179 ? -17.297 25.333 33.192  1.00 30.92  ? 179 ILE B O   1 
ATOM   5588 C CB  . ILE B 1 179 ? -15.393 26.381 30.849  1.00 32.38  ? 179 ILE B CB  1 
ATOM   5589 C CG1 . ILE B 1 179 ? -14.688 26.938 32.097  1.00 36.82  ? 179 ILE B CG1 1 
ATOM   5590 C CG2 . ILE B 1 179 ? -16.408 27.393 30.321  1.00 22.68  ? 179 ILE B CG2 1 
ATOM   5591 C CD1 . ILE B 1 179 ? -13.859 28.162 31.834  1.00 32.49  ? 179 ILE B CD1 1 
ATOM   5592 N N   . TYR B 1 180 ? -18.488 25.049 31.302  1.00 25.00  ? 180 TYR B N   1 
ATOM   5593 C CA  . TYR B 1 180 ? -19.738 25.029 32.054  1.00 22.79  ? 180 TYR B CA  1 
ATOM   5594 C C   . TYR B 1 180 ? -19.856 23.755 32.883  1.00 25.48  ? 180 TYR B C   1 
ATOM   5595 O O   . TYR B 1 180 ? -20.217 23.818 34.062  1.00 27.53  ? 180 TYR B O   1 
ATOM   5596 C CB  . TYR B 1 180 ? -20.937 25.206 31.117  1.00 21.19  ? 180 TYR B CB  1 
ATOM   5597 C CG  . TYR B 1 180 ? -21.054 26.637 30.600  1.00 24.94  ? 180 TYR B CG  1 
ATOM   5598 C CD1 . TYR B 1 180 ? -21.541 27.659 31.414  1.00 19.87  ? 180 TYR B CD1 1 
ATOM   5599 C CD2 . TYR B 1 180 ? -20.651 26.968 29.305  1.00 21.17  ? 180 TYR B CD2 1 
ATOM   5600 C CE1 . TYR B 1 180 ? -21.636 28.968 30.950  1.00 26.55  ? 180 TYR B CE1 1 
ATOM   5601 C CE2 . TYR B 1 180 ? -20.738 28.278 28.834  1.00 26.15  ? 180 TYR B CE2 1 
ATOM   5602 C CZ  . TYR B 1 180 ? -21.234 29.273 29.659  1.00 25.83  ? 180 TYR B CZ  1 
ATOM   5603 O OH  . TYR B 1 180 ? -21.329 30.567 29.185  1.00 22.72  ? 180 TYR B OH  1 
ATOM   5604 N N   . ARG B 1 181 ? -19.510 22.595 32.308  1.00 28.27  ? 181 ARG B N   1 
ATOM   5605 C CA  . ARG B 1 181 ? -19.494 21.366 33.101  1.00 27.12  ? 181 ARG B CA  1 
ATOM   5606 C C   . ARG B 1 181 ? -18.503 21.475 34.255  1.00 29.03  ? 181 ARG B C   1 
ATOM   5607 O O   . ARG B 1 181 ? -18.749 20.946 35.348  1.00 27.24  ? 181 ARG B O   1 
ATOM   5608 C CB  . ARG B 1 181 ? -19.141 20.154 32.230  1.00 24.78  ? 181 ARG B CB  1 
ATOM   5609 C CG  . ARG B 1 181 ? -20.049 19.902 31.028  1.00 25.66  ? 181 ARG B CG  1 
ATOM   5610 C CD  . ARG B 1 181 ? -19.700 18.585 30.309  1.00 29.53  ? 181 ARG B CD  1 
ATOM   5611 N NE  . ARG B 1 181 ? -20.382 18.495 29.019  1.00 37.58  ? 181 ARG B NE  1 
ATOM   5612 C CZ  . ARG B 1 181 ? -19.816 18.770 27.845  1.00 40.15  ? 181 ARG B CZ  1 
ATOM   5613 N NH1 . ARG B 1 181 ? -18.544 19.138 27.785  1.00 39.73  ? 181 ARG B NH1 1 
ATOM   5614 N NH2 . ARG B 1 181 ? -20.521 18.667 26.724  1.00 40.62  ? 181 ARG B NH2 1 
ATOM   5615 N N   . GLU B 1 182 ? -17.382 22.169 34.029  1.00 26.04  ? 182 GLU B N   1 
ATOM   5616 C CA  . GLU B 1 182 ? -16.332 22.262 35.039  1.00 28.46  ? 182 GLU B CA  1 
ATOM   5617 C C   . GLU B 1 182 ? -16.771 23.120 36.218  1.00 29.10  ? 182 GLU B C   1 
ATOM   5618 O O   . GLU B 1 182 ? -16.642 22.707 37.377  1.00 27.98  ? 182 GLU B O   1 
ATOM   5619 C CB  . GLU B 1 182 ? -15.046 22.815 34.415  1.00 32.78  ? 182 GLU B CB  1 
ATOM   5620 C CG  . GLU B 1 182 ? -13.967 23.192 35.433  1.00 40.38  ? 182 GLU B CG  1 
ATOM   5621 C CD  . GLU B 1 182 ? -12.797 23.967 34.821  1.00 49.82  ? 182 GLU B CD  1 
ATOM   5622 O OE1 . GLU B 1 182 ? -12.024 24.587 35.588  1.00 50.14  ? 182 GLU B OE1 1 
ATOM   5623 O OE2 . GLU B 1 182 ? -12.652 23.961 33.578  1.00 50.74  ? 182 GLU B OE2 1 
ATOM   5624 N N   . ILE B 1 183 ? -17.293 24.322 35.951  1.00 24.75  ? 183 ILE B N   1 
ATOM   5625 C CA  . ILE B 1 183 ? -17.729 25.169 37.059  1.00 26.65  ? 183 ILE B CA  1 
ATOM   5626 C C   . ILE B 1 183 ? -18.939 24.549 37.753  1.00 29.88  ? 183 ILE B C   1 
ATOM   5627 O O   . ILE B 1 183 ? -19.123 24.705 38.970  1.00 27.06  ? 183 ILE B O   1 
ATOM   5628 C CB  . ILE B 1 183 ? -18.017 26.603 36.567  1.00 37.64  ? 183 ILE B CB  1 
ATOM   5629 C CG1 . ILE B 1 183 ? -19.206 26.629 35.600  1.00 36.66  ? 183 ILE B CG1 1 
ATOM   5630 C CG2 . ILE B 1 183 ? -16.779 27.209 35.909  1.00 38.71  ? 183 ILE B CG2 1 
ATOM   5631 C CD1 . ILE B 1 183 ? -20.455 27.306 36.164  1.00 32.65  ? 183 ILE B CD1 1 
ATOM   5632 N N   . LYS B 1 184 ? -19.763 23.814 37.007  1.00 29.87  ? 184 LYS B N   1 
ATOM   5633 C CA  . LYS B 1 184 ? -20.915 23.142 37.596  1.00 27.28  ? 184 LYS B CA  1 
ATOM   5634 C C   . LYS B 1 184 ? -20.471 22.009 38.521  1.00 31.30  ? 184 LYS B C   1 
ATOM   5635 O O   . LYS B 1 184 ? -20.905 21.928 39.677  1.00 34.54  ? 184 LYS B O   1 
ATOM   5636 C CB  . LYS B 1 184 ? -21.815 22.625 36.473  1.00 30.38  ? 184 LYS B CB  1 
ATOM   5637 C CG  . LYS B 1 184 ? -23.183 22.145 36.873  1.00 36.46  ? 184 LYS B CG  1 
ATOM   5638 C CD  . LYS B 1 184 ? -23.946 21.708 35.630  1.00 36.01  ? 184 LYS B CD  1 
ATOM   5639 C CE  . LYS B 1 184 ? -25.188 20.917 35.986  1.00 37.31  ? 184 LYS B CE  1 
ATOM   5640 N NZ  . LYS B 1 184 ? -24.863 19.734 36.814  1.00 37.65  ? 184 LYS B NZ  1 
ATOM   5641 N N   . GLU B 1 185 ? -19.587 21.135 38.036  1.00 29.12  ? 185 GLU B N   1 
ATOM   5642 C CA  . GLU B 1 185 ? -19.116 20.023 38.856  1.00 35.59  ? 185 GLU B CA  1 
ATOM   5643 C C   . GLU B 1 185 ? -18.362 20.513 40.087  1.00 34.80  ? 185 GLU B C   1 
ATOM   5644 O O   . GLU B 1 185 ? -18.492 19.938 41.173  1.00 33.37  ? 185 GLU B O   1 
ATOM   5645 C CB  . GLU B 1 185 ? -18.224 19.100 38.026  1.00 43.72  ? 185 GLU B CB  1 
ATOM   5646 C CG  . GLU B 1 185 ? -18.962 18.242 37.018  1.00 51.70  ? 185 GLU B CG  1 
ATOM   5647 C CD  . GLU B 1 185 ? -18.068 17.169 36.421  1.00 57.81  ? 185 GLU B CD  1 
ATOM   5648 O OE1 . GLU B 1 185 ? -18.225 15.987 36.794  1.00 57.37  ? 185 GLU B OE1 1 
ATOM   5649 O OE2 . GLU B 1 185 ? -17.197 17.515 35.591  1.00 58.72  ? 185 GLU B OE2 1 
ATOM   5650 N N   . GLU B 1 186 ? -17.571 21.577 39.942  1.00 33.19  ? 186 GLU B N   1 
ATOM   5651 C CA  . GLU B 1 186 ? -16.779 22.105 41.048  1.00 36.48  ? 186 GLU B CA  1 
ATOM   5652 C C   . GLU B 1 186 ? -17.592 22.921 42.049  1.00 33.71  ? 186 GLU B C   1 
ATOM   5653 O O   . GLU B 1 186 ? -17.005 23.444 43.003  1.00 31.12  ? 186 GLU B O   1 
ATOM   5654 C CB  . GLU B 1 186 ? -15.632 22.961 40.506  1.00 42.81  ? 186 GLU B CB  1 
ATOM   5655 C CG  . GLU B 1 186 ? -14.556 22.159 39.790  1.00 46.42  ? 186 GLU B CG  1 
ATOM   5656 C CD  . GLU B 1 186 ? -13.669 23.027 38.916  1.00 54.79  ? 186 GLU B CD  1 
ATOM   5657 O OE1 . GLU B 1 186 ? -13.850 24.268 38.917  1.00 56.30  ? 186 GLU B OE1 1 
ATOM   5658 O OE2 . GLU B 1 186 ? -12.788 22.464 38.229  1.00 58.47  ? 186 GLU B OE2 1 
ATOM   5659 N N   . GLY B 1 187 ? -18.909 23.045 41.862  1.00 34.25  ? 187 GLY B N   1 
ATOM   5660 C CA  . GLY B 1 187 ? -19.750 23.788 42.783  1.00 30.45  ? 187 GLY B CA  1 
ATOM   5661 C C   . GLY B 1 187 ? -19.585 25.293 42.746  1.00 32.85  ? 187 GLY B C   1 
ATOM   5662 O O   . GLY B 1 187 ? -20.034 25.983 43.667  1.00 30.08  ? 187 GLY B O   1 
ATOM   5663 N N   . LYS B 1 188 ? -18.946 25.829 41.710  1.00 29.72  ? 188 LYS B N   1 
ATOM   5664 C CA  . LYS B 1 188 ? -18.760 27.268 41.607  1.00 27.94  ? 188 LYS B CA  1 
ATOM   5665 C C   . LYS B 1 188 ? -19.949 27.975 40.968  1.00 30.20  ? 188 LYS B C   1 
ATOM   5666 O O   . LYS B 1 188 ? -20.030 29.211 41.035  1.00 19.62  ? 188 LYS B O   1 
ATOM   5667 C CB  . LYS B 1 188 ? -17.490 27.573 40.809  1.00 33.75  ? 188 LYS B CB  1 
ATOM   5668 C CG  . LYS B 1 188 ? -16.208 27.018 41.422  1.00 28.52  ? 188 LYS B CG  1 
ATOM   5669 C CD  . LYS B 1 188 ? -15.026 27.220 40.479  1.00 31.09  ? 188 LYS B CD  1 
ATOM   5670 C CE  . LYS B 1 188 ? -13.694 26.913 41.164  1.00 40.06  ? 188 LYS B CE  1 
ATOM   5671 N NZ  . LYS B 1 188 ? -12.571 27.632 40.485  1.00 42.84  ? 188 LYS B NZ  1 
ATOM   5672 N N   . GLY B 1 189 ? -20.867 27.236 40.349  1.00 29.66  ? 189 GLY B N   1 
ATOM   5673 C CA  . GLY B 1 189 ? -22.054 27.850 39.790  1.00 28.48  ? 189 GLY B CA  1 
ATOM   5674 C C   . GLY B 1 189 ? -23.105 26.857 39.337  1.00 26.39  ? 189 GLY B C   1 
ATOM   5675 O O   . GLY B 1 189 ? -22.775 25.719 38.995  1.00 26.12  ? 189 GLY B O   1 
ATOM   5676 N N   . SER B 1 190 ? -24.370 27.266 39.328  1.00 20.49  ? 190 SER B N   1 
ATOM   5677 C CA  . SER B 1 190 ? -25.415 26.444 38.726  1.00 18.45  ? 190 SER B CA  1 
ATOM   5678 C C   . SER B 1 190 ? -25.580 26.829 37.262  1.00 21.98  ? 190 SER B C   1 
ATOM   5679 O O   . SER B 1 190 ? -25.275 27.958 36.862  1.00 22.12  ? 190 SER B O   1 
ATOM   5680 C CB  . SER B 1 190 ? -26.746 26.610 39.465  1.00 20.71  ? 190 SER B CB  1 
ATOM   5681 O OG  . SER B 1 190 ? -26.654 26.118 40.791  1.00 24.54  ? 190 SER B OG  1 
ATOM   5682 N N   . VAL B 1 191 ? -26.046 25.879 36.456  1.00 22.49  ? 191 VAL B N   1 
ATOM   5683 C CA  . VAL B 1 191 ? -26.347 26.133 35.053  1.00 25.38  ? 191 VAL B CA  1 
ATOM   5684 C C   . VAL B 1 191 ? -27.813 25.798 34.815  1.00 26.67  ? 191 VAL B C   1 
ATOM   5685 O O   . VAL B 1 191 ? -28.290 24.731 35.220  1.00 21.82  ? 191 VAL B O   1 
ATOM   5686 C CB  . VAL B 1 191 ? -25.436 25.341 34.098  1.00 25.54  ? 191 VAL B CB  1 
ATOM   5687 C CG1 . VAL B 1 191 ? -25.834 25.614 32.637  1.00 22.53  ? 191 VAL B CG1 1 
ATOM   5688 C CG2 . VAL B 1 191 ? -23.966 25.707 34.343  1.00 20.65  ? 191 VAL B CG2 1 
ATOM   5689 N N   . SER B 1 192 ? -28.525 26.730 34.194  1.00 24.98  ? 192 SER B N   1 
ATOM   5690 C CA  . SER B 1 192 ? -29.928 26.582 33.844  1.00 26.27  ? 192 SER B CA  1 
ATOM   5691 C C   . SER B 1 192 ? -30.067 26.609 32.326  1.00 20.05  ? 192 SER B C   1 
ATOM   5692 O O   . SER B 1 192 ? -29.089 26.774 31.587  1.00 20.45  ? 192 SER B O   1 
ATOM   5693 C CB  . SER B 1 192 ? -30.759 27.703 34.468  1.00 31.59  ? 192 SER B CB  1 
ATOM   5694 O OG  . SER B 1 192 ? -30.366 28.946 33.908  1.00 25.67  ? 192 SER B OG  1 
ATOM   5695 N N   . THR B 1 193 ? -31.301 26.453 31.865  1.00 25.36  ? 193 THR B N   1 
ATOM   5696 C CA  . THR B 1 193 ? -31.623 26.576 30.450  1.00 31.33  ? 193 THR B CA  1 
ATOM   5697 C C   . THR B 1 193 ? -32.984 27.261 30.327  1.00 27.96  ? 193 THR B C   1 
ATOM   5698 O O   . THR B 1 193 ? -33.642 27.560 31.328  1.00 25.03  ? 193 THR B O   1 
ATOM   5699 C CB  . THR B 1 193 ? -31.579 25.195 29.761  1.00 25.79  ? 193 THR B CB  1 
ATOM   5700 O OG1 . THR B 1 193 ? -31.569 25.363 28.335  1.00 24.46  ? 193 THR B OG1 1 
ATOM   5701 C CG2 . THR B 1 193 ? -32.765 24.321 30.181  1.00 22.65  ? 193 THR B CG2 1 
ATOM   5702 N N   . SER B 1 194 ? -33.394 27.550 29.095  1.00 23.73  ? 194 SER B N   1 
ATOM   5703 C CA  . SER B 1 194 ? -34.705 28.114 28.800  1.00 19.88  ? 194 SER B CA  1 
ATOM   5704 C C   . SER B 1 194 ? -35.456 27.200 27.835  1.00 28.05  ? 194 SER B C   1 
ATOM   5705 O O   . SER B 1 194 ? -34.847 26.330 27.198  1.00 22.39  ? 194 SER B O   1 
ATOM   5706 C CB  . SER B 1 194 ? -34.570 29.506 28.173  1.00 18.59  ? 194 SER B CB  1 
ATOM   5707 O OG  . SER B 1 194 ? -33.921 30.411 29.057  1.00 23.30  ? 194 SER B OG  1 
ATOM   5708 N N   . PRO B 1 195 ? -36.774 27.374 27.685  1.00 29.81  ? 195 PRO B N   1 
ATOM   5709 C CA  . PRO B 1 195 ? -37.478 26.682 26.594  1.00 28.34  ? 195 PRO B CA  1 
ATOM   5710 C C   . PRO B 1 195 ? -36.733 26.879 25.278  1.00 30.19  ? 195 PRO B C   1 
ATOM   5711 O O   . PRO B 1 195 ? -36.154 27.942 25.027  1.00 25.78  ? 195 PRO B O   1 
ATOM   5712 C CB  . PRO B 1 195 ? -38.859 27.345 26.584  1.00 37.77  ? 195 PRO B CB  1 
ATOM   5713 C CG  . PRO B 1 195 ? -39.068 27.764 28.009  1.00 40.72  ? 195 PRO B CG  1 
ATOM   5714 C CD  . PRO B 1 195 ? -37.702 28.163 28.521  1.00 33.81  ? 195 PRO B CD  1 
ATOM   5715 N N   . TYR B 1 196 ? -36.765 25.835 24.439  1.00 31.87  ? 196 TYR B N   1 
ATOM   5716 C CA  . TYR B 1 196 ? -35.711 25.568 23.460  1.00 27.72  ? 196 TYR B CA  1 
ATOM   5717 C C   . TYR B 1 196 ? -35.363 26.787 22.612  1.00 29.59  ? 196 TYR B C   1 
ATOM   5718 O O   . TYR B 1 196 ? -34.204 27.213 22.559  1.00 26.36  ? 196 TYR B O   1 
ATOM   5719 C CB  . TYR B 1 196 ? -36.116 24.392 22.560  1.00 28.38  ? 196 TYR B CB  1 
ATOM   5720 C CG  . TYR B 1 196 ? -34.930 23.680 21.927  1.00 30.11  ? 196 TYR B CG  1 
ATOM   5721 C CD1 . TYR B 1 196 ? -34.216 24.262 20.882  1.00 28.45  ? 196 TYR B CD1 1 
ATOM   5722 C CD2 . TYR B 1 196 ? -34.526 22.428 22.374  1.00 29.91  ? 196 TYR B CD2 1 
ATOM   5723 C CE1 . TYR B 1 196 ? -33.128 23.615 20.309  1.00 23.21  ? 196 TYR B CE1 1 
ATOM   5724 C CE2 . TYR B 1 196 ? -33.447 21.776 21.808  1.00 29.06  ? 196 TYR B CE2 1 
ATOM   5725 C CZ  . TYR B 1 196 ? -32.748 22.373 20.777  1.00 29.71  ? 196 TYR B CZ  1 
ATOM   5726 O OH  . TYR B 1 196 ? -31.668 21.711 20.215  1.00 28.14  ? 196 TYR B OH  1 
ATOM   5727 N N   . TYR B 1 197 ? -36.339 27.353 21.907  1.00 26.25  ? 197 TYR B N   1 
ATOM   5728 C CA  . TYR B 1 197 ? -36.001 28.439 21.002  1.00 26.11  ? 197 TYR B CA  1 
ATOM   5729 C C   . TYR B 1 197 ? -36.283 29.812 21.603  1.00 23.38  ? 197 TYR B C   1 
ATOM   5730 O O   . TYR B 1 197 ? -36.399 30.789 20.862  1.00 24.55  ? 197 TYR B O   1 
ATOM   5731 C CB  . TYR B 1 197 ? -36.705 28.251 19.662  1.00 23.82  ? 197 TYR B CB  1 
ATOM   5732 C CG  . TYR B 1 197 ? -36.115 27.086 18.904  1.00 22.88  ? 197 TYR B CG  1 
ATOM   5733 C CD1 . TYR B 1 197 ? -34.846 27.170 18.348  1.00 22.73  ? 197 TYR B CD1 1 
ATOM   5734 C CD2 . TYR B 1 197 ? -36.806 25.887 18.791  1.00 25.28  ? 197 TYR B CD2 1 
ATOM   5735 C CE1 . TYR B 1 197 ? -34.284 26.090 17.676  1.00 25.74  ? 197 TYR B CE1 1 
ATOM   5736 C CE2 . TYR B 1 197 ? -36.262 24.804 18.115  1.00 27.84  ? 197 TYR B CE2 1 
ATOM   5737 C CZ  . TYR B 1 197 ? -35.001 24.912 17.567  1.00 29.04  ? 197 TYR B CZ  1 
ATOM   5738 O OH  . TYR B 1 197 ? -34.465 23.840 16.907  1.00 37.50  ? 197 TYR B OH  1 
ATOM   5739 N N   . HIS B 1 198 ? -36.331 29.911 22.934  1.00 23.61  ? 198 HIS B N   1 
ATOM   5740 C CA  . HIS B 1 198 ? -36.520 31.191 23.615  1.00 18.81  ? 198 HIS B CA  1 
ATOM   5741 C C   . HIS B 1 198 ? -37.835 31.845 23.181  1.00 21.47  ? 198 HIS B C   1 
ATOM   5742 O O   . HIS B 1 198 ? -37.828 33.011 22.778  1.00 19.93  ? 198 HIS B O   1 
ATOM   5743 C CB  . HIS B 1 198 ? -35.322 32.107 23.325  1.00 19.75  ? 198 HIS B CB  1 
ATOM   5744 C CG  . HIS B 1 198 ? -35.110 33.200 24.327  1.00 23.35  ? 198 HIS B CG  1 
ATOM   5745 N ND1 . HIS B 1 198 ? -35.515 34.501 24.102  1.00 25.09  ? 198 HIS B ND1 1 
ATOM   5746 C CD2 . HIS B 1 198 ? -34.500 33.200 25.536  1.00 24.35  ? 198 HIS B CD2 1 
ATOM   5747 C CE1 . HIS B 1 198 ? -35.174 35.250 25.137  1.00 27.16  ? 198 HIS B CE1 1 
ATOM   5748 N NE2 . HIS B 1 198 ? -34.556 34.486 26.020  1.00 23.49  ? 198 HIS B NE2 1 
ATOM   5749 N N   . PRO B 1 199 ? -38.970 31.139 23.214  1.00 24.96  ? 199 PRO B N   1 
ATOM   5750 C CA  . PRO B 1 199 ? -40.246 31.762 22.852  1.00 28.27  ? 199 PRO B CA  1 
ATOM   5751 C C   . PRO B 1 199 ? -40.872 32.475 24.047  1.00 24.13  ? 199 PRO B C   1 
ATOM   5752 O O   . PRO B 1 199 ? -40.420 32.358 25.182  1.00 30.31  ? 199 PRO B O   1 
ATOM   5753 C CB  . PRO B 1 199 ? -41.103 30.559 22.437  1.00 20.16  ? 199 PRO B CB  1 
ATOM   5754 C CG  . PRO B 1 199 ? -40.689 29.518 23.386  1.00 22.91  ? 199 PRO B CG  1 
ATOM   5755 C CD  . PRO B 1 199 ? -39.181 29.732 23.618  1.00 27.68  ? 199 PRO B CD  1 
ATOM   5756 N N   . LEU B 1 200 ? -41.968 33.183 23.775  1.00 32.05  ? 200 LEU B N   1 
ATOM   5757 C CA  . LEU B 1 200 ? -42.772 33.777 24.844  1.00 26.09  ? 200 LEU B CA  1 
ATOM   5758 C C   . LEU B 1 200 ? -43.824 32.758 25.254  1.00 24.81  ? 200 LEU B C   1 
ATOM   5759 O O   . LEU B 1 200 ? -44.905 32.682 24.669  1.00 29.17  ? 200 LEU B O   1 
ATOM   5760 C CB  . LEU B 1 200 ? -43.410 35.080 24.389  1.00 31.27  ? 200 LEU B CB  1 
ATOM   5761 C CG  . LEU B 1 200 ? -42.478 36.252 24.132  1.00 31.11  ? 200 LEU B CG  1 
ATOM   5762 C CD1 . LEU B 1 200 ? -43.214 37.260 23.293  1.00 27.94  ? 200 LEU B CD1 1 
ATOM   5763 C CD2 . LEU B 1 200 ? -42.028 36.875 25.453  1.00 32.26  ? 200 LEU B CD2 1 
ATOM   5764 N N   . ILE B 1 201 ? -43.501 31.964 26.284  1.00 25.98  ? 201 ILE B N   1 
ATOM   5765 C CA  . ILE B 1 201 ? -44.390 30.864 26.680  1.00 27.73  ? 201 ILE B CA  1 
ATOM   5766 C C   . ILE B 1 201 ? -45.803 31.333 27.010  1.00 23.47  ? 201 ILE B C   1 
ATOM   5767 O O   . ILE B 1 201 ? -46.763 30.701 26.537  1.00 23.99  ? 201 ILE B O   1 
ATOM   5768 C CB  . ILE B 1 201 ? -43.751 30.051 27.829  1.00 28.37  ? 201 ILE B CB  1 
ATOM   5769 C CG1 . ILE B 1 201 ? -42.440 29.387 27.372  1.00 27.92  ? 201 ILE B CG1 1 
ATOM   5770 C CG2 . ILE B 1 201 ? -44.743 29.001 28.350  1.00 20.80  ? 201 ILE B CG2 1 
ATOM   5771 C CD1 . ILE B 1 201 ? -42.624 28.018 26.672  1.00 23.91  ? 201 ILE B CD1 1 
ATOM   5772 N N   . PRO B 1 202 ? -46.018 32.408 27.786  1.00 24.50  ? 202 PRO B N   1 
ATOM   5773 C CA  . PRO B 1 202 ? -47.413 32.786 28.116  1.00 23.93  ? 202 PRO B CA  1 
ATOM   5774 C C   . PRO B 1 202 ? -48.289 33.050 26.895  1.00 24.76  ? 202 PRO B C   1 
ATOM   5775 O O   . PRO B 1 202 ? -49.496 32.774 26.933  1.00 23.85  ? 202 PRO B O   1 
ATOM   5776 C CB  . PRO B 1 202 ? -47.242 34.055 28.965  1.00 20.41  ? 202 PRO B CB  1 
ATOM   5777 C CG  . PRO B 1 202 ? -45.848 33.949 29.539  1.00 23.65  ? 202 PRO B CG  1 
ATOM   5778 C CD  . PRO B 1 202 ? -45.043 33.307 28.443  1.00 25.51  ? 202 PRO B CD  1 
ATOM   5779 N N   . ILE B 1 203 ? -47.715 33.577 25.811  1.00 21.60  ? 203 ILE B N   1 
ATOM   5780 C CA  . ILE B 1 203 ? -48.506 33.848 24.616  1.00 25.20  ? 203 ILE B CA  1 
ATOM   5781 C C   . ILE B 1 203 ? -48.800 32.554 23.868  1.00 26.92  ? 203 ILE B C   1 
ATOM   5782 O O   . ILE B 1 203 ? -49.914 32.348 23.370  1.00 32.23  ? 203 ILE B O   1 
ATOM   5783 C CB  . ILE B 1 203 ? -47.789 34.879 23.729  1.00 31.61  ? 203 ILE B CB  1 
ATOM   5784 C CG1 . ILE B 1 203 ? -47.883 36.271 24.364  1.00 32.25  ? 203 ILE B CG1 1 
ATOM   5785 C CG2 . ILE B 1 203 ? -48.381 34.888 22.319  1.00 27.34  ? 203 ILE B CG2 1 
ATOM   5786 C CD1 . ILE B 1 203 ? -47.354 37.366 23.471  1.00 32.95  ? 203 ILE B CD1 1 
ATOM   5787 N N   . LEU B 1 204 ? -47.821 31.648 23.805  1.00 30.49  ? 204 LEU B N   1 
ATOM   5788 C CA  . LEU B 1 204 ? -48.070 30.341 23.207  1.00 31.39  ? 204 LEU B CA  1 
ATOM   5789 C C   . LEU B 1 204 ? -49.170 29.590 23.956  1.00 32.36  ? 204 LEU B C   1 
ATOM   5790 O O   . LEU B 1 204 ? -49.973 28.876 23.343  1.00 27.04  ? 204 LEU B O   1 
ATOM   5791 C CB  . LEU B 1 204 ? -46.785 29.518 23.193  1.00 30.11  ? 204 LEU B CB  1 
ATOM   5792 C CG  . LEU B 1 204 ? -45.602 29.986 22.345  1.00 29.03  ? 204 LEU B CG  1 
ATOM   5793 C CD1 . LEU B 1 204 ? -44.606 28.831 22.212  1.00 29.26  ? 204 LEU B CD1 1 
ATOM   5794 C CD2 . LEU B 1 204 ? -46.058 30.499 20.983  1.00 25.84  ? 204 LEU B CD2 1 
ATOM   5795 N N   . LEU B 1 205 ? -49.228 29.740 25.284  1.00 26.84  ? 205 LEU B N   1 
ATOM   5796 C CA  . LEU B 1 205 ? -50.263 29.047 26.045  1.00 28.93  ? 205 LEU B CA  1 
ATOM   5797 C C   . LEU B 1 205 ? -51.610 29.753 25.936  1.00 31.05  ? 205 LEU B C   1 
ATOM   5798 O O   . LEU B 1 205 ? -52.653 29.093 25.889  1.00 32.86  ? 205 LEU B O   1 
ATOM   5799 C CB  . LEU B 1 205 ? -49.853 28.928 27.511  1.00 26.06  ? 205 LEU B CB  1 
ATOM   5800 C CG  . LEU B 1 205 ? -48.716 27.965 27.853  1.00 23.35  ? 205 LEU B CG  1 
ATOM   5801 C CD1 . LEU B 1 205 ? -48.322 28.125 29.305  1.00 22.63  ? 205 LEU B CD1 1 
ATOM   5802 C CD2 . LEU B 1 205 ? -49.120 26.525 27.589  1.00 31.19  ? 205 LEU B CD2 1 
ATOM   5803 N N   . ASN B 1 206 ? -51.611 31.085 25.889  1.00 31.39  ? 206 ASN B N   1 
ATOM   5804 C CA  . ASN B 1 206 ? -52.857 31.844 25.912  1.00 32.77  ? 206 ASN B CA  1 
ATOM   5805 C C   . ASN B 1 206 ? -52.597 33.278 25.481  1.00 32.11  ? 206 ASN B C   1 
ATOM   5806 O O   . ASN B 1 206 ? -52.241 34.122 26.314  1.00 30.17  ? 206 ASN B O   1 
ATOM   5807 C CB  . ASN B 1 206 ? -53.482 31.828 27.308  1.00 38.18  ? 206 ASN B CB  1 
ATOM   5808 C CG  . ASN B 1 206 ? -54.842 32.518 27.353  1.00 45.74  ? 206 ASN B CG  1 
ATOM   5809 O OD1 . ASN B 1 206 ? -55.456 32.794 26.313  1.00 37.89  ? 206 ASN B OD1 1 
ATOM   5810 N ND2 . ASN B 1 206 ? -55.320 32.798 28.562  1.00 44.66  ? 206 ASN B ND2 1 
ATOM   5811 N N   . PRO B 1 207 ? -52.774 33.599 24.200  1.00 29.47  ? 207 PRO B N   1 
ATOM   5812 C CA  . PRO B 1 207 ? -52.487 34.966 23.749  1.00 29.97  ? 207 PRO B CA  1 
ATOM   5813 C C   . PRO B 1 207 ? -53.322 36.014 24.450  1.00 32.75  ? 207 PRO B C   1 
ATOM   5814 O O   . PRO B 1 207 ? -52.940 37.187 24.440  1.00 33.22  ? 207 PRO B O   1 
ATOM   5815 C CB  . PRO B 1 207 ? -52.792 34.915 22.245  1.00 30.60  ? 207 PRO B CB  1 
ATOM   5816 C CG  . PRO B 1 207 ? -52.714 33.461 21.891  1.00 32.03  ? 207 PRO B CG  1 
ATOM   5817 C CD  . PRO B 1 207 ? -53.214 32.732 23.098  1.00 30.64  ? 207 PRO B CD  1 
ATOM   5818 N N   . ASN B 1 208 ? -54.436 35.626 25.080  1.00 30.32  ? 208 ASN B N   1 
ATOM   5819 C CA  . ASN B 1 208 ? -55.260 36.584 25.805  1.00 32.35  ? 208 ASN B CA  1 
ATOM   5820 C C   . ASN B 1 208 ? -54.550 37.157 27.027  1.00 32.09  ? 208 ASN B C   1 
ATOM   5821 O O   . ASN B 1 208 ? -54.971 38.201 27.540  1.00 31.68  ? 208 ASN B O   1 
ATOM   5822 C CB  . ASN B 1 208 ? -56.582 35.930 26.217  1.00 32.86  ? 208 ASN B CB  1 
ATOM   5823 C CG  . ASN B 1 208 ? -57.563 35.835 25.063  1.00 38.53  ? 208 ASN B CG  1 
ATOM   5824 O OD1 . ASN B 1 208 ? -57.590 36.705 24.191  1.00 35.08  ? 208 ASN B OD1 1 
ATOM   5825 N ND2 . ASN B 1 208 ? -58.364 34.769 25.043  1.00 41.98  ? 208 ASN B ND2 1 
ATOM   5826 N N   . CYS B 1 209 ? -53.466 36.531 27.490  1.00 29.25  ? 209 CYS B N   1 
ATOM   5827 C CA  . CYS B 1 209 ? -52.795 37.062 28.671  1.00 29.36  ? 209 CYS B CA  1 
ATOM   5828 C C   . CYS B 1 209 ? -52.267 38.478 28.449  1.00 30.86  ? 209 CYS B C   1 
ATOM   5829 O O   . CYS B 1 209 ? -52.012 39.189 29.428  1.00 32.82  ? 209 CYS B O   1 
ATOM   5830 C CB  . CYS B 1 209 ? -51.666 36.125 29.111  1.00 31.62  ? 209 CYS B CB  1 
ATOM   5831 S SG  . CYS B 1 209 ? -50.257 36.072 27.989  1.00 32.11  ? 209 CYS B SG  1 
ATOM   5832 N N   . VAL B 1 210 ? -52.139 38.922 27.192  1.00 30.00  ? 210 VAL B N   1 
ATOM   5833 C CA  . VAL B 1 210 ? -51.629 40.267 26.939  1.00 30.25  ? 210 VAL B CA  1 
ATOM   5834 C C   . VAL B 1 210 ? -52.578 41.317 27.489  1.00 26.94  ? 210 VAL B C   1 
ATOM   5835 O O   . VAL B 1 210 ? -52.141 42.402 27.886  1.00 27.26  ? 210 VAL B O   1 
ATOM   5836 C CB  . VAL B 1 210 ? -51.353 40.493 25.437  1.00 34.82  ? 210 VAL B CB  1 
ATOM   5837 C CG1 . VAL B 1 210 ? -50.261 39.545 24.952  1.00 37.50  ? 210 VAL B CG1 1 
ATOM   5838 C CG2 . VAL B 1 210 ? -52.625 40.351 24.602  1.00 36.30  ? 210 VAL B CG2 1 
ATOM   5839 N N   . TYR B 1 211 ? -53.880 41.012 27.545  1.00 25.07  ? 211 TYR B N   1 
ATOM   5840 C CA  . TYR B 1 211 ? -54.859 41.957 28.070  1.00 30.29  ? 211 TYR B CA  1 
ATOM   5841 C C   . TYR B 1 211 ? -54.714 42.202 29.567  1.00 30.59  ? 211 TYR B C   1 
ATOM   5842 O O   . TYR B 1 211 ? -55.311 43.155 30.074  1.00 31.67  ? 211 TYR B O   1 
ATOM   5843 C CB  . TYR B 1 211 ? -56.283 41.476 27.764  1.00 30.91  ? 211 TYR B CB  1 
ATOM   5844 C CG  . TYR B 1 211 ? -56.512 41.239 26.289  1.00 34.31  ? 211 TYR B CG  1 
ATOM   5845 C CD1 . TYR B 1 211 ? -56.291 42.253 25.363  1.00 33.75  ? 211 TYR B CD1 1 
ATOM   5846 C CD2 . TYR B 1 211 ? -56.935 40.002 25.821  1.00 35.33  ? 211 TYR B CD2 1 
ATOM   5847 C CE1 . TYR B 1 211 ? -56.484 42.040 24.005  1.00 37.26  ? 211 TYR B CE1 1 
ATOM   5848 C CE2 . TYR B 1 211 ? -57.137 39.780 24.464  1.00 38.50  ? 211 TYR B CE2 1 
ATOM   5849 C CZ  . TYR B 1 211 ? -56.910 40.801 23.563  1.00 40.47  ? 211 TYR B CZ  1 
ATOM   5850 O OH  . TYR B 1 211 ? -57.108 40.590 22.218  1.00 42.46  ? 211 TYR B OH  1 
ATOM   5851 N N   . GLU B 1 212 ? -53.949 41.377 30.286  1.00 31.18  ? 212 GLU B N   1 
ATOM   5852 C CA  . GLU B 1 212 ? -53.807 41.601 31.721  1.00 34.01  ? 212 GLU B CA  1 
ATOM   5853 C C   . GLU B 1 212 ? -53.034 42.881 32.011  1.00 32.90  ? 212 GLU B C   1 
ATOM   5854 O O   . GLU B 1 212 ? -53.244 43.505 33.055  1.00 38.70  ? 212 GLU B O   1 
ATOM   5855 C CB  . GLU B 1 212 ? -53.136 40.394 32.379  1.00 37.78  ? 212 GLU B CB  1 
ATOM   5856 C CG  . GLU B 1 212 ? -53.946 39.119 32.224  1.00 41.73  ? 212 GLU B CG  1 
ATOM   5857 C CD  . GLU B 1 212 ? -53.283 37.915 32.853  1.00 42.87  ? 212 GLU B CD  1 
ATOM   5858 O OE1 . GLU B 1 212 ? -53.601 36.784 32.428  1.00 42.28  ? 212 GLU B OE1 1 
ATOM   5859 O OE2 . GLU B 1 212 ? -52.454 38.099 33.768  1.00 37.53  ? 212 GLU B OE2 1 
ATOM   5860 N N   . THR B 1 213 ? -52.154 43.294 31.100  1.00 31.10  ? 213 THR B N   1 
ATOM   5861 C CA  . THR B 1 213 ? -51.418 44.542 31.228  1.00 27.20  ? 213 THR B CA  1 
ATOM   5862 C C   . THR B 1 213 ? -51.737 45.556 30.138  1.00 31.43  ? 213 THR B C   1 
ATOM   5863 O O   . THR B 1 213 ? -51.702 46.756 30.411  1.00 33.09  ? 213 THR B O   1 
ATOM   5864 C CB  . THR B 1 213 ? -49.907 44.276 31.220  1.00 29.85  ? 213 THR B CB  1 
ATOM   5865 O OG1 . THR B 1 213 ? -49.570 43.492 30.063  1.00 34.71  ? 213 THR B OG1 1 
ATOM   5866 C CG2 . THR B 1 213 ? -49.490 43.536 32.492  1.00 33.85  ? 213 THR B CG2 1 
ATOM   5867 N N   . THR B 1 214 ? -52.040 45.116 28.914  1.00 33.23  ? 214 THR B N   1 
ATOM   5868 C CA  . THR B 1 214 ? -52.376 46.015 27.808  1.00 30.94  ? 214 THR B CA  1 
ATOM   5869 C C   . THR B 1 214 ? -53.772 45.688 27.286  1.00 30.29  ? 214 THR B C   1 
ATOM   5870 O O   . THR B 1 214 ? -53.928 45.170 26.173  1.00 31.62  ? 214 THR B O   1 
ATOM   5871 C CB  . THR B 1 214 ? -51.346 45.925 26.684  1.00 37.36  ? 214 THR B CB  1 
ATOM   5872 O OG1 . THR B 1 214 ? -51.284 44.579 26.196  1.00 33.74  ? 214 THR B OG1 1 
ATOM   5873 C CG2 . THR B 1 214 ? -49.969 46.349 27.186  1.00 35.74  ? 214 THR B CG2 1 
ATOM   5874 N N   . PRO B 1 215 ? -54.816 46.018 28.051  1.00 33.98  ? 215 PRO B N   1 
ATOM   5875 C CA  . PRO B 1 215 ? -56.174 45.583 27.672  1.00 37.70  ? 215 PRO B CA  1 
ATOM   5876 C C   . PRO B 1 215 ? -56.684 46.176 26.362  1.00 41.97  ? 215 PRO B C   1 
ATOM   5877 O O   . PRO B 1 215 ? -57.648 45.640 25.796  1.00 42.93  ? 215 PRO B O   1 
ATOM   5878 C CB  . PRO B 1 215 ? -57.034 46.044 28.859  1.00 39.19  ? 215 PRO B CB  1 
ATOM   5879 C CG  . PRO B 1 215 ? -56.269 47.187 29.457  1.00 36.18  ? 215 PRO B CG  1 
ATOM   5880 C CD  . PRO B 1 215 ? -54.811 46.855 29.264  1.00 31.99  ? 215 PRO B CD  1 
ATOM   5881 N N   . ASN B 1 216 ? -56.087 47.257 25.859  1.00 38.68  ? 216 ASN B N   1 
ATOM   5882 C CA  . ASN B 1 216 ? -56.539 47.888 24.626  1.00 40.69  ? 216 ASN B CA  1 
ATOM   5883 C C   . ASN B 1 216 ? -55.662 47.542 23.423  1.00 39.15  ? 216 ASN B C   1 
ATOM   5884 O O   . ASN B 1 216 ? -55.769 48.193 22.378  1.00 38.08  ? 216 ASN B O   1 
ATOM   5885 C CB  . ASN B 1 216 ? -56.604 49.406 24.809  1.00 47.47  ? 216 ASN B CB  1 
ATOM   5886 C CG  . ASN B 1 216 ? -57.602 49.821 25.872  1.00 52.48  ? 216 ASN B CG  1 
ATOM   5887 O OD1 . ASN B 1 216 ? -58.710 49.289 25.935  1.00 54.08  ? 216 ASN B OD1 1 
ATOM   5888 N ND2 . ASN B 1 216 ? -57.209 50.765 26.722  1.00 54.33  ? 216 ASN B ND2 1 
ATOM   5889 N N   . VAL B 1 217 ? -54.808 46.536 23.540  1.00 37.52  ? 217 VAL B N   1 
ATOM   5890 C CA  . VAL B 1 217 ? -53.905 46.194 22.449  1.00 37.89  ? 217 VAL B CA  1 
ATOM   5891 C C   . VAL B 1 217 ? -54.656 45.387 21.400  1.00 36.26  ? 217 VAL B C   1 
ATOM   5892 O O   . VAL B 1 217 ? -55.592 44.638 21.709  1.00 34.65  ? 217 VAL B O   1 
ATOM   5893 C CB  . VAL B 1 217 ? -52.671 45.440 22.990  1.00 38.64  ? 217 VAL B CB  1 
ATOM   5894 C CG1 . VAL B 1 217 ? -53.027 44.008 23.338  1.00 37.27  ? 217 VAL B CG1 1 
ATOM   5895 C CG2 . VAL B 1 217 ? -51.540 45.483 21.989  1.00 41.65  ? 217 VAL B CG2 1 
ATOM   5896 N N   . LYS B 1 218 ? -54.276 45.579 20.139  1.00 35.81  ? 218 LYS B N   1 
ATOM   5897 C CA  . LYS B 1 218 ? -54.802 44.789 19.036  1.00 36.54  ? 218 LYS B CA  1 
ATOM   5898 C C   . LYS B 1 218 ? -53.767 43.742 18.648  1.00 37.67  ? 218 LYS B C   1 
ATOM   5899 O O   . LYS B 1 218 ? -52.593 44.069 18.433  1.00 39.50  ? 218 LYS B O   1 
ATOM   5900 C CB  . LYS B 1 218 ? -55.134 45.667 17.831  1.00 43.21  ? 218 LYS B CB  1 
ATOM   5901 C CG  . LYS B 1 218 ? -55.935 46.926 18.176  1.00 50.28  ? 218 LYS B CG  1 
ATOM   5902 C CD  . LYS B 1 218 ? -57.056 47.147 17.182  1.00 56.00  ? 218 LYS B CD  1 
ATOM   5903 C CE  . LYS B 1 218 ? -57.338 48.636 16.980  1.00 61.93  ? 218 LYS B CE  1 
ATOM   5904 N NZ  . LYS B 1 218 ? -56.409 49.266 15.995  1.00 66.81  ? 218 LYS B NZ  1 
ATOM   5905 N N   . ILE B 1 219 ? -54.202 42.489 18.571  1.00 39.95  ? 219 ILE B N   1 
ATOM   5906 C CA  . ILE B 1 219 ? -53.332 41.378 18.189  1.00 44.03  ? 219 ILE B CA  1 
ATOM   5907 C C   . ILE B 1 219 ? -54.040 40.581 17.101  1.00 46.99  ? 219 ILE B C   1 
ATOM   5908 O O   . ILE B 1 219 ? -55.265 40.683 16.942  1.00 48.24  ? 219 ILE B O   1 
ATOM   5909 C CB  . ILE B 1 219 ? -52.974 40.482 19.403  1.00 38.40  ? 219 ILE B CB  1 
ATOM   5910 C CG1 . ILE B 1 219 ? -54.235 39.879 20.030  1.00 41.56  ? 219 ILE B CG1 1 
ATOM   5911 C CG2 . ILE B 1 219 ? -52.151 41.261 20.439  1.00 33.96  ? 219 ILE B CG2 1 
ATOM   5912 C CD1 . ILE B 1 219 ? -53.946 38.873 21.124  1.00 45.39  ? 219 ILE B CD1 1 
ATOM   5913 N N   . PRO B 1 220 ? -53.298 39.796 16.319  1.00 45.72  ? 220 PRO B N   1 
ATOM   5914 C CA  . PRO B 1 220 ? -53.930 39.012 15.252  1.00 47.87  ? 220 PRO B CA  1 
ATOM   5915 C C   . PRO B 1 220 ? -54.876 37.955 15.805  1.00 49.49  ? 220 PRO B C   1 
ATOM   5916 O O   . PRO B 1 220 ? -54.971 37.709 17.010  1.00 45.99  ? 220 PRO B O   1 
ATOM   5917 C CB  . PRO B 1 220 ? -52.742 38.372 14.520  1.00 46.10  ? 220 PRO B CB  1 
ATOM   5918 C CG  . PRO B 1 220 ? -51.631 38.429 15.467  1.00 45.77  ? 220 PRO B CG  1 
ATOM   5919 C CD  . PRO B 1 220 ? -51.831 39.679 16.271  1.00 45.35  ? 220 PRO B CD  1 
ATOM   5920 N N   . ASP B 1 221 ? -55.594 37.323 14.881  1.00 51.35  ? 221 ASP B N   1 
ATOM   5921 C CA  . ASP B 1 221 ? -56.519 36.250 15.225  1.00 52.85  ? 221 ASP B CA  1 
ATOM   5922 C C   . ASP B 1 221 ? -55.732 34.953 15.364  1.00 43.84  ? 221 ASP B C   1 
ATOM   5923 O O   . ASP B 1 221 ? -55.217 34.420 14.375  1.00 41.87  ? 221 ASP B O   1 
ATOM   5924 C CB  . ASP B 1 221 ? -57.610 36.123 14.166  1.00 59.32  ? 221 ASP B CB  1 
ATOM   5925 C CG  . ASP B 1 221 ? -58.280 34.764 14.188  1.00 68.85  ? 221 ASP B CG  1 
ATOM   5926 O OD1 . ASP B 1 221 ? -58.693 34.326 15.284  1.00 67.61  ? 221 ASP B OD1 1 
ATOM   5927 O OD2 . ASP B 1 221 ? -58.388 34.133 13.111  1.00 76.03  ? 221 ASP B OD2 1 
ATOM   5928 N N   . PHE B 1 222 ? -55.636 34.441 16.589  1.00 40.27  ? 222 PHE B N   1 
ATOM   5929 C CA  . PHE B 1 222 ? -54.874 33.221 16.850  1.00 37.72  ? 222 PHE B CA  1 
ATOM   5930 C C   . PHE B 1 222 ? -55.747 32.025 16.493  1.00 44.77  ? 222 PHE B C   1 
ATOM   5931 O O   . PHE B 1 222 ? -56.400 31.419 17.345  1.00 44.59  ? 222 PHE B O   1 
ATOM   5932 C CB  . PHE B 1 222 ? -54.408 33.179 18.298  1.00 35.00  ? 222 PHE B CB  1 
ATOM   5933 C CG  . PHE B 1 222 ? -53.043 33.760 18.498  1.00 34.68  ? 222 PHE B CG  1 
ATOM   5934 C CD1 . PHE B 1 222 ? -52.873 35.130 18.652  1.00 29.32  ? 222 PHE B CD1 1 
ATOM   5935 C CD2 . PHE B 1 222 ? -51.928 32.945 18.510  1.00 33.28  ? 222 PHE B CD2 1 
ATOM   5936 C CE1 . PHE B 1 222 ? -51.611 35.670 18.829  1.00 35.54  ? 222 PHE B CE1 1 
ATOM   5937 C CE2 . PHE B 1 222 ? -50.663 33.479 18.692  1.00 36.08  ? 222 PHE B CE2 1 
ATOM   5938 C CZ  . PHE B 1 222 ? -50.504 34.843 18.849  1.00 34.56  ? 222 PHE B CZ  1 
ATOM   5939 N N   . ALA B 1 223 ? -55.735 31.675 15.206  1.00 43.57  ? 223 ALA B N   1 
ATOM   5940 C CA  . ALA B 1 223 ? -56.649 30.694 14.645  1.00 44.04  ? 223 ALA B CA  1 
ATOM   5941 C C   . ALA B 1 223 ? -56.223 29.250 14.884  1.00 40.68  ? 223 ALA B C   1 
ATOM   5942 O O   . ALA B 1 223 ? -56.910 28.342 14.407  1.00 38.93  ? 223 ALA B O   1 
ATOM   5943 C CB  . ALA B 1 223 ? -56.810 30.938 13.143  1.00 44.25  ? 223 ALA B CB  1 
ATOM   5944 N N   . VAL B 1 224 ? -55.109 29.007 15.579  1.00 41.47  ? 224 VAL B N   1 
ATOM   5945 C CA  . VAL B 1 224 ? -54.708 27.662 15.977  1.00 41.07  ? 224 VAL B CA  1 
ATOM   5946 C C   . VAL B 1 224 ? -54.076 27.726 17.361  1.00 36.65  ? 224 VAL B C   1 
ATOM   5947 O O   . VAL B 1 224 ? -53.825 28.801 17.913  1.00 33.51  ? 224 VAL B O   1 
ATOM   5948 C CB  . VAL B 1 224 ? -53.732 27.002 14.980  1.00 43.73  ? 224 VAL B CB  1 
ATOM   5949 C CG1 . VAL B 1 224 ? -54.400 26.774 13.647  1.00 45.75  ? 224 VAL B CG1 1 
ATOM   5950 C CG2 . VAL B 1 224 ? -52.492 27.848 14.822  1.00 45.98  ? 224 VAL B CG2 1 
ATOM   5951 N N   . SER B 1 225 ? -53.807 26.547 17.915  1.00 36.24  ? 225 SER B N   1 
ATOM   5952 C CA  . SER B 1 225 ? -53.325 26.414 19.281  1.00 38.66  ? 225 SER B CA  1 
ATOM   5953 C C   . SER B 1 225 ? -51.822 26.191 19.285  1.00 37.51  ? 225 SER B C   1 
ATOM   5954 O O   . SER B 1 225 ? -51.317 25.301 18.592  1.00 28.54  ? 225 SER B O   1 
ATOM   5955 C CB  . SER B 1 225 ? -54.017 25.255 19.998  1.00 42.54  ? 225 SER B CB  1 
ATOM   5956 O OG  . SER B 1 225 ? -53.459 25.079 21.287  1.00 44.17  ? 225 SER B OG  1 
ATOM   5957 N N   . PHE B 1 226 ? -51.115 26.988 20.080  1.00 33.84  ? 226 PHE B N   1 
ATOM   5958 C CA  . PHE B 1 226 ? -49.689 26.808 20.294  1.00 31.37  ? 226 PHE B CA  1 
ATOM   5959 C C   . PHE B 1 226 ? -49.375 26.179 21.644  1.00 32.02  ? 226 PHE B C   1 
ATOM   5960 O O   . PHE B 1 226 ? -48.211 26.177 22.057  1.00 29.21  ? 226 PHE B O   1 
ATOM   5961 C CB  . PHE B 1 226 ? -48.968 28.146 20.168  1.00 30.92  ? 226 PHE B CB  1 
ATOM   5962 C CG  . PHE B 1 226 ? -48.866 28.639 18.763  1.00 33.58  ? 226 PHE B CG  1 
ATOM   5963 C CD1 . PHE B 1 226 ? -47.869 28.169 17.923  1.00 39.09  ? 226 PHE B CD1 1 
ATOM   5964 C CD2 . PHE B 1 226 ? -49.770 29.568 18.275  1.00 37.15  ? 226 PHE B CD2 1 
ATOM   5965 C CE1 . PHE B 1 226 ? -47.767 28.618 16.621  1.00 42.29  ? 226 PHE B CE1 1 
ATOM   5966 C CE2 . PHE B 1 226 ? -49.680 30.024 16.972  1.00 43.89  ? 226 PHE B CE2 1 
ATOM   5967 C CZ  . PHE B 1 226 ? -48.675 29.549 16.142  1.00 45.27  ? 226 PHE B CZ  1 
ATOM   5968 N N   . ARG B 1 227 ? -50.388 25.645 22.338  1.00 36.01  ? 227 ARG B N   1 
ATOM   5969 C CA  . ARG B 1 227 ? -50.187 25.159 23.703  1.00 35.96  ? 227 ARG B CA  1 
ATOM   5970 C C   . ARG B 1 227 ? -49.251 23.959 23.738  1.00 30.45  ? 227 ARG B C   1 
ATOM   5971 O O   . ARG B 1 227 ? -48.402 23.853 24.628  1.00 34.80  ? 227 ARG B O   1 
ATOM   5972 C CB  . ARG B 1 227 ? -51.528 24.798 24.341  1.00 34.74  ? 227 ARG B CB  1 
ATOM   5973 C CG  . ARG B 1 227 ? -52.513 25.957 24.421  1.00 41.55  ? 227 ARG B CG  1 
ATOM   5974 C CD  . ARG B 1 227 ? -53.800 25.545 25.128  1.00 45.03  ? 227 ARG B CD  1 
ATOM   5975 N NE  . ARG B 1 227 ? -53.532 24.951 26.436  1.00 42.77  ? 227 ARG B NE  1 
ATOM   5976 C CZ  . ARG B 1 227 ? -53.383 25.647 27.559  1.00 45.97  ? 227 ARG B CZ  1 
ATOM   5977 N NH1 . ARG B 1 227 ? -53.474 26.971 27.543  1.00 38.39  ? 227 ARG B NH1 1 
ATOM   5978 N NH2 . ARG B 1 227 ? -53.136 25.019 28.702  1.00 50.44  ? 227 ARG B NH2 1 
ATOM   5979 N N   . GLU B 1 228 ? -49.394 23.033 22.792  1.00 26.95  ? 228 GLU B N   1 
ATOM   5980 C CA  . GLU B 1 228 ? -48.510 21.879 22.841  1.00 31.96  ? 228 GLU B CA  1 
ATOM   5981 C C   . GLU B 1 228 ? -47.113 22.220 22.335  1.00 34.31  ? 228 GLU B C   1 
ATOM   5982 O O   . GLU B 1 228 ? -46.141 21.562 22.725  1.00 30.59  ? 228 GLU B O   1 
ATOM   5983 C CB  . GLU B 1 228 ? -49.125 20.715 22.063  1.00 43.24  ? 228 GLU B CB  1 
ATOM   5984 C CG  . GLU B 1 228 ? -49.977 19.825 22.970  1.00 56.31  ? 228 GLU B CG  1 
ATOM   5985 C CD  . GLU B 1 228 ? -50.653 18.692 22.235  1.00 67.14  ? 228 GLU B CD  1 
ATOM   5986 O OE1 . GLU B 1 228 ? -50.757 18.765 20.994  1.00 69.26  ? 228 GLU B OE1 1 
ATOM   5987 O OE2 . GLU B 1 228 ? -51.085 17.726 22.903  1.00 72.11  ? 228 GLU B OE2 1 
ATOM   5988 N N   . ASP B 1 229 ? -46.984 23.279 21.524  1.00 26.19  ? 229 ASP B N   1 
ATOM   5989 C CA  . ASP B 1 229 ? -45.659 23.771 21.154  1.00 29.55  ? 229 ASP B CA  1 
ATOM   5990 C C   . ASP B 1 229 ? -44.920 24.329 22.367  1.00 29.51  ? 229 ASP B C   1 
ATOM   5991 O O   . ASP B 1 229 ? -43.712 24.102 22.528  1.00 28.74  ? 229 ASP B O   1 
ATOM   5992 C CB  . ASP B 1 229 ? -45.776 24.822 20.054  1.00 29.74  ? 229 ASP B CB  1 
ATOM   5993 C CG  . ASP B 1 229 ? -45.980 24.200 18.680  1.00 30.68  ? 229 ASP B CG  1 
ATOM   5994 O OD1 . ASP B 1 229 ? -46.057 22.952 18.612  1.00 29.02  ? 229 ASP B OD1 1 
ATOM   5995 O OD2 . ASP B 1 229 ? -46.058 24.948 17.678  1.00 25.93  ? 229 ASP B OD2 1 
ATOM   5996 N N   . ALA B 1 230 ? -45.633 25.056 23.237  1.00 30.05  ? 230 ALA B N   1 
ATOM   5997 C CA  . ALA B 1 230 ? -45.042 25.511 24.494  1.00 29.37  ? 230 ALA B CA  1 
ATOM   5998 C C   . ALA B 1 230 ? -44.524 24.339 25.322  1.00 28.25  ? 230 ALA B C   1 
ATOM   5999 O O   . ALA B 1 230 ? -43.407 24.393 25.851  1.00 29.58  ? 230 ALA B O   1 
ATOM   6000 C CB  . ALA B 1 230 ? -46.061 26.325 25.289  1.00 27.11  ? 230 ALA B CB  1 
ATOM   6001 N N   . SER B 1 231 ? -45.318 23.270 25.450  1.00 28.80  ? 231 SER B N   1 
ATOM   6002 C CA  . SER B 1 231 ? -44.816 22.062 26.106  1.00 33.08  ? 231 SER B CA  1 
ATOM   6003 C C   . SER B 1 231 ? -43.563 21.533 25.419  1.00 30.00  ? 231 SER B C   1 
ATOM   6004 O O   . SER B 1 231 ? -42.604 21.124 26.088  1.00 27.96  ? 231 SER B O   1 
ATOM   6005 C CB  . SER B 1 231 ? -45.896 20.982 26.129  1.00 37.87  ? 231 SER B CB  1 
ATOM   6006 O OG  . SER B 1 231 ? -46.890 21.276 27.093  1.00 47.80  ? 231 SER B OG  1 
ATOM   6007 N N   . LYS B 1 232 ? -43.558 21.533 24.082  1.00 32.59  ? 232 LYS B N   1 
ATOM   6008 C CA  . LYS B 1 232 ? -42.423 21.005 23.330  1.00 35.59  ? 232 LYS B CA  1 
ATOM   6009 C C   . LYS B 1 232 ? -41.161 21.832 23.563  1.00 34.36  ? 232 LYS B C   1 
ATOM   6010 O O   . LYS B 1 232 ? -40.064 21.274 23.672  1.00 33.94  ? 232 LYS B O   1 
ATOM   6011 C CB  . LYS B 1 232 ? -42.755 20.953 21.836  1.00 37.16  ? 232 LYS B CB  1 
ATOM   6012 C CG  . LYS B 1 232 ? -43.334 19.629 21.342  1.00 46.06  ? 232 LYS B CG  1 
ATOM   6013 C CD  . LYS B 1 232 ? -43.955 19.786 19.950  1.00 50.71  ? 232 LYS B CD  1 
ATOM   6014 C CE  . LYS B 1 232 ? -44.602 18.497 19.461  1.00 57.82  ? 232 LYS B CE  1 
ATOM   6015 N NZ  . LYS B 1 232 ? -45.774 18.108 20.299  1.00 61.27  ? 232 LYS B NZ  1 
ATOM   6016 N N   . HIS B 1 233 ? -41.291 23.166 23.620  1.00 32.12  ? 233 HIS B N   1 
ATOM   6017 C CA  . HIS B 1 233 ? -40.132 24.008 23.908  1.00 29.28  ? 233 HIS B CA  1 
ATOM   6018 C C   . HIS B 1 233 ? -39.502 23.622 25.246  1.00 28.88  ? 233 HIS B C   1 
ATOM   6019 O O   . HIS B 1 233 ? -38.277 23.490 25.353  1.00 23.81  ? 233 HIS B O   1 
ATOM   6020 C CB  . HIS B 1 233 ? -40.528 25.496 23.908  1.00 30.45  ? 233 HIS B CB  1 
ATOM   6021 C CG  . HIS B 1 233 ? -40.684 26.100 22.538  1.00 30.29  ? 233 HIS B CG  1 
ATOM   6022 N ND1 . HIS B 1 233 ? -39.613 26.525 21.777  1.00 28.29  ? 233 HIS B ND1 1 
ATOM   6023 C CD2 . HIS B 1 233 ? -41.792 26.368 21.803  1.00 31.33  ? 233 HIS B CD2 1 
ATOM   6024 C CE1 . HIS B 1 233 ? -40.055 27.021 20.633  1.00 28.83  ? 233 HIS B CE1 1 
ATOM   6025 N NE2 . HIS B 1 233 ? -41.374 26.936 20.623  1.00 25.85  ? 233 HIS B NE2 1 
ATOM   6026 N N   . VAL B 1 234 ? -40.330 23.428 26.275  1.00 27.17  ? 234 VAL B N   1 
ATOM   6027 C CA  . VAL B 1 234 ? -39.828 23.070 27.600  1.00 25.31  ? 234 VAL B CA  1 
ATOM   6028 C C   . VAL B 1 234 ? -39.240 21.663 27.602  1.00 23.75  ? 234 VAL B C   1 
ATOM   6029 O O   . VAL B 1 234 ? -38.165 21.425 28.169  1.00 24.67  ? 234 VAL B O   1 
ATOM   6030 C CB  . VAL B 1 234 ? -40.954 23.210 28.638  1.00 26.12  ? 234 VAL B CB  1 
ATOM   6031 C CG1 . VAL B 1 234 ? -40.470 22.768 30.022  1.00 26.70  ? 234 VAL B CG1 1 
ATOM   6032 C CG2 . VAL B 1 234 ? -41.472 24.659 28.659  1.00 27.92  ? 234 VAL B CG2 1 
ATOM   6033 N N   . GLU B 1 235 ? -39.931 20.707 26.977  1.00 26.01  ? 235 GLU B N   1 
ATOM   6034 C CA  . GLU B 1 235 ? -39.483 19.319 27.037  1.00 27.06  ? 235 GLU B CA  1 
ATOM   6035 C C   . GLU B 1 235 ? -38.171 19.125 26.282  1.00 32.50  ? 235 GLU B C   1 
ATOM   6036 O O   . GLU B 1 235 ? -37.253 18.443 26.765  1.00 23.60  ? 235 GLU B O   1 
ATOM   6037 C CB  . GLU B 1 235 ? -40.571 18.397 26.485  1.00 39.52  ? 235 GLU B CB  1 
ATOM   6038 C CG  . GLU B 1 235 ? -40.430 16.949 26.925  1.00 53.32  ? 235 GLU B CG  1 
ATOM   6039 C CD  . GLU B 1 235 ? -40.179 16.815 28.418  1.00 61.21  ? 235 GLU B CD  1 
ATOM   6040 O OE1 . GLU B 1 235 ? -41.091 17.132 29.213  1.00 61.88  ? 235 GLU B OE1 1 
ATOM   6041 O OE2 . GLU B 1 235 ? -39.063 16.396 28.793  1.00 64.31  ? 235 GLU B OE2 1 
ATOM   6042 N N   . LEU B 1 236 ? -38.072 19.707 25.081  1.00 26.80  ? 236 LEU B N   1 
ATOM   6043 C CA  . LEU B 1 236 ? -36.864 19.539 24.285  1.00 26.71  ? 236 LEU B CA  1 
ATOM   6044 C C   . LEU B 1 236 ? -35.675 20.230 24.940  1.00 27.93  ? 236 LEU B C   1 
ATOM   6045 O O   . LEU B 1 236 ? -34.535 19.761 24.820  1.00 26.07  ? 236 LEU B O   1 
ATOM   6046 C CB  . LEU B 1 236 ? -37.094 20.077 22.869  1.00 27.81  ? 236 LEU B CB  1 
ATOM   6047 C CG  . LEU B 1 236 ? -38.095 19.335 21.970  1.00 32.67  ? 236 LEU B CG  1 
ATOM   6048 C CD1 . LEU B 1 236 ? -38.287 20.071 20.646  1.00 32.07  ? 236 LEU B CD1 1 
ATOM   6049 C CD2 . LEU B 1 236 ? -37.647 17.903 21.728  1.00 33.33  ? 236 LEU B CD2 1 
ATOM   6050 N N   . ALA B 1 237 ? -35.929 21.344 25.635  1.00 24.58  ? 237 ALA B N   1 
ATOM   6051 C CA  . ALA B 1 237 ? -34.875 22.016 26.380  1.00 22.90  ? 237 ALA B CA  1 
ATOM   6052 C C   . ALA B 1 237 ? -34.361 21.138 27.511  1.00 29.51  ? 237 ALA B C   1 
ATOM   6053 O O   . ALA B 1 237 ? -33.151 21.083 27.754  1.00 24.82  ? 237 ALA B O   1 
ATOM   6054 C CB  . ALA B 1 237 ? -35.390 23.349 26.924  1.00 20.19  ? 237 ALA B CB  1 
ATOM   6055 N N   . LYS B 1 238 ? -35.264 20.445 28.214  1.00 25.23  ? 238 LYS B N   1 
ATOM   6056 C CA  . LYS B 1 238 ? -34.822 19.526 29.255  1.00 30.04  ? 238 LYS B CA  1 
ATOM   6057 C C   . LYS B 1 238 ? -33.929 18.441 28.669  1.00 33.91  ? 238 LYS B C   1 
ATOM   6058 O O   . LYS B 1 238 ? -32.914 18.067 29.269  1.00 31.90  ? 238 LYS B O   1 
ATOM   6059 C CB  . LYS B 1 238 ? -36.027 18.901 29.955  1.00 31.12  ? 238 LYS B CB  1 
ATOM   6060 C CG  . LYS B 1 238 ? -36.872 19.890 30.729  1.00 29.37  ? 238 LYS B CG  1 
ATOM   6061 C CD  . LYS B 1 238 ? -38.151 19.220 31.202  1.00 32.87  ? 238 LYS B CD  1 
ATOM   6062 C CE  . LYS B 1 238 ? -37.857 17.970 32.033  1.00 31.29  ? 238 LYS B CE  1 
ATOM   6063 N NZ  . LYS B 1 238 ? -39.108 17.314 32.529  1.00 36.54  ? 238 LYS B NZ  1 
ATOM   6064 N N   . GLU B 1 239 ? -34.285 17.939 27.485  1.00 32.17  ? 239 GLU B N   1 
ATOM   6065 C CA  . GLU B 1 239 ? -33.490 16.892 26.853  1.00 33.28  ? 239 GLU B CA  1 
ATOM   6066 C C   . GLU B 1 239 ? -32.142 17.426 26.387  1.00 29.62  ? 239 GLU B C   1 
ATOM   6067 O O   . GLU B 1 239 ? -31.115 16.759 26.552  1.00 31.53  ? 239 GLU B O   1 
ATOM   6068 C CB  . GLU B 1 239 ? -34.268 16.289 25.686  1.00 35.32  ? 239 GLU B CB  1 
ATOM   6069 C CG  . GLU B 1 239 ? -35.513 15.535 26.125  1.00 44.08  ? 239 GLU B CG  1 
ATOM   6070 C CD  . GLU B 1 239 ? -36.554 15.412 25.026  1.00 58.40  ? 239 GLU B CD  1 
ATOM   6071 O OE1 . GLU B 1 239 ? -36.222 15.682 23.851  1.00 63.61  ? 239 GLU B OE1 1 
ATOM   6072 O OE2 . GLU B 1 239 ? -37.706 15.044 25.339  1.00 63.29  ? 239 GLU B OE2 1 
ATOM   6073 N N   . LYS B 1 240 ? -32.124 18.623 25.796  1.00 28.45  ? 240 LYS B N   1 
ATOM   6074 C CA  . LYS B 1 240 ? -30.857 19.186 25.341  1.00 30.43  ? 240 LYS B CA  1 
ATOM   6075 C C   . LYS B 1 240 ? -29.930 19.444 26.520  1.00 26.31  ? 240 LYS B C   1 
ATOM   6076 O O   . LYS B 1 240 ? -28.748 19.083 26.483  1.00 25.27  ? 240 LYS B O   1 
ATOM   6077 C CB  . LYS B 1 240 ? -31.109 20.466 24.542  1.00 30.95  ? 240 LYS B CB  1 
ATOM   6078 C CG  . LYS B 1 240 ? -29.867 21.042 23.859  1.00 30.46  ? 240 LYS B CG  1 
ATOM   6079 C CD  . LYS B 1 240 ? -29.347 20.122 22.760  1.00 26.76  ? 240 LYS B CD  1 
ATOM   6080 C CE  . LYS B 1 240 ? -27.942 20.535 22.332  1.00 33.09  ? 240 LYS B CE  1 
ATOM   6081 N NZ  . LYS B 1 240 ? -27.422 19.749 21.155  1.00 34.62  ? 240 LYS B NZ  1 
ATOM   6082 N N   . TYR B 1 241 ? -30.458 20.044 27.586  1.00 26.97  ? 241 TYR B N   1 
ATOM   6083 C CA  . TYR B 1 241 ? -29.664 20.236 28.794  1.00 30.97  ? 241 TYR B CA  1 
ATOM   6084 C C   . TYR B 1 241 ? -29.139 18.908 29.329  1.00 29.92  ? 241 TYR B C   1 
ATOM   6085 O O   . TYR B 1 241 ? -27.982 18.816 29.765  1.00 32.40  ? 241 TYR B O   1 
ATOM   6086 C CB  . TYR B 1 241 ? -30.507 20.950 29.840  1.00 30.68  ? 241 TYR B CB  1 
ATOM   6087 C CG  . TYR B 1 241 ? -29.796 21.271 31.134  1.00 29.28  ? 241 TYR B CG  1 
ATOM   6088 C CD1 . TYR B 1 241 ? -29.732 20.336 32.161  1.00 27.65  ? 241 TYR B CD1 1 
ATOM   6089 C CD2 . TYR B 1 241 ? -29.242 22.528 31.353  1.00 27.67  ? 241 TYR B CD2 1 
ATOM   6090 C CE1 . TYR B 1 241 ? -29.109 20.628 33.350  1.00 28.48  ? 241 TYR B CE1 1 
ATOM   6091 C CE2 . TYR B 1 241 ? -28.608 22.826 32.544  1.00 25.00  ? 241 TYR B CE2 1 
ATOM   6092 C CZ  . TYR B 1 241 ? -28.551 21.875 33.538  1.00 25.69  ? 241 TYR B CZ  1 
ATOM   6093 O OH  . TYR B 1 241 ? -27.928 22.166 34.730  1.00 27.43  ? 241 TYR B OH  1 
ATOM   6094 N N   . PHE B 1 242 ? -29.968 17.864 29.293  1.00 29.08  ? 242 PHE B N   1 
ATOM   6095 C CA  . PHE B 1 242 ? -29.530 16.559 29.783  1.00 29.38  ? 242 PHE B CA  1 
ATOM   6096 C C   . PHE B 1 242 ? -28.407 15.987 28.926  1.00 28.22  ? 242 PHE B C   1 
ATOM   6097 O O   . PHE B 1 242 ? -27.524 15.290 29.442  1.00 25.76  ? 242 PHE B O   1 
ATOM   6098 C CB  . PHE B 1 242 ? -30.696 15.568 29.828  1.00 26.47  ? 242 PHE B CB  1 
ATOM   6099 C CG  . PHE B 1 242 ? -30.311 14.214 30.389  1.00 33.06  ? 242 PHE B CG  1 
ATOM   6100 C CD1 . PHE B 1 242 ? -30.215 14.019 31.759  1.00 32.89  ? 242 PHE B CD1 1 
ATOM   6101 C CD2 . PHE B 1 242 ? -30.019 13.147 29.544  1.00 34.58  ? 242 PHE B CD2 1 
ATOM   6102 C CE1 . PHE B 1 242 ? -29.847 12.791 32.281  1.00 34.07  ? 242 PHE B CE1 1 
ATOM   6103 C CE2 . PHE B 1 242 ? -29.652 11.913 30.063  1.00 38.66  ? 242 PHE B CE2 1 
ATOM   6104 C CZ  . PHE B 1 242 ? -29.570 11.738 31.433  1.00 39.33  ? 242 PHE B CZ  1 
ATOM   6105 N N   . GLU B 1 243 ? -28.436 16.239 27.615  1.00 26.18  ? 243 GLU B N   1 
ATOM   6106 C CA  . GLU B 1 243 ? -27.375 15.720 26.758  1.00 30.28  ? 243 GLU B CA  1 
ATOM   6107 C C   . GLU B 1 243 ? -26.030 16.335 27.129  1.00 36.15  ? 243 GLU B C   1 
ATOM   6108 O O   . GLU B 1 243 ? -24.999 15.651 27.118  1.00 40.59  ? 243 GLU B O   1 
ATOM   6109 C CB  . GLU B 1 243 ? -27.707 15.980 25.285  1.00 38.43  ? 243 GLU B CB  1 
ATOM   6110 C CG  . GLU B 1 243 ? -26.565 15.660 24.306  1.00 49.27  ? 243 GLU B CG  1 
ATOM   6111 C CD  . GLU B 1 243 ? -26.664 16.429 22.983  1.00 57.94  ? 243 GLU B CD  1 
ATOM   6112 O OE1 . GLU B 1 243 ? -27.795 16.706 22.519  1.00 59.89  ? 243 GLU B OE1 1 
ATOM   6113 O OE2 . GLU B 1 243 ? -25.605 16.761 22.405  1.00 58.88  ? 243 GLU B OE2 1 
ATOM   6114 N N   . ILE B 1 244 ? -26.028 17.619 27.496  1.00 31.42  ? 244 ILE B N   1 
ATOM   6115 C CA  . ILE B 1 244 ? -24.778 18.313 27.768  1.00 31.26  ? 244 ILE B CA  1 
ATOM   6116 C C   . ILE B 1 244 ? -24.276 18.008 29.175  1.00 27.00  ? 244 ILE B C   1 
ATOM   6117 O O   . ILE B 1 244 ? -23.085 17.742 29.372  1.00 28.10  ? 244 ILE B O   1 
ATOM   6118 C CB  . ILE B 1 244 ? -24.960 19.826 27.533  1.00 32.88  ? 244 ILE B CB  1 
ATOM   6119 C CG1 . ILE B 1 244 ? -25.348 20.088 26.076  1.00 31.80  ? 244 ILE B CG1 1 
ATOM   6120 C CG2 . ILE B 1 244 ? -23.690 20.591 27.878  1.00 27.50  ? 244 ILE B CG2 1 
ATOM   6121 C CD1 . ILE B 1 244 ? -24.305 19.606 25.076  1.00 31.45  ? 244 ILE B CD1 1 
ATOM   6122 N N   . PHE B 1 245 ? -25.165 18.008 30.171  1.00 19.39  ? 245 PHE B N   1 
ATOM   6123 C CA  . PHE B 1 245 ? -24.736 17.972 31.564  1.00 23.30  ? 245 PHE B CA  1 
ATOM   6124 C C   . PHE B 1 245 ? -25.053 16.672 32.289  1.00 30.52  ? 245 PHE B C   1 
ATOM   6125 O O   . PHE B 1 245 ? -24.646 16.518 33.445  1.00 33.35  ? 245 PHE B O   1 
ATOM   6126 C CB  . PHE B 1 245 ? -25.354 19.149 32.323  1.00 23.59  ? 245 PHE B CB  1 
ATOM   6127 C CG  . PHE B 1 245 ? -24.900 20.490 31.819  1.00 27.24  ? 245 PHE B CG  1 
ATOM   6128 C CD1 . PHE B 1 245 ? -23.637 20.973 32.130  1.00 30.38  ? 245 PHE B CD1 1 
ATOM   6129 C CD2 . PHE B 1 245 ? -25.730 21.267 31.024  1.00 27.57  ? 245 PHE B CD2 1 
ATOM   6130 C CE1 . PHE B 1 245 ? -23.212 22.221 31.659  1.00 31.83  ? 245 PHE B CE1 1 
ATOM   6131 C CE2 . PHE B 1 245 ? -25.308 22.506 30.547  1.00 28.32  ? 245 PHE B CE2 1 
ATOM   6132 C CZ  . PHE B 1 245 ? -24.049 22.979 30.864  1.00 29.05  ? 245 PHE B CZ  1 
ATOM   6133 N N   . GLY B 1 246 ? -25.747 15.731 31.655  1.00 40.63  ? 246 GLY B N   1 
ATOM   6134 C CA  . GLY B 1 246 ? -26.106 14.503 32.348  1.00 41.27  ? 246 GLY B CA  1 
ATOM   6135 C C   . GLY B 1 246 ? -27.016 14.723 33.536  1.00 41.63  ? 246 GLY B C   1 
ATOM   6136 O O   . GLY B 1 246 ? -26.932 13.986 34.523  1.00 43.90  ? 246 GLY B O   1 
ATOM   6137 N N   . GLU B 1 247 ? -27.874 15.736 33.471  1.00 39.85  ? 247 GLU B N   1 
ATOM   6138 C CA  . GLU B 1 247 ? -28.814 16.061 34.534  1.00 43.27  ? 247 GLU B CA  1 
ATOM   6139 C C   . GLU B 1 247 ? -30.025 16.717 33.900  1.00 33.85  ? 247 GLU B C   1 
ATOM   6140 O O   . GLU B 1 247 ? -29.900 17.431 32.903  1.00 27.62  ? 247 GLU B O   1 
ATOM   6141 C CB  . GLU B 1 247 ? -28.221 17.029 35.573  1.00 51.52  ? 247 GLU B CB  1 
ATOM   6142 C CG  . GLU B 1 247 ? -27.332 16.413 36.629  1.00 58.74  ? 247 GLU B CG  1 
ATOM   6143 C CD  . GLU B 1 247 ? -26.965 17.413 37.715  1.00 62.68  ? 247 GLU B CD  1 
ATOM   6144 O OE1 . GLU B 1 247 ? -25.974 17.178 38.438  1.00 64.59  ? 247 GLU B OE1 1 
ATOM   6145 O OE2 . GLU B 1 247 ? -27.674 18.436 37.846  1.00 64.91  ? 247 GLU B OE2 1 
ATOM   6146 N N   . HIS B 1 248 ? -31.195 16.478 34.483  1.00 34.69  ? 248 HIS B N   1 
ATOM   6147 C CA  . HIS B 1 248 ? -32.331 17.272 34.036  1.00 35.60  ? 248 HIS B CA  1 
ATOM   6148 C C   . HIS B 1 248 ? -32.303 18.640 34.721  1.00 39.33  ? 248 HIS B C   1 
ATOM   6149 O O   . HIS B 1 248 ? -31.908 18.743 35.888  1.00 38.77  ? 248 HIS B O   1 
ATOM   6150 C CB  . HIS B 1 248 ? -33.642 16.547 34.331  1.00 37.27  ? 248 HIS B CB  1 
ATOM   6151 C CG  . HIS B 1 248 ? -33.834 15.305 33.515  1.00 48.57  ? 248 HIS B CG  1 
ATOM   6152 N ND1 . HIS B 1 248 ? -33.540 14.044 33.994  1.00 52.38  ? 248 HIS B ND1 1 
ATOM   6153 C CD2 . HIS B 1 248 ? -34.271 15.132 32.245  1.00 50.06  ? 248 HIS B CD2 1 
ATOM   6154 C CE1 . HIS B 1 248 ? -33.798 13.148 33.058  1.00 50.88  ? 248 HIS B CE1 1 
ATOM   6155 N NE2 . HIS B 1 248 ? -34.241 13.782 31.986  1.00 50.32  ? 248 HIS B NE2 1 
ATOM   6156 N N   . PRO B 1 249 ? -32.696 19.706 34.020  1.00 34.53  ? 249 PRO B N   1 
ATOM   6157 C CA  . PRO B 1 249 ? -32.574 21.055 34.596  1.00 30.38  ? 249 PRO B CA  1 
ATOM   6158 C C   . PRO B 1 249 ? -33.610 21.270 35.689  1.00 29.81  ? 249 PRO B C   1 
ATOM   6159 O O   . PRO B 1 249 ? -34.812 21.090 35.473  1.00 26.60  ? 249 PRO B O   1 
ATOM   6160 C CB  . PRO B 1 249 ? -32.813 21.979 33.395  1.00 26.52  ? 249 PRO B CB  1 
ATOM   6161 C CG  . PRO B 1 249 ? -33.695 21.179 32.484  1.00 27.29  ? 249 PRO B CG  1 
ATOM   6162 C CD  . PRO B 1 249 ? -33.322 19.722 32.684  1.00 31.06  ? 249 PRO B CD  1 
ATOM   6163 N N   . VAL B 1 250 ? -33.130 21.638 36.873  1.00 28.27  ? 250 VAL B N   1 
ATOM   6164 C CA  . VAL B 1 250 ? -34.019 22.003 37.970  1.00 31.65  ? 250 VAL B CA  1 
ATOM   6165 C C   . VAL B 1 250 ? -34.416 23.478 37.918  1.00 28.42  ? 250 VAL B C   1 
ATOM   6166 O O   . VAL B 1 250 ? -35.467 23.849 38.457  1.00 27.41  ? 250 VAL B O   1 
ATOM   6167 C CB  . VAL B 1 250 ? -33.366 21.679 39.326  1.00 37.98  ? 250 VAL B CB  1 
ATOM   6168 C CG1 . VAL B 1 250 ? -34.412 21.572 40.412  1.00 45.52  ? 250 VAL B CG1 1 
ATOM   6169 C CG2 . VAL B 1 250 ? -32.572 20.379 39.236  1.00 37.77  ? 250 VAL B CG2 1 
ATOM   6170 N N   . TYR B 1 251 ? -33.600 24.328 37.304  1.00 25.19  ? 251 TYR B N   1 
ATOM   6171 C CA  . TYR B 1 251 ? -33.892 25.743 37.167  1.00 29.84  ? 251 TYR B CA  1 
ATOM   6172 C C   . TYR B 1 251 ? -33.986 26.080 35.693  1.00 24.56  ? 251 TYR B C   1 
ATOM   6173 O O   . TYR B 1 251 ? -33.208 25.579 34.881  1.00 25.85  ? 251 TYR B O   1 
ATOM   6174 C CB  . TYR B 1 251 ? -32.814 26.631 37.795  1.00 36.24  ? 251 TYR B CB  1 
ATOM   6175 C CG  . TYR B 1 251 ? -32.239 26.045 39.035  1.00 36.29  ? 251 TYR B CG  1 
ATOM   6176 C CD1 . TYR B 1 251 ? -33.022 25.901 40.169  1.00 44.60  ? 251 TYR B CD1 1 
ATOM   6177 C CD2 . TYR B 1 251 ? -30.926 25.599 39.071  1.00 47.42  ? 251 TYR B CD2 1 
ATOM   6178 C CE1 . TYR B 1 251 ? -32.507 25.350 41.309  1.00 54.79  ? 251 TYR B CE1 1 
ATOM   6179 C CE2 . TYR B 1 251 ? -30.398 25.041 40.213  1.00 54.50  ? 251 TYR B CE2 1 
ATOM   6180 C CZ  . TYR B 1 251 ? -31.197 24.920 41.326  1.00 61.43  ? 251 TYR B CZ  1 
ATOM   6181 O OH  . TYR B 1 251 ? -30.691 24.357 42.461  1.00 70.06  ? 251 TYR B OH  1 
ATOM   6182 N N   . MET B 1 252 ? -34.953 26.919 35.365  1.00 21.81  ? 252 MET B N   1 
ATOM   6183 C CA  . MET B 1 252 ? -35.028 27.519 34.049  1.00 21.66  ? 252 MET B CA  1 
ATOM   6184 C C   . MET B 1 252 ? -35.155 29.022 34.185  1.00 20.83  ? 252 MET B C   1 
ATOM   6185 O O   . MET B 1 252 ? -35.784 29.524 35.121  1.00 23.04  ? 252 MET B O   1 
ATOM   6186 C CB  . MET B 1 252 ? -36.209 26.994 33.238  1.00 23.06  ? 252 MET B CB  1 
ATOM   6187 C CG  . MET B 1 252 ? -35.916 25.683 32.572  1.00 30.75  ? 252 MET B CG  1 
ATOM   6188 S SD  . MET B 1 252 ? -37.395 25.025 31.801  1.00 39.77  ? 252 MET B SD  1 
ATOM   6189 C CE  . MET B 1 252 ? -37.070 25.239 30.091  1.00 36.59  ? 252 MET B CE  1 
ATOM   6190 N N   . TRP B 1 253 ? -34.539 29.731 33.243  1.00 25.62  ? 253 TRP B N   1 
ATOM   6191 C CA  . TRP B 1 253 ? -34.825 31.137 33.026  1.00 19.16  ? 253 TRP B CA  1 
ATOM   6192 C C   . TRP B 1 253 ? -35.919 31.268 31.973  1.00 22.44  ? 253 TRP B C   1 
ATOM   6193 O O   . TRP B 1 253 ? -35.713 30.846 30.827  1.00 20.90  ? 253 TRP B O   1 
ATOM   6194 C CB  . TRP B 1 253 ? -33.568 31.873 32.577  1.00 26.81  ? 253 TRP B CB  1 
ATOM   6195 C CG  . TRP B 1 253 ? -33.848 33.256 32.097  1.00 21.90  ? 253 TRP B CG  1 
ATOM   6196 C CD1 . TRP B 1 253 ? -33.733 33.722 30.825  1.00 24.40  ? 253 TRP B CD1 1 
ATOM   6197 C CD2 . TRP B 1 253 ? -34.290 34.362 32.893  1.00 25.73  ? 253 TRP B CD2 1 
ATOM   6198 N NE1 . TRP B 1 253 ? -34.082 35.053 30.773  1.00 26.36  ? 253 TRP B NE1 1 
ATOM   6199 C CE2 . TRP B 1 253 ? -34.431 35.469 32.028  1.00 27.45  ? 253 TRP B CE2 1 
ATOM   6200 C CE3 . TRP B 1 253 ? -34.588 34.522 34.251  1.00 22.65  ? 253 TRP B CE3 1 
ATOM   6201 C CZ2 . TRP B 1 253 ? -34.854 36.721 32.475  1.00 25.82  ? 253 TRP B CZ2 1 
ATOM   6202 C CZ3 . TRP B 1 253 ? -35.020 35.777 34.697  1.00 25.13  ? 253 TRP B CZ3 1 
ATOM   6203 C CH2 . TRP B 1 253 ? -35.140 36.855 33.814  1.00 24.60  ? 253 TRP B CH2 1 
ATOM   6204 N N   . PRO B 1 254 ? -37.086 31.805 32.313  1.00 20.99  ? 254 PRO B N   1 
ATOM   6205 C CA  . PRO B 1 254 ? -38.111 32.053 31.305  1.00 18.35  ? 254 PRO B CA  1 
ATOM   6206 C C   . PRO B 1 254 ? -37.698 33.177 30.373  1.00 20.85  ? 254 PRO B C   1 
ATOM   6207 O O   . PRO B 1 254 ? -37.319 34.266 30.826  1.00 20.74  ? 254 PRO B O   1 
ATOM   6208 C CB  . PRO B 1 254 ? -39.348 32.442 32.134  1.00 35.54  ? 254 PRO B CB  1 
ATOM   6209 C CG  . PRO B 1 254 ? -38.807 32.916 33.420  1.00 30.97  ? 254 PRO B CG  1 
ATOM   6210 C CD  . PRO B 1 254 ? -37.557 32.115 33.674  1.00 26.32  ? 254 PRO B CD  1 
ATOM   6211 N N   . PRO B 1 255 ? -37.770 32.946 29.064  1.00 17.98  ? 255 PRO B N   1 
ATOM   6212 C CA  . PRO B 1 255 ? -37.341 33.961 28.095  1.00 17.67  ? 255 PRO B CA  1 
ATOM   6213 C C   . PRO B 1 255 ? -38.037 35.291 28.336  1.00 23.11  ? 255 PRO B C   1 
ATOM   6214 O O   . PRO B 1 255 ? -39.263 35.352 28.517  1.00 23.06  ? 255 PRO B O   1 
ATOM   6215 C CB  . PRO B 1 255 ? -37.744 33.347 26.751  1.00 23.12  ? 255 PRO B CB  1 
ATOM   6216 C CG  . PRO B 1 255 ? -37.703 31.862 26.996  1.00 22.24  ? 255 PRO B CG  1 
ATOM   6217 C CD  . PRO B 1 255 ? -38.155 31.679 28.418  1.00 25.34  ? 255 PRO B CD  1 
ATOM   6218 N N   . GLU B 1 256 ? -37.235 36.356 28.349  1.00 22.39  ? 256 GLU B N   1 
ATOM   6219 C CA  . GLU B 1 256 ? -37.706 37.719 28.594  1.00 22.14  ? 256 GLU B CA  1 
ATOM   6220 C C   . GLU B 1 256 ? -38.364 37.848 29.965  1.00 23.06  ? 256 GLU B C   1 
ATOM   6221 O O   . GLU B 1 256 ? -39.205 38.730 30.178  1.00 23.36  ? 256 GLU B O   1 
ATOM   6222 C CB  . GLU B 1 256 ? -38.660 38.186 27.484  1.00 21.63  ? 256 GLU B CB  1 
ATOM   6223 C CG  . GLU B 1 256 ? -38.201 37.829 26.082  1.00 21.98  ? 256 GLU B CG  1 
ATOM   6224 C CD  . GLU B 1 256 ? -36.978 38.615 25.643  1.00 25.63  ? 256 GLU B CD  1 
ATOM   6225 O OE1 . GLU B 1 256 ? -36.624 39.589 26.329  1.00 30.04  ? 256 GLU B OE1 1 
ATOM   6226 O OE2 . GLU B 1 256 ? -36.388 38.280 24.593  1.00 26.96  ? 256 GLU B OE2 1 
ATOM   6227 N N   . ALA B 1 257 ? -37.990 36.961 30.898  1.00 22.60  ? 257 ALA B N   1 
ATOM   6228 C CA  . ALA B 1 257 ? -38.564 36.901 32.243  1.00 19.54  ? 257 ALA B CA  1 
ATOM   6229 C C   . ALA B 1 257 ? -40.073 36.682 32.219  1.00 24.36  ? 257 ALA B C   1 
ATOM   6230 O O   . ALA B 1 257 ? -40.773 36.996 33.192  1.00 22.02  ? 257 ALA B O   1 
ATOM   6231 C CB  . ALA B 1 257 ? -38.232 38.166 33.049  1.00 25.97  ? 257 ALA B CB  1 
ATOM   6232 N N   . SER B 1 258 ? -40.595 36.141 31.125  1.00 23.62  ? 258 SER B N   1 
ATOM   6233 C CA  . SER B 1 258 ? -42.031 36.136 30.908  1.00 27.24  ? 258 SER B CA  1 
ATOM   6234 C C   . SER B 1 258 ? -42.696 35.046 31.731  1.00 26.69  ? 258 SER B C   1 
ATOM   6235 O O   . SER B 1 258 ? -42.359 33.863 31.606  1.00 24.27  ? 258 SER B O   1 
ATOM   6236 C CB  . SER B 1 258 ? -42.363 35.941 29.437  1.00 26.02  ? 258 SER B CB  1 
ATOM   6237 O OG  . SER B 1 258 ? -43.747 36.138 29.272  1.00 33.02  ? 258 SER B OG  1 
ATOM   6238 N N   . VAL B 1 259 ? -43.668 35.443 32.542  1.00 23.24  ? 259 VAL B N   1 
ATOM   6239 C CA  . VAL B 1 259 ? -44.467 34.501 33.301  1.00 21.48  ? 259 VAL B CA  1 
ATOM   6240 C C   . VAL B 1 259 ? -45.932 34.870 33.136  1.00 24.16  ? 259 VAL B C   1 
ATOM   6241 O O   . VAL B 1 259 ? -46.279 35.967 32.688  1.00 22.44  ? 259 VAL B O   1 
ATOM   6242 C CB  . VAL B 1 259 ? -44.072 34.471 34.792  1.00 27.51  ? 259 VAL B CB  1 
ATOM   6243 C CG1 . VAL B 1 259 ? -42.653 33.879 34.944  1.00 23.34  ? 259 VAL B CG1 1 
ATOM   6244 C CG2 . VAL B 1 259 ? -44.134 35.875 35.384  1.00 25.10  ? 259 VAL B CG2 1 
ATOM   6245 N N   . SER B 1 260 ? -46.778 33.892 33.449  1.00 21.73  ? 260 SER B N   1 
ATOM   6246 C CA  . SER B 1 260 ? -48.219 34.000 33.578  1.00 21.90  ? 260 SER B CA  1 
ATOM   6247 C C   . SER B 1 260 ? -48.619 32.880 34.532  1.00 27.89  ? 260 SER B C   1 
ATOM   6248 O O   . SER B 1 260 ? -47.831 31.966 34.791  1.00 23.74  ? 260 SER B O   1 
ATOM   6249 C CB  . SER B 1 260 ? -48.927 33.855 32.225  1.00 26.33  ? 260 SER B CB  1 
ATOM   6250 O OG  . SER B 1 260 ? -48.808 32.522 31.728  1.00 28.08  ? 260 SER B OG  1 
ATOM   6251 N N   . ASN B 1 261 ? -49.833 32.962 35.076  1.00 23.86  ? 261 ASN B N   1 
ATOM   6252 C CA  . ASN B 1 261 ? -50.295 31.881 35.940  1.00 18.10  ? 261 ASN B CA  1 
ATOM   6253 C C   . ASN B 1 261 ? -50.234 30.542 35.202  1.00 28.85  ? 261 ASN B C   1 
ATOM   6254 O O   . ASN B 1 261 ? -49.827 29.523 35.776  1.00 26.13  ? 261 ASN B O   1 
ATOM   6255 C CB  . ASN B 1 261 ? -51.720 32.161 36.437  1.00 26.89  ? 261 ASN B CB  1 
ATOM   6256 C CG  . ASN B 1 261 ? -51.794 33.322 37.435  1.00 31.15  ? 261 ASN B CG  1 
ATOM   6257 O OD1 . ASN B 1 261 ? -50.805 33.681 38.081  1.00 27.47  ? 261 ASN B OD1 1 
ATOM   6258 N ND2 . ASN B 1 261 ? -52.982 33.908 37.561  1.00 33.36  ? 261 ASN B ND2 1 
ATOM   6259 N N   . GLU B 1 262 ? -50.612 30.536 33.915  1.00 22.01  ? 262 GLU B N   1 
ATOM   6260 C CA  . GLU B 1 262 ? -50.561 29.311 33.121  1.00 29.22  ? 262 GLU B CA  1 
ATOM   6261 C C   . GLU B 1 262 ? -49.125 28.872 32.840  1.00 25.91  ? 262 GLU B C   1 
ATOM   6262 O O   . GLU B 1 262 ? -48.825 27.674 32.867  1.00 28.94  ? 262 GLU B O   1 
ATOM   6263 C CB  . GLU B 1 262 ? -51.316 29.504 31.807  1.00 34.59  ? 262 GLU B CB  1 
ATOM   6264 C CG  . GLU B 1 262 ? -52.809 29.178 31.867  1.00 39.91  ? 262 GLU B CG  1 
ATOM   6265 C CD  . GLU B 1 262 ? -53.519 29.510 30.561  1.00 41.17  ? 262 GLU B CD  1 
ATOM   6266 O OE1 . GLU B 1 262 ? -53.299 28.796 29.561  1.00 39.64  ? 262 GLU B OE1 1 
ATOM   6267 O OE2 . GLU B 1 262 ? -54.280 30.499 30.529  1.00 44.26  ? 262 GLU B OE2 1 
ATOM   6268 N N   . ALA B 1 263 ? -48.225 29.813 32.542  1.00 21.89  ? 263 ALA B N   1 
ATOM   6269 C CA  . ALA B 1 263 ? -46.843 29.417 32.268  1.00 19.86  ? 263 ALA B CA  1 
ATOM   6270 C C   . ALA B 1 263 ? -46.180 28.806 33.501  1.00 26.74  ? 263 ALA B C   1 
ATOM   6271 O O   . ALA B 1 263 ? -45.449 27.810 33.390  1.00 25.32  ? 263 ALA B O   1 
ATOM   6272 C CB  . ALA B 1 263 ? -46.035 30.606 31.758  1.00 18.27  ? 263 ALA B CB  1 
ATOM   6273 N N   . LEU B 1 264 ? -46.412 29.389 34.680  1.00 28.73  ? 264 LEU B N   1 
ATOM   6274 C CA  . LEU B 1 264 ? -45.817 28.842 35.895  1.00 26.82  ? 264 LEU B CA  1 
ATOM   6275 C C   . LEU B 1 264 ? -46.307 27.420 36.146  1.00 27.48  ? 264 LEU B C   1 
ATOM   6276 O O   . LEU B 1 264 ? -45.539 26.565 36.602  1.00 22.09  ? 264 LEU B O   1 
ATOM   6277 C CB  . LEU B 1 264 ? -46.125 29.740 37.100  1.00 27.22  ? 264 LEU B CB  1 
ATOM   6278 C CG  . LEU B 1 264 ? -45.421 31.111 37.081  1.00 27.91  ? 264 LEU B CG  1 
ATOM   6279 C CD1 . LEU B 1 264 ? -46.058 32.074 38.062  1.00 24.20  ? 264 LEU B CD1 1 
ATOM   6280 C CD2 . LEU B 1 264 ? -43.915 30.981 37.358  1.00 24.23  ? 264 LEU B CD2 1 
ATOM   6281 N N   . GLU B 1 265 ? -47.588 27.154 35.861  1.00 27.90  ? 265 GLU B N   1 
ATOM   6282 C CA  . GLU B 1 265 ? -48.111 25.795 35.984  1.00 28.80  ? 265 GLU B CA  1 
ATOM   6283 C C   . GLU B 1 265 ? -47.387 24.845 35.038  1.00 26.26  ? 265 GLU B C   1 
ATOM   6284 O O   . GLU B 1 265 ? -47.083 23.708 35.404  1.00 28.46  ? 265 GLU B O   1 
ATOM   6285 C CB  . GLU B 1 265 ? -49.617 25.775 35.705  1.00 28.77  ? 265 GLU B CB  1 
ATOM   6286 C CG  . GLU B 1 265 ? -50.457 26.481 36.753  1.00 43.13  ? 265 GLU B CG  1 
ATOM   6287 C CD  . GLU B 1 265 ? -51.941 26.170 36.622  1.00 54.33  ? 265 GLU B CD  1 
ATOM   6288 O OE1 . GLU B 1 265 ? -52.344 25.557 35.608  1.00 60.04  ? 265 GLU B OE1 1 
ATOM   6289 O OE2 . GLU B 1 265 ? -52.708 26.537 37.535  1.00 59.06  ? 265 GLU B OE2 1 
ATOM   6290 N N   . LEU B 1 266 ? -47.110 25.294 33.815  1.00 27.42  ? 266 LEU B N   1 
ATOM   6291 C CA  . LEU B 1 266 ? -46.415 24.434 32.862  1.00 26.79  ? 266 LEU B CA  1 
ATOM   6292 C C   . LEU B 1 266 ? -44.994 24.121 33.326  1.00 26.89  ? 266 LEU B C   1 
ATOM   6293 O O   . LEU B 1 266 ? -44.568 22.963 33.270  1.00 32.29  ? 266 LEU B O   1 
ATOM   6294 C CB  . LEU B 1 266 ? -46.400 25.073 31.476  1.00 27.94  ? 266 LEU B CB  1 
ATOM   6295 C CG  . LEU B 1 266 ? -45.550 24.346 30.435  1.00 30.47  ? 266 LEU B CG  1 
ATOM   6296 C CD1 . LEU B 1 266 ? -46.171 22.999 30.073  1.00 25.27  ? 266 LEU B CD1 1 
ATOM   6297 C CD2 . LEU B 1 266 ? -45.349 25.206 29.196  1.00 32.03  ? 266 LEU B CD2 1 
ATOM   6298 N N   . TYR B 1 267 ? -44.249 25.129 33.800  1.00 23.34  ? 267 TYR B N   1 
ATOM   6299 C CA  . TYR B 1 267 ? -42.910 24.865 34.333  1.00 25.13  ? 267 TYR B CA  1 
ATOM   6300 C C   . TYR B 1 267 ? -42.970 23.875 35.493  1.00 27.64  ? 267 TYR B C   1 
ATOM   6301 O O   . TYR B 1 267 ? -42.158 22.949 35.572  1.00 27.72  ? 267 TYR B O   1 
ATOM   6302 C CB  . TYR B 1 267 ? -42.243 26.167 34.782  1.00 25.15  ? 267 TYR B CB  1 
ATOM   6303 C CG  . TYR B 1 267 ? -41.773 27.045 33.646  1.00 26.03  ? 267 TYR B CG  1 
ATOM   6304 C CD1 . TYR B 1 267 ? -40.722 26.648 32.819  1.00 25.98  ? 267 TYR B CD1 1 
ATOM   6305 C CD2 . TYR B 1 267 ? -42.366 28.274 33.406  1.00 27.21  ? 267 TYR B CD2 1 
ATOM   6306 C CE1 . TYR B 1 267 ? -40.293 27.443 31.785  1.00 30.06  ? 267 TYR B CE1 1 
ATOM   6307 C CE2 . TYR B 1 267 ? -41.939 29.084 32.365  1.00 30.02  ? 267 TYR B CE2 1 
ATOM   6308 C CZ  . TYR B 1 267 ? -40.904 28.662 31.557  1.00 27.71  ? 267 TYR B CZ  1 
ATOM   6309 O OH  . TYR B 1 267 ? -40.479 29.465 30.525  1.00 28.22  ? 267 TYR B OH  1 
ATOM   6310 N N   . TYR B 1 268 ? -43.947 24.049 36.389  1.00 27.66  ? 268 TYR B N   1 
ATOM   6311 C CA  . TYR B 1 268 ? -44.121 23.136 37.517  1.00 25.54  ? 268 TYR B CA  1 
ATOM   6312 C C   . TYR B 1 268 ? -44.413 21.712 37.043  1.00 28.60  ? 268 TYR B C   1 
ATOM   6313 O O   . TYR B 1 268 ? -43.832 20.746 37.554  1.00 23.72  ? 268 TYR B O   1 
ATOM   6314 C CB  . TYR B 1 268 ? -45.255 23.647 38.417  1.00 25.57  ? 268 TYR B CB  1 
ATOM   6315 C CG  . TYR B 1 268 ? -45.911 22.570 39.252  1.00 34.86  ? 268 TYR B CG  1 
ATOM   6316 C CD1 . TYR B 1 268 ? -45.259 22.027 40.352  1.00 38.04  ? 268 TYR B CD1 1 
ATOM   6317 C CD2 . TYR B 1 268 ? -47.183 22.097 38.945  1.00 40.99  ? 268 TYR B CD2 1 
ATOM   6318 C CE1 . TYR B 1 268 ? -45.848 21.043 41.121  1.00 39.26  ? 268 TYR B CE1 1 
ATOM   6319 C CE2 . TYR B 1 268 ? -47.785 21.104 39.716  1.00 39.20  ? 268 TYR B CE2 1 
ATOM   6320 C CZ  . TYR B 1 268 ? -47.109 20.583 40.798  1.00 40.01  ? 268 TYR B CZ  1 
ATOM   6321 O OH  . TYR B 1 268 ? -47.698 19.601 41.564  1.00 42.20  ? 268 TYR B OH  1 
ATOM   6322 N N   . GLU B 1 269 ? -45.303 21.563 36.056  1.00 26.86  ? 269 GLU B N   1 
ATOM   6323 C CA  . GLU B 1 269 ? -45.693 20.226 35.621  1.00 30.39  ? 269 GLU B CA  1 
ATOM   6324 C C   . GLU B 1 269 ? -44.561 19.499 34.909  1.00 31.99  ? 269 GLU B C   1 
ATOM   6325 O O   . GLU B 1 269 ? -44.525 18.266 34.913  1.00 32.54  ? 269 GLU B O   1 
ATOM   6326 C CB  . GLU B 1 269 ? -46.932 20.298 34.734  1.00 34.99  ? 269 GLU B CB  1 
ATOM   6327 C CG  . GLU B 1 269 ? -48.139 20.627 35.578  1.00 47.69  ? 269 GLU B CG  1 
ATOM   6328 C CD  . GLU B 1 269 ? -48.643 19.434 36.375  1.00 64.85  ? 269 GLU B CD  1 
ATOM   6329 O OE1 . GLU B 1 269 ? -49.095 19.616 37.518  1.00 67.26  ? 269 GLU B OE1 1 
ATOM   6330 O OE2 . GLU B 1 269 ? -48.598 18.299 35.818  1.00 73.51  ? 269 GLU B OE2 1 
ATOM   6331 N N   . LYS B 1 270 ? -43.636 20.232 34.304  1.00 26.14  ? 270 LYS B N   1 
ATOM   6332 C CA  . LYS B 1 270 ? -42.490 19.614 33.654  1.00 25.63  ? 270 LYS B CA  1 
ATOM   6333 C C   . LYS B 1 270 ? -41.306 19.420 34.598  1.00 28.17  ? 270 LYS B C   1 
ATOM   6334 O O   . LYS B 1 270 ? -40.203 19.105 34.135  1.00 30.52  ? 270 LYS B O   1 
ATOM   6335 C CB  . LYS B 1 270 ? -42.083 20.446 32.435  1.00 33.01  ? 270 LYS B CB  1 
ATOM   6336 C CG  . LYS B 1 270 ? -43.140 20.453 31.333  1.00 38.15  ? 270 LYS B CG  1 
ATOM   6337 C CD  . LYS B 1 270 ? -43.763 19.069 31.171  1.00 46.92  ? 270 LYS B CD  1 
ATOM   6338 C CE  . LYS B 1 270 ? -44.890 19.066 30.148  1.00 54.07  ? 270 LYS B CE  1 
ATOM   6339 N NZ  . LYS B 1 270 ? -44.379 19.308 28.772  1.00 59.00  ? 270 LYS B NZ  1 
ATOM   6340 N N   . GLY B 1 271 ? -41.503 19.603 35.902  1.00 26.65  ? 271 GLY B N   1 
ATOM   6341 C CA  . GLY B 1 271 ? -40.477 19.300 36.879  1.00 28.86  ? 271 GLY B CA  1 
ATOM   6342 C C   . GLY B 1 271 ? -39.552 20.441 37.254  1.00 27.61  ? 271 GLY B C   1 
ATOM   6343 O O   . GLY B 1 271 ? -38.588 20.208 37.989  1.00 29.50  ? 271 GLY B O   1 
ATOM   6344 N N   . ILE B 1 272 ? -39.809 21.659 36.781  1.00 26.63  ? 272 ILE B N   1 
ATOM   6345 C CA  . ILE B 1 272 ? -38.974 22.805 37.133  1.00 29.36  ? 272 ILE B CA  1 
ATOM   6346 C C   . ILE B 1 272 ? -39.293 23.228 38.567  1.00 30.60  ? 272 ILE B C   1 
ATOM   6347 O O   . ILE B 1 272 ? -40.452 23.480 38.918  1.00 24.75  ? 272 ILE B O   1 
ATOM   6348 C CB  . ILE B 1 272 ? -39.190 23.948 36.131  1.00 28.79  ? 272 ILE B CB  1 
ATOM   6349 C CG1 . ILE B 1 272 ? -38.923 23.444 34.704  1.00 31.80  ? 272 ILE B CG1 1 
ATOM   6350 C CG2 . ILE B 1 272 ? -38.325 25.169 36.449  1.00 23.10  ? 272 ILE B CG2 1 
ATOM   6351 C CD1 . ILE B 1 272 ? -37.683 22.564 34.556  1.00 28.12  ? 272 ILE B CD1 1 
ATOM   6352 N N   . ASN B 1 273 ? -38.262 23.288 39.411  1.00 28.42  ? 273 ASN B N   1 
ATOM   6353 C CA  . ASN B 1 273 ? -38.454 23.623 40.817  1.00 24.77  ? 273 ASN B CA  1 
ATOM   6354 C C   . ASN B 1 273 ? -38.256 25.104 41.107  1.00 24.56  ? 273 ASN B C   1 
ATOM   6355 O O   . ASN B 1 273 ? -38.822 25.616 42.079  1.00 22.51  ? 273 ASN B O   1 
ATOM   6356 C CB  . ASN B 1 273 ? -37.503 22.800 41.693  1.00 30.60  ? 273 ASN B CB  1 
ATOM   6357 C CG  . ASN B 1 273 ? -38.077 22.506 43.072  1.00 46.85  ? 273 ASN B CG  1 
ATOM   6358 O OD1 . ASN B 1 273 ? -39.279 22.294 43.231  1.00 50.59  ? 273 ASN B OD1 1 
ATOM   6359 N ND2 . ASN B 1 273 ? -37.213 22.495 44.077  1.00 55.94  ? 273 ASN B ND2 1 
ATOM   6360 N N   . MET B 1 274 ? -37.477 25.812 40.293  1.00 21.33  ? 274 MET B N   1 
ATOM   6361 C CA  . MET B 1 274 ? -37.296 27.227 40.557  1.00 24.18  ? 274 MET B CA  1 
ATOM   6362 C C   . MET B 1 274 ? -37.134 27.987 39.245  1.00 23.72  ? 274 MET B C   1 
ATOM   6363 O O   . MET B 1 274 ? -36.608 27.465 38.257  1.00 26.63  ? 274 MET B O   1 
ATOM   6364 C CB  . MET B 1 274 ? -36.096 27.448 41.490  1.00 26.59  ? 274 MET B CB  1 
ATOM   6365 C CG  . MET B 1 274 ? -35.978 28.841 42.066  1.00 37.44  ? 274 MET B CG  1 
ATOM   6366 S SD  . MET B 1 274 ? -34.709 29.750 41.175  1.00 52.79  ? 274 MET B SD  1 
ATOM   6367 C CE  . MET B 1 274 ? -33.235 29.010 41.864  1.00 42.34  ? 274 MET B CE  1 
ATOM   6368 N N   . LEU B 1 275 ? -37.607 29.228 39.244  1.00 25.83  ? 275 LEU B N   1 
ATOM   6369 C CA  . LEU B 1 275 ? -37.286 30.155 38.172  1.00 24.42  ? 275 LEU B CA  1 
ATOM   6370 C C   . LEU B 1 275 ? -37.151 31.543 38.775  1.00 24.62  ? 275 LEU B C   1 
ATOM   6371 O O   . LEU B 1 275 ? -37.355 31.750 39.976  1.00 23.18  ? 275 LEU B O   1 
ATOM   6372 C CB  . LEU B 1 275 ? -38.335 30.116 37.051  1.00 27.57  ? 275 LEU B CB  1 
ATOM   6373 C CG  . LEU B 1 275 ? -39.806 30.304 37.422  1.00 33.34  ? 275 LEU B CG  1 
ATOM   6374 C CD1 . LEU B 1 275 ? -40.174 31.774 37.397  1.00 40.31  ? 275 LEU B CD1 1 
ATOM   6375 C CD2 . LEU B 1 275 ? -40.708 29.523 36.469  1.00 30.64  ? 275 LEU B CD2 1 
ATOM   6376 N N   . ALA B 1 276 ? -36.777 32.491 37.934  1.00 22.95  ? 276 ALA B N   1 
ATOM   6377 C CA  . ALA B 1 276 ? -36.778 33.889 38.319  1.00 30.10  ? 276 ALA B CA  1 
ATOM   6378 C C   . ALA B 1 276 ? -37.530 34.678 37.265  1.00 18.21  ? 276 ALA B C   1 
ATOM   6379 O O   . ALA B 1 276 ? -37.729 34.216 36.141  1.00 20.28  ? 276 ALA B O   1 
ATOM   6380 C CB  . ALA B 1 276 ? -35.355 34.449 38.491  1.00 31.62  ? 276 ALA B CB  1 
ATOM   6381 N N   . THR B 1 277 ? -37.971 35.866 37.644  1.00 17.89  ? 277 THR B N   1 
ATOM   6382 C CA  . THR B 1 277 ? -38.637 36.752 36.700  1.00 19.55  ? 277 THR B CA  1 
ATOM   6383 C C   . THR B 1 277 ? -38.339 38.184 37.149  1.00 22.47  ? 277 THR B C   1 
ATOM   6384 O O   . THR B 1 277 ? -37.380 38.414 37.894  1.00 27.33  ? 277 THR B O   1 
ATOM   6385 C CB  . THR B 1 277 ? -40.133 36.391 36.603  1.00 18.83  ? 277 THR B CB  1 
ATOM   6386 O OG1 . THR B 1 277 ? -40.803 37.276 35.696  1.00 21.51  ? 277 THR B OG1 1 
ATOM   6387 C CG2 . THR B 1 277 ? -40.775 36.460 37.959  1.00 20.26  ? 277 THR B CG2 1 
ATOM   6388 N N   . ASP B 1 278 ? -39.150 39.144 36.707  1.00 18.17  ? 278 ASP B N   1 
ATOM   6389 C CA  . ASP B 1 278 ? -38.798 40.553 36.839  1.00 22.19  ? 278 ASP B CA  1 
ATOM   6390 C C   . ASP B 1 278 ? -39.568 41.256 37.955  1.00 21.62  ? 278 ASP B C   1 
ATOM   6391 O O   . ASP B 1 278 ? -40.731 40.945 38.225  1.00 20.22  ? 278 ASP B O   1 
ATOM   6392 C CB  . ASP B 1 278 ? -39.051 41.290 35.530  1.00 19.96  ? 278 ASP B CB  1 
ATOM   6393 C CG  . ASP B 1 278 ? -38.550 42.702 35.583  1.00 24.79  ? 278 ASP B CG  1 
ATOM   6394 O OD1 . ASP B 1 278 ? -37.373 42.884 35.968  1.00 25.30  ? 278 ASP B OD1 1 
ATOM   6395 O OD2 . ASP B 1 278 ? -39.330 43.624 35.290  1.00 27.07  ? 278 ASP B OD2 1 
ATOM   6396 N N   . GLU B 1 279 ? -38.908 42.252 38.569  1.00 22.37  ? 279 GLU B N   1 
ATOM   6397 C CA  . GLU B 1 279 ? -39.503 43.020 39.665  1.00 24.12  ? 279 GLU B CA  1 
ATOM   6398 C C   . GLU B 1 279 ? -40.770 43.765 39.239  1.00 25.48  ? 279 GLU B C   1 
ATOM   6399 O O   . GLU B 1 279 ? -41.679 43.957 40.056  1.00 26.58  ? 279 GLU B O   1 
ATOM   6400 C CB  . GLU B 1 279 ? -38.463 44.000 40.228  1.00 22.87  ? 279 GLU B CB  1 
ATOM   6401 C CG  . GLU B 1 279 ? -38.929 44.818 41.404  1.00 25.63  ? 279 GLU B CG  1 
ATOM   6402 C CD  . GLU B 1 279 ? -37.808 45.634 42.036  1.00 34.85  ? 279 GLU B CD  1 
ATOM   6403 O OE1 . GLU B 1 279 ? -36.709 45.725 41.439  1.00 37.81  ? 279 GLU B OE1 1 
ATOM   6404 O OE2 . GLU B 1 279 ? -38.023 46.182 43.138  1.00 34.85  ? 279 GLU B OE2 1 
ATOM   6405 N N   . VAL B 1 280 ? -40.864 44.192 37.978  1.00 26.66  ? 280 VAL B N   1 
ATOM   6406 C CA  . VAL B 1 280 ? -42.080 44.883 37.542  1.00 27.37  ? 280 VAL B CA  1 
ATOM   6407 C C   . VAL B 1 280 ? -43.277 43.943 37.628  1.00 26.21  ? 280 VAL B C   1 
ATOM   6408 O O   . VAL B 1 280 ? -44.364 44.331 38.078  1.00 26.86  ? 280 VAL B O   1 
ATOM   6409 C CB  . VAL B 1 280 ? -41.897 45.462 36.123  1.00 29.36  ? 280 VAL B CB  1 
ATOM   6410 C CG1 . VAL B 1 280 ? -43.221 45.919 35.545  1.00 25.43  ? 280 VAL B CG1 1 
ATOM   6411 C CG2 . VAL B 1 280 ? -40.914 46.619 36.151  1.00 35.44  ? 280 VAL B CG2 1 
ATOM   6412 N N   . ILE B 1 281 ? -43.084 42.683 37.236  1.00 26.07  ? 281 ILE B N   1 
ATOM   6413 C CA  . ILE B 1 281 ? -44.134 41.674 37.372  1.00 25.59  ? 281 ILE B CA  1 
ATOM   6414 C C   . ILE B 1 281 ? -44.503 41.482 38.839  1.00 23.99  ? 281 ILE B C   1 
ATOM   6415 O O   . ILE B 1 281 ? -45.689 41.387 39.195  1.00 22.17  ? 281 ILE B O   1 
ATOM   6416 C CB  . ILE B 1 281 ? -43.679 40.355 36.720  1.00 30.88  ? 281 ILE B CB  1 
ATOM   6417 C CG1 . ILE B 1 281 ? -43.588 40.535 35.201  1.00 23.97  ? 281 ILE B CG1 1 
ATOM   6418 C CG2 . ILE B 1 281 ? -44.610 39.194 37.112  1.00 35.75  ? 281 ILE B CG2 1 
ATOM   6419 C CD1 . ILE B 1 281 ? -42.975 39.351 34.477  1.00 27.81  ? 281 ILE B CD1 1 
ATOM   6420 N N   . LEU B 1 282 ? -43.499 41.437 39.715  1.00 22.03  ? 282 LEU B N   1 
ATOM   6421 C CA  . LEU B 1 282 ? -43.775 41.389 41.148  1.00 25.63  ? 282 LEU B CA  1 
ATOM   6422 C C   . LEU B 1 282 ? -44.653 42.560 41.582  1.00 26.07  ? 282 LEU B C   1 
ATOM   6423 O O   . LEU B 1 282 ? -45.670 42.372 42.263  1.00 28.40  ? 282 LEU B O   1 
ATOM   6424 C CB  . LEU B 1 282 ? -42.470 41.389 41.934  1.00 24.26  ? 282 LEU B CB  1 
ATOM   6425 C CG  . LEU B 1 282 ? -42.669 41.301 43.446  1.00 27.98  ? 282 LEU B CG  1 
ATOM   6426 C CD1 . LEU B 1 282 ? -43.465 40.072 43.831  1.00 29.99  ? 282 LEU B CD1 1 
ATOM   6427 C CD2 . LEU B 1 282 ? -41.322 41.328 44.190  1.00 27.91  ? 282 LEU B CD2 1 
ATOM   6428 N N   . LYS B 1 283 ? -44.273 43.780 41.196  1.00 25.70  ? 283 LYS B N   1 
ATOM   6429 C CA  . LYS B 1 283 ? -45.049 44.949 41.595  1.00 28.90  ? 283 LYS B CA  1 
ATOM   6430 C C   . LYS B 1 283 ? -46.461 44.891 41.026  1.00 31.45  ? 283 LYS B C   1 
ATOM   6431 O O   . LYS B 1 283 ? -47.429 45.215 41.723  1.00 29.56  ? 283 LYS B O   1 
ATOM   6432 C CB  . LYS B 1 283 ? -44.340 46.230 41.155  1.00 35.28  ? 283 LYS B CB  1 
ATOM   6433 C CG  . LYS B 1 283 ? -42.929 46.399 41.726  1.00 38.93  ? 283 LYS B CG  1 
ATOM   6434 C CD  . LYS B 1 283 ? -42.864 45.976 43.183  1.00 42.56  ? 283 LYS B CD  1 
ATOM   6435 C CE  . LYS B 1 283 ? -42.357 47.108 44.062  1.00 48.81  ? 283 LYS B CE  1 
ATOM   6436 N NZ  . LYS B 1 283 ? -42.165 46.663 45.473  1.00 52.17  ? 283 LYS B NZ  1 
ATOM   6437 N N   . ASN B 1 284 ? -46.593 44.475 39.762  1.00 20.68  ? 284 ASN B N   1 
ATOM   6438 C CA  . ASN B 1 284 ? -47.894 44.324 39.121  1.00 29.74  ? 284 ASN B CA  1 
ATOM   6439 C C   . ASN B 1 284 ? -48.747 43.230 39.754  1.00 33.15  ? 284 ASN B C   1 
ATOM   6440 O O   . ASN B 1 284 ? -49.965 43.226 39.553  1.00 34.19  ? 284 ASN B O   1 
ATOM   6441 C CB  . ASN B 1 284 ? -47.711 44.019 37.634  1.00 30.65  ? 284 ASN B CB  1 
ATOM   6442 C CG  . ASN B 1 284 ? -47.245 45.224 36.843  1.00 34.19  ? 284 ASN B CG  1 
ATOM   6443 O OD1 . ASN B 1 284 ? -47.150 46.323 37.377  1.00 33.92  ? 284 ASN B OD1 1 
ATOM   6444 N ND2 . ASN B 1 284 ? -46.949 45.020 35.563  1.00 32.69  ? 284 ASN B ND2 1 
ATOM   6445 N N   . SER B 1 285 ? -48.143 42.302 40.492  1.00 31.74  ? 285 SER B N   1 
ATOM   6446 C CA  . SER B 1 285 ? -48.848 41.122 40.983  1.00 32.85  ? 285 SER B CA  1 
ATOM   6447 C C   . SER B 1 285 ? -49.100 41.138 42.479  1.00 35.12  ? 285 SER B C   1 
ATOM   6448 O O   . SER B 1 285 ? -50.128 40.634 42.926  1.00 34.89  ? 285 SER B O   1 
ATOM   6449 C CB  . SER B 1 285 ? -48.071 39.845 40.627  1.00 29.99  ? 285 SER B CB  1 
ATOM   6450 O OG  . SER B 1 285 ? -47.733 39.782 39.247  1.00 24.62  ? 285 SER B OG  1 
ATOM   6451 N N   . VAL B 1 286 ? -48.185 41.690 43.272  1.00 34.21  ? 286 VAL B N   1 
ATOM   6452 C CA  . VAL B 1 286 ? -48.278 41.685 44.726  1.00 32.21  ? 286 VAL B CA  1 
ATOM   6453 C C   . VAL B 1 286 ? -48.137 43.115 45.216  1.00 34.64  ? 286 VAL B C   1 
ATOM   6454 O O   . VAL B 1 286 ? -47.233 43.834 44.785  1.00 37.90  ? 286 VAL B O   1 
ATOM   6455 C CB  . VAL B 1 286 ? -47.191 40.805 45.367  1.00 33.39  ? 286 VAL B CB  1 
ATOM   6456 C CG1 . VAL B 1 286 ? -47.414 40.694 46.871  1.00 36.99  ? 286 VAL B CG1 1 
ATOM   6457 C CG2 . VAL B 1 286 ? -47.154 39.448 44.707  1.00 30.42  ? 286 VAL B CG2 1 
ATOM   6458 N N   . GLU B 1 287 ? -49.001 43.523 46.140  1.00 39.34  ? 287 GLU B N   1 
ATOM   6459 C CA  . GLU B 1 287 ? -49.022 44.933 46.514  1.00 44.85  ? 287 GLU B CA  1 
ATOM   6460 C C   . GLU B 1 287 ? -47.796 45.303 47.334  1.00 40.94  ? 287 GLU B C   1 
ATOM   6461 O O   . GLU B 1 287 ? -47.077 46.256 47.006  1.00 44.34  ? 287 GLU B O   1 
ATOM   6462 C CB  . GLU B 1 287 ? -50.353 45.267 47.238  1.00 51.98  ? 287 GLU B CB  1 
ATOM   6463 C CG  . GLU B 1 287 ? -50.271 45.338 48.799  1.00 58.76  ? 287 GLU B CG  1 
ATOM   6464 C CD  . GLU B 1 287 ? -51.572 45.745 49.422  1.00 68.06  ? 287 GLU B CD  1 
ATOM   6465 O OE1 . GLU B 1 287 ? -51.773 45.502 50.648  1.00 73.50  ? 287 GLU B OE1 1 
ATOM   6466 O OE2 . GLU B 1 287 ? -52.349 46.307 48.662  1.00 67.72  ? 287 GLU B OE2 1 
ATOM   6467 N N   . ARG B 1 288 ? -47.503 44.519 48.361  1.00 35.55  ? 288 ARG B N   1 
ATOM   6468 C CA  . ARG B 1 288 ? -46.416 44.831 49.305  1.00 43.29  ? 288 ARG B CA  1 
ATOM   6469 C C   . ARG B 1 288 ? -45.283 43.843 49.082  1.00 42.75  ? 288 ARG B C   1 
ATOM   6470 O O   . ARG B 1 288 ? -45.069 42.880 49.830  1.00 50.31  ? 288 ARG B O   1 
ATOM   6471 C CB  . ARG B 1 288 ? -46.908 44.844 50.734  1.00 52.21  ? 288 ARG B CB  1 
ATOM   6472 C CG  . ARG B 1 288 ? -47.218 46.235 51.147  1.00 57.61  ? 288 ARG B CG  1 
ATOM   6473 C CD  . ARG B 1 288 ? -47.371 46.408 52.606  1.00 59.56  ? 288 ARG B CD  1 
ATOM   6474 N NE  . ARG B 1 288 ? -47.444 45.113 53.262  1.00 56.38  ? 288 ARG B NE  1 
ATOM   6475 C CZ  . ARG B 1 288 ? -48.557 44.401 53.388  1.00 58.25  ? 288 ARG B CZ  1 
ATOM   6476 N NH1 . ARG B 1 288 ? -49.708 44.860 52.906  1.00 62.59  ? 288 ARG B NH1 1 
ATOM   6477 N NH2 . ARG B 1 288 ? -48.521 43.226 54.001  1.00 56.13  ? 288 ARG B NH2 1 
ATOM   6478 N N   . ALA B 1 289 ? -44.520 44.110 48.039  1.00 40.49  ? 289 ALA B N   1 
ATOM   6479 C CA  . ALA B 1 289 ? -43.705 43.077 47.428  1.00 42.03  ? 289 ALA B CA  1 
ATOM   6480 C C   . ALA B 1 289 ? -42.243 43.478 47.515  1.00 39.19  ? 289 ALA B C   1 
ATOM   6481 O O   . ALA B 1 289 ? -41.789 44.340 46.761  1.00 39.28  ? 289 ALA B O   1 
ATOM   6482 C CB  . ALA B 1 289 ? -44.167 42.850 46.009  1.00 42.23  ? 289 ALA B CB  1 
ATOM   6483 N N   . SER B 1 290 ? -41.541 42.851 48.394  1.00 34.32  ? 290 SER B N   1 
ATOM   6484 C CA  . SER B 1 290 ? -40.093 42.965 48.474  1.00 33.63  ? 290 SER B CA  1 
ATOM   6485 C C   . SER B 1 290 ? -39.449 41.959 47.519  1.00 26.57  ? 290 SER B C   1 
ATOM   6486 O O   . SER B 1 290 ? -39.800 40.770 47.556  1.00 22.43  ? 290 SER B O   1 
ATOM   6487 C CB  . SER B 1 290 ? -39.640 42.715 49.909  1.00 30.99  ? 290 SER B CB  1 
ATOM   6488 O OG  . SER B 1 290 ? -38.263 42.437 49.983  1.00 28.41  ? 290 SER B OG  1 
ATOM   6489 N N   . PRO B 1 291 ? -38.530 42.382 46.645  1.00 26.68  ? 291 PRO B N   1 
ATOM   6490 C CA  . PRO B 1 291 ? -37.848 41.426 45.764  1.00 27.53  ? 291 PRO B CA  1 
ATOM   6491 C C   . PRO B 1 291 ? -36.784 40.589 46.456  1.00 21.29  ? 291 PRO B C   1 
ATOM   6492 O O   . PRO B 1 291 ? -36.084 39.820 45.782  1.00 20.92  ? 291 PRO B O   1 
ATOM   6493 C CB  . PRO B 1 291 ? -37.210 42.339 44.709  1.00 29.36  ? 291 PRO B CB  1 
ATOM   6494 C CG  . PRO B 1 291 ? -36.906 43.577 45.465  1.00 29.75  ? 291 PRO B CG  1 
ATOM   6495 C CD  . PRO B 1 291 ? -38.053 43.758 46.432  1.00 30.36  ? 291 PRO B CD  1 
ATOM   6496 N N   . TYR B 1 292 ? -36.632 40.723 47.771  1.00 21.73  ? 292 TYR B N   1 
ATOM   6497 C CA  . TYR B 1 292 ? -35.535 40.091 48.484  1.00 20.72  ? 292 TYR B CA  1 
ATOM   6498 C C   . TYR B 1 292 ? -35.966 38.824 49.203  1.00 25.37  ? 292 TYR B C   1 
ATOM   6499 O O   . TYR B 1 292 ? -35.191 38.271 49.995  1.00 21.99  ? 292 TYR B O   1 
ATOM   6500 C CB  . TYR B 1 292 ? -34.910 41.103 49.451  1.00 22.70  ? 292 TYR B CB  1 
ATOM   6501 C CG  . TYR B 1 292 ? -34.539 42.384 48.738  1.00 24.60  ? 292 TYR B CG  1 
ATOM   6502 C CD1 . TYR B 1 292 ? -33.801 42.348 47.562  1.00 29.61  ? 292 TYR B CD1 1 
ATOM   6503 C CD2 . TYR B 1 292 ? -34.952 43.625 49.214  1.00 27.06  ? 292 TYR B CD2 1 
ATOM   6504 C CE1 . TYR B 1 292 ? -33.466 43.508 46.887  1.00 34.73  ? 292 TYR B CE1 1 
ATOM   6505 C CE2 . TYR B 1 292 ? -34.623 44.798 48.544  1.00 24.82  ? 292 TYR B CE2 1 
ATOM   6506 C CZ  . TYR B 1 292 ? -33.879 44.730 47.381  1.00 32.63  ? 292 TYR B CZ  1 
ATOM   6507 O OH  . TYR B 1 292 ? -33.544 45.876 46.701  1.00 37.10  ? 292 TYR B OH  1 
ATOM   6508 N N   . LEU B 1 293 ? -37.177 38.345 48.921  1.00 23.47  ? 293 LEU B N   1 
ATOM   6509 C CA  . LEU B 1 293 ? -37.745 37.132 49.480  1.00 23.64  ? 293 LEU B CA  1 
ATOM   6510 C C   . LEU B 1 293 ? -37.651 36.003 48.461  1.00 24.46  ? 293 LEU B C   1 
ATOM   6511 O O   . LEU B 1 293 ? -37.604 36.233 47.251  1.00 22.62  ? 293 LEU B O   1 
ATOM   6512 C CB  . LEU B 1 293 ? -39.222 37.346 49.856  1.00 27.36  ? 293 LEU B CB  1 
ATOM   6513 C CG  . LEU B 1 293 ? -39.631 38.046 51.158  1.00 27.02  ? 293 LEU B CG  1 
ATOM   6514 C CD1 . LEU B 1 293 ? -38.733 39.215 51.488  1.00 26.05  ? 293 LEU B CD1 1 
ATOM   6515 C CD2 . LEU B 1 293 ? -41.097 38.470 51.117  1.00 25.58  ? 293 LEU B CD2 1 
ATOM   6516 N N   . ARG B 1 294 ? -37.653 34.772 48.962  1.00 17.48  ? 294 ARG B N   1 
ATOM   6517 C CA  . ARG B 1 294 ? -37.962 33.620 48.120  1.00 18.10  ? 294 ARG B CA  1 
ATOM   6518 C C   . ARG B 1 294 ? -39.473 33.458 48.104  1.00 20.01  ? 294 ARG B C   1 
ATOM   6519 O O   . ARG B 1 294 ? -40.091 33.353 49.164  1.00 22.29  ? 294 ARG B O   1 
ATOM   6520 C CB  . ARG B 1 294 ? -37.310 32.330 48.620  1.00 17.13  ? 294 ARG B CB  1 
ATOM   6521 C CG  . ARG B 1 294 ? -37.624 31.123 47.716  1.00 23.24  ? 294 ARG B CG  1 
ATOM   6522 C CD  . ARG B 1 294 ? -36.747 29.901 48.003  1.00 26.46  ? 294 ARG B CD  1 
ATOM   6523 N NE  . ARG B 1 294 ? -36.928 29.442 49.375  1.00 26.79  ? 294 ARG B NE  1 
ATOM   6524 C CZ  . ARG B 1 294 ? -35.938 29.246 50.239  1.00 31.03  ? 294 ARG B CZ  1 
ATOM   6525 N NH1 . ARG B 1 294 ? -34.677 29.452 49.874  1.00 31.54  ? 294 ARG B NH1 1 
ATOM   6526 N NH2 . ARG B 1 294 ? -36.211 28.837 51.474  1.00 25.53  ? 294 ARG B NH2 1 
ATOM   6527 N N   . TYR B 1 295 ? -40.064 33.450 46.915  1.00 21.36  ? 295 TYR B N   1 
ATOM   6528 C CA  . TYR B 1 295 ? -41.507 33.301 46.788  1.00 25.34  ? 295 TYR B CA  1 
ATOM   6529 C C   . TYR B 1 295 ? -41.861 31.870 46.383  1.00 25.03  ? 295 TYR B C   1 
ATOM   6530 O O   . TYR B 1 295 ? -41.077 31.182 45.722  1.00 24.28  ? 295 TYR B O   1 
ATOM   6531 C CB  . TYR B 1 295 ? -42.071 34.295 45.766  1.00 23.21  ? 295 TYR B CB  1 
ATOM   6532 C CG  . TYR B 1 295 ? -42.075 35.740 46.244  1.00 25.18  ? 295 TYR B CG  1 
ATOM   6533 C CD1 . TYR B 1 295 ? -40.929 36.527 46.160  1.00 19.41  ? 295 TYR B CD1 1 
ATOM   6534 C CD2 . TYR B 1 295 ? -43.226 36.315 46.777  1.00 24.84  ? 295 TYR B CD2 1 
ATOM   6535 C CE1 . TYR B 1 295 ? -40.939 37.862 46.598  1.00 24.62  ? 295 TYR B CE1 1 
ATOM   6536 C CE2 . TYR B 1 295 ? -43.244 37.637 47.211  1.00 25.54  ? 295 TYR B CE2 1 
ATOM   6537 C CZ  . TYR B 1 295 ? -42.100 38.403 47.132  1.00 23.17  ? 295 TYR B CZ  1 
ATOM   6538 O OH  . TYR B 1 295 ? -42.128 39.718 47.568  1.00 28.49  ? 295 TYR B OH  1 
ATOM   6539 N N   . TYR B 1 296 ? -43.050 31.422 46.811  1.00 18.86  ? 296 TYR B N   1 
ATOM   6540 C CA  . TYR B 1 296 ? -43.624 30.138 46.414  1.00 23.58  ? 296 TYR B CA  1 
ATOM   6541 C C   . TYR B 1 296 ? -44.948 30.415 45.707  1.00 29.67  ? 296 TYR B C   1 
ATOM   6542 O O   . TYR B 1 296 ? -45.920 30.850 46.342  1.00 26.03  ? 296 TYR B O   1 
ATOM   6543 C CB  . TYR B 1 296 ? -43.847 29.213 47.614  1.00 24.46  ? 296 TYR B CB  1 
ATOM   6544 C CG  . TYR B 1 296 ? -42.619 28.961 48.457  1.00 27.19  ? 296 TYR B CG  1 
ATOM   6545 C CD1 . TYR B 1 296 ? -41.411 28.610 47.867  1.00 23.64  ? 296 TYR B CD1 1 
ATOM   6546 C CD2 . TYR B 1 296 ? -42.668 29.077 49.846  1.00 26.13  ? 296 TYR B CD2 1 
ATOM   6547 C CE1 . TYR B 1 296 ? -40.282 28.380 48.633  1.00 30.48  ? 296 TYR B CE1 1 
ATOM   6548 C CE2 . TYR B 1 296 ? -41.545 28.855 50.618  1.00 28.66  ? 296 TYR B CE2 1 
ATOM   6549 C CZ  . TYR B 1 296 ? -40.354 28.508 50.007  1.00 32.14  ? 296 TYR B CZ  1 
ATOM   6550 O OH  . TYR B 1 296 ? -39.229 28.287 50.770  1.00 34.45  ? 296 TYR B OH  1 
ATOM   6551 N N   . PHE B 1 297 ? -44.990 30.164 44.403  1.00 27.68  ? 297 PHE B N   1 
ATOM   6552 C CA  . PHE B 1 297 ? -46.225 30.330 43.648  1.00 28.62  ? 297 PHE B CA  1 
ATOM   6553 C C   . PHE B 1 297 ? -47.133 29.140 43.945  1.00 30.58  ? 297 PHE B C   1 
ATOM   6554 O O   . PHE B 1 297 ? -46.860 28.010 43.513  1.00 24.76  ? 297 PHE B O   1 
ATOM   6555 C CB  . PHE B 1 297 ? -45.937 30.459 42.154  1.00 27.54  ? 297 PHE B CB  1 
ATOM   6556 C CG  . PHE B 1 297 ? -47.173 30.632 41.313  1.00 24.69  ? 297 PHE B CG  1 
ATOM   6557 C CD1 . PHE B 1 297 ? -47.809 31.862 41.235  1.00 24.85  ? 297 PHE B CD1 1 
ATOM   6558 C CD2 . PHE B 1 297 ? -47.696 29.564 40.600  1.00 25.01  ? 297 PHE B CD2 1 
ATOM   6559 C CE1 . PHE B 1 297 ? -48.950 32.027 40.462  1.00 27.84  ? 297 PHE B CE1 1 
ATOM   6560 C CE2 . PHE B 1 297 ? -48.836 29.711 39.825  1.00 25.15  ? 297 PHE B CE2 1 
ATOM   6561 C CZ  . PHE B 1 297 ? -49.473 30.946 39.758  1.00 28.70  ? 297 PHE B CZ  1 
ATOM   6562 N N   . ARG B 1 298 ? -48.193 29.382 44.717  1.00 24.72  ? 298 ARG B N   1 
ATOM   6563 C CA  . ARG B 1 298 ? -49.193 28.359 45.027  1.00 25.23  ? 298 ARG B CA  1 
ATOM   6564 C C   . ARG B 1 298 ? -48.565 27.106 45.640  1.00 27.51  ? 298 ARG B C   1 
ATOM   6565 O O   . ARG B 1 298 ? -49.103 26.007 45.513  1.00 29.93  ? 298 ARG B O   1 
ATOM   6566 C CB  . ARG B 1 298 ? -50.010 28.005 43.780  1.00 29.41  ? 298 ARG B CB  1 
ATOM   6567 C CG  . ARG B 1 298 ? -50.753 29.198 43.185  1.00 24.59  ? 298 ARG B CG  1 
ATOM   6568 C CD  . ARG B 1 298 ? -51.606 28.842 41.984  1.00 23.92  ? 298 ARG B CD  1 
ATOM   6569 N NE  . ARG B 1 298 ? -52.172 30.045 41.374  1.00 23.57  ? 298 ARG B NE  1 
ATOM   6570 C CZ  . ARG B 1 298 ? -52.799 30.061 40.205  1.00 30.85  ? 298 ARG B CZ  1 
ATOM   6571 N NH1 . ARG B 1 298 ? -52.958 28.927 39.526  1.00 26.65  ? 298 ARG B NH1 1 
ATOM   6572 N NH2 . ARG B 1 298 ? -53.276 31.203 39.724  1.00 29.19  ? 298 ARG B NH2 1 
ATOM   6573 N N   . GLU B 1 299 ? -47.415 27.266 46.297  1.00 32.80  ? 299 GLU B N   1 
ATOM   6574 C CA  . GLU B 1 299 ? -46.639 26.181 46.909  1.00 36.15  ? 299 GLU B CA  1 
ATOM   6575 C C   . GLU B 1 299 ? -46.212 25.122 45.895  1.00 33.90  ? 299 GLU B C   1 
ATOM   6576 O O   . GLU B 1 299 ? -45.890 23.988 46.274  1.00 30.95  ? 299 GLU B O   1 
ATOM   6577 C CB  . GLU B 1 299 ? -47.397 25.515 48.069  1.00 34.02  ? 299 GLU B CB  1 
ATOM   6578 C CG  . GLU B 1 299 ? -47.750 26.446 49.219  1.00 35.10  ? 299 GLU B CG  1 
ATOM   6579 C CD  . GLU B 1 299 ? -46.583 26.721 50.162  1.00 36.25  ? 299 GLU B CD  1 
ATOM   6580 O OE1 . GLU B 1 299 ? -45.407 26.536 49.764  1.00 34.81  ? 299 GLU B OE1 1 
ATOM   6581 O OE2 . GLU B 1 299 ? -46.843 27.138 51.310  1.00 37.26  ? 299 GLU B OE2 1 
ATOM   6582 N N   . LEU B 1 300 ? -46.191 25.471 44.608  1.00 29.15  ? 300 LEU B N   1 
ATOM   6583 C CA  . LEU B 1 300 ? -45.843 24.520 43.560  1.00 32.14  ? 300 LEU B CA  1 
ATOM   6584 C C   . LEU B 1 300 ? -44.444 24.733 42.999  1.00 32.08  ? 300 LEU B C   1 
ATOM   6585 O O   . LEU B 1 300 ? -43.794 23.763 42.583  1.00 34.36  ? 300 LEU B O   1 
ATOM   6586 C CB  . LEU B 1 300 ? -46.858 24.597 42.416  1.00 30.60  ? 300 LEU B CB  1 
ATOM   6587 C CG  . LEU B 1 300 ? -48.327 24.329 42.780  1.00 33.26  ? 300 LEU B CG  1 
ATOM   6588 C CD1 . LEU B 1 300 ? -49.184 24.261 41.518  1.00 35.99  ? 300 LEU B CD1 1 
ATOM   6589 C CD2 . LEU B 1 300 ? -48.487 23.060 43.615  1.00 23.29  ? 300 LEU B CD2 1 
ATOM   6590 N N   . ILE B 1 301 ? -43.966 25.969 42.976  1.00 25.32  ? 301 ILE B N   1 
ATOM   6591 C CA  . ILE B 1 301 ? -42.703 26.283 42.325  1.00 19.85  ? 301 ILE B CA  1 
ATOM   6592 C C   . ILE B 1 301 ? -42.131 27.524 42.988  1.00 22.10  ? 301 ILE B C   1 
ATOM   6593 O O   . ILE B 1 301 ? -42.863 28.448 43.354  1.00 29.56  ? 301 ILE B O   1 
ATOM   6594 C CB  . ILE B 1 301 ? -42.880 26.470 40.802  1.00 22.69  ? 301 ILE B CB  1 
ATOM   6595 C CG1 . ILE B 1 301 ? -41.517 26.627 40.118  1.00 27.42  ? 301 ILE B CG1 1 
ATOM   6596 C CG2 . ILE B 1 301 ? -43.764 27.664 40.495  1.00 27.41  ? 301 ILE B CG2 1 
ATOM   6597 C CD1 . ILE B 1 301 ? -41.591 26.631 38.601  1.00 31.25  ? 301 ILE B CD1 1 
ATOM   6598 N N   . SER B 1 302 ? -40.821 27.523 43.176  1.00 25.03  ? 302 SER B N   1 
ATOM   6599 C CA  . SER B 1 302 ? -40.144 28.628 43.830  1.00 27.81  ? 302 SER B CA  1 
ATOM   6600 C C   . SER B 1 302 ? -39.765 29.677 42.792  1.00 28.02  ? 302 SER B C   1 
ATOM   6601 O O   . SER B 1 302 ? -39.315 29.346 41.690  1.00 26.47  ? 302 SER B O   1 
ATOM   6602 C CB  . SER B 1 302 ? -38.917 28.119 44.588  1.00 28.45  ? 302 SER B CB  1 
ATOM   6603 O OG  . SER B 1 302 ? -39.305 27.186 45.595  1.00 26.32  ? 302 SER B OG  1 
ATOM   6604 N N   . VAL B 1 303 ? -40.004 30.940 43.130  1.00 22.04  ? 303 VAL B N   1 
ATOM   6605 C CA  . VAL B 1 303 ? -39.789 32.068 42.225  1.00 26.02  ? 303 VAL B CA  1 
ATOM   6606 C C   . VAL B 1 303 ? -39.020 33.137 42.980  1.00 24.93  ? 303 VAL B C   1 
ATOM   6607 O O   . VAL B 1 303 ? -39.436 33.539 44.072  1.00 30.35  ? 303 VAL B O   1 
ATOM   6608 C CB  . VAL B 1 303 ? -41.109 32.673 41.693  1.00 27.19  ? 303 VAL B CB  1 
ATOM   6609 C CG1 . VAL B 1 303 ? -40.816 33.782 40.671  1.00 27.85  ? 303 VAL B CG1 1 
ATOM   6610 C CG2 . VAL B 1 303 ? -42.040 31.610 41.095  1.00 17.79  ? 303 VAL B CG2 1 
ATOM   6611 N N   . PHE B 1 304 ? -37.904 33.589 42.405  1.00 18.62  ? 304 PHE B N   1 
ATOM   6612 C CA  . PHE B 1 304 ? -37.238 34.813 42.827  1.00 22.14  ? 304 PHE B CA  1 
ATOM   6613 C C   . PHE B 1 304 ? -37.524 35.918 41.821  1.00 20.28  ? 304 PHE B C   1 
ATOM   6614 O O   . PHE B 1 304 ? -37.666 35.667 40.625  1.00 23.85  ? 304 PHE B O   1 
ATOM   6615 C CB  . PHE B 1 304 ? -35.727 34.607 42.944  1.00 22.21  ? 304 PHE B CB  1 
ATOM   6616 C CG  . PHE B 1 304 ? -35.316 33.821 44.146  1.00 25.70  ? 304 PHE B CG  1 
ATOM   6617 C CD1 . PHE B 1 304 ? -35.152 34.446 45.372  1.00 23.36  ? 304 PHE B CD1 1 
ATOM   6618 C CD2 . PHE B 1 304 ? -35.090 32.456 44.052  1.00 21.47  ? 304 PHE B CD2 1 
ATOM   6619 C CE1 . PHE B 1 304 ? -34.769 33.724 46.479  1.00 24.46  ? 304 PHE B CE1 1 
ATOM   6620 C CE2 . PHE B 1 304 ? -34.707 31.724 45.163  1.00 22.90  ? 304 PHE B CE2 1 
ATOM   6621 C CZ  . PHE B 1 304 ? -34.543 32.357 46.372  1.00 26.22  ? 304 PHE B CZ  1 
ATOM   6622 N N   . PHE B 1 305 ? -37.625 37.144 42.308  1.00 27.48  ? 305 PHE B N   1 
ATOM   6623 C CA  . PHE B 1 305 ? -37.825 38.293 41.436  1.00 20.99  ? 305 PHE B CA  1 
ATOM   6624 C C   . PHE B 1 305 ? -36.528 39.081 41.415  1.00 23.59  ? 305 PHE B C   1 
ATOM   6625 O O   . PHE B 1 305 ? -36.011 39.462 42.472  1.00 21.63  ? 305 PHE B O   1 
ATOM   6626 C CB  . PHE B 1 305 ? -38.998 39.152 41.899  1.00 17.36  ? 305 PHE B CB  1 
ATOM   6627 C CG  . PHE B 1 305 ? -40.318 38.436 41.821  1.00 24.75  ? 305 PHE B CG  1 
ATOM   6628 C CD1 . PHE B 1 305 ? -40.717 37.574 42.845  1.00 20.57  ? 305 PHE B CD1 1 
ATOM   6629 C CD2 . PHE B 1 305 ? -41.133 38.581 40.716  1.00 23.66  ? 305 PHE B CD2 1 
ATOM   6630 C CE1 . PHE B 1 305 ? -41.930 36.900 42.777  1.00 24.43  ? 305 PHE B CE1 1 
ATOM   6631 C CE2 . PHE B 1 305 ? -42.363 37.915 40.644  1.00 26.66  ? 305 PHE B CE2 1 
ATOM   6632 C CZ  . PHE B 1 305 ? -42.747 37.061 41.669  1.00 28.16  ? 305 PHE B CZ  1 
ATOM   6633 N N   . ARG B 1 306 ? -35.995 39.303 40.219  1.00 21.57  ? 306 ARG B N   1 
ATOM   6634 C CA  . ARG B 1 306 ? -34.681 39.920 40.113  1.00 24.83  ? 306 ARG B CA  1 
ATOM   6635 C C   . ARG B 1 306 ? -34.752 41.373 40.569  1.00 23.65  ? 306 ARG B C   1 
ATOM   6636 O O   . ARG B 1 306 ? -35.817 42.003 40.559  1.00 24.51  ? 306 ARG B O   1 
ATOM   6637 C CB  . ARG B 1 306 ? -34.169 39.831 38.678  1.00 24.82  ? 306 ARG B CB  1 
ATOM   6638 C CG  . ARG B 1 306 ? -34.892 40.767 37.723  1.00 27.23  ? 306 ARG B CG  1 
ATOM   6639 C CD  . ARG B 1 306 ? -34.097 41.031 36.463  1.00 28.06  ? 306 ARG B CD  1 
ATOM   6640 N NE  . ARG B 1 306 ? -34.659 42.185 35.779  1.00 32.12  ? 306 ARG B NE  1 
ATOM   6641 C CZ  . ARG B 1 306 ? -34.101 42.812 34.754  1.00 31.47  ? 306 ARG B CZ  1 
ATOM   6642 N NH1 . ARG B 1 306 ? -32.938 42.405 34.248  1.00 26.68  ? 306 ARG B NH1 1 
ATOM   6643 N NH2 . ARG B 1 306 ? -34.716 43.861 34.248  1.00 34.66  ? 306 ARG B NH2 1 
ATOM   6644 N N   . ASP B 1 307 ? -33.621 41.888 41.041  1.00 24.11  ? 307 ASP B N   1 
ATOM   6645 C CA  . ASP B 1 307 ? -33.531 43.300 41.410  1.00 25.60  ? 307 ASP B CA  1 
ATOM   6646 C C   . ASP B 1 307 ? -33.330 44.067 40.114  1.00 26.38  ? 307 ASP B C   1 
ATOM   6647 O O   . ASP B 1 307 ? -32.241 44.057 39.537  1.00 22.55  ? 307 ASP B O   1 
ATOM   6648 C CB  . ASP B 1 307 ? -32.393 43.543 42.402  1.00 27.24  ? 307 ASP B CB  1 
ATOM   6649 C CG  . ASP B 1 307 ? -32.357 44.986 42.930  1.00 33.19  ? 307 ASP B CG  1 
ATOM   6650 O OD1 . ASP B 1 307 ? -32.468 45.926 42.123  1.00 31.44  ? 307 ASP B OD1 1 
ATOM   6651 O OD2 . ASP B 1 307 ? -32.197 45.183 44.158  1.00 38.51  ? 307 ASP B OD2 1 
ATOM   6652 N N   . LYS B 1 308 ? -34.390 44.726 39.642  1.00 21.32  ? 308 LYS B N   1 
ATOM   6653 C CA  . LYS B 1 308 ? -34.323 45.394 38.345  1.00 26.67  ? 308 LYS B CA  1 
ATOM   6654 C C   . LYS B 1 308 ? -33.215 46.441 38.315  1.00 23.63  ? 308 LYS B C   1 
ATOM   6655 O O   . LYS B 1 308 ? -32.479 46.549 37.325  1.00 22.28  ? 308 LYS B O   1 
ATOM   6656 C CB  . LYS B 1 308 ? -35.677 46.024 38.024  1.00 23.12  ? 308 LYS B CB  1 
ATOM   6657 C CG  . LYS B 1 308 ? -35.795 46.696 36.662  1.00 30.31  ? 308 LYS B CG  1 
ATOM   6658 C CD  . LYS B 1 308 ? -37.158 47.388 36.574  1.00 35.65  ? 308 LYS B CD  1 
ATOM   6659 C CE  . LYS B 1 308 ? -37.416 48.051 35.231  1.00 36.74  ? 308 LYS B CE  1 
ATOM   6660 N NZ  . LYS B 1 308 ? -36.231 48.032 34.347  1.00 41.81  ? 308 LYS B NZ  1 
ATOM   6661 N N   . THR B 1 309 ? -33.075 47.217 39.396  1.00 21.76  ? 309 THR B N   1 
ATOM   6662 C CA  . THR B 1 309 ? -32.156 48.352 39.375  1.00 24.26  ? 309 THR B CA  1 
ATOM   6663 C C   . THR B 1 309 ? -30.712 47.884 39.265  1.00 26.63  ? 309 THR B C   1 
ATOM   6664 O O   . THR B 1 309 ? -29.960 48.371 38.415  1.00 24.62  ? 309 THR B O   1 
ATOM   6665 C CB  . THR B 1 309 ? -32.347 49.213 40.623  1.00 26.89  ? 309 THR B CB  1 
ATOM   6666 O OG1 . THR B 1 309 ? -33.669 49.749 40.637  1.00 26.37  ? 309 THR B OG1 1 
ATOM   6667 C CG2 . THR B 1 309 ? -31.358 50.369 40.642  1.00 26.82  ? 309 THR B CG2 1 
ATOM   6668 N N   . LEU B 1 310 ? -30.309 46.924 40.108  1.00 24.17  ? 310 LEU B N   1 
ATOM   6669 C CA  . LEU B 1 310 ? -28.939 46.415 40.053  1.00 23.07  ? 310 LEU B CA  1 
ATOM   6670 C C   . LEU B 1 310 ? -28.664 45.728 38.724  1.00 22.26  ? 310 LEU B C   1 
ATOM   6671 O O   . LEU B 1 310 ? -27.573 45.868 38.153  1.00 24.27  ? 310 LEU B O   1 
ATOM   6672 C CB  . LEU B 1 310 ? -28.688 45.456 41.218  1.00 29.14  ? 310 LEU B CB  1 
ATOM   6673 C CG  . LEU B 1 310 ? -28.812 46.075 42.614  1.00 31.06  ? 310 LEU B CG  1 
ATOM   6674 C CD1 . LEU B 1 310 ? -28.754 44.999 43.685  1.00 29.00  ? 310 LEU B CD1 1 
ATOM   6675 C CD2 . LEU B 1 310 ? -27.729 47.121 42.841  1.00 28.88  ? 310 LEU B CD2 1 
ATOM   6676 N N   . SER B 1 311 ? -29.647 44.990 38.210  1.00 19.24  ? 311 SER B N   1 
ATOM   6677 C CA  . SER B 1 311 ? -29.474 44.333 36.920  1.00 24.16  ? 311 SER B CA  1 
ATOM   6678 C C   . SER B 1 311 ? -29.332 45.357 35.802  1.00 25.19  ? 311 SER B C   1 
ATOM   6679 O O   . SER B 1 311 ? -28.483 45.204 34.914  1.00 27.41  ? 311 SER B O   1 
ATOM   6680 C CB  . SER B 1 311 ? -30.650 43.394 36.641  1.00 25.17  ? 311 SER B CB  1 
ATOM   6681 O OG  . SER B 1 311 ? -30.825 42.455 37.684  1.00 24.87  ? 311 SER B OG  1 
ATOM   6682 N N   . ASP B 1 312 ? -30.150 46.413 35.834  1.00 18.28  ? 312 ASP B N   1 
ATOM   6683 C CA  . ASP B 1 312 ? -30.058 47.471 34.822  1.00 26.11  ? 312 ASP B CA  1 
ATOM   6684 C C   . ASP B 1 312 ? -28.755 48.269 34.914  1.00 24.29  ? 312 ASP B C   1 
ATOM   6685 O O   . ASP B 1 312 ? -28.234 48.721 33.884  1.00 24.19  ? 312 ASP B O   1 
ATOM   6686 C CB  . ASP B 1 312 ? -31.246 48.432 34.943  1.00 23.80  ? 312 ASP B CB  1 
ATOM   6687 C CG  . ASP B 1 312 ? -32.529 47.862 34.356  1.00 25.83  ? 312 ASP B CG  1 
ATOM   6688 O OD1 . ASP B 1 312 ? -32.462 46.889 33.577  1.00 26.55  ? 312 ASP B OD1 1 
ATOM   6689 O OD2 . ASP B 1 312 ? -33.615 48.383 34.687  1.00 27.41  ? 312 ASP B OD2 1 
ATOM   6690 N N   . LEU B 1 313 ? -28.228 48.491 36.120  1.00 21.67  ? 313 LEU B N   1 
ATOM   6691 C CA  . LEU B 1 313 ? -26.969 49.219 36.233  1.00 25.16  ? 313 LEU B CA  1 
ATOM   6692 C C   . LEU B 1 313 ? -25.861 48.512 35.460  1.00 27.89  ? 313 LEU B C   1 
ATOM   6693 O O   . LEU B 1 313 ? -25.184 49.126 34.627  1.00 23.61  ? 313 LEU B O   1 
ATOM   6694 C CB  . LEU B 1 313 ? -26.579 49.389 37.697  1.00 26.40  ? 313 LEU B CB  1 
ATOM   6695 C CG  . LEU B 1 313 ? -27.443 50.414 38.431  1.00 27.59  ? 313 LEU B CG  1 
ATOM   6696 C CD1 . LEU B 1 313 ? -27.304 50.216 39.916  1.00 31.32  ? 313 LEU B CD1 1 
ATOM   6697 C CD2 . LEU B 1 313 ? -27.068 51.845 38.025  1.00 24.24  ? 313 LEU B CD2 1 
ATOM   6698 N N   . ILE B 1 314 ? -25.669 47.207 35.709  1.00 23.27  ? 314 ILE B N   1 
ATOM   6699 C CA  . ILE B 1 314 ? -24.601 46.495 35.013  1.00 28.24  ? 314 ILE B CA  1 
ATOM   6700 C C   . ILE B 1 314 ? -24.899 46.445 33.522  1.00 31.08  ? 314 ILE B C   1 
ATOM   6701 O O   . ILE B 1 314 ? -24.022 46.690 32.680  1.00 25.52  ? 314 ILE B O   1 
ATOM   6702 C CB  . ILE B 1 314 ? -24.414 45.080 35.606  1.00 25.04  ? 314 ILE B CB  1 
ATOM   6703 C CG1 . ILE B 1 314 ? -23.905 45.161 37.047  1.00 22.25  ? 314 ILE B CG1 1 
ATOM   6704 C CG2 . ILE B 1 314 ? -23.472 44.242 34.737  1.00 24.18  ? 314 ILE B CG2 1 
ATOM   6705 C CD1 . ILE B 1 314 ? -23.839 43.816 37.763  1.00 20.96  ? 314 ILE B CD1 1 
ATOM   6706 N N   . GLY B 1 315 ? -26.152 46.166 33.172  1.00 27.34  ? 315 GLY B N   1 
ATOM   6707 C CA  . GLY B 1 315 ? -26.468 45.870 31.789  1.00 31.40  ? 315 GLY B CA  1 
ATOM   6708 C C   . GLY B 1 315 ? -26.501 47.078 30.887  1.00 31.17  ? 315 GLY B C   1 
ATOM   6709 O O   . GLY B 1 315 ? -26.216 46.962 29.691  1.00 32.34  ? 315 GLY B O   1 
ATOM   6710 N N   . PHE B 1 316 ? -26.850 48.243 31.433  1.00 27.42  ? 316 PHE B N   1 
ATOM   6711 C CA  . PHE B 1 316 ? -27.096 49.428 30.625  1.00 29.21  ? 316 PHE B CA  1 
ATOM   6712 C C   . PHE B 1 316 ? -26.439 50.693 31.142  1.00 28.25  ? 316 PHE B C   1 
ATOM   6713 O O   . PHE B 1 316 ? -26.321 51.650 30.370  1.00 25.40  ? 316 PHE B O   1 
ATOM   6714 C CB  . PHE B 1 316 ? -28.604 49.695 30.508  1.00 26.60  ? 316 PHE B CB  1 
ATOM   6715 C CG  . PHE B 1 316 ? -29.388 48.536 29.976  1.00 34.04  ? 316 PHE B CG  1 
ATOM   6716 C CD1 . PHE B 1 316 ? -29.398 48.255 28.619  1.00 37.80  ? 316 PHE B CD1 1 
ATOM   6717 C CD2 . PHE B 1 316 ? -30.138 47.738 30.829  1.00 39.64  ? 316 PHE B CD2 1 
ATOM   6718 C CE1 . PHE B 1 316 ? -30.124 47.194 28.121  1.00 33.99  ? 316 PHE B CE1 1 
ATOM   6719 C CE2 . PHE B 1 316 ? -30.866 46.674 30.341  1.00 40.15  ? 316 PHE B CE2 1 
ATOM   6720 C CZ  . PHE B 1 316 ? -30.860 46.401 28.982  1.00 39.64  ? 316 PHE B CZ  1 
ATOM   6721 N N   . SER B 1 317 ? -26.037 50.750 32.413  1.00 22.16  ? 317 SER B N   1 
ATOM   6722 C CA  . SER B 1 317 ? -25.576 51.989 33.024  1.00 29.76  ? 317 SER B CA  1 
ATOM   6723 C C   . SER B 1 317 ? -24.059 52.077 33.122  1.00 33.77  ? 317 SER B C   1 
ATOM   6724 O O   . SER B 1 317 ? -23.465 53.056 32.656  1.00 29.06  ? 317 SER B O   1 
ATOM   6725 C CB  . SER B 1 317 ? -26.187 52.139 34.421  1.00 28.87  ? 317 SER B CB  1 
ATOM   6726 O OG  . SER B 1 317 ? -27.592 52.311 34.344  1.00 30.36  ? 317 SER B OG  1 
ATOM   6727 N N   . TYR B 1 318 ? -23.419 51.067 33.718  1.00 19.86  ? 318 TYR B N   1 
ATOM   6728 C CA  . TYR B 1 318 ? -22.046 51.216 34.181  1.00 24.04  ? 318 TYR B CA  1 
ATOM   6729 C C   . TYR B 1 318 ? -21.024 51.271 33.055  1.00 26.18  ? 318 TYR B C   1 
ATOM   6730 O O   . TYR B 1 318 ? -19.851 51.542 33.334  1.00 25.32  ? 318 TYR B O   1 
ATOM   6731 C CB  . TYR B 1 318 ? -21.688 50.070 35.124  1.00 27.74  ? 318 TYR B CB  1 
ATOM   6732 C CG  . TYR B 1 318 ? -22.284 50.174 36.507  1.00 26.97  ? 318 TYR B CG  1 
ATOM   6733 C CD1 . TYR B 1 318 ? -22.635 51.408 37.056  1.00 29.74  ? 318 TYR B CD1 1 
ATOM   6734 C CD2 . TYR B 1 318 ? -22.475 49.033 37.276  1.00 29.24  ? 318 TYR B CD2 1 
ATOM   6735 C CE1 . TYR B 1 318 ? -23.173 51.494 38.336  1.00 29.85  ? 318 TYR B CE1 1 
ATOM   6736 C CE2 . TYR B 1 318 ? -23.008 49.105 38.550  1.00 32.47  ? 318 TYR B CE2 1 
ATOM   6737 C CZ  . TYR B 1 318 ? -23.356 50.334 39.077  1.00 30.38  ? 318 TYR B CZ  1 
ATOM   6738 O OH  . TYR B 1 318 ? -23.882 50.385 40.351  1.00 28.12  ? 318 TYR B OH  1 
ATOM   6739 N N   . HIS B 1 319 ? -21.421 51.000 31.807  1.00 26.48  ? 319 HIS B N   1 
ATOM   6740 C CA  . HIS B 1 319 ? -20.507 51.240 30.693  1.00 30.98  ? 319 HIS B CA  1 
ATOM   6741 C C   . HIS B 1 319 ? -20.066 52.697 30.653  1.00 32.80  ? 319 HIS B C   1 
ATOM   6742 O O   . HIS B 1 319 ? -18.956 52.995 30.201  1.00 34.12  ? 319 HIS B O   1 
ATOM   6743 C CB  . HIS B 1 319 ? -21.165 50.860 29.363  1.00 27.94  ? 319 HIS B CB  1 
ATOM   6744 C CG  . HIS B 1 319 ? -22.202 51.846 28.900  1.00 27.13  ? 319 HIS B CG  1 
ATOM   6745 N ND1 . HIS B 1 319 ? -21.887 52.981 28.179  1.00 27.05  ? 319 HIS B ND1 1 
ATOM   6746 C CD2 . HIS B 1 319 ? -23.547 51.871 29.072  1.00 25.74  ? 319 HIS B CD2 1 
ATOM   6747 C CE1 . HIS B 1 319 ? -22.993 53.652 27.915  1.00 29.29  ? 319 HIS B CE1 1 
ATOM   6748 N NE2 . HIS B 1 319 ? -24.015 53.003 28.449  1.00 25.32  ? 319 HIS B NE2 1 
ATOM   6749 N N   . ALA B 1 320 ? -20.919 53.615 31.117  1.00 31.95  ? 320 ALA B N   1 
ATOM   6750 C CA  . ALA B 1 320 ? -20.641 55.047 31.078  1.00 36.04  ? 320 ALA B CA  1 
ATOM   6751 C C   . ALA B 1 320 ? -19.923 55.551 32.327  1.00 34.19  ? 320 ALA B C   1 
ATOM   6752 O O   . ALA B 1 320 ? -19.741 56.767 32.476  1.00 31.22  ? 320 ALA B O   1 
ATOM   6753 C CB  . ALA B 1 320 ? -21.943 55.831 30.877  1.00 34.08  ? 320 ALA B CB  1 
ATOM   6754 N N   . TRP B 1 321 ? -19.519 54.648 33.222  1.00 29.05  ? 321 TRP B N   1 
ATOM   6755 C CA  . TRP B 1 321 ? -18.881 54.996 34.482  1.00 30.52  ? 321 TRP B CA  1 
ATOM   6756 C C   . TRP B 1 321 ? -17.433 54.525 34.494  1.00 32.22  ? 321 TRP B C   1 
ATOM   6757 O O   . TRP B 1 321 ? -17.080 53.534 33.851  1.00 26.19  ? 321 TRP B O   1 
ATOM   6758 C CB  . TRP B 1 321 ? -19.581 54.345 35.681  1.00 22.31  ? 321 TRP B CB  1 
ATOM   6759 C CG  . TRP B 1 321 ? -21.023 54.666 35.896  1.00 22.13  ? 321 TRP B CG  1 
ATOM   6760 C CD1 . TRP B 1 321 ? -22.012 54.701 34.962  1.00 24.47  ? 321 TRP B CD1 1 
ATOM   6761 C CD2 . TRP B 1 321 ? -21.646 54.935 37.158  1.00 34.64  ? 321 TRP B CD2 1 
ATOM   6762 N NE1 . TRP B 1 321 ? -23.220 55.000 35.567  1.00 34.69  ? 321 TRP B NE1 1 
ATOM   6763 C CE2 . TRP B 1 321 ? -23.015 55.148 36.915  1.00 34.19  ? 321 TRP B CE2 1 
ATOM   6764 C CE3 . TRP B 1 321 ? -21.172 55.026 38.471  1.00 38.46  ? 321 TRP B CE3 1 
ATOM   6765 C CZ2 . TRP B 1 321 ? -23.917 55.447 37.937  1.00 38.04  ? 321 TRP B CZ2 1 
ATOM   6766 C CZ3 . TRP B 1 321 ? -22.068 55.328 39.485  1.00 35.79  ? 321 TRP B CZ3 1 
ATOM   6767 C CH2 . TRP B 1 321 ? -23.424 55.533 39.212  1.00 36.37  ? 321 TRP B CH2 1 
ATOM   6768 N N   . ASN B 1 322 ? -16.607 55.244 35.250  1.00 36.90  ? 322 ASN B N   1 
ATOM   6769 C CA  . ASN B 1 322 ? -15.323 54.715 35.685  1.00 39.92  ? 322 ASN B CA  1 
ATOM   6770 C C   . ASN B 1 322 ? -15.538 53.417 36.458  1.00 34.65  ? 322 ASN B C   1 
ATOM   6771 O O   . ASN B 1 322 ? -16.504 53.282 37.213  1.00 38.86  ? 322 ASN B O   1 
ATOM   6772 C CB  . ASN B 1 322 ? -14.616 55.758 36.560  1.00 50.94  ? 322 ASN B CB  1 
ATOM   6773 C CG  . ASN B 1 322 ? -13.351 55.238 37.203  1.00 61.52  ? 322 ASN B CG  1 
ATOM   6774 O OD1 . ASN B 1 322 ? -12.262 55.330 36.628  1.00 69.74  ? 322 ASN B OD1 1 
ATOM   6775 N ND2 . ASN B 1 322 ? -13.480 54.705 38.412  1.00 62.42  ? 322 ASN B ND2 1 
ATOM   6776 N N   . ALA B 1 323 ? -14.629 52.455 36.270  1.00 30.90  ? 323 ALA B N   1 
ATOM   6777 C CA  . ALA B 1 323 ? -14.829 51.123 36.840  1.00 36.80  ? 323 ALA B CA  1 
ATOM   6778 C C   . ALA B 1 323 ? -14.863 51.160 38.366  1.00 36.26  ? 323 ALA B C   1 
ATOM   6779 O O   . ALA B 1 323 ? -15.722 50.522 38.986  1.00 27.49  ? 323 ALA B O   1 
ATOM   6780 C CB  . ALA B 1 323 ? -13.737 50.169 36.354  1.00 40.04  ? 323 ALA B CB  1 
ATOM   6781 N N   . GLU B 1 324 ? -13.928 51.880 38.996  1.00 33.11  ? 324 GLU B N   1 
ATOM   6782 C CA  . GLU B 1 324 ? -13.940 51.955 40.456  1.00 36.76  ? 324 GLU B CA  1 
ATOM   6783 C C   . GLU B 1 324 ? -15.196 52.646 40.968  1.00 35.30  ? 324 GLU B C   1 
ATOM   6784 O O   . GLU B 1 324 ? -15.741 52.266 42.010  1.00 30.56  ? 324 GLU B O   1 
ATOM   6785 C CB  . GLU B 1 324 ? -12.690 52.670 40.976  1.00 46.53  ? 324 GLU B CB  1 
ATOM   6786 C CG  . GLU B 1 324 ? -12.713 52.916 42.487  1.00 54.33  ? 324 GLU B CG  1 
ATOM   6787 C CD  . GLU B 1 324 ? -12.258 51.701 43.289  1.00 63.84  ? 324 GLU B CD  1 
ATOM   6788 O OE1 . GLU B 1 324 ? -11.429 50.917 42.777  1.00 67.23  ? 324 GLU B OE1 1 
ATOM   6789 O OE2 . GLU B 1 324 ? -12.735 51.529 44.433  1.00 68.08  ? 324 GLU B OE2 1 
ATOM   6790 N N   . ASP B 1 325 ? -15.667 53.661 40.247  1.00 32.83  ? 325 ASP B N   1 
ATOM   6791 C CA  . ASP B 1 325 ? -16.869 54.365 40.681  1.00 36.35  ? 325 ASP B CA  1 
ATOM   6792 C C   . ASP B 1 325 ? -18.097 53.473 40.581  1.00 27.83  ? 325 ASP B C   1 
ATOM   6793 O O   . ASP B 1 325 ? -18.966 53.503 41.456  1.00 25.47  ? 325 ASP B O   1 
ATOM   6794 C CB  . ASP B 1 325 ? -17.071 55.638 39.859  1.00 42.92  ? 325 ASP B CB  1 
ATOM   6795 C CG  . ASP B 1 325 ? -16.068 56.716 40.202  1.00 58.38  ? 325 ASP B CG  1 
ATOM   6796 O OD1 . ASP B 1 325 ? -15.914 57.026 41.405  1.00 63.92  ? 325 ASP B OD1 1 
ATOM   6797 O OD2 . ASP B 1 325 ? -15.437 57.254 39.271  1.00 63.13  ? 325 ASP B OD2 1 
ATOM   6798 N N   . ALA B 1 326 ? -18.184 52.674 39.518  1.00 27.18  ? 326 ALA B N   1 
ATOM   6799 C CA  . ALA B 1 326 ? -19.326 51.781 39.359  1.00 30.65  ? 326 ALA B CA  1 
ATOM   6800 C C   . ALA B 1 326 ? -19.351 50.711 40.440  1.00 31.56  ? 326 ALA B C   1 
ATOM   6801 O O   . ALA B 1 326 ? -20.419 50.386 40.970  1.00 28.18  ? 326 ALA B O   1 
ATOM   6802 C CB  . ALA B 1 326 ? -19.303 51.131 37.977  1.00 25.15  ? 326 ALA B CB  1 
ATOM   6803 N N   . VAL B 1 327 ? -18.190 50.145 40.778  1.00 24.55  ? 327 VAL B N   1 
ATOM   6804 C CA  . VAL B 1 327 ? -18.160 49.095 41.795  1.00 25.41  ? 327 VAL B CA  1 
ATOM   6805 C C   . VAL B 1 327 ? -18.560 49.653 43.153  1.00 26.19  ? 327 VAL B C   1 
ATOM   6806 O O   . VAL B 1 327 ? -19.358 49.054 43.886  1.00 28.58  ? 327 VAL B O   1 
ATOM   6807 C CB  . VAL B 1 327 ? -16.772 48.438 41.848  1.00 28.20  ? 327 VAL B CB  1 
ATOM   6808 C CG1 . VAL B 1 327 ? -16.606 47.661 43.158  1.00 22.89  ? 327 VAL B CG1 1 
ATOM   6809 C CG2 . VAL B 1 327 ? -16.583 47.530 40.640  1.00 25.75  ? 327 VAL B CG2 1 
ATOM   6810 N N   . ARG B 1 328 ? -17.991 50.795 43.520  1.00 27.29  ? 328 ARG B N   1 
ATOM   6811 C CA  . ARG B 1 328 ? -18.394 51.453 44.754  1.00 31.50  ? 328 ARG B CA  1 
ATOM   6812 C C   . ARG B 1 328 ? -19.893 51.725 44.762  1.00 27.96  ? 328 ARG B C   1 
ATOM   6813 O O   . ARG B 1 328 ? -20.555 51.560 45.792  1.00 25.91  ? 328 ARG B O   1 
ATOM   6814 C CB  . ARG B 1 328 ? -17.610 52.755 44.924  1.00 32.23  ? 328 ARG B CB  1 
ATOM   6815 C CG  . ARG B 1 328 ? -18.271 53.739 45.860  1.00 36.35  ? 328 ARG B CG  1 
ATOM   6816 C CD  . ARG B 1 328 ? -17.326 54.862 46.259  1.00 39.16  ? 328 ARG B CD  1 
ATOM   6817 N NE  . ARG B 1 328 ? -16.200 55.024 45.340  1.00 46.61  ? 328 ARG B NE  1 
ATOM   6818 C CZ  . ARG B 1 328 ? -16.171 55.900 44.340  1.00 43.48  ? 328 ARG B CZ  1 
ATOM   6819 N NH1 . ARG B 1 328 ? -17.212 56.692 44.120  1.00 39.35  ? 328 ARG B NH1 1 
ATOM   6820 N NH2 . ARG B 1 328 ? -15.104 55.984 43.559  1.00 40.53  ? 328 ARG B NH2 1 
ATOM   6821 N N   . ASP B 1 329 ? -20.445 52.139 43.617  1.00 30.15  ? 329 ASP B N   1 
ATOM   6822 C CA  . ASP B 1 329 ? -21.876 52.422 43.537  1.00 27.44  ? 329 ASP B CA  1 
ATOM   6823 C C   . ASP B 1 329 ? -22.692 51.158 43.749  1.00 23.41  ? 329 ASP B C   1 
ATOM   6824 O O   . ASP B 1 329 ? -23.682 51.161 44.490  1.00 22.88  ? 329 ASP B O   1 
ATOM   6825 C CB  . ASP B 1 329 ? -22.218 53.053 42.182  1.00 29.17  ? 329 ASP B CB  1 
ATOM   6826 C CG  . ASP B 1 329 ? -23.728 53.307 42.019  1.00 29.52  ? 329 ASP B CG  1 
ATOM   6827 O OD1 . ASP B 1 329 ? -24.237 54.283 42.607  1.00 34.56  ? 329 ASP B OD1 1 
ATOM   6828 O OD2 . ASP B 1 329 ? -24.401 52.534 41.304  1.00 28.73  ? 329 ASP B OD2 1 
ATOM   6829 N N   . PHE B 1 330 ? -22.293 50.069 43.084  1.00 28.56  ? 330 PHE B N   1 
ATOM   6830 C CA  . PHE B 1 330 ? -22.980 48.790 43.218  1.00 22.80  ? 330 PHE B CA  1 
ATOM   6831 C C   . PHE B 1 330 ? -22.927 48.293 44.660  1.00 28.51  ? 330 PHE B C   1 
ATOM   6832 O O   . PHE B 1 330 ? -23.952 47.891 45.232  1.00 25.45  ? 330 PHE B O   1 
ATOM   6833 C CB  . PHE B 1 330 ? -22.337 47.785 42.252  1.00 25.32  ? 330 PHE B CB  1 
ATOM   6834 C CG  . PHE B 1 330 ? -23.085 46.483 42.099  1.00 25.75  ? 330 PHE B CG  1 
ATOM   6835 C CD1 . PHE B 1 330 ? -24.103 46.353 41.172  1.00 23.13  ? 330 PHE B CD1 1 
ATOM   6836 C CD2 . PHE B 1 330 ? -22.726 45.371 42.846  1.00 28.34  ? 330 PHE B CD2 1 
ATOM   6837 C CE1 . PHE B 1 330 ? -24.774 45.144 41.017  1.00 23.80  ? 330 PHE B CE1 1 
ATOM   6838 C CE2 . PHE B 1 330 ? -23.397 44.153 42.697  1.00 27.96  ? 330 PHE B CE2 1 
ATOM   6839 C CZ  . PHE B 1 330 ? -24.413 44.039 41.786  1.00 21.97  ? 330 PHE B CZ  1 
ATOM   6840 N N   . ILE B 1 331 ? -21.735 48.327 45.269  1.00 30.71  ? 331 ILE B N   1 
ATOM   6841 C CA  . ILE B 1 331 ? -21.569 47.822 46.631  1.00 34.08  ? 331 ILE B CA  1 
ATOM   6842 C C   . ILE B 1 331 ? -22.334 48.696 47.625  1.00 25.68  ? 331 ILE B C   1 
ATOM   6843 O O   . ILE B 1 331 ? -22.941 48.188 48.578  1.00 25.71  ? 331 ILE B O   1 
ATOM   6844 C CB  . ILE B 1 331 ? -20.070 47.725 46.985  1.00 39.28  ? 331 ILE B CB  1 
ATOM   6845 C CG1 . ILE B 1 331 ? -19.349 46.727 46.061  1.00 33.62  ? 331 ILE B CG1 1 
ATOM   6846 C CG2 . ILE B 1 331 ? -19.872 47.349 48.463  1.00 41.01  ? 331 ILE B CG2 1 
ATOM   6847 C CD1 . ILE B 1 331 ? -19.712 45.285 46.270  1.00 30.36  ? 331 ILE B CD1 1 
ATOM   6848 N N   . GLY B 1 332 ? -22.326 50.016 47.421  1.00 26.99  ? 332 GLY B N   1 
ATOM   6849 C CA  . GLY B 1 332 ? -23.103 50.889 48.292  1.00 26.84  ? 332 GLY B CA  1 
ATOM   6850 C C   . GLY B 1 332 ? -24.588 50.573 48.259  1.00 27.68  ? 332 GLY B C   1 
ATOM   6851 O O   . GLY B 1 332 ? -25.265 50.607 49.293  1.00 31.55  ? 332 GLY B O   1 
ATOM   6852 N N   . ARG B 1 333 ? -25.115 50.250 47.074  1.00 22.15  ? 333 ARG B N   1 
ATOM   6853 C CA  . ARG B 1 333 ? -26.519 49.855 46.983  1.00 28.58  ? 333 ARG B CA  1 
ATOM   6854 C C   . ARG B 1 333 ? -26.783 48.542 47.716  1.00 28.26  ? 333 ARG B C   1 
ATOM   6855 O O   . ARG B 1 333 ? -27.811 48.399 48.386  1.00 28.24  ? 333 ARG B O   1 
ATOM   6856 C CB  . ARG B 1 333 ? -26.949 49.751 45.521  1.00 30.09  ? 333 ARG B CB  1 
ATOM   6857 C CG  . ARG B 1 333 ? -27.143 51.094 44.846  1.00 26.34  ? 333 ARG B CG  1 
ATOM   6858 C CD  . ARG B 1 333 ? -27.308 50.909 43.351  1.00 24.22  ? 333 ARG B CD  1 
ATOM   6859 N NE  . ARG B 1 333 ? -27.148 52.147 42.593  1.00 30.16  ? 333 ARG B NE  1 
ATOM   6860 C CZ  . ARG B 1 333 ? -28.104 53.054 42.408  1.00 32.48  ? 333 ARG B CZ  1 
ATOM   6861 N NH1 . ARG B 1 333 ? -29.305 52.890 42.944  1.00 30.80  ? 333 ARG B NH1 1 
ATOM   6862 N NH2 . ARG B 1 333 ? -27.856 54.136 41.687  1.00 41.79  ? 333 ARG B NH2 1 
ATOM   6863 N N   . LEU B 1 334 ? -25.876 47.566 47.593  1.00 26.01  ? 334 LEU B N   1 
ATOM   6864 C CA  . LEU B 1 334 ? -25.995 46.350 48.395  1.00 24.65  ? 334 LEU B CA  1 
ATOM   6865 C C   . LEU B 1 334 ? -25.943 46.668 49.884  1.00 28.73  ? 334 LEU B C   1 
ATOM   6866 O O   . LEU B 1 334 ? -26.676 46.072 50.683  1.00 32.25  ? 334 LEU B O   1 
ATOM   6867 C CB  . LEU B 1 334 ? -24.888 45.357 48.033  1.00 19.95  ? 334 LEU B CB  1 
ATOM   6868 C CG  . LEU B 1 334 ? -24.908 44.756 46.630  1.00 23.30  ? 334 LEU B CG  1 
ATOM   6869 C CD1 . LEU B 1 334 ? -23.725 43.813 46.437  1.00 26.45  ? 334 LEU B CD1 1 
ATOM   6870 C CD2 . LEU B 1 334 ? -26.244 44.042 46.368  1.00 27.27  ? 334 LEU B CD2 1 
ATOM   6871 N N   . LYS B 1 335 ? -25.075 47.598 50.277  1.00 26.67  ? 335 LYS B N   1 
ATOM   6872 C CA  . LYS B 1 335 ? -24.981 47.968 51.687  1.00 31.11  ? 335 LYS B CA  1 
ATOM   6873 C C   . LYS B 1 335 ? -26.310 48.508 52.201  1.00 34.24  ? 335 LYS B C   1 
ATOM   6874 O O   . LYS B 1 335 ? -26.751 48.152 53.300  1.00 33.83  ? 335 LYS B O   1 
ATOM   6875 C CB  . LYS B 1 335 ? -23.857 48.988 51.875  1.00 32.74  ? 335 LYS B CB  1 
ATOM   6876 C CG  . LYS B 1 335 ? -23.646 49.455 53.302  1.00 35.17  ? 335 LYS B CG  1 
ATOM   6877 C CD  . LYS B 1 335 ? -22.495 50.448 53.355  1.00 37.04  ? 335 LYS B CD  1 
ATOM   6878 C CE  . LYS B 1 335 ? -22.760 51.549 54.368  1.00 44.73  ? 335 LYS B CE  1 
ATOM   6879 N NZ  . LYS B 1 335 ? -22.819 51.013 55.753  1.00 51.29  ? 335 LYS B NZ  1 
ATOM   6880 N N   . LYS B 1 336 ? -26.987 49.330 51.397  1.00 30.45  ? 336 LYS B N   1 
ATOM   6881 C CA  . LYS B 1 336 ? -28.239 49.926 51.840  1.00 34.45  ? 336 LYS B CA  1 
ATOM   6882 C C   . LYS B 1 336 ? -29.354 48.888 51.920  1.00 35.44  ? 336 LYS B C   1 
ATOM   6883 O O   . LYS B 1 336 ? -30.145 48.902 52.870  1.00 34.35  ? 336 LYS B O   1 
ATOM   6884 C CB  . LYS B 1 336 ? -28.620 51.083 50.916  1.00 35.92  ? 336 LYS B CB  1 
ATOM   6885 C CG  . LYS B 1 336 ? -27.582 52.194 50.938  1.00 44.40  ? 336 LYS B CG  1 
ATOM   6886 C CD  . LYS B 1 336 ? -27.892 53.303 49.948  1.00 53.49  ? 336 LYS B CD  1 
ATOM   6887 C CE  . LYS B 1 336 ? -26.769 54.336 49.916  1.00 57.50  ? 336 LYS B CE  1 
ATOM   6888 N NZ  . LYS B 1 336 ? -26.483 54.804 48.527  1.00 55.85  ? 336 LYS B NZ  1 
ATOM   6889 N N   . ILE B 1 337 ? -29.436 47.978 50.940  1.00 31.42  ? 337 ILE B N   1 
ATOM   6890 C CA  . ILE B 1 337 ? -30.355 46.843 51.057  1.00 24.59  ? 337 ILE B CA  1 
ATOM   6891 C C   . ILE B 1 337 ? -30.063 46.044 52.325  1.00 27.50  ? 337 ILE B C   1 
ATOM   6892 O O   . ILE B 1 337 ? -30.981 45.654 53.056  1.00 28.77  ? 337 ILE B O   1 
ATOM   6893 C CB  . ILE B 1 337 ? -30.262 45.948 49.807  1.00 22.99  ? 337 ILE B CB  1 
ATOM   6894 C CG1 . ILE B 1 337 ? -30.714 46.694 48.553  1.00 29.28  ? 337 ILE B CG1 1 
ATOM   6895 C CG2 . ILE B 1 337 ? -31.063 44.664 50.001  1.00 29.34  ? 337 ILE B CG2 1 
ATOM   6896 C CD1 . ILE B 1 337 ? -30.297 45.972 47.264  1.00 28.00  ? 337 ILE B CD1 1 
ATOM   6897 N N   . HIS B 1 338 ? -28.778 45.780 52.595  1.00 25.22  ? 338 HIS B N   1 
ATOM   6898 C CA  . HIS B 1 338 ? -28.386 45.024 53.785  1.00 30.16  ? 338 HIS B CA  1 
ATOM   6899 C C   . HIS B 1 338 ? -28.832 45.722 55.070  1.00 35.93  ? 338 HIS B C   1 
ATOM   6900 O O   . HIS B 1 338 ? -29.295 45.069 56.013  1.00 35.09  ? 338 HIS B O   1 
ATOM   6901 C CB  . HIS B 1 338 ? -26.869 44.827 53.781  1.00 28.75  ? 338 HIS B CB  1 
ATOM   6902 C CG  . HIS B 1 338 ? -26.351 43.999 54.915  1.00 40.75  ? 338 HIS B CG  1 
ATOM   6903 N ND1 . HIS B 1 338 ? -25.296 44.403 55.707  1.00 44.86  ? 338 HIS B ND1 1 
ATOM   6904 C CD2 . HIS B 1 338 ? -26.718 42.777 55.371  1.00 42.71  ? 338 HIS B CD2 1 
ATOM   6905 C CE1 . HIS B 1 338 ? -25.048 43.473 56.613  1.00 45.71  ? 338 HIS B CE1 1 
ATOM   6906 N NE2 . HIS B 1 338 ? -25.895 42.475 56.428  1.00 42.26  ? 338 HIS B NE2 1 
ATOM   6907 N N   . GLU B 1 339 ? -28.690 47.049 55.131  1.00 38.29  ? 339 GLU B N   1 
ATOM   6908 C CA  . GLU B 1 339 ? -29.081 47.790 56.327  1.00 41.91  ? 339 GLU B CA  1 
ATOM   6909 C C   . GLU B 1 339 ? -30.582 48.020 56.419  1.00 42.03  ? 339 GLU B C   1 
ATOM   6910 O O   . GLU B 1 339 ? -31.081 48.323 57.507  1.00 43.76  ? 339 GLU B O   1 
ATOM   6911 C CB  . GLU B 1 339 ? -28.390 49.154 56.374  1.00 43.20  ? 339 GLU B CB  1 
ATOM   6912 C CG  . GLU B 1 339 ? -26.884 49.145 56.292  1.00 46.85  ? 339 GLU B CG  1 
ATOM   6913 C CD  . GLU B 1 339 ? -26.339 50.538 56.000  1.00 52.30  ? 339 GLU B CD  1 
ATOM   6914 O OE1 . GLU B 1 339 ? -27.097 51.363 55.438  1.00 49.77  ? 339 GLU B OE1 1 
ATOM   6915 O OE2 . GLU B 1 339 ? -25.166 50.811 56.335  1.00 52.81  ? 339 GLU B OE2 1 
ATOM   6916 N N   . SER B 1 340 ? -31.308 47.899 55.305  1.00 38.25  ? 340 SER B N   1 
ATOM   6917 C CA  . SER B 1 340 ? -32.714 48.272 55.257  1.00 41.13  ? 340 SER B CA  1 
ATOM   6918 C C   . SER B 1 340 ? -33.648 47.173 55.745  1.00 41.67  ? 340 SER B C   1 
ATOM   6919 O O   . SER B 1 340 ? -34.837 47.440 55.945  1.00 41.31  ? 340 SER B O   1 
ATOM   6920 C CB  . SER B 1 340 ? -33.102 48.665 53.828  1.00 46.07  ? 340 SER B CB  1 
ATOM   6921 O OG  . SER B 1 340 ? -33.401 47.515 53.050  1.00 53.09  ? 340 SER B OG  1 
ATOM   6922 N N   . VAL B 1 341 ? -33.155 45.952 55.939  1.00 41.82  ? 341 VAL B N   1 
ATOM   6923 C CA  . VAL B 1 341 ? -34.015 44.829 56.282  1.00 39.72  ? 341 VAL B CA  1 
ATOM   6924 C C   . VAL B 1 341 ? -33.516 44.170 57.557  1.00 38.20  ? 341 VAL B C   1 
ATOM   6925 O O   . VAL B 1 341 ? -32.320 44.181 57.864  1.00 35.41  ? 341 VAL B O   1 
ATOM   6926 C CB  . VAL B 1 341 ? -34.086 43.790 55.145  1.00 40.89  ? 341 VAL B CB  1 
ATOM   6927 C CG1 . VAL B 1 341 ? -34.893 44.332 53.973  1.00 39.76  ? 341 VAL B CG1 1 
ATOM   6928 C CG2 . VAL B 1 341 ? -32.681 43.390 54.715  1.00 36.56  ? 341 VAL B CG2 1 
ATOM   6929 N N   . ASP B 1 342 ? -34.454 43.568 58.284  1.00 39.35  ? 342 ASP B N   1 
ATOM   6930 C CA  . ASP B 1 342 ? -34.172 42.836 59.508  1.00 42.88  ? 342 ASP B CA  1 
ATOM   6931 C C   . ASP B 1 342 ? -33.763 41.391 59.258  1.00 42.94  ? 342 ASP B C   1 
ATOM   6932 O O   . ASP B 1 342 ? -33.206 40.753 60.159  1.00 46.17  ? 342 ASP B O   1 
ATOM   6933 C CB  . ASP B 1 342 ? -35.408 42.866 60.414  1.00 56.07  ? 342 ASP B CB  1 
ATOM   6934 C CG  . ASP B 1 342 ? -36.693 42.539 59.658  1.00 70.64  ? 342 ASP B CG  1 
ATOM   6935 O OD1 . ASP B 1 342 ? -36.982 43.211 58.638  1.00 72.39  ? 342 ASP B OD1 1 
ATOM   6936 O OD2 . ASP B 1 342 ? -37.415 41.608 60.082  1.00 77.59  ? 342 ASP B OD2 1 
ATOM   6937 N N   . PHE B 1 343 ? -34.034 40.861 58.069  1.00 36.94  ? 343 PHE B N   1 
ATOM   6938 C CA  . PHE B 1 343 ? -33.710 39.497 57.681  1.00 31.79  ? 343 PHE B CA  1 
ATOM   6939 C C   . PHE B 1 343 ? -32.517 39.517 56.732  1.00 33.48  ? 343 PHE B C   1 
ATOM   6940 O O   . PHE B 1 343 ? -31.947 40.570 56.439  1.00 38.33  ? 343 PHE B O   1 
ATOM   6941 C CB  . PHE B 1 343 ? -34.927 38.817 57.038  1.00 25.40  ? 343 PHE B CB  1 
ATOM   6942 C CG  . PHE B 1 343 ? -35.493 39.574 55.861  1.00 25.35  ? 343 PHE B CG  1 
ATOM   6943 C CD1 . PHE B 1 343 ? -36.345 40.652 56.055  1.00 24.42  ? 343 PHE B CD1 1 
ATOM   6944 C CD2 . PHE B 1 343 ? -35.162 39.216 54.571  1.00 26.78  ? 343 PHE B CD2 1 
ATOM   6945 C CE1 . PHE B 1 343 ? -36.853 41.352 54.977  1.00 25.62  ? 343 PHE B CE1 1 
ATOM   6946 C CE2 . PHE B 1 343 ? -35.666 39.912 53.493  1.00 30.59  ? 343 PHE B CE2 1 
ATOM   6947 C CZ  . PHE B 1 343 ? -36.516 40.981 53.694  1.00 21.86  ? 343 PHE B CZ  1 
ATOM   6948 N N   . GLN B 1 344 ? -32.140 38.332 56.255  1.00 27.71  ? 344 GLN B N   1 
ATOM   6949 C CA  . GLN B 1 344 ? -31.051 38.184 55.299  1.00 28.98  ? 344 GLN B CA  1 
ATOM   6950 C C   . GLN B 1 344 ? -31.603 38.227 53.879  1.00 24.23  ? 344 GLN B C   1 
ATOM   6951 O O   . GLN B 1 344 ? -32.138 37.233 53.393  1.00 21.86  ? 344 GLN B O   1 
ATOM   6952 C CB  . GLN B 1 344 ? -30.299 36.875 55.540  1.00 33.52  ? 344 GLN B CB  1 
ATOM   6953 C CG  . GLN B 1 344 ? -29.653 36.755 56.922  1.00 33.24  ? 344 GLN B CG  1 
ATOM   6954 C CD  . GLN B 1 344 ? -28.714 35.572 57.006  1.00 30.27  ? 344 GLN B CD  1 
ATOM   6955 O OE1 . GLN B 1 344 ? -27.506 35.733 57.210  1.00 25.41  ? 344 GLN B OE1 1 
ATOM   6956 N NE2 . GLN B 1 344 ? -29.257 34.375 56.816  1.00 26.86  ? 344 GLN B NE2 1 
ATOM   6957 N N   . PRO B 1 345 ? -31.491 39.352 53.184  1.00 25.86  ? 345 PRO B N   1 
ATOM   6958 C CA  . PRO B 1 345 ? -32.097 39.456 51.856  1.00 27.05  ? 345 PRO B CA  1 
ATOM   6959 C C   . PRO B 1 345 ? -31.396 38.581 50.826  1.00 24.92  ? 345 PRO B C   1 
ATOM   6960 O O   . PRO B 1 345 ? -30.188 38.341 50.902  1.00 27.26  ? 345 PRO B O   1 
ATOM   6961 C CB  . PRO B 1 345 ? -31.929 40.942 51.516  1.00 23.20  ? 345 PRO B CB  1 
ATOM   6962 C CG  . PRO B 1 345 ? -30.719 41.340 52.255  1.00 24.72  ? 345 PRO B CG  1 
ATOM   6963 C CD  . PRO B 1 345 ? -30.729 40.558 53.541  1.00 26.54  ? 345 PRO B CD  1 
ATOM   6964 N N   . VAL B 1 346 ? -32.171 38.117 49.847  1.00 23.00  ? 346 VAL B N   1 
ATOM   6965 C CA  . VAL B 1 346 ? -31.648 37.448 48.658  1.00 18.26  ? 346 VAL B CA  1 
ATOM   6966 C C   . VAL B 1 346 ? -31.775 38.414 47.485  1.00 16.51  ? 346 VAL B C   1 
ATOM   6967 O O   . VAL B 1 346 ? -32.869 38.909 47.196  1.00 27.74  ? 346 VAL B O   1 
ATOM   6968 C CB  . VAL B 1 346 ? -32.388 36.133 48.371  1.00 24.62  ? 346 VAL B CB  1 
ATOM   6969 C CG1 . VAL B 1 346 ? -31.830 35.477 47.110  1.00 27.27  ? 346 VAL B CG1 1 
ATOM   6970 C CG2 . VAL B 1 346 ? -32.281 35.199 49.571  1.00 22.69  ? 346 VAL B CG2 1 
ATOM   6971 N N   . VAL B 1 347 ? -30.672 38.683 46.802  1.00 21.69  ? 347 VAL B N   1 
ATOM   6972 C CA  . VAL B 1 347 ? -30.625 39.728 45.780  1.00 23.89  ? 347 VAL B CA  1 
ATOM   6973 C C   . VAL B 1 347 ? -30.269 39.091 44.444  1.00 22.19  ? 347 VAL B C   1 
ATOM   6974 O O   . VAL B 1 347 ? -29.101 38.754 44.202  1.00 26.14  ? 347 VAL B O   1 
ATOM   6975 C CB  . VAL B 1 347 ? -29.623 40.827 46.148  1.00 25.71  ? 347 VAL B CB  1 
ATOM   6976 C CG1 . VAL B 1 347 ? -29.602 41.900 45.073  1.00 20.99  ? 347 VAL B CG1 1 
ATOM   6977 C CG2 . VAL B 1 347 ? -29.997 41.432 47.513  1.00 25.04  ? 347 VAL B CG2 1 
ATOM   6978 N N   . PHE B 1 348 ? -31.263 38.948 43.558  1.00 16.05  ? 348 PHE B N   1 
ATOM   6979 C CA  . PHE B 1 348 ? -31.028 38.357 42.248  1.00 18.10  ? 348 PHE B CA  1 
ATOM   6980 C C   . PHE B 1 348 ? -30.656 39.424 41.223  1.00 18.04  ? 348 PHE B C   1 
ATOM   6981 O O   . PHE B 1 348 ? -31.422 40.365 40.974  1.00 24.00  ? 348 PHE B O   1 
ATOM   6982 C CB  . PHE B 1 348 ? -32.241 37.566 41.779  1.00 19.74  ? 348 PHE B CB  1 
ATOM   6983 C CG  . PHE B 1 348 ? -32.138 36.102 42.057  1.00 20.18  ? 348 PHE B CG  1 
ATOM   6984 C CD1 . PHE B 1 348 ? -32.157 35.635 43.355  1.00 19.46  ? 348 PHE B CD1 1 
ATOM   6985 C CD2 . PHE B 1 348 ? -32.021 35.185 41.011  1.00 19.52  ? 348 PHE B CD2 1 
ATOM   6986 C CE1 . PHE B 1 348 ? -32.070 34.281 43.618  1.00 19.86  ? 348 PHE B CE1 1 
ATOM   6987 C CE2 . PHE B 1 348 ? -31.930 33.850 41.264  1.00 27.19  ? 348 PHE B CE2 1 
ATOM   6988 C CZ  . PHE B 1 348 ? -31.958 33.386 42.570  1.00 23.24  ? 348 PHE B CZ  1 
ATOM   6989 N N   . VAL B 1 349 ? -29.473 39.266 40.635  1.00 19.51  ? 349 VAL B N   1 
ATOM   6990 C CA  . VAL B 1 349 ? -28.974 40.098 39.549  1.00 18.74  ? 349 VAL B CA  1 
ATOM   6991 C C   . VAL B 1 349 ? -29.020 39.224 38.301  1.00 22.19  ? 349 VAL B C   1 
ATOM   6992 O O   . VAL B 1 349 ? -28.213 38.297 38.138  1.00 22.39  ? 349 VAL B O   1 
ATOM   6993 C CB  . VAL B 1 349 ? -27.558 40.612 39.835  1.00 20.98  ? 349 VAL B CB  1 
ATOM   6994 C CG1 . VAL B 1 349 ? -27.115 41.612 38.764  1.00 20.70  ? 349 VAL B CG1 1 
ATOM   6995 C CG2 . VAL B 1 349 ? -27.509 41.221 41.227  1.00 24.47  ? 349 VAL B CG2 1 
ATOM   6996 N N   . VAL B 1 350 ? -29.987 39.482 37.429  1.00 21.47  ? 350 VAL B N   1 
ATOM   6997 C CA  . VAL B 1 350 ? -30.245 38.628 36.276  1.00 22.79  ? 350 VAL B CA  1 
ATOM   6998 C C   . VAL B 1 350 ? -30.262 39.505 35.036  1.00 23.94  ? 350 VAL B C   1 
ATOM   6999 O O   . VAL B 1 350 ? -31.083 40.423 34.931  1.00 24.72  ? 350 VAL B O   1 
ATOM   7000 C CB  . VAL B 1 350 ? -31.571 37.865 36.410  1.00 21.08  ? 350 VAL B CB  1 
ATOM   7001 C CG1 . VAL B 1 350 ? -31.744 36.925 35.238  1.00 17.71  ? 350 VAL B CG1 1 
ATOM   7002 C CG2 . VAL B 1 350 ? -31.617 37.117 37.747  1.00 23.11  ? 350 VAL B CG2 1 
ATOM   7003 N N   . LEU B 1 351 ? -29.374 39.219 34.094  1.00 19.04  ? 351 LEU B N   1 
ATOM   7004 C CA  . LEU B 1 351 ? -29.359 39.976 32.851  1.00 22.66  ? 351 LEU B CA  1 
ATOM   7005 C C   . LEU B 1 351 ? -28.603 39.161 31.820  1.00 23.29  ? 351 LEU B C   1 
ATOM   7006 O O   . LEU B 1 351 ? -28.008 38.129 32.137  1.00 26.18  ? 351 LEU B O   1 
ATOM   7007 C CB  . LEU B 1 351 ? -28.729 41.362 33.045  1.00 17.68  ? 351 LEU B CB  1 
ATOM   7008 C CG  . LEU B 1 351 ? -27.245 41.383 33.428  1.00 26.71  ? 351 LEU B CG  1 
ATOM   7009 C CD1 . LEU B 1 351 ? -26.593 42.585 32.805  1.00 26.10  ? 351 LEU B CD1 1 
ATOM   7010 C CD2 . LEU B 1 351 ? -27.037 41.406 34.950  1.00 27.97  ? 351 LEU B CD2 1 
ATOM   7011 N N   . ASN B 1 352 ? -28.604 39.607 30.603  1.00 16.74  ? 352 ASN B N   1 
ATOM   7012 C CA  . ASN B 1 352 ? -27.808 38.993 29.560  1.00 21.44  ? 352 ASN B CA  1 
ATOM   7013 C C   . ASN B 1 352 ? -26.325 39.075 29.905  1.00 22.79  ? 352 ASN B C   1 
ATOM   7014 O O   . ASN B 1 352 ? -25.949 39.962 30.390  1.00 22.94  ? 352 ASN B O   1 
ATOM   7015 C CB  . ASN B 1 352 ? -28.027 39.581 28.199  1.00 21.34  ? 352 ASN B CB  1 
ATOM   7016 C CG  . ASN B 1 352 ? -29.055 38.902 27.492  1.00 31.68  ? 352 ASN B CG  1 
ATOM   7017 O OD1 . ASN B 1 352 ? -28.780 37.938 26.784  1.00 30.19  ? 352 ASN B OD1 1 
ATOM   7018 N ND2 . ASN B 1 352 ? -30.240 39.324 27.667  1.00 25.38  ? 352 ASN B ND2 1 
ATOM   7019 N N   . GLY B 1 353 ? -25.592 38.046 29.642  1.00 21.22  ? 353 GLY B N   1 
ATOM   7020 C CA  . GLY B 1 353 ? -24.197 37.955 30.002  1.00 20.44  ? 353 GLY B CA  1 
ATOM   7021 C C   . GLY B 1 353 ? -23.219 38.259 28.898  1.00 22.07  ? 353 GLY B C   1 
ATOM   7022 O O   . GLY B 1 353 ? -22.009 38.216 29.140  1.00 20.44  ? 353 GLY B O   1 
ATOM   7023 N N   . GLU B 1 354 ? -23.689 38.572 27.691  1.00 17.84  ? 354 GLU B N   1 
ATOM   7024 C CA  . GLU B 1 354 ? -22.783 38.762 26.566  1.00 22.19  ? 354 GLU B CA  1 
ATOM   7025 C C   . GLU B 1 354 ? -22.949 40.082 25.826  1.00 21.15  ? 354 GLU B C   1 
ATOM   7026 O O   . GLU B 1 354 ? -22.112 40.384 24.965  1.00 26.70  ? 354 GLU B O   1 
ATOM   7027 C CB  . GLU B 1 354 ? -22.936 37.609 25.557  1.00 26.61  ? 354 GLU B CB  1 
ATOM   7028 C CG  . GLU B 1 354 ? -24.152 37.741 24.638  1.00 24.01  ? 354 GLU B CG  1 
ATOM   7029 C CD  . GLU B 1 354 ? -25.434 37.237 25.277  1.00 25.80  ? 354 GLU B CD  1 
ATOM   7030 O OE1 . GLU B 1 354 ? -25.950 36.168 24.864  1.00 27.21  ? 354 GLU B OE1 1 
ATOM   7031 O OE2 . GLU B 1 354 ? -25.923 37.906 26.199  1.00 25.35  ? 354 GLU B OE2 1 
ATOM   7032 N N   . ASN B 1 355 ? -23.967 40.885 26.134  1.00 18.93  ? 355 ASN B N   1 
ATOM   7033 C CA  . ASN B 1 355 ? -24.306 42.036 25.299  1.00 20.52  ? 355 ASN B CA  1 
ATOM   7034 C C   . ASN B 1 355 ? -23.761 43.375 25.784  1.00 19.80  ? 355 ASN B C   1 
ATOM   7035 O O   . ASN B 1 355 ? -23.558 44.272 24.955  1.00 24.49  ? 355 ASN B O   1 
ATOM   7036 C CB  . ASN B 1 355 ? -25.830 42.143 25.164  1.00 20.68  ? 355 ASN B CB  1 
ATOM   7037 C CG  . ASN B 1 355 ? -26.401 40.996 24.380  1.00 27.19  ? 355 ASN B CG  1 
ATOM   7038 O OD1 . ASN B 1 355 ? -25.760 40.517 23.436  1.00 23.21  ? 355 ASN B OD1 1 
ATOM   7039 N ND2 . ASN B 1 355 ? -27.581 40.519 24.771  1.00 24.39  ? 355 ASN B ND2 1 
ATOM   7040 N N   . CYS B 1 356 ? -23.538 43.557 27.085  1.00 19.29  ? 356 CYS B N   1 
ATOM   7041 C CA  . CYS B 1 356 ? -23.154 44.874 27.591  1.00 18.58  ? 356 CYS B CA  1 
ATOM   7042 C C   . CYS B 1 356 ? -21.652 45.141 27.514  1.00 22.41  ? 356 CYS B C   1 
ATOM   7043 O O   . CYS B 1 356 ? -21.244 46.303 27.405  1.00 28.24  ? 356 CYS B O   1 
ATOM   7044 C CB  . CYS B 1 356 ? -23.627 45.052 29.040  1.00 20.45  ? 356 CYS B CB  1 
ATOM   7045 S SG  . CYS B 1 356 ? -23.247 43.668 30.146  1.00 23.91  ? 356 CYS B SG  1 
ATOM   7046 N N   . TRP B 1 357 ? -20.822 44.100 27.547  1.00 25.04  ? 357 TRP B N   1 
ATOM   7047 C CA  . TRP B 1 357 ? -19.392 44.304 27.766  1.00 22.77  ? 357 TRP B CA  1 
ATOM   7048 C C   . TRP B 1 357 ? -18.719 45.039 26.606  1.00 23.98  ? 357 TRP B C   1 
ATOM   7049 O O   . TRP B 1 357 ? -17.776 45.800 26.833  1.00 27.49  ? 357 TRP B O   1 
ATOM   7050 C CB  . TRP B 1 357 ? -18.726 42.956 28.026  1.00 24.83  ? 357 TRP B CB  1 
ATOM   7051 C CG  . TRP B 1 357 ? -19.515 42.147 29.007  1.00 28.27  ? 357 TRP B CG  1 
ATOM   7052 C CD1 . TRP B 1 357 ? -20.129 40.959 28.773  1.00 26.65  ? 357 TRP B CD1 1 
ATOM   7053 C CD2 . TRP B 1 357 ? -19.802 42.490 30.372  1.00 29.96  ? 357 TRP B CD2 1 
ATOM   7054 N NE1 . TRP B 1 357 ? -20.776 40.528 29.907  1.00 24.44  ? 357 TRP B NE1 1 
ATOM   7055 C CE2 . TRP B 1 357 ? -20.590 41.452 30.904  1.00 26.44  ? 357 TRP B CE2 1 
ATOM   7056 C CE3 . TRP B 1 357 ? -19.465 43.572 31.194  1.00 32.58  ? 357 TRP B CE3 1 
ATOM   7057 C CZ2 . TRP B 1 357 ? -21.046 41.457 32.220  1.00 19.59  ? 357 TRP B CZ2 1 
ATOM   7058 C CZ3 . TRP B 1 357 ? -19.925 43.581 32.508  1.00 30.59  ? 357 TRP B CZ3 1 
ATOM   7059 C CH2 . TRP B 1 357 ? -20.708 42.526 33.005  1.00 28.70  ? 357 TRP B CH2 1 
ATOM   7060 N N   . GLU B 1 358 ? -19.193 44.849 25.369  1.00 25.16  ? 358 GLU B N   1 
ATOM   7061 C CA  . GLU B 1 358 ? -18.586 45.547 24.231  1.00 23.82  ? 358 GLU B CA  1 
ATOM   7062 C C   . GLU B 1 358 ? -18.679 47.067 24.338  1.00 24.92  ? 358 GLU B C   1 
ATOM   7063 O O   . GLU B 1 358 ? -17.930 47.772 23.649  1.00 23.95  ? 358 GLU B O   1 
ATOM   7064 C CB  . GLU B 1 358 ? -19.238 45.093 22.929  1.00 27.02  ? 358 GLU B CB  1 
ATOM   7065 C CG  . GLU B 1 358 ? -20.718 45.423 22.834  1.00 24.67  ? 358 GLU B CG  1 
ATOM   7066 C CD  . GLU B 1 358 ? -21.442 44.477 21.902  1.00 32.02  ? 358 GLU B CD  1 
ATOM   7067 O OE1 . GLU B 1 358 ? -22.013 44.959 20.910  1.00 34.95  ? 358 GLU B OE1 1 
ATOM   7068 O OE2 . GLU B 1 358 ? -21.430 43.249 22.157  1.00 26.57  ? 358 GLU B OE2 1 
ATOM   7069 N N   . TYR B 1 359 ? -19.583 47.592 25.167  1.00 20.34  ? 359 TYR B N   1 
ATOM   7070 C CA  . TYR B 1 359 ? -19.673 49.027 25.395  1.00 28.30  ? 359 TYR B CA  1 
ATOM   7071 C C   . TYR B 1 359 ? -18.869 49.486 26.601  1.00 26.17  ? 359 TYR B C   1 
ATOM   7072 O O   . TYR B 1 359 ? -18.735 50.692 26.813  1.00 27.83  ? 359 TYR B O   1 
ATOM   7073 C CB  . TYR B 1 359 ? -21.139 49.454 25.555  1.00 31.89  ? 359 TYR B CB  1 
ATOM   7074 C CG  . TYR B 1 359 ? -22.009 49.047 24.382  1.00 33.08  ? 359 TYR B CG  1 
ATOM   7075 C CD1 . TYR B 1 359 ? -21.998 49.775 23.194  1.00 35.19  ? 359 TYR B CD1 1 
ATOM   7076 C CD2 . TYR B 1 359 ? -22.829 47.924 24.457  1.00 32.87  ? 359 TYR B CD2 1 
ATOM   7077 C CE1 . TYR B 1 359 ? -22.791 49.395 22.111  1.00 38.31  ? 359 TYR B CE1 1 
ATOM   7078 C CE2 . TYR B 1 359 ? -23.620 47.540 23.388  1.00 37.17  ? 359 TYR B CE2 1 
ATOM   7079 C CZ  . TYR B 1 359 ? -23.596 48.276 22.217  1.00 42.43  ? 359 TYR B CZ  1 
ATOM   7080 O OH  . TYR B 1 359 ? -24.384 47.887 21.158  1.00 48.89  ? 359 TYR B OH  1 
ATOM   7081 N N   . TYR B 1 360 ? -18.331 48.562 27.393  1.00 22.37  ? 360 TYR B N   1 
ATOM   7082 C CA  . TYR B 1 360 ? -17.452 48.930 28.490  1.00 23.59  ? 360 TYR B CA  1 
ATOM   7083 C C   . TYR B 1 360 ? -16.031 49.149 27.979  1.00 28.88  ? 360 TYR B C   1 
ATOM   7084 O O   . TYR B 1 360 ? -15.602 48.539 26.997  1.00 25.55  ? 360 TYR B O   1 
ATOM   7085 C CB  . TYR B 1 360 ? -17.414 47.833 29.545  1.00 25.79  ? 360 TYR B CB  1 
ATOM   7086 C CG  . TYR B 1 360 ? -18.584 47.745 30.496  1.00 26.34  ? 360 TYR B CG  1 
ATOM   7087 C CD1 . TYR B 1 360 ? -19.872 47.448 30.052  1.00 23.75  ? 360 TYR B CD1 1 
ATOM   7088 C CD2 . TYR B 1 360 ? -18.378 47.894 31.854  1.00 22.87  ? 360 TYR B CD2 1 
ATOM   7089 C CE1 . TYR B 1 360 ? -20.932 47.334 30.957  1.00 27.60  ? 360 TYR B CE1 1 
ATOM   7090 C CE2 . TYR B 1 360 ? -19.409 47.784 32.750  1.00 20.60  ? 360 TYR B CE2 1 
ATOM   7091 C CZ  . TYR B 1 360 ? -20.677 47.504 32.310  1.00 25.27  ? 360 TYR B CZ  1 
ATOM   7092 O OH  . TYR B 1 360 ? -21.665 47.403 33.258  1.00 22.23  ? 360 TYR B OH  1 
ATOM   7093 N N   . GLU B 1 361 ? -15.289 50.007 28.675  1.00 29.40  ? 361 GLU B N   1 
ATOM   7094 C CA  . GLU B 1 361 ? -13.871 50.155 28.380  1.00 33.93  ? 361 GLU B CA  1 
ATOM   7095 C C   . GLU B 1 361 ? -13.146 48.848 28.672  1.00 33.58  ? 361 GLU B C   1 
ATOM   7096 O O   . GLU B 1 361 ? -13.369 48.214 29.712  1.00 27.09  ? 361 GLU B O   1 
ATOM   7097 C CB  . GLU B 1 361 ? -13.267 51.299 29.198  1.00 38.92  ? 361 GLU B CB  1 
ATOM   7098 C CG  . GLU B 1 361 ? -13.950 52.648 28.987  1.00 49.53  ? 361 GLU B CG  1 
ATOM   7099 C CD  . GLU B 1 361 ? -13.931 53.109 27.534  1.00 54.70  ? 361 GLU B CD  1 
ATOM   7100 O OE1 . GLU B 1 361 ? -12.924 52.852 26.846  1.00 58.47  ? 361 GLU B OE1 1 
ATOM   7101 O OE2 . GLU B 1 361 ? -14.917 53.733 27.081  1.00 54.47  ? 361 GLU B OE2 1 
ATOM   7102 N N   . GLU B 1 362 ? -12.287 48.439 27.736  1.00 34.47  ? 362 GLU B N   1 
ATOM   7103 C CA  . GLU B 1 362 ? -11.566 47.168 27.827  1.00 30.83  ? 362 GLU B CA  1 
ATOM   7104 C C   . GLU B 1 362 ? -12.524 45.991 28.029  1.00 30.59  ? 362 GLU B C   1 
ATOM   7105 O O   . GLU B 1 362 ? -12.249 45.076 28.806  1.00 31.02  ? 362 GLU B O   1 
ATOM   7106 C CB  . GLU B 1 362 ? -10.522 47.206 28.942  1.00 36.96  ? 362 GLU B CB  1 
ATOM   7107 C CG  . GLU B 1 362 ? -9.170  47.756 28.535  1.00 51.67  ? 362 GLU B CG  1 
ATOM   7108 C CD  . GLU B 1 362 ? -8.292  48.047 29.736  1.00 63.06  ? 362 GLU B CD  1 
ATOM   7109 O OE1 . GLU B 1 362 ? -7.729  47.089 30.311  1.00 65.92  ? 362 GLU B OE1 1 
ATOM   7110 O OE2 . GLU B 1 362 ? -8.173  49.233 30.113  1.00 67.90  ? 362 GLU B OE2 1 
ATOM   7111 N N   . ASN B 1 363 ? -13.672 46.026 27.348  1.00 31.06  ? 363 ASN B N   1 
ATOM   7112 C CA  . ASN B 1 363 ? -14.561 44.864 27.253  1.00 26.69  ? 363 ASN B CA  1 
ATOM   7113 C C   . ASN B 1 363 ? -15.075 44.407 28.621  1.00 25.40  ? 363 ASN B C   1 
ATOM   7114 O O   . ASN B 1 363 ? -15.339 43.215 28.841  1.00 25.25  ? 363 ASN B O   1 
ATOM   7115 C CB  . ASN B 1 363 ? -13.854 43.714 26.528  1.00 23.83  ? 363 ASN B CB  1 
ATOM   7116 C CG  . ASN B 1 363 ? -14.803 42.643 26.078  1.00 27.04  ? 363 ASN B CG  1 
ATOM   7117 O OD1 . ASN B 1 363 ? -15.992 42.889 25.909  1.00 26.55  ? 363 ASN B OD1 1 
ATOM   7118 N ND2 . ASN B 1 363 ? -14.286 41.427 25.910  1.00 33.45  ? 363 ASN B ND2 1 
ATOM   7119 N N   . GLY B 1 364 ? -15.212 45.345 29.557  1.00 20.80  ? 364 GLY B N   1 
ATOM   7120 C CA  . GLY B 1 364 ? -15.746 45.048 30.871  1.00 27.31  ? 364 GLY B CA  1 
ATOM   7121 C C   . GLY B 1 364 ? -14.781 44.393 31.830  1.00 26.37  ? 364 GLY B C   1 
ATOM   7122 O O   . GLY B 1 364 ? -15.143 44.182 32.995  1.00 26.08  ? 364 GLY B O   1 
ATOM   7123 N N   . ILE B 1 365 ? -13.562 44.084 31.381  1.00 25.97  ? 365 ILE B N   1 
ATOM   7124 C CA  . ILE B 1 365 ? -12.607 43.388 32.243  1.00 25.06  ? 365 ILE B CA  1 
ATOM   7125 C C   . ILE B 1 365 ? -12.247 44.208 33.476  1.00 27.90  ? 365 ILE B C   1 
ATOM   7126 O O   . ILE B 1 365 ? -12.297 43.657 34.588  1.00 23.14  ? 365 ILE B O   1 
ATOM   7127 C CB  . ILE B 1 365 ? -11.377 42.956 31.421  1.00 24.77  ? 365 ILE B CB  1 
ATOM   7128 C CG1 . ILE B 1 365 ? -11.817 42.007 30.302  1.00 25.76  ? 365 ILE B CG1 1 
ATOM   7129 C CG2 . ILE B 1 365 ? -10.336 42.280 32.301  1.00 29.62  ? 365 ILE B CG2 1 
ATOM   7130 C CD1 . ILE B 1 365 ? -10.775 41.830 29.213  1.00 26.93  ? 365 ILE B CD1 1 
ATOM   7131 N N   . PRO B 1 366 ? -11.896 45.501 33.372  1.00 29.91  ? 366 PRO B N   1 
ATOM   7132 C CA  . PRO B 1 366 ? -11.637 46.270 34.600  1.00 30.05  ? 366 PRO B CA  1 
ATOM   7133 C C   . PRO B 1 366 ? -12.817 46.277 35.551  1.00 29.16  ? 366 PRO B C   1 
ATOM   7134 O O   . PRO B 1 366 ? -12.634 46.129 36.764  1.00 33.88  ? 366 PRO B O   1 
ATOM   7135 C CB  . PRO B 1 366 ? -11.318 47.679 34.075  1.00 27.72  ? 366 PRO B CB  1 
ATOM   7136 C CG  . PRO B 1 366 ? -10.799 47.450 32.689  1.00 30.86  ? 366 PRO B CG  1 
ATOM   7137 C CD  . PRO B 1 366 ? -11.631 46.310 32.165  1.00 30.16  ? 366 PRO B CD  1 
ATOM   7138 N N   . PHE B 1 367 ? -14.030 46.434 35.028  1.00 25.77  ? 367 PHE B N   1 
ATOM   7139 C CA  . PHE B 1 367 ? -15.210 46.425 35.881  1.00 25.66  ? 367 PHE B CA  1 
ATOM   7140 C C   . PHE B 1 367 ? -15.378 45.080 36.584  1.00 26.63  ? 367 PHE B C   1 
ATOM   7141 O O   . PHE B 1 367 ? -15.499 45.016 37.812  1.00 23.78  ? 367 PHE B O   1 
ATOM   7142 C CB  . PHE B 1 367 ? -16.454 46.748 35.059  1.00 23.63  ? 367 PHE B CB  1 
ATOM   7143 C CG  . PHE B 1 367 ? -17.731 46.575 35.830  1.00 25.27  ? 367 PHE B CG  1 
ATOM   7144 C CD1 . PHE B 1 367 ? -18.103 47.506 36.787  1.00 25.63  ? 367 PHE B CD1 1 
ATOM   7145 C CD2 . PHE B 1 367 ? -18.547 45.478 35.614  1.00 19.72  ? 367 PHE B CD2 1 
ATOM   7146 C CE1 . PHE B 1 367 ? -19.263 47.352 37.506  1.00 25.55  ? 367 PHE B CE1 1 
ATOM   7147 C CE2 . PHE B 1 367 ? -19.720 45.319 36.334  1.00 21.76  ? 367 PHE B CE2 1 
ATOM   7148 C CZ  . PHE B 1 367 ? -20.085 46.253 37.273  1.00 26.33  ? 367 PHE B CZ  1 
ATOM   7149 N N   . LEU B 1 368 ? -15.412 43.988 35.808  1.00 22.24  ? 368 LEU B N   1 
ATOM   7150 C CA  . LEU B 1 368 ? -15.750 42.689 36.384  1.00 24.35  ? 368 LEU B CA  1 
ATOM   7151 C C   . LEU B 1 368 ? -14.651 42.185 37.312  1.00 27.22  ? 368 LEU B C   1 
ATOM   7152 O O   . LEU B 1 368 ? -14.942 41.591 38.356  1.00 24.49  ? 368 LEU B O   1 
ATOM   7153 C CB  . LEU B 1 368 ? -16.021 41.674 35.272  1.00 22.68  ? 368 LEU B CB  1 
ATOM   7154 C CG  . LEU B 1 368 ? -17.436 41.651 34.675  1.00 22.66  ? 368 LEU B CG  1 
ATOM   7155 C CD1 . LEU B 1 368 ? -17.596 40.484 33.688  1.00 20.72  ? 368 LEU B CD1 1 
ATOM   7156 C CD2 . LEU B 1 368 ? -18.525 41.600 35.757  1.00 20.29  ? 368 LEU B CD2 1 
ATOM   7157 N N   . GLU B 1 369 ? -13.381 42.410 36.952  1.00 26.69  ? 369 GLU B N   1 
ATOM   7158 C CA  . GLU B 1 369 ? -12.297 42.008 37.842  1.00 28.70  ? 369 GLU B CA  1 
ATOM   7159 C C   . GLU B 1 369 ? -12.344 42.799 39.144  1.00 30.28  ? 369 GLU B C   1 
ATOM   7160 O O   . GLU B 1 369 ? -12.100 42.247 40.224  1.00 31.57  ? 369 GLU B O   1 
ATOM   7161 C CB  . GLU B 1 369 ? -10.943 42.175 37.145  1.00 33.40  ? 369 GLU B CB  1 
ATOM   7162 C CG  . GLU B 1 369 ? -10.700 41.159 36.033  1.00 29.26  ? 369 GLU B CG  1 
ATOM   7163 C CD  . GLU B 1 369 ? -9.266  41.142 35.540  1.00 31.33  ? 369 GLU B CD  1 
ATOM   7164 O OE1 . GLU B 1 369 ? -8.518  42.094 35.839  1.00 30.17  ? 369 GLU B OE1 1 
ATOM   7165 O OE2 . GLU B 1 369 ? -8.887  40.163 34.857  1.00 30.69  ? 369 GLU B OE2 1 
ATOM   7166 N N   . LYS B 1 370 ? -12.679 44.087 39.073  1.00 24.37  ? 370 LYS B N   1 
ATOM   7167 C CA  . LYS B 1 370 ? -12.809 44.863 40.302  1.00 28.46  ? 370 LYS B CA  1 
ATOM   7168 C C   . LYS B 1 370 ? -14.031 44.432 41.099  1.00 30.61  ? 370 LYS B C   1 
ATOM   7169 O O   . LYS B 1 370 ? -13.960 44.266 42.322  1.00 36.27  ? 370 LYS B O   1 
ATOM   7170 C CB  . LYS B 1 370 ? -12.885 46.356 39.993  1.00 28.40  ? 370 LYS B CB  1 
ATOM   7171 C CG  . LYS B 1 370 ? -12.919 47.198 41.255  1.00 37.79  ? 370 LYS B CG  1 
ATOM   7172 C CD  . LYS B 1 370 ? -12.915 48.678 40.931  1.00 43.46  ? 370 LYS B CD  1 
ATOM   7173 C CE  . LYS B 1 370 ? -11.772 49.032 39.999  1.00 42.98  ? 370 LYS B CE  1 
ATOM   7174 N NZ  . LYS B 1 370 ? -10.490 48.531 40.550  1.00 45.22  ? 370 LYS B NZ  1 
ATOM   7175 N N   . LEU B 1 371 ? -15.173 44.273 40.425  1.00 22.90  ? 371 LEU B N   1 
ATOM   7176 C CA  . LEU B 1 371 ? -16.386 43.859 41.123  1.00 23.55  ? 371 LEU B CA  1 
ATOM   7177 C C   . LEU B 1 371 ? -16.186 42.523 41.831  1.00 24.57  ? 371 LEU B C   1 
ATOM   7178 O O   . LEU B 1 371 ? -16.460 42.394 43.033  1.00 25.20  ? 371 LEU B O   1 
ATOM   7179 C CB  . LEU B 1 371 ? -17.553 43.777 40.139  1.00 23.09  ? 371 LEU B CB  1 
ATOM   7180 C CG  . LEU B 1 371 ? -18.869 43.277 40.728  1.00 27.20  ? 371 LEU B CG  1 
ATOM   7181 C CD1 . LEU B 1 371 ? -19.510 44.384 41.558  1.00 25.47  ? 371 LEU B CD1 1 
ATOM   7182 C CD2 . LEU B 1 371 ? -19.806 42.777 39.631  1.00 21.81  ? 371 LEU B CD2 1 
ATOM   7183 N N   . TYR B 1 372 ? -15.692 41.519 41.099  1.00 23.31  ? 372 TYR B N   1 
ATOM   7184 C CA  . TYR B 1 372 ? -15.521 40.187 41.669  1.00 24.45  ? 372 TYR B CA  1 
ATOM   7185 C C   . TYR B 1 372 ? -14.485 40.184 42.786  1.00 28.35  ? 372 TYR B C   1 
ATOM   7186 O O   . TYR B 1 372 ? -14.637 39.458 43.776  1.00 27.55  ? 372 TYR B O   1 
ATOM   7187 C CB  . TYR B 1 372 ? -15.116 39.198 40.581  1.00 26.07  ? 372 TYR B CB  1 
ATOM   7188 C CG  . TYR B 1 372 ? -16.196 38.916 39.575  1.00 20.94  ? 372 TYR B CG  1 
ATOM   7189 C CD1 . TYR B 1 372 ? -17.523 39.252 39.827  1.00 23.91  ? 372 TYR B CD1 1 
ATOM   7190 C CD2 . TYR B 1 372 ? -15.895 38.297 38.368  1.00 24.61  ? 372 TYR B CD2 1 
ATOM   7191 C CE1 . TYR B 1 372 ? -18.516 38.978 38.897  1.00 24.13  ? 372 TYR B CE1 1 
ATOM   7192 C CE2 . TYR B 1 372 ? -16.881 38.019 37.439  1.00 22.38  ? 372 TYR B CE2 1 
ATOM   7193 C CZ  . TYR B 1 372 ? -18.191 38.359 37.709  1.00 23.41  ? 372 TYR B CZ  1 
ATOM   7194 O OH  . TYR B 1 372 ? -19.172 38.078 36.774  1.00 18.80  ? 372 TYR B OH  1 
ATOM   7195 N N   . SER B 1 373 ? -13.408 40.961 42.631  1.00 29.49  ? 373 SER B N   1 
ATOM   7196 C CA  . SER B 1 373 ? -12.385 41.011 43.673  1.00 32.82  ? 373 SER B CA  1 
ATOM   7197 C C   . SER B 1 373 ? -12.914 41.688 44.929  1.00 33.11  ? 373 SER B C   1 
ATOM   7198 O O   . SER B 1 373 ? -12.573 41.288 46.050  1.00 32.85  ? 373 SER B O   1 
ATOM   7199 C CB  . SER B 1 373 ? -11.144 41.744 43.169  1.00 33.74  ? 373 SER B CB  1 
ATOM   7200 O OG  . SER B 1 373 ? -10.347 42.128 44.273  1.00 43.53  ? 373 SER B OG  1 
ATOM   7201 N N   . THR B 1 374 ? -13.741 42.722 44.757  1.00 31.76  ? 374 THR B N   1 
ATOM   7202 C CA  . THR B 1 374 ? -14.373 43.378 45.898  1.00 31.97  ? 374 THR B CA  1 
ATOM   7203 C C   . THR B 1 374 ? -15.382 42.460 46.578  1.00 33.14  ? 374 THR B C   1 
ATOM   7204 O O   . THR B 1 374 ? -15.413 42.365 47.814  1.00 29.74  ? 374 THR B O   1 
ATOM   7205 C CB  . THR B 1 374 ? -15.056 44.665 45.441  1.00 26.55  ? 374 THR B CB  1 
ATOM   7206 O OG1 . THR B 1 374 ? -14.091 45.512 44.807  1.00 26.83  ? 374 THR B OG1 1 
ATOM   7207 C CG2 . THR B 1 374 ? -15.674 45.392 46.619  1.00 34.46  ? 374 THR B CG2 1 
ATOM   7208 N N   . LEU B 1 375 ? -16.216 41.779 45.787  1.00 27.77  ? 375 LEU B N   1 
ATOM   7209 C CA  . LEU B 1 375 ? -17.242 40.910 46.356  1.00 25.97  ? 375 LEU B CA  1 
ATOM   7210 C C   . LEU B 1 375 ? -16.631 39.786 47.187  1.00 27.90  ? 375 LEU B C   1 
ATOM   7211 O O   . LEU B 1 375 ? -17.154 39.435 48.251  1.00 28.46  ? 375 LEU B O   1 
ATOM   7212 C CB  . LEU B 1 375 ? -18.115 40.329 45.243  1.00 27.31  ? 375 LEU B CB  1 
ATOM   7213 C CG  . LEU B 1 375 ? -19.122 41.261 44.565  1.00 29.19  ? 375 LEU B CG  1 
ATOM   7214 C CD1 . LEU B 1 375 ? -19.809 40.522 43.424  1.00 27.28  ? 375 LEU B CD1 1 
ATOM   7215 C CD2 . LEU B 1 375 ? -20.156 41.786 45.556  1.00 30.64  ? 375 LEU B CD2 1 
ATOM   7216 N N   . GLU B 1 376 ? -15.524 39.207 46.722  1.00 27.88  ? 376 GLU B N   1 
ATOM   7217 C CA  . GLU B 1 376 ? -14.919 38.121 47.481  1.00 32.04  ? 376 GLU B CA  1 
ATOM   7218 C C   . GLU B 1 376 ? -14.250 38.612 48.757  1.00 35.21  ? 376 GLU B C   1 
ATOM   7219 O O   . GLU B 1 376 ? -13.838 37.786 49.579  1.00 35.49  ? 376 GLU B O   1 
ATOM   7220 C CB  . GLU B 1 376 ? -13.918 37.363 46.611  1.00 33.08  ? 376 GLU B CB  1 
ATOM   7221 C CG  . GLU B 1 376 ? -12.720 38.175 46.225  1.00 38.49  ? 376 GLU B CG  1 
ATOM   7222 C CD  . GLU B 1 376 ? -11.647 37.357 45.536  1.00 42.36  ? 376 GLU B CD  1 
ATOM   7223 O OE1 . GLU B 1 376 ? -11.941 36.221 45.103  1.00 41.14  ? 376 GLU B OE1 1 
ATOM   7224 O OE2 . GLU B 1 376 ? -10.510 37.862 45.433  1.00 42.98  ? 376 GLU B OE2 1 
ATOM   7225 N N   . LYS B 1 377 ? -14.139 39.930 48.940  1.00 33.31  ? 377 LYS B N   1 
ATOM   7226 C CA  . LYS B 1 377 ? -13.571 40.504 50.153  1.00 32.93  ? 377 LYS B CA  1 
ATOM   7227 C C   . LYS B 1 377 ? -14.618 40.921 51.178  1.00 34.89  ? 377 LYS B C   1 
ATOM   7228 O O   . LYS B 1 377 ? -14.275 41.096 52.352  1.00 37.64  ? 377 LYS B O   1 
ATOM   7229 C CB  . LYS B 1 377 ? -12.700 41.722 49.807  1.00 34.40  ? 377 LYS B CB  1 
ATOM   7230 C CG  . LYS B 1 377 ? -11.332 41.367 49.242  1.00 39.29  ? 377 LYS B CG  1 
ATOM   7231 C CD  . LYS B 1 377 ? -10.592 42.605 48.769  1.00 46.15  ? 377 LYS B CD  1 
ATOM   7232 C CE  . LYS B 1 377 ? -9.315  42.226 48.037  1.00 52.86  ? 377 LYS B CE  1 
ATOM   7233 N NZ  . LYS B 1 377 ? -9.573  41.189 46.997  1.00 55.91  ? 377 LYS B NZ  1 
ATOM   7234 N N   . GLU B 1 378 ? -15.881 41.070 50.787  1.00 27.92  ? 378 GLU B N   1 
ATOM   7235 C CA  . GLU B 1 378 ? -16.890 41.562 51.718  1.00 31.91  ? 378 GLU B CA  1 
ATOM   7236 C C   . GLU B 1 378 ? -17.436 40.404 52.549  1.00 34.79  ? 378 GLU B C   1 
ATOM   7237 O O   . GLU B 1 378 ? -18.059 39.487 52.008  1.00 33.42  ? 378 GLU B O   1 
ATOM   7238 C CB  . GLU B 1 378 ? -18.005 42.277 50.965  1.00 31.42  ? 378 GLU B CB  1 
ATOM   7239 C CG  . GLU B 1 378 ? -17.516 43.385 50.037  1.00 34.99  ? 378 GLU B CG  1 
ATOM   7240 C CD  . GLU B 1 378 ? -17.279 44.702 50.751  1.00 40.89  ? 378 GLU B CD  1 
ATOM   7241 O OE1 . GLU B 1 378 ? -17.404 44.749 51.986  1.00 41.41  ? 378 GLU B OE1 1 
ATOM   7242 O OE2 . GLU B 1 378 ? -16.966 45.698 50.068  1.00 45.27  ? 378 GLU B OE2 1 
ATOM   7243 N N   . GLU B 1 379 ? -17.208 40.463 53.868  1.00 34.40  ? 379 GLU B N   1 
ATOM   7244 C CA  . GLU B 1 379 ? -17.660 39.408 54.776  1.00 31.00  ? 379 GLU B CA  1 
ATOM   7245 C C   . GLU B 1 379 ? -19.178 39.340 54.877  1.00 26.32  ? 379 GLU B C   1 
ATOM   7246 O O   . GLU B 1 379 ? -19.728 38.280 55.194  1.00 34.51  ? 379 GLU B O   1 
ATOM   7247 C CB  . GLU B 1 379 ? -17.091 39.633 56.178  1.00 30.55  ? 379 GLU B CB  1 
ATOM   7248 C CG  . GLU B 1 379 ? -15.616 39.329 56.341  1.00 39.71  ? 379 GLU B CG  1 
ATOM   7249 C CD  . GLU B 1 379 ? -15.149 39.579 57.766  1.00 47.75  ? 379 GLU B CD  1 
ATOM   7250 O OE1 . GLU B 1 379 ? -16.003 39.899 58.622  1.00 50.46  ? 379 GLU B OE1 1 
ATOM   7251 O OE2 . GLU B 1 379 ? -13.935 39.460 58.032  1.00 50.70  ? 379 GLU B OE2 1 
ATOM   7252 N N   . TRP B 1 380 ? -19.866 40.452 54.657  1.00 27.08  ? 380 TRP B N   1 
ATOM   7253 C CA  . TRP B 1 380 ? -21.309 40.510 54.831  1.00 23.25  ? 380 TRP B CA  1 
ATOM   7254 C C   . TRP B 1 380 ? -22.070 40.118 53.572  1.00 21.12  ? 380 TRP B C   1 
ATOM   7255 O O   . TRP B 1 380 ? -23.303 40.095 53.598  1.00 24.76  ? 380 TRP B O   1 
ATOM   7256 C CB  . TRP B 1 380 ? -21.723 41.917 55.266  1.00 26.98  ? 380 TRP B CB  1 
ATOM   7257 C CG  . TRP B 1 380 ? -21.210 42.984 54.355  1.00 28.79  ? 380 TRP B CG  1 
ATOM   7258 C CD1 . TRP B 1 380 ? -19.938 43.483 54.306  1.00 34.80  ? 380 TRP B CD1 1 
ATOM   7259 C CD2 . TRP B 1 380 ? -21.954 43.686 53.355  1.00 28.68  ? 380 TRP B CD2 1 
ATOM   7260 N NE1 . TRP B 1 380 ? -19.848 44.452 53.335  1.00 30.42  ? 380 TRP B NE1 1 
ATOM   7261 C CE2 . TRP B 1 380 ? -21.076 44.596 52.741  1.00 31.17  ? 380 TRP B CE2 1 
ATOM   7262 C CE3 . TRP B 1 380 ? -23.283 43.631 52.920  1.00 33.33  ? 380 TRP B CE3 1 
ATOM   7263 C CZ2 . TRP B 1 380 ? -21.483 45.447 51.710  1.00 34.91  ? 380 TRP B CZ2 1 
ATOM   7264 C CZ3 . TRP B 1 380 ? -23.682 44.476 51.903  1.00 35.16  ? 380 TRP B CZ3 1 
ATOM   7265 C CH2 . TRP B 1 380 ? -22.787 45.374 51.312  1.00 30.49  ? 380 TRP B CH2 1 
ATOM   7266 N N   . ILE B 1 381 ? -21.373 39.839 52.471  1.00 23.91  ? 381 ILE B N   1 
ATOM   7267 C CA  . ILE B 1 381 ? -21.979 39.362 51.228  1.00 26.51  ? 381 ILE B CA  1 
ATOM   7268 C C   . ILE B 1 381 ? -21.575 37.911 51.012  1.00 30.75  ? 381 ILE B C   1 
ATOM   7269 O O   . ILE B 1 381 ? -20.387 37.573 51.090  1.00 28.48  ? 381 ILE B O   1 
ATOM   7270 C CB  . ILE B 1 381 ? -21.552 40.214 50.019  1.00 27.97  ? 381 ILE B CB  1 
ATOM   7271 C CG1 . ILE B 1 381 ? -21.916 41.685 50.226  1.00 29.54  ? 381 ILE B CG1 1 
ATOM   7272 C CG2 . ILE B 1 381 ? -22.173 39.646 48.730  1.00 23.83  ? 381 ILE B CG2 1 
ATOM   7273 C CD1 . ILE B 1 381 ? -21.382 42.614 49.145  1.00 25.87  ? 381 ILE B CD1 1 
ATOM   7274 N N   . GLU B 1 382 ? -22.552 37.053 50.720  1.00 24.68  ? 382 GLU B N   1 
ATOM   7275 C CA  . GLU B 1 382 ? -22.273 35.676 50.327  1.00 26.96  ? 382 GLU B CA  1 
ATOM   7276 C C   . GLU B 1 382 ? -22.935 35.410 48.982  1.00 25.08  ? 382 GLU B C   1 
ATOM   7277 O O   . GLU B 1 382 ? -24.167 35.416 48.886  1.00 24.94  ? 382 GLU B O   1 
ATOM   7278 C CB  . GLU B 1 382 ? -22.769 34.694 51.382  1.00 28.74  ? 382 GLU B CB  1 
ATOM   7279 C CG  . GLU B 1 382 ? -22.684 33.250 50.960  1.00 40.26  ? 382 GLU B CG  1 
ATOM   7280 C CD  . GLU B 1 382 ? -22.909 32.307 52.126  1.00 50.07  ? 382 GLU B CD  1 
ATOM   7281 O OE1 . GLU B 1 382 ? -23.046 32.810 53.264  1.00 52.23  ? 382 GLU B OE1 1 
ATOM   7282 O OE2 . GLU B 1 382 ? -22.951 31.072 51.904  1.00 53.04  ? 382 GLU B OE2 1 
ATOM   7283 N N   . THR B 1 383 ? -22.126 35.195 47.942  1.00 25.13  ? 383 THR B N   1 
ATOM   7284 C CA  . THR B 1 383 ? -22.676 34.793 46.653  1.00 23.60  ? 383 THR B CA  1 
ATOM   7285 C C   . THR B 1 383 ? -23.114 33.332 46.703  1.00 26.45  ? 383 THR B C   1 
ATOM   7286 O O   . THR B 1 383 ? -22.508 32.506 47.393  1.00 25.11  ? 383 THR B O   1 
ATOM   7287 C CB  . THR B 1 383 ? -21.662 35.014 45.525  1.00 24.05  ? 383 THR B CB  1 
ATOM   7288 O OG1 . THR B 1 383 ? -20.462 34.272 45.782  1.00 24.90  ? 383 THR B OG1 1 
ATOM   7289 C CG2 . THR B 1 383 ? -21.321 36.501 45.400  1.00 24.14  ? 383 THR B CG2 1 
ATOM   7290 N N   . LEU B 1 384 ? -24.191 33.022 45.966  1.00 23.94  ? 384 LEU B N   1 
ATOM   7291 C CA  . LEU B 1 384 ? -24.846 31.722 46.010  1.00 23.10  ? 384 LEU B CA  1 
ATOM   7292 C C   . LEU B 1 384 ? -25.020 31.154 44.608  1.00 25.00  ? 384 LEU B C   1 
ATOM   7293 O O   . LEU B 1 384 ? -25.245 31.891 43.646  1.00 23.57  ? 384 LEU B O   1 
ATOM   7294 C CB  . LEU B 1 384 ? -26.236 31.806 46.651  1.00 24.87  ? 384 LEU B CB  1 
ATOM   7295 C CG  . LEU B 1 384 ? -26.336 32.433 48.039  1.00 27.30  ? 384 LEU B CG  1 
ATOM   7296 C CD1 . LEU B 1 384 ? -27.778 32.383 48.521  1.00 17.63  ? 384 LEU B CD1 1 
ATOM   7297 C CD2 . LEU B 1 384 ? -25.398 31.704 48.985  1.00 19.06  ? 384 LEU B CD2 1 
ATOM   7298 N N   . THR B 1 385 ? -24.922 29.831 44.506  1.00 21.47  ? 385 THR B N   1 
ATOM   7299 C CA  . THR B 1 385 ? -25.440 29.161 43.324  1.00 22.12  ? 385 THR B CA  1 
ATOM   7300 C C   . THR B 1 385 ? -26.964 29.179 43.375  1.00 20.23  ? 385 THR B C   1 
ATOM   7301 O O   . THR B 1 385 ? -27.562 29.415 44.424  1.00 18.26  ? 385 THR B O   1 
ATOM   7302 C CB  . THR B 1 385 ? -24.956 27.717 43.244  1.00 26.59  ? 385 THR B CB  1 
ATOM   7303 O OG1 . THR B 1 385 ? -25.524 26.969 44.332  1.00 23.86  ? 385 THR B OG1 1 
ATOM   7304 C CG2 . THR B 1 385 ? -23.439 27.643 43.304  1.00 25.22  ? 385 THR B CG2 1 
ATOM   7305 N N   . LEU B 1 386 ? -27.596 28.936 42.222  1.00 21.50  ? 386 LEU B N   1 
ATOM   7306 C CA  . LEU B 1 386 ? -29.052 28.822 42.220  1.00 22.06  ? 386 LEU B CA  1 
ATOM   7307 C C   . LEU B 1 386 ? -29.510 27.732 43.188  1.00 24.89  ? 386 LEU B C   1 
ATOM   7308 O O   . LEU B 1 386 ? -30.513 27.897 43.894  1.00 26.81  ? 386 LEU B O   1 
ATOM   7309 C CB  . LEU B 1 386 ? -29.558 28.543 40.806  1.00 22.75  ? 386 LEU B CB  1 
ATOM   7310 C CG  . LEU B 1 386 ? -29.184 29.565 39.717  1.00 23.63  ? 386 LEU B CG  1 
ATOM   7311 C CD1 . LEU B 1 386 ? -29.578 29.015 38.338  1.00 25.96  ? 386 LEU B CD1 1 
ATOM   7312 C CD2 . LEU B 1 386 ? -29.838 30.921 39.966  1.00 20.96  ? 386 LEU B CD2 1 
ATOM   7313 N N   . GLU B 1 387 ? -28.767 26.622 43.246  1.00 26.62  ? 387 GLU B N   1 
ATOM   7314 C CA  . GLU B 1 387 ? -29.091 25.533 44.170  1.00 30.96  ? 387 GLU B CA  1 
ATOM   7315 C C   . GLU B 1 387 ? -29.142 26.021 45.612  1.00 28.60  ? 387 GLU B C   1 
ATOM   7316 O O   . GLU B 1 387 ? -30.067 25.684 46.365  1.00 26.69  ? 387 GLU B O   1 
ATOM   7317 C CB  . GLU B 1 387 ? -28.061 24.408 44.032  1.00 32.96  ? 387 GLU B CB  1 
ATOM   7318 C CG  . GLU B 1 387 ? -28.249 23.263 45.011  1.00 42.28  ? 387 GLU B CG  1 
ATOM   7319 C CD  . GLU B 1 387 ? -29.371 22.328 44.607  1.00 56.46  ? 387 GLU B CD  1 
ATOM   7320 O OE1 . GLU B 1 387 ? -29.902 22.480 43.485  1.00 61.69  ? 387 GLU B OE1 1 
ATOM   7321 O OE2 . GLU B 1 387 ? -29.723 21.437 45.409  1.00 63.58  ? 387 GLU B OE2 1 
ATOM   7322 N N   . GLU B 1 388 ? -28.129 26.785 46.024  1.00 24.70  ? 388 GLU B N   1 
ATOM   7323 C CA  . GLU B 1 388 ? -28.101 27.302 47.388  1.00 21.71  ? 388 GLU B CA  1 
ATOM   7324 C C   . GLU B 1 388 ? -29.233 28.292 47.633  1.00 22.69  ? 388 GLU B C   1 
ATOM   7325 O O   . GLU B 1 388 ? -29.849 28.278 48.706  1.00 26.64  ? 388 GLU B O   1 
ATOM   7326 C CB  . GLU B 1 388 ? -26.752 27.957 47.670  1.00 23.57  ? 388 GLU B CB  1 
ATOM   7327 C CG  . GLU B 1 388 ? -25.618 26.966 47.791  1.00 27.67  ? 388 GLU B CG  1 
ATOM   7328 C CD  . GLU B 1 388 ? -24.267 27.632 47.745  1.00 33.37  ? 388 GLU B CD  1 
ATOM   7329 O OE1 . GLU B 1 388 ? -24.149 28.682 47.087  1.00 27.35  ? 388 GLU B OE1 1 
ATOM   7330 O OE2 . GLU B 1 388 ? -23.324 27.102 48.372  1.00 38.95  ? 388 GLU B OE2 1 
ATOM   7331 N N   . ALA B 1 389 ? -29.513 29.168 46.658  1.00 24.58  ? 389 ALA B N   1 
ATOM   7332 C CA  . ALA B 1 389 ? -30.606 30.130 46.802  1.00 19.30  ? 389 ALA B CA  1 
ATOM   7333 C C   . ALA B 1 389 ? -31.951 29.425 46.924  1.00 26.77  ? 389 ALA B C   1 
ATOM   7334 O O   . ALA B 1 389 ? -32.810 29.837 47.717  1.00 24.72  ? 389 ALA B O   1 
ATOM   7335 C CB  . ALA B 1 389 ? -30.618 31.093 45.613  1.00 21.26  ? 389 ALA B CB  1 
ATOM   7336 N N   . MET B 1 390 ? -32.152 28.361 46.142  1.00 27.40  ? 390 MET B N   1 
ATOM   7337 C CA  . MET B 1 390 ? -33.421 27.639 46.151  1.00 28.80  ? 390 MET B CA  1 
ATOM   7338 C C   . MET B 1 390 ? -33.661 26.917 47.476  1.00 27.70  ? 390 MET B C   1 
ATOM   7339 O O   . MET B 1 390 ? -34.817 26.781 47.896  1.00 25.06  ? 390 MET B O   1 
ATOM   7340 C CB  . MET B 1 390 ? -33.457 26.656 44.974  1.00 27.31  ? 390 MET B CB  1 
ATOM   7341 C CG  . MET B 1 390 ? -34.667 25.751 44.889  1.00 34.24  ? 390 MET B CG  1 
ATOM   7342 S SD  . MET B 1 390 ? -34.505 24.492 43.588  1.00 39.20  ? 390 MET B SD  1 
ATOM   7343 C CE  . MET B 1 390 ? -33.313 23.377 44.341  1.00 33.81  ? 390 MET B CE  1 
ATOM   7344 N N   . ARG B 1 391 ? -32.600 26.466 48.154  1.00 27.10  ? 391 ARG B N   1 
ATOM   7345 C CA  . ARG B 1 391 ? -32.732 25.606 49.328  1.00 32.21  ? 391 ARG B CA  1 
ATOM   7346 C C   . ARG B 1 391 ? -32.347 26.286 50.635  1.00 30.08  ? 391 ARG B C   1 
ATOM   7347 O O   . ARG B 1 391 ? -32.535 25.691 51.703  1.00 29.93  ? 391 ARG B O   1 
ATOM   7348 C CB  . ARG B 1 391 ? -31.889 24.330 49.157  1.00 40.98  ? 391 ARG B CB  1 
ATOM   7349 C CG  . ARG B 1 391 ? -32.274 23.475 47.955  1.00 47.79  ? 391 ARG B CG  1 
ATOM   7350 C CD  . ARG B 1 391 ? -31.631 22.091 48.000  1.00 58.01  ? 391 ARG B CD  1 
ATOM   7351 N NE  . ARG B 1 391 ? -32.391 21.125 47.209  1.00 65.21  ? 391 ARG B NE  1 
ATOM   7352 C CZ  . ARG B 1 391 ? -33.504 20.526 47.623  1.00 69.51  ? 391 ARG B CZ  1 
ATOM   7353 N NH1 . ARG B 1 391 ? -33.994 20.784 48.832  1.00 68.09  ? 391 ARG B NH1 1 
ATOM   7354 N NH2 . ARG B 1 391 ? -34.131 19.667 46.829  1.00 71.41  ? 391 ARG B NH2 1 
ATOM   7355 N N   . LYS B 1 392 ? -31.836 27.512 50.581  1.00 28.91  ? 392 LYS B N   1 
ATOM   7356 C CA  . LYS B 1 392 ? -31.353 28.189 51.777  1.00 29.06  ? 392 LYS B CA  1 
ATOM   7357 C C   . LYS B 1 392 ? -32.463 28.357 52.806  1.00 27.06  ? 392 LYS B C   1 
ATOM   7358 O O   . LYS B 1 392 ? -33.523 28.917 52.511  1.00 32.91  ? 392 LYS B O   1 
ATOM   7359 C CB  . LYS B 1 392 ? -30.787 29.552 51.402  1.00 29.14  ? 392 LYS B CB  1 
ATOM   7360 C CG  . LYS B 1 392 ? -30.079 30.258 52.527  1.00 33.27  ? 392 LYS B CG  1 
ATOM   7361 C CD  . LYS B 1 392 ? -28.778 30.838 52.026  1.00 39.46  ? 392 LYS B CD  1 
ATOM   7362 C CE  . LYS B 1 392 ? -27.613 29.937 52.361  1.00 40.36  ? 392 LYS B CE  1 
ATOM   7363 N NZ  . LYS B 1 392 ? -27.331 29.986 53.818  1.00 41.00  ? 392 LYS B NZ  1 
ATOM   7364 N N   . GLU B 1 393 ? -32.194 27.912 54.034  1.00 25.56  ? 393 GLU B N   1 
ATOM   7365 C CA  . GLU B 1 393 ? -33.221 27.913 55.072  1.00 34.20  ? 393 GLU B CA  1 
ATOM   7366 C C   . GLU B 1 393 ? -33.395 29.286 55.717  1.00 34.02  ? 393 GLU B C   1 
ATOM   7367 O O   . GLU B 1 393 ? -34.519 29.682 56.047  1.00 39.73  ? 393 GLU B O   1 
ATOM   7368 C CB  . GLU B 1 393 ? -32.887 26.871 56.137  1.00 40.11  ? 393 GLU B CB  1 
ATOM   7369 C CG  . GLU B 1 393 ? -32.907 25.450 55.620  1.00 49.96  ? 393 GLU B CG  1 
ATOM   7370 C CD  . GLU B 1 393 ? -32.720 24.433 56.723  1.00 61.45  ? 393 GLU B CD  1 
ATOM   7371 O OE1 . GLU B 1 393 ? -32.591 24.845 57.895  1.00 66.96  ? 393 GLU B OE1 1 
ATOM   7372 O OE2 . GLU B 1 393 ? -32.703 23.222 56.416  1.00 66.48  ? 393 GLU B OE2 1 
ATOM   7373 N N   . ASP B 1 394 ? -32.309 30.025 55.899  1.00 30.59  ? 394 ASP B N   1 
ATOM   7374 C CA  . ASP B 1 394 ? -32.326 31.229 56.727  1.00 31.48  ? 394 ASP B CA  1 
ATOM   7375 C C   . ASP B 1 394 ? -32.611 32.473 55.880  1.00 26.46  ? 394 ASP B C   1 
ATOM   7376 O O   . ASP B 1 394 ? -31.845 33.427 55.840  1.00 33.33  ? 394 ASP B O   1 
ATOM   7377 C CB  . ASP B 1 394 ? -31.009 31.358 57.484  1.00 33.08  ? 394 ASP B CB  1 
ATOM   7378 C CG  . ASP B 1 394 ? -29.792 31.123 56.592  1.00 47.46  ? 394 ASP B CG  1 
ATOM   7379 O OD1 . ASP B 1 394 ? -29.909 30.349 55.619  1.00 52.09  ? 394 ASP B OD1 1 
ATOM   7380 O OD2 . ASP B 1 394 ? -28.714 31.704 56.866  1.00 47.43  ? 394 ASP B OD2 1 
ATOM   7381 N N   . VAL B 1 395 ? -33.751 32.444 55.190  1.00 29.30  ? 395 VAL B N   1 
ATOM   7382 C CA  . VAL B 1 395 ? -34.206 33.560 54.373  1.00 26.40  ? 395 VAL B CA  1 
ATOM   7383 C C   . VAL B 1 395 ? -35.701 33.732 54.589  1.00 29.95  ? 395 VAL B C   1 
ATOM   7384 O O   . VAL B 1 395 ? -36.397 32.815 55.024  1.00 30.31  ? 395 VAL B O   1 
ATOM   7385 C CB  . VAL B 1 395 ? -33.902 33.353 52.868  1.00 33.56  ? 395 VAL B CB  1 
ATOM   7386 C CG1 . VAL B 1 395 ? -32.389 33.342 52.620  1.00 35.17  ? 395 VAL B CG1 1 
ATOM   7387 C CG2 . VAL B 1 395 ? -34.543 32.056 52.377  1.00 34.69  ? 395 VAL B CG2 1 
ATOM   7388 N N   . LYS B 1 396 ? -36.193 34.928 54.279  1.00 28.49  ? 396 LYS B N   1 
ATOM   7389 C CA  . LYS B 1 396 ? -37.613 35.215 54.389  1.00 26.00  ? 396 LYS B CA  1 
ATOM   7390 C C   . LYS B 1 396 ? -38.341 34.721 53.141  1.00 26.78  ? 396 LYS B C   1 
ATOM   7391 O O   . LYS B 1 396 ? -37.836 34.855 52.020  1.00 28.74  ? 396 LYS B O   1 
ATOM   7392 C CB  . LYS B 1 396 ? -37.836 36.719 54.574  1.00 26.12  ? 396 LYS B CB  1 
ATOM   7393 C CG  . LYS B 1 396 ? -39.271 37.104 54.924  1.00 26.81  ? 396 LYS B CG  1 
ATOM   7394 C CD  . LYS B 1 396 ? -39.295 38.444 55.620  1.00 31.04  ? 396 LYS B CD  1 
ATOM   7395 C CE  . LYS B 1 396 ? -40.687 39.046 55.666  1.00 32.15  ? 396 LYS B CE  1 
ATOM   7396 N NZ  . LYS B 1 396 ? -40.583 40.477 56.079  1.00 37.17  ? 396 LYS B NZ  1 
ATOM   7397 N N   . THR B 1 397 ? -39.539 34.160 53.337  1.00 22.98  ? 397 THR B N   1 
ATOM   7398 C CA  . THR B 1 397 ? -40.310 33.567 52.249  1.00 23.73  ? 397 THR B CA  1 
ATOM   7399 C C   . THR B 1 397 ? -41.733 34.110 52.246  1.00 28.18  ? 397 THR B C   1 
ATOM   7400 O O   . THR B 1 397 ? -42.219 34.639 53.248  1.00 31.32  ? 397 THR B O   1 
ATOM   7401 C CB  . THR B 1 397 ? -40.357 32.026 52.355  1.00 25.99  ? 397 THR B CB  1 
ATOM   7402 O OG1 . THR B 1 397 ? -40.936 31.645 53.615  1.00 28.66  ? 397 THR B OG1 1 
ATOM   7403 C CG2 . THR B 1 397 ? -38.959 31.435 52.247  1.00 22.26  ? 397 THR B CG2 1 
ATOM   7404 N N   . GLU B 1 398 ? -42.411 33.955 51.105  1.00 27.81  ? 398 GLU B N   1 
ATOM   7405 C CA  . GLU B 1 398 ? -43.794 34.393 50.969  1.00 26.92  ? 398 GLU B CA  1 
ATOM   7406 C C   . GLU B 1 398 ? -44.506 33.552 49.916  1.00 25.00  ? 398 GLU B C   1 
ATOM   7407 O O   . GLU B 1 398 ? -43.947 33.267 48.856  1.00 25.07  ? 398 GLU B O   1 
ATOM   7408 C CB  . GLU B 1 398 ? -43.888 35.880 50.589  1.00 26.74  ? 398 GLU B CB  1 
ATOM   7409 C CG  . GLU B 1 398 ? -45.342 36.379 50.466  1.00 31.26  ? 398 GLU B CG  1 
ATOM   7410 C CD  . GLU B 1 398 ? -45.442 37.877 50.175  1.00 44.55  ? 398 GLU B CD  1 
ATOM   7411 O OE1 . GLU B 1 398 ? -44.466 38.601 50.451  1.00 43.94  ? 398 GLU B OE1 1 
ATOM   7412 O OE2 . GLU B 1 398 ? -46.495 38.328 49.660  1.00 50.84  ? 398 GLU B OE2 1 
ATOM   7413 N N   . VAL B 1 399 ? -45.743 33.177 50.198  1.00 22.76  ? 399 VAL B N   1 
ATOM   7414 C CA  . VAL B 1 399 ? -46.557 32.449 49.231  1.00 31.17  ? 399 VAL B CA  1 
ATOM   7415 C C   . VAL B 1 399 ? -47.385 33.445 48.432  1.00 34.97  ? 399 VAL B C   1 
ATOM   7416 O O   . VAL B 1 399 ? -48.026 34.333 49.006  1.00 41.26  ? 399 VAL B O   1 
ATOM   7417 C CB  . VAL B 1 399 ? -47.463 31.421 49.931  1.00 35.03  ? 399 VAL B CB  1 
ATOM   7418 C CG1 . VAL B 1 399 ? -48.425 30.794 48.921  1.00 34.24  ? 399 VAL B CG1 1 
ATOM   7419 C CG2 . VAL B 1 399 ? -46.620 30.347 50.617  1.00 34.75  ? 399 VAL B CG2 1 
ATOM   7420 N N   . ILE B 1 400 ? -47.384 33.295 47.108  1.00 32.74  ? 400 ILE B N   1 
ATOM   7421 C CA  . ILE B 1 400 ? -48.230 34.104 46.237  1.00 33.79  ? 400 ILE B CA  1 
ATOM   7422 C C   . ILE B 1 400 ? -49.113 33.187 45.398  1.00 28.77  ? 400 ILE B C   1 
ATOM   7423 O O   . ILE B 1 400 ? -48.717 32.077 45.025  1.00 30.90  ? 400 ILE B O   1 
ATOM   7424 C CB  . ILE B 1 400 ? -47.395 35.036 45.335  1.00 37.02  ? 400 ILE B CB  1 
ATOM   7425 C CG1 . ILE B 1 400 ? -46.322 34.235 44.600  1.00 42.84  ? 400 ILE B CG1 1 
ATOM   7426 C CG2 . ILE B 1 400 ? -46.769 36.158 46.169  1.00 34.81  ? 400 ILE B CG2 1 
ATOM   7427 C CD1 . ILE B 1 400 ? -45.544 35.049 43.601  1.00 47.54  ? 400 ILE B CD1 1 
ATOM   7428 N N   . GLU B 1 401 ? -50.322 33.663 45.093  1.00 28.07  ? 401 GLU B N   1 
ATOM   7429 C CA  . GLU B 1 401 ? -51.313 32.851 44.394  1.00 25.44  ? 401 GLU B CA  1 
ATOM   7430 C C   . GLU B 1 401 ? -51.574 33.283 42.961  1.00 27.31  ? 401 GLU B C   1 
ATOM   7431 O O   . GLU B 1 401 ? -52.233 32.538 42.223  1.00 30.66  ? 401 GLU B O   1 
ATOM   7432 C CB  . GLU B 1 401 ? -52.646 32.856 45.160  1.00 34.86  ? 401 GLU B CB  1 
ATOM   7433 C CG  . GLU B 1 401 ? -52.530 32.365 46.586  1.00 44.30  ? 401 GLU B CG  1 
ATOM   7434 C CD  . GLU B 1 401 ? -52.319 30.862 46.679  1.00 49.00  ? 401 GLU B CD  1 
ATOM   7435 O OE1 . GLU B 1 401 ? -51.907 30.405 47.765  1.00 51.20  ? 401 GLU B OE1 1 
ATOM   7436 O OE2 . GLU B 1 401 ? -52.567 30.138 45.682  1.00 46.10  ? 401 GLU B OE2 1 
ATOM   7437 N N   . SER B 1 402 ? -51.087 34.449 42.538  1.00 25.14  ? 402 SER B N   1 
ATOM   7438 C CA  . SER B 1 402 ? -51.422 34.939 41.208  1.00 27.86  ? 402 SER B CA  1 
ATOM   7439 C C   . SER B 1 402 ? -50.372 35.940 40.746  1.00 31.49  ? 402 SER B C   1 
ATOM   7440 O O   . SER B 1 402 ? -49.896 36.757 41.538  1.00 29.34  ? 402 SER B O   1 
ATOM   7441 C CB  . SER B 1 402 ? -52.812 35.591 41.208  1.00 24.21  ? 402 SER B CB  1 
ATOM   7442 O OG  . SER B 1 402 ? -53.173 36.057 39.920  1.00 30.47  ? 402 SER B OG  1 
ATOM   7443 N N   . VAL B 1 403 ? -50.016 35.867 39.463  1.00 32.09  ? 403 VAL B N   1 
ATOM   7444 C CA  . VAL B 1 403 ? -49.151 36.858 38.832  1.00 31.34  ? 403 VAL B CA  1 
ATOM   7445 C C   . VAL B 1 403 ? -49.895 37.452 37.645  1.00 31.77  ? 403 VAL B C   1 
ATOM   7446 O O   . VAL B 1 403 ? -50.745 36.795 37.030  1.00 35.23  ? 403 VAL B O   1 
ATOM   7447 C CB  . VAL B 1 403 ? -47.789 36.278 38.377  1.00 31.53  ? 403 VAL B CB  1 
ATOM   7448 C CG1 . VAL B 1 403 ? -47.025 35.671 39.556  1.00 24.43  ? 403 VAL B CG1 1 
ATOM   7449 C CG2 . VAL B 1 403 ? -47.985 35.253 37.271  1.00 31.57  ? 403 VAL B CG2 1 
ATOM   7450 N N   . LYS B 1 404 ? -49.573 38.705 37.328  1.00 26.42  ? 404 LYS B N   1 
ATOM   7451 C CA  . LYS B 1 404 ? -50.073 39.341 36.115  1.00 28.56  ? 404 LYS B CA  1 
ATOM   7452 C C   . LYS B 1 404 ? -49.062 39.141 34.989  1.00 28.27  ? 404 LYS B C   1 
ATOM   7453 O O   . LYS B 1 404 ? -47.880 39.485 35.141  1.00 28.65  ? 404 LYS B O   1 
ATOM   7454 C CB  . LYS B 1 404 ? -50.345 40.825 36.354  1.00 32.71  ? 404 LYS B CB  1 
ATOM   7455 C CG  . LYS B 1 404 ? -51.644 41.077 37.121  1.00 47.35  ? 404 LYS B CG  1 
ATOM   7456 C CD  . LYS B 1 404 ? -52.874 40.661 36.300  1.00 54.68  ? 404 LYS B CD  1 
ATOM   7457 C CE  . LYS B 1 404 ? -53.467 39.321 36.757  1.00 57.02  ? 404 LYS B CE  1 
ATOM   7458 N NZ  . LYS B 1 404 ? -54.954 39.304 36.676  1.00 58.81  ? 404 LYS B NZ  1 
ATOM   7459 N N   . ALA B 1 405 ? -49.526 38.597 33.862  1.00 24.67  ? 405 ALA B N   1 
ATOM   7460 C CA  . ALA B 1 405 ? -48.616 38.177 32.801  1.00 26.09  ? 405 ALA B CA  1 
ATOM   7461 C C   . ALA B 1 405 ? -47.841 39.363 32.249  1.00 24.21  ? 405 ALA B C   1 
ATOM   7462 O O   . ALA B 1 405 ? -48.390 40.443 32.041  1.00 23.16  ? 405 ALA B O   1 
ATOM   7463 C CB  . ALA B 1 405 ? -49.381 37.483 31.673  1.00 27.06  ? 405 ALA B CB  1 
ATOM   7464 N N   . GLY B 1 406 ? -46.553 39.155 32.018  1.00 26.23  ? 406 GLY B N   1 
ATOM   7465 C CA  . GLY B 1 406 ? -45.715 40.216 31.503  1.00 22.56  ? 406 GLY B CA  1 
ATOM   7466 C C   . GLY B 1 406 ? -44.335 39.690 31.177  1.00 26.25  ? 406 GLY B C   1 
ATOM   7467 O O   . GLY B 1 406 ? -44.084 38.484 31.195  1.00 22.78  ? 406 GLY B O   1 
ATOM   7468 N N   . THR B 1 407 ? -43.452 40.626 30.842  1.00 20.90  ? 407 THR B N   1 
ATOM   7469 C CA  . THR B 1 407 ? -42.041 40.377 30.597  1.00 21.29  ? 407 THR B CA  1 
ATOM   7470 C C   . THR B 1 407 ? -41.248 41.408 31.382  1.00 21.33  ? 407 THR B C   1 
ATOM   7471 O O   . THR B 1 407 ? -41.817 42.260 32.070  1.00 19.04  ? 407 THR B O   1 
ATOM   7472 C CB  . THR B 1 407 ? -41.691 40.493 29.110  1.00 24.85  ? 407 THR B CB  1 
ATOM   7473 O OG1 . THR B 1 407 ? -41.795 41.870 28.732  1.00 23.95  ? 407 THR B OG1 1 
ATOM   7474 C CG2 . THR B 1 407 ? -42.630 39.634 28.226  1.00 21.20  ? 407 THR B CG2 1 
ATOM   7475 N N   . TRP B 1 408 ? -39.921 41.359 31.256  1.00 20.78  ? 408 TRP B N   1 
ATOM   7476 C CA  . TRP B 1 408 ? -39.098 42.389 31.875  1.00 19.30  ? 408 TRP B CA  1 
ATOM   7477 C C   . TRP B 1 408 ? -39.017 43.661 31.031  1.00 25.41  ? 408 TRP B C   1 
ATOM   7478 O O   . TRP B 1 408 ? -38.368 44.632 31.446  1.00 27.09  ? 408 TRP B O   1 
ATOM   7479 C CB  . TRP B 1 408 ? -37.695 41.845 32.178  1.00 20.29  ? 408 TRP B CB  1 
ATOM   7480 C CG  . TRP B 1 408 ? -36.910 41.304 31.011  1.00 20.50  ? 408 TRP B CG  1 
ATOM   7481 C CD1 . TRP B 1 408 ? -37.273 41.293 29.699  1.00 22.34  ? 408 TRP B CD1 1 
ATOM   7482 C CD2 . TRP B 1 408 ? -35.615 40.692 31.077  1.00 23.37  ? 408 TRP B CD2 1 
ATOM   7483 N NE1 . TRP B 1 408 ? -36.285 40.709 28.942  1.00 30.58  ? 408 TRP B NE1 1 
ATOM   7484 C CE2 . TRP B 1 408 ? -35.257 40.328 29.765  1.00 24.06  ? 408 TRP B CE2 1 
ATOM   7485 C CE3 . TRP B 1 408 ? -34.729 40.409 32.126  1.00 18.43  ? 408 TRP B CE3 1 
ATOM   7486 C CZ2 . TRP B 1 408 ? -34.041 39.707 29.464  1.00 24.77  ? 408 TRP B CZ2 1 
ATOM   7487 C CZ3 . TRP B 1 408 ? -33.527 39.788 31.828  1.00 20.93  ? 408 TRP B CZ3 1 
ATOM   7488 C CH2 . TRP B 1 408 ? -33.196 39.437 30.511  1.00 20.31  ? 408 TRP B CH2 1 
ATOM   7489 N N   . PHE B 1 409 ? -39.666 43.690 29.868  1.00 21.52  ? 409 PHE B N   1 
ATOM   7490 C CA  . PHE B 1 409 ? -39.865 44.939 29.135  1.00 32.95  ? 409 PHE B CA  1 
ATOM   7491 C C   . PHE B 1 409 ? -41.169 45.569 29.628  1.00 28.73  ? 409 PHE B C   1 
ATOM   7492 O O   . PHE B 1 409 ? -42.260 45.247 29.154  1.00 31.06  ? 409 PHE B O   1 
ATOM   7493 C CB  . PHE B 1 409 ? -39.886 44.687 27.633  1.00 41.98  ? 409 PHE B CB  1 
ATOM   7494 C CG  . PHE B 1 409 ? -40.147 45.926 26.815  1.00 50.06  ? 409 PHE B CG  1 
ATOM   7495 C CD1 . PHE B 1 409 ? -39.104 46.769 26.464  1.00 46.27  ? 409 PHE B CD1 1 
ATOM   7496 C CD2 . PHE B 1 409 ? -41.437 46.248 26.405  1.00 53.35  ? 409 PHE B CD2 1 
ATOM   7497 C CE1 . PHE B 1 409 ? -39.338 47.908 25.718  1.00 50.03  ? 409 PHE B CE1 1 
ATOM   7498 C CE2 . PHE B 1 409 ? -41.678 47.388 25.660  1.00 56.56  ? 409 PHE B CE2 1 
ATOM   7499 C CZ  . PHE B 1 409 ? -40.626 48.219 25.314  1.00 55.44  ? 409 PHE B CZ  1 
ATOM   7500 N N   . ASP B 1 410 ? -41.052 46.470 30.607  1.00 28.89  ? 410 ASP B N   1 
ATOM   7501 C CA  . ASP B 1 410 ? -42.169 47.251 31.158  1.00 35.53  ? 410 ASP B CA  1 
ATOM   7502 C C   . ASP B 1 410 ? -43.298 46.387 31.712  1.00 33.96  ? 410 ASP B C   1 
ATOM   7503 O O   . ASP B 1 410 ? -44.429 46.866 31.842  1.00 31.51  ? 410 ASP B O   1 
ATOM   7504 C CB  . ASP B 1 410 ? -42.753 48.218 30.121  1.00 40.94  ? 410 ASP B CB  1 
ATOM   7505 C CG  . ASP B 1 410 ? -41.738 49.214 29.614  1.00 50.60  ? 410 ASP B CG  1 
ATOM   7506 O OD1 . ASP B 1 410 ? -40.787 49.525 30.360  1.00 52.95  ? 410 ASP B OD1 1 
ATOM   7507 O OD2 . ASP B 1 410 ? -41.896 49.686 28.468  1.00 53.08  ? 410 ASP B OD2 1 
ATOM   7508 N N   . GLY B 1 411 ? -43.029 45.119 32.027  1.00 22.98  ? 411 GLY B N   1 
ATOM   7509 C CA  . GLY B 1 411 ? -44.081 44.228 32.486  1.00 21.21  ? 411 GLY B CA  1 
ATOM   7510 C C   . GLY B 1 411 ? -45.161 43.887 31.480  1.00 24.87  ? 411 GLY B C   1 
ATOM   7511 O O   . GLY B 1 411 ? -46.247 43.469 31.882  1.00 33.44  ? 411 GLY B O   1 
ATOM   7512 N N   . ASN B 1 412 ? -44.914 44.056 30.182  1.00 29.37  ? 412 ASN B N   1 
ATOM   7513 C CA  . ASN B 1 412 ? -45.932 43.763 29.180  1.00 27.41  ? 412 ASN B CA  1 
ATOM   7514 C C   . ASN B 1 412 ? -45.279 43.122 27.961  1.00 28.41  ? 412 ASN B C   1 
ATOM   7515 O O   . ASN B 1 412 ? -44.068 42.885 27.932  1.00 30.59  ? 412 ASN B O   1 
ATOM   7516 C CB  . ASN B 1 412 ? -46.728 45.020 28.808  1.00 29.43  ? 412 ASN B CB  1 
ATOM   7517 C CG  . ASN B 1 412 ? -45.867 46.123 28.221  1.00 29.73  ? 412 ASN B CG  1 
ATOM   7518 O OD1 . ASN B 1 412 ? -45.094 45.908 27.284  1.00 31.29  ? 412 ASN B OD1 1 
ATOM   7519 N ND2 . ASN B 1 412 ? -46.023 47.324 28.752  1.00 30.84  ? 412 ASN B ND2 1 
ATOM   7520 N N   . PHE B 1 413 ? -46.097 42.842 26.942  1.00 24.34  ? 413 PHE B N   1 
ATOM   7521 C CA  . PHE B 1 413 ? -45.653 42.125 25.751  1.00 31.40  ? 413 PHE B CA  1 
ATOM   7522 C C   . PHE B 1 413 ? -45.528 43.019 24.522  1.00 32.62  ? 413 PHE B C   1 
ATOM   7523 O O   . PHE B 1 413 ? -45.356 42.500 23.410  1.00 27.55  ? 413 PHE B O   1 
ATOM   7524 C CB  . PHE B 1 413 ? -46.605 40.963 25.448  1.00 33.70  ? 413 PHE B CB  1 
ATOM   7525 C CG  . PHE B 1 413 ? -46.661 39.932 26.537  1.00 30.50  ? 413 PHE B CG  1 
ATOM   7526 C CD1 . PHE B 1 413 ? -45.735 38.897 26.581  1.00 26.88  ? 413 PHE B CD1 1 
ATOM   7527 C CD2 . PHE B 1 413 ? -47.628 40.000 27.519  1.00 25.83  ? 413 PHE B CD2 1 
ATOM   7528 C CE1 . PHE B 1 413 ? -45.774 37.955 27.596  1.00 22.99  ? 413 PHE B CE1 1 
ATOM   7529 C CE2 . PHE B 1 413 ? -47.680 39.058 28.533  1.00 26.54  ? 413 PHE B CE2 1 
ATOM   7530 C CZ  . PHE B 1 413 ? -46.754 38.037 28.574  1.00 23.93  ? 413 PHE B CZ  1 
ATOM   7531 N N   . LEU B 1 414 ? -45.601 44.345 24.684  1.00 21.00  ? 414 LEU B N   1 
ATOM   7532 C CA  . LEU B 1 414 ? -45.633 45.223 23.520  1.00 33.69  ? 414 LEU B CA  1 
ATOM   7533 C C   . LEU B 1 414 ? -44.358 45.164 22.684  1.00 32.23  ? 414 LEU B C   1 
ATOM   7534 O O   . LEU B 1 414 ? -44.364 45.660 21.554  1.00 33.48  ? 414 LEU B O   1 
ATOM   7535 C CB  . LEU B 1 414 ? -45.904 46.665 23.960  1.00 36.11  ? 414 LEU B CB  1 
ATOM   7536 C CG  . LEU B 1 414 ? -47.290 46.869 24.567  1.00 35.43  ? 414 LEU B CG  1 
ATOM   7537 C CD1 . LEU B 1 414 ? -47.592 48.345 24.737  1.00 36.39  ? 414 LEU B CD1 1 
ATOM   7538 C CD2 . LEU B 1 414 ? -48.358 46.183 23.712  1.00 35.22  ? 414 LEU B CD2 1 
ATOM   7539 N N   . LYS B 1 415 ? -43.283 44.554 23.186  1.00 34.83  ? 415 LYS B N   1 
ATOM   7540 C CA  . LYS B 1 415 ? -42.047 44.464 22.413  1.00 33.63  ? 415 LYS B CA  1 
ATOM   7541 C C   . LYS B 1 415 ? -42.082 43.353 21.366  1.00 31.22  ? 415 LYS B C   1 
ATOM   7542 O O   . LYS B 1 415 ? -41.242 43.346 20.455  1.00 29.14  ? 415 LYS B O   1 
ATOM   7543 C CB  . LYS B 1 415 ? -40.865 44.269 23.372  1.00 37.68  ? 415 LYS B CB  1 
ATOM   7544 C CG  . LYS B 1 415 ? -39.497 44.168 22.729  1.00 47.03  ? 415 LYS B CG  1 
ATOM   7545 C CD  . LYS B 1 415 ? -39.019 45.512 22.216  1.00 56.14  ? 415 LYS B CD  1 
ATOM   7546 C CE  . LYS B 1 415 ? -38.203 45.347 20.946  1.00 60.88  ? 415 LYS B CE  1 
ATOM   7547 N NZ  . LYS B 1 415 ? -37.534 46.618 20.556  1.00 63.07  ? 415 LYS B NZ  1 
ATOM   7548 N N   . TRP B 1 416 ? -43.035 42.424 21.454  1.00 23.11  ? 416 TRP B N   1 
ATOM   7549 C CA  . TRP B 1 416 ? -43.094 41.304 20.520  1.00 24.76  ? 416 TRP B CA  1 
ATOM   7550 C C   . TRP B 1 416 ? -44.441 41.163 19.833  1.00 29.03  ? 416 TRP B C   1 
ATOM   7551 O O   . TRP B 1 416 ? -44.598 40.278 18.983  1.00 27.71  ? 416 TRP B O   1 
ATOM   7552 C CB  . TRP B 1 416 ? -42.768 39.984 21.230  1.00 22.19  ? 416 TRP B CB  1 
ATOM   7553 C CG  . TRP B 1 416 ? -41.471 40.031 21.996  1.00 28.52  ? 416 TRP B CG  1 
ATOM   7554 C CD1 . TRP B 1 416 ? -40.249 39.556 21.583  1.00 29.27  ? 416 TRP B CD1 1 
ATOM   7555 C CD2 . TRP B 1 416 ? -41.265 40.586 23.302  1.00 30.09  ? 416 TRP B CD2 1 
ATOM   7556 N NE1 . TRP B 1 416 ? -39.300 39.784 22.556  1.00 24.28  ? 416 TRP B NE1 1 
ATOM   7557 C CE2 . TRP B 1 416 ? -39.896 40.414 23.620  1.00 30.23  ? 416 TRP B CE2 1 
ATOM   7558 C CE3 . TRP B 1 416 ? -42.104 41.214 24.235  1.00 27.31  ? 416 TRP B CE3 1 
ATOM   7559 C CZ2 . TRP B 1 416 ? -39.349 40.848 24.831  1.00 31.92  ? 416 TRP B CZ2 1 
ATOM   7560 C CZ3 . TRP B 1 416 ? -41.558 41.643 25.444  1.00 26.61  ? 416 TRP B CZ3 1 
ATOM   7561 C CH2 . TRP B 1 416 ? -40.193 41.458 25.728  1.00 31.81  ? 416 TRP B CH2 1 
ATOM   7562 N N   . ILE B 1 417 ? -45.412 42.003 20.178  1.00 25.62  ? 417 ILE B N   1 
ATOM   7563 C CA  . ILE B 1 417 ? -46.753 41.908 19.622  1.00 29.78  ? 417 ILE B CA  1 
ATOM   7564 C C   . ILE B 1 417 ? -47.442 43.227 19.913  1.00 34.55  ? 417 ILE B C   1 
ATOM   7565 O O   . ILE B 1 417 ? -47.067 43.942 20.847  1.00 32.51  ? 417 ILE B O   1 
ATOM   7566 C CB  . ILE B 1 417 ? -47.518 40.706 20.233  1.00 31.03  ? 417 ILE B CB  1 
ATOM   7567 C CG1 . ILE B 1 417 ? -48.720 40.321 19.367  1.00 34.64  ? 417 ILE B CG1 1 
ATOM   7568 C CG2 . ILE B 1 417 ? -47.940 41.002 21.677  1.00 35.18  ? 417 ILE B CG2 1 
ATOM   7569 C CD1 . ILE B 1 417 ? -49.219 38.909 19.644  1.00 31.11  ? 417 ILE B CD1 1 
ATOM   7570 N N   . GLY B 1 418 ? -48.446 43.559 19.107  1.00 37.51  ? 418 GLY B N   1 
ATOM   7571 C CA  . GLY B 1 418 ? -49.288 44.709 19.372  1.00 39.25  ? 418 GLY B CA  1 
ATOM   7572 C C   . GLY B 1 418 ? -49.181 45.856 18.389  1.00 42.88  ? 418 GLY B C   1 
ATOM   7573 O O   . GLY B 1 418 ? -50.008 46.776 18.462  1.00 43.59  ? 418 GLY B O   1 
ATOM   7574 N N   . ASN B 1 419 ? -48.206 45.882 17.486  1.00 45.00  ? 419 ASN B N   1 
ATOM   7575 C CA  . ASN B 1 419 ? -48.198 46.880 16.426  1.00 49.16  ? 419 ASN B CA  1 
ATOM   7576 C C   . ASN B 1 419 ? -48.243 46.177 15.073  1.00 49.94  ? 419 ASN B C   1 
ATOM   7577 O O   . ASN B 1 419 ? -48.077 44.958 14.981  1.00 50.11  ? 419 ASN B O   1 
ATOM   7578 C CB  . ASN B 1 419 ? -46.988 47.827 16.543  1.00 51.93  ? 419 ASN B CB  1 
ATOM   7579 C CG  . ASN B 1 419 ? -45.665 47.166 16.188  1.00 54.05  ? 419 ASN B CG  1 
ATOM   7580 O OD1 . ASN B 1 419 ? -45.597 45.973 15.907  1.00 60.07  ? 419 ASN B OD1 1 
ATOM   7581 N ND2 . ASN B 1 419 ? -44.599 47.956 16.201  1.00 53.34  ? 419 ASN B ND2 1 
ATOM   7582 N N   . LYS B 1 420 ? -48.467 46.970 14.018  1.00 43.27  ? 420 LYS B N   1 
ATOM   7583 C CA  . LYS B 1 420 ? -48.770 46.408 12.703  1.00 41.32  ? 420 LYS B CA  1 
ATOM   7584 C C   . LYS B 1 420 ? -47.688 45.442 12.235  1.00 42.94  ? 420 LYS B C   1 
ATOM   7585 O O   . LYS B 1 420 ? -47.990 44.355 11.726  1.00 40.64  ? 420 LYS B O   1 
ATOM   7586 C CB  . LYS B 1 420 ? -48.948 47.534 11.682  1.00 36.88  ? 420 LYS B CB  1 
ATOM   7587 C CG  . LYS B 1 420 ? -49.304 47.044 10.289  1.00 44.87  ? 420 LYS B CG  1 
ATOM   7588 C CD  . LYS B 1 420 ? -49.081 48.120 9.239   1.00 51.99  ? 420 LYS B CD  1 
ATOM   7589 C CE  . LYS B 1 420 ? -48.678 47.511 7.903   1.00 57.13  ? 420 LYS B CE  1 
ATOM   7590 N NZ  . LYS B 1 420 ? -49.290 48.217 6.744   1.00 59.89  ? 420 LYS B NZ  1 
ATOM   7591 N N   . GLU B 1 421 ? -46.423 45.826 12.395  1.00 44.97  ? 421 GLU B N   1 
ATOM   7592 C CA  . GLU B 1 421 ? -45.315 45.004 11.925  1.00 48.46  ? 421 GLU B CA  1 
ATOM   7593 C C   . GLU B 1 421 ? -45.220 43.706 12.722  1.00 45.03  ? 421 GLU B C   1 
ATOM   7594 O O   . GLU B 1 421 ? -45.157 42.613 12.145  1.00 43.03  ? 421 GLU B O   1 
ATOM   7595 C CB  . GLU B 1 421 ? -44.007 45.801 12.017  1.00 57.93  ? 421 GLU B CB  1 
ATOM   7596 C CG  . GLU B 1 421 ? -44.109 47.304 11.654  1.00 64.72  ? 421 GLU B CG  1 
ATOM   7597 C CD  . GLU B 1 421 ? -44.718 48.172 12.759  1.00 70.35  ? 421 GLU B CD  1 
ATOM   7598 O OE1 . GLU B 1 421 ? -45.810 47.824 13.255  1.00 73.08  ? 421 GLU B OE1 1 
ATOM   7599 O OE2 . GLU B 1 421 ? -44.113 49.205 13.124  1.00 72.84  ? 421 GLU B OE2 1 
ATOM   7600 N N   . LYS B 1 422 ? -45.220 43.807 14.056  1.00 42.60  ? 422 LYS B N   1 
ATOM   7601 C CA  . LYS B 1 422 ? -45.087 42.609 14.879  1.00 35.45  ? 422 LYS B CA  1 
ATOM   7602 C C   . LYS B 1 422 ? -46.293 41.699 14.729  1.00 35.63  ? 422 LYS B C   1 
ATOM   7603 O O   . LYS B 1 422 ? -46.148 40.471 14.758  1.00 37.00  ? 422 LYS B O   1 
ATOM   7604 C CB  . LYS B 1 422 ? -44.888 42.985 16.348  1.00 36.84  ? 422 LYS B CB  1 
ATOM   7605 C CG  . LYS B 1 422 ? -43.561 43.686 16.643  1.00 37.75  ? 422 LYS B CG  1 
ATOM   7606 C CD  . LYS B 1 422 ? -43.571 44.325 18.023  1.00 35.44  ? 422 LYS B CD  1 
ATOM   7607 C CE  . LYS B 1 422 ? -42.398 45.281 18.194  1.00 35.20  ? 422 LYS B CE  1 
ATOM   7608 N NZ  . LYS B 1 422 ? -41.097 44.612 17.912  1.00 34.68  ? 422 LYS B NZ  1 
ATOM   7609 N N   . ASN B 1 423 ? -47.484 42.277 14.548  1.00 32.44  ? 423 ASN B N   1 
ATOM   7610 C CA  . ASN B 1 423 ? -48.676 41.461 14.362  1.00 29.54  ? 423 ASN B CA  1 
ATOM   7611 C C   . ASN B 1 423 ? -48.591 40.646 13.077  1.00 35.18  ? 423 ASN B C   1 
ATOM   7612 O O   . ASN B 1 423 ? -48.970 39.470 13.056  1.00 37.29  ? 423 ASN B O   1 
ATOM   7613 C CB  . ASN B 1 423 ? -49.921 42.348 14.379  1.00 28.86  ? 423 ASN B CB  1 
ATOM   7614 C CG  . ASN B 1 423 ? -50.313 42.760 15.783  1.00 31.67  ? 423 ASN B CG  1 
ATOM   7615 O OD1 . ASN B 1 423 ? -49.755 42.255 16.759  1.00 26.98  ? 423 ASN B OD1 1 
ATOM   7616 N ND2 . ASN B 1 423 ? -51.273 43.678 15.897  1.00 31.85  ? 423 ASN B ND2 1 
ATOM   7617 N N   . GLU B 1 424 ? -48.068 41.242 12.002  1.00 38.88  ? 424 GLU B N   1 
ATOM   7618 C CA  . GLU B 1 424 ? -47.982 40.525 10.735  1.00 41.89  ? 424 GLU B CA  1 
ATOM   7619 C C   . GLU B 1 424 ? -47.122 39.274 10.862  1.00 37.78  ? 424 GLU B C   1 
ATOM   7620 O O   . GLU B 1 424 ? -47.444 38.228 10.286  1.00 39.41  ? 424 GLU B O   1 
ATOM   7621 C CB  . GLU B 1 424 ? -47.444 41.453 9.645   1.00 51.89  ? 424 GLU B CB  1 
ATOM   7622 C CG  . GLU B 1 424 ? -48.313 41.495 8.388   1.00 65.09  ? 424 GLU B CG  1 
ATOM   7623 C CD  . GLU B 1 424 ? -48.149 40.257 7.517   1.00 72.59  ? 424 GLU B CD  1 
ATOM   7624 O OE1 . GLU B 1 424 ? -49.157 39.753 6.983   1.00 75.11  ? 424 GLU B OE1 1 
ATOM   7625 O OE2 . GLU B 1 424 ? -47.005 39.792 7.358   1.00 75.14  ? 424 GLU B OE2 1 
ATOM   7626 N N   . TYR B 1 425 ? -46.033 39.356 11.630  1.00 32.59  ? 425 TYR B N   1 
ATOM   7627 C CA  . TYR B 1 425 ? -45.211 38.178 11.871  1.00 35.85  ? 425 TYR B CA  1 
ATOM   7628 C C   . TYR B 1 425 ? -46.008 37.083 12.573  1.00 34.35  ? 425 TYR B C   1 
ATOM   7629 O O   . TYR B 1 425 ? -45.947 35.908 12.186  1.00 31.70  ? 425 TYR B O   1 
ATOM   7630 C CB  . TYR B 1 425 ? -43.985 38.562 12.693  1.00 36.73  ? 425 TYR B CB  1 
ATOM   7631 C CG  . TYR B 1 425 ? -42.728 38.691 11.876  1.00 32.80  ? 425 TYR B CG  1 
ATOM   7632 C CD1 . TYR B 1 425 ? -42.738 39.326 10.642  1.00 26.19  ? 425 TYR B CD1 1 
ATOM   7633 C CD2 . TYR B 1 425 ? -41.531 38.176 12.341  1.00 30.65  ? 425 TYR B CD2 1 
ATOM   7634 C CE1 . TYR B 1 425 ? -41.584 39.448 9.903   1.00 31.22  ? 425 TYR B CE1 1 
ATOM   7635 C CE2 . TYR B 1 425 ? -40.378 38.292 11.612  1.00 29.82  ? 425 TYR B CE2 1 
ATOM   7636 C CZ  . TYR B 1 425 ? -40.409 38.922 10.395  1.00 35.28  ? 425 TYR B CZ  1 
ATOM   7637 O OH  . TYR B 1 425 ? -39.244 39.037 9.681   1.00 42.69  ? 425 TYR B OH  1 
ATOM   7638 N N   . TRP B 1 426 ? -46.759 37.452 13.617  1.00 25.87  ? 426 TRP B N   1 
ATOM   7639 C CA  . TRP B 1 426 ? -47.615 36.476 14.283  1.00 29.68  ? 426 TRP B CA  1 
ATOM   7640 C C   . TRP B 1 426 ? -48.645 35.911 13.316  1.00 32.65  ? 426 TRP B C   1 
ATOM   7641 O O   . TRP B 1 426 ? -48.896 34.701 13.301  1.00 30.64  ? 426 TRP B O   1 
ATOM   7642 C CB  . TRP B 1 426 ? -48.289 37.108 15.503  1.00 27.94  ? 426 TRP B CB  1 
ATOM   7643 C CG  . TRP B 1 426 ? -47.329 37.340 16.630  1.00 23.44  ? 426 TRP B CG  1 
ATOM   7644 C CD1 . TRP B 1 426 ? -46.709 38.517 16.954  1.00 28.79  ? 426 TRP B CD1 1 
ATOM   7645 C CD2 . TRP B 1 426 ? -46.860 36.369 17.577  1.00 27.62  ? 426 TRP B CD2 1 
ATOM   7646 N NE1 . TRP B 1 426 ? -45.891 38.339 18.043  1.00 28.53  ? 426 TRP B NE1 1 
ATOM   7647 C CE2 . TRP B 1 426 ? -45.967 37.029 18.446  1.00 29.67  ? 426 TRP B CE2 1 
ATOM   7648 C CE3 . TRP B 1 426 ? -47.114 35.007 17.775  1.00 28.95  ? 426 TRP B CE3 1 
ATOM   7649 C CZ2 . TRP B 1 426 ? -45.319 36.373 19.493  1.00 29.51  ? 426 TRP B CZ2 1 
ATOM   7650 C CZ3 . TRP B 1 426 ? -46.468 34.353 18.818  1.00 29.74  ? 426 TRP B CZ3 1 
ATOM   7651 C CH2 . TRP B 1 426 ? -45.577 35.034 19.659  1.00 30.06  ? 426 TRP B CH2 1 
ATOM   7652 N N   . LYS B 1 427 ? -49.231 36.773 12.482  1.00 35.62  ? 427 LYS B N   1 
ATOM   7653 C CA  . LYS B 1 427 ? -50.143 36.304 11.445  1.00 37.21  ? 427 LYS B CA  1 
ATOM   7654 C C   . LYS B 1 427 ? -49.471 35.274 10.539  1.00 38.02  ? 427 LYS B C   1 
ATOM   7655 O O   . LYS B 1 427 ? -50.049 34.218 10.259  1.00 39.30  ? 427 LYS B O   1 
ATOM   7656 C CB  . LYS B 1 427 ? -50.655 37.492 10.631  1.00 38.65  ? 427 LYS B CB  1 
ATOM   7657 C CG  . LYS B 1 427 ? -51.936 37.216 9.863   1.00 41.16  ? 427 LYS B CG  1 
ATOM   7658 C CD  . LYS B 1 427 ? -52.429 38.474 9.166   1.00 48.38  ? 427 LYS B CD  1 
ATOM   7659 C CE  . LYS B 1 427 ? -51.818 38.583 7.785   1.00 54.17  ? 427 LYS B CE  1 
ATOM   7660 N NZ  . LYS B 1 427 ? -52.288 39.752 6.981   1.00 54.89  ? 427 LYS B NZ  1 
ATOM   7661 N N   . ILE B 1 428 ? -48.247 35.560 10.077  1.00 40.16  ? 428 ILE B N   1 
ATOM   7662 C CA  . ILE B 1 428 ? -47.513 34.582 9.276   1.00 37.25  ? 428 ILE B CA  1 
ATOM   7663 C C   . ILE B 1 428 ? -47.293 33.307 10.072  1.00 33.19  ? 428 ILE B C   1 
ATOM   7664 O O   . ILE B 1 428 ? -47.478 32.196 9.560   1.00 34.38  ? 428 ILE B O   1 
ATOM   7665 C CB  . ILE B 1 428 ? -46.171 35.161 8.797   1.00 36.61  ? 428 ILE B CB  1 
ATOM   7666 C CG1 . ILE B 1 428 ? -46.384 36.301 7.808   1.00 35.51  ? 428 ILE B CG1 1 
ATOM   7667 C CG2 . ILE B 1 428 ? -45.294 34.057 8.203   1.00 34.43  ? 428 ILE B CG2 1 
ATOM   7668 C CD1 . ILE B 1 428 ? -45.321 37.331 7.931   1.00 37.59  ? 428 ILE B CD1 1 
ATOM   7669 N N   . LEU B 1 429 ? -46.884 33.448 11.334  1.00 33.33  ? 429 LEU B N   1 
ATOM   7670 C CA  . LEU B 1 429 ? -46.670 32.281 12.180  1.00 36.27  ? 429 LEU B CA  1 
ATOM   7671 C C   . LEU B 1 429 ? -47.947 31.464 12.320  1.00 33.31  ? 429 LEU B C   1 
ATOM   7672 O O   . LEU B 1 429 ? -47.915 30.233 12.207  1.00 32.65  ? 429 LEU B O   1 
ATOM   7673 C CB  . LEU B 1 429 ? -46.152 32.712 13.555  1.00 30.18  ? 429 LEU B CB  1 
ATOM   7674 C CG  . LEU B 1 429 ? -45.693 31.575 14.479  1.00 33.26  ? 429 LEU B CG  1 
ATOM   7675 C CD1 . LEU B 1 429 ? -44.385 30.963 13.990  1.00 40.54  ? 429 LEU B CD1 1 
ATOM   7676 C CD2 . LEU B 1 429 ? -45.547 32.045 15.927  1.00 29.59  ? 429 LEU B CD2 1 
ATOM   7677 N N   . ILE B 1 430 ? -49.082 32.129 12.564  1.00 37.05  ? 430 ILE B N   1 
ATOM   7678 C CA  . ILE B 1 430 ? -50.350 31.416 12.725  1.00 32.73  ? 430 ILE B CA  1 
ATOM   7679 C C   . ILE B 1 430 ? -50.702 30.657 11.450  1.00 36.91  ? 430 ILE B C   1 
ATOM   7680 O O   . ILE B 1 430 ? -51.063 29.474 11.497  1.00 37.95  ? 430 ILE B O   1 
ATOM   7681 C CB  . ILE B 1 430 ? -51.469 32.394 13.140  1.00 33.33  ? 430 ILE B CB  1 
ATOM   7682 C CG1 . ILE B 1 430 ? -51.348 32.747 14.623  1.00 33.60  ? 430 ILE B CG1 1 
ATOM   7683 C CG2 . ILE B 1 430 ? -52.841 31.808 12.883  1.00 32.65  ? 430 ILE B CG2 1 
ATOM   7684 C CD1 . ILE B 1 430 ? -51.759 34.168 14.932  1.00 36.66  ? 430 ILE B CD1 1 
ATOM   7685 N N   . GLU B 1 431 ? -50.569 31.307 10.290  1.00 37.54  ? 431 GLU B N   1 
ATOM   7686 C CA  . GLU B 1 431 ? -50.957 30.654 9.043   1.00 38.53  ? 431 GLU B CA  1 
ATOM   7687 C C   . GLU B 1 431 ? -50.017 29.501 8.698   1.00 34.64  ? 431 GLU B C   1 
ATOM   7688 O O   . GLU B 1 431 ? -50.462 28.456 8.203   1.00 38.27  ? 431 GLU B O   1 
ATOM   7689 C CB  . GLU B 1 431 ? -51.004 31.672 7.903   1.00 46.85  ? 431 GLU B CB  1 
ATOM   7690 C CG  . GLU B 1 431 ? -52.285 32.487 7.878   1.00 57.26  ? 431 GLU B CG  1 
ATOM   7691 C CD  . GLU B 1 431 ? -53.524 31.646 8.150   1.00 70.08  ? 431 GLU B CD  1 
ATOM   7692 O OE1 . GLU B 1 431 ? -53.699 30.606 7.476   1.00 74.28  ? 431 GLU B OE1 1 
ATOM   7693 O OE2 . GLU B 1 431 ? -54.324 32.023 9.035   1.00 75.39  ? 431 GLU B OE2 1 
ATOM   7694 N N   . ALA B 1 432 ? -48.718 29.658 8.963   1.00 24.54  ? 432 ALA B N   1 
ATOM   7695 C CA  . ALA B 1 432 ? -47.774 28.574 8.713   1.00 27.52  ? 432 ALA B CA  1 
ATOM   7696 C C   . ALA B 1 432 ? -47.960 27.427 9.692   1.00 33.16  ? 432 ALA B C   1 
ATOM   7697 O O   . ALA B 1 432 ? -47.728 26.266 9.336   1.00 34.97  ? 432 ALA B O   1 
ATOM   7698 C CB  . ALA B 1 432 ? -46.340 29.096 8.789   1.00 29.20  ? 432 ALA B CB  1 
ATOM   7699 N N   . LYS B 1 433 ? -48.362 27.728 10.932  1.00 33.98  ? 433 LYS B N   1 
ATOM   7700 C CA  . LYS B 1 433 ? -48.603 26.670 11.908  1.00 33.70  ? 433 LYS B CA  1 
ATOM   7701 C C   . LYS B 1 433 ? -49.680 25.703 11.435  1.00 37.70  ? 433 LYS B C   1 
ATOM   7702 O O   . LYS B 1 433 ? -49.577 24.495 11.685  1.00 36.29  ? 433 LYS B O   1 
ATOM   7703 C CB  . LYS B 1 433 ? -48.979 27.280 13.260  1.00 33.58  ? 433 LYS B CB  1 
ATOM   7704 C CG  . LYS B 1 433 ? -49.452 26.272 14.296  1.00 33.01  ? 433 LYS B CG  1 
ATOM   7705 C CD  . LYS B 1 433 ? -48.333 25.366 14.801  1.00 30.02  ? 433 LYS B CD  1 
ATOM   7706 C CE  . LYS B 1 433 ? -48.894 24.292 15.725  1.00 38.75  ? 433 LYS B CE  1 
ATOM   7707 N NZ  . LYS B 1 433 ? -47.840 23.382 16.276  1.00 40.24  ? 433 LYS B NZ  1 
ATOM   7708 N N   . LYS B 1 434 ? -50.705 26.205 10.733  1.00 39.08  ? 434 LYS B N   1 
ATOM   7709 C CA  . LYS B 1 434 ? -51.772 25.345 10.224  1.00 43.78  ? 434 LYS B CA  1 
ATOM   7710 C C   . LYS B 1 434 ? -51.269 24.309 9.227   1.00 45.30  ? 434 LYS B C   1 
ATOM   7711 O O   . LYS B 1 434 ? -51.925 23.280 9.038   1.00 46.77  ? 434 LYS B O   1 
ATOM   7712 C CB  . LYS B 1 434 ? -52.861 26.192 9.558   1.00 46.22  ? 434 LYS B CB  1 
ATOM   7713 C CG  . LYS B 1 434 ? -53.402 27.295 10.440  1.00 44.99  ? 434 LYS B CG  1 
ATOM   7714 C CD  . LYS B 1 434 ? -54.393 28.178 9.713   1.00 50.53  ? 434 LYS B CD  1 
ATOM   7715 C CE  . LYS B 1 434 ? -55.104 29.077 10.705  1.00 55.82  ? 434 LYS B CE  1 
ATOM   7716 N NZ  . LYS B 1 434 ? -55.781 30.228 10.046  1.00 62.21  ? 434 LYS B NZ  1 
ATOM   7717 N N   . LYS B 1 435 ? -50.135 24.561 8.575   1.00 47.00  ? 435 LYS B N   1 
ATOM   7718 C CA  . LYS B 1 435 ? -49.578 23.650 7.582   1.00 47.93  ? 435 LYS B CA  1 
ATOM   7719 C C   . LYS B 1 435 ? -48.172 23.188 7.957   1.00 46.65  ? 435 LYS B C   1 
ATOM   7720 O O   . LYS B 1 435 ? -47.420 22.727 7.093   1.00 46.54  ? 435 LYS B O   1 
ATOM   7721 C CB  . LYS B 1 435 ? -49.573 24.311 6.201   1.00 51.15  ? 435 LYS B CB  1 
ATOM   7722 C CG  . LYS B 1 435 ? -50.922 24.864 5.770   1.00 57.23  ? 435 LYS B CG  1 
ATOM   7723 C CD  . LYS B 1 435 ? -50.823 25.630 4.458   1.00 61.13  ? 435 LYS B CD  1 
ATOM   7724 C CE  . LYS B 1 435 ? -50.411 24.721 3.309   1.00 62.56  ? 435 LYS B CE  1 
ATOM   7725 N NZ  . LYS B 1 435 ? -50.899 25.214 1.986   1.00 63.07  ? 435 LYS B NZ  1 
ATOM   7726 N N   . ALA B 1 436 ? -47.799 23.309 9.226   1.00 43.84  ? 436 ALA B N   1 
ATOM   7727 C CA  . ALA B 1 436 ? -46.471 22.898 9.654   1.00 45.30  ? 436 ALA B CA  1 
ATOM   7728 C C   . ALA B 1 436 ? -46.357 21.379 9.645   1.00 40.34  ? 436 ALA B C   1 
ATOM   7729 O O   . ALA B 1 436 ? -47.307 20.668 9.975   1.00 41.89  ? 436 ALA B O   1 
ATOM   7730 C CB  . ALA B 1 436 ? -46.172 23.444 11.050  1.00 46.83  ? 436 ALA B CB  1 
ATOM   7731 N N   . LYS B 1 437 ? -45.181 20.882 9.261   1.00 35.77  ? 437 LYS B N   1 
ATOM   7732 C CA  . LYS B 1 437 ? -44.940 19.447 9.186   1.00 37.39  ? 437 LYS B CA  1 
ATOM   7733 C C   . LYS B 1 437 ? -43.662 19.019 9.889   1.00 40.05  ? 437 LYS B C   1 
ATOM   7734 O O   . LYS B 1 437 ? -43.327 17.828 9.859   1.00 40.95  ? 437 LYS B O   1 
ATOM   7735 C CB  . LYS B 1 437 ? -44.899 18.990 7.719   1.00 40.93  ? 437 LYS B CB  1 
ATOM   7736 C CG  . LYS B 1 437 ? -46.225 19.186 6.985   1.00 49.92  ? 437 LYS B CG  1 
ATOM   7737 C CD  . LYS B 1 437 ? -46.019 19.495 5.515   1.00 56.13  ? 437 LYS B CD  1 
ATOM   7738 C CE  . LYS B 1 437 ? -47.319 19.943 4.855   1.00 58.42  ? 437 LYS B CE  1 
ATOM   7739 N NZ  . LYS B 1 437 ? -47.683 21.364 5.155   1.00 55.41  ? 437 LYS B NZ  1 
ATOM   7740 N N   . ASN B 1 438 ? -42.946 19.941 10.521  1.00 37.42  ? 438 ASN B N   1 
ATOM   7741 C CA  . ASN B 1 438 ? -41.726 19.610 11.240  1.00 38.55  ? 438 ASN B CA  1 
ATOM   7742 C C   . ASN B 1 438 ? -41.495 20.681 12.300  1.00 38.35  ? 438 ASN B C   1 
ATOM   7743 O O   . ASN B 1 438 ? -42.282 21.621 12.448  1.00 42.76  ? 438 ASN B O   1 
ATOM   7744 C CB  . ASN B 1 438 ? -40.541 19.485 10.282  1.00 35.34  ? 438 ASN B CB  1 
ATOM   7745 C CG  . ASN B 1 438 ? -40.333 20.733 9.464   1.00 37.53  ? 438 ASN B CG  1 
ATOM   7746 O OD1 . ASN B 1 438 ? -39.904 21.765 9.986   1.00 35.78  ? 438 ASN B OD1 1 
ATOM   7747 N ND2 . ASN B 1 438 ? -40.644 20.656 8.177   1.00 38.60  ? 438 ASN B ND2 1 
ATOM   7748 N N   . ASP B 1 439 ? -40.401 20.532 13.038  1.00 36.09  ? 439 ASP B N   1 
ATOM   7749 C CA  . ASP B 1 439 ? -40.128 21.389 14.181  1.00 32.48  ? 439 ASP B CA  1 
ATOM   7750 C C   . ASP B 1 439 ? -39.512 22.728 13.807  1.00 31.81  ? 439 ASP B C   1 
ATOM   7751 O O   . ASP B 1 439 ? -39.156 23.485 14.709  1.00 33.07  ? 439 ASP B O   1 
ATOM   7752 C CB  . ASP B 1 439 ? -39.224 20.662 15.176  1.00 31.53  ? 439 ASP B CB  1 
ATOM   7753 C CG  . ASP B 1 439 ? -39.988 19.671 16.025  1.00 39.12  ? 439 ASP B CG  1 
ATOM   7754 O OD1 . ASP B 1 439 ? -41.235 19.729 16.017  1.00 38.20  ? 439 ASP B OD1 1 
ATOM   7755 O OD2 . ASP B 1 439 ? -39.349 18.828 16.687  1.00 45.28  ? 439 ASP B OD2 1 
ATOM   7756 N N   . TYR B 1 440 ? -39.374 23.058 12.520  1.00 33.81  ? 440 TYR B N   1 
ATOM   7757 C CA  . TYR B 1 440 ? -38.922 24.402 12.198  1.00 33.48  ? 440 TYR B CA  1 
ATOM   7758 C C   . TYR B 1 440 ? -39.961 25.441 12.592  1.00 34.71  ? 440 TYR B C   1 
ATOM   7759 O O   . TYR B 1 440 ? -39.608 26.612 12.764  1.00 31.78  ? 440 TYR B O   1 
ATOM   7760 C CB  . TYR B 1 440 ? -38.551 24.515 10.715  1.00 38.21  ? 440 TYR B CB  1 
ATOM   7761 C CG  . TYR B 1 440 ? -37.079 24.237 10.462  1.00 37.60  ? 440 TYR B CG  1 
ATOM   7762 C CD1 . TYR B 1 440 ? -36.104 25.163 10.814  1.00 38.01  ? 440 TYR B CD1 1 
ATOM   7763 C CD2 . TYR B 1 440 ? -36.663 23.037 9.899   1.00 35.81  ? 440 TYR B CD2 1 
ATOM   7764 C CE1 . TYR B 1 440 ? -34.751 24.904 10.599  1.00 41.10  ? 440 TYR B CE1 1 
ATOM   7765 C CE2 . TYR B 1 440 ? -35.315 22.773 9.679   1.00 35.04  ? 440 TYR B CE2 1 
ATOM   7766 C CZ  . TYR B 1 440 ? -34.367 23.704 10.034  1.00 40.63  ? 440 TYR B CZ  1 
ATOM   7767 O OH  . TYR B 1 440 ? -33.030 23.436 9.817   1.00 41.53  ? 440 TYR B OH  1 
ATOM   7768 N N   . ILE B 1 441 ? -41.220 25.029 12.785  1.00 32.99  ? 441 ILE B N   1 
ATOM   7769 C CA  . ILE B 1 441 ? -42.216 25.934 13.353  1.00 34.55  ? 441 ILE B CA  1 
ATOM   7770 C C   . ILE B 1 441 ? -41.814 26.367 14.759  1.00 31.88  ? 441 ILE B C   1 
ATOM   7771 O O   . ILE B 1 441 ? -42.113 27.491 15.179  1.00 29.95  ? 441 ILE B O   1 
ATOM   7772 C CB  . ILE B 1 441 ? -43.626 25.291 13.325  1.00 35.69  ? 441 ILE B CB  1 
ATOM   7773 C CG1 . ILE B 1 441 ? -44.708 26.364 13.494  1.00 35.86  ? 441 ILE B CG1 1 
ATOM   7774 C CG2 . ILE B 1 441 ? -43.780 24.211 14.387  1.00 31.32  ? 441 ILE B CG2 1 
ATOM   7775 C CD1 . ILE B 1 441 ? -44.802 27.315 12.311  1.00 32.90  ? 441 ILE B CD1 1 
ATOM   7776 N N   . LEU B 1 442 ? -41.124 25.502 15.508  1.00 28.99  ? 442 LEU B N   1 
ATOM   7777 C CA  . LEU B 1 442 ? -40.658 25.914 16.829  1.00 29.21  ? 442 LEU B CA  1 
ATOM   7778 C C   . LEU B 1 442 ? -39.538 26.945 16.720  1.00 26.40  ? 442 LEU B C   1 
ATOM   7779 O O   . LEU B 1 442 ? -39.452 27.858 17.549  1.00 28.80  ? 442 LEU B O   1 
ATOM   7780 C CB  . LEU B 1 442 ? -40.192 24.700 17.637  1.00 28.51  ? 442 LEU B CB  1 
ATOM   7781 C CG  . LEU B 1 442 ? -41.218 23.582 17.855  1.00 32.33  ? 442 LEU B CG  1 
ATOM   7782 C CD1 . LEU B 1 442 ? -40.544 22.341 18.432  1.00 34.52  ? 442 LEU B CD1 1 
ATOM   7783 C CD2 . LEU B 1 442 ? -42.359 24.045 18.747  1.00 34.85  ? 442 LEU B CD2 1 
ATOM   7784 N N   . VAL B 1 443 ? -38.652 26.799 15.725  1.00 27.88  ? 443 VAL B N   1 
ATOM   7785 C CA  . VAL B 1 443 ? -37.589 27.785 15.522  1.00 26.91  ? 443 VAL B CA  1 
ATOM   7786 C C   . VAL B 1 443 ? -38.192 29.159 15.283  1.00 28.94  ? 443 VAL B C   1 
ATOM   7787 O O   . VAL B 1 443 ? -37.729 30.163 15.840  1.00 29.16  ? 443 VAL B O   1 
ATOM   7788 C CB  . VAL B 1 443 ? -36.673 27.381 14.349  1.00 24.68  ? 443 VAL B CB  1 
ATOM   7789 C CG1 . VAL B 1 443 ? -35.574 28.434 14.158  1.00 21.55  ? 443 VAL B CG1 1 
ATOM   7790 C CG2 . VAL B 1 443 ? -36.077 25.998 14.568  1.00 27.18  ? 443 VAL B CG2 1 
ATOM   7791 N N   . ALA B 1 444 ? -39.246 29.216 14.458  1.00 30.49  ? 444 ALA B N   1 
ATOM   7792 C CA  . ALA B 1 444 ? -39.902 30.471 14.108  1.00 29.36  ? 444 ALA B CA  1 
ATOM   7793 C C   . ALA B 1 444 ? -40.662 31.070 15.282  1.00 28.59  ? 444 ALA B C   1 
ATOM   7794 O O   . ALA B 1 444 ? -41.017 32.251 15.235  1.00 28.24  ? 444 ALA B O   1 
ATOM   7795 C CB  . ALA B 1 444 ? -40.842 30.256 12.918  1.00 27.62  ? 444 ALA B CB  1 
ATOM   7796 N N   . GLU B 1 445 ? -40.896 30.297 16.340  1.00 28.55  ? 445 GLU B N   1 
ATOM   7797 C CA  . GLU B 1 445 ? -41.538 30.836 17.533  1.00 31.18  ? 445 GLU B CA  1 
ATOM   7798 C C   . GLU B 1 445 ? -40.560 31.518 18.489  1.00 27.81  ? 445 GLU B C   1 
ATOM   7799 O O   . GLU B 1 445 ? -40.989 32.021 19.532  1.00 28.77  ? 445 GLU B O   1 
ATOM   7800 C CB  . GLU B 1 445 ? -42.305 29.722 18.249  1.00 32.70  ? 445 GLU B CB  1 
ATOM   7801 C CG  . GLU B 1 445 ? -43.519 29.226 17.451  1.00 31.95  ? 445 GLU B CG  1 
ATOM   7802 C CD  . GLU B 1 445 ? -43.964 27.822 17.845  1.00 36.29  ? 445 GLU B CD  1 
ATOM   7803 O OE1 . GLU B 1 445 ? -43.416 27.278 18.827  1.00 32.70  ? 445 GLU B OE1 1 
ATOM   7804 O OE2 . GLU B 1 445 ? -44.860 27.263 17.170  1.00 32.73  ? 445 GLU B OE2 1 
ATOM   7805 N N   . GLY B 1 446 ? -39.274 31.573 18.155  1.00 30.50  ? 446 GLY B N   1 
ATOM   7806 C CA  . GLY B 1 446 ? -38.336 32.312 18.987  1.00 20.44  ? 446 GLY B CA  1 
ATOM   7807 C C   . GLY B 1 446 ? -38.711 33.784 19.082  1.00 27.69  ? 446 GLY B C   1 
ATOM   7808 O O   . GLY B 1 446 ? -39.191 34.388 18.121  1.00 25.15  ? 446 GLY B O   1 
ATOM   7809 N N   . SER B 1 447 ? -38.502 34.361 20.273  1.00 27.72  ? 447 SER B N   1 
ATOM   7810 C CA  . SER B 1 447 ? -38.890 35.749 20.505  1.00 21.95  ? 447 SER B CA  1 
ATOM   7811 C C   . SER B 1 447 ? -38.111 36.713 19.622  1.00 20.65  ? 447 SER B C   1 
ATOM   7812 O O   . SER B 1 447 ? -38.606 37.797 19.306  1.00 22.87  ? 447 SER B O   1 
ATOM   7813 C CB  . SER B 1 447 ? -38.695 36.114 21.976  1.00 19.74  ? 447 SER B CB  1 
ATOM   7814 O OG  . SER B 1 447 ? -37.315 36.186 22.320  1.00 26.05  ? 447 SER B OG  1 
ATOM   7815 N N   . ASP B 1 448 ? -36.898 36.336 19.204  1.00 22.42  ? 448 ASP B N   1 
ATOM   7816 C CA  . ASP B 1 448 ? -36.009 37.293 18.547  1.00 25.57  ? 448 ASP B CA  1 
ATOM   7817 C C   . ASP B 1 448 ? -36.601 37.815 17.238  1.00 26.91  ? 448 ASP B C   1 
ATOM   7818 O O   . ASP B 1 448 ? -36.429 38.994 16.893  1.00 24.07  ? 448 ASP B O   1 
ATOM   7819 C CB  . ASP B 1 448 ? -34.646 36.641 18.300  1.00 24.30  ? 448 ASP B CB  1 
ATOM   7820 C CG  . ASP B 1 448 ? -34.045 36.047 19.566  1.00 27.32  ? 448 ASP B CG  1 
ATOM   7821 O OD1 . ASP B 1 448 ? -34.488 34.957 19.994  1.00 27.48  ? 448 ASP B OD1 1 
ATOM   7822 O OD2 . ASP B 1 448 ? -33.124 36.668 20.134  1.00 31.52  ? 448 ASP B OD2 1 
ATOM   7823 N N   . TRP B 1 449 ? -37.295 36.950 16.491  1.00 24.79  ? 449 TRP B N   1 
ATOM   7824 C CA  . TRP B 1 449 ? -37.853 37.360 15.206  1.00 18.95  ? 449 TRP B CA  1 
ATOM   7825 C C   . TRP B 1 449 ? -38.839 38.508 15.371  1.00 22.38  ? 449 TRP B C   1 
ATOM   7826 O O   . TRP B 1 449 ? -38.860 39.445 14.559  1.00 19.50  ? 449 TRP B O   1 
ATOM   7827 C CB  . TRP B 1 449 ? -38.522 36.161 14.531  1.00 26.55  ? 449 TRP B CB  1 
ATOM   7828 C CG  . TRP B 1 449 ? -37.727 34.889 14.649  1.00 29.55  ? 449 TRP B CG  1 
ATOM   7829 C CD1 . TRP B 1 449 ? -38.140 33.702 15.200  1.00 28.85  ? 449 TRP B CD1 1 
ATOM   7830 C CD2 . TRP B 1 449 ? -36.376 34.681 14.214  1.00 30.98  ? 449 TRP B CD2 1 
ATOM   7831 N NE1 . TRP B 1 449 ? -37.129 32.772 15.127  1.00 31.42  ? 449 TRP B NE1 1 
ATOM   7832 C CE2 . TRP B 1 449 ? -36.037 33.344 14.525  1.00 31.99  ? 449 TRP B CE2 1 
ATOM   7833 C CE3 . TRP B 1 449 ? -35.418 35.498 13.589  1.00 27.96  ? 449 TRP B CE3 1 
ATOM   7834 C CZ2 . TRP B 1 449 ? -34.777 32.800 14.235  1.00 30.67  ? 449 TRP B CZ2 1 
ATOM   7835 C CZ3 . TRP B 1 449 ? -34.159 34.954 13.302  1.00 26.59  ? 449 TRP B CZ3 1 
ATOM   7836 C CH2 . TRP B 1 449 ? -33.856 33.618 13.622  1.00 27.26  ? 449 TRP B CH2 1 
ATOM   7837 N N   . PHE B 1 450 ? -39.667 38.445 16.412  1.00 24.33  ? 450 PHE B N   1 
ATOM   7838 C CA  . PHE B 1 450 ? -40.669 39.472 16.670  1.00 27.25  ? 450 PHE B CA  1 
ATOM   7839 C C   . PHE B 1 450 ? -40.056 40.700 17.316  1.00 32.60  ? 450 PHE B C   1 
ATOM   7840 O O   . PHE B 1 450 ? -40.558 41.816 17.123  1.00 34.22  ? 450 PHE B O   1 
ATOM   7841 C CB  . PHE B 1 450 ? -41.778 38.899 17.559  1.00 25.43  ? 450 PHE B CB  1 
ATOM   7842 C CG  . PHE B 1 450 ? -42.348 37.617 17.034  1.00 30.13  ? 450 PHE B CG  1 
ATOM   7843 C CD1 . PHE B 1 450 ? -43.414 37.633 16.149  1.00 28.25  ? 450 PHE B CD1 1 
ATOM   7844 C CD2 . PHE B 1 450 ? -41.795 36.399 17.393  1.00 27.68  ? 450 PHE B CD2 1 
ATOM   7845 C CE1 . PHE B 1 450 ? -43.934 36.451 15.653  1.00 27.95  ? 450 PHE B CE1 1 
ATOM   7846 C CE2 . PHE B 1 450 ? -42.309 35.218 16.897  1.00 25.30  ? 450 PHE B CE2 1 
ATOM   7847 C CZ  . PHE B 1 450 ? -43.376 35.249 16.019  1.00 26.69  ? 450 PHE B CZ  1 
ATOM   7848 N N   . TRP B 1 451 ? -38.975 40.506 18.071  1.00 27.08  ? 451 TRP B N   1 
ATOM   7849 C CA  . TRP B 1 451 ? -38.291 41.626 18.707  1.00 29.24  ? 451 TRP B CA  1 
ATOM   7850 C C   . TRP B 1 451 ? -37.833 42.647 17.677  1.00 31.94  ? 451 TRP B C   1 
ATOM   7851 O O   . TRP B 1 451 ? -38.039 43.855 17.849  1.00 29.00  ? 451 TRP B O   1 
ATOM   7852 C CB  . TRP B 1 451 ? -37.100 41.106 19.509  1.00 26.13  ? 451 TRP B CB  1 
ATOM   7853 C CG  . TRP B 1 451 ? -36.618 41.992 20.613  1.00 37.05  ? 451 TRP B CG  1 
ATOM   7854 C CD1 . TRP B 1 451 ? -37.032 41.979 21.916  1.00 44.46  ? 451 TRP B CD1 1 
ATOM   7855 C CD2 . TRP B 1 451 ? -35.589 42.985 20.532  1.00 40.14  ? 451 TRP B CD2 1 
ATOM   7856 N NE1 . TRP B 1 451 ? -36.337 42.913 22.645  1.00 42.72  ? 451 TRP B NE1 1 
ATOM   7857 C CE2 . TRP B 1 451 ? -35.449 43.549 21.818  1.00 42.73  ? 451 TRP B CE2 1 
ATOM   7858 C CE3 . TRP B 1 451 ? -34.782 43.463 19.495  1.00 43.37  ? 451 TRP B CE3 1 
ATOM   7859 C CZ2 . TRP B 1 451 ? -34.538 44.567 22.093  1.00 42.43  ? 451 TRP B CZ2 1 
ATOM   7860 C CZ3 . TRP B 1 451 ? -33.879 44.474 19.770  1.00 43.74  ? 451 TRP B CZ3 1 
ATOM   7861 C CH2 . TRP B 1 451 ? -33.762 45.013 21.060  1.00 45.55  ? 451 TRP B CH2 1 
ATOM   7862 N N   . TRP B 1 452 ? -37.210 42.175 16.589  1.00 28.11  ? 452 TRP B N   1 
ATOM   7863 C CA  . TRP B 1 452 ? -36.599 43.073 15.617  1.00 36.87  ? 452 TRP B CA  1 
ATOM   7864 C C   . TRP B 1 452 ? -37.597 43.623 14.607  1.00 45.85  ? 452 TRP B C   1 
ATOM   7865 O O   . TRP B 1 452 ? -37.339 44.672 14.007  1.00 32.78  ? 452 TRP B O   1 
ATOM   7866 C CB  . TRP B 1 452 ? -35.461 42.354 14.876  1.00 36.51  ? 452 TRP B CB  1 
ATOM   7867 C CG  . TRP B 1 452 ? -34.309 42.036 15.771  1.00 34.10  ? 452 TRP B CG  1 
ATOM   7868 C CD1 . TRP B 1 452 ? -33.977 40.816 16.283  1.00 32.15  ? 452 TRP B CD1 1 
ATOM   7869 C CD2 . TRP B 1 452 ? -33.344 42.965 16.284  1.00 34.81  ? 452 TRP B CD2 1 
ATOM   7870 N NE1 . TRP B 1 452 ? -32.867 40.929 17.086  1.00 29.49  ? 452 TRP B NE1 1 
ATOM   7871 C CE2 . TRP B 1 452 ? -32.454 42.235 17.098  1.00 30.74  ? 452 TRP B CE2 1 
ATOM   7872 C CE3 . TRP B 1 452 ? -33.149 44.347 16.134  1.00 41.63  ? 452 TRP B CE3 1 
ATOM   7873 C CZ2 . TRP B 1 452 ? -31.383 42.835 17.760  1.00 35.47  ? 452 TRP B CZ2 1 
ATOM   7874 C CZ3 . TRP B 1 452 ? -32.078 44.943 16.788  1.00 41.52  ? 452 TRP B CZ3 1 
ATOM   7875 C CH2 . TRP B 1 452 ? -31.209 44.185 17.591  1.00 38.93  ? 452 TRP B CH2 1 
ATOM   7876 N N   . GLN B 1 453 ? -38.726 42.953 14.417  1.00 68.03  ? 453 GLN B N   1 
ATOM   7877 C CA  . GLN B 1 453 ? -39.617 43.263 13.305  1.00 74.94  ? 453 GLN B CA  1 
ATOM   7878 C C   . GLN B 1 453 ? -40.810 44.077 13.799  1.00 77.95  ? 453 GLN B C   1 
ATOM   7879 O O   . GLN B 1 453 ? -41.939 43.599 13.909  1.00 83.91  ? 453 GLN B O   1 
ATOM   7880 C CB  . GLN B 1 453 ? -40.039 41.978 12.611  1.00 80.69  ? 453 GLN B CB  1 
ATOM   7881 C CG  . GLN B 1 453 ? -38.858 41.264 11.981  1.00 85.14  ? 453 GLN B CG  1 
ATOM   7882 C CD  . GLN B 1 453 ? -38.457 41.868 10.654  1.00 86.90  ? 453 GLN B CD  1 
ATOM   7883 O OE1 . GLN B 1 453 ? -39.297 42.386 9.920   1.00 88.97  ? 453 GLN B OE1 1 
ATOM   7884 N NE2 . GLN B 1 453 ? -37.172 41.794 10.332  1.00 84.63  ? 453 GLN B NE2 1 
ATOM   7885 N N   . GLY B 1 454 ? -40.520 45.343 14.086  1.00 75.57  ? 454 GLY B N   1 
ATOM   7886 C CA  . GLY B 1 454 ? -41.525 46.307 14.481  1.00 79.83  ? 454 GLY B CA  1 
ATOM   7887 C C   . GLY B 1 454 ? -40.907 47.564 15.056  1.00 83.45  ? 454 GLY B C   1 
ATOM   7888 O O   . GLY B 1 454 ? -41.495 48.203 15.935  1.00 83.66  ? 454 GLY B O   1 
ATOM   7889 N N   . GLU B 1 455 ? -39.724 47.932 14.564  1.00 85.23  ? 455 GLU B N   1 
ATOM   7890 C CA  . GLU B 1 455 ? -38.935 48.986 15.186  1.00 86.55  ? 455 GLU B CA  1 
ATOM   7891 C C   . GLU B 1 455 ? -38.119 49.719 14.127  1.00 92.49  ? 455 GLU B C   1 
ATOM   7892 O O   . GLU B 1 455 ? -38.225 49.450 12.926  1.00 94.33  ? 455 GLU B O   1 
ATOM   7893 C CB  . GLU B 1 455 ? -38.013 48.411 16.266  1.00 82.43  ? 455 GLU B CB  1 
ATOM   7894 C CG  . GLU B 1 455 ? -38.509 48.622 17.682  1.00 81.92  ? 455 GLU B CG  1 
ATOM   7895 C CD  . GLU B 1 455 ? -39.351 47.466 18.177  1.00 84.05  ? 455 GLU B CD  1 
ATOM   7896 O OE1 . GLU B 1 455 ? -39.882 47.553 19.305  1.00 84.17  ? 455 GLU B OE1 1 
ATOM   7897 O OE2 . GLU B 1 455 ? -39.480 46.467 17.441  1.00 86.11  ? 455 GLU B OE2 1 
ATOM   7898 N N   . GLU B 1 456 ? -37.300 50.658 14.602  1.00 95.63  ? 456 GLU B N   1 
ATOM   7899 C CA  . GLU B 1 456 ? -36.346 51.374 13.766  1.00 98.30  ? 456 GLU B CA  1 
ATOM   7900 C C   . GLU B 1 456 ? -35.444 50.398 13.018  1.00 96.25  ? 456 GLU B C   1 
ATOM   7901 O O   . GLU B 1 456 ? -34.736 49.600 13.636  1.00 94.18  ? 456 GLU B O   1 
ATOM   7902 C CB  . GLU B 1 456 ? -35.510 52.314 14.638  1.00 100.81 ? 456 GLU B CB  1 
ATOM   7903 C CG  . GLU B 1 456 ? -36.325 53.339 15.411  1.00 102.33 ? 456 GLU B CG  1 
ATOM   7904 C CD  . GLU B 1 456 ? -36.836 54.452 14.524  1.00 104.73 ? 456 GLU B CD  1 
ATOM   7905 O OE1 . GLU B 1 456 ? -37.870 55.067 14.865  1.00 105.70 ? 456 GLU B OE1 1 
ATOM   7906 O OE2 . GLU B 1 456 ? -36.201 54.712 13.483  1.00 105.58 ? 456 GLU B OE2 1 
ATOM   7907 N N   . LYS B 1 457 ? -35.471 50.479 11.689  1.00 95.45  ? 457 LYS B N   1 
ATOM   7908 C CA  . LYS B 1 457 ? -34.812 49.494 10.841  1.00 91.79  ? 457 LYS B CA  1 
ATOM   7909 C C   . LYS B 1 457 ? -33.304 49.720 10.828  1.00 90.11  ? 457 LYS B C   1 
ATOM   7910 O O   . LYS B 1 457 ? -32.824 50.779 10.409  1.00 92.64  ? 457 LYS B O   1 
ATOM   7911 C CB  . LYS B 1 457 ? -35.385 49.557 9.425   1.00 89.07  ? 457 LYS B CB  1 
ATOM   7912 C CG  . LYS B 1 457 ? -36.892 49.795 9.378   1.00 84.15  ? 457 LYS B CG  1 
ATOM   7913 C CD  . LYS B 1 457 ? -37.455 49.491 7.998   1.00 79.12  ? 457 LYS B CD  1 
ATOM   7914 C CE  . LYS B 1 457 ? -38.969 49.355 8.028   1.00 75.72  ? 457 LYS B CE  1 
ATOM   7915 N NZ  . LYS B 1 457 ? -39.555 49.841 9.306   1.00 73.20  ? 457 LYS B NZ  1 
ATOM   7916 N N   . ALA B 1 458 ? -32.564 48.716 11.270  1.00 85.38  ? 458 ALA B N   1 
ATOM   7917 C CA  . ALA B 1 458 ? -31.120 48.748 11.455  1.00 81.08  ? 458 ALA B CA  1 
ATOM   7918 C C   . ALA B 1 458 ? -30.414 48.020 10.319  1.00 79.27  ? 458 ALA B C   1 
ATOM   7919 O O   . ALA B 1 458 ? -31.041 47.292 9.545   1.00 77.35  ? 458 ALA B O   1 
ATOM   7920 C CB  . ALA B 1 458 ? -30.774 48.126 12.807  1.00 78.21  ? 458 ALA B CB  1 
ATOM   7921 N N   . PRO B 1 459 ? -29.077 48.198 10.180  1.00 79.94  ? 459 PRO B N   1 
ATOM   7922 C CA  . PRO B 1 459 ? -28.370 47.650 9.005   1.00 79.26  ? 459 PRO B CA  1 
ATOM   7923 C C   . PRO B 1 459 ? -28.351 46.137 8.821   1.00 78.09  ? 459 PRO B C   1 
ATOM   7924 O O   . PRO B 1 459 ? -27.790 45.681 7.817   1.00 80.61  ? 459 PRO B O   1 
ATOM   7925 C CB  . PRO B 1 459 ? -26.938 48.173 9.198   1.00 79.31  ? 459 PRO B CB  1 
ATOM   7926 C CG  . PRO B 1 459 ? -27.098 49.432 9.947   1.00 80.08  ? 459 PRO B CG  1 
ATOM   7927 C CD  . PRO B 1 459 ? -28.251 49.200 10.884  1.00 80.76  ? 459 PRO B CD  1 
ATOM   7928 N N   . PHE B 1 460 ? -28.920 45.329 9.729   1.00 71.08  ? 460 PHE B N   1 
ATOM   7929 C CA  . PHE B 1 460 ? -28.928 43.886 9.494   1.00 59.47  ? 460 PHE B CA  1 
ATOM   7930 C C   . PHE B 1 460 ? -30.239 43.198 9.850   1.00 52.30  ? 460 PHE B C   1 
ATOM   7931 O O   . PHE B 1 460 ? -30.283 41.960 9.849   1.00 53.18  ? 460 PHE B O   1 
ATOM   7932 C CB  . PHE B 1 460 ? -27.783 43.193 10.248  1.00 57.80  ? 460 PHE B CB  1 
ATOM   7933 C CG  . PHE B 1 460 ? -26.428 43.454 9.664   1.00 58.90  ? 460 PHE B CG  1 
ATOM   7934 C CD1 . PHE B 1 460 ? -26.149 43.127 8.343   1.00 57.80  ? 460 PHE B CD1 1 
ATOM   7935 C CD2 . PHE B 1 460 ? -25.431 44.028 10.431  1.00 59.66  ? 460 PHE B CD2 1 
ATOM   7936 C CE1 . PHE B 1 460 ? -24.900 43.378 7.800   1.00 53.18  ? 460 PHE B CE1 1 
ATOM   7937 C CE2 . PHE B 1 460 ? -24.181 44.277 9.896   1.00 57.98  ? 460 PHE B CE2 1 
ATOM   7938 C CZ  . PHE B 1 460 ? -23.916 43.951 8.579   1.00 54.46  ? 460 PHE B CZ  1 
ATOM   7939 N N   . VAL B 1 461 ? -31.305 43.944 10.147  1.00 48.38  ? 461 VAL B N   1 
ATOM   7940 C CA  . VAL B 1 461 ? -32.597 43.327 10.440  1.00 50.68  ? 461 VAL B CA  1 
ATOM   7941 C C   . VAL B 1 461 ? -33.176 42.648 9.200   1.00 51.90  ? 461 VAL B C   1 
ATOM   7942 O O   . VAL B 1 461 ? -34.053 41.787 9.315   1.00 57.07  ? 461 VAL B O   1 
ATOM   7943 C CB  . VAL B 1 461 ? -33.561 44.376 11.046  1.00 53.66  ? 461 VAL B CB  1 
ATOM   7944 C CG1 . VAL B 1 461 ? -33.749 45.560 10.102  1.00 57.33  ? 461 VAL B CG1 1 
ATOM   7945 C CG2 . VAL B 1 461 ? -34.902 43.759 11.432  1.00 50.52  ? 461 VAL B CG2 1 
ATOM   7946 N N   . GLU B 1 462 ? -32.692 43.016 8.012   1.00 48.71  ? 462 GLU B N   1 
ATOM   7947 C CA  . GLU B 1 462 ? -33.066 42.286 6.798   1.00 47.27  ? 462 GLU B CA  1 
ATOM   7948 C C   . GLU B 1 462 ? -32.715 40.804 6.911   1.00 42.46  ? 462 GLU B C   1 
ATOM   7949 O O   . GLU B 1 462 ? -33.439 39.944 6.399   1.00 39.04  ? 462 GLU B O   1 
ATOM   7950 C CB  . GLU B 1 462 ? -32.384 42.914 5.572   1.00 55.90  ? 462 GLU B CB  1 
ATOM   7951 C CG  . GLU B 1 462 ? -30.934 42.457 5.350   1.00 66.85  ? 462 GLU B CG  1 
ATOM   7952 C CD  . GLU B 1 462 ? -30.246 43.175 4.204   1.00 75.47  ? 462 GLU B CD  1 
ATOM   7953 O OE1 . GLU B 1 462 ? -29.805 44.328 4.407   1.00 78.04  ? 462 GLU B OE1 1 
ATOM   7954 O OE2 . GLU B 1 462 ? -30.145 42.585 3.104   1.00 77.15  ? 462 GLU B OE2 1 
ATOM   7955 N N   . VAL B 1 463 ? -31.602 40.493 7.578   1.00 38.48  ? 463 VAL B N   1 
ATOM   7956 C CA  . VAL B 1 463 ? -31.195 39.101 7.717   1.00 36.14  ? 463 VAL B CA  1 
ATOM   7957 C C   . VAL B 1 463 ? -32.130 38.361 8.663   1.00 32.71  ? 463 VAL B C   1 
ATOM   7958 O O   . VAL B 1 463 ? -32.480 37.200 8.425   1.00 31.99  ? 463 VAL B O   1 
ATOM   7959 C CB  . VAL B 1 463 ? -29.732 39.005 8.189   1.00 35.39  ? 463 VAL B CB  1 
ATOM   7960 C CG1 . VAL B 1 463 ? -29.306 37.556 8.263   1.00 33.27  ? 463 VAL B CG1 1 
ATOM   7961 C CG2 . VAL B 1 463 ? -28.825 39.790 7.252   1.00 37.54  ? 463 VAL B CG2 1 
ATOM   7962 N N   . PHE B 1 464 ? -32.554 39.021 9.749   1.00 33.51  ? 464 PHE B N   1 
ATOM   7963 C CA  . PHE B 1 464 ? -33.510 38.402 10.665  1.00 33.83  ? 464 PHE B CA  1 
ATOM   7964 C C   . PHE B 1 464 ? -34.820 38.081 9.960   1.00 28.34  ? 464 PHE B C   1 
ATOM   7965 O O   . PHE B 1 464 ? -35.423 37.031 10.203  1.00 25.93  ? 464 PHE B O   1 
ATOM   7966 C CB  . PHE B 1 464 ? -33.763 39.312 11.869  1.00 34.18  ? 464 PHE B CB  1 
ATOM   7967 C CG  . PHE B 1 464 ? -32.639 39.330 12.857  1.00 34.01  ? 464 PHE B CG  1 
ATOM   7968 C CD1 . PHE B 1 464 ? -32.476 38.292 13.756  1.00 31.96  ? 464 PHE B CD1 1 
ATOM   7969 C CD2 . PHE B 1 464 ? -31.734 40.383 12.881  1.00 40.09  ? 464 PHE B CD2 1 
ATOM   7970 C CE1 . PHE B 1 464 ? -31.431 38.301 14.677  1.00 35.90  ? 464 PHE B CE1 1 
ATOM   7971 C CE2 . PHE B 1 464 ? -30.682 40.399 13.796  1.00 39.52  ? 464 PHE B CE2 1 
ATOM   7972 C CZ  . PHE B 1 464 ? -30.534 39.355 14.695  1.00 36.24  ? 464 PHE B CZ  1 
ATOM   7973 N N   . ASP B 1 465 ? -35.274 38.973 9.078   1.00 32.02  ? 465 ASP B N   1 
ATOM   7974 C CA  . ASP B 1 465 ? -36.481 38.693 8.308   1.00 32.30  ? 465 ASP B CA  1 
ATOM   7975 C C   . ASP B 1 465 ? -36.255 37.546 7.327   1.00 30.78  ? 465 ASP B C   1 
ATOM   7976 O O   . ASP B 1 465 ? -37.138 36.699 7.141   1.00 29.65  ? 465 ASP B O   1 
ATOM   7977 C CB  . ASP B 1 465 ? -36.944 39.958 7.577   1.00 32.71  ? 465 ASP B CB  1 
ATOM   7978 C CG  . ASP B 1 465 ? -38.212 39.735 6.760   1.00 38.48  ? 465 ASP B CG  1 
ATOM   7979 O OD1 . ASP B 1 465 ? -39.298 39.607 7.366   1.00 33.41  ? 465 ASP B OD1 1 
ATOM   7980 O OD2 . ASP B 1 465 ? -38.113 39.675 5.512   1.00 40.91  ? 465 ASP B OD2 1 
ATOM   7981 N N   . LYS B 1 466 ? -35.082 37.504 6.688   1.00 27.53  ? 466 LYS B N   1 
ATOM   7982 C CA  . LYS B 1 466 ? -34.765 36.399 5.786   1.00 37.01  ? 466 LYS B CA  1 
ATOM   7983 C C   . LYS B 1 466 ? -34.794 35.061 6.516   1.00 33.04  ? 466 LYS B C   1 
ATOM   7984 O O   . LYS B 1 466 ? -35.326 34.073 5.997   1.00 29.34  ? 466 LYS B O   1 
ATOM   7985 C CB  . LYS B 1 466 ? -33.398 36.625 5.136   1.00 44.10  ? 466 LYS B CB  1 
ATOM   7986 C CG  . LYS B 1 466 ? -32.929 35.470 4.260   1.00 52.91  ? 466 LYS B CG  1 
ATOM   7987 C CD  . LYS B 1 466 ? -33.704 35.418 2.948   1.00 59.93  ? 466 LYS B CD  1 
ATOM   7988 C CE  . LYS B 1 466 ? -34.125 33.992 2.597   1.00 62.71  ? 466 LYS B CE  1 
ATOM   7989 N NZ  . LYS B 1 466 ? -35.562 33.727 2.924   1.00 61.75  ? 466 LYS B NZ  1 
ATOM   7990 N N   . LEU B 1 467 ? -34.234 35.014 7.727   1.00 32.85  ? 467 LEU B N   1 
ATOM   7991 C CA  . LEU B 1 467 ? -34.207 33.774 8.497   1.00 25.88  ? 467 LEU B CA  1 
ATOM   7992 C C   . LEU B 1 467 ? -35.613 33.343 8.909   1.00 30.63  ? 467 LEU B C   1 
ATOM   7993 O O   . LEU B 1 467 ? -35.997 32.181 8.723   1.00 33.91  ? 467 LEU B O   1 
ATOM   7994 C CB  . LEU B 1 467 ? -33.311 33.951 9.725   1.00 25.35  ? 467 LEU B CB  1 
ATOM   7995 C CG  . LEU B 1 467 ? -31.804 34.074 9.480   1.00 22.33  ? 467 LEU B CG  1 
ATOM   7996 C CD1 . LEU B 1 467 ? -31.128 34.929 10.556  1.00 26.81  ? 467 LEU B CD1 1 
ATOM   7997 C CD2 . LEU B 1 467 ? -31.177 32.704 9.438   1.00 23.82  ? 467 LEU B CD2 1 
ATOM   7998 N N   . PHE B 1 468 ? -36.396 34.260 9.480   1.00 30.10  ? 468 PHE B N   1 
ATOM   7999 C CA  . PHE B 1 468 ? -37.756 33.916 9.895   1.00 28.38  ? 468 PHE B CA  1 
ATOM   8000 C C   . PHE B 1 468 ? -38.578 33.379 8.722   1.00 28.50  ? 468 PHE B C   1 
ATOM   8001 O O   . PHE B 1 468 ? -39.230 32.332 8.835   1.00 32.95  ? 468 PHE B O   1 
ATOM   8002 C CB  . PHE B 1 468 ? -38.440 35.130 10.519  1.00 26.71  ? 468 PHE B CB  1 
ATOM   8003 C CG  . PHE B 1 468 ? -39.884 34.900 10.854  1.00 25.58  ? 468 PHE B CG  1 
ATOM   8004 C CD1 . PHE B 1 468 ? -40.242 34.171 11.977  1.00 24.30  ? 468 PHE B CD1 1 
ATOM   8005 C CD2 . PHE B 1 468 ? -40.886 35.416 10.050  1.00 28.10  ? 468 PHE B CD2 1 
ATOM   8006 C CE1 . PHE B 1 468 ? -41.578 33.966 12.293  1.00 32.03  ? 468 PHE B CE1 1 
ATOM   8007 C CE2 . PHE B 1 468 ? -42.225 35.208 10.362  1.00 25.76  ? 468 PHE B CE2 1 
ATOM   8008 C CZ  . PHE B 1 468 ? -42.568 34.484 11.479  1.00 25.14  ? 468 PHE B CZ  1 
ATOM   8009 N N   . ARG B 1 469 ? -38.534 34.068 7.576   1.00 25.58  ? 469 ARG B N   1 
ATOM   8010 C CA  . ARG B 1 469 ? -39.250 33.592 6.392   1.00 37.61  ? 469 ARG B CA  1 
ATOM   8011 C C   . ARG B 1 469 ? -38.728 32.235 5.932   1.00 37.19  ? 469 ARG B C   1 
ATOM   8012 O O   . ARG B 1 469 ? -39.497 31.396 5.442   1.00 34.38  ? 469 ARG B O   1 
ATOM   8013 C CB  . ARG B 1 469 ? -39.134 34.609 5.256   1.00 30.29  ? 469 ARG B CB  1 
ATOM   8014 C CG  . ARG B 1 469 ? -39.805 35.940 5.532   1.00 34.14  ? 469 ARG B CG  1 
ATOM   8015 C CD  . ARG B 1 469 ? -39.878 36.787 4.260   1.00 39.29  ? 469 ARG B CD  1 
ATOM   8016 N NE  . ARG B 1 469 ? -38.577 37.307 3.826   1.00 41.58  ? 469 ARG B NE  1 
ATOM   8017 C CZ  . ARG B 1 469 ? -37.821 36.756 2.876   1.00 45.75  ? 469 ARG B CZ  1 
ATOM   8018 N NH1 . ARG B 1 469 ? -38.212 35.649 2.254   1.00 43.11  ? 469 ARG B NH1 1 
ATOM   8019 N NH2 . ARG B 1 469 ? -36.660 37.306 2.549   1.00 49.62  ? 469 ARG B NH2 1 
ATOM   8020 N N   . SER B 1 470 ? -37.418 32.016 6.060   1.00 34.53  ? 470 SER B N   1 
ATOM   8021 C CA  . SER B 1 470 ? -36.828 30.738 5.680   1.00 35.35  ? 470 SER B CA  1 
ATOM   8022 C C   . SER B 1 470 ? -37.330 29.618 6.579   1.00 31.18  ? 470 SER B C   1 
ATOM   8023 O O   . SER B 1 470 ? -37.709 28.546 6.098   1.00 30.74  ? 470 SER B O   1 
ATOM   8024 C CB  . SER B 1 470 ? -35.303 30.828 5.748   1.00 39.54  ? 470 SER B CB  1 
ATOM   8025 O OG  . SER B 1 470 ? -34.784 31.539 4.640   1.00 48.41  ? 470 SER B OG  1 
ATOM   8026 N N   . PHE B 1 471 ? -37.317 29.848 7.897   1.00 27.39  ? 471 PHE B N   1 
ATOM   8027 C CA  . PHE B 1 471 ? -37.809 28.848 8.841   1.00 31.44  ? 471 PHE B CA  1 
ATOM   8028 C C   . PHE B 1 471 ? -39.301 28.589 8.651   1.00 31.62  ? 471 PHE B C   1 
ATOM   8029 O O   . PHE B 1 471 ? -39.753 27.441 8.739   1.00 29.65  ? 471 PHE B O   1 
ATOM   8030 C CB  . PHE B 1 471 ? -37.526 29.298 10.277  1.00 27.40  ? 471 PHE B CB  1 
ATOM   8031 C CG  . PHE B 1 471 ? -36.065 29.451 10.594  1.00 29.27  ? 471 PHE B CG  1 
ATOM   8032 C CD1 . PHE B 1 471 ? -35.145 28.521 10.152  1.00 29.02  ? 471 PHE B CD1 1 
ATOM   8033 C CD2 . PHE B 1 471 ? -35.611 30.536 11.341  1.00 32.98  ? 471 PHE B CD2 1 
ATOM   8034 C CE1 . PHE B 1 471 ? -33.791 28.666 10.440  1.00 28.74  ? 471 PHE B CE1 1 
ATOM   8035 C CE2 . PHE B 1 471 ? -34.260 30.683 11.638  1.00 23.47  ? 471 PHE B CE2 1 
ATOM   8036 C CZ  . PHE B 1 471 ? -33.349 29.737 11.184  1.00 28.22  ? 471 PHE B CZ  1 
ATOM   8037 N N   . VAL B 1 472 ? -40.081 29.643 8.389   1.00 35.08  ? 472 VAL B N   1 
ATOM   8038 C CA  . VAL B 1 472 ? -41.519 29.472 8.196   1.00 38.03  ? 472 VAL B CA  1 
ATOM   8039 C C   . VAL B 1 472 ? -41.793 28.670 6.932   1.00 34.88  ? 472 VAL B C   1 
ATOM   8040 O O   . VAL B 1 472 ? -42.690 27.822 6.900   1.00 36.45  ? 472 VAL B O   1 
ATOM   8041 C CB  . VAL B 1 472 ? -42.224 30.843 8.169   1.00 35.71  ? 472 VAL B CB  1 
ATOM   8042 C CG1 . VAL B 1 472 ? -43.522 30.777 7.378   1.00 38.79  ? 472 VAL B CG1 1 
ATOM   8043 C CG2 . VAL B 1 472 ? -42.489 31.335 9.590   1.00 30.48  ? 472 VAL B CG2 1 
ATOM   8044 N N   . ARG B 1 473 ? -41.023 28.918 5.869   1.00 39.19  ? 473 ARG B N   1 
ATOM   8045 C CA  . ARG B 1 473 ? -41.207 28.153 4.638   1.00 39.90  ? 473 ARG B CA  1 
ATOM   8046 C C   . ARG B 1 473 ? -40.782 26.704 4.837   1.00 33.83  ? 473 ARG B C   1 
ATOM   8047 O O   . ARG B 1 473 ? -41.514 25.773 4.483   1.00 33.62  ? 473 ARG B O   1 
ATOM   8048 C CB  . ARG B 1 473 ? -40.427 28.807 3.495   1.00 45.03  ? 473 ARG B CB  1 
ATOM   8049 C CG  . ARG B 1 473 ? -40.269 27.930 2.257   1.00 52.86  ? 473 ARG B CG  1 
ATOM   8050 C CD  . ARG B 1 473 ? -39.915 28.758 1.029   1.00 58.80  ? 473 ARG B CD  1 
ATOM   8051 N NE  . ARG B 1 473 ? -38.561 28.497 0.538   1.00 63.14  ? 473 ARG B NE  1 
ATOM   8052 C CZ  . ARG B 1 473 ? -38.244 27.542 -0.334  1.00 60.74  ? 473 ARG B CZ  1 
ATOM   8053 N NH1 . ARG B 1 473 ? -39.182 26.737 -0.815  1.00 63.80  ? 473 ARG B NH1 1 
ATOM   8054 N NH2 . ARG B 1 473 ? -36.986 27.389 -0.728  1.00 52.05  ? 473 ARG B NH2 1 
ATOM   8055 N N   . ARG B 1 474 ? -39.612 26.502 5.435   1.00 28.30  ? 474 ARG B N   1 
ATOM   8056 C CA  . ARG B 1 474 ? -39.108 25.156 5.671   1.00 33.46  ? 474 ARG B CA  1 
ATOM   8057 C C   . ARG B 1 474 ? -40.040 24.353 6.576   1.00 37.93  ? 474 ARG B C   1 
ATOM   8058 O O   . ARG B 1 474 ? -40.226 23.147 6.372   1.00 39.89  ? 474 ARG B O   1 
ATOM   8059 C CB  . ARG B 1 474 ? -37.705 25.236 6.276   1.00 34.55  ? 474 ARG B CB  1 
ATOM   8060 C CG  . ARG B 1 474 ? -37.098 23.890 6.606   1.00 38.48  ? 474 ARG B CG  1 
ATOM   8061 C CD  . ARG B 1 474 ? -36.454 23.239 5.393   1.00 50.17  ? 474 ARG B CD  1 
ATOM   8062 N NE  . ARG B 1 474 ? -35.730 22.028 5.776   1.00 59.52  ? 474 ARG B NE  1 
ATOM   8063 C CZ  . ARG B 1 474 ? -36.293 20.830 5.906   1.00 62.85  ? 474 ARG B CZ  1 
ATOM   8064 N NH1 . ARG B 1 474 ? -37.592 20.675 5.674   1.00 58.35  ? 474 ARG B NH1 1 
ATOM   8065 N NH2 . ARG B 1 474 ? -35.558 19.785 6.265   1.00 65.85  ? 474 ARG B NH2 1 
ATOM   8066 N N   . ALA B 1 475 ? -40.648 25.004 7.569   1.00 39.31  ? 475 ALA B N   1 
ATOM   8067 C CA  . ALA B 1 475 ? -41.512 24.297 8.511   1.00 41.42  ? 475 ALA B CA  1 
ATOM   8068 C C   . ALA B 1 475 ? -42.716 23.657 7.835   1.00 41.60  ? 475 ALA B C   1 
ATOM   8069 O O   . ALA B 1 475 ? -43.319 22.742 8.409   1.00 38.74  ? 475 ALA B O   1 
ATOM   8070 C CB  . ALA B 1 475 ? -41.993 25.252 9.603   1.00 42.70  ? 475 ALA B CB  1 
ATOM   8071 N N   . GLN B 1 476 ? -43.083 24.127 6.644   1.00 38.67  ? 476 GLN B N   1 
ATOM   8072 C CA  . GLN B 1 476 ? -44.203 23.593 5.882   1.00 43.66  ? 476 GLN B CA  1 
ATOM   8073 C C   . GLN B 1 476 ? -43.767 22.599 4.811   1.00 48.60  ? 476 GLN B C   1 
ATOM   8074 O O   . GLN B 1 476 ? -44.610 22.130 4.038   1.00 45.01  ? 476 GLN B O   1 
ATOM   8075 C CB  . GLN B 1 476 ? -44.993 24.744 5.243   1.00 41.86  ? 476 GLN B CB  1 
ATOM   8076 C CG  . GLN B 1 476 ? -45.484 25.788 6.243   1.00 45.25  ? 476 GLN B CG  1 
ATOM   8077 C CD  . GLN B 1 476 ? -45.945 27.077 5.579   1.00 54.48  ? 476 GLN B CD  1 
ATOM   8078 O OE1 . GLN B 1 476 ? -47.142 27.289 5.365   1.00 59.42  ? 476 GLN B OE1 1 
ATOM   8079 N NE2 . GLN B 1 476 ? -44.995 27.946 5.253   1.00 55.24  ? 476 GLN B NE2 1 
ATOM   8080 N N   . GLU B 1 477 ? -42.481 22.263 4.750   1.00 49.99  ? 477 GLU B N   1 
ATOM   8081 C CA  . GLU B 1 477 ? -41.975 21.313 3.762   1.00 56.12  ? 477 GLU B CA  1 
ATOM   8082 C C   . GLU B 1 477 ? -41.400 20.074 4.433   1.00 57.60  ? 477 GLU B C   1 
ATOM   8083 O O   . GLU B 1 477 ? -42.118 19.321 5.085   1.00 59.07  ? 477 GLU B O   1 
ATOM   8084 C CB  . GLU B 1 477 ? -40.907 21.964 2.883   1.00 60.07  ? 477 GLU B CB  1 
ATOM   8085 C CG  . GLU B 1 477 ? -41.451 22.952 1.866   1.00 64.64  ? 477 GLU B CG  1 
ATOM   8086 C CD  . GLU B 1 477 ? -40.353 23.747 1.188   1.00 68.82  ? 477 GLU B CD  1 
ATOM   8087 O OE1 . GLU B 1 477 ? -39.169 23.543 1.537   1.00 68.50  ? 477 GLU B OE1 1 
ATOM   8088 O OE2 . GLU B 1 477 ? -40.672 24.571 0.305   1.00 71.09  ? 477 GLU B OE2 1 
HETATM 8089 C C1  . GLC C 2 .   ? 4.160   25.426 65.081  1.00 38.28  ? 1   GLC C C1  1 
HETATM 8090 C C2  . GLC C 2 .   ? 4.579   26.253 66.311  1.00 42.43  ? 1   GLC C C2  1 
HETATM 8091 C C3  . GLC C 2 .   ? 4.594   25.417 67.559  1.00 45.52  ? 1   GLC C C3  1 
HETATM 8092 C C4  . GLC C 2 .   ? 3.424   24.472 67.514  1.00 43.27  ? 1   GLC C C4  1 
HETATM 8093 C C5  . GLC C 2 .   ? 3.656   23.434 66.466  1.00 41.59  ? 1   GLC C C5  1 
HETATM 8094 C C6  . GLC C 2 .   ? 2.401   22.562 66.305  1.00 41.72  ? 1   GLC C C6  1 
HETATM 8095 O O1  . GLC C 2 .   ? 5.054   25.665 63.989  1.00 33.58  ? 1   GLC C O1  1 
HETATM 8096 O O2  . GLC C 2 .   ? 5.853   26.855 66.156  1.00 45.84  ? 1   GLC C O2  1 
HETATM 8097 O O3  . GLC C 2 .   ? 4.497   26.329 68.650  1.00 46.38  ? 1   GLC C O3  1 
HETATM 8098 O O4  . GLC C 2 .   ? 3.431   23.651 68.645  1.00 37.76  ? 1   GLC C O4  1 
HETATM 8099 O O5  . GLC C 2 .   ? 4.074   24.017 65.247  1.00 42.88  ? 1   GLC C O5  1 
HETATM 8100 O O6  . GLC C 2 .   ? 1.287   23.217 65.716  1.00 39.92  ? 1   GLC C O6  1 
HETATM 8101 C C1  . GLC C 2 .   ? 3.080   24.265 69.891  1.00 36.67  ? 2   GLC C C1  1 
HETATM 8102 C C2  . GLC C 2 .   ? 3.986   23.671 70.950  1.00 37.78  ? 2   GLC C C2  1 
HETATM 8103 C C3  . GLC C 2 .   ? 3.779   22.160 70.975  1.00 27.88  ? 2   GLC C C3  1 
HETATM 8104 C C4  . GLC C 2 .   ? 2.288   21.849 71.226  1.00 32.80  ? 2   GLC C C4  1 
HETATM 8105 C C5  . GLC C 2 .   ? 1.369   22.690 70.326  1.00 40.21  ? 2   GLC C C5  1 
HETATM 8106 C C6  . GLC C 2 .   ? -0.075  22.624 70.813  1.00 49.47  ? 2   GLC C C6  1 
HETATM 8107 O O2  . GLC C 2 .   ? 5.327   24.013 70.653  1.00 43.10  ? 2   GLC C O2  1 
HETATM 8108 O O3  . GLC C 2 .   ? 4.634   21.693 71.993  1.00 24.44  ? 2   GLC C O3  1 
HETATM 8109 O O4  . GLC C 2 .   ? 1.855   20.500 71.030  1.00 24.35  ? 2   GLC C O4  1 
HETATM 8110 O O5  . GLC C 2 .   ? 1.736   24.050 70.259  1.00 36.71  ? 2   GLC C O5  1 
HETATM 8111 O O6  . GLC C 2 .   ? -0.772  21.643 70.076  1.00 57.93  ? 2   GLC C O6  1 
HETATM 8112 C C1  . GLC C 2 .   ? 2.509   19.488 71.838  1.00 24.54  ? 3   GLC C C1  1 
HETATM 8113 C C2  . GLC C 2 .   ? 1.785   18.155 71.617  1.00 20.81  ? 3   GLC C C2  1 
HETATM 8114 C C3  . GLC C 2 .   ? 0.371   18.241 72.185  1.00 19.99  ? 3   GLC C C3  1 
HETATM 8115 C C4  . GLC C 2 .   ? 0.405   18.589 73.668  1.00 19.11  ? 3   GLC C C4  1 
HETATM 8116 C C5  . GLC C 2 .   ? 1.246   19.844 73.892  1.00 23.62  ? 3   GLC C C5  1 
HETATM 8117 C C6  . GLC C 2 .   ? 1.510   20.126 75.368  1.00 18.60  ? 3   GLC C C6  1 
HETATM 8118 O O2  . GLC C 2 .   ? 1.681   17.894 70.230  1.00 15.18  ? 3   GLC C O2  1 
HETATM 8119 O O3  . GLC C 2 .   ? -0.321  17.029 71.923  1.00 20.98  ? 3   GLC C O3  1 
HETATM 8120 O O4  . GLC C 2 .   ? -0.904  18.871 74.107  1.00 20.35  ? 3   GLC C O4  1 
HETATM 8121 O O5  . GLC C 2 .   ? 2.499   19.783 73.228  1.00 22.41  ? 3   GLC C O5  1 
HETATM 8122 O O6  . GLC C 2 .   ? 2.330   19.122 75.933  1.00 21.23  ? 3   GLC C O6  1 
HETATM 8123 C C1  . GLC C 2 .   ? -1.537  17.718 74.690  1.00 25.87  ? 4   GLC C C1  1 
HETATM 8124 C C2  . GLC C 2 .   ? -3.026  17.727 74.316  1.00 23.54  ? 4   GLC C C2  1 
HETATM 8125 C C3  . GLC C 2 .   ? -3.735  18.939 74.915  1.00 20.64  ? 4   GLC C C3  1 
HETATM 8126 C C4  . GLC C 2 .   ? -3.502  18.994 76.422  1.00 23.00  ? 4   GLC C C4  1 
HETATM 8127 C C5  . GLC C 2 .   ? -2.007  18.869 76.725  1.00 22.00  ? 4   GLC C C5  1 
HETATM 8128 C C6  . GLC C 2 .   ? -1.757  18.699 78.214  1.00 22.56  ? 4   GLC C C6  1 
HETATM 8129 O O2  . GLC C 2 .   ? -3.173  17.672 72.908  1.00 18.05  ? 4   GLC C O2  1 
HETATM 8130 O O3  . GLC C 2 .   ? -5.118  18.886 74.649  1.00 20.29  ? 4   GLC C O3  1 
HETATM 8131 O O4  . GLC C 2 .   ? -4.010  20.226 76.892  1.00 17.94  ? 4   GLC C O4  1 
HETATM 8132 O O5  . GLC C 2 .   ? -1.430  17.736 76.096  1.00 23.90  ? 4   GLC C O5  1 
HETATM 8133 O O6  . GLC C 2 .   ? -0.363  18.645 78.401  1.00 22.17  ? 4   GLC C O6  1 
HETATM 8134 C C1  . GLC C 2 .   ? -4.979  20.037 77.937  1.00 20.51  ? 5   GLC C C1  1 
HETATM 8135 C C2  . GLC C 2 .   ? -6.283  20.682 77.496  1.00 19.97  ? 5   GLC C C2  1 
HETATM 8136 C C3  . GLC C 2 .   ? -6.080  22.183 77.324  1.00 19.69  ? 5   GLC C C3  1 
HETATM 8137 C C4  . GLC C 2 .   ? -5.530  22.786 78.608  1.00 21.23  ? 5   GLC C C4  1 
HETATM 8138 C C5  . GLC C 2 .   ? -4.264  22.037 79.017  1.00 18.76  ? 5   GLC C C5  1 
HETATM 8139 C C6  . GLC C 2 .   ? -3.757  22.539 80.367  1.00 19.73  ? 5   GLC C C6  1 
HETATM 8140 O O2  . GLC C 2 .   ? -6.697  20.105 76.272  1.00 19.89  ? 5   GLC C O2  1 
HETATM 8141 O O3  . GLC C 2 .   ? -7.276  22.839 76.957  1.00 21.97  ? 5   GLC C O3  1 
HETATM 8142 O O4  . GLC C 2 .   ? -5.262  24.146 78.369  1.00 24.81  ? 5   GLC C O4  1 
HETATM 8143 O O5  . GLC C 2 .   ? -4.527  20.650 79.130  1.00 22.40  ? 5   GLC C O5  1 
HETATM 8144 O O6  . GLC C 2 .   ? -4.827  22.510 81.281  1.00 23.80  ? 5   GLC C O6  1 
HETATM 8145 C C1  . GLC C 2 .   ? -5.958  24.981 79.323  1.00 34.49  ? 6   GLC C C1  1 
HETATM 8146 C C2  . GLC C 2 .   ? -6.889  25.944 78.604  1.00 31.89  ? 6   GLC C C2  1 
HETATM 8147 C C3  . GLC C 2 .   ? -6.083  26.793 77.646  1.00 40.24  ? 6   GLC C C3  1 
HETATM 8148 C C4  . GLC C 2 .   ? -5.003  27.565 78.411  1.00 45.73  ? 6   GLC C C4  1 
HETATM 8149 C C5  . GLC C 2 .   ? -4.210  26.615 79.314  1.00 38.92  ? 6   GLC C C5  1 
HETATM 8150 C C6  . GLC C 2 .   ? -3.359  27.397 80.312  1.00 44.75  ? 6   GLC C C6  1 
HETATM 8151 O O2  . GLC C 2 .   ? -7.884  25.267 77.881  1.00 30.51  ? 6   GLC C O2  1 
HETATM 8152 O O3  . GLC C 2 .   ? -6.996  27.636 76.986  1.00 41.02  ? 6   GLC C O3  1 
HETATM 8153 O O4  . GLC C 2 .   ? -4.093  28.192 77.520  1.00 55.70  ? 6   GLC C O4  1 
HETATM 8154 O O5  . GLC C 2 .   ? -5.049  25.762 80.075  1.00 37.58  ? 6   GLC C O5  1 
HETATM 8155 O O6  . GLC C 2 .   ? -4.182  27.812 81.380  1.00 44.43  ? 6   GLC C O6  1 
HETATM 8156 C C1  . GLC C 2 .   ? -4.503  29.527 77.115  1.00 62.10  ? 7   GLC C C1  1 
HETATM 8157 C C2  . GLC C 2 .   ? -4.156  29.706 75.637  1.00 64.72  ? 7   GLC C C2  1 
HETATM 8158 C C3  . GLC C 2 .   ? -2.657  29.540 75.428  1.00 67.20  ? 7   GLC C C3  1 
HETATM 8159 C C4  . GLC C 2 .   ? -1.845  30.415 76.377  1.00 67.15  ? 7   GLC C C4  1 
HETATM 8160 C C5  . GLC C 2 .   ? -2.433  30.552 77.783  1.00 64.80  ? 7   GLC C C5  1 
HETATM 8161 C C6  . GLC C 2 .   ? -1.915  31.856 78.386  1.00 63.42  ? 7   GLC C C6  1 
HETATM 8162 O O2  . GLC C 2 .   ? -4.844  28.751 74.858  1.00 66.56  ? 7   GLC C O2  1 
HETATM 8163 O O3  . GLC C 2 .   ? -2.322  29.888 74.101  1.00 70.33  ? 7   GLC C O3  1 
HETATM 8164 O O4  . GLC C 2 .   ? -0.537  29.879 76.474  1.00 69.84  ? 7   GLC C O4  1 
HETATM 8165 O O5  . GLC C 2 .   ? -3.851  30.572 77.824  1.00 64.83  ? 7   GLC C O5  1 
HETATM 8166 O O6  . GLC C 2 .   ? -2.590  32.128 79.594  1.00 66.60  ? 7   GLC C O6  1 
HETATM 8167 C C1  . GLC D 3 .   ? -34.380 45.741 31.736  1.00 50.06  ? 1   GLC D C1  1 
HETATM 8168 C C2  . GLC D 3 .   ? -34.929 46.565 30.552  1.00 50.71  ? 1   GLC D C2  1 
HETATM 8169 C C3  . GLC D 3 .   ? -34.999 45.858 29.211  1.00 49.79  ? 1   GLC D C3  1 
HETATM 8170 C C4  . GLC D 3 .   ? -33.995 44.753 29.104  1.00 46.81  ? 1   GLC D C4  1 
HETATM 8171 C C5  . GLC D 3 .   ? -34.119 43.797 30.254  1.00 46.55  ? 1   GLC D C5  1 
HETATM 8172 C C6  . GLC D 3 .   ? -33.021 42.769 30.146  1.00 45.75  ? 1   GLC D C6  1 
HETATM 8173 O O1  . GLC D 3 .   ? -35.387 45.645 32.733  1.00 51.07  ? 1   GLC D O1  1 
HETATM 8174 O O2  . GLC D 3 .   ? -36.226 47.045 30.894  1.00 47.08  ? 1   GLC D O2  1 
HETATM 8175 O O3  . GLC D 3 .   ? -34.693 46.833 28.223  1.00 52.53  ? 1   GLC D O3  1 
HETATM 8176 O O4  . GLC D 3 .   ? -34.359 43.961 28.014  1.00 41.94  ? 1   GLC D O4  1 
HETATM 8177 O O5  . GLC D 3 .   ? -33.934 44.415 31.504  1.00 46.33  ? 1   GLC D O5  1 
HETATM 8178 O O6  . GLC D 3 .   ? -31.764 43.411 30.322  1.00 45.91  ? 1   GLC D O6  1 
HETATM 8179 C C1  . GLC D 3 .   ? -34.052 44.406 26.680  1.00 39.96  ? 2   GLC D C1  1 
HETATM 8180 C C2  . GLC D 3 .   ? -35.066 43.680 25.833  1.00 41.85  ? 2   GLC D C2  1 
HETATM 8181 C C3  . GLC D 3 .   ? -34.794 42.191 25.958  1.00 39.22  ? 2   GLC D C3  1 
HETATM 8182 C C4  . GLC D 3 .   ? -33.350 41.905 25.514  1.00 32.80  ? 2   GLC D C4  1 
HETATM 8183 C C5  . GLC D 3 .   ? -32.347 42.788 26.246  1.00 38.31  ? 2   GLC D C5  1 
HETATM 8184 C C6  . GLC D 3 .   ? -30.996 42.654 25.547  1.00 44.48  ? 2   GLC D C6  1 
HETATM 8185 O O2  . GLC D 3 .   ? -36.340 43.931 26.376  1.00 47.80  ? 2   GLC D O2  1 
HETATM 8186 O O3  . GLC D 3 .   ? -35.788 41.544 25.196  1.00 40.30  ? 2   GLC D O3  1 
HETATM 8187 O O4  . GLC D 3 .   ? -32.866 40.592 25.730  1.00 28.65  ? 2   GLC D O4  1 
HETATM 8188 O O5  . GLC D 3 .   ? -32.736 44.145 26.231  1.00 38.74  ? 2   GLC D O5  1 
HETATM 8189 O O6  . GLC D 3 .   ? -30.032 42.108 26.423  1.00 48.08  ? 2   GLC D O6  1 
HETATM 8190 C C1  . GLC D 3 .   ? -33.616 39.524 25.100  1.00 25.14  ? 3   GLC D C1  1 
HETATM 8191 C C2  . GLC D 3 .   ? -32.809 38.240 25.294  1.00 27.64  ? 3   GLC D C2  1 
HETATM 8192 C C3  . GLC D 3 .   ? -31.521 38.302 24.476  1.00 27.00  ? 3   GLC D C3  1 
HETATM 8193 C C4  . GLC D 3 .   ? -31.773 38.645 22.998  1.00 21.32  ? 3   GLC D C4  1 
HETATM 8194 C C5  . GLC D 3 .   ? -32.675 39.871 22.884  1.00 25.15  ? 3   GLC D C5  1 
HETATM 8195 C C6  . GLC D 3 .   ? -33.096 40.184 21.445  1.00 22.60  ? 3   GLC D C6  1 
HETATM 8196 O O2  . GLC D 3 .   ? -32.523 38.088 26.675  1.00 24.59  ? 3   GLC D O2  1 
HETATM 8197 O O3  . GLC D 3 .   ? -30.847 37.073 24.622  1.00 31.55  ? 3   GLC D O3  1 
HETATM 8198 O O4  . GLC D 3 .   ? -30.543 38.973 22.379  1.00 24.79  ? 3   GLC D O4  1 
HETATM 8199 O O5  . GLC D 3 .   ? -33.831 39.735 23.706  1.00 24.04  ? 3   GLC D O5  1 
HETATM 8200 O O6  . GLC D 3 .   ? -34.053 39.233 21.043  1.00 20.39  ? 3   GLC D O6  1 
HETATM 8201 C C1  . GLC D 3 .   ? -29.970 37.834 21.715  1.00 24.80  ? 4   GLC D C1  1 
HETATM 8202 C C2  . GLC D 3 .   ? -28.452 37.891 21.904  1.00 19.33  ? 4   GLC D C2  1 
HETATM 8203 C C3  . GLC D 3 .   ? -27.888 39.124 21.209  1.00 19.16  ? 4   GLC D C3  1 
HETATM 8204 C C4  . GLC D 3 .   ? -28.337 39.156 19.745  1.00 25.05  ? 4   GLC D C4  1 
HETATM 8205 C C5  . GLC D 3 .   ? -29.862 39.006 19.638  1.00 26.01  ? 4   GLC D C5  1 
HETATM 8206 C C6  . GLC D 3 .   ? -30.331 38.905 18.180  1.00 30.88  ? 4   GLC D C6  1 
HETATM 8207 O O2  . GLC D 3 .   ? -28.087 37.891 23.273  1.00 22.23  ? 4   GLC D O2  1 
HETATM 8208 O O3  . GLC D 3 .   ? -26.481 39.108 21.278  1.00 24.89  ? 4   GLC D O3  1 
HETATM 8209 O O4  . GLC D 3 .   ? -27.909 40.376 19.169  1.00 28.90  ? 4   GLC D O4  1 
HETATM 8210 O O5  . GLC D 3 .   ? -30.295 37.846 20.329  1.00 25.65  ? 4   GLC D O5  1 
HETATM 8211 O O6  . GLC D 3 .   ? -31.719 38.659 18.089  1.00 26.90  ? 4   GLC D O6  1 
HETATM 8212 C C1  . GLC D 3 .   ? -27.097 40.151 18.004  1.00 26.02  ? 5   GLC D C1  1 
HETATM 8213 C C2  . GLC D 3 .   ? -25.721 40.769 18.230  1.00 27.23  ? 5   GLC D C2  1 
HETATM 8214 C C3  . GLC D 3 .   ? -25.843 42.285 18.433  1.00 29.02  ? 5   GLC D C3  1 
HETATM 8215 C C4  . GLC D 3 .   ? -26.593 42.922 17.271  1.00 29.12  ? 5   GLC D C4  1 
HETATM 8216 C C5  . GLC D 3 .   ? -27.901 42.163 16.995  1.00 27.22  ? 5   GLC D C5  1 
HETATM 8217 C C6  . GLC D 3 .   ? -28.607 42.651 15.728  1.00 31.05  ? 5   GLC D C6  1 
HETATM 8218 O O2  . GLC D 3 .   ? -25.096 40.141 19.331  1.00 25.42  ? 5   GLC D O2  1 
HETATM 8219 O O3  . GLC D 3 .   ? -24.573 42.892 18.536  1.00 27.24  ? 5   GLC D O3  1 
HETATM 8220 O O4  . GLC D 3 .   ? -26.824 44.285 17.593  1.00 34.39  ? 5   GLC D O4  1 
HETATM 8221 O O5  . GLC D 3 .   ? -27.683 40.760 16.872  1.00 26.44  ? 5   GLC D O5  1 
HETATM 8222 O O6  . GLC D 3 .   ? -27.786 42.448 14.593  1.00 31.20  ? 5   GLC D O6  1 
HETATM 8223 C C1  . GLC D 3 .   ? -26.322 45.136 16.541  1.00 35.37  ? 6   GLC D C1  1 
HETATM 8224 C C2  . GLC D 3 .   ? -25.281 46.102 17.077  1.00 34.65  ? 6   GLC D C2  1 
HETATM 8225 C C3  . GLC D 3 .   ? -25.890 46.879 18.228  1.00 42.58  ? 6   GLC D C3  1 
HETATM 8226 C C4  . GLC D 3 .   ? -27.188 47.554 17.782  1.00 49.17  ? 6   GLC D C4  1 
HETATM 8227 C C5  . GLC D 3 .   ? -28.097 46.579 17.029  1.00 41.12  ? 6   GLC D C5  1 
HETATM 8228 C C6  . GLC D 3 .   ? -29.250 47.288 16.338  1.00 41.73  ? 6   GLC D C6  1 
HETATM 8229 O O2  . GLC D 3 .   ? -24.132 45.424 17.510  1.00 42.02  ? 6   GLC D O2  1 
HETATM 8230 O O3  . GLC D 3 .   ? -24.956 47.840 18.652  1.00 45.20  ? 6   GLC D O3  1 
HETATM 8231 O O4  . GLC D 3 .   ? -27.861 48.065 18.911  1.00 55.49  ? 6   GLC D O4  1 
HETATM 8232 O O5  . GLC D 3 .   ? -27.362 45.924 16.016  1.00 35.40  ? 6   GLC D O5  1 
HETATM 8233 O O6  . GLC D 3 .   ? -28.845 47.486 15.002  1.00 40.08  ? 6   GLC D O6  1 
HETATM 8234 C C1  . GOL E 4 .   ? -15.587 18.668 65.254  1.00 26.85  ? 501 GOL A C1  1 
HETATM 8235 O O1  . GOL E 4 .   ? -16.179 18.318 66.463  1.00 21.47  ? 501 GOL A O1  1 
HETATM 8236 C C2  . GOL E 4 .   ? -14.187 19.262 65.607  1.00 28.38  ? 501 GOL A C2  1 
HETATM 8237 O O2  . GOL E 4 .   ? -13.341 18.315 66.192  1.00 27.50  ? 501 GOL A O2  1 
HETATM 8238 C C3  . GOL E 4 .   ? -13.607 19.773 64.276  1.00 28.55  ? 501 GOL A C3  1 
HETATM 8239 O O3  . GOL E 4 .   ? -14.451 20.754 63.814  1.00 23.00  ? 501 GOL A O3  1 
HETATM 8240 C C1  . GOL F 4 .   ? -16.521 40.326 29.902  1.00 29.01  ? 501 GOL B C1  1 
HETATM 8241 O O1  . GOL F 4 .   ? -15.518 40.902 30.718  1.00 25.09  ? 501 GOL B O1  1 
HETATM 8242 C C2  . GOL F 4 .   ? -15.934 39.081 29.160  1.00 30.90  ? 501 GOL B C2  1 
HETATM 8243 O O2  . GOL F 4 .   ? -16.875 38.485 28.294  1.00 28.19  ? 501 GOL B O2  1 
HETATM 8244 C C3  . GOL F 4 .   ? -14.662 39.593 28.435  1.00 34.11  ? 501 GOL B C3  1 
HETATM 8245 O O3  . GOL F 4 .   ? -13.952 38.514 27.864  1.00 23.15  ? 501 GOL B O3  1 
HETATM 8246 O O   . HOH G 5 .   ? -12.528 30.807 63.470  1.00 50.47  ? 601 HOH A O   1 
HETATM 8247 O O   . HOH G 5 .   ? -4.337  26.349 83.303  1.00 53.21  ? 602 HOH A O   1 
HETATM 8248 O O   . HOH G 5 .   ? -13.828 30.525 50.369  1.00 45.82  ? 603 HOH A O   1 
HETATM 8249 O O   . HOH G 5 .   ? -12.927 38.945 53.742  1.00 45.33  ? 604 HOH A O   1 
HETATM 8250 O O   . HOH G 5 .   ? -16.438 31.661 60.367  1.00 38.81  ? 605 HOH A O   1 
HETATM 8251 O O   . HOH G 5 .   ? -23.346 8.057  81.181  1.00 38.30  ? 606 HOH A O   1 
HETATM 8252 O O   . HOH G 5 .   ? -20.927 9.394  62.872  1.00 50.43  ? 607 HOH A O   1 
HETATM 8253 O O   . HOH G 5 .   ? -20.674 25.920 71.734  1.00 29.96  ? 608 HOH A O   1 
HETATM 8254 O O   . HOH G 5 .   ? -0.833  14.737 97.073  1.00 43.28  ? 609 HOH A O   1 
HETATM 8255 O O   . HOH G 5 .   ? -23.081 21.551 58.383  1.00 47.85  ? 610 HOH A O   1 
HETATM 8256 O O   . HOH G 5 .   ? 17.361  6.790  46.774  1.00 42.15  ? 611 HOH A O   1 
HETATM 8257 O O   . HOH G 5 .   ? -10.174 22.294 70.628  1.00 20.25  ? 612 HOH A O   1 
HETATM 8258 O O   . HOH G 5 .   ? 19.954  27.450 80.580  1.00 31.48  ? 613 HOH A O   1 
HETATM 8259 O O   . HOH G 5 .   ? -30.261 8.293  78.292  1.00 49.18  ? 614 HOH A O   1 
HETATM 8260 O O   . HOH G 5 .   ? -10.781 24.461 94.367  1.00 59.36  ? 615 HOH A O   1 
HETATM 8261 O O   . HOH G 5 .   ? 23.290  12.550 89.959  1.00 47.89  ? 616 HOH A O   1 
HETATM 8262 O O   . HOH G 5 .   ? 26.935  23.836 70.787  1.00 38.41  ? 617 HOH A O   1 
HETATM 8263 O O   . HOH G 5 .   ? 6.361   26.859 54.968  1.00 30.82  ? 618 HOH A O   1 
HETATM 8264 O O   . HOH G 5 .   ? -31.674 14.011 90.465  1.00 34.22  ? 619 HOH A O   1 
HETATM 8265 O O   . HOH G 5 .   ? 19.724  12.364 69.916  1.00 19.05  ? 620 HOH A O   1 
HETATM 8266 O O   . HOH G 5 .   ? -3.951  3.875  47.039  1.00 43.46  ? 621 HOH A O   1 
HETATM 8267 O O   . HOH G 5 .   ? 25.632  25.975 77.948  1.00 47.37  ? 622 HOH A O   1 
HETATM 8268 O O   . HOH G 5 .   ? 17.209  24.343 53.368  1.00 32.66  ? 623 HOH A O   1 
HETATM 8269 O O   . HOH G 5 .   ? 18.962  26.088 55.014  1.00 40.53  ? 624 HOH A O   1 
HETATM 8270 O O   . HOH G 5 .   ? -19.873 15.125 71.273  1.00 20.49  ? 625 HOH A O   1 
HETATM 8271 O O   . HOH G 5 .   ? 12.481  6.977  45.149  1.00 33.53  ? 626 HOH A O   1 
HETATM 8272 O O   . HOH G 5 .   ? 0.266   31.171 61.755  1.00 39.35  ? 627 HOH A O   1 
HETATM 8273 O O   . HOH G 5 .   ? 19.228  20.817 69.111  1.00 28.03  ? 628 HOH A O   1 
HETATM 8274 O O   . HOH G 5 .   ? -36.439 16.299 81.741  1.00 22.57  ? 629 HOH A O   1 
HETATM 8275 O O   . HOH G 5 .   ? 4.903   18.589 75.144  1.00 25.27  ? 630 HOH A O   1 
HETATM 8276 O O   . HOH G 5 .   ? 1.196   3.379  61.047  1.00 37.48  ? 631 HOH A O   1 
HETATM 8277 O O   . HOH G 5 .   ? -19.807 12.262 59.321  1.00 40.68  ? 632 HOH A O   1 
HETATM 8278 O O   . HOH G 5 .   ? -11.128 15.180 86.090  1.00 24.43  ? 633 HOH A O   1 
HETATM 8279 O O   . HOH G 5 .   ? -8.306  14.428 47.217  1.00 31.41  ? 634 HOH A O   1 
HETATM 8280 O O   . HOH G 5 .   ? 14.169  26.409 78.750  1.00 40.65  ? 635 HOH A O   1 
HETATM 8281 O O   . HOH G 5 .   ? -14.722 1.464  69.238  1.00 25.64  ? 636 HOH A O   1 
HETATM 8282 O O   . HOH G 5 .   ? 11.233  11.440 68.462  1.00 26.75  ? 637 HOH A O   1 
HETATM 8283 O O   . HOH G 5 .   ? 10.204  13.036 70.514  1.00 23.06  ? 638 HOH A O   1 
HETATM 8284 O O   . HOH G 5 .   ? 9.399   16.983 52.700  1.00 17.37  ? 639 HOH A O   1 
HETATM 8285 O O   . HOH G 5 .   ? 21.158  15.613 87.734  1.00 29.46  ? 640 HOH A O   1 
HETATM 8286 O O   . HOH G 5 .   ? -12.385 9.104  51.596  1.00 51.52  ? 641 HOH A O   1 
HETATM 8287 O O   . HOH G 5 .   ? 24.246  23.676 49.087  1.00 38.02  ? 642 HOH A O   1 
HETATM 8288 O O   . HOH G 5 .   ? -15.527 15.156 92.015  1.00 26.46  ? 643 HOH A O   1 
HETATM 8289 O O   . HOH G 5 .   ? -2.489  10.014 41.006  1.00 50.72  ? 644 HOH A O   1 
HETATM 8290 O O   . HOH G 5 .   ? -17.939 22.227 70.839  1.00 23.43  ? 645 HOH A O   1 
HETATM 8291 O O   . HOH G 5 .   ? 17.991  23.347 72.035  1.00 30.44  ? 646 HOH A O   1 
HETATM 8292 O O   . HOH G 5 .   ? -10.129 5.447  86.872  1.00 26.43  ? 647 HOH A O   1 
HETATM 8293 O O   . HOH G 5 .   ? -19.091 32.083 78.034  1.00 44.86  ? 648 HOH A O   1 
HETATM 8294 O O   . HOH G 5 .   ? -17.509 14.742 62.483  1.00 19.25  ? 649 HOH A O   1 
HETATM 8295 O O   . HOH G 5 .   ? 3.879   16.201 69.047  1.00 17.01  ? 650 HOH A O   1 
HETATM 8296 O O   . HOH G 5 .   ? -4.936  21.599 67.183  1.00 25.90  ? 651 HOH A O   1 
HETATM 8297 O O   . HOH G 5 .   ? -20.142 14.439 68.503  1.00 22.80  ? 652 HOH A O   1 
HETATM 8298 O O   . HOH G 5 .   ? -9.350  13.067 81.297  1.00 23.99  ? 653 HOH A O   1 
HETATM 8299 O O   . HOH G 5 .   ? -11.519 31.570 78.705  1.00 36.18  ? 654 HOH A O   1 
HETATM 8300 O O   . HOH G 5 .   ? -34.248 17.750 65.774  1.00 47.07  ? 655 HOH A O   1 
HETATM 8301 O O   . HOH G 5 .   ? -10.945 15.917 60.225  1.00 22.86  ? 656 HOH A O   1 
HETATM 8302 O O   . HOH G 5 .   ? -14.417 29.800 61.219  1.00 29.06  ? 657 HOH A O   1 
HETATM 8303 O O   . HOH G 5 .   ? -3.793  4.072  51.217  1.00 32.65  ? 658 HOH A O   1 
HETATM 8304 O O   . HOH G 5 .   ? -31.717 32.022 86.902  1.00 46.14  ? 659 HOH A O   1 
HETATM 8305 O O   . HOH G 5 .   ? 1.340   20.115 92.704  1.00 28.24  ? 660 HOH A O   1 
HETATM 8306 O O   . HOH G 5 .   ? 7.538   15.826 44.983  1.00 25.78  ? 661 HOH A O   1 
HETATM 8307 O O   . HOH G 5 .   ? 13.038  0.050  59.420  1.00 38.06  ? 662 HOH A O   1 
HETATM 8308 O O   . HOH G 5 .   ? -26.475 22.306 66.442  1.00 40.08  ? 663 HOH A O   1 
HETATM 8309 O O   . HOH G 5 .   ? 21.298  15.133 64.985  1.00 20.75  ? 664 HOH A O   1 
HETATM 8310 O O   . HOH G 5 .   ? -8.724  16.773 46.223  1.00 30.64  ? 665 HOH A O   1 
HETATM 8311 O O   . HOH G 5 .   ? -22.562 19.899 63.298  1.00 29.70  ? 666 HOH A O   1 
HETATM 8312 O O   . HOH G 5 .   ? -32.127 23.926 85.473  1.00 29.11  ? 667 HOH A O   1 
HETATM 8313 O O   . HOH G 5 .   ? -17.453 32.526 75.109  1.00 35.51  ? 668 HOH A O   1 
HETATM 8314 O O   . HOH G 5 .   ? 21.702  10.535 79.802  1.00 34.80  ? 669 HOH A O   1 
HETATM 8315 O O   . HOH G 5 .   ? 13.245  12.313 42.452  1.00 35.65  ? 670 HOH A O   1 
HETATM 8316 O O   . HOH G 5 .   ? -5.561  9.502  47.128  1.00 41.94  ? 671 HOH A O   1 
HETATM 8317 O O   . HOH G 5 .   ? -6.094  -2.597 76.715  1.00 38.35  ? 672 HOH A O   1 
HETATM 8318 O O   . HOH G 5 .   ? -19.315 29.455 68.012  1.00 31.89  ? 673 HOH A O   1 
HETATM 8319 O O   . HOH G 5 .   ? -27.749 30.171 76.565  1.00 28.29  ? 674 HOH A O   1 
HETATM 8320 O O   . HOH G 5 .   ? 17.180  -0.493 69.491  1.00 50.50  ? 675 HOH A O   1 
HETATM 8321 O O   . HOH G 5 .   ? 3.107   -3.598 59.463  1.00 36.54  ? 676 HOH A O   1 
HETATM 8322 O O   . HOH G 5 .   ? -2.799  2.912  55.516  1.00 31.25  ? 677 HOH A O   1 
HETATM 8323 O O   . HOH G 5 .   ? -15.991 36.686 52.529  1.00 44.08  ? 678 HOH A O   1 
HETATM 8324 O O   . HOH G 5 .   ? 27.534  12.143 86.678  1.00 44.96  ? 679 HOH A O   1 
HETATM 8325 O O   . HOH G 5 .   ? 10.279  24.414 46.677  1.00 36.58  ? 680 HOH A O   1 
HETATM 8326 O O   . HOH G 5 .   ? 22.243  29.296 72.986  1.00 35.67  ? 681 HOH A O   1 
HETATM 8327 O O   . HOH G 5 .   ? -7.667  22.388 74.393  1.00 29.96  ? 682 HOH A O   1 
HETATM 8328 O O   . HOH G 5 .   ? -24.611 21.140 96.935  1.00 34.85  ? 683 HOH A O   1 
HETATM 8329 O O   . HOH G 5 .   ? -3.959  33.481 67.668  1.00 31.23  ? 684 HOH A O   1 
HETATM 8330 O O   . HOH G 5 .   ? -11.183 32.227 73.152  1.00 50.25  ? 685 HOH A O   1 
HETATM 8331 O O   . HOH G 5 .   ? 15.582  20.204 47.466  1.00 35.89  ? 686 HOH A O   1 
HETATM 8332 O O   . HOH G 5 .   ? 3.213   5.282  42.667  1.00 48.05  ? 687 HOH A O   1 
HETATM 8333 O O   . HOH G 5 .   ? -8.124  29.512 78.882  1.00 32.97  ? 688 HOH A O   1 
HETATM 8334 O O   . HOH G 5 .   ? 3.014   22.267 86.320  1.00 46.05  ? 689 HOH A O   1 
HETATM 8335 O O   . HOH G 5 .   ? 1.656   29.234 48.925  1.00 47.21  ? 690 HOH A O   1 
HETATM 8336 O O   . HOH G 5 .   ? -4.358  13.655 53.526  1.00 21.45  ? 691 HOH A O   1 
HETATM 8337 O O   . HOH G 5 .   ? -13.227 3.497  71.697  1.00 19.61  ? 692 HOH A O   1 
HETATM 8338 O O   . HOH G 5 .   ? 16.689  26.529 65.283  1.00 25.70  ? 693 HOH A O   1 
HETATM 8339 O O   . HOH G 5 .   ? 20.743  8.905  78.009  1.00 32.13  ? 694 HOH A O   1 
HETATM 8340 O O   . HOH G 5 .   ? -6.076  -2.420 60.782  1.00 28.10  ? 695 HOH A O   1 
HETATM 8341 O O   . HOH G 5 .   ? -26.726 32.064 73.648  1.00 34.43  ? 696 HOH A O   1 
HETATM 8342 O O   . HOH G 5 .   ? -25.614 9.264  81.613  1.00 47.95  ? 697 HOH A O   1 
HETATM 8343 O O   . HOH G 5 .   ? -12.529 23.118 42.136  1.00 44.97  ? 698 HOH A O   1 
HETATM 8344 O O   . HOH G 5 .   ? 2.798   12.148 78.094  1.00 19.42  ? 699 HOH A O   1 
HETATM 8345 O O   . HOH G 5 .   ? 6.749   14.717 40.172  1.00 33.54  ? 700 HOH A O   1 
HETATM 8346 O O   . HOH G 5 .   ? 1.086   24.220 63.467  1.00 33.11  ? 701 HOH A O   1 
HETATM 8347 O O   . HOH G 5 .   ? -0.169  1.467  58.893  1.00 46.87  ? 702 HOH A O   1 
HETATM 8348 O O   . HOH G 5 .   ? 15.564  0.866  54.902  1.00 44.23  ? 703 HOH A O   1 
HETATM 8349 O O   . HOH G 5 .   ? 23.155  8.907  76.428  1.00 50.18  ? 704 HOH A O   1 
HETATM 8350 O O   . HOH G 5 .   ? 5.477   19.439 52.901  1.00 27.30  ? 705 HOH A O   1 
HETATM 8351 O O   . HOH G 5 .   ? -6.453  28.968 64.153  1.00 22.16  ? 706 HOH A O   1 
HETATM 8352 O O   . HOH G 5 .   ? 24.325  5.293  77.857  1.00 40.74  ? 707 HOH A O   1 
HETATM 8353 O O   . HOH G 5 .   ? 22.017  16.728 55.445  1.00 43.90  ? 708 HOH A O   1 
HETATM 8354 O O   . HOH G 5 .   ? -0.837  4.109  80.213  1.00 31.75  ? 709 HOH A O   1 
HETATM 8355 O O   . HOH G 5 .   ? -15.310 13.462 68.837  1.00 23.28  ? 710 HOH A O   1 
HETATM 8356 O O   . HOH G 5 .   ? 8.316   27.644 66.368  1.00 32.12  ? 711 HOH A O   1 
HETATM 8357 O O   . HOH G 5 .   ? -8.014  17.684 90.330  1.00 39.76  ? 712 HOH A O   1 
HETATM 8358 O O   . HOH G 5 .   ? 18.066  2.904  72.250  1.00 44.79  ? 713 HOH A O   1 
HETATM 8359 O O   . HOH G 5 .   ? 22.434  18.348 87.949  1.00 32.10  ? 714 HOH A O   1 
HETATM 8360 O O   . HOH G 5 .   ? -13.414 4.135  50.834  1.00 45.76  ? 715 HOH A O   1 
HETATM 8361 O O   . HOH G 5 .   ? 22.649  3.143  54.366  1.00 40.86  ? 716 HOH A O   1 
HETATM 8362 O O   . HOH G 5 .   ? -15.232 27.363 61.835  1.00 22.68  ? 717 HOH A O   1 
HETATM 8363 O O   . HOH G 5 .   ? -12.136 30.368 59.755  1.00 30.52  ? 718 HOH A O   1 
HETATM 8364 O O   . HOH G 5 .   ? -18.004 7.159  90.266  1.00 49.82  ? 719 HOH A O   1 
HETATM 8365 O O   . HOH G 5 .   ? 16.646  0.109  90.150  1.00 56.41  ? 720 HOH A O   1 
HETATM 8366 O O   . HOH G 5 .   ? 14.315  9.858  94.091  1.00 34.95  ? 721 HOH A O   1 
HETATM 8367 O O   . HOH G 5 .   ? 4.306   20.201 85.190  1.00 22.43  ? 722 HOH A O   1 
HETATM 8368 O O   . HOH G 5 .   ? 9.379   14.899 93.360  1.00 34.09  ? 723 HOH A O   1 
HETATM 8369 O O   . HOH G 5 .   ? -31.141 9.364  80.051  1.00 50.56  ? 724 HOH A O   1 
HETATM 8370 O O   . HOH G 5 .   ? -2.383  5.642  86.856  1.00 33.22  ? 725 HOH A O   1 
HETATM 8371 O O   . HOH G 5 .   ? -17.531 36.673 58.907  1.00 49.12  ? 726 HOH A O   1 
HETATM 8372 O O   . HOH G 5 .   ? 14.040  1.717  84.783  1.00 46.66  ? 727 HOH A O   1 
HETATM 8373 O O   . HOH G 5 .   ? -33.855 18.184 87.122  1.00 23.21  ? 728 HOH A O   1 
HETATM 8374 O O   . HOH G 5 .   ? -0.508  12.830 37.655  1.00 49.73  ? 729 HOH A O   1 
HETATM 8375 O O   . HOH G 5 .   ? 20.372  5.329  67.840  1.00 32.38  ? 730 HOH A O   1 
HETATM 8376 O O   . HOH G 5 .   ? 17.118  21.886 64.549  1.00 34.50  ? 731 HOH A O   1 
HETATM 8377 O O   . HOH G 5 .   ? -5.192  27.718 68.445  1.00 50.84  ? 732 HOH A O   1 
HETATM 8378 O O   . HOH G 5 .   ? -12.875 -0.765 70.205  1.00 31.81  ? 733 HOH A O   1 
HETATM 8379 O O   . HOH G 5 .   ? -5.621  3.385  54.447  1.00 44.88  ? 734 HOH A O   1 
HETATM 8380 O O   . HOH G 5 .   ? -23.643 23.731 66.176  1.00 41.97  ? 735 HOH A O   1 
HETATM 8381 O O   . HOH G 5 .   ? 24.872  12.411 65.063  1.00 34.31  ? 736 HOH A O   1 
HETATM 8382 O O   . HOH G 5 .   ? -7.207  28.154 66.822  1.00 24.62  ? 737 HOH A O   1 
HETATM 8383 O O   . HOH G 5 .   ? 23.220  15.514 53.478  1.00 39.79  ? 738 HOH A O   1 
HETATM 8384 O O   . HOH G 5 .   ? -31.511 25.454 95.344  1.00 30.13  ? 739 HOH A O   1 
HETATM 8385 O O   . HOH G 5 .   ? 17.333  23.895 88.775  1.00 42.34  ? 740 HOH A O   1 
HETATM 8386 O O   . HOH G 5 .   ? -2.351  3.047  58.298  1.00 26.93  ? 741 HOH A O   1 
HETATM 8387 O O   . HOH G 5 .   ? 24.724  15.328 79.338  1.00 39.70  ? 742 HOH A O   1 
HETATM 8388 O O   . HOH G 5 .   ? 6.695   30.210 64.530  1.00 48.04  ? 743 HOH A O   1 
HETATM 8389 O O   . HOH G 5 .   ? -1.827  -0.886 77.207  1.00 40.41  ? 744 HOH A O   1 
HETATM 8390 O O   . HOH G 5 .   ? -25.268 20.237 59.360  1.00 45.55  ? 745 HOH A O   1 
HETATM 8391 O O   . HOH G 5 .   ? -23.013 8.158  67.008  1.00 48.10  ? 746 HOH A O   1 
HETATM 8392 O O   . HOH G 5 .   ? 15.885  30.022 84.970  1.00 39.23  ? 747 HOH A O   1 
HETATM 8393 O O   . HOH G 5 .   ? -6.387  24.161 73.250  1.00 50.05  ? 748 HOH A O   1 
HETATM 8394 O O   . HOH G 5 .   ? -10.601 11.927 96.363  1.00 49.02  ? 749 HOH A O   1 
HETATM 8395 O O   . HOH G 5 .   ? 13.790  12.097 92.575  1.00 30.48  ? 750 HOH A O   1 
HETATM 8396 O O   . HOH G 5 .   ? -18.793 4.988  63.584  1.00 43.75  ? 751 HOH A O   1 
HETATM 8397 O O   . HOH G 5 .   ? 22.130  22.247 49.848  1.00 33.95  ? 752 HOH A O   1 
HETATM 8398 O O   . HOH G 5 .   ? 3.313   27.405 52.145  1.00 38.85  ? 753 HOH A O   1 
HETATM 8399 O O   . HOH G 5 .   ? 23.126  23.381 46.855  1.00 56.82  ? 754 HOH A O   1 
HETATM 8400 O O   . HOH G 5 .   ? 1.949   10.641 80.254  1.00 21.86  ? 755 HOH A O   1 
HETATM 8401 O O   . HOH G 5 .   ? 6.531   -2.334 85.019  1.00 48.63  ? 756 HOH A O   1 
HETATM 8402 O O   . HOH G 5 .   ? -0.782  22.196 66.579  1.00 30.88  ? 757 HOH A O   1 
HETATM 8403 O O   . HOH G 5 .   ? -19.948 12.461 97.104  1.00 54.61  ? 758 HOH A O   1 
HETATM 8404 O O   . HOH G 5 .   ? -13.002 -2.479 61.246  1.00 51.82  ? 759 HOH A O   1 
HETATM 8405 O O   . HOH G 5 .   ? -11.533 33.632 67.986  1.00 50.03  ? 760 HOH A O   1 
HETATM 8406 O O   . HOH G 5 .   ? 24.151  14.342 65.919  1.00 35.55  ? 761 HOH A O   1 
HETATM 8407 O O   . HOH G 5 .   ? 1.919   29.347 51.455  1.00 32.86  ? 762 HOH A O   1 
HETATM 8408 O O   . HOH G 5 .   ? -4.038  0.223  56.002  1.00 40.28  ? 763 HOH A O   1 
HETATM 8409 O O   . HOH G 5 .   ? 5.577   -2.462 93.263  1.00 51.51  ? 764 HOH A O   1 
HETATM 8410 O O   . HOH G 5 .   ? 25.328  11.186 67.026  1.00 41.20  ? 765 HOH A O   1 
HETATM 8411 O O   . HOH G 5 .   ? -25.056 9.049  67.169  1.00 46.89  ? 766 HOH A O   1 
HETATM 8412 O O   . HOH G 5 .   ? -15.765 0.203  73.213  1.00 41.36  ? 767 HOH A O   1 
HETATM 8413 O O   . HOH G 5 .   ? -17.849 3.527  64.922  1.00 42.64  ? 768 HOH A O   1 
HETATM 8414 O O   . HOH G 5 .   ? 25.149  10.008 63.562  1.00 37.83  ? 769 HOH A O   1 
HETATM 8415 O O   . HOH G 5 .   ? -3.249  -0.537 79.335  1.00 46.37  ? 770 HOH A O   1 
HETATM 8416 O O   . HOH G 5 .   ? -13.660 33.459 67.592  1.00 52.08  ? 771 HOH A O   1 
HETATM 8417 O O   . HOH G 5 .   ? 24.522  13.198 67.899  1.00 40.14  ? 772 HOH A O   1 
HETATM 8418 O O   . HOH G 5 .   ? -2.986  23.617 67.114  1.00 38.90  ? 773 HOH A O   1 
HETATM 8419 O O   . HOH G 5 .   ? -12.288 -0.376 74.860  1.00 43.83  ? 774 HOH A O   1 
HETATM 8420 O O   . HOH G 5 .   ? -3.082  23.430 73.371  1.00 42.80  ? 775 HOH A O   1 
HETATM 8421 O O   . HOH G 5 .   ? 17.330  27.963 67.315  1.00 60.56  ? 776 HOH A O   1 
HETATM 8422 O O   . HOH G 5 .   ? 24.909  9.966  75.398  1.00 48.23  ? 777 HOH A O   1 
HETATM 8423 O O   . HOH G 5 .   ? -7.547  38.138 59.217  1.00 46.00  ? 778 HOH A O   1 
HETATM 8424 O O   . HOH G 5 .   ? -35.182 24.442 84.876  1.00 50.89  ? 779 HOH A O   1 
HETATM 8425 O O   . HOH G 5 .   ? 4.241   29.570 65.659  1.00 59.46  ? 780 HOH A O   1 
HETATM 8426 O O   . HOH G 5 .   ? -22.328 27.317 70.498  1.00 45.72  ? 781 HOH A O   1 
HETATM 8427 O O   . HOH G 5 .   ? -20.597 21.682 53.221  1.00 53.83  ? 782 HOH A O   1 
HETATM 8428 O O   . HOH G 5 .   ? -19.941 23.802 52.913  1.00 43.13  ? 783 HOH A O   1 
HETATM 8429 O O   . HOH G 5 .   ? 15.409  28.904 78.223  1.00 53.12  ? 784 HOH A O   1 
HETATM 8430 O O   . HOH G 5 .   ? 13.033  9.843  42.342  1.00 50.64  ? 785 HOH A O   1 
HETATM 8431 O O   . HOH G 5 .   ? -28.411 30.049 74.223  1.00 39.94  ? 786 HOH A O   1 
HETATM 8432 O O   . HOH G 5 .   ? -13.047 0.703  72.995  1.00 40.86  ? 787 HOH A O   1 
HETATM 8433 O O   . HOH G 5 .   ? -1.750  22.898 75.172  1.00 41.51  ? 788 HOH A O   1 
HETATM 8434 O O   . HOH G 5 .   ? -21.951 3.353  58.991  1.00 53.26  ? 789 HOH A O   1 
HETATM 8435 O O   . HOH G 5 .   ? 22.691  17.319 52.162  1.00 53.88  ? 790 HOH A O   1 
HETATM 8436 O O   . HOH H 5 .   ? -16.599 33.749 -1.425  1.00 60.01  ? 601 HOH B O   1 
HETATM 8437 O O   . HOH H 5 .   ? -36.452 38.784 22.370  1.00 24.90  ? 602 HOH B O   1 
HETATM 8438 O O   . HOH H 5 .   ? -21.772 22.358 6.949   1.00 60.47  ? 603 HOH B O   1 
HETATM 8439 O O   . HOH H 5 .   ? -41.698 23.140 40.816  1.00 37.20  ? 604 HOH B O   1 
HETATM 8440 O O   . HOH H 5 .   ? -22.246 35.291 9.004   1.00 27.59  ? 605 HOH B O   1 
HETATM 8441 O O   . HOH H 5 .   ? -48.634 37.535 48.959  1.00 52.28  ? 606 HOH B O   1 
HETATM 8442 O O   . HOH H 5 .   ? -12.117 52.699 15.438  1.00 59.64  ? 607 HOH B O   1 
HETATM 8443 O O   . HOH H 5 .   ? -13.584 33.369 -3.732  1.00 49.40  ? 608 HOH B O   1 
HETATM 8444 O O   . HOH H 5 .   ? -50.163 41.123 30.034  1.00 36.98  ? 609 HOH B O   1 
HETATM 8445 O O   . HOH H 5 .   ? -40.345 34.704 1.503   1.00 47.49  ? 610 HOH B O   1 
HETATM 8446 O O   . HOH H 5 .   ? -39.287 18.342 13.043  1.00 49.53  ? 611 HOH B O   1 
HETATM 8447 O O   . HOH H 5 .   ? -29.861 51.434 34.711  1.00 39.83  ? 612 HOH B O   1 
HETATM 8448 O O   . HOH H 5 .   ? -39.192 41.144 58.437  1.00 38.34  ? 613 HOH B O   1 
HETATM 8449 O O   . HOH H 5 .   ? -2.888  41.565 25.730  1.00 41.87  ? 614 HOH B O   1 
HETATM 8450 O O   . HOH H 5 .   ? -23.839 34.206 42.370  1.00 21.64  ? 615 HOH B O   1 
HETATM 8451 O O   . HOH H 5 .   ? -34.910 47.362 41.942  1.00 35.39  ? 616 HOH B O   1 
HETATM 8452 O O   . HOH H 5 .   ? -56.615 31.691 24.407  1.00 38.74  ? 617 HOH B O   1 
HETATM 8453 O O   . HOH H 5 .   ? -24.753 46.987 7.154   1.00 53.48  ? 618 HOH B O   1 
HETATM 8454 O O   . HOH H 5 .   ? -12.829 42.418 22.930  1.00 31.08  ? 619 HOH B O   1 
HETATM 8455 O O   . HOH H 5 .   ? -20.526 42.328 24.512  1.00 25.96  ? 620 HOH B O   1 
HETATM 8456 O O   . HOH H 5 .   ? -1.805  51.597 14.657  1.00 49.82  ? 621 HOH B O   1 
HETATM 8457 O O   . HOH H 5 .   ? -19.863 32.326 -4.135  1.00 39.96  ? 622 HOH B O   1 
HETATM 8458 O O   . HOH H 5 .   ? -3.427  33.071 0.973   1.00 41.20  ? 623 HOH B O   1 
HETATM 8459 O O   . HOH H 5 .   ? -18.908 37.661 48.854  1.00 38.94  ? 624 HOH B O   1 
HETATM 8460 O O   . HOH H 5 .   ? -41.718 31.679 30.021  1.00 27.41  ? 625 HOH B O   1 
HETATM 8461 O O   . HOH H 5 .   ? -24.468 24.665 44.856  1.00 34.06  ? 626 HOH B O   1 
HETATM 8462 O O   . HOH H 5 .   ? -23.361 25.852 8.765   1.00 35.50  ? 627 HOH B O   1 
HETATM 8463 O O   . HOH H 5 .   ? -50.594 34.635 49.231  1.00 54.58  ? 628 HOH B O   1 
HETATM 8464 O O   . HOH H 5 .   ? -5.423  48.061 -5.614  1.00 50.19  ? 629 HOH B O   1 
HETATM 8465 O O   . HOH H 5 .   ? -11.225 35.184 22.750  1.00 28.18  ? 630 HOH B O   1 
HETATM 8466 O O   . HOH H 5 .   ? -37.776 45.264 33.996  1.00 33.05  ? 631 HOH B O   1 
HETATM 8467 O O   . HOH H 5 .   ? -16.932 17.475 33.000  1.00 51.76  ? 632 HOH B O   1 
HETATM 8468 O O   . HOH H 5 .   ? -40.934 33.083 27.634  1.00 31.83  ? 633 HOH B O   1 
HETATM 8469 O O   . HOH H 5 .   ? -11.360 41.102 26.079  1.00 34.16  ? 634 HOH B O   1 
HETATM 8470 O O   . HOH H 5 .   ? -43.206 41.127 50.357  1.00 36.60  ? 635 HOH B O   1 
HETATM 8471 O O   . HOH H 5 .   ? -21.754 30.274 48.543  1.00 36.14  ? 636 HOH B O   1 
HETATM 8472 O O   . HOH H 5 .   ? -26.659 53.758 28.848  1.00 42.72  ? 637 HOH B O   1 
HETATM 8473 O O   . HOH H 5 .   ? -25.405 41.874 28.672  1.00 21.44  ? 638 HOH B O   1 
HETATM 8474 O O   . HOH H 5 .   ? -33.850 39.712 44.402  1.00 37.15  ? 639 HOH B O   1 
HETATM 8475 O O   . HOH H 5 .   ? -18.542 36.531 34.745  1.00 22.25  ? 640 HOH B O   1 
HETATM 8476 O O   . HOH H 5 .   ? -12.264 35.212 31.711  1.00 26.86  ? 641 HOH B O   1 
HETATM 8477 O O   . HOH H 5 .   ? -10.314 45.974 21.512  1.00 41.98  ? 642 HOH B O   1 
HETATM 8478 O O   . HOH H 5 .   ? -37.525 37.731 45.083  1.00 21.89  ? 643 HOH B O   1 
HETATM 8479 O O   . HOH H 5 .   ? -22.395 16.023 26.804  1.00 42.94  ? 644 HOH B O   1 
HETATM 8480 O O   . HOH H 5 .   ? -9.867  32.737 34.019  1.00 45.85  ? 645 HOH B O   1 
HETATM 8481 O O   . HOH H 5 .   ? -22.398 51.520 58.322  1.00 47.06  ? 646 HOH B O   1 
HETATM 8482 O O   . HOH H 5 .   ? -7.595  43.897 29.565  1.00 49.38  ? 647 HOH B O   1 
HETATM 8483 O O   . HOH H 5 .   ? -20.546 51.579 16.356  1.00 38.19  ? 648 HOH B O   1 
HETATM 8484 O O   . HOH H 5 .   ? -23.177 33.116 14.219  1.00 29.28  ? 649 HOH B O   1 
HETATM 8485 O O   . HOH H 5 .   ? -37.432 26.490 47.412  1.00 33.18  ? 650 HOH B O   1 
HETATM 8486 O O   . HOH H 5 .   ? -50.337 32.465 29.532  1.00 31.39  ? 651 HOH B O   1 
HETATM 8487 O O   . HOH H 5 .   ? -40.106 42.057 53.962  1.00 33.90  ? 652 HOH B O   1 
HETATM 8488 O O   . HOH H 5 .   ? -51.201 43.007 51.516  1.00 56.13  ? 653 HOH B O   1 
HETATM 8489 O O   . HOH H 5 .   ? -7.584  29.840 6.341   1.00 41.42  ? 654 HOH B O   1 
HETATM 8490 O O   . HOH H 5 .   ? -40.819 17.117 4.201   1.00 40.88  ? 655 HOH B O   1 
HETATM 8491 O O   . HOH H 5 .   ? -17.632 50.704 34.641  1.00 36.68  ? 656 HOH B O   1 
HETATM 8492 O O   . HOH H 5 .   ? -50.893 36.062 46.214  1.00 51.67  ? 657 HOH B O   1 
HETATM 8493 O O   . HOH H 5 .   ? -17.908 23.746 23.155  1.00 32.89  ? 658 HOH B O   1 
HETATM 8494 O O   . HOH H 5 .   ? -19.198 35.187 2.370   1.00 35.75  ? 659 HOH B O   1 
HETATM 8495 O O   . HOH H 5 .   ? -14.415 47.834 32.204  1.00 27.86  ? 660 HOH B O   1 
HETATM 8496 O O   . HOH H 5 .   ? -51.140 35.311 34.580  1.00 27.94  ? 661 HOH B O   1 
HETATM 8497 O O   . HOH H 5 .   ? -34.812 32.195 19.134  1.00 24.55  ? 662 HOH B O   1 
HETATM 8498 O O   . HOH H 5 .   ? -39.005 28.040 53.489  1.00 38.08  ? 663 HOH B O   1 
HETATM 8499 O O   . HOH H 5 .   ? -37.254 45.898 59.100  1.00 55.78  ? 664 HOH B O   1 
HETATM 8500 O O   . HOH H 5 .   ? -52.849 32.835 30.457  1.00 40.20  ? 665 HOH B O   1 
HETATM 8501 O O   . HOH H 5 .   ? -9.208  27.856 12.127  1.00 42.77  ? 666 HOH B O   1 
HETATM 8502 O O   . HOH H 5 .   ? -34.383 36.370 28.017  1.00 20.85  ? 667 HOH B O   1 
HETATM 8503 O O   . HOH H 5 .   ? -16.459 18.084 29.254  1.00 45.58  ? 668 HOH B O   1 
HETATM 8504 O O   . HOH H 5 .   ? -16.447 51.605 30.606  1.00 36.40  ? 669 HOH B O   1 
HETATM 8505 O O   . HOH H 5 .   ? -49.070 23.252 27.240  1.00 49.14  ? 670 HOH B O   1 
HETATM 8506 O O   . HOH H 5 .   ? -31.172 44.484 33.094  1.00 35.53  ? 671 HOH B O   1 
HETATM 8507 O O   . HOH H 5 .   ? -59.681 37.354 22.487  1.00 37.25  ? 672 HOH B O   1 
HETATM 8508 O O   . HOH H 5 .   ? -19.691 40.155 -5.657  1.00 37.01  ? 673 HOH B O   1 
HETATM 8509 O O   . HOH H 5 .   ? -30.057 49.839 47.589  1.00 37.32  ? 674 HOH B O   1 
HETATM 8510 O O   . HOH H 5 .   ? -50.363 37.147 44.264  1.00 51.91  ? 675 HOH B O   1 
HETATM 8511 O O   . HOH H 5 .   ? -33.766 50.601 36.384  1.00 50.03  ? 676 HOH B O   1 
HETATM 8512 O O   . HOH H 5 .   ? -2.518  54.413 6.329   1.00 56.13  ? 677 HOH B O   1 
HETATM 8513 O O   . HOH H 5 .   ? -18.870 35.101 47.957  1.00 33.80  ? 678 HOH B O   1 
HETATM 8514 O O   . HOH H 5 .   ? -23.576 49.394 30.947  1.00 27.99  ? 679 HOH B O   1 
HETATM 8515 O O   . HOH H 5 .   ? -3.826  47.851 19.745  1.00 45.65  ? 680 HOH B O   1 
HETATM 8516 O O   . HOH H 5 .   ? -46.929 42.260 34.344  1.00 30.56  ? 681 HOH B O   1 
HETATM 8517 O O   . HOH H 5 .   ? -24.283 49.533 16.296  1.00 48.42  ? 682 HOH B O   1 
HETATM 8518 O O   . HOH H 5 .   ? -22.966 23.522 40.806  1.00 40.75  ? 683 HOH B O   1 
HETATM 8519 O O   . HOH H 5 .   ? -34.754 36.599 52.249  1.00 28.96  ? 684 HOH B O   1 
HETATM 8520 O O   . HOH H 5 .   ? -49.103 43.053 27.202  1.00 39.29  ? 685 HOH B O   1 
HETATM 8521 O O   . HOH H 5 .   ? -11.591 49.728 25.291  1.00 40.61  ? 686 HOH B O   1 
HETATM 8522 O O   . HOH H 5 .   ? -43.300 35.386 55.778  1.00 54.46  ? 687 HOH B O   1 
HETATM 8523 O O   . HOH H 5 .   ? -55.913 28.967 28.429  1.00 45.43  ? 688 HOH B O   1 
HETATM 8524 O O   . HOH H 5 .   ? -14.897 59.823 40.391  1.00 47.87  ? 689 HOH B O   1 
HETATM 8525 O O   . HOH H 5 .   ? -48.983 21.262 17.811  1.00 34.13  ? 690 HOH B O   1 
HETATM 8526 O O   . HOH H 5 .   ? -23.981 42.481 21.125  1.00 37.53  ? 691 HOH B O   1 
HETATM 8527 O O   . HOH H 5 .   ? -25.820 23.387 40.937  1.00 41.03  ? 692 HOH B O   1 
HETATM 8528 O O   . HOH H 5 .   ? -37.621 44.670 51.650  1.00 47.46  ? 693 HOH B O   1 
HETATM 8529 O O   . HOH H 5 .   ? -32.803 53.614 10.786  1.00 45.68  ? 694 HOH B O   1 
HETATM 8530 O O   . HOH H 5 .   ? -15.223 33.739 25.503  1.00 22.51  ? 695 HOH B O   1 
HETATM 8531 O O   . HOH H 5 .   ? -2.229  51.807 4.291   1.00 40.75  ? 696 HOH B O   1 
HETATM 8532 O O   . HOH H 5 .   ? -8.299  32.351 0.660   1.00 36.34  ? 697 HOH B O   1 
HETATM 8533 O O   . HOH H 5 .   ? -18.604 35.612 52.193  1.00 38.08  ? 698 HOH B O   1 
HETATM 8534 O O   . HOH H 5 .   ? -8.529  25.378 16.403  1.00 40.79  ? 699 HOH B O   1 
HETATM 8535 O O   . HOH H 5 .   ? -9.610  23.331 22.413  1.00 54.50  ? 700 HOH B O   1 
HETATM 8536 O O   . HOH H 5 .   ? -23.868 36.982 61.823  1.00 61.36  ? 701 HOH B O   1 
HETATM 8537 O O   . HOH H 5 .   ? -47.001 46.864 44.045  1.00 42.64  ? 702 HOH B O   1 
HETATM 8538 O O   . HOH H 5 .   ? -21.244 36.323 0.882   1.00 57.34  ? 703 HOH B O   1 
HETATM 8539 O O   . HOH H 5 .   ? -23.861 28.354 51.537  1.00 60.10  ? 704 HOH B O   1 
HETATM 8540 O O   . HOH H 5 .   ? -7.667  51.760 31.424  1.00 49.37  ? 705 HOH B O   1 
HETATM 8541 O O   . HOH H 5 .   ? -51.763 22.805 20.716  1.00 45.29  ? 706 HOH B O   1 
HETATM 8542 O O   . HOH H 5 .   ? -32.507 22.322 6.408   1.00 51.20  ? 707 HOH B O   1 
HETATM 8543 O O   . HOH H 5 .   ? -49.289 23.429 19.473  1.00 31.16  ? 708 HOH B O   1 
HETATM 8544 O O   . HOH H 5 .   ? -55.431 29.254 25.065  1.00 42.70  ? 709 HOH B O   1 
HETATM 8545 O O   . HOH H 5 .   ? -10.476 34.505 24.932  1.00 28.56  ? 710 HOH B O   1 
HETATM 8546 O O   . HOH H 5 .   ? -43.830 31.502 53.322  1.00 38.50  ? 711 HOH B O   1 
HETATM 8547 O O   . HOH H 5 .   ? -4.672  33.365 37.286  1.00 57.91  ? 712 HOH B O   1 
HETATM 8548 O O   . HOH H 5 .   ? -58.116 33.394 27.618  1.00 42.51  ? 713 HOH B O   1 
HETATM 8549 O O   . HOH H 5 .   ? -30.555 25.386 9.816   1.00 42.57  ? 714 HOH B O   1 
HETATM 8550 O O   . HOH H 5 .   ? -33.166 35.617 57.281  1.00 36.39  ? 715 HOH B O   1 
HETATM 8551 O O   . HOH H 5 .   ? -46.836 33.790 52.854  1.00 29.97  ? 716 HOH B O   1 
HETATM 8552 O O   . HOH H 5 .   ? -38.453 47.805 30.949  1.00 41.12  ? 717 HOH B O   1 
HETATM 8553 O O   . HOH H 5 .   ? -8.359  45.037 35.992  1.00 40.31  ? 718 HOH B O   1 
HETATM 8554 O O   . HOH H 5 .   ? -29.701 42.157 29.565  1.00 37.48  ? 719 HOH B O   1 
HETATM 8555 O O   . HOH H 5 .   ? -40.394 33.548 56.109  1.00 36.13  ? 720 HOH B O   1 
HETATM 8556 O O   . HOH H 5 .   ? -44.687 33.951 54.744  1.00 44.82  ? 721 HOH B O   1 
HETATM 8557 O O   . HOH H 5 .   ? -55.486 31.388 37.750  1.00 52.95  ? 722 HOH B O   1 
HETATM 8558 O O   . HOH H 5 .   ? -9.028  43.527 21.739  1.00 33.56  ? 723 HOH B O   1 
HETATM 8559 O O   . HOH H 5 .   ? -14.416 33.349 48.946  1.00 39.43  ? 724 HOH B O   1 
HETATM 8560 O O   . HOH H 5 .   ? -4.099  50.025 15.505  1.00 40.20  ? 725 HOH B O   1 
HETATM 8561 O O   . HOH H 5 .   ? -17.386 25.650 12.185  1.00 39.39  ? 726 HOH B O   1 
HETATM 8562 O O   . HOH H 5 .   ? 0.849   43.310 31.028  1.00 59.34  ? 727 HOH B O   1 
HETATM 8563 O O   . HOH H 5 .   ? -32.573 48.169 44.266  1.00 39.06  ? 728 HOH B O   1 
HETATM 8564 O O   . HOH H 5 .   ? -10.500 44.846 45.584  1.00 52.49  ? 729 HOH B O   1 
HETATM 8565 O O   . HOH H 5 .   ? -23.256 48.364 28.323  1.00 26.40  ? 730 HOH B O   1 
HETATM 8566 O O   . HOH H 5 .   ? -21.850 24.767 45.781  1.00 43.59  ? 731 HOH B O   1 
HETATM 8567 O O   . HOH H 5 .   ? -41.447 16.084 11.592  1.00 51.06  ? 732 HOH B O   1 
HETATM 8568 O O   . HOH H 5 .   ? -6.958  57.356 6.182   1.00 36.81  ? 733 HOH B O   1 
HETATM 8569 O O   . HOH H 5 .   ? -26.666 23.313 38.094  1.00 24.97  ? 734 HOH B O   1 
HETATM 8570 O O   . HOH H 5 .   ? -28.827 21.317 38.013  1.00 53.17  ? 735 HOH B O   1 
HETATM 8571 O O   . HOH H 5 .   ? -25.500 47.888 26.793  1.00 31.14  ? 736 HOH B O   1 
HETATM 8572 O O   . HOH H 5 .   ? -24.733 21.266 39.550  1.00 41.60  ? 737 HOH B O   1 
HETATM 8573 O O   . HOH H 5 .   ? -34.267 30.579 17.043  1.00 20.12  ? 738 HOH B O   1 
HETATM 8574 O O   . HOH H 5 .   ? -53.537 48.839 26.882  1.00 38.41  ? 739 HOH B O   1 
HETATM 8575 O O   . HOH H 5 .   ? -52.543 32.842 32.704  1.00 31.44  ? 740 HOH B O   1 
HETATM 8576 O O   . HOH H 5 .   ? -18.087 19.241 24.574  1.00 44.81  ? 741 HOH B O   1 
HETATM 8577 O O   . HOH H 5 .   ? -18.228 20.974 21.817  1.00 51.62  ? 742 HOH B O   1 
HETATM 8578 O O   . HOH H 5 .   ? -13.903 28.144 48.816  1.00 46.57  ? 743 HOH B O   1 
HETATM 8579 O O   . HOH H 5 .   ? -55.781 33.663 39.569  1.00 39.34  ? 744 HOH B O   1 
HETATM 8580 O O   . HOH H 5 .   ? -27.356 44.001 28.323  1.00 35.54  ? 745 HOH B O   1 
HETATM 8581 O O   . HOH H 5 .   ? -53.644 43.954 13.292  1.00 61.75  ? 746 HOH B O   1 
HETATM 8582 O O   . HOH H 5 .   ? -4.714  44.407 30.664  1.00 55.33  ? 747 HOH B O   1 
HETATM 8583 O O   . HOH H 5 .   ? -17.553 30.985 -3.283  1.00 42.70  ? 748 HOH B O   1 
HETATM 8584 O O   . HOH H 5 .   ? -53.736 41.667 13.174  1.00 52.49  ? 749 HOH B O   1 
HETATM 8585 O O   . HOH H 5 .   ? -33.491 22.220 13.713  1.00 47.63  ? 750 HOH B O   1 
HETATM 8586 O O   . HOH H 5 .   ? -5.012  49.758 20.496  1.00 54.46  ? 751 HOH B O   1 
HETATM 8587 O O   . HOH H 5 .   ? -15.232 50.322 32.815  1.00 34.52  ? 752 HOH B O   1 
HETATM 8588 O O   . HOH H 5 .   ? -22.056 46.208 56.787  1.00 59.28  ? 753 HOH B O   1 
HETATM 8589 O O   . HOH H 5 .   ? -35.826 21.482 13.634  1.00 46.60  ? 754 HOH B O   1 
HETATM 8590 O O   . HOH H 5 .   ? -29.049 44.869 26.174  1.00 48.35  ? 755 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LYS A 2   ? 0.4368 0.5425 0.3486 0.0110  0.0134  -0.0081 2   LYS A N   
2    C CA  . LYS A 2   ? 0.4875 0.5950 0.4080 0.0113  0.0148  -0.0043 2   LYS A CA  
3    C C   . LYS A 2   ? 0.4080 0.5058 0.3351 0.0064  0.0117  -0.0045 2   LYS A C   
4    O O   . LYS A 2   ? 0.4413 0.5390 0.3722 0.0011  0.0088  -0.0020 2   LYS A O   
5    C CB  . LYS A 2   ? 0.5260 0.6483 0.4530 0.0104  0.0159  0.0037  2   LYS A CB  
6    C CG  . LYS A 2   ? 0.5265 0.6519 0.4614 0.0113  0.0174  0.0079  2   LYS A CG  
7    C CD  . LYS A 2   ? 0.6075 0.7479 0.5484 0.0104  0.0181  0.0162  2   LYS A CD  
8    C CE  . LYS A 2   ? 0.6590 0.8010 0.6071 0.0035  0.0143  0.0208  2   LYS A CE  
9    N NZ  . LYS A 2   ? 0.6441 0.8006 0.5986 0.0023  0.0145  0.0293  2   LYS A NZ  
10   N N   . LYS A 3   ? 0.3374 0.4273 0.2661 0.0083  0.0124  -0.0072 3   LYS A N   
11   C CA  . LYS A 3   ? 0.3162 0.3971 0.2508 0.0044  0.0099  -0.0074 3   LYS A CA  
12   C C   . LYS A 3   ? 0.3025 0.3872 0.2456 0.0039  0.0109  -0.0027 3   LYS A C   
13   O O   . LYS A 3   ? 0.2754 0.3675 0.2194 0.0074  0.0137  -0.0003 3   LYS A O   
14   C CB  . LYS A 3   ? 0.3079 0.3760 0.2381 0.0063  0.0093  -0.0140 3   LYS A CB  
15   C CG  . LYS A 3   ? 0.4724 0.5352 0.3931 0.0072  0.0080  -0.0193 3   LYS A CG  
16   C CD  . LYS A 3   ? 0.5732 0.6298 0.4950 0.0016  0.0040  -0.0197 3   LYS A CD  
17   C CE  . LYS A 3   ? 0.6589 0.7029 0.5748 0.0023  0.0019  -0.0260 3   LYS A CE  
18   N NZ  . LYS A 3   ? 0.7200 0.7583 0.6373 -0.0032 -0.0021 -0.0257 3   LYS A NZ  
19   N N   . LEU A 4   ? 0.2944 0.3742 0.2436 -0.0006 0.0084  -0.0012 4   LEU A N   
20   C CA  . LEU A 4   ? 0.2671 0.3467 0.2234 -0.0013 0.0087  0.0018  4   LEU A CA  
21   C C   . LEU A 4   ? 0.2405 0.3088 0.1964 -0.0004 0.0083  -0.0028 4   LEU A C   
22   O O   . LEU A 4   ? 0.3015 0.3618 0.2560 -0.0026 0.0060  -0.0058 4   LEU A O   
23   C CB  . LEU A 4   ? 0.2407 0.3224 0.2039 -0.0066 0.0062  0.0066  4   LEU A CB  
24   C CG  . LEU A 4   ? 0.3014 0.3824 0.2714 -0.0078 0.0060  0.0097  4   LEU A CG  
25   C CD1 . LEU A 4   ? 0.2710 0.3590 0.2468 -0.0116 0.0044  0.0160  4   LEU A CD1 
26   C CD2 . LEU A 4   ? 0.2676 0.3372 0.2390 -0.0095 0.0044  0.0065  4   LEU A CD2 
27   N N   . PHE A 5   ? 0.2370 0.3053 0.1944 0.0028  0.0105  -0.0030 5   PHE A N   
28   C CA  . PHE A 5   ? 0.2834 0.3418 0.2410 0.0039  0.0103  -0.0069 5   PHE A CA  
29   C C   . PHE A 5   ? 0.2652 0.3217 0.2302 0.0006  0.0090  -0.0039 5   PHE A C   
30   O O   . PHE A 5   ? 0.3075 0.3703 0.2770 0.0004  0.0100  0.0004  5   PHE A O   
31   C CB  . PHE A 5   ? 0.2561 0.3149 0.2109 0.0095  0.0134  -0.0092 5   PHE A CB  
32   C CG  . PHE A 5   ? 0.3107 0.3696 0.2569 0.0133  0.0147  -0.0132 5   PHE A CG  
33   C CD1 . PHE A 5   ? 0.3507 0.4019 0.2915 0.0121  0.0123  -0.0177 5   PHE A CD1 
34   C CD2 . PHE A 5   ? 0.3572 0.4241 0.3006 0.0182  0.0181  -0.0121 5   PHE A CD2 
35   C CE1 . PHE A 5   ? 0.3717 0.4225 0.3038 0.0155  0.0132  -0.0217 5   PHE A CE1 
36   C CE2 . PHE A 5   ? 0.4102 0.4770 0.3450 0.0220  0.0194  -0.0161 5   PHE A CE2 
37   C CZ  . PHE A 5   ? 0.3759 0.4343 0.3046 0.0206  0.0168  -0.0211 5   PHE A CZ  
38   N N   . LEU A 6   ? 0.2244 0.2724 0.1906 -0.0020 0.0066  -0.0061 6   LEU A N   
39   C CA  . LEU A 6   ? 0.1846 0.2300 0.1568 -0.0051 0.0052  -0.0038 6   LEU A CA  
40   C C   . LEU A 6   ? 0.2489 0.2867 0.2220 -0.0036 0.0053  -0.0068 6   LEU A C   
41   O O   . LEU A 6   ? 0.2628 0.2941 0.2326 -0.0026 0.0046  -0.0109 6   LEU A O   
42   C CB  . LEU A 6   ? 0.2360 0.2788 0.2094 -0.0094 0.0025  -0.0029 6   LEU A CB  
43   C CG  . LEU A 6   ? 0.1882 0.2282 0.1671 -0.0125 0.0009  -0.0005 6   LEU A CG  
44   C CD1 . LEU A 6   ? 0.3293 0.3753 0.3122 -0.0130 0.0017  0.0037  6   LEU A CD1 
45   C CD2 . LEU A 6   ? 0.2589 0.2975 0.2384 -0.0161 -0.0014 0.0006  6   LEU A CD2 
46   N N   . VAL A 7   ? 0.2148 0.2536 0.1926 -0.0037 0.0060  -0.0045 7   VAL A N   
47   C CA  . VAL A 7   ? 0.2566 0.2895 0.2361 -0.0022 0.0063  -0.0066 7   VAL A CA  
48   C C   . VAL A 7   ? 0.2369 0.2678 0.2215 -0.0055 0.0048  -0.0043 7   VAL A C   
49   O O   . VAL A 7   ? 0.2953 0.3307 0.2832 -0.0065 0.0052  -0.0007 7   VAL A O   
50   C CB  . VAL A 7   ? 0.2843 0.3209 0.2641 0.0018  0.0091  -0.0064 7   VAL A CB  
51   C CG1 . VAL A 7   ? 0.3020 0.3322 0.2836 0.0032  0.0092  -0.0088 7   VAL A CG1 
52   C CG2 . VAL A 7   ? 0.2781 0.3175 0.2522 0.0054  0.0110  -0.0084 7   VAL A CG2 
53   N N   . PHE A 8   ? 0.2241 0.2481 0.2091 -0.0071 0.0029  -0.0062 8   PHE A N   
54   C CA  . PHE A 8   ? 0.2291 0.2504 0.2183 -0.0095 0.0017  -0.0046 8   PHE A CA  
55   C C   . PHE A 8   ? 0.2319 0.2509 0.2233 -0.0075 0.0026  -0.0056 8   PHE A C   
56   O O   . PHE A 8   ? 0.2369 0.2524 0.2267 -0.0052 0.0029  -0.0086 8   PHE A O   
57   C CB  . PHE A 8   ? 0.2264 0.2424 0.2155 -0.0118 -0.0005 -0.0056 8   PHE A CB  
58   C CG  . PHE A 8   ? 0.2436 0.2619 0.2320 -0.0143 -0.0016 -0.0037 8   PHE A CG  
59   C CD1 . PHE A 8   ? 0.2589 0.2786 0.2503 -0.0167 -0.0023 -0.0007 8   PHE A CD1 
60   C CD2 . PHE A 8   ? 0.2861 0.3052 0.2710 -0.0144 -0.0021 -0.0049 8   PHE A CD2 
61   C CE1 . PHE A 8   ? 0.3209 0.3425 0.3121 -0.0190 -0.0035 0.0012  8   PHE A CE1 
62   C CE2 . PHE A 8   ? 0.2612 0.2829 0.2460 -0.0169 -0.0031 -0.0027 8   PHE A CE2 
63   C CZ  . PHE A 8   ? 0.2084 0.2315 0.1968 -0.0191 -0.0038 0.0004  8   PHE A CZ  
64   N N   . TRP A 9   ? 0.2114 0.2323 0.2065 -0.0084 0.0029  -0.0030 9   TRP A N   
65   C CA  . TRP A 9   ? 0.3041 0.3234 0.3020 -0.0070 0.0036  -0.0034 9   TRP A CA  
66   C C   . TRP A 9   ? 0.2506 0.2684 0.2516 -0.0096 0.0023  -0.0014 9   TRP A C   
67   O O   . TRP A 9   ? 0.1683 0.1896 0.1707 -0.0112 0.0023  0.0015  9   TRP A O   
68   C CB  . TRP A 9   ? 0.2901 0.3149 0.2888 -0.0046 0.0059  -0.0019 9   TRP A CB  
69   C CG  . TRP A 9   ? 0.2297 0.2529 0.2308 -0.0022 0.0071  -0.0027 9   TRP A CG  
70   C CD1 . TRP A 9   ? 0.1936 0.2117 0.1970 -0.0025 0.0060  -0.0041 9   TRP A CD1 
71   C CD2 . TRP A 9   ? 0.2138 0.2414 0.2161 0.0007  0.0095  -0.0015 9   TRP A CD2 
72   N NE1 . TRP A 9   ? 0.1830 0.2017 0.1889 0.0000  0.0075  -0.0040 9   TRP A NE1 
73   C CE2 . TRP A 9   ? 0.1785 0.2029 0.1838 0.0020  0.0098  -0.0024 9   TRP A CE2 
74   C CE3 . TRP A 9   ? 0.2357 0.2702 0.2372 0.0025  0.0116  0.0007  9   TRP A CE3 
75   C CZ2 . TRP A 9   ? 0.2494 0.2768 0.2568 0.0051  0.0121  -0.0015 9   TRP A CZ2 
76   C CZ3 . TRP A 9   ? 0.2371 0.2748 0.2405 0.0057  0.0140  0.0018  9   TRP A CZ3 
77   C CH2 . TRP A 9   ? 0.2884 0.3224 0.2949 0.0070  0.0143  0.0007  9   TRP A CH2 
78   N N   . TRP A 10  ? 0.2215 0.2340 0.2234 -0.0102 0.0011  -0.0030 10  TRP A N   
79   C CA  . TRP A 10  ? 0.1935 0.2041 0.1977 -0.0122 0.0000  -0.0016 10  TRP A CA  
80   C C   . TRP A 10  ? 0.2252 0.2360 0.2325 -0.0112 0.0006  -0.0010 10  TRP A C   
81   O O   . TRP A 10  ? 0.2420 0.2507 0.2505 -0.0095 0.0008  -0.0027 10  TRP A O   
82   C CB  . TRP A 10  ? 0.1585 0.1642 0.1622 -0.0130 -0.0016 -0.0029 10  TRP A CB  
83   C CG  . TRP A 10  ? 0.2007 0.2061 0.2016 -0.0141 -0.0024 -0.0033 10  TRP A CG  
84   C CD1 . TRP A 10  ? 0.2014 0.2049 0.2000 -0.0135 -0.0030 -0.0053 10  TRP A CD1 
85   C CD2 . TRP A 10  ? 0.1471 0.1541 0.1474 -0.0162 -0.0030 -0.0014 10  TRP A CD2 
86   N NE1 . TRP A 10  ? 0.2918 0.2962 0.2886 -0.0151 -0.0037 -0.0045 10  TRP A NE1 
87   C CE2 . TRP A 10  ? 0.2140 0.2206 0.2121 -0.0167 -0.0036 -0.0021 10  TRP A CE2 
88   C CE3 . TRP A 10  ? 0.1907 0.1991 0.1921 -0.0177 -0.0032 0.0008  10  TRP A CE3 
89   C CZ2 . TRP A 10  ? 0.2409 0.2488 0.2383 -0.0187 -0.0044 -0.0004 10  TRP A CZ2 
90   C CZ3 . TRP A 10  ? 0.2962 0.3051 0.2966 -0.0196 -0.0041 0.0022  10  TRP A CZ3 
91   C CH2 . TRP A 10  ? 0.2447 0.2537 0.2435 -0.0200 -0.0046 0.0017  10  TRP A CH2 
92   N N   . HIS A 11  ? 0.1820 0.1952 0.1909 -0.0126 0.0007  0.0014  11  HIS A N   
93   C CA  . HIS A 11  ? 0.1788 0.1932 0.1908 -0.0121 0.0013  0.0026  11  HIS A CA  
94   C C   . HIS A 11  ? 0.2358 0.2472 0.2492 -0.0133 0.0001  0.0027  11  HIS A C   
95   O O   . HIS A 11  ? 0.2621 0.2724 0.2740 -0.0152 -0.0010 0.0035  11  HIS A O   
96   C CB  . HIS A 11  ? 0.1733 0.1927 0.1862 -0.0130 0.0019  0.0055  11  HIS A CB  
97   C CG  . HIS A 11  ? 0.2374 0.2580 0.2533 -0.0135 0.0019  0.0074  11  HIS A CG  
98   N ND1 . HIS A 11  ? 0.2289 0.2502 0.2478 -0.0116 0.0030  0.0071  11  HIS A ND1 
99   C CD2 . HIS A 11  ? 0.2560 0.2773 0.2722 -0.0159 0.0008  0.0096  11  HIS A CD2 
100  C CE1 . HIS A 11  ? 0.2572 0.2802 0.2786 -0.0128 0.0028  0.0094  11  HIS A CE1 
101  N NE2 . HIS A 11  ? 0.2559 0.2788 0.2753 -0.0155 0.0014  0.0107  11  HIS A NE2 
102  N N   . MET A 12  ? 0.1975 0.2076 0.2136 -0.0121 0.0002  0.0021  12  MET A N   
103  C CA  . MET A 12  ? 0.2082 0.2163 0.2259 -0.0128 -0.0008 0.0025  12  MET A CA  
104  C C   . MET A 12  ? 0.2122 0.2228 0.2333 -0.0126 -0.0003 0.0042  12  MET A C   
105  O O   . MET A 12  ? 0.2549 0.2667 0.2787 -0.0110 0.0005  0.0041  12  MET A O   
106  C CB  . MET A 12  ? 0.1718 0.1763 0.1904 -0.0117 -0.0016 0.0009  12  MET A CB  
107  C CG  . MET A 12  ? 0.2356 0.2377 0.2511 -0.0117 -0.0022 -0.0008 12  MET A CG  
108  S SD  . MET A 12  ? 0.2479 0.2492 0.2604 -0.0137 -0.0029 -0.0001 12  MET A SD  
109  C CE  . MET A 12  ? 0.2461 0.2445 0.2567 -0.0136 -0.0039 -0.0018 12  MET A CE  
110  N N   . HIS A 13  ? 0.2020 0.2132 0.2229 -0.0142 -0.0008 0.0057  13  HIS A N   
111  C CA  . HIS A 13  ? 0.2288 0.2430 0.2525 -0.0146 -0.0005 0.0077  13  HIS A CA  
112  C C   . HIS A 13  ? 0.1642 0.1774 0.1869 -0.0158 -0.0014 0.0085  13  HIS A C   
113  O O   . HIS A 13  ? 0.2013 0.2122 0.2203 -0.0169 -0.0022 0.0080  13  HIS A O   
114  C CB  . HIS A 13  ? 0.2155 0.2334 0.2390 -0.0155 0.0001  0.0096  13  HIS A CB  
115  C CG  . HIS A 13  ? 0.2569 0.2778 0.2826 -0.0167 0.0000  0.0121  13  HIS A CG  
116  N ND1 . HIS A 13  ? 0.2132 0.2362 0.2435 -0.0156 0.0006  0.0131  13  HIS A ND1 
117  C CD2 . HIS A 13  ? 0.2036 0.2259 0.2277 -0.0190 -0.0009 0.0141  13  HIS A CD2 
118  C CE1 . HIS A 13  ? 0.2378 0.2638 0.2692 -0.0173 0.0003  0.0156  13  HIS A CE1 
119  N NE2 . HIS A 13  ? 0.2137 0.2391 0.2410 -0.0194 -0.0008 0.0162  13  HIS A NE2 
120  N N   . GLN A 14  ? 0.1738 0.1890 0.1998 -0.0156 -0.0014 0.0098  14  GLN A N   
121  C CA  . GLN A 14  ? 0.1318 0.1474 0.1567 -0.0167 -0.0020 0.0109  14  GLN A CA  
122  C C   . GLN A 14  ? 0.1630 0.1829 0.1915 -0.0172 -0.0017 0.0132  14  GLN A C   
123  O O   . GLN A 14  ? 0.2132 0.2351 0.2466 -0.0159 -0.0010 0.0138  14  GLN A O   
124  C CB  . GLN A 14  ? 0.1279 0.1418 0.1532 -0.0156 -0.0024 0.0105  14  GLN A CB  
125  C CG  . GLN A 14  ? 0.1508 0.1607 0.1729 -0.0152 -0.0027 0.0088  14  GLN A CG  
126  C CD  . GLN A 14  ? 0.2092 0.2168 0.2259 -0.0164 -0.0032 0.0083  14  GLN A CD  
127  O OE1 . GLN A 14  ? 0.1960 0.2043 0.2109 -0.0175 -0.0035 0.0091  14  GLN A OE1 
128  N NE2 . GLN A 14  ? 0.1940 0.1986 0.2083 -0.0164 -0.0034 0.0069  14  GLN A NE2 
129  N N   . PRO A 15  ? 0.1995 0.2208 0.2260 -0.0191 -0.0023 0.0147  15  PRO A N   
130  C CA  . PRO A 15  ? 0.2244 0.2502 0.2546 -0.0199 -0.0022 0.0173  15  PRO A CA  
131  C C   . PRO A 15  ? 0.1862 0.2131 0.2194 -0.0187 -0.0022 0.0178  15  PRO A C   
132  O O   . PRO A 15  ? 0.2052 0.2294 0.2368 -0.0176 -0.0024 0.0163  15  PRO A O   
133  C CB  . PRO A 15  ? 0.1484 0.1742 0.1743 -0.0225 -0.0034 0.0185  15  PRO A CB  
134  C CG  . PRO A 15  ? 0.2152 0.2357 0.2351 -0.0226 -0.0043 0.0160  15  PRO A CG  
135  C CD  . PRO A 15  ? 0.2083 0.2267 0.2289 -0.0208 -0.0035 0.0141  15  PRO A CD  
136  N N   . LEU A 16  ? 0.1590 0.1905 0.1970 -0.0191 -0.0019 0.0203  16  LEU A N   
137  C CA  . LEU A 16  ? 0.2364 0.2701 0.2782 -0.0181 -0.0020 0.0214  16  LEU A CA  
138  C C   . LEU A 16  ? 0.2809 0.3146 0.3183 -0.0190 -0.0027 0.0217  16  LEU A C   
139  O O   . LEU A 16  ? 0.2361 0.2719 0.2715 -0.0209 -0.0032 0.0231  16  LEU A O   
140  C CB  . LEU A 16  ? 0.1867 0.2256 0.2354 -0.0182 -0.0016 0.0244  16  LEU A CB  
141  C CG  . LEU A 16  ? 0.2299 0.2720 0.2839 -0.0174 -0.0019 0.0262  16  LEU A CG  
142  C CD1 . LEU A 16  ? 0.2460 0.2850 0.3020 -0.0152 -0.0022 0.0246  16  LEU A CD1 
143  C CD2 . LEU A 16  ? 0.2287 0.2761 0.2900 -0.0177 -0.0016 0.0294  16  LEU A CD2 
144  N N   . TYR A 17  ? 0.2546 0.2860 0.2902 -0.0175 -0.0028 0.0204  17  TYR A N   
145  C CA  . TYR A 17  ? 0.2044 0.2355 0.2352 -0.0175 -0.0031 0.0203  17  TYR A CA  
146  C C   . TYR A 17  ? 0.2787 0.3153 0.3137 -0.0170 -0.0031 0.0230  17  TYR A C   
147  O O   . TYR A 17  ? 0.2951 0.3322 0.3261 -0.0166 -0.0031 0.0232  17  TYR A O   
148  C CB  . TYR A 17  ? 0.2214 0.2479 0.2482 -0.0159 -0.0030 0.0181  17  TYR A CB  
149  C CG  . TYR A 17  ? 0.1946 0.2159 0.2166 -0.0166 -0.0032 0.0157  17  TYR A CG  
150  C CD1 . TYR A 17  ? 0.2131 0.2321 0.2292 -0.0185 -0.0040 0.0149  17  TYR A CD1 
151  C CD2 . TYR A 17  ? 0.1730 0.1917 0.1963 -0.0157 -0.0030 0.0143  17  TYR A CD2 
152  C CE1 . TYR A 17  ? 0.2105 0.2250 0.2228 -0.0193 -0.0045 0.0131  17  TYR A CE1 
153  C CE2 . TYR A 17  ? 0.2333 0.2482 0.2527 -0.0165 -0.0032 0.0125  17  TYR A CE2 
154  C CZ  . TYR A 17  ? 0.2119 0.2249 0.2261 -0.0182 -0.0040 0.0120  17  TYR A CZ  
155  O OH  . TYR A 17  ? 0.2792 0.2887 0.2902 -0.0191 -0.0045 0.0106  17  TYR A OH  
156  N N   . ARG A 18  ? 0.2618 0.3023 0.3044 -0.0167 -0.0030 0.0251  18  ARG A N   
157  C CA  . ARG A 18  ? 0.2653 0.3115 0.3134 -0.0161 -0.0031 0.0281  18  ARG A CA  
158  C C   . ARG A 18  ? 0.2536 0.3047 0.3023 -0.0180 -0.0033 0.0305  18  ARG A C   
159  O O   . ARG A 18  ? 0.2680 0.3209 0.3202 -0.0194 -0.0032 0.0317  18  ARG A O   
160  C CB  . ARG A 18  ? 0.2998 0.3471 0.3561 -0.0150 -0.0033 0.0293  18  ARG A CB  
161  C CG  . ARG A 18  ? 0.3238 0.3772 0.3871 -0.0143 -0.0038 0.0330  18  ARG A CG  
162  C CD  . ARG A 18  ? 0.3983 0.4517 0.4697 -0.0137 -0.0043 0.0339  18  ARG A CD  
163  N NE  . ARG A 18  ? 0.3906 0.4486 0.4692 -0.0130 -0.0053 0.0374  18  ARG A NE  
164  C CZ  . ARG A 18  ? 0.3890 0.4535 0.4736 -0.0137 -0.0056 0.0410  18  ARG A CZ  
165  N NH1 . ARG A 18  ? 0.3948 0.4618 0.4788 -0.0153 -0.0049 0.0416  18  ARG A NH1 
166  N NH2 . ARG A 18  ? 0.3934 0.4624 0.4850 -0.0131 -0.0067 0.0445  18  ARG A NH2 
167  N N   . GLU A 19  ? 0.2219 0.2754 0.2671 -0.0181 -0.0034 0.0314  19  GLU A N   
168  C CA  . GLU A 19  ? 0.2023 0.2607 0.2475 -0.0202 -0.0039 0.0338  19  GLU A CA  
169  C C   . GLU A 19  ? 0.2592 0.3246 0.3144 -0.0204 -0.0039 0.0377  19  GLU A C   
170  O O   . GLU A 19  ? 0.2423 0.3106 0.3027 -0.0186 -0.0038 0.0393  19  GLU A O   
171  C CB  . GLU A 19  ? 0.2753 0.3345 0.3139 -0.0197 -0.0040 0.0335  19  GLU A CB  
172  C CG  . GLU A 19  ? 0.4122 0.4723 0.4453 -0.0225 -0.0049 0.0339  19  GLU A CG  
173  C CD  . GLU A 19  ? 0.5143 0.5829 0.5527 -0.0236 -0.0052 0.0381  19  GLU A CD  
174  O OE1 . GLU A 19  ? 0.4836 0.5574 0.5293 -0.0220 -0.0046 0.0405  19  GLU A OE1 
175  O OE2 . GLU A 19  ? 0.5717 0.6421 0.6074 -0.0264 -0.0061 0.0392  19  GLU A OE2 
176  N N   . PRO A 20  ? 0.2922 0.3605 0.3509 -0.0225 -0.0040 0.0398  20  PRO A N   
177  C CA  . PRO A 20  ? 0.3606 0.4346 0.4298 -0.0224 -0.0039 0.0433  20  PRO A CA  
178  C C   . PRO A 20  ? 0.3620 0.4435 0.4355 -0.0225 -0.0043 0.0471  20  PRO A C   
179  O O   . PRO A 20  ? 0.3423 0.4279 0.4250 -0.0218 -0.0045 0.0500  20  PRO A O   
180  C CB  . PRO A 20  ? 0.3609 0.4363 0.4315 -0.0247 -0.0038 0.0448  20  PRO A CB  
181  C CG  . PRO A 20  ? 0.2663 0.3392 0.3274 -0.0268 -0.0045 0.0433  20  PRO A CG  
182  C CD  . PRO A 20  ? 0.2708 0.3373 0.3245 -0.0251 -0.0044 0.0392  20  PRO A CD  
183  N N   . TYR A 21  ? 0.2810 0.3643 0.3482 -0.0232 -0.0046 0.0472  21  TYR A N   
184  C CA  . TYR A 21  ? 0.2779 0.3694 0.3493 -0.0232 -0.0049 0.0511  21  TYR A CA  
185  C C   . TYR A 21  ? 0.3414 0.4337 0.4129 -0.0203 -0.0046 0.0511  21  TYR A C   
186  O O   . TYR A 21  ? 0.3613 0.4599 0.4411 -0.0195 -0.0050 0.0548  21  TYR A O   
187  C CB  . TYR A 21  ? 0.2911 0.3852 0.3558 -0.0255 -0.0054 0.0517  21  TYR A CB  
188  C CG  . TYR A 21  ? 0.4066 0.5019 0.4728 -0.0287 -0.0059 0.0533  21  TYR A CG  
189  C CD1 . TYR A 21  ? 0.4287 0.5317 0.5045 -0.0302 -0.0061 0.0581  21  TYR A CD1 
190  C CD2 . TYR A 21  ? 0.4108 0.4999 0.4694 -0.0304 -0.0064 0.0505  21  TYR A CD2 
191  C CE1 . TYR A 21  ? 0.4115 0.5161 0.4891 -0.0331 -0.0064 0.0601  21  TYR A CE1 
192  C CE2 . TYR A 21  ? 0.3712 0.4621 0.4317 -0.0335 -0.0069 0.0527  21  TYR A CE2 
193  C CZ  . TYR A 21  ? 0.4085 0.5072 0.4784 -0.0347 -0.0068 0.0575  21  TYR A CZ  
194  O OH  . TYR A 21  ? 0.4494 0.5505 0.5217 -0.0376 -0.0073 0.0603  21  TYR A OH  
195  N N   . THR A 22  ? 0.3406 0.4269 0.4034 -0.0187 -0.0042 0.0473  22  THR A N   
196  C CA  . THR A 22  ? 0.3271 0.4142 0.3898 -0.0158 -0.0037 0.0476  22  THR A CA  
197  C C   . THR A 22  ? 0.3373 0.4203 0.4047 -0.0142 -0.0039 0.0467  22  THR A C   
198  O O   . THR A 22  ? 0.2468 0.3321 0.3177 -0.0122 -0.0040 0.0485  22  THR A O   
199  C CB  . THR A 22  ? 0.3453 0.4281 0.3964 -0.0145 -0.0030 0.0443  22  THR A CB  
200  O OG1 . THR A 22  ? 0.2800 0.3537 0.3252 -0.0148 -0.0030 0.0398  22  THR A OG1 
201  C CG2 . THR A 22  ? 0.2926 0.3784 0.3378 -0.0161 -0.0033 0.0447  22  THR A CG2 
202  N N   . GLY A 23  ? 0.2660 0.3431 0.3334 -0.0152 -0.0040 0.0441  23  GLY A N   
203  C CA  . GLY A 23  ? 0.2809 0.3530 0.3510 -0.0138 -0.0042 0.0425  23  GLY A CA  
204  C C   . GLY A 23  ? 0.3545 0.4209 0.4172 -0.0122 -0.0037 0.0393  23  GLY A C   
205  O O   . GLY A 23  ? 0.4397 0.5026 0.5045 -0.0110 -0.0041 0.0385  23  GLY A O   
206  N N   . GLU A 24  ? 0.2675 0.3326 0.3216 -0.0120 -0.0030 0.0376  24  GLU A N   
207  C CA  . GLU A 24  ? 0.2301 0.2897 0.2771 -0.0102 -0.0023 0.0348  24  GLU A CA  
208  C C   . GLU A 24  ? 0.3097 0.3615 0.3518 -0.0113 -0.0024 0.0308  24  GLU A C   
209  O O   . GLU A 24  ? 0.2648 0.3154 0.3045 -0.0135 -0.0027 0.0297  24  GLU A O   
210  C CB  . GLU A 24  ? 0.2648 0.3258 0.3043 -0.0092 -0.0016 0.0344  24  GLU A CB  
211  C CG  . GLU A 24  ? 0.3661 0.4358 0.4098 -0.0080 -0.0014 0.0387  24  GLU A CG  
212  C CD  . GLU A 24  ? 0.5918 0.6625 0.6269 -0.0064 -0.0004 0.0380  24  GLU A CD  
213  O OE1 . GLU A 24  ? 0.5890 0.6545 0.6154 -0.0075 -0.0005 0.0346  24  GLU A OE1 
214  O OE2 . GLU A 24  ? 0.7286 0.8051 0.7654 -0.0039 0.0003  0.0408  24  GLU A OE2 
215  N N   . TYR A 25  ? 0.2577 0.3049 0.2987 -0.0099 -0.0022 0.0290  25  TYR A N   
216  C CA  . TYR A 25  ? 0.2510 0.2910 0.2864 -0.0107 -0.0022 0.0253  25  TYR A CA  
217  C C   . TYR A 25  ? 0.2370 0.2738 0.2633 -0.0103 -0.0017 0.0232  25  TYR A C   
218  O O   . TYR A 25  ? 0.2555 0.2916 0.2790 -0.0079 -0.0010 0.0231  25  TYR A O   
219  C CB  . TYR A 25  ? 0.2337 0.2702 0.2713 -0.0096 -0.0023 0.0244  25  TYR A CB  
220  C CG  . TYR A 25  ? 0.2508 0.2876 0.2950 -0.0105 -0.0030 0.0248  25  TYR A CG  
221  C CD1 . TYR A 25  ? 0.2987 0.3403 0.3509 -0.0102 -0.0037 0.0279  25  TYR A CD1 
222  C CD2 . TYR A 25  ? 0.3081 0.3403 0.3505 -0.0114 -0.0031 0.0222  25  TYR A CD2 
223  C CE1 . TYR A 25  ? 0.2613 0.3022 0.3191 -0.0107 -0.0044 0.0280  25  TYR A CE1 
224  C CE2 . TYR A 25  ? 0.2994 0.3316 0.3471 -0.0117 -0.0035 0.0223  25  TYR A CE2 
225  C CZ  . TYR A 25  ? 0.3107 0.3468 0.3659 -0.0112 -0.0042 0.0250  25  TYR A CZ  
226  O OH  . TYR A 25  ? 0.3598 0.3949 0.4199 -0.0112 -0.0047 0.0248  25  TYR A OH  
227  N N   . LEU A 26  ? 0.2198 0.2545 0.2414 -0.0124 -0.0022 0.0218  26  LEU A N   
228  C CA  . LEU A 26  ? 0.2170 0.2484 0.2297 -0.0124 -0.0024 0.0199  26  LEU A CA  
229  C C   . LEU A 26  ? 0.2220 0.2459 0.2287 -0.0118 -0.0024 0.0166  26  LEU A C   
230  O O   . LEU A 26  ? 0.2823 0.3025 0.2815 -0.0109 -0.0023 0.0148  26  LEU A O   
231  C CB  . LEU A 26  ? 0.2481 0.2803 0.2584 -0.0155 -0.0035 0.0201  26  LEU A CB  
232  C CG  . LEU A 26  ? 0.2622 0.3021 0.2776 -0.0164 -0.0036 0.0235  26  LEU A CG  
233  C CD1 . LEU A 26  ? 0.2871 0.3272 0.2980 -0.0194 -0.0049 0.0237  26  LEU A CD1 
234  C CD2 . LEU A 26  ? 0.2899 0.3345 0.3064 -0.0137 -0.0027 0.0253  26  LEU A CD2 
235  N N   . LEU A 27  ? 0.2007 0.2222 0.2103 -0.0123 -0.0024 0.0158  27  LEU A N   
236  C CA  . LEU A 27  ? 0.1908 0.2060 0.1962 -0.0116 -0.0024 0.0134  27  LEU A CA  
237  C C   . LEU A 27  ? 0.2067 0.2226 0.2177 -0.0103 -0.0018 0.0141  27  LEU A C   
238  O O   . LEU A 27  ? 0.2581 0.2778 0.2757 -0.0107 -0.0020 0.0158  27  LEU A O   
239  C CB  . LEU A 27  ? 0.1744 0.1855 0.1767 -0.0143 -0.0036 0.0117  27  LEU A CB  
240  C CG  . LEU A 27  ? 0.2561 0.2652 0.2522 -0.0163 -0.0049 0.0109  27  LEU A CG  
241  C CD1 . LEU A 27  ? 0.2758 0.2828 0.2714 -0.0193 -0.0063 0.0106  27  LEU A CD1 
242  C CD2 . LEU A 27  ? 0.2911 0.2948 0.2794 -0.0146 -0.0049 0.0088  27  LEU A CD2 
243  N N   . PRO A 28  ? 0.2493 0.2614 0.2579 -0.0087 -0.0014 0.0129  28  PRO A N   
244  C CA  . PRO A 28  ? 0.2859 0.2987 0.2995 -0.0076 -0.0012 0.0139  28  PRO A CA  
245  C C   . PRO A 28  ? 0.2811 0.2903 0.2950 -0.0090 -0.0017 0.0122  28  PRO A C   
246  O O   . PRO A 28  ? 0.2711 0.2795 0.2873 -0.0082 -0.0017 0.0126  28  PRO A O   
247  C CB  . PRO A 28  ? 0.2566 0.2679 0.2670 -0.0050 -0.0002 0.0141  28  PRO A CB  
248  C CG  . PRO A 28  ? 0.3251 0.3313 0.3275 -0.0053 -0.0002 0.0115  28  PRO A CG  
249  C CD  . PRO A 28  ? 0.3005 0.3080 0.3017 -0.0076 -0.0011 0.0111  28  PRO A CD  
250  N N   . TRP A 29  ? 0.1765 0.1840 0.1881 -0.0111 -0.0023 0.0108  29  TRP A N   
251  C CA  . TRP A 29  ? 0.2149 0.2192 0.2256 -0.0122 -0.0027 0.0092  29  TRP A CA  
252  C C   . TRP A 29  ? 0.2180 0.2239 0.2341 -0.0122 -0.0028 0.0097  29  TRP A C   
253  O O   . TRP A 29  ? 0.2624 0.2659 0.2781 -0.0122 -0.0030 0.0087  29  TRP A O   
254  C CB  . TRP A 29  ? 0.2276 0.2307 0.2353 -0.0145 -0.0034 0.0083  29  TRP A CB  
255  C CG  . TRP A 29  ? 0.3234 0.3233 0.3248 -0.0149 -0.0040 0.0074  29  TRP A CG  
256  C CD1 . TRP A 29  ? 0.3125 0.3129 0.3113 -0.0166 -0.0048 0.0077  29  TRP A CD1 
257  C CD2 . TRP A 29  ? 0.3077 0.3027 0.3043 -0.0139 -0.0040 0.0061  29  TRP A CD2 
258  N NE1 . TRP A 29  ? 0.3359 0.3315 0.3282 -0.0166 -0.0056 0.0063  29  TRP A NE1 
259  C CE2 . TRP A 29  ? 0.3109 0.3031 0.3019 -0.0148 -0.0050 0.0052  29  TRP A CE2 
260  C CE3 . TRP A 29  ? 0.2724 0.2652 0.2691 -0.0123 -0.0034 0.0056  29  TRP A CE3 
261  C CZ2 . TRP A 29  ? 0.3161 0.3027 0.3013 -0.0138 -0.0052 0.0036  29  TRP A CZ2 
262  C CZ3 . TRP A 29  ? 0.2499 0.2380 0.2415 -0.0113 -0.0034 0.0044  29  TRP A CZ3 
263  C CH2 . TRP A 29  ? 0.2892 0.2740 0.2751 -0.0119 -0.0043 0.0033  29  TRP A CH2 
264  N N   . THR A 30  ? 0.1740 0.1837 0.1949 -0.0121 -0.0028 0.0111  30  THR A N   
265  C CA  . THR A 30  ? 0.1550 0.1652 0.1807 -0.0118 -0.0031 0.0112  30  THR A CA  
266  C C   . THR A 30  ? 0.2268 0.2360 0.2541 -0.0105 -0.0035 0.0119  30  THR A C   
267  O O   . THR A 30  ? 0.2742 0.2810 0.3019 -0.0106 -0.0041 0.0110  30  THR A O   
268  C CB  . THR A 30  ? 0.1905 0.2046 0.2214 -0.0118 -0.0032 0.0128  30  THR A CB  
269  O OG1 . THR A 30  ? 0.2151 0.2304 0.2451 -0.0131 -0.0029 0.0125  30  THR A OG1 
270  C CG2 . THR A 30  ? 0.2440 0.2577 0.2797 -0.0112 -0.0039 0.0128  30  THR A CG2 
271  N N   . PHE A 31  ? 0.2639 0.2749 0.2917 -0.0093 -0.0033 0.0138  31  PHE A N   
272  C CA  . PHE A 31  ? 0.2330 0.2437 0.2625 -0.0080 -0.0036 0.0153  31  PHE A CA  
273  C C   . PHE A 31  ? 0.2037 0.2102 0.2291 -0.0081 -0.0035 0.0137  31  PHE A C   
274  O O   . PHE A 31  ? 0.2648 0.2699 0.2919 -0.0083 -0.0043 0.0139  31  PHE A O   
275  C CB  . PHE A 31  ? 0.1940 0.2081 0.2240 -0.0063 -0.0029 0.0178  31  PHE A CB  
276  C CG  . PHE A 31  ? 0.1819 0.1965 0.2137 -0.0048 -0.0031 0.0200  31  PHE A CG  
277  C CD1 . PHE A 31  ? 0.2041 0.2211 0.2422 -0.0047 -0.0044 0.0228  31  PHE A CD1 
278  C CD2 . PHE A 31  ? 0.2798 0.2923 0.3071 -0.0035 -0.0020 0.0198  31  PHE A CD2 
279  C CE1 . PHE A 31  ? 0.2663 0.2842 0.3063 -0.0036 -0.0048 0.0255  31  PHE A CE1 
280  C CE2 . PHE A 31  ? 0.3093 0.3228 0.3386 -0.0020 -0.0020 0.0224  31  PHE A CE2 
281  C CZ  . PHE A 31  ? 0.2600 0.2765 0.2958 -0.0021 -0.0034 0.0255  31  PHE A CZ  
282  N N   . PHE A 32  ? 0.2701 0.2745 0.2901 -0.0082 -0.0026 0.0123  32  PHE A N   
283  C CA  . PHE A 32  ? 0.2230 0.2238 0.2396 -0.0081 -0.0025 0.0113  32  PHE A CA  
284  C C   . PHE A 32  ? 0.2258 0.2244 0.2421 -0.0098 -0.0032 0.0096  32  PHE A C   
285  O O   . PHE A 32  ? 0.2332 0.2301 0.2496 -0.0099 -0.0036 0.0096  32  PHE A O   
286  C CB  . PHE A 32  ? 0.2739 0.2722 0.2847 -0.0077 -0.0018 0.0101  32  PHE A CB  
287  C CG  . PHE A 32  ? 0.3130 0.3126 0.3228 -0.0052 -0.0007 0.0116  32  PHE A CG  
288  C CD1 . PHE A 32  ? 0.3069 0.3073 0.3189 -0.0034 -0.0002 0.0137  32  PHE A CD1 
289  C CD2 . PHE A 32  ? 0.3026 0.3027 0.3091 -0.0046 -0.0002 0.0112  32  PHE A CD2 
290  C CE1 . PHE A 32  ? 0.2309 0.2331 0.2420 -0.0007 0.0010  0.0155  32  PHE A CE1 
291  C CE2 . PHE A 32  ? 0.3125 0.3140 0.3175 -0.0019 0.0009  0.0125  32  PHE A CE2 
292  C CZ  . PHE A 32  ? 0.2682 0.2710 0.2756 0.0003  0.0017  0.0147  32  PHE A CZ  
293  N N   . HIS A 33  ? 0.1896 0.1888 0.2058 -0.0111 -0.0034 0.0083  33  HIS A N   
294  C CA  . HIS A 33  ? 0.2280 0.2259 0.2440 -0.0123 -0.0039 0.0069  33  HIS A CA  
295  C C   . HIS A 33  ? 0.2338 0.2322 0.2537 -0.0120 -0.0046 0.0072  33  HIS A C   
296  O O   . HIS A 33  ? 0.2356 0.2324 0.2548 -0.0125 -0.0052 0.0061  33  HIS A O   
297  C CB  . HIS A 33  ? 0.1544 0.1531 0.1690 -0.0136 -0.0037 0.0059  33  HIS A CB  
298  C CG  . HIS A 33  ? 0.1911 0.1879 0.2012 -0.0145 -0.0038 0.0053  33  HIS A CG  
299  N ND1 . HIS A 33  ? 0.2606 0.2549 0.2682 -0.0151 -0.0041 0.0046  33  HIS A ND1 
300  C CD2 . HIS A 33  ? 0.2178 0.2144 0.2253 -0.0151 -0.0038 0.0055  33  HIS A CD2 
301  C CE1 . HIS A 33  ? 0.2055 0.1979 0.2095 -0.0160 -0.0044 0.0044  33  HIS A CE1 
302  N NE2 . HIS A 33  ? 0.1992 0.1927 0.2028 -0.0160 -0.0044 0.0048  33  HIS A NE2 
303  N N   . ALA A 34  ? 0.1922 0.1927 0.2162 -0.0112 -0.0049 0.0087  34  ALA A N   
304  C CA  . ALA A 34  ? 0.2423 0.2425 0.2701 -0.0110 -0.0062 0.0092  34  ALA A CA  
305  C C   . ALA A 34  ? 0.2115 0.2101 0.2393 -0.0109 -0.0071 0.0104  34  ALA A C   
306  O O   . ALA A 34  ? 0.2306 0.2271 0.2585 -0.0115 -0.0083 0.0097  34  ALA A O   
307  C CB  . ALA A 34  ? 0.2029 0.2060 0.2357 -0.0103 -0.0067 0.0111  34  ALA A CB  
308  N N   . VAL A 35  ? 0.2121 0.2118 0.2396 -0.0100 -0.0065 0.0124  35  VAL A N   
309  C CA  . VAL A 35  ? 0.2459 0.2448 0.2741 -0.0098 -0.0072 0.0143  35  VAL A CA  
310  C C   . VAL A 35  ? 0.3001 0.2961 0.3243 -0.0106 -0.0069 0.0127  35  VAL A C   
311  O O   . VAL A 35  ? 0.2973 0.2922 0.3223 -0.0112 -0.0080 0.0137  35  VAL A O   
312  C CB  . VAL A 35  ? 0.1702 0.1718 0.1997 -0.0080 -0.0063 0.0173  35  VAL A CB  
313  C CG1 . VAL A 35  ? 0.2172 0.2225 0.2509 -0.0072 -0.0066 0.0193  35  VAL A CG1 
314  C CG2 . VAL A 35  ? 0.2312 0.2317 0.2556 -0.0071 -0.0044 0.0162  35  VAL A CG2 
315  N N   . LYS A 36  ? 0.2503 0.2453 0.2707 -0.0110 -0.0058 0.0105  36  LYS A N   
316  C CA  . LYS A 36  ? 0.2305 0.2232 0.2475 -0.0119 -0.0057 0.0095  36  LYS A CA  
317  C C   . LYS A 36  ? 0.2520 0.2439 0.2679 -0.0134 -0.0064 0.0073  36  LYS A C   
318  O O   . LYS A 36  ? 0.2168 0.2074 0.2318 -0.0143 -0.0070 0.0073  36  LYS A O   
319  C CB  . LYS A 36  ? 0.2547 0.2464 0.2680 -0.0116 -0.0045 0.0087  36  LYS A CB  
320  C CG  . LYS A 36  ? 0.2082 0.1975 0.2185 -0.0125 -0.0045 0.0080  36  LYS A CG  
321  C CD  . LYS A 36  ? 0.2050 0.1923 0.2116 -0.0121 -0.0038 0.0074  36  LYS A CD  
322  C CE  . LYS A 36  ? 0.2194 0.2066 0.2239 -0.0137 -0.0041 0.0057  36  LYS A CE  
323  N NZ  . LYS A 36  ? 0.1935 0.1807 0.1976 -0.0155 -0.0049 0.0050  36  LYS A NZ  
324  N N   . ASP A 37  ? 0.2587 0.2515 0.2746 -0.0136 -0.0061 0.0058  37  ASP A N   
325  C CA  . ASP A 37  ? 0.2664 0.2591 0.2806 -0.0145 -0.0062 0.0039  37  ASP A CA  
326  C C   . ASP A 37  ? 0.1893 0.1822 0.2053 -0.0141 -0.0068 0.0028  37  ASP A C   
327  O O   . ASP A 37  ? 0.2454 0.2373 0.2599 -0.0145 -0.0073 0.0013  37  ASP A O   
328  C CB  . ASP A 37  ? 0.2362 0.2298 0.2480 -0.0150 -0.0053 0.0032  37  ASP A CB  
329  C CG  . ASP A 37  ? 0.2472 0.2396 0.2569 -0.0153 -0.0050 0.0040  37  ASP A CG  
330  O OD1 . ASP A 37  ? 0.2356 0.2265 0.2439 -0.0158 -0.0053 0.0043  37  ASP A OD1 
331  O OD2 . ASP A 37  ? 0.2750 0.2678 0.2844 -0.0148 -0.0046 0.0044  37  ASP A OD2 
332  N N   . TYR A 38  ? 0.1672 0.1612 0.1863 -0.0133 -0.0067 0.0034  38  TYR A N   
333  C CA  . TYR A 38  ? 0.1389 0.1330 0.1597 -0.0127 -0.0070 0.0021  38  TYR A CA  
334  C C   . TYR A 38  ? 0.2003 0.1917 0.2221 -0.0127 -0.0089 0.0016  38  TYR A C   
335  O O   . TYR A 38  ? 0.2055 0.1955 0.2264 -0.0122 -0.0092 -0.0004 38  TYR A O   
336  C CB  . TYR A 38  ? 0.2090 0.2053 0.2332 -0.0119 -0.0066 0.0033  38  TYR A CB  
337  C CG  . TYR A 38  ? 0.2434 0.2421 0.2662 -0.0122 -0.0051 0.0034  38  TYR A CG  
338  C CD1 . TYR A 38  ? 0.2406 0.2396 0.2601 -0.0129 -0.0043 0.0023  38  TYR A CD1 
339  C CD2 . TYR A 38  ? 0.2307 0.2318 0.2555 -0.0121 -0.0047 0.0051  38  TYR A CD2 
340  C CE1 . TYR A 38  ? 0.3028 0.3039 0.3212 -0.0135 -0.0035 0.0029  38  TYR A CE1 
341  C CE2 . TYR A 38  ? 0.2393 0.2422 0.2624 -0.0127 -0.0038 0.0054  38  TYR A CE2 
342  C CZ  . TYR A 38  ? 0.2298 0.2325 0.2499 -0.0136 -0.0033 0.0044  38  TYR A CZ  
343  O OH  . TYR A 38  ? 0.2748 0.2793 0.2935 -0.0146 -0.0029 0.0051  38  TYR A OH  
344  N N   . TYR A 39  ? 0.2015 0.1921 0.2250 -0.0131 -0.0102 0.0035  39  TYR A N   
345  C CA  . TYR A 39  ? 0.1624 0.1501 0.1861 -0.0137 -0.0124 0.0033  39  TYR A CA  
346  C C   . TYR A 39  ? 0.2092 0.1955 0.2287 -0.0148 -0.0125 0.0023  39  TYR A C   
347  O O   . TYR A 39  ? 0.1974 0.1813 0.2148 -0.0151 -0.0137 0.0003  39  TYR A O   
348  C CB  . TYR A 39  ? 0.2097 0.1978 0.2375 -0.0138 -0.0139 0.0067  39  TYR A CB  
349  C CG  . TYR A 39  ? 0.2389 0.2239 0.2671 -0.0150 -0.0168 0.0072  39  TYR A CG  
350  C CD1 . TYR A 39  ? 0.2129 0.1952 0.2430 -0.0150 -0.0190 0.0062  39  TYR A CD1 
351  C CD2 . TYR A 39  ? 0.2694 0.2540 0.2964 -0.0161 -0.0175 0.0087  39  TYR A CD2 
352  C CE1 . TYR A 39  ? 0.2740 0.2529 0.3041 -0.0163 -0.0221 0.0066  39  TYR A CE1 
353  C CE2 . TYR A 39  ? 0.3093 0.2911 0.3366 -0.0176 -0.0204 0.0095  39  TYR A CE2 
354  C CZ  . TYR A 39  ? 0.3243 0.3030 0.3529 -0.0177 -0.0229 0.0084  39  TYR A CZ  
355  O OH  . TYR A 39  ? 0.4163 0.3917 0.4449 -0.0194 -0.0263 0.0091  39  TYR A OH  
356  N N   . ASP A 40  ? 0.1746 0.1623 0.1926 -0.0152 -0.0113 0.0034  40  ASP A N   
357  C CA  . ASP A 40  ? 0.1985 0.1853 0.2140 -0.0165 -0.0118 0.0035  40  ASP A CA  
358  C C   . ASP A 40  ? 0.1907 0.1777 0.2023 -0.0169 -0.0111 0.0009  40  ASP A C   
359  O O   . ASP A 40  ? 0.2391 0.2250 0.2485 -0.0179 -0.0122 0.0003  40  ASP A O   
360  C CB  . ASP A 40  ? 0.2604 0.2483 0.2762 -0.0165 -0.0109 0.0059  40  ASP A CB  
361  C CG  . ASP A 40  ? 0.3256 0.3136 0.3450 -0.0163 -0.0120 0.0091  40  ASP A CG  
362  O OD1 . ASP A 40  ? 0.2712 0.2580 0.2909 -0.0175 -0.0137 0.0103  40  ASP A OD1 
363  O OD2 . ASP A 40  ? 0.2837 0.2732 0.3055 -0.0150 -0.0113 0.0108  40  ASP A OD2 
364  N N   . MET A 41  ? 0.2020 0.1907 0.2127 -0.0161 -0.0095 -0.0003 41  MET A N   
365  C CA  . MET A 41  ? 0.1974 0.1872 0.2048 -0.0163 -0.0087 -0.0021 41  MET A CA  
366  C C   . MET A 41  ? 0.2407 0.2287 0.2465 -0.0157 -0.0097 -0.0044 41  MET A C   
367  O O   . MET A 41  ? 0.2173 0.2050 0.2201 -0.0165 -0.0103 -0.0052 41  MET A O   
368  C CB  . MET A 41  ? 0.1380 0.1305 0.1454 -0.0156 -0.0070 -0.0023 41  MET A CB  
369  C CG  . MET A 41  ? 0.1827 0.1764 0.1898 -0.0166 -0.0064 -0.0006 41  MET A CG  
370  S SD  . MET A 41  ? 0.2039 0.1985 0.2080 -0.0181 -0.0066 -0.0003 41  MET A SD  
371  C CE  . MET A 41  ? 0.2028 0.2012 0.2055 -0.0178 -0.0054 -0.0011 41  MET A CE  
372  N N   . PRO A 42  ? 0.2420 0.2283 0.2495 -0.0144 -0.0102 -0.0054 42  PRO A N   
373  C CA  . PRO A 42  ? 0.2290 0.2122 0.2343 -0.0139 -0.0116 -0.0079 42  PRO A CA  
374  C C   . PRO A 42  ? 0.1797 0.1597 0.1846 -0.0155 -0.0143 -0.0072 42  PRO A C   
375  O O   . PRO A 42  ? 0.2606 0.2382 0.2619 -0.0158 -0.0156 -0.0093 42  PRO A O   
376  C CB  . PRO A 42  ? 0.2496 0.2314 0.2578 -0.0122 -0.0117 -0.0086 42  PRO A CB  
377  C CG  . PRO A 42  ? 0.2131 0.1971 0.2258 -0.0125 -0.0112 -0.0058 42  PRO A CG  
378  C CD  . PRO A 42  ? 0.2031 0.1902 0.2144 -0.0134 -0.0096 -0.0045 42  PRO A CD  
379  N N   . ALA A 43  ? 0.1542 0.1344 0.1625 -0.0166 -0.0152 -0.0042 43  ALA A N   
380  C CA  . ALA A 43  ? 0.2489 0.2268 0.2576 -0.0184 -0.0179 -0.0027 43  ALA A CA  
381  C C   . ALA A 43  ? 0.3355 0.3141 0.3405 -0.0199 -0.0179 -0.0026 43  ALA A C   
382  O O   . ALA A 43  ? 0.3407 0.3172 0.3451 -0.0216 -0.0204 -0.0018 43  ALA A O   
383  C CB  . ALA A 43  ? 0.2521 0.2311 0.2656 -0.0188 -0.0183 0.0012  43  ALA A CB  
384  N N   . TYR A 44  ? 0.2897 0.2714 0.2927 -0.0197 -0.0157 -0.0032 44  TYR A N   
385  C CA  . TYR A 44  ? 0.2369 0.2197 0.2365 -0.0212 -0.0159 -0.0033 44  TYR A CA  
386  C C   . TYR A 44  ? 0.2926 0.2730 0.2879 -0.0213 -0.0174 -0.0062 44  TYR A C   
387  O O   . TYR A 44  ? 0.2644 0.2446 0.2572 -0.0230 -0.0188 -0.0060 44  TYR A O   
388  C CB  . TYR A 44  ? 0.2286 0.2152 0.2269 -0.0209 -0.0135 -0.0034 44  TYR A CB  
389  C CG  . TYR A 44  ? 0.2224 0.2107 0.2232 -0.0216 -0.0126 -0.0006 44  TYR A CG  
390  C CD1 . TYR A 44  ? 0.2551 0.2444 0.2557 -0.0233 -0.0131 0.0014  44  TYR A CD1 
391  C CD2 . TYR A 44  ? 0.1599 0.1487 0.1631 -0.0204 -0.0113 0.0001  44  TYR A CD2 
392  C CE1 . TYR A 44  ? 0.2322 0.2224 0.2349 -0.0235 -0.0122 0.0038  44  TYR A CE1 
393  C CE2 . TYR A 44  ? 0.2546 0.2442 0.2592 -0.0207 -0.0105 0.0022  44  TYR A CE2 
394  C CZ  . TYR A 44  ? 0.2797 0.2697 0.2840 -0.0221 -0.0109 0.0039  44  TYR A CZ  
395  O OH  . TYR A 44  ? 0.3592 0.3493 0.3648 -0.0221 -0.0101 0.0058  44  TYR A OH  
396  N N   . LEU A 45  ? 0.2870 0.2655 0.2812 -0.0193 -0.0172 -0.0091 45  LEU A N   
397  C CA  . LEU A 45  ? 0.2531 0.2286 0.2423 -0.0188 -0.0184 -0.0124 45  LEU A CA  
398  C C   . LEU A 45  ? 0.2965 0.2671 0.2853 -0.0206 -0.0222 -0.0121 45  LEU A C   
399  O O   . LEU A 45  ? 0.3051 0.2727 0.2889 -0.0207 -0.0238 -0.0148 45  LEU A O   
400  C CB  . LEU A 45  ? 0.2784 0.2526 0.2671 -0.0158 -0.0172 -0.0153 45  LEU A CB  
401  C CG  . LEU A 45  ? 0.2855 0.2649 0.2741 -0.0141 -0.0137 -0.0154 45  LEU A CG  
402  C CD1 . LEU A 45  ? 0.2360 0.2145 0.2259 -0.0113 -0.0124 -0.0171 45  LEU A CD1 
403  C CD2 . LEU A 45  ? 0.2346 0.2169 0.2180 -0.0138 -0.0126 -0.0168 45  LEU A CD2 
404  N N   . LYS A 46  ? 0.3217 0.2915 0.3154 -0.0220 -0.0237 -0.0088 46  LYS A N   
405  C CA  . LYS A 46  ? 0.3967 0.3626 0.3905 -0.0242 -0.0276 -0.0075 46  LYS A CA  
406  C C   . LYS A 46  ? 0.4245 0.3920 0.4163 -0.0268 -0.0285 -0.0057 46  LYS A C   
407  O O   . LYS A 46  ? 0.3736 0.3377 0.3634 -0.0289 -0.0319 -0.0054 46  LYS A O   
408  C CB  . LYS A 46  ? 0.3559 0.3215 0.3562 -0.0247 -0.0289 -0.0038 46  LYS A CB  
409  C CG  . LYS A 46  ? 0.4906 0.4560 0.4940 -0.0222 -0.0275 -0.0048 46  LYS A CG  
410  C CD  . LYS A 46  ? 0.6026 0.5657 0.6111 -0.0229 -0.0305 -0.0022 46  LYS A CD  
411  C CE  . LYS A 46  ? 0.6401 0.6066 0.6532 -0.0242 -0.0306 0.0030  46  LYS A CE  
412  N NZ  . LYS A 46  ? 0.6892 0.6564 0.7085 -0.0235 -0.0314 0.0059  46  LYS A NZ  
413  N N   . ASP A 47  ? 0.3766 0.3491 0.3689 -0.0269 -0.0259 -0.0042 47  ASP A N   
414  C CA  . ASP A 47  ? 0.3751 0.3498 0.3665 -0.0294 -0.0265 -0.0018 47  ASP A CA  
415  C C   . ASP A 47  ? 0.3912 0.3686 0.3775 -0.0294 -0.0252 -0.0040 47  ASP A C   
416  O O   . ASP A 47  ? 0.4236 0.4024 0.4084 -0.0317 -0.0263 -0.0025 47  ASP A O   
417  C CB  . ASP A 47  ? 0.4203 0.3985 0.4168 -0.0297 -0.0249 0.0025  47  ASP A CB  
418  C CG  . ASP A 47  ? 0.5061 0.4828 0.5078 -0.0297 -0.0262 0.0055  47  ASP A CG  
419  O OD1 . ASP A 47  ? 0.4562 0.4295 0.4581 -0.0309 -0.0295 0.0059  47  ASP A OD1 
420  O OD2 . ASP A 47  ? 0.4916 0.4705 0.4971 -0.0285 -0.0242 0.0077  47  ASP A OD2 
421  N N   . PHE A 48  ? 0.3686 0.3473 0.3526 -0.0270 -0.0228 -0.0071 48  PHE A N   
422  C CA  . PHE A 48  ? 0.3274 0.3098 0.3071 -0.0267 -0.0213 -0.0087 48  PHE A CA  
423  C C   . PHE A 48  ? 0.2829 0.2631 0.2573 -0.0242 -0.0210 -0.0132 48  PHE A C   
424  O O   . PHE A 48  ? 0.3088 0.2873 0.2845 -0.0218 -0.0200 -0.0149 48  PHE A O   
425  C CB  . PHE A 48  ? 0.2931 0.2808 0.2755 -0.0259 -0.0183 -0.0069 48  PHE A CB  
426  C CG  . PHE A 48  ? 0.3187 0.3079 0.3058 -0.0278 -0.0184 -0.0028 48  PHE A CG  
427  C CD1 . PHE A 48  ? 0.3227 0.3147 0.3095 -0.0300 -0.0189 -0.0005 48  PHE A CD1 
428  C CD2 . PHE A 48  ? 0.2866 0.2743 0.2782 -0.0271 -0.0179 -0.0012 48  PHE A CD2 
429  C CE1 . PHE A 48  ? 0.4149 0.4078 0.4060 -0.0314 -0.0188 0.0033  48  PHE A CE1 
430  C CE2 . PHE A 48  ? 0.3681 0.3569 0.3635 -0.0282 -0.0178 0.0024  48  PHE A CE2 
431  C CZ  . PHE A 48  ? 0.4623 0.4534 0.4575 -0.0303 -0.0182 0.0046  48  PHE A CZ  
432  N N   . GLU A 49  ? 0.2409 0.2216 0.2095 -0.0246 -0.0217 -0.0152 49  GLU A N   
433  C CA  . GLU A 49  ? 0.3926 0.3709 0.3552 -0.0219 -0.0214 -0.0198 49  GLU A CA  
434  C C   . GLU A 49  ? 0.4470 0.4316 0.4084 -0.0194 -0.0177 -0.0203 49  GLU A C   
435  O O   . GLU A 49  ? 0.4528 0.4416 0.4100 -0.0193 -0.0168 -0.0207 49  GLU A O   
436  C CB  . GLU A 49  ? 0.3880 0.3632 0.3440 -0.0234 -0.0242 -0.0218 49  GLU A CB  
437  C CG  . GLU A 49  ? 0.6117 0.5792 0.5679 -0.0251 -0.0284 -0.0222 49  GLU A CG  
438  C CD  . GLU A 49  ? 0.7848 0.7455 0.7384 -0.0223 -0.0291 -0.0265 49  GLU A CD  
439  O OE1 . GLU A 49  ? 0.8218 0.7821 0.7694 -0.0193 -0.0277 -0.0306 49  GLU A OE1 
440  O OE2 . GLU A 49  ? 0.8469 0.8030 0.8048 -0.0228 -0.0312 -0.0255 49  GLU A OE2 
441  N N   . ILE A 50  ? 0.4381 0.4240 0.4038 -0.0176 -0.0155 -0.0197 50  ILE A N   
442  C CA  . ILE A 50  ? 0.3489 0.3404 0.3145 -0.0151 -0.0121 -0.0197 50  ILE A CA  
443  C C   . ILE A 50  ? 0.3271 0.3159 0.2944 -0.0121 -0.0109 -0.0215 50  ILE A C   
444  O O   . ILE A 50  ? 0.3496 0.3328 0.3191 -0.0123 -0.0127 -0.0221 50  ILE A O   
445  C CB  . ILE A 50  ? 0.3075 0.3048 0.2780 -0.0168 -0.0108 -0.0155 50  ILE A CB  
446  C CG1 . ILE A 50  ? 0.3226 0.3169 0.2988 -0.0180 -0.0116 -0.0136 50  ILE A CG1 
447  C CG2 . ILE A 50  ? 0.3385 0.3392 0.3078 -0.0197 -0.0119 -0.0134 50  ILE A CG2 
448  C CD1 . ILE A 50  ? 0.3231 0.3217 0.3036 -0.0190 -0.0102 -0.0102 50  ILE A CD1 
449  N N   . LYS A 51  ? 0.2803 0.2736 0.2470 -0.0094 -0.0080 -0.0218 51  LYS A N   
450  C CA  . LYS A 51  ? 0.2424 0.2349 0.2119 -0.0067 -0.0063 -0.0225 51  LYS A CA  
451  C C   . LYS A 51  ? 0.2597 0.2565 0.2351 -0.0079 -0.0050 -0.0187 51  LYS A C   
452  O O   . LYS A 51  ? 0.2838 0.2864 0.2597 -0.0090 -0.0040 -0.0162 51  LYS A O   
453  C CB  . LYS A 51  ? 0.1886 0.1836 0.1540 -0.0027 -0.0037 -0.0248 51  LYS A CB  
454  C CG  . LYS A 51  ? 0.3203 0.3117 0.2781 -0.0013 -0.0048 -0.0287 51  LYS A CG  
455  C CD  . LYS A 51  ? 0.3541 0.3360 0.3109 -0.0010 -0.0076 -0.0319 51  LYS A CD  
456  C CE  . LYS A 51  ? 0.3730 0.3507 0.3213 0.0010  -0.0085 -0.0365 51  LYS A CE  
457  N NZ  . LYS A 51  ? 0.5222 0.4900 0.4693 0.0005  -0.0121 -0.0394 51  LYS A NZ  
458  N N   . LEU A 52  ? 0.2177 0.2118 0.1976 -0.0076 -0.0051 -0.0183 52  LEU A N   
459  C CA  . LEU A 52  ? 0.2331 0.2305 0.2180 -0.0083 -0.0039 -0.0152 52  LEU A CA  
460  C C   . LEU A 52  ? 0.2859 0.2819 0.2733 -0.0059 -0.0029 -0.0160 52  LEU A C   
461  O O   . LEU A 52  ? 0.2939 0.2846 0.2818 -0.0051 -0.0043 -0.0180 52  LEU A O   
462  C CB  . LEU A 52  ? 0.3114 0.3071 0.2997 -0.0113 -0.0056 -0.0130 52  LEU A CB  
463  C CG  . LEU A 52  ? 0.2812 0.2781 0.2686 -0.0140 -0.0068 -0.0113 52  LEU A CG  
464  C CD1 . LEU A 52  ? 0.2469 0.2409 0.2378 -0.0159 -0.0083 -0.0095 52  LEU A CD1 
465  C CD2 . LEU A 52  ? 0.2045 0.2074 0.1919 -0.0147 -0.0054 -0.0091 52  LEU A CD2 
466  N N   . ASN A 53  ? 0.2471 0.2480 0.2366 -0.0049 -0.0006 -0.0142 53  ASN A N   
467  C CA  . ASN A 53  ? 0.2503 0.2512 0.2428 -0.0027 0.0007  -0.0143 53  ASN A CA  
468  C C   . ASN A 53  ? 0.2547 0.2570 0.2523 -0.0045 0.0006  -0.0113 53  ASN A C   
469  O O   . ASN A 53  ? 0.2230 0.2277 0.2213 -0.0068 0.0003  -0.0091 53  ASN A O   
470  C CB  . ASN A 53  ? 0.2431 0.2493 0.2342 0.0002  0.0035  -0.0140 53  ASN A CB  
471  C CG  . ASN A 53  ? 0.2699 0.2757 0.2551 0.0022  0.0039  -0.0168 53  ASN A CG  
472  O OD1 . ASN A 53  ? 0.2293 0.2301 0.2119 0.0045  0.0036  -0.0202 53  ASN A OD1 
473  N ND2 . ASN A 53  ? 0.2260 0.2369 0.2088 0.0012  0.0045  -0.0153 53  ASN A ND2 
474  N N   . PHE A 54  ? 0.2421 0.2428 0.2431 -0.0033 0.0008  -0.0114 54  PHE A N   
475  C CA  . PHE A 54  ? 0.1895 0.1910 0.1950 -0.0049 0.0005  -0.0089 54  PHE A CA  
476  C C   . PHE A 54  ? 0.2042 0.2082 0.2130 -0.0030 0.0021  -0.0079 54  PHE A C   
477  O O   . PHE A 54  ? 0.2497 0.2524 0.2584 -0.0003 0.0030  -0.0097 54  PHE A O   
478  C CB  . PHE A 54  ? 0.2520 0.2487 0.2595 -0.0060 -0.0018 -0.0094 54  PHE A CB  
479  C CG  . PHE A 54  ? 0.2245 0.2190 0.2294 -0.0078 -0.0034 -0.0098 54  PHE A CG  
480  C CD1 . PHE A 54  ? 0.2156 0.2067 0.2170 -0.0073 -0.0046 -0.0123 54  PHE A CD1 
481  C CD2 . PHE A 54  ? 0.2531 0.2487 0.2586 -0.0101 -0.0039 -0.0077 54  PHE A CD2 
482  C CE1 . PHE A 54  ? 0.2477 0.2372 0.2470 -0.0092 -0.0062 -0.0123 54  PHE A CE1 
483  C CE2 . PHE A 54  ? 0.2497 0.2436 0.2533 -0.0117 -0.0053 -0.0077 54  PHE A CE2 
484  C CZ  . PHE A 54  ? 0.2153 0.2065 0.2160 -0.0114 -0.0064 -0.0098 54  PHE A CZ  
485  N N   . ASN A 55  ? 0.2406 0.2480 0.2523 -0.0046 0.0025  -0.0050 55  ASN A N   
486  C CA  . ASN A 55  ? 0.3066 0.3164 0.3222 -0.0036 0.0037  -0.0034 55  ASN A CA  
487  C C   . ASN A 55  ? 0.2682 0.2764 0.2875 -0.0051 0.0023  -0.0023 55  ASN A C   
488  O O   . ASN A 55  ? 0.2322 0.2401 0.2508 -0.0074 0.0013  -0.0013 55  ASN A O   
489  C CB  . ASN A 55  ? 0.2521 0.2679 0.2682 -0.0043 0.0051  -0.0003 55  ASN A CB  
490  C CG  . ASN A 55  ? 0.2571 0.2759 0.2775 -0.0032 0.0064  0.0017  55  ASN A CG  
491  O OD1 . ASN A 55  ? 0.2147 0.2336 0.2360 -0.0003 0.0078  0.0007  55  ASN A OD1 
492  N ND2 . ASN A 55  ? 0.1534 0.1745 0.1763 -0.0055 0.0058  0.0045  55  ASN A ND2 
493  N N   . LEU A 56  ? 0.2837 0.2910 0.3067 -0.0037 0.0024  -0.0023 56  LEU A N   
494  C CA  . LEU A 56  ? 0.2861 0.2929 0.3130 -0.0049 0.0013  -0.0008 56  LEU A CA  
495  C C   . LEU A 56  ? 0.2791 0.2899 0.3104 -0.0044 0.0026  0.0016  56  LEU A C   
496  O O   . LEU A 56  ? 0.2717 0.2825 0.3051 -0.0021 0.0035  0.0010  56  LEU A O   
497  C CB  . LEU A 56  ? 0.2380 0.2401 0.2666 -0.0042 -0.0005 -0.0024 56  LEU A CB  
498  C CG  . LEU A 56  ? 0.2848 0.2830 0.3095 -0.0050 -0.0020 -0.0043 56  LEU A CG  
499  C CD1 . LEU A 56  ? 0.3180 0.3112 0.3439 -0.0041 -0.0040 -0.0060 56  LEU A CD1 
500  C CD2 . LEU A 56  ? 0.2059 0.2048 0.2302 -0.0074 -0.0029 -0.0026 56  LEU A CD2 
501  N N   . THR A 57  ? 0.2340 0.2480 0.2663 -0.0064 0.0025  0.0041  57  THR A N   
502  C CA  . THR A 57  ? 0.1839 0.2019 0.2204 -0.0063 0.0035  0.0068  57  THR A CA  
503  C C   . THR A 57  ? 0.1596 0.1765 0.2012 -0.0056 0.0026  0.0071  57  THR A C   
504  O O   . THR A 57  ? 0.1715 0.1855 0.2131 -0.0063 0.0010  0.0064  57  THR A O   
505  C CB  . THR A 57  ? 0.1801 0.2016 0.2160 -0.0089 0.0033  0.0095  57  THR A CB  
506  O OG1 . THR A 57  ? 0.1992 0.2189 0.2345 -0.0106 0.0018  0.0095  57  THR A OG1 
507  C CG2 . THR A 57  ? 0.1634 0.1860 0.1949 -0.0098 0.0037  0.0096  57  THR A CG2 
508  N N   . PRO A 58  ? 0.1988 0.2183 0.2450 -0.0044 0.0036  0.0087  58  PRO A N   
509  C CA  . PRO A 58  ? 0.2420 0.2608 0.2938 -0.0039 0.0026  0.0095  58  PRO A CA  
510  C C   . PRO A 58  ? 0.2824 0.3034 0.3360 -0.0062 0.0014  0.0118  58  PRO A C   
511  O O   . PRO A 58  ? 0.2946 0.3138 0.3506 -0.0063 -0.0002 0.0118  58  PRO A O   
512  C CB  . PRO A 58  ? 0.2465 0.2686 0.3027 -0.0021 0.0043  0.0112  58  PRO A CB  
513  C CG  . PRO A 58  ? 0.2010 0.2237 0.2531 -0.0006 0.0063  0.0101  58  PRO A CG  
514  C CD  . PRO A 58  ? 0.1560 0.1793 0.2029 -0.0031 0.0058  0.0101  58  PRO A CD  
515  N N   . VAL A 59  ? 0.1844 0.2092 0.2365 -0.0082 0.0019  0.0139  59  VAL A N   
516  C CA  . VAL A 59  ? 0.1957 0.2222 0.2481 -0.0102 0.0009  0.0156  59  VAL A CA  
517  C C   . VAL A 59  ? 0.2091 0.2316 0.2580 -0.0105 -0.0004 0.0137  59  VAL A C   
518  O O   . VAL A 59  ? 0.2180 0.2409 0.2688 -0.0108 -0.0014 0.0148  59  VAL A O   
519  C CB  . VAL A 59  ? 0.2351 0.2651 0.2851 -0.0124 0.0013  0.0176  59  VAL A CB  
520  C CG1 . VAL A 59  ? 0.2918 0.3198 0.3357 -0.0131 0.0015  0.0161  59  VAL A CG1 
521  C CG2 . VAL A 59  ? 0.1949 0.2266 0.2447 -0.0142 0.0003  0.0193  59  VAL A CG2 
522  N N   . LEU A 60  ? 0.2517 0.2709 0.2957 -0.0103 -0.0003 0.0113  60  LEU A N   
523  C CA  . LEU A 60  ? 0.3022 0.3179 0.3435 -0.0105 -0.0015 0.0099  60  LEU A CA  
524  C C   . LEU A 60  ? 0.2162 0.2295 0.2611 -0.0092 -0.0026 0.0094  60  LEU A C   
525  O O   . LEU A 60  ? 0.2393 0.2522 0.2853 -0.0095 -0.0038 0.0103  60  LEU A O   
526  C CB  . LEU A 60  ? 0.2644 0.2775 0.3003 -0.0108 -0.0012 0.0078  60  LEU A CB  
527  C CG  . LEU A 60  ? 0.2521 0.2613 0.2856 -0.0108 -0.0024 0.0064  60  LEU A CG  
528  C CD1 . LEU A 60  ? 0.2450 0.2547 0.2782 -0.0116 -0.0030 0.0078  60  LEU A CD1 
529  C CD2 . LEU A 60  ? 0.2407 0.2482 0.2694 -0.0112 -0.0021 0.0046  60  LEU A CD2 
530  N N   . ILE A 61  ? 0.2657 0.2774 0.3123 -0.0077 -0.0025 0.0081  61  ILE A N   
531  C CA  . ILE A 61  ? 0.2415 0.2502 0.2915 -0.0067 -0.0041 0.0075  61  ILE A CA  
532  C C   . ILE A 61  ? 0.2253 0.2369 0.2814 -0.0071 -0.0051 0.0106  61  ILE A C   
533  O O   . ILE A 61  ? 0.2346 0.2449 0.2929 -0.0073 -0.0070 0.0114  61  ILE A O   
534  C CB  . ILE A 61  ? 0.2810 0.2873 0.3318 -0.0047 -0.0037 0.0055  61  ILE A CB  
535  C CG1 . ILE A 61  ? 0.2399 0.2434 0.2844 -0.0041 -0.0029 0.0025  61  ILE A CG1 
536  C CG2 . ILE A 61  ? 0.2779 0.2803 0.3326 -0.0038 -0.0059 0.0051  61  ILE A CG2 
537  C CD1 . ILE A 61  ? 0.3488 0.3505 0.3930 -0.0016 -0.0019 0.0004  61  ILE A CD1 
538  N N   . ASP A 62  ? 0.2444 0.2607 0.3036 -0.0073 -0.0040 0.0127  62  ASP A N   
539  C CA  . ASP A 62  ? 0.2935 0.3136 0.3586 -0.0078 -0.0048 0.0160  62  ASP A CA  
540  C C   . ASP A 62  ? 0.2719 0.2931 0.3355 -0.0088 -0.0057 0.0173  62  ASP A C   
541  O O   . ASP A 62  ? 0.2893 0.3116 0.3574 -0.0087 -0.0072 0.0194  62  ASP A O   
542  C CB  . ASP A 62  ? 0.2998 0.3252 0.3670 -0.0084 -0.0033 0.0183  62  ASP A CB  
543  C CG  . ASP A 62  ? 0.3531 0.3789 0.4245 -0.0070 -0.0025 0.0184  62  ASP A CG  
544  O OD1 . ASP A 62  ? 0.3344 0.3566 0.4086 -0.0055 -0.0036 0.0172  62  ASP A OD1 
545  O OD2 . ASP A 62  ? 0.3095 0.3389 0.3812 -0.0074 -0.0009 0.0197  62  ASP A OD2 
546  N N   . GLN A 63  ? 0.2775 0.2987 0.3352 -0.0097 -0.0047 0.0164  63  GLN A N   
547  C CA  . GLN A 63  ? 0.2145 0.2366 0.2703 -0.0101 -0.0051 0.0176  63  GLN A CA  
548  C C   . GLN A 63  ? 0.2237 0.2423 0.2790 -0.0096 -0.0065 0.0169  63  GLN A C   
549  O O   . GLN A 63  ? 0.2286 0.2489 0.2861 -0.0093 -0.0074 0.0192  63  GLN A O   
550  C CB  . GLN A 63  ? 0.1904 0.2123 0.2396 -0.0111 -0.0040 0.0166  63  GLN A CB  
551  C CG  . GLN A 63  ? 0.2398 0.2650 0.2890 -0.0121 -0.0030 0.0175  63  GLN A CG  
552  C CD  . GLN A 63  ? 0.2835 0.3075 0.3260 -0.0133 -0.0026 0.0164  63  GLN A CD  
553  O OE1 . GLN A 63  ? 0.2655 0.2892 0.3048 -0.0135 -0.0027 0.0165  63  GLN A OE1 
554  N NE2 . GLN A 63  ? 0.2247 0.2479 0.2650 -0.0140 -0.0020 0.0154  63  GLN A NE2 
555  N N   . ILE A 64  ? 0.3183 0.3322 0.3705 -0.0094 -0.0067 0.0141  64  ILE A N   
556  C CA  . ILE A 64  ? 0.2198 0.2302 0.2719 -0.0092 -0.0083 0.0136  64  ILE A CA  
557  C C   . ILE A 64  ? 0.3048 0.3158 0.3636 -0.0088 -0.0104 0.0159  64  ILE A C   
558  O O   . ILE A 64  ? 0.2578 0.2690 0.3185 -0.0089 -0.0119 0.0179  64  ILE A O   
559  C CB  . ILE A 64  ? 0.2662 0.2719 0.3142 -0.0090 -0.0082 0.0102  64  ILE A CB  
560  C CG1 . ILE A 64  ? 0.2487 0.2540 0.2905 -0.0097 -0.0068 0.0087  64  ILE A CG1 
561  C CG2 . ILE A 64  ? 0.3380 0.3398 0.3868 -0.0090 -0.0105 0.0099  64  ILE A CG2 
562  C CD1 . ILE A 64  ? 0.2399 0.2416 0.2777 -0.0096 -0.0068 0.0059  64  ILE A CD1 
563  N N   . GLN A 65  ? 0.2266 0.2381 0.2895 -0.0083 -0.0105 0.0159  65  GLN A N   
564  C CA  . GLN A 65  ? 0.2723 0.2841 0.3423 -0.0081 -0.0129 0.0182  65  GLN A CA  
565  C C   . GLN A 65  ? 0.2736 0.2914 0.3480 -0.0085 -0.0132 0.0226  65  GLN A C   
566  O O   . GLN A 65  ? 0.2638 0.2822 0.3426 -0.0086 -0.0154 0.0253  65  GLN A O   
567  C CB  . GLN A 65  ? 0.2466 0.2579 0.3203 -0.0073 -0.0127 0.0175  65  GLN A CB  
568  C CG  . GLN A 65  ? 0.2848 0.2898 0.3551 -0.0063 -0.0129 0.0135  65  GLN A CG  
569  C CD  . GLN A 65  ? 0.3272 0.3319 0.4012 -0.0049 -0.0124 0.0130  65  GLN A CD  
570  O OE1 . GLN A 65  ? 0.4049 0.4140 0.4800 -0.0047 -0.0102 0.0140  65  GLN A OE1 
571  N NE2 . GLN A 65  ? 0.3407 0.3402 0.4169 -0.0040 -0.0146 0.0116  65  GLN A NE2 
572  N N   . GLU A 66  ? 0.2400 0.2624 0.3132 -0.0087 -0.0111 0.0235  66  GLU A N   
573  C CA  . GLU A 66  ? 0.2422 0.2708 0.3191 -0.0088 -0.0112 0.0275  66  GLU A CA  
574  C C   . GLU A 66  ? 0.2671 0.2960 0.3414 -0.0085 -0.0116 0.0287  66  GLU A C   
575  O O   . GLU A 66  ? 0.3028 0.3356 0.3818 -0.0082 -0.0127 0.0325  66  GLU A O   
576  C CB  . GLU A 66  ? 0.2476 0.2805 0.3226 -0.0092 -0.0091 0.0279  66  GLU A CB  
577  C CG  . GLU A 66  ? 0.4165 0.4565 0.4970 -0.0093 -0.0095 0.0323  66  GLU A CG  
578  C CD  . GLU A 66  ? 0.6032 0.6475 0.6814 -0.0100 -0.0077 0.0328  66  GLU A CD  
579  O OE1 . GLU A 66  ? 0.6543 0.7042 0.7337 -0.0100 -0.0076 0.0358  66  GLU A OE1 
580  O OE2 . GLU A 66  ? 0.6308 0.6732 0.7060 -0.0106 -0.0066 0.0305  66  GLU A OE2 
581  N N   . TYR A 67  ? 0.2199 0.2449 0.2873 -0.0085 -0.0105 0.0258  67  TYR A N   
582  C CA  . TYR A 67  ? 0.2683 0.2933 0.3337 -0.0080 -0.0108 0.0271  67  TYR A CA  
583  C C   . TYR A 67  ? 0.3160 0.3387 0.3855 -0.0082 -0.0135 0.0286  67  TYR A C   
584  O O   . TYR A 67  ? 0.3027 0.3284 0.3751 -0.0077 -0.0144 0.0323  67  TYR A O   
585  C CB  . TYR A 67  ? 0.2363 0.2574 0.2937 -0.0080 -0.0092 0.0239  67  TYR A CB  
586  C CG  . TYR A 67  ? 0.2324 0.2556 0.2851 -0.0078 -0.0071 0.0233  67  TYR A CG  
587  C CD1 . TYR A 67  ? 0.1926 0.2180 0.2430 -0.0067 -0.0062 0.0250  67  TYR A CD1 
588  C CD2 . TYR A 67  ? 0.2302 0.2529 0.2802 -0.0086 -0.0060 0.0211  67  TYR A CD2 
589  C CE1 . TYR A 67  ? 0.1539 0.1800 0.1989 -0.0064 -0.0045 0.0240  67  TYR A CE1 
590  C CE2 . TYR A 67  ? 0.2512 0.2750 0.2963 -0.0088 -0.0046 0.0206  67  TYR A CE2 
591  C CZ  . TYR A 67  ? 0.1872 0.2122 0.2295 -0.0077 -0.0040 0.0217  67  TYR A CZ  
592  O OH  . TYR A 67  ? 0.2087 0.2338 0.2456 -0.0079 -0.0029 0.0207  67  TYR A OH  
593  N N   . ALA A 68  ? 0.2349 0.2524 0.3043 -0.0088 -0.0148 0.0260  68  ALA A N   
594  C CA  . ALA A 68  ? 0.2131 0.2275 0.2857 -0.0093 -0.0179 0.0272  68  ALA A CA  
595  C C   . ALA A 68  ? 0.2538 0.2720 0.3348 -0.0094 -0.0202 0.0317  68  ALA A C   
596  O O   . ALA A 68  ? 0.2888 0.3074 0.3733 -0.0098 -0.0227 0.0350  68  ALA A O   
597  C CB  . ALA A 68  ? 0.2604 0.2681 0.3306 -0.0097 -0.0189 0.0230  68  ALA A CB  
598  N N   . GLN A 69  ? 0.2344 0.2560 0.3193 -0.0091 -0.0196 0.0325  69  GLN A N   
599  C CA  . GLN A 69  ? 0.3517 0.3779 0.4453 -0.0093 -0.0217 0.0372  69  GLN A CA  
600  C C   . GLN A 69  ? 0.4057 0.4398 0.5014 -0.0087 -0.0208 0.0418  69  GLN A C   
601  O O   . GLN A 69  ? 0.3961 0.4353 0.4994 -0.0088 -0.0225 0.0465  69  GLN A O   
602  C CB  . GLN A 69  ? 0.3387 0.3658 0.4360 -0.0092 -0.0213 0.0364  69  GLN A CB  
603  C CG  . GLN A 69  ? 0.4212 0.4409 0.5176 -0.0092 -0.0224 0.0324  69  GLN A CG  
604  C CD  . GLN A 69  ? 0.5493 0.5701 0.6469 -0.0086 -0.0205 0.0309  69  GLN A CD  
605  O OE1 . GLN A 69  ? 0.6238 0.6509 0.7231 -0.0086 -0.0187 0.0331  69  GLN A OE1 
606  N NE2 . GLN A 69  ? 0.5167 0.5313 0.6133 -0.0079 -0.0210 0.0274  69  GLN A NE2 
607  N N   . GLY A 70  ? 0.3076 0.3429 0.3968 -0.0080 -0.0181 0.0407  70  GLY A N   
608  C CA  . GLY A 70  ? 0.2881 0.3306 0.3781 -0.0069 -0.0168 0.0446  70  GLY A CA  
609  C C   . GLY A 70  ? 0.3573 0.4060 0.4497 -0.0066 -0.0155 0.0462  70  GLY A C   
610  O O   . GLY A 70  ? 0.3194 0.3753 0.4151 -0.0058 -0.0153 0.0506  70  GLY A O   
611  N N   . LYS A 71  ? 0.3793 0.4260 0.4701 -0.0073 -0.0145 0.0429  71  LYS A N   
612  C CA  . LYS A 71  ? 0.4305 0.4829 0.5233 -0.0075 -0.0133 0.0444  71  LYS A CA  
613  C C   . LYS A 71  ? 0.3602 0.4127 0.4448 -0.0073 -0.0104 0.0416  71  LYS A C   
614  O O   . LYS A 71  ? 0.3870 0.4445 0.4722 -0.0076 -0.0094 0.0429  71  LYS A O   
615  C CB  . LYS A 71  ? 0.4791 0.5302 0.5770 -0.0085 -0.0143 0.0437  71  LYS A CB  
616  C CG  . LYS A 71  ? 0.5253 0.5753 0.6315 -0.0088 -0.0176 0.0461  71  LYS A CG  
617  C CD  . LYS A 71  ? 0.5520 0.5991 0.6616 -0.0092 -0.0180 0.0443  71  LYS A CD  
618  C CE  . LYS A 71  ? 0.5268 0.5712 0.6442 -0.0095 -0.0216 0.0461  71  LYS A CE  
619  N NZ  . LYS A 71  ? 0.5273 0.5698 0.6487 -0.0094 -0.0218 0.0449  71  LYS A NZ  
620  N N   . ALA A 72  ? 0.2655 0.3125 0.3425 -0.0070 -0.0093 0.0380  72  ALA A N   
621  C CA  . ALA A 72  ? 0.2854 0.3312 0.3543 -0.0071 -0.0071 0.0351  72  ALA A CA  
622  C C   . ALA A 72  ? 0.2719 0.3220 0.3378 -0.0056 -0.0059 0.0371  72  ALA A C   
623  O O   . ALA A 72  ? 0.3074 0.3569 0.3717 -0.0042 -0.0058 0.0379  72  ALA A O   
624  C CB  . ALA A 72  ? 0.2684 0.3069 0.3311 -0.0073 -0.0067 0.0309  72  ALA A CB  
625  N N   . LYS A 73  ? 0.3054 0.3599 0.3700 -0.0059 -0.0050 0.0379  73  LYS A N   
626  C CA  . LYS A 73  ? 0.3190 0.3772 0.3792 -0.0043 -0.0036 0.0392  73  LYS A CA  
627  C C   . LYS A 73  ? 0.3192 0.3718 0.3694 -0.0043 -0.0023 0.0348  73  LYS A C   
628  O O   . LYS A 73  ? 0.2827 0.3351 0.3290 -0.0057 -0.0019 0.0333  73  LYS A O   
629  C CB  . LYS A 73  ? 0.3360 0.4020 0.3998 -0.0047 -0.0036 0.0424  73  LYS A CB  
630  C CG  . LYS A 73  ? 0.4200 0.4921 0.4946 -0.0048 -0.0052 0.0473  73  LYS A CG  
631  C CD  . LYS A 73  ? 0.5075 0.5874 0.5864 -0.0057 -0.0053 0.0505  73  LYS A CD  
632  C CE  . LYS A 73  ? 0.5597 0.6377 0.6406 -0.0081 -0.0058 0.0489  73  LYS A CE  
633  N NZ  . LYS A 73  ? 0.5989 0.6741 0.6873 -0.0088 -0.0074 0.0492  73  LYS A NZ  
634  N N   . ASP A 74  ? 0.3071 0.3550 0.3532 -0.0030 -0.0018 0.0331  74  ASP A N   
635  C CA  . ASP A 74  ? 0.2928 0.3342 0.3301 -0.0032 -0.0009 0.0290  74  ASP A CA  
636  C C   . ASP A 74  ? 0.3004 0.3427 0.3313 -0.0008 0.0006  0.0290  74  ASP A C   
637  O O   . ASP A 74  ? 0.3838 0.4272 0.4150 0.0017  0.0013  0.0306  74  ASP A O   
638  C CB  . ASP A 74  ? 0.2586 0.2944 0.2956 -0.0031 -0.0013 0.0272  74  ASP A CB  
639  C CG  . ASP A 74  ? 0.3062 0.3354 0.3353 -0.0036 -0.0007 0.0232  74  ASP A CG  
640  O OD1 . ASP A 74  ? 0.2549 0.2828 0.2775 -0.0023 0.0004  0.0222  74  ASP A OD1 
641  O OD2 . ASP A 74  ? 0.3703 0.3955 0.3994 -0.0051 -0.0013 0.0212  74  ASP A OD2 
642  N N   . VAL A 75  ? 0.2247 0.2665 0.2498 -0.0015 0.0009  0.0273  75  VAL A N   
643  C CA  . VAL A 75  ? 0.3181 0.3611 0.3368 0.0009  0.0022  0.0273  75  VAL A CA  
644  C C   . VAL A 75  ? 0.3295 0.3664 0.3420 0.0032  0.0033  0.0250  75  VAL A C   
645  O O   . VAL A 75  ? 0.3403 0.3795 0.3513 0.0066  0.0047  0.0265  75  VAL A O   
646  C CB  . VAL A 75  ? 0.3834 0.4259 0.3962 -0.0008 0.0019  0.0255  75  VAL A CB  
647  C CG1 . VAL A 75  ? 0.3671 0.4172 0.3867 -0.0026 0.0011  0.0288  75  VAL A CG1 
648  C CG2 . VAL A 75  ? 0.4086 0.4436 0.4167 -0.0034 0.0009  0.0217  75  VAL A CG2 
649  N N   . PHE A 76  ? 0.2247 0.2544 0.2340 0.0016  0.0027  0.0216  76  PHE A N   
650  C CA  . PHE A 76  ? 0.3395 0.3636 0.3435 0.0037  0.0036  0.0197  76  PHE A CA  
651  C C   . PHE A 76  ? 0.3499 0.3762 0.3595 0.0057  0.0042  0.0225  76  PHE A C   
652  O O   . PHE A 76  ? 0.3949 0.4202 0.4015 0.0087  0.0057  0.0229  76  PHE A O   
653  C CB  . PHE A 76  ? 0.3931 0.4097 0.3933 0.0013  0.0026  0.0160  76  PHE A CB  
654  C CG  . PHE A 76  ? 0.5160 0.5267 0.5106 0.0032  0.0034  0.0141  76  PHE A CG  
655  C CD1 . PHE A 76  ? 0.5553 0.5622 0.5416 0.0049  0.0040  0.0119  76  PHE A CD1 
656  C CD2 . PHE A 76  ? 0.5368 0.5456 0.5345 0.0036  0.0035  0.0145  76  PHE A CD2 
657  C CE1 . PHE A 76  ? 0.6213 0.6224 0.6026 0.0071  0.0049  0.0102  76  PHE A CE1 
658  C CE2 . PHE A 76  ? 0.5952 0.5990 0.5884 0.0055  0.0044  0.0132  76  PHE A CE2 
659  C CZ  . PHE A 76  ? 0.6222 0.6221 0.6074 0.0074  0.0051  0.0110  76  PHE A CZ  
660  N N   . LEU A 77  ? 0.3371 0.3664 0.3547 0.0040  0.0030  0.0246  77  LEU A N   
661  C CA  . LEU A 77  ? 0.3439 0.3752 0.3671 0.0053  0.0030  0.0277  77  LEU A CA  
662  C C   . LEU A 77  ? 0.3225 0.3610 0.3485 0.0083  0.0040  0.0321  77  LEU A C   
663  O O   . LEU A 77  ? 0.2675 0.3071 0.2950 0.0106  0.0047  0.0346  77  LEU A O   
664  C CB  . LEU A 77  ? 0.3173 0.3491 0.3476 0.0026  0.0010  0.0285  77  LEU A CB  
665  C CG  . LEU A 77  ? 0.3905 0.4224 0.4261 0.0028  0.0001  0.0308  77  LEU A CG  
666  C CD1 . LEU A 77  ? 0.3952 0.4214 0.4262 0.0034  0.0007  0.0288  77  LEU A CD1 
667  C CD2 . LEU A 77  ? 0.3251 0.3564 0.3663 0.0002  -0.0020 0.0307  77  LEU A CD2 
668  N N   . GLU A 78  ? 0.3342 0.3783 0.3614 0.0084  0.0041  0.0336  78  GLU A N   
669  C CA  . GLU A 78  ? 0.2986 0.3504 0.3283 0.0115  0.0052  0.0382  78  GLU A CA  
670  C C   . GLU A 78  ? 0.3062 0.3562 0.3279 0.0154  0.0077  0.0371  78  GLU A C   
671  O O   . GLU A 78  ? 0.3365 0.3913 0.3600 0.0187  0.0090  0.0409  78  GLU A O   
672  C CB  . GLU A 78  ? 0.3886 0.4474 0.4213 0.0108  0.0048  0.0403  78  GLU A CB  
673  C CG  . GLU A 78  ? 0.5774 0.6359 0.6153 0.0068  0.0027  0.0396  78  GLU A CG  
674  C CD  . GLU A 78  ? 0.7359 0.7948 0.7828 0.0053  0.0008  0.0420  78  GLU A CD  
675  O OE1 . GLU A 78  ? 0.7631 0.8285 0.8172 0.0063  0.0001  0.0470  78  GLU A OE1 
676  O OE2 . GLU A 78  ? 0.7553 0.8081 0.8020 0.0031  -0.0002 0.0389  78  GLU A OE2 
677  N N   . ALA A 79  ? 0.3022 0.3451 0.3149 0.0151  0.0082  0.0321  79  ALA A N   
678  C CA  . ALA A 79  ? 0.3528 0.3924 0.3573 0.0189  0.0104  0.0304  79  ALA A CA  
679  C C   . ALA A 79  ? 0.4153 0.4514 0.4209 0.0204  0.0111  0.0310  79  ALA A C   
680  O O   . ALA A 79  ? 0.4513 0.4872 0.4531 0.0245  0.0132  0.0317  79  ALA A O   
681  C CB  . ALA A 79  ? 0.2800 0.3120 0.2750 0.0177  0.0102  0.0249  79  ALA A CB  
682  N N   . ILE A 80  ? 0.3737 0.4070 0.3841 0.0172  0.0093  0.0307  80  ILE A N   
683  C CA  . ILE A 80  ? 0.3299 0.3607 0.3422 0.0180  0.0095  0.0318  80  ILE A CA  
684  C C   . ILE A 80  ? 0.3033 0.3418 0.3234 0.0198  0.0097  0.0380  80  ILE A C   
685  O O   . ILE A 80  ? 0.2933 0.3326 0.3135 0.0228  0.0112  0.0404  80  ILE A O   
686  C CB  . ILE A 80  ? 0.3874 0.4128 0.4016 0.0139  0.0074  0.0292  80  ILE A CB  
687  C CG1 . ILE A 80  ? 0.4531 0.4707 0.4594 0.0125  0.0073  0.0238  80  ILE A CG1 
688  C CG2 . ILE A 80  ? 0.3076 0.3323 0.3259 0.0140  0.0071  0.0316  80  ILE A CG2 
689  C CD1 . ILE A 80  ? 0.5303 0.5423 0.5313 0.0147  0.0087  0.0222  80  ILE A CD1 
690  N N   . ARG A 81  ? 0.3612 0.4057 0.3885 0.0180  0.0081  0.0409  81  ARG A N   
691  C CA  . ARG A 81  ? 0.3250 0.3764 0.3609 0.0187  0.0073  0.0471  81  ARG A CA  
692  C C   . ARG A 81  ? 0.2912 0.3504 0.3273 0.0231  0.0095  0.0517  81  ARG A C   
693  O O   . ARG A 81  ? 0.2393 0.3031 0.2805 0.0250  0.0097  0.0570  81  ARG A O   
694  C CB  . ARG A 81  ? 0.3920 0.4466 0.4355 0.0152  0.0045  0.0487  81  ARG A CB  
695  C CG  . ARG A 81  ? 0.5501 0.6130 0.6030 0.0158  0.0032  0.0557  81  ARG A CG  
696  C CD  . ARG A 81  ? 0.6184 0.6836 0.6785 0.0125  0.0003  0.0569  81  ARG A CD  
697  N NE  . ARG A 81  ? 0.7156 0.7746 0.7782 0.0092  -0.0022 0.0548  81  ARG A NE  
698  C CZ  . ARG A 81  ? 0.7518 0.8103 0.8191 0.0085  -0.0041 0.0579  81  ARG A CZ  
699  N NH1 . ARG A 81  ? 0.7627 0.8271 0.8334 0.0109  -0.0037 0.0637  81  ARG A NH1 
700  N NH2 . ARG A 81  ? 0.7206 0.7729 0.7889 0.0055  -0.0064 0.0553  81  ARG A NH2 
701  N N   . LYS A 82  ? 0.2661 0.3454 0.3108 0.0021  0.0251  0.0079  82  LYS A N   
702  C CA  . LYS A 82  ? 0.2792 0.3638 0.3255 0.0044  0.0272  0.0064  82  LYS A CA  
703  C C   . LYS A 82  ? 0.3009 0.3813 0.3492 0.0071  0.0272  0.0040  82  LYS A C   
704  O O   . LYS A 82  ? 0.2661 0.3394 0.3131 0.0070  0.0259  0.0025  82  LYS A O   
705  C CB  . LYS A 82  ? 0.3755 0.4641 0.4175 0.0029  0.0283  0.0044  82  LYS A CB  
706  C CG  . LYS A 82  ? 0.4785 0.5754 0.5211 0.0017  0.0296  0.0079  82  LYS A CG  
707  C CD  . LYS A 82  ? 0.5305 0.6342 0.5694 0.0007  0.0308  0.0064  82  LYS A CD  
708  C CE  . LYS A 82  ? 0.5497 0.6519 0.5837 -0.0029 0.0291  0.0053  82  LYS A CE  
709  N NZ  . LYS A 82  ? 0.6078 0.7187 0.6381 -0.0045 0.0299  0.0045  82  LYS A NZ  
710  N N   . ASP A 83  ? 0.2331 0.3181 0.2853 0.0098  0.0290  0.0041  83  ASP A N   
711  C CA  . ASP A 83  ? 0.2542 0.3363 0.3083 0.0127  0.0302  0.0018  83  ASP A CA  
712  C C   . ASP A 83  ? 0.2668 0.3454 0.3153 0.0116  0.0316  -0.0027 83  ASP A C   
713  O O   . ASP A 83  ? 0.2428 0.3258 0.2870 0.0096  0.0324  -0.0039 83  ASP A O   
714  C CB  . ASP A 83  ? 0.2850 0.3735 0.3439 0.0156  0.0326  0.0026  83  ASP A CB  
715  C CG  . ASP A 83  ? 0.3679 0.4533 0.4307 0.0191  0.0341  0.0013  83  ASP A CG  
716  O OD1 . ASP A 83  ? 0.3761 0.4577 0.4356 0.0196  0.0362  -0.0025 83  ASP A OD1 
717  O OD2 . ASP A 83  ? 0.3562 0.4432 0.4256 0.0212  0.0335  0.0041  83  ASP A OD2 
718  N N   . PRO A 84  ? 0.3134 0.3844 0.3620 0.0126  0.0318  -0.0050 84  PRO A N   
719  C CA  . PRO A 84  ? 0.3232 0.3898 0.3663 0.0108  0.0334  -0.0099 84  PRO A CA  
720  C C   . PRO A 84  ? 0.3604 0.4317 0.4003 0.0109  0.0367  -0.0134 84  PRO A C   
721  O O   . PRO A 84  ? 0.2845 0.3551 0.3181 0.0078  0.0374  -0.0172 84  PRO A O   
722  C CB  . PRO A 84  ? 0.3377 0.3954 0.3838 0.0129  0.0342  -0.0110 84  PRO A CB  
723  C CG  . PRO A 84  ? 0.3059 0.3632 0.3570 0.0142  0.0311  -0.0059 84  PRO A CG  
724  C CD  . PRO A 84  ? 0.2773 0.3432 0.3310 0.0148  0.0304  -0.0028 84  PRO A CD  
725  N N   . ASP A 85  ? 0.3187 0.3947 0.3627 0.0142  0.0389  -0.0122 85  ASP A N   
726  C CA  . ASP A 85  ? 0.2858 0.3672 0.3265 0.0144  0.0422  -0.0149 85  ASP A CA  
727  C C   . ASP A 85  ? 0.2747 0.3647 0.3109 0.0113  0.0410  -0.0137 85  ASP A C   
728  O O   . ASP A 85  ? 0.2679 0.3626 0.2990 0.0102  0.0431  -0.0163 85  ASP A O   
729  C CB  . ASP A 85  ? 0.2505 0.3361 0.2977 0.0188  0.0445  -0.0127 85  ASP A CB  
730  C CG  . ASP A 85  ? 0.4382 0.5168 0.4903 0.0223  0.0468  -0.0138 85  ASP A CG  
731  O OD1 . ASP A 85  ? 0.5087 0.5793 0.5580 0.0215  0.0482  -0.0177 85  ASP A OD1 
732  O OD2 . ASP A 85  ? 0.5026 0.5839 0.5621 0.0259  0.0476  -0.0106 85  ASP A OD2 
733  N N   . ASP A 86  ? 0.2580 0.3503 0.2959 0.0100  0.0379  -0.0094 86  ASP A N   
734  C CA  . ASP A 86  ? 0.3085 0.4091 0.3438 0.0074  0.0371  -0.0069 86  ASP A CA  
735  C C   . ASP A 86  ? 0.2543 0.3529 0.2839 0.0031  0.0350  -0.0085 86  ASP A C   
736  O O   . ASP A 86  ? 0.3332 0.4394 0.3604 0.0007  0.0344  -0.0064 86  ASP A O   
737  C CB  . ASP A 86  ? 0.2891 0.3932 0.3302 0.0084  0.0360  -0.0012 86  ASP A CB  
738  C CG  . ASP A 86  ? 0.3913 0.4992 0.4383 0.0121  0.0381  0.0007  86  ASP A CG  
739  O OD1 . ASP A 86  ? 0.4154 0.5266 0.4615 0.0138  0.0408  -0.0014 86  ASP A OD1 
740  O OD2 . ASP A 86  ? 0.4626 0.5703 0.5152 0.0130  0.0372  0.0040  86  ASP A OD2 
741  N N   . LEU A 87  ? 0.2154 0.3047 0.2434 0.0021  0.0341  -0.0117 87  LEU A N   
742  C CA  . LEU A 87  ? 0.2579 0.3447 0.2814 -0.0022 0.0320  -0.0131 87  LEU A CA  
743  C C   . LEU A 87  ? 0.2944 0.3860 0.3110 -0.0056 0.0329  -0.0170 87  LEU A C   
744  O O   . LEU A 87  ? 0.2926 0.3830 0.3062 -0.0051 0.0356  -0.0217 87  LEU A O   
745  C CB  . LEU A 87  ? 0.3224 0.3977 0.3464 -0.0021 0.0315  -0.0157 87  LEU A CB  
746  C CG  . LEU A 87  ? 0.3204 0.3913 0.3494 -0.0004 0.0294  -0.0113 87  LEU A CG  
747  C CD1 . LEU A 87  ? 0.2980 0.3581 0.3281 0.0003  0.0293  -0.0134 87  LEU A CD1 
748  C CD2 . LEU A 87  ? 0.2439 0.3179 0.2721 -0.0033 0.0270  -0.0076 87  LEU A CD2 
749  N N   . GLU A 88  ? 0.2678 0.3649 0.2818 -0.0094 0.0308  -0.0151 88  GLU A N   
750  C CA  . GLU A 88  ? 0.2851 0.3864 0.2920 -0.0139 0.0307  -0.0190 88  GLU A CA  
751  C C   . GLU A 88  ? 0.3021 0.3929 0.3057 -0.0166 0.0305  -0.0248 88  GLU A C   
752  O O   . GLU A 88  ? 0.2535 0.3357 0.2605 -0.0157 0.0295  -0.0239 88  GLU A O   
753  C CB  . GLU A 88  ? 0.2799 0.3912 0.2863 -0.0170 0.0283  -0.0141 88  GLU A CB  
754  C CG  . GLU A 88  ? 0.2908 0.4117 0.3017 -0.0140 0.0291  -0.0077 88  GLU A CG  
755  C CD  . GLU A 88  ? 0.4604 0.5886 0.4737 -0.0159 0.0273  -0.0012 88  GLU A CD  
756  O OE1 . GLU A 88  ? 0.4171 0.5422 0.4293 -0.0192 0.0251  -0.0014 88  GLU A OE1 
757  O OE2 . GLU A 88  ? 0.5598 0.6967 0.5769 -0.0139 0.0285  0.0043  88  GLU A OE2 
758  N N   . LYS A 89  ? 0.2519 0.3436 0.2488 -0.0201 0.0318  -0.0308 89  LYS A N   
759  C CA  . LYS A 89  ? 0.3006 0.3825 0.2942 -0.0235 0.0321  -0.0367 89  LYS A CA  
760  C C   . LYS A 89  ? 0.3208 0.4012 0.3160 -0.0265 0.0286  -0.0339 89  LYS A C   
761  O O   . LYS A 89  ? 0.2861 0.3556 0.2830 -0.0266 0.0287  -0.0358 89  LYS A O   
762  C CB  . LYS A 89  ? 0.3119 0.3971 0.2970 -0.0283 0.0337  -0.0436 89  LYS A CB  
763  C CG  . LYS A 89  ? 0.3895 0.4738 0.3724 -0.0254 0.0382  -0.0475 89  LYS A CG  
764  C CD  . LYS A 89  ? 0.4376 0.5285 0.4108 -0.0306 0.0395  -0.0534 89  LYS A CD  
765  C CE  . LYS A 89  ? 0.4410 0.5339 0.4123 -0.0271 0.0439  -0.0554 89  LYS A CE  
766  N NZ  . LYS A 89  ? 0.5785 0.6722 0.5395 -0.0321 0.0468  -0.0637 89  LYS A NZ  
767  N N   . GLU A 90  ? 0.2520 0.3431 0.2473 -0.0286 0.0258  -0.0287 90  GLU A N   
768  C CA  . GLU A 90  ? 0.3128 0.4026 0.3102 -0.0311 0.0229  -0.0253 90  GLU A CA  
769  C C   . GLU A 90  ? 0.3311 0.4130 0.3348 -0.0269 0.0227  -0.0212 90  GLU A C   
770  O O   . GLU A 90  ? 0.2748 0.3500 0.2800 -0.0283 0.0213  -0.0205 90  GLU A O   
771  C CB  . GLU A 90  ? 0.4146 0.5180 0.4122 -0.0335 0.0206  -0.0195 90  GLU A CB  
772  C CG  . GLU A 90  ? 0.5755 0.6907 0.5674 -0.0373 0.0203  -0.0213 90  GLU A CG  
773  C CD  . GLU A 90  ? 0.7031 0.8319 0.6972 -0.0391 0.0180  -0.0138 90  GLU A CD  
774  O OE1 . GLU A 90  ? 0.7436 0.8820 0.7332 -0.0442 0.0162  -0.0146 90  GLU A OE1 
775  O OE2 . GLU A 90  ? 0.7414 0.8714 0.7420 -0.0355 0.0181  -0.0070 90  GLU A OE2 
776  N N   . GLU A 91  ? 0.2572 0.3404 0.2647 -0.0221 0.0239  -0.0181 91  GLU A N   
777  C CA  . GLU A 91  ? 0.2631 0.3399 0.2759 -0.0187 0.0233  -0.0142 91  GLU A CA  
778  C C   . GLU A 91  ? 0.2593 0.3238 0.2730 -0.0171 0.0243  -0.0178 91  GLU A C   
779  O O   . GLU A 91  ? 0.3146 0.3723 0.3306 -0.0166 0.0231  -0.0157 91  GLU A O   
780  C CB  . GLU A 91  ? 0.3170 0.3992 0.3338 -0.0146 0.0243  -0.0101 91  GLU A CB  
781  C CG  . GLU A 91  ? 0.3096 0.4031 0.3273 -0.0157 0.0238  -0.0050 91  GLU A CG  
782  C CD  . GLU A 91  ? 0.3719 0.4703 0.3937 -0.0119 0.0254  -0.0014 91  GLU A CD  
783  O OE1 . GLU A 91  ? 0.2886 0.3881 0.3101 -0.0096 0.0272  -0.0040 91  GLU A OE1 
784  O OE2 . GLU A 91  ? 0.3645 0.4654 0.3901 -0.0113 0.0253  0.0039  91  GLU A OE2 
785  N N   . VAL A 92  ? 0.2863 0.3478 0.2982 -0.0161 0.0268  -0.0230 92  VAL A N   
786  C CA  . VAL A 92  ? 0.3009 0.3507 0.3142 -0.0147 0.0284  -0.0264 92  VAL A CA  
787  C C   . VAL A 92  ? 0.3376 0.3812 0.3486 -0.0188 0.0275  -0.0288 92  VAL A C   
788  O O   . VAL A 92  ? 0.4139 0.4487 0.4278 -0.0176 0.0272  -0.0276 92  VAL A O   
789  C CB  . VAL A 92  ? 0.3476 0.3956 0.3593 -0.0132 0.0323  -0.0317 92  VAL A CB  
790  C CG1 . VAL A 92  ? 0.3237 0.3594 0.3381 -0.0112 0.0347  -0.0345 92  VAL A CG1 
791  C CG2 . VAL A 92  ? 0.2744 0.3290 0.2890 -0.0089 0.0332  -0.0289 92  VAL A CG2 
792  N N   . GLU A 93  ? 0.3203 0.3686 0.3262 -0.0239 0.0270  -0.0319 93  GLU A N   
793  C CA  . GLU A 93  ? 0.3457 0.3886 0.3499 -0.0284 0.0260  -0.0341 93  GLU A CA  
794  C C   . GLU A 93  ? 0.2982 0.3405 0.3060 -0.0282 0.0231  -0.0279 93  GLU A C   
795  O O   . GLU A 93  ? 0.3439 0.3773 0.3533 -0.0286 0.0230  -0.0281 93  GLU A O   
796  C CB  . GLU A 93  ? 0.3282 0.3788 0.3265 -0.0345 0.0252  -0.0378 93  GLU A CB  
797  C CG  . GLU A 93  ? 0.4935 0.5425 0.4867 -0.0360 0.0285  -0.0454 93  GLU A CG  
798  C CD  . GLU A 93  ? 0.5968 0.6575 0.5835 -0.0414 0.0272  -0.0477 93  GLU A CD  
799  O OE1 . GLU A 93  ? 0.6365 0.7066 0.6235 -0.0439 0.0236  -0.0429 93  GLU A OE1 
800  O OE2 . GLU A 93  ? 0.6215 0.6822 0.6028 -0.0432 0.0299  -0.0541 93  GLU A OE2 
801  N N   . LYS A 94  ? 0.2962 0.3475 0.3054 -0.0273 0.0213  -0.0223 94  LYS A N   
802  C CA  . LYS A 94  ? 0.3888 0.4393 0.4011 -0.0271 0.0193  -0.0165 94  LYS A CA  
803  C C   . LYS A 94  ? 0.3336 0.3747 0.3494 -0.0229 0.0198  -0.0146 94  LYS A C   
804  O O   . LYS A 94  ? 0.3086 0.3438 0.3257 -0.0235 0.0188  -0.0124 94  LYS A O   
805  C CB  . LYS A 94  ? 0.4760 0.5374 0.4896 -0.0264 0.0184  -0.0109 94  LYS A CB  
806  C CG  . LYS A 94  ? 0.5468 0.6177 0.5588 -0.0309 0.0170  -0.0092 94  LYS A CG  
807  C CD  . LYS A 94  ? 0.6572 0.7311 0.6643 -0.0351 0.0169  -0.0151 94  LYS A CD  
808  C CE  . LYS A 94  ? 0.6824 0.7710 0.6876 -0.0373 0.0161  -0.0131 94  LYS A CE  
809  N NZ  . LYS A 94  ? 0.6687 0.7605 0.6678 -0.0421 0.0160  -0.0195 94  LYS A NZ  
810  N N   . LEU A 95  ? 0.3042 0.3443 0.3216 -0.0189 0.0211  -0.0152 95  LEU A N   
811  C CA  . LEU A 95  ? 0.3152 0.3479 0.3362 -0.0150 0.0213  -0.0130 95  LEU A CA  
812  C C   . LEU A 95  ? 0.2846 0.3067 0.3060 -0.0154 0.0224  -0.0160 95  LEU A C   
813  O O   . LEU A 95  ? 0.2680 0.2839 0.2915 -0.0142 0.0216  -0.0131 95  LEU A O   
814  C CB  . LEU A 95  ? 0.2769 0.3123 0.3002 -0.0110 0.0226  -0.0130 95  LEU A CB  
815  C CG  . LEU A 95  ? 0.5015 0.5312 0.5292 -0.0068 0.0228  -0.0110 95  LEU A CG  
816  C CD1 . LEU A 95  ? 0.5193 0.5480 0.5483 -0.0065 0.0204  -0.0057 95  LEU A CD1 
817  C CD2 . LEU A 95  ? 0.5614 0.5955 0.5917 -0.0033 0.0243  -0.0111 95  LEU A CD2 
818  N N   . ILE A 96  ? 0.2578 0.2776 0.2770 -0.0170 0.0247  -0.0219 96  ILE A N   
819  C CA  . ILE A 96  ? 0.3343 0.3434 0.3544 -0.0175 0.0267  -0.0252 96  ILE A CA  
820  C C   . ILE A 96  ? 0.3240 0.3302 0.3430 -0.0215 0.0250  -0.0244 96  ILE A C   
821  O O   . ILE A 96  ? 0.3293 0.3271 0.3508 -0.0205 0.0254  -0.0229 96  ILE A O   
822  C CB  . ILE A 96  ? 0.3105 0.3178 0.3280 -0.0189 0.0302  -0.0323 96  ILE A CB  
823  C CG1 . ILE A 96  ? 0.3036 0.3115 0.3235 -0.0140 0.0326  -0.0326 96  ILE A CG1 
824  C CG2 . ILE A 96  ? 0.3278 0.3240 0.3457 -0.0208 0.0328  -0.0365 96  ILE A CG2 
825  C CD1 . ILE A 96  ? 0.3202 0.3268 0.3370 -0.0153 0.0367  -0.0397 96  ILE A CD1 
826  N N   . GLU A 97  ? 0.3225 0.3361 0.3381 -0.0259 0.0233  -0.0249 97  GLU A N   
827  C CA  . GLU A 97  ? 0.3305 0.3421 0.3457 -0.0298 0.0217  -0.0238 97  GLU A CA  
828  C C   . GLU A 97  ? 0.2785 0.2875 0.2968 -0.0274 0.0201  -0.0173 97  GLU A C   
829  O O   . GLU A 97  ? 0.2624 0.2639 0.2820 -0.0282 0.0202  -0.0164 97  GLU A O   
830  C CB  . GLU A 97  ? 0.3979 0.4201 0.4100 -0.0347 0.0198  -0.0241 97  GLU A CB  
831  C CG  . GLU A 97  ? 0.5618 0.5868 0.5695 -0.0387 0.0211  -0.0311 97  GLU A CG  
832  C CD  . GLU A 97  ? 0.7077 0.7467 0.7124 -0.0414 0.0192  -0.0300 97  GLU A CD  
833  O OE1 . GLU A 97  ? 0.7436 0.7868 0.7439 -0.0462 0.0193  -0.0351 97  GLU A OE1 
834  O OE2 . GLU A 97  ? 0.7482 0.7943 0.7549 -0.0388 0.0178  -0.0241 97  GLU A OE2 
835  N N   . PHE A 98  ? 0.3128 0.3276 0.3319 -0.0246 0.0190  -0.0129 98  PHE A N   
836  C CA  . PHE A 98  ? 0.2735 0.2860 0.2944 -0.0227 0.0177  -0.0071 98  PHE A CA  
837  C C   . PHE A 98  ? 0.3112 0.3142 0.3344 -0.0194 0.0185  -0.0064 98  PHE A C   
838  O O   . PHE A 98  ? 0.2870 0.2847 0.3107 -0.0196 0.0179  -0.0033 98  PHE A O   
839  C CB  . PHE A 98  ? 0.2626 0.2827 0.2840 -0.0206 0.0170  -0.0035 98  PHE A CB  
840  C CG  . PHE A 98  ? 0.2873 0.3060 0.3094 -0.0198 0.0161  0.0019  98  PHE A CG  
841  C CD1 . PHE A 98  ? 0.2845 0.3057 0.3061 -0.0225 0.0157  0.0048  98  PHE A CD1 
842  C CD2 . PHE A 98  ? 0.2987 0.3140 0.3220 -0.0165 0.0158  0.0041  98  PHE A CD2 
843  C CE1 . PHE A 98  ? 0.2761 0.2952 0.2979 -0.0219 0.0156  0.0093  98  PHE A CE1 
844  C CE2 . PHE A 98  ? 0.3101 0.3240 0.3330 -0.0164 0.0151  0.0085  98  PHE A CE2 
845  C CZ  . PHE A 98  ? 0.2723 0.2875 0.2941 -0.0191 0.0153  0.0109  98  PHE A CZ  
846  N N   . THR A 99  ? 0.2704 0.2717 0.2951 -0.0163 0.0199  -0.0085 99  THR A N   
847  C CA  . THR A 99  ? 0.2663 0.2594 0.2942 -0.0130 0.0209  -0.0073 99  THR A CA  
848  C C   . THR A 99  ? 0.2741 0.2585 0.3024 -0.0151 0.0223  -0.0093 99  THR A C   
849  O O   . THR A 99  ? 0.2820 0.2603 0.3122 -0.0138 0.0221  -0.0058 99  THR A O   
850  C CB  . THR A 99  ? 0.2955 0.2884 0.3258 -0.0096 0.0230  -0.0097 99  THR A CB  
851  O OG1 . THR A 99  ? 0.2778 0.2790 0.3080 -0.0080 0.0218  -0.0081 99  THR A OG1 
852  C CG2 . THR A 99  ? 0.3211 0.3068 0.3559 -0.0057 0.0240  -0.0071 99  THR A CG2 
853  N N   . LYS A 100 ? 0.2716 0.2554 0.2981 -0.0185 0.0240  -0.0149 100 LYS A N   
854  C CA  . LYS A 100 ? 0.2920 0.2674 0.3193 -0.0211 0.0258  -0.0177 100 LYS A CA  
855  C C   . LYS A 100 ? 0.3962 0.3706 0.4231 -0.0235 0.0238  -0.0139 100 LYS A C   
856  O O   . LYS A 100 ? 0.3792 0.3452 0.4082 -0.0236 0.0250  -0.0132 100 LYS A O   
857  C CB  . LYS A 100 ? 0.3659 0.3425 0.3902 -0.0256 0.0275  -0.0248 100 LYS A CB  
858  C CG  . LYS A 100 ? 0.4997 0.4710 0.5250 -0.0239 0.0316  -0.0301 100 LYS A CG  
859  C CD  . LYS A 100 ? 0.6225 0.5947 0.6436 -0.0293 0.0334  -0.0380 100 LYS A CD  
860  C CE  . LYS A 100 ? 0.7385 0.7136 0.7571 -0.0355 0.0309  -0.0386 100 LYS A CE  
861  N NZ  . LYS A 100 ? 0.7881 0.7538 0.8100 -0.0364 0.0317  -0.0373 100 LYS A NZ  
862  N N   . LEU A 101 ? 0.3450 0.3276 0.3697 -0.0252 0.0211  -0.0112 101 LEU A N   
863  C CA  . LEU A 101 ? 0.3691 0.3510 0.3936 -0.0273 0.0197  -0.0072 101 LEU A CA  
864  C C   . LEU A 101 ? 0.3605 0.3368 0.3866 -0.0237 0.0194  -0.0018 101 LEU A C   
865  O O   . LEU A 101 ? 0.3476 0.3183 0.3745 -0.0247 0.0196  0.0004  101 LEU A O   
866  C CB  . LEU A 101 ? 0.3326 0.3247 0.3552 -0.0293 0.0177  -0.0048 101 LEU A CB  
867  C CG  . LEU A 101 ? 0.4263 0.4189 0.4492 -0.0310 0.0168  0.0001  101 LEU A CG  
868  C CD1 . LEU A 101 ? 0.4702 0.4602 0.4938 -0.0355 0.0170  -0.0018 101 LEU A CD1 
869  C CD2 . LEU A 101 ? 0.3864 0.3888 0.4085 -0.0315 0.0157  0.0033  101 LEU A CD2 
870  N N   . ASN A 102 ? 0.2432 0.2213 0.2697 -0.0197 0.0189  0.0003  102 ASN A N   
871  C CA  . ASN A 102 ? 0.2964 0.2712 0.3235 -0.0168 0.0181  0.0056  102 ASN A CA  
872  C C   . ASN A 102 ? 0.2827 0.2505 0.3131 -0.0133 0.0195  0.0060  102 ASN A C   
873  O O   . ASN A 102 ? 0.2384 0.2041 0.2694 -0.0107 0.0186  0.0108  102 ASN A O   
874  C CB  . ASN A 102 ? 0.2984 0.2803 0.3240 -0.0152 0.0163  0.0083  102 ASN A CB  
875  C CG  . ASN A 102 ? 0.2973 0.2851 0.3204 -0.0181 0.0156  0.0095  102 ASN A CG  
876  O OD1 . ASN A 102 ? 0.3875 0.3730 0.4095 -0.0197 0.0155  0.0125  102 ASN A OD1 
877  N ND2 . ASN A 102 ? 0.2598 0.2553 0.2826 -0.0187 0.0155  0.0076  102 ASN A ND2 
878  N N   . TYR A 103 ? 0.3303 0.2945 0.3630 -0.0133 0.0220  0.0014  103 TYR A N   
879  C CA  . TYR A 103 ? 0.4043 0.3633 0.4413 -0.0092 0.0241  0.0016  103 TYR A CA  
880  C C   . TYR A 103 ? 0.3571 0.3090 0.3968 -0.0072 0.0246  0.0066  103 TYR A C   
881  O O   . TYR A 103 ? 0.3146 0.2654 0.3576 -0.0030 0.0248  0.0103  103 TYR A O   
882  C CB  . TYR A 103 ? 0.3595 0.3146 0.3979 -0.0105 0.0278  -0.0050 103 TYR A CB  
883  C CG  . TYR A 103 ? 0.4421 0.3913 0.4859 -0.0063 0.0312  -0.0051 103 TYR A CG  
884  C CD1 . TYR A 103 ? 0.4675 0.4208 0.5130 -0.0030 0.0318  -0.0055 103 TYR A CD1 
885  C CD2 . TYR A 103 ? 0.4481 0.3875 0.4959 -0.0055 0.0344  -0.0045 103 TYR A CD2 
886  C CE1 . TYR A 103 ? 0.4679 0.4160 0.5193 0.0012  0.0355  -0.0050 103 TYR A CE1 
887  C CE2 . TYR A 103 ? 0.4998 0.4337 0.5536 -0.0013 0.0382  -0.0040 103 TYR A CE2 
888  C CZ  . TYR A 103 ? 0.5070 0.4454 0.5626 0.0021  0.0388  -0.0041 103 TYR A CZ  
889  O OH  . TYR A 103 ? 0.6031 0.5363 0.6655 0.0065  0.0431  -0.0030 103 TYR A OH  
890  N N   . GLU A 104 ? 0.2929 0.2403 0.3316 -0.0100 0.0248  0.0071  104 GLU A N   
891  C CA  . GLU A 104 ? 0.3488 0.2890 0.3902 -0.0081 0.0258  0.0117  104 GLU A CA  
892  C C   . GLU A 104 ? 0.3867 0.3295 0.4251 -0.0073 0.0228  0.0181  104 GLU A C   
893  O O   . GLU A 104 ? 0.3409 0.2785 0.3806 -0.0059 0.0233  0.0226  104 GLU A O   
894  C CB  . GLU A 104 ? 0.3867 0.3196 0.4293 -0.0114 0.0283  0.0089  104 GLU A CB  
895  C CG  . GLU A 104 ? 0.4536 0.3820 0.4990 -0.0127 0.0321  0.0021  104 GLU A CG  
896  C CD  . GLU A 104 ? 0.5652 0.4868 0.6166 -0.0081 0.0357  0.0033  104 GLU A CD  
897  O OE1 . GLU A 104 ? 0.5880 0.5076 0.6420 -0.0044 0.0353  0.0101  104 GLU A OE1 
898  O OE2 . GLU A 104 ? 0.6109 0.5294 0.6645 -0.0082 0.0393  -0.0022 104 GLU A OE2 
899  N N   . LYS A 105 ? 0.3012 0.2517 0.3353 -0.0084 0.0201  0.0186  105 LYS A N   
900  C CA  . LYS A 105 ? 0.2615 0.2140 0.2920 -0.0082 0.0177  0.0239  105 LYS A CA  
901  C C   . LYS A 105 ? 0.2790 0.2328 0.3110 -0.0042 0.0164  0.0283  105 LYS A C   
902  O O   . LYS A 105 ? 0.2920 0.2491 0.3269 -0.0019 0.0164  0.0271  105 LYS A O   
903  C CB  . LYS A 105 ? 0.2502 0.2100 0.2764 -0.0107 0.0160  0.0228  105 LYS A CB  
904  C CG  . LYS A 105 ? 0.2647 0.2244 0.2897 -0.0147 0.0169  0.0204  105 LYS A CG  
905  C CD  . LYS A 105 ? 0.2908 0.2584 0.3134 -0.0166 0.0159  0.0190  105 LYS A CD  
906  C CE  . LYS A 105 ? 0.2944 0.2627 0.3166 -0.0206 0.0167  0.0180  105 LYS A CE  
907  N NZ  . LYS A 105 ? 0.2698 0.2456 0.2900 -0.0220 0.0162  0.0188  105 LYS A NZ  
908  N N   . PRO A 106 ? 0.3376 0.2895 0.3677 -0.0034 0.0154  0.0338  106 PRO A N   
909  C CA  . PRO A 106 ? 0.2317 0.1863 0.2631 0.0000  0.0136  0.0387  106 PRO A CA  
910  C C   . PRO A 106 ? 0.3358 0.2990 0.3656 0.0002  0.0110  0.0382  106 PRO A C   
911  O O   . PRO A 106 ? 0.3645 0.3310 0.3981 0.0033  0.0102  0.0401  106 PRO A O   
912  C CB  . PRO A 106 ? 0.3270 0.2791 0.3541 -0.0007 0.0125  0.0441  106 PRO A CB  
913  C CG  . PRO A 106 ? 0.3182 0.2631 0.3453 -0.0029 0.0152  0.0424  106 PRO A CG  
914  C CD  . PRO A 106 ? 0.3401 0.2866 0.3676 -0.0055 0.0161  0.0360  106 PRO A CD  
915  N N   . ILE A 107 ? 0.2740 0.2409 0.2989 -0.0030 0.0101  0.0358  107 ILE A N   
916  C CA  . ILE A 107 ? 0.2878 0.2625 0.3117 -0.0029 0.0081  0.0351  107 ILE A CA  
917  C C   . ILE A 107 ? 0.2994 0.2770 0.3283 -0.0011 0.0092  0.0313  107 ILE A C   
918  O O   . ILE A 107 ? 0.2454 0.2293 0.2754 -0.0001 0.0077  0.0314  107 ILE A O   
919  C CB  . ILE A 107 ? 0.3185 0.2959 0.3368 -0.0066 0.0079  0.0336  107 ILE A CB  
920  C CG1 . ILE A 107 ? 0.2958 0.2716 0.3145 -0.0087 0.0101  0.0295  107 ILE A CG1 
921  C CG2 . ILE A 107 ? 0.3221 0.2970 0.3349 -0.0083 0.0071  0.0374  107 ILE A CG2 
922  C CD1 . ILE A 107 ? 0.2994 0.2798 0.3149 -0.0114 0.0103  0.0281  107 ILE A CD1 
923  N N   . TYR A 108 ? 0.2895 0.2625 0.3214 -0.0009 0.0118  0.0278  108 TYR A N   
924  C CA  . TYR A 108 ? 0.2781 0.2528 0.3142 0.0008  0.0135  0.0239  108 TYR A CA  
925  C C   . TYR A 108 ? 0.2994 0.2706 0.3418 0.0049  0.0151  0.0259  108 TYR A C   
926  O O   . TYR A 108 ? 0.2943 0.2649 0.3407 0.0064  0.0176  0.0225  108 TYR A O   
927  C CB  . TYR A 108 ? 0.2784 0.2508 0.3136 -0.0020 0.0158  0.0182  108 TYR A CB  
928  C CG  . TYR A 108 ? 0.2595 0.2389 0.2914 -0.0045 0.0149  0.0154  108 TYR A CG  
929  C CD1 . TYR A 108 ? 0.3213 0.3031 0.3489 -0.0071 0.0134  0.0173  108 TYR A CD1 
930  C CD2 . TYR A 108 ? 0.3636 0.3471 0.3968 -0.0042 0.0160  0.0113  108 TYR A CD2 
931  C CE1 . TYR A 108 ? 0.2263 0.2146 0.2519 -0.0091 0.0131  0.0156  108 TYR A CE1 
932  C CE2 . TYR A 108 ? 0.3149 0.3055 0.3455 -0.0062 0.0153  0.0095  108 TYR A CE2 
933  C CZ  . TYR A 108 ? 0.2671 0.2600 0.2943 -0.0086 0.0139  0.0119  108 TYR A CZ  
934  O OH  . TYR A 108 ? 0.2952 0.2950 0.3209 -0.0103 0.0139  0.0109  108 TYR A OH  
935  N N   . ARG A 109 ? 0.2604 0.2298 0.3041 0.0068  0.0140  0.0317  109 ARG A N   
936  C CA  . ARG A 109 ? 0.3515 0.3177 0.4023 0.0110  0.0160  0.0347  109 ARG A CA  
937  C C   . ARG A 109 ? 0.3932 0.3670 0.4477 0.0140  0.0143  0.0372  109 ARG A C   
938  O O   . ARG A 109 ? 0.3938 0.3721 0.4490 0.0155  0.0114  0.0432  109 ARG A O   
939  C CB  . ARG A 109 ? 0.4329 0.3947 0.4842 0.0120  0.0156  0.0407  109 ARG A CB  
940  C CG  . ARG A 109 ? 0.5774 0.5325 0.6365 0.0157  0.0196  0.0425  109 ARG A CG  
941  C CD  . ARG A 109 ? 0.6925 0.6431 0.7518 0.0165  0.0195  0.0487  109 ARG A CD  
942  N NE  . ARG A 109 ? 0.6854 0.6306 0.7392 0.0126  0.0200  0.0460  109 ARG A NE  
943  C CZ  . ARG A 109 ? 0.6203 0.5643 0.6701 0.0115  0.0184  0.0505  109 ARG A CZ  
944  N NH1 . ARG A 109 ? 0.6485 0.5967 0.6981 0.0137  0.0158  0.0577  109 ARG A NH1 
945  N NH2 . ARG A 109 ? 0.5340 0.4731 0.5798 0.0080  0.0193  0.0481  109 ARG A NH2 
946  N N   . PHE A 110 ? 0.3118 0.2875 0.3687 0.0146  0.0162  0.0325  110 PHE A N   
947  C CA  . PHE A 110 ? 0.2843 0.2659 0.3469 0.0181  0.0161  0.0343  110 PHE A CA  
948  C C   . PHE A 110 ? 0.3213 0.2972 0.3905 0.0211  0.0214  0.0316  110 PHE A C   
949  O O   . PHE A 110 ? 0.3711 0.3426 0.4381 0.0190  0.0244  0.0250  110 PHE A O   
950  C CB  . PHE A 110 ? 0.2580 0.2473 0.3175 0.0163  0.0144  0.0308  110 PHE A CB  
951  C CG  . PHE A 110 ? 0.2785 0.2730 0.3317 0.0131  0.0101  0.0325  110 PHE A CG  
952  C CD1 . PHE A 110 ? 0.3673 0.3594 0.4138 0.0091  0.0099  0.0296  110 PHE A CD1 
953  C CD2 . PHE A 110 ? 0.3147 0.3167 0.3689 0.0138  0.0067  0.0369  110 PHE A CD2 
954  C CE1 . PHE A 110 ? 0.4598 0.4558 0.5007 0.0062  0.0070  0.0310  110 PHE A CE1 
955  C CE2 . PHE A 110 ? 0.3155 0.3215 0.3635 0.0103  0.0035  0.0377  110 PHE A CE2 
956  C CZ  . PHE A 110 ? 0.4136 0.4162 0.4550 0.0067  0.0040  0.0347  110 PHE A CZ  
957  N N   . GLU A 111 ? 0.4006 0.3768 0.4779 0.0257  0.0227  0.0368  111 GLU A N   
958  C CA  . GLU A 111 ? 0.4051 0.3748 0.4894 0.0289  0.0288  0.0345  111 GLU A CA  
959  C C   . GLU A 111 ? 0.3572 0.3287 0.4403 0.0281  0.0311  0.0274  111 GLU A C   
960  O O   . GLU A 111 ? 0.3579 0.3222 0.4417 0.0277  0.0362  0.0216  111 GLU A O   
961  C CB  . GLU A 111 ? 0.4615 0.4334 0.5558 0.0345  0.0298  0.0424  111 GLU A CB  
962  C CG  . GLU A 111 ? 0.5762 0.5416 0.6790 0.0385  0.0369  0.0407  111 GLU A CG  
963  C CD  . GLU A 111 ? 0.7312 0.6845 0.8360 0.0386  0.0421  0.0392  111 GLU A CD  
964  O OE1 . GLU A 111 ? 0.7754 0.7269 0.8813 0.0392  0.0407  0.0451  111 GLU A OE1 
965  O OE2 . GLU A 111 ? 0.7855 0.7312 0.8908 0.0378  0.0478  0.0320  111 GLU A OE2 
966  N N   . ARG A 112 ? 0.2147 0.1955 0.2957 0.0275  0.0275  0.0276  112 ARG A N   
967  C CA  . ARG A 112 ? 0.3187 0.3019 0.3986 0.0270  0.0297  0.0215  112 ARG A CA  
968  C C   . ARG A 112 ? 0.3610 0.3403 0.4333 0.0223  0.0309  0.0139  112 ARG A C   
969  O O   . ARG A 112 ? 0.3572 0.3346 0.4288 0.0219  0.0347  0.0080  112 ARG A O   
970  C CB  . ARG A 112 ? 0.2615 0.2555 0.3407 0.0269  0.0256  0.0236  112 ARG A CB  
971  C CG  . ARG A 112 ? 0.3260 0.3235 0.4043 0.0266  0.0277  0.0181  112 ARG A CG  
972  C CD  . ARG A 112 ? 0.3445 0.3383 0.4299 0.0307  0.0335  0.0168  112 ARG A CD  
973  N NE  . ARG A 112 ? 0.4120 0.4115 0.4976 0.0313  0.0348  0.0136  112 ARG A NE  
974  C CZ  . ARG A 112 ? 0.3599 0.3567 0.4497 0.0341  0.0403  0.0108  112 ARG A CZ  
975  N NH1 . ARG A 112 ? 0.3455 0.3333 0.4400 0.0365  0.0455  0.0105  112 ARG A NH1 
976  N NH2 . ARG A 112 ? 0.3008 0.3033 0.3901 0.0344  0.0413  0.0082  112 ARG A NH2 
977  N N   . ILE A 113 ? 0.3360 0.3141 0.4023 0.0186  0.0280  0.0141  113 ILE A N   
978  C CA  . ILE A 113 ? 0.3216 0.2967 0.3815 0.0140  0.0289  0.0077  113 ILE A CA  
979  C C   . ILE A 113 ? 0.3523 0.3175 0.4142 0.0138  0.0341  0.0035  113 ILE A C   
980  O O   . ILE A 113 ? 0.3963 0.3598 0.4550 0.0111  0.0367  -0.0033 113 ILE A O   
981  C CB  . ILE A 113 ? 0.3072 0.2833 0.3614 0.0104  0.0250  0.0097  113 ILE A CB  
982  C CG1 . ILE A 113 ? 0.3264 0.3118 0.3774 0.0094  0.0210  0.0116  113 ILE A CG1 
983  C CG2 . ILE A 113 ? 0.3385 0.3106 0.3879 0.0059  0.0263  0.0041  113 ILE A CG2 
984  C CD1 . ILE A 113 ? 0.3440 0.3300 0.3894 0.0059  0.0180  0.0134  113 ILE A CD1 
985  N N   . ARG A 114 ? 0.3273 0.2859 0.3945 0.0165  0.0359  0.0075  114 ARG A N   
986  C CA  . ARG A 114 ? 0.3537 0.3019 0.4242 0.0167  0.0418  0.0037  114 ARG A CA  
987  C C   . ARG A 114 ? 0.4119 0.3589 0.4854 0.0186  0.0468  -0.0009 114 ARG A C   
988  O O   . ARG A 114 ? 0.4757 0.4163 0.5473 0.0161  0.0513  -0.0080 114 ARG A O   
989  C CB  . ARG A 114 ? 0.4003 0.3427 0.4777 0.0203  0.0433  0.0103  114 ARG A CB  
990  C CG  . ARG A 114 ? 0.5192 0.4642 0.5941 0.0196  0.0382  0.0167  114 ARG A CG  
991  C CD  . ARG A 114 ? 0.6427 0.5794 0.7226 0.0215  0.0407  0.0211  114 ARG A CD  
992  N NE  . ARG A 114 ? 0.7543 0.6947 0.8401 0.0264  0.0391  0.0303  114 ARG A NE  
993  C CZ  . ARG A 114 ? 0.7833 0.7295 0.8660 0.0260  0.0337  0.0365  114 ARG A CZ  
994  N NH1 . ARG A 114 ? 0.7678 0.7159 0.8420 0.0215  0.0300  0.0343  114 ARG A NH1 
995  N NH2 . ARG A 114 ? 0.8305 0.7809 0.9186 0.0302  0.0321  0.0449  114 ARG A NH2 
996  N N   . GLU A 115 ? 0.4440 0.3972 0.5221 0.0229  0.0463  0.0030  115 GLU A N   
997  C CA  . GLU A 115 ? 0.4419 0.3940 0.5234 0.0252  0.0515  -0.0008 115 GLU A CA  
998  C C   . GLU A 115 ? 0.4147 0.3704 0.4883 0.0210  0.0514  -0.0087 115 GLU A C   
999  O O   . GLU A 115 ? 0.3931 0.3434 0.4655 0.0199  0.0568  -0.0155 115 GLU A O   
1000 C CB  . GLU A 115 ? 0.5076 0.4668 0.5964 0.0306  0.0504  0.0058  115 GLU A CB  
1001 C CG  . GLU A 115 ? 0.5341 0.4917 0.6315 0.0351  0.0504  0.0145  115 GLU A CG  
1002 C CD  . GLU A 115 ? 0.6337 0.6011 0.7375 0.0394  0.0477  0.0215  115 GLU A CD  
1003 O OE1 . GLU A 115 ? 0.6370 0.6103 0.7397 0.0394  0.0476  0.0188  115 GLU A OE1 
1004 O OE2 . GLU A 115 ? 0.6708 0.6405 0.7806 0.0425  0.0457  0.0299  115 GLU A OE2 
1005 N N   . LEU A 116 ? 0.3813 0.3462 0.4494 0.0186  0.0456  -0.0077 116 LEU A N   
1006 C CA  . LEU A 116 ? 0.4143 0.3844 0.4755 0.0151  0.0452  -0.0137 116 LEU A CA  
1007 C C   . LEU A 116 ? 0.4424 0.4070 0.4973 0.0097  0.0470  -0.0207 116 LEU A C   
1008 O O   . LEU A 116 ? 0.4323 0.3972 0.4832 0.0074  0.0498  -0.0273 116 LEU A O   
1009 C CB  . LEU A 116 ? 0.3971 0.3775 0.4547 0.0137  0.0391  -0.0103 116 LEU A CB  
1010 C CG  . LEU A 116 ? 0.4159 0.4033 0.4790 0.0180  0.0369  -0.0041 116 LEU A CG  
1011 C CD1 . LEU A 116 ? 0.3799 0.3760 0.4391 0.0159  0.0312  -0.0011 116 LEU A CD1 
1012 C CD2 . LEU A 116 ? 0.3883 0.3780 0.4545 0.0209  0.0407  -0.0065 116 LEU A CD2 
1013 N N   . MET A 117 ? 0.4728 0.4331 0.5265 0.0073  0.0452  -0.0193 117 MET A N   
1014 C CA  . MET A 117 ? 0.5425 0.4983 0.5909 0.0017  0.0464  -0.0256 117 MET A CA  
1015 C C   . MET A 117 ? 0.5321 0.4768 0.5830 0.0016  0.0532  -0.0309 117 MET A C   
1016 O O   . MET A 117 ? 0.5268 0.4675 0.5731 -0.0037 0.0548  -0.0373 117 MET A O   
1017 C CB  . MET A 117 ? 0.4780 0.4329 0.5248 -0.0009 0.0425  -0.0221 117 MET A CB  
1018 C CG  . MET A 117 ? 0.5097 0.4747 0.5533 -0.0015 0.0366  -0.0176 117 MET A CG  
1019 S SD  . MET A 117 ? 0.5352 0.5094 0.5712 -0.0067 0.0346  -0.0225 117 MET A SD  
1020 C CE  . MET A 117 ? 0.5351 0.5167 0.5725 -0.0027 0.0354  -0.0223 117 MET A CE  
1021 N N   . ASN A 118 ? 0.4824 0.4221 0.5408 0.0070  0.0574  -0.0284 118 ASN A N   
1022 C CA  . ASN A 118 ? 0.5890 0.5175 0.6507 0.0074  0.0651  -0.0334 118 ASN A CA  
1023 C C   . ASN A 118 ? 0.6346 0.5639 0.6960 0.0089  0.0698  -0.0381 118 ASN A C   
1024 O O   . ASN A 118 ? 0.6792 0.5990 0.7442 0.0101  0.0772  -0.0420 118 ASN A O   
1025 C CB  . ASN A 118 ? 0.6785 0.5995 0.7499 0.0126  0.0679  -0.0269 118 ASN A CB  
1026 C CG  . ASN A 118 ? 0.7859 0.7019 0.8573 0.0102  0.0660  -0.0246 118 ASN A CG  
1027 O OD1 . ASN A 118 ? 0.8581 0.7662 0.9368 0.0133  0.0695  -0.0208 118 ASN A OD1 
1028 N ND2 . ASN A 118 ? 0.8225 0.7434 0.8865 0.0050  0.0608  -0.0263 118 ASN A ND2 
1029 N N   . LYS A 119 ? 0.6229 0.5630 0.6805 0.0090  0.0661  -0.0378 119 LYS A N   
1030 C CA  . LYS A 119 ? 0.6439 0.5860 0.7006 0.0104  0.0702  -0.0420 119 LYS A CA  
1031 C C   . LYS A 119 ? 0.6374 0.5818 0.6837 0.0038  0.0705  -0.0507 119 LYS A C   
1032 O O   . LYS A 119 ? 0.5888 0.5393 0.6289 -0.0008 0.0650  -0.0511 119 LYS A O   
1033 C CB  . LYS A 119 ? 0.6283 0.5813 0.6879 0.0147  0.0664  -0.0358 119 LYS A CB  
1034 C CG  . LYS A 119 ? 0.6749 0.6278 0.7445 0.0207  0.0655  -0.0268 119 LYS A CG  
1035 C CD  . LYS A 119 ? 0.7066 0.6695 0.7798 0.0247  0.0628  -0.0216 119 LYS A CD  
1036 C CE  . LYS A 119 ? 0.7280 0.6879 0.8124 0.0313  0.0671  -0.0164 119 LYS A CE  
1037 N NZ  . LYS A 119 ? 0.7461 0.7129 0.8338 0.0348  0.0684  -0.0154 119 LYS A NZ  
1038 N N   . GLU A 120 ? 0.6550 0.5947 0.6995 0.0034  0.0771  -0.0576 120 GLU A N   
1039 C CA  . GLU A 120 ? 0.7015 0.6435 0.7355 -0.0033 0.0778  -0.0663 120 GLU A CA  
1040 C C   . GLU A 120 ? 0.6473 0.6037 0.6761 -0.0040 0.0722  -0.0645 120 GLU A C   
1041 O O   . GLU A 120 ? 0.5970 0.5601 0.6185 -0.0095 0.0677  -0.0663 120 GLU A O   
1042 C CB  . GLU A 120 ? 0.7699 0.7030 0.8030 -0.0034 0.0869  -0.0741 120 GLU A CB  
1043 C CG  . GLU A 120 ? 0.8202 0.7392 0.8623 0.0004  0.0938  -0.0734 120 GLU A CG  
1044 C CD  . GLU A 120 ? 0.8935 0.8028 0.9352 0.0006  0.1040  -0.0811 120 GLU A CD  
1045 O OE1 . GLU A 120 ? 0.9032 0.8126 0.9348 -0.0056 0.1059  -0.0903 120 GLU A OE1 
1046 O OE2 . GLU A 120 ? 0.9321 0.8338 0.9837 0.0068  0.1102  -0.0779 120 GLU A OE2 
1047 N N   . LYS A 121 ? 0.6463 0.6078 0.6795 0.0015  0.0727  -0.0603 121 LYS A N   
1048 C CA  . LYS A 121 ? 0.6266 0.6012 0.6566 0.0018  0.0681  -0.0576 121 LYS A CA  
1049 C C   . LYS A 121 ? 0.5708 0.5502 0.6093 0.0078  0.0647  -0.0484 121 LYS A C   
1050 O O   . LYS A 121 ? 0.5356 0.5088 0.5825 0.0125  0.0672  -0.0447 121 LYS A O   
1051 C CB  . LYS A 121 ? 0.6744 0.6515 0.7001 0.0018  0.0729  -0.0631 121 LYS A CB  
1052 C CG  . LYS A 121 ? 0.6905 0.6793 0.7072 -0.0027 0.0691  -0.0651 121 LYS A CG  
1053 C CD  . LYS A 121 ? 0.7687 0.7594 0.7807 -0.0025 0.0743  -0.0705 121 LYS A CD  
1054 C CE  . LYS A 121 ? 0.8538 0.8431 0.8746 0.0050  0.0782  -0.0666 121 LYS A CE  
1055 N NZ  . LYS A 121 ? 0.9189 0.9190 0.9448 0.0088  0.0727  -0.0582 121 LYS A NZ  
1056 N N   . LEU A 122 ? 0.5184 0.5090 0.5550 0.0074  0.0592  -0.0445 122 LEU A N   
1057 C CA  . LEU A 122 ? 0.4521 0.4480 0.4957 0.0120  0.0556  -0.0363 122 LEU A CA  
1058 C C   . LEU A 122 ? 0.4420 0.4474 0.4860 0.0142  0.0556  -0.0352 122 LEU A C   
1059 O O   . LEU A 122 ? 0.3667 0.3790 0.4039 0.0110  0.0545  -0.0380 122 LEU A O   
1060 C CB  . LEU A 122 ? 0.5192 0.5190 0.5615 0.0097  0.0490  -0.0318 122 LEU A CB  
1061 C CG  . LEU A 122 ? 0.5509 0.5424 0.5919 0.0067  0.0487  -0.0331 122 LEU A CG  
1062 C CD1 . LEU A 122 ? 0.5909 0.5878 0.6266 0.0022  0.0433  -0.0319 122 LEU A CD1 
1063 C CD2 . LEU A 122 ? 0.5336 0.5187 0.5825 0.0109  0.0489  -0.0277 122 LEU A CD2 
1064 N N   . ASN A 123 ? 0.3705 0.3769 0.4227 0.0197  0.0568  -0.0306 123 ASN A N   
1065 C CA  . ASN A 123 ? 0.3723 0.3876 0.4263 0.0222  0.0569  -0.0287 123 ASN A CA  
1066 C C   . ASN A 123 ? 0.3466 0.3709 0.4019 0.0219  0.0505  -0.0227 123 ASN A C   
1067 O O   . ASN A 123 ? 0.3457 0.3692 0.3992 0.0194  0.0463  -0.0207 123 ASN A O   
1068 C CB  . ASN A 123 ? 0.3636 0.3761 0.4265 0.0280  0.0617  -0.0267 123 ASN A CB  
1069 C CG  . ASN A 123 ? 0.3803 0.3895 0.4522 0.0316  0.0599  -0.0201 123 ASN A CG  
1070 O OD1 . ASN A 123 ? 0.3385 0.3505 0.4106 0.0303  0.0542  -0.0158 123 ASN A OD1 
1071 N ND2 . ASN A 123 ? 0.4166 0.4204 0.4964 0.0361  0.0652  -0.0190 123 ASN A ND2 
1072 N N   . ARG A 124 ? 0.3696 0.4020 0.4282 0.0244  0.0501  -0.0198 124 ARG A N   
1073 C CA  . ARG A 124 ? 0.3356 0.3763 0.3951 0.0236  0.0448  -0.0149 124 ARG A CA  
1074 C C   . ARG A 124 ? 0.3536 0.3926 0.4188 0.0250  0.0411  -0.0092 124 ARG A C   
1075 O O   . ARG A 124 ? 0.3220 0.3630 0.3847 0.0224  0.0367  -0.0069 124 ARG A O   
1076 C CB  . ARG A 124 ? 0.3434 0.3926 0.4061 0.0261  0.0459  -0.0132 124 ARG A CB  
1077 C CG  . ARG A 124 ? 0.3071 0.3645 0.3710 0.0251  0.0414  -0.0086 124 ARG A CG  
1078 C CD  . ARG A 124 ? 0.3894 0.4546 0.4580 0.0278  0.0429  -0.0067 124 ARG A CD  
1079 N NE  . ARG A 124 ? 0.3620 0.4342 0.4324 0.0266  0.0391  -0.0025 124 ARG A NE  
1080 C CZ  . ARG A 124 ? 0.4218 0.4951 0.4980 0.0275  0.0360  0.0021  124 ARG A CZ  
1081 N NH1 . ARG A 124 ? 0.4123 0.4813 0.4938 0.0300  0.0359  0.0039  124 ARG A NH1 
1082 N NH2 . ARG A 124 ? 0.4261 0.5052 0.5031 0.0257  0.0333  0.0050  124 ARG A NH2 
1083 N N   . GLU A 125 ? 0.3323 0.3680 0.4051 0.0291  0.0430  -0.0066 125 GLU A N   
1084 C CA  . GLU A 125 ? 0.3687 0.4034 0.4468 0.0304  0.0394  -0.0008 125 GLU A CA  
1085 C C   . GLU A 125 ? 0.3097 0.3374 0.3830 0.0274  0.0376  -0.0016 125 GLU A C   
1086 O O   . GLU A 125 ? 0.2729 0.3020 0.3460 0.0261  0.0330  0.0023  125 GLU A O   
1087 C CB  . GLU A 125 ? 0.3766 0.4087 0.4642 0.0355  0.0426  0.0023  125 GLU A CB  
1088 C CG  . GLU A 125 ? 0.5572 0.5956 0.6506 0.0389  0.0450  0.0034  125 GLU A CG  
1089 C CD  . GLU A 125 ? 0.6808 0.7212 0.7855 0.0436  0.0451  0.0100  125 GLU A CD  
1090 O OE1 . GLU A 125 ? 0.7067 0.7545 0.8172 0.0459  0.0452  0.0126  125 GLU A OE1 
1091 O OE2 . GLU A 125 ? 0.7335 0.7686 0.8420 0.0450  0.0451  0.0129  125 GLU A OE2 
1092 N N   . GLU A 126 ? 0.3073 0.3275 0.3770 0.0261  0.0413  -0.0069 126 GLU A N   
1093 C CA  . GLU A 126 ? 0.3404 0.3536 0.4066 0.0234  0.0400  -0.0076 126 GLU A CA  
1094 C C   . GLU A 126 ? 0.2202 0.2371 0.2788 0.0185  0.0360  -0.0087 126 GLU A C   
1095 O O   . GLU A 126 ? 0.2606 0.2750 0.3177 0.0167  0.0330  -0.0064 126 GLU A O   
1096 C CB  . GLU A 126 ? 0.3385 0.3422 0.4034 0.0231  0.0456  -0.0133 126 GLU A CB  
1097 C CG  . GLU A 126 ? 0.2894 0.2871 0.3631 0.0281  0.0497  -0.0108 126 GLU A CG  
1098 C CD  . GLU A 126 ? 0.3682 0.3587 0.4417 0.0287  0.0570  -0.0171 126 GLU A CD  
1099 O OE1 . GLU A 126 ? 0.3984 0.3895 0.4640 0.0250  0.0584  -0.0237 126 GLU A OE1 
1100 O OE2 . GLU A 126 ? 0.3956 0.3800 0.4767 0.0329  0.0617  -0.0153 126 GLU A OE2 
1101 N N   . LEU A 127 ? 0.2757 0.2987 0.3298 0.0166  0.0363  -0.0117 127 LEU A N   
1102 C CA  . LEU A 127 ? 0.3138 0.3414 0.3621 0.0124  0.0328  -0.0116 127 LEU A CA  
1103 C C   . LEU A 127 ? 0.2840 0.3167 0.3347 0.0128  0.0287  -0.0058 127 LEU A C   
1104 O O   . LEU A 127 ? 0.2777 0.3102 0.3252 0.0100  0.0258  -0.0042 127 LEU A O   
1105 C CB  . LEU A 127 ? 0.2728 0.3068 0.3165 0.0106  0.0343  -0.0153 127 LEU A CB  
1106 C CG  . LEU A 127 ? 0.2438 0.2733 0.2825 0.0082  0.0378  -0.0219 127 LEU A CG  
1107 C CD1 . LEU A 127 ? 0.3243 0.3611 0.3591 0.0073  0.0397  -0.0249 127 LEU A CD1 
1108 C CD2 . LEU A 127 ? 0.2924 0.3184 0.3263 0.0036  0.0358  -0.0234 127 LEU A CD2 
1109 N N   . LEU A 128 ? 0.2773 0.3143 0.3336 0.0161  0.0285  -0.0026 128 LEU A N   
1110 C CA  . LEU A 128 ? 0.2375 0.2792 0.2960 0.0160  0.0247  0.0024  128 LEU A CA  
1111 C C   . LEU A 128 ? 0.2165 0.2529 0.2754 0.0156  0.0221  0.0056  128 LEU A C   
1112 O O   . LEU A 128 ? 0.2884 0.3263 0.3449 0.0132  0.0190  0.0081  128 LEU A O   
1113 C CB  . LEU A 128 ? 0.2495 0.2968 0.3149 0.0195  0.0250  0.0052  128 LEU A CB  
1114 C CG  . LEU A 128 ? 0.3126 0.3684 0.3784 0.0191  0.0251  0.0054  128 LEU A CG  
1115 C CD1 . LEU A 128 ? 0.3174 0.3777 0.3910 0.0228  0.0260  0.0078  128 LEU A CD1 
1116 C CD2 . LEU A 128 ? 0.2654 0.3245 0.3286 0.0158  0.0218  0.0078  128 LEU A CD2 
1117 N N   . ASP A 129 ? 0.1860 0.2161 0.2480 0.0179  0.0238  0.0057  129 ASP A N   
1118 C CA  . ASP A 129 ? 0.2135 0.2384 0.2758 0.0176  0.0217  0.0089  129 ASP A CA  
1119 C C   . ASP A 129 ? 0.2494 0.2697 0.3049 0.0136  0.0210  0.0065  129 ASP A C   
1120 O O   . ASP A 129 ? 0.3267 0.3461 0.3800 0.0118  0.0181  0.0095  129 ASP A O   
1121 C CB  . ASP A 129 ? 0.2200 0.2389 0.2881 0.0213  0.0245  0.0098  129 ASP A CB  
1122 C CG  . ASP A 129 ? 0.3136 0.3374 0.3897 0.0253  0.0240  0.0146  129 ASP A CG  
1123 O OD1 . ASP A 129 ? 0.3187 0.3505 0.3956 0.0250  0.0219  0.0160  129 ASP A OD1 
1124 O OD2 . ASP A 129 ? 0.3113 0.3313 0.3937 0.0288  0.0259  0.0173  129 ASP A OD2 
1125 N N   . LEU A 130 ? 0.1877 0.2057 0.2397 0.0119  0.0237  0.0013  130 LEU A N   
1126 C CA  . LEU A 130 ? 0.2714 0.2860 0.3178 0.0079  0.0231  -0.0008 130 LEU A CA  
1127 C C   . LEU A 130 ? 0.2973 0.3178 0.3400 0.0051  0.0201  0.0012  130 LEU A C   
1128 O O   . LEU A 130 ? 0.2277 0.2457 0.2677 0.0028  0.0183  0.0029  130 LEU A O   
1129 C CB  . LEU A 130 ? 0.3461 0.3587 0.3894 0.0061  0.0263  -0.0070 130 LEU A CB  
1130 C CG  . LEU A 130 ? 0.3544 0.3635 0.3927 0.0017  0.0259  -0.0095 130 LEU A CG  
1131 C CD1 . LEU A 130 ? 0.3363 0.3361 0.3765 0.0021  0.0263  -0.0083 130 LEU A CD1 
1132 C CD2 . LEU A 130 ? 0.3220 0.3317 0.3567 -0.0007 0.0286  -0.0158 130 LEU A CD2 
1133 N N   . GLN A 131 ? 0.2819 0.3101 0.3250 0.0054  0.0202  0.0010  131 GLN A N   
1134 C CA  . GLN A 131 ? 0.1782 0.2120 0.2192 0.0033  0.0183  0.0034  131 GLN A CA  
1135 C C   . GLN A 131 ? 0.2192 0.2519 0.2612 0.0035  0.0156  0.0078  131 GLN A C   
1136 O O   . GLN A 131 ? 0.2437 0.2752 0.2824 0.0009  0.0143  0.0094  131 GLN A O   
1137 C CB  . GLN A 131 ? 0.1573 0.1992 0.2001 0.0044  0.0194  0.0030  131 GLN A CB  
1138 C CG  . GLN A 131 ? 0.2150 0.2602 0.2552 0.0034  0.0217  -0.0009 131 GLN A CG  
1139 C CD  . GLN A 131 ? 0.2544 0.3072 0.2969 0.0053  0.0231  -0.0008 131 GLN A CD  
1140 O OE1 . GLN A 131 ? 0.2532 0.3070 0.3004 0.0083  0.0235  0.0003  131 GLN A OE1 
1141 N NE2 . GLN A 131 ? 0.2530 0.3120 0.2930 0.0034  0.0239  -0.0014 131 GLN A NE2 
1142 N N   . THR A 132 ? 0.2106 0.2441 0.2572 0.0064  0.0149  0.0100  132 THR A N   
1143 C CA  . THR A 132 ? 0.1623 0.1968 0.2094 0.0060  0.0120  0.0142  132 THR A CA  
1144 C C   . THR A 132 ? 0.1395 0.1672 0.1844 0.0052  0.0106  0.0161  132 THR A C   
1145 O O   . THR A 132 ? 0.2422 0.2696 0.2841 0.0031  0.0086  0.0186  132 THR A O   
1146 C CB  . THR A 132 ? 0.1913 0.2302 0.2445 0.0091  0.0113  0.0165  132 THR A CB  
1147 O OG1 . THR A 132 ? 0.2474 0.2919 0.3031 0.0102  0.0133  0.0145  132 THR A OG1 
1148 C CG2 . THR A 132 ? 0.2167 0.2589 0.2697 0.0076  0.0081  0.0203  132 THR A CG2 
1149 N N   . LEU A 133 ? 0.2470 0.2690 0.2935 0.0068  0.0122  0.0150  133 LEU A N   
1150 C CA  . LEU A 133 ? 0.2366 0.2519 0.2817 0.0064  0.0113  0.0171  133 LEU A CA  
1151 C C   . LEU A 133 ? 0.3009 0.3131 0.3402 0.0027  0.0114  0.0157  133 LEU A C   
1152 O O   . LEU A 133 ? 0.2452 0.2534 0.2821 0.0015  0.0101  0.0183  133 LEU A O   
1153 C CB  . LEU A 133 ? 0.2164 0.2259 0.2656 0.0093  0.0138  0.0162  133 LEU A CB  
1154 C CG  . LEU A 133 ? 0.2353 0.2468 0.2913 0.0134  0.0135  0.0200  133 LEU A CG  
1155 C CD1 . LEU A 133 ? 0.2759 0.2821 0.3368 0.0165  0.0176  0.0180  133 LEU A CD1 
1156 C CD2 . LEU A 133 ? 0.3134 0.3244 0.3696 0.0136  0.0104  0.0258  133 LEU A CD2 
1157 N N   . ASN A 134 ? 0.3088 0.3231 0.3460 0.0008  0.0129  0.0120  134 ASN A N   
1158 C CA  . ASN A 134 ? 0.2925 0.3055 0.3252 -0.0028 0.0128  0.0115  134 ASN A CA  
1159 C C   . ASN A 134 ? 0.2941 0.3103 0.3245 -0.0044 0.0113  0.0146  134 ASN A C   
1160 O O   . ASN A 134 ? 0.2670 0.2797 0.2942 -0.0065 0.0109  0.0164  134 ASN A O   
1161 C CB  . ASN A 134 ? 0.2310 0.2475 0.2626 -0.0044 0.0146  0.0076  134 ASN A CB  
1162 C CG  . ASN A 134 ? 0.2837 0.2948 0.3146 -0.0055 0.0161  0.0042  134 ASN A CG  
1163 O OD1 . ASN A 134 ? 0.3095 0.3171 0.3382 -0.0081 0.0159  0.0043  134 ASN A OD1 
1164 N ND2 . ASN A 134 ? 0.2394 0.2495 0.2724 -0.0037 0.0180  0.0009  134 ASN A ND2 
1165 N N   . LEU A 135 ? 0.2396 0.2620 0.2716 -0.0036 0.0109  0.0152  135 LEU A N   
1166 C CA  . LEU A 135 ? 0.2411 0.2656 0.2711 -0.0053 0.0099  0.0178  135 LEU A CA  
1167 C C   . LEU A 135 ? 0.2359 0.2564 0.2643 -0.0054 0.0077  0.0209  135 LEU A C   
1168 O O   . LEU A 135 ? 0.2428 0.2604 0.2670 -0.0078 0.0075  0.0225  135 LEU A O   
1169 C CB  . LEU A 135 ? 0.2729 0.3045 0.3060 -0.0043 0.0099  0.0177  135 LEU A CB  
1170 C CG  . LEU A 135 ? 0.3390 0.3761 0.3726 -0.0052 0.0120  0.0163  135 LEU A CG  
1171 C CD1 . LEU A 135 ? 0.3220 0.3652 0.3591 -0.0041 0.0119  0.0169  135 LEU A CD1 
1172 C CD2 . LEU A 135 ? 0.3429 0.3788 0.3730 -0.0083 0.0132  0.0174  135 LEU A CD2 
1173 N N   . LEU A 136 ? 0.2317 0.2522 0.2637 -0.0026 0.0063  0.0222  136 LEU A N   
1174 C CA  . LEU A 136 ? 0.1588 0.1777 0.1897 -0.0025 0.0038  0.0260  136 LEU A CA  
1175 C C   . LEU A 136 ? 0.2626 0.2743 0.2904 -0.0033 0.0039  0.0274  136 LEU A C   
1176 O O   . LEU A 136 ? 0.2627 0.2728 0.2871 -0.0045 0.0021  0.0305  136 LEU A O   
1177 C CB  . LEU A 136 ? 0.1382 0.1599 0.1751 0.0010  0.0026  0.0279  136 LEU A CB  
1178 C CG  . LEU A 136 ? 0.2665 0.2962 0.3064 0.0013  0.0015  0.0281  136 LEU A CG  
1179 C CD1 . LEU A 136 ? 0.2534 0.2860 0.3005 0.0053  0.0010  0.0301  136 LEU A CD1 
1180 C CD2 . LEU A 136 ? 0.2551 0.2876 0.2910 -0.0020 -0.0010 0.0303  136 LEU A CD2 
1181 N N   . ALA A 137 ? 0.2961 0.3033 0.3246 -0.0029 0.0060  0.0250  137 ALA A N   
1182 C CA  . ALA A 137 ? 0.2737 0.2738 0.2998 -0.0038 0.0064  0.0262  137 ALA A CA  
1183 C C   . ALA A 137 ? 0.2248 0.2234 0.2451 -0.0073 0.0066  0.0270  137 ALA A C   
1184 O O   . ALA A 137 ? 0.2345 0.2279 0.2521 -0.0081 0.0065  0.0292  137 ALA A O   
1185 C CB  . ALA A 137 ? 0.2727 0.2688 0.3009 -0.0033 0.0088  0.0227  137 ALA A CB  
1186 N N   . TRP A 138 ? 0.2069 0.2100 0.2259 -0.0091 0.0073  0.0254  138 TRP A N   
1187 C CA  . TRP A 138 ? 0.2476 0.2492 0.2618 -0.0123 0.0083  0.0264  138 TRP A CA  
1188 C C   . TRP A 138 ? 0.2202 0.2241 0.2314 -0.0136 0.0071  0.0282  138 TRP A C   
1189 O O   . TRP A 138 ? 0.2684 0.2718 0.2760 -0.0163 0.0087  0.0284  138 TRP A O   
1190 C CB  . TRP A 138 ? 0.2561 0.2609 0.2712 -0.0136 0.0106  0.0241  138 TRP A CB  
1191 C CG  . TRP A 138 ? 0.2586 0.2613 0.2755 -0.0135 0.0115  0.0223  138 TRP A CG  
1192 C CD1 . TRP A 138 ? 0.2472 0.2520 0.2675 -0.0119 0.0117  0.0194  138 TRP A CD1 
1193 C CD2 . TRP A 138 ? 0.2486 0.2465 0.2640 -0.0153 0.0126  0.0229  138 TRP A CD2 
1194 N NE1 . TRP A 138 ? 0.3108 0.3126 0.3313 -0.0131 0.0126  0.0178  138 TRP A NE1 
1195 C CE2 . TRP A 138 ? 0.2773 0.2751 0.2953 -0.0152 0.0130  0.0201  138 TRP A CE2 
1196 C CE3 . TRP A 138 ? 0.2824 0.2761 0.2945 -0.0172 0.0135  0.0255  138 TRP A CE3 
1197 C CZ2 . TRP A 138 ? 0.2868 0.2808 0.3045 -0.0171 0.0139  0.0199  138 TRP A CZ2 
1198 C CZ3 . TRP A 138 ? 0.3378 0.3277 0.3501 -0.0186 0.0146  0.0257  138 TRP A CZ3 
1199 C CH2 . TRP A 138 ? 0.3219 0.3123 0.3372 -0.0187 0.0146  0.0230  138 TRP A CH2 
1200 N N   . CYS A 139 ? 0.2304 0.2368 0.2430 -0.0120 0.0045  0.0297  139 CYS A N   
1201 C CA  . CYS A 139 ? 0.2471 0.2566 0.2566 -0.0139 0.0029  0.0311  139 CYS A CA  
1202 C C   . CYS A 139 ? 0.2861 0.2905 0.2887 -0.0166 0.0028  0.0333  139 CYS A C   
1203 O O   . CYS A 139 ? 0.2819 0.2820 0.2836 -0.0155 0.0020  0.0356  139 CYS A O   
1204 C CB  . CYS A 139 ? 0.2015 0.2157 0.2149 -0.0116 -0.0003 0.0330  139 CYS A CB  
1205 S SG  . CYS A 139 ? 0.3118 0.3325 0.3228 -0.0145 -0.0027 0.0339  139 CYS A SG  
1206 N N   . GLY A 140 ? 0.2761 0.2809 0.2740 -0.0201 0.0041  0.0326  140 GLY A N   
1207 C CA  . GLY A 140 ? 0.2960 0.2958 0.2865 -0.0230 0.0046  0.0343  140 GLY A CA  
1208 C C   . GLY A 140 ? 0.2530 0.2553 0.2398 -0.0241 0.0009  0.0367  140 GLY A C   
1209 O O   . GLY A 140 ? 0.2316 0.2401 0.2221 -0.0228 -0.0022 0.0374  140 GLY A O   
1210 N N   . ARG A 141 ? 0.2542 0.2520 0.2334 -0.0267 0.0013  0.0383  141 ARG A N   
1211 C CA  . ARG A 141 ? 0.3080 0.3084 0.2826 -0.0281 -0.0025 0.0412  141 ARG A CA  
1212 C C   . ARG A 141 ? 0.3269 0.3344 0.3007 -0.0308 -0.0047 0.0399  141 ARG A C   
1213 O O   . ARG A 141 ? 0.2631 0.2770 0.2388 -0.0301 -0.0091 0.0425  141 ARG A O   
1214 C CB  . ARG A 141 ? 0.1795 0.1736 0.1447 -0.0312 -0.0009 0.0426  141 ARG A CB  
1215 C CG  . ARG A 141 ? 0.2237 0.2212 0.1827 -0.0334 -0.0049 0.0457  141 ARG A CG  
1216 C CD  . ARG A 141 ? 0.3080 0.2990 0.2570 -0.0363 -0.0031 0.0472  141 ARG A CD  
1217 N NE  . ARG A 141 ? 0.5359 0.5253 0.4771 -0.0417 -0.0004 0.0435  141 ARG A NE  
1218 C CZ  . ARG A 141 ? 0.4120 0.4033 0.3440 -0.0463 -0.0021 0.0438  141 ARG A CZ  
1219 N NH1 . ARG A 141 ? 0.4382 0.4337 0.3675 -0.0460 -0.0068 0.0483  141 ARG A NH1 
1220 N NH2 . ARG A 141 ? 0.4648 0.4535 0.3903 -0.0514 0.0014  0.0396  141 ARG A NH2 
1221 N N   . THR A 142 ? 0.2635 0.2705 0.2354 -0.0340 -0.0015 0.0361  142 THR A N   
1222 C CA  . THR A 142 ? 0.2879 0.3011 0.2588 -0.0374 -0.0030 0.0344  142 THR A CA  
1223 C C   . THR A 142 ? 0.2995 0.3207 0.2797 -0.0341 -0.0060 0.0348  142 THR A C   
1224 O O   . THR A 142 ? 0.3320 0.3601 0.3130 -0.0349 -0.0103 0.0366  142 THR A O   
1225 C CB  . THR A 142 ? 0.3078 0.3178 0.2764 -0.0408 0.0022  0.0303  142 THR A CB  
1226 O OG1 . THR A 142 ? 0.2587 0.2612 0.2182 -0.0443 0.0053  0.0300  142 THR A OG1 
1227 C CG2 . THR A 142 ? 0.2320 0.2484 0.2009 -0.0444 0.0010  0.0280  142 THR A CG2 
1228 N N   . LEU A 143 ? 0.2685 0.2894 0.2559 -0.0304 -0.0038 0.0334  143 LEU A N   
1229 C CA  . LEU A 143 ? 0.3150 0.3429 0.3111 -0.0271 -0.0059 0.0337  143 LEU A CA  
1230 C C   . LEU A 143 ? 0.3651 0.3947 0.3656 -0.0229 -0.0093 0.0375  143 LEU A C   
1231 O O   . LEU A 143 ? 0.3024 0.3386 0.3097 -0.0204 -0.0115 0.0387  143 LEU A O   
1232 C CB  . LEU A 143 ? 0.2353 0.2627 0.2368 -0.0250 -0.0021 0.0308  143 LEU A CB  
1233 C CG  . LEU A 143 ? 0.2777 0.3052 0.2776 -0.0284 0.0015  0.0277  143 LEU A CG  
1234 C CD1 . LEU A 143 ? 0.2079 0.2366 0.2141 -0.0256 0.0047  0.0259  143 LEU A CD1 
1235 C CD2 . LEU A 143 ? 0.3024 0.3360 0.3023 -0.0315 -0.0006 0.0271  143 LEU A CD2 
1236 N N   . ARG A 144 ? 0.3110 0.3349 0.3084 -0.0218 -0.0092 0.0397  144 ARG A N   
1237 C CA  . ARG A 144 ? 0.3078 0.3332 0.3093 -0.0180 -0.0121 0.0441  144 ARG A CA  
1238 C C   . ARG A 144 ? 0.3700 0.4029 0.3707 -0.0196 -0.0168 0.0478  144 ARG A C   
1239 O O   . ARG A 144 ? 0.3725 0.4107 0.3801 -0.0161 -0.0193 0.0514  144 ARG A O   
1240 C CB  . ARG A 144 ? 0.3162 0.3338 0.3142 -0.0171 -0.0109 0.0461  144 ARG A CB  
1241 C CG  . ARG A 144 ? 0.3707 0.3831 0.3741 -0.0134 -0.0079 0.0444  144 ARG A CG  
1242 C CD  . ARG A 144 ? 0.4291 0.4335 0.4290 -0.0133 -0.0063 0.0461  144 ARG A CD  
1243 N NE  . ARG A 144 ? 0.4404 0.4398 0.4444 -0.0111 -0.0033 0.0436  144 ARG A NE  
1244 C CZ  . ARG A 144 ? 0.4904 0.4880 0.5006 -0.0073 -0.0030 0.0447  144 ARG A CZ  
1245 N NH1 . ARG A 144 ? 0.4720 0.4725 0.4858 -0.0047 -0.0053 0.0490  144 ARG A NH1 
1246 N NH2 . ARG A 144 ? 0.4500 0.4431 0.4630 -0.0063 -0.0001 0.0418  144 ARG A NH2 
1247 N N   . LYS A 145 ? 0.4187 0.4526 0.4111 -0.0249 -0.0177 0.0470  145 LYS A N   
1248 C CA  . LYS A 145 ? 0.4545 0.4970 0.4456 -0.0275 -0.0225 0.0499  145 LYS A CA  
1249 C C   . LYS A 145 ? 0.4053 0.4556 0.4028 -0.0279 -0.0234 0.0479  145 LYS A C   
1250 O O   . LYS A 145 ? 0.4096 0.4685 0.4128 -0.0266 -0.0274 0.0515  145 LYS A O   
1251 C CB  . LYS A 145 ? 0.5018 0.5424 0.4810 -0.0338 -0.0229 0.0490  145 LYS A CB  
1252 C CG  . LYS A 145 ? 0.5983 0.6336 0.5711 -0.0334 -0.0232 0.0528  145 LYS A CG  
1253 C CD  . LYS A 145 ? 0.6564 0.6818 0.6204 -0.0365 -0.0185 0.0491  145 LYS A CD  
1254 C CE  . LYS A 145 ? 0.7098 0.7319 0.6645 -0.0385 -0.0194 0.0526  145 LYS A CE  
1255 N NZ  . LYS A 145 ? 0.6935 0.7110 0.6518 -0.0333 -0.0189 0.0568  145 LYS A NZ  
1256 N N   . ASP A 146 ? 0.4114 0.4591 0.4087 -0.0295 -0.0196 0.0426  146 ASP A N   
1257 C CA  . ASP A 146 ? 0.3828 0.4376 0.3856 -0.0305 -0.0202 0.0406  146 ASP A CA  
1258 C C   . ASP A 146 ? 0.4185 0.4772 0.4326 -0.0245 -0.0203 0.0420  146 ASP A C   
1259 O O   . ASP A 146 ? 0.4817 0.5488 0.5019 -0.0240 -0.0229 0.0435  146 ASP A O   
1260 C CB  . ASP A 146 ? 0.4275 0.4781 0.4271 -0.0338 -0.0154 0.0352  146 ASP A CB  
1261 C CG  . ASP A 146 ? 0.4858 0.5322 0.4745 -0.0401 -0.0144 0.0333  146 ASP A CG  
1262 O OD1 . ASP A 146 ? 0.5380 0.5860 0.5208 -0.0425 -0.0180 0.0360  146 ASP A OD1 
1263 O OD2 . ASP A 146 ? 0.5418 0.5832 0.5277 -0.0426 -0.0096 0.0293  146 ASP A OD2 
1264 N N   . LEU A 147 ? 0.3638 0.4165 0.3807 -0.0201 -0.0174 0.0415  147 LEU A N   
1265 C CA  . LEU A 147 ? 0.3364 0.3914 0.3629 -0.0147 -0.0165 0.0418  147 LEU A CA  
1266 C C   . LEU A 147 ? 0.3239 0.3791 0.3550 -0.0103 -0.0184 0.0467  147 LEU A C   
1267 O O   . LEU A 147 ? 0.3781 0.4313 0.4155 -0.0057 -0.0162 0.0464  147 LEU A O   
1268 C CB  . LEU A 147 ? 0.3450 0.3940 0.3721 -0.0130 -0.0117 0.0377  147 LEU A CB  
1269 C CG  . LEU A 147 ? 0.4023 0.4505 0.4261 -0.0165 -0.0087 0.0335  147 LEU A CG  
1270 C CD1 . LEU A 147 ? 0.3558 0.3982 0.3793 -0.0150 -0.0044 0.0306  147 LEU A CD1 
1271 C CD2 . LEU A 147 ? 0.4430 0.4989 0.4724 -0.0168 -0.0091 0.0325  147 LEU A CD2 
1272 N N   . LYS A 148 ? 0.2406 0.2981 0.2686 -0.0117 -0.0221 0.0513  148 LYS A N   
1273 C CA  . LYS A 148 ? 0.3472 0.4036 0.3792 -0.0074 -0.0231 0.0565  148 LYS A CA  
1274 C C   . LYS A 148 ? 0.3983 0.4597 0.4421 -0.0020 -0.0230 0.0588  148 LYS A C   
1275 O O   . LYS A 148 ? 0.3825 0.4393 0.4313 0.0026  -0.0208 0.0604  148 LYS A O   
1276 C CB  . LYS A 148 ? 0.3793 0.4397 0.4065 -0.0099 -0.0276 0.0618  148 LYS A CB  
1277 C CG  . LYS A 148 ? 0.4752 0.5472 0.5091 -0.0091 -0.0321 0.0675  148 LYS A CG  
1278 C CD  . LYS A 148 ? 0.5887 0.6657 0.6164 -0.0124 -0.0368 0.0728  148 LYS A CD  
1279 C CE  . LYS A 148 ? 0.7035 0.7721 0.7261 -0.0111 -0.0354 0.0751  148 LYS A CE  
1280 N NZ  . LYS A 148 ? 0.7286 0.7929 0.7605 -0.0041 -0.0326 0.0780  148 LYS A NZ  
1281 N N   . ASP A 149 ? 0.3609 0.4308 0.4095 -0.0027 -0.0246 0.0588  149 ASP A N   
1282 C CA  . ASP A 149 ? 0.4275 0.5027 0.4877 0.0024  -0.0244 0.0618  149 ASP A CA  
1283 C C   . ASP A 149 ? 0.4413 0.5104 0.5056 0.0062  -0.0191 0.0572  149 ASP A C   
1284 O O   . ASP A 149 ? 0.4386 0.5064 0.5106 0.0113  -0.0171 0.0593  149 ASP A O   
1285 C CB  . ASP A 149 ? 0.4223 0.5087 0.4867 0.0003  -0.0277 0.0632  149 ASP A CB  
1286 C CG  . ASP A 149 ? 0.4558 0.5496 0.5162 -0.0039 -0.0333 0.0679  149 ASP A CG  
1287 O OD1 . ASP A 149 ? 0.5141 0.6078 0.5742 -0.0023 -0.0352 0.0735  149 ASP A OD1 
1288 O OD2 . ASP A 149 ? 0.5018 0.6015 0.5591 -0.0091 -0.0357 0.0661  149 ASP A OD2 
1289 N N   . LEU A 150 ? 0.3823 0.4477 0.4415 0.0037  -0.0166 0.0510  150 LEU A N   
1290 C CA  . LEU A 150 ? 0.3709 0.4307 0.4324 0.0066  -0.0119 0.0466  150 LEU A CA  
1291 C C   . LEU A 150 ? 0.3243 0.3747 0.3832 0.0083  -0.0097 0.0463  150 LEU A C   
1292 O O   . LEU A 150 ? 0.2859 0.3324 0.3494 0.0120  -0.0064 0.0449  150 LEU A O   
1293 C CB  . LEU A 150 ? 0.3570 0.4161 0.4140 0.0034  -0.0098 0.0411  150 LEU A CB  
1294 C CG  . LEU A 150 ? 0.4118 0.4792 0.4720 0.0018  -0.0109 0.0405  150 LEU A CG  
1295 C CD1 . LEU A 150 ? 0.3693 0.4350 0.4245 -0.0015 -0.0084 0.0357  150 LEU A CD1 
1296 C CD2 . LEU A 150 ? 0.3834 0.4556 0.4536 0.0065  -0.0096 0.0416  150 LEU A CD2 
1297 N N   . LEU A 151 ? 0.3695 0.4161 0.4211 0.0053  -0.0112 0.0473  151 LEU A N   
1298 C CA  . LEU A 151 ? 0.3901 0.4280 0.4394 0.0065  -0.0092 0.0473  151 LEU A CA  
1299 C C   . LEU A 151 ? 0.4277 0.4649 0.4846 0.0113  -0.0089 0.0520  151 LEU A C   
1300 O O   . LEU A 151 ? 0.4655 0.4962 0.5254 0.0141  -0.0052 0.0503  151 LEU A O   
1301 C CB  . LEU A 151 ? 0.4653 0.4999 0.5057 0.0026  -0.0109 0.0484  151 LEU A CB  
1302 C CG  . LEU A 151 ? 0.4707 0.5005 0.5035 -0.0012 -0.0089 0.0436  151 LEU A CG  
1303 C CD1 . LEU A 151 ? 0.4840 0.5121 0.5085 -0.0051 -0.0108 0.0457  151 LEU A CD1 
1304 C CD2 . LEU A 151 ? 0.4149 0.4369 0.4481 0.0004  -0.0052 0.0406  151 LEU A CD2 
1305 N N   . ASN A 152 ? 0.4446 0.4887 0.5048 0.0121  -0.0125 0.0582  152 ASN A N   
1306 C CA  . ASN A 152 ? 0.4703 0.5149 0.5390 0.0170  -0.0120 0.0641  152 ASN A CA  
1307 C C   . ASN A 152 ? 0.4358 0.4820 0.5144 0.0215  -0.0089 0.0633  152 ASN A C   
1308 O O   . ASN A 152 ? 0.4137 0.4579 0.5001 0.0261  -0.0066 0.0671  152 ASN A O   
1309 C CB  . ASN A 152 ? 0.4927 0.5461 0.5625 0.0163  -0.0171 0.0717  152 ASN A CB  
1310 C CG  . ASN A 152 ? 0.5238 0.5748 0.5840 0.0126  -0.0197 0.0735  152 ASN A CG  
1311 O OD1 . ASN A 152 ? 0.5250 0.5669 0.5791 0.0113  -0.0172 0.0700  152 ASN A OD1 
1312 N ND2 . ASN A 152 ? 0.5197 0.5792 0.5785 0.0106  -0.0246 0.0792  152 ASN A ND2 
1313 N N   . LYS A 153 ? 0.4209 0.4709 0.4996 0.0203  -0.0085 0.0589  153 LYS A N   
1314 C CA  . LYS A 153 ? 0.4298 0.4803 0.5166 0.0242  -0.0047 0.0570  153 LYS A CA  
1315 C C   . LYS A 153 ? 0.4577 0.4977 0.5449 0.0266  0.0007  0.0532  153 LYS A C   
1316 O O   . LYS A 153 ? 0.4562 0.4939 0.5515 0.0312  0.0041  0.0551  153 LYS A O   
1317 C CB  . LYS A 153 ? 0.4184 0.4733 0.5031 0.0218  -0.0047 0.0520  153 LYS A CB  
1318 C CG  . LYS A 153 ? 0.4595 0.5189 0.5530 0.0254  -0.0023 0.0518  153 LYS A CG  
1319 C CD  . LYS A 153 ? 0.2911 0.3536 0.3818 0.0230  -0.0015 0.0465  153 LYS A CD  
1320 C CE  . LYS A 153 ? 0.2796 0.3430 0.3776 0.0272  0.0027  0.0448  153 LYS A CE  
1321 N NZ  . LYS A 153 ? 0.4189 0.4875 0.5162 0.0255  0.0032  0.0413  153 LYS A NZ  
1322 N N   . GLY A 154 ? 0.3535 0.3870 0.4323 0.0234  0.0017  0.0479  154 GLY A N   
1323 C CA  . GLY A 154 ? 0.3504 0.3739 0.4282 0.0243  0.0061  0.0442  154 GLY A CA  
1324 C C   . GLY A 154 ? 0.3335 0.3545 0.4139 0.0260  0.0108  0.0385  154 GLY A C   
1325 O O   . GLY A 154 ? 0.3396 0.3526 0.4177 0.0255  0.0142  0.0342  154 GLY A O   
1326 N N   . ARG A 155 ? 0.3768 0.4045 0.4616 0.0275  0.0111  0.0382  155 ARG A N   
1327 C CA  . ARG A 155 ? 0.3363 0.3617 0.4242 0.0297  0.0160  0.0335  155 ARG A CA  
1328 C C   . ARG A 155 ? 0.2793 0.3139 0.3708 0.0306  0.0151  0.0339  155 ARG A C   
1329 O O   . ARG A 155 ? 0.3178 0.3599 0.4105 0.0297  0.0108  0.0382  155 ARG A O   
1330 C CB  . ARG A 155 ? 0.3407 0.3601 0.4362 0.0343  0.0205  0.0353  155 ARG A CB  
1331 C CG  . ARG A 155 ? 0.4321 0.4575 0.5374 0.0384  0.0191  0.0435  155 ARG A CG  
1332 C CD  . ARG A 155 ? 0.4306 0.4495 0.5446 0.0434  0.0245  0.0458  155 ARG A CD  
1333 N NE  . ARG A 155 ? 0.4342 0.4439 0.5455 0.0427  0.0259  0.0457  155 ARG A NE  
1334 C CZ  . ARG A 155 ? 0.4257 0.4250 0.5358 0.0427  0.0316  0.0401  155 ARG A CZ  
1335 N NH1 . ARG A 155 ? 0.4896 0.4809 0.5978 0.0419  0.0326  0.0405  155 ARG A NH1 
1336 N NH2 . ARG A 155 ? 0.4138 0.4108 0.5244 0.0434  0.0363  0.0340  155 ARG A NH2 
1337 N N   . ASN A 156 ? 0.2845 0.3182 0.3776 0.0321  0.0194  0.0294  156 ASN A N   
1338 C CA  . ASN A 156 ? 0.3408 0.3823 0.4387 0.0338  0.0199  0.0298  156 ASN A CA  
1339 C C   . ASN A 156 ? 0.3073 0.3564 0.4009 0.0301  0.0158  0.0296  156 ASN A C   
1340 O O   . ASN A 156 ? 0.2415 0.2987 0.3400 0.0307  0.0133  0.0333  156 ASN A O   
1341 C CB  . ASN A 156 ? 0.3314 0.3773 0.4403 0.0383  0.0199  0.0364  156 ASN A CB  
1342 C CG  . ASN A 156 ? 0.4349 0.4729 0.5493 0.0424  0.0246  0.0376  156 ASN A CG  
1343 O OD1 . ASN A 156 ? 0.4876 0.5177 0.5995 0.0427  0.0296  0.0319  156 ASN A OD1 
1344 N ND2 . ASN A 156 ? 0.3700 0.4104 0.4922 0.0453  0.0231  0.0452  156 ASN A ND2 
1345 N N   . TYR A 157 ? 0.2071 0.2537 0.2922 0.0262  0.0154  0.0253  157 TYR A N   
1346 C CA  . TYR A 157 ? 0.2420 0.2943 0.3229 0.0226  0.0125  0.0250  157 TYR A CA  
1347 C C   . TYR A 157 ? 0.2403 0.2978 0.3227 0.0232  0.0148  0.0222  157 TYR A C   
1348 O O   . TYR A 157 ? 0.3304 0.3854 0.4125 0.0248  0.0188  0.0184  157 TYR A O   
1349 C CB  . TYR A 157 ? 0.2150 0.2626 0.2870 0.0185  0.0116  0.0225  157 TYR A CB  
1350 C CG  . TYR A 157 ? 0.2352 0.2789 0.3053 0.0175  0.0087  0.0260  157 TYR A CG  
1351 C CD1 . TYR A 157 ? 0.2783 0.3265 0.3481 0.0157  0.0046  0.0300  157 TYR A CD1 
1352 C CD2 . TYR A 157 ? 0.1799 0.2155 0.2486 0.0182  0.0103  0.0252  157 TYR A CD2 
1353 C CE1 . TYR A 157 ? 0.2251 0.2703 0.2926 0.0147  0.0021  0.0335  157 TYR A CE1 
1354 C CE2 . TYR A 157 ? 0.2182 0.2505 0.2854 0.0175  0.0079  0.0289  157 TYR A CE2 
1355 C CZ  . TYR A 157 ? 0.2481 0.2854 0.3144 0.0159  0.0038  0.0332  157 TYR A CZ  
1356 O OH  . TYR A 157 ? 0.2637 0.2982 0.3278 0.0150  0.0014  0.0370  157 TYR A OH  
1357 N N   . THR A 158 ? 0.1838 0.2485 0.2674 0.0216  0.0126  0.0239  158 THR A N   
1358 C CA  . THR A 158 ? 0.1687 0.2388 0.2538 0.0219  0.0148  0.0218  158 THR A CA  
1359 C C   . THR A 158 ? 0.1867 0.2572 0.2649 0.0180  0.0146  0.0193  158 THR A C   
1360 O O   . THR A 158 ? 0.2439 0.3120 0.3173 0.0148  0.0123  0.0200  158 THR A O   
1361 C CB  . THR A 158 ? 0.2048 0.2830 0.2974 0.0230  0.0132  0.0253  158 THR A CB  
1362 O OG1 . THR A 158 ? 0.2094 0.2909 0.2996 0.0189  0.0094  0.0271  158 THR A OG1 
1363 C CG2 . THR A 158 ? 0.2254 0.3043 0.3260 0.0268  0.0128  0.0294  158 THR A CG2 
1364 N N   . GLN A 159 ? 0.2226 0.2659 0.2775 0.0080  -0.0057 0.0504  159 GLN A N   
1365 C CA  . GLN A 159 ? 0.2761 0.3165 0.3292 0.0043  -0.0083 0.0478  159 GLN A CA  
1366 C C   . GLN A 159 ? 0.3076 0.3495 0.3617 0.0002  -0.0119 0.0494  159 GLN A C   
1367 O O   . GLN A 159 ? 0.2893 0.3260 0.3416 -0.0025 -0.0137 0.0464  159 GLN A O   
1368 C CB  . GLN A 159 ? 0.2623 0.3067 0.3160 0.0044  -0.0081 0.0486  159 GLN A CB  
1369 C CG  . GLN A 159 ? 0.2997 0.3412 0.3520 0.0011  -0.0104 0.0465  159 GLN A CG  
1370 C CD  . GLN A 159 ? 0.3148 0.3490 0.3636 0.0015  -0.0095 0.0415  159 GLN A CD  
1371 O OE1 . GLN A 159 ? 0.2844 0.3161 0.3315 0.0042  -0.0067 0.0393  159 GLN A OE1 
1372 N NE2 . GLN A 159 ? 0.2913 0.3222 0.3392 -0.0014 -0.0117 0.0398  159 GLN A NE2 
1373 N N   . GLU A 160 ? 0.2139 0.2631 0.2711 -0.0005 -0.0129 0.0539  160 GLU A N   
1374 C CA  . GLU A 160 ? 0.2569 0.3080 0.3148 -0.0050 -0.0163 0.0551  160 GLU A CA  
1375 C C   . GLU A 160 ? 0.1879 0.2347 0.2440 -0.0061 -0.0171 0.0531  160 GLU A C   
1376 O O   . GLU A 160 ? 0.2862 0.3296 0.3408 -0.0098 -0.0194 0.0509  160 GLU A O   
1377 C CB  . GLU A 160 ? 0.2786 0.3396 0.3402 -0.0057 -0.0172 0.0605  160 GLU A CB  
1378 C CG  . GLU A 160 ? 0.3677 0.4315 0.4298 -0.0104 -0.0204 0.0618  160 GLU A CG  
1379 C CD  . GLU A 160 ? 0.5975 0.6573 0.6584 -0.0152 -0.0229 0.0593  160 GLU A CD  
1380 O OE1 . GLU A 160 ? 0.6764 0.7351 0.7376 -0.0154 -0.0227 0.0589  160 GLU A OE1 
1381 O OE2 . GLU A 160 ? 0.6885 0.7462 0.7480 -0.0189 -0.0250 0.0578  160 GLU A OE2 
1382 N N   . GLU A 161 ? 0.1745 0.2214 0.2308 -0.0027 -0.0150 0.0540  161 GLU A N   
1383 C CA  . GLU A 161 ? 0.2054 0.2485 0.2601 -0.0033 -0.0154 0.0525  161 GLU A CA  
1384 C C   . GLU A 161 ? 0.2246 0.2585 0.2758 -0.0039 -0.0152 0.0471  161 GLU A C   
1385 O O   . GLU A 161 ? 0.2704 0.3010 0.3197 -0.0066 -0.0168 0.0450  161 GLU A O   
1386 C CB  . GLU A 161 ? 0.2227 0.2677 0.2788 0.0010  -0.0127 0.0551  161 GLU A CB  
1387 C CG  . GLU A 161 ? 0.2689 0.3241 0.3288 0.0015  -0.0132 0.0612  161 GLU A CG  
1388 C CD  . GLU A 161 ? 0.3349 0.3923 0.3972 0.0068  -0.0098 0.0644  161 GLU A CD  
1389 O OE1 . GLU A 161 ? 0.2880 0.3381 0.3488 0.0099  -0.0069 0.0616  161 GLU A OE1 
1390 O OE2 . GLU A 161 ? 0.3804 0.4467 0.4462 0.0077  -0.0099 0.0698  161 GLU A OE2 
1391 N N   . LYS A 162 ? 0.2393 0.2695 0.2895 -0.0016 -0.0131 0.0447  162 LYS A N   
1392 C CA  . LYS A 162 ? 0.2500 0.2724 0.2971 -0.0024 -0.0130 0.0399  162 LYS A CA  
1393 C C   . LYS A 162 ? 0.2830 0.3040 0.3294 -0.0064 -0.0158 0.0383  162 LYS A C   
1394 O O   . LYS A 162 ? 0.2539 0.2699 0.2984 -0.0081 -0.0167 0.0353  162 LYS A O   
1395 C CB  . LYS A 162 ? 0.2428 0.2629 0.2889 0.0005  -0.0104 0.0379  162 LYS A CB  
1396 C CG  . LYS A 162 ? 0.2023 0.2158 0.2455 -0.0003 -0.0102 0.0332  162 LYS A CG  
1397 C CD  . LYS A 162 ? 0.2228 0.2353 0.2649 0.0021  -0.0077 0.0313  162 LYS A CD  
1398 C CE  . LYS A 162 ? 0.2868 0.3042 0.3299 0.0017  -0.0083 0.0330  162 LYS A CE  
1399 N NZ  . LYS A 162 ? 0.2365 0.2532 0.2778 0.0034  -0.0061 0.0306  162 LYS A NZ  
1400 N N   . GLU A 163 ? 0.1918 0.2171 0.2400 -0.0078 -0.0170 0.0405  163 GLU A N   
1401 C CA  . GLU A 163 ? 0.2766 0.3004 0.3248 -0.0115 -0.0194 0.0395  163 GLU A CA  
1402 C C   . GLU A 163 ? 0.2772 0.3012 0.3252 -0.0150 -0.0215 0.0397  163 GLU A C   
1403 O O   . GLU A 163 ? 0.2760 0.2957 0.3228 -0.0177 -0.0229 0.0372  163 GLU A O   
1404 C CB  . GLU A 163 ? 0.3199 0.3486 0.3704 -0.0122 -0.0200 0.0424  163 GLU A CB  
1405 C CG  . GLU A 163 ? 0.3586 0.3865 0.4086 -0.0100 -0.0184 0.0414  163 GLU A CG  
1406 C CD  . GLU A 163 ? 0.4934 0.5275 0.5459 -0.0103 -0.0187 0.0450  163 GLU A CD  
1407 O OE1 . GLU A 163 ? 0.5123 0.5473 0.5645 -0.0085 -0.0174 0.0447  163 GLU A OE1 
1408 O OE2 . GLU A 163 ? 0.4922 0.5308 0.5470 -0.0125 -0.0202 0.0480  163 GLU A OE2 
1409 N N   . TYR A 164 ? 0.2663 0.2957 0.3155 -0.0148 -0.0217 0.0427  164 TYR A N   
1410 C CA  . TYR A 164 ? 0.3132 0.3436 0.3617 -0.0183 -0.0237 0.0427  164 TYR A CA  
1411 C C   . TYR A 164 ? 0.3179 0.3418 0.3634 -0.0182 -0.0233 0.0388  164 TYR A C   
1412 O O   . TYR A 164 ? 0.2871 0.3078 0.3310 -0.0215 -0.0248 0.0363  164 TYR A O   
1413 C CB  . TYR A 164 ? 0.2671 0.3056 0.3176 -0.0177 -0.0239 0.0471  164 TYR A CB  
1414 C CG  . TYR A 164 ? 0.3418 0.3829 0.3914 -0.0217 -0.0261 0.0474  164 TYR A CG  
1415 C CD1 . TYR A 164 ? 0.4266 0.4699 0.4766 -0.0266 -0.0286 0.0475  164 TYR A CD1 
1416 C CD2 . TYR A 164 ? 0.3390 0.3801 0.3873 -0.0209 -0.0258 0.0473  164 TYR A CD2 
1417 C CE1 . TYR A 164 ? 0.4321 0.4779 0.4808 -0.0308 -0.0306 0.0472  164 TYR A CE1 
1418 C CE2 . TYR A 164 ? 0.3637 0.4080 0.4108 -0.0249 -0.0279 0.0475  164 TYR A CE2 
1419 C CZ  . TYR A 164 ? 0.4490 0.4956 0.4961 -0.0299 -0.0303 0.0472  164 TYR A CZ  
1420 O OH  . TYR A 164 ? 0.4888 0.5388 0.5343 -0.0343 -0.0323 0.0468  164 TYR A OH  
1421 N N   . VAL A 165 ? 0.2296 0.2512 0.2744 -0.0145 -0.0211 0.0383  165 VAL A N   
1422 C CA  . VAL A 165 ? 0.2113 0.2270 0.2536 -0.0142 -0.0205 0.0349  165 VAL A CA  
1423 C C   . VAL A 165 ? 0.1793 0.1887 0.2198 -0.0157 -0.0210 0.0308  165 VAL A C   
1424 O O   . VAL A 165 ? 0.2856 0.2915 0.3243 -0.0179 -0.0219 0.0282  165 VAL A O   
1425 C CB  . VAL A 165 ? 0.2040 0.2179 0.2461 -0.0100 -0.0178 0.0351  165 VAL A CB  
1426 C CG1 . VAL A 165 ? 0.1909 0.1981 0.2304 -0.0099 -0.0170 0.0312  165 VAL A CG1 
1427 C CG2 . VAL A 165 ? 0.1983 0.2179 0.2422 -0.0084 -0.0172 0.0393  165 VAL A CG2 
1428 N N   . LEU A 166 ? 0.1650 0.1734 0.2062 -0.0144 -0.0203 0.0304  166 LEU A N   
1429 C CA  . LEU A 166 ? 0.2452 0.2488 0.2856 -0.0155 -0.0207 0.0274  166 LEU A CA  
1430 C C   . LEU A 166 ? 0.2852 0.2878 0.3257 -0.0194 -0.0227 0.0268  166 LEU A C   
1431 O O   . LEU A 166 ? 0.3069 0.3045 0.3461 -0.0206 -0.0230 0.0238  166 LEU A O   
1432 C CB  . LEU A 166 ? 0.2674 0.2721 0.3090 -0.0138 -0.0199 0.0282  166 LEU A CB  
1433 C CG  . LEU A 166 ? 0.3891 0.3914 0.4293 -0.0109 -0.0178 0.0262  166 LEU A CG  
1434 C CD1 . LEU A 166 ? 0.4650 0.4697 0.5061 -0.0099 -0.0172 0.0271  166 LEU A CD1 
1435 C CD2 . LEU A 166 ? 0.3215 0.3181 0.3597 -0.0115 -0.0177 0.0225  166 LEU A CD2 
1436 N N   . ASN A 167 ? 0.2114 0.2188 0.2537 -0.0214 -0.0240 0.0297  167 ASN A N   
1437 C CA  . ASN A 167 ? 0.2733 0.2797 0.3157 -0.0256 -0.0259 0.0290  167 ASN A CA  
1438 C C   . ASN A 167 ? 0.2439 0.2481 0.2838 -0.0276 -0.0265 0.0266  167 ASN A C   
1439 O O   . ASN A 167 ? 0.3271 0.3265 0.3659 -0.0300 -0.0269 0.0236  167 ASN A O   
1440 C CB  . ASN A 167 ? 0.3104 0.3232 0.3550 -0.0277 -0.0272 0.0327  167 ASN A CB  
1441 C CG  . ASN A 167 ? 0.5402 0.5543 0.5873 -0.0273 -0.0271 0.0346  167 ASN A CG  
1442 O OD1 . ASN A 167 ? 0.5654 0.5747 0.6125 -0.0267 -0.0266 0.0329  167 ASN A OD1 
1443 N ND2 . ASN A 167 ? 0.6543 0.6752 0.7036 -0.0276 -0.0276 0.0386  167 ASN A ND2 
1444 N N   . LYS A 168 ? 0.2042 0.2120 0.2434 -0.0266 -0.0262 0.0279  168 LYS A N   
1445 C CA  . LYS A 168 ? 0.2287 0.2355 0.2655 -0.0286 -0.0268 0.0259  168 LYS A CA  
1446 C C   . LYS A 168 ? 0.1999 0.1998 0.2346 -0.0273 -0.0256 0.0220  168 LYS A C   
1447 O O   . LYS A 168 ? 0.2478 0.2447 0.2805 -0.0296 -0.0261 0.0192  168 LYS A O   
1448 C CB  . LYS A 168 ? 0.2541 0.2669 0.2911 -0.0275 -0.0267 0.0290  168 LYS A CB  
1449 C CG  . LYS A 168 ? 0.3113 0.3322 0.3507 -0.0288 -0.0279 0.0333  168 LYS A CG  
1450 C CD  . LYS A 168 ? 0.3718 0.3941 0.4107 -0.0341 -0.0301 0.0325  168 LYS A CD  
1451 C CE  . LYS A 168 ? 0.4812 0.5047 0.5173 -0.0372 -0.0312 0.0310  168 LYS A CE  
1452 N NZ  . LYS A 168 ? 0.5086 0.5351 0.5441 -0.0428 -0.0334 0.0306  168 LYS A NZ  
1453 N N   . TYR A 169 ? 0.2020 0.1997 0.2372 -0.0237 -0.0240 0.0218  169 TYR A N   
1454 C CA  . TYR A 169 ? 0.1868 0.1787 0.2202 -0.0226 -0.0229 0.0183  169 TYR A CA  
1455 C C   . TYR A 169 ? 0.2203 0.2078 0.2537 -0.0243 -0.0233 0.0157  169 TYR A C   
1456 O O   . TYR A 169 ? 0.2722 0.2558 0.3039 -0.0252 -0.0231 0.0127  169 TYR A O   
1457 C CB  . TYR A 169 ? 0.2065 0.1975 0.2405 -0.0189 -0.0211 0.0186  169 TYR A CB  
1458 C CG  . TYR A 169 ? 0.1915 0.1839 0.2250 -0.0167 -0.0198 0.0198  169 TYR A CG  
1459 C CD1 . TYR A 169 ? 0.2314 0.2277 0.2648 -0.0175 -0.0203 0.0220  169 TYR A CD1 
1460 C CD2 . TYR A 169 ? 0.2247 0.2147 0.2578 -0.0139 -0.0179 0.0188  169 TYR A CD2 
1461 C CE1 . TYR A 169 ? 0.2893 0.2866 0.3227 -0.0151 -0.0189 0.0237  169 TYR A CE1 
1462 C CE2 . TYR A 169 ? 0.1768 0.1671 0.2097 -0.0118 -0.0163 0.0199  169 TYR A CE2 
1463 C CZ  . TYR A 169 ? 0.2596 0.2535 0.2929 -0.0122 -0.0167 0.0226  169 TYR A CZ  
1464 O OH  . TYR A 169 ? 0.2478 0.2418 0.2813 -0.0098 -0.0149 0.0242  169 TYR A OH  
1465 N N   . PHE A 170 ? 0.2193 0.2073 0.2548 -0.0248 -0.0238 0.0171  170 PHE A N   
1466 C CA  . PHE A 170 ? 0.2214 0.2049 0.2574 -0.0262 -0.0240 0.0152  170 PHE A CA  
1467 C C   . PHE A 170 ? 0.2742 0.2561 0.3092 -0.0300 -0.0250 0.0135  170 PHE A C   
1468 O O   . PHE A 170 ? 0.2210 0.1977 0.2554 -0.0310 -0.0246 0.0107  170 PHE A O   
1469 C CB  . PHE A 170 ? 0.2018 0.1867 0.2405 -0.0256 -0.0242 0.0176  170 PHE A CB  
1470 C CG  . PHE A 170 ? 0.2379 0.2221 0.2771 -0.0224 -0.0230 0.0175  170 PHE A CG  
1471 C CD1 . PHE A 170 ? 0.2420 0.2220 0.2813 -0.0218 -0.0224 0.0154  170 PHE A CD1 
1472 C CD2 . PHE A 170 ? 0.3361 0.3243 0.3757 -0.0200 -0.0223 0.0195  170 PHE A CD2 
1473 C CE1 . PHE A 170 ? 0.2835 0.2638 0.3230 -0.0192 -0.0214 0.0153  170 PHE A CE1 
1474 C CE2 . PHE A 170 ? 0.3453 0.3332 0.3848 -0.0176 -0.0212 0.0189  170 PHE A CE2 
1475 C CZ  . PHE A 170 ? 0.3553 0.3396 0.3948 -0.0174 -0.0209 0.0169  170 PHE A CZ  
1476 N N   . GLU A 171 ? 0.2247 0.2111 0.2593 -0.0323 -0.0262 0.0152  171 GLU A N   
1477 C CA  . GLU A 171 ? 0.3475 0.3331 0.3802 -0.0364 -0.0271 0.0131  171 GLU A CA  
1478 C C   . GLU A 171 ? 0.3542 0.3368 0.3840 -0.0362 -0.0263 0.0097  171 GLU A C   
1479 O O   . GLU A 171 ? 0.3427 0.3210 0.3710 -0.0385 -0.0262 0.0064  171 GLU A O   
1480 C CB  . GLU A 171 ? 0.3387 0.3315 0.3715 -0.0386 -0.0287 0.0160  171 GLU A CB  
1481 C CG  . GLU A 171 ? 0.4793 0.4756 0.5150 -0.0397 -0.0296 0.0193  171 GLU A CG  
1482 C CD  . GLU A 171 ? 0.5628 0.5672 0.5989 -0.0422 -0.0312 0.0223  171 GLU A CD  
1483 O OE1 . GLU A 171 ? 0.5585 0.5657 0.5923 -0.0436 -0.0317 0.0217  171 GLU A OE1 
1484 O OE2 . GLU A 171 ? 0.6375 0.6460 0.6761 -0.0429 -0.0319 0.0255  171 GLU A OE2 
1485 N N   . ILE A 172 ? 0.2566 0.2411 0.2856 -0.0333 -0.0256 0.0106  172 ILE A N   
1486 C CA  . ILE A 172 ? 0.2747 0.2568 0.3011 -0.0329 -0.0248 0.0078  172 ILE A CA  
1487 C C   . ILE A 172 ? 0.2742 0.2498 0.3007 -0.0318 -0.0236 0.0046  172 ILE A C   
1488 O O   . ILE A 172 ? 0.2668 0.2392 0.2915 -0.0334 -0.0231 0.0014  172 ILE A O   
1489 C CB  . ILE A 172 ? 0.3119 0.2969 0.3382 -0.0299 -0.0241 0.0098  172 ILE A CB  
1490 C CG1 . ILE A 172 ? 0.3267 0.3184 0.3527 -0.0310 -0.0251 0.0129  172 ILE A CG1 
1491 C CG2 . ILE A 172 ? 0.2958 0.2775 0.3199 -0.0289 -0.0229 0.0071  172 ILE A CG2 
1492 C CD1 . ILE A 172 ? 0.2986 0.2923 0.3219 -0.0345 -0.0260 0.0115  172 ILE A CD1 
1493 N N   . ILE A 173 ? 0.2777 0.2520 0.3064 -0.0291 -0.0229 0.0056  173 ILE A N   
1494 C CA  . ILE A 173 ? 0.2508 0.2201 0.2801 -0.0279 -0.0218 0.0034  173 ILE A CA  
1495 C C   . ILE A 173 ? 0.3146 0.2799 0.3444 -0.0304 -0.0218 0.0015  173 ILE A C   
1496 O O   . ILE A 173 ? 0.3820 0.3429 0.4110 -0.0303 -0.0208 -0.0014 173 ILE A O   
1497 C CB  . ILE A 173 ? 0.2928 0.2628 0.3245 -0.0249 -0.0213 0.0053  173 ILE A CB  
1498 C CG1 . ILE A 173 ? 0.2084 0.1810 0.2393 -0.0226 -0.0207 0.0061  173 ILE A CG1 
1499 C CG2 . ILE A 173 ? 0.2510 0.2168 0.2839 -0.0238 -0.0203 0.0037  173 ILE A CG2 
1500 C CD1 . ILE A 173 ? 0.2452 0.2195 0.2777 -0.0201 -0.0202 0.0080  173 ILE A CD1 
1501 N N   . LYS A 174 ? 0.2831 0.2496 0.3141 -0.0326 -0.0229 0.0031  174 LYS A N   
1502 C CA  . LYS A 174 ? 0.2800 0.2419 0.3115 -0.0353 -0.0228 0.0013  174 LYS A CA  
1503 C C   . LYS A 174 ? 0.2987 0.2584 0.3271 -0.0383 -0.0226 -0.0024 174 LYS A C   
1504 O O   . LYS A 174 ? 0.3137 0.2678 0.3421 -0.0398 -0.0216 -0.0051 174 LYS A O   
1505 C CB  . LYS A 174 ? 0.3111 0.2752 0.3446 -0.0375 -0.0241 0.0040  174 LYS A CB  
1506 C CG  . LYS A 174 ? 0.3641 0.3296 0.4009 -0.0349 -0.0240 0.0075  174 LYS A CG  
1507 C CD  . LYS A 174 ? 0.4529 0.4202 0.4920 -0.0374 -0.0251 0.0101  174 LYS A CD  
1508 C CE  . LYS A 174 ? 0.4856 0.4580 0.5270 -0.0350 -0.0255 0.0142  174 LYS A CE  
1509 N NZ  . LYS A 174 ? 0.5453 0.5155 0.5889 -0.0319 -0.0244 0.0151  174 LYS A NZ  
1510 N N   . LYS A 175 ? 0.2598 0.2237 0.2854 -0.0392 -0.0233 -0.0026 175 LYS A N   
1511 C CA  . LYS A 175 ? 0.2886 0.2518 0.3106 -0.0421 -0.0232 -0.0060 175 LYS A CA  
1512 C C   . LYS A 175 ? 0.3390 0.3001 0.3592 -0.0400 -0.0216 -0.0085 175 LYS A C   
1513 O O   . LYS A 175 ? 0.3419 0.3027 0.3590 -0.0422 -0.0213 -0.0114 175 LYS A O   
1514 C CB  . LYS A 175 ? 0.3261 0.2966 0.3463 -0.0445 -0.0249 -0.0041 175 LYS A CB  
1515 C CG  . LYS A 175 ? 0.3726 0.3460 0.3940 -0.0478 -0.0265 -0.0021 175 LYS A CG  
1516 C CD  . LYS A 175 ? 0.4106 0.3927 0.4323 -0.0478 -0.0281 0.0021  175 LYS A CD  
1517 C CE  . LYS A 175 ? 0.5793 0.5661 0.5974 -0.0511 -0.0291 0.0011  175 LYS A CE  
1518 N NZ  . LYS A 175 ? 0.6560 0.6498 0.6745 -0.0549 -0.0311 0.0037  175 LYS A NZ  
1519 N N   . THR A 176 ? 0.2713 0.2314 0.2934 -0.0360 -0.0207 -0.0075 176 THR A N   
1520 C CA  . THR A 176 ? 0.2823 0.2420 0.3029 -0.0341 -0.0195 -0.0091 176 THR A CA  
1521 C C   . THR A 176 ? 0.3234 0.2777 0.3429 -0.0345 -0.0178 -0.0131 176 THR A C   
1522 O O   . THR A 176 ? 0.3088 0.2635 0.3254 -0.0355 -0.0172 -0.0155 176 THR A O   
1523 C CB  . THR A 176 ? 0.3601 0.3207 0.3828 -0.0302 -0.0191 -0.0069 176 THR A CB  
1524 O OG1 . THR A 176 ? 0.2805 0.2459 0.3035 -0.0297 -0.0201 -0.0036 176 THR A OG1 
1525 C CG2 . THR A 176 ? 0.2622 0.2219 0.2837 -0.0284 -0.0177 -0.0086 176 THR A CG2 
1526 N N   . LEU A 177 ? 0.2401 0.1897 0.2622 -0.0336 -0.0169 -0.0137 177 LEU A N   
1527 C CA  . LEU A 177 ? 0.3210 0.2653 0.3426 -0.0337 -0.0149 -0.0174 177 LEU A CA  
1528 C C   . LEU A 177 ? 0.3478 0.2904 0.3662 -0.0380 -0.0149 -0.0207 177 LEU A C   
1529 O O   . LEU A 177 ? 0.2956 0.2358 0.3116 -0.0386 -0.0133 -0.0244 177 LEU A O   
1530 C CB  . LEU A 177 ? 0.3427 0.2823 0.3683 -0.0317 -0.0137 -0.0167 177 LEU A CB  
1531 C CG  . LEU A 177 ? 0.3408 0.2825 0.3694 -0.0276 -0.0135 -0.0139 177 LEU A CG  
1532 C CD1 . LEU A 177 ? 0.3188 0.2564 0.3513 -0.0256 -0.0122 -0.0131 177 LEU A CD1 
1533 C CD2 . LEU A 177 ? 0.4638 0.4073 0.4908 -0.0258 -0.0127 -0.0152 177 LEU A CD2 
1534 N N   . SER A 178 ? 0.2565 0.2008 0.2745 -0.0411 -0.0166 -0.0196 178 SER A N   
1535 C CA  . SER A 178 ? 0.2296 0.1734 0.2442 -0.0459 -0.0168 -0.0228 178 SER A CA  
1536 C C   . SER A 178 ? 0.2731 0.2218 0.2834 -0.0472 -0.0172 -0.0241 178 SER A C   
1537 O O   . SER A 178 ? 0.2350 0.1823 0.2418 -0.0502 -0.0164 -0.0281 178 SER A O   
1538 C CB  . SER A 178 ? 0.3418 0.2882 0.3570 -0.0493 -0.0189 -0.0206 178 SER A CB  
1539 O OG  . SER A 178 ? 0.3996 0.3405 0.4182 -0.0491 -0.0182 -0.0202 178 SER A OG  
1540 N N   . ILE A 179 ? 0.2492 0.2040 0.2597 -0.0452 -0.0184 -0.0206 179 ILE A N   
1541 C CA  . ILE A 179 ? 0.2990 0.2587 0.3057 -0.0465 -0.0188 -0.0213 179 ILE A CA  
1542 C C   . ILE A 179 ? 0.3184 0.2751 0.3236 -0.0449 -0.0166 -0.0246 179 ILE A C   
1543 O O   . ILE A 179 ? 0.2915 0.2498 0.2928 -0.0472 -0.0162 -0.0273 179 ILE A O   
1544 C CB  . ILE A 179 ? 0.3430 0.3096 0.3505 -0.0449 -0.0203 -0.0165 179 ILE A CB  
1545 C CG1 . ILE A 179 ? 0.3995 0.3721 0.4032 -0.0471 -0.0210 -0.0166 179 ILE A CG1 
1546 C CG2 . ILE A 179 ? 0.2808 0.2463 0.2906 -0.0401 -0.0193 -0.0148 179 ILE A CG2 
1547 C CD1 . ILE A 179 ? 0.4486 0.4288 0.4528 -0.0478 -0.0231 -0.0119 179 ILE A CD1 
1548 N N   . TYR A 180 ? 0.3020 0.2547 0.3101 -0.0410 -0.0151 -0.0244 180 TYR A N   
1549 C CA  . TYR A 180 ? 0.3052 0.2554 0.3124 -0.0394 -0.0129 -0.0273 180 TYR A CA  
1550 C C   . TYR A 180 ? 0.2984 0.2434 0.3035 -0.0417 -0.0112 -0.0322 180 TYR A C   
1551 O O   . TYR A 180 ? 0.2871 0.2326 0.2889 -0.0428 -0.0099 -0.0353 180 TYR A O   
1552 C CB  . TYR A 180 ? 0.3373 0.2852 0.3483 -0.0350 -0.0119 -0.0257 180 TYR A CB  
1553 C CG  . TYR A 180 ? 0.3245 0.2772 0.3363 -0.0328 -0.0128 -0.0222 180 TYR A CG  
1554 C CD1 . TYR A 180 ? 0.2434 0.1988 0.2532 -0.0322 -0.0122 -0.0226 180 TYR A CD1 
1555 C CD2 . TYR A 180 ? 0.2229 0.1772 0.2373 -0.0315 -0.0142 -0.0186 180 TYR A CD2 
1556 C CE1 . TYR A 180 ? 0.2028 0.1618 0.2134 -0.0305 -0.0128 -0.0196 180 TYR A CE1 
1557 C CE2 . TYR A 180 ? 0.2051 0.1630 0.2201 -0.0297 -0.0147 -0.0159 180 TYR A CE2 
1558 C CZ  . TYR A 180 ? 0.2481 0.2079 0.2613 -0.0292 -0.0140 -0.0164 180 TYR A CZ  
1559 O OH  . TYR A 180 ? 0.2985 0.2609 0.3124 -0.0275 -0.0143 -0.0137 180 TYR A OH  
1560 N N   . ARG A 181 ? 0.3314 0.2715 0.3384 -0.0429 -0.0109 -0.0330 181 ARG A N   
1561 C CA  . ARG A 181 ? 0.2910 0.2254 0.2960 -0.0455 -0.0090 -0.0380 181 ARG A CA  
1562 C C   . ARG A 181 ? 0.3503 0.2883 0.3499 -0.0505 -0.0099 -0.0406 181 ARG A C   
1563 O O   . ARG A 181 ? 0.3174 0.2530 0.3135 -0.0522 -0.0080 -0.0454 181 ARG A O   
1564 C CB  . ARG A 181 ? 0.2877 0.2162 0.2958 -0.0462 -0.0087 -0.0378 181 ARG A CB  
1565 C CG  . ARG A 181 ? 0.2858 0.2109 0.2995 -0.0416 -0.0078 -0.0349 181 ARG A CG  
1566 C CD  . ARG A 181 ? 0.3779 0.2966 0.3944 -0.0428 -0.0072 -0.0350 181 ARG A CD  
1567 N NE  . ARG A 181 ? 0.5137 0.4310 0.5356 -0.0386 -0.0068 -0.0311 181 ARG A NE  
1568 C CZ  . ARG A 181 ? 0.5622 0.4823 0.5869 -0.0382 -0.0089 -0.0267 181 ARG A CZ  
1569 N NH1 . ARG A 181 ? 0.5143 0.4385 0.5372 -0.0416 -0.0113 -0.0255 181 ARG A NH1 
1570 N NH2 . ARG A 181 ? 0.6061 0.5254 0.6353 -0.0344 -0.0084 -0.0234 181 ARG A NH2 
1571 N N   . GLU A 182 ? 0.3471 0.2913 0.3458 -0.0529 -0.0128 -0.0376 182 GLU A N   
1572 C CA  . GLU A 182 ? 0.4107 0.3599 0.4046 -0.0580 -0.0141 -0.0394 182 GLU A CA  
1573 C C   . GLU A 182 ? 0.3675 0.3214 0.3576 -0.0577 -0.0135 -0.0406 182 GLU A C   
1574 O O   . GLU A 182 ? 0.3273 0.2814 0.3128 -0.0611 -0.0125 -0.0450 182 GLU A O   
1575 C CB  . GLU A 182 ? 0.4095 0.3656 0.4041 -0.0599 -0.0172 -0.0349 182 GLU A CB  
1576 C CG  . GLU A 182 ? 0.5187 0.4810 0.5084 -0.0654 -0.0188 -0.0364 182 GLU A CG  
1577 C CD  . GLU A 182 ? 0.5976 0.5673 0.5885 -0.0674 -0.0218 -0.0317 182 GLU A CD  
1578 O OE1 . GLU A 182 ? 0.6477 0.6187 0.6428 -0.0639 -0.0227 -0.0269 182 GLU A OE1 
1579 O OE2 . GLU A 182 ? 0.5249 0.4996 0.5124 -0.0727 -0.0233 -0.0328 182 GLU A OE2 
1580 N N   . ILE A 183 ? 0.3240 0.2819 0.3157 -0.0540 -0.0140 -0.0367 183 ILE A N   
1581 C CA  . ILE A 183 ? 0.3060 0.2688 0.2945 -0.0539 -0.0135 -0.0372 183 ILE A CA  
1582 C C   . ILE A 183 ? 0.3261 0.2835 0.3133 -0.0527 -0.0104 -0.0420 183 ILE A C   
1583 O O   . ILE A 183 ? 0.3397 0.3000 0.3228 -0.0543 -0.0095 -0.0446 183 ILE A O   
1584 C CB  . ILE A 183 ? 0.3094 0.2769 0.3003 -0.0503 -0.0145 -0.0320 183 ILE A CB  
1585 C CG1 . ILE A 183 ? 0.3757 0.3381 0.3708 -0.0455 -0.0130 -0.0311 183 ILE A CG1 
1586 C CG2 . ILE A 183 ? 0.3480 0.3205 0.3403 -0.0511 -0.0172 -0.0273 183 ILE A CG2 
1587 C CD1 . ILE A 183 ? 0.3438 0.3064 0.3384 -0.0430 -0.0112 -0.0321 183 ILE A CD1 
1588 N N   . LYS A 184 ? 0.2953 0.2454 0.2862 -0.0498 -0.0086 -0.0431 184 LYS A N   
1589 C CA  . LYS A 184 ? 0.3749 0.3196 0.3652 -0.0483 -0.0053 -0.0475 184 LYS A CA  
1590 C C   . LYS A 184 ? 0.3828 0.3238 0.3690 -0.0526 -0.0039 -0.0532 184 LYS A C   
1591 O O   . LYS A 184 ? 0.4170 0.3578 0.3996 -0.0534 -0.0018 -0.0572 184 LYS A O   
1592 C CB  . LYS A 184 ? 0.3675 0.3061 0.3633 -0.0440 -0.0039 -0.0463 184 LYS A CB  
1593 C CG  . LYS A 184 ? 0.3972 0.3305 0.3935 -0.0417 -0.0002 -0.0501 184 LYS A CG  
1594 C CD  . LYS A 184 ? 0.4181 0.3464 0.4203 -0.0374 0.0010  -0.0481 184 LYS A CD  
1595 C CE  . LYS A 184 ? 0.4155 0.3385 0.4186 -0.0349 0.0048  -0.0516 184 LYS A CE  
1596 N NZ  . LYS A 184 ? 0.4245 0.3425 0.4240 -0.0384 0.0069  -0.0573 184 LYS A NZ  
1597 N N   . GLU A 185 ? 0.2577 0.1958 0.2444 -0.0556 -0.0049 -0.0537 185 GLU A N   
1598 C CA  . GLU A 185 ? 0.3322 0.2661 0.3149 -0.0603 -0.0035 -0.0595 185 GLU A CA  
1599 C C   . GLU A 185 ? 0.3551 0.2967 0.3315 -0.0650 -0.0048 -0.0614 185 GLU A C   
1600 O O   . GLU A 185 ? 0.3677 0.3072 0.3396 -0.0679 -0.0027 -0.0671 185 GLU A O   
1601 C CB  . GLU A 185 ? 0.3466 0.2765 0.3315 -0.0629 -0.0047 -0.0589 185 GLU A CB  
1602 C CG  . GLU A 185 ? 0.4438 0.3673 0.4254 -0.0677 -0.0029 -0.0652 185 GLU A CG  
1603 C CD  . GLU A 185 ? 0.4922 0.4078 0.4779 -0.0681 -0.0025 -0.0647 185 GLU A CD  
1604 O OE1 . GLU A 185 ? 0.4875 0.4030 0.4786 -0.0642 -0.0036 -0.0595 185 GLU A OE1 
1605 O OE2 . GLU A 185 ? 0.5888 0.4985 0.5722 -0.0724 -0.0011 -0.0696 185 GLU A OE2 
1606 N N   . GLU A 186 ? 0.3520 0.3026 0.3281 -0.0658 -0.0080 -0.0566 186 GLU A N   
1607 C CA  . GLU A 186 ? 0.3856 0.3448 0.3561 -0.0704 -0.0096 -0.0574 186 GLU A CA  
1608 C C   . GLU A 186 ? 0.4050 0.3684 0.3727 -0.0687 -0.0082 -0.0580 186 GLU A C   
1609 O O   . GLU A 186 ? 0.4248 0.3956 0.3875 -0.0724 -0.0091 -0.0589 186 GLU A O   
1610 C CB  . GLU A 186 ? 0.4371 0.4048 0.4087 -0.0716 -0.0134 -0.0514 186 GLU A CB  
1611 C CG  . GLU A 186 ? 0.4786 0.4437 0.4524 -0.0742 -0.0149 -0.0507 186 GLU A CG  
1612 C CD  . GLU A 186 ? 0.5014 0.4753 0.4767 -0.0750 -0.0184 -0.0446 186 GLU A CD  
1613 O OE1 . GLU A 186 ? 0.5486 0.5275 0.5258 -0.0713 -0.0193 -0.0398 186 GLU A OE1 
1614 O OE2 . GLU A 186 ? 0.4996 0.4754 0.4744 -0.0794 -0.0202 -0.0445 186 GLU A OE2 
1615 N N   . GLY A 187 ? 0.3666 0.3261 0.3374 -0.0635 -0.0061 -0.0574 187 GLY A N   
1616 C CA  . GLY A 187 ? 0.3576 0.3213 0.3261 -0.0620 -0.0048 -0.0578 187 GLY A CA  
1617 C C   . GLY A 187 ? 0.3248 0.2972 0.2942 -0.0606 -0.0072 -0.0516 187 GLY A C   
1618 O O   . GLY A 187 ? 0.3600 0.3381 0.3265 -0.0609 -0.0068 -0.0514 187 GLY A O   
1619 N N   . LYS A 188 ? 0.3162 0.2898 0.2896 -0.0592 -0.0096 -0.0465 188 LYS A N   
1620 C CA  . LYS A 188 ? 0.3887 0.3696 0.3633 -0.0575 -0.0115 -0.0406 188 LYS A CA  
1621 C C   . LYS A 188 ? 0.3293 0.3078 0.3077 -0.0524 -0.0102 -0.0383 188 LYS A C   
1622 O O   . LYS A 188 ? 0.2874 0.2711 0.2663 -0.0509 -0.0109 -0.0343 188 LYS A O   
1623 C CB  . LYS A 188 ? 0.3857 0.3695 0.3627 -0.0583 -0.0144 -0.0361 188 LYS A CB  
1624 C CG  . LYS A 188 ? 0.4019 0.3902 0.3754 -0.0639 -0.0162 -0.0373 188 LYS A CG  
1625 C CD  . LYS A 188 ? 0.5028 0.4927 0.4797 -0.0640 -0.0187 -0.0330 188 LYS A CD  
1626 C CE  . LYS A 188 ? 0.5200 0.5182 0.4939 -0.0692 -0.0212 -0.0319 188 LYS A CE  
1627 N NZ  . LYS A 188 ? 0.5664 0.5620 0.5358 -0.0744 -0.0205 -0.0383 188 LYS A NZ  
1628 N N   . GLY A 189 ? 0.3334 0.3044 0.3147 -0.0497 -0.0083 -0.0406 189 GLY A N   
1629 C CA  . GLY A 189 ? 0.3899 0.3590 0.3744 -0.0452 -0.0068 -0.0392 189 GLY A CA  
1630 C C   . GLY A 189 ? 0.3536 0.3150 0.3407 -0.0429 -0.0046 -0.0423 189 GLY A C   
1631 O O   . GLY A 189 ? 0.3400 0.2966 0.3274 -0.0443 -0.0043 -0.0448 189 GLY A O   
1632 N N   . SER A 190 ? 0.3330 0.2936 0.3225 -0.0394 -0.0029 -0.0418 190 SER A N   
1633 C CA  . SER A 190 ? 0.2844 0.2389 0.2774 -0.0364 -0.0007 -0.0435 190 SER A CA  
1634 C C   . SER A 190 ? 0.2747 0.2282 0.2727 -0.0335 -0.0020 -0.0394 190 SER A C   
1635 O O   . SER A 190 ? 0.2577 0.2152 0.2564 -0.0330 -0.0038 -0.0356 190 SER A O   
1636 C CB  . SER A 190 ? 0.2405 0.1956 0.2332 -0.0344 0.0020  -0.0455 190 SER A CB  
1637 O OG  . SER A 190 ? 0.2979 0.2532 0.2857 -0.0370 0.0037  -0.0500 190 SER A OG  
1638 N N   . VAL A 191 ? 0.2632 0.2113 0.2647 -0.0315 -0.0009 -0.0401 191 VAL A N   
1639 C CA  . VAL A 191 ? 0.2516 0.1991 0.2578 -0.0287 -0.0019 -0.0364 191 VAL A CA  
1640 C C   . VAL A 191 ? 0.2605 0.2061 0.2701 -0.0251 0.0004  -0.0368 191 VAL A C   
1641 O O   . VAL A 191 ? 0.2957 0.2371 0.3058 -0.0244 0.0028  -0.0398 191 VAL A O   
1642 C CB  . VAL A 191 ? 0.2556 0.1997 0.2636 -0.0295 -0.0032 -0.0355 191 VAL A CB  
1643 C CG1 . VAL A 191 ? 0.2889 0.2337 0.3014 -0.0267 -0.0043 -0.0314 191 VAL A CG1 
1644 C CG2 . VAL A 191 ? 0.2592 0.2061 0.2639 -0.0333 -0.0055 -0.0350 191 VAL A CG2 
1645 N N   . SER A 192 ? 0.2274 0.1762 0.2395 -0.0229 -0.0002 -0.0337 192 SER A N   
1646 C CA  . SER A 192 ? 0.2416 0.1903 0.2573 -0.0197 0.0015  -0.0333 192 SER A CA  
1647 C C   . SER A 192 ? 0.2341 0.1827 0.2540 -0.0177 0.0002  -0.0299 192 SER A C   
1648 O O   . SER A 192 ? 0.2403 0.1890 0.2602 -0.0188 -0.0019 -0.0280 192 SER A O   
1649 C CB  . SER A 192 ? 0.2626 0.2162 0.2773 -0.0192 0.0020  -0.0327 192 SER A CB  
1650 O OG  . SER A 192 ? 0.2423 0.1992 0.2573 -0.0197 -0.0002 -0.0295 192 SER A OG  
1651 N N   . THR A 193 ? 0.2624 0.2115 0.2861 -0.0148 0.0016  -0.0290 193 THR A N   
1652 C CA  . THR A 193 ? 0.2856 0.2364 0.3132 -0.0130 0.0004  -0.0256 193 THR A CA  
1653 C C   . THR A 193 ? 0.3157 0.2710 0.3453 -0.0112 0.0012  -0.0244 193 THR A C   
1654 O O   . THR A 193 ? 0.2811 0.2379 0.3093 -0.0112 0.0027  -0.0261 193 THR A O   
1655 C CB  . THR A 193 ? 0.2911 0.2379 0.3220 -0.0115 0.0010  -0.0249 193 THR A CB  
1656 O OG1 . THR A 193 ? 0.3001 0.2492 0.3339 -0.0105 -0.0007 -0.0214 193 THR A OG1 
1657 C CG2 . THR A 193 ? 0.2828 0.2278 0.3166 -0.0088 0.0040  -0.0260 193 THR A CG2 
1658 N N   . SER A 194 ? 0.2910 0.2491 0.3236 -0.0099 0.0001  -0.0215 194 SER A N   
1659 C CA  . SER A 194 ? 0.2996 0.2626 0.3346 -0.0085 0.0005  -0.0200 194 SER A CA  
1660 C C   . SER A 194 ? 0.2596 0.2234 0.2995 -0.0058 0.0011  -0.0178 194 SER A C   
1661 O O   . SER A 194 ? 0.2397 0.2005 0.2809 -0.0054 0.0006  -0.0169 194 SER A O   
1662 C CB  . SER A 194 ? 0.2144 0.1809 0.2482 -0.0101 -0.0015 -0.0184 194 SER A CB  
1663 O OG  . SER A 194 ? 0.2660 0.2318 0.2957 -0.0124 -0.0020 -0.0197 194 SER A OG  
1664 N N   . PRO A 195 ? 0.2183 0.1867 0.2612 -0.0040 0.0021  -0.0166 195 PRO A N   
1665 C CA  . PRO A 195 ? 0.2510 0.2218 0.2988 -0.0015 0.0022  -0.0136 195 PRO A CA  
1666 C C   . PRO A 195 ? 0.2132 0.1849 0.2612 -0.0025 -0.0003 -0.0114 195 PRO A C   
1667 O O   . PRO A 195 ? 0.2837 0.2566 0.3287 -0.0048 -0.0020 -0.0116 195 PRO A O   
1668 C CB  . PRO A 195 ? 0.3238 0.3016 0.3738 -0.0006 0.0028  -0.0123 195 PRO A CB  
1669 C CG  . PRO A 195 ? 0.4351 0.4122 0.4823 -0.0016 0.0042  -0.0152 195 PRO A CG  
1670 C CD  . PRO A 195 ? 0.3101 0.2825 0.3524 -0.0043 0.0031  -0.0175 195 PRO A CD  
1671 N N   . TYR A 196 ? 0.2531 0.2241 0.3047 -0.0005 -0.0001 -0.0090 196 TYR A N   
1672 C CA  . TYR A 196 ? 0.2440 0.2130 0.2953 -0.0013 -0.0018 -0.0076 196 TYR A CA  
1673 C C   . TYR A 196 ? 0.2507 0.2235 0.2997 -0.0034 -0.0042 -0.0068 196 TYR A C   
1674 O O   . TYR A 196 ? 0.2662 0.2361 0.3120 -0.0053 -0.0054 -0.0078 196 TYR A O   
1675 C CB  . TYR A 196 ? 0.2297 0.1997 0.2862 0.0014  -0.0013 -0.0041 196 TYR A CB  
1676 C CG  . TYR A 196 ? 0.2360 0.2014 0.2925 0.0009  -0.0021 -0.0032 196 TYR A CG  
1677 C CD1 . TYR A 196 ? 0.1912 0.1586 0.2460 -0.0008 -0.0045 -0.0020 196 TYR A CD1 
1678 C CD2 . TYR A 196 ? 0.2949 0.2538 0.3532 0.0021  -0.0003 -0.0037 196 TYR A CD2 
1679 C CE1 . TYR A 196 ? 0.2534 0.2172 0.3085 -0.0014 -0.0052 -0.0009 196 TYR A CE1 
1680 C CE2 . TYR A 196 ? 0.2769 0.2318 0.3354 0.0013  -0.0011 -0.0028 196 TYR A CE2 
1681 C CZ  . TYR A 196 ? 0.3184 0.2761 0.3754 -0.0004 -0.0036 -0.0012 196 TYR A CZ  
1682 O OH  . TYR A 196 ? 0.2945 0.2486 0.3521 -0.0013 -0.0043 0.0000  196 TYR A OH  
1683 N N   . TYR A 197 ? 0.2268 0.2061 0.2774 -0.0031 -0.0048 -0.0050 197 TYR A N   
1684 C CA  . TYR A 197 ? 0.2616 0.2441 0.3101 -0.0051 -0.0068 -0.0045 197 TYR A CA  
1685 C C   . TYR A 197 ? 0.2154 0.1994 0.2608 -0.0072 -0.0068 -0.0066 197 TYR A C   
1686 O O   . TYR A 197 ? 0.1621 0.1497 0.2065 -0.0087 -0.0079 -0.0063 197 TYR A O   
1687 C CB  . TYR A 197 ? 0.2243 0.2131 0.2759 -0.0042 -0.0076 -0.0013 197 TYR A CB  
1688 C CG  . TYR A 197 ? 0.2120 0.1990 0.2663 -0.0025 -0.0078 0.0012  197 TYR A CG  
1689 C CD1 . TYR A 197 ? 0.2117 0.1958 0.2640 -0.0037 -0.0090 0.0013  197 TYR A CD1 
1690 C CD2 . TYR A 197 ? 0.2554 0.2434 0.3144 0.0003  -0.0065 0.0037  197 TYR A CD2 
1691 C CE1 . TYR A 197 ? 0.2154 0.1978 0.2702 -0.0024 -0.0091 0.0037  197 TYR A CE1 
1692 C CE2 . TYR A 197 ? 0.2460 0.2318 0.3077 0.0018  -0.0064 0.0062  197 TYR A CE2 
1693 C CZ  . TYR A 197 ? 0.2580 0.2410 0.3174 0.0002  -0.0078 0.0062  197 TYR A CZ  
1694 O OH  . TYR A 197 ? 0.3793 0.3602 0.4413 0.0014  -0.0078 0.0088  197 TYR A OH  
1695 N N   . HIS A 198 ? 0.1883 0.1693 0.2322 -0.0075 -0.0056 -0.0088 198 HIS A N   
1696 C CA  . HIS A 198 ? 0.1941 0.1759 0.2351 -0.0095 -0.0056 -0.0106 198 HIS A CA  
1697 C C   . HIS A 198 ? 0.2793 0.2676 0.3218 -0.0100 -0.0056 -0.0097 198 HIS A C   
1698 O O   . HIS A 198 ? 0.2277 0.2174 0.2682 -0.0122 -0.0064 -0.0102 198 HIS A O   
1699 C CB  . HIS A 198 ? 0.2105 0.1896 0.2480 -0.0115 -0.0069 -0.0111 198 HIS A CB  
1700 C CG  . HIS A 198 ? 0.2105 0.1883 0.2449 -0.0134 -0.0065 -0.0128 198 HIS A CG  
1701 N ND1 . HIS A 198 ? 0.2595 0.2398 0.2929 -0.0151 -0.0067 -0.0129 198 HIS A ND1 
1702 C CD2 . HIS A 198 ? 0.2361 0.2105 0.2681 -0.0140 -0.0060 -0.0142 198 HIS A CD2 
1703 C CE1 . HIS A 198 ? 0.2509 0.2290 0.2817 -0.0164 -0.0062 -0.0140 198 HIS A CE1 
1704 N NE2 . HIS A 198 ? 0.2302 0.2052 0.2601 -0.0157 -0.0058 -0.0147 198 HIS A NE2 
1705 N N   . PRO A 199 ? 0.2905 0.2829 0.3367 -0.0081 -0.0046 -0.0084 199 PRO A N   
1706 C CA  . PRO A 199 ? 0.2781 0.2777 0.3259 -0.0089 -0.0048 -0.0074 199 PRO A CA  
1707 C C   . PRO A 199 ? 0.2855 0.2859 0.3321 -0.0101 -0.0036 -0.0090 199 PRO A C   
1708 O O   . PRO A 199 ? 0.2962 0.2922 0.3411 -0.0098 -0.0025 -0.0108 199 PRO A O   
1709 C CB  . PRO A 199 ? 0.2714 0.2753 0.3242 -0.0059 -0.0042 -0.0046 199 PRO A CB  
1710 C CG  . PRO A 199 ? 0.2376 0.2357 0.2911 -0.0035 -0.0024 -0.0054 199 PRO A CG  
1711 C CD  . PRO A 199 ? 0.3157 0.3064 0.3650 -0.0051 -0.0032 -0.0076 199 PRO A CD  
1712 N N   . LEU A 200 ? 0.3084 0.3153 0.3560 -0.0116 -0.0039 -0.0084 200 LEU A N   
1713 C CA  . LEU A 200 ? 0.1951 0.2046 0.2427 -0.0125 -0.0027 -0.0092 200 LEU A CA  
1714 C C   . LEU A 200 ? 0.2303 0.2440 0.2822 -0.0094 -0.0012 -0.0077 200 LEU A C   
1715 O O   . LEU A 200 ? 0.2314 0.2528 0.2868 -0.0091 -0.0014 -0.0055 200 LEU A O   
1716 C CB  . LEU A 200 ? 0.2677 0.2819 0.3144 -0.0159 -0.0037 -0.0093 200 LEU A CB  
1717 C CG  . LEU A 200 ? 0.3698 0.3790 0.4122 -0.0189 -0.0046 -0.0111 200 LEU A CG  
1718 C CD1 . LEU A 200 ? 0.4560 0.4700 0.4980 -0.0223 -0.0054 -0.0112 200 LEU A CD1 
1719 C CD2 . LEU A 200 ? 0.4331 0.4370 0.4727 -0.0196 -0.0036 -0.0127 200 LEU A CD2 
1720 N N   . ILE A 201 ? 0.3027 0.3118 0.3546 -0.0072 0.0006  -0.0088 201 ILE A N   
1721 C CA  . ILE A 201 ? 0.2946 0.3065 0.3507 -0.0038 0.0027  -0.0076 201 ILE A CA  
1722 C C   . ILE A 201 ? 0.3088 0.3289 0.3672 -0.0042 0.0035  -0.0065 201 ILE A C   
1723 O O   . ILE A 201 ? 0.2255 0.2519 0.2887 -0.0018 0.0042  -0.0038 201 ILE A O   
1724 C CB  . ILE A 201 ? 0.2880 0.2928 0.3426 -0.0020 0.0047  -0.0100 201 ILE A CB  
1725 C CG1 . ILE A 201 ? 0.2613 0.2591 0.3147 -0.0014 0.0040  -0.0104 201 ILE A CG1 
1726 C CG2 . ILE A 201 ? 0.2427 0.2500 0.3015 0.0016  0.0075  -0.0092 201 ILE A CG2 
1727 C CD1 . ILE A 201 ? 0.2018 0.2005 0.2599 0.0018  0.0045  -0.0077 201 ILE A CD1 
1728 N N   . PRO A 202 ? 0.2368 0.2578 0.2924 -0.0070 0.0035  -0.0081 202 PRO A N   
1729 C CA  . PRO A 202 ? 0.2237 0.2530 0.2819 -0.0075 0.0044  -0.0069 202 PRO A CA  
1730 C C   . PRO A 202 ? 0.2474 0.2852 0.3087 -0.0087 0.0027  -0.0042 202 PRO A C   
1731 O O   . PRO A 202 ? 0.1904 0.2365 0.2558 -0.0075 0.0036  -0.0019 202 PRO A O   
1732 C CB  . PRO A 202 ? 0.1958 0.2232 0.2499 -0.0111 0.0043  -0.0090 202 PRO A CB  
1733 C CG  . PRO A 202 ? 0.2117 0.2299 0.2618 -0.0107 0.0046  -0.0114 202 PRO A CG  
1734 C CD  . PRO A 202 ? 0.2257 0.2402 0.2761 -0.0095 0.0032  -0.0108 202 PRO A CD  
1735 N N   . ILE A 203 ? 0.1966 0.2331 0.2558 -0.0110 0.0005  -0.0042 203 ILE A N   
1736 C CA  . ILE A 203 ? 0.2277 0.2727 0.2893 -0.0126 -0.0012 -0.0020 203 ILE A CA  
1737 C C   . ILE A 203 ? 0.2351 0.2843 0.3015 -0.0087 -0.0010 0.0014  203 ILE A C   
1738 O O   . ILE A 203 ? 0.2530 0.3120 0.3235 -0.0081 -0.0011 0.0043  203 ILE A O   
1739 C CB  . ILE A 203 ? 0.2841 0.3261 0.3415 -0.0164 -0.0033 -0.0035 203 ILE A CB  
1740 C CG1 . ILE A 203 ? 0.3239 0.3643 0.3780 -0.0205 -0.0033 -0.0059 203 ILE A CG1 
1741 C CG2 . ILE A 203 ? 0.1791 0.2294 0.2385 -0.0177 -0.0051 -0.0013 203 ILE A CG2 
1742 C CD1 . ILE A 203 ? 0.3605 0.3974 0.4106 -0.0242 -0.0048 -0.0076 203 ILE A CD1 
1743 N N   . LEU A 204 ? 0.1852 0.2274 0.2514 -0.0059 -0.0007 0.0012  204 LEU A N   
1744 C CA  . LEU A 204 ? 0.2350 0.2798 0.3060 -0.0018 0.0000  0.0046  204 LEU A CA  
1745 C C   . LEU A 204 ? 0.2194 0.2694 0.2954 0.0016  0.0024  0.0066  204 LEU A C   
1746 O O   . LEU A 204 ? 0.1940 0.2521 0.2753 0.0039  0.0026  0.0106  204 LEU A O   
1747 C CB  . LEU A 204 ? 0.2186 0.2534 0.2884 0.0004  0.0005  0.0036  204 LEU A CB  
1748 C CG  . LEU A 204 ? 0.2035 0.2334 0.2693 -0.0021 -0.0017 0.0023  204 LEU A CG  
1749 C CD1 . LEU A 204 ? 0.2382 0.2611 0.3047 0.0006  -0.0012 0.0028  204 LEU A CD1 
1750 C CD2 . LEU A 204 ? 0.1984 0.2364 0.2649 -0.0042 -0.0039 0.0045  204 LEU A CD2 
1751 N N   . LEU A 205 ? 0.2123 0.2581 0.2869 0.0021  0.0045  0.0041  205 LEU A N   
1752 C CA  . LEU A 205 ? 0.2738 0.3243 0.3530 0.0056  0.0073  0.0056  205 LEU A CA  
1753 C C   . LEU A 205 ? 0.2598 0.3223 0.3415 0.0037  0.0066  0.0079  205 LEU A C   
1754 O O   . LEU A 205 ? 0.2670 0.3378 0.3545 0.0067  0.0079  0.0115  205 LEU A O   
1755 C CB  . LEU A 205 ? 0.2512 0.2944 0.3275 0.0063  0.0097  0.0020  205 LEU A CB  
1756 C CG  . LEU A 205 ? 0.2617 0.2939 0.3362 0.0084  0.0108  -0.0001 205 LEU A CG  
1757 C CD1 . LEU A 205 ? 0.2548 0.2810 0.3257 0.0082  0.0130  -0.0041 205 LEU A CD1 
1758 C CD2 . LEU A 205 ? 0.2400 0.2731 0.3204 0.0134  0.0127  0.0029  205 LEU A CD2 
1759 N N   . ASN A 206 ? 0.1793 0.2430 0.2571 -0.0013 0.0048  0.0059  206 ASN A N   
1760 C CA  . ASN A 206 ? 0.1622 0.2367 0.2420 -0.0036 0.0044  0.0075  206 ASN A CA  
1761 C C   . ASN A 206 ? 0.1997 0.2744 0.2749 -0.0097 0.0019  0.0055  206 ASN A C   
1762 O O   . ASN A 206 ? 0.2252 0.2954 0.2966 -0.0125 0.0022  0.0026  206 ASN A O   
1763 C CB  . ASN A 206 ? 0.2062 0.2816 0.2870 -0.0022 0.0072  0.0067  206 ASN A CB  
1764 C CG  . ASN A 206 ? 0.3037 0.3902 0.3864 -0.0051 0.0068  0.0082  206 ASN A CG  
1765 O OD1 . ASN A 206 ? 0.2876 0.3829 0.3723 -0.0074 0.0048  0.0107  206 ASN A OD1 
1766 N ND2 . ASN A 206 ? 0.2861 0.3727 0.3681 -0.0054 0.0088  0.0068  206 ASN A ND2 
1767 N N   . PRO A 207 ? 0.2254 0.3052 0.3010 -0.0118 -0.0005 0.0071  207 PRO A N   
1768 C CA  . PRO A 207 ? 0.2174 0.2961 0.2883 -0.0175 -0.0027 0.0046  207 PRO A CA  
1769 C C   . PRO A 207 ? 0.3225 0.4052 0.3924 -0.0217 -0.0025 0.0035  207 PRO A C   
1770 O O   . PRO A 207 ? 0.2730 0.3512 0.3385 -0.0261 -0.0034 0.0007  207 PRO A O   
1771 C CB  . PRO A 207 ? 0.2613 0.3480 0.3340 -0.0187 -0.0048 0.0072  207 PRO A CB  
1772 C CG  . PRO A 207 ? 0.3343 0.4216 0.4113 -0.0130 -0.0040 0.0104  207 PRO A CG  
1773 C CD  . PRO A 207 ? 0.3059 0.3921 0.3860 -0.0089 -0.0012 0.0110  207 PRO A CD  
1774 N N   . ASN A 208 ? 0.2883 0.3793 0.3624 -0.0203 -0.0011 0.0057  208 ASN A N   
1775 C CA  . ASN A 208 ? 0.2974 0.3929 0.3710 -0.0243 -0.0008 0.0050  208 ASN A CA  
1776 C C   . ASN A 208 ? 0.2996 0.3860 0.3696 -0.0246 0.0008  0.0021  208 ASN A C   
1777 O O   . ASN A 208 ? 0.2363 0.3249 0.3053 -0.0284 0.0010  0.0013  208 ASN A O   
1778 C CB  . ASN A 208 ? 0.2714 0.3796 0.3511 -0.0225 0.0002  0.0088  208 ASN A CB  
1779 C CG  . ASN A 208 ? 0.2895 0.4088 0.3726 -0.0233 -0.0018 0.0121  208 ASN A CG  
1780 O OD1 . ASN A 208 ? 0.3003 0.4207 0.3806 -0.0279 -0.0041 0.0109  208 ASN A OD1 
1781 N ND2 . ASN A 208 ? 0.3452 0.4732 0.4345 -0.0187 -0.0007 0.0163  208 ASN A ND2 
1782 N N   . CYS A 209 ? 0.3050 0.3817 0.3732 -0.0210 0.0020  0.0006  209 CYS A N   
1783 C CA  . CYS A 209 ? 0.3359 0.4047 0.4004 -0.0216 0.0034  -0.0020 209 CYS A CA  
1784 C C   . CYS A 209 ? 0.3450 0.4083 0.4047 -0.0267 0.0019  -0.0044 209 CYS A C   
1785 O O   . CYS A 209 ? 0.2610 0.3199 0.3180 -0.0281 0.0030  -0.0059 209 CYS A O   
1786 C CB  . CYS A 209 ? 0.3064 0.3664 0.3697 -0.0173 0.0046  -0.0033 209 CYS A CB  
1787 S SG  . CYS A 209 ? 0.3334 0.3839 0.3928 -0.0178 0.0026  -0.0049 209 CYS A SG  
1788 N N   . VAL A 210 ? 0.3297 0.3934 0.3882 -0.0294 -0.0002 -0.0046 210 VAL A N   
1789 C CA  . VAL A 210 ? 0.2765 0.3346 0.3307 -0.0342 -0.0011 -0.0069 210 VAL A CA  
1790 C C   . VAL A 210 ? 0.2233 0.2862 0.2777 -0.0385 -0.0007 -0.0069 210 VAL A C   
1791 O O   . VAL A 210 ? 0.2077 0.2645 0.2588 -0.0417 -0.0004 -0.0087 210 VAL A O   
1792 C CB  . VAL A 210 ? 0.3490 0.4071 0.4020 -0.0361 -0.0031 -0.0074 210 VAL A CB  
1793 C CG1 . VAL A 210 ? 0.2807 0.3340 0.3337 -0.0317 -0.0035 -0.0071 210 VAL A CG1 
1794 C CG2 . VAL A 210 ? 0.3461 0.4159 0.4022 -0.0384 -0.0043 -0.0056 210 VAL A CG2 
1795 N N   . TYR A 211 ? 0.2306 0.3044 0.2891 -0.0387 -0.0005 -0.0047 211 TYR A N   
1796 C CA  . TYR A 211 ? 0.2654 0.3449 0.3247 -0.0431 -0.0002 -0.0044 211 TYR A CA  
1797 C C   . TYR A 211 ? 0.2918 0.3687 0.3507 -0.0420 0.0020  -0.0044 211 TYR A C   
1798 O O   . TYR A 211 ? 0.3525 0.4335 0.4119 -0.0456 0.0025  -0.0040 211 TYR A O   
1799 C CB  . TYR A 211 ? 0.2472 0.3405 0.3114 -0.0434 -0.0007 -0.0015 211 TYR A CB  
1800 C CG  . TYR A 211 ? 0.2697 0.3674 0.3344 -0.0448 -0.0029 -0.0011 211 TYR A CG  
1801 C CD1 . TYR A 211 ? 0.3278 0.4221 0.3887 -0.0501 -0.0044 -0.0035 211 TYR A CD1 
1802 C CD2 . TYR A 211 ? 0.3319 0.4368 0.4007 -0.0407 -0.0032 0.0018  211 TYR A CD2 
1803 C CE1 . TYR A 211 ? 0.3595 0.4583 0.4204 -0.0515 -0.0063 -0.0033 211 TYR A CE1 
1804 C CE2 . TYR A 211 ? 0.3665 0.4763 0.4357 -0.0420 -0.0053 0.0026  211 TYR A CE2 
1805 C CZ  . TYR A 211 ? 0.4175 0.5245 0.4826 -0.0475 -0.0069 -0.0001 211 TYR A CZ  
1806 O OH  . TYR A 211 ? 0.4803 0.5928 0.5454 -0.0489 -0.0089 0.0005  211 TYR A OH  
1807 N N   . GLU A 212 ? 0.2701 0.3408 0.3280 -0.0374 0.0033  -0.0049 212 GLU A N   
1808 C CA  . GLU A 212 ? 0.3233 0.3914 0.3800 -0.0369 0.0052  -0.0053 212 GLU A CA  
1809 C C   . GLU A 212 ? 0.3584 0.4189 0.4109 -0.0410 0.0050  -0.0069 212 GLU A C   
1810 O O   . GLU A 212 ? 0.3863 0.4475 0.4382 -0.0427 0.0063  -0.0065 212 GLU A O   
1811 C CB  . GLU A 212 ? 0.3395 0.4028 0.3957 -0.0315 0.0067  -0.0059 212 GLU A CB  
1812 C CG  . GLU A 212 ? 0.3667 0.4366 0.4275 -0.0269 0.0076  -0.0042 212 GLU A CG  
1813 C CD  . GLU A 212 ? 0.4779 0.5422 0.5380 -0.0220 0.0094  -0.0052 212 GLU A CD  
1814 O OE1 . GLU A 212 ? 0.5411 0.6073 0.6044 -0.0179 0.0101  -0.0042 212 GLU A OE1 
1815 O OE2 . GLU A 212 ? 0.4757 0.5336 0.5320 -0.0224 0.0103  -0.0071 212 GLU A OE2 
1816 N N   . THR A 213 ? 0.3511 0.4047 0.4007 -0.0426 0.0035  -0.0084 213 THR A N   
1817 C CA  . THR A 213 ? 0.3690 0.4145 0.4149 -0.0459 0.0036  -0.0097 213 THR A CA  
1818 C C   . THR A 213 ? 0.3684 0.4136 0.4135 -0.0510 0.0024  -0.0107 213 THR A C   
1819 O O   . THR A 213 ? 0.3853 0.4261 0.4285 -0.0547 0.0030  -0.0112 213 THR A O   
1820 C CB  . THR A 213 ? 0.3300 0.3657 0.3727 -0.0432 0.0035  -0.0109 213 THR A CB  
1821 O OG1 . THR A 213 ? 0.4016 0.4366 0.4446 -0.0412 0.0021  -0.0115 213 THR A OG1 
1822 C CG2 . THR A 213 ? 0.2889 0.3237 0.3313 -0.0394 0.0049  -0.0106 213 THR A CG2 
1823 N N   . THR A 214 ? 0.3592 0.4084 0.4054 -0.0515 0.0009  -0.0109 214 THR A N   
1824 C CA  . THR A 214 ? 0.3249 0.3739 0.3697 -0.0566 -0.0002 -0.0124 214 THR A CA  
1825 C C   . THR A 214 ? 0.3184 0.3797 0.3666 -0.0585 -0.0013 -0.0112 214 THR A C   
1826 O O   . THR A 214 ? 0.3228 0.3881 0.3719 -0.0577 -0.0027 -0.0110 214 THR A O   
1827 C CB  . THR A 214 ? 0.3547 0.3965 0.3968 -0.0557 -0.0012 -0.0142 214 THR A CB  
1828 O OG1 . THR A 214 ? 0.2929 0.3388 0.3369 -0.0515 -0.0022 -0.0132 214 THR A OG1 
1829 C CG2 . THR A 214 ? 0.2684 0.2989 0.3074 -0.0539 -0.0002 -0.0151 214 THR A CG2 
1830 N N   . PRO A 215 ? 0.2959 0.3641 0.3463 -0.0613 -0.0007 -0.0099 215 PRO A N   
1831 C CA  . PRO A 215 ? 0.3079 0.3894 0.3622 -0.0630 -0.0017 -0.0082 215 PRO A CA  
1832 C C   . PRO A 215 ? 0.3187 0.4030 0.3717 -0.0680 -0.0035 -0.0098 215 PRO A C   
1833 O O   . PRO A 215 ? 0.3577 0.4531 0.4135 -0.0685 -0.0048 -0.0081 215 PRO A O   
1834 C CB  . PRO A 215 ? 0.3630 0.4496 0.4191 -0.0658 -0.0004 -0.0068 215 PRO A CB  
1835 C CG  . PRO A 215 ? 0.3926 0.4678 0.4452 -0.0674 0.0009  -0.0084 215 PRO A CG  
1836 C CD  . PRO A 215 ? 0.3645 0.4298 0.4144 -0.0626 0.0011  -0.0095 215 PRO A CD  
1837 N N   . ASN A 216 ? 0.2687 0.3436 0.3174 -0.0718 -0.0035 -0.0128 216 ASN A N   
1838 C CA  . ASN A 216 ? 0.4166 0.4942 0.4637 -0.0773 -0.0049 -0.0149 216 ASN A CA  
1839 C C   . ASN A 216 ? 0.4615 0.5365 0.5066 -0.0753 -0.0062 -0.0162 216 ASN A C   
1840 O O   . ASN A 216 ? 0.5148 0.5907 0.5576 -0.0798 -0.0071 -0.0186 216 ASN A O   
1841 C CB  . ASN A 216 ? 0.5033 0.5726 0.5471 -0.0832 -0.0038 -0.0178 216 ASN A CB  
1842 C CG  . ASN A 216 ? 0.6365 0.7114 0.6825 -0.0873 -0.0031 -0.0166 216 ASN A CG  
1843 O OD1 . ASN A 216 ? 0.7041 0.7918 0.7534 -0.0891 -0.0041 -0.0147 216 ASN A OD1 
1844 N ND2 . ASN A 216 ? 0.7053 0.7712 0.7497 -0.0888 -0.0013 -0.0172 216 ASN A ND2 
1845 N N   . VAL A 217 ? 0.4014 0.4736 0.4473 -0.0689 -0.0061 -0.0149 217 VAL A N   
1846 C CA  . VAL A 217 ? 0.3919 0.4606 0.4358 -0.0668 -0.0071 -0.0159 217 VAL A CA  
1847 C C   . VAL A 217 ? 0.2849 0.3663 0.3317 -0.0664 -0.0089 -0.0138 217 VAL A C   
1848 O O   . VAL A 217 ? 0.3619 0.4533 0.4131 -0.0647 -0.0091 -0.0106 217 VAL A O   
1849 C CB  . VAL A 217 ? 0.4260 0.4860 0.4694 -0.0605 -0.0063 -0.0153 217 VAL A CB  
1850 C CG1 . VAL A 217 ? 0.3414 0.4083 0.3891 -0.0550 -0.0064 -0.0119 217 VAL A CG1 
1851 C CG2 . VAL A 217 ? 0.4361 0.4886 0.4761 -0.0599 -0.0068 -0.0173 217 VAL A CG2 
1852 N N   . LYS A 218 ? 0.3128 0.3942 0.3571 -0.0682 -0.0102 -0.0155 218 LYS A N   
1853 C CA  . LYS A 218 ? 0.3016 0.3946 0.3483 -0.0674 -0.0121 -0.0132 218 LYS A CA  
1854 C C   . LYS A 218 ? 0.3138 0.4037 0.3616 -0.0607 -0.0122 -0.0113 218 LYS A C   
1855 O O   . LYS A 218 ? 0.2956 0.3744 0.3402 -0.0590 -0.0116 -0.0133 218 LYS A O   
1856 C CB  . LYS A 218 ? 0.2775 0.3730 0.3206 -0.0732 -0.0134 -0.0161 218 LYS A CB  
1857 C CG  . LYS A 218 ? 0.4145 0.5129 0.4560 -0.0807 -0.0133 -0.0186 218 LYS A CG  
1858 C CD  . LYS A 218 ? 0.5162 0.6196 0.5545 -0.0861 -0.0148 -0.0212 218 LYS A CD  
1859 C CE  . LYS A 218 ? 0.6524 0.7442 0.6852 -0.0914 -0.0135 -0.0267 218 LYS A CE  
1860 N NZ  . LYS A 218 ? 0.7279 0.8199 0.7564 -0.0945 -0.0143 -0.0300 218 LYS A NZ  
1861 N N   . ILE A 219 ? 0.1994 0.2988 0.2519 -0.0569 -0.0128 -0.0072 219 ILE A N   
1862 C CA  . ILE A 219 ? 0.2559 0.3529 0.3097 -0.0510 -0.0129 -0.0052 219 ILE A CA  
1863 C C   . ILE A 219 ? 0.2571 0.3671 0.3140 -0.0507 -0.0147 -0.0018 219 ILE A C   
1864 O O   . ILE A 219 ? 0.3094 0.4315 0.3689 -0.0535 -0.0155 0.0000  219 ILE A O   
1865 C CB  . ILE A 219 ? 0.2202 0.3134 0.2772 -0.0451 -0.0112 -0.0031 219 ILE A CB  
1866 C CG1 . ILE A 219 ? 0.3228 0.4280 0.3855 -0.0435 -0.0110 0.0008  219 ILE A CG1 
1867 C CG2 . ILE A 219 ? 0.2448 0.3262 0.2987 -0.0456 -0.0096 -0.0061 219 ILE A CG2 
1868 C CD1 . ILE A 219 ? 0.3617 0.4642 0.4281 -0.0368 -0.0091 0.0031  219 ILE A CD1 
1869 N N   . PRO A 220 ? 0.2456 0.3544 0.3025 -0.0475 -0.0154 -0.0006 220 PRO A N   
1870 C CA  . PRO A 220 ? 0.2576 0.3794 0.3177 -0.0470 -0.0171 0.0032  220 PRO A CA  
1871 C C   . PRO A 220 ? 0.2388 0.3696 0.3057 -0.0425 -0.0165 0.0084  220 PRO A C   
1872 O O   . PRO A 220 ? 0.1907 0.3168 0.2597 -0.0392 -0.0146 0.0089  220 PRO A O   
1873 C CB  . PRO A 220 ? 0.2876 0.4036 0.3460 -0.0440 -0.0175 0.0033  220 PRO A CB  
1874 C CG  . PRO A 220 ? 0.3418 0.4432 0.3984 -0.0408 -0.0158 0.0012  220 PRO A CG  
1875 C CD  . PRO A 220 ? 0.2489 0.3449 0.3027 -0.0446 -0.0148 -0.0025 220 PRO A CD  
1876 N N   . ASP A 221 ? 0.2348 0.3790 0.3052 -0.0423 -0.0180 0.0126  221 ASP A N   
1877 C CA  . ASP A 221 ? 0.2503 0.4046 0.3279 -0.0376 -0.0174 0.0184  221 ASP A CA  
1878 C C   . ASP A 221 ? 0.2351 0.3823 0.3154 -0.0304 -0.0161 0.0209  221 ASP A C   
1879 O O   . ASP A 221 ? 0.2399 0.3884 0.3203 -0.0289 -0.0172 0.0228  221 ASP A O   
1880 C CB  . ASP A 221 ? 0.1781 0.3498 0.2585 -0.0401 -0.0196 0.0223  221 ASP A CB  
1881 C CG  . ASP A 221 ? 0.2773 0.4609 0.3657 -0.0353 -0.0189 0.0289  221 ASP A CG  
1882 O OD1 . ASP A 221 ? 0.2670 0.4499 0.3583 -0.0335 -0.0171 0.0293  221 ASP A OD1 
1883 O OD2 . ASP A 221 ? 0.3616 0.5558 0.4538 -0.0333 -0.0201 0.0339  221 ASP A OD2 
1884 N N   . PHE A 222 ? 0.1926 0.3326 0.2751 -0.0261 -0.0137 0.0209  222 PHE A N   
1885 C CA  . PHE A 222 ? 0.2144 0.3463 0.2991 -0.0196 -0.0122 0.0225  222 PHE A CA  
1886 C C   . PHE A 222 ? 0.2317 0.3744 0.3239 -0.0147 -0.0116 0.0291  222 PHE A C   
1887 O O   . PHE A 222 ? 0.2495 0.3935 0.3464 -0.0106 -0.0094 0.0313  222 PHE A O   
1888 C CB  . PHE A 222 ? 0.2476 0.3675 0.3310 -0.0174 -0.0097 0.0195  222 PHE A CB  
1889 C CG  . PHE A 222 ? 0.2447 0.3510 0.3215 -0.0196 -0.0099 0.0143  222 PHE A CG  
1890 C CD1 . PHE A 222 ? 0.2591 0.3631 0.3310 -0.0253 -0.0107 0.0103  222 PHE A CD1 
1891 C CD2 . PHE A 222 ? 0.2735 0.3695 0.3492 -0.0161 -0.0093 0.0137  222 PHE A CD2 
1892 C CE1 . PHE A 222 ? 0.2653 0.3572 0.3317 -0.0269 -0.0107 0.0060  222 PHE A CE1 
1893 C CE2 . PHE A 222 ? 0.2583 0.3429 0.3284 -0.0181 -0.0095 0.0094  222 PHE A CE2 
1894 C CZ  . PHE A 222 ? 0.2124 0.2950 0.2779 -0.0232 -0.0102 0.0057  222 PHE A CZ  
1895 N N   . ALA A 223 ? 0.2130 0.3635 0.3065 -0.0150 -0.0135 0.0324  223 ALA A N   
1896 C CA  . ALA A 223 ? 0.3113 0.4742 0.4121 -0.0109 -0.0134 0.0394  223 ALA A CA  
1897 C C   . ALA A 223 ? 0.3199 0.4756 0.4248 -0.0038 -0.0113 0.0425  223 ALA A C   
1898 O O   . ALA A 223 ? 0.3536 0.5186 0.4649 0.0001  -0.0110 0.0488  223 ALA A O   
1899 C CB  . ALA A 223 ? 0.3635 0.5389 0.4637 -0.0146 -0.0164 0.0419  223 ALA A CB  
1900 N N   . VAL A 224 ? 0.3030 0.4428 0.4045 -0.0021 -0.0098 0.0384  224 VAL A N   
1901 C CA  . VAL A 224 ? 0.1944 0.3259 0.2995 0.0042  -0.0074 0.0405  224 VAL A CA  
1902 C C   . VAL A 224 ? 0.2192 0.3377 0.3220 0.0055  -0.0050 0.0357  224 VAL A C   
1903 O O   . VAL A 224 ? 0.2817 0.3961 0.3793 0.0013  -0.0055 0.0308  224 VAL A O   
1904 C CB  . VAL A 224 ? 0.3151 0.4404 0.4183 0.0049  -0.0085 0.0409  224 VAL A CB  
1905 C CG1 . VAL A 224 ? 0.4035 0.5415 0.5116 0.0063  -0.0099 0.0475  224 VAL A CG1 
1906 C CG2 . VAL A 224 ? 0.2690 0.3879 0.3642 -0.0006 -0.0105 0.0352  224 VAL A CG2 
1907 N N   . SER A 225 ? 0.2291 0.3407 0.3355 0.0111  -0.0022 0.0372  225 SER A N   
1908 C CA  . SER A 225 ? 0.2368 0.3362 0.3412 0.0128  0.0004  0.0329  225 SER A CA  
1909 C C   . SER A 225 ? 0.2715 0.3571 0.3715 0.0127  0.0003  0.0296  225 SER A C   
1910 O O   . SER A 225 ? 0.2101 0.2935 0.3123 0.0154  0.0003  0.0324  225 SER A O   
1911 C CB  . SER A 225 ? 0.2827 0.3831 0.3939 0.0190  0.0040  0.0361  225 SER A CB  
1912 O OG  . SER A 225 ? 0.3058 0.3939 0.4145 0.0204  0.0066  0.0316  225 SER A OG  
1913 N N   . PHE A 226 ? 0.2385 0.3152 0.3324 0.0098  0.0002  0.0240  226 PHE A N   
1914 C CA  . PHE A 226 ? 0.2109 0.2745 0.3006 0.0097  0.0004  0.0205  226 PHE A CA  
1915 C C   . PHE A 226 ? 0.1901 0.2445 0.2801 0.0127  0.0035  0.0180  226 PHE A C   
1916 O O   . PHE A 226 ? 0.2213 0.2650 0.3072 0.0121  0.0038  0.0146  226 PHE A O   
1917 C CB  . PHE A 226 ? 0.2225 0.2825 0.3052 0.0043  -0.0019 0.0161  226 PHE A CB  
1918 C CG  . PHE A 226 ? 0.2701 0.3367 0.3514 0.0010  -0.0048 0.0175  226 PHE A CG  
1919 C CD1 . PHE A 226 ? 0.2589 0.3215 0.3388 0.0011  -0.0060 0.0179  226 PHE A CD1 
1920 C CD2 . PHE A 226 ? 0.2550 0.3319 0.3362 -0.0024 -0.0062 0.0180  226 PHE A CD2 
1921 C CE1 . PHE A 226 ? 0.2304 0.2992 0.3085 -0.0020 -0.0086 0.0188  226 PHE A CE1 
1922 C CE2 . PHE A 226 ? 0.2764 0.3593 0.3558 -0.0058 -0.0088 0.0187  226 PHE A CE2 
1923 C CZ  . PHE A 226 ? 0.2689 0.3478 0.3466 -0.0055 -0.0099 0.0190  226 PHE A CZ  
1924 N N   . ARG A 227 ? 0.2089 0.2677 0.3034 0.0159  0.0061  0.0198  227 ARG A N   
1925 C CA  . ARG A 227 ? 0.2432 0.2937 0.3373 0.0184  0.0093  0.0168  227 ARG A CA  
1926 C C   . ARG A 227 ? 0.2681 0.3083 0.3631 0.0216  0.0110  0.0166  227 ARG A C   
1927 O O   . ARG A 227 ? 0.2277 0.2577 0.3189 0.0213  0.0123  0.0122  227 ARG A O   
1928 C CB  . ARG A 227 ? 0.2832 0.3413 0.3826 0.0216  0.0120  0.0191  227 ARG A CB  
1929 C CG  . ARG A 227 ? 0.3123 0.3800 0.4106 0.0180  0.0107  0.0189  227 ARG A CG  
1930 C CD  . ARG A 227 ? 0.4192 0.4956 0.5235 0.0215  0.0133  0.0219  227 ARG A CD  
1931 N NE  . ARG A 227 ? 0.4318 0.5005 0.5361 0.0248  0.0172  0.0191  227 ARG A NE  
1932 C CZ  . ARG A 227 ? 0.5019 0.5662 0.6014 0.0225  0.0180  0.0145  227 ARG A CZ  
1933 N NH1 . ARG A 227 ? 0.4420 0.5080 0.5365 0.0170  0.0152  0.0123  227 ARG A NH1 
1934 N NH2 . ARG A 227 ? 0.5157 0.5735 0.6151 0.0255  0.0216  0.0120  227 ARG A NH2 
1935 N N   . GLU A 228 ? 0.2026 0.2457 0.3027 0.0246  0.0110  0.0213  228 GLU A N   
1936 C CA  . GLU A 228 ? 0.3022 0.3353 0.4034 0.0274  0.0126  0.0214  228 GLU A CA  
1937 C C   . GLU A 228 ? 0.2701 0.2952 0.3653 0.0237  0.0102  0.0182  228 GLU A C   
1938 O O   . GLU A 228 ? 0.3082 0.3223 0.4014 0.0242  0.0116  0.0153  228 GLU A O   
1939 C CB  . GLU A 228 ? 0.3115 0.3504 0.4200 0.0314  0.0131  0.0280  228 GLU A CB  
1940 C CG  . GLU A 228 ? 0.5563 0.5878 0.6696 0.0367  0.0173  0.0291  228 GLU A CG  
1941 C CD  . GLU A 228 ? 0.7381 0.7560 0.8480 0.0360  0.0177  0.0258  228 GLU A CD  
1942 O OE1 . GLU A 228 ? 0.7957 0.8133 0.9047 0.0343  0.0151  0.0275  228 GLU A OE1 
1943 O OE2 . GLU A 228 ? 0.7912 0.7993 0.8994 0.0369  0.0205  0.0215  228 GLU A OE2 
1944 N N   . ASP A 229 ? 0.2746 0.3049 0.3670 0.0199  0.0067  0.0186  229 ASP A N   
1945 C CA  . ASP A 229 ? 0.2288 0.2520 0.3154 0.0166  0.0046  0.0156  229 ASP A CA  
1946 C C   . ASP A 229 ? 0.2344 0.2498 0.3155 0.0142  0.0052  0.0099  229 ASP A C   
1947 O O   . ASP A 229 ? 0.2281 0.2349 0.3055 0.0130  0.0048  0.0072  229 ASP A O   
1948 C CB  . ASP A 229 ? 0.2085 0.2392 0.2930 0.0130  0.0011  0.0167  229 ASP A CB  
1949 C CG  . ASP A 229 ? 0.2413 0.2785 0.3301 0.0146  0.0000  0.0221  229 ASP A CG  
1950 O OD1 . ASP A 229 ? 0.2711 0.3058 0.3646 0.0185  0.0018  0.0251  229 ASP A OD1 
1951 O OD2 . ASP A 229 ? 0.2468 0.2916 0.3342 0.0119  -0.0025 0.0234  229 ASP A OD2 
1952 N N   . ALA A 230 ? 0.2768 0.2957 0.3572 0.0136  0.0062  0.0082  230 ALA A N   
1953 C CA  . ALA A 230 ? 0.3237 0.3359 0.3990 0.0117  0.0069  0.0033  230 ALA A CA  
1954 C C   . ALA A 230 ? 0.2318 0.2346 0.3073 0.0142  0.0097  0.0012  230 ALA A C   
1955 O O   . ALA A 230 ? 0.2621 0.2570 0.3329 0.0122  0.0094  -0.0023 230 ALA A O   
1956 C CB  . ALA A 230 ? 0.2813 0.2998 0.3566 0.0109  0.0077  0.0026  230 ALA A CB  
1957 N N   . SER A 231 ? 0.2359 0.2394 0.3167 0.0185  0.0126  0.0034  231 SER A N   
1958 C CA  . SER A 231 ? 0.2899 0.2837 0.3713 0.0210  0.0155  0.0014  231 SER A CA  
1959 C C   . SER A 231 ? 0.3072 0.2941 0.3873 0.0199  0.0141  0.0014  231 SER A C   
1960 O O   . SER A 231 ? 0.3183 0.2960 0.3950 0.0190  0.0150  -0.0023 231 SER A O   
1961 C CB  . SER A 231 ? 0.3058 0.3019 0.3943 0.0262  0.0189  0.0047  231 SER A CB  
1962 O OG  . SER A 231 ? 0.4960 0.4937 0.5848 0.0277  0.0217  0.0027  231 SER A OG  
1963 N N   . LYS A 232 ? 0.2979 0.2895 0.3804 0.0200  0.0118  0.0056  232 LYS A N   
1964 C CA  . LYS A 232 ? 0.2537 0.2396 0.3356 0.0192  0.0105  0.0063  232 LYS A CA  
1965 C C   . LYS A 232 ? 0.2918 0.2724 0.3668 0.0149  0.0084  0.0022  232 LYS A C   
1966 O O   . LYS A 232 ? 0.3362 0.3084 0.4094 0.0142  0.0089  0.0001  232 LYS A O   
1967 C CB  . LYS A 232 ? 0.2768 0.2706 0.3621 0.0197  0.0083  0.0116  232 LYS A CB  
1968 C CG  . LYS A 232 ? 0.4818 0.4713 0.5704 0.0216  0.0086  0.0147  232 LYS A CG  
1969 C CD  . LYS A 232 ? 0.5849 0.5841 0.6791 0.0239  0.0077  0.0211  232 LYS A CD  
1970 C CE  . LYS A 232 ? 0.6146 0.6177 0.7150 0.0284  0.0108  0.0240  232 LYS A CE  
1971 N NZ  . LYS A 232 ? 0.6533 0.6697 0.7581 0.0295  0.0094  0.0297  232 LYS A NZ  
1972 N N   . HIS A 233 ? 0.3079 0.2935 0.3793 0.0118  0.0060  0.0012  233 HIS A N   
1973 C CA  . HIS A 233 ? 0.2978 0.2789 0.3630 0.0080  0.0043  -0.0023 233 HIS A CA  
1974 C C   . HIS A 233 ? 0.2865 0.2596 0.3488 0.0076  0.0062  -0.0065 233 HIS A C   
1975 O O   . HIS A 233 ? 0.2138 0.1810 0.2729 0.0057  0.0054  -0.0085 233 HIS A O   
1976 C CB  . HIS A 233 ? 0.3157 0.3026 0.3779 0.0053  0.0025  -0.0032 233 HIS A CB  
1977 C CG  . HIS A 233 ? 0.2485 0.2419 0.3114 0.0041  0.0001  -0.0004 233 HIS A CG  
1978 N ND1 . HIS A 233 ? 0.2142 0.2058 0.2746 0.0021  -0.0021 -0.0004 233 HIS A ND1 
1979 C CD2 . HIS A 233 ? 0.2262 0.2286 0.2920 0.0045  -0.0005 0.0023  233 HIS A CD2 
1980 C CE1 . HIS A 233 ? 0.2049 0.2034 0.2662 0.0013  -0.0037 0.0020  233 HIS A CE1 
1981 N NE2 . HIS A 233 ? 0.2197 0.2251 0.2842 0.0026  -0.0030 0.0036  233 HIS A NE2 
1982 N N   . VAL A 234 ? 0.2433 0.2169 0.3067 0.0093  0.0088  -0.0080 234 VAL A N   
1983 C CA  . VAL A 234 ? 0.2462 0.2130 0.3062 0.0086  0.0108  -0.0124 234 VAL A CA  
1984 C C   . VAL A 234 ? 0.2614 0.2202 0.3231 0.0102  0.0128  -0.0131 234 VAL A C   
1985 O O   . VAL A 234 ? 0.2404 0.1925 0.2981 0.0080  0.0128  -0.0164 234 VAL A O   
1986 C CB  . VAL A 234 ? 0.2454 0.2155 0.3060 0.0101  0.0133  -0.0137 234 VAL A CB  
1987 C CG1 . VAL A 234 ? 0.2775 0.2412 0.3338 0.0089  0.0153  -0.0186 234 VAL A CG1 
1988 C CG2 . VAL A 234 ? 0.2937 0.2716 0.3530 0.0081  0.0114  -0.0128 234 VAL A CG2 
1989 N N   . GLU A 235 ? 0.2664 0.2258 0.3340 0.0140  0.0145  -0.0098 235 GLU A N   
1990 C CA  . GLU A 235 ? 0.3399 0.2910 0.4098 0.0158  0.0168  -0.0102 235 GLU A CA  
1991 C C   . GLU A 235 ? 0.2895 0.2364 0.3577 0.0133  0.0144  -0.0097 235 GLU A C   
1992 O O   . GLU A 235 ? 0.2754 0.2140 0.3413 0.0118  0.0153  -0.0127 235 GLU A O   
1993 C CB  . GLU A 235 ? 0.4320 0.3856 0.5093 0.0206  0.0191  -0.0058 235 GLU A CB  
1994 C CG  . GLU A 235 ? 0.6005 0.5451 0.6806 0.0234  0.0233  -0.0071 235 GLU A CG  
1995 C CD  . GLU A 235 ? 0.7065 0.6463 0.7828 0.0229  0.0262  -0.0129 235 GLU A CD  
1996 O OE1 . GLU A 235 ? 0.7725 0.7176 0.8500 0.0249  0.0278  -0.0130 235 GLU A OE1 
1997 O OE2 . GLU A 235 ? 0.7638 0.6952 0.8360 0.0203  0.0268  -0.0173 235 GLU A OE2 
1998 N N   . LEU A 236 ? 0.2959 0.2485 0.3651 0.0126  0.0114  -0.0059 236 LEU A N   
1999 C CA  . LEU A 236 ? 0.2929 0.2423 0.3607 0.0104  0.0091  -0.0051 236 LEU A CA  
2000 C C   . LEU A 236 ? 0.2593 0.2057 0.3206 0.0062  0.0074  -0.0092 236 LEU A C   
2001 O O   . LEU A 236 ? 0.2395 0.1806 0.2991 0.0042  0.0067  -0.0101 236 LEU A O   
2002 C CB  . LEU A 236 ? 0.2904 0.2475 0.3604 0.0107  0.0064  -0.0004 236 LEU A CB  
2003 C CG  . LEU A 236 ? 0.3357 0.2978 0.4124 0.0145  0.0075  0.0048  236 LEU A CG  
2004 C CD1 . LEU A 236 ? 0.3861 0.3569 0.4633 0.0137  0.0044  0.0085  236 LEU A CD1 
2005 C CD2 . LEU A 236 ? 0.3047 0.2599 0.3855 0.0168  0.0096  0.0066  236 LEU A CD2 
2006 N N   . ALA A 237 ? 0.2819 0.2319 0.3397 0.0047  0.0068  -0.0114 237 ALA A N   
2007 C CA  . ALA A 237 ? 0.2552 0.2027 0.3070 0.0011  0.0055  -0.0150 237 ALA A CA  
2008 C C   . ALA A 237 ? 0.2746 0.2145 0.3243 0.0003  0.0078  -0.0190 237 ALA A C   
2009 O O   . ALA A 237 ? 0.2706 0.2069 0.3167 -0.0028 0.0066  -0.0210 237 ALA A O   
2010 C CB  . ALA A 237 ? 0.2299 0.1829 0.2790 0.0000  0.0049  -0.0161 237 ALA A CB  
2011 N N   . LYS A 238 ? 0.2638 0.2017 0.3156 0.0028  0.0111  -0.0203 238 LYS A N   
2012 C CA  . LYS A 238 ? 0.2614 0.1914 0.3113 0.0021  0.0136  -0.0245 238 LYS A CA  
2013 C C   . LYS A 238 ? 0.3114 0.2349 0.3632 0.0016  0.0137  -0.0238 238 LYS A C   
2014 O O   . LYS A 238 ? 0.3169 0.2344 0.3652 -0.0013 0.0140  -0.0272 238 LYS A O   
2015 C CB  . LYS A 238 ? 0.2797 0.2086 0.3323 0.0055  0.0176  -0.0258 238 LYS A CB  
2016 C CG  . LYS A 238 ? 0.2709 0.2059 0.3215 0.0056  0.0180  -0.0271 238 LYS A CG  
2017 C CD  . LYS A 238 ? 0.3212 0.2567 0.3759 0.0098  0.0219  -0.0270 238 LYS A CD  
2018 C CE  . LYS A 238 ? 0.3168 0.2432 0.3712 0.0106  0.0257  -0.0309 238 LYS A CE  
2019 N NZ  . LYS A 238 ? 0.3314 0.2582 0.3899 0.0151  0.0301  -0.0310 238 LYS A NZ  
2020 N N   . GLU A 239 ? 0.2596 0.1843 0.3168 0.0043  0.0135  -0.0191 239 GLU A N   
2021 C CA  . GLU A 239 ? 0.3138 0.2326 0.3733 0.0040  0.0136  -0.0177 239 GLU A CA  
2022 C C   . GLU A 239 ? 0.3374 0.2564 0.3930 -0.0002 0.0102  -0.0180 239 GLU A C   
2023 O O   . GLU A 239 ? 0.3694 0.2821 0.4235 -0.0026 0.0104  -0.0200 239 GLU A O   
2024 C CB  . GLU A 239 ? 0.2857 0.2076 0.3518 0.0077  0.0137  -0.0119 239 GLU A CB  
2025 C CG  . GLU A 239 ? 0.4183 0.3403 0.4898 0.0125  0.0173  -0.0103 239 GLU A CG  
2026 C CD  . GLU A 239 ? 0.6979 0.6228 0.7760 0.0157  0.0171  -0.0039 239 GLU A CD  
2027 O OE1 . GLU A 239 ? 0.7873 0.7145 0.8706 0.0200  0.0196  -0.0012 239 GLU A OE1 
2028 O OE2 . GLU A 239 ? 0.8068 0.7325 0.8850 0.0140  0.0146  -0.0014 239 GLU A OE2 
2029 N N   . LYS A 240 ? 0.3831 0.3096 0.4372 -0.0010 0.0071  -0.0160 240 LYS A N   
2030 C CA  . LYS A 240 ? 0.3387 0.2661 0.3896 -0.0044 0.0040  -0.0156 240 LYS A CA  
2031 C C   . LYS A 240 ? 0.3597 0.2838 0.4050 -0.0081 0.0038  -0.0202 240 LYS A C   
2032 O O   . LYS A 240 ? 0.3058 0.2266 0.3495 -0.0110 0.0028  -0.0210 240 LYS A O   
2033 C CB  . LYS A 240 ? 0.2542 0.1898 0.3046 -0.0043 0.0014  -0.0129 240 LYS A CB  
2034 C CG  . LYS A 240 ? 0.2427 0.1799 0.2906 -0.0071 -0.0016 -0.0119 240 LYS A CG  
2035 C CD  . LYS A 240 ? 0.2138 0.1490 0.2650 -0.0068 -0.0021 -0.0089 240 LYS A CD  
2036 C CE  . LYS A 240 ? 0.3347 0.2709 0.3831 -0.0098 -0.0046 -0.0084 240 LYS A CE  
2037 N NZ  . LYS A 240 ? 0.3418 0.2774 0.3935 -0.0094 -0.0053 -0.0048 240 LYS A NZ  
2038 N N   . TYR A 241 ? 0.3156 0.2413 0.3581 -0.0083 0.0048  -0.0232 241 TYR A N   
2039 C CA  . TYR A 241 ? 0.3201 0.2436 0.3571 -0.0118 0.0048  -0.0275 241 TYR A CA  
2040 C C   . TYR A 241 ? 0.3006 0.2160 0.3372 -0.0132 0.0070  -0.0307 241 TYR A C   
2041 O O   . TYR A 241 ? 0.3092 0.2224 0.3421 -0.0170 0.0059  -0.0330 241 TYR A O   
2042 C CB  . TYR A 241 ? 0.3233 0.2502 0.3580 -0.0112 0.0060  -0.0297 241 TYR A CB  
2043 C CG  . TYR A 241 ? 0.3074 0.2338 0.3363 -0.0147 0.0058  -0.0337 241 TYR A CG  
2044 C CD1 . TYR A 241 ? 0.3153 0.2361 0.3420 -0.0160 0.0083  -0.0382 241 TYR A CD1 
2045 C CD2 . TYR A 241 ? 0.2804 0.2122 0.3059 -0.0167 0.0034  -0.0331 241 TYR A CD2 
2046 C CE1 . TYR A 241 ? 0.3196 0.2409 0.3407 -0.0194 0.0082  -0.0418 241 TYR A CE1 
2047 C CE2 . TYR A 241 ? 0.2507 0.1831 0.2710 -0.0199 0.0033  -0.0361 241 TYR A CE2 
2048 C CZ  . TYR A 241 ? 0.2540 0.1815 0.2720 -0.0214 0.0055  -0.0405 241 TYR A CZ  
2049 O OH  . TYR A 241 ? 0.3015 0.2303 0.3141 -0.0248 0.0054  -0.0437 241 TYR A OH  
2050 N N   . PHE A 242 ? 0.2582 0.1692 0.2987 -0.0101 0.0101  -0.0309 242 PHE A N   
2051 C CA  . PHE A 242 ? 0.3173 0.2194 0.3582 -0.0110 0.0127  -0.0338 242 PHE A CA  
2052 C C   . PHE A 242 ? 0.3529 0.2521 0.3947 -0.0134 0.0108  -0.0320 242 PHE A C   
2053 O O   . PHE A 242 ? 0.3433 0.2371 0.3823 -0.0171 0.0112  -0.0353 242 PHE A O   
2054 C CB  . PHE A 242 ? 0.3938 0.2923 0.4401 -0.0063 0.0165  -0.0329 242 PHE A CB  
2055 C CG  . PHE A 242 ? 0.5156 0.4039 0.5630 -0.0067 0.0198  -0.0358 242 PHE A CG  
2056 C CD1 . PHE A 242 ? 0.5751 0.4581 0.6174 -0.0101 0.0214  -0.0420 242 PHE A CD1 
2057 C CD2 . PHE A 242 ? 0.6362 0.5201 0.6898 -0.0037 0.0214  -0.0322 242 PHE A CD2 
2058 C CE1 . PHE A 242 ? 0.6481 0.5209 0.6912 -0.0108 0.0248  -0.0451 242 PHE A CE1 
2059 C CE2 . PHE A 242 ? 0.7474 0.6209 0.8024 -0.0040 0.0249  -0.0349 242 PHE A CE2 
2060 C CZ  . PHE A 242 ? 0.7293 0.5969 0.7789 -0.0077 0.0266  -0.0416 242 PHE A CZ  
2061 N N   . GLU A 243 ? 0.3669 0.2700 0.4125 -0.0116 0.0088  -0.0267 243 GLU A N   
2062 C CA  . GLU A 243 ? 0.3926 0.2940 0.4394 -0.0137 0.0069  -0.0243 243 GLU A CA  
2063 C C   . GLU A 243 ? 0.3961 0.2994 0.4375 -0.0186 0.0042  -0.0263 243 GLU A C   
2064 O O   . GLU A 243 ? 0.3667 0.2656 0.4072 -0.0219 0.0039  -0.0274 243 GLU A O   
2065 C CB  . GLU A 243 ? 0.4639 0.3712 0.5149 -0.0110 0.0050  -0.0183 243 GLU A CB  
2066 C CG  . GLU A 243 ? 0.5828 0.4928 0.6331 -0.0136 0.0018  -0.0157 243 GLU A CG  
2067 C CD  . GLU A 243 ? 0.7426 0.6585 0.7969 -0.0109 0.0003  -0.0100 243 GLU A CD  
2068 O OE1 . GLU A 243 ? 0.8610 0.7787 0.9191 -0.0071 0.0017  -0.0078 243 GLU A OE1 
2069 O OE2 . GLU A 243 ? 0.6870 0.6064 0.7406 -0.0126 -0.0023 -0.0077 243 GLU A OE2 
2070 N N   . ILE A 244 ? 0.3536 0.2634 0.3915 -0.0193 0.0024  -0.0268 244 ILE A N   
2071 C CA  . ILE A 244 ? 0.2762 0.1892 0.3096 -0.0233 -0.0004 -0.0275 244 ILE A CA  
2072 C C   . ILE A 244 ? 0.3285 0.2384 0.3571 -0.0270 0.0007  -0.0328 244 ILE A C   
2073 O O   . ILE A 244 ? 0.3098 0.2185 0.3359 -0.0311 -0.0006 -0.0341 244 ILE A O   
2074 C CB  . ILE A 244 ? 0.3159 0.2370 0.3482 -0.0223 -0.0025 -0.0252 244 ILE A CB  
2075 C CG1 . ILE A 244 ? 0.2879 0.2123 0.3246 -0.0192 -0.0035 -0.0204 244 ILE A CG1 
2076 C CG2 . ILE A 244 ? 0.3061 0.2309 0.3341 -0.0260 -0.0051 -0.0256 244 ILE A CG2 
2077 C CD1 . ILE A 244 ? 0.3211 0.2445 0.3599 -0.0203 -0.0050 -0.0174 244 ILE A CD1 
2078 N N   . PHE A 245 ? 0.2864 0.1954 0.3133 -0.0258 0.0030  -0.0361 245 PHE A N   
2079 C CA  . PHE A 245 ? 0.2789 0.1865 0.3004 -0.0293 0.0039  -0.0412 245 PHE A CA  
2080 C C   . PHE A 245 ? 0.3330 0.2319 0.3546 -0.0295 0.0076  -0.0457 245 PHE A C   
2081 O O   . PHE A 245 ? 0.3717 0.2689 0.3884 -0.0329 0.0086  -0.0506 245 PHE A O   
2082 C CB  . PHE A 245 ? 0.2934 0.2070 0.3120 -0.0284 0.0037  -0.0419 245 PHE A CB  
2083 C CG  . PHE A 245 ? 0.3315 0.2528 0.3495 -0.0286 0.0004  -0.0381 245 PHE A CG  
2084 C CD1 . PHE A 245 ? 0.3143 0.2390 0.3287 -0.0325 -0.0021 -0.0381 245 PHE A CD1 
2085 C CD2 . PHE A 245 ? 0.3446 0.2698 0.3656 -0.0249 -0.0001 -0.0346 245 PHE A CD2 
2086 C CE1 . PHE A 245 ? 0.2937 0.2249 0.3078 -0.0323 -0.0047 -0.0345 245 PHE A CE1 
2087 C CE2 . PHE A 245 ? 0.3503 0.2817 0.3707 -0.0252 -0.0028 -0.0314 245 PHE A CE2 
2088 C CZ  . PHE A 245 ? 0.2337 0.1677 0.2507 -0.0286 -0.0050 -0.0313 245 PHE A CZ  
2089 N N   . GLY A 246 ? 0.3335 0.2270 0.3603 -0.0261 0.0099  -0.0442 246 GLY A N   
2090 C CA  . GLY A 246 ? 0.3581 0.2424 0.3856 -0.0261 0.0139  -0.0483 246 GLY A CA  
2091 C C   . GLY A 246 ? 0.4659 0.3492 0.4922 -0.0237 0.0173  -0.0519 246 GLY A C   
2092 O O   . GLY A 246 ? 0.4200 0.2952 0.4462 -0.0237 0.0211  -0.0560 246 GLY A O   
2093 N N   . GLU A 247 ? 0.4628 0.3537 0.4882 -0.0218 0.0163  -0.0505 247 GLU A N   
2094 C CA  . GLU A 247 ? 0.5405 0.4320 0.5645 -0.0197 0.0193  -0.0536 247 GLU A CA  
2095 C C   . GLU A 247 ? 0.4076 0.3059 0.4355 -0.0151 0.0186  -0.0489 247 GLU A C   
2096 O O   . GLU A 247 ? 0.3047 0.2086 0.3341 -0.0150 0.0153  -0.0445 247 GLU A O   
2097 C CB  . GLU A 247 ? 0.5791 0.4738 0.5958 -0.0240 0.0185  -0.0580 247 GLU A CB  
2098 C CG  . GLU A 247 ? 0.7264 0.6267 0.7412 -0.0222 0.0197  -0.0590 247 GLU A CG  
2099 C CD  . GLU A 247 ? 0.8052 0.7123 0.8139 -0.0262 0.0170  -0.0601 247 GLU A CD  
2100 O OE1 . GLU A 247 ? 0.8334 0.7401 0.8388 -0.0307 0.0149  -0.0612 247 GLU A OE1 
2101 O OE2 . GLU A 247 ? 0.8473 0.7604 0.8548 -0.0249 0.0170  -0.0596 247 GLU A OE2 
2102 N N   . HIS A 248 ? 0.3278 0.2258 0.3577 -0.0115 0.0220  -0.0500 248 HIS A N   
2103 C CA  . HIS A 248 ? 0.3625 0.2680 0.3956 -0.0078 0.0213  -0.0459 248 HIS A CA  
2104 C C   . HIS A 248 ? 0.3525 0.2652 0.3806 -0.0100 0.0193  -0.0468 248 HIS A C   
2105 O O   . HIS A 248 ? 0.3765 0.2884 0.3996 -0.0126 0.0204  -0.0513 248 HIS A O   
2106 C CB  . HIS A 248 ? 0.4327 0.3363 0.4701 -0.0030 0.0255  -0.0460 248 HIS A CB  
2107 C CG  . HIS A 248 ? 0.5491 0.4473 0.5928 0.0003  0.0273  -0.0432 248 HIS A CG  
2108 N ND1 . HIS A 248 ? 0.5929 0.4815 0.6378 0.0010  0.0312  -0.0463 248 HIS A ND1 
2109 C CD2 . HIS A 248 ? 0.5533 0.4543 0.6026 0.0028  0.0257  -0.0373 248 HIS A CD2 
2110 C CE1 . HIS A 248 ? 0.6024 0.4880 0.6537 0.0041  0.0320  -0.0422 248 HIS A CE1 
2111 N NE2 . HIS A 248 ? 0.5850 0.4785 0.6390 0.0053  0.0286  -0.0366 248 HIS A NE2 
2112 N N   . PRO A 249 ? 0.3054 0.2253 0.3348 -0.0092 0.0165  -0.0426 249 PRO A N   
2113 C CA  . PRO A 249 ? 0.3573 0.2836 0.3824 -0.0113 0.0147  -0.0431 249 PRO A CA  
2114 C C   . PRO A 249 ? 0.3724 0.3011 0.3969 -0.0095 0.0176  -0.0453 249 PRO A C   
2115 O O   . PRO A 249 ? 0.3561 0.2858 0.3852 -0.0056 0.0196  -0.0437 249 PRO A O   
2116 C CB  . PRO A 249 ? 0.3647 0.2969 0.3924 -0.0103 0.0116  -0.0380 249 PRO A CB  
2117 C CG  . PRO A 249 ? 0.3307 0.2617 0.3646 -0.0064 0.0129  -0.0351 249 PRO A CG  
2118 C CD  . PRO A 249 ? 0.3498 0.2725 0.3847 -0.0063 0.0151  -0.0373 249 PRO A CD  
2119 N N   . VAL A 250 ? 0.3907 0.3209 0.4096 -0.0124 0.0178  -0.0486 250 VAL A N   
2120 C CA  . VAL A 250 ? 0.4087 0.3423 0.4264 -0.0112 0.0203  -0.0505 250 VAL A CA  
2121 C C   . VAL A 250 ? 0.3414 0.2832 0.3582 -0.0117 0.0180  -0.0476 250 VAL A C   
2122 O O   . VAL A 250 ? 0.2705 0.2163 0.2879 -0.0101 0.0198  -0.0477 250 VAL A O   
2123 C CB  . VAL A 250 ? 0.4283 0.3586 0.4403 -0.0140 0.0225  -0.0563 250 VAL A CB  
2124 C CG1 . VAL A 250 ? 0.4933 0.4254 0.5000 -0.0189 0.0193  -0.0571 250 VAL A CG1 
2125 C CG2 . VAL A 250 ? 0.4786 0.4127 0.4891 -0.0128 0.0252  -0.0585 250 VAL A CG2 
2126 N N   . TYR A 251 ? 0.2701 0.2143 0.2858 -0.0140 0.0144  -0.0449 251 TYR A N   
2127 C CA  . TYR A 251 ? 0.3286 0.2794 0.3438 -0.0145 0.0123  -0.0419 251 TYR A CA  
2128 C C   . TYR A 251 ? 0.3127 0.2649 0.3322 -0.0129 0.0101  -0.0376 251 TYR A C   
2129 O O   . TYR A 251 ? 0.3230 0.2717 0.3441 -0.0129 0.0089  -0.0366 251 TYR A O   
2130 C CB  . TYR A 251 ? 0.4386 0.3916 0.4486 -0.0184 0.0101  -0.0423 251 TYR A CB  
2131 C CG  . TYR A 251 ? 0.5025 0.4532 0.5079 -0.0208 0.0115  -0.0468 251 TYR A CG  
2132 C CD1 . TYR A 251 ? 0.5530 0.5052 0.5561 -0.0206 0.0143  -0.0498 251 TYR A CD1 
2133 C CD2 . TYR A 251 ? 0.5511 0.4982 0.5541 -0.0235 0.0102  -0.0482 251 TYR A CD2 
2134 C CE1 . TYR A 251 ? 0.6356 0.5858 0.6340 -0.0230 0.0158  -0.0544 251 TYR A CE1 
2135 C CE2 . TYR A 251 ? 0.5633 0.5085 0.5616 -0.0263 0.0116  -0.0528 251 TYR A CE2 
2136 C CZ  . TYR A 251 ? 0.6530 0.5996 0.6489 -0.0261 0.0145  -0.0560 251 TYR A CZ  
2137 O OH  . TYR A 251 ? 0.7780 0.7230 0.7688 -0.0290 0.0161  -0.0610 251 TYR A OH  
2138 N N   . MET A 252 ? 0.2355 0.1929 0.2568 -0.0119 0.0097  -0.0351 252 MET A N   
2139 C CA  . MET A 252 ? 0.2304 0.1899 0.2549 -0.0111 0.0075  -0.0313 252 MET A CA  
2140 C C   . MET A 252 ? 0.2951 0.2595 0.3180 -0.0126 0.0060  -0.0296 252 MET A C   
2141 O O   . MET A 252 ? 0.2353 0.2028 0.2568 -0.0131 0.0071  -0.0304 252 MET A O   
2142 C CB  . MET A 252 ? 0.3318 0.2925 0.3618 -0.0077 0.0088  -0.0296 252 MET A CB  
2143 C CG  . MET A 252 ? 0.3692 0.3248 0.4019 -0.0059 0.0096  -0.0296 252 MET A CG  
2144 S SD  . MET A 252 ? 0.3236 0.2820 0.3633 -0.0021 0.0101  -0.0258 252 MET A SD  
2145 C CE  . MET A 252 ? 0.3139 0.2651 0.3559 -0.0007 0.0108  -0.0258 252 MET A CE  
2146 N N   . TRP A 253 ? 0.2752 0.2401 0.2985 -0.0135 0.0035  -0.0272 253 TRP A N   
2147 C CA  . TRP A 253 ? 0.2197 0.1884 0.2426 -0.0146 0.0023  -0.0251 253 TRP A CA  
2148 C C   . TRP A 253 ? 0.2464 0.2179 0.2735 -0.0129 0.0022  -0.0231 253 TRP A C   
2149 O O   . TRP A 253 ? 0.2392 0.2096 0.2684 -0.0120 0.0011  -0.0217 253 TRP A O   
2150 C CB  . TRP A 253 ? 0.2807 0.2482 0.3016 -0.0164 0.0000  -0.0238 253 TRP A CB  
2151 C CG  . TRP A 253 ? 0.2360 0.2063 0.2572 -0.0172 -0.0009 -0.0217 253 TRP A CG  
2152 C CD1 . TRP A 253 ? 0.3010 0.2715 0.3239 -0.0170 -0.0023 -0.0199 253 TRP A CD1 
2153 C CD2 . TRP A 253 ? 0.2748 0.2478 0.2945 -0.0184 -0.0004 -0.0214 253 TRP A CD2 
2154 N NE1 . TRP A 253 ? 0.3297 0.3023 0.3521 -0.0181 -0.0025 -0.0188 253 TRP A NE1 
2155 C CE2 . TRP A 253 ? 0.3549 0.3291 0.3756 -0.0190 -0.0013 -0.0195 253 TRP A CE2 
2156 C CE3 . TRP A 253 ? 0.2782 0.2530 0.2958 -0.0192 0.0010  -0.0227 253 TRP A CE3 
2157 C CZ2 . TRP A 253 ? 0.2960 0.2722 0.3158 -0.0204 -0.0010 -0.0186 253 TRP A CZ2 
2158 C CZ3 . TRP A 253 ? 0.2716 0.2492 0.2884 -0.0204 0.0012  -0.0214 253 TRP A CZ3 
2159 C CH2 . TRP A 253 ? 0.2394 0.2175 0.2575 -0.0210 0.0003  -0.0193 253 TRP A CH2 
2160 N N   . PRO A 254 ? 0.2146 0.1903 0.2430 -0.0125 0.0033  -0.0228 254 PRO A N   
2161 C CA  . PRO A 254 ? 0.2256 0.2052 0.2578 -0.0114 0.0029  -0.0207 254 PRO A CA  
2162 C C   . PRO A 254 ? 0.2300 0.2102 0.2614 -0.0132 0.0008  -0.0191 254 PRO A C   
2163 O O   . PRO A 254 ? 0.2448 0.2247 0.2734 -0.0153 0.0003  -0.0192 254 PRO A O   
2164 C CB  . PRO A 254 ? 0.2797 0.2639 0.3127 -0.0112 0.0046  -0.0209 254 PRO A CB  
2165 C CG  . PRO A 254 ? 0.3330 0.3162 0.3619 -0.0131 0.0051  -0.0224 254 PRO A CG  
2166 C CD  . PRO A 254 ? 0.2840 0.2618 0.3102 -0.0133 0.0048  -0.0241 254 PRO A CD  
2167 N N   . PRO A 255 ? 0.2502 0.2311 0.2840 -0.0125 -0.0004 -0.0175 255 PRO A N   
2168 C CA  . PRO A 255 ? 0.2387 0.2199 0.2716 -0.0142 -0.0021 -0.0164 255 PRO A CA  
2169 C C   . PRO A 255 ? 0.2287 0.2129 0.2607 -0.0162 -0.0020 -0.0163 255 PRO A C   
2170 O O   . PRO A 255 ? 0.2245 0.2131 0.2585 -0.0160 -0.0011 -0.0160 255 PRO A O   
2171 C CB  . PRO A 255 ? 0.2629 0.2464 0.2990 -0.0128 -0.0029 -0.0148 255 PRO A CB  
2172 C CG  . PRO A 255 ? 0.2492 0.2309 0.2873 -0.0103 -0.0018 -0.0149 255 PRO A CG  
2173 C CD  . PRO A 255 ? 0.2555 0.2369 0.2929 -0.0099 0.0001  -0.0166 255 PRO A CD  
2174 N N   . GLU A 256 ? 0.2794 0.2611 0.3087 -0.0181 -0.0027 -0.0163 256 GLU A N   
2175 C CA  . GLU A 256 ? 0.2476 0.2307 0.2758 -0.0203 -0.0024 -0.0161 256 GLU A CA  
2176 C C   . GLU A 256 ? 0.2459 0.2310 0.2737 -0.0206 -0.0010 -0.0166 256 GLU A C   
2177 O O   . GLU A 256 ? 0.2111 0.1992 0.2395 -0.0221 -0.0004 -0.0163 256 GLU A O   
2178 C CB  . GLU A 256 ? 0.2910 0.2778 0.3211 -0.0214 -0.0029 -0.0156 256 GLU A CB  
2179 C CG  . GLU A 256 ? 0.3138 0.3002 0.3447 -0.0209 -0.0042 -0.0151 256 GLU A CG  
2180 C CD  . GLU A 256 ? 0.2839 0.2657 0.3122 -0.0219 -0.0048 -0.0152 256 GLU A CD  
2181 O OE1 . GLU A 256 ? 0.2866 0.2662 0.3130 -0.0234 -0.0042 -0.0153 256 GLU A OE1 
2182 O OE2 . GLU A 256 ? 0.3070 0.2878 0.3355 -0.0211 -0.0057 -0.0148 256 GLU A OE2 
2183 N N   . ALA A 257 ? 0.2349 0.2185 0.2616 -0.0194 -0.0002 -0.0176 257 ALA A N   
2184 C CA  . ALA A 257 ? 0.2672 0.2531 0.2933 -0.0195 0.0014  -0.0183 257 ALA A CA  
2185 C C   . ALA A 257 ? 0.2752 0.2662 0.3046 -0.0186 0.0025  -0.0181 257 ALA A C   
2186 O O   . ALA A 257 ? 0.2551 0.2492 0.2844 -0.0190 0.0039  -0.0183 257 ALA A O   
2187 C CB  . ALA A 257 ? 0.2106 0.1965 0.2342 -0.0218 0.0016  -0.0177 257 ALA A CB  
2188 N N   . SER A 258 ? 0.2565 0.2492 0.2889 -0.0174 0.0019  -0.0173 258 SER A N   
2189 C CA  . SER A 258 ? 0.1986 0.1975 0.2344 -0.0170 0.0025  -0.0163 258 SER A CA  
2190 C C   . SER A 258 ? 0.2511 0.2519 0.2888 -0.0144 0.0046  -0.0169 258 SER A C   
2191 O O   . SER A 258 ? 0.2148 0.2130 0.2535 -0.0119 0.0050  -0.0174 258 SER A O   
2192 C CB  . SER A 258 ? 0.3032 0.3043 0.3416 -0.0167 0.0011  -0.0150 258 SER A CB  
2193 O OG  . SER A 258 ? 0.4024 0.4103 0.4434 -0.0175 0.0013  -0.0138 258 SER A OG  
2194 N N   . VAL A 259 ? 0.2556 0.2611 0.2941 -0.0148 0.0060  -0.0168 259 VAL A N   
2195 C CA  . VAL A 259 ? 0.1962 0.2045 0.2369 -0.0121 0.0083  -0.0172 259 VAL A CA  
2196 C C   . VAL A 259 ? 0.2431 0.2595 0.2873 -0.0124 0.0089  -0.0153 259 VAL A C   
2197 O O   . VAL A 259 ? 0.2415 0.2610 0.2856 -0.0154 0.0077  -0.0143 259 VAL A O   
2198 C CB  . VAL A 259 ? 0.2692 0.2752 0.3066 -0.0122 0.0101  -0.0193 259 VAL A CB  
2199 C CG1 . VAL A 259 ? 0.2181 0.2169 0.2521 -0.0121 0.0095  -0.0211 259 VAL A CG1 
2200 C CG2 . VAL A 259 ? 0.2853 0.2938 0.3204 -0.0153 0.0099  -0.0189 259 VAL A CG2 
2201 N N   . SER A 260 ? 0.3156 0.3355 0.3633 -0.0092 0.0109  -0.0149 260 SER A N   
2202 C CA  . SER A 260 ? 0.3134 0.3419 0.3649 -0.0088 0.0121  -0.0131 260 SER A CA  
2203 C C   . SER A 260 ? 0.2767 0.3055 0.3300 -0.0048 0.0153  -0.0140 260 SER A C   
2204 O O   . SER A 260 ? 0.2704 0.2926 0.3222 -0.0028 0.0163  -0.0160 260 SER A O   
2205 C CB  . SER A 260 ? 0.2719 0.3064 0.3277 -0.0087 0.0106  -0.0104 260 SER A CB  
2206 O OG  . SER A 260 ? 0.2887 0.3223 0.3477 -0.0048 0.0111  -0.0094 260 SER A OG  
2207 N N   . ASN A 261 ? 0.2092 0.2458 0.2659 -0.0037 0.0171  -0.0126 261 ASN A N   
2208 C CA  . ASN A 261 ? 0.2315 0.2687 0.2903 0.0004  0.0206  -0.0134 261 ASN A CA  
2209 C C   . ASN A 261 ? 0.2212 0.2555 0.2836 0.0045  0.0213  -0.0126 261 ASN A C   
2210 O O   . ASN A 261 ? 0.2174 0.2459 0.2792 0.0073  0.0237  -0.0148 261 ASN A O   
2211 C CB  . ASN A 261 ? 0.2398 0.2871 0.3026 0.0011  0.0223  -0.0113 261 ASN A CB  
2212 C CG  . ASN A 261 ? 0.2601 0.3099 0.3196 -0.0024 0.0225  -0.0122 261 ASN A CG  
2213 O OD1 . ASN A 261 ? 0.2328 0.2765 0.2869 -0.0046 0.0219  -0.0145 261 ASN A OD1 
2214 N ND2 . ASN A 261 ? 0.2922 0.3514 0.3549 -0.0030 0.0231  -0.0099 261 ASN A ND2 
2215 N N   . GLU A 262 ? 0.2250 0.2634 0.2911 0.0046  0.0193  -0.0095 262 GLU A N   
2216 C CA  . GLU A 262 ? 0.2286 0.2648 0.2985 0.0085  0.0199  -0.0079 262 GLU A CA  
2217 C C   . GLU A 262 ? 0.2399 0.2657 0.3061 0.0080  0.0188  -0.0103 262 GLU A C   
2218 O O   . GLU A 262 ? 0.2490 0.2695 0.3167 0.0113  0.0206  -0.0109 262 GLU A O   
2219 C CB  . GLU A 262 ? 0.2486 0.2929 0.3230 0.0082  0.0177  -0.0037 262 GLU A CB  
2220 C CG  . GLU A 262 ? 0.2737 0.3293 0.3534 0.0098  0.0192  -0.0007 262 GLU A CG  
2221 C CD  . GLU A 262 ? 0.4578 0.5226 0.5419 0.0093  0.0169  0.0037  262 GLU A CD  
2222 O OE1 . GLU A 262 ? 0.5112 0.5747 0.5978 0.0117  0.0164  0.0057  262 GLU A OE1 
2223 O OE2 . GLU A 262 ? 0.4711 0.5447 0.5559 0.0063  0.0157  0.0051  262 GLU A OE2 
2224 N N   . ALA A 263 ? 0.2537 0.2764 0.3152 0.0039  0.0160  -0.0115 263 ALA A N   
2225 C CA  . ALA A 263 ? 0.2761 0.2898 0.3342 0.0033  0.0148  -0.0134 263 ALA A CA  
2226 C C   . ALA A 263 ? 0.2552 0.2622 0.3103 0.0043  0.0172  -0.0170 263 ALA A C   
2227 O O   . ALA A 263 ? 0.2269 0.2274 0.2820 0.0061  0.0180  -0.0182 263 ALA A O   
2228 C CB  . ALA A 263 ? 0.1777 0.1900 0.2316 -0.0011 0.0117  -0.0138 263 ALA A CB  
2229 N N   . LEU A 264 ? 0.2841 0.2928 0.3365 0.0030  0.0186  -0.0188 264 LEU A N   
2230 C CA  . LEU A 264 ? 0.2954 0.2987 0.3444 0.0036  0.0210  -0.0225 264 LEU A CA  
2231 C C   . LEU A 264 ? 0.3056 0.3072 0.3582 0.0081  0.0245  -0.0231 264 LEU A C   
2232 O O   . LEU A 264 ? 0.2807 0.2751 0.3312 0.0089  0.0262  -0.0263 264 LEU A O   
2233 C CB  . LEU A 264 ? 0.2507 0.2578 0.2966 0.0014  0.0218  -0.0237 264 LEU A CB  
2234 C CG  . LEU A 264 ? 0.3237 0.3303 0.3651 -0.0030 0.0190  -0.0238 264 LEU A CG  
2235 C CD1 . LEU A 264 ? 0.3491 0.3617 0.3894 -0.0048 0.0198  -0.0234 264 LEU A CD1 
2236 C CD2 . LEU A 264 ? 0.2821 0.2814 0.3183 -0.0045 0.0185  -0.0267 264 LEU A CD2 
2237 N N   . GLU A 265 ? 0.2256 0.2339 0.2840 0.0110  0.0259  -0.0202 265 GLU A N   
2238 C CA  . GLU A 265 ? 0.2507 0.2575 0.3136 0.0159  0.0295  -0.0200 265 GLU A CA  
2239 C C   . GLU A 265 ? 0.2826 0.2827 0.3473 0.0175  0.0289  -0.0193 265 GLU A C   
2240 O O   . GLU A 265 ? 0.3272 0.3204 0.3924 0.0202  0.0318  -0.0215 265 GLU A O   
2241 C CB  . GLU A 265 ? 0.2396 0.2564 0.3089 0.0187  0.0307  -0.0160 265 GLU A CB  
2242 C CG  . GLU A 265 ? 0.3119 0.3352 0.3804 0.0181  0.0325  -0.0167 265 GLU A CG  
2243 C CD  . GLU A 265 ? 0.4481 0.4680 0.5161 0.0212  0.0372  -0.0200 265 GLU A CD  
2244 O OE1 . GLU A 265 ? 0.4852 0.4982 0.5548 0.0245  0.0396  -0.0213 265 GLU A OE1 
2245 O OE2 . GLU A 265 ? 0.5334 0.5575 0.5994 0.0203  0.0387  -0.0214 265 GLU A OE2 
2246 N N   . LEU A 266 ? 0.2754 0.2773 0.3410 0.0159  0.0253  -0.0164 266 LEU A N   
2247 C CA  . LEU A 266 ? 0.2347 0.2309 0.3019 0.0172  0.0245  -0.0153 266 LEU A CA  
2248 C C   . LEU A 266 ? 0.2230 0.2091 0.2848 0.0151  0.0243  -0.0195 266 LEU A C   
2249 O O   . LEU A 266 ? 0.2678 0.2470 0.3309 0.0172  0.0261  -0.0204 266 LEU A O   
2250 C CB  . LEU A 266 ? 0.2266 0.2277 0.2952 0.0153  0.0206  -0.0117 266 LEU A CB  
2251 C CG  . LEU A 266 ? 0.2628 0.2585 0.3324 0.0159  0.0192  -0.0104 266 LEU A CG  
2252 C CD1 . LEU A 266 ? 0.3336 0.3288 0.4095 0.0209  0.0220  -0.0078 266 LEU A CD1 
2253 C CD2 . LEU A 266 ? 0.2274 0.2280 0.2968 0.0133  0.0153  -0.0076 266 LEU A CD2 
2254 N N   . TYR A 267 ? 0.2749 0.2602 0.3309 0.0109  0.0222  -0.0217 267 TYR A N   
2255 C CA  . TYR A 267 ? 0.2685 0.2456 0.3193 0.0087  0.0220  -0.0255 267 TYR A CA  
2256 C C   . TYR A 267 ? 0.3072 0.2793 0.3570 0.0106  0.0260  -0.0293 267 TYR A C   
2257 O O   . TYR A 267 ? 0.3271 0.2913 0.3752 0.0104  0.0269  -0.0319 267 TYR A O   
2258 C CB  . TYR A 267 ? 0.2791 0.2577 0.3243 0.0044  0.0195  -0.0268 267 TYR A CB  
2259 C CG  . TYR A 267 ? 0.2585 0.2387 0.3033 0.0020  0.0156  -0.0243 267 TYR A CG  
2260 C CD1 . TYR A 267 ? 0.3202 0.2956 0.3649 0.0017  0.0140  -0.0237 267 TYR A CD1 
2261 C CD2 . TYR A 267 ? 0.2671 0.2535 0.3114 0.0000  0.0139  -0.0225 267 TYR A CD2 
2262 C CE1 . TYR A 267 ? 0.2459 0.2229 0.2901 -0.0003 0.0107  -0.0216 267 TYR A CE1 
2263 C CE2 . TYR A 267 ? 0.2881 0.2755 0.3319 -0.0021 0.0107  -0.0206 267 TYR A CE2 
2264 C CZ  . TYR A 267 ? 0.2100 0.1927 0.2537 -0.0021 0.0092  -0.0202 267 TYR A CZ  
2265 O OH  . TYR A 267 ? 0.2333 0.2168 0.2762 -0.0040 0.0064  -0.0185 267 TYR A OH  
2266 N N   . TYR A 268 ? 0.2549 0.2316 0.3058 0.0122  0.0287  -0.0299 268 TYR A N   
2267 C CA  . TYR A 268 ? 0.2654 0.2377 0.3153 0.0141  0.0330  -0.0338 268 TYR A CA  
2268 C C   . TYR A 268 ? 0.3259 0.2931 0.3811 0.0185  0.0359  -0.0331 268 TYR A C   
2269 O O   . TYR A 268 ? 0.2643 0.2231 0.3177 0.0189  0.0383  -0.0368 268 TYR A O   
2270 C CB  . TYR A 268 ? 0.2597 0.2390 0.3100 0.0152  0.0353  -0.0341 268 TYR A CB  
2271 C CG  . TYR A 268 ? 0.3242 0.3002 0.3756 0.0187  0.0405  -0.0372 268 TYR A CG  
2272 C CD1 . TYR A 268 ? 0.3697 0.3385 0.4157 0.0172  0.0425  -0.0427 268 TYR A CD1 
2273 C CD2 . TYR A 268 ? 0.2989 0.2795 0.3567 0.0235  0.0436  -0.0345 268 TYR A CD2 
2274 C CE1 . TYR A 268 ? 0.4098 0.3750 0.4565 0.0203  0.0477  -0.0460 268 TYR A CE1 
2275 C CE2 . TYR A 268 ? 0.3965 0.3738 0.4556 0.0270  0.0488  -0.0374 268 TYR A CE2 
2276 C CZ  . TYR A 268 ? 0.4208 0.3899 0.4741 0.0255  0.0509  -0.0433 268 TYR A CZ  
2277 O OH  . TYR A 268 ? 0.4550 0.4203 0.5093 0.0290  0.0565  -0.0466 268 TYR A OH  
2278 N N   . GLU A 269 ? 0.2966 0.2692 0.3585 0.0218  0.0358  -0.0282 269 GLU A N   
2279 C CA  . GLU A 269 ? 0.3415 0.3098 0.4092 0.0264  0.0387  -0.0265 269 GLU A CA  
2280 C C   . GLU A 269 ? 0.3515 0.3111 0.4180 0.0250  0.0372  -0.0271 269 GLU A C   
2281 O O   . GLU A 269 ? 0.3815 0.3337 0.4506 0.0278  0.0402  -0.0279 269 GLU A O   
2282 C CB  . GLU A 269 ? 0.3601 0.3374 0.4351 0.0297  0.0382  -0.0203 269 GLU A CB  
2283 C CG  . GLU A 269 ? 0.4641 0.4501 0.5414 0.0317  0.0404  -0.0194 269 GLU A CG  
2284 C CD  . GLU A 269 ? 0.6429 0.6400 0.7264 0.0334  0.0387  -0.0132 269 GLU A CD  
2285 O OE1 . GLU A 269 ? 0.6687 0.6671 0.7535 0.0322  0.0353  -0.0100 269 GLU A OE1 
2286 O OE2 . GLU A 269 ? 0.7112 0.7162 0.7981 0.0357  0.0407  -0.0115 269 GLU A OE2 
2287 N N   . LYS A 270 ? 0.2674 0.2274 0.3302 0.0209  0.0327  -0.0267 270 LYS A N   
2288 C CA  . LYS A 270 ? 0.2803 0.2331 0.3419 0.0192  0.0309  -0.0270 270 LYS A CA  
2289 C C   . LYS A 270 ? 0.3301 0.2750 0.3851 0.0157  0.0314  -0.0327 270 LYS A C   
2290 O O   . LYS A 270 ? 0.3065 0.2465 0.3592 0.0131  0.0292  -0.0333 270 LYS A O   
2291 C CB  . LYS A 270 ? 0.3557 0.3133 0.4169 0.0167  0.0261  -0.0235 270 LYS A CB  
2292 C CG  . LYS A 270 ? 0.3847 0.3498 0.4525 0.0196  0.0252  -0.0177 270 LYS A CG  
2293 C CD  . LYS A 270 ? 0.4704 0.4316 0.5442 0.0239  0.0280  -0.0153 270 LYS A CD  
2294 C CE  . LYS A 270 ? 0.5419 0.5114 0.6220 0.0266  0.0268  -0.0090 270 LYS A CE  
2295 N NZ  . LYS A 270 ? 0.6081 0.5777 0.6951 0.0322  0.0310  -0.0065 270 LYS A NZ  
2296 N N   . GLY A 271 ? 0.3023 0.2466 0.3541 0.0155  0.0342  -0.0369 271 GLY A N   
2297 C CA  . GLY A 271 ? 0.3826 0.3200 0.4282 0.0123  0.0352  -0.0426 271 GLY A CA  
2298 C C   . GLY A 271 ? 0.3399 0.2799 0.3789 0.0072  0.0316  -0.0441 271 GLY A C   
2299 O O   . GLY A 271 ? 0.3245 0.2594 0.3583 0.0040  0.0317  -0.0483 271 GLY A O   
2300 N N   . ILE A 272 ? 0.2431 0.1907 0.2822 0.0061  0.0284  -0.0407 272 ILE A N   
2301 C CA  . ILE A 272 ? 0.2395 0.1896 0.2730 0.0017  0.0252  -0.0415 272 ILE A CA  
2302 C C   . ILE A 272 ? 0.3079 0.2608 0.3372 0.0005  0.0271  -0.0448 272 ILE A C   
2303 O O   . ILE A 272 ? 0.3013 0.2590 0.3329 0.0029  0.0292  -0.0441 272 ILE A O   
2304 C CB  . ILE A 272 ? 0.2891 0.2456 0.3243 0.0011  0.0216  -0.0369 272 ILE A CB  
2305 C CG1 . ILE A 272 ? 0.2981 0.2531 0.3379 0.0027  0.0200  -0.0334 272 ILE A CG1 
2306 C CG2 . ILE A 272 ? 0.2615 0.2198 0.2914 -0.0032 0.0185  -0.0373 272 ILE A CG2 
2307 C CD1 . ILE A 272 ? 0.4037 0.3513 0.4419 0.0011  0.0192  -0.0348 272 ILE A CD1 
2308 N N   . ASN A 273 ? 0.2966 0.2472 0.3197 -0.0032 0.0264  -0.0482 273 ASN A N   
2309 C CA  . ASN A 273 ? 0.3327 0.2861 0.3514 -0.0046 0.0283  -0.0515 273 ASN A CA  
2310 C C   . ASN A 273 ? 0.3445 0.3047 0.3600 -0.0075 0.0255  -0.0496 273 ASN A C   
2311 O O   . ASN A 273 ? 0.3361 0.3010 0.3495 -0.0078 0.0270  -0.0506 273 ASN A O   
2312 C CB  . ASN A 273 ? 0.4968 0.4441 0.5103 -0.0070 0.0299  -0.0569 273 ASN A CB  
2313 C CG  . ASN A 273 ? 0.6735 0.6149 0.6891 -0.0040 0.0346  -0.0603 273 ASN A CG  
2314 O OD1 . ASN A 273 ? 0.7133 0.6484 0.7323 -0.0023 0.0353  -0.0600 273 ASN A OD1 
2315 N ND2 . ASN A 273 ? 0.7800 0.7235 0.7937 -0.0031 0.0381  -0.0634 273 ASN A ND2 
2316 N N   . MET A 274 ? 0.2611 0.2220 0.2763 -0.0095 0.0216  -0.0467 274 MET A N   
2317 C CA  . MET A 274 ? 0.3102 0.2769 0.3228 -0.0121 0.0192  -0.0446 274 MET A CA  
2318 C C   . MET A 274 ? 0.3453 0.3130 0.3606 -0.0122 0.0159  -0.0403 274 MET A C   
2319 O O   . MET A 274 ? 0.3503 0.3141 0.3672 -0.0120 0.0145  -0.0396 274 MET A O   
2320 C CB  . MET A 274 ? 0.3273 0.2935 0.3335 -0.0159 0.0184  -0.0471 274 MET A CB  
2321 C CG  . MET A 274 ? 0.5024 0.4748 0.5060 -0.0182 0.0167  -0.0449 274 MET A CG  
2322 S SD  . MET A 274 ? 0.7386 0.7108 0.7415 -0.0205 0.0124  -0.0414 274 MET A SD  
2323 C CE  . MET A 274 ? 0.6439 0.6134 0.6412 -0.0238 0.0121  -0.0450 274 MET A CE  
2324 N N   . LEU A 275 ? 0.3064 0.2796 0.3223 -0.0128 0.0148  -0.0376 275 LEU A N   
2325 C CA  . LEU A 275 ? 0.3155 0.2899 0.3327 -0.0137 0.0117  -0.0341 275 LEU A CA  
2326 C C   . LEU A 275 ? 0.3197 0.2983 0.3341 -0.0162 0.0107  -0.0327 275 LEU A C   
2327 O O   . LEU A 275 ? 0.2605 0.2418 0.2723 -0.0170 0.0123  -0.0342 275 LEU A O   
2328 C CB  . LEU A 275 ? 0.4033 0.3795 0.4259 -0.0112 0.0117  -0.0316 275 LEU A CB  
2329 C CG  . LEU A 275 ? 0.4647 0.4458 0.4900 -0.0094 0.0140  -0.0312 275 LEU A CG  
2330 C CD1 . LEU A 275 ? 0.5027 0.4893 0.5276 -0.0112 0.0129  -0.0290 275 LEU A CD1 
2331 C CD2 . LEU A 275 ? 0.4194 0.4010 0.4503 -0.0061 0.0147  -0.0297 275 LEU A CD2 
2332 N N   . ALA A 276 ? 0.2728 0.2520 0.2878 -0.0172 0.0083  -0.0299 276 ALA A N   
2333 C CA  . ALA A 276 ? 0.2768 0.2597 0.2904 -0.0192 0.0076  -0.0278 276 ALA A CA  
2334 C C   . ALA A 276 ? 0.3188 0.3035 0.3359 -0.0187 0.0067  -0.0252 276 ALA A C   
2335 O O   . ALA A 276 ? 0.3193 0.3024 0.3393 -0.0174 0.0059  -0.0246 276 ALA A O   
2336 C CB  . ALA A 276 ? 0.2053 0.1869 0.2155 -0.0215 0.0057  -0.0269 276 ALA A CB  
2337 N N   . THR A 277 ? 0.2706 0.2590 0.2876 -0.0200 0.0069  -0.0237 277 THR A N   
2338 C CA  . THR A 277 ? 0.2987 0.2886 0.3183 -0.0206 0.0060  -0.0214 277 THR A CA  
2339 C C   . THR A 277 ? 0.2956 0.2865 0.3132 -0.0230 0.0055  -0.0196 277 THR A C   
2340 O O   . THR A 277 ? 0.2559 0.2460 0.2702 -0.0240 0.0054  -0.0196 277 THR A O   
2341 C CB  . THR A 277 ? 0.3034 0.2977 0.3265 -0.0193 0.0074  -0.0213 277 THR A CB  
2342 O OG1 . THR A 277 ? 0.2835 0.2797 0.3089 -0.0204 0.0063  -0.0194 277 THR A OG1 
2343 C CG2 . THR A 277 ? 0.2560 0.2544 0.2780 -0.0198 0.0094  -0.0218 277 THR A CG2 
2344 N N   . ASP A 278 ? 0.2219 0.2144 0.2414 -0.0241 0.0052  -0.0179 278 ASP A N   
2345 C CA  . ASP A 278 ? 0.2182 0.2103 0.2364 -0.0264 0.0048  -0.0159 278 ASP A CA  
2346 C C   . ASP A 278 ? 0.2427 0.2390 0.2604 -0.0277 0.0064  -0.0150 278 ASP A C   
2347 O O   . ASP A 278 ? 0.3099 0.3103 0.3292 -0.0271 0.0076  -0.0158 278 ASP A O   
2348 C CB  . ASP A 278 ? 0.2230 0.2136 0.2432 -0.0274 0.0039  -0.0147 278 ASP A CB  
2349 C CG  . ASP A 278 ? 0.3044 0.2927 0.3233 -0.0294 0.0037  -0.0127 278 ASP A CG  
2350 O OD1 . ASP A 278 ? 0.3499 0.3354 0.3668 -0.0293 0.0032  -0.0119 278 ASP A OD1 
2351 O OD2 . ASP A 278 ? 0.3948 0.3843 0.4150 -0.0313 0.0043  -0.0117 278 ASP A OD2 
2352 N N   . GLU A 279 ? 0.3294 0.3250 0.3452 -0.0294 0.0063  -0.0131 279 GLU A N   
2353 C CA  . GLU A 279 ? 0.3502 0.3497 0.3654 -0.0310 0.0076  -0.0116 279 GLU A CA  
2354 C C   . GLU A 279 ? 0.3282 0.3301 0.3463 -0.0324 0.0082  -0.0107 279 GLU A C   
2355 O O   . GLU A 279 ? 0.3448 0.3514 0.3633 -0.0332 0.0096  -0.0102 279 GLU A O   
2356 C CB  . GLU A 279 ? 0.3400 0.3378 0.3531 -0.0324 0.0073  -0.0090 279 GLU A CB  
2357 C CG  . GLU A 279 ? 0.3810 0.3830 0.3930 -0.0339 0.0086  -0.0070 279 GLU A CG  
2358 C CD  . GLU A 279 ? 0.4628 0.4641 0.4725 -0.0348 0.0083  -0.0041 279 GLU A CD  
2359 O OE1 . GLU A 279 ? 0.4395 0.4372 0.4483 -0.0341 0.0071  -0.0038 279 GLU A OE1 
2360 O OE2 . GLU A 279 ? 0.4876 0.4924 0.4966 -0.0362 0.0094  -0.0018 279 GLU A OE2 
2361 N N   . VAL A 280 ? 0.2936 0.2927 0.3136 -0.0330 0.0072  -0.0106 280 VAL A N   
2362 C CA  . VAL A 280 ? 0.2735 0.2754 0.2962 -0.0348 0.0077  -0.0101 280 VAL A CA  
2363 C C   . VAL A 280 ? 0.2939 0.3014 0.3188 -0.0334 0.0083  -0.0114 280 VAL A C   
2364 O O   . VAL A 280 ? 0.2398 0.2522 0.2666 -0.0348 0.0092  -0.0107 280 VAL A O   
2365 C CB  . VAL A 280 ? 0.2940 0.2917 0.3177 -0.0360 0.0065  -0.0101 280 VAL A CB  
2366 C CG1 . VAL A 280 ? 0.3384 0.3398 0.3648 -0.0382 0.0067  -0.0101 280 VAL A CG1 
2367 C CG2 . VAL A 280 ? 0.3466 0.3390 0.3687 -0.0373 0.0065  -0.0084 280 VAL A CG2 
2368 N N   . ILE A 281 ? 0.2819 0.2889 0.3068 -0.0306 0.0081  -0.0132 281 ILE A N   
2369 C CA  . ILE A 281 ? 0.2573 0.2694 0.2848 -0.0286 0.0091  -0.0141 281 ILE A CA  
2370 C C   . ILE A 281 ? 0.3200 0.3365 0.3466 -0.0285 0.0111  -0.0141 281 ILE A C   
2371 O O   . ILE A 281 ? 0.3049 0.3273 0.3340 -0.0285 0.0123  -0.0136 281 ILE A O   
2372 C CB  . ILE A 281 ? 0.2469 0.2565 0.2746 -0.0255 0.0087  -0.0159 281 ILE A CB  
2373 C CG1 . ILE A 281 ? 0.3468 0.3522 0.3750 -0.0257 0.0067  -0.0157 281 ILE A CG1 
2374 C CG2 . ILE A 281 ? 0.2081 0.2227 0.2390 -0.0232 0.0101  -0.0164 281 ILE A CG2 
2375 C CD1 . ILE A 281 ? 0.3868 0.3945 0.4172 -0.0278 0.0059  -0.0146 281 ILE A CD1 
2376 N N   . LEU A 282 ? 0.2909 0.3052 0.3140 -0.0284 0.0115  -0.0145 282 LEU A N   
2377 C CA  . LEU A 282 ? 0.3316 0.3503 0.3532 -0.0286 0.0134  -0.0146 282 LEU A CA  
2378 C C   . LEU A 282 ? 0.3210 0.3441 0.3439 -0.0312 0.0140  -0.0121 282 LEU A C   
2379 O O   . LEU A 282 ? 0.2968 0.3259 0.3214 -0.0310 0.0157  -0.0120 282 LEU A O   
2380 C CB  . LEU A 282 ? 0.3480 0.3641 0.3652 -0.0289 0.0133  -0.0150 282 LEU A CB  
2381 C CG  . LEU A 282 ? 0.3744 0.3952 0.3892 -0.0288 0.0154  -0.0157 282 LEU A CG  
2382 C CD1 . LEU A 282 ? 0.3381 0.3616 0.3545 -0.0262 0.0173  -0.0183 282 LEU A CD1 
2383 C CD2 . LEU A 282 ? 0.3622 0.3810 0.3724 -0.0293 0.0150  -0.0163 282 LEU A CD2 
2384 N N   . LYS A 283 ? 0.2982 0.3182 0.3207 -0.0338 0.0129  -0.0101 283 LYS A N   
2385 C CA  . LYS A 283 ? 0.3778 0.4012 0.4015 -0.0367 0.0136  -0.0077 283 LYS A CA  
2386 C C   . LYS A 283 ? 0.2617 0.2894 0.2894 -0.0375 0.0137  -0.0076 283 LYS A C   
2387 O O   . LYS A 283 ? 0.3127 0.3459 0.3418 -0.0392 0.0149  -0.0062 283 LYS A O   
2388 C CB  . LYS A 283 ? 0.5193 0.5374 0.5419 -0.0391 0.0127  -0.0055 283 LYS A CB  
2389 C CG  . LYS A 283 ? 0.6592 0.6743 0.6782 -0.0384 0.0125  -0.0049 283 LYS A CG  
2390 C CD  . LYS A 283 ? 0.7448 0.7653 0.7618 -0.0385 0.0141  -0.0040 283 LYS A CD  
2391 C CE  . LYS A 283 ? 0.7402 0.7593 0.7534 -0.0376 0.0137  -0.0040 283 LYS A CE  
2392 N NZ  . LYS A 283 ? 0.7519 0.7654 0.7646 -0.0360 0.0120  -0.0057 283 LYS A NZ  
2393 N N   . ASN A 284 ? 0.2326 0.2586 0.2620 -0.0364 0.0125  -0.0089 284 ASN A N   
2394 C CA  . ASN A 284 ? 0.2686 0.3002 0.3019 -0.0370 0.0125  -0.0087 284 ASN A CA  
2395 C C   . ASN A 284 ? 0.2807 0.3191 0.3160 -0.0343 0.0142  -0.0092 284 ASN A C   
2396 O O   . ASN A 284 ? 0.2468 0.2919 0.2855 -0.0350 0.0147  -0.0082 284 ASN A O   
2397 C CB  . ASN A 284 ? 0.3512 0.3798 0.3857 -0.0364 0.0107  -0.0097 284 ASN A CB  
2398 C CG  . ASN A 284 ? 0.3784 0.4017 0.4119 -0.0397 0.0094  -0.0092 284 ASN A CG  
2399 O OD1 . ASN A 284 ? 0.3658 0.3875 0.3982 -0.0424 0.0099  -0.0079 284 ASN A OD1 
2400 N ND2 . ASN A 284 ? 0.3405 0.3611 0.3745 -0.0393 0.0079  -0.0102 284 ASN A ND2 
2401 N N   . SER A 285 ? 0.2649 0.3019 0.2982 -0.0312 0.0152  -0.0108 285 SER A N   
2402 C CA  . SER A 285 ? 0.2881 0.3302 0.3234 -0.0279 0.0172  -0.0118 285 SER A CA  
2403 C C   . SER A 285 ? 0.3426 0.3890 0.3764 -0.0277 0.0196  -0.0118 285 SER A C   
2404 O O   . SER A 285 ? 0.3694 0.4219 0.4058 -0.0256 0.0216  -0.0120 285 SER A O   
2405 C CB  . SER A 285 ? 0.2871 0.3242 0.3215 -0.0244 0.0171  -0.0142 285 SER A CB  
2406 O OG  . SER A 285 ? 0.3196 0.3524 0.3549 -0.0245 0.0148  -0.0141 285 SER A OG  
2407 N N   . VAL A 286 ? 0.3041 0.3481 0.3340 -0.0295 0.0196  -0.0115 286 VAL A N   
2408 C CA  . VAL A 286 ? 0.3620 0.4104 0.3898 -0.0295 0.0218  -0.0115 286 VAL A CA  
2409 C C   . VAL A 286 ? 0.4349 0.4847 0.4617 -0.0334 0.0214  -0.0085 286 VAL A C   
2410 O O   . VAL A 286 ? 0.4390 0.4833 0.4642 -0.0354 0.0197  -0.0074 286 VAL A O   
2411 C CB  . VAL A 286 ? 0.3464 0.3911 0.3698 -0.0277 0.0225  -0.0141 286 VAL A CB  
2412 C CG1 . VAL A 286 ? 0.3957 0.4461 0.4171 -0.0273 0.0252  -0.0147 286 VAL A CG1 
2413 C CG2 . VAL A 286 ? 0.3922 0.4328 0.4165 -0.0243 0.0224  -0.0169 286 VAL A CG2 
2414 N N   . GLU A 287 ? 0.3612 0.4184 0.3893 -0.0345 0.0233  -0.0070 287 GLU A N   
2415 C CA  . GLU A 287 ? 0.3573 0.4162 0.3851 -0.0383 0.0231  -0.0038 287 GLU A CA  
2416 C C   . GLU A 287 ? 0.3968 0.4513 0.4201 -0.0394 0.0226  -0.0029 287 GLU A C   
2417 O O   . GLU A 287 ? 0.4242 0.4742 0.4472 -0.0418 0.0213  -0.0008 287 GLU A O   
2418 C CB  . GLU A 287 ? 0.3600 0.4282 0.3896 -0.0389 0.0254  -0.0023 287 GLU A CB  
2419 C CG  . GLU A 287 ? 0.4169 0.4902 0.4516 -0.0399 0.0253  -0.0012 287 GLU A CG  
2420 C CD  . GLU A 287 ? 0.5261 0.6092 0.5629 -0.0407 0.0276  0.0006  287 GLU A CD  
2421 O OE1 . GLU A 287 ? 0.5132 0.5993 0.5473 -0.0404 0.0294  0.0010  287 GLU A OE1 
2422 O OE2 . GLU A 287 ? 0.5165 0.6052 0.5578 -0.0416 0.0275  0.0018  287 GLU A OE2 
2423 N N   . ARG A 288 ? 0.3580 0.4140 0.3778 -0.0375 0.0239  -0.0046 288 ARG A N   
2424 C CA  . ARG A 288 ? 0.3463 0.3996 0.3617 -0.0385 0.0234  -0.0037 288 ARG A CA  
2425 C C   . ARG A 288 ? 0.3195 0.3695 0.3318 -0.0358 0.0232  -0.0075 288 ARG A C   
2426 O O   . ARG A 288 ? 0.4048 0.4583 0.4161 -0.0338 0.0251  -0.0102 288 ARG A O   
2427 C CB  . ARG A 288 ? 0.4059 0.4662 0.4195 -0.0400 0.0252  -0.0015 288 ARG A CB  
2428 C CG  . ARG A 288 ? 0.3910 0.4500 0.4002 -0.0411 0.0247  0.0001  288 ARG A CG  
2429 C CD  . ARG A 288 ? 0.4083 0.4735 0.4136 -0.0403 0.0266  -0.0015 288 ARG A CD  
2430 N NE  . ARG A 288 ? 0.4864 0.5597 0.4931 -0.0412 0.0289  0.0002  288 ARG A NE  
2431 C CZ  . ARG A 288 ? 0.4059 0.4853 0.4112 -0.0397 0.0313  -0.0023 288 ARG A CZ  
2432 N NH1 . ARG A 288 ? 0.2854 0.3725 0.2923 -0.0406 0.0333  -0.0003 288 ARG A NH1 
2433 N NH2 . ARG A 288 ? 0.4577 0.5354 0.4600 -0.0373 0.0320  -0.0069 288 ARG A NH2 
2434 N N   . ALA A 289 ? 0.3471 0.3903 0.3581 -0.0358 0.0211  -0.0076 289 ALA A N   
2435 C CA  . ALA A 289 ? 0.3580 0.3975 0.3666 -0.0336 0.0207  -0.0112 289 ALA A CA  
2436 C C   . ALA A 289 ? 0.3449 0.3796 0.3506 -0.0346 0.0187  -0.0102 289 ALA A C   
2437 O O   . ALA A 289 ? 0.3857 0.4163 0.3930 -0.0356 0.0170  -0.0078 289 ALA A O   
2438 C CB  . ALA A 289 ? 0.4454 0.4815 0.4574 -0.0313 0.0202  -0.0135 289 ALA A CB  
2439 N N   . SER A 290 ? 0.3300 0.3656 0.3314 -0.0343 0.0190  -0.0120 290 SER A N   
2440 C CA  . SER A 290 ? 0.3607 0.3926 0.3594 -0.0351 0.0171  -0.0109 290 SER A CA  
2441 C C   . SER A 290 ? 0.3616 0.3875 0.3605 -0.0334 0.0158  -0.0141 290 SER A C   
2442 O O   . SER A 290 ? 0.3071 0.3327 0.3057 -0.0316 0.0170  -0.0180 290 SER A O   
2443 C CB  . SER A 290 ? 0.3344 0.3711 0.3282 -0.0363 0.0177  -0.0110 290 SER A CB  
2444 O OG  . SER A 290 ? 0.3135 0.3473 0.3047 -0.0369 0.0158  -0.0107 290 SER A OG  
2445 N N   . PRO A 291 ? 0.3735 0.3945 0.3730 -0.0337 0.0137  -0.0124 291 PRO A N   
2446 C CA  . PRO A 291 ? 0.3050 0.3207 0.3045 -0.0322 0.0124  -0.0150 291 PRO A CA  
2447 C C   . PRO A 291 ? 0.2642 0.2798 0.2594 -0.0327 0.0119  -0.0170 291 PRO A C   
2448 O O   . PRO A 291 ? 0.3242 0.3354 0.3193 -0.0319 0.0106  -0.0186 291 PRO A O   
2449 C CB  . PRO A 291 ? 0.3399 0.3513 0.3418 -0.0326 0.0105  -0.0120 291 PRO A CB  
2450 C CG  . PRO A 291 ? 0.2833 0.2973 0.2839 -0.0346 0.0105  -0.0080 291 PRO A CG  
2451 C CD  . PRO A 291 ? 0.2766 0.2969 0.2766 -0.0353 0.0125  -0.0079 291 PRO A CD  
2452 N N   . TYR A 292 ? 0.2518 0.2728 0.2434 -0.0341 0.0128  -0.0168 292 TYR A N   
2453 C CA  . TYR A 292 ? 0.2627 0.2847 0.2496 -0.0352 0.0123  -0.0186 292 TYR A CA  
2454 C C   . TYR A 292 ? 0.2592 0.2821 0.2434 -0.0347 0.0143  -0.0239 292 TYR A C   
2455 O O   . TYR A 292 ? 0.3092 0.3338 0.2888 -0.0362 0.0143  -0.0261 292 TYR A O   
2456 C CB  . TYR A 292 ? 0.2894 0.3171 0.2735 -0.0375 0.0118  -0.0147 292 TYR A CB  
2457 C CG  . TYR A 292 ? 0.3493 0.3753 0.3362 -0.0378 0.0102  -0.0093 292 TYR A CG  
2458 C CD1 . TYR A 292 ? 0.2691 0.2891 0.2583 -0.0368 0.0084  -0.0088 292 TYR A CD1 
2459 C CD2 . TYR A 292 ? 0.3899 0.4200 0.3772 -0.0389 0.0108  -0.0047 292 TYR A CD2 
2460 C CE1 . TYR A 292 ? 0.3758 0.3937 0.3675 -0.0368 0.0074  -0.0042 292 TYR A CE1 
2461 C CE2 . TYR A 292 ? 0.4101 0.4378 0.4003 -0.0390 0.0097  0.0001  292 TYR A CE2 
2462 C CZ  . TYR A 292 ? 0.3763 0.3977 0.3687 -0.0379 0.0082  0.0002  292 TYR A CZ  
2463 O OH  . TYR A 292 ? 0.4120 0.4303 0.4070 -0.0379 0.0076  0.0046  292 TYR A OH  
2464 N N   . LEU A 293 ? 0.2923 0.3143 0.2793 -0.0327 0.0162  -0.0261 293 LEU A N   
2465 C CA  . LEU A 293 ? 0.2942 0.3164 0.2795 -0.0315 0.0188  -0.0311 293 LEU A CA  
2466 C C   . LEU A 293 ? 0.2959 0.3111 0.2838 -0.0292 0.0187  -0.0340 293 LEU A C   
2467 O O   . LEU A 293 ? 0.2946 0.3063 0.2865 -0.0282 0.0170  -0.0319 293 LEU A O   
2468 C CB  . LEU A 293 ? 0.2872 0.3143 0.2745 -0.0304 0.0215  -0.0309 293 LEU A CB  
2469 C CG  . LEU A 293 ? 0.4151 0.4500 0.3995 -0.0322 0.0227  -0.0291 293 LEU A CG  
2470 C CD1 . LEU A 293 ? 0.4652 0.5021 0.4505 -0.0342 0.0206  -0.0234 293 LEU A CD1 
2471 C CD2 . LEU A 293 ? 0.4225 0.4614 0.4092 -0.0306 0.0257  -0.0299 293 LEU A CD2 
2472 N N   . ARG A 294 ? 0.2626 0.2760 0.2484 -0.0285 0.0207  -0.0389 294 ARG A N   
2473 C CA  . ARG A 294 ? 0.2665 0.2737 0.2554 -0.0258 0.0214  -0.0415 294 ARG A CA  
2474 C C   . ARG A 294 ? 0.2765 0.2858 0.2696 -0.0229 0.0241  -0.0416 294 ARG A C   
2475 O O   . ARG A 294 ? 0.2723 0.2861 0.2637 -0.0227 0.0267  -0.0431 294 ARG A O   
2476 C CB  . ARG A 294 ? 0.2799 0.2832 0.2650 -0.0264 0.0226  -0.0467 294 ARG A CB  
2477 C CG  . ARG A 294 ? 0.3211 0.3174 0.3099 -0.0235 0.0236  -0.0491 294 ARG A CG  
2478 C CD  . ARG A 294 ? 0.2998 0.2908 0.2847 -0.0248 0.0243  -0.0540 294 ARG A CD  
2479 N NE  . ARG A 294 ? 0.2939 0.2871 0.2743 -0.0256 0.0276  -0.0585 294 ARG A NE  
2480 C CZ  . ARG A 294 ? 0.3627 0.3572 0.3368 -0.0291 0.0274  -0.0614 294 ARG A CZ  
2481 N NH1 . ARG A 294 ? 0.3265 0.3206 0.2983 -0.0321 0.0240  -0.0600 294 ARG A NH1 
2482 N NH2 . ARG A 294 ? 0.3259 0.3227 0.2960 -0.0297 0.0307  -0.0657 294 ARG A NH2 
2483 N N   . TYR A 295 ? 0.3140 0.3208 0.3124 -0.0207 0.0233  -0.0398 295 TYR A N   
2484 C CA  . TYR A 295 ? 0.3244 0.3342 0.3274 -0.0180 0.0255  -0.0391 295 TYR A CA  
2485 C C   . TYR A 295 ? 0.2970 0.3022 0.3028 -0.0147 0.0275  -0.0420 295 TYR A C   
2486 O O   . TYR A 295 ? 0.2967 0.2958 0.3029 -0.0143 0.0262  -0.0428 295 TYR A O   
2487 C CB  . TYR A 295 ? 0.3092 0.3212 0.3166 -0.0181 0.0235  -0.0346 295 TYR A CB  
2488 C CG  . TYR A 295 ? 0.3027 0.3199 0.3085 -0.0209 0.0226  -0.0315 295 TYR A CG  
2489 C CD1 . TYR A 295 ? 0.2437 0.2594 0.2465 -0.0236 0.0201  -0.0298 295 TYR A CD1 
2490 C CD2 . TYR A 295 ? 0.3027 0.3264 0.3103 -0.0208 0.0244  -0.0300 295 TYR A CD2 
2491 C CE1 . TYR A 295 ? 0.2854 0.3054 0.2871 -0.0259 0.0195  -0.0265 295 TYR A CE1 
2492 C CE2 . TYR A 295 ? 0.2319 0.2599 0.2381 -0.0235 0.0236  -0.0269 295 TYR A CE2 
2493 C CZ  . TYR A 295 ? 0.2472 0.2730 0.2505 -0.0260 0.0213  -0.0252 295 TYR A CZ  
2494 O OH  . TYR A 295 ? 0.3049 0.3346 0.3073 -0.0285 0.0207  -0.0216 295 TYR A OH  
2495 N N   . TYR A 296 ? 0.2154 0.2238 0.2234 -0.0121 0.0309  -0.0430 296 TYR A N   
2496 C CA  . TYR A 296 ? 0.2618 0.2665 0.2734 -0.0082 0.0334  -0.0450 296 TYR A CA  
2497 C C   . TYR A 296 ? 0.3375 0.3470 0.3558 -0.0057 0.0337  -0.0414 296 TYR A C   
2498 O O   . TYR A 296 ? 0.3233 0.3396 0.3427 -0.0052 0.0355  -0.0403 296 TYR A O   
2499 C CB  . TYR A 296 ? 0.3107 0.3151 0.3195 -0.0070 0.0377  -0.0498 296 TYR A CB  
2500 C CG  . TYR A 296 ? 0.4242 0.4253 0.4259 -0.0101 0.0375  -0.0537 296 TYR A CG  
2501 C CD1 . TYR A 296 ? 0.4465 0.4417 0.4463 -0.0121 0.0347  -0.0543 296 TYR A CD1 
2502 C CD2 . TYR A 296 ? 0.4875 0.4920 0.4843 -0.0113 0.0403  -0.0570 296 TYR A CD2 
2503 C CE1 . TYR A 296 ? 0.4573 0.4502 0.4506 -0.0153 0.0345  -0.0579 296 TYR A CE1 
2504 C CE2 . TYR A 296 ? 0.4437 0.4461 0.4338 -0.0145 0.0400  -0.0607 296 TYR A CE2 
2505 C CZ  . TYR A 296 ? 0.4393 0.4360 0.4278 -0.0166 0.0371  -0.0611 296 TYR A CZ  
2506 O OH  . TYR A 296 ? 0.4330 0.4284 0.4149 -0.0202 0.0367  -0.0646 296 TYR A OH  
2507 N N   . PHE A 297 ? 0.2854 0.2920 0.3080 -0.0042 0.0320  -0.0393 297 PHE A N   
2508 C CA  . PHE A 297 ? 0.2731 0.2847 0.3020 -0.0019 0.0322  -0.0358 297 PHE A CA  
2509 C C   . PHE A 297 ? 0.2872 0.2992 0.3196 0.0026  0.0364  -0.0373 297 PHE A C   
2510 O O   . PHE A 297 ? 0.2900 0.2958 0.3239 0.0051  0.0376  -0.0389 297 PHE A O   
2511 C CB  . PHE A 297 ? 0.3106 0.3198 0.3426 -0.0020 0.0289  -0.0331 297 PHE A CB  
2512 C CG  . PHE A 297 ? 0.3084 0.3232 0.3468 0.0002  0.0289  -0.0294 297 PHE A CG  
2513 C CD1 . PHE A 297 ? 0.3303 0.3523 0.3701 -0.0019 0.0275  -0.0265 297 PHE A CD1 
2514 C CD2 . PHE A 297 ? 0.2581 0.2714 0.3013 0.0041  0.0303  -0.0289 297 PHE A CD2 
2515 C CE1 . PHE A 297 ? 0.2720 0.3002 0.3176 -0.0004 0.0274  -0.0231 297 PHE A CE1 
2516 C CE2 . PHE A 297 ? 0.2303 0.2501 0.2796 0.0060  0.0302  -0.0251 297 PHE A CE2 
2517 C CZ  . PHE A 297 ? 0.2238 0.2514 0.2742 0.0036  0.0286  -0.0224 297 PHE A CZ  
2518 N N   . ARG A 298 ? 0.2841 0.3032 0.3178 0.0037  0.0390  -0.0369 298 ARG A N   
2519 C CA  . ARG A 298 ? 0.2764 0.2973 0.3141 0.0083  0.0434  -0.0377 298 ARG A CA  
2520 C C   . ARG A 298 ? 0.3140 0.3272 0.3486 0.0101  0.0468  -0.0430 298 ARG A C   
2521 O O   . ARG A 298 ? 0.2975 0.3091 0.3358 0.0144  0.0504  -0.0439 298 ARG A O   
2522 C CB  . ARG A 298 ? 0.2789 0.3018 0.3241 0.0117  0.0431  -0.0339 298 ARG A CB  
2523 C CG  . ARG A 298 ? 0.2652 0.2975 0.3140 0.0102  0.0407  -0.0291 298 ARG A CG  
2524 C CD  . ARG A 298 ? 0.3256 0.3609 0.3813 0.0126  0.0395  -0.0250 298 ARG A CD  
2525 N NE  . ARG A 298 ? 0.3091 0.3523 0.3665 0.0095  0.0365  -0.0212 298 ARG A NE  
2526 C CZ  . ARG A 298 ? 0.3167 0.3646 0.3791 0.0099  0.0345  -0.0173 298 ARG A CZ  
2527 N NH1 . ARG A 298 ? 0.3249 0.3713 0.3919 0.0137  0.0352  -0.0159 298 ARG A NH1 
2528 N NH2 . ARG A 298 ? 0.3044 0.3589 0.3674 0.0063  0.0319  -0.0147 298 ARG A NH2 
2529 N N   . GLU A 299 ? 0.3829 0.3914 0.4106 0.0065  0.0457  -0.0464 299 GLU A N   
2530 C CA  . GLU A 299 ? 0.3138 0.3142 0.3375 0.0069  0.0482  -0.0519 299 GLU A CA  
2531 C C   . GLU A 299 ? 0.3036 0.2958 0.3306 0.0092  0.0480  -0.0520 299 GLU A C   
2532 O O   . GLU A 299 ? 0.3220 0.3073 0.3481 0.0109  0.0512  -0.0561 299 GLU A O   
2533 C CB  . GLU A 299 ? 0.3665 0.3686 0.3896 0.0096  0.0537  -0.0554 299 GLU A CB  
2534 C CG  . GLU A 299 ? 0.3958 0.4062 0.4151 0.0074  0.0544  -0.0556 299 GLU A CG  
2535 C CD  . GLU A 299 ? 0.4355 0.4438 0.4463 0.0027  0.0532  -0.0592 299 GLU A CD  
2536 O OE1 . GLU A 299 ? 0.4380 0.4407 0.4463 0.0000  0.0500  -0.0598 299 GLU A OE1 
2537 O OE2 . GLU A 299 ? 0.5112 0.5245 0.5181 0.0016  0.0554  -0.0613 299 GLU A OE2 
2538 N N   . LEU A 300 ? 0.2385 0.2314 0.2694 0.0091  0.0444  -0.0476 300 LEU A N   
2539 C CA  . LEU A 300 ? 0.3028 0.2892 0.3373 0.0110  0.0437  -0.0467 300 LEU A CA  
2540 C C   . LEU A 300 ? 0.3670 0.3474 0.3973 0.0072  0.0400  -0.0476 300 LEU A C   
2541 O O   . LEU A 300 ? 0.3650 0.3375 0.3954 0.0079  0.0405  -0.0495 300 LEU A O   
2542 C CB  . LEU A 300 ? 0.3224 0.3143 0.3640 0.0134  0.0421  -0.0410 300 LEU A CB  
2543 C CG  . LEU A 300 ? 0.4476 0.4440 0.4962 0.0186  0.0456  -0.0387 300 LEU A CG  
2544 C CD1 . LEU A 300 ? 0.5795 0.5793 0.6269 0.0201  0.0499  -0.0413 300 LEU A CD1 
2545 C CD2 . LEU A 300 ? 0.3879 0.3930 0.4416 0.0188  0.0429  -0.0329 300 LEU A CD2 
2546 N N   . ILE A 301 ? 0.2276 0.2116 0.2547 0.0033  0.0363  -0.0459 301 ILE A N   
2547 C CA  . ILE A 301 ? 0.2485 0.2282 0.2729 0.0002  0.0325  -0.0456 301 ILE A CA  
2548 C C   . ILE A 301 ? 0.3064 0.2902 0.3256 -0.0040 0.0301  -0.0453 301 ILE A C   
2549 O O   . ILE A 301 ? 0.3032 0.2938 0.3230 -0.0044 0.0301  -0.0433 301 ILE A O   
2550 C CB  . ILE A 301 ? 0.3378 0.3177 0.3673 0.0014  0.0297  -0.0412 301 ILE A CB  
2551 C CG1 . ILE A 301 ? 0.3054 0.2810 0.3322 -0.0017 0.0260  -0.0408 301 ILE A CG1 
2552 C CG2 . ILE A 301 ? 0.3422 0.3305 0.3748 0.0015  0.0285  -0.0372 301 ILE A CG2 
2553 C CD1 . ILE A 301 ? 0.2551 0.2304 0.2865 -0.0004 0.0237  -0.0370 301 ILE A CD1 
2554 N N   . SER A 302 ? 0.2869 0.2667 0.3013 -0.0072 0.0283  -0.0472 302 SER A N   
2555 C CA  . SER A 302 ? 0.2995 0.2831 0.3091 -0.0109 0.0262  -0.0466 302 SER A CA  
2556 C C   . SER A 302 ? 0.2947 0.2801 0.3061 -0.0123 0.0223  -0.0421 302 SER A C   
2557 O O   . SER A 302 ? 0.3065 0.2880 0.3201 -0.0117 0.0205  -0.0408 302 SER A O   
2558 C CB  . SER A 302 ? 0.3616 0.3414 0.3652 -0.0138 0.0259  -0.0502 302 SER A CB  
2559 O OG  . SER A 302 ? 0.3868 0.3646 0.3886 -0.0128 0.0298  -0.0549 302 SER A OG  
2560 N N   . VAL A 303 ? 0.2543 0.2452 0.2645 -0.0141 0.0213  -0.0399 303 VAL A N   
2561 C CA  . VAL A 303 ? 0.2935 0.2858 0.3051 -0.0155 0.0182  -0.0359 303 VAL A CA  
2562 C C   . VAL A 303 ? 0.3085 0.3030 0.3157 -0.0189 0.0167  -0.0349 303 VAL A C   
2563 O O   . VAL A 303 ? 0.3391 0.3379 0.3438 -0.0198 0.0182  -0.0354 303 VAL A O   
2564 C CB  . VAL A 303 ? 0.3075 0.3046 0.3238 -0.0142 0.0185  -0.0330 303 VAL A CB  
2565 C CG1 . VAL A 303 ? 0.3084 0.3060 0.3258 -0.0160 0.0155  -0.0296 303 VAL A CG1 
2566 C CG2 . VAL A 303 ? 0.2634 0.2596 0.2845 -0.0106 0.0201  -0.0334 303 VAL A CG2 
2567 N N   . PHE A 304 ? 0.2240 0.2160 0.2302 -0.0205 0.0139  -0.0333 304 PHE A N   
2568 C CA  . PHE A 304 ? 0.2577 0.2521 0.2611 -0.0231 0.0123  -0.0309 304 PHE A CA  
2569 C C   . PHE A 304 ? 0.2982 0.2931 0.3049 -0.0233 0.0106  -0.0271 304 PHE A C   
2570 O O   . PHE A 304 ? 0.2990 0.2910 0.3087 -0.0220 0.0096  -0.0266 304 PHE A O   
2571 C CB  . PHE A 304 ? 0.2786 0.2704 0.2784 -0.0249 0.0106  -0.0316 304 PHE A CB  
2572 C CG  . PHE A 304 ? 0.2707 0.2632 0.2660 -0.0261 0.0121  -0.0351 304 PHE A CG  
2573 C CD1 . PHE A 304 ? 0.2607 0.2585 0.2523 -0.0281 0.0126  -0.0347 304 PHE A CD1 
2574 C CD2 . PHE A 304 ? 0.2309 0.2190 0.2256 -0.0253 0.0131  -0.0390 304 PHE A CD2 
2575 C CE1 . PHE A 304 ? 0.2769 0.2760 0.2638 -0.0295 0.0140  -0.0383 304 PHE A CE1 
2576 C CE2 . PHE A 304 ? 0.2405 0.2290 0.2306 -0.0268 0.0146  -0.0428 304 PHE A CE2 
2577 C CZ  . PHE A 304 ? 0.2616 0.2559 0.2476 -0.0290 0.0150  -0.0426 304 PHE A CZ  
2578 N N   . PHE A 305 ? 0.2170 0.2155 0.2228 -0.0250 0.0105  -0.0246 305 PHE A N   
2579 C CA  . PHE A 305 ? 0.1777 0.1760 0.1860 -0.0257 0.0091  -0.0214 305 PHE A CA  
2580 C C   . PHE A 305 ? 0.2511 0.2477 0.2570 -0.0274 0.0073  -0.0193 305 PHE A C   
2581 O O   . PHE A 305 ? 0.2804 0.2797 0.2833 -0.0288 0.0076  -0.0184 305 PHE A O   
2582 C CB  . PHE A 305 ? 0.1869 0.1899 0.1967 -0.0264 0.0104  -0.0198 305 PHE A CB  
2583 C CG  . PHE A 305 ? 0.2846 0.2903 0.2971 -0.0245 0.0122  -0.0215 305 PHE A CG  
2584 C CD1 . PHE A 305 ? 0.3637 0.3718 0.3746 -0.0235 0.0144  -0.0239 305 PHE A CD1 
2585 C CD2 . PHE A 305 ? 0.2777 0.2837 0.2943 -0.0237 0.0118  -0.0206 305 PHE A CD2 
2586 C CE1 . PHE A 305 ? 0.3229 0.3335 0.3367 -0.0213 0.0164  -0.0252 305 PHE A CE1 
2587 C CE2 . PHE A 305 ? 0.2731 0.2824 0.2928 -0.0217 0.0136  -0.0215 305 PHE A CE2 
2588 C CZ  . PHE A 305 ? 0.3177 0.3291 0.3361 -0.0203 0.0159  -0.0237 305 PHE A CZ  
2589 N N   . ARG A 306 ? 0.2663 0.2590 0.2737 -0.0271 0.0056  -0.0182 306 ARG A N   
2590 C CA  . ARG A 306 ? 0.3176 0.3087 0.3231 -0.0282 0.0041  -0.0161 306 ARG A CA  
2591 C C   . ARG A 306 ? 0.3168 0.3101 0.3222 -0.0297 0.0044  -0.0127 306 ARG A C   
2592 O O   . ARG A 306 ? 0.2917 0.2862 0.2991 -0.0300 0.0053  -0.0118 306 ARG A O   
2593 C CB  . ARG A 306 ? 0.3404 0.3272 0.3479 -0.0273 0.0025  -0.0156 306 ARG A CB  
2594 C CG  . ARG A 306 ? 0.3230 0.3087 0.3335 -0.0273 0.0025  -0.0141 306 ARG A CG  
2595 C CD  . ARG A 306 ? 0.3706 0.3524 0.3825 -0.0267 0.0010  -0.0135 306 ARG A CD  
2596 N NE  . ARG A 306 ? 0.3308 0.3117 0.3445 -0.0274 0.0013  -0.0120 306 ARG A NE  
2597 C CZ  . ARG A 306 ? 0.2940 0.2717 0.3085 -0.0275 0.0006  -0.0106 306 ARG A CZ  
2598 N NH1 . ARG A 306 ? 0.2406 0.2158 0.2544 -0.0267 -0.0005 -0.0102 306 ARG A NH1 
2599 N NH2 . ARG A 306 ? 0.2790 0.2560 0.2949 -0.0286 0.0012  -0.0099 306 ARG A NH2 
2600 N N   . ASP A 307 ? 0.2662 0.2602 0.2693 -0.0307 0.0037  -0.0105 307 ASP A N   
2601 C CA  . ASP A 307 ? 0.2414 0.2364 0.2448 -0.0318 0.0039  -0.0065 307 ASP A CA  
2602 C C   . ASP A 307 ? 0.2289 0.2191 0.2352 -0.0313 0.0032  -0.0049 307 ASP A C   
2603 O O   . ASP A 307 ? 0.2400 0.2276 0.2461 -0.0306 0.0020  -0.0040 307 ASP A O   
2604 C CB  . ASP A 307 ? 0.2102 0.2082 0.2107 -0.0327 0.0033  -0.0042 307 ASP A CB  
2605 C CG  . ASP A 307 ? 0.3744 0.3746 0.3753 -0.0338 0.0040  0.0003  307 ASP A CG  
2606 O OD1 . ASP A 307 ? 0.3896 0.3861 0.3931 -0.0335 0.0041  0.0026  307 ASP A OD1 
2607 O OD2 . ASP A 307 ? 0.4282 0.4336 0.4265 -0.0349 0.0045  0.0015  307 ASP A OD2 
2608 N N   . LYS A 308 ? 0.2551 0.2443 0.2637 -0.0317 0.0040  -0.0046 308 LYS A N   
2609 C CA  . LYS A 308 ? 0.2846 0.2691 0.2956 -0.0315 0.0036  -0.0039 308 LYS A CA  
2610 C C   . LYS A 308 ? 0.2858 0.2678 0.2968 -0.0317 0.0036  -0.0003 308 LYS A C   
2611 O O   . LYS A 308 ? 0.2449 0.2229 0.2567 -0.0308 0.0029  0.0000  308 LYS A O   
2612 C CB  . LYS A 308 ? 0.3049 0.2897 0.3181 -0.0326 0.0047  -0.0043 308 LYS A CB  
2613 C CG  . LYS A 308 ? 0.2728 0.2529 0.2880 -0.0332 0.0046  -0.0040 308 LYS A CG  
2614 C CD  . LYS A 308 ? 0.3333 0.3151 0.3504 -0.0349 0.0055  -0.0048 308 LYS A CD  
2615 C CE  . LYS A 308 ? 0.3827 0.3605 0.4014 -0.0359 0.0054  -0.0055 308 LYS A CE  
2616 N NZ  . LYS A 308 ? 0.3587 0.3313 0.3770 -0.0349 0.0048  -0.0050 308 LYS A NZ  
2617 N N   . THR A 309 ? 0.3231 0.3075 0.3333 -0.0327 0.0045  0.0028  309 THR A N   
2618 C CA  . THR A 309 ? 0.2924 0.2744 0.3031 -0.0326 0.0047  0.0069  309 THR A CA  
2619 C C   . THR A 309 ? 0.2721 0.2542 0.2818 -0.0311 0.0034  0.0077  309 THR A C   
2620 O O   . THR A 309 ? 0.2811 0.2590 0.2921 -0.0301 0.0032  0.0090  309 THR A O   
2621 C CB  . THR A 309 ? 0.3496 0.3354 0.3597 -0.0338 0.0059  0.0105  309 THR A CB  
2622 O OG1 . THR A 309 ? 0.3788 0.3650 0.3902 -0.0354 0.0072  0.0098  309 THR A OG1 
2623 C CG2 . THR A 309 ? 0.2896 0.2727 0.3011 -0.0333 0.0065  0.0153  309 THR A CG2 
2624 N N   . LEU A 310 ? 0.2617 0.2485 0.2688 -0.0313 0.0025  0.0070  310 LEU A N   
2625 C CA  . LEU A 310 ? 0.2558 0.2435 0.2616 -0.0305 0.0010  0.0078  310 LEU A CA  
2626 C C   . LEU A 310 ? 0.3035 0.2871 0.3104 -0.0293 0.0000  0.0050  310 LEU A C   
2627 O O   . LEU A 310 ? 0.3177 0.2999 0.3251 -0.0283 -0.0009 0.0066  310 LEU A O   
2628 C CB  . LEU A 310 ? 0.2815 0.2751 0.2839 -0.0316 0.0004  0.0065  310 LEU A CB  
2629 C CG  . LEU A 310 ? 0.3473 0.3466 0.3482 -0.0329 0.0012  0.0096  310 LEU A CG  
2630 C CD1 . LEU A 310 ? 0.3484 0.3530 0.3454 -0.0342 0.0008  0.0068  310 LEU A CD1 
2631 C CD2 . LEU A 310 ? 0.3142 0.3149 0.3157 -0.0325 0.0008  0.0152  310 LEU A CD2 
2632 N N   . SER A 311 ? 0.2455 0.2277 0.2529 -0.0292 0.0001  0.0011  311 SER A N   
2633 C CA  . SER A 311 ? 0.2365 0.2151 0.2450 -0.0281 -0.0008 -0.0012 311 SER A CA  
2634 C C   . SER A 311 ? 0.2675 0.2416 0.2783 -0.0273 -0.0005 0.0004  311 SER A C   
2635 O O   . SER A 311 ? 0.2557 0.2277 0.2672 -0.0262 -0.0013 0.0007  311 SER A O   
2636 C CB  . SER A 311 ? 0.2453 0.2239 0.2543 -0.0280 -0.0006 -0.0050 311 SER A CB  
2637 O OG  . SER A 311 ? 0.2806 0.2627 0.2875 -0.0285 -0.0005 -0.0069 311 SER A OG  
2638 N N   . ASP A 312 ? 0.2021 0.1749 0.2142 -0.0281 0.0010  0.0014  312 ASP A N   
2639 C CA  . ASP A 312 ? 0.2622 0.2301 0.2762 -0.0278 0.0018  0.0026  312 ASP A CA  
2640 C C   . ASP A 312 ? 0.2749 0.2415 0.2892 -0.0268 0.0021  0.0065  312 ASP A C   
2641 O O   . ASP A 312 ? 0.2806 0.2430 0.2963 -0.0257 0.0025  0.0071  312 ASP A O   
2642 C CB  . ASP A 312 ? 0.2852 0.2519 0.3003 -0.0295 0.0034  0.0026  312 ASP A CB  
2643 C CG  . ASP A 312 ? 0.3812 0.3484 0.3969 -0.0303 0.0032  -0.0010 312 ASP A CG  
2644 O OD1 . ASP A 312 ? 0.4258 0.3933 0.4414 -0.0293 0.0020  -0.0034 312 ASP A OD1 
2645 O OD2 . ASP A 312 ? 0.4149 0.3827 0.4314 -0.0320 0.0042  -0.0012 312 ASP A OD2 
2646 N N   . LEU A 313 ? 0.2722 0.2427 0.2854 -0.0270 0.0021  0.0095  313 LEU A N   
2647 C CA  . LEU A 313 ? 0.2154 0.1857 0.2294 -0.0258 0.0024  0.0141  313 LEU A CA  
2648 C C   . LEU A 313 ? 0.2568 0.2269 0.2709 -0.0242 0.0010  0.0138  313 LEU A C   
2649 O O   . LEU A 313 ? 0.2316 0.1983 0.2475 -0.0227 0.0017  0.0159  313 LEU A O   
2650 C CB  . LEU A 313 ? 0.1956 0.1718 0.2082 -0.0266 0.0023  0.0174  313 LEU A CB  
2651 C CG  . LEU A 313 ? 0.2884 0.2642 0.3018 -0.0278 0.0042  0.0193  313 LEU A CG  
2652 C CD1 . LEU A 313 ? 0.2792 0.2620 0.2906 -0.0289 0.0040  0.0219  313 LEU A CD1 
2653 C CD2 . LEU A 313 ? 0.2466 0.2168 0.2627 -0.0268 0.0061  0.0229  313 LEU A CD2 
2654 N N   . ILE A 314 ? 0.2836 0.2568 0.2959 -0.0246 -0.0007 0.0112  314 ILE A N   
2655 C CA  . ILE A 314 ? 0.2989 0.2722 0.3113 -0.0235 -0.0021 0.0109  314 ILE A CA  
2656 C C   . ILE A 314 ? 0.2745 0.2427 0.2884 -0.0225 -0.0019 0.0085  314 ILE A C   
2657 O O   . ILE A 314 ? 0.2332 0.1994 0.2485 -0.0210 -0.0018 0.0099  314 ILE A O   
2658 C CB  . ILE A 314 ? 0.2436 0.2212 0.2536 -0.0246 -0.0039 0.0085  314 ILE A CB  
2659 C CG1 . ILE A 314 ? 0.3119 0.2953 0.3199 -0.0258 -0.0042 0.0112  314 ILE A CG1 
2660 C CG2 . ILE A 314 ? 0.2020 0.1791 0.2123 -0.0238 -0.0053 0.0077  314 ILE A CG2 
2661 C CD1 . ILE A 314 ? 0.4160 0.4035 0.4210 -0.0274 -0.0056 0.0085  314 ILE A CD1 
2662 N N   . GLY A 315 ? 0.2073 0.1739 0.2212 -0.0234 -0.0016 0.0050  315 GLY A N   
2663 C CA  . GLY A 315 ? 0.2562 0.2194 0.2713 -0.0228 -0.0017 0.0024  315 GLY A CA  
2664 C C   . GLY A 315 ? 0.3032 0.2617 0.3198 -0.0222 0.0000  0.0035  315 GLY A C   
2665 O O   . GLY A 315 ? 0.2820 0.2380 0.2993 -0.0214 -0.0001 0.0022  315 GLY A O   
2666 N N   . PHE A 316 ? 0.2892 0.2463 0.3062 -0.0227 0.0016  0.0058  316 PHE A N   
2667 C CA  . PHE A 316 ? 0.2651 0.2167 0.2835 -0.0226 0.0036  0.0060  316 PHE A CA  
2668 C C   . PHE A 316 ? 0.3175 0.2671 0.3372 -0.0217 0.0054  0.0103  316 PHE A C   
2669 O O   . PHE A 316 ? 0.3203 0.2645 0.3412 -0.0209 0.0073  0.0107  316 PHE A O   
2670 C CB  . PHE A 316 ? 0.3216 0.2720 0.3401 -0.0248 0.0044  0.0033  316 PHE A CB  
2671 C CG  . PHE A 316 ? 0.4064 0.3585 0.4243 -0.0255 0.0030  -0.0006 316 PHE A CG  
2672 C CD1 . PHE A 316 ? 0.4517 0.4015 0.4700 -0.0251 0.0029  -0.0027 316 PHE A CD1 
2673 C CD2 . PHE A 316 ? 0.4681 0.4246 0.4853 -0.0264 0.0019  -0.0020 316 PHE A CD2 
2674 C CE1 . PHE A 316 ? 0.4756 0.4277 0.4937 -0.0255 0.0016  -0.0057 316 PHE A CE1 
2675 C CE2 . PHE A 316 ? 0.5429 0.5011 0.5602 -0.0266 0.0009  -0.0050 316 PHE A CE2 
2676 C CZ  . PHE A 316 ? 0.5167 0.4730 0.5346 -0.0262 0.0006  -0.0066 316 PHE A CZ  
2677 N N   . SER A 317 ? 0.2631 0.2165 0.2825 -0.0217 0.0052  0.0137  317 SER A N   
2678 C CA  . SER A 317 ? 0.2302 0.1820 0.2511 -0.0209 0.0071  0.0185  317 SER A CA  
2679 C C   . SER A 317 ? 0.2484 0.2027 0.2702 -0.0184 0.0067  0.0226  317 SER A C   
2680 O O   . SER A 317 ? 0.2466 0.1971 0.2706 -0.0165 0.0087  0.0255  317 SER A O   
2681 C CB  . SER A 317 ? 0.2748 0.2303 0.2950 -0.0226 0.0073  0.0204  317 SER A CB  
2682 O OG  . SER A 317 ? 0.3354 0.2893 0.3551 -0.0248 0.0078  0.0170  317 SER A OG  
2683 N N   . TYR A 318 ? 0.3253 0.2860 0.3455 -0.0186 0.0044  0.0230  318 TYR A N   
2684 C CA  . TYR A 318 ? 0.3458 0.3109 0.3668 -0.0169 0.0039  0.0278  318 TYR A CA  
2685 C C   . TYR A 318 ? 0.3021 0.2649 0.3250 -0.0144 0.0042  0.0286  318 TYR A C   
2686 O O   . TYR A 318 ? 0.3184 0.2843 0.3429 -0.0126 0.0043  0.0334  318 TYR A O   
2687 C CB  . TYR A 318 ? 0.2262 0.1990 0.2448 -0.0184 0.0012  0.0273  318 TYR A CB  
2688 C CG  . TYR A 318 ? 0.2384 0.2154 0.2553 -0.0203 0.0012  0.0283  318 TYR A CG  
2689 C CD1 . TYR A 318 ? 0.2131 0.1884 0.2314 -0.0202 0.0033  0.0317  318 TYR A CD1 
2690 C CD2 . TYR A 318 ? 0.2943 0.2768 0.3081 -0.0223 -0.0007 0.0260  318 TYR A CD2 
2691 C CE1 . TYR A 318 ? 0.2522 0.2320 0.2689 -0.0220 0.0033  0.0330  318 TYR A CE1 
2692 C CE2 . TYR A 318 ? 0.2388 0.2255 0.2508 -0.0240 -0.0006 0.0267  318 TYR A CE2 
2693 C CZ  . TYR A 318 ? 0.2837 0.2696 0.2972 -0.0239 0.0013  0.0304  318 TYR A CZ  
2694 O OH  . TYR A 318 ? 0.2667 0.2575 0.2782 -0.0257 0.0014  0.0313  318 TYR A OH  
2695 N N   . HIS A 319 ? 0.2882 0.2465 0.3110 -0.0143 0.0043  0.0244  319 HIS A N   
2696 C CA  . HIS A 319 ? 0.2606 0.2162 0.2853 -0.0118 0.0052  0.0252  319 HIS A CA  
2697 C C   . HIS A 319 ? 0.3219 0.2731 0.3492 -0.0097 0.0083  0.0293  319 HIS A C   
2698 O O   . HIS A 319 ? 0.2898 0.2414 0.3192 -0.0069 0.0091  0.0326  319 HIS A O   
2699 C CB  . HIS A 319 ? 0.1802 0.1314 0.2041 -0.0123 0.0051  0.0199  319 HIS A CB  
2700 C CG  . HIS A 319 ? 0.2997 0.2441 0.3240 -0.0130 0.0076  0.0178  319 HIS A CG  
2701 N ND1 . HIS A 319 ? 0.3111 0.2496 0.3371 -0.0113 0.0104  0.0185  319 HIS A ND1 
2702 C CD2 . HIS A 319 ? 0.3064 0.2491 0.3296 -0.0155 0.0078  0.0150  319 HIS A CD2 
2703 C CE1 . HIS A 319 ? 0.3796 0.3127 0.4053 -0.0130 0.0121  0.0159  319 HIS A CE1 
2704 N NE2 . HIS A 319 ? 0.3200 0.2559 0.3441 -0.0156 0.0105  0.0139  319 HIS A NE2 
2705 N N   . ALA A 320 ? 0.2705 0.2178 0.2981 -0.0107 0.0102  0.0296  320 ALA A N   
2706 C CA  . ALA A 320 ? 0.3245 0.2666 0.3550 -0.0088 0.0136  0.0334  320 ALA A CA  
2707 C C   . ALA A 320 ? 0.3124 0.2594 0.3445 -0.0076 0.0139  0.0402  320 ALA A C   
2708 O O   . ALA A 320 ? 0.3171 0.2598 0.3519 -0.0060 0.0169  0.0441  320 ALA A O   
2709 C CB  . ALA A 320 ? 0.2412 0.1758 0.2715 -0.0107 0.0158  0.0304  320 ALA A CB  
2710 N N   . TRP A 321 ? 0.2766 0.2323 0.3072 -0.0085 0.0110  0.0417  321 TRP A N   
2711 C CA  . TRP A 321 ? 0.2681 0.2301 0.2999 -0.0078 0.0109  0.0483  321 TRP A CA  
2712 C C   . TRP A 321 ? 0.3086 0.2772 0.3415 -0.0057 0.0094  0.0520  321 TRP A C   
2713 O O   . TRP A 321 ? 0.2983 0.2682 0.3302 -0.0057 0.0077  0.0489  321 TRP A O   
2714 C CB  . TRP A 321 ? 0.2771 0.2455 0.3059 -0.0109 0.0088  0.0477  321 TRP A CB  
2715 C CG  . TRP A 321 ? 0.3085 0.2729 0.3362 -0.0133 0.0098  0.0449  321 TRP A CG  
2716 C CD1 . TRP A 321 ? 0.2222 0.1795 0.2494 -0.0144 0.0108  0.0396  321 TRP A CD1 
2717 C CD2 . TRP A 321 ? 0.2957 0.2644 0.3225 -0.0151 0.0098  0.0473  321 TRP A CD2 
2718 N NE1 . TRP A 321 ? 0.2910 0.2478 0.3172 -0.0169 0.0113  0.0387  321 TRP A NE1 
2719 C CE2 . TRP A 321 ? 0.3367 0.3003 0.3627 -0.0172 0.0109  0.0434  321 TRP A CE2 
2720 C CE3 . TRP A 321 ? 0.3898 0.3669 0.4164 -0.0153 0.0090  0.0527  321 TRP A CE3 
2721 C CZ2 . TRP A 321 ? 0.3468 0.3131 0.3720 -0.0193 0.0112  0.0446  321 TRP A CZ2 
2722 C CZ3 . TRP A 321 ? 0.3791 0.3587 0.4045 -0.0174 0.0094  0.0539  321 TRP A CZ3 
2723 C CH2 . TRP A 321 ? 0.3362 0.3103 0.3611 -0.0193 0.0106  0.0499  321 TRP A CH2 
2724 N N   . ASN A 322 ? 0.2923 0.2661 0.3274 -0.0042 0.0100  0.0590  322 ASN A N   
2725 C CA  . ASN A 322 ? 0.3757 0.3590 0.4112 -0.0033 0.0079  0.0631  322 ASN A CA  
2726 C C   . ASN A 322 ? 0.3831 0.3742 0.4143 -0.0070 0.0042  0.0601  322 ASN A C   
2727 O O   . ASN A 322 ? 0.3552 0.3466 0.3840 -0.0096 0.0038  0.0580  322 ASN A O   
2728 C CB  . ASN A 322 ? 0.4837 0.4711 0.5228 -0.0008 0.0096  0.0718  322 ASN A CB  
2729 C CG  . ASN A 322 ? 0.5326 0.5328 0.5712 -0.0015 0.0068  0.0765  322 ASN A CG  
2730 O OD1 . ASN A 322 ? 0.5664 0.5730 0.6019 -0.0046 0.0047  0.0762  322 ASN A OD1 
2731 N ND2 . ASN A 322 ? 0.4728 0.4772 0.5144 0.0013  0.0068  0.0809  322 ASN A ND2 
2732 N N   . ALA A 323 ? 0.3699 0.3142 0.4024 0.0065  0.0216  0.0345  323 ALA A N   
2733 C CA  . ALA A 323 ? 0.3380 0.2907 0.3633 0.0046  0.0173  0.0361  323 ALA A CA  
2734 C C   . ALA A 323 ? 0.2880 0.2424 0.3120 0.0045  0.0135  0.0433  323 ALA A C   
2735 O O   . ALA A 323 ? 0.2657 0.2230 0.2825 0.0013  0.0114  0.0434  323 ALA A O   
2736 C CB  . ALA A 323 ? 0.3502 0.3104 0.3770 0.0066  0.0163  0.0356  323 ALA A CB  
2737 N N   . GLU A 324 ? 0.3683 0.3214 0.3995 0.0077  0.0126  0.0495  324 GLU A N   
2738 C CA  . GLU A 324 ? 0.4008 0.3562 0.4301 0.0066  0.0087  0.0569  324 GLU A CA  
2739 C C   . GLU A 324 ? 0.4056 0.3556 0.4303 0.0029  0.0091  0.0572  324 GLU A C   
2740 O O   . GLU A 324 ? 0.3416 0.2957 0.3598 -0.0003 0.0066  0.0596  324 GLU A O   
2741 C CB  . GLU A 324 ? 0.4731 0.4281 0.5119 0.0104  0.0072  0.0642  324 GLU A CB  
2742 C CG  . GLU A 324 ? 0.6165 0.5789 0.6602 0.0138  0.0061  0.0652  324 GLU A CG  
2743 C CD  . GLU A 324 ? 0.7593 0.7187 0.8120 0.0178  0.0105  0.0606  324 GLU A CD  
2744 O OE1 . GLU A 324 ? 0.8022 0.7672 0.8622 0.0213  0.0099  0.0628  324 GLU A OE1 
2745 O OE2 . GLU A 324 ? 0.7833 0.7353 0.8359 0.0171  0.0147  0.0547  324 GLU A OE2 
2746 N N   . ASP A 325 ? 0.3227 0.2638 0.3506 0.0028  0.0125  0.0545  325 ASP A N   
2747 C CA  . ASP A 325 ? 0.3651 0.3010 0.3888 -0.0012 0.0130  0.0550  325 ASP A CA  
2748 C C   . ASP A 325 ? 0.3427 0.2828 0.3576 -0.0054 0.0132  0.0497  325 ASP A C   
2749 O O   . ASP A 325 ? 0.3112 0.2530 0.3211 -0.0090 0.0120  0.0514  325 ASP A O   
2750 C CB  . ASP A 325 ? 0.4993 0.4239 0.5284 -0.0005 0.0167  0.0529  325 ASP A CB  
2751 C CG  . ASP A 325 ? 0.6735 0.5930 0.7130 0.0039  0.0163  0.0588  325 ASP A CG  
2752 O OD1 . ASP A 325 ? 0.7060 0.6294 0.7469 0.0045  0.0122  0.0668  325 ASP A OD1 
2753 O OD2 . ASP A 325 ? 0.7122 0.6238 0.7586 0.0066  0.0200  0.0556  325 ASP A OD2 
2754 N N   . ALA A 326 ? 0.2949 0.2371 0.3085 -0.0051 0.0148  0.0433  326 ALA A N   
2755 C CA  . ALA A 326 ? 0.2637 0.2106 0.2704 -0.0086 0.0143  0.0388  326 ALA A CA  
2756 C C   . ALA A 326 ? 0.3204 0.2754 0.3227 -0.0093 0.0109  0.0417  326 ALA A C   
2757 O O   . ALA A 326 ? 0.2596 0.2173 0.2574 -0.0124 0.0104  0.0408  326 ALA A O   
2758 C CB  . ALA A 326 ? 0.2888 0.2374 0.2950 -0.0081 0.0156  0.0328  326 ALA A CB  
2759 N N   . VAL A 327 ? 0.3022 0.2616 0.3060 -0.0065 0.0087  0.0449  327 VAL A N   
2760 C CA  . VAL A 327 ? 0.3064 0.2731 0.3055 -0.0075 0.0058  0.0470  327 VAL A CA  
2761 C C   . VAL A 327 ? 0.3562 0.3227 0.3534 -0.0099 0.0048  0.0521  327 VAL A C   
2762 O O   . VAL A 327 ? 0.3552 0.3265 0.3471 -0.0126 0.0039  0.0518  327 VAL A O   
2763 C CB  . VAL A 327 ? 0.3629 0.3341 0.3636 -0.0047 0.0036  0.0491  327 VAL A CB  
2764 C CG1 . VAL A 327 ? 0.2754 0.2529 0.2708 -0.0063 0.0006  0.0520  327 VAL A CG1 
2765 C CG2 . VAL A 327 ? 0.3769 0.3495 0.3777 -0.0036 0.0043  0.0437  327 VAL A CG2 
2766 N N   . ARG A 328 ? 0.2904 0.2515 0.2922 -0.0090 0.0050  0.0571  328 ARG A N   
2767 C CA  . ARG A 328 ? 0.3668 0.3274 0.3666 -0.0121 0.0039  0.0626  328 ARG A CA  
2768 C C   . ARG A 328 ? 0.3476 0.3071 0.3431 -0.0162 0.0058  0.0591  328 ARG A C   
2769 O O   . ARG A 328 ? 0.3796 0.3436 0.3700 -0.0198 0.0050  0.0607  328 ARG A O   
2770 C CB  . ARG A 328 ? 0.3023 0.2559 0.3089 -0.0104 0.0035  0.0686  328 ARG A CB  
2771 C CG  . ARG A 328 ? 0.4237 0.3755 0.4282 -0.0144 0.0020  0.0750  328 ARG A CG  
2772 C CD  . ARG A 328 ? 0.5283 0.4723 0.5407 -0.0123 0.0010  0.0818  328 ARG A CD  
2773 N NE  . ARG A 328 ? 0.6223 0.5560 0.6390 -0.0115 0.0043  0.0784  328 ARG A NE  
2774 C CZ  . ARG A 328 ? 0.6815 0.6089 0.7068 -0.0067 0.0062  0.0768  328 ARG A CZ  
2775 N NH1 . ARG A 328 ? 0.7119 0.6431 0.7429 -0.0020 0.0050  0.0786  328 ARG A NH1 
2776 N NH2 . ARG A 328 ? 0.6972 0.6147 0.7251 -0.0068 0.0096  0.0730  328 ARG A NH2 
2777 N N   . ASP A 329 ? 0.3824 0.3367 0.3798 -0.0161 0.0084  0.0542  329 ASP A N   
2778 C CA  . ASP A 329 ? 0.3769 0.3308 0.3707 -0.0202 0.0101  0.0509  329 ASP A CA  
2779 C C   . ASP A 329 ? 0.3430 0.3058 0.3323 -0.0216 0.0095  0.0472  329 ASP A C   
2780 O O   . ASP A 329 ? 0.3242 0.2911 0.3101 -0.0251 0.0096  0.0476  329 ASP A O   
2781 C CB  . ASP A 329 ? 0.3418 0.2886 0.3381 -0.0201 0.0128  0.0462  329 ASP A CB  
2782 C CG  . ASP A 329 ? 0.3488 0.2955 0.3418 -0.0248 0.0143  0.0431  329 ASP A CG  
2783 O OD1 . ASP A 329 ? 0.3743 0.3165 0.3669 -0.0278 0.0148  0.0462  329 ASP A OD1 
2784 O OD2 . ASP A 329 ? 0.3245 0.2758 0.3156 -0.0258 0.0145  0.0382  329 ASP A OD2 
2785 N N   . PHE A 330 ? 0.3066 0.2726 0.2962 -0.0190 0.0089  0.0435  330 PHE A N   
2786 C CA  . PHE A 330 ? 0.3198 0.2932 0.3063 -0.0196 0.0081  0.0399  330 PHE A CA  
2787 C C   . PHE A 330 ? 0.3470 0.3262 0.3300 -0.0208 0.0068  0.0428  330 PHE A C   
2788 O O   . PHE A 330 ? 0.2991 0.2833 0.2797 -0.0233 0.0075  0.0409  330 PHE A O   
2789 C CB  . PHE A 330 ? 0.2646 0.2393 0.2521 -0.0166 0.0070  0.0368  330 PHE A CB  
2790 C CG  . PHE A 330 ? 0.3288 0.3090 0.3145 -0.0171 0.0061  0.0324  330 PHE A CG  
2791 C CD1 . PHE A 330 ? 0.3187 0.2986 0.3052 -0.0189 0.0068  0.0286  330 PHE A CD1 
2792 C CD2 . PHE A 330 ? 0.2946 0.2801 0.2782 -0.0160 0.0042  0.0324  330 PHE A CD2 
2793 C CE1 . PHE A 330 ? 0.3692 0.3543 0.3555 -0.0190 0.0054  0.0254  330 PHE A CE1 
2794 C CE2 . PHE A 330 ? 0.3675 0.3571 0.3506 -0.0160 0.0032  0.0285  330 PHE A CE2 
2795 C CZ  . PHE A 330 ? 0.3316 0.3212 0.3166 -0.0173 0.0037  0.0253  330 PHE A CZ  
2796 N N   . ILE A 331 ? 0.3381 0.3174 0.3209 -0.0193 0.0051  0.0473  331 ILE A N   
2797 C CA  . ILE A 331 ? 0.3618 0.3467 0.3403 -0.0213 0.0038  0.0502  331 ILE A CA  
2798 C C   . ILE A 331 ? 0.3872 0.3725 0.3634 -0.0257 0.0049  0.0529  331 ILE A C   
2799 O O   . ILE A 331 ? 0.3776 0.3690 0.3494 -0.0288 0.0054  0.0519  331 ILE A O   
2800 C CB  . ILE A 331 ? 0.4033 0.3882 0.3824 -0.0195 0.0013  0.0554  331 ILE A CB  
2801 C CG1 . ILE A 331 ? 0.4311 0.4172 0.4115 -0.0160 0.0002  0.0524  331 ILE A CG1 
2802 C CG2 . ILE A 331 ? 0.3931 0.3835 0.3665 -0.0229 -0.0002 0.0591  331 ILE A CG2 
2803 C CD1 . ILE A 331 ? 0.4480 0.4393 0.4242 -0.0166 -0.0001 0.0474  331 ILE A CD1 
2804 N N   . GLY A 332 ? 0.3384 0.3170 0.3175 -0.0264 0.0055  0.0561  332 GLY A N   
2805 C CA  . GLY A 332 ? 0.3030 0.2814 0.2797 -0.0312 0.0062  0.0593  332 GLY A CA  
2806 C C   . GLY A 332 ? 0.3369 0.3198 0.3115 -0.0342 0.0086  0.0541  332 GLY A C   
2807 O O   . GLY A 332 ? 0.4052 0.3932 0.3760 -0.0385 0.0093  0.0552  332 GLY A O   
2808 N N   . ARG A 333 ? 0.3265 0.3083 0.3040 -0.0322 0.0098  0.0486  333 ARG A N   
2809 C CA  . ARG A 333 ? 0.3380 0.3252 0.3149 -0.0347 0.0116  0.0440  333 ARG A CA  
2810 C C   . ARG A 333 ? 0.2951 0.2915 0.2698 -0.0345 0.0117  0.0411  333 ARG A C   
2811 O O   . ARG A 333 ? 0.3254 0.3281 0.2985 -0.0379 0.0134  0.0398  333 ARG A O   
2812 C CB  . ARG A 333 ? 0.2862 0.2704 0.2666 -0.0330 0.0122  0.0394  333 ARG A CB  
2813 C CG  . ARG A 333 ? 0.2900 0.2648 0.2721 -0.0342 0.0130  0.0410  333 ARG A CG  
2814 C CD  . ARG A 333 ? 0.3380 0.3095 0.3226 -0.0324 0.0133  0.0365  333 ARG A CD  
2815 N NE  . ARG A 333 ? 0.3730 0.3351 0.3586 -0.0339 0.0148  0.0368  333 ARG A NE  
2816 C CZ  . ARG A 333 ? 0.4164 0.3769 0.4013 -0.0383 0.0161  0.0356  333 ARG A CZ  
2817 N NH1 . ARG A 333 ? 0.3788 0.3475 0.3626 -0.0414 0.0162  0.0345  333 ARG A NH1 
2818 N NH2 . ARG A 333 ? 0.4069 0.3578 0.3924 -0.0398 0.0176  0.0355  333 ARG A NH2 
2819 N N   . LEU A 334 ? 0.3105 0.3078 0.2850 -0.0309 0.0101  0.0399  334 LEU A N   
2820 C CA  . LEU A 334 ? 0.3115 0.3162 0.2836 -0.0308 0.0104  0.0369  334 LEU A CA  
2821 C C   . LEU A 334 ? 0.3397 0.3487 0.3066 -0.0350 0.0111  0.0400  334 LEU A C   
2822 O O   . LEU A 334 ? 0.3055 0.3216 0.2705 -0.0370 0.0131  0.0367  334 LEU A O   
2823 C CB  . LEU A 334 ? 0.2930 0.2966 0.2650 -0.0269 0.0082  0.0359  334 LEU A CB  
2824 C CG  . LEU A 334 ? 0.3294 0.3302 0.3056 -0.0234 0.0072  0.0325  334 LEU A CG  
2825 C CD1 . LEU A 334 ? 0.2779 0.2774 0.2533 -0.0204 0.0048  0.0329  334 LEU A CD1 
2826 C CD2 . LEU A 334 ? 0.3139 0.3196 0.2926 -0.0234 0.0082  0.0271  334 LEU A CD2 
2827 N N   . LYS A 335 ? 0.3547 0.3597 0.3196 -0.0365 0.0096  0.0465  335 LYS A N   
2828 C CA  . LYS A 335 ? 0.3513 0.3603 0.3105 -0.0416 0.0098  0.0504  335 LYS A CA  
2829 C C   . LYS A 335 ? 0.3325 0.3450 0.2909 -0.0464 0.0125  0.0496  335 LYS A C   
2830 O O   . LYS A 335 ? 0.3290 0.3487 0.2827 -0.0508 0.0142  0.0489  335 LYS A O   
2831 C CB  . LYS A 335 ? 0.4280 0.4317 0.3864 -0.0423 0.0068  0.0586  335 LYS A CB  
2832 C CG  . LYS A 335 ? 0.5393 0.5481 0.4907 -0.0478 0.0059  0.0633  335 LYS A CG  
2833 C CD  . LYS A 335 ? 0.5770 0.5815 0.5288 -0.0479 0.0020  0.0721  335 LYS A CD  
2834 C CE  . LYS A 335 ? 0.6633 0.6641 0.6150 -0.0522 0.0012  0.0790  335 LYS A CE  
2835 N NZ  . LYS A 335 ? 0.7084 0.7159 0.6519 -0.0601 0.0012  0.0822  335 LYS A NZ  
2836 N N   . LYS A 336 ? 0.2739 0.2817 0.2364 -0.0461 0.0132  0.0494  336 LYS A N   
2837 C CA  . LYS A 336 ? 0.2927 0.3041 0.2547 -0.0510 0.0156  0.0487  336 LYS A CA  
2838 C C   . LYS A 336 ? 0.3770 0.3979 0.3405 -0.0509 0.0184  0.0416  336 LYS A C   
2839 O O   . LYS A 336 ? 0.4376 0.4659 0.3987 -0.0555 0.0209  0.0406  336 LYS A O   
2840 C CB  . LYS A 336 ? 0.3740 0.3775 0.3398 -0.0510 0.0155  0.0499  336 LYS A CB  
2841 C CG  . LYS A 336 ? 0.6002 0.6083 0.5666 -0.0556 0.0180  0.0478  336 LYS A CG  
2842 C CD  . LYS A 336 ? 0.7238 0.7262 0.6946 -0.0545 0.0182  0.0455  336 LYS A CD  
2843 C CE  . LYS A 336 ? 0.7741 0.7853 0.7476 -0.0565 0.0205  0.0405  336 LYS A CE  
2844 N NZ  . LYS A 336 ? 0.8097 0.8175 0.7878 -0.0540 0.0199  0.0370  336 LYS A NZ  
2845 N N   . ILE A 337 ? 0.3653 0.3861 0.3331 -0.0457 0.0180  0.0367  337 ILE A N   
2846 C CA  . ILE A 337 ? 0.3050 0.3343 0.2755 -0.0446 0.0202  0.0302  337 ILE A CA  
2847 C C   . ILE A 337 ? 0.3695 0.4052 0.3353 -0.0461 0.0217  0.0287  337 ILE A C   
2848 O O   . ILE A 337 ? 0.3780 0.4224 0.3439 -0.0487 0.0250  0.0250  337 ILE A O   
2849 C CB  . ILE A 337 ? 0.2969 0.3238 0.2729 -0.0389 0.0186  0.0264  337 ILE A CB  
2850 C CG1 . ILE A 337 ? 0.3358 0.3573 0.3155 -0.0388 0.0176  0.0272  337 ILE A CG1 
2851 C CG2 . ILE A 337 ? 0.3032 0.3382 0.2832 -0.0370 0.0203  0.0201  337 ILE A CG2 
2852 C CD1 . ILE A 337 ? 0.3313 0.3488 0.3145 -0.0341 0.0153  0.0250  337 ILE A CD1 
2853 N N   . HIS A 338 ? 0.3452 0.3772 0.3067 -0.0450 0.0195  0.0314  338 HIS A N   
2854 C CA  . HIS A 338 ? 0.3570 0.3944 0.3127 -0.0470 0.0206  0.0299  338 HIS A CA  
2855 C C   . HIS A 338 ? 0.4129 0.4564 0.3632 -0.0542 0.0231  0.0320  338 HIS A C   
2856 O O   . HIS A 338 ? 0.3630 0.4143 0.3102 -0.0568 0.0263  0.0276  338 HIS A O   
2857 C CB  . HIS A 338 ? 0.3751 0.4072 0.3268 -0.0457 0.0171  0.0341  338 HIS A CB  
2858 C CG  . HIS A 338 ? 0.4064 0.4434 0.3510 -0.0485 0.0179  0.0329  338 HIS A CG  
2859 N ND1 . HIS A 338 ? 0.4393 0.4772 0.3766 -0.0538 0.0166  0.0389  338 HIS A ND1 
2860 C CD2 . HIS A 338 ? 0.4013 0.4422 0.3449 -0.0472 0.0197  0.0263  338 HIS A CD2 
2861 C CE1 . HIS A 338 ? 0.4191 0.4615 0.3503 -0.0561 0.0177  0.0358  338 HIS A CE1 
2862 N NE2 . HIS A 338 ? 0.4351 0.4791 0.3701 -0.0520 0.0198  0.0278  338 HIS A NE2 
2863 N N   . GLU A 339 ? 0.3937 0.4334 0.3424 -0.0578 0.0218  0.0385  339 GLU A N   
2864 C CA  . GLU A 339 ? 0.4363 0.4812 0.3789 -0.0655 0.0234  0.0419  339 GLU A CA  
2865 C C   . GLU A 339 ? 0.4150 0.4668 0.3605 -0.0684 0.0273  0.0381  339 GLU A C   
2866 O O   . GLU A 339 ? 0.4121 0.4711 0.3525 -0.0752 0.0298  0.0387  339 GLU A O   
2867 C CB  . GLU A 339 ? 0.4486 0.4859 0.3889 -0.0682 0.0198  0.0513  339 GLU A CB  
2868 C CG  . GLU A 339 ? 0.5124 0.5438 0.4507 -0.0659 0.0156  0.0564  339 GLU A CG  
2869 C CD  . GLU A 339 ? 0.6522 0.6743 0.5927 -0.0658 0.0121  0.0648  339 GLU A CD  
2870 O OE1 . GLU A 339 ? 0.7164 0.7347 0.6557 -0.0649 0.0085  0.0706  339 GLU A OE1 
2871 O OE2 . GLU A 339 ? 0.6959 0.7142 0.6396 -0.0667 0.0128  0.0656  339 GLU A OE2 
2872 N N   . SER A 340 ? 0.4325 0.4831 0.3859 -0.0642 0.0278  0.0345  340 SER A N   
2873 C CA  . SER A 340 ? 0.4370 0.4937 0.3940 -0.0673 0.0307  0.0322  340 SER A CA  
2874 C C   . SER A 340 ? 0.4634 0.5316 0.4242 -0.0663 0.0350  0.0241  340 SER A C   
2875 O O   . SER A 340 ? 0.4332 0.5092 0.3974 -0.0694 0.0380  0.0220  340 SER A O   
2876 C CB  . SER A 340 ? 0.4654 0.5155 0.4289 -0.0641 0.0289  0.0328  340 SER A CB  
2877 O OG  . SER A 340 ? 0.4807 0.5331 0.4514 -0.0583 0.0292  0.0267  340 SER A OG  
2878 N N   . VAL A 341 ? 0.5197 0.5891 0.4807 -0.0622 0.0355  0.0196  341 VAL A N   
2879 C CA  . VAL A 341 ? 0.5103 0.5897 0.4759 -0.0607 0.0398  0.0115  341 VAL A CA  
2880 C C   . VAL A 341 ? 0.5187 0.6011 0.4770 -0.0626 0.0417  0.0090  341 VAL A C   
2881 O O   . VAL A 341 ? 0.4369 0.5126 0.3888 -0.0624 0.0386  0.0125  341 VAL A O   
2882 C CB  . VAL A 341 ? 0.4901 0.5678 0.4657 -0.0529 0.0385  0.0068  341 VAL A CB  
2883 C CG1 . VAL A 341 ? 0.5213 0.5992 0.5042 -0.0525 0.0376  0.0082  341 VAL A CG1 
2884 C CG2 . VAL A 341 ? 0.4126 0.4800 0.3863 -0.0481 0.0341  0.0088  341 VAL A CG2 
2885 N N   . ASP A 342 ? 0.5303 0.6234 0.4897 -0.0649 0.0471  0.0026  342 ASP A N   
2886 C CA  . ASP A 342 ? 0.5695 0.6669 0.5218 -0.0677 0.0502  -0.0015 342 ASP A CA  
2887 C C   . ASP A 342 ? 0.5541 0.6488 0.5107 -0.0607 0.0503  -0.0080 342 ASP A C   
2888 O O   . ASP A 342 ? 0.6019 0.6959 0.5513 -0.0622 0.0511  -0.0103 342 ASP A O   
2889 C CB  . ASP A 342 ? 0.7059 0.8164 0.6583 -0.0731 0.0568  -0.0066 342 ASP A CB  
2890 C CG  . ASP A 342 ? 0.7849 0.9020 0.7511 -0.0679 0.0598  -0.0130 342 ASP A CG  
2891 O OD1 . ASP A 342 ? 0.8247 0.9429 0.7971 -0.0622 0.0617  -0.0202 342 ASP A OD1 
2892 O OD2 . ASP A 342 ? 0.7866 0.9067 0.7582 -0.0691 0.0595  -0.0103 342 ASP A OD2 
2893 N N   . PHE A 343 ? 0.4762 0.5698 0.4445 -0.0536 0.0494  -0.0111 343 PHE A N   
2894 C CA  . PHE A 343 ? 0.3726 0.4628 0.3462 -0.0467 0.0488  -0.0167 343 PHE A CA  
2895 C C   . PHE A 343 ? 0.3267 0.4051 0.2986 -0.0429 0.0423  -0.0115 343 PHE A C   
2896 O O   . PHE A 343 ? 0.3481 0.4213 0.3150 -0.0452 0.0389  -0.0041 343 PHE A O   
2897 C CB  . PHE A 343 ? 0.3790 0.4749 0.3668 -0.0415 0.0508  -0.0222 343 PHE A CB  
2898 C CG  . PHE A 343 ? 0.4036 0.4986 0.3982 -0.0404 0.0477  -0.0175 343 PHE A CG  
2899 C CD1 . PHE A 343 ? 0.4123 0.5144 0.4071 -0.0456 0.0500  -0.0153 343 PHE A CD1 
2900 C CD2 . PHE A 343 ? 0.4119 0.4992 0.4119 -0.0348 0.0426  -0.0153 343 PHE A CD2 
2901 C CE1 . PHE A 343 ? 0.3787 0.4797 0.3790 -0.0453 0.0473  -0.0112 343 PHE A CE1 
2902 C CE2 . PHE A 343 ? 0.4032 0.4897 0.4084 -0.0347 0.0399  -0.0114 343 PHE A CE2 
2903 C CZ  . PHE A 343 ? 0.3710 0.4641 0.3764 -0.0399 0.0423  -0.0094 343 PHE A CZ  
2904 N N   . GLN A 344 ? 0.2854 0.3596 0.2616 -0.0369 0.0408  -0.0154 344 GLN A N   
2905 C CA  . GLN A 344 ? 0.2756 0.3396 0.2500 -0.0336 0.0350  -0.0111 344 GLN A CA  
2906 C C   . GLN A 344 ? 0.2979 0.3592 0.2822 -0.0288 0.0319  -0.0098 344 GLN A C   
2907 O O   . GLN A 344 ? 0.2789 0.3412 0.2718 -0.0240 0.0318  -0.0143 344 GLN A O   
2908 C CB  . GLN A 344 ? 0.3403 0.4005 0.3121 -0.0310 0.0345  -0.0154 344 GLN A CB  
2909 C CG  . GLN A 344 ? 0.3612 0.4243 0.3221 -0.0367 0.0377  -0.0170 344 GLN A CG  
2910 C CD  . GLN A 344 ? 0.3952 0.4528 0.3513 -0.0352 0.0362  -0.0198 344 GLN A CD  
2911 O OE1 . GLN A 344 ? 0.4206 0.4742 0.3675 -0.0381 0.0332  -0.0150 344 GLN A OE1 
2912 N NE2 . GLN A 344 ? 0.4072 0.4645 0.3701 -0.0306 0.0380  -0.0272 344 GLN A NE2 
2913 N N   . PRO A 345 ? 0.3452 0.4030 0.3286 -0.0302 0.0292  -0.0036 345 PRO A N   
2914 C CA  . PRO A 345 ? 0.2773 0.3332 0.2691 -0.0269 0.0266  -0.0026 345 PRO A CA  
2915 C C   . PRO A 345 ? 0.3079 0.3564 0.3016 -0.0221 0.0221  -0.0025 345 PRO A C   
2916 O O   . PRO A 345 ? 0.3627 0.4054 0.3498 -0.0219 0.0200  -0.0005 345 PRO A O   
2917 C CB  . PRO A 345 ? 0.2340 0.2869 0.2222 -0.0307 0.0254  0.0037  345 PRO A CB  
2918 C CG  . PRO A 345 ? 0.3425 0.3915 0.3207 -0.0335 0.0248  0.0075  345 PRO A CG  
2919 C CD  . PRO A 345 ? 0.3836 0.4384 0.3584 -0.0349 0.0282  0.0029  345 PRO A CD  
2920 N N   . VAL A 346 ? 0.2655 0.3149 0.2683 -0.0186 0.0205  -0.0044 346 VAL A N   
2921 C CA  . VAL A 346 ? 0.3219 0.3646 0.3267 -0.0149 0.0158  -0.0034 346 VAL A CA  
2922 C C   . VAL A 346 ? 0.2794 0.3187 0.2850 -0.0161 0.0131  0.0010  346 VAL A C   
2923 O O   . VAL A 346 ? 0.2485 0.2921 0.2599 -0.0171 0.0137  0.0009  346 VAL A O   
2924 C CB  . VAL A 346 ? 0.2831 0.3284 0.2974 -0.0106 0.0149  -0.0079 346 VAL A CB  
2925 C CG1 . VAL A 346 ? 0.3296 0.3677 0.3447 -0.0078 0.0096  -0.0062 346 VAL A CG1 
2926 C CG2 . VAL A 346 ? 0.2265 0.2747 0.2404 -0.0095 0.0185  -0.0135 346 VAL A CG2 
2927 N N   . VAL A 347 ? 0.2300 0.2620 0.2300 -0.0162 0.0105  0.0045  347 VAL A N   
2928 C CA  . VAL A 347 ? 0.2931 0.3210 0.2927 -0.0178 0.0088  0.0081  347 VAL A CA  
2929 C C   . VAL A 347 ? 0.3098 0.3331 0.3113 -0.0153 0.0047  0.0083  347 VAL A C   
2930 O O   . VAL A 347 ? 0.2476 0.2664 0.2451 -0.0138 0.0029  0.0091  347 VAL A O   
2931 C CB  . VAL A 347 ? 0.2862 0.3095 0.2786 -0.0202 0.0096  0.0123  347 VAL A CB  
2932 C CG1 . VAL A 347 ? 0.2821 0.3005 0.2748 -0.0216 0.0085  0.0150  347 VAL A CG1 
2933 C CG2 . VAL A 347 ? 0.2377 0.2658 0.2273 -0.0235 0.0132  0.0127  347 VAL A CG2 
2934 N N   . PHE A 348 ? 0.2873 0.3122 0.2944 -0.0157 0.0032  0.0080  348 PHE A N   
2935 C CA  . PHE A 348 ? 0.3231 0.3448 0.3321 -0.0143 -0.0010 0.0082  348 PHE A CA  
2936 C C   . PHE A 348 ? 0.2884 0.3052 0.2940 -0.0170 -0.0018 0.0108  348 PHE A C   
2937 O O   . PHE A 348 ? 0.1953 0.2132 0.2020 -0.0200 -0.0006 0.0115  348 PHE A O   
2938 C CB  . PHE A 348 ? 0.3668 0.3939 0.3846 -0.0133 -0.0028 0.0065  348 PHE A CB  
2939 C CG  . PHE A 348 ? 0.3215 0.3492 0.3432 -0.0094 -0.0047 0.0042  348 PHE A CG  
2940 C CD1 . PHE A 348 ? 0.2848 0.3157 0.3076 -0.0074 -0.0016 0.0010  348 PHE A CD1 
2941 C CD2 . PHE A 348 ? 0.2539 0.2789 0.2781 -0.0082 -0.0096 0.0049  348 PHE A CD2 
2942 C CE1 . PHE A 348 ? 0.3539 0.3842 0.3804 -0.0039 -0.0030 -0.0017 348 PHE A CE1 
2943 C CE2 . PHE A 348 ? 0.4064 0.4309 0.4346 -0.0047 -0.0116 0.0029  348 PHE A CE2 
2944 C CZ  . PHE A 348 ? 0.4414 0.4682 0.4710 -0.0023 -0.0082 -0.0006 348 PHE A CZ  
2945 N N   . VAL A 349 ? 0.2461 0.2574 0.2475 -0.0161 -0.0036 0.0119  349 VAL A N   
2946 C CA  . VAL A 349 ? 0.2772 0.2836 0.2757 -0.0183 -0.0041 0.0134  349 VAL A CA  
2947 C C   . VAL A 349 ? 0.3101 0.3161 0.3102 -0.0185 -0.0080 0.0129  349 VAL A C   
2948 O O   . VAL A 349 ? 0.2741 0.2788 0.2730 -0.0164 -0.0104 0.0128  349 VAL A O   
2949 C CB  . VAL A 349 ? 0.2282 0.2298 0.2216 -0.0173 -0.0028 0.0152  349 VAL A CB  
2950 C CG1 . VAL A 349 ? 0.2368 0.2334 0.2283 -0.0191 -0.0025 0.0159  349 VAL A CG1 
2951 C CG2 . VAL A 349 ? 0.2798 0.2821 0.2715 -0.0177 0.0003  0.0165  349 VAL A CG2 
2952 N N   . VAL A 350 ? 0.1988 0.2064 0.2013 -0.0215 -0.0091 0.0128  350 VAL A N   
2953 C CA  . VAL A 350 ? 0.2117 0.2201 0.2160 -0.0227 -0.0135 0.0130  350 VAL A CA  
2954 C C   . VAL A 350 ? 0.2438 0.2495 0.2448 -0.0273 -0.0133 0.0133  350 VAL A C   
2955 O O   . VAL A 350 ? 0.2159 0.2228 0.2177 -0.0304 -0.0116 0.0132  350 VAL A O   
2956 C CB  . VAL A 350 ? 0.1761 0.1907 0.1881 -0.0222 -0.0159 0.0128  350 VAL A CB  
2957 C CG1 . VAL A 350 ? 0.1584 0.1734 0.1722 -0.0238 -0.0213 0.0140  350 VAL A CG1 
2958 C CG2 . VAL A 350 ? 0.2095 0.2267 0.2252 -0.0175 -0.0150 0.0114  350 VAL A CG2 
2959 N N   . LEU A 351 ? 0.2973 0.2997 0.2944 -0.0283 -0.0150 0.0134  351 LEU A N   
2960 C CA  . LEU A 351 ? 0.3320 0.3319 0.3252 -0.0333 -0.0146 0.0128  351 LEU A CA  
2961 C C   . LEU A 351 ? 0.2860 0.2850 0.2763 -0.0345 -0.0180 0.0131  351 LEU A C   
2962 O O   . LEU A 351 ? 0.2661 0.2654 0.2571 -0.0312 -0.0203 0.0139  351 LEU A O   
2963 C CB  . LEU A 351 ? 0.2954 0.2902 0.2851 -0.0335 -0.0095 0.0119  351 LEU A CB  
2964 C CG  . LEU A 351 ? 0.2972 0.2886 0.2848 -0.0296 -0.0078 0.0121  351 LEU A CG  
2965 C CD1 . LEU A 351 ? 0.3248 0.3110 0.3092 -0.0314 -0.0042 0.0108  351 LEU A CD1 
2966 C CD2 . LEU A 351 ? 0.2277 0.2197 0.2170 -0.0256 -0.0061 0.0134  351 LEU A CD2 
2967 N N   . ASN A 352 ? 0.2005 0.1983 0.1870 -0.0398 -0.0181 0.0123  352 ASN A N   
2968 C CA  . ASN A 352 ? 0.2105 0.2077 0.1932 -0.0419 -0.0206 0.0124  352 ASN A CA  
2969 C C   . ASN A 352 ? 0.2478 0.2419 0.2283 -0.0380 -0.0179 0.0117  352 ASN A C   
2970 O O   . ASN A 352 ? 0.2478 0.2389 0.2281 -0.0358 -0.0133 0.0107  352 ASN A O   
2971 C CB  . ASN A 352 ? 0.2493 0.2457 0.2271 -0.0489 -0.0198 0.0108  352 ASN A CB  
2972 C CG  . ASN A 352 ? 0.3488 0.3496 0.3276 -0.0540 -0.0252 0.0128  352 ASN A CG  
2973 O OD1 . ASN A 352 ? 0.3321 0.3353 0.3139 -0.0558 -0.0258 0.0134  352 ASN A OD1 
2974 N ND2 . ASN A 352 ? 0.4088 0.4111 0.3852 -0.0566 -0.0298 0.0142  352 ASN A ND2 
2975 N N   . GLY A 353 ? 0.2554 0.2503 0.2345 -0.0374 -0.0213 0.0128  353 GLY A N   
2976 C CA  . GLY A 353 ? 0.2164 0.2096 0.1939 -0.0340 -0.0196 0.0128  353 GLY A CA  
2977 C C   . GLY A 353 ? 0.2108 0.2031 0.1840 -0.0369 -0.0177 0.0112  353 GLY A C   
2978 O O   . GLY A 353 ? 0.2595 0.2513 0.2321 -0.0342 -0.0162 0.0114  353 GLY A O   
2979 N N   . GLU A 354 ? 0.2121 0.2048 0.1823 -0.0429 -0.0175 0.0097  354 GLU A N   
2980 C CA  . GLU A 354 ? 0.2643 0.2571 0.2301 -0.0465 -0.0156 0.0076  354 GLU A CA  
2981 C C   . GLU A 354 ? 0.2544 0.2448 0.2181 -0.0502 -0.0102 0.0038  354 GLU A C   
2982 O O   . GLU A 354 ? 0.2300 0.2203 0.1907 -0.0527 -0.0072 0.0011  354 GLU A O   
2983 C CB  . GLU A 354 ? 0.2341 0.2302 0.1963 -0.0518 -0.0212 0.0091  354 GLU A CB  
2984 C CG  . GLU A 354 ? 0.1812 0.1787 0.1410 -0.0589 -0.0236 0.0089  354 GLU A CG  
2985 C CD  . GLU A 354 ? 0.3512 0.3500 0.3159 -0.0575 -0.0283 0.0121  354 GLU A CD  
2986 O OE1 . GLU A 354 ? 0.3157 0.3172 0.2804 -0.0608 -0.0346 0.0151  354 GLU A OE1 
2987 O OE2 . GLU A 354 ? 0.3064 0.3040 0.2754 -0.0531 -0.0258 0.0117  354 GLU A OE2 
2988 N N   . ASN A 355 ? 0.2558 0.2441 0.2210 -0.0509 -0.0086 0.0031  355 ASN A N   
2989 C CA  . ASN A 355 ? 0.3068 0.2923 0.2687 -0.0561 -0.0043 -0.0007 355 ASN A CA  
2990 C C   . ASN A 355 ? 0.3430 0.3229 0.3073 -0.0525 0.0023  -0.0031 355 ASN A C   
2991 O O   . ASN A 355 ? 0.2726 0.2492 0.2344 -0.0560 0.0070  -0.0073 355 ASN A O   
2992 C CB  . ASN A 355 ? 0.2876 0.2744 0.2487 -0.0611 -0.0070 0.0001  355 ASN A CB  
2993 C CG  . ASN A 355 ? 0.2906 0.2825 0.2487 -0.0669 -0.0132 0.0021  355 ASN A CG  
2994 O OD1 . ASN A 355 ? 0.3048 0.2982 0.2588 -0.0699 -0.0140 0.0013  355 ASN A OD1 
2995 N ND2 . ASN A 355 ? 0.2864 0.2813 0.2470 -0.0685 -0.0178 0.0050  355 ASN A ND2 
2996 N N   . CYS A 356 ? 0.2993 0.2779 0.2685 -0.0459 0.0027  -0.0007 356 CYS A N   
2997 C CA  . CYS A 356 ? 0.3003 0.2731 0.2721 -0.0429 0.0081  -0.0020 356 CYS A CA  
2998 C C   . CYS A 356 ? 0.3235 0.2949 0.2976 -0.0389 0.0115  -0.0029 356 CYS A C   
2999 O O   . CYS A 356 ? 0.2731 0.2392 0.2495 -0.0375 0.0166  -0.0051 356 CYS A O   
3000 C CB  . CYS A 356 ? 0.2808 0.2530 0.2563 -0.0387 0.0071  0.0014  356 CYS A CB  
3001 S SG  . CYS A 356 ? 0.2444 0.2217 0.2225 -0.0331 0.0026  0.0057  356 CYS A SG  
3002 N N   . TRP A 357 ? 0.2615 0.2376 0.2356 -0.0371 0.0088  -0.0013 357 TRP A N   
3003 C CA  . TRP A 357 ? 0.2599 0.2361 0.2377 -0.0323 0.0114  -0.0009 357 TRP A CA  
3004 C C   . TRP A 357 ? 0.2469 0.2213 0.2248 -0.0343 0.0169  -0.0058 357 TRP A C   
3005 O O   . TRP A 357 ? 0.2406 0.2128 0.2238 -0.0299 0.0208  -0.0061 357 TRP A O   
3006 C CB  . TRP A 357 ? 0.2569 0.2389 0.2341 -0.0307 0.0068  0.0022  357 TRP A CB  
3007 C CG  . TRP A 357 ? 0.2938 0.2772 0.2706 -0.0293 0.0018  0.0058  357 TRP A CG  
3008 C CD1 . TRP A 357 ? 0.2793 0.2660 0.2533 -0.0317 -0.0035 0.0070  357 TRP A CD1 
3009 C CD2 . TRP A 357 ? 0.2323 0.2138 0.2122 -0.0253 0.0019  0.0084  357 TRP A CD2 
3010 N NE1 . TRP A 357 ? 0.2717 0.2586 0.2474 -0.0289 -0.0061 0.0096  357 TRP A NE1 
3011 C CE2 . TRP A 357 ? 0.2708 0.2550 0.2496 -0.0253 -0.0028 0.0104  357 TRP A CE2 
3012 C CE3 . TRP A 357 ? 0.2592 0.2370 0.2428 -0.0219 0.0054  0.0094  357 TRP A CE3 
3013 C CZ2 . TRP A 357 ? 0.2470 0.2310 0.2279 -0.0223 -0.0034 0.0126  357 TRP A CZ2 
3014 C CZ3 . TRP A 357 ? 0.2956 0.2732 0.2806 -0.0195 0.0041  0.0124  357 TRP A CZ3 
3015 C CH2 . TRP A 357 ? 0.3072 0.2881 0.2904 -0.0199 0.0001  0.0136  357 TRP A CH2 
3016 N N   . GLU A 358 ? 0.2577 0.2330 0.2300 -0.0411 0.0174  -0.0096 358 GLU A N   
3017 C CA  . GLU A 358 ? 0.2634 0.2375 0.2351 -0.0438 0.0233  -0.0153 358 GLU A CA  
3018 C C   . GLU A 358 ? 0.3035 0.2696 0.2788 -0.0423 0.0296  -0.0187 358 GLU A C   
3019 O O   . GLU A 358 ? 0.3381 0.3024 0.3153 -0.0424 0.0354  -0.0235 358 GLU A O   
3020 C CB  . GLU A 358 ? 0.2285 0.2054 0.1920 -0.0529 0.0222  -0.0186 358 GLU A CB  
3021 C CG  . GLU A 358 ? 0.2121 0.1860 0.1714 -0.0580 0.0205  -0.0189 358 GLU A CG  
3022 C CD  . GLU A 358 ? 0.3895 0.3687 0.3413 -0.0663 0.0158  -0.0187 358 GLU A CD  
3023 O OE1 . GLU A 358 ? 0.4205 0.3987 0.3666 -0.0740 0.0183  -0.0231 358 GLU A OE1 
3024 O OE2 . GLU A 358 ? 0.3610 0.3452 0.3128 -0.0654 0.0095  -0.0140 358 GLU A OE2 
3025 N N   . TYR A 359 ? 0.2558 0.2171 0.2322 -0.0410 0.0287  -0.0165 359 TYR A N   
3026 C CA  . TYR A 359 ? 0.3880 0.3407 0.3681 -0.0393 0.0340  -0.0188 359 TYR A CA  
3027 C C   . TYR A 359 ? 0.3727 0.3230 0.3612 -0.0310 0.0345  -0.0144 359 TYR A C   
3028 O O   . TYR A 359 ? 0.2988 0.2415 0.2917 -0.0288 0.0388  -0.0157 359 TYR A O   
3029 C CB  . TYR A 359 ? 0.3351 0.2837 0.3110 -0.0439 0.0329  -0.0188 359 TYR A CB  
3030 C CG  . TYR A 359 ? 0.3981 0.3495 0.3659 -0.0527 0.0317  -0.0223 359 TYR A CG  
3031 C CD1 . TYR A 359 ? 0.4064 0.3538 0.3704 -0.0583 0.0371  -0.0291 359 TYR A CD1 
3032 C CD2 . TYR A 359 ? 0.4154 0.3734 0.3794 -0.0557 0.0252  -0.0188 359 TYR A CD2 
3033 C CE1 . TYR A 359 ? 0.4519 0.4023 0.4075 -0.0674 0.0358  -0.0319 359 TYR A CE1 
3034 C CE2 . TYR A 359 ? 0.4977 0.4588 0.4547 -0.0641 0.0234  -0.0210 359 TYR A CE2 
3035 C CZ  . TYR A 359 ? 0.5180 0.4754 0.4702 -0.0703 0.0285  -0.0274 359 TYR A CZ  
3036 O OH  . TYR A 359 ? 0.5927 0.5537 0.5372 -0.0797 0.0263  -0.0291 359 TYR A OH  
3037 N N   . TYR A 360 ? 0.3188 0.2751 0.3093 -0.0269 0.0301  -0.0092 360 TYR A N   
3038 C CA  . TYR A 360 ? 0.2659 0.2213 0.2639 -0.0199 0.0302  -0.0047 360 TYR A CA  
3039 C C   . TYR A 360 ? 0.3031 0.2607 0.3068 -0.0166 0.0336  -0.0064 360 TYR A C   
3040 O O   . TYR A 360 ? 0.2697 0.2325 0.2705 -0.0194 0.0340  -0.0096 360 TYR A O   
3041 C CB  . TYR A 360 ? 0.2889 0.2502 0.2861 -0.0175 0.0242  0.0013  360 TYR A CB  
3042 C CG  . TYR A 360 ? 0.2274 0.1877 0.2219 -0.0185 0.0209  0.0044  360 TYR A CG  
3043 C CD1 . TYR A 360 ? 0.2830 0.2446 0.2717 -0.0235 0.0187  0.0026  360 TYR A CD1 
3044 C CD2 . TYR A 360 ? 0.2663 0.2257 0.2642 -0.0145 0.0195  0.0094  360 TYR A CD2 
3045 C CE1 . TYR A 360 ? 0.2432 0.2053 0.2307 -0.0240 0.0159  0.0053  360 TYR A CE1 
3046 C CE2 . TYR A 360 ? 0.3052 0.2649 0.3007 -0.0156 0.0169  0.0119  360 TYR A CE2 
3047 C CZ  . TYR A 360 ? 0.2614 0.2226 0.2522 -0.0200 0.0154  0.0096  360 TYR A CZ  
3048 O OH  . TYR A 360 ? 0.2622 0.2246 0.2518 -0.0208 0.0133  0.0119  360 TYR A OH  
3049 N N   . GLU A 361 ? 0.3687 0.3231 0.3810 -0.0107 0.0356  -0.0037 361 GLU A N   
3050 C CA  . GLU A 361 ? 0.4083 0.3666 0.4281 -0.0065 0.0381  -0.0040 361 GLU A CA  
3051 C C   . GLU A 361 ? 0.3170 0.2853 0.3347 -0.0061 0.0332  -0.0003 361 GLU A C   
3052 O O   . GLU A 361 ? 0.2717 0.2422 0.2866 -0.0054 0.0279  0.0050  361 GLU A O   
3053 C CB  . GLU A 361 ? 0.5032 0.4570 0.5337 0.0001  0.0397  0.0001  361 GLU A CB  
3054 C CG  . GLU A 361 ? 0.6969 0.6397 0.7291 0.0000  0.0425  -0.0009 361 GLU A CG  
3055 C CD  . GLU A 361 ? 0.8414 0.7822 0.8693 -0.0009 0.0377  0.0048  361 GLU A CD  
3056 O OE1 . GLU A 361 ? 0.7922 0.7355 0.8112 -0.0057 0.0349  0.0038  361 GLU A OE1 
3057 O OE2 . GLU A 361 ? 0.9018 0.8391 0.9357 0.0030  0.0366  0.0103  361 GLU A OE2 
3058 N N   . GLU A 362 ? 0.3198 0.2939 0.3386 -0.0068 0.0352  -0.0035 362 GLU A N   
3059 C CA  . GLU A 362 ? 0.4060 0.3894 0.4231 -0.0068 0.0310  -0.0004 362 GLU A CA  
3060 C C   . GLU A 362 ? 0.3027 0.2879 0.3098 -0.0112 0.0251  0.0014  362 GLU A C   
3061 O O   . GLU A 362 ? 0.2783 0.2676 0.2840 -0.0099 0.0200  0.0063  362 GLU A O   
3062 C CB  . GLU A 362 ? 0.5103 0.4968 0.5354 -0.0005 0.0290  0.0062  362 GLU A CB  
3063 C CG  . GLU A 362 ? 0.6580 0.6440 0.6951 0.0046  0.0343  0.0053  362 GLU A CG  
3064 C CD  . GLU A 362 ? 0.7871 0.7827 0.8282 0.0052  0.0355  0.0044  362 GLU A CD  
3065 O OE1 . GLU A 362 ? 0.8265 0.8227 0.8709 0.0044  0.0415  -0.0020 362 GLU A OE1 
3066 O OE2 . GLU A 362 ? 0.8571 0.8598 0.8976 0.0060  0.0305  0.0097  362 GLU A OE2 
3067 N N   . ASN A 363 ? 0.2955 0.2773 0.2960 -0.0166 0.0257  -0.0027 363 ASN A N   
3068 C CA  . ASN A 363 ? 0.2882 0.2723 0.2804 -0.0212 0.0203  -0.0017 363 ASN A CA  
3069 C C   . ASN A 363 ? 0.3037 0.2870 0.2957 -0.0184 0.0155  0.0038  363 ASN A C   
3070 O O   . ASN A 363 ? 0.3169 0.3038 0.3048 -0.0196 0.0104  0.0062  363 ASN A O   
3071 C CB  . ASN A 363 ? 0.2911 0.2826 0.2797 -0.0241 0.0177  -0.0019 363 ASN A CB  
3072 C CG  . ASN A 363 ? 0.3142 0.3071 0.2947 -0.0296 0.0126  -0.0016 363 ASN A CG  
3073 O OD1 . ASN A 363 ? 0.3348 0.3242 0.3118 -0.0334 0.0128  -0.0037 363 ASN A OD1 
3074 N ND2 . ASN A 363 ? 0.2832 0.2812 0.2611 -0.0303 0.0076  0.0014  363 ASN A ND2 
3075 N N   . GLY A 364 ? 0.2914 0.2696 0.2878 -0.0148 0.0173  0.0056  364 GLY A N   
3076 C CA  . GLY A 364 ? 0.2751 0.2526 0.2711 -0.0128 0.0137  0.0102  364 GLY A CA  
3077 C C   . GLY A 364 ? 0.2624 0.2446 0.2603 -0.0092 0.0105  0.0152  364 GLY A C   
3078 O O   . GLY A 364 ? 0.2823 0.2645 0.2790 -0.0081 0.0076  0.0187  364 GLY A O   
3079 N N   . ILE A 365 ? 0.2511 0.2376 0.2520 -0.0077 0.0111  0.0155  365 ILE A N   
3080 C CA  . ILE A 365 ? 0.2380 0.2297 0.2394 -0.0054 0.0074  0.0202  365 ILE A CA  
3081 C C   . ILE A 365 ? 0.3168 0.3070 0.3236 -0.0012 0.0075  0.0252  365 ILE A C   
3082 O O   . ILE A 365 ? 0.2954 0.2872 0.2996 -0.0008 0.0038  0.0291  365 ILE A O   
3083 C CB  . ILE A 365 ? 0.2896 0.2874 0.2927 -0.0057 0.0079  0.0192  365 ILE A CB  
3084 C CG1 . ILE A 365 ? 0.2721 0.2722 0.2677 -0.0109 0.0055  0.0162  365 ILE A CG1 
3085 C CG2 . ILE A 365 ? 0.2584 0.2616 0.2641 -0.0029 0.0050  0.0246  365 ILE A CG2 
3086 C CD1 . ILE A 365 ? 0.2852 0.2899 0.2813 -0.0132 0.0079  0.0129  365 ILE A CD1 
3087 N N   . PRO A 366 ? 0.3176 0.3043 0.3318 0.0016  0.0115  0.0252  366 PRO A N   
3088 C CA  . PRO A 366 ? 0.2699 0.2547 0.2888 0.0050  0.0107  0.0310  366 PRO A CA  
3089 C C   . PRO A 366 ? 0.2941 0.2753 0.3078 0.0032  0.0088  0.0325  366 PRO A C   
3090 O O   . PRO A 366 ? 0.2571 0.2402 0.2699 0.0039  0.0057  0.0376  366 PRO A O   
3091 C CB  . PRO A 366 ? 0.3245 0.3044 0.3524 0.0079  0.0157  0.0296  366 PRO A CB  
3092 C CG  . PRO A 366 ? 0.3224 0.3054 0.3516 0.0072  0.0187  0.0244  366 PRO A CG  
3093 C CD  . PRO A 366 ? 0.3214 0.3061 0.3406 0.0021  0.0168  0.0206  366 PRO A CD  
3094 N N   . PHE A 367 ? 0.3261 0.3029 0.3360 0.0003  0.0104  0.0281  367 PHE A N   
3095 C CA  . PHE A 367 ? 0.3558 0.3303 0.3615 -0.0015 0.0090  0.0292  367 PHE A CA  
3096 C C   . PHE A 367 ? 0.2785 0.2583 0.2785 -0.0028 0.0046  0.0307  367 PHE A C   
3097 O O   . PHE A 367 ? 0.2920 0.2728 0.2908 -0.0024 0.0028  0.0345  367 PHE A O   
3098 C CB  . PHE A 367 ? 0.3710 0.3409 0.3739 -0.0048 0.0113  0.0242  367 PHE A CB  
3099 C CG  . PHE A 367 ? 0.3433 0.3128 0.3421 -0.0071 0.0096  0.0249  367 PHE A CG  
3100 C CD1 . PHE A 367 ? 0.2981 0.2640 0.2983 -0.0067 0.0103  0.0281  367 PHE A CD1 
3101 C CD2 . PHE A 367 ? 0.2651 0.2381 0.2589 -0.0098 0.0072  0.0226  367 PHE A CD2 
3102 C CE1 . PHE A 367 ? 0.3513 0.3180 0.3479 -0.0092 0.0092  0.0284  367 PHE A CE1 
3103 C CE2 . PHE A 367 ? 0.2571 0.2307 0.2485 -0.0115 0.0060  0.0229  367 PHE A CE2 
3104 C CZ  . PHE A 367 ? 0.2798 0.2507 0.2724 -0.0113 0.0072  0.0256  367 PHE A CZ  
3105 N N   . LEU A 368 ? 0.2175 0.2005 0.2139 -0.0045 0.0030  0.0277  368 LEU A N   
3106 C CA  . LEU A 368 ? 0.2558 0.2425 0.2472 -0.0056 -0.0009 0.0284  368 LEU A CA  
3107 C C   . LEU A 368 ? 0.2724 0.2630 0.2638 -0.0039 -0.0033 0.0328  368 LEU A C   
3108 O O   . LEU A 368 ? 0.2371 0.2293 0.2251 -0.0044 -0.0056 0.0344  368 LEU A O   
3109 C CB  . LEU A 368 ? 0.2582 0.2467 0.2463 -0.0081 -0.0025 0.0248  368 LEU A CB  
3110 C CG  . LEU A 368 ? 0.2644 0.2505 0.2506 -0.0111 -0.0020 0.0211  368 LEU A CG  
3111 C CD1 . LEU A 368 ? 0.2351 0.2235 0.2178 -0.0139 -0.0048 0.0189  368 LEU A CD1 
3112 C CD2 . LEU A 368 ? 0.2613 0.2465 0.2467 -0.0112 -0.0025 0.0218  368 LEU A CD2 
3113 N N   . GLU A 369 ? 0.2890 0.2818 0.2845 -0.0020 -0.0028 0.0346  369 GLU A N   
3114 C CA  . GLU A 369 ? 0.2678 0.2650 0.2636 -0.0009 -0.0054 0.0395  369 GLU A CA  
3115 C C   . GLU A 369 ? 0.2889 0.2848 0.2860 0.0000  -0.0056 0.0441  369 GLU A C   
3116 O O   . GLU A 369 ? 0.2919 0.2907 0.2853 -0.0010 -0.0083 0.0472  369 GLU A O   
3117 C CB  . GLU A 369 ? 0.2805 0.2814 0.2817 0.0009  -0.0047 0.0407  369 GLU A CB  
3118 C CG  . GLU A 369 ? 0.2772 0.2807 0.2757 -0.0011 -0.0052 0.0368  369 GLU A CG  
3119 C CD  . GLU A 369 ? 0.3185 0.3277 0.3218 0.0002  -0.0049 0.0382  369 GLU A CD  
3120 O OE1 . GLU A 369 ? 0.2980 0.3084 0.3089 0.0034  -0.0031 0.0414  369 GLU A OE1 
3121 O OE2 . GLU A 369 ? 0.3340 0.3468 0.3338 -0.0021 -0.0065 0.0365  369 GLU A OE2 
3122 N N   . LYS A 370 ? 0.2689 0.2602 0.2708 0.0013  -0.0026 0.0446  370 LYS A N   
3123 C CA  . LYS A 370 ? 0.3100 0.2998 0.3129 0.0015  -0.0030 0.0495  370 LYS A CA  
3124 C C   . LYS A 370 ? 0.3518 0.3406 0.3480 -0.0014 -0.0037 0.0480  370 LYS A C   
3125 O O   . LYS A 370 ? 0.2976 0.2883 0.2909 -0.0028 -0.0054 0.0518  370 LYS A O   
3126 C CB  . LYS A 370 ? 0.4200 0.4040 0.4301 0.0035  0.0001  0.0504  370 LYS A CB  
3127 C CG  . LYS A 370 ? 0.5410 0.5264 0.5601 0.0072  0.0008  0.0533  370 LYS A CG  
3128 C CD  . LYS A 370 ? 0.6137 0.5919 0.6405 0.0095  0.0041  0.0541  370 LYS A CD  
3129 C CE  . LYS A 370 ? 0.6488 0.6267 0.6841 0.0129  0.0074  0.0514  370 LYS A CE  
3130 N NZ  . LYS A 370 ? 0.6459 0.6303 0.6884 0.0160  0.0054  0.0567  370 LYS A NZ  
3131 N N   . LEU A 371 ? 0.3092 0.2959 0.3030 -0.0028 -0.0022 0.0425  371 LEU A N   
3132 C CA  . LEU A 371 ? 0.3346 0.3215 0.3236 -0.0052 -0.0026 0.0407  371 LEU A CA  
3133 C C   . LEU A 371 ? 0.3690 0.3605 0.3528 -0.0061 -0.0054 0.0407  371 LEU A C   
3134 O O   . LEU A 371 ? 0.2819 0.2752 0.2623 -0.0077 -0.0060 0.0422  371 LEU A O   
3135 C CB  . LEU A 371 ? 0.3042 0.2887 0.2927 -0.0064 -0.0010 0.0354  371 LEU A CB  
3136 C CG  . LEU A 371 ? 0.3148 0.3010 0.2997 -0.0084 -0.0016 0.0329  371 LEU A CG  
3137 C CD1 . LEU A 371 ? 0.2825 0.2682 0.2669 -0.0098 -0.0002 0.0353  371 LEU A CD1 
3138 C CD2 . LEU A 371 ? 0.2800 0.2650 0.2652 -0.0098 -0.0009 0.0284  371 LEU A CD2 
3139 N N   . TYR A 372 ? 0.3273 0.3207 0.3101 -0.0057 -0.0071 0.0388  372 TYR A N   
3140 C CA  . TYR A 372 ? 0.2816 0.2781 0.2593 -0.0068 -0.0098 0.0381  372 TYR A CA  
3141 C C   . TYR A 372 ? 0.3467 0.3463 0.3225 -0.0072 -0.0116 0.0430  372 TYR A C   
3142 O O   . TYR A 372 ? 0.3009 0.3023 0.2716 -0.0091 -0.0127 0.0428  372 TYR A O   
3143 C CB  . TYR A 372 ? 0.2354 0.2325 0.2124 -0.0068 -0.0116 0.0354  372 TYR A CB  
3144 C CG  . TYR A 372 ? 0.2470 0.2419 0.2245 -0.0075 -0.0110 0.0309  372 TYR A CG  
3145 C CD1 . TYR A 372 ? 0.2582 0.2517 0.2360 -0.0081 -0.0096 0.0288  372 TYR A CD1 
3146 C CD2 . TYR A 372 ? 0.2357 0.2308 0.2134 -0.0080 -0.0122 0.0291  372 TYR A CD2 
3147 C CE1 . TYR A 372 ? 0.2314 0.2238 0.2102 -0.0091 -0.0097 0.0254  372 TYR A CE1 
3148 C CE2 . TYR A 372 ? 0.2429 0.2366 0.2207 -0.0094 -0.0124 0.0257  372 TYR A CE2 
3149 C CZ  . TYR A 372 ? 0.2658 0.2581 0.2443 -0.0099 -0.0113 0.0241  372 TYR A CZ  
3150 O OH  . TYR A 372 ? 0.2816 0.2732 0.2606 -0.0116 -0.0120 0.0214  372 TYR A OH  
3151 N N   . SER A 373 ? 0.3148 0.3153 0.2949 -0.0058 -0.0117 0.0473  373 SER A N   
3152 C CA  . SER A 373 ? 0.3411 0.3452 0.3200 -0.0066 -0.0138 0.0530  373 SER A CA  
3153 C C   . SER A 373 ? 0.4230 0.4266 0.3999 -0.0085 -0.0132 0.0559  373 SER A C   
3154 O O   . SER A 373 ? 0.4214 0.4283 0.3934 -0.0111 -0.0152 0.0589  373 SER A O   
3155 C CB  . SER A 373 ? 0.3292 0.3349 0.3153 -0.0041 -0.0141 0.0574  373 SER A CB  
3156 O OG  . SER A 373 ? 0.4209 0.4297 0.4074 -0.0050 -0.0162 0.0641  373 SER A OG  
3157 N N   . THR A 374 ? 0.3365 0.3362 0.3164 -0.0079 -0.0106 0.0550  374 THR A N   
3158 C CA  . THR A 374 ? 0.3749 0.3742 0.3526 -0.0103 -0.0100 0.0577  374 THR A CA  
3159 C C   . THR A 374 ? 0.3607 0.3618 0.3315 -0.0131 -0.0094 0.0534  374 THR A C   
3160 O O   . THR A 374 ? 0.4012 0.4052 0.3670 -0.0163 -0.0100 0.0555  374 THR A O   
3161 C CB  . THR A 374 ? 0.3320 0.3261 0.3149 -0.0092 -0.0073 0.0578  374 THR A CB  
3162 O OG1 . THR A 374 ? 0.3071 0.2990 0.2974 -0.0060 -0.0073 0.0611  374 THR A OG1 
3163 C CG2 . THR A 374 ? 0.3906 0.3843 0.3710 -0.0123 -0.0069 0.0611  374 THR A CG2 
3164 N N   . LEU A 375 ? 0.3195 0.3191 0.2904 -0.0121 -0.0081 0.0472  375 LEU A N   
3165 C CA  . LEU A 375 ? 0.3070 0.3083 0.2735 -0.0139 -0.0073 0.0426  375 LEU A CA  
3166 C C   . LEU A 375 ? 0.2823 0.2870 0.2429 -0.0157 -0.0092 0.0425  375 LEU A C   
3167 O O   . LEU A 375 ? 0.3939 0.4010 0.3498 -0.0186 -0.0082 0.0416  375 LEU A O   
3168 C CB  . LEU A 375 ? 0.3084 0.3080 0.2774 -0.0122 -0.0067 0.0369  375 LEU A CB  
3169 C CG  . LEU A 375 ? 0.3160 0.3128 0.2892 -0.0119 -0.0044 0.0356  375 LEU A CG  
3170 C CD1 . LEU A 375 ? 0.3229 0.3187 0.2981 -0.0108 -0.0048 0.0309  375 LEU A CD1 
3171 C CD2 . LEU A 375 ? 0.3616 0.3599 0.3334 -0.0142 -0.0023 0.0354  375 LEU A CD2 
3172 N N   . GLU A 376 ? 0.3203 0.3253 0.2807 -0.0146 -0.0117 0.0434  376 GLU A N   
3173 C CA  . GLU A 376 ? 0.3364 0.3437 0.2907 -0.0166 -0.0137 0.0430  376 GLU A CA  
3174 C C   . GLU A 376 ? 0.3751 0.3858 0.3248 -0.0202 -0.0145 0.0480  376 GLU A C   
3175 O O   . GLU A 376 ? 0.4129 0.4257 0.3559 -0.0232 -0.0153 0.0466  376 GLU A O   
3176 C CB  . GLU A 376 ? 0.4052 0.4122 0.3611 -0.0149 -0.0163 0.0435  376 GLU A CB  
3177 C CG  . GLU A 376 ? 0.5291 0.5393 0.4812 -0.0169 -0.0193 0.0472  376 GLU A CG  
3178 C CD  . GLU A 376 ? 0.5556 0.5660 0.5106 -0.0151 -0.0213 0.0477  376 GLU A CD  
3179 O OE1 . GLU A 376 ? 0.5233 0.5359 0.4833 -0.0137 -0.0219 0.0524  376 GLU A OE1 
3180 O OE2 . GLU A 376 ? 0.5882 0.5968 0.5412 -0.0150 -0.0223 0.0435  376 GLU A OE2 
3181 N N   . LYS A 377 ? 0.3433 0.3544 0.2962 -0.0203 -0.0144 0.0536  377 LYS A N   
3182 C CA  . LYS A 377 ? 0.3812 0.3958 0.3298 -0.0243 -0.0158 0.0595  377 LYS A CA  
3183 C C   . LYS A 377 ? 0.4359 0.4511 0.3817 -0.0275 -0.0133 0.0593  377 LYS A C   
3184 O O   . LYS A 377 ? 0.4716 0.4900 0.4126 -0.0319 -0.0144 0.0640  377 LYS A O   
3185 C CB  . LYS A 377 ? 0.3663 0.3815 0.3209 -0.0228 -0.0182 0.0674  377 LYS A CB  
3186 C CG  . LYS A 377 ? 0.3935 0.4106 0.3500 -0.0210 -0.0209 0.0686  377 LYS A CG  
3187 C CD  . LYS A 377 ? 0.4102 0.4278 0.3760 -0.0177 -0.0222 0.0749  377 LYS A CD  
3188 C CE  . LYS A 377 ? 0.4912 0.5093 0.4614 -0.0143 -0.0228 0.0729  377 LYS A CE  
3189 N NZ  . LYS A 377 ? 0.5620 0.5859 0.5338 -0.0151 -0.0264 0.0790  377 LYS A NZ  
3190 N N   . GLU A 378 ? 0.3508 0.3634 0.2991 -0.0259 -0.0102 0.0542  378 GLU A N   
3191 C CA  . GLU A 378 ? 0.4726 0.4865 0.4184 -0.0292 -0.0075 0.0536  378 GLU A CA  
3192 C C   . GLU A 378 ? 0.4546 0.4720 0.3935 -0.0322 -0.0057 0.0477  378 GLU A C   
3193 O O   . GLU A 378 ? 0.4741 0.4906 0.4145 -0.0299 -0.0040 0.0408  378 GLU A O   
3194 C CB  . GLU A 378 ? 0.5502 0.5607 0.5021 -0.0266 -0.0050 0.0510  378 GLU A CB  
3195 C CG  . GLU A 378 ? 0.6404 0.6465 0.5990 -0.0240 -0.0059 0.0559  378 GLU A CG  
3196 C CD  . GLU A 378 ? 0.8011 0.8073 0.7593 -0.0271 -0.0068 0.0634  378 GLU A CD  
3197 O OE1 . GLU A 378 ? 0.8568 0.8670 0.8085 -0.0320 -0.0067 0.0649  378 GLU A OE1 
3198 O OE2 . GLU A 378 ? 0.8607 0.8629 0.8250 -0.0247 -0.0077 0.0679  378 GLU A OE2 
3199 N N   . GLU A 379 ? 0.5801 0.6015 0.5116 -0.0377 -0.0061 0.0505  379 GLU A N   
3200 C CA  . GLU A 379 ? 0.6549 0.6799 0.5787 -0.0416 -0.0038 0.0449  379 GLU A CA  
3201 C C   . GLU A 379 ? 0.5687 0.5945 0.4947 -0.0408 0.0008  0.0376  379 GLU A C   
3202 O O   . GLU A 379 ? 0.5785 0.6049 0.5034 -0.0400 0.0029  0.0302  379 GLU A O   
3203 C CB  . GLU A 379 ? 0.7843 0.8139 0.7000 -0.0488 -0.0045 0.0503  379 GLU A CB  
3204 C CG  . GLU A 379 ? 0.9302 0.9643 0.8370 -0.0543 -0.0012 0.0446  379 GLU A CG  
3205 C CD  . GLU A 379 ? 1.0202 1.0587 0.9173 -0.0620 -0.0034 0.0503  379 GLU A CD  
3206 O OE1 . GLU A 379 ? 1.0465 1.0867 0.9358 -0.0654 -0.0031 0.0465  379 GLU A OE1 
3207 O OE2 . GLU A 379 ? 1.0666 1.1065 0.9636 -0.0650 -0.0057 0.0587  379 GLU A OE2 
3208 N N   . TRP A 380 ? 0.4691 0.4951 0.3989 -0.0411 0.0024  0.0396  380 TRP A N   
3209 C CA  . TRP A 380 ? 0.4327 0.4612 0.3643 -0.0415 0.0067  0.0337  380 TRP A CA  
3210 C C   . TRP A 380 ? 0.4340 0.4594 0.3740 -0.0355 0.0073  0.0289  380 TRP A C   
3211 O O   . TRP A 380 ? 0.3973 0.4255 0.3405 -0.0353 0.0106  0.0239  380 TRP A O   
3212 C CB  . TRP A 380 ? 0.4113 0.4416 0.3425 -0.0453 0.0078  0.0385  380 TRP A CB  
3213 C CG  . TRP A 380 ? 0.3773 0.4023 0.3138 -0.0429 0.0048  0.0453  380 TRP A CG  
3214 C CD1 . TRP A 380 ? 0.4308 0.4537 0.3663 -0.0435 0.0010  0.0531  380 TRP A CD1 
3215 C CD2 . TRP A 380 ? 0.4012 0.4222 0.3451 -0.0394 0.0055  0.0448  380 TRP A CD2 
3216 N NE1 . TRP A 380 ? 0.4647 0.4821 0.4072 -0.0401 -0.0002 0.0569  380 TRP A NE1 
3217 C CE2 . TRP A 380 ? 0.4045 0.4204 0.3516 -0.0379 0.0026  0.0517  380 TRP A CE2 
3218 C CE3 . TRP A 380 ? 0.3828 0.4044 0.3314 -0.0376 0.0084  0.0391  380 TRP A CE3 
3219 C CZ2 . TRP A 380 ? 0.3507 0.3613 0.3044 -0.0350 0.0029  0.0524  380 TRP A CZ2 
3220 C CZ3 . TRP A 380 ? 0.2967 0.3136 0.2514 -0.0352 0.0081  0.0405  380 TRP A CZ3 
3221 C CH2 . TRP A 380 ? 0.3062 0.3173 0.2629 -0.0340 0.0056  0.0466  380 TRP A CH2 
3222 N N   . ILE A 381 ? 0.3097 0.3304 0.2537 -0.0312 0.0042  0.0303  381 ILE A N   
3223 C CA  . ILE A 381 ? 0.3297 0.3475 0.2806 -0.0264 0.0041  0.0262  381 ILE A CA  
3224 C C   . ILE A 381 ? 0.3725 0.3893 0.3223 -0.0243 0.0028  0.0218  381 ILE A C   
3225 O O   . ILE A 381 ? 0.4339 0.4494 0.3795 -0.0249 0.0002  0.0243  381 ILE A O   
3226 C CB  . ILE A 381 ? 0.2777 0.2907 0.2334 -0.0236 0.0019  0.0305  381 ILE A CB  
3227 C CG1 . ILE A 381 ? 0.3484 0.3609 0.3059 -0.0255 0.0032  0.0344  381 ILE A CG1 
3228 C CG2 . ILE A 381 ? 0.2902 0.3008 0.2517 -0.0197 0.0013  0.0264  381 ILE A CG2 
3229 C CD1 . ILE A 381 ? 0.3690 0.3762 0.3316 -0.0228 0.0018  0.0375  381 ILE A CD1 
3230 N N   . GLU A 382 ? 0.3394 0.3567 0.2934 -0.0220 0.0043  0.0157  382 GLU A N   
3231 C CA  . GLU A 382 ? 0.2869 0.3017 0.2415 -0.0194 0.0026  0.0116  382 GLU A CA  
3232 C C   . GLU A 382 ? 0.2936 0.3061 0.2562 -0.0155 0.0011  0.0101  382 GLU A C   
3233 O O   . GLU A 382 ? 0.2786 0.2933 0.2466 -0.0144 0.0032  0.0068  382 GLU A O   
3234 C CB  . GLU A 382 ? 0.3712 0.3888 0.3235 -0.0206 0.0056  0.0054  382 GLU A CB  
3235 C CG  . GLU A 382 ? 0.5024 0.5162 0.4560 -0.0179 0.0039  0.0008  382 GLU A CG  
3236 C CD  . GLU A 382 ? 0.7000 0.7158 0.6519 -0.0188 0.0075  -0.0062 382 GLU A CD  
3237 O OE1 . GLU A 382 ? 0.7417 0.7617 0.6876 -0.0231 0.0108  -0.0069 382 GLU A OE1 
3238 O OE2 . GLU A 382 ? 0.7440 0.7570 0.7006 -0.0156 0.0071  -0.0112 382 GLU A OE2 
3239 N N   . THR A 383 ? 0.2779 0.2864 0.2410 -0.0138 -0.0024 0.0128  383 THR A N   
3240 C CA  . THR A 383 ? 0.2924 0.2987 0.2617 -0.0110 -0.0044 0.0112  383 THR A CA  
3241 C C   . THR A 383 ? 0.2992 0.3045 0.2703 -0.0092 -0.0052 0.0063  383 THR A C   
3242 O O   . THR A 383 ? 0.3272 0.3316 0.2936 -0.0100 -0.0054 0.0045  383 THR A O   
3243 C CB  . THR A 383 ? 0.3105 0.3133 0.2792 -0.0104 -0.0076 0.0149  383 THR A CB  
3244 O OG1 . THR A 383 ? 0.3522 0.3537 0.3156 -0.0110 -0.0097 0.0160  383 THR A OG1 
3245 C CG2 . THR A 383 ? 0.2944 0.2974 0.2633 -0.0114 -0.0063 0.0193  383 THR A CG2 
3246 N N   . LEU A 384 ? 0.2349 0.2404 0.2133 -0.0071 -0.0059 0.0041  384 LEU A N   
3247 C CA  . LEU A 384 ? 0.2560 0.2609 0.2386 -0.0049 -0.0065 -0.0005 384 LEU A CA  
3248 C C   . LEU A 384 ? 0.2716 0.2733 0.2592 -0.0031 -0.0110 0.0003  384 LEU A C   
3249 O O   . LEU A 384 ? 0.2513 0.2537 0.2417 -0.0035 -0.0121 0.0029  384 LEU A O   
3250 C CB  . LEU A 384 ? 0.2504 0.2606 0.2390 -0.0042 -0.0026 -0.0042 384 LEU A CB  
3251 C CG  . LEU A 384 ? 0.2849 0.2994 0.2691 -0.0067 0.0024  -0.0058 384 LEU A CG  
3252 C CD1 . LEU A 384 ? 0.2603 0.2805 0.2521 -0.0056 0.0060  -0.0103 384 LEU A CD1 
3253 C CD2 . LEU A 384 ? 0.2696 0.2820 0.2462 -0.0081 0.0029  -0.0078 384 LEU A CD2 
3254 N N   . THR A 385 ? 0.2232 0.2211 0.2113 -0.0016 -0.0137 -0.0018 385 THR A N   
3255 C CA  . THR A 385 ? 0.1977 0.1934 0.1922 0.0000  -0.0180 -0.0013 385 THR A CA  
3256 C C   . THR A 385 ? 0.1898 0.1896 0.1941 0.0021  -0.0166 -0.0036 385 THR A C   
3257 O O   . THR A 385 ? 0.2213 0.2253 0.2277 0.0027  -0.0120 -0.0068 385 THR A O   
3258 C CB  . THR A 385 ? 0.2129 0.2030 0.2064 0.0011  -0.0214 -0.0030 385 THR A CB  
3259 O OG1 . THR A 385 ? 0.2879 0.2782 0.2855 0.0034  -0.0187 -0.0083 385 THR A OG1 
3260 C CG2 . THR A 385 ? 0.2187 0.2056 0.2021 -0.0013 -0.0223 -0.0013 385 THR A CG2 
3261 N N   . LEU A 386 ? 0.2063 0.2058 0.2170 0.0028  -0.0206 -0.0018 386 LEU A N   
3262 C CA  . LEU A 386 ? 0.2622 0.2664 0.2838 0.0048  -0.0201 -0.0034 386 LEU A CA  
3263 C C   . LEU A 386 ? 0.2880 0.2919 0.3153 0.0083  -0.0183 -0.0085 386 LEU A C   
3264 O O   . LEU A 386 ? 0.2489 0.2586 0.2833 0.0100  -0.0146 -0.0115 386 LEU A O   
3265 C CB  . LEU A 386 ? 0.2222 0.2258 0.2494 0.0044  -0.0258 0.0000  386 LEU A CB  
3266 C CG  . LEU A 386 ? 0.2530 0.2566 0.2754 0.0006  -0.0277 0.0043  386 LEU A CG  
3267 C CD1 . LEU A 386 ? 0.2581 0.2615 0.2859 -0.0005 -0.0336 0.0073  386 LEU A CD1 
3268 C CD2 . LEU A 386 ? 0.2473 0.2560 0.2694 -0.0011 -0.0232 0.0044  386 LEU A CD2 
3269 N N   . GLU A 387 ? 0.3165 0.3139 0.3409 0.0093  -0.0207 -0.0098 387 GLU A N   
3270 C CA  . GLU A 387 ? 0.3250 0.3207 0.3545 0.0127  -0.0187 -0.0154 387 GLU A CA  
3271 C C   . GLU A 387 ? 0.2412 0.2411 0.2668 0.0120  -0.0115 -0.0200 387 GLU A C   
3272 O O   . GLU A 387 ? 0.2898 0.2935 0.3231 0.0146  -0.0076 -0.0250 387 GLU A O   
3273 C CB  . GLU A 387 ? 0.4113 0.3980 0.4361 0.0128  -0.0224 -0.0158 387 GLU A CB  
3274 C CG  . GLU A 387 ? 0.4920 0.4753 0.5229 0.0165  -0.0207 -0.0220 387 GLU A CG  
3275 C CD  . GLU A 387 ? 0.6778 0.6520 0.7006 0.0154  -0.0227 -0.0234 387 GLU A CD  
3276 O OE1 . GLU A 387 ? 0.7642 0.7325 0.7932 0.0185  -0.0241 -0.0269 387 GLU A OE1 
3277 O OE2 . GLU A 387 ? 0.7450 0.7178 0.7557 0.0115  -0.0230 -0.0210 387 GLU A OE2 
3278 N N   . GLU A 388 ? 0.2446 0.2442 0.2585 0.0083  -0.0098 -0.0182 388 GLU A N   
3279 C CA  . GLU A 388 ? 0.2842 0.2880 0.2929 0.0065  -0.0036 -0.0216 388 GLU A CA  
3280 C C   . GLU A 388 ? 0.2944 0.3067 0.3091 0.0064  0.0003  -0.0219 388 GLU A C   
3281 O O   . GLU A 388 ? 0.3416 0.3589 0.3590 0.0067  0.0056  -0.0268 388 GLU A O   
3282 C CB  . GLU A 388 ? 0.3027 0.3047 0.2985 0.0024  -0.0037 -0.0181 388 GLU A CB  
3283 C CG  . GLU A 388 ? 0.3241 0.3191 0.3127 0.0016  -0.0062 -0.0190 388 GLU A CG  
3284 C CD  . GLU A 388 ? 0.3982 0.3920 0.3762 -0.0021 -0.0079 -0.0139 388 GLU A CD  
3285 O OE1 . GLU A 388 ? 0.3466 0.3430 0.3244 -0.0031 -0.0086 -0.0091 388 GLU A OE1 
3286 O OE2 . GLU A 388 ? 0.4814 0.4717 0.4515 -0.0041 -0.0085 -0.0147 388 GLU A OE2 
3287 N N   . ALA A 389 ? 0.3319 0.3462 0.3486 0.0055  -0.0021 -0.0169 389 ALA A N   
3288 C CA  . ALA A 389 ? 0.2201 0.2423 0.2425 0.0049  0.0011  -0.0169 389 ALA A CA  
3289 C C   . ALA A 389 ? 0.2677 0.2945 0.3034 0.0086  0.0021  -0.0209 389 ALA A C   
3290 O O   . ALA A 389 ? 0.3380 0.3724 0.3782 0.0084  0.0069  -0.0237 389 ALA A O   
3291 C CB  . ALA A 389 ? 0.1820 0.2043 0.2040 0.0029  -0.0020 -0.0112 389 ALA A CB  
3292 N N   . MET A 390 ? 0.3269 0.3494 0.3695 0.0120  -0.0025 -0.0209 390 MET A N   
3293 C CA  . MET A 390 ? 0.3322 0.3587 0.3894 0.0162  -0.0021 -0.0243 390 MET A CA  
3294 C C   . MET A 390 ? 0.3916 0.4195 0.4507 0.0184  0.0037  -0.0318 390 MET A C   
3295 O O   . MET A 390 ? 0.3845 0.4201 0.4539 0.0205  0.0078  -0.0357 390 MET A O   
3296 C CB  . MET A 390 ? 0.3040 0.3246 0.3676 0.0190  -0.0092 -0.0216 390 MET A CB  
3297 C CG  . MET A 390 ? 0.4397 0.4637 0.5201 0.0240  -0.0098 -0.0244 390 MET A CG  
3298 S SD  . MET A 390 ? 0.5392 0.5570 0.6284 0.0265  -0.0193 -0.0195 390 MET A SD  
3299 C CE  . MET A 390 ? 0.5519 0.5578 0.6359 0.0286  -0.0202 -0.0235 390 MET A CE  
3300 N N   . ARG A 391 ? 0.3121 0.3331 0.3615 0.0175  0.0045  -0.0343 391 ARG A N   
3301 C CA  . ARG A 391 ? 0.3995 0.4202 0.4498 0.0190  0.0099  -0.0422 391 ARG A CA  
3302 C C   . ARG A 391 ? 0.4099 0.4354 0.4495 0.0144  0.0165  -0.0449 391 ARG A C   
3303 O O   . ARG A 391 ? 0.4281 0.4540 0.4662 0.0145  0.0218  -0.0519 391 ARG A O   
3304 C CB  . ARG A 391 ? 0.3995 0.4093 0.4459 0.0204  0.0066  -0.0439 391 ARG A CB  
3305 C CG  . ARG A 391 ? 0.4749 0.4789 0.5304 0.0240  -0.0008 -0.0402 391 ARG A CG  
3306 C CD  . ARG A 391 ? 0.6004 0.5935 0.6542 0.0258  -0.0034 -0.0430 391 ARG A CD  
3307 N NE  . ARG A 391 ? 0.7575 0.7481 0.8271 0.0314  -0.0066 -0.0443 391 ARG A NE  
3308 C CZ  . ARG A 391 ? 0.8412 0.8243 0.9139 0.0326  -0.0144 -0.0396 391 ARG A CZ  
3309 N NH1 . ARG A 391 ? 0.8419 0.8199 0.9028 0.0285  -0.0193 -0.0340 391 ARG A NH1 
3310 N NH2 . ARG A 391 ? 0.8522 0.8334 0.9404 0.0378  -0.0173 -0.0404 391 ARG A NH2 
3311 N N   . LYS A 392 ? 0.3312 0.3604 0.3635 0.0102  0.0165  -0.0397 392 LYS A N   
3312 C CA  . LYS A 392 ? 0.3857 0.4188 0.4070 0.0051  0.0216  -0.0408 392 LYS A CA  
3313 C C   . LYS A 392 ? 0.4209 0.4634 0.4484 0.0052  0.0288  -0.0472 392 LYS A C   
3314 O O   . LYS A 392 ? 0.3769 0.4266 0.4148 0.0068  0.0298  -0.0468 392 LYS A O   
3315 C CB  . LYS A 392 ? 0.4043 0.4391 0.4192 0.0013  0.0196  -0.0333 392 LYS A CB  
3316 C CG  . LYS A 392 ? 0.5113 0.5468 0.5126 -0.0043 0.0223  -0.0319 392 LYS A CG  
3317 C CD  . LYS A 392 ? 0.6050 0.6324 0.5964 -0.0054 0.0191  -0.0305 392 LYS A CD  
3318 C CE  . LYS A 392 ? 0.7197 0.7469 0.7000 -0.0103 0.0181  -0.0243 392 LYS A CE  
3319 N NZ  . LYS A 392 ? 0.8011 0.8226 0.7714 -0.0124 0.0160  -0.0236 392 LYS A NZ  
3320 N N   . GLU A 393 ? 0.4715 0.5142 0.4923 0.0030  0.0340  -0.0533 393 GLU A N   
3321 C CA  . GLU A 393 ? 0.4997 0.5517 0.5257 0.0025  0.0417  -0.0606 393 GLU A CA  
3322 C C   . GLU A 393 ? 0.4273 0.4880 0.4460 -0.0037 0.0456  -0.0582 393 GLU A C   
3323 O O   . GLU A 393 ? 0.4635 0.5342 0.4900 -0.0038 0.0502  -0.0610 393 GLU A O   
3324 C CB  . GLU A 393 ? 0.5226 0.5711 0.5442 0.0022  0.0462  -0.0692 393 GLU A CB  
3325 C CG  . GLU A 393 ? 0.6517 0.7097 0.6791 0.0019  0.0551  -0.0782 393 GLU A CG  
3326 C CD  . GLU A 393 ? 0.7800 0.8349 0.7979 -0.0011 0.0604  -0.0864 393 GLU A CD  
3327 O OE1 . GLU A 393 ? 0.8208 0.8843 0.8381 -0.0041 0.0684  -0.0934 393 GLU A OE1 
3328 O OE2 . GLU A 393 ? 0.8165 0.8607 0.8272 -0.0011 0.0567  -0.0861 393 GLU A OE2 
3329 N N   . ASP A 394 ? 0.3727 0.4302 0.3771 -0.0091 0.0434  -0.0526 394 ASP A N   
3330 C CA  . ASP A 394 ? 0.4318 0.4965 0.4280 -0.0158 0.0468  -0.0501 394 ASP A CA  
3331 C C   . ASP A 394 ? 0.4268 0.4937 0.4261 -0.0163 0.0435  -0.0424 394 ASP A C   
3332 O O   . ASP A 394 ? 0.4760 0.5414 0.4660 -0.0208 0.0415  -0.0358 394 ASP A O   
3333 C CB  . ASP A 394 ? 0.4711 0.5316 0.4510 -0.0217 0.0462  -0.0477 394 ASP A CB  
3334 C CG  . ASP A 394 ? 0.5768 0.6269 0.5524 -0.0199 0.0390  -0.0419 394 ASP A CG  
3335 O OD1 . ASP A 394 ? 0.5956 0.6416 0.5800 -0.0145 0.0347  -0.0398 394 ASP A OD1 
3336 O OD2 . ASP A 394 ? 0.6055 0.6524 0.5689 -0.0244 0.0377  -0.0391 394 ASP A OD2 
3337 N N   . VAL A 395 ? 0.4187 0.4892 0.4316 -0.0119 0.0430  -0.0431 395 VAL A N   
3338 C CA  . VAL A 395 ? 0.4298 0.5026 0.4464 -0.0126 0.0402  -0.0367 395 VAL A CA  
3339 C C   . VAL A 395 ? 0.4269 0.5109 0.4552 -0.0118 0.0445  -0.0403 395 VAL A C   
3340 O O   . VAL A 395 ? 0.3662 0.4553 0.4022 -0.0091 0.0488  -0.0476 395 VAL A O   
3341 C CB  . VAL A 395 ? 0.4005 0.4654 0.4215 -0.0084 0.0331  -0.0320 395 VAL A CB  
3342 C CG1 . VAL A 395 ? 0.3586 0.4137 0.3681 -0.0096 0.0291  -0.0281 395 VAL A CG1 
3343 C CG2 . VAL A 395 ? 0.4020 0.4665 0.4359 -0.0021 0.0319  -0.0363 395 VAL A CG2 
3344 N N   . LYS A 396 ? 0.4163 0.5041 0.4463 -0.0143 0.0433  -0.0352 396 LYS A N   
3345 C CA  . LYS A 396 ? 0.3945 0.4937 0.4356 -0.0143 0.0468  -0.0374 396 LYS A CA  
3346 C C   . LYS A 396 ? 0.3901 0.4894 0.4453 -0.0087 0.0424  -0.0363 396 LYS A C   
3347 O O   . LYS A 396 ? 0.2745 0.3656 0.3283 -0.0073 0.0363  -0.0312 396 LYS A O   
3348 C CB  . LYS A 396 ? 0.4772 0.5811 0.5124 -0.0209 0.0479  -0.0325 396 LYS A CB  
3349 C CG  . LYS A 396 ? 0.5704 0.6790 0.5951 -0.0272 0.0534  -0.0345 396 LYS A CG  
3350 C CD  . LYS A 396 ? 0.5898 0.7105 0.6180 -0.0319 0.0578  -0.0347 396 LYS A CD  
3351 C CE  . LYS A 396 ? 0.6098 0.7358 0.6267 -0.0392 0.0631  -0.0362 396 LYS A CE  
3352 N NZ  . LYS A 396 ? 0.6367 0.7682 0.6555 -0.0378 0.0691  -0.0454 396 LYS A NZ  
3353 N N   . THR A 397 ? 0.3095 0.2523 0.1966 -0.0128 0.0364  0.0182  397 THR A N   
3354 C CA  . THR A 397 ? 0.3575 0.3084 0.2564 -0.0101 0.0367  0.0139  397 THR A CA  
3355 C C   . THR A 397 ? 0.4577 0.4196 0.3603 -0.0153 0.0421  0.0128  397 THR A C   
3356 O O   . THR A 397 ? 0.4578 0.4236 0.3539 -0.0198 0.0462  0.0141  397 THR A O   
3357 C CB  . THR A 397 ? 0.4857 0.4427 0.3881 -0.0033 0.0352  0.0086  397 THR A CB  
3358 O OG1 . THR A 397 ? 0.6532 0.6130 0.5671 0.0006  0.0330  0.0059  397 THR A OG1 
3359 C CG2 . THR A 397 ? 0.3948 0.3646 0.2960 -0.0043 0.0402  0.0049  397 THR A CG2 
3360 N N   . GLU A 398 ? 0.4116 0.3787 0.3247 -0.0147 0.0420  0.0105  398 GLU A N   
3361 C CA  . GLU A 398 ? 0.4139 0.3910 0.3318 -0.0197 0.0465  0.0096  398 GLU A CA  
3362 C C   . GLU A 398 ? 0.4170 0.4029 0.3473 -0.0163 0.0458  0.0053  398 GLU A C   
3363 O O   . GLU A 398 ? 0.3582 0.3388 0.2933 -0.0124 0.0416  0.0050  398 GLU A O   
3364 C CB  . GLU A 398 ? 0.3910 0.3607 0.3065 -0.0263 0.0472  0.0145  398 GLU A CB  
3365 C CG  . GLU A 398 ? 0.4020 0.3816 0.3213 -0.0325 0.0520  0.0141  398 GLU A CG  
3366 C CD  . GLU A 398 ? 0.4679 0.4394 0.3855 -0.0390 0.0523  0.0187  398 GLU A CD  
3367 O OE1 . GLU A 398 ? 0.4934 0.4703 0.4179 -0.0426 0.0539  0.0178  398 GLU A OE1 
3368 O OE2 . GLU A 398 ? 0.5003 0.4598 0.4096 -0.0406 0.0508  0.0232  398 GLU A OE2 
3369 N N   . VAL A 399 ? 0.3481 0.3475 0.2834 -0.0178 0.0499  0.0022  399 VAL A N   
3370 C CA  . VAL A 399 ? 0.2966 0.3057 0.2439 -0.0154 0.0496  -0.0016 399 VAL A CA  
3371 C C   . VAL A 399 ? 0.3776 0.3879 0.3290 -0.0214 0.0509  0.0002  399 VAL A C   
3372 O O   . VAL A 399 ? 0.3373 0.3486 0.2845 -0.0278 0.0545  0.0026  399 VAL A O   
3373 C CB  . VAL A 399 ? 0.3988 0.4225 0.3503 -0.0134 0.0532  -0.0062 399 VAL A CB  
3374 C CG1 . VAL A 399 ? 0.3594 0.3938 0.3237 -0.0118 0.0532  -0.0095 399 VAL A CG1 
3375 C CG2 . VAL A 399 ? 0.4356 0.4581 0.3839 -0.0069 0.0515  -0.0088 399 VAL A CG2 
3376 N N   . ILE A 400 ? 0.4003 0.4105 0.3598 -0.0195 0.0480  -0.0008 400 ILE A N   
3377 C CA  . ILE A 400 ? 0.3987 0.4124 0.3635 -0.0247 0.0493  -0.0003 400 ILE A CA  
3378 C C   . ILE A 400 ? 0.3715 0.3972 0.3480 -0.0215 0.0487  -0.0044 400 ILE A C   
3379 O O   . ILE A 400 ? 0.3390 0.3658 0.3196 -0.0149 0.0459  -0.0066 400 ILE A O   
3380 C CB  . ILE A 400 ? 0.4318 0.4323 0.3942 -0.0270 0.0462  0.0031  400 ILE A CB  
3381 C CG1 . ILE A 400 ? 0.4499 0.4429 0.4139 -0.0203 0.0412  0.0028  400 ILE A CG1 
3382 C CG2 . ILE A 400 ? 0.4992 0.4893 0.4510 -0.0315 0.0474  0.0076  400 ILE A CG2 
3383 C CD1 . ILE A 400 ? 0.4581 0.4383 0.4197 -0.0222 0.0384  0.0059  400 ILE A CD1 
3384 N N   . GLU A 401 ? 0.3257 0.3605 0.3077 -0.0264 0.0514  -0.0051 401 GLU A N   
3385 C CA  . GLU A 401 ? 0.3245 0.3727 0.3177 -0.0242 0.0516  -0.0088 401 GLU A CA  
3386 C C   . GLU A 401 ? 0.3336 0.3813 0.3332 -0.0254 0.0488  -0.0089 401 GLU A C   
3387 O O   . GLU A 401 ? 0.3108 0.3679 0.3196 -0.0222 0.0476  -0.0116 401 GLU A O   
3388 C CB  . GLU A 401 ? 0.3914 0.4532 0.3875 -0.0284 0.0569  -0.0103 401 GLU A CB  
3389 C CG  . GLU A 401 ? 0.5097 0.5744 0.5000 -0.0269 0.0601  -0.0110 401 GLU A CG  
3390 C CD  . GLU A 401 ? 0.6328 0.7021 0.6271 -0.0188 0.0585  -0.0147 401 GLU A CD  
3391 O OE1 . GLU A 401 ? 0.6901 0.7564 0.6777 -0.0162 0.0593  -0.0151 401 GLU A OE1 
3392 O OE2 . GLU A 401 ? 0.6748 0.7505 0.6789 -0.0152 0.0564  -0.0172 401 GLU A OE2 
3393 N N   . SER A 402 ? 0.3129 0.3501 0.3080 -0.0297 0.0478  -0.0059 402 SER A N   
3394 C CA  . SER A 402 ? 0.3186 0.3560 0.3194 -0.0316 0.0456  -0.0063 402 SER A CA  
3395 C C   . SER A 402 ? 0.3349 0.3566 0.3290 -0.0337 0.0433  -0.0032 402 SER A C   
3396 O O   . SER A 402 ? 0.3652 0.3782 0.3511 -0.0369 0.0448  -0.0002 402 SER A O   
3397 C CB  . SER A 402 ? 0.3454 0.3936 0.3513 -0.0381 0.0488  -0.0073 402 SER A CB  
3398 O OG  . SER A 402 ? 0.3762 0.4272 0.3888 -0.0390 0.0464  -0.0086 402 SER A OG  
3399 N N   . VAL A 403 ? 0.2902 0.3085 0.2880 -0.0318 0.0398  -0.0038 403 VAL A N   
3400 C CA  . VAL A 403 ? 0.3214 0.3257 0.3141 -0.0338 0.0377  -0.0013 403 VAL A CA  
3401 C C   . VAL A 403 ? 0.2996 0.3070 0.2977 -0.0376 0.0371  -0.0027 403 VAL A C   
3402 O O   . VAL A 403 ? 0.2969 0.3158 0.3028 -0.0364 0.0366  -0.0055 403 VAL A O   
3403 C CB  . VAL A 403 ? 0.3243 0.3189 0.3149 -0.0271 0.0338  -0.0005 403 VAL A CB  
3404 C CG1 . VAL A 403 ? 0.3630 0.3533 0.3475 -0.0240 0.0342  0.0010  403 VAL A CG1 
3405 C CG2 . VAL A 403 ? 0.3319 0.3343 0.3307 -0.0215 0.0311  -0.0032 403 VAL A CG2 
3406 N N   . LYS A 404 ? 0.2455 0.2425 0.2392 -0.0425 0.0370  -0.0008 404 LYS A N   
3407 C CA  . LYS A 404 ? 0.2561 0.2534 0.2537 -0.0458 0.0357  -0.0022 404 LYS A CA  
3408 C C   . LYS A 404 ? 0.3622 0.3512 0.3595 -0.0406 0.0317  -0.0024 404 LYS A C   
3409 O O   . LYS A 404 ? 0.4054 0.3817 0.3967 -0.0387 0.0305  0.0001  404 LYS A O   
3410 C CB  . LYS A 404 ? 0.3205 0.3108 0.3142 -0.0537 0.0376  -0.0004 404 LYS A CB  
3411 C CG  . LYS A 404 ? 0.4111 0.4022 0.4089 -0.0578 0.0365  -0.0024 404 LYS A CG  
3412 C CD  . LYS A 404 ? 0.5471 0.5327 0.5421 -0.0662 0.0386  -0.0008 404 LYS A CD  
3413 C CE  . LYS A 404 ? 0.6088 0.6074 0.6078 -0.0714 0.0421  -0.0015 404 LYS A CE  
3414 N NZ  . LYS A 404 ? 0.6575 0.6548 0.6513 -0.0731 0.0454  0.0017  404 LYS A NZ  
3415 N N   . ALA A 405 ? 0.2718 0.2684 0.2758 -0.0381 0.0296  -0.0051 405 ALA A N   
3416 C CA  . ALA A 405 ? 0.2893 0.2799 0.2936 -0.0325 0.0260  -0.0052 405 ALA A CA  
3417 C C   . ALA A 405 ? 0.2609 0.2372 0.2599 -0.0350 0.0250  -0.0038 405 ALA A C   
3418 O O   . ALA A 405 ? 0.2852 0.2592 0.2831 -0.0414 0.0263  -0.0040 405 ALA A O   
3419 C CB  . ALA A 405 ? 0.3148 0.3166 0.3269 -0.0305 0.0241  -0.0081 405 ALA A CB  
3420 N N   . GLY A 406 ? 0.2546 0.2213 0.2507 -0.0299 0.0226  -0.0023 406 GLY A N   
3421 C CA  . GLY A 406 ? 0.3210 0.2742 0.3128 -0.0313 0.0215  -0.0011 406 GLY A CA  
3422 C C   . GLY A 406 ? 0.3141 0.2587 0.3038 -0.0247 0.0189  0.0006  406 GLY A C   
3423 O O   . GLY A 406 ? 0.2895 0.2391 0.2817 -0.0190 0.0176  0.0007  406 GLY A O   
3424 N N   . THR A 407 ? 0.2591 0.1909 0.2448 -0.0255 0.0180  0.0020  407 THR A N   
3425 C CA  . THR A 407 ? 0.2601 0.1820 0.2435 -0.0199 0.0157  0.0040  407 THR A CA  
3426 C C   . THR A 407 ? 0.2789 0.1869 0.2557 -0.0224 0.0164  0.0073  407 THR A C   
3427 O O   . THR A 407 ? 0.2581 0.1642 0.2322 -0.0284 0.0186  0.0079  407 THR A O   
3428 C CB  . THR A 407 ? 0.2785 0.1986 0.2644 -0.0174 0.0136  0.0023  407 THR A CB  
3429 O OG1 . THR A 407 ? 0.3048 0.2156 0.2878 -0.0220 0.0143  0.0021  407 THR A OG1 
3430 C CG2 . THR A 407 ? 0.2351 0.1694 0.2274 -0.0170 0.0132  -0.0011 407 THR A CG2 
3431 N N   . TRP A 408 ? 0.2602 0.1581 0.2346 -0.0179 0.0144  0.0095  408 TRP A N   
3432 C CA  . TRP A 408 ? 0.2868 0.1711 0.2554 -0.0201 0.0147  0.0128  408 TRP A CA  
3433 C C   . TRP A 408 ? 0.3416 0.2176 0.3096 -0.0236 0.0148  0.0119  408 TRP A C   
3434 O O   . TRP A 408 ? 0.3286 0.1925 0.2924 -0.0256 0.0150  0.0146  408 TRP A O   
3435 C CB  . TRP A 408 ? 0.2771 0.1538 0.2435 -0.0142 0.0125  0.0159  408 TRP A CB  
3436 C CG  . TRP A 408 ? 0.3111 0.1866 0.2810 -0.0083 0.0099  0.0151  408 TRP A CG  
3437 C CD1 . TRP A 408 ? 0.3318 0.2112 0.3057 -0.0077 0.0094  0.0121  408 TRP A CD1 
3438 C CD2 . TRP A 408 ? 0.2775 0.1472 0.2468 -0.0023 0.0075  0.0176  408 TRP A CD2 
3439 N NE1 . TRP A 408 ? 0.3212 0.1980 0.2972 -0.0016 0.0071  0.0127  408 TRP A NE1 
3440 C CE2 . TRP A 408 ? 0.3224 0.1932 0.2960 0.0018  0.0058  0.0161  408 TRP A CE2 
3441 C CE3 . TRP A 408 ? 0.2622 0.1262 0.2279 0.0000  0.0065  0.0210  408 TRP A CE3 
3442 C CZ2 . TRP A 408 ? 0.2777 0.1442 0.2525 0.0080  0.0034  0.0180  408 TRP A CZ2 
3443 C CZ3 . TRP A 408 ? 0.3151 0.1746 0.2820 0.0061  0.0037  0.0227  408 TRP A CZ3 
3444 C CH2 . TRP A 408 ? 0.3037 0.1645 0.2754 0.0100  0.0023  0.0213  408 TRP A CH2 
3445 N N   . PHE A 409 ? 0.2817 0.1637 0.2539 -0.0244 0.0147  0.0082  409 PHE A N   
3446 C CA  . PHE A 409 ? 0.3100 0.1854 0.2816 -0.0286 0.0151  0.0066  409 PHE A CA  
3447 C C   . PHE A 409 ? 0.3748 0.2552 0.3467 -0.0361 0.0175  0.0053  409 PHE A C   
3448 O O   . PHE A 409 ? 0.3411 0.2328 0.3169 -0.0380 0.0179  0.0020  409 PHE A O   
3449 C CB  . PHE A 409 ? 0.4043 0.2834 0.3797 -0.0255 0.0135  0.0032  409 PHE A CB  
3450 C CG  . PHE A 409 ? 0.5723 0.4464 0.5474 -0.0302 0.0140  0.0004  409 PHE A CG  
3451 C CD1 . PHE A 409 ? 0.6039 0.4641 0.5762 -0.0299 0.0136  0.0013  409 PHE A CD1 
3452 C CD2 . PHE A 409 ? 0.6612 0.5447 0.6392 -0.0348 0.0149  -0.0032 409 PHE A CD2 
3453 C CE1 . PHE A 409 ? 0.6432 0.4984 0.6154 -0.0341 0.0141  -0.0016 409 PHE A CE1 
3454 C CE2 . PHE A 409 ? 0.6843 0.5630 0.6620 -0.0392 0.0151  -0.0061 409 PHE A CE2 
3455 C CZ  . PHE A 409 ? 0.6870 0.5514 0.6617 -0.0389 0.0148  -0.0054 409 PHE A CZ  
3456 N N   . ASP A 410 ? 0.3588 0.2310 0.3266 -0.0406 0.0189  0.0081  410 ASP A N   
3457 C CA  . ASP A 410 ? 0.4623 0.3373 0.4299 -0.0482 0.0213  0.0078  410 ASP A CA  
3458 C C   . ASP A 410 ? 0.5144 0.4043 0.4846 -0.0495 0.0229  0.0068  410 ASP A C   
3459 O O   . ASP A 410 ? 0.5026 0.3982 0.4744 -0.0557 0.0249  0.0057  410 ASP A O   
3460 C CB  . ASP A 410 ? 0.5473 0.4210 0.5172 -0.0526 0.0213  0.0041  410 ASP A CB  
3461 C CG  . ASP A 410 ? 0.7114 0.5697 0.6787 -0.0523 0.0203  0.0048  410 ASP A CG  
3462 O OD1 . ASP A 410 ? 0.7540 0.6016 0.7174 -0.0514 0.0202  0.0089  410 ASP A OD1 
3463 O OD2 . ASP A 410 ? 0.7550 0.6120 0.7244 -0.0530 0.0195  0.0012  410 ASP A OD2 
3464 N N   . GLY A 411 ? 0.4028 0.2995 0.3741 -0.0437 0.0221  0.0072  411 GLY A N   
3465 C CA  . GLY A 411 ? 0.3409 0.2522 0.3155 -0.0440 0.0235  0.0059  411 GLY A CA  
3466 C C   . GLY A 411 ? 0.3264 0.2497 0.3073 -0.0448 0.0232  0.0017  411 GLY A C   
3467 O O   . GLY A 411 ? 0.3868 0.3223 0.3710 -0.0469 0.0248  0.0004  411 GLY A O   
3468 N N   . ASN A 412 ? 0.3115 0.2323 0.2943 -0.0431 0.0212  -0.0006 412 ASN A N   
3469 C CA  . ASN A 412 ? 0.3517 0.2835 0.3400 -0.0443 0.0206  -0.0045 412 ASN A CA  
3470 C C   . ASN A 412 ? 0.3496 0.2811 0.3398 -0.0382 0.0178  -0.0060 412 ASN A C   
3471 O O   . ASN A 412 ? 0.2860 0.2094 0.2737 -0.0330 0.0164  -0.0039 412 ASN A O   
3472 C CB  . ASN A 412 ? 0.3385 0.2682 0.3269 -0.0520 0.0217  -0.0064 412 ASN A CB  
3473 C CG  . ASN A 412 ? 0.3659 0.2812 0.3508 -0.0528 0.0206  -0.0065 412 ASN A CG  
3474 O OD1 . ASN A 412 ? 0.3571 0.2695 0.3423 -0.0481 0.0186  -0.0078 412 ASN A OD1 
3475 N ND2 . ASN A 412 ? 0.3499 0.2564 0.3319 -0.0587 0.0221  -0.0053 412 ASN A ND2 
3476 N N   . PHE A 413 ? 0.3227 0.2635 0.3173 -0.0388 0.0169  -0.0094 413 PHE A N   
3477 C CA  . PHE A 413 ? 0.2889 0.2330 0.2861 -0.0330 0.0143  -0.0108 413 PHE A CA  
3478 C C   . PHE A 413 ? 0.3031 0.2411 0.2990 -0.0344 0.0132  -0.0132 413 PHE A C   
3479 O O   . PHE A 413 ? 0.2419 0.1839 0.2399 -0.0305 0.0113  -0.0147 413 PHE A O   
3480 C CB  . PHE A 413 ? 0.2314 0.1921 0.2349 -0.0317 0.0138  -0.0126 413 PHE A CB  
3481 C CG  . PHE A 413 ? 0.2799 0.2466 0.2851 -0.0284 0.0145  -0.0105 413 PHE A CG  
3482 C CD1 . PHE A 413 ? 0.2684 0.2342 0.2742 -0.0212 0.0128  -0.0088 413 PHE A CD1 
3483 C CD2 . PHE A 413 ? 0.2719 0.2448 0.2781 -0.0325 0.0169  -0.0104 413 PHE A CD2 
3484 C CE1 . PHE A 413 ? 0.3102 0.2809 0.3174 -0.0181 0.0134  -0.0073 413 PHE A CE1 
3485 C CE2 . PHE A 413 ? 0.3128 0.2912 0.3203 -0.0294 0.0178  -0.0089 413 PHE A CE2 
3486 C CZ  . PHE A 413 ? 0.3101 0.2872 0.3180 -0.0222 0.0159  -0.0076 413 PHE A CZ  
3487 N N   . LEU A 414 ? 0.2529 0.1813 0.2454 -0.0399 0.0144  -0.0136 414 LEU A N   
3488 C CA  . LEU A 414 ? 0.2651 0.1884 0.2567 -0.0421 0.0136  -0.0168 414 LEU A CA  
3489 C C   . LEU A 414 ? 0.2793 0.1940 0.2687 -0.0363 0.0120  -0.0164 414 LEU A C   
3490 O O   . LEU A 414 ? 0.3454 0.2582 0.3344 -0.0367 0.0111  -0.0195 414 LEU A O   
3491 C CB  . LEU A 414 ? 0.2973 0.2112 0.2860 -0.0493 0.0152  -0.0170 414 LEU A CB  
3492 C CG  . LEU A 414 ? 0.3931 0.3159 0.3843 -0.0558 0.0169  -0.0174 414 LEU A CG  
3493 C CD1 . LEU A 414 ? 0.4125 0.3258 0.4014 -0.0632 0.0183  -0.0178 414 LEU A CD1 
3494 C CD2 . LEU A 414 ? 0.3397 0.2777 0.3362 -0.0566 0.0159  -0.0210 414 LEU A CD2 
3495 N N   . LYS A 415 ? 0.3284 0.2384 0.3165 -0.0307 0.0116  -0.0129 415 LYS A N   
3496 C CA  . LYS A 415 ? 0.3968 0.2999 0.3837 -0.0250 0.0101  -0.0124 415 LYS A CA  
3497 C C   . LYS A 415 ? 0.3702 0.2842 0.3608 -0.0204 0.0083  -0.0140 415 LYS A C   
3498 O O   . LYS A 415 ? 0.3535 0.2634 0.3435 -0.0161 0.0072  -0.0143 415 LYS A O   
3499 C CB  . LYS A 415 ? 0.3902 0.2850 0.3749 -0.0205 0.0099  -0.0080 415 LYS A CB  
3500 C CG  . LYS A 415 ? 0.5865 0.4654 0.5669 -0.0218 0.0105  -0.0065 415 LYS A CG  
3501 C CD  . LYS A 415 ? 0.7090 0.5820 0.6888 -0.0217 0.0100  -0.0095 415 LYS A CD  
3502 C CE  . LYS A 415 ? 0.7753 0.6451 0.7555 -0.0144 0.0086  -0.0082 415 LYS A CE  
3503 N NZ  . LYS A 415 ? 0.8094 0.6713 0.7882 -0.0140 0.0085  -0.0108 415 LYS A NZ  
3504 N N   . TRP A 416 ? 0.3154 0.2433 0.3101 -0.0209 0.0081  -0.0150 416 TRP A N   
3505 C CA  . TRP A 416 ? 0.2447 0.1834 0.2434 -0.0162 0.0062  -0.0156 416 TRP A CA  
3506 C C   . TRP A 416 ? 0.3197 0.2712 0.3219 -0.0196 0.0057  -0.0191 416 TRP A C   
3507 O O   . TRP A 416 ? 0.2713 0.2320 0.2767 -0.0160 0.0040  -0.0197 416 TRP A O   
3508 C CB  . TRP A 416 ? 0.2492 0.1932 0.2508 -0.0112 0.0057  -0.0124 416 TRP A CB  
3509 C CG  . TRP A 416 ? 0.3097 0.2421 0.3081 -0.0078 0.0058  -0.0089 416 TRP A CG  
3510 C CD1 . TRP A 416 ? 0.2669 0.1941 0.2651 -0.0018 0.0044  -0.0070 416 TRP A CD1 
3511 C CD2 . TRP A 416 ? 0.2955 0.2201 0.2906 -0.0102 0.0073  -0.0067 416 TRP A CD2 
3512 N NE1 . TRP A 416 ? 0.3043 0.2210 0.2994 -0.0003 0.0047  -0.0038 416 TRP A NE1 
3513 C CE2 . TRP A 416 ? 0.3316 0.2466 0.3245 -0.0054 0.0065  -0.0036 416 TRP A CE2 
3514 C CE3 . TRP A 416 ? 0.2486 0.1740 0.2424 -0.0160 0.0093  -0.0069 416 TRP A CE3 
3515 C CZ2 . TRP A 416 ? 0.3612 0.2672 0.3504 -0.0063 0.0074  -0.0007 416 TRP A CZ2 
3516 C CZ3 . TRP A 416 ? 0.3836 0.3001 0.3734 -0.0169 0.0104  -0.0039 416 TRP A CZ3 
3517 C CH2 . TRP A 416 ? 0.3669 0.2737 0.3543 -0.0120 0.0094  -0.0008 416 TRP A CH2 
3518 N N   . ILE A 417 ? 0.2827 0.2354 0.2846 -0.0265 0.0071  -0.0210 417 ILE A N   
3519 C CA  . ILE A 417 ? 0.3232 0.2886 0.3289 -0.0302 0.0065  -0.0242 417 ILE A CA  
3520 C C   . ILE A 417 ? 0.3905 0.3511 0.3941 -0.0381 0.0080  -0.0265 417 ILE A C   
3521 O O   . ILE A 417 ? 0.3749 0.3254 0.3754 -0.0406 0.0097  -0.0247 417 ILE A O   
3522 C CB  . ILE A 417 ? 0.2776 0.2566 0.2887 -0.0288 0.0065  -0.0229 417 ILE A CB  
3523 C CG1 . ILE A 417 ? 0.2705 0.2640 0.2864 -0.0314 0.0053  -0.0259 417 ILE A CG1 
3524 C CG2 . ILE A 417 ? 0.2522 0.2289 0.2627 -0.0319 0.0089  -0.0209 417 ILE A CG2 
3525 C CD1 . ILE A 417 ? 0.2513 0.2585 0.2734 -0.0274 0.0044  -0.0245 417 ILE A CD1 
3526 N N   . GLY A 418 ? 0.3771 0.3444 0.3823 -0.0421 0.0071  -0.0303 418 GLY A N   
3527 C CA  . GLY A 418 ? 0.3881 0.3531 0.3926 -0.0501 0.0083  -0.0326 418 GLY A CA  
3528 C C   . GLY A 418 ? 0.4469 0.4044 0.4482 -0.0532 0.0075  -0.0365 418 GLY A C   
3529 O O   . GLY A 418 ? 0.6046 0.5621 0.6062 -0.0601 0.0080  -0.0391 418 GLY A O   
3530 N N   . ASN A 419 ? 0.4696 0.4206 0.4678 -0.0486 0.0065  -0.0372 419 ASN A N   
3531 C CA  . ASN A 419 ? 0.4494 0.3952 0.4448 -0.0512 0.0057  -0.0417 419 ASN A CA  
3532 C C   . ASN A 419 ? 0.4433 0.3993 0.4398 -0.0475 0.0034  -0.0439 419 ASN A C   
3533 O O   . ASN A 419 ? 0.4483 0.4134 0.4476 -0.0424 0.0025  -0.0415 419 ASN A O   
3534 C CB  . ASN A 419 ? 0.4734 0.4018 0.4638 -0.0498 0.0067  -0.0412 419 ASN A CB  
3535 C CG  . ASN A 419 ? 0.4519 0.3768 0.4410 -0.0415 0.0062  -0.0384 419 ASN A CG  
3536 O OD1 . ASN A 419 ? 0.4408 0.3753 0.4317 -0.0369 0.0048  -0.0383 419 ASN A OD1 
3537 N ND2 . ASN A 419 ? 0.4739 0.3848 0.4599 -0.0397 0.0074  -0.0360 419 ASN A ND2 
3538 N N   . LYS A 420 ? 0.4222 0.3764 0.4164 -0.0502 0.0025  -0.0486 420 LYS A N   
3539 C CA  . LYS A 420 ? 0.4440 0.4088 0.4387 -0.0478 0.0003  -0.0511 420 LYS A CA  
3540 C C   . LYS A 420 ? 0.4663 0.4313 0.4604 -0.0394 -0.0003 -0.0482 420 LYS A C   
3541 O O   . LYS A 420 ? 0.4246 0.4019 0.4216 -0.0359 -0.0019 -0.0471 420 LYS A O   
3542 C CB  . LYS A 420 ? 0.5406 0.5011 0.5317 -0.0517 -0.0005 -0.0569 420 LYS A CB  
3543 C CG  . LYS A 420 ? 0.6447 0.6173 0.6360 -0.0501 -0.0029 -0.0597 420 LYS A CG  
3544 C CD  . LYS A 420 ? 0.7077 0.6738 0.6939 -0.0521 -0.0034 -0.0653 420 LYS A CD  
3545 C CE  . LYS A 420 ? 0.7555 0.7328 0.7408 -0.0491 -0.0057 -0.0674 420 LYS A CE  
3546 N NZ  . LYS A 420 ? 0.7929 0.7772 0.7804 -0.0416 -0.0061 -0.0624 420 LYS A NZ  
3547 N N   . GLU A 421 ? 0.4131 0.3645 0.4037 -0.0362 0.0010  -0.0466 421 GLU A N   
3548 C CA  . GLU A 421 ? 0.4187 0.3695 0.4086 -0.0285 0.0005  -0.0441 421 GLU A CA  
3549 C C   . GLU A 421 ? 0.3450 0.3018 0.3390 -0.0240 0.0004  -0.0388 421 GLU A C   
3550 O O   . GLU A 421 ? 0.2958 0.2614 0.2922 -0.0189 -0.0011 -0.0371 421 GLU A O   
3551 C CB  . GLU A 421 ? 0.4871 0.4217 0.4727 -0.0265 0.0020  -0.0440 421 GLU A CB  
3552 C CG  . GLU A 421 ? 0.6200 0.5498 0.6014 -0.0281 0.0019  -0.0492 421 GLU A CG  
3553 C CD  . GLU A 421 ? 0.8139 0.7368 0.7936 -0.0358 0.0026  -0.0532 421 GLU A CD  
3554 O OE1 . GLU A 421 ? 0.8526 0.7727 0.8340 -0.0396 0.0036  -0.0513 421 GLU A OE1 
3555 O OE2 . GLU A 421 ? 0.8994 0.8198 0.8762 -0.0380 0.0023  -0.0583 421 GLU A OE2 
3556 N N   . LYS A 422 ? 0.3680 0.3203 0.3630 -0.0258 0.0017  -0.0362 422 LYS A N   
3557 C CA  . LYS A 422 ? 0.3241 0.2819 0.3227 -0.0217 0.0016  -0.0318 422 LYS A CA  
3558 C C   . LYS A 422 ? 0.3270 0.3016 0.3309 -0.0223 0.0002  -0.0322 422 LYS A C   
3559 O O   . LYS A 422 ? 0.3012 0.2834 0.3086 -0.0171 -0.0009 -0.0295 422 LYS A O   
3560 C CB  . LYS A 422 ? 0.3565 0.3061 0.3543 -0.0239 0.0035  -0.0293 422 LYS A CB  
3561 C CG  . LYS A 422 ? 0.3142 0.2475 0.3076 -0.0221 0.0045  -0.0276 422 LYS A CG  
3562 C CD  . LYS A 422 ? 0.2773 0.2033 0.2697 -0.0248 0.0062  -0.0250 422 LYS A CD  
3563 C CE  . LYS A 422 ? 0.3438 0.2530 0.3316 -0.0246 0.0072  -0.0240 422 LYS A CE  
3564 N NZ  . LYS A 422 ? 0.2792 0.1837 0.2664 -0.0174 0.0063  -0.0219 422 LYS A NZ  
3565 N N   . ASN A 423 ? 0.2830 0.2635 0.2879 -0.0286 0.0001  -0.0355 423 ASN A N   
3566 C CA  . ASN A 423 ? 0.2874 0.2841 0.2976 -0.0295 -0.0013 -0.0361 423 ASN A CA  
3567 C C   . ASN A 423 ? 0.3417 0.3470 0.3530 -0.0253 -0.0037 -0.0367 423 ASN A C   
3568 O O   . ASN A 423 ? 0.2949 0.3128 0.3113 -0.0228 -0.0052 -0.0352 423 ASN A O   
3569 C CB  . ASN A 423 ? 0.2241 0.2248 0.2352 -0.0375 -0.0011 -0.0397 423 ASN A CB  
3570 C CG  . ASN A 423 ? 0.4090 0.4066 0.4212 -0.0416 0.0012  -0.0382 423 ASN A CG  
3571 O OD1 . ASN A 423 ? 0.2230 0.2158 0.2351 -0.0384 0.0025  -0.0346 423 ASN A OD1 
3572 N ND2 . ASN A 423 ? 0.3587 0.3589 0.3719 -0.0488 0.0016  -0.0410 423 ASN A ND2 
3573 N N   . GLU A 424 ? 0.3589 0.3576 0.3654 -0.0246 -0.0041 -0.0390 424 GLU A N   
3574 C CA  . GLU A 424 ? 0.3590 0.3654 0.3658 -0.0203 -0.0062 -0.0392 424 GLU A CA  
3575 C C   . GLU A 424 ? 0.3242 0.3329 0.3340 -0.0128 -0.0067 -0.0342 424 GLU A C   
3576 O O   . GLU A 424 ? 0.2364 0.2569 0.2499 -0.0097 -0.0087 -0.0328 424 GLU A O   
3577 C CB  . GLU A 424 ? 0.3748 0.3727 0.3755 -0.0205 -0.0060 -0.0425 424 GLU A CB  
3578 C CG  . GLU A 424 ? 0.4349 0.4399 0.4349 -0.0157 -0.0078 -0.0424 424 GLU A CG  
3579 C CD  . GLU A 424 ? 0.5697 0.5906 0.5728 -0.0178 -0.0103 -0.0440 424 GLU A CD  
3580 O OE1 . GLU A 424 ? 0.6167 0.6409 0.6201 -0.0242 -0.0106 -0.0475 424 GLU A OE1 
3581 O OE2 . GLU A 424 ? 0.6058 0.6362 0.6114 -0.0131 -0.0120 -0.0415 424 GLU A OE2 
3582 N N   . TYR A 425 ? 0.3325 0.3299 0.3408 -0.0100 -0.0051 -0.0314 425 TYR A N   
3583 C CA  . TYR A 425 ? 0.3012 0.3004 0.3126 -0.0032 -0.0058 -0.0268 425 TYR A CA  
3584 C C   . TYR A 425 ? 0.2438 0.2549 0.2617 -0.0029 -0.0066 -0.0249 425 TYR A C   
3585 O O   . TYR A 425 ? 0.2357 0.2553 0.2579 0.0020  -0.0082 -0.0223 425 TYR A O   
3586 C CB  . TYR A 425 ? 0.3108 0.2960 0.3197 -0.0009 -0.0041 -0.0242 425 TYR A CB  
3587 C CG  . TYR A 425 ? 0.3123 0.2884 0.3174 0.0031  -0.0039 -0.0238 425 TYR A CG  
3588 C CD1 . TYR A 425 ? 0.2866 0.2643 0.2889 0.0026  -0.0044 -0.0269 425 TYR A CD1 
3589 C CD2 . TYR A 425 ? 0.3024 0.2686 0.3068 0.0073  -0.0032 -0.0204 425 TYR A CD2 
3590 C CE1 . TYR A 425 ? 0.2389 0.2086 0.2379 0.0064  -0.0039 -0.0266 425 TYR A CE1 
3591 C CE2 . TYR A 425 ? 0.3043 0.2624 0.3058 0.0109  -0.0029 -0.0199 425 TYR A CE2 
3592 C CZ  . TYR A 425 ? 0.2780 0.2380 0.2769 0.0105  -0.0031 -0.0230 425 TYR A CZ  
3593 O OH  . TYR A 425 ? 0.3619 0.3144 0.3582 0.0142  -0.0025 -0.0226 425 TYR A OH  
3594 N N   . TRP A 426 ? 0.2272 0.2392 0.2462 -0.0079 -0.0053 -0.0260 426 TRP A N   
3595 C CA  . TRP A 426 ? 0.2141 0.2378 0.2395 -0.0075 -0.0059 -0.0246 426 TRP A CA  
3596 C C   . TRP A 426 ? 0.2362 0.2747 0.2658 -0.0077 -0.0082 -0.0259 426 TRP A C   
3597 O O   . TRP A 426 ? 0.2028 0.2512 0.2382 -0.0038 -0.0096 -0.0235 426 TRP A O   
3598 C CB  . TRP A 426 ? 0.2768 0.2988 0.3023 -0.0131 -0.0038 -0.0256 426 TRP A CB  
3599 C CG  . TRP A 426 ? 0.2467 0.2572 0.2697 -0.0117 -0.0018 -0.0230 426 TRP A CG  
3600 C CD1 . TRP A 426 ? 0.2930 0.2899 0.3103 -0.0148 0.0000  -0.0235 426 TRP A CD1 
3601 C CD2 . TRP A 426 ? 0.2942 0.3056 0.3200 -0.0069 -0.0017 -0.0196 426 TRP A CD2 
3602 N NE1 . TRP A 426 ? 0.2396 0.2294 0.2560 -0.0122 0.0011  -0.0204 426 TRP A NE1 
3603 C CE2 . TRP A 426 ? 0.2739 0.2723 0.2953 -0.0074 0.0001  -0.0181 426 TRP A CE2 
3604 C CE3 . TRP A 426 ? 0.3195 0.3413 0.3514 -0.0023 -0.0031 -0.0177 426 TRP A CE3 
3605 C CZ2 . TRP A 426 ? 0.2987 0.2945 0.3210 -0.0036 0.0006  -0.0151 426 TRP A CZ2 
3606 C CZ3 . TRP A 426 ? 0.2968 0.3155 0.3300 0.0016  -0.0026 -0.0148 426 TRP A CZ3 
3607 C CH2 . TRP A 426 ? 0.2758 0.2818 0.3040 0.0009  -0.0008 -0.0136 426 TRP A CH2 
3608 N N   . LYS A 427 ? 0.2642 0.3045 0.2911 -0.0122 -0.0088 -0.0296 427 LYS A N   
3609 C CA  . LYS A 427 ? 0.2780 0.3322 0.3082 -0.0124 -0.0114 -0.0308 427 LYS A CA  
3610 C C   . LYS A 427 ? 0.2099 0.2677 0.2412 -0.0055 -0.0132 -0.0279 427 LYS A C   
3611 O O   . LYS A 427 ? 0.2165 0.2869 0.2535 -0.0030 -0.0153 -0.0262 427 LYS A O   
3612 C CB  . LYS A 427 ? 0.3192 0.3729 0.3451 -0.0181 -0.0118 -0.0356 427 LYS A CB  
3613 C CG  . LYS A 427 ? 0.3985 0.4529 0.4251 -0.0255 -0.0107 -0.0384 427 LYS A CG  
3614 C CD  . LYS A 427 ? 0.4604 0.5072 0.4810 -0.0309 -0.0104 -0.0431 427 LYS A CD  
3615 C CE  . LYS A 427 ? 0.5448 0.6036 0.5671 -0.0356 -0.0127 -0.0467 427 LYS A CE  
3616 N NZ  . LYS A 427 ? 0.5766 0.6285 0.5946 -0.0426 -0.0121 -0.0516 427 LYS A NZ  
3617 N N   . ILE A 428 ? 0.2307 0.2776 0.2569 -0.0023 -0.0126 -0.0272 428 ILE A N   
3618 C CA  . ILE A 428 ? 0.2288 0.2785 0.2560 0.0041  -0.0141 -0.0241 428 ILE A CA  
3619 C C   . ILE A 428 ? 0.2604 0.3145 0.2941 0.0091  -0.0147 -0.0196 428 ILE A C   
3620 O O   . ILE A 428 ? 0.2279 0.2922 0.2663 0.0129  -0.0169 -0.0171 428 ILE A O   
3621 C CB  . ILE A 428 ? 0.2756 0.3121 0.2965 0.0064  -0.0128 -0.0241 428 ILE A CB  
3622 C CG1 . ILE A 428 ? 0.2713 0.3062 0.2864 0.0025  -0.0128 -0.0288 428 ILE A CG1 
3623 C CG2 . ILE A 428 ? 0.1819 0.2196 0.2048 0.0137  -0.0139 -0.0198 428 ILE A CG2 
3624 C CD1 . ILE A 428 ? 0.2629 0.2825 0.2716 0.0022  -0.0107 -0.0304 428 ILE A CD1 
3625 N N   . LEU A 429 ? 0.2100 0.2563 0.2441 0.0092  -0.0129 -0.0184 429 LEU A N   
3626 C CA  . LEU A 429 ? 0.1835 0.2329 0.2234 0.0137  -0.0133 -0.0147 429 LEU A CA  
3627 C C   . LEU A 429 ? 0.2321 0.2961 0.2792 0.0127  -0.0146 -0.0147 429 LEU A C   
3628 O O   . LEU A 429 ? 0.2654 0.3368 0.3185 0.0175  -0.0163 -0.0117 429 LEU A O   
3629 C CB  . LEU A 429 ? 0.2466 0.2847 0.2844 0.0131  -0.0110 -0.0140 429 LEU A CB  
3630 C CG  . LEU A 429 ? 0.3100 0.3486 0.3526 0.0181  -0.0113 -0.0104 429 LEU A CG  
3631 C CD1 . LEU A 429 ? 0.2884 0.3227 0.3311 0.0244  -0.0125 -0.0071 429 LEU A CD1 
3632 C CD2 . LEU A 429 ? 0.3253 0.3549 0.3654 0.0160  -0.0089 -0.0105 429 LEU A CD2 
3633 N N   . ILE A 430 ? 0.2362 0.3044 0.2831 0.0066  -0.0139 -0.0180 430 ILE A N   
3634 C CA  . ILE A 430 ? 0.2321 0.3145 0.2863 0.0054  -0.0150 -0.0182 430 ILE A CA  
3635 C C   . ILE A 430 ? 0.3097 0.4041 0.3678 0.0081  -0.0181 -0.0171 430 ILE A C   
3636 O O   . ILE A 430 ? 0.3016 0.4057 0.3670 0.0117  -0.0197 -0.0147 430 ILE A O   
3637 C CB  . ILE A 430 ? 0.2571 0.3415 0.3102 -0.0021 -0.0136 -0.0220 430 ILE A CB  
3638 C CG1 . ILE A 430 ? 0.1975 0.2733 0.2490 -0.0043 -0.0106 -0.0220 430 ILE A CG1 
3639 C CG2 . ILE A 430 ? 0.3347 0.4355 0.3952 -0.0038 -0.0153 -0.0227 430 ILE A CG2 
3640 C CD1 . ILE A 430 ? 0.1818 0.2520 0.2286 -0.0116 -0.0088 -0.0255 430 ILE A CD1 
3641 N N   . GLU A 431 ? 0.3576 0.4514 0.4107 0.0064  -0.0191 -0.0190 431 GLU A N   
3642 C CA  . GLU A 431 ? 0.2837 0.3888 0.3395 0.0088  -0.0222 -0.0178 431 GLU A CA  
3643 C C   . GLU A 431 ? 0.2497 0.3543 0.3081 0.0162  -0.0233 -0.0131 431 GLU A C   
3644 O O   . GLU A 431 ? 0.3036 0.4194 0.3684 0.0194  -0.0258 -0.0104 431 GLU A O   
3645 C CB  . GLU A 431 ? 0.3663 0.4698 0.4151 0.0056  -0.0227 -0.0210 431 GLU A CB  
3646 C CG  . GLU A 431 ? 0.5429 0.6584 0.5934 0.0005  -0.0246 -0.0240 431 GLU A CG  
3647 C CD  . GLU A 431 ? 0.6254 0.7564 0.6833 0.0037  -0.0278 -0.0211 431 GLU A CD  
3648 O OE1 . GLU A 431 ? 0.6185 0.7594 0.6831 0.0018  -0.0286 -0.0212 431 GLU A OE1 
3649 O OE2 . GLU A 431 ? 0.6493 0.7827 0.7066 0.0082  -0.0295 -0.0184 431 GLU A OE2 
3650 N N   . ALA A 432 ? 0.1733 0.2649 0.2273 0.0189  -0.0217 -0.0118 432 ALA A N   
3651 C CA  . ALA A 432 ? 0.2419 0.3324 0.2988 0.0257  -0.0227 -0.0072 432 ALA A CA  
3652 C C   . ALA A 432 ? 0.3503 0.4458 0.4154 0.0290  -0.0233 -0.0044 432 ALA A C   
3653 O O   . ALA A 432 ? 0.3759 0.4774 0.4466 0.0340  -0.0254 -0.0007 432 ALA A O   
3654 C CB  . ALA A 432 ? 0.2020 0.2775 0.2529 0.0276  -0.0208 -0.0066 432 ALA A CB  
3655 N N   . LYS A 433 ? 0.3014 0.3942 0.3674 0.0262  -0.0214 -0.0062 433 LYS A N   
3656 C CA  . LYS A 433 ? 0.2888 0.3860 0.3623 0.0292  -0.0216 -0.0042 433 LYS A CA  
3657 C C   . LYS A 433 ? 0.2909 0.4038 0.3726 0.0303  -0.0242 -0.0032 433 LYS A C   
3658 O O   . LYS A 433 ? 0.3515 0.4691 0.4403 0.0350  -0.0254 -0.0003 433 LYS A O   
3659 C CB  . LYS A 433 ? 0.2401 0.3324 0.3121 0.0252  -0.0188 -0.0067 433 LYS A CB  
3660 C CG  . LYS A 433 ? 0.2742 0.3720 0.3535 0.0274  -0.0186 -0.0056 433 LYS A CG  
3661 C CD  . LYS A 433 ? 0.2284 0.3200 0.3096 0.0337  -0.0191 -0.0022 433 LYS A CD  
3662 C CE  . LYS A 433 ? 0.2570 0.3537 0.3452 0.0359  -0.0188 -0.0018 433 LYS A CE  
3663 N NZ  . LYS A 433 ? 0.3133 0.4044 0.4038 0.0422  -0.0198 0.0014  433 LYS A NZ  
3664 N N   . LYS A 434 ? 0.2803 0.4014 0.3613 0.0260  -0.0251 -0.0055 434 LYS A N   
3665 C CA  . LYS A 434 ? 0.3394 0.4759 0.4281 0.0270  -0.0279 -0.0043 434 LYS A CA  
3666 C C   . LYS A 434 ? 0.3665 0.5070 0.4584 0.0329  -0.0307 0.0000  434 LYS A C   
3667 O O   . LYS A 434 ? 0.3492 0.5001 0.4497 0.0360  -0.0328 0.0026  434 LYS A O   
3668 C CB  . LYS A 434 ? 0.3973 0.5411 0.4837 0.0211  -0.0287 -0.0077 434 LYS A CB  
3669 C CG  . LYS A 434 ? 0.4223 0.5646 0.5071 0.0148  -0.0263 -0.0118 434 LYS A CG  
3670 C CD  . LYS A 434 ? 0.4010 0.5490 0.4828 0.0088  -0.0273 -0.0153 434 LYS A CD  
3671 C CE  . LYS A 434 ? 0.4272 0.5774 0.5104 0.0027  -0.0254 -0.0186 434 LYS A CE  
3672 N NZ  . LYS A 434 ? 0.5535 0.7034 0.6310 -0.0039 -0.0256 -0.0227 434 LYS A NZ  
3673 N N   . LYS A 435 ? 0.3006 0.4331 0.3862 0.0345  -0.0306 0.0011  435 LYS A N   
3674 C CA  . LYS A 435 ? 0.3210 0.4567 0.4086 0.0397  -0.0330 0.0054  435 LYS A CA  
3675 C C   . LYS A 435 ? 0.3852 0.5105 0.4728 0.0449  -0.0322 0.0086  435 LYS A C   
3676 O O   . LYS A 435 ? 0.3668 0.4918 0.4543 0.0488  -0.0335 0.0121  435 LYS A O   
3677 C CB  . LYS A 435 ? 0.4191 0.5558 0.4997 0.0376  -0.0337 0.0042  435 LYS A CB  
3678 C CG  . LYS A 435 ? 0.5434 0.6865 0.6214 0.0312  -0.0338 -0.0003 435 LYS A CG  
3679 C CD  . LYS A 435 ? 0.5765 0.7192 0.6465 0.0291  -0.0343 -0.0021 435 LYS A CD  
3680 C CE  . LYS A 435 ? 0.6218 0.7695 0.6888 0.0223  -0.0345 -0.0071 435 LYS A CE  
3681 N NZ  . LYS A 435 ? 0.6662 0.8102 0.7239 0.0197  -0.0343 -0.0101 435 LYS A NZ  
3682 N N   . ALA A 436 ? 0.3064 0.4510 0.3965 -0.0197 -0.0229 0.0487  436 ALA A N   
3683 C CA  . ALA A 436 ? 0.3195 0.4618 0.4173 -0.0142 -0.0193 0.0511  436 ALA A CA  
3684 C C   . ALA A 436 ? 0.3568 0.5025 0.4654 -0.0099 -0.0165 0.0541  436 ALA A C   
3685 O O   . ALA A 436 ? 0.2964 0.4400 0.4061 -0.0124 -0.0169 0.0517  436 ALA A O   
3686 C CB  . ALA A 436 ? 0.2745 0.4078 0.3729 -0.0179 -0.0191 0.0471  436 ALA A CB  
3687 N N   . LYS A 437 ? 0.2884 0.4312 0.3980 -0.0031 -0.0129 0.0568  437 LYS A N   
3688 C CA  . LYS A 437 ? 0.2997 0.4365 0.4109 0.0005  -0.0099 0.0569  437 LYS A CA  
3689 C C   . LYS A 437 ? 0.3278 0.4539 0.4395 0.0039  -0.0065 0.0552  437 LYS A C   
3690 O O   . LYS A 437 ? 0.2952 0.4157 0.4070 0.0057  -0.0047 0.0543  437 LYS A O   
3691 C CB  . LYS A 437 ? 0.2900 0.4336 0.3998 0.0047  -0.0091 0.0617  437 LYS A CB  
3692 C CG  . LYS A 437 ? 0.2908 0.4447 0.3995 0.0014  -0.0125 0.0632  437 LYS A CG  
3693 C CD  . LYS A 437 ? 0.3767 0.5398 0.4823 0.0057  -0.0124 0.0681  437 LYS A CD  
3694 C CE  . LYS A 437 ? 0.4602 0.6344 0.5628 0.0019  -0.0166 0.0689  437 LYS A CE  
3695 N NZ  . LYS A 437 ? 0.4686 0.6427 0.5623 -0.0020 -0.0201 0.0654  437 LYS A NZ  
3696 N N   . ASN A 438 ? 0.3300 0.4531 0.4414 0.0045  -0.0059 0.0544  438 ASN A N   
3697 C CA  . ASN A 438 ? 0.3447 0.4576 0.4553 0.0077  -0.0028 0.0527  438 ASN A CA  
3698 C C   . ASN A 438 ? 0.3428 0.4524 0.4541 0.0057  -0.0033 0.0506  438 ASN A C   
3699 O O   . ASN A 438 ? 0.2843 0.3998 0.3965 0.0017  -0.0061 0.0508  438 ASN A O   
3700 C CB  . ASN A 438 ? 0.2948 0.4071 0.4032 0.0137  -0.0001 0.0562  438 ASN A CB  
3701 C CG  . ASN A 438 ? 0.3251 0.4450 0.4320 0.0166  -0.0007 0.0597  438 ASN A CG  
3702 O OD1 . ASN A 438 ? 0.3736 0.4923 0.4805 0.0169  -0.0010 0.0590  438 ASN A OD1 
3703 N ND2 . ASN A 438 ? 0.2943 0.4221 0.3992 0.0192  -0.0010 0.0633  438 ASN A ND2 
3704 N N   . ASP A 439 ? 0.2993 0.3996 0.4094 0.0079  -0.0008 0.0485  439 ASP A N   
3705 C CA  . ASP A 439 ? 0.3194 0.4152 0.4303 0.0059  -0.0010 0.0461  439 ASP A CA  
3706 C C   . ASP A 439 ? 0.3143 0.4129 0.4262 0.0081  -0.0010 0.0490  439 ASP A C   
3707 O O   . ASP A 439 ? 0.2653 0.3598 0.3786 0.0065  -0.0011 0.0475  439 ASP A O   
3708 C CB  . ASP A 439 ? 0.3247 0.4100 0.4329 0.0075  0.0013  0.0429  439 ASP A CB  
3709 C CG  . ASP A 439 ? 0.4251 0.5077 0.5319 0.0044  0.0003  0.0387  439 ASP A CG  
3710 O OD1 . ASP A 439 ? 0.4318 0.5194 0.5399 0.0011  -0.0017 0.0378  439 ASP A OD1 
3711 O OD2 . ASP A 439 ? 0.4825 0.5585 0.5888 0.0053  0.0017  0.0390  439 ASP A OD2 
3712 N N   . TYR A 440 ? 0.2404 0.3458 0.3511 0.0123  -0.0009 0.0531  440 TYR A N   
3713 C CA  . TYR A 440 ? 0.1973 0.2886 0.2898 0.0126  -0.0011 0.0492  440 TYR A CA  
3714 C C   . TYR A 440 ? 0.1561 0.2408 0.2376 0.0047  -0.0048 0.0441  440 TYR A C   
3715 O O   . TYR A 440 ? 0.2527 0.3240 0.3203 0.0036  -0.0052 0.0399  440 TYR A O   
3716 C CB  . TYR A 440 ? 0.2314 0.3228 0.3150 0.0179  -0.0002 0.0510  440 TYR A CB  
3717 C CG  . TYR A 440 ? 0.3053 0.3942 0.3918 0.0258  0.0038  0.0535  440 TYR A CG  
3718 C CD1 . TYR A 440 ? 0.2440 0.3192 0.3218 0.0276  0.0052  0.0502  440 TYR A CD1 
3719 C CD2 . TYR A 440 ? 0.2805 0.3802 0.3787 0.0311  0.0061  0.0590  440 TYR A CD2 
3720 C CE1 . TYR A 440 ? 0.2930 0.3658 0.3736 0.0350  0.0089  0.0523  440 TYR A CE1 
3721 C CE2 . TYR A 440 ? 0.2950 0.3856 0.3885 0.0354  0.0096  0.0580  440 TYR A CE2 
3722 C CZ  . TYR A 440 ? 0.3564 0.4382 0.4460 0.0390  0.0111  0.0566  440 TYR A CZ  
3723 O OH  . TYR A 440 ? 0.4561 0.5292 0.5406 0.0419  0.0142  0.0549  440 TYR A OH  
3724 N N   . ILE A 441 ? 0.1583 0.2523 0.2462 -0.0008 -0.0074 0.0444  441 ILE A N   
3725 C CA  . ILE A 441 ? 0.1434 0.2317 0.2230 -0.0087 -0.0107 0.0396  441 ILE A CA  
3726 C C   . ILE A 441 ? 0.2120 0.2922 0.2931 -0.0115 -0.0103 0.0367  441 ILE A C   
3727 O O   . ILE A 441 ? 0.2609 0.3304 0.3302 -0.0163 -0.0121 0.0322  441 ILE A O   
3728 C CB  . ILE A 441 ? 0.1667 0.2674 0.2540 -0.0138 -0.0135 0.0407  441 ILE A CB  
3729 C CG1 . ILE A 441 ? 0.2265 0.3210 0.3008 -0.0211 -0.0171 0.0357  441 ILE A CG1 
3730 C CG2 . ILE A 441 ? 0.2044 0.3145 0.3101 -0.0159 -0.0132 0.0424  441 ILE A CG2 
3731 C CD1 . ILE A 441 ? 0.2543 0.3414 0.3113 -0.0194 -0.0178 0.0339  441 ILE A CD1 
3732 N N   . LEU A 442 ? 0.1575 0.2425 0.2530 -0.0086 -0.0079 0.0392  442 LEU A N   
3733 C CA  . LEU A 442 ? 0.1515 0.2289 0.2481 -0.0110 -0.0074 0.0365  442 LEU A CA  
3734 C C   . LEU A 442 ? 0.1736 0.2359 0.2571 -0.0075 -0.0058 0.0343  442 LEU A C   
3735 O O   . LEU A 442 ? 0.2424 0.2943 0.3188 -0.0112 -0.0066 0.0307  442 LEU A O   
3736 C CB  . LEU A 442 ? 0.1276 0.2137 0.2423 -0.0085 -0.0051 0.0393  442 LEU A CB  
3737 C CG  . LEU A 442 ? 0.2106 0.2974 0.3225 -0.0095 -0.0055 0.0363  442 LEU A CG  
3738 C CD1 . LEU A 442 ? 0.2588 0.3382 0.3679 -0.0055 -0.0028 0.0337  442 LEU A CD1 
3739 C CD2 . LEU A 442 ? 0.1227 0.2097 0.2323 -0.0169 -0.0083 0.0325  442 LEU A CD2 
3740 N N   . VAL A 443 ? 0.1730 0.2341 0.2538 -0.0003 -0.0034 0.0367  443 VAL A N   
3741 C CA  . VAL A 443 ? 0.1347 0.1816 0.2030 0.0033  -0.0019 0.0344  443 VAL A CA  
3742 C C   . VAL A 443 ? 0.1899 0.2255 0.2406 -0.0016 -0.0048 0.0296  443 VAL A C   
3743 O O   . VAL A 443 ? 0.2715 0.2942 0.3133 -0.0031 -0.0051 0.0262  443 VAL A O   
3744 C CB  . VAL A 443 ? 0.1327 0.1814 0.2004 0.0116  0.0008  0.0376  443 VAL A CB  
3745 C CG1 . VAL A 443 ? 0.1869 0.2208 0.2419 0.0152  0.0023  0.0350  443 VAL A CG1 
3746 C CG2 . VAL A 443 ? 0.1335 0.1939 0.2193 0.0165  0.0037  0.0426  443 VAL A CG2 
3747 N N   . ALA A 444 ? 0.2262 0.2664 0.2716 -0.0041 -0.0071 0.0294  444 ALA A N   
3748 C CA  . ALA A 444 ? 0.2403 0.2713 0.2698 -0.0090 -0.0101 0.0248  444 ALA A CA  
3749 C C   . ALA A 444 ? 0.2547 0.2814 0.2833 -0.0170 -0.0126 0.0215  444 ALA A C   
3750 O O   . ALA A 444 ? 0.2914 0.3076 0.3066 -0.0209 -0.0147 0.0172  444 ALA A O   
3751 C CB  . ALA A 444 ? 0.1845 0.2238 0.2109 -0.0100 -0.0119 0.0256  444 ALA A CB  
3752 N N   . GLU A 445 ? 0.1962 0.2310 0.2388 -0.0195 -0.0124 0.0231  445 GLU A N   
3753 C CA  . GLU A 445 ? 0.2485 0.2792 0.2901 -0.0271 -0.0146 0.0199  445 GLU A CA  
3754 C C   . GLU A 445 ? 0.1906 0.2093 0.2288 -0.0267 -0.0133 0.0180  445 GLU A C   
3755 O O   . GLU A 445 ? 0.2088 0.2231 0.2454 -0.0329 -0.0150 0.0154  445 GLU A O   
3756 C CB  . GLU A 445 ? 0.2503 0.2949 0.3079 -0.0308 -0.0152 0.0218  445 GLU A CB  
3757 C CG  . GLU A 445 ? 0.2271 0.2825 0.2867 -0.0329 -0.0173 0.0230  445 GLU A CG  
3758 C CD  . GLU A 445 ? 0.2239 0.2952 0.3020 -0.0338 -0.0172 0.0262  445 GLU A CD  
3759 O OE1 . GLU A 445 ? 0.2330 0.3072 0.3225 -0.0334 -0.0156 0.0271  445 GLU A OE1 
3760 O OE2 . GLU A 445 ? 0.2615 0.3426 0.3428 -0.0349 -0.0187 0.0277  445 GLU A OE2 
3761 N N   . GLY A 446 ? 0.1910 0.2041 0.2276 -0.0197 -0.0105 0.0192  446 GLY A N   
3762 C CA  . GLY A 446 ? 0.2117 0.2128 0.2444 -0.0191 -0.0094 0.0174  446 GLY A CA  
3763 C C   . GLY A 446 ? 0.2376 0.2243 0.2540 -0.0238 -0.0119 0.0128  446 GLY A C   
3764 O O   . GLY A 446 ? 0.2842 0.2669 0.2893 -0.0243 -0.0135 0.0109  446 GLY A O   
3765 N N   . SER A 447 ? 0.2636 0.2425 0.2789 -0.0272 -0.0123 0.0109  447 SER A N   
3766 C CA  . SER A 447 ? 0.2413 0.2067 0.2425 -0.0325 -0.0149 0.0067  447 SER A CA  
3767 C C   . SER A 447 ? 0.3433 0.2960 0.3306 -0.0281 -0.0145 0.0048  447 SER A C   
3768 O O   . SER A 447 ? 0.2821 0.2261 0.2568 -0.0318 -0.0170 0.0014  447 SER A O   
3769 C CB  . SER A 447 ? 0.1862 0.1461 0.1899 -0.0361 -0.0149 0.0058  447 SER A CB  
3770 O OG  . SER A 447 ? 0.2177 0.1730 0.2242 -0.0297 -0.0119 0.0073  447 SER A OG  
3771 N N   . ASP A 448 ? 0.2381 0.1899 0.2279 -0.0202 -0.0114 0.0068  448 ASP A N   
3772 C CA  . ASP A 448 ? 0.2011 0.1400 0.1786 -0.0158 -0.0108 0.0048  448 ASP A CA  
3773 C C   . ASP A 448 ? 0.2048 0.1421 0.1712 -0.0159 -0.0125 0.0027  448 ASP A C   
3774 O O   . ASP A 448 ? 0.2555 0.1803 0.2088 -0.0166 -0.0140 -0.0009 448 ASP A O   
3775 C CB  . ASP A 448 ? 0.2626 0.2031 0.2464 -0.0071 -0.0070 0.0076  448 ASP A CB  
3776 C CG  . ASP A 448 ? 0.2611 0.2040 0.2566 -0.0065 -0.0051 0.0097  448 ASP A CG  
3777 O OD1 . ASP A 448 ? 0.2644 0.2203 0.2731 -0.0076 -0.0045 0.0124  448 ASP A OD1 
3778 O OD2 . ASP A 448 ? 0.2603 0.1924 0.2520 -0.0049 -0.0042 0.0084  448 ASP A OD2 
3779 N N   . TRP A 449 ? 0.2262 0.1763 0.1978 -0.0150 -0.0125 0.0049  449 TRP A N   
3780 C CA  . TRP A 449 ? 0.2087 0.1584 0.1701 -0.0148 -0.0141 0.0030  449 TRP A CA  
3781 C C   . TRP A 449 ? 0.2430 0.1850 0.1938 -0.0225 -0.0179 -0.0014 449 TRP A C   
3782 O O   . TRP A 449 ? 0.2504 0.1841 0.1884 -0.0224 -0.0193 -0.0048 449 TRP A O   
3783 C CB  . TRP A 449 ? 0.2284 0.1943 0.1984 -0.0134 -0.0137 0.0066  449 TRP A CB  
3784 C CG  . TRP A 449 ? 0.2486 0.2239 0.2327 -0.0076 -0.0103 0.0114  449 TRP A CG  
3785 C CD1 . TRP A 449 ? 0.2311 0.2189 0.2302 -0.0090 -0.0097 0.0148  449 TRP A CD1 
3786 C CD2 . TRP A 449 ? 0.2818 0.2546 0.2667 0.0005  -0.0070 0.0132  449 TRP A CD2 
3787 N NE1 . TRP A 449 ? 0.2273 0.2207 0.2367 -0.0022 -0.0062 0.0187  449 TRP A NE1 
3788 C CE2 . TRP A 449 ? 0.2440 0.2283 0.2449 0.0037  -0.0045 0.0179  449 TRP A CE2 
3789 C CE3 . TRP A 449 ? 0.2139 0.1760 0.1879 0.0053  -0.0059 0.0112  449 TRP A CE3 
3790 C CZ2 . TRP A 449 ? 0.2410 0.2263 0.2470 0.0115  -0.0009 0.0206  449 TRP A CZ2 
3791 C CZ3 . TRP A 449 ? 0.1850 0.1482 0.1639 0.0132  -0.0023 0.0139  449 TRP A CZ3 
3792 C CH2 . TRP A 449 ? 0.1930 0.1677 0.1878 0.0162  0.0002  0.0187  449 TRP A CH2 
3793 N N   . PHE A 450 ? 0.2708 0.2153 0.2268 -0.0292 -0.0195 -0.0016 450 PHE A N   
3794 C CA  . PHE A 450 ? 0.2472 0.1850 0.1943 -0.0369 -0.0230 -0.0056 450 PHE A CA  
3795 C C   . PHE A 450 ? 0.3041 0.2256 0.2423 -0.0384 -0.0237 -0.0087 450 PHE A C   
3796 O O   . PHE A 450 ? 0.2767 0.1888 0.2035 -0.0425 -0.0263 -0.0126 450 PHE A O   
3797 C CB  . PHE A 450 ? 0.2536 0.2012 0.2103 -0.0436 -0.0245 -0.0045 450 PHE A CB  
3798 C CG  . PHE A 450 ? 0.2949 0.2587 0.2612 -0.0424 -0.0241 -0.0014 450 PHE A CG  
3799 C CD1 . PHE A 450 ? 0.2664 0.2407 0.2462 -0.0376 -0.0213 0.0030  450 PHE A CD1 
3800 C CD2 . PHE A 450 ? 0.2549 0.2235 0.2167 -0.0461 -0.0267 -0.0030 450 PHE A CD2 
3801 C CE1 . PHE A 450 ? 0.2794 0.2684 0.2683 -0.0365 -0.0211 0.0060  450 PHE A CE1 
3802 C CE2 . PHE A 450 ? 0.2894 0.2729 0.2600 -0.0450 -0.0265 0.0001  450 PHE A CE2 
3803 C CZ  . PHE A 450 ? 0.2640 0.2577 0.2483 -0.0402 -0.0237 0.0047  450 PHE A CZ  
3804 N N   . TRP A 451 ? 0.3190 0.2369 0.2623 -0.0350 -0.0213 -0.0069 451 TRP A N   
3805 C CA  . TRP A 451 ? 0.3235 0.2258 0.2589 -0.0355 -0.0216 -0.0094 451 TRP A CA  
3806 C C   . TRP A 451 ? 0.3980 0.2892 0.3201 -0.0319 -0.0221 -0.0125 451 TRP A C   
3807 O O   . TRP A 451 ? 0.3544 0.2332 0.2662 -0.0355 -0.0243 -0.0162 451 TRP A O   
3808 C CB  . TRP A 451 ? 0.3002 0.2027 0.2445 -0.0309 -0.0185 -0.0065 451 TRP A CB  
3809 C CG  . TRP A 451 ? 0.3663 0.2568 0.3072 -0.0335 -0.0190 -0.0079 451 TRP A CG  
3810 C CD1 . TRP A 451 ? 0.4101 0.3022 0.3569 -0.0391 -0.0198 -0.0073 451 TRP A CD1 
3811 C CD2 . TRP A 451 ? 0.4819 0.3575 0.4134 -0.0305 -0.0188 -0.0100 451 TRP A CD2 
3812 N NE1 . TRP A 451 ? 0.5291 0.4081 0.4703 -0.0399 -0.0201 -0.0087 451 TRP A NE1 
3813 C CE2 . TRP A 451 ? 0.5406 0.4089 0.4724 -0.0346 -0.0195 -0.0104 451 TRP A CE2 
3814 C CE3 . TRP A 451 ? 0.5678 0.4354 0.4905 -0.0248 -0.0181 -0.0117 451 TRP A CE3 
3815 C CZ2 . TRP A 451 ? 0.5231 0.3764 0.4470 -0.0332 -0.0197 -0.0122 451 TRP A CZ2 
3816 C CZ3 . TRP A 451 ? 0.6286 0.4814 0.5437 -0.0233 -0.0183 -0.0138 451 TRP A CZ3 
3817 C CH2 . TRP A 451 ? 0.6282 0.4738 0.5439 -0.0275 -0.0191 -0.0139 451 TRP A CH2 
3818 N N   . TRP A 452 ? 0.3616 0.2574 0.2842 -0.0248 -0.0199 -0.0111 452 TRP A N   
3819 C CA  . TRP A 452 ? 0.3670 0.2530 0.2779 -0.0207 -0.0200 -0.0141 452 TRP A CA  
3820 C C   . TRP A 452 ? 0.4232 0.3098 0.3250 -0.0238 -0.0228 -0.0172 452 TRP A C   
3821 O O   . TRP A 452 ? 0.4309 0.3067 0.3211 -0.0230 -0.0240 -0.0211 452 TRP A O   
3822 C CB  . TRP A 452 ? 0.3172 0.2078 0.2324 -0.0117 -0.0164 -0.0113 452 TRP A CB  
3823 C CG  . TRP A 452 ? 0.3238 0.2109 0.2457 -0.0083 -0.0139 -0.0091 452 TRP A CG  
3824 C CD1 . TRP A 452 ? 0.2866 0.1839 0.2222 -0.0060 -0.0114 -0.0048 452 TRP A CD1 
3825 C CD2 . TRP A 452 ? 0.2807 0.1529 0.1964 -0.0070 -0.0138 -0.0114 452 TRP A CD2 
3826 N NE1 . TRP A 452 ? 0.2903 0.1802 0.2282 -0.0033 -0.0096 -0.0043 452 TRP A NE1 
3827 C CE2 . TRP A 452 ? 0.3016 0.1761 0.2275 -0.0039 -0.0110 -0.0082 452 TRP A CE2 
3828 C CE3 . TRP A 452 ? 0.3636 0.2210 0.2665 -0.0083 -0.0157 -0.0158 452 TRP A CE3 
3829 C CZ2 . TRP A 452 ? 0.3766 0.2391 0.2998 -0.0019 -0.0103 -0.0091 452 TRP A CZ2 
3830 C CZ3 . TRP A 452 ? 0.4084 0.2537 0.3089 -0.0064 -0.0150 -0.0166 452 TRP A CZ3 
3831 C CH2 . TRP A 452 ? 0.4333 0.2811 0.3437 -0.0032 -0.0123 -0.0133 452 TRP A CH2 
3832 N N   . GLN A 453 ? 0.4047 0.3033 0.3114 -0.0273 -0.0239 -0.0159 453 GLN A N   
3833 C CA  . GLN A 453 ? 0.4510 0.3517 0.3497 -0.0296 -0.0263 -0.0187 453 GLN A CA  
3834 C C   . GLN A 453 ? 0.4277 0.3165 0.3162 -0.0364 -0.0298 -0.0236 453 GLN A C   
3835 O O   . GLN A 453 ? 0.4234 0.3084 0.3143 -0.0420 -0.0309 -0.0238 453 GLN A O   
3836 C CB  . GLN A 453 ? 0.4140 0.3308 0.3213 -0.0320 -0.0267 -0.0159 453 GLN A CB  
3837 C CG  . GLN A 453 ? 0.4807 0.4002 0.3806 -0.0361 -0.0298 -0.0189 453 GLN A CG  
3838 C CD  . GLN A 453 ? 0.5424 0.4639 0.4355 -0.0304 -0.0291 -0.0197 453 GLN A CD  
3839 O OE1 . GLN A 453 ? 0.4165 0.3353 0.3088 -0.0234 -0.0265 -0.0187 453 GLN A OE1 
3840 N NE2 . GLN A 453 ? 0.4936 0.4201 0.3816 -0.0333 -0.0315 -0.0217 453 GLN A NE2 
3841 N N   . GLY A 454 ? 0.5405 0.4235 0.4177 -0.0358 -0.0314 -0.0276 454 GLY A N   
3842 C CA  . GLY A 454 ? 0.6370 0.5094 0.5048 -0.0423 -0.0348 -0.0323 454 GLY A CA  
3843 C C   . GLY A 454 ? 0.7970 0.6543 0.6608 -0.0435 -0.0352 -0.0341 454 GLY A C   
3844 O O   . GLY A 454 ? 0.8060 0.6552 0.6649 -0.0501 -0.0379 -0.0369 454 GLY A O   
3845 N N   . GLU A 455 ? 0.9342 0.7874 0.8003 -0.0374 -0.0324 -0.0322 455 GLU A N   
3846 C CA  . GLU A 455 ? 1.0382 0.8761 0.8993 -0.0371 -0.0326 -0.0341 455 GLU A CA  
3847 C C   . GLU A 455 ? 1.1508 0.9812 1.0035 -0.0307 -0.0319 -0.0369 455 GLU A C   
3848 O O   . GLU A 455 ? 1.1547 0.9928 1.0100 -0.0242 -0.0294 -0.0351 455 GLU A O   
3849 C CB  . GLU A 455 ? 1.0270 0.8658 0.8977 -0.0350 -0.0300 -0.0300 455 GLU A CB  
3850 C CG  . GLU A 455 ? 1.0120 0.8614 0.8932 -0.0399 -0.0300 -0.0268 455 GLU A CG  
3851 C CD  . GLU A 455 ? 0.9972 0.8391 0.8758 -0.0481 -0.0327 -0.0285 455 GLU A CD  
3852 O OE1 . GLU A 455 ? 0.9200 0.7704 0.8058 -0.0534 -0.0334 -0.0268 455 GLU A OE1 
3853 O OE2 . GLU A 455 ? 1.0357 0.8632 0.9054 -0.0494 -0.0343 -0.0316 455 GLU A OE2 
3854 N N   . GLU A 456 ? 1.2359 1.0520 1.0787 -0.0328 -0.0342 -0.0414 456 GLU A N   
3855 C CA  . GLU A 456 ? 1.3289 1.1336 1.1642 -0.0274 -0.0336 -0.0443 456 GLU A CA  
3856 C C   . GLU A 456 ? 1.3580 1.1696 1.1972 -0.0186 -0.0300 -0.0418 456 GLU A C   
3857 O O   . GLU A 456 ? 1.3550 1.1709 1.2031 -0.0156 -0.0273 -0.0375 456 GLU A O   
3858 C CB  . GLU A 456 ? 1.3591 1.1498 1.1933 -0.0291 -0.0342 -0.0448 456 GLU A CB  
3859 C CG  . GLU A 456 ? 1.3999 1.1782 1.2280 -0.0234 -0.0334 -0.0473 456 GLU A CG  
3860 C CD  . GLU A 456 ? 1.4293 1.2121 1.2638 -0.0155 -0.0294 -0.0437 456 GLU A CD  
3861 O OE1 . GLU A 456 ? 1.4257 1.2121 1.2689 -0.0157 -0.0277 -0.0395 456 GLU A OE1 
3862 O OE2 . GLU A 456 ? 1.4415 1.2247 1.2726 -0.0091 -0.0280 -0.0451 456 GLU A OE2 
3863 N N   . LYS A 457 ? 1.3503 1.1634 1.1833 -0.0145 -0.0299 -0.0443 457 LYS A N   
3864 C CA  . LYS A 457 ? 1.2941 1.1161 1.1310 -0.0067 -0.0265 -0.0416 457 LYS A CA  
3865 C C   . LYS A 457 ? 1.2615 1.0735 1.0963 -0.0004 -0.0245 -0.0424 457 LYS A C   
3866 O O   . LYS A 457 ? 1.2855 1.0865 1.1110 0.0007  -0.0259 -0.0471 457 LYS A O   
3867 C CB  . LYS A 457 ? 1.2694 1.0993 1.1012 -0.0052 -0.0272 -0.0437 457 LYS A CB  
3868 C CG  . LYS A 457 ? 1.2425 1.0852 1.0788 -0.0103 -0.0285 -0.0416 457 LYS A CG  
3869 C CD  . LYS A 457 ? 1.2278 1.0835 1.0767 -0.0079 -0.0255 -0.0353 457 LYS A CD  
3870 C CE  . LYS A 457 ? 1.2354 1.0970 1.0861 0.0007  -0.0222 -0.0332 457 LYS A CE  
3871 N NZ  . LYS A 457 ? 1.2174 1.0837 1.0792 0.0047  -0.0188 -0.0279 457 LYS A NZ  
3872 N N   . ALA A 458 ? 1.1885 1.0047 1.0323 0.0037  -0.0213 -0.0379 458 ALA A N   
3873 C CA  . ALA A 458 ? 1.1469 0.9551 0.9910 0.0098  -0.0190 -0.0377 458 ALA A CA  
3874 C C   . ALA A 458 ? 1.0885 0.9076 0.9378 0.0175  -0.0153 -0.0345 458 ALA A C   
3875 O O   . ALA A 458 ? 1.0737 0.9067 0.9279 0.0173  -0.0147 -0.0318 458 ALA A O   
3876 C CB  . ALA A 458 ? 1.1427 0.9460 0.9933 0.0076  -0.0185 -0.0351 458 ALA A CB  
3877 N N   . PRO A 459 ? 1.0408 0.8544 0.8895 0.0242  -0.0130 -0.0347 459 PRO A N   
3878 C CA  . PRO A 459 ? 0.9910 0.8151 0.8450 0.0315  -0.0093 -0.0315 459 PRO A CA  
3879 C C   . PRO A 459 ? 0.9249 0.7628 0.7919 0.0312  -0.0073 -0.0254 459 PRO A C   
3880 O O   . PRO A 459 ? 0.9259 0.7628 0.7996 0.0280  -0.0074 -0.0232 459 PRO A O   
3881 C CB  . PRO A 459 ? 1.0118 0.8257 0.8647 0.0376  -0.0073 -0.0324 459 PRO A CB  
3882 C CG  . PRO A 459 ? 1.0218 0.8195 0.8682 0.0333  -0.0100 -0.0362 459 PRO A CG  
3883 C CD  . PRO A 459 ? 1.0373 0.8344 0.8785 0.0256  -0.0138 -0.0387 459 PRO A CD  
3884 N N   . PHE A 460 ? 0.8602 0.7115 0.7309 0.0346  -0.0056 -0.0227 460 PHE A N   
3885 C CA  . PHE A 460 ? 0.7696 0.6353 0.6532 0.0360  -0.0032 -0.0168 460 PHE A CA  
3886 C C   . PHE A 460 ? 0.7108 0.5837 0.6003 0.0287  -0.0052 -0.0149 460 PHE A C   
3887 O O   . PHE A 460 ? 0.6985 0.5836 0.5993 0.0294  -0.0035 -0.0101 460 PHE A O   
3888 C CB  . PHE A 460 ? 0.7332 0.5975 0.6256 0.0408  0.0001  -0.0136 460 PHE A CB  
3889 C CG  . PHE A 460 ? 0.7735 0.6294 0.6605 0.0477  0.0020  -0.0157 460 PHE A CG  
3890 C CD1 . PHE A 460 ? 0.8025 0.6656 0.6892 0.0540  0.0044  -0.0146 460 PHE A CD1 
3891 C CD2 . PHE A 460 ? 0.8282 0.6691 0.7104 0.0478  0.0015  -0.0187 460 PHE A CD2 
3892 C CE1 . PHE A 460 ? 0.8526 0.7082 0.7343 0.0603  0.0062  -0.0167 460 PHE A CE1 
3893 C CE2 . PHE A 460 ? 0.8658 0.6989 0.7431 0.0542  0.0032  -0.0209 460 PHE A CE2 
3894 C CZ  . PHE A 460 ? 0.8635 0.7040 0.7406 0.0604  0.0055  -0.0200 460 PHE A CZ  
3895 N N   . VAL A 461 ? 0.6663 0.5321 0.5488 0.0218  -0.0088 -0.0186 461 VAL A N   
3896 C CA  . VAL A 461 ? 0.6243 0.4979 0.5121 0.0150  -0.0107 -0.0169 461 VAL A CA  
3897 C C   . VAL A 461 ? 0.5744 0.4613 0.4629 0.0149  -0.0111 -0.0156 461 VAL A C   
3898 O O   . VAL A 461 ? 0.5458 0.4436 0.4423 0.0114  -0.0116 -0.0127 461 VAL A O   
3899 C CB  . VAL A 461 ? 0.7091 0.5715 0.5894 0.0075  -0.0144 -0.0211 461 VAL A CB  
3900 C CG1 . VAL A 461 ? 0.7165 0.5867 0.6038 0.0004  -0.0160 -0.0191 461 VAL A CG1 
3901 C CG2 . VAL A 461 ? 0.7184 0.5665 0.5964 0.0083  -0.0140 -0.0226 461 VAL A CG2 
3902 N N   . GLU A 462 ? 0.4408 0.3277 0.3213 0.0189  -0.0109 -0.0178 462 GLU A N   
3903 C CA  . GLU A 462 ? 0.4084 0.3090 0.2902 0.0203  -0.0107 -0.0158 462 GLU A CA  
3904 C C   . GLU A 462 ? 0.3950 0.3089 0.2900 0.0246  -0.0074 -0.0094 462 GLU A C   
3905 O O   . GLU A 462 ? 0.4573 0.3844 0.3572 0.0240  -0.0075 -0.0065 462 GLU A O   
3906 C CB  . GLU A 462 ? 0.5376 0.4355 0.4087 0.0246  -0.0106 -0.0192 462 GLU A CB  
3907 C CG  . GLU A 462 ? 0.7152 0.6046 0.5740 0.0198  -0.0143 -0.0253 462 GLU A CG  
3908 C CD  . GLU A 462 ? 0.8633 0.7468 0.7114 0.0246  -0.0141 -0.0295 462 GLU A CD  
3909 O OE1 . GLU A 462 ? 0.9190 0.8108 0.7685 0.0306  -0.0116 -0.0273 462 GLU A OE1 
3910 O OE2 . GLU A 462 ? 0.9042 0.7749 0.7427 0.0222  -0.0164 -0.0350 462 GLU A OE2 
3911 N N   . VAL A 463 ? 0.4094 0.3202 0.3107 0.0292  -0.0045 -0.0072 463 VAL A N   
3912 C CA  . VAL A 463 ? 0.3664 0.2896 0.2810 0.0334  -0.0014 -0.0013 463 VAL A CA  
3913 C C   . VAL A 463 ? 0.3273 0.2589 0.2527 0.0279  -0.0024 0.0018  463 VAL A C   
3914 O O   . VAL A 463 ? 0.3202 0.2657 0.2555 0.0290  -0.0012 0.0062  463 VAL A O   
3915 C CB  . VAL A 463 ? 0.3235 0.2405 0.2419 0.0394  0.0019  -0.0001 463 VAL A CB  
3916 C CG1 . VAL A 463 ? 0.3018 0.2317 0.2352 0.0435  0.0051  0.0060  463 VAL A CG1 
3917 C CG2 . VAL A 463 ? 0.3081 0.2176 0.2160 0.0450  0.0029  -0.0032 463 VAL A CG2 
3918 N N   . PHE A 464 ? 0.3029 0.2265 0.2271 0.0219  -0.0045 -0.0006 464 PHE A N   
3919 C CA  . PHE A 464 ? 0.3386 0.2701 0.2723 0.0161  -0.0057 0.0016  464 PHE A CA  
3920 C C   . PHE A 464 ? 0.2582 0.1998 0.1908 0.0123  -0.0080 0.0018  464 PHE A C   
3921 O O   . PHE A 464 ? 0.3138 0.2677 0.2572 0.0104  -0.0079 0.0054  464 PHE A O   
3922 C CB  . PHE A 464 ? 0.3246 0.2448 0.2550 0.0100  -0.0079 -0.0015 464 PHE A CB  
3923 C CG  . PHE A 464 ? 0.3257 0.2393 0.2612 0.0128  -0.0056 -0.0005 464 PHE A CG  
3924 C CD1 . PHE A 464 ? 0.4142 0.3146 0.3413 0.0166  -0.0049 -0.0032 464 PHE A CD1 
3925 C CD2 . PHE A 464 ? 0.3082 0.2292 0.2571 0.0119  -0.0043 0.0030  464 PHE A CD2 
3926 C CE1 . PHE A 464 ? 0.4116 0.3059 0.3432 0.0193  -0.0029 -0.0023 464 PHE A CE1 
3927 C CE2 . PHE A 464 ? 0.3520 0.2673 0.3056 0.0146  -0.0023 0.0038  464 PHE A CE2 
3928 C CZ  . PHE A 464 ? 0.3122 0.2140 0.2570 0.0184  -0.0015 0.0012  464 PHE A CZ  
3929 N N   . ASP A 465 ? 0.2992 0.2359 0.2191 0.0110  -0.0101 -0.0022 465 ASP A N   
3930 C CA  . ASP A 465 ? 0.2540 0.2003 0.1725 0.0075  -0.0123 -0.0022 465 ASP A CA  
3931 C C   . ASP A 465 ? 0.3157 0.2759 0.2406 0.0131  -0.0101 0.0024  465 ASP A C   
3932 O O   . ASP A 465 ? 0.2676 0.2403 0.1993 0.0107  -0.0109 0.0052  465 ASP A O   
3933 C CB  . ASP A 465 ? 0.3042 0.2417 0.2075 0.0050  -0.0151 -0.0079 465 ASP A CB  
3934 C CG  . ASP A 465 ? 0.3285 0.2763 0.2294 0.0027  -0.0171 -0.0080 465 ASP A CG  
3935 O OD1 . ASP A 465 ? 0.3377 0.2899 0.2416 -0.0038 -0.0195 -0.0081 465 ASP A OD1 
3936 O OD2 . ASP A 465 ? 0.3719 0.3239 0.2683 0.0074  -0.0162 -0.0078 465 ASP A OD2 
3937 N N   . LYS A 466 ? 0.2580 0.2164 0.1811 0.0204  -0.0073 0.0033  466 LYS A N   
3938 C CA  . LYS A 466 ? 0.3047 0.2762 0.2346 0.0261  -0.0048 0.0082  466 LYS A CA  
3939 C C   . LYS A 466 ? 0.2829 0.2651 0.2294 0.0264  -0.0031 0.0138  466 LYS A C   
3940 O O   . LYS A 466 ? 0.3041 0.3001 0.2582 0.0272  -0.0028 0.0180  466 LYS A O   
3941 C CB  . LYS A 466 ? 0.4020 0.3679 0.3272 0.0338  -0.0019 0.0078  466 LYS A CB  
3942 C CG  . LYS A 466 ? 0.5354 0.5132 0.4706 0.0405  0.0016  0.0137  466 LYS A CG  
3943 C CD  . LYS A 466 ? 0.6666 0.6546 0.5978 0.0423  0.0012  0.0149  466 LYS A CD  
3944 C CE  . LYS A 466 ? 0.7631 0.7658 0.7068 0.0470  0.0040  0.0218  466 LYS A CE  
3945 N NZ  . LYS A 466 ? 0.7985 0.8137 0.7413 0.0460  0.0026  0.0238  466 LYS A NZ  
3946 N N   . LEU A 467 ? 0.2564 0.2327 0.2090 0.0259  -0.0020 0.0140  467 LEU A N   
3947 C CA  . LEU A 467 ? 0.2054 0.1915 0.1743 0.0264  -0.0003 0.0189  467 LEU A CA  
3948 C C   . LEU A 467 ? 0.2563 0.2509 0.2312 0.0194  -0.0030 0.0197  467 LEU A C   
3949 O O   . LEU A 467 ? 0.2471 0.2554 0.2337 0.0201  -0.0024 0.0242  467 LEU A O   
3950 C CB  . LEU A 467 ? 0.1860 0.1632 0.1590 0.0273  0.0012  0.0183  467 LEU A CB  
3951 C CG  . LEU A 467 ? 0.2702 0.2425 0.2431 0.0352  0.0048  0.0193  467 LEU A CG  
3952 C CD1 . LEU A 467 ? 0.2311 0.1909 0.2033 0.0348  0.0053  0.0170  467 LEU A CD1 
3953 C CD2 . LEU A 467 ? 0.2934 0.2791 0.2806 0.0404  0.0078  0.0252  467 LEU A CD2 
3954 N N   . PHE A 468 ? 0.2506 0.2373 0.2180 0.0126  -0.0061 0.0153  468 PHE A N   
3955 C CA  . PHE A 468 ? 0.2304 0.2246 0.2029 0.0057  -0.0088 0.0156  468 PHE A CA  
3956 C C   . PHE A 468 ? 0.2734 0.2801 0.2468 0.0060  -0.0097 0.0178  468 PHE A C   
3957 O O   . PHE A 468 ? 0.2476 0.2671 0.2333 0.0052  -0.0096 0.0218  468 PHE A O   
3958 C CB  . PHE A 468 ? 0.2613 0.2444 0.2233 -0.0014 -0.0121 0.0102  468 PHE A CB  
3959 C CG  . PHE A 468 ? 0.3021 0.2924 0.2671 -0.0087 -0.0151 0.0098  468 PHE A CG  
3960 C CD1 . PHE A 468 ? 0.3012 0.2976 0.2784 -0.0125 -0.0153 0.0117  468 PHE A CD1 
3961 C CD2 . PHE A 468 ? 0.1933 0.1845 0.1489 -0.0119 -0.0179 0.0072  468 PHE A CD2 
3962 C CE1 . PHE A 468 ? 0.2759 0.2789 0.2560 -0.0194 -0.0181 0.0111  468 PHE A CE1 
3963 C CE2 . PHE A 468 ? 0.3015 0.2992 0.2598 -0.0187 -0.0207 0.0066  468 PHE A CE2 
3964 C CZ  . PHE A 468 ? 0.2642 0.2678 0.2348 -0.0225 -0.0208 0.0085  468 PHE A CZ  
3965 N N   . ARG A 469 ? 0.2994 0.3027 0.2602 0.0075  -0.0106 0.0153  469 ARG A N   
3966 C CA  . ARG A 469 ? 0.3098 0.3245 0.2700 0.0074  -0.0118 0.0170  469 ARG A CA  
3967 C C   . ARG A 469 ? 0.3558 0.3832 0.3268 0.0138  -0.0089 0.0231  469 ARG A C   
3968 O O   . ARG A 469 ? 0.3072 0.3473 0.2838 0.0129  -0.0097 0.0263  469 ARG A O   
3969 C CB  . ARG A 469 ? 0.2665 0.2743 0.2104 0.0077  -0.0133 0.0125  469 ARG A CB  
3970 C CG  . ARG A 469 ? 0.2839 0.2804 0.2176 0.0009  -0.0166 0.0065  469 ARG A CG  
3971 C CD  . ARG A 469 ? 0.3327 0.3225 0.2508 0.0015  -0.0181 0.0017  469 ARG A CD  
3972 N NE  . ARG A 469 ? 0.3294 0.3083 0.2379 -0.0051 -0.0214 -0.0041 469 ARG A NE  
3973 C CZ  . ARG A 469 ? 0.3606 0.3430 0.2656 -0.0109 -0.0246 -0.0063 469 ARG A CZ  
3974 N NH1 . ARG A 469 ? 0.2733 0.2699 0.1836 -0.0111 -0.0251 -0.0031 469 ARG A NH1 
3975 N NH2 . ARG A 469 ? 0.3531 0.3247 0.2495 -0.0166 -0.0274 -0.0116 469 ARG A NH2 
3976 N N   . SER A 470 ? 0.3087 0.3329 0.2828 0.0201  -0.0055 0.0250  470 SER A N   
3977 C CA  . SER A 470 ? 0.3059 0.3421 0.2917 0.0261  -0.0026 0.0312  470 SER A CA  
3978 C C   . SER A 470 ? 0.2167 0.2630 0.2195 0.0239  -0.0024 0.0352  470 SER A C   
3979 O O   . SER A 470 ? 0.2390 0.2989 0.2516 0.0256  -0.0018 0.0401  470 SER A O   
3980 C CB  . SER A 470 ? 0.3174 0.3471 0.3028 0.0331  0.0010  0.0318  470 SER A CB  
3981 O OG  . SER A 470 ? 0.3946 0.4189 0.3665 0.0366  0.0013  0.0293  470 SER A OG  
3982 N N   . PHE A 471 ? 0.2164 0.2565 0.2233 0.0204  -0.0027 0.0334  471 PHE A N   
3983 C CA  . PHE A 471 ? 0.2109 0.2605 0.2339 0.0178  -0.0027 0.0365  471 PHE A CA  
3984 C C   . PHE A 471 ? 0.2597 0.3185 0.2848 0.0118  -0.0060 0.0367  471 PHE A C   
3985 O O   . PHE A 471 ? 0.2443 0.3162 0.2831 0.0117  -0.0058 0.0410  471 PHE A O   
3986 C CB  . PHE A 471 ? 0.2347 0.2752 0.2600 0.0148  -0.0026 0.0339  471 PHE A CB  
3987 C CG  . PHE A 471 ? 0.3202 0.3533 0.3468 0.0208  0.0008  0.0344  471 PHE A CG  
3988 C CD1 . PHE A 471 ? 0.3603 0.4013 0.3972 0.0277  0.0041  0.0392  471 PHE A CD1 
3989 C CD2 . PHE A 471 ? 0.2328 0.2513 0.2506 0.0196  0.0006  0.0301  471 PHE A CD2 
3990 C CE1 . PHE A 471 ? 0.3659 0.4001 0.4040 0.0333  0.0072  0.0395  471 PHE A CE1 
3991 C CE2 . PHE A 471 ? 0.2419 0.2537 0.2608 0.0251  0.0036  0.0305  471 PHE A CE2 
3992 C CZ  . PHE A 471 ? 0.2631 0.2827 0.2921 0.0320  0.0069  0.0350  471 PHE A CZ  
3993 N N   . VAL A 472 ? 0.2925 0.3447 0.3043 0.0068  -0.0090 0.0320  472 VAL A N   
3994 C CA  . VAL A 472 ? 0.2988 0.3591 0.3116 0.0009  -0.0122 0.0318  472 VAL A CA  
3995 C C   . VAL A 472 ? 0.2945 0.3673 0.3098 0.0045  -0.0119 0.0359  472 VAL A C   
3996 O O   . VAL A 472 ? 0.2751 0.3603 0.3007 0.0023  -0.0131 0.0390  472 VAL A O   
3997 C CB  . VAL A 472 ? 0.3683 0.4180 0.3658 -0.0050 -0.0154 0.0256  472 VAL A CB  
3998 C CG1 . VAL A 472 ? 0.4426 0.5005 0.4368 -0.0087 -0.0184 0.0252  472 VAL A CG1 
3999 C CG2 . VAL A 472 ? 0.3238 0.3669 0.3238 -0.0110 -0.0166 0.0227  472 VAL A CG2 
4000 N N   . ARG A 473 ? 0.2819 0.3520 0.2885 0.0101  -0.0103 0.0362  473 ARG A N   
4001 C CA  . ARG A 473 ? 0.3326 0.4148 0.3414 0.0140  -0.0098 0.0405  473 ARG A CA  
4002 C C   . ARG A 473 ? 0.3210 0.4149 0.3475 0.0181  -0.0072 0.0471  473 ARG A C   
4003 O O   . ARG A 473 ? 0.3935 0.5005 0.4288 0.0176  -0.0081 0.0512  473 ARG A O   
4004 C CB  . ARG A 473 ? 0.3985 0.4748 0.3942 0.0193  -0.0084 0.0391  473 ARG A CB  
4005 C CG  . ARG A 473 ? 0.5212 0.6085 0.5143 0.0216  -0.0089 0.0419  473 ARG A CG  
4006 C CD  . ARG A 473 ? 0.6020 0.6893 0.5913 0.0295  -0.0057 0.0441  473 ARG A CD  
4007 N NE  . ARG A 473 ? 0.6789 0.7766 0.6646 0.0314  -0.0063 0.0465  473 ARG A NE  
4008 C CZ  . ARG A 473 ? 0.7385 0.8330 0.7104 0.0339  -0.0063 0.0439  473 ARG A CZ  
4009 N NH1 . ARG A 473 ? 0.7270 0.8076 0.6877 0.0349  -0.0058 0.0386  473 ARG A NH1 
4010 N NH2 . ARG A 473 ? 0.7628 0.8681 0.7324 0.0354  -0.0069 0.0465  473 ARG A NH2 
4011 N N   . ARG A 474 ? 0.3155 0.4048 0.3479 0.0222  -0.0042 0.0483  474 ARG A N   
4012 C CA  . ARG A 474 ? 0.3221 0.4220 0.3719 0.0264  -0.0016 0.0543  474 ARG A CA  
4013 C C   . ARG A 474 ? 0.3044 0.4134 0.3686 0.0214  -0.0033 0.0560  474 ARG A C   
4014 O O   . ARG A 474 ? 0.3320 0.4541 0.4100 0.0233  -0.0027 0.0613  474 ARG A O   
4015 C CB  . ARG A 474 ? 0.3526 0.4444 0.4050 0.0313  0.0018  0.0543  474 ARG A CB  
4016 C CG  . ARG A 474 ? 0.4299 0.5317 0.5011 0.0353  0.0045  0.0600  474 ARG A CG  
4017 C CD  . ARG A 474 ? 0.5381 0.6484 0.6124 0.0422  0.0069  0.0653  474 ARG A CD  
4018 N NE  . ARG A 474 ? 0.6440 0.7535 0.7286 0.0441  0.0102  0.0670  474 ARG A NE  
4019 C CZ  . ARG A 474 ? 0.6977 0.8080 0.7872 0.0395  0.0104  0.0669  474 ARG A CZ  
4020 N NH1 . ARG A 474 ? 0.6702 0.7894 0.7630 0.0361  0.0078  0.0685  474 ARG A NH1 
4021 N NH2 . ARG A 474 ? 0.6875 0.7891 0.7775 0.0384  0.0126  0.0648  474 ARG A NH2 
4022 N N   . ALA A 475 ? 0.3448 0.4473 0.4063 0.0149  -0.0056 0.0515  475 ALA A N   
4023 C CA  . ALA A 475 ? 0.2568 0.3675 0.3313 0.0096  -0.0074 0.0523  475 ALA A CA  
4024 C C   . ALA A 475 ? 0.3186 0.4423 0.3974 0.0073  -0.0097 0.0550  475 ALA A C   
4025 O O   . ALA A 475 ? 0.3687 0.5026 0.4621 0.0049  -0.0106 0.0574  475 ALA A O   
4026 C CB  . ALA A 475 ? 0.1814 0.2822 0.2491 0.0025  -0.0098 0.0465  475 ALA A CB  
4027 N N   . GLN A 476 ? 0.3420 0.4659 0.4089 0.0081  -0.0109 0.0546  476 GLN A N   
4028 C CA  . GLN A 476 ? 0.3677 0.5034 0.4371 0.0056  -0.0134 0.0568  476 GLN A CA  
4029 C C   . GLN A 476 ? 0.4359 0.5831 0.5125 0.0119  -0.0115 0.0633  476 GLN A C   
4030 O O   . GLN A 476 ? 0.4886 0.6461 0.5670 0.0106  -0.0135 0.0657  476 GLN A O   
4031 C CB  . GLN A 476 ? 0.3011 0.4305 0.3529 0.0016  -0.0163 0.0518  476 GLN A CB  
4032 C CG  . GLN A 476 ? 0.3641 0.4820 0.4086 -0.0049 -0.0183 0.0455  476 GLN A CG  
4033 C CD  . GLN A 476 ? 0.4266 0.5362 0.4528 -0.0081 -0.0208 0.0401  476 GLN A CD  
4034 O OE1 . GLN A 476 ? 0.5700 0.6854 0.5935 -0.0120 -0.0237 0.0394  476 GLN A OE1 
4035 N NE2 . GLN A 476 ? 0.2973 0.3933 0.3113 -0.0065 -0.0198 0.0363  476 GLN A NE2 
4036 N N   . GLU A 477 ? 0.4059 0.5521 0.4873 0.0185  -0.0078 0.0664  477 GLU A N   
4037 C CA  . GLU A 477 ? 0.4333 0.5902 0.5220 0.0248  -0.0057 0.0729  477 GLU A CA  
4038 C C   . GLU A 477 ? 0.4518 0.6034 0.5502 0.0246  -0.0025 0.0733  477 GLU A C   
4039 O O   . GLU A 477 ? 0.4325 0.5753 0.5337 0.0228  -0.0016 0.0701  477 GLU A O   
4040 C CB  . GLU A 477 ? 0.4317 0.5814 0.5089 0.0310  -0.0030 0.0726  477 GLU A CB  
4041 C CG  . GLU A 477 ? 0.5658 0.7116 0.6248 0.0299  -0.0049 0.0693  477 GLU A CG  
4042 C CD  . GLU A 477 ? 0.6744 0.8081 0.7195 0.0341  -0.0028 0.0661  477 GLU A CD  
4043 O OE1 . GLU A 477 ? 0.6894 0.8203 0.7400 0.0392  0.0006  0.0680  477 GLU A OE1 
4044 O OE2 . GLU A 477 ? 0.7072 0.8344 0.7363 0.0322  -0.0045 0.0615  477 GLU A OE2 
4045 N N   . LYS B 2   ? 0.4145 0.5378 0.4105 -0.0618 -0.0581 0.0114  2   LYS B N   
4046 C CA  . LYS B 2   ? 0.4550 0.5724 0.4480 -0.0633 -0.0551 0.0118  2   LYS B CA  
4047 C C   . LYS B 2   ? 0.3493 0.4672 0.3471 -0.0628 -0.0544 0.0101  2   LYS B C   
4048 O O   . LYS B 2   ? 0.4288 0.5528 0.4338 -0.0626 -0.0524 0.0064  2   LYS B O   
4049 C CB  . LYS B 2   ? 0.5619 0.6802 0.5550 -0.0650 -0.0506 0.0094  2   LYS B CB  
4050 C CG  . LYS B 2   ? 0.6398 0.7534 0.6316 -0.0663 -0.0471 0.0086  2   LYS B CG  
4051 C CD  . LYS B 2   ? 0.6798 0.7940 0.6715 -0.0675 -0.0430 0.0065  2   LYS B CD  
4052 C CE  . LYS B 2   ? 0.6680 0.7893 0.6671 -0.0671 -0.0410 0.0022  2   LYS B CE  
4053 N NZ  . LYS B 2   ? 0.6810 0.8039 0.6792 -0.0678 -0.0389 0.0008  2   LYS B NZ  
4054 N N   . LYS B 3   ? 0.3452 0.4568 0.3389 -0.0626 -0.0559 0.0127  3   LYS B N   
4055 C CA  . LYS B 3   ? 0.3249 0.4367 0.3221 -0.0622 -0.0554 0.0115  3   LYS B CA  
4056 C C   . LYS B 3   ? 0.3042 0.4109 0.2981 -0.0639 -0.0518 0.0110  3   LYS B C   
4057 O O   . LYS B 3   ? 0.3300 0.4313 0.3179 -0.0650 -0.0506 0.0124  3   LYS B O   
4058 C CB  . LYS B 3   ? 0.3766 0.4843 0.3718 -0.0600 -0.0599 0.0146  3   LYS B CB  
4059 C CG  . LYS B 3   ? 0.4206 0.5325 0.4180 -0.0581 -0.0645 0.0158  3   LYS B CG  
4060 C CD  . LYS B 3   ? 0.4494 0.5629 0.4545 -0.0541 -0.0639 0.0137  3   LYS B CD  
4061 C CE  . LYS B 3   ? 0.4858 0.6052 0.4940 -0.0524 -0.0688 0.0144  3   LYS B CE  
4062 N NZ  . LYS B 3   ? 0.5657 0.6967 0.5802 -0.0541 -0.0683 0.0109  3   LYS B NZ  
4063 N N   . LEU B 4   ? 0.2658 0.3724 0.2641 -0.0630 -0.0485 0.0087  4   LEU B N   
4064 C CA  . LEU B 4   ? 0.2957 0.3945 0.2902 -0.0627 -0.0448 0.0087  4   LEU B CA  
4065 C C   . LEU B 4   ? 0.3377 0.4281 0.3299 -0.0587 -0.0453 0.0105  4   LEU B C   
4066 O O   . LEU B 4   ? 0.3339 0.4256 0.3315 -0.0555 -0.0448 0.0094  4   LEU B O   
4067 C CB  . LEU B 4   ? 0.2345 0.3364 0.2351 -0.0631 -0.0392 0.0050  4   LEU B CB  
4068 C CG  . LEU B 4   ? 0.2807 0.3750 0.2776 -0.0627 -0.0350 0.0049  4   LEU B CG  
4069 C CD1 . LEU B 4   ? 0.2309 0.3296 0.2318 -0.0652 -0.0309 0.0020  4   LEU B CD1 
4070 C CD2 . LEU B 4   ? 0.3363 0.4244 0.3339 -0.0584 -0.0324 0.0050  4   LEU B CD2 
4071 N N   . PHE B 5   ? 0.2951 0.3773 0.2798 -0.0587 -0.0463 0.0128  5   PHE B N   
4072 C CA  . PHE B 5   ? 0.2793 0.3531 0.2614 -0.0549 -0.0469 0.0142  5   PHE B CA  
4073 C C   . PHE B 5   ? 0.2958 0.3646 0.2773 -0.0532 -0.0418 0.0125  5   PHE B C   
4074 O O   . PHE B 5   ? 0.2676 0.3335 0.2447 -0.0551 -0.0401 0.0124  5   PHE B O   
4075 C CB  . PHE B 5   ? 0.2460 0.3135 0.2206 -0.0556 -0.0512 0.0177  5   PHE B CB  
4076 C CG  . PHE B 5   ? 0.2305 0.3019 0.2047 -0.0570 -0.0563 0.0202  5   PHE B CG  
4077 C CD1 . PHE B 5   ? 0.2760 0.3506 0.2550 -0.0544 -0.0586 0.0203  5   PHE B CD1 
4078 C CD2 . PHE B 5   ? 0.3264 0.3985 0.2955 -0.0608 -0.0588 0.0223  5   PHE B CD2 
4079 C CE1 . PHE B 5   ? 0.3861 0.4642 0.3644 -0.0554 -0.0635 0.0229  5   PHE B CE1 
4080 C CE2 . PHE B 5   ? 0.3935 0.4684 0.3621 -0.0614 -0.0625 0.0247  5   PHE B CE2 
4081 C CZ  . PHE B 5   ? 0.4539 0.5326 0.4265 -0.0593 -0.0658 0.0253  5   PHE B CZ  
4082 N N   . LEU B 6   ? 0.2732 0.3410 0.2589 -0.0496 -0.0395 0.0111  6   LEU B N   
4083 C CA  . LEU B 6   ? 0.3342 0.3982 0.3199 -0.0477 -0.0343 0.0094  6   LEU B CA  
4084 C C   . LEU B 6   ? 0.3121 0.3678 0.2939 -0.0438 -0.0351 0.0104  6   LEU B C   
4085 O O   . LEU B 6   ? 0.3085 0.3640 0.2927 -0.0412 -0.0377 0.0109  6   LEU B O   
4086 C CB  . LEU B 6   ? 0.2511 0.3214 0.2455 -0.0467 -0.0301 0.0066  6   LEU B CB  
4087 C CG  . LEU B 6   ? 0.2439 0.3113 0.2390 -0.0452 -0.0240 0.0049  6   LEU B CG  
4088 C CD1 . LEU B 6   ? 0.2216 0.2868 0.2120 -0.0479 -0.0217 0.0050  6   LEU B CD1 
4089 C CD2 . LEU B 6   ? 0.3046 0.3789 0.3092 -0.0447 -0.0202 0.0023  6   LEU B CD2 
4090 N N   . VAL B 7   ? 0.2328 0.2819 0.2088 -0.0433 -0.0330 0.0105  7   VAL B N   
4091 C CA  . VAL B 7   ? 0.2843 0.3253 0.2557 -0.0398 -0.0340 0.0112  7   VAL B CA  
4092 C C   . VAL B 7   ? 0.2380 0.2759 0.2086 -0.0374 -0.0284 0.0095  7   VAL B C   
4093 O O   . VAL B 7   ? 0.3092 0.3451 0.2758 -0.0389 -0.0260 0.0092  7   VAL B O   
4094 C CB  . VAL B 7   ? 0.2749 0.3100 0.2389 -0.0413 -0.0378 0.0134  7   VAL B CB  
4095 C CG1 . VAL B 7   ? 0.3195 0.3466 0.2798 -0.0375 -0.0393 0.0137  7   VAL B CG1 
4096 C CG2 . VAL B 7   ? 0.2758 0.3145 0.2403 -0.0443 -0.0427 0.0155  7   VAL B CG2 
4097 N N   . PHE B 8   ? 0.1984 0.2365 0.1729 -0.0338 -0.0263 0.0082  8   PHE B N   
4098 C CA  . PHE B 8   ? 0.2251 0.2596 0.1980 -0.0309 -0.0214 0.0068  8   PHE B CA  
4099 C C   . PHE B 8   ? 0.2898 0.3160 0.2561 -0.0279 -0.0234 0.0073  8   PHE B C   
4100 O O   . PHE B 8   ? 0.2909 0.3153 0.2577 -0.0261 -0.0275 0.0078  8   PHE B O   
4101 C CB  . PHE B 8   ? 0.2770 0.3158 0.2573 -0.0284 -0.0179 0.0049  8   PHE B CB  
4102 C CG  . PHE B 8   ? 0.3558 0.4021 0.3429 -0.0309 -0.0144 0.0037  8   PHE B CG  
4103 C CD1 . PHE B 8   ? 0.3167 0.3628 0.3032 -0.0318 -0.0089 0.0030  8   PHE B CD1 
4104 C CD2 . PHE B 8   ? 0.3196 0.3731 0.3138 -0.0324 -0.0167 0.0032  8   PHE B CD2 
4105 C CE1 . PHE B 8   ? 0.3523 0.4052 0.3457 -0.0342 -0.0056 0.0018  8   PHE B CE1 
4106 C CE2 . PHE B 8   ? 0.3330 0.3937 0.3340 -0.0347 -0.0136 0.0017  8   PHE B CE2 
4107 C CZ  . PHE B 8   ? 0.3702 0.4305 0.3711 -0.0357 -0.0080 0.0010  8   PHE B CZ  
4108 N N   . TRP B 9   ? 0.2550 0.2764 0.2154 -0.0270 -0.0206 0.0070  9   TRP B N   
4109 C CA  . TRP B 9   ? 0.3078 0.3214 0.2617 -0.0240 -0.0223 0.0069  9   TRP B CA  
4110 C C   . TRP B 9   ? 0.2839 0.2953 0.2352 -0.0213 -0.0167 0.0055  9   TRP B C   
4111 O O   . TRP B 9   ? 0.2824 0.2922 0.2294 -0.0226 -0.0143 0.0057  9   TRP B O   
4112 C CB  . TRP B 9   ? 0.3250 0.3345 0.2728 -0.0264 -0.0261 0.0083  9   TRP B CB  
4113 C CG  . TRP B 9   ? 0.2286 0.2308 0.1713 -0.0238 -0.0295 0.0083  9   TRP B CG  
4114 C CD1 . TRP B 9   ? 0.2583 0.2570 0.2008 -0.0193 -0.0293 0.0070  9   TRP B CD1 
4115 C CD2 . TRP B 9   ? 0.2335 0.2312 0.1711 -0.0256 -0.0335 0.0094  9   TRP B CD2 
4116 N NE1 . TRP B 9   ? 0.2178 0.2099 0.1554 -0.0181 -0.0331 0.0071  9   TRP B NE1 
4117 C CE2 . TRP B 9   ? 0.2995 0.2909 0.2342 -0.0221 -0.0357 0.0087  9   TRP B CE2 
4118 C CE3 . TRP B 9   ? 0.2458 0.2446 0.1813 -0.0300 -0.0353 0.0108  9   TRP B CE3 
4119 C CZ2 . TRP B 9   ? 0.3749 0.3608 0.3049 -0.0229 -0.0397 0.0093  9   TRP B CZ2 
4120 C CZ3 . TRP B 9   ? 0.3728 0.3662 0.3035 -0.0309 -0.0391 0.0115  9   TRP B CZ3 
4121 C CH2 . TRP B 9   ? 0.3785 0.3655 0.3066 -0.0274 -0.0413 0.0108  9   TRP B CH2 
4122 N N   . TRP B 10  ? 0.2384 0.2498 0.1924 -0.0174 -0.0146 0.0041  10  TRP B N   
4123 C CA  . TRP B 10  ? 0.2504 0.2603 0.2023 -0.0144 -0.0090 0.0028  10  TRP B CA  
4124 C C   . TRP B 10  ? 0.2695 0.2720 0.2137 -0.0111 -0.0103 0.0022  10  TRP B C   
4125 O O   . TRP B 10  ? 0.2886 0.2886 0.2330 -0.0086 -0.0137 0.0015  10  TRP B O   
4126 C CB  . TRP B 10  ? 0.2392 0.2534 0.1983 -0.0120 -0.0060 0.0013  10  TRP B CB  
4127 C CG  . TRP B 10  ? 0.3085 0.3304 0.2762 -0.0148 -0.0047 0.0013  10  TRP B CG  
4128 C CD1 . TRP B 10  ? 0.2944 0.3210 0.2691 -0.0154 -0.0080 0.0011  10  TRP B CD1 
4129 C CD2 . TRP B 10  ? 0.2928 0.3186 0.2630 -0.0174 0.0002  0.0014  10  TRP B CD2 
4130 N NE1 . TRP B 10  ? 0.2612 0.2947 0.2427 -0.0181 -0.0055 0.0007  10  TRP B NE1 
4131 C CE2 . TRP B 10  ? 0.2959 0.3291 0.2752 -0.0195 -0.0004 0.0009  10  TRP B CE2 
4132 C CE3 . TRP B 10  ? 0.2615 0.2852 0.2275 -0.0180 0.0048  0.0018  10  TRP B CE3 
4133 C CZ2 . TRP B 10  ? 0.2901 0.3287 0.2747 -0.0223 0.0037  0.0005  10  TRP B CZ2 
4134 C CZ3 . TRP B 10  ? 0.3135 0.3422 0.2847 -0.0208 0.0089  0.0018  10  TRP B CZ3 
4135 C CH2 . TRP B 10  ? 0.2555 0.2916 0.2361 -0.0230 0.0083  0.0010  10  TRP B CH2 
4136 N N   . HIS B 11  ? 0.2428 0.2420 0.1805 -0.0108 -0.0074 0.0023  11  HIS B N   
4137 C CA  . HIS B 11  ? 0.3131 0.3056 0.2429 -0.0079 -0.0088 0.0015  11  HIS B CA  
4138 C C   . HIS B 11  ? 0.3456 0.3368 0.2733 -0.0034 -0.0040 -0.0001 11  HIS B C   
4139 O O   . HIS B 11  ? 0.3353 0.3286 0.2631 -0.0035 0.0016  0.0002  11  HIS B O   
4140 C CB  . HIS B 11  ? 0.2779 0.2675 0.2014 -0.0103 -0.0094 0.0025  11  HIS B CB  
4141 C CG  . HIS B 11  ? 0.3441 0.3274 0.2593 -0.0070 -0.0095 0.0014  11  HIS B CG  
4142 N ND1 . HIS B 11  ? 0.3065 0.2853 0.2189 -0.0047 -0.0138 0.0002  11  HIS B ND1 
4143 C CD2 . HIS B 11  ? 0.3423 0.3232 0.2513 -0.0057 -0.0059 0.0012  11  HIS B CD2 
4144 C CE1 . HIS B 11  ? 0.2726 0.2468 0.1776 -0.0020 -0.0130 -0.0009 11  HIS B CE1 
4145 N NE2 . HIS B 11  ? 0.3172 0.2925 0.2197 -0.0024 -0.0082 -0.0002 11  HIS B NE2 
4146 N N   . MET B 12  ? 0.3393 0.3272 0.2652 0.0005  -0.0060 -0.0018 12  MET B N   
4147 C CA  . MET B 12  ? 0.2965 0.2836 0.2206 0.0050  -0.0018 -0.0036 12  MET B CA  
4148 C C   . MET B 12  ? 0.3251 0.3059 0.2403 0.0081  -0.0033 -0.0049 12  MET B C   
4149 O O   . MET B 12  ? 0.3214 0.2985 0.2354 0.0088  -0.0087 -0.0057 12  MET B O   
4150 C CB  . MET B 12  ? 0.2461 0.2358 0.1770 0.0074  -0.0027 -0.0053 12  MET B CB  
4151 C CG  . MET B 12  ? 0.2754 0.2715 0.2157 0.0045  -0.0027 -0.0043 12  MET B CG  
4152 S SD  . MET B 12  ? 0.2984 0.3003 0.2423 0.0023  0.0048  -0.0035 12  MET B SD  
4153 C CE  . MET B 12  ? 0.2813 0.2908 0.2374 0.0007  0.0038  -0.0039 12  MET B CE  
4154 N N   . HIS B 13  ? 0.3314 0.3108 0.2406 0.0101  0.0015  -0.0051 13  HIS B N   
4155 C CA  . HIS B 13  ? 0.2962 0.2699 0.1965 0.0131  0.0001  -0.0065 13  HIS B CA  
4156 C C   . HIS B 13  ? 0.3656 0.3391 0.2609 0.0168  0.0062  -0.0072 13  HIS B C   
4157 O O   . HIS B 13  ? 0.3283 0.3049 0.2249 0.0157  0.0117  -0.0056 13  HIS B O   
4158 C CB  . HIS B 13  ? 0.2357 0.2064 0.1310 0.0102  -0.0024 -0.0051 13  HIS B CB  
4159 C CG  . HIS B 13  ? 0.2944 0.2599 0.1803 0.0134  -0.0030 -0.0065 13  HIS B CG  
4160 N ND1 . HIS B 13  ? 0.3146 0.2762 0.1977 0.0167  -0.0068 -0.0091 13  HIS B ND1 
4161 C CD2 . HIS B 13  ? 0.3341 0.2975 0.2128 0.0140  -0.0003 -0.0059 13  HIS B CD2 
4162 C CE1 . HIS B 13  ? 0.3003 0.2581 0.1750 0.0192  -0.0065 -0.0102 13  HIS B CE1 
4163 N NE2 . HIS B 13  ? 0.2863 0.2450 0.1579 0.0177  -0.0026 -0.0082 13  HIS B NE2 
4164 N N   . GLN B 14  ? 0.3354 0.3051 0.2247 0.0213  0.0052  -0.0096 14  GLN B N   
4165 C CA  . GLN B 14  ? 0.3248 0.2932 0.2066 0.0250  0.0101  -0.0103 14  GLN B CA  
4166 C C   . GLN B 14  ? 0.3603 0.3232 0.2338 0.0280  0.0063  -0.0124 14  GLN B C   
4167 O O   . GLN B 14  ? 0.3531 0.3141 0.2283 0.0293  0.0012  -0.0147 14  GLN B O   
4168 C CB  . GLN B 14  ? 0.2697 0.2413 0.1543 0.0286  0.0146  -0.0120 14  GLN B CB  
4169 C CG  . GLN B 14  ? 0.2421 0.2194 0.1349 0.0261  0.0192  -0.0104 14  GLN B CG  
4170 C CD  . GLN B 14  ? 0.4162 0.3947 0.3065 0.0241  0.0250  -0.0075 14  GLN B CD  
4171 O OE1 . GLN B 14  ? 0.3552 0.3304 0.2365 0.0259  0.0272  -0.0068 14  GLN B OE1 
4172 N NE2 . GLN B 14  ? 0.3405 0.3236 0.2389 0.0203  0.0274  -0.0057 14  GLN B NE2 
4173 N N   . PRO B 15  ? 0.3275 0.2878 0.1924 0.0291  0.0083  -0.0118 15  PRO B N   
4174 C CA  . PRO B 15  ? 0.4002 0.3557 0.2569 0.0328  0.0050  -0.0143 15  PRO B CA  
4175 C C   . PRO B 15  ? 0.4562 0.4119 0.3109 0.0382  0.0067  -0.0175 15  PRO B C   
4176 O O   . PRO B 15  ? 0.4008 0.3603 0.2594 0.0393  0.0113  -0.0175 15  PRO B O   
4177 C CB  . PRO B 15  ? 0.3303 0.2839 0.1787 0.0328  0.0078  -0.0125 15  PRO B CB  
4178 C CG  . PRO B 15  ? 0.3665 0.3240 0.2177 0.0312  0.0146  -0.0095 15  PRO B CG  
4179 C CD  . PRO B 15  ? 0.2501 0.2117 0.1125 0.0275  0.0137  -0.0087 15  PRO B CD  
4180 N N   . LEU B 16  ? 0.4155 0.3674 0.2645 0.0417  0.0030  -0.0207 16  LEU B N   
4181 C CA  . LEU B 16  ? 0.4390 0.3912 0.2863 0.0470  0.0039  -0.0244 16  LEU B CA  
4182 C C   . LEU B 16  ? 0.4443 0.3975 0.2836 0.0505  0.0105  -0.0240 16  LEU B C   
4183 O O   . LEU B 16  ? 0.4166 0.3670 0.2469 0.0521  0.0107  -0.0238 16  LEU B O   
4184 C CB  . LEU B 16  ? 0.4000 0.3478 0.2440 0.0497  -0.0023 -0.0282 16  LEU B CB  
4185 C CG  . LEU B 16  ? 0.3797 0.3279 0.2239 0.0549  -0.0026 -0.0327 16  LEU B CG  
4186 C CD1 . LEU B 16  ? 0.3486 0.3002 0.2033 0.0539  -0.0023 -0.0328 16  LEU B CD1 
4187 C CD2 . LEU B 16  ? 0.3618 0.3055 0.2035 0.0572  -0.0091 -0.0367 16  LEU B CD2 
4188 N N   . TYR B 17  ? 0.4577 0.4151 0.3005 0.0517  0.0160  -0.0238 17  TYR B N   
4189 C CA  . TYR B 17  ? 0.3850 0.3439 0.2210 0.0548  0.0229  -0.0231 17  TYR B CA  
4190 C C   . TYR B 17  ? 0.4543 0.4128 0.2847 0.0609  0.0230  -0.0275 17  TYR B C   
4191 O O   . TYR B 17  ? 0.4228 0.3823 0.2461 0.0641  0.0285  -0.0273 17  TYR B O   
4192 C CB  . TYR B 17  ? 0.4112 0.3752 0.2541 0.0528  0.0293  -0.0207 17  TYR B CB  
4193 C CG  . TYR B 17  ? 0.4277 0.3927 0.2754 0.0471  0.0303  -0.0164 17  TYR B CG  
4194 C CD1 . TYR B 17  ? 0.3279 0.2905 0.1691 0.0456  0.0318  -0.0133 17  TYR B CD1 
4195 C CD2 . TYR B 17  ? 0.4036 0.3723 0.2627 0.0433  0.0296  -0.0156 17  TYR B CD2 
4196 C CE1 . TYR B 17  ? 0.3992 0.3629 0.2452 0.0404  0.0327  -0.0098 17  TYR B CE1 
4197 C CE2 . TYR B 17  ? 0.3033 0.2733 0.1669 0.0382  0.0305  -0.0121 17  TYR B CE2 
4198 C CZ  . TYR B 17  ? 0.3408 0.3083 0.1979 0.0367  0.0320  -0.0093 17  TYR B CZ  
4199 O OH  . TYR B 17  ? 0.3352 0.3041 0.1970 0.0318  0.0327  -0.0062 17  TYR B OH  
4200 N N   . ARG B 18  ? 0.4404 0.3973 0.2738 0.0625  0.0171  -0.0315 18  ARG B N   
4201 C CA  . ARG B 18  ? 0.4355 0.3925 0.2655 0.0682  0.0166  -0.0364 18  ARG B CA  
4202 C C   . ARG B 18  ? 0.4702 0.4231 0.2893 0.0714  0.0140  -0.0382 18  ARG B C   
4203 O O   . ARG B 18  ? 0.4637 0.4128 0.2827 0.0702  0.0077  -0.0393 18  ARG B O   
4204 C CB  . ARG B 18  ? 0.3934 0.3504 0.2326 0.0685  0.0112  -0.0398 18  ARG B CB  
4205 C CG  . ARG B 18  ? 0.4383 0.3965 0.2768 0.0742  0.0113  -0.0452 18  ARG B CG  
4206 C CD  . ARG B 18  ? 0.4731 0.4296 0.3200 0.0742  0.0044  -0.0485 18  ARG B CD  
4207 N NE  . ARG B 18  ? 0.4762 0.4343 0.3241 0.0795  0.0044  -0.0539 18  ARG B NE  
4208 C CZ  . ARG B 18  ? 0.4954 0.4510 0.3376 0.0840  0.0014  -0.0585 18  ARG B CZ  
4209 N NH1 . ARG B 18  ? 0.5404 0.4917 0.3754 0.0837  -0.0019 -0.0583 18  ARG B NH1 
4210 N NH2 . ARG B 18  ? 0.5565 0.5142 0.4005 0.0887  0.0017  -0.0636 18  ARG B NH2 
4211 N N   . GLU B 19  ? 0.4613 0.4151 0.2710 0.0753  0.0190  -0.0384 19  GLU B N   
4212 C CA  . GLU B 19  ? 0.4959 0.4462 0.2945 0.0790  0.0167  -0.0406 19  GLU B CA  
4213 C C   . GLU B 19  ? 0.5275 0.4769 0.3267 0.0833  0.0116  -0.0469 19  GLU B C   
4214 O O   . GLU B 19  ? 0.5531 0.5056 0.3556 0.0861  0.0137  -0.0499 19  GLU B O   
4215 C CB  . GLU B 19  ? 0.5859 0.5378 0.3743 0.0823  0.0237  -0.0389 19  GLU B CB  
4216 C CG  . GLU B 19  ? 0.6862 0.6344 0.4626 0.0848  0.0220  -0.0390 19  GLU B CG  
4217 C CD  . GLU B 19  ? 0.7162 0.6639 0.4887 0.0900  0.0182  -0.0448 19  GLU B CD  
4218 O OE1 . GLU B 19  ? 0.7142 0.6652 0.4862 0.0937  0.0213  -0.0475 19  GLU B OE1 
4219 O OE2 . GLU B 19  ? 0.7475 0.6921 0.5198 0.0895  0.0119  -0.0465 19  GLU B OE2 
4220 N N   . PRO B 20  ? 0.5108 0.4560 0.3072 0.0839  0.0051  -0.0494 20  PRO B N   
4221 C CA  . PRO B 20  ? 0.5485 0.4925 0.3478 0.0872  -0.0003 -0.0555 20  PRO B CA  
4222 C C   . PRO B 20  ? 0.5296 0.4753 0.3214 0.0939  0.0018  -0.0603 20  PRO B C   
4223 O O   . PRO B 20  ? 0.6037 0.5502 0.4000 0.0968  -0.0008 -0.0653 20  PRO B O   
4224 C CB  . PRO B 20  ? 0.5655 0.5046 0.3634 0.0855  -0.0072 -0.0564 20  PRO B CB  
4225 C CG  . PRO B 20  ? 0.5324 0.4705 0.3221 0.0838  -0.0045 -0.0520 20  PRO B CG  
4226 C CD  . PRO B 20  ? 0.5233 0.4648 0.3160 0.0808  0.0021  -0.0468 20  PRO B CD  
4227 N N   . TYR B 21  ? 0.4832 0.4297 0.2637 0.0967  0.0063  -0.0590 21  TYR B N   
4228 C CA  . TYR B 21  ? 0.5193 0.4684 0.2957 0.1018  0.0077  -0.0626 21  TYR B CA  
4229 C C   . TYR B 21  ? 0.5485 0.5026 0.3253 0.1041  0.0148  -0.0629 21  TYR B C   
4230 O O   . TYR B 21  ? 0.5160 0.4725 0.2950 0.1080  0.0142  -0.0681 21  TYR B O   
4231 C CB  . TYR B 21  ? 0.5568 0.5058 0.3273 0.1015  0.0084  -0.0595 21  TYR B CB  
4232 C CG  . TYR B 21  ? 0.5795 0.5245 0.3507 0.1000  0.0012  -0.0606 21  TYR B CG  
4233 C CD1 . TYR B 21  ? 0.5882 0.5325 0.3607 0.1030  -0.0043 -0.0660 21  TYR B CD1 
4234 C CD2 . TYR B 21  ? 0.5978 0.5399 0.3693 0.0954  -0.0001 -0.0562 21  TYR B CD2 
4235 C CE1 . TYR B 21  ? 0.6307 0.5716 0.4049 0.1014  -0.0106 -0.0670 21  TYR B CE1 
4236 C CE2 . TYR B 21  ? 0.6308 0.5697 0.4039 0.0938  -0.0064 -0.0573 21  TYR B CE2 
4237 C CZ  . TYR B 21  ? 0.6270 0.5653 0.4015 0.0968  -0.0115 -0.0626 21  TYR B CZ  
4238 O OH  . TYR B 21  ? 0.6587 0.5942 0.4356 0.0951  -0.0175 -0.0636 21  TYR B OH  
4239 N N   . THR B 22  ? 0.5273 0.4833 0.3027 0.1017  0.0214  -0.0576 22  THR B N   
4240 C CA  . THR B 22  ? 0.5303 0.4913 0.3080 0.1032  0.0283  -0.0576 22  THR B CA  
4241 C C   . THR B 22  ? 0.5527 0.5156 0.3447 0.1007  0.0261  -0.0592 22  THR B C   
4242 O O   . THR B 22  ? 0.5072 0.4746 0.3033 0.1028  0.0297  -0.0615 22  THR B O   
4243 C CB  . THR B 22  ? 0.5198 0.4825 0.2948 0.1002  0.0358  -0.0509 22  THR B CB  
4244 O OG1 . THR B 22  ? 0.5849 0.5450 0.3650 0.0943  0.0337  -0.0464 22  THR B OG1 
4245 C CG2 . THR B 22  ? 0.5499 0.5127 0.3180 0.1005  0.0378  -0.0479 22  THR B CG2 
4246 N N   . GLY B 23  ? 0.5090 0.4687 0.3086 0.0963  0.0202  -0.0579 23  GLY B N   
4247 C CA  . GLY B 23  ? 0.5284 0.4896 0.3413 0.0935  0.0182  -0.0584 23  GLY B CA  
4248 C C   . GLY B 23  ? 0.5911 0.5562 0.4100 0.0897  0.0242  -0.0538 23  GLY B C   
4249 O O   . GLY B 23  ? 0.6512 0.6187 0.4810 0.0881  0.0235  -0.0544 23  GLY B O   
4250 N N   . GLU B 24  ? 0.5329 0.4986 0.3454 0.0883  0.0299  -0.0491 24  GLU B N   
4251 C CA  . GLU B 24  ? 0.4800 0.4498 0.2972 0.0853  0.0367  -0.0450 24  GLU B CA  
4252 C C   . GLU B 24  ? 0.5101 0.4780 0.3307 0.0792  0.0358  -0.0396 24  GLU B C   
4253 O O   . GLU B 24  ? 0.4746 0.4383 0.2888 0.0781  0.0330  -0.0378 24  GLU B O   
4254 C CB  . GLU B 24  ? 0.4579 0.4303 0.2658 0.0883  0.0449  -0.0436 24  GLU B CB  
4255 C CG  . GLU B 24  ? 0.5111 0.4872 0.3171 0.0939  0.0475  -0.0488 24  GLU B CG  
4256 C CD  . GLU B 24  ? 0.5991 0.5781 0.3960 0.0964  0.0561  -0.0468 24  GLU B CD  
4257 O OE1 . GLU B 24  ? 0.5894 0.5655 0.3762 0.0963  0.0579  -0.0432 24  GLU B OE1 
4258 O OE2 . GLU B 24  ? 0.6194 0.6036 0.4193 0.0985  0.0612  -0.0489 24  GLU B OE2 
4259 N N   . TYR B 25  ? 0.4286 0.3999 0.2593 0.0754  0.0382  -0.0374 25  TYR B N   
4260 C CA  . TYR B 25  ? 0.4258 0.3963 0.2603 0.0697  0.0384  -0.0323 25  TYR B CA  
4261 C C   . TYR B 25  ? 0.4206 0.3919 0.2481 0.0692  0.0459  -0.0281 25  TYR B C   
4262 O O   . TYR B 25  ? 0.4468 0.4223 0.2760 0.0700  0.0527  -0.0275 25  TYR B O   
4263 C CB  . TYR B 25  ? 0.4680 0.4424 0.3158 0.0661  0.0383  -0.0317 25  TYR B CB  
4264 C CG  . TYR B 25  ? 0.5368 0.5092 0.3917 0.0648  0.0302  -0.0338 25  TYR B CG  
4265 C CD1 . TYR B 25  ? 0.5692 0.5409 0.4254 0.0688  0.0262  -0.0389 25  TYR B CD1 
4266 C CD2 . TYR B 25  ? 0.4943 0.4655 0.3547 0.0596  0.0266  -0.0308 25  TYR B CD2 
4267 C CE1 . TYR B 25  ? 0.5080 0.4774 0.3709 0.0675  0.0188  -0.0405 25  TYR B CE1 
4268 C CE2 . TYR B 25  ? 0.4412 0.4103 0.3077 0.0583  0.0193  -0.0323 25  TYR B CE2 
4269 C CZ  . TYR B 25  ? 0.4307 0.3988 0.2985 0.0622  0.0155  -0.0369 25  TYR B CZ  
4270 O OH  . TYR B 25  ? 0.4752 0.4409 0.3492 0.0609  0.0084  -0.0381 25  TYR B OH  
4271 N N   . LEU B 26  ? 0.4644 0.4315 0.2842 0.0680  0.0446  -0.0254 26  LEU B N   
4272 C CA  . LEU B 26  ? 0.4377 0.4045 0.2493 0.0683  0.0510  -0.0214 26  LEU B CA  
4273 C C   . LEU B 26  ? 0.4936 0.4626 0.3120 0.0631  0.0555  -0.0166 26  LEU B C   
4274 O O   . LEU B 26  ? 0.4547 0.4241 0.2683 0.0631  0.0621  -0.0132 26  LEU B O   
4275 C CB  . LEU B 26  ? 0.4318 0.3933 0.2327 0.0694  0.0476  -0.0206 26  LEU B CB  
4276 C CG  . LEU B 26  ? 0.4784 0.4373 0.2719 0.0744  0.0425  -0.0254 26  LEU B CG  
4277 C CD1 . LEU B 26  ? 0.5431 0.4975 0.3251 0.0758  0.0409  -0.0240 26  LEU B CD1 
4278 C CD2 . LEU B 26  ? 0.4827 0.4448 0.2730 0.0797  0.0463  -0.0289 26  LEU B CD2 
4279 N N   . LEU B 27  ? 0.4619 0.4321 0.2911 0.0587  0.0521  -0.0163 27  LEU B N   
4280 C CA  . LEU B 27  ? 0.4494 0.4223 0.2866 0.0537  0.0559  -0.0125 27  LEU B CA  
4281 C C   . LEU B 27  ? 0.4377 0.4152 0.2876 0.0520  0.0547  -0.0145 27  LEU B C   
4282 O O   . LEU B 27  ? 0.4673 0.4441 0.3206 0.0528  0.0484  -0.0177 27  LEU B O   
4283 C CB  . LEU B 27  ? 0.5070 0.4768 0.3441 0.0494  0.0523  -0.0094 27  LEU B CB  
4284 C CG  . LEU B 27  ? 0.5364 0.5023 0.3627 0.0501  0.0547  -0.0063 27  LEU B CG  
4285 C CD1 . LEU B 27  ? 0.5180 0.4812 0.3457 0.0457  0.0505  -0.0040 27  LEU B CD1 
4286 C CD2 . LEU B 27  ? 0.5354 0.5036 0.3606 0.0501  0.0637  -0.0030 27  LEU B CD2 
4287 N N   . PRO B 28  ? 0.4067 0.3888 0.2642 0.0496  0.0604  -0.0127 28  PRO B N   
4288 C CA  . PRO B 28  ? 0.4067 0.3937 0.2765 0.0484  0.0597  -0.0149 28  PRO B CA  
4289 C C   . PRO B 28  ? 0.4042 0.3924 0.2836 0.0431  0.0559  -0.0133 28  PRO B C   
4290 O O   . PRO B 28  ? 0.3652 0.3580 0.2552 0.0417  0.0561  -0.0144 28  PRO B O   
4291 C CB  . PRO B 28  ? 0.4631 0.4550 0.3355 0.0488  0.0687  -0.0139 28  PRO B CB  
4292 C CG  . PRO B 28  ? 0.4709 0.4604 0.3373 0.0466  0.0732  -0.0091 28  PRO B CG  
4293 C CD  . PRO B 28  ? 0.4860 0.4691 0.3412 0.0481  0.0682  -0.0087 28  PRO B CD  
4294 N N   . TRP B 29  ? 0.3199 0.3042 0.1959 0.0403  0.0523  -0.0109 29  TRP B N   
4295 C CA  . TRP B 29  ? 0.3524 0.3385 0.2369 0.0349  0.0501  -0.0088 29  TRP B CA  
4296 C C   . TRP B 29  ? 0.4018 0.3893 0.2944 0.0341  0.0436  -0.0113 29  TRP B C   
4297 O O   . TRP B 29  ? 0.3599 0.3516 0.2625 0.0308  0.0434  -0.0107 29  TRP B O   
4298 C CB  . TRP B 29  ? 0.3510 0.3328 0.2296 0.0324  0.0476  -0.0061 29  TRP B CB  
4299 C CG  . TRP B 29  ? 0.4025 0.3828 0.2742 0.0325  0.0537  -0.0030 29  TRP B CG  
4300 C CD1 . TRP B 29  ? 0.4611 0.4363 0.3215 0.0345  0.0531  -0.0020 29  TRP B CD1 
4301 C CD2 . TRP B 29  ? 0.4504 0.4339 0.3261 0.0305  0.0611  -0.0004 29  TRP B CD2 
4302 N NE1 . TRP B 29  ? 0.4656 0.4404 0.3224 0.0340  0.0596  0.0013  29  TRP B NE1 
4303 C CE2 . TRP B 29  ? 0.4804 0.4603 0.3466 0.0314  0.0647  0.0024  29  TRP B CE2 
4304 C CE3 . TRP B 29  ? 0.4491 0.4383 0.3358 0.0281  0.0650  -0.0003 29  TRP B CE3 
4305 C CZ2 . TRP B 29  ? 0.4220 0.4033 0.2893 0.0299  0.0722  0.0057  29  TRP B CZ2 
4306 C CZ3 . TRP B 29  ? 0.4926 0.4836 0.3809 0.0265  0.0724  0.0026  29  TRP B CZ3 
4307 C CH2 . TRP B 29  ? 0.4571 0.4440 0.3358 0.0273  0.0760  0.0057  29  TRP B CH2 
4308 N N   . THR B 30  ? 0.4093 0.3935 0.2981 0.0371  0.0381  -0.0140 30  THR B N   
4309 C CA  . THR B 30  ? 0.4004 0.3855 0.2969 0.0367  0.0322  -0.0162 30  THR B CA  
4310 C C   . THR B 30  ? 0.4012 0.3920 0.3067 0.0378  0.0353  -0.0180 30  THR B C   
4311 O O   . THR B 30  ? 0.4095 0.4035 0.3246 0.0353  0.0328  -0.0180 30  THR B O   
4312 C CB  . THR B 30  ? 0.4489 0.4293 0.3400 0.0401  0.0263  -0.0190 30  THR B CB  
4313 O OG1 . THR B 30  ? 0.4141 0.3896 0.2978 0.0386  0.0231  -0.0175 30  THR B OG1 
4314 C CG2 . THR B 30  ? 0.4819 0.4629 0.3814 0.0395  0.0201  -0.0208 30  THR B CG2 
4315 N N   . PHE B 31  ? 0.3404 0.3330 0.2432 0.0416  0.0409  -0.0197 31  PHE B N   
4316 C CA  . PHE B 31  ? 0.3533 0.3517 0.2650 0.0427  0.0444  -0.0217 31  PHE B CA  
4317 C C   . PHE B 31  ? 0.3577 0.3610 0.2780 0.0383  0.0482  -0.0192 31  PHE B C   
4318 O O   . PHE B 31  ? 0.3152 0.3230 0.2460 0.0372  0.0469  -0.0205 31  PHE B O   
4319 C CB  . PHE B 31  ? 0.3845 0.3842 0.2909 0.0472  0.0505  -0.0237 31  PHE B CB  
4320 C CG  . PHE B 31  ? 0.4002 0.4065 0.3158 0.0481  0.0554  -0.0257 31  PHE B CG  
4321 C CD1 . PHE B 31  ? 0.2978 0.3062 0.2197 0.0509  0.0521  -0.0298 31  PHE B CD1 
4322 C CD2 . PHE B 31  ? 0.3729 0.3833 0.2915 0.0460  0.0631  -0.0234 31  PHE B CD2 
4323 C CE1 . PHE B 31  ? 0.3241 0.3390 0.2549 0.0518  0.0565  -0.0320 31  PHE B CE1 
4324 C CE2 . PHE B 31  ? 0.3267 0.3437 0.2545 0.0467  0.0677  -0.0256 31  PHE B CE2 
4325 C CZ  . PHE B 31  ? 0.3424 0.3617 0.2763 0.0497  0.0643  -0.0299 31  PHE B CZ  
4326 N N   . PHE B 32  ? 0.3357 0.3383 0.2519 0.0358  0.0527  -0.0158 32  PHE B N   
4327 C CA  . PHE B 32  ? 0.2615 0.2691 0.1860 0.0319  0.0573  -0.0137 32  PHE B CA  
4328 C C   . PHE B 32  ? 0.2870 0.2955 0.2186 0.0275  0.0519  -0.0125 32  PHE B C   
4329 O O   . PHE B 32  ? 0.3099 0.3239 0.2520 0.0253  0.0528  -0.0130 32  PHE B O   
4330 C CB  . PHE B 32  ? 0.2957 0.3017 0.2135 0.0310  0.0640  -0.0104 32  PHE B CB  
4331 C CG  . PHE B 32  ? 0.4145 0.4224 0.3293 0.0344  0.0716  -0.0112 32  PHE B CG  
4332 C CD1 . PHE B 32  ? 0.3901 0.4043 0.3144 0.0346  0.0760  -0.0130 32  PHE B CD1 
4333 C CD2 . PHE B 32  ? 0.4516 0.4552 0.3541 0.0375  0.0742  -0.0102 32  PHE B CD2 
4334 C CE1 . PHE B 32  ? 0.4089 0.4252 0.3306 0.0376  0.0833  -0.0138 32  PHE B CE1 
4335 C CE2 . PHE B 32  ? 0.4788 0.4844 0.3781 0.0406  0.0813  -0.0108 32  PHE B CE2 
4336 C CZ  . PHE B 32  ? 0.4280 0.4400 0.3369 0.0406  0.0860  -0.0126 32  PHE B CZ  
4337 N N   . HIS B 33  ? 0.2749 0.2786 0.2011 0.0261  0.0462  -0.0113 33  HIS B N   
4338 C CA  . HIS B 33  ? 0.3167 0.3215 0.2491 0.0221  0.0407  -0.0103 33  HIS B CA  
4339 C C   . HIS B 33  ? 0.3212 0.3279 0.2606 0.0232  0.0353  -0.0129 33  HIS B C   
4340 O O   . HIS B 33  ? 0.3035 0.3134 0.2508 0.0201  0.0323  -0.0124 33  HIS B O   
4341 C CB  . HIS B 33  ? 0.2657 0.2649 0.1902 0.0203  0.0364  -0.0083 33  HIS B CB  
4342 C CG  . HIS B 33  ? 0.3076 0.3061 0.2284 0.0178  0.0410  -0.0054 33  HIS B CG  
4343 N ND1 . HIS B 33  ? 0.3136 0.3164 0.2419 0.0137  0.0438  -0.0036 33  HIS B ND1 
4344 C CD2 . HIS B 33  ? 0.3273 0.3215 0.2382 0.0191  0.0435  -0.0039 33  HIS B CD2 
4345 C CE1 . HIS B 33  ? 0.3298 0.3307 0.2532 0.0125  0.0477  -0.0012 33  HIS B CE1 
4346 N NE2 . HIS B 33  ? 0.3439 0.3395 0.2565 0.0157  0.0476  -0.0011 33  HIS B NE2 
4347 N N   . ALA B 34  ? 0.2744 0.2792 0.2111 0.0277  0.0339  -0.0157 34  ALA B N   
4348 C CA  . ALA B 34  ? 0.3189 0.3254 0.2629 0.0291  0.0289  -0.0182 34  ALA B CA  
4349 C C   . ALA B 34  ? 0.3349 0.3485 0.2895 0.0291  0.0328  -0.0196 34  ALA B C   
4350 O O   . ALA B 34  ? 0.3372 0.3540 0.3005 0.0275  0.0291  -0.0201 34  ALA B O   
4351 C CB  . ALA B 34  ? 0.2676 0.2701 0.2062 0.0340  0.0263  -0.0212 34  ALA B CB  
4352 N N   . VAL B 35  ? 0.2923 0.3086 0.2464 0.0308  0.0404  -0.0204 35  VAL B N   
4353 C CA  . VAL B 35  ? 0.2842 0.3077 0.2490 0.0308  0.0444  -0.0221 35  VAL B CA  
4354 C C   . VAL B 35  ? 0.3194 0.3471 0.2915 0.0258  0.0458  -0.0198 35  VAL B C   
4355 O O   . VAL B 35  ? 0.3216 0.3551 0.3044 0.0248  0.0454  -0.0212 35  VAL B O   
4356 C CB  . VAL B 35  ? 0.3572 0.3827 0.3197 0.0338  0.0524  -0.0235 35  VAL B CB  
4357 C CG1 . VAL B 35  ? 0.3708 0.3927 0.3262 0.0389  0.0507  -0.0263 35  VAL B CG1 
4358 C CG2 . VAL B 35  ? 0.3745 0.3987 0.3307 0.0317  0.0587  -0.0201 35  VAL B CG2 
4359 N N   . LYS B 36  ? 0.2785 0.3036 0.2452 0.0226  0.0471  -0.0164 36  LYS B N   
4360 C CA  . LYS B 36  ? 0.3026 0.3317 0.2759 0.0179  0.0490  -0.0145 36  LYS B CA  
4361 C C   . LYS B 36  ? 0.3463 0.3751 0.3224 0.0146  0.0417  -0.0134 36  LYS B C   
4362 O O   . LYS B 36  ? 0.2916 0.3258 0.2771 0.0118  0.0413  -0.0135 36  LYS B O   
4363 C CB  . LYS B 36  ? 0.2964 0.3232 0.2633 0.0161  0.0548  -0.0115 36  LYS B CB  
4364 C CG  . LYS B 36  ? 0.3216 0.3527 0.2959 0.0114  0.0578  -0.0098 36  LYS B CG  
4365 C CD  . LYS B 36  ? 0.3229 0.3519 0.2920 0.0102  0.0646  -0.0070 36  LYS B CD  
4366 C CE  . LYS B 36  ? 0.2353 0.2585 0.1957 0.0082  0.0614  -0.0042 36  LYS B CE  
4367 N NZ  . LYS B 36  ? 0.3010 0.3258 0.2664 0.0042  0.0558  -0.0037 36  LYS B NZ  
4368 N N   . ASP B 37  ? 0.3549 0.3777 0.3230 0.0149  0.0361  -0.0124 37  ASP B N   
4369 C CA  . ASP B 37  ? 0.3402 0.3622 0.3091 0.0111  0.0302  -0.0105 37  ASP B CA  
4370 C C   . ASP B 37  ? 0.3062 0.3252 0.2742 0.0124  0.0222  -0.0113 37  ASP B C   
4371 O O   . ASP B 37  ? 0.2308 0.2521 0.2042 0.0099  0.0176  -0.0108 37  ASP B O   
4372 C CB  . ASP B 37  ? 0.3162 0.3339 0.2767 0.0089  0.0311  -0.0078 37  ASP B CB  
4373 C CG  . ASP B 37  ? 0.3559 0.3756 0.3167 0.0075  0.0388  -0.0065 37  ASP B CG  
4374 O OD1 . ASP B 37  ? 0.2731 0.2984 0.2426 0.0046  0.0414  -0.0063 37  ASP B OD1 
4375 O OD2 . ASP B 37  ? 0.3630 0.3784 0.3152 0.0094  0.0423  -0.0057 37  ASP B OD2 
4376 N N   . TYR B 38  ? 0.3406 0.3544 0.3019 0.0161  0.0202  -0.0126 38  TYR B N   
4377 C CA  . TYR B 38  ? 0.2962 0.3060 0.2558 0.0166  0.0124  -0.0127 38  TYR B CA  
4378 C C   . TYR B 38  ? 0.2943 0.3076 0.2631 0.0176  0.0086  -0.0144 38  TYR B C   
4379 O O   . TYR B 38  ? 0.2993 0.3110 0.2694 0.0162  0.0022  -0.0134 38  TYR B O   
4380 C CB  . TYR B 38  ? 0.2810 0.2844 0.2316 0.0204  0.0112  -0.0141 38  TYR B CB  
4381 C CG  . TYR B 38  ? 0.2822 0.2814 0.2231 0.0193  0.0131  -0.0122 38  TYR B CG  
4382 C CD1 . TYR B 38  ? 0.2951 0.2940 0.2349 0.0148  0.0118  -0.0094 38  TYR B CD1 
4383 C CD2 . TYR B 38  ? 0.2995 0.2952 0.2324 0.0229  0.0162  -0.0134 38  TYR B CD2 
4384 C CE1 . TYR B 38  ? 0.3484 0.3435 0.2798 0.0139  0.0133  -0.0079 38  TYR B CE1 
4385 C CE2 . TYR B 38  ? 0.2979 0.2898 0.2218 0.0222  0.0177  -0.0117 38  TYR B CE2 
4386 C CZ  . TYR B 38  ? 0.3389 0.3304 0.2623 0.0177  0.0162  -0.0090 38  TYR B CZ  
4387 O OH  . TYR B 38  ? 0.2749 0.2627 0.1899 0.0170  0.0174  -0.0075 38  TYR B OH  
4388 N N   . TYR B 39  ? 0.2800 0.2981 0.2554 0.0199  0.0125  -0.0167 39  TYR B N   
4389 C CA  . TYR B 39  ? 0.2880 0.3103 0.2731 0.0207  0.0090  -0.0183 39  TYR B CA  
4390 C C   . TYR B 39  ? 0.3020 0.3308 0.2952 0.0168  0.0099  -0.0171 39  TYR B C   
4391 O O   . TYR B 39  ? 0.2570 0.2876 0.2553 0.0155  0.0045  -0.0166 39  TYR B O   
4392 C CB  . TYR B 39  ? 0.2483 0.2729 0.2372 0.0252  0.0123  -0.0219 39  TYR B CB  
4393 C CG  . TYR B 39  ? 0.2902 0.3201 0.2902 0.0263  0.0096  -0.0239 39  TYR B CG  
4394 C CD1 . TYR B 39  ? 0.3466 0.3737 0.3483 0.0288  0.0029  -0.0251 39  TYR B CD1 
4395 C CD2 . TYR B 39  ? 0.2970 0.3344 0.3060 0.0247  0.0137  -0.0247 39  TYR B CD2 
4396 C CE1 . TYR B 39  ? 0.3679 0.3996 0.3797 0.0299  0.0001  -0.0268 39  TYR B CE1 
4397 C CE2 . TYR B 39  ? 0.3109 0.3534 0.3302 0.0259  0.0109  -0.0267 39  TYR B CE2 
4398 C CZ  . TYR B 39  ? 0.3904 0.4299 0.4108 0.0286  0.0041  -0.0277 39  TYR B CZ  
4399 O OH  . TYR B 39  ? 0.4101 0.4545 0.4406 0.0299  0.0010  -0.0297 39  TYR B OH  
4400 N N   . ASP B 40  ? 0.2734 0.3058 0.2678 0.0149  0.0167  -0.0167 40  ASP B N   
4401 C CA  . ASP B 40  ? 0.2578 0.2972 0.2612 0.0116  0.0183  -0.0164 40  ASP B CA  
4402 C C   . ASP B 40  ? 0.3095 0.3487 0.3119 0.0071  0.0141  -0.0136 40  ASP B C   
4403 O O   . ASP B 40  ? 0.3390 0.3836 0.3492 0.0049  0.0121  -0.0137 40  ASP B O   
4404 C CB  . ASP B 40  ? 0.2772 0.3200 0.2823 0.0108  0.0269  -0.0166 40  ASP B CB  
4405 C CG  . ASP B 40  ? 0.3396 0.3866 0.3511 0.0142  0.0313  -0.0198 40  ASP B CG  
4406 O OD1 . ASP B 40  ? 0.3529 0.4063 0.3749 0.0139  0.0305  -0.0217 40  ASP B OD1 
4407 O OD2 . ASP B 40  ? 0.3023 0.3465 0.3082 0.0172  0.0352  -0.0207 40  ASP B OD2 
4408 N N   . MET B 41  ? 0.2997 0.3329 0.2927 0.0058  0.0126  -0.0113 41  MET B N   
4409 C CA  . MET B 41  ? 0.2692 0.3025 0.2613 0.0015  0.0087  -0.0089 41  MET B CA  
4410 C C   . MET B 41  ? 0.2770 0.3109 0.2724 0.0012  0.0011  -0.0087 41  MET B C   
4411 O O   . MET B 41  ? 0.3117 0.3510 0.3133 -0.0017 -0.0005 -0.0082 41  MET B O   
4412 C CB  . MET B 41  ? 0.2533 0.2802 0.2348 0.0003  0.0086  -0.0069 41  MET B CB  
4413 C CG  . MET B 41  ? 0.2948 0.3225 0.2743 -0.0014 0.0154  -0.0061 41  MET B CG  
4414 S SD  . MET B 41  ? 0.2876 0.3227 0.2755 -0.0066 0.0173  -0.0053 41  MET B SD  
4415 C CE  . MET B 41  ? 0.2538 0.2854 0.2354 -0.0103 0.0116  -0.0028 41  MET B CE  
4416 N N   . PRO B 42  ? 0.2780 0.3070 0.2702 0.0041  -0.0036 -0.0090 42  PRO B N   
4417 C CA  . PRO B 42  ? 0.2920 0.3220 0.2887 0.0041  -0.0104 -0.0086 42  PRO B CA  
4418 C C   . PRO B 42  ? 0.2944 0.3310 0.3014 0.0059  -0.0099 -0.0109 42  PRO B C   
4419 O O   . PRO B 42  ? 0.2905 0.3300 0.3025 0.0049  -0.0147 -0.0103 42  PRO B O   
4420 C CB  . PRO B 42  ? 0.3366 0.3591 0.3273 0.0070  -0.0147 -0.0086 42  PRO B CB  
4421 C CG  . PRO B 42  ? 0.2938 0.3134 0.2801 0.0102  -0.0096 -0.0106 42  PRO B CG  
4422 C CD  . PRO B 42  ? 0.2707 0.2929 0.2553 0.0076  -0.0033 -0.0098 42  PRO B CD  
4423 N N   . ALA B 43  ? 0.2595 0.2988 0.2700 0.0084  -0.0041 -0.0136 43  ALA B N   
4424 C CA  . ALA B 43  ? 0.2595 0.3054 0.2805 0.0102  -0.0036 -0.0161 43  ALA B CA  
4425 C C   . ALA B 43  ? 0.3040 0.3573 0.3324 0.0065  -0.0031 -0.0158 43  ALA B C   
4426 O O   . ALA B 43  ? 0.3346 0.3935 0.3720 0.0076  -0.0049 -0.0175 43  ALA B O   
4427 C CB  . ALA B 43  ? 0.1956 0.2432 0.2188 0.0134  0.0031  -0.0191 43  ALA B CB  
4428 N N   . TYR B 44  ? 0.2333 0.2871 0.2586 0.0025  -0.0010 -0.0138 44  TYR B N   
4429 C CA  . TYR B 44  ? 0.2699 0.3307 0.3020 -0.0012 -0.0011 -0.0135 44  TYR B CA  
4430 C C   . TYR B 44  ? 0.2882 0.3507 0.3231 -0.0017 -0.0088 -0.0126 44  TYR B C   
4431 O O   . TYR B 44  ? 0.2729 0.3426 0.3157 -0.0033 -0.0097 -0.0136 44  TYR B O   
4432 C CB  . TYR B 44  ? 0.2816 0.3414 0.3085 -0.0054 0.0013  -0.0113 44  TYR B CB  
4433 C CG  . TYR B 44  ? 0.3256 0.3869 0.3536 -0.0062 0.0094  -0.0122 44  TYR B CG  
4434 C CD1 . TYR B 44  ? 0.3496 0.4185 0.3867 -0.0085 0.0132  -0.0136 44  TYR B CD1 
4435 C CD2 . TYR B 44  ? 0.2975 0.3528 0.3175 -0.0046 0.0134  -0.0115 44  TYR B CD2 
4436 C CE1 . TYR B 44  ? 0.3049 0.3750 0.3434 -0.0093 0.0208  -0.0140 44  TYR B CE1 
4437 C CE2 . TYR B 44  ? 0.3267 0.3832 0.3473 -0.0052 0.0209  -0.0118 44  TYR B CE2 
4438 C CZ  . TYR B 44  ? 0.3491 0.4128 0.3790 -0.0077 0.0247  -0.0129 44  TYR B CZ  
4439 O OH  . TYR B 44  ? 0.3313 0.3959 0.3624 -0.0085 0.0323  -0.0130 44  TYR B OH  
4440 N N   . LEU B 45  ? 0.2867 0.3427 0.3150 -0.0006 -0.0144 -0.0108 45  LEU B N   
4441 C CA  . LEU B 45  ? 0.3259 0.3825 0.3558 -0.0010 -0.0219 -0.0093 45  LEU B CA  
4442 C C   . LEU B 45  ? 0.3328 0.3936 0.3715 0.0024  -0.0242 -0.0116 45  LEU B C   
4443 O O   . LEU B 45  ? 0.3223 0.3853 0.3639 0.0020  -0.0300 -0.0106 45  LEU B O   
4444 C CB  . LEU B 45  ? 0.2552 0.3031 0.2760 -0.0006 -0.0268 -0.0066 45  LEU B CB  
4445 C CG  . LEU B 45  ? 0.3062 0.3502 0.3184 -0.0044 -0.0262 -0.0040 45  LEU B CG  
4446 C CD1 . LEU B 45  ? 0.2426 0.2776 0.2463 -0.0032 -0.0297 -0.0024 45  LEU B CD1 
4447 C CD2 . LEU B 45  ? 0.2746 0.3232 0.2879 -0.0088 -0.0289 -0.0021 45  LEU B CD2 
4448 N N   . LYS B 46  ? 0.3024 0.3645 0.3454 0.0058  -0.0199 -0.0148 46  LYS B N   
4449 C CA  . LYS B 46  ? 0.2977 0.3649 0.3503 0.0088  -0.0217 -0.0175 46  LYS B CA  
4450 C C   . LYS B 46  ? 0.3746 0.4515 0.4366 0.0066  -0.0196 -0.0191 46  LYS B C   
4451 O O   . LYS B 46  ? 0.3631 0.4450 0.4329 0.0082  -0.0231 -0.0207 46  LYS B O   
4452 C CB  . LYS B 46  ? 0.3167 0.3828 0.3713 0.0131  -0.0177 -0.0207 46  LYS B CB  
4453 C CG  . LYS B 46  ? 0.4673 0.5242 0.5127 0.0153  -0.0188 -0.0197 46  LYS B CG  
4454 C CD  . LYS B 46  ? 0.5880 0.6443 0.6346 0.0192  -0.0138 -0.0231 46  LYS B CD  
4455 C CE  . LYS B 46  ? 0.6822 0.7312 0.7242 0.0231  -0.0180 -0.0235 46  LYS B CE  
4456 N NZ  . LYS B 46  ? 0.6932 0.7436 0.7394 0.0277  -0.0145 -0.0276 46  LYS B NZ  
4457 N N   . ASP B 47  ? 0.3743 0.4539 0.4358 0.0030  -0.0143 -0.0189 47  ASP B N   
4458 C CA  . ASP B 47  ? 0.3840 0.4729 0.4550 0.0009  -0.0115 -0.0210 47  ASP B CA  
4459 C C   . ASP B 47  ? 0.4073 0.4994 0.4776 -0.0035 -0.0142 -0.0190 47  ASP B C   
4460 O O   . ASP B 47  ? 0.3586 0.4588 0.4376 -0.0049 -0.0140 -0.0209 47  ASP B O   
4461 C CB  . ASP B 47  ? 0.3650 0.4556 0.4381 0.0002  -0.0025 -0.0228 47  ASP B CB  
4462 C CG  . ASP B 47  ? 0.4278 0.5190 0.5053 0.0045  0.0011  -0.0259 47  ASP B CG  
4463 O OD1 . ASP B 47  ? 0.4663 0.5584 0.5479 0.0078  -0.0032 -0.0275 47  ASP B OD1 
4464 O OD2 . ASP B 47  ? 0.4687 0.5595 0.5457 0.0045  0.0084  -0.0268 47  ASP B OD2 
4465 N N   . PHE B 48  ? 0.3690 0.4551 0.4295 -0.0058 -0.0167 -0.0155 48  PHE B N   
4466 C CA  . PHE B 48  ? 0.3681 0.4570 0.4271 -0.0100 -0.0193 -0.0136 48  PHE B CA  
4467 C C   . PHE B 48  ? 0.3638 0.4471 0.4151 -0.0101 -0.0265 -0.0101 48  PHE B C   
4468 O O   . PHE B 48  ? 0.3525 0.4277 0.3958 -0.0090 -0.0272 -0.0083 48  PHE B O   
4469 C CB  . PHE B 48  ? 0.4238 0.5117 0.4789 -0.0135 -0.0138 -0.0129 48  PHE B CB  
4470 C CG  . PHE B 48  ? 0.3839 0.4756 0.4456 -0.0133 -0.0061 -0.0157 48  PHE B CG  
4471 C CD1 . PHE B 48  ? 0.3736 0.4605 0.4323 -0.0107 -0.0012 -0.0163 48  PHE B CD1 
4472 C CD2 . PHE B 48  ? 0.3295 0.4297 0.4002 -0.0157 -0.0036 -0.0179 48  PHE B CD2 
4473 C CE1 . PHE B 48  ? 0.3374 0.4279 0.4020 -0.0106 0.0062  -0.0185 48  PHE B CE1 
4474 C CE2 . PHE B 48  ? 0.2620 0.3656 0.3393 -0.0157 0.0037  -0.0203 48  PHE B CE2 
4475 C CZ  . PHE B 48  ? 0.2496 0.3481 0.3236 -0.0132 0.0087  -0.0205 48  PHE B CZ  
4476 N N   . GLU B 49  ? 0.3628 0.4507 0.4168 -0.0114 -0.0320 -0.0093 49  GLU B N   
4477 C CA  . GLU B 49  ? 0.4541 0.5369 0.5015 -0.0113 -0.0390 -0.0058 49  GLU B CA  
4478 C C   . GLU B 49  ? 0.4660 0.5471 0.5059 -0.0158 -0.0397 -0.0029 49  GLU B C   
4479 O O   . GLU B 49  ? 0.4875 0.5731 0.5278 -0.0185 -0.0432 -0.0017 49  GLU B O   
4480 C CB  . GLU B 49  ? 0.5933 0.6812 0.6467 -0.0097 -0.0449 -0.0060 49  GLU B CB  
4481 C CG  . GLU B 49  ? 0.7301 0.8115 0.7773 -0.0086 -0.0521 -0.0023 49  GLU B CG  
4482 C CD  . GLU B 49  ? 0.8147 0.8962 0.8673 -0.0039 -0.0563 -0.0032 49  GLU B CD  
4483 O OE1 . GLU B 49  ? 0.8300 0.9186 0.8892 -0.0034 -0.0593 -0.0042 49  GLU B OE1 
4484 O OE2 . GLU B 49  ? 0.8378 0.9124 0.8882 -0.0007 -0.0568 -0.0032 49  GLU B OE2 
4485 N N   . ILE B 50  ? 0.4174 0.4921 0.4504 -0.0165 -0.0363 -0.0021 50  ILE B N   
4486 C CA  . ILE B 50  ? 0.3500 0.4215 0.3751 -0.0203 -0.0369 0.0006  50  ILE B CA  
4487 C C   . ILE B 50  ? 0.3237 0.3853 0.3403 -0.0187 -0.0387 0.0027  50  ILE B C   
4488 O O   . ILE B 50  ? 0.3763 0.4340 0.3936 -0.0148 -0.0397 0.0020  50  ILE B O   
4489 C CB  . ILE B 50  ? 0.2936 0.3677 0.3191 -0.0231 -0.0306 -0.0008 50  ILE B CB  
4490 C CG1 . ILE B 50  ? 0.3283 0.3990 0.3540 -0.0204 -0.0246 -0.0027 50  ILE B CG1 
4491 C CG2 . ILE B 50  ? 0.3061 0.3901 0.3404 -0.0251 -0.0293 -0.0030 50  ILE B CG2 
4492 C CD1 . ILE B 50  ? 0.3519 0.4224 0.3755 -0.0230 -0.0188 -0.0030 50  ILE B CD1 
4493 N N   . LYS B 51  ? 0.2906 0.3481 0.2995 -0.0217 -0.0394 0.0049  51  LYS B N   
4494 C CA  . LYS B 51  ? 0.2652 0.3134 0.2659 -0.0206 -0.0407 0.0066  51  LYS B CA  
4495 C C   . LYS B 51  ? 0.2701 0.3154 0.2668 -0.0212 -0.0349 0.0055  51  LYS B C   
4496 O O   . LYS B 51  ? 0.2468 0.2955 0.2434 -0.0244 -0.0320 0.0053  51  LYS B O   
4497 C CB  . LYS B 51  ? 0.2988 0.3442 0.2937 -0.0235 -0.0460 0.0100  51  LYS B CB  
4498 C CG  . LYS B 51  ? 0.3769 0.4264 0.3751 -0.0241 -0.0515 0.0117  51  LYS B CG  
4499 C CD  . LYS B 51  ? 0.3369 0.3838 0.3383 -0.0197 -0.0548 0.0116  51  LYS B CD  
4500 C CE  . LYS B 51  ? 0.3828 0.4325 0.3859 -0.0202 -0.0610 0.0140  51  LYS B CE  
4501 N NZ  . LYS B 51  ? 0.5572 0.6055 0.5650 -0.0157 -0.0641 0.0135  51  LYS B NZ  
4502 N N   . LEU B 52  ? 0.2420 0.2809 0.2354 -0.0178 -0.0335 0.0048  52  LEU B N   
4503 C CA  . LEU B 52  ? 0.2978 0.3330 0.2862 -0.0177 -0.0285 0.0040  52  LEU B CA  
4504 C C   . LEU B 52  ? 0.3362 0.3627 0.3172 -0.0157 -0.0311 0.0049  52  LEU B C   
4505 O O   . LEU B 52  ? 0.3083 0.3318 0.2903 -0.0126 -0.0342 0.0046  52  LEU B O   
4506 C CB  . LEU B 52  ? 0.2859 0.3236 0.2788 -0.0149 -0.0225 0.0012  52  LEU B CB  
4507 C CG  . LEU B 52  ? 0.2906 0.3370 0.2919 -0.0166 -0.0190 -0.0003 52  LEU B CG  
4508 C CD1 . LEU B 52  ? 0.2675 0.3154 0.2730 -0.0136 -0.0129 -0.0028 52  LEU B CD1 
4509 C CD2 . LEU B 52  ? 0.2545 0.3032 0.2541 -0.0211 -0.0170 0.0007  52  LEU B CD2 
4510 N N   . ASN B 53  ? 0.2739 0.2962 0.2478 -0.0175 -0.0300 0.0058  53  ASN B N   
4511 C CA  . ASN B 53  ? 0.2411 0.2554 0.2082 -0.0161 -0.0327 0.0064  53  ASN B CA  
4512 C C   . ASN B 53  ? 0.2799 0.2903 0.2423 -0.0137 -0.0280 0.0047  53  ASN B C   
4513 O O   . ASN B 53  ? 0.3057 0.3192 0.2688 -0.0145 -0.0227 0.0039  53  ASN B O   
4514 C CB  . ASN B 53  ? 0.3085 0.3208 0.2709 -0.0200 -0.0365 0.0089  53  ASN B CB  
4515 C CG  . ASN B 53  ? 0.3310 0.3477 0.2974 -0.0225 -0.0408 0.0108  53  ASN B CG  
4516 O OD1 . ASN B 53  ? 0.2888 0.3037 0.2570 -0.0207 -0.0451 0.0117  53  ASN B OD1 
4517 N ND2 . ASN B 53  ? 0.2624 0.2851 0.2306 -0.0263 -0.0397 0.0114  53  ASN B ND2 
4518 N N   . PHE B 54  ? 0.2549 0.2588 0.2130 -0.0107 -0.0298 0.0041  54  PHE B N   
4519 C CA  . PHE B 54  ? 0.2895 0.2900 0.2432 -0.0076 -0.0255 0.0022  54  PHE B CA  
4520 C C   . PHE B 54  ? 0.2727 0.2658 0.2189 -0.0069 -0.0284 0.0023  54  PHE B C   
4521 O O   . PHE B 54  ? 0.3577 0.3473 0.3036 -0.0069 -0.0338 0.0032  54  PHE B O   
4522 C CB  . PHE B 54  ? 0.2546 0.2561 0.2125 -0.0031 -0.0234 -0.0002 54  PHE B CB  
4523 C CG  . PHE B 54  ? 0.3154 0.3244 0.2813 -0.0036 -0.0203 -0.0008 54  PHE B CG  
4524 C CD1 . PHE B 54  ? 0.2173 0.2303 0.1900 -0.0042 -0.0239 -0.0003 54  PHE B CD1 
4525 C CD2 . PHE B 54  ? 0.3026 0.3148 0.2694 -0.0034 -0.0137 -0.0018 54  PHE B CD2 
4526 C CE1 . PHE B 54  ? 0.2710 0.2912 0.2514 -0.0047 -0.0212 -0.0012 54  PHE B CE1 
4527 C CE2 . PHE B 54  ? 0.2293 0.2484 0.2040 -0.0040 -0.0107 -0.0026 54  PHE B CE2 
4528 C CZ  . PHE B 54  ? 0.2848 0.3082 0.2666 -0.0046 -0.0145 -0.0025 54  PHE B CZ  
4529 N N   . ASN B 55  ? 0.2660 0.2565 0.2063 -0.0061 -0.0249 0.0015  55  ASN B N   
4530 C CA  . ASN B 55  ? 0.3188 0.3024 0.2519 -0.0045 -0.0268 0.0008  55  ASN B CA  
4531 C C   . ASN B 55  ? 0.3750 0.3566 0.3058 0.0005  -0.0233 -0.0018 55  ASN B C   
4532 O O   . ASN B 55  ? 0.3421 0.3268 0.2734 0.0014  -0.0177 -0.0024 55  ASN B O   
4533 C CB  . ASN B 55  ? 0.3064 0.2887 0.2339 -0.0076 -0.0259 0.0018  55  ASN B CB  
4534 C CG  . ASN B 55  ? 0.2813 0.2568 0.2018 -0.0061 -0.0285 0.0009  55  ASN B CG  
4535 O OD1 . ASN B 55  ? 0.3238 0.2962 0.2440 -0.0072 -0.0335 0.0015  55  ASN B OD1 
4536 N ND2 . ASN B 55  ? 0.3188 0.2920 0.2337 -0.0035 -0.0250 -0.0006 55  ASN B ND2 
4537 N N   . LEU B 56  ? 0.3539 0.3303 0.2823 0.0037  -0.0264 -0.0034 56  LEU B N   
4538 C CA  . LEU B 56  ? 0.3264 0.3007 0.2519 0.0087  -0.0235 -0.0063 56  LEU B CA  
4539 C C   . LEU B 56  ? 0.2684 0.2363 0.1864 0.0102  -0.0259 -0.0075 56  LEU B C   
4540 O O   . LEU B 56  ? 0.3552 0.3191 0.2734 0.0101  -0.0313 -0.0076 56  LEU B O   
4541 C CB  . LEU B 56  ? 0.3349 0.3101 0.2663 0.0122  -0.0249 -0.0081 56  LEU B CB  
4542 C CG  . LEU B 56  ? 0.3624 0.3440 0.3023 0.0116  -0.0232 -0.0077 56  LEU B CG  
4543 C CD1 . LEU B 56  ? 0.3762 0.3571 0.3217 0.0147  -0.0269 -0.0093 56  LEU B CD1 
4544 C CD2 . LEU B 56  ? 0.3555 0.3413 0.2958 0.0130  -0.0160 -0.0087 56  LEU B CD2 
4545 N N   . THR B 57  ? 0.3200 0.2867 0.2315 0.0115  -0.0221 -0.0083 57  THR B N   
4546 C CA  . THR B 57  ? 0.3923 0.3532 0.2966 0.0131  -0.0244 -0.0098 57  THR B CA  
4547 C C   . THR B 57  ? 0.3422 0.3001 0.2462 0.0182  -0.0260 -0.0131 57  THR B C   
4548 O O   . THR B 57  ? 0.3160 0.2765 0.2228 0.0213  -0.0229 -0.0145 57  THR B O   
4549 C CB  . THR B 57  ? 0.3409 0.3013 0.2380 0.0135  -0.0202 -0.0097 57  THR B CB  
4550 O OG1 . THR B 57  ? 0.3398 0.3018 0.2352 0.0175  -0.0149 -0.0113 57  THR B OG1 
4551 C CG2 . THR B 57  ? 0.2523 0.2164 0.1509 0.0086  -0.0182 -0.0067 57  THR B CG2 
4552 N N   . PRO B 58  ? 0.2575 0.2136 0.3025 -0.0345 -0.0096 -0.0093 58  PRO B N   
4553 C CA  . PRO B 58  ? 0.2879 0.2365 0.3218 -0.0326 -0.0099 -0.0177 58  PRO B CA  
4554 C C   . PRO B 58  ? 0.3617 0.3183 0.3826 -0.0280 -0.0143 -0.0194 58  PRO B C   
4555 O O   . PRO B 58  ? 0.3327 0.2840 0.3414 -0.0238 -0.0125 -0.0227 58  PRO B O   
4556 C CB  . PRO B 58  ? 0.3194 0.2626 0.3618 -0.0391 -0.0133 -0.0265 58  PRO B CB  
4557 C CG  . PRO B 58  ? 0.3313 0.2746 0.3895 -0.0440 -0.0117 -0.0216 58  PRO B CG  
4558 C CD  . PRO B 58  ? 0.2444 0.1998 0.3038 -0.0416 -0.0124 -0.0120 58  PRO B CD  
4559 N N   . VAL B 59  ? 0.2784 0.2474 0.3013 -0.0284 -0.0200 -0.0172 59  VAL B N   
4560 C CA  . VAL B 59  ? 0.3223 0.2990 0.3325 -0.0237 -0.0241 -0.0187 59  VAL B CA  
4561 C C   . VAL B 59  ? 0.2800 0.2585 0.2804 -0.0168 -0.0193 -0.0112 59  VAL B C   
4562 O O   . VAL B 59  ? 0.3435 0.3227 0.3305 -0.0119 -0.0200 -0.0134 59  VAL B O   
4563 C CB  . VAL B 59  ? 0.2778 0.2675 0.2927 -0.0257 -0.0314 -0.0182 59  VAL B CB  
4564 C CG1 . VAL B 59  ? 0.2569 0.2544 0.2812 -0.0263 -0.0298 -0.0081 59  VAL B CG1 
4565 C CG2 . VAL B 59  ? 0.2980 0.2954 0.2992 -0.0206 -0.0358 -0.0203 59  VAL B CG2 
4566 N N   . LEU B 60  ? 0.2765 0.2559 0.2834 -0.0164 -0.0143 -0.0024 60  LEU B N   
4567 C CA  . LEU B 60  ? 0.3061 0.2865 0.3041 -0.0100 -0.0091 0.0044  60  LEU B CA  
4568 C C   . LEU B 60  ? 0.2528 0.2207 0.2428 -0.0075 -0.0038 0.0011  60  LEU B C   
4569 O O   . LEU B 60  ? 0.3177 0.2853 0.2949 -0.0017 -0.0020 0.0016  60  LEU B O   
4570 C CB  . LEU B 60  ? 0.2911 0.2758 0.2986 -0.0104 -0.0051 0.0145  60  LEU B CB  
4571 C CG  . LEU B 60  ? 0.2895 0.2720 0.2900 -0.0047 0.0018  0.0211  60  LEU B CG  
4572 C CD1 . LEU B 60  ? 0.2656 0.2562 0.2536 0.0014  0.0003  0.0234  60  LEU B CD1 
4573 C CD2 . LEU B 60  ? 0.2668 0.2515 0.2785 -0.0060 0.0064  0.0301  60  LEU B CD2 
4574 N N   . ILE B 61  ? 0.3098 0.2671 0.3071 -0.0115 -0.0010 -0.0023 61  ILE B N   
4575 C CA  . ILE B 61  ? 0.3311 0.2761 0.3212 -0.0094 0.0041  -0.0061 61  ILE B CA  
4576 C C   . ILE B 61  ? 0.3698 0.3130 0.3466 -0.0068 0.0007  -0.0140 61  ILE B C   
4577 O O   . ILE B 61  ? 0.3608 0.2992 0.3261 -0.0017 0.0043  -0.0141 61  ILE B O   
4578 C CB  . ILE B 61  ? 0.3186 0.2528 0.3192 -0.0148 0.0067  -0.0096 61  ILE B CB  
4579 C CG1 . ILE B 61  ? 0.2512 0.1860 0.2633 -0.0164 0.0112  -0.0012 61  ILE B CG1 
4580 C CG2 . ILE B 61  ? 0.3698 0.2910 0.3625 -0.0127 0.0115  -0.0145 61  ILE B CG2 
4581 C CD1 . ILE B 61  ? 0.2678 0.1930 0.2914 -0.0219 0.0135  -0.0041 61  ILE B CD1 
4582 N N   . ASP B 62  ? 0.2961 0.2433 0.2744 -0.0100 -0.0062 -0.0206 62  ASP B N   
4583 C CA  . ASP B 62  ? 0.4553 0.4012 0.4212 -0.0077 -0.0098 -0.0285 62  ASP B CA  
4584 C C   . ASP B 62  ? 0.4523 0.4044 0.4047 -0.0006 -0.0094 -0.0243 62  ASP B C   
4585 O O   . ASP B 62  ? 0.3824 0.3286 0.3228 0.0035  -0.0072 -0.0274 62  ASP B O   
4586 C CB  . ASP B 62  ? 0.4317 0.3836 0.4016 -0.0120 -0.0178 -0.0352 62  ASP B CB  
4587 C CG  . ASP B 62  ? 0.4728 0.4168 0.4531 -0.0186 -0.0186 -0.0420 62  ASP B CG  
4588 O OD1 . ASP B 62  ? 0.4989 0.4308 0.4789 -0.0192 -0.0135 -0.0448 62  ASP B OD1 
4589 O OD2 . ASP B 62  ? 0.4587 0.4086 0.4476 -0.0233 -0.0241 -0.0447 62  ASP B OD2 
4590 N N   . GLN B 63  ? 0.4018 0.3658 0.3563 0.0009  -0.0113 -0.0172 63  GLN B N   
4591 C CA  . GLN B 63  ? 0.3221 0.2929 0.2643 0.0076  -0.0113 -0.0131 63  GLN B CA  
4592 C C   . GLN B 63  ? 0.3468 0.3120 0.2832 0.0124  -0.0036 -0.0074 63  GLN B C   
4593 O O   . GLN B 63  ? 0.3978 0.3620 0.3211 0.0179  -0.0022 -0.0079 63  GLN B O   
4594 C CB  . GLN B 63  ? 0.2974 0.2820 0.2444 0.0077  -0.0149 -0.0067 63  GLN B CB  
4595 C CG  . GLN B 63  ? 0.2696 0.2600 0.2240 0.0025  -0.0223 -0.0117 63  GLN B CG  
4596 C CD  . GLN B 63  ? 0.4702 0.4738 0.4311 0.0021  -0.0254 -0.0049 63  GLN B CD  
4597 O OE1 . GLN B 63  ? 0.4605 0.4730 0.4134 0.0065  -0.0277 -0.0022 63  GLN B OE1 
4598 N NE2 . GLN B 63  ? 0.4017 0.4064 0.3772 -0.0033 -0.0253 -0.0021 63  GLN B NE2 
4599 N N   . ILE B 64  ? 0.3976 0.3592 0.3437 0.0105  0.0016  -0.0020 64  ILE B N   
4600 C CA  . ILE B 64  ? 0.3468 0.3026 0.2879 0.0149  0.0090  0.0029  64  ILE B CA  
4601 C C   . ILE B 64  ? 0.3607 0.3048 0.2918 0.0167  0.0113  -0.0042 64  ILE B C   
4602 O O   . ILE B 64  ? 0.3773 0.3193 0.2970 0.0224  0.0147  -0.0026 64  ILE B O   
4603 C CB  . ILE B 64  ? 0.3576 0.3108 0.3115 0.0120  0.0140  0.0089  64  ILE B CB  
4604 C CG1 . ILE B 64  ? 0.3611 0.3263 0.3214 0.0125  0.0135  0.0179  64  ILE B CG1 
4605 C CG2 . ILE B 64  ? 0.4301 0.3733 0.3794 0.0154  0.0217  0.0110  64  ILE B CG2 
4606 C CD1 . ILE B 64  ? 0.3134 0.2772 0.2874 0.0090  0.0174  0.0237  64  ILE B CD1 
4607 N N   . GLN B 65  ? 0.3015 0.2381 0.2366 0.0119  0.0093  -0.0123 65  GLN B N   
4608 C CA  . GLN B 65  ? 0.4119 0.3372 0.3381 0.0133  0.0114  -0.0195 65  GLN B CA  
4609 C C   . GLN B 65  ? 0.4522 0.3806 0.3637 0.0177  0.0078  -0.0236 65  GLN B C   
4610 O O   . GLN B 65  ? 0.4410 0.3634 0.3413 0.0222  0.0114  -0.0246 65  GLN B O   
4611 C CB  . GLN B 65  ? 0.4469 0.3643 0.3810 0.0070  0.0096  -0.0275 65  GLN B CB  
4612 C CG  . GLN B 65  ? 0.4525 0.3619 0.3980 0.0036  0.0151  -0.0248 65  GLN B CG  
4613 C CD  . GLN B 65  ? 0.5125 0.4143 0.4661 -0.0027 0.0133  -0.0330 65  GLN B CD  
4614 O OE1 . GLN B 65  ? 0.4201 0.3272 0.3791 -0.0068 0.0070  -0.0371 65  GLN B OE1 
4615 N NE2 . GLN B 65  ? 0.6302 0.5194 0.5845 -0.0034 0.0188  -0.0354 65  GLN B NE2 
4616 N N   . GLU B 66  ? 0.4776 0.4155 0.3891 0.0164  0.0007  -0.0261 66  GLU B N   
4617 C CA  . GLU B 66  ? 0.4866 0.4281 0.3842 0.0207  -0.0031 -0.0300 66  GLU B CA  
4618 C C   . GLU B 66  ? 0.4617 0.4072 0.3493 0.0278  0.0006  -0.0227 66  GLU B C   
4619 O O   . GLU B 66  ? 0.4358 0.3775 0.3102 0.0323  0.0017  -0.0254 66  GLU B O   
4620 C CB  . GLU B 66  ? 0.4897 0.4419 0.3900 0.0183  -0.0112 -0.0328 66  GLU B CB  
4621 C CG  . GLU B 66  ? 0.5564 0.5101 0.4438 0.0210  -0.0161 -0.0400 66  GLU B CG  
4622 C CD  . GLU B 66  ? 0.6067 0.5701 0.4976 0.0181  -0.0244 -0.0439 66  GLU B CD  
4623 O OE1 . GLU B 66  ? 0.5676 0.5358 0.4715 0.0134  -0.0264 -0.0417 66  GLU B OE1 
4624 O OE2 . GLU B 66  ? 0.6390 0.6054 0.5195 0.0206  -0.0288 -0.0492 66  GLU B OE2 
4625 N N   . TYR B 67  ? 0.3323 0.2850 0.2259 0.0287  0.0027  -0.0135 67  TYR B N   
4626 C CA  . TYR B 67  ? 0.3611 0.3175 0.2459 0.0353  0.0066  -0.0064 67  TYR B CA  
4627 C C   . TYR B 67  ? 0.4880 0.4334 0.3677 0.0382  0.0139  -0.0057 67  TYR B C   
4628 O O   . TYR B 67  ? 0.5233 0.4674 0.3906 0.0439  0.0162  -0.0048 67  TYR B O   
4629 C CB  . TYR B 67  ? 0.3219 0.2881 0.2156 0.0352  0.0076  0.0032  67  TYR B CB  
4630 C CG  . TYR B 67  ? 0.3818 0.3610 0.2752 0.0357  0.0016  0.0051  67  TYR B CG  
4631 C CD1 . TYR B 67  ? 0.3583 0.3442 0.2406 0.0419  0.0014  0.0084  67  TYR B CD1 
4632 C CD2 . TYR B 67  ? 0.3865 0.3713 0.2911 0.0302  -0.0036 0.0038  67  TYR B CD2 
4633 C CE1 . TYR B 67  ? 0.3815 0.3795 0.2635 0.0426  -0.0039 0.0104  67  TYR B CE1 
4634 C CE2 . TYR B 67  ? 0.3475 0.3445 0.2519 0.0309  -0.0090 0.0057  67  TYR B CE2 
4635 C CZ  . TYR B 67  ? 0.3625 0.3660 0.2555 0.0371  -0.0091 0.0090  67  TYR B CZ  
4636 O OH  . TYR B 67  ? 0.3225 0.3381 0.2153 0.0380  -0.0143 0.0111  67  TYR B OH  
4637 N N   . ALA B 68  ? 0.5058 0.4432 0.3950 0.0343  0.0176  -0.0059 68  ALA B N   
4638 C CA  . ALA B 68  ? 0.4569 0.3835 0.3424 0.0367  0.0247  -0.0052 68  ALA B CA  
4639 C C   . ALA B 68  ? 0.4815 0.3995 0.3545 0.0389  0.0245  -0.0131 68  ALA B C   
4640 O O   . ALA B 68  ? 0.5140 0.4276 0.3770 0.0440  0.0291  -0.0117 68  ALA B O   
4641 C CB  . ALA B 68  ? 0.4477 0.3673 0.3464 0.0314  0.0277  -0.0050 68  ALA B CB  
4642 N N   . GLN B 69  ? 0.3629 0.2786 0.2366 0.0350  0.0194  -0.0217 69  GLN B N   
4643 C CA  . GLN B 69  ? 0.4764 0.3841 0.3387 0.0366  0.0190  -0.0298 69  GLN B CA  
4644 C C   . GLN B 69  ? 0.6058 0.5198 0.4543 0.0421  0.0159  -0.0303 69  GLN B C   
4645 O O   . GLN B 69  ? 0.6702 0.5780 0.5076 0.0444  0.0159  -0.0363 69  GLN B O   
4646 C CB  . GLN B 69  ? 0.4454 0.3489 0.3133 0.0306  0.0144  -0.0391 69  GLN B CB  
4647 C CG  . GLN B 69  ? 0.5571 0.4518 0.4372 0.0254  0.0181  -0.0400 69  GLN B CG  
4648 C CD  . GLN B 69  ? 0.6486 0.5425 0.5377 0.0187  0.0128  -0.0476 69  GLN B CD  
4649 O OE1 . GLN B 69  ? 0.7392 0.6382 0.6244 0.0179  0.0064  -0.0532 69  GLN B OE1 
4650 N NE2 . GLN B 69  ? 0.6128 0.5004 0.5139 0.0138  0.0155  -0.0477 69  GLN B NE2 
4651 N N   . GLY B 70  ? 0.5981 0.5240 0.4468 0.0442  0.0135  -0.0242 70  GLY B N   
4652 C CA  . GLY B 70  ? 0.5781 0.5104 0.4139 0.0496  0.0108  -0.0241 70  GLY B CA  
4653 C C   . GLY B 70  ? 0.5753 0.5120 0.4076 0.0479  0.0030  -0.0316 70  GLY B C   
4654 O O   . GLY B 70  ? 0.5883 0.5262 0.4077 0.0522  0.0011  -0.0345 70  GLY B O   
4655 N N   . LYS B 71  ? 0.5837 0.5228 0.4271 0.0417  -0.0015 -0.0350 71  LYS B N   
4656 C CA  . LYS B 71  ? 0.5634 0.5070 0.4046 0.0397  -0.0092 -0.0426 71  LYS B CA  
4657 C C   . LYS B 71  ? 0.5099 0.4674 0.3559 0.0391  -0.0146 -0.0386 71  LYS B C   
4658 O O   . LYS B 71  ? 0.4850 0.4478 0.3285 0.0381  -0.0213 -0.0442 71  LYS B O   
4659 C CB  . LYS B 71  ? 0.6262 0.5623 0.4757 0.0331  -0.0110 -0.0508 71  LYS B CB  
4660 C CG  . LYS B 71  ? 0.6918 0.6138 0.5369 0.0332  -0.0059 -0.0557 71  LYS B CG  
4661 C CD  . LYS B 71  ? 0.7525 0.6669 0.6103 0.0263  -0.0051 -0.0599 71  LYS B CD  
4662 C CE  . LYS B 71  ? 0.7985 0.7063 0.6532 0.0234  -0.0085 -0.0714 71  LYS B CE  
4663 N NZ  . LYS B 71  ? 0.7969 0.7042 0.6653 0.0160  -0.0118 -0.0760 71  LYS B NZ  
4664 N N   . ALA B 72  ? 0.4614 0.4249 0.3143 0.0397  -0.0119 -0.0293 72  ALA B N   
4665 C CA  . ALA B 72  ? 0.4632 0.4397 0.3215 0.0390  -0.0166 -0.0250 72  ALA B CA  
4666 C C   . ALA B 72  ? 0.5574 0.5418 0.4026 0.0454  -0.0188 -0.0231 72  ALA B C   
4667 O O   . ALA B 72  ? 0.5767 0.5609 0.4146 0.0509  -0.0140 -0.0174 72  ALA B O   
4668 C CB  . ALA B 72  ? 0.4118 0.3918 0.2816 0.0377  -0.0126 -0.0156 72  ALA B CB  
4669 N N   . LYS B 73  ? 0.5560 0.5474 0.3984 0.0449  -0.0260 -0.0280 73  LYS B N   
4670 C CA  . LYS B 73  ? 0.5801 0.5801 0.4108 0.0509  -0.0286 -0.0261 73  LYS B CA  
4671 C C   . LYS B 73  ? 0.5111 0.5235 0.3492 0.0507  -0.0306 -0.0184 73  LYS B C   
4672 O O   . LYS B 73  ? 0.5068 0.5268 0.3496 0.0479  -0.0369 -0.0208 73  LYS B O   
4673 C CB  . LYS B 73  ? 0.6109 0.6115 0.4333 0.0509  -0.0352 -0.0356 73  LYS B CB  
4674 C CG  . LYS B 73  ? 0.6544 0.6423 0.4705 0.0504  -0.0334 -0.0438 73  LYS B CG  
4675 C CD  . LYS B 73  ? 0.7530 0.7420 0.5620 0.0499  -0.0402 -0.0538 73  LYS B CD  
4676 C CE  . LYS B 73  ? 0.7945 0.7866 0.6154 0.0430  -0.0461 -0.0592 73  LYS B CE  
4677 N NZ  . LYS B 73  ? 0.7765 0.7579 0.6074 0.0370  -0.0434 -0.0633 73  LYS B NZ  
4678 N N   . ASP B 74  ? 0.4259 0.4405 0.2650 0.0538  -0.0250 -0.0091 74  ASP B N   
4679 C CA  . ASP B 74  ? 0.3958 0.4214 0.2428 0.0536  -0.0256 -0.0010 74  ASP B CA  
4680 C C   . ASP B 74  ? 0.4538 0.4887 0.2897 0.0600  -0.0273 0.0025  74  ASP B C   
4681 O O   . ASP B 74  ? 0.4856 0.5183 0.3113 0.0657  -0.0229 0.0056  74  ASP B O   
4682 C CB  . ASP B 74  ? 0.3683 0.3911 0.2233 0.0531  -0.0184 0.0071  74  ASP B CB  
4683 C CG  . ASP B 74  ? 0.4610 0.4942 0.3266 0.0517  -0.0187 0.0152  74  ASP B CG  
4684 O OD1 . ASP B 74  ? 0.4407 0.4842 0.3021 0.0549  -0.0216 0.0183  74  ASP B OD1 
4685 O OD2 . ASP B 74  ? 0.4669 0.4979 0.3449 0.0474  -0.0159 0.0185  74  ASP B OD2 
4686 N N   . VAL B 75  ? 0.4568 0.5021 0.2951 0.0591  -0.0335 0.0022  75  VAL B N   
4687 C CA  . VAL B 75  ? 0.4874 0.5414 0.3145 0.0652  -0.0359 0.0042  75  VAL B CA  
4688 C C   . VAL B 75  ? 0.4748 0.5345 0.3018 0.0695  -0.0307 0.0149  75  VAL B C   
4689 O O   . VAL B 75  ? 0.4919 0.5538 0.3070 0.0759  -0.0291 0.0173  75  VAL B O   
4690 C CB  . VAL B 75  ? 0.6087 0.6723 0.4385 0.0630  -0.0441 0.0008  75  VAL B CB  
4691 C CG1 . VAL B 75  ? 0.6723 0.7301 0.5039 0.0581  -0.0489 -0.0099 75  VAL B CG1 
4692 C CG2 . VAL B 75  ? 0.6272 0.6993 0.4708 0.0595  -0.0448 0.0073  75  VAL B CG2 
4693 N N   . PHE B 76  ? 0.4822 0.5441 0.3223 0.0661  -0.0278 0.0213  76  PHE B N   
4694 C CA  . PHE B 76  ? 0.4478 0.5144 0.2885 0.0698  -0.0222 0.0313  76  PHE B CA  
4695 C C   . PHE B 76  ? 0.4157 0.4733 0.2500 0.0734  -0.0150 0.0331  76  PHE B C   
4696 O O   . PHE B 76  ? 0.3701 0.4302 0.1991 0.0784  -0.0109 0.0385  76  PHE B O   
4697 C CB  . PHE B 76  ? 0.5218 0.5929 0.3785 0.0650  -0.0211 0.0373  76  PHE B CB  
4698 C CG  . PHE B 76  ? 0.6311 0.7144 0.4923 0.0641  -0.0263 0.0398  76  PHE B CG  
4699 C CD1 . PHE B 76  ? 0.5981 0.6838 0.4643 0.0595  -0.0333 0.0335  76  PHE B CD1 
4700 C CD2 . PHE B 76  ? 0.6170 0.7084 0.4793 0.0673  -0.0237 0.0476  76  PHE B CD2 
4701 C CE1 . PHE B 76  ? 0.5546 0.6517 0.4248 0.0588  -0.0381 0.0358  76  PHE B CE1 
4702 C CE2 . PHE B 76  ? 0.5874 0.6877 0.4566 0.0652  -0.0276 0.0489  76  PHE B CE2 
4703 C CZ  . PHE B 76  ? 0.5657 0.6718 0.4349 0.0629  -0.0358 0.0445  76  PHE B CZ  
4704 N N   . LEU B 77  ? 0.4365 0.4830 0.2732 0.0701  -0.0131 0.0283  77  LEU B N   
4705 C CA  . LEU B 77  ? 0.5151 0.5526 0.3454 0.0734  -0.0065 0.0292  77  LEU B CA  
4706 C C   . LEU B 77  ? 0.5654 0.6007 0.3788 0.0794  -0.0071 0.0254  77  LEU B C   
4707 O O   . LEU B 77  ? 0.5002 0.5319 0.3060 0.0843  -0.0016 0.0286  77  LEU B O   
4708 C CB  . LEU B 77  ? 0.5609 0.5871 0.3977 0.0684  -0.0046 0.0244  77  LEU B CB  
4709 C CG  . LEU B 77  ? 0.5538 0.5720 0.3928 0.0692  0.0033  0.0285  77  LEU B CG  
4710 C CD1 . LEU B 77  ? 0.5865 0.6118 0.4313 0.0711  0.0077  0.0387  77  LEU B CD1 
4711 C CD2 . LEU B 77  ? 0.3864 0.3958 0.2357 0.0629  0.0040  0.0244  77  LEU B CD2 
4712 N N   . GLU B 78  ? 0.5744 0.6116 0.3819 0.0792  -0.0137 0.0184  78  GLU B N   
4713 C CA  . GLU B 78  ? 0.6419 0.6777 0.4332 0.0851  -0.0146 0.0149  78  GLU B CA  
4714 C C   . GLU B 78  ? 0.6069 0.6509 0.3969 0.0893  -0.0129 0.0215  78  GLU B C   
4715 O O   . GLU B 78  ? 0.6060 0.6462 0.3928 0.0919  -0.0094 0.0215  78  GLU B O   
4716 C CB  . GLU B 78  ? 0.7038 0.7403 0.4909 0.0832  -0.0222 0.0056  78  GLU B CB  
4717 C CG  . GLU B 78  ? 0.7864 0.8124 0.5768 0.0781  -0.0232 -0.0028 78  GLU B CG  
4718 C CD  . GLU B 78  ? 0.8855 0.9003 0.6653 0.0813  -0.0188 -0.0061 78  GLU B CD  
4719 O OE1 . GLU B 78  ? 0.9097 0.9255 0.6763 0.0875  -0.0179 -0.0054 78  GLU B OE1 
4720 O OE2 . GLU B 78  ? 0.9014 0.9064 0.6861 0.0776  -0.0161 -0.0093 78  GLU B OE2 
4721 N N   . ALA B 79  ? 0.5641 0.6177 0.3649 0.0869  -0.0147 0.0262  79  ALA B N   
4722 C CA  . ALA B 79  ? 0.5061 0.5650 0.3153 0.0873  -0.0120 0.0312  79  ALA B CA  
4723 C C   . ALA B 79  ? 0.5521 0.6074 0.3717 0.0866  -0.0042 0.0366  79  ALA B C   
4724 O O   . ALA B 79  ? 0.5451 0.6017 0.3690 0.0880  -0.0012 0.0388  79  ALA B O   
4725 C CB  . ALA B 79  ? 0.4205 0.4896 0.2384 0.0847  -0.0159 0.0339  79  ALA B CB  
4726 N N   . ILE B 80  ? 0.4704 0.5212 0.2944 0.0845  -0.0012 0.0384  80  ILE B N   
4727 C CA  . ILE B 80  ? 0.4518 0.4986 0.2858 0.0837  0.0058  0.0424  80  ILE B CA  
4728 C C   . ILE B 80  ? 0.5157 0.5539 0.3413 0.0869  0.0090  0.0394  80  ILE B C   
4729 O O   . ILE B 80  ? 0.4869 0.5243 0.3178 0.0881  0.0128  0.0411  80  ILE B O   
4730 C CB  . ILE B 80  ? 0.4626 0.5077 0.3051 0.0801  0.0079  0.0453  80  ILE B CB  
4731 C CG1 . ILE B 80  ? 0.4934 0.5474 0.3466 0.0765  0.0052  0.0489  80  ILE B CG1 
4732 C CG2 . ILE B 80  ? 0.5199 0.5600 0.3718 0.0794  0.0146  0.0479  80  ILE B CG2 
4733 C CD1 . ILE B 80  ? 0.5847 0.6423 0.4542 0.0741  0.0093  0.0533  80  ILE B CD1 
4734 N N   . ARG B 81  ? 0.5480 0.5795 0.3604 0.0884  0.0073  0.0344  81  ARG B N   
4735 C CA  . ARG B 81  ? 0.5142 0.5363 0.3191 0.0910  0.0108  0.0316  81  ARG B CA  
4736 C C   . ARG B 81  ? 0.4911 0.5141 0.2904 0.0944  0.0101  0.0297  81  ARG B C   
4737 O O   . ARG B 81  ? 0.5206 0.5393 0.3214 0.0960  0.0142  0.0305  81  ARG B O   
4738 C CB  . ARG B 81  ? 0.5763 0.5901 0.3677 0.0917  0.0090  0.0255  81  ARG B CB  
4739 C CG  . ARG B 81  ? 0.6861 0.6888 0.4707 0.0938  0.0135  0.0226  81  ARG B CG  
4740 C CD  . ARG B 81  ? 0.7364 0.7304 0.5054 0.0949  0.0109  0.0143  81  ARG B CD  
4741 N NE  . ARG B 81  ? 0.7441 0.7335 0.5251 0.0887  0.0115  0.0130  81  ARG B NE  
4742 C CZ  . ARG B 81  ? 0.7775 0.7580 0.5622 0.0877  0.0173  0.0141  81  ARG B CZ  
4743 N NH1 . ARG B 81  ? 0.7777 0.7532 0.5537 0.0927  0.0230  0.0165  81  ARG B NH1 
4744 N NH2 . ARG B 81  ? 0.7509 0.7276 0.5481 0.0816  0.0175  0.0128  81  ARG B NH2 
4745 N N   . LYS B 82  ? 0.5053 0.5340 0.2987 0.0954  0.0047  0.0272  82  LYS B N   
4746 C CA  . LYS B 82  ? 0.5657 0.5941 0.3511 0.0988  0.0035  0.0244  82  LYS B CA  
4747 C C   . LYS B 82  ? 0.6303 0.6616 0.4253 0.0997  0.0075  0.0291  82  LYS B C   
4748 O O   . LYS B 82  ? 0.5878 0.6244 0.3957 0.0975  0.0093  0.0339  82  LYS B O   
4749 C CB  . LYS B 82  ? 0.6176 0.6526 0.3966 0.0993  -0.0033 0.0211  82  LYS B CB  
4750 C CG  . LYS B 82  ? 0.7188 0.7494 0.4844 0.0998  -0.0082 0.0133  82  LYS B CG  
4751 C CD  . LYS B 82  ? 0.7652 0.8039 0.5284 0.0991  -0.0155 0.0104  82  LYS B CD  
4752 C CE  . LYS B 82  ? 0.8122 0.8512 0.5656 0.1022  -0.0185 0.0058  82  LYS B CE  
4753 N NZ  . LYS B 82  ? 0.8829 0.9307 0.6352 0.1018  -0.0254 0.0035  82  LYS B NZ  
4754 N N   . ASP B 83  ? 0.6125 0.6399 0.4011 0.1029  0.0088  0.0271  83  ASP B N   
4755 C CA  . ASP B 83  ? 0.5417 0.5725 0.3369 0.1044  0.0112  0.0303  83  ASP B CA  
4756 C C   . ASP B 83  ? 0.4976 0.5373 0.2951 0.1042  0.0077  0.0315  83  ASP B C   
4757 O O   . ASP B 83  ? 0.4913 0.5332 0.2796 0.1050  0.0027  0.0280  83  ASP B O   
4758 C CB  . ASP B 83  ? 0.5690 0.5945 0.3549 0.1081  0.0120  0.0274  83  ASP B CB  
4759 C CG  . ASP B 83  ? 0.5939 0.6202 0.3883 0.1095  0.0160  0.0308  83  ASP B CG  
4760 O OD1 . ASP B 83  ? 0.5003 0.5331 0.2997 0.1101  0.0155  0.0330  83  ASP B OD1 
4761 O OD2 . ASP B 83  ? 0.6195 0.6398 0.4155 0.1101  0.0196  0.0311  83  ASP B OD2 
4762 N N   . PRO B 84  ? 0.4550 0.5002 0.2651 0.1031  0.0100  0.0360  84  PRO B N   
4763 C CA  . PRO B 84  ? 0.4218 0.4751 0.2343 0.1030  0.0071  0.0372  84  PRO B CA  
4764 C C   . PRO B 84  ? 0.4823 0.5365 0.2838 0.1067  0.0041  0.0342  84  PRO B C   
4765 O O   . PRO B 84  ? 0.5162 0.5760 0.3147 0.1067  -0.0002 0.0333  84  PRO B O   
4766 C CB  . PRO B 84  ? 0.4117 0.4682 0.2384 0.1021  0.0114  0.0416  84  PRO B CB  
4767 C CG  . PRO B 84  ? 0.4104 0.4624 0.2445 0.0999  0.0151  0.0430  84  PRO B CG  
4768 C CD  . PRO B 84  ? 0.4491 0.4931 0.2720 0.1016  0.0151  0.0396  84  PRO B CD  
4769 N N   . ASP B 85  ? 0.4810 0.5298 0.2763 0.1097  0.0060  0.0325  85  ASP B N   
4770 C CA  . ASP B 85  ? 0.5052 0.5544 0.2897 0.1132  0.0032  0.0294  85  ASP B CA  
4771 C C   . ASP B 85  ? 0.5556 0.6041 0.3280 0.1133  -0.0024 0.0241  85  ASP B C   
4772 O O   . ASP B 85  ? 0.5643 0.6153 0.3288 0.1155  -0.0061 0.0213  85  ASP B O   
4773 C CB  . ASP B 85  ? 0.5637 0.6068 0.3443 0.1163  0.0065  0.0286  85  ASP B CB  
4774 C CG  . ASP B 85  ? 0.5986 0.6438 0.3901 0.1171  0.0108  0.0328  85  ASP B CG  
4775 O OD1 . ASP B 85  ? 0.6059 0.6578 0.4050 0.1164  0.0107  0.0356  85  ASP B OD1 
4776 O OD2 . ASP B 85  ? 0.6006 0.6407 0.3930 0.1184  0.0142  0.0331  85  ASP B OD2 
4777 N N   . ASP B 86  ? 0.5645 0.6095 0.3355 0.1109  -0.0033 0.0223  86  ASP B N   
4778 C CA  . ASP B 86  ? 0.5881 0.6322 0.3483 0.1106  -0.0089 0.0164  86  ASP B CA  
4779 C C   . ASP B 86  ? 0.5560 0.6073 0.3206 0.1076  -0.0132 0.0169  86  ASP B C   
4780 O O   . ASP B 86  ? 0.5616 0.6129 0.3186 0.1069  -0.0186 0.0115  86  ASP B O   
4781 C CB  . ASP B 86  ? 0.6407 0.6757 0.3953 0.1100  -0.0074 0.0130  86  ASP B CB  
4782 C CG  . ASP B 86  ? 0.6600 0.6876 0.4095 0.1128  -0.0036 0.0120  86  ASP B CG  
4783 O OD1 . ASP B 86  ? 0.6426 0.6720 0.3894 0.1156  -0.0038 0.0120  86  ASP B OD1 
4784 O OD2 . ASP B 86  ? 0.6871 0.7071 0.4358 0.1123  -0.0003 0.0112  86  ASP B OD2 
4785 N N   . LEU B 87  ? 0.4695 0.5267 0.2463 0.1058  -0.0113 0.0227  87  LEU B N   
4786 C CA  . LEU B 87  ? 0.4330 0.4971 0.2153 0.1028  -0.0151 0.0237  87  LEU B CA  
4787 C C   . LEU B 87  ? 0.4880 0.5587 0.2655 0.1040  -0.0207 0.0213  87  LEU B C   
4788 O O   . LEU B 87  ? 0.4846 0.5576 0.2618 0.1066  -0.0195 0.0227  87  LEU B O   
4789 C CB  . LEU B 87  ? 0.4572 0.5250 0.2546 0.1002  -0.0108 0.0305  87  LEU B CB  
4790 C CG  . LEU B 87  ? 0.5403 0.6037 0.3454 0.0976  -0.0064 0.0332  87  LEU B CG  
4791 C CD1 . LEU B 87  ? 0.5355 0.6032 0.3560 0.0953  -0.0024 0.0391  87  LEU B CD1 
4792 C CD2 . LEU B 87  ? 0.4875 0.5501 0.2898 0.0951  -0.0101 0.0308  87  LEU B CD2 
4793 N N   . GLU B 88  ? 0.4770 0.5511 0.2512 0.1022  -0.0269 0.0175  88  GLU B N   
4794 C CA  . GLU B 88  ? 0.5053 0.5874 0.2787 0.1024  -0.0324 0.0162  88  GLU B CA  
4795 C C   . GLU B 88  ? 0.5153 0.6042 0.3018 0.1002  -0.0305 0.0228  88  GLU B C   
4796 O O   . GLU B 88  ? 0.4480 0.5360 0.2442 0.0977  -0.0265 0.0272  88  GLU B O   
4797 C CB  . GLU B 88  ? 0.5222 0.6060 0.2896 0.1007  -0.0400 0.0095  88  GLU B CB  
4798 C CG  . GLU B 88  ? 0.5700 0.6467 0.3243 0.1025  -0.0422 0.0017  88  GLU B CG  
4799 C CD  . GLU B 88  ? 0.6589 0.7346 0.4099 0.0998  -0.0479 -0.0052 88  GLU B CD  
4800 O OE1 . GLU B 88  ? 0.6408 0.7195 0.4001 0.0965  -0.0486 -0.0027 88  GLU B OE1 
4801 O OE2 . GLU B 88  ? 0.6692 0.7408 0.4097 0.1008  -0.0518 -0.0134 88  GLU B OE2 
4802 N N   . LYS B 89  ? 0.4563 0.6439 0.4307 0.0662  0.0348  0.0644  89  LYS B N   
4803 C CA  . LYS B 89  ? 0.5437 0.7292 0.5228 0.0678  0.0372  0.0736  89  LYS B CA  
4804 C C   . LYS B 89  ? 0.5441 0.7220 0.5258 0.0657  0.0349  0.0727  89  LYS B C   
4805 O O   . LYS B 89  ? 0.4956 0.6642 0.4824 0.0654  0.0370  0.0775  89  LYS B O   
4806 C CB  . LYS B 89  ? 0.5885 0.7888 0.5647 0.0720  0.0392  0.0812  89  LYS B CB  
4807 C CG  . LYS B 89  ? 0.6349 0.8341 0.6147 0.0744  0.0417  0.0907  89  LYS B CG  
4808 C CD  . LYS B 89  ? 0.7034 0.8922 0.6885 0.0748  0.0470  0.0971  89  LYS B CD  
4809 C CE  . LYS B 89  ? 0.7442 0.9236 0.7338 0.0751  0.0491  0.1029  89  LYS B CE  
4810 N NZ  . LYS B 89  ? 0.7434 0.9079 0.7385 0.0724  0.0530  0.1044  89  LYS B NZ  
4811 N N   . GLU B 90  ? 0.5201 0.7015 0.4980 0.0638  0.0308  0.0664  90  GLU B N   
4812 C CA  . GLU B 90  ? 0.4585 0.6331 0.4388 0.0616  0.0285  0.0651  90  GLU B CA  
4813 C C   . GLU B 90  ? 0.4001 0.5579 0.3851 0.0587  0.0285  0.0620  90  GLU B C   
4814 O O   . GLU B 90  ? 0.3679 0.5179 0.3570 0.0578  0.0286  0.0646  90  GLU B O   
4815 C CB  . GLU B 90  ? 0.4340 0.6154 0.4090 0.0592  0.0244  0.0576  90  GLU B CB  
4816 C CG  . GLU B 90  ? 0.5080 0.6904 0.4844 0.0581  0.0222  0.0588  90  GLU B CG  
4817 C CD  . GLU B 90  ? 0.6715 0.8379 0.6514 0.0545  0.0207  0.0543  90  GLU B CD  
4818 O OE1 . GLU B 90  ? 0.7295 0.8858 0.7095 0.0526  0.0207  0.0488  90  GLU B OE1 
4819 O OE2 . GLU B 90  ? 0.7586 0.9232 0.7410 0.0540  0.0197  0.0565  90  GLU B OE2 
4820 N N   . GLU B 91  ? 0.3164 0.4693 0.3007 0.0576  0.0286  0.0568  91  GLU B N   
4821 C CA  . GLU B 91  ? 0.4006 0.5399 0.3889 0.0551  0.0283  0.0534  91  GLU B CA  
4822 C C   . GLU B 91  ? 0.4267 0.5602 0.4208 0.0553  0.0318  0.0596  91  GLU B C   
4823 O O   . GLU B 91  ? 0.4171 0.5403 0.4154 0.0529  0.0316  0.0592  91  GLU B O   
4824 C CB  . GLU B 91  ? 0.4370 0.5745 0.4224 0.0545  0.0275  0.0461  91  GLU B CB  
4825 C CG  . GLU B 91  ? 0.4855 0.6260 0.4647 0.0533  0.0247  0.0388  91  GLU B CG  
4826 C CD  . GLU B 91  ? 0.5357 0.6743 0.5112 0.0537  0.0253  0.0323  91  GLU B CD  
4827 O OE1 . GLU B 91  ? 0.5789 0.7078 0.5537 0.0520  0.0241  0.0263  91  GLU B OE1 
4828 O OE2 . GLU B 91  ? 0.5086 0.6552 0.4820 0.0561  0.0273  0.0336  91  GLU B OE2 
4829 N N   . VAL B 92  ? 0.4091 0.5492 0.4034 0.0577  0.0352  0.0649  92  VAL B N   
4830 C CA  . VAL B 92  ? 0.4365 0.5712 0.4361 0.0572  0.0393  0.0710  92  VAL B CA  
4831 C C   . VAL B 92  ? 0.5027 0.6331 0.5047 0.0573  0.0406  0.0765  92  VAL B C   
4832 O O   . VAL B 92  ? 0.4321 0.5529 0.4386 0.0552  0.0431  0.0790  92  VAL B O   
4833 C CB  . VAL B 92  ? 0.3839 0.5266 0.3828 0.0597  0.0432  0.0760  92  VAL B CB  
4834 C CG1 . VAL B 92  ? 0.3092 0.4586 0.3045 0.0606  0.0418  0.0705  92  VAL B CG1 
4835 C CG2 . VAL B 92  ? 0.4737 0.6252 0.4702 0.0633  0.0451  0.0831  92  VAL B CG2 
4836 N N   . GLU B 93  ? 0.5531 0.6908 0.5518 0.0596  0.0390  0.0782  93  GLU B N   
4837 C CA  . GLU B 93  ? 0.5732 0.7078 0.5740 0.0605  0.0400  0.0834  93  GLU B CA  
4838 C C   . GLU B 93  ? 0.4954 0.6189 0.4987 0.0568  0.0372  0.0784  93  GLU B C   
4839 O O   . GLU B 93  ? 0.5155 0.6295 0.5227 0.0557  0.0397  0.0817  93  GLU B O   
4840 C CB  . GLU B 93  ? 0.6297 0.7779 0.6263 0.0640  0.0384  0.0860  93  GLU B CB  
4841 C CG  . GLU B 93  ? 0.7634 0.9116 0.7619 0.0667  0.0405  0.0935  93  GLU B CG  
4842 C CD  . GLU B 93  ? 0.8532 1.0163 0.8479 0.0693  0.0374  0.0942  93  GLU B CD  
4843 O OE1 . GLU B 93  ? 0.8543 1.0160 0.8499 0.0682  0.0350  0.0928  93  GLU B OE1 
4844 O OE2 . GLU B 93  ? 0.8704 1.0475 0.8611 0.0721  0.0375  0.0962  93  GLU B OE2 
4845 N N   . LYS B 94  ? 0.4137 0.5376 0.4145 0.0548  0.0326  0.0704  94  LYS B N   
4846 C CA  . LYS B 94  ? 0.4002 0.5138 0.4030 0.0513  0.0300  0.0655  94  LYS B CA  
4847 C C   . LYS B 94  ? 0.3549 0.4571 0.3622 0.0487  0.0320  0.0651  94  LYS B C   
4848 O O   . LYS B 94  ? 0.3558 0.4491 0.3663 0.0466  0.0321  0.0654  94  LYS B O   
4849 C CB  . LYS B 94  ? 0.5298 0.6450 0.5286 0.0497  0.0257  0.0570  94  LYS B CB  
4850 C CG  . LYS B 94  ? 0.6365 0.7604 0.6312 0.0500  0.0229  0.0553  94  LYS B CG  
4851 C CD  . LYS B 94  ? 0.7016 0.8225 0.6930 0.0469  0.0194  0.0462  94  LYS B CD  
4852 C CE  . LYS B 94  ? 0.7331 0.8640 0.7203 0.0462  0.0168  0.0438  94  LYS B CE  
4853 N NZ  . LYS B 94  ? 0.7770 0.9175 0.7656 0.0490  0.0179  0.0518  94  LYS B NZ  
4854 N N   . LEU B 95  ? 0.4127 0.5162 0.4204 0.0486  0.0334  0.0642  95  LEU B N   
4855 C CA  . LEU B 95  ? 0.3841 0.4796 0.3962 0.0457  0.0351  0.0636  95  LEU B CA  
4856 C C   . LEU B 95  ? 0.3646 0.4545 0.3805 0.0447  0.0397  0.0699  95  LEU B C   
4857 O O   . LEU B 95  ? 0.3183 0.3992 0.3377 0.0413  0.0402  0.0689  95  LEU B O   
4858 C CB  . LEU B 95  ? 0.4471 0.5475 0.4588 0.0463  0.0362  0.0622  95  LEU B CB  
4859 C CG  . LEU B 95  ? 0.4812 0.5767 0.4964 0.0434  0.0361  0.0589  95  LEU B CG  
4860 C CD1 . LEU B 95  ? 0.4992 0.5926 0.5123 0.0435  0.0320  0.0520  95  LEU B CD1 
4861 C CD2 . LEU B 95  ? 0.4447 0.5464 0.4611 0.0440  0.0391  0.0607  95  LEU B CD2 
4862 N N   . ILE B 96  ? 0.3750 0.4700 0.3902 0.0476  0.0433  0.0765  96  ILE B N   
4863 C CA  . ILE B 96  ? 0.3670 0.4553 0.3852 0.0470  0.0489  0.0829  96  ILE B CA  
4864 C C   . ILE B 96  ? 0.4047 0.4859 0.4241 0.0467  0.0486  0.0841  96  ILE B C   
4865 O O   . ILE B 96  ? 0.3991 0.4697 0.4217 0.0435  0.0514  0.0846  96  ILE B O   
4866 C CB  . ILE B 96  ? 0.4003 0.4959 0.4170 0.0510  0.0532  0.0903  96  ILE B CB  
4867 C CG1 . ILE B 96  ? 0.3906 0.4912 0.4073 0.0502  0.0546  0.0893  96  ILE B CG1 
4868 C CG2 . ILE B 96  ? 0.4808 0.5684 0.4998 0.0513  0.0597  0.0977  96  ILE B CG2 
4869 C CD1 . ILE B 96  ? 0.4360 0.5455 0.4503 0.0543  0.0582  0.0958  96  ILE B CD1 
4870 N N   . GLU B 97  ? 0.3961 0.4832 0.4126 0.0497  0.0453  0.0840  97  GLU B N   
4871 C CA  . GLU B 97  ? 0.3973 0.4791 0.4148 0.0499  0.0450  0.0854  97  GLU B CA  
4872 C C   . GLU B 97  ? 0.3593 0.4312 0.3791 0.0451  0.0423  0.0791  97  GLU B C   
4873 O O   . GLU B 97  ? 0.3574 0.4204 0.3795 0.0438  0.0443  0.0806  97  GLU B O   
4874 C CB  . GLU B 97  ? 0.4829 0.5755 0.4970 0.0532  0.0412  0.0854  97  GLU B CB  
4875 C CG  . GLU B 97  ? 0.6696 0.7726 0.6818 0.0587  0.0441  0.0933  97  GLU B CG  
4876 C CD  . GLU B 97  ? 0.7980 0.9144 0.8065 0.0610  0.0396  0.0920  97  GLU B CD  
4877 O OE1 . GLU B 97  ? 0.8357 0.9641 0.8406 0.0628  0.0383  0.0916  97  GLU B OE1 
4878 O OE2 . GLU B 97  ? 0.8438 0.9593 0.8530 0.0606  0.0375  0.0910  97  GLU B OE2 
4879 N N   . PHE B 98  ? 0.3080 0.3813 0.3268 0.0430  0.0381  0.0721  98  PHE B N   
4880 C CA  . PHE B 98  ? 0.3125 0.3772 0.3332 0.0389  0.0356  0.0666  98  PHE B CA  
4881 C C   . PHE B 98  ? 0.3416 0.3981 0.3662 0.0354  0.0395  0.0676  98  PHE B C   
4882 O O   . PHE B 98  ? 0.3862 0.4342 0.4130 0.0324  0.0398  0.0663  98  PHE B O   
4883 C CB  . PHE B 98  ? 0.2640 0.3319 0.2824 0.0383  0.0311  0.0598  98  PHE B CB  
4884 C CG  . PHE B 98  ? 0.2572 0.3176 0.2768 0.0351  0.0282  0.0545  98  PHE B CG  
4885 C CD1 . PHE B 98  ? 0.3527 0.4111 0.3707 0.0348  0.0251  0.0519  98  PHE B CD1 
4886 C CD2 . PHE B 98  ? 0.3622 0.4185 0.3843 0.0324  0.0286  0.0521  98  PHE B CD2 
4887 C CE1 . PHE B 98  ? 0.3369 0.3882 0.3559 0.0321  0.0227  0.0474  98  PHE B CE1 
4888 C CE2 . PHE B 98  ? 0.3973 0.4476 0.4203 0.0300  0.0260  0.0477  98  PHE B CE2 
4889 C CZ  . PHE B 98  ? 0.3460 0.3932 0.3673 0.0299  0.0231  0.0455  98  PHE B CZ  
4890 N N   . THR B 99  ? 0.3133 0.3730 0.3387 0.0352  0.0426  0.0696  99  THR B N   
4891 C CA  . THR B 99  ? 0.3677 0.4207 0.3966 0.0311  0.0470  0.0708  99  THR B CA  
4892 C C   . THR B 99  ? 0.3996 0.4442 0.4298 0.0308  0.0520  0.0759  99  THR B C   
4893 O O   . THR B 99  ? 0.3914 0.4269 0.4241 0.0265  0.0541  0.0744  99  THR B O   
4894 C CB  . THR B 99  ? 0.3945 0.4535 0.4238 0.0312  0.0500  0.0728  99  THR B CB  
4895 O OG1 . THR B 99  ? 0.3948 0.4617 0.4225 0.0324  0.0457  0.0683  99  THR B OG1 
4896 C CG2 . THR B 99  ? 0.3447 0.3979 0.3778 0.0256  0.0543  0.0727  99  THR B CG2 
4897 N N   . LYS B 100 ? 0.4276 0.4753 0.4559 0.0357  0.0543  0.0819  100 LYS B N   
4898 C CA  . LYS B 100 ? 0.4231 0.4628 0.4525 0.0367  0.0598  0.0877  100 LYS B CA  
4899 C C   . LYS B 100 ? 0.3906 0.4234 0.4207 0.0354  0.0575  0.0850  100 LYS B C   
4900 O O   . LYS B 100 ? 0.3953 0.4173 0.4273 0.0331  0.0620  0.0864  100 LYS B O   
4901 C CB  . LYS B 100 ? 0.4456 0.4924 0.4725 0.0434  0.0620  0.0951  100 LYS B CB  
4902 C CG  . LYS B 100 ? 0.5079 0.5621 0.5337 0.0452  0.0646  0.0985  100 LYS B CG  
4903 C CD  . LYS B 100 ? 0.6387 0.6907 0.6642 0.0492  0.0722  0.1079  100 LYS B CD  
4904 C CE  . LYS B 100 ? 0.6826 0.7406 0.7073 0.0499  0.0752  0.1108  100 LYS B CE  
4905 N NZ  . LYS B 100 ? 0.7342 0.7812 0.7609 0.0473  0.0839  0.1152  100 LYS B NZ  
4906 N N   . LEU B 101 ? 0.3381 0.3766 0.3665 0.0367  0.0510  0.0809  101 LEU B N   
4907 C CA  . LEU B 101 ? 0.4235 0.4562 0.4526 0.0356  0.0489  0.0786  101 LEU B CA  
4908 C C   . LEU B 101 ? 0.4248 0.4479 0.4564 0.0295  0.0490  0.0737  101 LEU B C   
4909 O O   . LEU B 101 ? 0.4459 0.4604 0.4787 0.0279  0.0507  0.0737  101 LEU B O   
4910 C CB  . LEU B 101 ? 0.4579 0.4987 0.4846 0.0373  0.0421  0.0747  101 LEU B CB  
4911 C CG  . LEU B 101 ? 0.5040 0.5399 0.5312 0.0357  0.0391  0.0715  101 LEU B CG  
4912 C CD1 . LEU B 101 ? 0.4836 0.5184 0.5114 0.0390  0.0422  0.0773  101 LEU B CD1 
4913 C CD2 . LEU B 101 ? 0.4506 0.4929 0.4753 0.0355  0.0327  0.0657  101 LEU B CD2 
4914 N N   . ASN B 102 ? 0.3872 0.4123 0.4194 0.0263  0.0475  0.0696  102 ASN B N   
4915 C CA  . ASN B 102 ? 0.3560 0.3751 0.3903 0.0207  0.0469  0.0646  102 ASN B CA  
4916 C C   . ASN B 102 ? 0.3565 0.3707 0.3931 0.0163  0.0528  0.0659  102 ASN B C   
4917 O O   . ASN B 102 ? 0.3881 0.3991 0.4266 0.0110  0.0526  0.0617  102 ASN B O   
4918 C CB  . ASN B 102 ? 0.3877 0.4131 0.4214 0.0200  0.0411  0.0590  102 ASN B CB  
4919 C CG  . ASN B 102 ? 0.3737 0.4018 0.4049 0.0227  0.0356  0.0563  102 ASN B CG  
4920 O OD1 . ASN B 102 ? 0.3855 0.4083 0.4169 0.0216  0.0341  0.0546  102 ASN B OD1 
4921 N ND2 . ASN B 102 ? 0.4024 0.4386 0.4311 0.0260  0.0330  0.0555  102 ASN B ND2 
4922 N N   . TYR B 103 ? 0.3820 0.3957 0.4185 0.0184  0.0584  0.0718  103 TYR B N   
4923 C CA  . TYR B 103 ? 0.4286 0.4397 0.4668 0.0142  0.0641  0.0729  103 TYR B CA  
4924 C C   . TYR B 103 ? 0.3947 0.3950 0.4349 0.0075  0.0680  0.0703  103 TYR B C   
4925 O O   . TYR B 103 ? 0.4037 0.4046 0.4457 0.0015  0.0695  0.0671  103 TYR B O   
4926 C CB  . TYR B 103 ? 0.4894 0.5001 0.5265 0.0182  0.0701  0.0804  103 TYR B CB  
4927 C CG  . TYR B 103 ? 0.4928 0.5005 0.5314 0.0140  0.0768  0.0822  103 TYR B CG  
4928 C CD1 . TYR B 103 ? 0.4747 0.4920 0.5137 0.0134  0.0758  0.0814  103 TYR B CD1 
4929 C CD2 . TYR B 103 ? 0.4495 0.4446 0.4889 0.0105  0.0848  0.0846  103 TYR B CD2 
4930 C CE1 . TYR B 103 ? 0.4967 0.5119 0.5371 0.0091  0.0821  0.0830  103 TYR B CE1 
4931 C CE2 . TYR B 103 ? 0.4894 0.4812 0.5300 0.0058  0.0915  0.0858  103 TYR B CE2 
4932 C CZ  . TYR B 103 ? 0.5601 0.5625 0.6013 0.0051  0.0900  0.0851  103 TYR B CZ  
4933 O OH  . TYR B 103 ? 0.6338 0.6336 0.6762 -0.0001 0.0968  0.0863  103 TYR B OH  
4934 N N   . GLU B 104 ? 0.4095 0.4008 0.4493 0.0081  0.0697  0.0713  104 GLU B N   
4935 C CA  . GLU B 104 ? 0.4738 0.4536 0.5148 0.0018  0.0746  0.0692  104 GLU B CA  
4936 C C   . GLU B 104 ? 0.4268 0.4070 0.4688 -0.0028 0.0693  0.0621  104 GLU B C   
4937 O O   . GLU B 104 ? 0.4905 0.4623 0.5332 -0.0086 0.0728  0.0594  104 GLU B O   
4938 C CB  . GLU B 104 ? 0.5657 0.5346 0.6058 0.0050  0.0803  0.0743  104 GLU B CB  
4939 C CG  . GLU B 104 ? 0.6687 0.6356 0.7079 0.0096  0.0871  0.0822  104 GLU B CG  
4940 C CD  . GLU B 104 ? 0.7690 0.7290 0.8090 0.0037  0.0951  0.0827  104 GLU B CD  
4941 O OE1 . GLU B 104 ? 0.7895 0.7442 0.8307 -0.0044 0.0965  0.0769  104 GLU B OE1 
4942 O OE2 . GLU B 104 ? 0.7904 0.7509 0.8296 0.0068  0.1001  0.0887  104 GLU B OE2 
4943 N N   . LYS B 105 ? 0.3942 0.3834 0.4357 -0.0004 0.0616  0.0592  105 LYS B N   
4944 C CA  . LYS B 105 ? 0.3727 0.3624 0.4149 -0.0039 0.0568  0.0533  105 LYS B CA  
4945 C C   . LYS B 105 ? 0.4225 0.4160 0.4667 -0.0106 0.0574  0.0492  105 LYS B C   
4946 O O   . LYS B 105 ? 0.3929 0.3932 0.4378 -0.0109 0.0583  0.0501  105 LYS B O   
4947 C CB  . LYS B 105 ? 0.3511 0.3484 0.3919 0.0007  0.0492  0.0515  105 LYS B CB  
4948 C CG  . LYS B 105 ? 0.3928 0.3869 0.4319 0.0053  0.0475  0.0534  105 LYS B CG  
4949 C CD  . LYS B 105 ? 0.3769 0.3793 0.4141 0.0102  0.0416  0.0528  105 LYS B CD  
4950 C CE  . LYS B 105 ? 0.3209 0.3223 0.3566 0.0144  0.0405  0.0552  105 LYS B CE  
4951 N NZ  . LYS B 105 ? 0.3352 0.3444 0.3686 0.0178  0.0347  0.0532  105 LYS B NZ  
4952 N N   . PRO B 106 ? 0.3880 0.3783 0.4329 -0.0162 0.0570  0.0447  106 PRO B N   
4953 C CA  . PRO B 106 ? 0.3777 0.3744 0.4246 -0.0229 0.0570  0.0405  106 PRO B CA  
4954 C C   . PRO B 106 ? 0.3718 0.3820 0.4194 -0.0202 0.0514  0.0394  106 PRO B C   
4955 O O   . PRO B 106 ? 0.4154 0.4331 0.4648 -0.0238 0.0527  0.0384  106 PRO B O   
4956 C CB  . PRO B 106 ? 0.4403 0.4329 0.4873 -0.0276 0.0557  0.0360  106 PRO B CB  
4957 C CG  . PRO B 106 ? 0.3982 0.3781 0.4435 -0.0254 0.0589  0.0385  106 PRO B CG  
4958 C CD  . PRO B 106 ? 0.3765 0.3577 0.4206 -0.0170 0.0571  0.0434  106 PRO B CD  
4959 N N   . ILE B 107 ? 0.3380 0.3512 0.3841 -0.0141 0.0456  0.0394  107 ILE B N   
4960 C CA  . ILE B 107 ? 0.3497 0.3743 0.3960 -0.0110 0.0410  0.0383  107 ILE B CA  
4961 C C   . ILE B 107 ? 0.3617 0.3917 0.4079 -0.0079 0.0428  0.0415  107 ILE B C   
4962 O O   . ILE B 107 ? 0.2878 0.3276 0.3345 -0.0061 0.0403  0.0407  107 ILE B O   
4963 C CB  . ILE B 107 ? 0.3898 0.4145 0.4339 -0.0056 0.0352  0.0371  107 ILE B CB  
4964 C CG1 . ILE B 107 ? 0.3467 0.3670 0.3883 -0.0003 0.0352  0.0403  107 ILE B CG1 
4965 C CG2 . ILE B 107 ? 0.3576 0.3777 0.4017 -0.0086 0.0333  0.0340  107 ILE B CG2 
4966 C CD1 . ILE B 107 ? 0.3393 0.3611 0.3785 0.0046  0.0299  0.0388  107 ILE B CD1 
4967 N N   . TYR B 108 ? 0.4402 0.4643 0.4857 -0.0069 0.0474  0.0456  108 TYR B N   
4968 C CA  . TYR B 108 ? 0.3513 0.3803 0.3966 -0.0041 0.0498  0.0492  108 TYR B CA  
4969 C C   . TYR B 108 ? 0.4235 0.4524 0.4710 -0.0099 0.0559  0.0502  108 TYR B C   
4970 O O   . TYR B 108 ? 0.3829 0.4134 0.4302 -0.0081 0.0595  0.0541  108 TYR B O   
4971 C CB  . TYR B 108 ? 0.3716 0.3959 0.4144 0.0015  0.0509  0.0538  108 TYR B CB  
4972 C CG  . TYR B 108 ? 0.3552 0.3856 0.3955 0.0077  0.0452  0.0532  108 TYR B CG  
4973 C CD1 . TYR B 108 ? 0.2862 0.3153 0.3254 0.0088  0.0402  0.0497  108 TYR B CD1 
4974 C CD2 . TYR B 108 ? 0.3973 0.4347 0.4361 0.0121  0.0453  0.0558  108 TYR B CD2 
4975 C CE1 . TYR B 108 ? 0.2957 0.3294 0.3323 0.0137  0.0357  0.0486  108 TYR B CE1 
4976 C CE2 . TYR B 108 ? 0.3712 0.4140 0.4072 0.0170  0.0406  0.0545  108 TYR B CE2 
4977 C CZ  . TYR B 108 ? 0.3397 0.3801 0.3745 0.0176  0.0360  0.0507  108 TYR B CZ  
4978 O OH  . TYR B 108 ? 0.3464 0.3910 0.3781 0.0217  0.0320  0.0489  108 TYR B OH  
4979 N N   . ARG B 109 ? 0.4211 0.4489 0.4707 -0.0172 0.0574  0.0466  109 ARG B N   
4980 C CA  . ARG B 109 ? 0.4938 0.5199 0.5452 -0.0243 0.0641  0.0467  109 ARG B CA  
4981 C C   . ARG B 109 ? 0.4490 0.4890 0.5027 -0.0261 0.0632  0.0456  109 ARG B C   
4982 O O   . ARG B 109 ? 0.4776 0.5251 0.5337 -0.0319 0.0623  0.0416  109 ARG B O   
4983 C CB  . ARG B 109 ? 0.5582 0.5775 0.6105 -0.0321 0.0665  0.0427  109 ARG B CB  
4984 C CG  . ARG B 109 ? 0.6840 0.6927 0.7364 -0.0381 0.0755  0.0440  109 ARG B CG  
4985 C CD  . ARG B 109 ? 0.7389 0.7351 0.7903 -0.0420 0.0781  0.0417  109 ARG B CD  
4986 N NE  . ARG B 109 ? 0.7405 0.7426 0.7931 -0.0486 0.0748  0.0353  109 ARG B NE  
4987 C CZ  . ARG B 109 ? 0.7754 0.7704 0.8270 -0.0511 0.0743  0.0322  109 ARG B CZ  
4988 N NH1 . ARG B 109 ? 0.7652 0.7467 0.8147 -0.0474 0.0768  0.0349  109 ARG B NH1 
4989 N NH2 . ARG B 109 ? 0.8117 0.8142 0.8643 -0.0570 0.0712  0.0266  109 ARG B NH2 
4990 N N   . PHE B 110 ? 0.4204 0.4651 0.4734 -0.0207 0.0634  0.0494  110 PHE B N   
4991 C CA  . PHE B 110 ? 0.3777 0.4351 0.4326 -0.0215 0.0636  0.0494  110 PHE B CA  
4992 C C   . PHE B 110 ? 0.3878 0.4416 0.4428 -0.0231 0.0708  0.0538  110 PHE B C   
4993 O O   . PHE B 110 ? 0.4017 0.4491 0.4541 -0.0176 0.0726  0.0584  110 PHE B O   
4994 C CB  . PHE B 110 ? 0.3463 0.4132 0.3999 -0.0135 0.0577  0.0499  110 PHE B CB  
4995 C CG  . PHE B 110 ? 0.3978 0.4683 0.4512 -0.0113 0.0512  0.0461  110 PHE B CG  
4996 C CD1 . PHE B 110 ? 0.3999 0.4820 0.4559 -0.0135 0.0488  0.0430  110 PHE B CD1 
4997 C CD2 . PHE B 110 ? 0.4901 0.5532 0.5407 -0.0067 0.0477  0.0459  110 PHE B CD2 
4998 C CE1 . PHE B 110 ? 0.3838 0.4690 0.4393 -0.0108 0.0433  0.0403  110 PHE B CE1 
4999 C CE2 . PHE B 110 ? 0.4905 0.5560 0.5406 -0.0047 0.0423  0.0427  110 PHE B CE2 
5000 C CZ  . PHE B 110 ? 0.4545 0.5305 0.5069 -0.0064 0.0402  0.0401  110 PHE B CZ  
5001 N N   . GLU B 111 ? 0.3983 0.4568 0.4559 -0.0304 0.0750  0.0524  111 GLU B N   
5002 C CA  . GLU B 111 ? 0.4261 0.4804 0.4837 -0.0326 0.0827  0.0566  111 GLU B CA  
5003 C C   . GLU B 111 ? 0.3752 0.4355 0.4313 -0.0244 0.0816  0.0615  111 GLU B C   
5004 O O   . GLU B 111 ? 0.4175 0.4712 0.4720 -0.0223 0.0871  0.0668  111 GLU B O   
5005 C CB  . GLU B 111 ? 0.5017 0.5625 0.5627 -0.0424 0.0868  0.0536  111 GLU B CB  
5006 C CG  . GLU B 111 ? 0.6010 0.6583 0.6622 -0.0453 0.0952  0.0578  111 GLU B CG  
5007 C CD  . GLU B 111 ? 0.7582 0.8309 0.8227 -0.0504 0.0959  0.0560  111 GLU B CD  
5008 O OE1 . GLU B 111 ? 0.8257 0.9007 0.8903 -0.0492 0.1001  0.0601  111 GLU B OE1 
5009 O OE2 . GLU B 111 ? 0.8029 0.8865 0.8702 -0.0554 0.0922  0.0506  111 GLU B OE2 
5010 N N   . ARG B 112 ? 0.3841 0.4568 0.4403 -0.0194 0.0751  0.0599  112 ARG B N   
5011 C CA  . ARG B 112 ? 0.3541 0.4332 0.4085 -0.0120 0.0741  0.0637  112 ARG B CA  
5012 C C   . ARG B 112 ? 0.3619 0.4329 0.4122 -0.0047 0.0730  0.0673  112 ARG B C   
5013 O O   . ARG B 112 ? 0.3905 0.4624 0.4388 -0.0003 0.0754  0.0722  112 ARG B O   
5014 C CB  . ARG B 112 ? 0.3430 0.4362 0.3981 -0.0086 0.0679  0.0607  112 ARG B CB  
5015 C CG  . ARG B 112 ? 0.4001 0.5004 0.4529 -0.0011 0.0667  0.0636  112 ARG B CG  
5016 C CD  . ARG B 112 ? 0.4382 0.5420 0.4919 -0.0029 0.0728  0.0677  112 ARG B CD  
5017 N NE  . ARG B 112 ? 0.4697 0.5849 0.5221 0.0030  0.0708  0.0689  112 ARG B NE  
5018 C CZ  . ARG B 112 ? 0.4744 0.5934 0.5261 0.0044  0.0751  0.0732  112 ARG B CZ  
5019 N NH1 . ARG B 112 ? 0.4271 0.5388 0.4793 0.0003  0.0818  0.0771  112 ARG B NH1 
5020 N NH2 . ARG B 112 ? 0.4909 0.6206 0.5412 0.0099  0.0730  0.0735  112 ARG B NH2 
5021 N N   . ILE B 113 ? 0.3807 0.4448 0.4299 -0.0035 0.0693  0.0652  113 ILE B N   
5022 C CA  . ILE B 113 ? 0.3441 0.4015 0.3898 0.0027  0.0686  0.0686  113 ILE B CA  
5023 C C   . ILE B 113 ? 0.4170 0.4645 0.4621 0.0017  0.0763  0.0742  113 ILE B C   
5024 O O   . ILE B 113 ? 0.4124 0.4596 0.4550 0.0076  0.0778  0.0795  113 ILE B O   
5025 C CB  . ILE B 113 ? 0.3316 0.3837 0.3765 0.0034  0.0637  0.0650  113 ILE B CB  
5026 C CG1 . ILE B 113 ? 0.3288 0.3897 0.3729 0.0069  0.0565  0.0610  113 ILE B CG1 
5027 C CG2 . ILE B 113 ? 0.3084 0.3525 0.3506 0.0080  0.0645  0.0690  113 ILE B CG2 
5028 C CD1 . ILE B 113 ? 0.3587 0.4147 0.4022 0.0071  0.0517  0.0572  113 ILE B CD1 
5029 N N   . ARG B 114 ? 0.4607 0.5005 0.5081 -0.0058 0.0817  0.0732  114 ARG B N   
5030 C CA  . ARG B 114 ? 0.4785 0.5074 0.5252 -0.0071 0.0904  0.0786  114 ARG B CA  
5031 C C   . ARG B 114 ? 0.4691 0.5040 0.5153 -0.0046 0.0943  0.0837  114 ARG B C   
5032 O O   . ARG B 114 ? 0.4229 0.4525 0.4669 0.0000  0.0990  0.0904  114 ARG B O   
5033 C CB  . ARG B 114 ? 0.6000 0.6201 0.6490 -0.0169 0.0960  0.0753  114 ARG B CB  
5034 C CG  . ARG B 114 ? 0.7400 0.7621 0.7907 -0.0217 0.0907  0.0680  114 ARG B CG  
5035 C CD  . ARG B 114 ? 0.8516 0.8611 0.9030 -0.0298 0.0963  0.0653  114 ARG B CD  
5036 N NE  . ARG B 114 ? 0.9129 0.9095 0.9619 -0.0258 0.0976  0.0678  114 ARG B NE  
5037 C CZ  . ARG B 114 ? 0.8756 0.8719 0.9241 -0.0231 0.0914  0.0651  114 ARG B CZ  
5038 N NH1 . ARG B 114 ? 0.7988 0.8058 0.8485 -0.0239 0.0837  0.0599  114 ARG B NH1 
5039 N NH2 . ARG B 114 ? 0.8802 0.8654 0.9267 -0.0194 0.0932  0.0678  114 ARG B NH2 
5040 N N   . GLU B 115 ? 0.4655 0.5120 0.5137 -0.0072 0.0926  0.0811  115 GLU B N   
5041 C CA  . GLU B 115 ? 0.4621 0.5156 0.5098 -0.0049 0.0960  0.0857  115 GLU B CA  
5042 C C   . GLU B 115 ? 0.4377 0.4969 0.4818 0.0050  0.0922  0.0896  115 GLU B C   
5043 O O   . GLU B 115 ? 0.4389 0.4973 0.4810 0.0090  0.0968  0.0962  115 GLU B O   
5044 C CB  . GLU B 115 ? 0.4698 0.5365 0.5204 -0.0090 0.0939  0.0815  115 GLU B CB  
5045 C CG  . GLU B 115 ? 0.5181 0.5829 0.5725 -0.0197 0.0984  0.0779  115 GLU B CG  
5046 C CD  . GLU B 115 ? 0.5710 0.6519 0.6286 -0.0231 0.0961  0.0744  115 GLU B CD  
5047 O OE1 . GLU B 115 ? 0.5804 0.6636 0.6412 -0.0318 0.0975  0.0700  115 GLU B OE1 
5048 O OE2 . GLU B 115 ? 0.5700 0.6619 0.6269 -0.0171 0.0931  0.0761  115 GLU B OE2 
5049 N N   . LEU B 116 ? 0.4454 0.5106 0.4884 0.0089  0.0841  0.0857  116 LEU B N   
5050 C CA  . LEU B 116 ? 0.4158 0.4885 0.4552 0.0171  0.0801  0.0879  116 LEU B CA  
5051 C C   . LEU B 116 ? 0.3907 0.4567 0.4272 0.0221  0.0822  0.0936  116 LEU B C   
5052 O O   . LEU B 116 ? 0.4026 0.4743 0.4363 0.0279  0.0830  0.0985  116 LEU B O   
5053 C CB  . LEU B 116 ? 0.4008 0.4798 0.4396 0.0192  0.0718  0.0818  116 LEU B CB  
5054 C CG  . LEU B 116 ? 0.3947 0.4827 0.4361 0.0161  0.0695  0.0770  116 LEU B CG  
5055 C CD1 . LEU B 116 ? 0.4034 0.4947 0.4439 0.0185  0.0622  0.0713  116 LEU B CD1 
5056 C CD2 . LEU B 116 ? 0.4026 0.5006 0.4434 0.0185  0.0716  0.0798  116 LEU B CD2 
5057 N N   . MET B 117 ? 0.4379 0.4927 0.4751 0.0202  0.0832  0.0931  117 MET B N   
5058 C CA  . MET B 117 ? 0.4856 0.5347 0.5203 0.0254  0.0851  0.0986  117 MET B CA  
5059 C C   . MET B 117 ? 0.5902 0.6331 0.6245 0.0263  0.0943  0.1067  117 MET B C   
5060 O O   . MET B 117 ? 0.6316 0.6738 0.6635 0.0327  0.0962  0.1131  117 MET B O   
5061 C CB  . MET B 117 ? 0.4185 0.4576 0.4542 0.0231  0.0835  0.0955  117 MET B CB  
5062 C CG  . MET B 117 ? 0.4290 0.4735 0.4643 0.0238  0.0747  0.0889  117 MET B CG  
5063 S SD  . MET B 117 ? 0.5808 0.6347 0.6118 0.0322  0.0690  0.0907  117 MET B SD  
5064 C CE  . MET B 117 ? 0.5556 0.6228 0.5856 0.0331  0.0643  0.0865  117 MET B CE  
5065 N N   . ASN B 118 ? 0.6404 0.6794 0.6769 0.0203  0.1002  0.1067  118 ASN B N   
5066 C CA  . ASN B 118 ? 0.7120 0.7444 0.7479 0.0208  0.1098  0.1143  118 ASN B CA  
5067 C C   . ASN B 118 ? 0.6736 0.7176 0.7080 0.0249  0.1107  0.1188  118 ASN B C   
5068 O O   . ASN B 118 ? 0.6597 0.6992 0.6936 0.0248  0.1189  0.1251  118 ASN B O   
5069 C CB  . ASN B 118 ? 0.7823 0.8039 0.8211 0.0112  0.1167  0.1119  118 ASN B CB  
5070 C CG  . ASN B 118 ? 0.8429 0.8487 0.8820 0.0084  0.1205  0.1112  118 ASN B CG  
5071 O OD1 . ASN B 118 ? 0.8732 0.8741 0.9103 0.0147  0.1207  0.1155  118 ASN B OD1 
5072 N ND2 . ASN B 118 ? 0.8386 0.8371 0.8802 -0.0013 0.1236  0.1058  118 ASN B ND2 
5073 N N   . LYS B 119 ? 0.6729 0.7309 0.7061 0.0284  0.1029  0.1157  119 LYS B N   
5074 C CA  . LYS B 119 ? 0.6563 0.7263 0.6875 0.0325  0.1032  0.1192  119 LYS B CA  
5075 C C   . LYS B 119 ? 0.6525 0.7286 0.6795 0.0416  0.1014  0.1249  119 LYS B C   
5076 O O   . LYS B 119 ? 0.6451 0.7214 0.6708 0.0446  0.0963  0.1231  119 LYS B O   
5077 C CB  . LYS B 119 ? 0.6098 0.6919 0.6420 0.0309  0.0965  0.1121  119 LYS B CB  
5078 C CG  . LYS B 119 ? 0.6111 0.6918 0.6476 0.0224  0.0984  0.1074  119 LYS B CG  
5079 C CD  . LYS B 119 ? 0.6337 0.7286 0.6707 0.0228  0.0939  0.1032  119 LYS B CD  
5080 C CE  . LYS B 119 ? 0.6916 0.7878 0.7331 0.0151  0.0928  0.0968  119 LYS B CE  
5081 N NZ  . LYS B 119 ? 0.7316 0.8213 0.7762 0.0074  0.1008  0.0986  119 LYS B NZ  
5082 N N   . GLU B 120 ? 0.6887 0.7709 0.7136 0.0457  0.1058  0.1319  120 GLU B N   
5083 C CA  . GLU B 120 ? 0.7281 0.8198 0.7487 0.0543  0.1039  0.1373  120 GLU B CA  
5084 C C   . GLU B 120 ? 0.7419 0.8485 0.7602 0.0565  0.0953  0.1314  120 GLU B C   
5085 O O   . GLU B 120 ? 0.8068 0.9198 0.8221 0.0612  0.0902  0.1310  120 GLU B O   
5086 C CB  . GLU B 120 ? 0.7301 0.8234 0.7489 0.0581  0.1119  0.1472  120 GLU B CB  
5087 C CG  . GLU B 120 ? 0.7741 0.8813 0.7882 0.0669  0.1099  0.1530  120 GLU B CG  
5088 C CD  . GLU B 120 ? 0.8679 0.9807 0.8801 0.0699  0.1163  0.1610  120 GLU B CD  
5089 O OE1 . GLU B 120 ? 0.8854 0.9895 0.9001 0.0652  0.1233  0.1628  120 GLU B OE1 
5090 O OE2 . GLU B 120 ? 0.8824 1.0090 0.8906 0.0768  0.1146  0.1654  120 GLU B OE2 
5091 N N   . LYS B 121 ? 0.6600 0.7722 0.6795 0.0531  0.0939  0.1267  121 LYS B N   
5092 C CA  . LYS B 121 ? 0.6396 0.7646 0.6566 0.0553  0.0870  0.1211  121 LYS B CA  
5093 C C   . LYS B 121 ? 0.6112 0.7351 0.6316 0.0496  0.0836  0.1127  121 LYS B C   
5094 O O   . LYS B 121 ? 0.5722 0.6905 0.5966 0.0440  0.0876  0.1123  121 LYS B O   
5095 C CB  . LYS B 121 ? 0.6830 0.8201 0.6969 0.0594  0.0895  0.1259  121 LYS B CB  
5096 C CG  . LYS B 121 ? 0.7539 0.9041 0.7647 0.0617  0.0834  0.1201  121 LYS B CG  
5097 C CD  . LYS B 121 ? 0.8187 0.9786 0.8282 0.0632  0.0869  0.1233  121 LYS B CD  
5098 C CE  . LYS B 121 ? 0.8204 0.9929 0.8261 0.0658  0.0815  0.1175  121 LYS B CE  
5099 N NZ  . LYS B 121 ? 0.7959 0.9658 0.8037 0.0624  0.0765  0.1081  121 LYS B NZ  
5100 N N   . LEU B 122 ? 0.5996 0.7291 0.6182 0.0509  0.0766  0.1059  122 LEU B N   
5101 C CA  . LEU B 122 ? 0.5215 0.6506 0.5429 0.0468  0.0730  0.0982  122 LEU B CA  
5102 C C   . LEU B 122 ? 0.4897 0.6308 0.5085 0.0497  0.0700  0.0947  122 LEU B C   
5103 O O   . LEU B 122 ? 0.4177 0.5648 0.4318 0.0542  0.0666  0.0935  122 LEU B O   
5104 C CB  . LEU B 122 ? 0.5195 0.6417 0.5413 0.0455  0.0678  0.0928  122 LEU B CB  
5105 C CG  . LEU B 122 ? 0.5421 0.6525 0.5657 0.0435  0.0703  0.0959  122 LEU B CG  
5106 C CD1 . LEU B 122 ? 0.5640 0.6726 0.5851 0.0460  0.0651  0.0934  122 LEU B CD1 
5107 C CD2 . LEU B 122 ? 0.5349 0.6368 0.5635 0.0367  0.0723  0.0932  122 LEU B CD2 
5108 N N   . ASN B 123 ? 0.5070 0.6519 0.5288 0.0470  0.0714  0.0929  123 ASN B N   
5109 C CA  . ASN B 123 ? 0.5575 0.7131 0.5773 0.0499  0.0691  0.0893  123 ASN B CA  
5110 C C   . ASN B 123 ? 0.5306 0.6846 0.5504 0.0498  0.0634  0.0816  123 ASN B C   
5111 O O   . ASN B 123 ? 0.4490 0.5945 0.4700 0.0477  0.0609  0.0792  123 ASN B O   
5112 C CB  . ASN B 123 ? 0.5849 0.7467 0.6080 0.0476  0.0735  0.0914  123 ASN B CB  
5113 C CG  . ASN B 123 ? 0.6186 0.7745 0.6478 0.0408  0.0756  0.0904  123 ASN B CG  
5114 O OD1 . ASN B 123 ? 0.5829 0.7337 0.6142 0.0384  0.0721  0.0857  123 ASN B OD1 
5115 N ND2 . ASN B 123 ? 0.5928 0.7499 0.6249 0.0372  0.0816  0.0947  123 ASN B ND2 
5116 N N   . ARG B 124 ? 0.5141 0.6760 0.5324 0.0523  0.0617  0.0777  124 ARG B N   
5117 C CA  . ARG B 124 ? 0.5396 0.6997 0.5573 0.0531  0.0571  0.0709  124 ARG B CA  
5118 C C   . ARG B 124 ? 0.5196 0.6750 0.5431 0.0486  0.0566  0.0689  124 ARG B C   
5119 O O   . ARG B 124 ? 0.5055 0.6550 0.5290 0.0482  0.0529  0.0648  124 ARG B O   
5120 C CB  . ARG B 124 ? 0.5264 0.6957 0.5412 0.0573  0.0566  0.0679  124 ARG B CB  
5121 C CG  . ARG B 124 ? 0.5303 0.6971 0.5442 0.0589  0.0529  0.0613  124 ARG B CG  
5122 C CD  . ARG B 124 ? 0.5179 0.6932 0.5299 0.0629  0.0538  0.0589  124 ARG B CD  
5123 N NE  . ARG B 124 ? 0.4792 0.6514 0.4912 0.0648  0.0514  0.0536  124 ARG B NE  
5124 C CZ  . ARG B 124 ? 0.4173 0.5911 0.4348 0.0635  0.0515  0.0533  124 ARG B CZ  
5125 N NH1 . ARG B 124 ? 0.4297 0.6079 0.4531 0.0593  0.0537  0.0572  124 ARG B NH1 
5126 N NH2 . ARG B 124 ? 0.3894 0.5603 0.4062 0.0662  0.0496  0.0490  124 ARG B NH2 
5127 N N   . GLU B 125 ? 0.5377 0.6962 0.5661 0.0447  0.0604  0.0719  125 GLU B N   
5128 C CA  . GLU B 125 ? 0.5519 0.7081 0.5859 0.0395  0.0602  0.0700  125 GLU B CA  
5129 C C   . GLU B 125 ? 0.4897 0.6341 0.5247 0.0359  0.0595  0.0701  125 GLU B C   
5130 O O   . GLU B 125 ? 0.4471 0.5873 0.4835 0.0344  0.0563  0.0662  125 GLU B O   
5131 C CB  . GLU B 125 ? 0.6841 0.8466 0.7227 0.0351  0.0651  0.0731  125 GLU B CB  
5132 C CG  . GLU B 125 ? 0.8384 1.0130 0.8783 0.0373  0.0648  0.0712  125 GLU B CG  
5133 C CD  . GLU B 125 ? 0.9605 1.1392 0.9947 0.0447  0.0628  0.0700  125 GLU B CD  
5134 O OE1 . GLU B 125 ? 0.9870 1.1705 1.0205 0.0484  0.0604  0.0662  125 GLU B OE1 
5135 O OE2 . GLU B 125 ? 0.9922 1.1694 1.0223 0.0470  0.0642  0.0730  125 GLU B OE2 
5136 N N   . GLU B 126 ? 0.4168 0.5560 0.4510 0.0347  0.0631  0.0749  126 GLU B N   
5137 C CA  . GLU B 126 ? 0.3770 0.5046 0.4120 0.0317  0.0634  0.0757  126 GLU B CA  
5138 C C   . GLU B 126 ? 0.3364 0.4595 0.3680 0.0351  0.0580  0.0724  126 GLU B C   
5139 O O   . GLU B 126 ? 0.3517 0.4670 0.3847 0.0325  0.0561  0.0701  126 GLU B O   
5140 C CB  . GLU B 126 ? 0.4431 0.5667 0.4774 0.0313  0.0690  0.0824  126 GLU B CB  
5141 C CG  . GLU B 126 ? 0.4495 0.5743 0.4878 0.0259  0.0750  0.0850  126 GLU B CG  
5142 C CD  . GLU B 126 ? 0.5338 0.6601 0.5703 0.0278  0.0808  0.0920  126 GLU B CD  
5143 O OE1 . GLU B 126 ? 0.5364 0.6632 0.5686 0.0336  0.0801  0.0954  126 GLU B OE1 
5144 O OE2 . GLU B 126 ? 0.5841 0.7118 0.6236 0.0233  0.0862  0.0942  126 GLU B OE2 
5145 N N   . LEU B 127 ? 0.3013 0.4295 0.3281 0.0406  0.0557  0.0719  127 LEU B N   
5146 C CA  . LEU B 127 ? 0.3044 0.4289 0.3277 0.0432  0.0509  0.0681  127 LEU B CA  
5147 C C   . LEU B 127 ? 0.3023 0.4252 0.3268 0.0424  0.0472  0.0621  127 LEU B C   
5148 O O   . LEU B 127 ? 0.3518 0.4678 0.3757 0.0418  0.0441  0.0592  127 LEU B O   
5149 C CB  . LEU B 127 ? 0.3381 0.4693 0.3556 0.0483  0.0497  0.0681  127 LEU B CB  
5150 C CG  . LEU B 127 ? 0.4086 0.5410 0.4237 0.0502  0.0522  0.0741  127 LEU B CG  
5151 C CD1 . LEU B 127 ? 0.3990 0.5406 0.4082 0.0548  0.0507  0.0734  127 LEU B CD1 
5152 C CD2 . LEU B 127 ? 0.4240 0.5478 0.4396 0.0490  0.0512  0.0753  127 LEU B CD2 
5153 N N   . LEU B 128 ? 0.3036 0.4335 0.3300 0.0427  0.0478  0.0605  128 LEU B N   
5154 C CA  . LEU B 128 ? 0.3741 0.5036 0.4022 0.0425  0.0449  0.0559  128 LEU B CA  
5155 C C   . LEU B 128 ? 0.3447 0.4683 0.3774 0.0372  0.0447  0.0556  128 LEU B C   
5156 O O   . LEU B 128 ? 0.3011 0.4198 0.3337 0.0370  0.0414  0.0521  128 LEU B O   
5157 C CB  . LEU B 128 ? 0.4138 0.5537 0.4436 0.0443  0.0461  0.0553  128 LEU B CB  
5158 C CG  . LEU B 128 ? 0.4192 0.5631 0.4444 0.0503  0.0447  0.0522  128 LEU B CG  
5159 C CD1 . LEU B 128 ? 0.4447 0.5996 0.4723 0.0521  0.0466  0.0525  128 LEU B CD1 
5160 C CD2 . LEU B 128 ? 0.4157 0.5521 0.4384 0.0522  0.0410  0.0475  128 LEU B CD2 
5161 N N   . ASP B 129 ? 0.3594 0.4830 0.3956 0.0324  0.0485  0.0590  129 ASP B N   
5162 C CA  . ASP B 129 ? 0.3456 0.4631 0.3857 0.0265  0.0490  0.0585  129 ASP B CA  
5163 C C   . ASP B 129 ? 0.3551 0.4614 0.3931 0.0264  0.0475  0.0584  129 ASP B C   
5164 O O   . ASP B 129 ? 0.3635 0.4642 0.4032 0.0234  0.0456  0.0559  129 ASP B O   
5165 C CB  . ASP B 129 ? 0.3827 0.5016 0.4264 0.0211  0.0545  0.0620  129 ASP B CB  
5166 C CG  . ASP B 129 ? 0.3816 0.5120 0.4290 0.0189  0.0557  0.0611  129 ASP B CG  
5167 O OD1 . ASP B 129 ? 0.3901 0.5281 0.4368 0.0232  0.0526  0.0587  129 ASP B OD1 
5168 O OD2 . ASP B 129 ? 0.3646 0.4964 0.4155 0.0129  0.0600  0.0627  129 ASP B OD2 
5169 N N   . LEU B 130 ? 0.3898 0.4936 0.4242 0.0296  0.0482  0.0612  130 LEU B N   
5170 C CA  . LEU B 130 ? 0.4017 0.4966 0.4343 0.0299  0.0469  0.0616  130 LEU B CA  
5171 C C   . LEU B 130 ? 0.4370 0.5300 0.4671 0.0324  0.0415  0.0568  130 LEU B C   
5172 O O   . LEU B 130 ? 0.3438 0.4293 0.3744 0.0305  0.0397  0.0551  130 LEU B O   
5173 C CB  . LEU B 130 ? 0.3772 0.4727 0.4068 0.0331  0.0492  0.0666  130 LEU B CB  
5174 C CG  . LEU B 130 ? 0.4598 0.5471 0.4884 0.0333  0.0493  0.0687  130 LEU B CG  
5175 C CD1 . LEU B 130 ? 0.5128 0.5912 0.5452 0.0281  0.0530  0.0703  130 LEU B CD1 
5176 C CD2 . LEU B 130 ? 0.4696 0.5607 0.4949 0.0377  0.0514  0.0741  130 LEU B CD2 
5177 N N   . GLN B 131 ? 0.3927 0.4917 0.4196 0.0365  0.0394  0.0544  131 GLN B N   
5178 C CA  . GLN B 131 ? 0.3403 0.4366 0.3646 0.0386  0.0352  0.0494  131 GLN B CA  
5179 C C   . GLN B 131 ? 0.3465 0.4401 0.3742 0.0361  0.0337  0.0466  131 GLN B C   
5180 O O   . GLN B 131 ? 0.3147 0.4014 0.3418 0.0353  0.0311  0.0442  131 GLN B O   
5181 C CB  . GLN B 131 ? 0.2454 0.3482 0.2658 0.0431  0.0345  0.0472  131 GLN B CB  
5182 C CG  . GLN B 131 ? 0.2481 0.3549 0.2641 0.0458  0.0352  0.0489  131 GLN B CG  
5183 C CD  . GLN B 131 ? 0.3728 0.4869 0.3855 0.0496  0.0356  0.0469  131 GLN B CD  
5184 O OE1 . GLN B 131 ? 0.3910 0.5104 0.4061 0.0502  0.0373  0.0474  131 GLN B OE1 
5185 N NE2 . GLN B 131 ? 0.4314 0.5463 0.4383 0.0521  0.0341  0.0442  131 GLN B NE2 
5186 N N   . THR B 132 ? 0.3434 0.4434 0.3746 0.0347  0.0354  0.0472  132 THR B N   
5187 C CA  . THR B 132 ? 0.3304 0.4312 0.3647 0.0331  0.0338  0.0447  132 THR B CA  
5188 C C   . THR B 132 ? 0.3162 0.4108 0.3536 0.0274  0.0340  0.0449  132 THR B C   
5189 O O   . THR B 132 ? 0.3897 0.4811 0.4277 0.0266  0.0315  0.0424  132 THR B O   
5190 C CB  . THR B 132 ? 0.3495 0.4614 0.3869 0.0332  0.0355  0.0454  132 THR B CB  
5191 O OG1 . THR B 132 ? 0.3104 0.4278 0.3445 0.0387  0.0359  0.0452  132 THR B OG1 
5192 C CG2 . THR B 132 ? 0.3187 0.4337 0.3587 0.0329  0.0335  0.0430  132 THR B CG2 
5193 N N   . LEU B 133 ? 0.2657 0.3582 0.3049 0.0236  0.0374  0.0481  133 LEU B N   
5194 C CA  . LEU B 133 ? 0.3031 0.3884 0.3447 0.0180  0.0384  0.0480  133 LEU B CA  
5195 C C   . LEU B 133 ? 0.3055 0.3809 0.3445 0.0191  0.0362  0.0473  133 LEU B C   
5196 O O   . LEU B 133 ? 0.3633 0.4328 0.4037 0.0156  0.0356  0.0458  133 LEU B O   
5197 C CB  . LEU B 133 ? 0.3269 0.4113 0.3707 0.0137  0.0438  0.0516  133 LEU B CB  
5198 C CG  . LEU B 133 ? 0.3047 0.3987 0.3523 0.0099  0.0462  0.0515  133 LEU B CG  
5199 C CD1 . LEU B 133 ? 0.3297 0.4232 0.3785 0.0069  0.0522  0.0555  133 LEU B CD1 
5200 C CD2 . LEU B 133 ? 0.2755 0.3705 0.3265 0.0043  0.0453  0.0483  133 LEU B CD2 
5201 N N   . ASN B 134 ? 0.2779 0.3521 0.3129 0.0237  0.0351  0.0482  134 ASN B N   
5202 C CA  . ASN B 134 ? 0.3197 0.3865 0.3522 0.0249  0.0324  0.0469  134 ASN B CA  
5203 C C   . ASN B 134 ? 0.3676 0.4329 0.3995 0.0255  0.0285  0.0424  134 ASN B C   
5204 O O   . ASN B 134 ? 0.4237 0.4822 0.4558 0.0238  0.0269  0.0410  134 ASN B O   
5205 C CB  . ASN B 134 ? 0.3242 0.3928 0.3526 0.0292  0.0319  0.0483  134 ASN B CB  
5206 C CG  . ASN B 134 ? 0.3426 0.4089 0.3713 0.0289  0.0353  0.0533  134 ASN B CG  
5207 O OD1 . ASN B 134 ? 0.3327 0.3929 0.3609 0.0284  0.0349  0.0541  134 ASN B OD1 
5208 N ND2 . ASN B 134 ? 0.2875 0.3587 0.3167 0.0295  0.0389  0.0571  134 ASN B ND2 
5209 N N   . LEU B 135 ? 0.2701 0.3413 0.3012 0.0284  0.0273  0.0405  135 LEU B N   
5210 C CA  . LEU B 135 ? 0.3118 0.3813 0.3424 0.0296  0.0244  0.0370  135 LEU B CA  
5211 C C   . LEU B 135 ? 0.3296 0.3991 0.3642 0.0254  0.0243  0.0367  135 LEU B C   
5212 O O   . LEU B 135 ? 0.3359 0.3997 0.3704 0.0242  0.0223  0.0349  135 LEU B O   
5213 C CB  . LEU B 135 ? 0.3301 0.4059 0.3589 0.0343  0.0240  0.0356  135 LEU B CB  
5214 C CG  . LEU B 135 ? 0.3337 0.4090 0.3574 0.0384  0.0238  0.0344  135 LEU B CG  
5215 C CD1 . LEU B 135 ? 0.3219 0.4037 0.3443 0.0428  0.0246  0.0333  135 LEU B CD1 
5216 C CD2 . LEU B 135 ? 0.3702 0.4369 0.3902 0.0390  0.0214  0.0314  135 LEU B CD2 
5217 N N   . LEU B 136 ? 0.2570 0.3338 0.2954 0.0226  0.0267  0.0382  136 LEU B N   
5218 C CA  . LEU B 136 ? 0.2844 0.3642 0.3266 0.0181  0.0267  0.0373  136 LEU B CA  
5219 C C   . LEU B 136 ? 0.3556 0.4265 0.3986 0.0130  0.0272  0.0371  136 LEU B C   
5220 O O   . LEU B 136 ? 0.3427 0.4134 0.3872 0.0102  0.0259  0.0352  136 LEU B O   
5221 C CB  . LEU B 136 ? 0.2330 0.3231 0.2788 0.0152  0.0296  0.0388  136 LEU B CB  
5222 C CG  . LEU B 136 ? 0.3234 0.4245 0.3694 0.0199  0.0291  0.0389  136 LEU B CG  
5223 C CD1 . LEU B 136 ? 0.2895 0.4013 0.3393 0.0164  0.0323  0.0405  136 LEU B CD1 
5224 C CD2 . LEU B 136 ? 0.3106 0.4150 0.3569 0.0226  0.0260  0.0369  136 LEU B CD2 
5225 N N   . ALA B 137 ? 0.3113 0.3756 0.3532 0.0122  0.0294  0.0392  137 ALA B N   
5226 C CA  . ALA B 137 ? 0.3040 0.3591 0.3464 0.0083  0.0305  0.0392  137 ALA B CA  
5227 C C   . ALA B 137 ? 0.2755 0.3250 0.3162 0.0094  0.0267  0.0367  137 ALA B C   
5228 O O   . ALA B 137 ? 0.3479 0.3926 0.3898 0.0054  0.0269  0.0355  137 ALA B O   
5229 C CB  . ALA B 137 ? 0.2679 0.3174 0.3088 0.0094  0.0334  0.0427  137 ALA B CB  
5230 N N   . TRP B 138 ? 0.2544 0.3042 0.2921 0.0145  0.0237  0.0355  138 TRP B N   
5231 C CA  . TRP B 138 ? 0.2842 0.3282 0.3200 0.0157  0.0205  0.0332  138 TRP B CA  
5232 C C   . TRP B 138 ? 0.3412 0.3894 0.3775 0.0168  0.0183  0.0311  138 TRP B C   
5233 O O   . TRP B 138 ? 0.3687 0.4126 0.4027 0.0191  0.0158  0.0293  138 TRP B O   
5234 C CB  . TRP B 138 ? 0.3192 0.3597 0.3509 0.0199  0.0190  0.0328  138 TRP B CB  
5235 C CG  . TRP B 138 ? 0.3304 0.3681 0.3616 0.0194  0.0208  0.0354  138 TRP B CG  
5236 C CD1 . TRP B 138 ? 0.3195 0.3614 0.3506 0.0206  0.0233  0.0383  138 TRP B CD1 
5237 C CD2 . TRP B 138 ? 0.3028 0.3335 0.3335 0.0181  0.0206  0.0359  138 TRP B CD2 
5238 N NE1 . TRP B 138 ? 0.2864 0.3245 0.3170 0.0205  0.0248  0.0409  138 TRP B NE1 
5239 C CE2 . TRP B 138 ? 0.3086 0.3400 0.3390 0.0190  0.0232  0.0395  138 TRP B CE2 
5240 C CE3 . TRP B 138 ? 0.2805 0.3049 0.3110 0.0166  0.0187  0.0339  138 TRP B CE3 
5241 C CZ2 . TRP B 138 ? 0.3030 0.3295 0.3331 0.0189  0.0239  0.0414  138 TRP B CZ2 
5242 C CZ3 . TRP B 138 ? 0.2615 0.2808 0.2917 0.0159  0.0193  0.0354  138 TRP B CZ3 
5243 C CH2 . TRP B 138 ? 0.2888 0.3095 0.3189 0.0172  0.0219  0.0392  138 TRP B CH2 
5244 N N   . CYS B 139 ? 0.2889 0.3460 0.3282 0.0152  0.0194  0.0315  139 CYS B N   
5245 C CA  . CYS B 139 ? 0.2609 0.3242 0.3011 0.0166  0.0175  0.0304  139 CYS B CA  
5246 C C   . CYS B 139 ? 0.3272 0.3860 0.3678 0.0135  0.0159  0.0289  139 CYS B C   
5247 O O   . CYS B 139 ? 0.3346 0.3911 0.3771 0.0077  0.0173  0.0287  139 CYS B O   
5248 C CB  . CYS B 139 ? 0.2732 0.3490 0.3171 0.0146  0.0191  0.0313  139 CYS B CB  
5249 S SG  . CYS B 139 ? 0.3792 0.4667 0.4247 0.0174  0.0171  0.0309  139 CYS B SG  
5250 N N   . GLY B 140 ? 0.3110 0.3682 0.3497 0.0172  0.0135  0.0280  140 GLY B N   
5251 C CA  . GLY B 140 ? 0.3161 0.3700 0.3549 0.0148  0.0120  0.0269  140 GLY B CA  
5252 C C   . GLY B 140 ? 0.3177 0.3829 0.3596 0.0125  0.0117  0.0270  140 GLY B C   
5253 O O   . GLY B 140 ? 0.3600 0.4365 0.4041 0.0134  0.0125  0.0280  140 GLY B O   
5254 N N   . ARG B 141 ? 0.2436 0.3068 0.2856 0.0096  0.0104  0.0259  141 ARG B N   
5255 C CA  . ARG B 141 ? 0.2158 0.2909 0.2606 0.0066  0.0099  0.0257  141 ARG B CA  
5256 C C   . ARG B 141 ? 0.2664 0.3530 0.3116 0.0128  0.0089  0.0275  141 ARG B C   
5257 O O   . ARG B 141 ? 0.2332 0.3342 0.2817 0.0110  0.0094  0.0281  141 ARG B O   
5258 C CB  . ARG B 141 ? 0.2383 0.3084 0.2820 0.0041  0.0084  0.0244  141 ARG B CB  
5259 C CG  . ARG B 141 ? 0.3019 0.3850 0.3477 0.0010  0.0074  0.0240  141 ARG B CG  
5260 C CD  . ARG B 141 ? 0.2989 0.3755 0.3433 -0.0025 0.0064  0.0223  141 ARG B CD  
5261 N NE  . ARG B 141 ? 0.3604 0.4501 0.4060 -0.0043 0.0050  0.0222  141 ARG B NE  
5262 C CZ  . ARG B 141 ? 0.2769 0.3704 0.3210 0.0014  0.0028  0.0242  141 ARG B CZ  
5263 N NH1 . ARG B 141 ? 0.2742 0.3579 0.3154 0.0088  0.0022  0.0260  141 ARG B NH1 
5264 N NH2 . ARG B 141 ? 0.2570 0.3642 0.3023 -0.0005 0.0016  0.0244  141 ARG B NH2 
5265 N N   . THR B 142 ? 0.2772 0.3578 0.3191 0.0200  0.0079  0.0285  142 THR B N   
5266 C CA  . THR B 142 ? 0.3679 0.4578 0.4098 0.0269  0.0076  0.0307  142 THR B CA  
5267 C C   . THR B 142 ? 0.4508 0.5507 0.4948 0.0286  0.0092  0.0318  142 THR B C   
5268 O O   . THR B 142 ? 0.4888 0.6039 0.5356 0.0301  0.0093  0.0335  142 THR B O   
5269 C CB  . THR B 142 ? 0.4470 0.5253 0.4843 0.0341  0.0074  0.0311  142 THR B CB  
5270 O OG1 . THR B 142 ? 0.4486 0.5198 0.4841 0.0330  0.0060  0.0306  142 THR B OG1 
5271 C CG2 . THR B 142 ? 0.5140 0.6001 0.5507 0.0423  0.0082  0.0337  142 THR B CG2 
5272 N N   . LEU B 143 ? 0.3541 0.4467 0.3969 0.0285  0.0106  0.0310  143 LEU B N   
5273 C CA  . LEU B 143 ? 0.3590 0.4601 0.4030 0.0312  0.0123  0.0323  143 LEU B CA  
5274 C C   . LEU B 143 ? 0.3873 0.5006 0.4360 0.0247  0.0135  0.0324  143 LEU B C   
5275 O O   . LEU B 143 ? 0.2955 0.4174 0.3459 0.0263  0.0150  0.0336  143 LEU B O   
5276 C CB  . LEU B 143 ? 0.3797 0.4699 0.4202 0.0340  0.0133  0.0316  143 LEU B CB  
5277 C CG  . LEU B 143 ? 0.3047 0.3887 0.3408 0.0422  0.0133  0.0316  143 LEU B CG  
5278 C CD1 . LEU B 143 ? 0.3130 0.3883 0.3455 0.0439  0.0145  0.0302  143 LEU B CD1 
5279 C CD2 . LEU B 143 ? 0.3133 0.4087 0.3505 0.0488  0.0142  0.0339  143 LEU B CD2 
5280 N N   . ARG B 144 ? 0.3854 0.5001 0.4362 0.0173  0.0131  0.0311  144 ARG B N   
5281 C CA  . ARG B 144 ? 0.4315 0.5566 0.4864 0.0101  0.0149  0.0306  144 ARG B CA  
5282 C C   . ARG B 144 ? 0.4146 0.5596 0.4730 0.0115  0.0148  0.0321  144 ARG B C   
5283 O O   . ARG B 144 ? 0.3998 0.5541 0.4612 0.0078  0.0169  0.0322  144 ARG B O   
5284 C CB  . ARG B 144 ? 0.5220 0.6434 0.5779 0.0015  0.0152  0.0283  144 ARG B CB  
5285 C CG  . ARG B 144 ? 0.5906 0.6971 0.6451 -0.0026 0.0174  0.0273  144 ARG B CG  
5286 C CD  . ARG B 144 ? 0.6151 0.7109 0.6679 -0.0059 0.0164  0.0255  144 ARG B CD  
5287 N NE  . ARG B 144 ? 0.6094 0.7129 0.6645 -0.0133 0.0168  0.0234  144 ARG B NE  
5288 C CZ  . ARG B 144 ? 0.5800 0.6917 0.6353 -0.0127 0.0141  0.0229  144 ARG B CZ  
5289 N NH1 . ARG B 144 ? 0.5185 0.6308 0.5720 -0.0045 0.0114  0.0248  144 ARG B NH1 
5290 N NH2 . ARG B 144 ? 0.5819 0.7015 0.6390 -0.0203 0.0146  0.0205  144 ARG B NH2 
5291 N N   . LYS B 145 ? 0.3726 0.5252 0.4308 0.0168  0.0127  0.0334  145 LYS B N   
5292 C CA  . LYS B 145 ? 0.3857 0.5591 0.4474 0.0191  0.0127  0.0355  145 LYS B CA  
5293 C C   . LYS B 145 ? 0.3441 0.5199 0.4054 0.0266  0.0142  0.0377  145 LYS B C   
5294 O O   . LYS B 145 ? 0.4227 0.6125 0.4875 0.0252  0.0156  0.0386  145 LYS B O   
5295 C CB  . LYS B 145 ? 0.4821 0.6639 0.5436 0.0233  0.0103  0.0372  145 LYS B CB  
5296 C CG  . LYS B 145 ? 0.6434 0.8210 0.7018 0.0352  0.0099  0.0403  145 LYS B CG  
5297 C CD  . LYS B 145 ? 0.6716 0.8279 0.7251 0.0387  0.0101  0.0393  145 LYS B CD  
5298 C CE  . LYS B 145 ? 0.7037 0.8567 0.7537 0.0500  0.0102  0.0424  145 LYS B CE  
5299 N NZ  . LYS B 145 ? 0.7098 0.8422 0.7551 0.0521  0.0113  0.0405  145 LYS B NZ  
5300 N N   . ASP B 146 ? 0.3824 0.5447 0.4393 0.0343  0.0141  0.0384  146 ASP B N   
5301 C CA  . ASP B 146 ? 0.3886 0.5529 0.4444 0.0419  0.0159  0.0402  146 ASP B CA  
5302 C C   . ASP B 146 ? 0.3926 0.5556 0.4493 0.0380  0.0179  0.0393  146 ASP B C   
5303 O O   . ASP B 146 ? 0.3922 0.5642 0.4500 0.0418  0.0196  0.0408  146 ASP B O   
5304 C CB  . ASP B 146 ? 0.4836 0.6321 0.5338 0.0499  0.0159  0.0402  146 ASP B CB  
5305 C CG  . ASP B 146 ? 0.6229 0.7755 0.6721 0.0575  0.0154  0.0426  146 ASP B CG  
5306 O OD1 . ASP B 146 ? 0.6229 0.7928 0.6760 0.0575  0.0147  0.0448  146 ASP B OD1 
5307 O OD2 . ASP B 146 ? 0.6617 0.8002 0.7060 0.0633  0.0159  0.0424  146 ASP B OD2 
5308 N N   . LEU B 147 ? 0.3883 0.5398 0.4441 0.0313  0.0181  0.0372  147 LEU B N   
5309 C CA  . LEU B 147 ? 0.3273 0.4760 0.3834 0.0281  0.0205  0.0370  147 LEU B CA  
5310 C C   . LEU B 147 ? 0.3426 0.5003 0.4031 0.0189  0.0221  0.0365  147 LEU B C   
5311 O O   . LEU B 147 ? 0.4209 0.5746 0.4817 0.0151  0.0245  0.0366  147 LEU B O   
5312 C CB  . LEU B 147 ? 0.2939 0.4239 0.3457 0.0275  0.0204  0.0356  147 LEU B CB  
5313 C CG  . LEU B 147 ? 0.3198 0.4392 0.3665 0.0352  0.0193  0.0352  147 LEU B CG  
5314 C CD1 . LEU B 147 ? 0.3012 0.4053 0.3443 0.0335  0.0192  0.0338  147 LEU B CD1 
5315 C CD2 . LEU B 147 ? 0.4326 0.5581 0.4781 0.0424  0.0207  0.0364  147 LEU B CD2 
5316 N N   . LYS B 148 ? 0.2560 0.4260 0.3199 0.0149  0.0211  0.0361  148 LYS B N   
5317 C CA  . LYS B 148 ? 0.3125 0.4899 0.3803 0.0047  0.0231  0.0347  148 LYS B CA  
5318 C C   . LYS B 148 ? 0.3512 0.5384 0.4216 0.0036  0.0261  0.0360  148 LYS B C   
5319 O O   . LYS B 148 ? 0.3287 0.5137 0.4005 -0.0040 0.0291  0.0351  148 LYS B O   
5320 C CB  . LYS B 148 ? 0.3851 0.5773 0.4560 0.0006  0.0214  0.0337  148 LYS B CB  
5321 C CG  . LYS B 148 ? 0.3714 0.5715 0.4460 -0.0113 0.0239  0.0313  148 LYS B CG  
5322 C CD  . LYS B 148 ? 0.3680 0.5843 0.4453 -0.0159 0.0220  0.0297  148 LYS B CD  
5323 C CE  . LYS B 148 ? 0.4395 0.6441 0.5141 -0.0187 0.0202  0.0275  148 LYS B CE  
5324 N NZ  . LYS B 148 ? 0.4837 0.7053 0.5601 -0.0206 0.0176  0.0268  148 LYS B NZ  
5325 N N   . ASP B 149 ? 0.3230 0.5204 0.3938 0.0114  0.0257  0.0383  149 ASP B N   
5326 C CA  . ASP B 149 ? 0.3422 0.5490 0.4152 0.0112  0.0285  0.0397  149 ASP B CA  
5327 C C   . ASP B 149 ? 0.3744 0.5662 0.4447 0.0100  0.0310  0.0399  149 ASP B C   
5328 O O   . ASP B 149 ? 0.3808 0.5748 0.4532 0.0036  0.0343  0.0400  149 ASP B O   
5329 C CB  . ASP B 149 ? 0.3772 0.5945 0.4502 0.0213  0.0279  0.0422  149 ASP B CB  
5330 C CG  . ASP B 149 ? 0.5080 0.7352 0.5831 0.0217  0.0309  0.0438  149 ASP B CG  
5331 O OD1 . ASP B 149 ? 0.5829 0.8228 0.6625 0.0139  0.0326  0.0435  149 ASP B OD1 
5332 O OD2 . ASP B 149 ? 0.5625 0.7848 0.6346 0.0291  0.0317  0.0451  149 ASP B OD2 
5333 N N   . LEU B 150 ? 0.3156 0.4923 0.3810 0.0162  0.0298  0.0399  150 LEU B N   
5334 C CA  . LEU B 150 ? 0.3459 0.5102 0.4084 0.0160  0.0318  0.0405  150 LEU B CA  
5335 C C   . LEU B 150 ? 0.4086 0.5623 0.4713 0.0079  0.0334  0.0395  150 LEU B C   
5336 O O   . LEU B 150 ? 0.4353 0.5840 0.4976 0.0051  0.0366  0.0408  150 LEU B O   
5337 C CB  . LEU B 150 ? 0.3602 0.5132 0.4174 0.0242  0.0300  0.0404  150 LEU B CB  
5338 C CG  . LEU B 150 ? 0.3558 0.5167 0.4118 0.0327  0.0299  0.0414  150 LEU B CG  
5339 C CD1 . LEU B 150 ? 0.3197 0.4682 0.3699 0.0397  0.0285  0.0403  150 LEU B CD1 
5340 C CD2 . LEU B 150 ? 0.3041 0.4736 0.3616 0.0323  0.0330  0.0432  150 LEU B CD2 
5341 N N   . LEU B 151 ? 0.4299 0.5798 0.4929 0.0043  0.0315  0.0376  151 LEU B N   
5342 C CA  . LEU B 151 ? 0.4172 0.5574 0.4806 -0.0038 0.0336  0.0364  151 LEU B CA  
5343 C C   . LEU B 151 ? 0.4403 0.5892 0.5076 -0.0124 0.0376  0.0361  151 LEU B C   
5344 O O   . LEU B 151 ? 0.3943 0.5346 0.4615 -0.0176 0.0416  0.0365  151 LEU B O   
5345 C CB  . LEU B 151 ? 0.3768 0.5120 0.4395 -0.0056 0.0308  0.0341  151 LEU B CB  
5346 C CG  . LEU B 151 ? 0.3491 0.4705 0.4075 0.0003  0.0280  0.0340  151 LEU B CG  
5347 C CD1 . LEU B 151 ? 0.2653 0.3866 0.3234 0.0002  0.0247  0.0321  151 LEU B CD1 
5348 C CD2 . LEU B 151 ? 0.3977 0.5040 0.4539 -0.0022 0.0302  0.0344  151 LEU B CD2 
5349 N N   . ASN B 152 ? 0.4008 0.5675 0.4719 -0.0141 0.0369  0.0355  152 ASN B N   
5350 C CA  . ASN B 152 ? 0.3847 0.5619 0.4598 -0.0229 0.0407  0.0347  152 ASN B CA  
5351 C C   . ASN B 152 ? 0.4694 0.6462 0.5445 -0.0220 0.0446  0.0374  152 ASN B C   
5352 O O   . ASN B 152 ? 0.5078 0.6836 0.5846 -0.0300 0.0494  0.0372  152 ASN B O   
5353 C CB  . ASN B 152 ? 0.3670 0.5661 0.4461 -0.0238 0.0387  0.0339  152 ASN B CB  
5354 C CG  . ASN B 152 ? 0.3317 0.5349 0.4120 -0.0302 0.0369  0.0307  152 ASN B CG  
5355 O OD1 . ASN B 152 ? 0.3760 0.5647 0.4539 -0.0331 0.0369  0.0289  152 ASN B OD1 
5356 N ND2 . ASN B 152 ? 0.3522 0.5767 0.4363 -0.0322 0.0355  0.0300  152 ASN B ND2 
5357 N N   . LYS B 153 ? 0.4127 0.5905 0.4859 -0.0126 0.0430  0.0399  153 LYS B N   
5358 C CA  . LYS B 153 ? 0.4058 0.5848 0.4787 -0.0110 0.0465  0.0426  153 LYS B CA  
5359 C C   . LYS B 153 ? 0.4219 0.5846 0.4925 -0.0143 0.0504  0.0439  153 LYS B C   
5360 O O   . LYS B 153 ? 0.4643 0.6280 0.5365 -0.0199 0.0553  0.0451  153 LYS B O   
5361 C CB  . LYS B 153 ? 0.3709 0.5518 0.4411 0.0000  0.0439  0.0443  153 LYS B CB  
5362 C CG  . LYS B 153 ? 0.3897 0.5783 0.4605 0.0024  0.0469  0.0469  153 LYS B CG  
5363 C CD  . LYS B 153 ? 0.3420 0.5328 0.4097 0.0131  0.0446  0.0478  153 LYS B CD  
5364 C CE  . LYS B 153 ? 0.3776 0.5788 0.4462 0.0154  0.0475  0.0502  153 LYS B CE  
5365 N NZ  . LYS B 153 ? 0.4547 0.6585 0.5202 0.0257  0.0456  0.0505  153 LYS B NZ  
5366 N N   . GLY B 154 ? 0.3813 0.5290 0.4480 -0.0110 0.0485  0.0438  154 GLY B N   
5367 C CA  . GLY B 154 ? 0.4013 0.5338 0.4658 -0.0133 0.0521  0.0455  154 GLY B CA  
5368 C C   . GLY B 154 ? 0.3868 0.5167 0.4489 -0.0084 0.0545  0.0494  154 GLY B C   
5369 O O   . GLY B 154 ? 0.3178 0.4352 0.3774 -0.0081 0.0569  0.0516  154 GLY B O   
5370 N N   . ARG B 155 ? 0.3559 0.4975 0.4185 -0.0042 0.0541  0.0506  155 ARG B N   
5371 C CA  . ARG B 155 ? 0.3759 0.5165 0.4363 -0.0004 0.0569  0.0543  155 ARG B CA  
5372 C C   . ARG B 155 ? 0.4152 0.5693 0.4757 0.0056  0.0552  0.0545  155 ARG B C   
5373 O O   . ARG B 155 ? 0.4360 0.6009 0.4991 0.0060  0.0528  0.0524  155 ARG B O   
5374 C CB  . ARG B 155 ? 0.3756 0.5145 0.4380 -0.0073 0.0636  0.0568  155 ARG B CB  
5375 C CG  . ARG B 155 ? 0.4275 0.5802 0.4948 -0.0138 0.0658  0.0555  155 ARG B CG  
5376 C CD  . ARG B 155 ? 0.4683 0.6180 0.5372 -0.0212 0.0731  0.0578  155 ARG B CD  
5377 N NE  . ARG B 155 ? 0.5667 0.7018 0.6351 -0.0276 0.0762  0.0569  155 ARG B NE  
5378 C CZ  . ARG B 155 ? 0.6160 0.7365 0.6816 -0.0270 0.0806  0.0605  155 ARG B CZ  
5379 N NH1 . ARG B 155 ? 0.6933 0.8133 0.7564 -0.0207 0.0821  0.0653  155 ARG B NH1 
5380 N NH2 . ARG B 155 ? 0.5765 0.6837 0.6417 -0.0325 0.0838  0.0596  155 ARG B NH2 
5381 N N   . ASN B 156 ? 0.3995 0.5534 0.4571 0.0104  0.0568  0.0574  156 ASN B N   
5382 C CA  . ASN B 156 ? 0.4358 0.6019 0.4931 0.0158  0.0565  0.0581  156 ASN B CA  
5383 C C   . ASN B 156 ? 0.4114 0.5804 0.4670 0.0225  0.0515  0.0551  156 ASN B C   
5384 O O   . ASN B 156 ? 0.4214 0.6025 0.4795 0.0244  0.0507  0.0542  156 ASN B O   
5385 C CB  . ASN B 156 ? 0.5059 0.6854 0.5684 0.0106  0.0597  0.0587  156 ASN B CB  
5386 C CG  . ASN B 156 ? 0.5461 0.7214 0.6101 0.0034  0.0655  0.0615  156 ASN B CG  
5387 O OD1 . ASN B 156 ? 0.5754 0.7410 0.6360 0.0050  0.0679  0.0645  156 ASN B OD1 
5388 N ND2 . ASN B 156 ? 0.5478 0.7305 0.6167 -0.0047 0.0683  0.0605  156 ASN B ND2 
5389 N N   . TYR B 157 ? 0.3635 0.5214 0.4147 0.0263  0.0486  0.0539  157 TYR B N   
5390 C CA  . TYR B 157 ? 0.3641 0.5219 0.4129 0.0324  0.0447  0.0510  157 TYR B CA  
5391 C C   . TYR B 157 ? 0.4039 0.5651 0.4486 0.0396  0.0449  0.0512  157 TYR B C   
5392 O O   . TYR B 157 ? 0.3805 0.5396 0.4223 0.0405  0.0468  0.0531  157 TYR B O   
5393 C CB  . TYR B 157 ? 0.3666 0.5110 0.4126 0.0323  0.0417  0.0491  157 TYR B CB  
5394 C CG  . TYR B 157 ? 0.3572 0.4980 0.4068 0.0256  0.0415  0.0484  157 TYR B CG  
5395 C CD1 . TYR B 157 ? 0.3153 0.4614 0.3676 0.0247  0.0393  0.0463  157 TYR B CD1 
5396 C CD2 . TYR B 157 ? 0.3650 0.4975 0.4150 0.0202  0.0438  0.0500  157 TYR B CD2 
5397 C CE1 . TYR B 157 ? 0.2795 0.4233 0.3348 0.0181  0.0391  0.0453  157 TYR B CE1 
5398 C CE2 . TYR B 157 ? 0.3191 0.4478 0.3720 0.0137  0.0440  0.0488  157 TYR B CE2 
5399 C CZ  . TYR B 157 ? 0.3141 0.4488 0.3696 0.0124  0.0415  0.0462  157 TYR B CZ  
5400 O OH  . TYR B 157 ? 0.2900 0.4218 0.3480 0.0056  0.0417  0.0446  157 TYR B OH  
5401 N N   . THR B 158 ? 0.3260 0.4925 0.3701 0.0450  0.0434  0.0493  158 THR B N   
5402 C CA  . THR B 158 ? 0.3757 0.5441 0.4152 0.0521  0.0438  0.0484  158 THR B CA  
5403 C C   . THR B 158 ? 0.3775 0.5337 0.4112 0.0558  0.0412  0.0453  158 THR B C   
5404 O O   . THR B 158 ? 0.4494 0.5972 0.4831 0.0536  0.0388  0.0438  158 THR B O   
5405 C CB  . THR B 158 ? 0.3427 0.5232 0.3846 0.0565  0.0445  0.0483  158 THR B CB  
5406 O OG1 . THR B 158 ? 0.4066 0.5838 0.4484 0.0592  0.0419  0.0462  158 THR B OG1 
5407 C CG2 . THR B 158 ? 0.3358 0.5292 0.3843 0.0513  0.0464  0.0509  158 THR B CG2 
5408 N N   . GLN B 159 ? 0.3159 0.4713 0.3441 0.0609  0.0419  0.0439  159 GLN B N   
5409 C CA  . GLN B 159 ? 0.3873 0.5318 0.4096 0.0640  0.0399  0.0401  159 GLN B CA  
5410 C C   . GLN B 159 ? 0.4433 0.5848 0.4659 0.0672  0.0386  0.0378  159 GLN B C   
5411 O O   . GLN B 159 ? 0.4247 0.5555 0.4446 0.0671  0.0366  0.0353  159 GLN B O   
5412 C CB  . GLN B 159 ? 0.4193 0.5650 0.4355 0.0683  0.0415  0.0385  159 GLN B CB  
5413 C CG  . GLN B 159 ? 0.3333 0.4686 0.3426 0.0713  0.0403  0.0337  159 GLN B CG  
5414 C CD  . GLN B 159 ? 0.3412 0.4680 0.3480 0.0675  0.0380  0.0327  159 GLN B CD  
5415 O OE1 . GLN B 159 ? 0.3320 0.4613 0.3401 0.0641  0.0381  0.0357  159 GLN B OE1 
5416 N NE2 . GLN B 159 ? 0.2998 0.4166 0.3029 0.0681  0.0363  0.0286  159 GLN B NE2 
5417 N N   . GLU B 160 ? 0.3380 0.4893 0.3641 0.0701  0.0400  0.0391  160 GLU B N   
5418 C CA  . GLU B 160 ? 0.3597 0.5095 0.3864 0.0741  0.0391  0.0380  160 GLU B CA  
5419 C C   . GLU B 160 ? 0.3537 0.5003 0.3842 0.0692  0.0365  0.0385  160 GLU B C   
5420 O O   . GLU B 160 ? 0.3597 0.4977 0.3881 0.0711  0.0349  0.0367  160 GLU B O   
5421 C CB  . GLU B 160 ? 0.4454 0.6090 0.4754 0.0788  0.0413  0.0401  160 GLU B CB  
5422 C CG  . GLU B 160 ? 0.5662 0.7323 0.5988 0.0821  0.0405  0.0407  160 GLU B CG  
5423 C CD  . GLU B 160 ? 0.6594 0.8406 0.6951 0.0879  0.0429  0.0431  160 GLU B CD  
5424 O OE1 . GLU B 160 ? 0.6730 0.8520 0.7062 0.0956  0.0443  0.0428  160 GLU B OE1 
5425 O OE2 . GLU B 160 ? 0.6926 0.8877 0.7333 0.0848  0.0438  0.0456  160 GLU B OE2 
5426 N N   . GLU B 161 ? 0.3184 0.4712 0.3541 0.0627  0.0363  0.0408  161 GLU B N   
5427 C CA  . GLU B 161 ? 0.3216 0.4714 0.3606 0.0575  0.0340  0.0409  161 GLU B CA  
5428 C C   . GLU B 161 ? 0.3485 0.4832 0.3837 0.0552  0.0321  0.0388  161 GLU B C   
5429 O O   . GLU B 161 ? 0.3789 0.5073 0.4141 0.0545  0.0300  0.0376  161 GLU B O   
5430 C CB  . GLU B 161 ? 0.3208 0.4796 0.3657 0.0503  0.0351  0.0432  161 GLU B CB  
5431 C CG  . GLU B 161 ? 0.3266 0.5025 0.3765 0.0510  0.0365  0.0450  161 GLU B CG  
5432 C CD  . GLU B 161 ? 0.4528 0.6371 0.5076 0.0434  0.0387  0.0468  161 GLU B CD  
5433 O OE1 . GLU B 161 ? 0.4661 0.6422 0.5196 0.0389  0.0399  0.0473  161 GLU B OE1 
5434 O OE2 . GLU B 161 ? 0.4791 0.6785 0.5387 0.0420  0.0397  0.0480  161 GLU B OE2 
5435 N N   . LYS B 162 ? 0.3389 0.4688 0.3710 0.0543  0.0329  0.0388  162 LYS B N   
5436 C CA  . LYS B 162 ? 0.3475 0.4649 0.3759 0.0525  0.0311  0.0370  162 LYS B CA  
5437 C C   . LYS B 162 ? 0.3808 0.4899 0.4043 0.0571  0.0297  0.0336  162 LYS B C   
5438 O O   . LYS B 162 ? 0.3092 0.4088 0.3313 0.0554  0.0277  0.0319  162 LYS B O   
5439 C CB  . LYS B 162 ? 0.3201 0.4366 0.3457 0.0516  0.0324  0.0381  162 LYS B CB  
5440 C CG  . LYS B 162 ? 0.2639 0.3698 0.2856 0.0504  0.0306  0.0365  162 LYS B CG  
5441 C CD  . LYS B 162 ? 0.3178 0.4255 0.3365 0.0506  0.0319  0.0380  162 LYS B CD  
5442 C CE  . LYS B 162 ? 0.4027 0.5151 0.4170 0.0555  0.0331  0.0362  162 LYS B CE  
5443 N NZ  . LYS B 162 ? 0.3703 0.4852 0.3806 0.0560  0.0339  0.0372  162 LYS B NZ  
5444 N N   . GLU B 163 ? 0.3951 0.5070 0.4157 0.0630  0.0313  0.0324  163 GLU B N   
5445 C CA  . GLU B 163 ? 0.3576 0.4602 0.3731 0.0674  0.0311  0.0289  163 GLU B CA  
5446 C C   . GLU B 163 ? 0.3782 0.4795 0.3962 0.0689  0.0301  0.0294  163 GLU B C   
5447 O O   . GLU B 163 ? 0.3815 0.4722 0.3961 0.0704  0.0294  0.0270  163 GLU B O   
5448 C CB  . GLU B 163 ? 0.3784 0.4835 0.3897 0.0734  0.0339  0.0274  163 GLU B CB  
5449 C CG  . GLU B 163 ? 0.4293 0.5326 0.4356 0.0724  0.0346  0.0255  163 GLU B CG  
5450 C CD  . GLU B 163 ? 0.5562 0.6649 0.5592 0.0776  0.0378  0.0246  163 GLU B CD  
5451 O OE1 . GLU B 163 ? 0.6187 0.7331 0.6238 0.0822  0.0397  0.0258  163 GLU B OE1 
5452 O OE2 . GLU B 163 ? 0.5623 0.6705 0.5606 0.0771  0.0384  0.0226  163 GLU B OE2 
5453 N N   . TYR B 164 ? 0.3151 0.4277 0.3390 0.0684  0.0303  0.0325  164 TYR B N   
5454 C CA  . TYR B 164 ? 0.4003 0.5140 0.4270 0.0694  0.0290  0.0334  164 TYR B CA  
5455 C C   . TYR B 164 ? 0.3863 0.4914 0.4136 0.0638  0.0263  0.0325  164 TYR B C   
5456 O O   . TYR B 164 ? 0.3906 0.4886 0.4163 0.0656  0.0253  0.0316  164 TYR B O   
5457 C CB  . TYR B 164 ? 0.4120 0.5422 0.4452 0.0686  0.0295  0.0367  164 TYR B CB  
5458 C CG  . TYR B 164 ? 0.4810 0.6152 0.5173 0.0694  0.0280  0.0380  164 TYR B CG  
5459 C CD1 . TYR B 164 ? 0.4513 0.5853 0.4857 0.0773  0.0290  0.0387  164 TYR B CD1 
5460 C CD2 . TYR B 164 ? 0.5125 0.6505 0.5532 0.0623  0.0260  0.0387  164 TYR B CD2 
5461 C CE1 . TYR B 164 ? 0.4308 0.5695 0.4677 0.0785  0.0278  0.0405  164 TYR B CE1 
5462 C CE2 . TYR B 164 ? 0.4808 0.6238 0.5240 0.0628  0.0245  0.0398  164 TYR B CE2 
5463 C CZ  . TYR B 164 ? 0.4522 0.5961 0.4935 0.0712  0.0253  0.0410  164 TYR B CZ  
5464 O OH  . TYR B 164 ? 0.5481 0.6982 0.5918 0.0724  0.0239  0.0428  164 TYR B OH  
5465 N N   . VAL B 165 ? 0.3679 0.4731 0.3972 0.0573  0.0256  0.0330  165 VAL B N   
5466 C CA  . VAL B 165 ? 0.3326 0.4294 0.3624 0.0522  0.0234  0.0323  165 VAL B CA  
5467 C C   . VAL B 165 ? 0.3547 0.4380 0.3787 0.0540  0.0225  0.0293  165 VAL B C   
5468 O O   . VAL B 165 ? 0.3680 0.4442 0.3914 0.0534  0.0209  0.0283  165 VAL B O   
5469 C CB  . VAL B 165 ? 0.3239 0.4222 0.3563 0.0458  0.0239  0.0337  165 VAL B CB  
5470 C CG1 . VAL B 165 ? 0.3078 0.3961 0.3399 0.0412  0.0222  0.0328  165 VAL B CG1 
5471 C CG2 . VAL B 165 ? 0.2962 0.4070 0.3343 0.0426  0.0251  0.0360  165 VAL B CG2 
5472 N N   . LEU B 166 ? 0.3323 0.4126 0.3519 0.0561  0.0236  0.0278  166 LEU B N   
5473 C CA  . LEU B 166 ? 0.3738 0.4424 0.3877 0.0570  0.0230  0.0243  166 LEU B CA  
5474 C C   . LEU B 166 ? 0.4098 0.4724 0.4211 0.0617  0.0236  0.0227  166 LEU B C   
5475 O O   . LEU B 166 ? 0.4452 0.4972 0.4535 0.0609  0.0227  0.0204  166 LEU B O   
5476 C CB  . LEU B 166 ? 0.3787 0.4476 0.3880 0.0584  0.0244  0.0226  166 LEU B CB  
5477 C CG  . LEU B 166 ? 0.4096 0.4810 0.4194 0.0543  0.0239  0.0239  166 LEU B CG  
5478 C CD1 . LEU B 166 ? 0.4632 0.5359 0.4677 0.0564  0.0252  0.0218  166 LEU B CD1 
5479 C CD2 . LEU B 166 ? 0.3299 0.3939 0.3399 0.0500  0.0216  0.0234  166 LEU B CD2 
5480 N N   . ASN B 167 ? 0.3958 0.4650 0.4080 0.0670  0.0256  0.0241  167 ASN B N   
5481 C CA  . ASN B 167 ? 0.4152 0.4790 0.4251 0.0726  0.0269  0.0235  167 ASN B CA  
5482 C C   . ASN B 167 ? 0.4023 0.4643 0.4151 0.0708  0.0248  0.0251  167 ASN B C   
5483 O O   . ASN B 167 ? 0.3756 0.4268 0.3851 0.0724  0.0250  0.0235  167 ASN B O   
5484 C CB  . ASN B 167 ? 0.4839 0.5575 0.4950 0.0790  0.0296  0.0257  167 ASN B CB  
5485 C CG  . ASN B 167 ? 0.5866 0.6603 0.5935 0.0820  0.0324  0.0237  167 ASN B CG  
5486 O OD1 . ASN B 167 ? 0.6271 0.6912 0.6286 0.0805  0.0328  0.0199  167 ASN B OD1 
5487 N ND2 . ASN B 167 ? 0.5727 0.6582 0.5821 0.0859  0.0343  0.0261  167 ASN B ND2 
5488 N N   . LYS B 168 ? 0.2898 0.3624 0.3087 0.0672  0.0231  0.0279  168 LYS B N   
5489 C CA  . LYS B 168 ? 0.2624 0.3347 0.2841 0.0647  0.0209  0.0291  168 LYS B CA  
5490 C C   . LYS B 168 ? 0.3190 0.3797 0.3389 0.0593  0.0190  0.0269  168 LYS B C   
5491 O O   . LYS B 168 ? 0.3134 0.3685 0.3330 0.0587  0.0177  0.0268  168 LYS B O   
5492 C CB  . LYS B 168 ? 0.3330 0.4198 0.3613 0.0609  0.0200  0.0319  168 LYS B CB  
5493 C CG  . LYS B 168 ? 0.3854 0.4866 0.4164 0.0656  0.0218  0.0344  168 LYS B CG  
5494 C CD  . LYS B 168 ? 0.3925 0.4946 0.4221 0.0733  0.0228  0.0360  168 LYS B CD  
5495 C CE  . LYS B 168 ? 0.4291 0.5358 0.4618 0.0714  0.0207  0.0378  168 LYS B CE  
5496 N NZ  . LYS B 168 ? 0.4465 0.5529 0.4775 0.0796  0.0219  0.0401  168 LYS B NZ  
5497 N N   . TYR B 169 ? 0.2908 0.3488 0.3096 0.0556  0.0187  0.0254  169 TYR B N   
5498 C CA  . TYR B 169 ? 0.3519 0.4003 0.3692 0.0510  0.0170  0.0236  169 TYR B CA  
5499 C C   . TYR B 169 ? 0.3438 0.3800 0.3553 0.0536  0.0174  0.0205  169 TYR B C   
5500 O O   . TYR B 169 ? 0.3119 0.3402 0.3225 0.0512  0.0160  0.0195  169 TYR B O   
5501 C CB  . TYR B 169 ? 0.3055 0.3556 0.3230 0.0474  0.0170  0.0236  169 TYR B CB  
5502 C CG  . TYR B 169 ? 0.3007 0.3578 0.3237 0.0426  0.0167  0.0263  169 TYR B CG  
5503 C CD1 . TYR B 169 ? 0.3096 0.3727 0.3367 0.0413  0.0164  0.0279  169 TYR B CD1 
5504 C CD2 . TYR B 169 ? 0.3232 0.3807 0.3467 0.0393  0.0172  0.0272  169 TYR B CD2 
5505 C CE1 . TYR B 169 ? 0.3233 0.3920 0.3550 0.0359  0.0167  0.0296  169 TYR B CE1 
5506 C CE2 . TYR B 169 ? 0.3002 0.3620 0.3281 0.0348  0.0179  0.0296  169 TYR B CE2 
5507 C CZ  . TYR B 169 ? 0.2665 0.3334 0.2984 0.0327  0.0178  0.0303  169 TYR B CZ  
5508 O OH  . TYR B 169 ? 0.3192 0.3895 0.3549 0.0273  0.0191  0.0319  169 TYR B OH  
5509 N N   . PHE B 170 ? 0.3588 0.3931 0.3661 0.0581  0.0197  0.0188  170 PHE B N   
5510 C CA  . PHE B 170 ? 0.3731 0.3949 0.3744 0.0600  0.0210  0.0153  170 PHE B CA  
5511 C C   . PHE B 170 ? 0.3754 0.3928 0.3765 0.0641  0.0220  0.0166  170 PHE B C   
5512 O O   . PHE B 170 ? 0.3328 0.3386 0.3303 0.0637  0.0224  0.0145  170 PHE B O   
5513 C CB  . PHE B 170 ? 0.3888 0.4092 0.3851 0.0633  0.0238  0.0125  170 PHE B CB  
5514 C CG  . PHE B 170 ? 0.4022 0.4228 0.3963 0.0589  0.0229  0.0100  170 PHE B CG  
5515 C CD1 . PHE B 170 ? 0.4166 0.4278 0.4064 0.0555  0.0223  0.0061  170 PHE B CD1 
5516 C CD2 . PHE B 170 ? 0.3976 0.4286 0.3939 0.0581  0.0227  0.0117  170 PHE B CD2 
5517 C CE1 . PHE B 170 ? 0.4321 0.4459 0.4199 0.0517  0.0212  0.0041  170 PHE B CE1 
5518 C CE2 . PHE B 170 ? 0.4477 0.4802 0.4419 0.0548  0.0219  0.0102  170 PHE B CE2 
5519 C CZ  . PHE B 170 ? 0.4518 0.4764 0.4418 0.0517  0.0210  0.0064  170 PHE B CZ  
5520 N N   . GLU B 171 ? 0.3659 0.3929 0.3708 0.0678  0.0224  0.0203  171 GLU B N   
5521 C CA  . GLU B 171 ? 0.4109 0.4363 0.4164 0.0716  0.0229  0.0226  171 GLU B CA  
5522 C C   . GLU B 171 ? 0.3741 0.3951 0.3811 0.0665  0.0200  0.0227  171 GLU B C   
5523 O O   . GLU B 171 ? 0.3983 0.4099 0.4026 0.0682  0.0208  0.0224  171 GLU B O   
5524 C CB  . GLU B 171 ? 0.4691 0.5096 0.4795 0.0753  0.0232  0.0269  171 GLU B CB  
5525 C CG  . GLU B 171 ? 0.6301 0.6756 0.6392 0.0812  0.0263  0.0273  171 GLU B CG  
5526 C CD  . GLU B 171 ? 0.7056 0.7620 0.7175 0.0881  0.0279  0.0317  171 GLU B CD  
5527 O OE1 . GLU B 171 ? 0.6247 0.6922 0.6418 0.0862  0.0255  0.0347  171 GLU B OE1 
5528 O OE2 . GLU B 171 ? 0.7684 0.8229 0.7772 0.0955  0.0317  0.0321  171 GLU B OE2 
5529 N N   . ILE B 172 ? 0.2975 0.3250 0.3088 0.0603  0.0173  0.0232  172 ILE B N   
5530 C CA  . ILE B 172 ? 0.3280 0.3517 0.3408 0.0552  0.0148  0.0231  172 ILE B CA  
5531 C C   . ILE B 172 ? 0.3191 0.3288 0.3272 0.0532  0.0148  0.0197  172 ILE B C   
5532 O O   . ILE B 172 ? 0.3119 0.3144 0.3189 0.0525  0.0142  0.0194  172 ILE B O   
5533 C CB  . ILE B 172 ? 0.3710 0.4028 0.3887 0.0490  0.0129  0.0239  172 ILE B CB  
5534 C CG1 . ILE B 172 ? 0.4552 0.5015 0.4778 0.0496  0.0129  0.0269  172 ILE B CG1 
5535 C CG2 . ILE B 172 ? 0.3078 0.3339 0.3263 0.0436  0.0108  0.0232  172 ILE B CG2 
5536 C CD1 . ILE B 172 ? 0.4541 0.5046 0.4786 0.0508  0.0120  0.0289  172 ILE B CD1 
5537 N N   . ILE B 173 ? 0.2998 0.3063 0.3050 0.0522  0.0155  0.0169  173 ILE B N   
5538 C CA  . ILE B 173 ? 0.3213 0.3166 0.3220 0.0497  0.0155  0.0133  173 ILE B CA  
5539 C C   . ILE B 173 ? 0.3449 0.3293 0.3407 0.0537  0.0181  0.0117  173 ILE B C   
5540 O O   . ILE B 173 ? 0.3169 0.2920 0.3107 0.0515  0.0178  0.0103  173 ILE B O   
5541 C CB  . ILE B 173 ? 0.3627 0.3592 0.3610 0.0481  0.0160  0.0107  173 ILE B CB  
5542 C CG1 . ILE B 173 ? 0.4418 0.4477 0.4447 0.0443  0.0140  0.0129  173 ILE B CG1 
5543 C CG2 . ILE B 173 ? 0.3536 0.3400 0.3470 0.0452  0.0161  0.0064  173 ILE B CG2 
5544 C CD1 . ILE B 173 ? 0.4575 0.4661 0.4583 0.0428  0.0142  0.0112  173 ILE B CD1 
5545 N N   . LYS B 174 ? 0.3564 0.3414 0.3503 0.0597  0.0211  0.0123  174 LYS B N   
5546 C CA  . LYS B 174 ? 0.4402 0.4137 0.4291 0.0644  0.0248  0.0113  174 LYS B CA  
5547 C C   . LYS B 174 ? 0.4121 0.3829 0.4025 0.0659  0.0243  0.0145  174 LYS B C   
5548 O O   . LYS B 174 ? 0.4066 0.3650 0.3927 0.0679  0.0270  0.0134  174 LYS B O   
5549 C CB  . LYS B 174 ? 0.4696 0.4457 0.4568 0.0716  0.0285  0.0123  174 LYS B CB  
5550 C CG  . LYS B 174 ? 0.6374 0.6054 0.6183 0.0720  0.0318  0.0073  174 LYS B CG  
5551 C CD  . LYS B 174 ? 0.7488 0.7005 0.7237 0.0692  0.0337  0.0029  174 LYS B CD  
5552 C CE  . LYS B 174 ? 0.7564 0.6965 0.7281 0.0749  0.0379  0.0044  174 LYS B CE  
5553 N NZ  . LYS B 174 ? 0.7208 0.6450 0.6870 0.0706  0.0398  -0.0003 174 LYS B NZ  
5554 N N   . LYS B 175 ? 0.4139 0.3960 0.4102 0.0647  0.0212  0.0182  175 LYS B N   
5555 C CA  . LYS B 175 ? 0.3929 0.3752 0.3909 0.0661  0.0205  0.0215  175 LYS B CA  
5556 C C   . LYS B 175 ? 0.4353 0.4138 0.4345 0.0593  0.0175  0.0203  175 LYS B C   
5557 O O   . LYS B 175 ? 0.3928 0.3722 0.3935 0.0595  0.0165  0.0228  175 LYS B O   
5558 C CB  . LYS B 175 ? 0.4355 0.4340 0.4390 0.0687  0.0193  0.0260  175 LYS B CB  
5559 C CG  . LYS B 175 ? 0.4652 0.4689 0.4679 0.0768  0.0225  0.0283  175 LYS B CG  
5560 C CD  . LYS B 175 ? 0.5055 0.5283 0.5144 0.0776  0.0207  0.0322  175 LYS B CD  
5561 C CE  . LYS B 175 ? 0.5988 0.6284 0.6076 0.0870  0.0238  0.0362  175 LYS B CE  
5562 N NZ  . LYS B 175 ? 0.6063 0.6412 0.6151 0.0899  0.0259  0.0355  175 LYS B NZ  
5563 N N   . THR B 176 ? 0.4122 0.3871 0.4106 0.0537  0.0161  0.0167  176 THR B N   
5564 C CA  . THR B 176 ? 0.3441 0.3186 0.3449 0.0474  0.0131  0.0163  176 THR B CA  
5565 C C   . THR B 176 ? 0.3717 0.3342 0.3692 0.0464  0.0137  0.0151  176 THR B C   
5566 O O   . THR B 176 ? 0.3947 0.3580 0.3943 0.0447  0.0121  0.0169  176 THR B O   
5567 C CB  . THR B 176 ? 0.3047 0.2809 0.3060 0.0425  0.0118  0.0138  176 THR B CB  
5568 O OG1 . THR B 176 ? 0.3049 0.2930 0.3104 0.0426  0.0110  0.0158  176 THR B OG1 
5569 C CG2 . THR B 176 ? 0.2515 0.2249 0.2543 0.0367  0.0095  0.0130  176 THR B CG2 
5570 N N   . LEU B 177 ? 0.2744 0.2256 0.2665 0.0470  0.0163  0.0117  177 LEU B N   
5571 C CA  . LEU B 177 ? 0.4019 0.3412 0.3906 0.0455  0.0174  0.0104  177 LEU B CA  
5572 C C   . LEU B 177 ? 0.3716 0.3081 0.3597 0.0510  0.0193  0.0142  177 LEU B C   
5573 O O   . LEU B 177 ? 0.3224 0.2531 0.3098 0.0496  0.0191  0.0150  177 LEU B O   
5574 C CB  . LEU B 177 ? 0.4243 0.3524 0.4071 0.0440  0.0202  0.0054  177 LEU B CB  
5575 C CG  . LEU B 177 ? 0.4174 0.3493 0.4008 0.0377  0.0178  0.0018  177 LEU B CG  
5576 C CD1 . LEU B 177 ? 0.5078 0.4311 0.4852 0.0359  0.0206  -0.0036 177 LEU B CD1 
5577 C CD2 . LEU B 177 ? 0.3717 0.3048 0.3582 0.0321  0.0146  0.0021  177 LEU B CD2 
5578 N N   . SER B 178 ? 0.3135 0.2552 0.3019 0.0576  0.0212  0.0170  178 SER B N   
5579 C CA  . SER B 178 ? 0.3207 0.2630 0.3090 0.0638  0.0229  0.0218  178 SER B CA  
5580 C C   . SER B 178 ? 0.3223 0.2749 0.3157 0.0614  0.0191  0.0250  178 SER B C   
5581 O O   . SER B 178 ? 0.3997 0.3492 0.3922 0.0633  0.0197  0.0277  178 SER B O   
5582 C CB  . SER B 178 ? 0.3367 0.2860 0.3254 0.0715  0.0253  0.0247  178 SER B CB  
5583 O OG  . SER B 178 ? 0.4373 0.3761 0.4208 0.0742  0.0296  0.0216  178 SER B OG  
5584 N N   . ILE B 179 ? 0.3846 0.3495 0.3829 0.0572  0.0155  0.0249  179 ILE B N   
5585 C CA  . ILE B 179 ? 0.3920 0.3669 0.3946 0.0548  0.0125  0.0275  179 ILE B CA  
5586 C C   . ILE B 179 ? 0.3837 0.3505 0.3855 0.0494  0.0111  0.0259  179 ILE B C   
5587 O O   . ILE B 179 ? 0.4003 0.3709 0.4035 0.0489  0.0098  0.0282  179 ILE B O   
5588 C CB  . ILE B 179 ? 0.4111 0.4003 0.4190 0.0513  0.0099  0.0276  179 ILE B CB  
5589 C CG1 . ILE B 179 ? 0.4618 0.4636 0.4735 0.0508  0.0080  0.0309  179 ILE B CG1 
5590 C CG2 . ILE B 179 ? 0.2886 0.2752 0.2979 0.0440  0.0080  0.0242  179 ILE B CG2 
5591 C CD1 . ILE B 179 ? 0.4004 0.4168 0.4171 0.0475  0.0064  0.0311  179 ILE B CD1 
5592 N N   . TYR B 180 ? 0.3313 0.2878 0.3307 0.0455  0.0114  0.0219  180 TYR B N   
5593 C CA  . TYR B 180 ? 0.3064 0.2550 0.3047 0.0411  0.0105  0.0206  180 TYR B CA  
5594 C C   . TYR B 180 ? 0.3450 0.2839 0.3392 0.0451  0.0132  0.0223  180 TYR B C   
5595 O O   . TYR B 180 ? 0.3709 0.3094 0.3656 0.0438  0.0123  0.0240  180 TYR B O   
5596 C CB  . TYR B 180 ? 0.2887 0.2308 0.2855 0.0360  0.0102  0.0162  180 TYR B CB  
5597 C CG  . TYR B 180 ? 0.3317 0.2831 0.3329 0.0317  0.0074  0.0155  180 TYR B CG  
5598 C CD1 . TYR B 180 ? 0.2651 0.2202 0.2697 0.0273  0.0051  0.0162  180 TYR B CD1 
5599 C CD2 . TYR B 180 ? 0.2824 0.2381 0.2840 0.0322  0.0077  0.0144  180 TYR B CD2 
5600 C CE1 . TYR B 180 ? 0.3462 0.3082 0.3544 0.0237  0.0036  0.0159  180 TYR B CE1 
5601 C CE2 . TYR B 180 ? 0.3416 0.3051 0.3469 0.0287  0.0059  0.0144  180 TYR B CE2 
5602 C CZ  . TYR B 180 ? 0.3356 0.3016 0.3442 0.0246  0.0041  0.0152  180 TYR B CZ  
5603 O OH  . TYR B 180 ? 0.2930 0.2651 0.3050 0.0214  0.0032  0.0155  180 TYR B OH  
5604 N N   . ARG B 181 ? 0.3844 0.3152 0.3743 0.0502  0.0171  0.0221  181 ARG B N   
5605 C CA  . ARG B 181 ? 0.3745 0.2955 0.3604 0.0549  0.0207  0.0246  181 ARG B CA  
5606 C C   . ARG B 181 ? 0.3943 0.3258 0.3827 0.0599  0.0199  0.0304  181 ARG B C   
5607 O O   . ARG B 181 ? 0.3738 0.3009 0.3605 0.0616  0.0210  0.0332  181 ARG B O   
5608 C CB  . ARG B 181 ? 0.3502 0.2606 0.3309 0.0602  0.0259  0.0235  181 ARG B CB  
5609 C CG  . ARG B 181 ? 0.3656 0.2663 0.3430 0.0553  0.0272  0.0172  181 ARG B CG  
5610 C CD  . ARG B 181 ? 0.4208 0.3090 0.3920 0.0604  0.0333  0.0157  181 ARG B CD  
5611 N NE  . ARG B 181 ? 0.5256 0.4084 0.4939 0.0553  0.0341  0.0093  181 ARG B NE  
5612 C CZ  . ARG B 181 ? 0.5560 0.4449 0.5247 0.0564  0.0340  0.0074  181 ARG B CZ  
5613 N NH1 . ARG B 181 ? 0.5459 0.4458 0.5178 0.0622  0.0334  0.0115  181 ARG B NH1 
5614 N NH2 . ARG B 181 ? 0.5644 0.4491 0.5301 0.0514  0.0346  0.0015  181 ARG B NH2 
5615 N N   . GLU B 182 ? 0.3501 0.2965 0.3426 0.0620  0.0181  0.0324  182 GLU B N   
5616 C CA  . GLU B 182 ? 0.3756 0.3350 0.3706 0.0667  0.0173  0.0379  182 GLU B CA  
5617 C C   . GLU B 182 ? 0.3806 0.3468 0.3785 0.0612  0.0136  0.0384  182 GLU B C   
5618 O O   . GLU B 182 ? 0.3660 0.3340 0.3630 0.0641  0.0140  0.0422  182 GLU B O   
5619 C CB  . GLU B 182 ? 0.4242 0.3987 0.4229 0.0693  0.0164  0.0393  182 GLU B CB  
5620 C CG  . GLU B 182 ? 0.5131 0.5055 0.5155 0.0721  0.0146  0.0442  182 GLU B CG  
5621 C CD  . GLU B 182 ? 0.6256 0.6347 0.6326 0.0725  0.0132  0.0447  182 GLU B CD  
5622 O OE1 . GLU B 182 ? 0.6228 0.6487 0.6336 0.0719  0.0109  0.0473  182 GLU B OE1 
5623 O OE2 . GLU B 182 ? 0.6385 0.6443 0.6450 0.0729  0.0144  0.0424  182 GLU B OE2 
5624 N N   . ILE B 183 ? 0.3231 0.2931 0.3242 0.0535  0.0103  0.0348  183 ILE B N   
5625 C CA  . ILE B 183 ? 0.3445 0.3201 0.3480 0.0481  0.0074  0.0349  183 ILE B CA  
5626 C C   . ILE B 183 ? 0.3910 0.3533 0.3910 0.0466  0.0083  0.0343  183 ILE B C   
5627 O O   . ILE B 183 ? 0.3540 0.3197 0.3544 0.0453  0.0072  0.0361  183 ILE B O   
5628 C CB  . ILE B 183 ? 0.4806 0.4616 0.4880 0.0407  0.0047  0.0313  183 ILE B CB  
5629 C CG1 . ILE B 183 ? 0.4727 0.4416 0.4785 0.0371  0.0051  0.0273  183 ILE B CG1 
5630 C CG2 . ILE B 183 ? 0.4886 0.4828 0.4995 0.0419  0.0041  0.0321  183 ILE B CG2 
5631 C CD1 . ILE B 183 ? 0.4232 0.3877 0.4297 0.0305  0.0035  0.0251  183 ILE B CD1 
5632 N N   . LYS B 184 ? 0.3969 0.3447 0.3934 0.0464  0.0106  0.0316  184 LYS B N   
5633 C CA  . LYS B 184 ? 0.3696 0.3044 0.3626 0.0447  0.0120  0.0309  184 LYS B CA  
5634 C C   . LYS B 184 ? 0.4227 0.3540 0.4124 0.0514  0.0150  0.0356  184 LYS B C   
5635 O O   . LYS B 184 ? 0.4643 0.3947 0.4534 0.0505  0.0146  0.0376  184 LYS B O   
5636 C CB  . LYS B 184 ? 0.4143 0.3360 0.4042 0.0423  0.0140  0.0264  184 LYS B CB  
5637 C CG  . LYS B 184 ? 0.4963 0.4058 0.4833 0.0382  0.0151  0.0242  184 LYS B CG  
5638 C CD  . LYS B 184 ? 0.4948 0.3945 0.4790 0.0352  0.0168  0.0192  184 LYS B CD  
5639 C CE  . LYS B 184 ? 0.5169 0.4033 0.4973 0.0318  0.0190  0.0171  184 LYS B CE  
5640 N NZ  . LYS B 184 ? 0.5256 0.4028 0.5020 0.0371  0.0232  0.0206  184 LYS B NZ  
5641 N N   . GLU B 185 ? 0.3965 0.3259 0.3840 0.0587  0.0184  0.0380  185 GLU B N   
5642 C CA  . GLU B 185 ? 0.4809 0.4064 0.4651 0.0664  0.0221  0.0434  185 GLU B CA  
5643 C C   . GLU B 185 ? 0.4643 0.4063 0.4516 0.0687  0.0194  0.0485  185 GLU B C   
5644 O O   . GLU B 185 ? 0.4477 0.3875 0.4327 0.0717  0.0209  0.0525  185 GLU B O   
5645 C CB  . GLU B 185 ? 0.5860 0.5075 0.5675 0.0744  0.0265  0.0452  185 GLU B CB  
5646 C CG  . GLU B 185 ? 0.6952 0.5977 0.6717 0.0732  0.0308  0.0406  185 GLU B CG  
5647 C CD  . GLU B 185 ? 0.7757 0.6721 0.7486 0.0822  0.0364  0.0430  185 GLU B CD  
5648 O OE1 . GLU B 185 ? 0.7766 0.6589 0.7443 0.0870  0.0420  0.0454  185 GLU B OE1 
5649 O OE2 . GLU B 185 ? 0.7835 0.6890 0.7587 0.0846  0.0357  0.0427  185 GLU B OE2 
5650 N N   . GLU B 186 ? 0.4366 0.3957 0.4288 0.0669  0.0158  0.0483  186 GLU B N   
5651 C CA  . GLU B 186 ? 0.4713 0.4483 0.4665 0.0681  0.0132  0.0523  186 GLU B CA  
5652 C C   . GLU B 186 ? 0.4348 0.4146 0.4314 0.0606  0.0099  0.0505  186 GLU B C   
5653 O O   . GLU B 186 ? 0.3961 0.3913 0.3949 0.0602  0.0076  0.0530  186 GLU B O   
5654 C CB  . GLU B 186 ? 0.5441 0.5385 0.5440 0.0679  0.0108  0.0521  186 GLU B CB  
5655 C CG  . GLU B 186 ? 0.5893 0.5859 0.5883 0.0768  0.0140  0.0554  186 GLU B CG  
5656 C CD  . GLU B 186 ? 0.6895 0.6994 0.6929 0.0751  0.0120  0.0537  186 GLU B CD  
5657 O OE1 . GLU B 186 ? 0.7049 0.7223 0.7119 0.0669  0.0084  0.0502  186 GLU B OE1 
5658 O OE2 . GLU B 186 ? 0.7353 0.7478 0.7383 0.0820  0.0146  0.0560  186 GLU B OE2 
5659 N N   . GLY B 187 ? 0.4466 0.4128 0.4418 0.0546  0.0098  0.0462  187 GLY B N   
5660 C CA  . GLY B 187 ? 0.3978 0.3653 0.3940 0.0479  0.0072  0.0445  187 GLY B CA  
5661 C C   . GLY B 187 ? 0.4225 0.4022 0.4235 0.0410  0.0035  0.0413  187 GLY B C   
5662 O O   . GLY B 187 ? 0.3858 0.3695 0.3877 0.0360  0.0016  0.0403  187 GLY B O   
5663 N N   . LYS B 188 ? 0.3801 0.3653 0.3838 0.0405  0.0029  0.0396  188 LYS B N   
5664 C CA  . LYS B 188 ? 0.3527 0.3481 0.3606 0.0339  0.0003  0.0366  188 LYS B CA  
5665 C C   . LYS B 188 ? 0.3845 0.3699 0.3930 0.0275  -0.0002 0.0319  188 LYS B C   
5666 O O   . LYS B 188 ? 0.2477 0.2387 0.2592 0.0216  -0.0017 0.0295  188 LYS B O   
5667 C CB  . LYS B 188 ? 0.4216 0.4284 0.4322 0.0362  0.0001  0.0373  188 LYS B CB  
5668 C CG  . LYS B 188 ? 0.3509 0.3713 0.3617 0.0427  0.0004  0.0422  188 LYS B CG  
5669 C CD  . LYS B 188 ? 0.3791 0.4098 0.3926 0.0453  0.0006  0.0428  188 LYS B CD  
5670 C CE  . LYS B 188 ? 0.4862 0.5350 0.5010 0.0507  0.0004  0.0477  188 LYS B CE  
5671 N NZ  . LYS B 188 ? 0.5151 0.5787 0.5340 0.0496  -0.0005 0.0471  188 LYS B NZ  
5672 N N   . GLY B 189 ? 0.3834 0.3545 0.3891 0.0285  0.0014  0.0307  189 GLY B N   
5673 C CA  . GLY B 189 ? 0.3707 0.3342 0.3771 0.0229  0.0009  0.0268  189 GLY B CA  
5674 C C   . GLY B 189 ? 0.3503 0.2994 0.3531 0.0236  0.0027  0.0255  189 GLY B C   
5675 O O   . GLY B 189 ? 0.3498 0.2932 0.3495 0.0286  0.0049  0.0268  189 GLY B O   
5676 N N   . SER B 190 ? 0.2774 0.2205 0.2804 0.0185  0.0021  0.0228  190 SER B N   
5677 C CA  . SER B 190 ? 0.2566 0.1878 0.2566 0.0179  0.0037  0.0207  190 SER B CA  
5678 C C   . SER B 190 ? 0.3010 0.2323 0.3019 0.0164  0.0035  0.0179  190 SER B C   
5679 O O   . SER B 190 ? 0.2989 0.2381 0.3034 0.0146  0.0019  0.0175  190 SER B O   
5680 C CB  . SER B 190 ? 0.2871 0.2131 0.2867 0.0133  0.0032  0.0195  190 SER B CB  
5681 O OG  . SER B 190 ? 0.3364 0.2615 0.3344 0.0149  0.0038  0.0222  190 SER B OG  
5682 N N   . VAL B 191 ? 0.3113 0.2341 0.3090 0.0171  0.0053  0.0159  191 VAL B N   
5683 C CA  . VAL B 191 ? 0.3477 0.2708 0.3456 0.0155  0.0052  0.0130  191 VAL B CA  
5684 C C   . VAL B 191 ? 0.3671 0.2832 0.3632 0.0111  0.0056  0.0099  191 VAL B C   
5685 O O   . VAL B 191 ? 0.3100 0.2168 0.3025 0.0110  0.0076  0.0092  191 VAL B O   
5686 C CB  . VAL B 191 ? 0.3511 0.2726 0.3465 0.0200  0.0072  0.0127  191 VAL B CB  
5687 C CG1 . VAL B 191 ? 0.3127 0.2354 0.3080 0.0178  0.0070  0.0094  191 VAL B CG1 
5688 C CG2 . VAL B 191 ? 0.2854 0.2160 0.2831 0.0244  0.0067  0.0161  191 VAL B CG2 
5689 N N   . SER B 192 ? 0.3432 0.2640 0.3418 0.0074  0.0039  0.0083  192 SER B N   
5690 C CA  . SER B 192 ? 0.3609 0.2786 0.3586 0.0031  0.0039  0.0055  192 SER B CA  
5691 C C   . SER B 192 ? 0.2813 0.2021 0.2783 0.0024  0.0039  0.0030  192 SER B C   
5692 O O   . SER B 192 ? 0.2851 0.2096 0.2823 0.0054  0.0040  0.0035  192 SER B O   
5693 C CB  . SER B 192 ? 0.4255 0.3478 0.4269 -0.0002 0.0021  0.0065  192 SER B CB  
5694 O OG  . SER B 192 ? 0.3466 0.2772 0.3516 0.0002  0.0009  0.0077  192 SER B OG  
5695 N N   . THR B 193 ? 0.3491 0.2694 0.3452 -0.0017 0.0038  0.0002  193 THR B N   
5696 C CA  . THR B 193 ? 0.4232 0.3486 0.4187 -0.0030 0.0035  -0.0023 193 THR B CA  
5697 C C   . THR B 193 ? 0.3777 0.3092 0.3756 -0.0071 0.0019  -0.0027 193 THR B C   
5698 O O   . THR B 193 ? 0.3403 0.2707 0.3400 -0.0088 0.0014  -0.0015 193 THR B O   
5699 C CB  . THR B 193 ? 0.3572 0.2753 0.3472 -0.0035 0.0060  -0.0063 193 THR B CB  
5700 O OG1 . THR B 193 ? 0.3385 0.2631 0.3277 -0.0040 0.0057  -0.0085 193 THR B OG1 
5701 C CG2 . THR B 193 ? 0.3207 0.2318 0.3079 -0.0082 0.0074  -0.0094 193 THR B CG2 
5702 N N   . SER B 194 ? 0.3216 0.2606 0.3195 -0.0083 0.0013  -0.0042 194 SER B N   
5703 C CA  . SER B 194 ? 0.2696 0.2163 0.2695 -0.0116 0.0000  -0.0045 194 SER B CA  
5704 C C   . SER B 194 ? 0.3737 0.3221 0.3698 -0.0154 0.0006  -0.0093 194 SER B C   
5705 O O   . SER B 194 ? 0.3049 0.2489 0.2970 -0.0151 0.0021  -0.0123 194 SER B O   
5706 C CB  . SER B 194 ? 0.2484 0.2055 0.2523 -0.0092 -0.0012 -0.0010 194 SER B CB  
5707 O OG  . SER B 194 ? 0.3075 0.2630 0.3147 -0.0067 -0.0013 0.0028  194 SER B OG  
5708 N N   . PRO B 195 ? 0.3934 0.3488 0.3906 -0.0193 -0.0004 -0.0103 195 PRO B N   
5709 C CA  . PRO B 195 ? 0.3741 0.3348 0.3680 -0.0235 -0.0001 -0.0151 195 PRO B CA  
5710 C C   . PRO B 195 ? 0.3959 0.3627 0.3886 -0.0210 -0.0003 -0.0155 195 PRO B C   
5711 O O   . PRO B 195 ? 0.3371 0.3096 0.3330 -0.0167 -0.0014 -0.0111 195 PRO B O   
5712 C CB  . PRO B 195 ? 0.4884 0.4608 0.4857 -0.0263 -0.0018 -0.0139 195 PRO B CB  
5713 C CG  . PRO B 195 ? 0.5266 0.4934 0.5271 -0.0254 -0.0018 -0.0106 195 PRO B CG  
5714 C CD  . PRO B 195 ? 0.4413 0.4006 0.4426 -0.0202 -0.0014 -0.0074 195 PRO B CD  
5715 N N   . TYR B 196 ? 0.4193 0.3846 0.4069 -0.0241 0.0011  -0.0210 196 TYR B N   
5716 C CA  . TYR B 196 ? 0.3680 0.3326 0.3526 -0.0215 0.0021  -0.0225 196 TYR B CA  
5717 C C   . TYR B 196 ? 0.3864 0.3638 0.3743 -0.0176 0.0002  -0.0183 196 TYR B C   
5718 O O   . TYR B 196 ? 0.3457 0.3209 0.3348 -0.0127 0.0004  -0.0153 196 TYR B O   
5719 C CB  . TYR B 196 ? 0.3788 0.3424 0.3572 -0.0267 0.0040  -0.0297 196 TYR B CB  
5720 C CG  . TYR B 196 ? 0.4047 0.3606 0.3786 -0.0241 0.0066  -0.0323 196 TYR B CG  
5721 C CD1 . TYR B 196 ? 0.3807 0.3452 0.3550 -0.0204 0.0057  -0.0308 196 TYR B CD1 
5722 C CD2 . TYR B 196 ? 0.4092 0.3490 0.3782 -0.0248 0.0103  -0.0359 196 TYR B CD2 
5723 C CE1 . TYR B 196 ? 0.3179 0.2758 0.2881 -0.0178 0.0082  -0.0331 196 TYR B CE1 
5724 C CE2 . TYR B 196 ? 0.4022 0.3347 0.3670 -0.0218 0.0132  -0.0379 196 TYR B CE2 
5725 C CZ  . TYR B 196 ? 0.4072 0.3490 0.3726 -0.0183 0.0120  -0.0366 196 TYR B CZ  
5726 O OH  . TYR B 196 ? 0.3910 0.3258 0.3522 -0.0150 0.0151  -0.0386 196 TYR B OH  
5727 N N   . TYR B 197 ? 0.3388 0.3304 0.3282 -0.0196 -0.0016 -0.0179 197 TYR B N   
5728 C CA  . TYR B 197 ? 0.3324 0.3357 0.3242 -0.0156 -0.0027 -0.0137 197 TYR B CA  
5729 C C   . TYR B 197 ? 0.2941 0.3022 0.2920 -0.0123 -0.0039 -0.0070 197 TYR B C   
5730 O O   . TYR B 197 ? 0.3044 0.3239 0.3046 -0.0096 -0.0045 -0.0030 197 TYR B O   
5731 C CB  . TYR B 197 ? 0.2995 0.3168 0.2887 -0.0186 -0.0035 -0.0168 197 TYR B CB  
5732 C CG  . TYR B 197 ? 0.2915 0.3035 0.2744 -0.0207 -0.0017 -0.0232 197 TYR B CG  
5733 C CD1 . TYR B 197 ? 0.2909 0.3001 0.2726 -0.0163 -0.0007 -0.0222 197 TYR B CD1 
5734 C CD2 . TYR B 197 ? 0.3244 0.3335 0.3026 -0.0273 -0.0005 -0.0303 197 TYR B CD2 
5735 C CE1 . TYR B 197 ? 0.3330 0.3365 0.3087 -0.0178 0.0014  -0.0281 197 TYR B CE1 
5736 C CE2 . TYR B 197 ? 0.3612 0.3637 0.3330 -0.0294 0.0019  -0.0366 197 TYR B CE2 
5737 C CZ  . TYR B 197 ? 0.3777 0.3774 0.3484 -0.0243 0.0030  -0.0353 197 TYR B CZ  
5738 O OH  . TYR B 197 ? 0.4893 0.4820 0.4536 -0.0259 0.0059  -0.0415 197 TYR B OH  
5739 N N   . HIS B 198 ? 0.2994 0.2982 0.2996 -0.0123 -0.0036 -0.0054 198 HIS B N   
5740 C CA  . HIS B 198 ? 0.2361 0.2372 0.2415 -0.0094 -0.0039 0.0005  198 HIS B CA  
5741 C C   . HIS B 198 ? 0.2645 0.2791 0.2723 -0.0102 -0.0048 0.0027  198 HIS B C   
5742 O O   . HIS B 198 ? 0.2414 0.2635 0.2523 -0.0063 -0.0046 0.0079  198 HIS B O   
5743 C CB  . HIS B 198 ? 0.2474 0.2482 0.2547 -0.0045 -0.0032 0.0045  198 HIS B CB  
5744 C CG  . HIS B 198 ? 0.2928 0.2898 0.3045 -0.0022 -0.0025 0.0092  198 HIS B CG  
5745 N ND1 . HIS B 198 ? 0.3113 0.3154 0.3265 0.0003  -0.0019 0.0143  198 HIS B ND1 
5746 C CD2 . HIS B 198 ? 0.3085 0.2954 0.3211 -0.0021 -0.0019 0.0096  198 HIS B CD2 
5747 C CE1 . HIS B 198 ? 0.3388 0.3362 0.3568 0.0013  -0.0007 0.0169  198 HIS B CE1 
5748 N NE2 . HIS B 198 ? 0.2960 0.2838 0.3126 -0.0002 -0.0010 0.0140  198 HIS B NE2 
5749 N N   . PRO B 199 ? 0.3077 0.3264 0.3141 -0.0149 -0.0056 -0.0008 199 PRO B N   
5750 C CA  . PRO B 199 ? 0.3438 0.3775 0.3530 -0.0153 -0.0065 0.0017  199 PRO B CA  
5751 C C   . PRO B 199 ? 0.2908 0.3217 0.3042 -0.0142 -0.0061 0.0056  199 PRO B C   
5752 O O   . PRO B 199 ? 0.3733 0.3912 0.3871 -0.0142 -0.0053 0.0054  199 PRO B O   
5753 C CB  . PRO B 199 ? 0.2406 0.2793 0.2460 -0.0219 -0.0073 -0.0047 199 PRO B CB  
5754 C CG  . PRO B 199 ? 0.2820 0.3038 0.2847 -0.0250 -0.0062 -0.0091 199 PRO B CG  
5755 C CD  . PRO B 199 ? 0.3464 0.3565 0.3488 -0.0202 -0.0052 -0.0072 199 PRO B CD  
5756 N N   . LEU B 200 ? 0.3857 0.4301 0.4021 -0.0132 -0.0065 0.0092  200 LEU B N   
5757 C CA  . LEU B 200 ? 0.3092 0.3527 0.3295 -0.0125 -0.0058 0.0124  200 LEU B CA  
5758 C C   . LEU B 200 ? 0.2927 0.3383 0.3117 -0.0187 -0.0068 0.0077  200 LEU B C   
5759 O O   . LEU B 200 ? 0.3426 0.4033 0.3622 -0.0208 -0.0078 0.0074  200 LEU B O   
5760 C CB  . LEU B 200 ? 0.3691 0.4256 0.3934 -0.0074 -0.0050 0.0193  200 LEU B CB  
5761 C CG  . LEU B 200 ? 0.3677 0.4207 0.3937 -0.0012 -0.0030 0.0248  200 LEU B CG  
5762 C CD1 . LEU B 200 ? 0.3215 0.3901 0.3501 0.0036  -0.0021 0.0311  200 LEU B CD1 
5763 C CD2 . LEU B 200 ? 0.3865 0.4249 0.4145 0.0003  -0.0010 0.0268  200 LEU B CD2 
5764 N N   . ILE B 201 ? 0.3413 0.3152 0.3307 -0.0064 -0.0285 0.0136  201 ILE B N   
5765 C CA  . ILE B 201 ? 0.3590 0.3357 0.3589 -0.0137 -0.0299 0.0133  201 ILE B CA  
5766 C C   . ILE B 201 ? 0.2952 0.2884 0.3081 -0.0149 -0.0313 0.0174  201 ILE B C   
5767 O O   . ILE B 201 ? 0.2973 0.2975 0.3168 -0.0209 -0.0361 0.0155  201 ILE B O   
5768 C CB  . ILE B 201 ? 0.3705 0.3365 0.3710 -0.0152 -0.0243 0.0142  201 ILE B CB  
5769 C CG1 . ILE B 201 ? 0.3740 0.3245 0.3622 -0.0146 -0.0236 0.0098  201 ILE B CG1 
5770 C CG2 . ILE B 201 ? 0.2700 0.2390 0.2815 -0.0228 -0.0250 0.0145  201 ILE B CG2 
5771 C CD1 . ILE B 201 ? 0.3261 0.2695 0.3129 -0.0217 -0.0274 0.0046  201 ILE B CD1 
5772 N N   . PRO B 202 ? 0.3047 0.3047 0.3215 -0.0096 -0.0274 0.0227  202 PRO B N   
5773 C CA  . PRO B 202 ? 0.2877 0.3038 0.3176 -0.0107 -0.0285 0.0267  202 PRO B CA  
5774 C C   . PRO B 202 ? 0.2936 0.3218 0.3255 -0.0114 -0.0356 0.0252  202 PRO B C   
5775 O O   . PRO B 202 ? 0.2740 0.3151 0.3173 -0.0156 -0.0385 0.0263  202 PRO B O   
5776 C CB  . PRO B 202 ? 0.2423 0.2610 0.2722 -0.0034 -0.0227 0.0322  202 PRO B CB  
5777 C CG  . PRO B 202 ? 0.2915 0.2951 0.3118 -0.0012 -0.0174 0.0314  202 PRO B CG  
5778 C CD  . PRO B 202 ? 0.3219 0.3157 0.3318 -0.0029 -0.0213 0.0255  202 PRO B CD  
5779 N N   . ILE B 203 ? 0.2582 0.2832 0.2791 -0.0075 -0.0384 0.0226  203 ILE B N   
5780 C CA  . ILE B 203 ? 0.2997 0.3362 0.3215 -0.0078 -0.0452 0.0213  203 ILE B CA  
5781 C C   . ILE B 203 ? 0.3215 0.3569 0.3443 -0.0165 -0.0509 0.0157  203 ILE B C   
5782 O O   . ILE B 203 ? 0.3816 0.4307 0.4123 -0.0206 -0.0562 0.0153  203 ILE B O   
5783 C CB  . ILE B 203 ? 0.3865 0.4192 0.3956 -0.0006 -0.0459 0.0206  203 ILE B CB  
5784 C CG1 . ILE B 203 ? 0.3926 0.4303 0.4024 0.0075  -0.0410 0.0266  203 ILE B CG1 
5785 C CG2 . ILE B 203 ? 0.3301 0.3714 0.3374 -0.0019 -0.0538 0.0177  203 ILE B CG2 
5786 C CD1 . ILE B 203 ? 0.4063 0.4415 0.4040 0.0146  -0.0416 0.0263  203 ILE B CD1 
5787 N N   . LEU B 204 ? 0.3747 0.3941 0.3896 -0.0197 -0.0497 0.0113  204 LEU B N   
5788 C CA  . LEU B 204 ? 0.3872 0.4032 0.4022 -0.0285 -0.0540 0.0060  204 LEU B CA  
5789 C C   . LEU B 204 ? 0.3921 0.4164 0.4210 -0.0357 -0.0539 0.0075  204 LEU B C   
5790 O O   . LEU B 204 ? 0.3211 0.3520 0.3543 -0.0431 -0.0591 0.0043  204 LEU B O   
5791 C CB  . LEU B 204 ? 0.3812 0.3774 0.3853 -0.0296 -0.0513 0.0019  204 LEU B CB  
5792 C CG  . LEU B 204 ? 0.3758 0.3618 0.3653 -0.0241 -0.0516 -0.0010 204 LEU B CG  
5793 C CD1 . LEU B 204 ? 0.3874 0.3558 0.3683 -0.0275 -0.0501 -0.0058 204 LEU B CD1 
5794 C CD2 . LEU B 204 ? 0.3338 0.3285 0.3196 -0.0235 -0.0583 -0.0031 204 LEU B CD2 
5795 N N   . LEU B 205 ? 0.3199 0.3443 0.3557 -0.0340 -0.0481 0.0121  205 LEU B N   
5796 C CA  . LEU B 205 ? 0.3394 0.3715 0.3884 -0.0409 -0.0475 0.0136  205 LEU B CA  
5797 C C   . LEU B 205 ? 0.3552 0.4088 0.4159 -0.0405 -0.0507 0.0172  205 LEU B C   
5798 O O   . LEU B 205 ? 0.3714 0.4352 0.4418 -0.0480 -0.0538 0.0162  205 LEU B O   
5799 C CB  . LEU B 205 ? 0.3046 0.3289 0.3566 -0.0394 -0.0399 0.0174  205 LEU B CB  
5800 C CG  . LEU B 205 ? 0.2799 0.2843 0.3232 -0.0411 -0.0363 0.0145  205 LEU B CG  
5801 C CD1 . LEU B 205 ? 0.2714 0.2709 0.3177 -0.0380 -0.0290 0.0191  205 LEU B CD1 
5802 C CD2 . LEU B 205 ? 0.3801 0.3795 0.4253 -0.0511 -0.0386 0.0100  205 LEU B CD2 
5803 N N   . ASN B 206 ? 0.3573 0.4183 0.4170 -0.0317 -0.0499 0.0213  206 ASN B N   
5804 C CA  . ASN B 206 ? 0.3642 0.4458 0.4352 -0.0298 -0.0520 0.0256  206 ASN B CA  
5805 C C   . ASN B 206 ? 0.3566 0.4419 0.4214 -0.0195 -0.0517 0.0287  206 ASN B C   
5806 O O   . ASN B 206 ? 0.3333 0.4157 0.3973 -0.0129 -0.0458 0.0332  206 ASN B O   
5807 C CB  . ASN B 206 ? 0.4266 0.5139 0.5100 -0.0308 -0.0467 0.0305  206 ASN B CB  
5808 C CG  . ASN B 206 ? 0.5107 0.6202 0.6069 -0.0291 -0.0488 0.0350  206 ASN B CG  
5809 O OD1 . ASN B 206 ? 0.4067 0.5288 0.5039 -0.0289 -0.0550 0.0341  206 ASN B OD1 
5810 N ND2 . ASN B 206 ? 0.4921 0.6068 0.5980 -0.0278 -0.0435 0.0401  206 ASN B ND2 
5811 N N   . PRO B 207 ? 0.3227 0.4142 0.3826 -0.0181 -0.0579 0.0265  207 PRO B N   
5812 C CA  . PRO B 207 ? 0.3309 0.4244 0.3835 -0.0082 -0.0573 0.0294  207 PRO B CA  
5813 C C   . PRO B 207 ? 0.3585 0.4657 0.4203 -0.0020 -0.0542 0.0364  207 PRO B C   
5814 O O   . PRO B 207 ? 0.3673 0.4724 0.4225 0.0068  -0.0510 0.0396  207 PRO B O   
5815 C CB  . PRO B 207 ? 0.3380 0.4385 0.3861 -0.0095 -0.0654 0.0257  207 PRO B CB  
5816 C CG  . PRO B 207 ? 0.3583 0.4527 0.4062 -0.0199 -0.0690 0.0194  207 PRO B CG  
5817 C CD  . PRO B 207 ? 0.3361 0.4322 0.3959 -0.0257 -0.0654 0.0211  207 PRO B CD  
5818 N N   . ASN B 208 ? 0.3182 0.4389 0.3948 -0.0064 -0.0544 0.0389  208 ASN B N   
5819 C CA  . ASN B 208 ? 0.3364 0.4703 0.4224 -0.0005 -0.0509 0.0457  208 ASN B CA  
5820 C C   . ASN B 208 ? 0.3381 0.4602 0.4211 0.0045  -0.0420 0.0494  208 ASN B C   
5821 O O   . ASN B 208 ? 0.3293 0.4585 0.4158 0.0114  -0.0381 0.0551  208 ASN B O   
5822 C CB  . ASN B 208 ? 0.3316 0.4826 0.4345 -0.0073 -0.0531 0.0470  208 ASN B CB  
5823 C CG  . ASN B 208 ? 0.3957 0.5649 0.5034 -0.0097 -0.0615 0.0456  208 ASN B CG  
5824 O OD1 . ASN B 208 ? 0.3521 0.5267 0.4540 -0.0028 -0.0644 0.0468  208 ASN B OD1 
5825 N ND2 . ASN B 208 ? 0.4328 0.6115 0.5508 -0.0196 -0.0654 0.0431  208 ASN B ND2 
5826 N N   . CYS B 209 ? 0.3103 0.4146 0.3863 0.0015  -0.0386 0.0464  209 CYS B N   
5827 C CA  . CYS B 209 ? 0.3160 0.4103 0.3891 0.0058  -0.0304 0.0498  209 CYS B CA  
5828 C C   . CYS B 209 ? 0.3396 0.4304 0.4025 0.0156  -0.0272 0.0526  209 CYS B C   
5829 O O   . CYS B 209 ? 0.3660 0.4528 0.4281 0.0201  -0.0202 0.0566  209 CYS B O   
5830 C CB  . CYS B 209 ? 0.3528 0.4293 0.4193 0.0012  -0.0278 0.0459  209 CYS B CB  
5831 S SG  . CYS B 209 ? 0.3702 0.4310 0.4188 0.0030  -0.0302 0.0402  209 CYS B SG  
5832 N N   . VAL B 210 ? 0.3310 0.4233 0.3857 0.0190  -0.0319 0.0505  210 VAL B N   
5833 C CA  . VAL B 210 ? 0.3392 0.4271 0.3831 0.0281  -0.0286 0.0530  210 VAL B CA  
5834 C C   . VAL B 210 ? 0.2908 0.3908 0.3421 0.0344  -0.0251 0.0598  210 VAL B C   
5835 O O   . VAL B 210 ? 0.2994 0.3932 0.3434 0.0414  -0.0189 0.0631  210 VAL B O   
5836 C CB  . VAL B 210 ? 0.4008 0.4880 0.4343 0.0303  -0.0346 0.0495  210 VAL B CB  
5837 C CG1 . VAL B 210 ? 0.4425 0.5153 0.4669 0.0250  -0.0369 0.0428  210 VAL B CG1 
5838 C CG2 . VAL B 210 ? 0.4103 0.5161 0.4529 0.0290  -0.0420 0.0500  210 VAL B CG2 
5839 N N   . TYR B 211 ? 0.2565 0.3739 0.3222 0.0320  -0.0285 0.0621  211 TYR B N   
5840 C CA  . TYR B 211 ? 0.3156 0.4459 0.3896 0.0381  -0.0251 0.0688  211 TYR B CA  
5841 C C   . TYR B 211 ? 0.3200 0.4446 0.3976 0.0389  -0.0165 0.0726  211 TYR B C   
5842 O O   . TYR B 211 ? 0.3301 0.4616 0.4115 0.0452  -0.0120 0.0783  211 TYR B O   
5843 C CB  . TYR B 211 ? 0.3112 0.4629 0.4005 0.0345  -0.0312 0.0699  211 TYR B CB  
5844 C CG  . TYR B 211 ? 0.3528 0.5119 0.4390 0.0334  -0.0400 0.0663  211 TYR B CG  
5845 C CD1 . TYR B 211 ? 0.3494 0.5080 0.4249 0.0416  -0.0413 0.0674  211 TYR B CD1 
5846 C CD2 . TYR B 211 ? 0.3611 0.5270 0.4542 0.0238  -0.0468 0.0617  211 TYR B CD2 
5847 C CE1 . TYR B 211 ? 0.3928 0.5581 0.4649 0.0406  -0.0495 0.0641  211 TYR B CE1 
5848 C CE2 . TYR B 211 ? 0.4002 0.5728 0.4898 0.0223  -0.0549 0.0582  211 TYR B CE2 
5849 C CZ  . TYR B 211 ? 0.4287 0.6012 0.5079 0.0308  -0.0564 0.0595  211 TYR B CZ  
5850 O OH  . TYR B 211 ? 0.4529 0.6322 0.5283 0.0293  -0.0645 0.0561  211 TYR B OH  
5851 N N   . GLU B 212 ? 0.3321 0.4443 0.4083 0.0330  -0.0138 0.0697  212 GLU B N   
5852 C CA  . GLU B 212 ? 0.3686 0.4757 0.4480 0.0335  -0.0057 0.0734  212 GLU B CA  
5853 C C   . GLU B 212 ? 0.3622 0.4587 0.4292 0.0415  0.0012  0.0760  212 GLU B C   
5854 O O   . GLU B 212 ? 0.4348 0.5313 0.5045 0.0446  0.0081  0.0806  212 GLU B O   
5855 C CB  . GLU B 212 ? 0.4198 0.5160 0.4998 0.0256  -0.0047 0.0698  212 GLU B CB  
5856 C CG  . GLU B 212 ? 0.4627 0.5682 0.5548 0.0171  -0.0104 0.0674  212 GLU B CG  
5857 C CD  . GLU B 212 ? 0.4812 0.5747 0.5729 0.0097  -0.0090 0.0640  212 GLU B CD  
5858 O OE1 . GLU B 212 ? 0.4713 0.5672 0.5678 0.0023  -0.0142 0.0602  212 GLU B OE1 
5859 O OE2 . GLU B 212 ? 0.4193 0.5010 0.5056 0.0112  -0.0026 0.0652  212 GLU B OE2 
5860 N N   . THR B 213 ? 0.3471 0.4344 0.4000 0.0447  -0.0003 0.0730  213 THR B N   
5861 C CA  . THR B 213 ? 0.3055 0.3827 0.3453 0.0519  0.0060  0.0750  213 THR B CA  
5862 C C   . THR B 213 ? 0.3597 0.4416 0.3929 0.0594  0.0037  0.0765  213 THR B C   
5863 O O   . THR B 213 ? 0.3838 0.4627 0.4107 0.0665  0.0098  0.0804  213 THR B O   
5864 C CB  . THR B 213 ? 0.3493 0.4090 0.3758 0.0497  0.0079  0.0703  213 THR B CB  
5865 O OG1 . THR B 213 ? 0.4125 0.4708 0.4354 0.0461  0.0003  0.0648  213 THR B OG1 
5866 C CG2 . THR B 213 ? 0.4005 0.4542 0.4316 0.0442  0.0121  0.0702  213 THR B CG2 
5867 N N   . THR B 214 ? 0.3799 0.4687 0.4137 0.0580  -0.0045 0.0734  214 THR B N   
5868 C CA  . THR B 214 ? 0.3513 0.4454 0.3789 0.0651  -0.0074 0.0748  214 THR B CA  
5869 C C   . THR B 214 ? 0.3317 0.4463 0.3730 0.0645  -0.0142 0.0766  214 THR B C   
5870 O O   . THR B 214 ? 0.3468 0.4669 0.3876 0.0619  -0.0221 0.0731  214 THR B O   
5871 C CB  . THR B 214 ? 0.4411 0.5242 0.4542 0.0648  -0.0111 0.0693  214 THR B CB  
5872 O OG1 . THR B 214 ? 0.3932 0.4780 0.4108 0.0565  -0.0182 0.0639  214 THR B OG1 
5873 C CG2 . THR B 214 ? 0.4315 0.4958 0.4308 0.0658  -0.0041 0.0678  214 THR B CG2 
5874 N N   . PRO B 215 ? 0.3703 0.4971 0.4236 0.0669  -0.0112 0.0822  215 PRO B N   
5875 C CA  . PRO B 215 ? 0.4053 0.5536 0.4736 0.0651  -0.0177 0.0839  215 PRO B CA  
5876 C C   . PRO B 215 ? 0.4571 0.6158 0.5218 0.0712  -0.0235 0.0849  215 PRO B C   
5877 O O   . PRO B 215 ? 0.4598 0.6361 0.5352 0.0683  -0.0306 0.0846  215 PRO B O   
5878 C CB  . PRO B 215 ? 0.4174 0.5744 0.4971 0.0682  -0.0115 0.0903  215 PRO B CB  
5879 C CG  . PRO B 215 ? 0.3885 0.5302 0.4559 0.0753  -0.0022 0.0932  215 PRO B CG  
5880 C CD  . PRO B 215 ? 0.3467 0.4688 0.4000 0.0716  -0.0017 0.0874  215 PRO B CD  
5881 N N   . ASN B 216 ? 0.4236 0.5725 0.4735 0.0793  -0.0206 0.0860  216 ASN B N   
5882 C CA  . ASN B 216 ? 0.4476 0.6055 0.4930 0.0860  -0.0255 0.0874  216 ASN B CA  
5883 C C   . ASN B 216 ? 0.4356 0.5839 0.4681 0.0834  -0.0312 0.0812  216 ASN B C   
5884 O O   . ASN B 216 ? 0.4237 0.5749 0.4482 0.0896  -0.0343 0.0820  216 ASN B O   
5885 C CB  . ASN B 216 ? 0.5375 0.6916 0.5746 0.0977  -0.0182 0.0936  216 ASN B CB  
5886 C CG  . ASN B 216 ? 0.5929 0.7583 0.6428 0.1013  -0.0129 0.1003  216 ASN B CG  
5887 O OD1 . ASN B 216 ? 0.6014 0.7861 0.6672 0.0988  -0.0174 0.1020  216 ASN B OD1 
5888 N ND2 . ASN B 216 ? 0.6228 0.7760 0.6655 0.1069  -0.0031 0.1039  216 ASN B ND2 
5889 N N   . VAL B 217 ? 0.4195 0.5566 0.4496 0.0748  -0.0325 0.0751  217 VAL B N   
5890 C CA  . VAL B 217 ? 0.4319 0.5587 0.4493 0.0723  -0.0372 0.0690  217 VAL B CA  
5891 C C   . VAL B 217 ? 0.4038 0.5456 0.4282 0.0675  -0.0474 0.0661  217 VAL B C   
5892 O O   . VAL B 217 ? 0.3736 0.5300 0.4130 0.0620  -0.0509 0.0666  217 VAL B O   
5893 C CB  . VAL B 217 ? 0.4491 0.5580 0.4610 0.0655  -0.0342 0.0639  217 VAL B CB  
5894 C CG1 . VAL B 217 ? 0.4256 0.5402 0.4502 0.0553  -0.0383 0.0606  217 VAL B CG1 
5895 C CG2 . VAL B 217 ? 0.4974 0.5923 0.4929 0.0658  -0.0363 0.0587  217 VAL B CG2 
5896 N N   . LYS B 218 ? 0.4031 0.5417 0.4159 0.0696  -0.0522 0.0632  218 LYS B N   
5897 C CA  . LYS B 218 ? 0.4072 0.5575 0.4237 0.0643  -0.0621 0.0594  218 LYS B CA  
5898 C C   . LYS B 218 ? 0.4289 0.5646 0.4379 0.0559  -0.0647 0.0516  218 LYS B C   
5899 O O   . LYS B 218 ? 0.4628 0.5808 0.4572 0.0582  -0.0614 0.0491  218 LYS B O   
5900 C CB  . LYS B 218 ? 0.4919 0.6494 0.5005 0.0722  -0.0661 0.0614  218 LYS B CB  
5901 C CG  . LYS B 218 ? 0.5769 0.7447 0.5888 0.0830  -0.0619 0.0696  218 LYS B CG  
5902 C CD  . LYS B 218 ? 0.6406 0.8295 0.6575 0.0866  -0.0695 0.0722  218 LYS B CD  
5903 C CE  . LYS B 218 ? 0.7174 0.9084 0.7273 0.1000  -0.0654 0.0790  218 LYS B CE  
5904 N NZ  . LYS B 218 ? 0.7908 0.9666 0.7811 0.1050  -0.0654 0.0768  218 LYS B NZ  
5905 N N   . ILE B 219 ? 0.4522 0.5950 0.4708 0.0462  -0.0701 0.0478  219 ILE B N   
5906 C CA  . ILE B 219 ? 0.5103 0.6400 0.5227 0.0378  -0.0728 0.0404  219 ILE B CA  
5907 C C   . ILE B 219 ? 0.5422 0.6846 0.5585 0.0314  -0.0823 0.0366  219 ILE B C   
5908 O O   . ILE B 219 ? 0.5476 0.7103 0.5750 0.0316  -0.0864 0.0397  219 ILE B O   
5909 C CB  . ILE B 219 ? 0.4396 0.5607 0.4586 0.0310  -0.0682 0.0389  219 ILE B CB  
5910 C CG1 . ILE B 219 ? 0.4679 0.6062 0.5050 0.0256  -0.0700 0.0412  219 ILE B CG1 
5911 C CG2 . ILE B 219 ? 0.3897 0.4974 0.4032 0.0368  -0.0588 0.0422  219 ILE B CG2 
5912 C CD1 . ILE B 219 ? 0.5171 0.6471 0.5605 0.0180  -0.0662 0.0394  219 ILE B CD1 
5913 N N   . PRO B 220 ? 0.5329 0.6642 0.5401 0.0256  -0.0860 0.0298  220 PRO B N   
5914 C CA  . PRO B 220 ? 0.5556 0.6979 0.5652 0.0188  -0.0950 0.0256  220 PRO B CA  
5915 C C   . PRO B 220 ? 0.5668 0.7213 0.5923 0.0093  -0.0974 0.0249  220 PRO B C   
5916 O O   . PRO B 220 ? 0.5201 0.6730 0.5544 0.0074  -0.0921 0.0271  220 PRO B O   
5917 C CB  . PRO B 220 ? 0.5443 0.6677 0.5397 0.0146  -0.0964 0.0184  220 PRO B CB  
5918 C CG  . PRO B 220 ? 0.5480 0.6527 0.5382 0.0164  -0.0883 0.0184  220 PRO B CG  
5919 C CD  . PRO B 220 ? 0.5405 0.6491 0.5334 0.0257  -0.0822 0.0256  220 PRO B CD  
5920 N N   . ASP B 221 ? 0.5850 0.7522 0.6138 0.0028  -0.1055 0.0216  221 ASP B N   
5921 C CA  . ASP B 221 ? 0.5953 0.7746 0.6381 -0.0075 -0.1085 0.0199  221 ASP B CA  
5922 C C   . ASP B 221 ? 0.4887 0.6499 0.5269 -0.0173 -0.1075 0.0131  221 ASP B C   
5923 O O   . ASP B 221 ? 0.4702 0.6228 0.4979 -0.0215 -0.1116 0.0072  221 ASP B O   
5924 C CB  . ASP B 221 ? 0.6684 0.8694 0.7161 -0.0108 -0.1175 0.0191  221 ASP B CB  
5925 C CG  . ASP B 221 ? 0.7834 0.9920 0.8407 -0.0244 -0.1217 0.0144  221 ASP B CG  
5926 O OD1 . ASP B 221 ? 0.7627 0.9742 0.8318 -0.0285 -0.1178 0.0162  221 ASP B OD1 
5927 O OD2 . ASP B 221 ? 0.8750 1.0862 0.9274 -0.0312 -0.1285 0.0089  221 ASP B OD2 
5928 N N   . PHE B 222 ? 0.4432 0.5981 0.4887 -0.0208 -0.1018 0.0141  222 PHE B N   
5929 C CA  . PHE B 222 ? 0.4185 0.5552 0.4596 -0.0292 -0.0998 0.0083  222 PHE B CA  
5930 C C   . PHE B 222 ? 0.5019 0.6483 0.5507 -0.0414 -0.1054 0.0040  222 PHE B C   
5931 O O   . PHE B 222 ? 0.4937 0.6460 0.5544 -0.0474 -0.1036 0.0050  222 PHE B O   
5932 C CB  . PHE B 222 ? 0.3863 0.5122 0.4313 -0.0276 -0.0914 0.0114  222 PHE B CB  
5933 C CG  . PHE B 222 ? 0.3929 0.4997 0.4250 -0.0201 -0.0858 0.0117  222 PHE B CG  
5934 C CD1 . PHE B 222 ? 0.3253 0.4344 0.3543 -0.0093 -0.0826 0.0169  222 PHE B CD1 
5935 C CD2 . PHE B 222 ? 0.3851 0.4717 0.4077 -0.0238 -0.0835 0.0067  222 PHE B CD2 
5936 C CE1 . PHE B 222 ? 0.4138 0.5057 0.4306 -0.0031 -0.0773 0.0169  222 PHE B CE1 
5937 C CE2 . PHE B 222 ? 0.4297 0.5002 0.4408 -0.0171 -0.0785 0.0069  222 PHE B CE2 
5938 C CZ  . PHE B 222 ? 0.4106 0.4839 0.4188 -0.0071 -0.0754 0.0119  222 PHE B CZ  
5939 N N   . ALA B 223 ? 0.4890 0.6364 0.5301 -0.0454 -0.1121 -0.0011 223 ALA B N   
5940 C CA  . ALA B 223 ? 0.4889 0.6482 0.5361 -0.0568 -0.1185 -0.0054 223 ALA B CA  
5941 C C   . ALA B 223 ? 0.4529 0.5957 0.4973 -0.0679 -0.1167 -0.0116 223 ALA B C   
5942 O O   . ALA B 223 ? 0.4271 0.5772 0.4750 -0.0787 -0.1215 -0.0160 223 ALA B O   
5943 C CB  . ALA B 223 ? 0.4917 0.6588 0.5308 -0.0566 -0.1264 -0.0084 223 ALA B CB  
5944 N N   . VAL B 224 ? 0.4724 0.5932 0.5101 -0.0657 -0.1099 -0.0122 224 VAL B N   
5945 C CA  . VAL B 224 ? 0.4735 0.5779 0.5091 -0.0751 -0.1070 -0.0171 224 VAL B CA  
5946 C C   . VAL B 224 ? 0.4208 0.5127 0.4588 -0.0708 -0.0985 -0.0133 224 VAL B C   
5947 O O   . VAL B 224 ? 0.3800 0.4740 0.4193 -0.0608 -0.0948 -0.0077 224 VAL B O   
5948 C CB  . VAL B 224 ? 0.5187 0.6045 0.5383 -0.0783 -0.1088 -0.0241 224 VAL B CB  
5949 C CG1 . VAL B 224 ? 0.5412 0.6387 0.5584 -0.0844 -0.1172 -0.0284 224 VAL B CG1 
5950 C CG2 . VAL B 224 ? 0.5558 0.6280 0.5633 -0.0674 -0.1056 -0.0228 224 VAL B CG2 
5951 N N   . SER B 225 ? 0.4204 0.4986 0.4581 -0.0784 -0.0950 -0.0165 225 SER B N   
5952 C CA  . SER B 225 ? 0.4536 0.5209 0.4945 -0.0760 -0.0872 -0.0132 225 SER B CA  
5953 C C   . SER B 225 ? 0.4516 0.4950 0.4784 -0.0720 -0.0829 -0.0156 225 SER B C   
5954 O O   . SER B 225 ? 0.3457 0.3758 0.3628 -0.0774 -0.0844 -0.0216 225 SER B O   
5955 C CB  . SER B 225 ? 0.4996 0.5672 0.5497 -0.0866 -0.0855 -0.0144 225 SER B CB  
5956 O OG  . SER B 225 ? 0.5237 0.5790 0.5754 -0.0840 -0.0779 -0.0114 225 SER B OG  
5957 N N   . PHE B 226 ? 0.4074 0.4454 0.4329 -0.0628 -0.0773 -0.0110 226 PHE B N   
5958 C CA  . PHE B 226 ? 0.3872 0.4041 0.4008 -0.0587 -0.0724 -0.0125 226 PHE B CA  
5959 C C   . PHE B 226 ? 0.3974 0.4041 0.4151 -0.0601 -0.0655 -0.0104 226 PHE B C   
5960 O O   . PHE B 226 ? 0.3695 0.3611 0.3792 -0.0553 -0.0606 -0.0102 226 PHE B O   
5961 C CB  . PHE B 226 ? 0.3836 0.4004 0.3908 -0.0475 -0.0708 -0.0093 226 PHE B CB  
5962 C CG  . PHE B 226 ? 0.4191 0.4392 0.4176 -0.0453 -0.0766 -0.0122 226 PHE B CG  
5963 C CD1 . PHE B 226 ? 0.4986 0.5033 0.4834 -0.0460 -0.0775 -0.0177 226 PHE B CD1 
5964 C CD2 . PHE B 226 ? 0.4564 0.4950 0.4601 -0.0423 -0.0811 -0.0094 226 PHE B CD2 
5965 C CE1 . PHE B 226 ? 0.5411 0.5484 0.5174 -0.0441 -0.0828 -0.0205 226 PHE B CE1 
5966 C CE2 . PHE B 226 ? 0.5436 0.5851 0.5387 -0.0401 -0.0865 -0.0119 226 PHE B CE2 
5967 C CZ  . PHE B 226 ? 0.5711 0.5967 0.5523 -0.0412 -0.0874 -0.0176 226 PHE B CZ  
5968 N N   . ARG B 227 ? 0.4411 0.4561 0.4710 -0.0667 -0.0650 -0.0089 227 ARG B N   
5969 C CA  . ARG B 227 ? 0.4417 0.4485 0.4763 -0.0675 -0.0582 -0.0061 227 ARG B CA  
5970 C C   . ARG B 227 ? 0.3823 0.3674 0.4072 -0.0712 -0.0552 -0.0105 227 ARG B C   
5971 O O   . ARG B 227 ? 0.4426 0.4155 0.4643 -0.0671 -0.0491 -0.0083 227 ARG B O   
5972 C CB  . ARG B 227 ? 0.4166 0.4372 0.4660 -0.0745 -0.0586 -0.0040 227 ARG B CB  
5973 C CG  . ARG B 227 ? 0.4918 0.5349 0.5521 -0.0704 -0.0610 0.0010  227 ARG B CG  
5974 C CD  . ARG B 227 ? 0.5263 0.5829 0.6016 -0.0774 -0.0608 0.0032  227 ARG B CD  
5975 N NE  . ARG B 227 ? 0.5004 0.5460 0.5788 -0.0791 -0.0538 0.0052  227 ARG B NE  
5976 C CZ  . ARG B 227 ? 0.5390 0.5858 0.6220 -0.0725 -0.0483 0.0110  227 ARG B CZ  
5977 N NH1 . ARG B 227 ? 0.4386 0.4964 0.5236 -0.0639 -0.0486 0.0154  227 ARG B NH1 
5978 N NH2 . ARG B 227 ? 0.5983 0.6347 0.6834 -0.0747 -0.0424 0.0126  227 ARG B NH2 
5979 N N   . GLU B 228 ? 0.3416 0.3214 0.3611 -0.0789 -0.0591 -0.0165 228 GLU B N   
5980 C CA  . GLU B 228 ? 0.4154 0.3736 0.4252 -0.0820 -0.0556 -0.0205 228 GLU B CA  
5981 C C   . GLU B 228 ? 0.4542 0.3991 0.4502 -0.0742 -0.0544 -0.0221 228 GLU B C   
5982 O O   . GLU B 228 ? 0.4156 0.3429 0.4040 -0.0728 -0.0496 -0.0231 228 GLU B O   
5983 C CB  . GLU B 228 ? 0.5599 0.5152 0.5679 -0.0935 -0.0594 -0.0266 228 GLU B CB  
5984 C CG  . GLU B 228 ? 0.7219 0.6781 0.7395 -0.1020 -0.0566 -0.0258 228 GLU B CG  
5985 C CD  . GLU B 228 ? 0.8604 0.8143 0.8764 -0.1144 -0.0600 -0.0320 228 GLU B CD  
5986 O OE1 . GLU B 228 ? 0.8878 0.8455 0.8981 -0.1167 -0.0658 -0.0363 228 GLU B OE1 
5987 O OE2 . GLU B 228 ? 0.9239 0.8721 0.9438 -0.1220 -0.0566 -0.0326 228 GLU B OE2 
5988 N N   . ASP B 229 ? 0.3497 0.3031 0.3423 -0.0685 -0.0583 -0.0219 229 ASP B N   
5989 C CA  . ASP B 229 ? 0.4000 0.3425 0.3804 -0.0604 -0.0566 -0.0226 229 ASP B CA  
5990 C C   . ASP B 229 ? 0.4002 0.3390 0.3819 -0.0526 -0.0499 -0.0173 229 ASP B C   
5991 O O   . ASP B 229 ? 0.3984 0.3226 0.3708 -0.0485 -0.0460 -0.0183 229 ASP B O   
5992 C CB  . ASP B 229 ? 0.4000 0.3531 0.3767 -0.0563 -0.0620 -0.0233 229 ASP B CB  
5993 C CG  . ASP B 229 ? 0.4151 0.3659 0.3848 -0.0626 -0.0680 -0.0298 229 ASP B CG  
5994 O OD1 . ASP B 229 ? 0.3980 0.3389 0.3659 -0.0705 -0.0676 -0.0338 229 ASP B OD1 
5995 O OD2 . ASP B 229 ? 0.3539 0.3121 0.3194 -0.0598 -0.0728 -0.0308 229 ASP B OD2 
5996 N N   . ALA B 230 ? 0.3988 0.3510 0.3918 -0.0505 -0.0485 -0.0118 230 ALA B N   
5997 C CA  . ALA B 230 ? 0.3906 0.3397 0.3855 -0.0444 -0.0420 -0.0067 230 ALA B CA  
5998 C C   . ALA B 230 ? 0.3819 0.3160 0.3753 -0.0474 -0.0369 -0.0073 230 ALA B C   
5999 O O   . ALA B 230 ? 0.4044 0.3281 0.3915 -0.0419 -0.0321 -0.0060 230 ALA B O   
6000 C CB  . ALA B 230 ? 0.3521 0.3178 0.3600 -0.0431 -0.0413 -0.0010 230 ALA B CB  
6001 N N   . SER B 231 ? 0.3874 0.3205 0.3863 -0.0560 -0.0378 -0.0091 231 SER B N   
6002 C CA  . SER B 231 ? 0.4481 0.3649 0.4439 -0.0591 -0.0330 -0.0101 231 SER B CA  
6003 C C   . SER B 231 ? 0.4196 0.3193 0.4009 -0.0567 -0.0322 -0.0144 231 SER B C   
6004 O O   . SER B 231 ? 0.3997 0.2866 0.3760 -0.0530 -0.0268 -0.0132 231 SER B O   
6005 C CB  . SER B 231 ? 0.5064 0.4239 0.5086 -0.0697 -0.0344 -0.0123 231 SER B CB  
6006 O OG  . SER B 231 ? 0.6234 0.5538 0.6391 -0.0716 -0.0331 -0.0076 231 SER B OG  
6007 N N   . LYS B 232 ? 0.4547 0.3543 0.4293 -0.0586 -0.0374 -0.0193 232 LYS B N   
6008 C CA  . LYS B 232 ? 0.5027 0.3861 0.4635 -0.0567 -0.0368 -0.0239 232 LYS B CA  
6009 C C   . LYS B 232 ? 0.4905 0.3704 0.4446 -0.0465 -0.0336 -0.0215 232 LYS B C   
6010 O O   . LYS B 232 ? 0.4929 0.3582 0.4383 -0.0435 -0.0297 -0.0228 232 LYS B O   
6011 C CB  . LYS B 232 ? 0.5237 0.4094 0.4790 -0.0609 -0.0434 -0.0295 232 LYS B CB  
6012 C CG  . LYS B 232 ? 0.6396 0.5175 0.5931 -0.0713 -0.0452 -0.0346 232 LYS B CG  
6013 C CD  . LYS B 232 ? 0.6966 0.5825 0.6477 -0.0761 -0.0526 -0.0393 232 LYS B CD  
6014 C CE  . LYS B 232 ? 0.7895 0.6687 0.7389 -0.0876 -0.0543 -0.0447 232 LYS B CE  
6015 N NZ  . LYS B 232 ? 0.8259 0.7139 0.7881 -0.0947 -0.0537 -0.0423 232 LYS B NZ  
6016 N N   . HIS B 233 ? 0.4564 0.3497 0.4142 -0.0411 -0.0348 -0.0182 233 HIS B N   
6017 C CA  . HIS B 233 ? 0.4232 0.3141 0.3750 -0.0321 -0.0313 -0.0159 233 HIS B CA  
6018 C C   . HIS B 233 ? 0.4201 0.3036 0.3734 -0.0294 -0.0246 -0.0122 233 HIS B C   
6019 O O   . HIS B 233 ? 0.3622 0.2355 0.3069 -0.0245 -0.0211 -0.0127 233 HIS B O   
6020 C CB  . HIS B 233 ? 0.4315 0.3377 0.3877 -0.0275 -0.0330 -0.0123 233 HIS B CB  
6021 C CG  . HIS B 233 ? 0.4295 0.3410 0.3804 -0.0269 -0.0388 -0.0156 233 HIS B CG  
6022 N ND1 . HIS B 233 ? 0.4104 0.3153 0.3493 -0.0219 -0.0389 -0.0181 233 HIS B ND1 
6023 C CD2 . HIS B 233 ? 0.4372 0.3605 0.3929 -0.0306 -0.0446 -0.0165 233 HIS B CD2 
6024 C CE1 . HIS B 233 ? 0.4159 0.3273 0.3521 -0.0225 -0.0444 -0.0205 233 HIS B CE1 
6025 N NE2 . HIS B 233 ? 0.3710 0.2939 0.3172 -0.0276 -0.0481 -0.0195 233 HIS B NE2 
6026 N N   . VAL B 234 ? 0.3931 0.2821 0.3572 -0.0326 -0.0226 -0.0085 234 VAL B N   
6027 C CA  . VAL B 234 ? 0.3709 0.2538 0.3369 -0.0302 -0.0163 -0.0046 234 VAL B CA  
6028 C C   . VAL B 234 ? 0.3591 0.2248 0.3184 -0.0327 -0.0138 -0.0075 234 VAL B C   
6029 O O   . VAL B 234 ? 0.3757 0.2323 0.3294 -0.0277 -0.0091 -0.0061 234 VAL B O   
6030 C CB  . VAL B 234 ? 0.3733 0.2665 0.3526 -0.0335 -0.0150 0.0000  234 VAL B CB  
6031 C CG1 . VAL B 234 ? 0.3824 0.2688 0.3634 -0.0315 -0.0085 0.0040  234 VAL B CG1 
6032 C CG2 . VAL B 234 ? 0.3887 0.2982 0.3739 -0.0299 -0.0168 0.0033  234 VAL B CG2 
6033 N N   . GLU B 235 ? 0.3893 0.2504 0.3487 -0.0404 -0.0166 -0.0115 235 GLU B N   
6034 C CA  . GLU B 235 ? 0.4105 0.2541 0.3634 -0.0432 -0.0136 -0.0141 235 GLU B CA  
6035 C C   . GLU B 235 ? 0.4880 0.3194 0.4274 -0.0381 -0.0129 -0.0175 235 GLU B C   
6036 O O   . GLU B 235 ? 0.3816 0.2000 0.3150 -0.0347 -0.0079 -0.0169 235 GLU B O   
6037 C CB  . GLU B 235 ? 0.5682 0.4098 0.5237 -0.0535 -0.0168 -0.0181 235 GLU B CB  
6038 C CG  . GLU B 235 ? 0.7499 0.5743 0.7017 -0.0577 -0.0123 -0.0193 235 GLU B CG  
6039 C CD  . GLU B 235 ? 0.8491 0.6710 0.8055 -0.0541 -0.0061 -0.0135 235 GLU B CD  
6040 O OE1 . GLU B 235 ? 0.8501 0.6831 0.8178 -0.0569 -0.0058 -0.0098 235 GLU B OE1 
6041 O OE2 . GLU B 235 ? 0.8952 0.7045 0.8438 -0.0484 -0.0014 -0.0126 235 GLU B OE2 
6042 N N   . LEU B 236 ? 0.4161 0.2517 0.3506 -0.0374 -0.0177 -0.0211 236 LEU B N   
6043 C CA  . LEU B 236 ? 0.4229 0.2473 0.3445 -0.0329 -0.0172 -0.0247 236 LEU B CA  
6044 C C   . LEU B 236 ? 0.4393 0.2642 0.3579 -0.0236 -0.0129 -0.0211 236 LEU B C   
6045 O O   . LEU B 236 ? 0.4226 0.2359 0.3319 -0.0193 -0.0098 -0.0225 236 LEU B O   
6046 C CB  . LEU B 236 ? 0.4366 0.2663 0.3538 -0.0345 -0.0234 -0.0292 236 LEU B CB  
6047 C CG  . LEU B 236 ? 0.4986 0.3268 0.4160 -0.0439 -0.0281 -0.0341 236 LEU B CG  
6048 C CD1 . LEU B 236 ? 0.4897 0.3256 0.4032 -0.0442 -0.0344 -0.0376 236 LEU B CD1 
6049 C CD2 . LEU B 236 ? 0.5163 0.3252 0.4250 -0.0473 -0.0254 -0.0381 236 LEU B CD2 
6050 N N   . ALA B 237 ? 0.3898 0.2283 0.3159 -0.0205 -0.0125 -0.0165 237 ALA B N   
6051 C CA  . ALA B 237 ? 0.3687 0.2088 0.2925 -0.0126 -0.0082 -0.0128 237 ALA B CA  
6052 C C   . ALA B 237 ? 0.4554 0.2864 0.3796 -0.0110 -0.0023 -0.0099 237 ALA B C   
6053 O O   . ALA B 237 ? 0.4002 0.2255 0.3175 -0.0049 0.0013  -0.0092 237 ALA B O   
6054 C CB  . ALA B 237 ? 0.3265 0.1822 0.2583 -0.0106 -0.0086 -0.0085 237 ALA B CB  
6055 N N   . LYS B 238 ? 0.3989 0.2288 0.3308 -0.0163 -0.0012 -0.0080 238 LYS B N   
6056 C CA  . LYS B 238 ? 0.4633 0.2833 0.3948 -0.0149 0.0044  -0.0053 238 LYS B CA  
6057 C C   . LYS B 238 ? 0.5217 0.3249 0.4419 -0.0136 0.0061  -0.0090 238 LYS B C   
6058 O O   . LYS B 238 ? 0.5002 0.2962 0.4156 -0.0079 0.0108  -0.0069 238 LYS B O   
6059 C CB  . LYS B 238 ? 0.4736 0.2942 0.4145 -0.0219 0.0050  -0.0034 238 LYS B CB  
6060 C CG  . LYS B 238 ? 0.4423 0.2788 0.3947 -0.0226 0.0045  0.0011  238 LYS B CG  
6061 C CD  . LYS B 238 ? 0.4834 0.3207 0.4449 -0.0305 0.0043  0.0019  238 LYS B CD  
6062 C CE  . LYS B 238 ? 0.4688 0.2918 0.4281 -0.0314 0.0097  0.0034  238 LYS B CE  
6063 N NZ  . LYS B 238 ? 0.5323 0.3558 0.5003 -0.0396 0.0100  0.0041  238 LYS B NZ  
6064 N N   . GLU B 239 ? 0.5032 0.3004 0.4188 -0.0185 0.0023  -0.0146 239 GLU B N   
6065 C CA  . GLU B 239 ? 0.5267 0.3069 0.4309 -0.0176 0.0041  -0.0185 239 GLU B CA  
6066 C C   . GLU B 239 ? 0.4836 0.2630 0.3789 -0.0094 0.0049  -0.0194 239 GLU B C   
6067 O O   . GLU B 239 ? 0.5140 0.2821 0.4018 -0.0045 0.0091  -0.0193 239 GLU B O   
6068 C CB  . GLU B 239 ? 0.5553 0.3300 0.4566 -0.0257 -0.0003 -0.0244 239 GLU B CB  
6069 C CG  . GLU B 239 ? 0.6643 0.4375 0.5730 -0.0345 -0.0003 -0.0241 239 GLU B CG  
6070 C CD  . GLU B 239 ? 0.8443 0.6206 0.7540 -0.0434 -0.0063 -0.0293 239 GLU B CD  
6071 O OE1 . GLU B 239 ? 0.9129 0.6887 0.8154 -0.0428 -0.0099 -0.0336 239 GLU B OE1 
6072 O OE2 . GLU B 239 ? 0.9025 0.6823 0.8200 -0.0512 -0.0073 -0.0290 239 GLU B OE2 
6073 N N   . LYS B 240 ? 0.4645 0.2559 0.3604 -0.0077 0.0010  -0.0203 240 LYS B N   
6074 C CA  . LYS B 240 ? 0.4925 0.2838 0.3800 -0.0005 0.0018  -0.0214 240 LYS B CA  
6075 C C   . LYS B 240 ? 0.4391 0.2329 0.3274 0.0066  0.0072  -0.0163 240 LYS B C   
6076 O O   . LYS B 240 ? 0.4311 0.2176 0.3115 0.0123  0.0105  -0.0167 240 LYS B O   
6077 C CB  . LYS B 240 ? 0.4949 0.2983 0.3828 -0.0005 -0.0030 -0.0230 240 LYS B CB  
6078 C CG  . LYS B 240 ? 0.4922 0.2949 0.3704 0.0058  -0.0027 -0.0251 240 LYS B CG  
6079 C CD  . LYS B 240 ? 0.4535 0.2421 0.3210 0.0052  -0.0033 -0.0307 240 LYS B CD  
6080 C CE  . LYS B 240 ? 0.5374 0.3243 0.3954 0.0124  -0.0014 -0.0321 240 LYS B CE  
6081 N NZ  . LYS B 240 ? 0.5649 0.3385 0.4120 0.0120  -0.0021 -0.0378 240 LYS B NZ  
6082 N N   . TYR B 241 ? 0.4408 0.2452 0.3386 0.0063  0.0083  -0.0113 241 TYR B N   
6083 C CA  . TYR B 241 ? 0.4901 0.2973 0.3891 0.0122  0.0134  -0.0063 241 TYR B CA  
6084 C C   . TYR B 241 ? 0.4827 0.2763 0.3780 0.0141  0.0180  -0.0052 241 TYR B C   
6085 O O   . TYR B 241 ? 0.5164 0.3080 0.4068 0.0208  0.0219  -0.0033 241 TYR B O   
6086 C CB  . TYR B 241 ? 0.4789 0.2981 0.3889 0.0103  0.0138  -0.0014 241 TYR B CB  
6087 C CG  . TYR B 241 ? 0.4591 0.2828 0.3707 0.0156  0.0188  0.0039  241 TYR B CG  
6088 C CD1 . TYR B 241 ? 0.4399 0.2570 0.3536 0.0161  0.0230  0.0073  241 TYR B CD1 
6089 C CD2 . TYR B 241 ? 0.4351 0.2700 0.3462 0.0197  0.0194  0.0056  241 TYR B CD2 
6090 C CE1 . TYR B 241 ? 0.4483 0.2703 0.3635 0.0208  0.0273  0.0123  241 TYR B CE1 
6091 C CE2 . TYR B 241 ? 0.3993 0.2390 0.3118 0.0239  0.0239  0.0103  241 TYR B CE2 
6092 C CZ  . TYR B 241 ? 0.4092 0.2430 0.3240 0.0245  0.0277  0.0137  241 TYR B CZ  
6093 O OH  . TYR B 241 ? 0.4291 0.2682 0.3451 0.0286  0.0320  0.0185  241 TYR B OH  
6094 N N   . PHE B 242 ? 0.4746 0.2587 0.3717 0.0082  0.0178  -0.0064 242 PHE B N   
6095 C CA  . PHE B 242 ? 0.4848 0.2541 0.3775 0.0099  0.0226  -0.0054 242 PHE B CA  
6096 C C   . PHE B 242 ? 0.4779 0.2356 0.3586 0.0146  0.0238  -0.0090 242 PHE B C   
6097 O O   . PHE B 242 ? 0.4513 0.2005 0.3270 0.0202  0.0287  -0.0069 242 PHE B O   
6098 C CB  . PHE B 242 ? 0.4496 0.2102 0.3458 0.0017  0.0222  -0.0065 242 PHE B CB  
6099 C CG  . PHE B 242 ? 0.5404 0.2843 0.4316 0.0033  0.0277  -0.0051 242 PHE B CG  
6100 C CD1 . PHE B 242 ? 0.5365 0.2812 0.4321 0.0061  0.0323  0.0008  242 PHE B CD1 
6101 C CD2 . PHE B 242 ? 0.5685 0.2956 0.4498 0.0022  0.0287  -0.0096 242 PHE B CD2 
6102 C CE1 . PHE B 242 ? 0.5584 0.2875 0.4487 0.0082  0.0377  0.0024  242 PHE B CE1 
6103 C CE2 . PHE B 242 ? 0.6274 0.3382 0.5032 0.0042  0.0343  -0.0081 242 PHE B CE2 
6104 C CZ  . PHE B 242 ? 0.6341 0.3460 0.5144 0.0074  0.0388  -0.0019 242 PHE B CZ  
6105 N N   . GLU B 243 ? 0.4541 0.2110 0.3298 0.0124  0.0196  -0.0145 243 GLU B N   
6106 C CA  . GLU B 243 ? 0.5136 0.2594 0.3776 0.0168  0.0209  -0.0182 243 GLU B CA  
6107 C C   . GLU B 243 ? 0.5869 0.3392 0.4476 0.0260  0.0237  -0.0156 243 GLU B C   
6108 O O   . GLU B 243 ? 0.6487 0.3917 0.5019 0.0319  0.0276  -0.0156 243 GLU B O   
6109 C CB  . GLU B 243 ? 0.6186 0.3636 0.4781 0.0124  0.0155  -0.0244 243 GLU B CB  
6110 C CG  . GLU B 243 ? 0.7631 0.4985 0.6105 0.0172  0.0165  -0.0285 243 GLU B CG  
6111 C CD  . GLU B 243 ? 0.8724 0.6129 0.7160 0.0150  0.0110  -0.0336 243 GLU B CD  
6112 O OE1 . GLU B 243 ? 0.8941 0.6393 0.7422 0.0078  0.0062  -0.0356 243 GLU B OE1 
6113 O OE2 . GLU B 243 ? 0.8870 0.6271 0.7230 0.0206  0.0116  -0.0354 243 GLU B OE2 
6114 N N   . ILE B 244 ? 0.5197 0.2882 0.3861 0.0274  0.0222  -0.0132 244 ILE B N   
6115 C CA  . ILE B 244 ? 0.5162 0.2923 0.3793 0.0351  0.0245  -0.0113 244 ILE B CA  
6116 C C   . ILE B 244 ? 0.4607 0.2384 0.3267 0.0399  0.0298  -0.0053 244 ILE B C   
6117 O O   . ILE B 244 ? 0.4771 0.2529 0.3375 0.0468  0.0333  -0.0042 244 ILE B O   
6118 C CB  . ILE B 244 ? 0.5305 0.3219 0.3969 0.0342  0.0211  -0.0115 244 ILE B CB  
6119 C CG1 . ILE B 244 ? 0.5190 0.3083 0.3810 0.0304  0.0160  -0.0174 244 ILE B CG1 
6120 C CG2 . ILE B 244 ? 0.4606 0.2607 0.3235 0.0412  0.0239  -0.0097 244 ILE B CG2 
6121 C CD1 . ILE B 244 ? 0.5214 0.3012 0.3722 0.0341  0.0167  -0.0218 244 ILE B CD1 
6122 N N   . PHE B 245 ? 0.3601 0.1415 0.2350 0.0364  0.0304  -0.0014 245 PHE B N   
6123 C CA  . PHE B 245 ? 0.4069 0.1928 0.2854 0.0407  0.0349  0.0047  245 PHE B CA  
6124 C C   . PHE B 245 ? 0.5022 0.2758 0.3816 0.0400  0.0385  0.0073  245 PHE B C   
6125 O O   . PHE B 245 ? 0.5365 0.3126 0.4179 0.0441  0.0425  0.0125  245 PHE B O   
6126 C CB  . PHE B 245 ? 0.4025 0.2037 0.2900 0.0382  0.0337  0.0080  245 PHE B CB  
6127 C CG  . PHE B 245 ? 0.4452 0.2585 0.3311 0.0399  0.0315  0.0064  245 PHE B CG  
6128 C CD1 . PHE B 245 ? 0.4844 0.3042 0.3658 0.0463  0.0343  0.0078  245 PHE B CD1 
6129 C CD2 . PHE B 245 ? 0.4470 0.2652 0.3353 0.0350  0.0268  0.0033  245 PHE B CD2 
6130 C CE1 . PHE B 245 ? 0.5001 0.3302 0.3792 0.0473  0.0326  0.0061  245 PHE B CE1 
6131 C CE2 . PHE B 245 ? 0.4540 0.2821 0.3398 0.0367  0.0252  0.0019  245 PHE B CE2 
6132 C CZ  . PHE B 245 ? 0.4631 0.2966 0.3440 0.0426  0.0283  0.0031  245 PHE B CZ  
6133 N N   . GLY B 246 ? 0.5033 0.4561 0.5842 0.0466  -0.0148 -0.0076 246 GLY B N   
6134 C CA  . GLY B 246 ? 0.5198 0.4556 0.5928 0.0486  -0.0124 -0.0058 246 GLY B CA  
6135 C C   . GLY B 246 ? 0.5314 0.4589 0.5914 0.0477  -0.0152 -0.0010 246 GLY B C   
6136 O O   . GLY B 246 ? 0.5667 0.4804 0.6207 0.0519  -0.0168 0.0025  246 GLY B O   
6137 N N   . GLU B 247 ? 0.5078 0.4432 0.5632 0.0424  -0.0158 -0.0006 247 GLU B N   
6138 C CA  . GLU B 247 ? 0.5575 0.4861 0.6006 0.0409  -0.0179 0.0037  247 GLU B CA  
6139 C C   . GLU B 247 ? 0.4366 0.3735 0.4759 0.0329  -0.0143 0.0017  247 GLU B C   
6140 O O   . GLU B 247 ? 0.3505 0.3015 0.3974 0.0299  -0.0134 -0.0014 247 GLU B O   
6141 C CB  . GLU B 247 ? 0.6613 0.5924 0.7039 0.0453  -0.0262 0.0085  247 GLU B CB  
6142 C CG  . GLU B 247 ? 0.7567 0.6767 0.7986 0.0529  -0.0309 0.0124  247 GLU B CG  
6143 C CD  . GLU B 247 ? 0.8069 0.7288 0.8458 0.0558  -0.0387 0.0173  247 GLU B CD  
6144 O OE1 . GLU B 247 ? 0.8318 0.7492 0.8732 0.0622  -0.0438 0.0204  247 GLU B OE1 
6145 O OE2 . GLU B 247 ? 0.8347 0.7627 0.8689 0.0517  -0.0396 0.0182  247 GLU B OE2 
6146 N N   . HIS B 248 ? 0.4540 0.3823 0.4817 0.0295  -0.0122 0.0035  248 HIS B N   
6147 C CA  . HIS B 248 ? 0.4637 0.4008 0.4880 0.0225  -0.0098 0.0026  248 HIS B CA  
6148 C C   . HIS B 248 ? 0.5091 0.4530 0.5321 0.0235  -0.0159 0.0064  248 HIS B C   
6149 O O   . HIS B 248 ? 0.5060 0.4423 0.5247 0.0283  -0.0210 0.0106  248 HIS B O   
6150 C CB  . HIS B 248 ? 0.4922 0.4187 0.5051 0.0180  -0.0049 0.0029  248 HIS B CB  
6151 C CG  . HIS B 248 ? 0.6368 0.5581 0.6506 0.0154  0.0019  -0.0013 248 HIS B CG  
6152 N ND1 . HIS B 248 ? 0.6912 0.5974 0.7014 0.0190  0.0036  -0.0009 248 HIS B ND1 
6153 C CD2 . HIS B 248 ? 0.6518 0.5808 0.6693 0.0094  0.0077  -0.0060 248 HIS B CD2 
6154 C CE1 . HIS B 248 ? 0.6724 0.5769 0.6840 0.0153  0.0103  -0.0053 248 HIS B CE1 
6155 N NE2 . HIS B 248 ? 0.6593 0.5776 0.6752 0.0093  0.0129  -0.0085 248 HIS B NE2 
6156 N N   . PRO B 249 ? 0.4426 0.4005 0.4690 0.0192  -0.0155 0.0051  249 PRO B N   
6157 C CA  . PRO B 249 ? 0.3878 0.3527 0.4138 0.0203  -0.0210 0.0083  249 PRO B CA  
6158 C C   . PRO B 249 ? 0.3873 0.3439 0.4012 0.0187  -0.0216 0.0123  249 PRO B C   
6159 O O   . PRO B 249 ? 0.3491 0.3044 0.3572 0.0133  -0.0170 0.0116  249 PRO B O   
6160 C CB  . PRO B 249 ? 0.3311 0.3126 0.3640 0.0154  -0.0192 0.0053  249 PRO B CB  
6161 C CG  . PRO B 249 ? 0.3414 0.3224 0.3732 0.0097  -0.0121 0.0017  249 PRO B CG  
6162 C CD  . PRO B 249 ? 0.3941 0.3617 0.4243 0.0126  -0.0098 0.0007  249 PRO B CD  
6163 N N   . VAL B 250 ? 0.3711 0.3219 0.3811 0.0232  -0.0273 0.0165  250 VAL B N   
6164 C CA  . VAL B 250 ? 0.4201 0.3636 0.4187 0.0219  -0.0284 0.0204  250 VAL B CA  
6165 C C   . VAL B 250 ? 0.3752 0.3302 0.3744 0.0191  -0.0301 0.0216  250 VAL B C   
6166 O O   . VAL B 250 ? 0.3662 0.3181 0.3570 0.0159  -0.0288 0.0237  250 VAL B O   
6167 C CB  . VAL B 250 ? 0.5064 0.4373 0.4994 0.0276  -0.0336 0.0246  250 VAL B CB  
6168 C CG1 . VAL B 250 ? 0.6102 0.5294 0.5899 0.0256  -0.0329 0.0279  250 VAL B CG1 
6169 C CG2 . VAL B 250 ? 0.5054 0.4279 0.5016 0.0319  -0.0331 0.0234  250 VAL B CG2 
6170 N N   . TYR B 251 ? 0.3269 0.2946 0.3355 0.0203  -0.0327 0.0204  251 TYR B N   
6171 C CA  . TYR B 251 ? 0.3816 0.3606 0.3914 0.0178  -0.0342 0.0213  251 TYR B CA  
6172 C C   . TYR B 251 ? 0.3069 0.3003 0.3259 0.0140  -0.0308 0.0172  251 TYR B C   
6173 O O   . TYR B 251 ? 0.3192 0.3165 0.3465 0.0153  -0.0301 0.0139  251 TYR B O   
6174 C CB  . TYR B 251 ? 0.4608 0.4429 0.4732 0.0223  -0.0408 0.0237  251 TYR B CB  
6175 C CG  . TYR B 251 ? 0.4678 0.4366 0.4744 0.0273  -0.0449 0.0270  251 TYR B CG  
6176 C CD1 . TYR B 251 ? 0.5811 0.5380 0.5758 0.0266  -0.0450 0.0305  251 TYR B CD1 
6177 C CD2 . TYR B 251 ? 0.6069 0.5748 0.6199 0.0326  -0.0486 0.0267  251 TYR B CD2 
6178 C CE1 . TYR B 251 ? 0.7161 0.6606 0.7051 0.0309  -0.0488 0.0336  251 TYR B CE1 
6179 C CE2 . TYR B 251 ? 0.7024 0.6582 0.7102 0.0372  -0.0526 0.0300  251 TYR B CE2 
6180 C CZ  . TYR B 251 ? 0.7981 0.7422 0.7937 0.0363  -0.0528 0.0335  251 TYR B CZ  
6181 O OH  . TYR B 251 ? 0.9135 0.8453 0.9033 0.0406  -0.0568 0.0370  251 TYR B OH  
6182 N N   . MET B 252 ? 0.2701 0.2711 0.2875 0.0092  -0.0286 0.0175  252 MET B N   
6183 C CA  . MET B 252 ? 0.2603 0.2764 0.2862 0.0055  -0.0264 0.0144  252 MET B CA  
6184 C C   . MET B 252 ? 0.2466 0.2719 0.2730 0.0047  -0.0290 0.0165  252 MET B C   
6185 O O   . MET B 252 ? 0.2788 0.2992 0.2975 0.0044  -0.0300 0.0201  252 MET B O   
6186 C CB  . MET B 252 ? 0.2780 0.2959 0.3024 -0.0005 -0.0201 0.0121  252 MET B CB  
6187 C CG  . MET B 252 ? 0.3757 0.3896 0.4031 -0.0007 -0.0167 0.0084  252 MET B CG  
6188 S SD  . MET B 252 ? 0.4910 0.5054 0.5145 -0.0083 -0.0094 0.0062  252 MET B SD  
6189 C CE  . MET B 252 ? 0.4419 0.4720 0.4765 -0.0122 -0.0068 0.0014  252 MET B CE  
6190 N N   . TRP B 253 ? 0.2998 0.3382 0.3354 0.0042  -0.0299 0.0143  253 TRP B N   
6191 C CA  . TRP B 253 ? 0.2138 0.2631 0.2510 0.0021  -0.0309 0.0155  253 TRP B CA  
6192 C C   . TRP B 253 ? 0.2519 0.3098 0.2907 -0.0041 -0.0258 0.0138  253 TRP B C   
6193 O O   . TRP B 253 ? 0.2280 0.2927 0.2736 -0.0063 -0.0233 0.0100  253 TRP B O   
6194 C CB  . TRP B 253 ? 0.3046 0.3636 0.3505 0.0047  -0.0347 0.0141  253 TRP B CB  
6195 C CG  . TRP B 253 ? 0.2374 0.3087 0.2861 0.0020  -0.0349 0.0147  253 TRP B CG  
6196 C CD1 . TRP B 253 ? 0.2620 0.3463 0.3186 -0.0010 -0.0333 0.0117  253 TRP B CD1 
6197 C CD2 . TRP B 253 ? 0.2878 0.3589 0.3310 0.0019  -0.0367 0.0185  253 TRP B CD2 
6198 N NE1 . TRP B 253 ? 0.2842 0.3767 0.3408 -0.0027 -0.0341 0.0136  253 TRP B NE1 
6199 C CE2 . TRP B 253 ? 0.3033 0.3878 0.3518 -0.0010 -0.0360 0.0177  253 TRP B CE2 
6200 C CE3 . TRP B 253 ? 0.2554 0.3159 0.2894 0.0039  -0.0387 0.0224  253 TRP B CE3 
6201 C CZ2 . TRP B 253 ? 0.2827 0.3703 0.3280 -0.0017 -0.0370 0.0208  253 TRP B CZ2 
6202 C CZ3 . TRP B 253 ? 0.2869 0.3505 0.3175 0.0028  -0.0395 0.0253  253 TRP B CZ3 
6203 C CH2 . TRP B 253 ? 0.2738 0.3507 0.3101 0.0002  -0.0387 0.0245  253 TRP B CH2 
6204 N N   . PRO B 254 ? 0.2355 0.2935 0.2686 -0.0072 -0.0240 0.0165  254 PRO B N   
6205 C CA  . PRO B 254 ? 0.1981 0.2658 0.2334 -0.0131 -0.0196 0.0153  254 PRO B CA  
6206 C C   . PRO B 254 ? 0.2220 0.3046 0.2654 -0.0143 -0.0208 0.0142  254 PRO B C   
6207 O O   . PRO B 254 ? 0.2196 0.3052 0.2633 -0.0120 -0.0242 0.0164  254 PRO B O   
6208 C CB  . PRO B 254 ? 0.4201 0.4831 0.4470 -0.0149 -0.0182 0.0191  254 PRO B CB  
6209 C CG  . PRO B 254 ? 0.3665 0.4215 0.3885 -0.0102 -0.0226 0.0223  254 PRO B CG  
6210 C CD  . PRO B 254 ? 0.3093 0.3576 0.3331 -0.0056 -0.0256 0.0207  254 PRO B CD  
6211 N N   . PRO B 255 ? 0.1804 0.2724 0.2303 -0.0180 -0.0180 0.0107  255 PRO B N   
6212 C CA  . PRO B 255 ? 0.1690 0.2754 0.2268 -0.0195 -0.0190 0.0094  255 PRO B CA  
6213 C C   . PRO B 255 ? 0.2366 0.3490 0.2925 -0.0208 -0.0196 0.0129  255 PRO B C   
6214 O O   . PRO B 255 ? 0.2378 0.3493 0.2890 -0.0239 -0.0168 0.0151  255 PRO B O   
6215 C CB  . PRO B 255 ? 0.2343 0.3478 0.2965 -0.0247 -0.0146 0.0057  255 PRO B CB  
6216 C CG  . PRO B 255 ? 0.2280 0.3300 0.2870 -0.0240 -0.0125 0.0038  255 PRO B CG  
6217 C CD  . PRO B 255 ? 0.2745 0.3638 0.3245 -0.0212 -0.0137 0.0076  255 PRO B CD  
6218 N N   . GLU B 256 ? 0.2242 0.3427 0.2839 -0.0184 -0.0231 0.0135  256 GLU B N   
6219 C CA  . GLU B 256 ? 0.2195 0.3436 0.2779 -0.0191 -0.0239 0.0168  256 GLU B CA  
6220 C C   . GLU B 256 ? 0.2379 0.3512 0.2872 -0.0174 -0.0243 0.0209  256 GLU B C   
6221 O O   . GLU B 256 ? 0.2414 0.3577 0.2883 -0.0191 -0.0231 0.0239  256 GLU B O   
6222 C CB  . GLU B 256 ? 0.2080 0.3440 0.2699 -0.0246 -0.0204 0.0166  256 GLU B CB  
6223 C CG  . GLU B 256 ? 0.2066 0.3522 0.2764 -0.0274 -0.0192 0.0122  256 GLU B CG  
6224 C CD  . GLU B 256 ? 0.2481 0.4012 0.3244 -0.0253 -0.0225 0.0105  256 GLU B CD  
6225 O OE1 . GLU B 256 ? 0.3046 0.4572 0.3795 -0.0223 -0.0255 0.0130  256 GLU B OE1 
6226 O OE2 . GLU B 256 ? 0.2607 0.4202 0.3434 -0.0269 -0.0219 0.0066  256 GLU B OE2 
6227 N N   . ALA B 257 ? 0.2379 0.3385 0.2822 -0.0141 -0.0257 0.0212  257 ALA B N   
6228 C CA  . ALA B 257 ? 0.2063 0.2950 0.2412 -0.0126 -0.0260 0.0248  257 ALA B CA  
6229 C C   . ALA B 257 ? 0.2692 0.3567 0.2996 -0.0168 -0.0214 0.0263  257 ALA B C   
6230 O O   . ALA B 257 ? 0.2442 0.3250 0.2675 -0.0166 -0.0209 0.0297  257 ALA B O   
6231 C CB  . ALA B 257 ? 0.2886 0.3773 0.3210 -0.0101 -0.0293 0.0279  257 ALA B CB  
6232 N N   . SER B 258 ? 0.2563 0.3504 0.2908 -0.0209 -0.0179 0.0238  258 SER B N   
6233 C CA  . SER B 258 ? 0.3021 0.3988 0.3341 -0.0255 -0.0135 0.0253  258 SER B CA  
6234 C C   . SER B 258 ? 0.3022 0.3856 0.3261 -0.0258 -0.0114 0.0260  258 SER B C   
6235 O O   . SER B 258 ? 0.2738 0.3511 0.2971 -0.0254 -0.0108 0.0234  258 SER B O   
6236 C CB  . SER B 258 ? 0.2804 0.3891 0.3193 -0.0303 -0.0106 0.0224  258 SER B CB  
6237 O OG  . SER B 258 ? 0.3684 0.4809 0.4054 -0.0347 -0.0070 0.0245  258 SER B OG  
6238 N N   . VAL B 259 ? 0.2621 0.3411 0.2797 -0.0265 -0.0101 0.0295  259 VAL B N   
6239 C CA  . VAL B 259 ? 0.2466 0.3137 0.2560 -0.0275 -0.0075 0.0304  259 VAL B CA  
6240 C C   . VAL B 259 ? 0.2793 0.3514 0.2874 -0.0320 -0.0034 0.0325  259 VAL B C   
6241 O O   . VAL B 259 ? 0.2524 0.3354 0.2648 -0.0335 -0.0031 0.0340  259 VAL B O   
6242 C CB  . VAL B 259 ? 0.3304 0.3833 0.3317 -0.0231 -0.0104 0.0328  259 VAL B CB  
6243 C CG1 . VAL B 259 ? 0.2788 0.3262 0.2816 -0.0186 -0.0144 0.0308  259 VAL B CG1 
6244 C CG2 . VAL B 259 ? 0.2993 0.3549 0.2995 -0.0217 -0.0122 0.0362  259 VAL B CG2 
6245 N N   . SER B 260 ? 0.2530 0.3173 0.2553 -0.0344 -0.0002 0.0324  260 SER B N   
6246 C CA  . SER B 260 ? 0.2559 0.3213 0.2549 -0.0383 0.0039  0.0345  260 SER B CA  
6247 C C   . SER B 260 ? 0.3400 0.3900 0.3297 -0.0382 0.0055  0.0346  260 SER B C   
6248 O O   . SER B 260 ? 0.2913 0.3321 0.2785 -0.0357 0.0039  0.0326  260 SER B O   
6249 C CB  . SER B 260 ? 0.3055 0.3841 0.3109 -0.0438 0.0073  0.0328  260 SER B CB  
6250 O OG  . SER B 260 ? 0.3291 0.4040 0.3339 -0.0458 0.0091  0.0292  260 SER B OG  
6251 N N   . ASN B 261 ? 0.2917 0.3386 0.2762 -0.0406 0.0086  0.0370  261 ASN B N   
6252 C CA  . ASN B 261 ? 0.2267 0.2591 0.2019 -0.0410 0.0106  0.0370  261 ASN B CA  
6253 C C   . ASN B 261 ? 0.3631 0.3940 0.3390 -0.0435 0.0127  0.0333  261 ASN B C   
6254 O O   . ASN B 261 ? 0.3350 0.3528 0.3051 -0.0416 0.0122  0.0321  261 ASN B O   
6255 C CB  . ASN B 261 ? 0.3399 0.3714 0.3106 -0.0443 0.0144  0.0398  261 ASN B CB  
6256 C CG  . ASN B 261 ? 0.3957 0.4243 0.3633 -0.0416 0.0128  0.0436  261 ASN B CG  
6257 O OD1 . ASN B 261 ? 0.3518 0.3746 0.3175 -0.0371 0.0088  0.0442  261 ASN B OD1 
6258 N ND2 . ASN B 261 ? 0.4225 0.4554 0.3897 -0.0444 0.0161  0.0460  261 ASN B ND2 
6259 N N   . GLU B 262 ? 0.2698 0.3138 0.2528 -0.0478 0.0150  0.0314  262 GLU B N   
6260 C CA  . GLU B 262 ? 0.3609 0.4044 0.3448 -0.0507 0.0174  0.0275  262 GLU B CA  
6261 C C   . GLU B 262 ? 0.3188 0.3595 0.3060 -0.0469 0.0143  0.0247  262 GLU B C   
6262 O O   . GLU B 262 ? 0.3613 0.3928 0.3453 -0.0467 0.0154  0.0222  262 GLU B O   
6263 C CB  . GLU B 262 ? 0.4216 0.4805 0.4121 -0.0567 0.0205  0.0264  262 GLU B CB  
6264 C CG  . GLU B 262 ? 0.4901 0.5495 0.4766 -0.0620 0.0252  0.0276  262 GLU B CG  
6265 C CD  . GLU B 262 ? 0.4981 0.5744 0.4918 -0.0678 0.0276  0.0270  262 GLU B CD  
6266 O OE1 . GLU B 262 ? 0.4763 0.5568 0.4730 -0.0710 0.0290  0.0235  262 GLU B OE1 
6267 O OE2 . GLU B 262 ? 0.5333 0.6186 0.5297 -0.0692 0.0281  0.0302  262 GLU B OE2 
6268 N N   . ALA B 263 ? 0.2632 0.3117 0.2569 -0.0439 0.0105  0.0249  263 ALA B N   
6269 C CA  . ALA B 263 ? 0.2369 0.2834 0.2344 -0.0402 0.0076  0.0222  263 ALA B CA  
6270 C C   . ALA B 263 ? 0.3317 0.3619 0.3222 -0.0350 0.0051  0.0231  263 ALA B C   
6271 O O   . ALA B 263 ? 0.3160 0.3395 0.3066 -0.0332 0.0048  0.0205  263 ALA B O   
6272 C CB  . ALA B 263 ? 0.2101 0.2684 0.2157 -0.0381 0.0040  0.0224  263 ALA B CB  
6273 N N   . LEU B 264 ? 0.3612 0.3846 0.3456 -0.0326 0.0033  0.0267  264 LEU B N   
6274 C CA  . LEU B 264 ? 0.3447 0.3524 0.3218 -0.0280 0.0006  0.0279  264 LEU B CA  
6275 C C   . LEU B 264 ? 0.3593 0.3551 0.3297 -0.0297 0.0040  0.0265  264 LEU B C   
6276 O O   . LEU B 264 ? 0.2956 0.2805 0.2631 -0.0262 0.0023  0.0257  264 LEU B O   
6277 C CB  . LEU B 264 ? 0.3535 0.3562 0.3245 -0.0262 -0.0013 0.0321  264 LEU B CB  
6278 C CG  . LEU B 264 ? 0.3576 0.3690 0.3339 -0.0235 -0.0053 0.0336  264 LEU B CG  
6279 C CD1 . LEU B 264 ? 0.3134 0.3220 0.2840 -0.0234 -0.0055 0.0375  264 LEU B CD1 
6280 C CD2 . LEU B 264 ? 0.3117 0.3191 0.2899 -0.0181 -0.0104 0.0328  264 LEU B CD2 
6281 N N   . GLU B 265 ? 0.3648 0.3626 0.3326 -0.0351 0.0088  0.0264  265 GLU B N   
6282 C CA  . GLU B 265 ? 0.3819 0.3692 0.3434 -0.0374 0.0125  0.0247  265 GLU B CA  
6283 C C   . GLU B 265 ? 0.3476 0.3359 0.3140 -0.0376 0.0135  0.0206  265 GLU B C   
6284 O O   . GLU B 265 ? 0.3813 0.3571 0.3429 -0.0360 0.0142  0.0193  265 GLU B O   
6285 C CB  . GLU B 265 ? 0.3807 0.3725 0.3398 -0.0437 0.0176  0.0251  265 GLU B CB  
6286 C CG  . GLU B 265 ? 0.5659 0.5538 0.5188 -0.0437 0.0177  0.0290  265 GLU B CG  
6287 C CD  . GLU B 265 ? 0.7086 0.6979 0.6579 -0.0497 0.0230  0.0293  265 GLU B CD  
6288 O OE1 . GLU B 265 ? 0.7777 0.7732 0.7302 -0.0542 0.0264  0.0265  265 GLU B OE1 
6289 O OE2 . GLU B 265 ? 0.7723 0.7564 0.7155 -0.0501 0.0239  0.0322  265 GLU B OE2 
6290 N N   . LEU B 266 ? 0.3543 0.3572 0.3302 -0.0395 0.0136  0.0184  266 LEU B N   
6291 C CA  . LEU B 266 ? 0.3443 0.3485 0.3251 -0.0400 0.0149  0.0143  266 LEU B CA  
6292 C C   . LEU B 266 ? 0.3477 0.3440 0.3298 -0.0333 0.0107  0.0138  266 LEU B C   
6293 O O   . LEU B 266 ? 0.4197 0.4070 0.4002 -0.0323 0.0122  0.0115  266 LEU B O   
6294 C CB  . LEU B 266 ? 0.3498 0.3716 0.3403 -0.0436 0.0157  0.0122  266 LEU B CB  
6295 C CG  . LEU B 266 ? 0.3788 0.4034 0.3755 -0.0439 0.0168  0.0077  266 LEU B CG  
6296 C CD1 . LEU B 266 ? 0.3167 0.3346 0.3090 -0.0484 0.0222  0.0049  266 LEU B CD1 
6297 C CD2 . LEU B 266 ? 0.3896 0.4315 0.3959 -0.0466 0.0163  0.0062  266 LEU B CD2 
6298 N N   . TYR B 267 ? 0.3010 0.3001 0.2858 -0.0288 0.0057  0.0161  267 TYR B N   
6299 C CA  . TYR B 267 ? 0.3258 0.3175 0.3116 -0.0224 0.0013  0.0162  267 TYR B CA  
6300 C C   . TYR B 267 ? 0.3668 0.3406 0.3429 -0.0198 0.0013  0.0177  267 TYR B C   
6301 O O   . TYR B 267 ? 0.3704 0.3361 0.3469 -0.0165 0.0006  0.0162  267 TYR B O   
6302 C CB  . TYR B 267 ? 0.3231 0.3204 0.3120 -0.0186 -0.0040 0.0188  267 TYR B CB  
6303 C CG  . TYR B 267 ? 0.3254 0.3390 0.3247 -0.0196 -0.0049 0.0170  267 TYR B CG  
6304 C CD1 . TYR B 267 ? 0.3207 0.3384 0.3278 -0.0180 -0.0057 0.0136  267 TYR B CD1 
6305 C CD2 . TYR B 267 ? 0.3360 0.3606 0.3374 -0.0222 -0.0050 0.0187  267 TYR B CD2 
6306 C CE1 . TYR B 267 ? 0.3646 0.3969 0.3809 -0.0192 -0.0064 0.0118  267 TYR B CE1 
6307 C CE2 . TYR B 267 ? 0.3636 0.4029 0.3742 -0.0232 -0.0059 0.0171  267 TYR B CE2 
6308 C CZ  . TYR B 267 ? 0.3307 0.3737 0.3485 -0.0219 -0.0066 0.0136  267 TYR B CZ  
6309 O OH  . TYR B 267 ? 0.3294 0.3867 0.3560 -0.0231 -0.0074 0.0119  267 TYR B OH  
6310 N N   . TYR B 268 ? 0.3721 0.3394 0.3395 -0.0214 0.0023  0.0207  268 TYR B N   
6311 C CA  . TYR B 268 ? 0.3544 0.3043 0.3116 -0.0195 0.0025  0.0222  268 TYR B CA  
6312 C C   . TYR B 268 ? 0.3963 0.3393 0.3512 -0.0220 0.0073  0.0191  268 TYR B C   
6313 O O   . TYR B 268 ? 0.3398 0.2702 0.2911 -0.0186 0.0065  0.0189  268 TYR B O   
6314 C CB  . TYR B 268 ? 0.3590 0.3049 0.3077 -0.0218 0.0035  0.0256  268 TYR B CB  
6315 C CG  . TYR B 268 ? 0.4856 0.4156 0.4234 -0.0228 0.0062  0.0262  268 TYR B CG  
6316 C CD1 . TYR B 268 ? 0.5330 0.4481 0.4642 -0.0180 0.0031  0.0281  268 TYR B CD1 
6317 C CD2 . TYR B 268 ? 0.5646 0.4944 0.4984 -0.0286 0.0119  0.0251  268 TYR B CD2 
6318 C CE1 . TYR B 268 ? 0.5570 0.4570 0.4777 -0.0190 0.0055  0.0288  268 TYR B CE1 
6319 C CE2 . TYR B 268 ? 0.5504 0.4652 0.4738 -0.0297 0.0145  0.0256  268 TYR B CE2 
6320 C CZ  . TYR B 268 ? 0.5678 0.4676 0.4847 -0.0248 0.0113  0.0274  268 TYR B CZ  
6321 O OH  . TYR B 268 ? 0.6042 0.4887 0.5103 -0.0259 0.0139  0.0279  268 TYR B OH  
6322 N N   . GLU B 269 ? 0.3707 0.3220 0.3279 -0.0281 0.0122  0.0166  269 GLU B N   
6323 C CA  . GLU B 269 ? 0.4186 0.3632 0.3727 -0.0313 0.0173  0.0136  269 GLU B CA  
6324 C C   . GLU B 269 ? 0.4370 0.3811 0.3975 -0.0288 0.0171  0.0102  269 GLU B C   
6325 O O   . GLU B 269 ? 0.4487 0.3822 0.4054 -0.0290 0.0202  0.0083  269 GLU B O   
6326 C CB  . GLU B 269 ? 0.4734 0.4278 0.4283 -0.0390 0.0225  0.0119  269 GLU B CB  
6327 C CG  . GLU B 269 ? 0.6382 0.5888 0.5849 -0.0415 0.0237  0.0150  269 GLU B CG  
6328 C CD  . GLU B 269 ? 0.8649 0.7985 0.8007 -0.0421 0.0267  0.0151  269 GLU B CD  
6329 O OE1 . GLU B 269 ? 0.9009 0.8257 0.8288 -0.0410 0.0257  0.0183  269 GLU B OE1 
6330 O OE2 . GLU B 269 ? 0.9763 0.9053 0.9115 -0.0441 0.0303  0.0118  269 GLU B OE2 
6331 N N   . LYS B 270 ? 0.3560 0.3112 0.3262 -0.0264 0.0139  0.0094  270 LYS B N   
6332 C CA  . LYS B 270 ? 0.3472 0.3024 0.3242 -0.0235 0.0136  0.0062  270 LYS B CA  
6333 C C   . LYS B 270 ? 0.3829 0.3280 0.3593 -0.0158 0.0085  0.0082  270 LYS B C   
6334 O O   . LYS B 270 ? 0.4099 0.3563 0.3935 -0.0124 0.0073  0.0062  270 LYS B O   
6335 C CB  . LYS B 270 ? 0.4312 0.4039 0.4193 -0.0253 0.0130  0.0039  270 LYS B CB  
6336 C CG  . LYS B 270 ? 0.4924 0.4752 0.4818 -0.0332 0.0182  0.0015  270 LYS B CG  
6337 C CD  . LYS B 270 ? 0.6088 0.5817 0.5921 -0.0369 0.0240  -0.0010 270 LYS B CD  
6338 C CE  . LYS B 270 ? 0.6959 0.6787 0.6797 -0.0453 0.0291  -0.0031 270 LYS B CE  
6339 N NZ  . LYS B 270 ? 0.7506 0.7469 0.7443 -0.0477 0.0300  -0.0067 270 LYS B NZ  
6340 N N   . GLY B 271 ? 0.3696 0.3049 0.3379 -0.0131 0.0056  0.0123  271 GLY B N   
6341 C CA  . GLY B 271 ? 0.4019 0.3263 0.3683 -0.0062 0.0009  0.0146  271 GLY B CA  
6342 C C   . GLY B 271 ? 0.3821 0.3133 0.3536 -0.0016 -0.0056 0.0170  271 GLY B C   
6343 O O   . GLY B 271 ? 0.4088 0.3322 0.3798 0.0043  -0.0099 0.0188  271 GLY B O   
6344 N N   . ILE B 272 ? 0.3635 0.3086 0.3396 -0.0040 -0.0064 0.0171  272 ILE B N   
6345 C CA  . ILE B 272 ? 0.3945 0.3461 0.3749 -0.0002 -0.0123 0.0193  272 ILE B CA  
6346 C C   . ILE B 272 ? 0.4166 0.3588 0.3872 0.0016  -0.0154 0.0240  272 ILE B C   
6347 O O   . ILE B 272 ? 0.3454 0.2858 0.3092 -0.0022 -0.0128 0.0254  272 ILE B O   
6348 C CB  . ILE B 272 ? 0.3789 0.3480 0.3670 -0.0036 -0.0117 0.0180  272 ILE B CB  
6349 C CG1 . ILE B 272 ? 0.4113 0.3888 0.4081 -0.0061 -0.0082 0.0132  272 ILE B CG1 
6350 C CG2 . ILE B 272 ? 0.3031 0.2792 0.2955 0.0000  -0.0175 0.0200  272 ILE B CG2 
6351 C CD1 . ILE B 272 ? 0.3648 0.3372 0.3665 -0.0013 -0.0096 0.0112  272 ILE B CD1 
6352 N N   . ASN B 273 ? 0.3912 0.3273 0.3611 0.0073  -0.0208 0.0263  273 ASN B N   
6353 C CA  . ASN B 273 ? 0.3516 0.2778 0.3118 0.0091  -0.0241 0.0307  273 ASN B CA  
6354 C C   . ASN B 273 ? 0.3454 0.2804 0.3073 0.0096  -0.0279 0.0329  273 ASN B C   
6355 O O   . ASN B 273 ? 0.3240 0.2536 0.2776 0.0088  -0.0288 0.0361  273 ASN B O   
6356 C CB  . ASN B 273 ? 0.4308 0.3441 0.3879 0.0148  -0.0279 0.0325  273 ASN B CB  
6357 C CG  . ASN B 273 ? 0.6460 0.5441 0.5900 0.0150  -0.0287 0.0362  273 ASN B CG  
6358 O OD1 . ASN B 273 ? 0.6974 0.5909 0.6341 0.0107  -0.0244 0.0363  273 ASN B OD1 
6359 N ND2 . ASN B 273 ? 0.7648 0.6551 0.7056 0.0199  -0.0343 0.0394  273 ASN B ND2 
6360 N N   . MET B 274 ? 0.2967 0.2450 0.2689 0.0106  -0.0299 0.0312  274 MET B N   
6361 C CA  . MET B 274 ? 0.3296 0.2859 0.3031 0.0109  -0.0333 0.0333  274 MET B CA  
6362 C C   . MET B 274 ? 0.3146 0.2879 0.2989 0.0088  -0.0321 0.0303  274 MET B C   
6363 O O   . MET B 274 ? 0.3469 0.3257 0.3393 0.0091  -0.0309 0.0269  274 MET B O   
6364 C CB  . MET B 274 ? 0.3621 0.3135 0.3347 0.0164  -0.0398 0.0359  274 MET B CB  
6365 C CG  . MET B 274 ? 0.4986 0.4547 0.4694 0.0165  -0.0433 0.0386  274 MET B CG  
6366 S SD  . MET B 274 ? 0.6834 0.6554 0.6671 0.0188  -0.0470 0.0366  274 MET B SD  
6367 C CE  . MET B 274 ? 0.5533 0.5173 0.5382 0.0253  -0.0529 0.0378  274 MET B CE  
6368 N N   . LEU B 275 ? 0.3386 0.3199 0.3228 0.0065  -0.0323 0.0317  275 LEU B N   
6369 C CA  . LEU B 275 ? 0.3123 0.3095 0.3062 0.0052  -0.0324 0.0297  275 LEU B CA  
6370 C C   . LEU B 275 ? 0.3141 0.3151 0.3063 0.0060  -0.0357 0.0327  275 LEU B C   
6371 O O   . LEU B 275 ? 0.3019 0.2934 0.2854 0.0071  -0.0375 0.0360  275 LEU B O   
6372 C CB  . LEU B 275 ? 0.3482 0.3540 0.3453 -0.0004 -0.0268 0.0274  275 LEU B CB  
6373 C CG  . LEU B 275 ? 0.4248 0.4277 0.4144 -0.0046 -0.0229 0.0294  275 LEU B CG  
6374 C CD1 . LEU B 275 ? 0.5094 0.5219 0.5004 -0.0061 -0.0235 0.0314  275 LEU B CD1 
6375 C CD2 . LEU B 275 ? 0.3891 0.3950 0.3803 -0.0093 -0.0173 0.0266  275 LEU B CD2 
6376 N N   . ALA B 276 ? 0.2856 0.3003 0.2860 0.0052  -0.0364 0.0313  276 ALA B N   
6377 C CA  . ALA B 276 ? 0.3749 0.3947 0.3742 0.0051  -0.0386 0.0337  276 ALA B CA  
6378 C C   . ALA B 276 ? 0.2182 0.2511 0.2227 0.0008  -0.0350 0.0325  276 ALA B C   
6379 O O   . ALA B 276 ? 0.2400 0.2799 0.2507 -0.0016 -0.0320 0.0295  276 ALA B O   
6380 C CB  . ALA B 276 ? 0.3913 0.4147 0.3952 0.0092  -0.0442 0.0337  276 ALA B CB  
6381 N N   . THR B 277 ? 0.2139 0.2499 0.2158 -0.0004 -0.0351 0.0350  277 THR B N   
6382 C CA  . THR B 277 ? 0.2290 0.2778 0.2360 -0.0041 -0.0322 0.0345  277 THR B CA  
6383 C C   . THR B 277 ? 0.2650 0.3177 0.2713 -0.0030 -0.0347 0.0369  277 THR B C   
6384 O O   . THR B 277 ? 0.3287 0.3767 0.3329 0.0005  -0.0391 0.0378  277 THR B O   
6385 C CB  . THR B 277 ? 0.2218 0.2688 0.2248 -0.0083 -0.0269 0.0353  277 THR B CB  
6386 O OG1 . THR B 277 ? 0.2497 0.3096 0.2579 -0.0118 -0.0242 0.0352  277 THR B OG1 
6387 C CG2 . THR B 277 ? 0.2476 0.2824 0.2400 -0.0078 -0.0267 0.0388  277 THR B CG2 
6388 N N   . ASP B 278 ? 0.2071 0.2682 0.2150 -0.0061 -0.0320 0.0379  278 ASP B N   
6389 C CA  . ASP B 278 ? 0.2556 0.3227 0.2648 -0.0054 -0.0339 0.0395  278 ASP B CA  
6390 C C   . ASP B 278 ? 0.2537 0.3135 0.2542 -0.0059 -0.0328 0.0433  278 ASP B C   
6391 O O   . ASP B 278 ? 0.2390 0.2943 0.2349 -0.0082 -0.0290 0.0448  278 ASP B O   
6392 C CB  . ASP B 278 ? 0.2195 0.3016 0.2371 -0.0082 -0.0318 0.0381  278 ASP B CB  
6393 C CG  . ASP B 278 ? 0.2780 0.3664 0.2975 -0.0073 -0.0339 0.0393  278 ASP B CG  
6394 O OD1 . ASP B 278 ? 0.2850 0.3716 0.3048 -0.0042 -0.0382 0.0388  278 ASP B OD1 
6395 O OD2 . ASP B 278 ? 0.3045 0.3993 0.3249 -0.0096 -0.0312 0.0410  278 ASP B OD2 
6396 N N   . GLU B 279 ? 0.2791 0.2529 0.3179 0.0084  0.0045  -0.0091 279 GLU B N   
6397 C CA  . GLU B 279 ? 0.2989 0.2767 0.3409 0.0101  0.0097  -0.0114 279 GLU B CA  
6398 C C   . GLU B 279 ? 0.3140 0.2924 0.3618 0.0154  0.0108  -0.0090 279 GLU B C   
6399 O O   . GLU B 279 ? 0.3237 0.3098 0.3764 0.0177  0.0135  -0.0087 279 GLU B O   
6400 C CB  . GLU B 279 ? 0.2873 0.2581 0.3236 0.0091  0.0141  -0.0168 279 GLU B CB  
6401 C CG  . GLU B 279 ? 0.3213 0.2942 0.3584 0.0114  0.0191  -0.0202 279 GLU B CG  
6402 C CD  . GLU B 279 ? 0.4428 0.4081 0.4733 0.0093  0.0221  -0.0259 279 GLU B CD  
6403 O OE1 . GLU B 279 ? 0.4838 0.4424 0.5103 0.0062  0.0207  -0.0265 279 GLU B OE1 
6404 O OE2 . GLU B 279 ? 0.4429 0.4091 0.4720 0.0109  0.0258  -0.0296 279 GLU B OE2 
6405 N N   . VAL B 280 ? 0.3314 0.3027 0.3789 0.0177  0.0088  -0.0071 280 VAL B N   
6406 C CA  . VAL B 280 ? 0.3383 0.3104 0.3913 0.0230  0.0095  -0.0046 280 VAL B CA  
6407 C C   . VAL B 280 ? 0.3168 0.3010 0.3780 0.0232  0.0061  0.0003  280 VAL B C   
6408 O O   . VAL B 280 ? 0.3204 0.3121 0.3881 0.0269  0.0086  0.0019  280 VAL B O   
6409 C CB  . VAL B 280 ? 0.3678 0.3297 0.4182 0.0255  0.0077  -0.0032 280 VAL B CB  
6410 C CG1 . VAL B 280 ? 0.3152 0.2793 0.3718 0.0308  0.0070  0.0004  280 VAL B CG1 
6411 C CG2 . VAL B 280 ? 0.4506 0.4013 0.4947 0.0255  0.0118  -0.0073 280 VAL B CG2 
6412 N N   . ILE B 281 ? 0.3143 0.3010 0.3752 0.0193  0.0003  0.0030  281 ILE B N   
6413 C CA  . ILE B 281 ? 0.3020 0.2997 0.3706 0.0179  -0.0040 0.0080  281 ILE B CA  
6414 C C   . ILE B 281 ? 0.2765 0.2856 0.3494 0.0168  0.0000  0.0077  281 ILE B C   
6415 O O   . ILE B 281 ? 0.2467 0.2671 0.3284 0.0184  0.0004  0.0118  281 ILE B O   
6416 C CB  . ILE B 281 ? 0.3710 0.3661 0.4361 0.0137  -0.0115 0.0101  281 ILE B CB  
6417 C CG1 . ILE B 281 ? 0.2879 0.2734 0.3494 0.0162  -0.0157 0.0114  281 ILE B CG1 
6418 C CG2 . ILE B 281 ? 0.4264 0.4327 0.4991 0.0105  -0.0162 0.0152  281 ILE B CG2 
6419 C CD1 . ILE B 281 ? 0.3404 0.3206 0.3955 0.0134  -0.0229 0.0123  281 ILE B CD1 
6420 N N   . LEU B 282 ? 0.2543 0.2615 0.3212 0.0142  0.0032  0.0033  282 LEU B N   
6421 C CA  . LEU B 282 ? 0.2958 0.3129 0.3651 0.0139  0.0077  0.0024  282 LEU B CA  
6422 C C   . LEU B 282 ? 0.2988 0.3196 0.3721 0.0201  0.0135  0.0017  282 LEU B C   
6423 O O   . LEU B 282 ? 0.3216 0.3552 0.4022 0.0218  0.0153  0.0051  282 LEU B O   
6424 C CB  . LEU B 282 ? 0.2827 0.2952 0.3437 0.0109  0.0103  -0.0031 282 LEU B CB  
6425 C CG  . LEU B 282 ? 0.3263 0.3485 0.3883 0.0107  0.0148  -0.0044 282 LEU B CG  
6426 C CD1 . LEU B 282 ? 0.3450 0.3803 0.4141 0.0080  0.0117  0.0016  282 LEU B CD1 
6427 C CD2 . LEU B 282 ? 0.3300 0.3471 0.3833 0.0077  0.0168  -0.0101 282 LEU B CD2 
6428 N N   . LYS B 283 ? 0.2995 0.3091 0.3679 0.0237  0.0166  -0.0023 283 LYS B N   
6429 C CA  . LYS B 283 ? 0.3390 0.3498 0.4095 0.0304  0.0220  -0.0036 283 LYS B CA  
6430 C C   . LYS B 283 ? 0.3649 0.3847 0.4452 0.0344  0.0203  0.0026  283 LYS B C   
6431 O O   . LYS B 283 ? 0.3358 0.3659 0.4216 0.0390  0.0242  0.0043  283 LYS B O   
6432 C CB  . LYS B 283 ? 0.4275 0.4225 0.4905 0.0330  0.0244  -0.0087 283 LYS B CB  
6433 C CG  . LYS B 283 ? 0.4797 0.4661 0.5336 0.0288  0.0259  -0.0146 283 LYS B CG  
6434 C CD  . LYS B 283 ? 0.5230 0.5182 0.5760 0.0275  0.0287  -0.0168 283 LYS B CD  
6435 C CE  . LYS B 283 ? 0.6074 0.5944 0.6528 0.0299  0.0336  -0.0235 283 LYS B CE  
6436 N NZ  . LYS B 283 ? 0.6481 0.6430 0.6911 0.0285  0.0360  -0.0260 283 LYS B NZ  
6437 N N   . ASN B 284 ? 0.2288 0.2454 0.3114 0.0328  0.0144  0.0063  284 ASN B N   
6438 C CA  . ASN B 284 ? 0.3375 0.3627 0.4299 0.0357  0.0115  0.0126  284 ASN B CA  
6439 C C   . ASN B 284 ? 0.3719 0.4142 0.4735 0.0328  0.0094  0.0183  284 ASN B C   
6440 O O   . ASN B 284 ? 0.3782 0.4313 0.4896 0.0357  0.0084  0.0239  284 ASN B O   
6441 C CB  . ASN B 284 ? 0.3523 0.3690 0.4432 0.0341  0.0048  0.0148  284 ASN B CB  
6442 C CG  . ASN B 284 ? 0.4040 0.4064 0.4886 0.0383  0.0069  0.0114  284 ASN B CG  
6443 O OD1 . ASN B 284 ? 0.4030 0.4012 0.4848 0.0424  0.0129  0.0076  284 ASN B OD1 
6444 N ND2 . ASN B 284 ? 0.3887 0.3829 0.4704 0.0374  0.0017  0.0129  284 ASN B ND2 
6445 N N   . SER B 285 ? 0.3538 0.3992 0.4531 0.0271  0.0085  0.0176  285 SER B N   
6446 C CA  . SER B 285 ? 0.3601 0.4203 0.4678 0.0230  0.0053  0.0238  285 SER B CA  
6447 C C   . SER B 285 ? 0.3840 0.4564 0.4940 0.0240  0.0116  0.0236  285 SER B C   
6448 O O   . SER B 285 ? 0.3725 0.4607 0.4924 0.0237  0.0114  0.0301  285 SER B O   
6449 C CB  . SER B 285 ? 0.3269 0.3819 0.4306 0.0155  -0.0017 0.0244  285 SER B CB  
6450 O OG  . SER B 285 ? 0.2643 0.3073 0.3640 0.0150  -0.0075 0.0241  285 SER B OG  
6451 N N   . VAL B 286 ? 0.3778 0.4436 0.4786 0.0251  0.0170  0.0168  286 VAL B N   
6452 C CA  . VAL B 286 ? 0.3492 0.4250 0.4497 0.0263  0.0228  0.0158  286 VAL B CA  
6453 C C   . VAL B 286 ? 0.3841 0.4536 0.4783 0.0336  0.0300  0.0094  286 VAL B C   
6454 O O   . VAL B 286 ? 0.4337 0.4873 0.5192 0.0341  0.0303  0.0034  286 VAL B O   
6455 C CB  . VAL B 286 ? 0.3672 0.4403 0.4610 0.0198  0.0214  0.0132  286 VAL B CB  
6456 C CG1 . VAL B 286 ? 0.4086 0.4939 0.5028 0.0210  0.0270  0.0133  286 VAL B CG1 
6457 C CG2 . VAL B 286 ? 0.3280 0.4024 0.4254 0.0127  0.0132  0.0184  286 VAL B CG2 
6458 N N   . GLU B 287 ? 0.4385 0.5200 0.5364 0.0395  0.0358  0.0109  287 GLU B N   
6459 C CA  . GLU B 287 ? 0.5127 0.5872 0.6043 0.0477  0.0421  0.0050  287 GLU B CA  
6460 C C   . GLU B 287 ? 0.4711 0.5343 0.5501 0.0465  0.0448  -0.0034 287 GLU B C   
6461 O O   . GLU B 287 ? 0.5224 0.5692 0.5930 0.0480  0.0455  -0.0097 287 GLU B O   
6462 C CB  . GLU B 287 ? 0.5950 0.6862 0.6938 0.0557  0.0475  0.0092  287 GLU B CB  
6463 C CG  . GLU B 287 ? 0.6800 0.7789 0.7736 0.0588  0.0539  0.0063  287 GLU B CG  
6464 C CD  . GLU B 287 ? 0.7902 0.9056 0.8902 0.0679  0.0597  0.0106  287 GLU B CD  
6465 O OE1 . GLU B 287 ? 0.8554 0.9828 0.9544 0.0702  0.0644  0.0113  287 GLU B OE1 
6466 O OE2 . GLU B 287 ? 0.7836 0.8999 0.8894 0.0730  0.0595  0.0133  287 GLU B OE2 
6467 N N   . ARG B 288 ? 0.4006 0.4721 0.4782 0.0429  0.0458  -0.0032 288 ARG B N   
6468 C CA  . ARG B 288 ? 0.5053 0.5684 0.5712 0.0420  0.0485  -0.0109 288 ARG B CA  
6469 C C   . ARG B 288 ? 0.5010 0.5593 0.5640 0.0326  0.0434  -0.0115 288 ARG B C   
6470 O O   . ARG B 288 ? 0.5937 0.6607 0.6570 0.0285  0.0428  -0.0097 288 ARG B O   
6471 C CB  . ARG B 288 ? 0.6145 0.6901 0.6792 0.0466  0.0543  -0.0110 288 ARG B CB  
6472 C CG  . ARG B 288 ? 0.6871 0.7564 0.7454 0.0562  0.0599  -0.0164 288 ARG B CG  
6473 C CD  . ARG B 288 ? 0.7112 0.7880 0.7637 0.0613  0.0656  -0.0190 288 ARG B CD  
6474 N NE  . ARG B 288 ? 0.6640 0.7566 0.7214 0.0561  0.0650  -0.0136 288 ARG B NE  
6475 C CZ  . ARG B 288 ? 0.6773 0.7896 0.7463 0.0570  0.0659  -0.0046 288 ARG B CZ  
6476 N NH1 . ARG B 288 ? 0.7271 0.8468 0.8044 0.0633  0.0677  0.0000  288 ARG B NH1 
6477 N NH2 . ARG B 288 ? 0.6451 0.7700 0.7178 0.0514  0.0650  0.0002  288 ARG B NH2 
6478 N N   . ALA B 289 ? 0.4782 0.5224 0.5379 0.0298  0.0397  -0.0140 289 ALA B N   
6479 C CA  . ALA B 289 ? 0.4988 0.5399 0.5581 0.0220  0.0339  -0.0124 289 ALA B CA  
6480 C C   . ALA B 289 ? 0.4708 0.4983 0.5198 0.0189  0.0337  -0.0194 289 ALA B C   
6481 O O   . ALA B 289 ? 0.4773 0.4923 0.5228 0.0199  0.0334  -0.0225 289 ALA B O   
6482 C CB  . ALA B 289 ? 0.5000 0.5389 0.5656 0.0213  0.0290  -0.0076 289 ALA B CB  
6483 N N   . SER B 290 ? 0.4095 0.4402 0.4544 0.0151  0.0338  -0.0213 290 SER B N   
6484 C CA  . SER B 290 ? 0.4070 0.4274 0.4433 0.0109  0.0327  -0.0267 290 SER B CA  
6485 C C   . SER B 290 ? 0.3179 0.3363 0.3553 0.0053  0.0268  -0.0236 290 SER B C   
6486 O O   . SER B 290 ? 0.2612 0.2883 0.3027 0.0027  0.0239  -0.0187 290 SER B O   
6487 C CB  . SER B 290 ? 0.3737 0.3993 0.4047 0.0097  0.0352  -0.0301 290 SER B CB  
6488 O OG  . SER B 290 ? 0.3451 0.3645 0.3697 0.0044  0.0329  -0.0336 290 SER B OG  
6489 N N   . PRO B 291 ? 0.3245 0.3315 0.3579 0.0035  0.0249  -0.0260 291 PRO B N   
6490 C CA  . PRO B 291 ? 0.3360 0.3410 0.3688 -0.0007 0.0197  -0.0234 291 PRO B CA  
6491 C C   . PRO B 291 ? 0.2579 0.2652 0.2858 -0.0053 0.0184  -0.0251 291 PRO B C   
6492 O O   . PRO B 291 ? 0.2546 0.2596 0.2806 -0.0082 0.0143  -0.0235 291 PRO B O   
6493 C CB  . PRO B 291 ? 0.3643 0.3571 0.3941 -0.0001 0.0194  -0.0254 291 PRO B CB  
6494 C CG  . PRO B 291 ? 0.3724 0.3598 0.3981 0.0014  0.0239  -0.0310 291 PRO B CG  
6495 C CD  . PRO B 291 ? 0.3766 0.3717 0.4053 0.0055  0.0274  -0.0309 291 PRO B CD  
6496 N N   . TYR B 292 ? 0.2630 0.2747 0.2881 -0.0055 0.0217  -0.0284 292 TYR B N   
6497 C CA  . TYR B 292 ? 0.2513 0.2648 0.2711 -0.0096 0.0208  -0.0306 292 TYR B CA  
6498 C C   . TYR B 292 ? 0.3059 0.3302 0.3278 -0.0112 0.0194  -0.0269 292 TYR B C   
6499 O O   . TYR B 292 ? 0.2636 0.2907 0.2810 -0.0140 0.0191  -0.0286 292 TYR B O   
6500 C CB  . TYR B 292 ? 0.2797 0.2893 0.2935 -0.0093 0.0246  -0.0372 292 TYR B CB  
6501 C CG  . TYR B 292 ? 0.3082 0.3062 0.3202 -0.0082 0.0255  -0.0403 292 TYR B CG  
6502 C CD1 . TYR B 292 ? 0.3739 0.3656 0.3858 -0.0105 0.0225  -0.0389 292 TYR B CD1 
6503 C CD2 . TYR B 292 ? 0.3418 0.3346 0.3518 -0.0045 0.0292  -0.0443 292 TYR B CD2 
6504 C CE1 . TYR B 292 ? 0.4425 0.4238 0.4531 -0.0098 0.0233  -0.0409 292 TYR B CE1 
6505 C CE2 . TYR B 292 ? 0.3180 0.2990 0.3262 -0.0038 0.0296  -0.0468 292 TYR B CE2 
6506 C CZ  . TYR B 292 ? 0.4184 0.3940 0.4274 -0.0068 0.0267  -0.0448 292 TYR B CZ  
6507 O OH  . TYR B 292 ? 0.4793 0.4435 0.4868 -0.0066 0.0271  -0.0464 292 TYR B OH  
6508 N N   . LEU B 293 ? 0.2774 0.3080 0.3063 -0.0097 0.0183  -0.0213 293 LEU B N   
6509 C CA  . LEU B 293 ? 0.2750 0.3159 0.3075 -0.0117 0.0165  -0.0163 293 LEU B CA  
6510 C C   . LEU B 293 ? 0.2856 0.3241 0.3197 -0.0148 0.0097  -0.0117 293 LEU B C   
6511 O O   . LEU B 293 ? 0.2646 0.2956 0.2991 -0.0139 0.0070  -0.0113 293 LEU B O   
6512 C CB  . LEU B 293 ? 0.3162 0.3669 0.3565 -0.0083 0.0194  -0.0123 293 LEU B CB  
6513 C CG  . LEU B 293 ? 0.3100 0.3675 0.3491 -0.0045 0.0259  -0.0149 293 LEU B CG  
6514 C CD1 . LEU B 293 ? 0.3036 0.3516 0.3344 -0.0027 0.0293  -0.0230 293 LEU B CD1 
6515 C CD2 . LEU B 293 ? 0.2863 0.3520 0.3337 0.0002  0.0287  -0.0107 293 LEU B CD2 
6516 N N   . ARG B 294 ? 0.1953 0.2396 0.2295 -0.0180 0.0068  -0.0083 294 ARG B N   
6517 C CA  . ARG B 294 ? 0.2027 0.2457 0.2394 -0.0205 -0.0001 -0.0028 294 ARG B CA  
6518 C C   . ARG B 294 ? 0.2207 0.2722 0.2673 -0.0199 -0.0007 0.0034  294 ARG B C   
6519 O O   . ARG B 294 ? 0.2447 0.3070 0.2951 -0.0200 0.0027  0.0057  294 ARG B O   
6520 C CB  . ARG B 294 ? 0.1916 0.2357 0.2238 -0.0243 -0.0039 -0.0013 294 ARG B CB  
6521 C CG  . ARG B 294 ? 0.2698 0.3100 0.3032 -0.0266 -0.0120 0.0040  294 ARG B CG  
6522 C CD  . ARG B 294 ? 0.3138 0.3513 0.3403 -0.0296 -0.0163 0.0044  294 ARG B CD  
6523 N NE  . ARG B 294 ? 0.3143 0.3615 0.3420 -0.0318 -0.0139 0.0063  294 ARG B NE  
6524 C CZ  . ARG B 294 ? 0.3698 0.4181 0.3910 -0.0325 -0.0118 0.0030  294 ARG B CZ  
6525 N NH1 . ARG B 294 ? 0.3814 0.4222 0.3948 -0.0314 -0.0121 -0.0021 294 ARG B NH1 
6526 N NH2 . ARG B 294 ? 0.2967 0.3542 0.3190 -0.0342 -0.0096 0.0052  294 ARG B NH2 
6527 N N   . TYR B 295 ? 0.2378 0.2853 0.2885 -0.0192 -0.0048 0.0064  295 TYR B N   
6528 C CA  . TYR B 295 ? 0.2819 0.3380 0.3430 -0.0190 -0.0060 0.0128  295 TYR B CA  
6529 C C   . TYR B 295 ? 0.2769 0.3333 0.3406 -0.0237 -0.0144 0.0191  295 TYR B C   
6530 O O   . TYR B 295 ? 0.2732 0.3194 0.3300 -0.0255 -0.0200 0.0180  295 TYR B O   
6531 C CB  . TYR B 295 ? 0.2550 0.3071 0.3197 -0.0149 -0.0054 0.0124  295 TYR B CB  
6532 C CG  . TYR B 295 ? 0.2799 0.3328 0.3439 -0.0099 0.0027  0.0075  295 TYR B CG  
6533 C CD1 . TYR B 295 ? 0.2131 0.2559 0.2686 -0.0086 0.0055  0.0005  295 TYR B CD1 
6534 C CD2 . TYR B 295 ? 0.2695 0.3330 0.3411 -0.0064 0.0072  0.0101  295 TYR B CD2 
6535 C CE1 . TYR B 295 ? 0.2800 0.3215 0.3340 -0.0043 0.0120  -0.0041 295 TYR B CE1 
6536 C CE2 . TYR B 295 ? 0.2794 0.3420 0.3490 -0.0011 0.0141  0.0052  295 TYR B CE2 
6537 C CZ  . TYR B 295 ? 0.2564 0.3071 0.3168 -0.0003 0.0162  -0.0020 295 TYR B CZ  
6538 O OH  . TYR B 295 ? 0.3256 0.3735 0.3833 0.0048  0.0223  -0.0069 295 TYR B OH  
6539 N N   . TYR B 296 ? 0.1917 0.2600 0.2651 -0.0256 -0.0152 0.0261  296 TYR B N   
6540 C CA  . TYR B 296 ? 0.2497 0.3187 0.3274 -0.0306 -0.0238 0.0331  296 TYR B CA  
6541 C C   . TYR B 296 ? 0.3213 0.3960 0.4100 -0.0298 -0.0261 0.0386  296 TYR B C   
6542 O O   . TYR B 296 ? 0.2674 0.3561 0.3655 -0.0284 -0.0213 0.0424  296 TYR B O   
6543 C CB  . TYR B 296 ? 0.2565 0.3359 0.3370 -0.0349 -0.0237 0.0380  296 TYR B CB  
6544 C CG  . TYR B 296 ? 0.2955 0.3715 0.3660 -0.0354 -0.0209 0.0330  296 TYR B CG  
6545 C CD1 . TYR B 296 ? 0.2589 0.3209 0.3186 -0.0357 -0.0248 0.0282  296 TYR B CD1 
6546 C CD2 . TYR B 296 ? 0.2780 0.3653 0.3493 -0.0352 -0.0144 0.0334  296 TYR B CD2 
6547 C CE1 . TYR B 296 ? 0.3491 0.4089 0.4000 -0.0361 -0.0225 0.0239  296 TYR B CE1 
6548 C CE2 . TYR B 296 ? 0.3142 0.3987 0.3763 -0.0356 -0.0123 0.0289  296 TYR B CE2 
6549 C CZ  . TYR B 296 ? 0.3660 0.4369 0.4183 -0.0363 -0.0164 0.0242  296 TYR B CZ  
6550 O OH  . TYR B 296 ? 0.3988 0.4677 0.4423 -0.0366 -0.0144 0.0200  296 TYR B OH  
6551 N N   . PHE B 297 ? 0.3001 0.3644 0.3874 -0.0302 -0.0334 0.0391  297 PHE B N   
6552 C CA  . PHE B 297 ? 0.3071 0.3760 0.4045 -0.0298 -0.0370 0.0446  297 PHE B CA  
6553 C C   . PHE B 297 ? 0.3260 0.4037 0.4322 -0.0362 -0.0435 0.0536  297 PHE B C   
6554 O O   . PHE B 297 ? 0.2567 0.3255 0.3586 -0.0409 -0.0524 0.0554  297 PHE B O   
6555 C CB  . PHE B 297 ? 0.3001 0.3545 0.3919 -0.0279 -0.0429 0.0419  297 PHE B CB  
6556 C CG  . PHE B 297 ? 0.2594 0.3178 0.3610 -0.0274 -0.0473 0.0473  297 PHE B CG  
6557 C CD1 . PHE B 297 ? 0.2569 0.3222 0.3650 -0.0222 -0.0410 0.0469  297 PHE B CD1 
6558 C CD2 . PHE B 297 ? 0.2638 0.3187 0.3679 -0.0321 -0.0581 0.0527  297 PHE B CD2 
6559 C CE1 . PHE B 297 ? 0.2902 0.3602 0.4076 -0.0214 -0.0450 0.0520  297 PHE B CE1 
6560 C CE2 . PHE B 297 ? 0.2610 0.3201 0.3744 -0.0320 -0.0628 0.0578  297 PHE B CE2 
6561 C CZ  . PHE B 297 ? 0.3009 0.3684 0.4214 -0.0266 -0.0561 0.0577  297 PHE B CZ  
6562 N N   . ARG B 298 ? 0.2419 0.3372 0.3602 -0.0364 -0.0391 0.0594  298 ARG B N   
6563 C CA  . ARG B 298 ? 0.2409 0.3475 0.3702 -0.0428 -0.0448 0.0694  298 ARG B CA  
6564 C C   . ARG B 298 ? 0.2731 0.3756 0.3965 -0.0488 -0.0490 0.0709  298 ARG B C   
6565 O O   . ARG B 298 ? 0.3016 0.4053 0.4302 -0.0554 -0.0575 0.0782  298 ARG B O   
6566 C CB  . ARG B 298 ? 0.2930 0.3960 0.4285 -0.0453 -0.0546 0.0743  298 ARG B CB  
6567 C CG  . ARG B 298 ? 0.2277 0.3362 0.3702 -0.0393 -0.0508 0.0740  298 ARG B CG  
6568 C CD  . ARG B 298 ? 0.2180 0.3240 0.3670 -0.0418 -0.0609 0.0792  298 ARG B CD  
6569 N NE  . ARG B 298 ? 0.2107 0.3203 0.3645 -0.0352 -0.0569 0.0779  298 ARG B NE  
6570 C CZ  . ARG B 298 ? 0.3028 0.4088 0.4606 -0.0352 -0.0643 0.0805  298 ARG B CZ  
6571 N NH1 . ARG B 298 ? 0.2523 0.3507 0.4097 -0.0417 -0.0764 0.0844  298 ARG B NH1 
6572 N NH2 . ARG B 298 ? 0.2793 0.3888 0.4409 -0.0286 -0.0599 0.0792  298 ARG B NH2 
6573 N N   . GLU B 299 ? 0.3455 0.4427 0.4581 -0.0467 -0.0436 0.0641  299 GLU B N   
6574 C CA  . GLU B 299 ? 0.3921 0.4843 0.4972 -0.0512 -0.0466 0.0642  299 GLU B CA  
6575 C C   . GLU B 299 ? 0.3717 0.4468 0.4696 -0.0549 -0.0583 0.0643  299 GLU B C   
6576 O O   . GLU B 299 ? 0.3370 0.4082 0.4309 -0.0598 -0.0635 0.0670  299 GLU B O   
6577 C CB  . GLU B 299 ? 0.3565 0.4650 0.4710 -0.0560 -0.0455 0.0729  299 GLU B CB  
6578 C CG  . GLU B 299 ? 0.3628 0.4884 0.4825 -0.0515 -0.0337 0.0728  299 GLU B CG  
6579 C CD  . GLU B 299 ? 0.3821 0.5048 0.4904 -0.0486 -0.0267 0.0654  299 GLU B CD  
6580 O OE1 . GLU B 299 ? 0.3731 0.4801 0.4694 -0.0484 -0.0294 0.0586  299 GLU B OE1 
6581 O OE2 . GLU B 299 ? 0.3894 0.5258 0.5005 -0.0463 -0.0185 0.0664  299 GLU B OE2 
6582 N N   . LEU B 300 ? 0.3161 0.3804 0.4111 -0.0523 -0.0626 0.0613  300 LEU B N   
6583 C CA  . LEU B 300 ? 0.3622 0.4097 0.4493 -0.0547 -0.0739 0.0611  300 LEU B CA  
6584 C C   . LEU B 300 ? 0.3718 0.4035 0.4435 -0.0498 -0.0731 0.0520  300 LEU B C   
6585 O O   . LEU B 300 ? 0.4086 0.4268 0.4702 -0.0513 -0.0806 0.0509  300 LEU B O   
6586 C CB  . LEU B 300 ? 0.3409 0.3868 0.4351 -0.0553 -0.0809 0.0650  300 LEU B CB  
6587 C CG  . LEU B 300 ? 0.3637 0.4257 0.4745 -0.0605 -0.0833 0.0752  300 LEU B CG  
6588 C CD1 . LEU B 300 ? 0.3979 0.4556 0.5139 -0.0615 -0.0924 0.0786  300 LEU B CD1 
6589 C CD2 . LEU B 300 ? 0.2354 0.3009 0.3487 -0.0681 -0.0882 0.0819  300 LEU B CD2 
6590 N N   . ILE B 301 ? 0.2865 0.3196 0.3560 -0.0441 -0.0643 0.0459  301 ILE B N   
6591 C CA  . ILE B 301 ? 0.2259 0.2456 0.2825 -0.0395 -0.0635 0.0382  301 ILE B CA  
6592 C C   . ILE B 301 ? 0.2526 0.2783 0.3086 -0.0354 -0.0521 0.0326  301 ILE B C   
6593 O O   . ILE B 301 ? 0.3408 0.3770 0.4055 -0.0338 -0.0459 0.0336  301 ILE B O   
6594 C CB  . ILE B 301 ? 0.2666 0.2753 0.3203 -0.0366 -0.0694 0.0373  301 ILE B CB  
6595 C CG1 . ILE B 301 ? 0.3357 0.3310 0.3753 -0.0320 -0.0690 0.0304  301 ILE B CG1 
6596 C CG2 . ILE B 301 ? 0.3205 0.3371 0.3839 -0.0338 -0.0647 0.0381  301 ILE B CG2 
6597 C CD1 . ILE B 301 ? 0.3899 0.3732 0.4243 -0.0288 -0.0757 0.0296  301 ILE B CD1 
6598 N N   . SER B 302 ? 0.2955 0.3146 0.3409 -0.0337 -0.0496 0.0269  302 SER B N   
6599 C CA  . SER B 302 ? 0.3299 0.3531 0.3735 -0.0306 -0.0400 0.0213  302 SER B CA  
6600 C C   . SER B 302 ? 0.3362 0.3519 0.3766 -0.0259 -0.0379 0.0169  302 SER B C   
6601 O O   . SER B 302 ? 0.3224 0.3272 0.3561 -0.0244 -0.0433 0.0159  302 SER B O   
6602 C CB  . SER B 302 ? 0.3417 0.3628 0.3764 -0.0316 -0.0386 0.0179  302 SER B CB  
6603 O OG  . SER B 302 ? 0.3113 0.3397 0.3491 -0.0359 -0.0402 0.0224  302 SER B OG  
6604 N N   . VAL B 303 ? 0.2570 0.2784 0.3019 -0.0232 -0.0302 0.0145  303 VAL B N   
6605 C CA  . VAL B 303 ? 0.3102 0.3252 0.3534 -0.0189 -0.0276 0.0111  303 VAL B CA  
6606 C C   . VAL B 303 ? 0.2968 0.3134 0.3372 -0.0171 -0.0192 0.0054  303 VAL B C   
6607 O O   . VAL B 303 ? 0.3610 0.3865 0.4058 -0.0172 -0.0140 0.0053  303 VAL B O   
6608 C CB  . VAL B 303 ? 0.3206 0.3396 0.3731 -0.0169 -0.0277 0.0146  303 VAL B CB  
6609 C CG1 . VAL B 303 ? 0.3325 0.3434 0.3822 -0.0124 -0.0256 0.0113  303 VAL B CG1 
6610 C CG2 . VAL B 303 ? 0.1998 0.2192 0.2570 -0.0197 -0.0365 0.0210  303 VAL B CG2 
6611 N N   . PHE B 304 ? 0.2222 0.2301 0.2550 -0.0153 -0.0182 0.0011  304 PHE B N   
6612 C CA  . PHE B 304 ? 0.2677 0.2750 0.2985 -0.0136 -0.0112 -0.0040 304 PHE B CA  
6613 C C   . PHE B 304 ? 0.2456 0.2471 0.2780 -0.0100 -0.0097 -0.0047 304 PHE B C   
6614 O O   . PHE B 304 ? 0.2931 0.2887 0.3244 -0.0086 -0.0143 -0.0025 304 PHE B O   
6615 C CB  . PHE B 304 ? 0.2730 0.2758 0.2951 -0.0148 -0.0109 -0.0078 304 PHE B CB  
6616 C CG  . PHE B 304 ? 0.3159 0.3247 0.3359 -0.0178 -0.0106 -0.0083 304 PHE B CG  
6617 C CD1 . PHE B 304 ? 0.2842 0.2986 0.3049 -0.0184 -0.0048 -0.0115 304 PHE B CD1 
6618 C CD2 . PHE B 304 ? 0.2637 0.2716 0.2803 -0.0197 -0.0164 -0.0057 304 PHE B CD2 
6619 C CE1 . PHE B 304 ? 0.2970 0.3170 0.3153 -0.0210 -0.0046 -0.0118 304 PHE B CE1 
6620 C CE2 . PHE B 304 ? 0.2808 0.2939 0.2953 -0.0224 -0.0162 -0.0058 304 PHE B CE2 
6621 C CZ  . PHE B 304 ? 0.3204 0.3400 0.3359 -0.0230 -0.0101 -0.0088 304 PHE B CZ  
6622 N N   . PHE B 305 ? 0.3358 0.3382 0.3700 -0.0082 -0.0035 -0.0077 305 PHE B N   
6623 C CA  . PHE B 305 ? 0.2554 0.2516 0.2906 -0.0047 -0.0017 -0.0086 305 PHE B CA  
6624 C C   . PHE B 305 ? 0.2928 0.2821 0.3215 -0.0050 0.0016  -0.0133 305 PHE B C   
6625 O O   . PHE B 305 ? 0.2678 0.2592 0.2946 -0.0064 0.0055  -0.0170 305 PHE B O   
6626 C CB  . PHE B 305 ? 0.2055 0.2067 0.2475 -0.0017 0.0024  -0.0080 305 PHE B CB  
6627 C CG  . PHE B 305 ? 0.2937 0.3030 0.3436 -0.0015 -0.0009 -0.0024 305 PHE B CG  
6628 C CD1 . PHE B 305 ? 0.2363 0.2557 0.2894 -0.0042 -0.0012 -0.0001 305 PHE B CD1 
6629 C CD2 . PHE B 305 ? 0.2793 0.2865 0.3333 0.0009  -0.0041 0.0011  305 PHE B CD2 
6630 C CE1 . PHE B 305 ? 0.2796 0.3075 0.3411 -0.0049 -0.0046 0.0060  305 PHE B CE1 
6631 C CE2 . PHE B 305 ? 0.3116 0.3273 0.3739 0.0004  -0.0077 0.0069  305 PHE B CE2 
6632 C CZ  . PHE B 305 ? 0.3259 0.3520 0.3921 -0.0028 -0.0081 0.0095  305 PHE B CZ  
6633 N N   . ARG B 306 ? 0.2708 0.2524 0.2962 -0.0038 -0.0003 -0.0128 306 ARG B N   
6634 C CA  . ARG B 306 ? 0.3157 0.2920 0.3356 -0.0048 0.0021  -0.0160 306 ARG B CA  
6635 C C   . ARG B 306 ? 0.3015 0.2746 0.3227 -0.0039 0.0075  -0.0193 306 ARG B C   
6636 O O   . ARG B 306 ? 0.3109 0.2838 0.3365 -0.0009 0.0091  -0.0187 306 ARG B O   
6637 C CB  . ARG B 306 ? 0.3191 0.2888 0.3353 -0.0031 -0.0009 -0.0139 306 ARG B CB  
6638 C CG  . ARG B 306 ? 0.3505 0.3148 0.3694 0.0005  -0.0002 -0.0122 306 ARG B CG  
6639 C CD  . ARG B 306 ? 0.3649 0.3223 0.3790 0.0021  -0.0012 -0.0109 306 ARG B CD  
6640 N NE  . ARG B 306 ? 0.4173 0.3691 0.4338 0.0051  0.0008  -0.0100 306 ARG B NE  
6641 C CZ  . ARG B 306 ? 0.4123 0.3577 0.4258 0.0067  0.0014  -0.0086 306 ARG B CZ  
6642 N NH1 . ARG B 306 ? 0.3537 0.2983 0.3616 0.0060  0.0004  -0.0079 306 ARG B NH1 
6643 N NH2 . ARG B 306 ? 0.4536 0.3938 0.4695 0.0095  0.0032  -0.0078 306 ARG B NH2 
6644 N N   . ASP B 307 ? 0.3094 0.2801 0.3267 -0.0064 0.0100  -0.0229 307 ASP B N   
6645 C CA  . ASP B 307 ? 0.3302 0.2953 0.3473 -0.0060 0.0142  -0.0263 307 ASP B CA  
6646 C C   . ASP B 307 ? 0.3431 0.2997 0.3597 -0.0044 0.0139  -0.0245 307 ASP B C   
6647 O O   . ASP B 307 ? 0.2964 0.2504 0.3099 -0.0064 0.0131  -0.0238 307 ASP B O   
6648 C CB  . ASP B 307 ? 0.3522 0.3175 0.3654 -0.0101 0.0160  -0.0306 307 ASP B CB  
6649 C CG  . ASP B 307 ? 0.4303 0.3884 0.4423 -0.0099 0.0195  -0.0348 307 ASP B CG  
6650 O OD1 . ASP B 307 ? 0.4108 0.3607 0.4233 -0.0082 0.0202  -0.0340 307 ASP B OD1 
6651 O OD2 . ASP B 307 ? 0.4978 0.4577 0.5077 -0.0112 0.0213  -0.0389 307 ASP B OD2 
6652 N N   . LYS B 308 ? 0.2790 0.2321 0.2989 -0.0004 0.0147  -0.0231 308 LYS B N   
6653 C CA  . LYS B 308 ? 0.3495 0.2948 0.3690 0.0018  0.0143  -0.0206 308 LYS B CA  
6654 C C   . LYS B 308 ? 0.3146 0.2523 0.3308 -0.0009 0.0166  -0.0227 308 LYS B C   
6655 O O   . LYS B 308 ? 0.2993 0.2335 0.3135 -0.0016 0.0157  -0.0201 308 LYS B O   
6656 C CB  . LYS B 308 ? 0.3040 0.2470 0.3276 0.0067  0.0151  -0.0193 308 LYS B CB  
6657 C CG  . LYS B 308 ? 0.3977 0.3328 0.4210 0.0097  0.0144  -0.0162 308 LYS B CG  
6658 C CD  . LYS B 308 ? 0.4644 0.3981 0.4920 0.0149  0.0157  -0.0155 308 LYS B CD  
6659 C CE  . LYS B 308 ? 0.4808 0.4068 0.5082 0.0184  0.0149  -0.0122 308 LYS B CE  
6660 N NZ  . LYS B 308 ? 0.5483 0.4693 0.5711 0.0160  0.0138  -0.0105 308 LYS B NZ  
6661 N N   . THR B 309 ? 0.2921 0.2272 0.3074 -0.0025 0.0194  -0.0272 309 THR B N   
6662 C CA  . THR B 309 ? 0.3277 0.2539 0.3402 -0.0054 0.0210  -0.0291 309 THR B CA  
6663 C C   . THR B 309 ? 0.3574 0.2868 0.3677 -0.0106 0.0198  -0.0283 309 THR B C   
6664 O O   . THR B 309 ? 0.3336 0.2585 0.3433 -0.0122 0.0197  -0.0257 309 THR B O   
6665 C CB  . THR B 309 ? 0.3629 0.2848 0.3738 -0.0057 0.0235  -0.0346 309 THR B CB  
6666 O OG1 . THR B 309 ? 0.3567 0.2756 0.3695 0.0001  0.0251  -0.0349 309 THR B OG1 
6667 C CG2 . THR B 309 ? 0.3665 0.2780 0.3744 -0.0097 0.0241  -0.0366 309 THR B CG2 
6668 N N   . LEU B 310 ? 0.3237 0.2616 0.3331 -0.0130 0.0189  -0.0300 310 LEU B N   
6669 C CA  . LEU B 310 ? 0.3089 0.2512 0.3163 -0.0174 0.0177  -0.0292 310 LEU B CA  
6670 C C   . LEU B 310 ? 0.2980 0.2426 0.3051 -0.0154 0.0157  -0.0239 310 LEU B C   
6671 O O   . LEU B 310 ? 0.3238 0.2686 0.3296 -0.0176 0.0157  -0.0216 310 LEU B O   
6672 C CB  . LEU B 310 ? 0.3833 0.3343 0.3895 -0.0195 0.0170  -0.0319 310 LEU B CB  
6673 C CG  . LEU B 310 ? 0.4086 0.3580 0.4137 -0.0213 0.0189  -0.0374 310 LEU B CG  
6674 C CD1 . LEU B 310 ? 0.3797 0.3385 0.3835 -0.0224 0.0181  -0.0392 310 LEU B CD1 
6675 C CD2 . LEU B 310 ? 0.3835 0.3268 0.3869 -0.0261 0.0194  -0.0397 310 LEU B CD2 
6676 N N   . SER B 311 ? 0.2589 0.2053 0.2668 -0.0111 0.0139  -0.0217 311 SER B N   
6677 C CA  . SER B 311 ? 0.3216 0.2687 0.3277 -0.0083 0.0115  -0.0172 311 SER B CA  
6678 C C   . SER B 311 ? 0.3371 0.2769 0.3433 -0.0068 0.0127  -0.0143 311 SER B C   
6679 O O   . SER B 311 ? 0.3658 0.3063 0.3694 -0.0065 0.0123  -0.0109 311 SER B O   
6680 C CB  . SER B 311 ? 0.3333 0.2826 0.3403 -0.0044 0.0084  -0.0156 311 SER B CB  
6681 O OG  . SER B 311 ? 0.3272 0.2832 0.3345 -0.0061 0.0072  -0.0176 311 SER B OG  
6682 N N   . ASP B 312 ? 0.2510 0.1839 0.2597 -0.0054 0.0145  -0.0153 312 ASP B N   
6683 C CA  . ASP B 312 ? 0.3529 0.2777 0.3615 -0.0041 0.0158  -0.0124 312 ASP B CA  
6684 C C   . ASP B 312 ? 0.3308 0.2532 0.3387 -0.0092 0.0177  -0.0122 312 ASP B C   
6685 O O   . ASP B 312 ? 0.3309 0.2502 0.3380 -0.0089 0.0182  -0.0079 312 ASP B O   
6686 C CB  . ASP B 312 ? 0.3252 0.2427 0.3364 -0.0012 0.0172  -0.0138 312 ASP B CB  
6687 C CG  . ASP B 312 ? 0.3498 0.2691 0.3626 0.0043  0.0151  -0.0117 312 ASP B CG  
6688 O OD1 . ASP B 312 ? 0.3581 0.2814 0.3693 0.0061  0.0121  -0.0086 312 ASP B OD1 
6689 O OD2 . ASP B 312 ? 0.3697 0.2865 0.3854 0.0072  0.0161  -0.0131 312 ASP B OD2 
6690 N N   . LEU B 313 ? 0.2973 0.2208 0.3054 -0.0140 0.0186  -0.0163 313 LEU B N   
6691 C CA  . LEU B 313 ? 0.3421 0.2639 0.3502 -0.0197 0.0197  -0.0158 313 LEU B CA  
6692 C C   . LEU B 313 ? 0.3742 0.3040 0.3813 -0.0206 0.0190  -0.0111 313 LEU B C   
6693 O O   . LEU B 313 ? 0.3205 0.2482 0.3282 -0.0219 0.0199  -0.0067 313 LEU B O   
6694 C CB  . LEU B 313 ? 0.3574 0.2802 0.3653 -0.0246 0.0199  -0.0214 313 LEU B CB  
6695 C CG  . LEU B 313 ? 0.3760 0.2888 0.3836 -0.0238 0.0210  -0.0260 313 LEU B CG  
6696 C CD1 . LEU B 313 ? 0.4227 0.3385 0.4287 -0.0265 0.0209  -0.0318 313 LEU B CD1 
6697 C CD2 . LEU B 313 ? 0.3375 0.2385 0.3452 -0.0265 0.0217  -0.0249 313 LEU B CD2 
6698 N N   . ILE B 314 ? 0.3131 0.2524 0.3186 -0.0194 0.0174  -0.0115 314 ILE B N   
6699 C CA  . ILE B 314 ? 0.3741 0.3211 0.3777 -0.0191 0.0168  -0.0073 314 ILE B CA  
6700 C C   . ILE B 314 ? 0.4116 0.3560 0.4132 -0.0136 0.0165  -0.0021 314 ILE B C   
6701 O O   . ILE B 314 ? 0.3407 0.2873 0.3417 -0.0137 0.0177  0.0027  314 ILE B O   
6702 C CB  . ILE B 314 ? 0.3314 0.2874 0.3325 -0.0183 0.0148  -0.0092 314 ILE B CB  
6703 C CG1 . ILE B 314 ? 0.2944 0.2541 0.2970 -0.0239 0.0152  -0.0137 314 ILE B CG1 
6704 C CG2 . ILE B 314 ? 0.3192 0.2825 0.3170 -0.0157 0.0139  -0.0047 314 ILE B CG2 
6705 C CD1 . ILE B 314 ? 0.2762 0.2437 0.2764 -0.0231 0.0132  -0.0158 314 ILE B CD1 
6706 N N   . GLY B 315 ? 0.3660 0.3061 0.3668 -0.0087 0.0150  -0.0027 315 GLY B N   
6707 C CA  . GLY B 315 ? 0.4190 0.3573 0.4167 -0.0028 0.0138  0.0018  315 GLY B CA  
6708 C C   . GLY B 315 ? 0.4181 0.3492 0.4169 -0.0021 0.0159  0.0055  315 GLY B C   
6709 O O   . GLY B 315 ? 0.4339 0.3654 0.4295 0.0018  0.0158  0.0103  315 GLY B O   
6710 N N   . PHE B 316 ? 0.3717 0.2958 0.3742 -0.0053 0.0177  0.0033  316 PHE B N   
6711 C CA  . PHE B 316 ? 0.3971 0.3123 0.4005 -0.0042 0.0193  0.0066  316 PHE B CA  
6712 C C   . PHE B 316 ? 0.3858 0.2955 0.3920 -0.0106 0.0216  0.0061  316 PHE B C   
6713 O O   . PHE B 316 ? 0.3518 0.2548 0.3585 -0.0107 0.0229  0.0102  316 PHE B O   
6714 C CB  . PHE B 316 ? 0.3662 0.2743 0.3704 0.0004  0.0185  0.0048  316 PHE B CB  
6715 C CG  . PHE B 316 ? 0.4597 0.3719 0.4617 0.0062  0.0154  0.0055  316 PHE B CG  
6716 C CD1 . PHE B 316 ? 0.5088 0.4205 0.5071 0.0111  0.0140  0.0104  316 PHE B CD1 
6717 C CD2 . PHE B 316 ? 0.5289 0.4450 0.5323 0.0066  0.0134  0.0015  316 PHE B CD2 
6718 C CE1 . PHE B 316 ? 0.4606 0.3745 0.4562 0.0161  0.0102  0.0107  316 PHE B CE1 
6719 C CE2 . PHE B 316 ? 0.5349 0.4540 0.5365 0.0110  0.0098  0.0025  316 PHE B CE2 
6720 C CZ  . PHE B 316 ? 0.5304 0.4478 0.5279 0.0157  0.0078  0.0068  316 PHE B CZ  
6721 N N   . SER B 317 ? 0.3075 0.2190 0.3154 -0.0160 0.0217  0.0014  317 SER B N   
6722 C CA  . SER B 317 ? 0.4057 0.3096 0.4156 -0.0221 0.0228  -0.0001 317 SER B CA  
6723 C C   . SER B 317 ? 0.4537 0.3640 0.4652 -0.0288 0.0231  0.0027  317 SER B C   
6724 O O   . SER B 317 ? 0.3952 0.3005 0.4084 -0.0326 0.0240  0.0068  317 SER B O   
6725 C CB  . SER B 317 ? 0.3955 0.2959 0.4054 -0.0234 0.0224  -0.0076 317 SER B CB  
6726 O OG  . SER B 317 ? 0.4166 0.3108 0.4260 -0.0175 0.0225  -0.0096 317 SER B OG  
6727 N N   . TYR B 318 ? 0.2739 0.1956 0.2852 -0.0305 0.0223  0.0011  318 TYR B N   
6728 C CA  . TYR B 318 ? 0.3239 0.2520 0.3375 -0.0377 0.0223  0.0024  318 TYR B CA  
6729 C C   . TYR B 318 ? 0.3483 0.2831 0.3633 -0.0384 0.0236  0.0106  318 TYR B C   
6730 O O   . TYR B 318 ? 0.3343 0.2750 0.3526 -0.0449 0.0236  0.0129  318 TYR B O   
6731 C CB  . TYR B 318 ? 0.3676 0.3064 0.3801 -0.0384 0.0211  -0.0015 318 TYR B CB  
6732 C CG  . TYR B 318 ? 0.3595 0.2938 0.3713 -0.0403 0.0201  -0.0092 318 TYR B CG  
6733 C CD1 . TYR B 318 ? 0.3986 0.3206 0.4109 -0.0434 0.0201  -0.0126 318 TYR B CD1 
6734 C CD2 . TYR B 318 ? 0.3863 0.3283 0.3963 -0.0385 0.0191  -0.0130 318 TYR B CD2 
6735 C CE1 . TYR B 318 ? 0.4019 0.3200 0.4123 -0.0441 0.0194  -0.0198 318 TYR B CE1 
6736 C CE2 . TYR B 318 ? 0.4286 0.3676 0.4376 -0.0397 0.0186  -0.0196 318 TYR B CE2 
6737 C CZ  . TYR B 318 ? 0.4060 0.3334 0.4150 -0.0422 0.0189  -0.0231 318 TYR B CZ  
6738 O OH  . TYR B 318 ? 0.3789 0.3037 0.3858 -0.0425 0.0186  -0.0297 318 TYR B OH  
6739 N N   . HIS B 319 ? 0.3529 0.2877 0.3656 -0.0318 0.0245  0.0152  319 HIS B N   
6740 C CA  . HIS B 319 ? 0.4076 0.3479 0.4214 -0.0319 0.0262  0.0236  319 HIS B CA  
6741 C C   . HIS B 319 ? 0.4318 0.3643 0.4500 -0.0390 0.0271  0.0268  319 HIS B C   
6742 O O   . HIS B 319 ? 0.4452 0.3847 0.4666 -0.0430 0.0283  0.0335  319 HIS B O   
6743 C CB  . HIS B 319 ? 0.3711 0.3100 0.3805 -0.0231 0.0268  0.0275  319 HIS B CB  
6744 C CG  . HIS B 319 ? 0.3655 0.2904 0.3748 -0.0212 0.0270  0.0277  319 HIS B CG  
6745 N ND1 . HIS B 319 ? 0.3659 0.2849 0.3772 -0.0235 0.0288  0.0336  319 HIS B ND1 
6746 C CD2 . HIS B 319 ? 0.3515 0.2674 0.3591 -0.0170 0.0258  0.0230  319 HIS B CD2 
6747 C CE1 . HIS B 319 ? 0.3987 0.3051 0.4089 -0.0205 0.0285  0.0322  319 HIS B CE1 
6748 N NE2 . HIS B 319 ? 0.3498 0.2545 0.3580 -0.0164 0.0268  0.0258  319 HIS B NE2 
6749 N N   . ALA B 320 ? 0.4259 0.3438 0.4442 -0.0405 0.0263  0.0224  320 ALA B N   
6750 C CA  . ALA B 320 ? 0.4804 0.3874 0.5017 -0.0468 0.0264  0.0249  320 ALA B CA  
6751 C C   . ALA B 320 ? 0.4565 0.3619 0.4808 -0.0562 0.0245  0.0210  320 ALA B C   
6752 O O   . ALA B 320 ? 0.4220 0.3160 0.4481 -0.0622 0.0235  0.0218  320 ALA B O   
6753 C CB  . ALA B 320 ? 0.4618 0.3525 0.4806 -0.0426 0.0263  0.0223  320 ALA B CB  
6754 N N   . TRP B 321 ? 0.3879 0.3038 0.4122 -0.0576 0.0235  0.0168  321 TRP B N   
6755 C CA  . TRP B 321 ? 0.4061 0.3212 0.4323 -0.0658 0.0212  0.0123  321 TRP B CA  
6756 C C   . TRP B 321 ? 0.4207 0.3522 0.4513 -0.0712 0.0211  0.0172  321 TRP B C   
6757 O O   . TRP B 321 ? 0.3398 0.2849 0.3702 -0.0665 0.0228  0.0214  321 TRP B O   
6758 C CB  . TRP B 321 ? 0.3036 0.2181 0.3261 -0.0632 0.0199  0.0030  321 TRP B CB  
6759 C CG  . TRP B 321 ? 0.3070 0.2084 0.3256 -0.0576 0.0201  -0.0026 321 TRP B CG  
6760 C CD1 . TRP B 321 ? 0.3389 0.2351 0.3559 -0.0503 0.0217  -0.0004 321 TRP B CD1 
6761 C CD2 . TRP B 321 ? 0.4692 0.3623 0.4847 -0.0580 0.0188  -0.0111 321 TRP B CD2 
6762 N NE1 . TRP B 321 ? 0.4728 0.3586 0.4867 -0.0464 0.0215  -0.0068 321 TRP B NE1 
6763 C CE2 . TRP B 321 ? 0.4675 0.3513 0.4802 -0.0508 0.0199  -0.0134 321 TRP B CE2 
6764 C CE3 . TRP B 321 ? 0.5179 0.4109 0.5324 -0.0635 0.0167  -0.0168 321 TRP B CE3 
6765 C CZ2 . TRP B 321 ? 0.5202 0.3955 0.5295 -0.0485 0.0195  -0.0209 321 TRP B CZ2 
6766 C CZ3 . TRP B 321 ? 0.4887 0.3722 0.4989 -0.0612 0.0161  -0.0247 321 TRP B CZ3 
6767 C CH2 . TRP B 321 ? 0.4997 0.3748 0.5073 -0.0535 0.0177  -0.0265 321 TRP B CH2 
6768 N N   . ASN B 322 ? 0.4794 0.4091 0.5136 -0.0808 0.0187  0.0166  322 ASN B N   
6769 C CA  . ASN B 322 ? 0.5109 0.4567 0.5493 -0.0863 0.0177  0.0189  322 ASN B CA  
6770 C C   . ASN B 322 ? 0.4423 0.3973 0.4771 -0.0816 0.0175  0.0127  322 ASN B C   
6771 O O   . ASN B 322 ? 0.5000 0.4463 0.5301 -0.0786 0.0166  0.0048  322 ASN B O   
6772 C CB  . ASN B 322 ? 0.6514 0.5906 0.6934 -0.0977 0.0141  0.0174  322 ASN B CB  
6773 C CG  . ASN B 322 ? 0.7784 0.7340 0.8249 -0.1039 0.0123  0.0187  322 ASN B CG  
6774 O OD1 . ASN B 322 ? 0.8762 0.8440 0.9294 -0.1085 0.0129  0.0274  322 ASN B OD1 
6775 N ND2 . ASN B 322 ? 0.7906 0.7472 0.8338 -0.1040 0.0103  0.0105  322 ASN B ND2 
6776 N N   . ALA B 323 ? 0.3881 0.3610 0.4249 -0.0808 0.0183  0.0168  323 ALA B N   
6777 C CA  . ALA B 323 ? 0.4612 0.4429 0.4941 -0.0754 0.0182  0.0120  323 ALA B CA  
6778 C C   . ALA B 323 ? 0.4559 0.4343 0.4876 -0.0802 0.0153  0.0037  323 ALA B C   
6779 O O   . ALA B 323 ? 0.3474 0.3228 0.3742 -0.0754 0.0150  -0.0028 323 ALA B O   
6780 C CB  . ALA B 323 ? 0.4952 0.4962 0.5301 -0.0735 0.0195  0.0183  323 ALA B CB  
6781 N N   . GLU B 324 ? 0.4142 0.3936 0.4502 -0.0897 0.0128  0.0041  324 GLU B N   
6782 C CA  . GLU B 324 ? 0.4624 0.4380 0.4962 -0.0940 0.0096  -0.0041 324 GLU B CA  
6783 C C   . GLU B 324 ? 0.4522 0.4086 0.4806 -0.0921 0.0090  -0.0115 324 GLU B C   
6784 O O   . GLU B 324 ? 0.3946 0.3484 0.4182 -0.0901 0.0080  -0.0191 324 GLU B O   
6785 C CB  . GLU B 324 ? 0.5831 0.5624 0.6225 -0.1050 0.0063  -0.0020 324 GLU B CB  
6786 C CG  . GLU B 324 ? 0.6852 0.6579 0.7212 -0.1099 0.0024  -0.0109 324 GLU B CG  
6787 C CD  . GLU B 324 ? 0.8011 0.7889 0.8358 -0.1082 0.0018  -0.0136 324 GLU B CD  
6788 O OE1 . GLU B 324 ? 0.8369 0.8419 0.8757 -0.1072 0.0031  -0.0074 324 GLU B OE1 
6789 O OE2 . GLU B 324 ? 0.8583 0.8408 0.8876 -0.1075 0.0001  -0.0218 324 GLU B OE2 
6790 N N   . ASP B 325 ? 0.4250 0.3684 0.4539 -0.0923 0.0097  -0.0091 325 ASP B N   
6791 C CA  . ASP B 325 ? 0.4774 0.4026 0.5010 -0.0895 0.0093  -0.0158 325 ASP B CA  
6792 C C   . ASP B 325 ? 0.3708 0.2968 0.3900 -0.0794 0.0119  -0.0190 325 ASP B C   
6793 O O   . ASP B 325 ? 0.3449 0.2634 0.3594 -0.0765 0.0115  -0.0263 325 ASP B O   
6794 C CB  . ASP B 325 ? 0.5649 0.4759 0.5899 -0.0915 0.0094  -0.0119 325 ASP B CB  
6795 C CG  . ASP B 325 ? 0.7616 0.6668 0.7899 -0.1025 0.0057  -0.0104 325 ASP B CG  
6796 O OD1 . ASP B 325 ? 0.8346 0.7340 0.8601 -0.1070 0.0022  -0.0172 325 ASP B OD1 
6797 O OD2 . ASP B 325 ? 0.8195 0.7260 0.8532 -0.1067 0.0060  -0.0021 325 ASP B OD2 
6798 N N   . ALA B 326 ? 0.3589 0.2942 0.3795 -0.0738 0.0144  -0.0135 326 ALA B N   
6799 C CA  . ALA B 326 ? 0.4038 0.3401 0.4207 -0.0649 0.0160  -0.0158 326 ALA B CA  
6800 C C   . ALA B 326 ? 0.4133 0.3583 0.4278 -0.0637 0.0151  -0.0210 326 ALA B C   
6801 O O   . ALA B 326 ? 0.3729 0.3140 0.3839 -0.0591 0.0155  -0.0260 326 ALA B O   
6802 C CB  . ALA B 326 ? 0.3313 0.2750 0.3492 -0.0595 0.0179  -0.0087 326 ALA B CB  
6803 N N   . VAL B 327 ? 0.3197 0.2771 0.3360 -0.0678 0.0140  -0.0194 327 VAL B N   
6804 C CA  . VAL B 327 ? 0.3286 0.2944 0.3423 -0.0666 0.0131  -0.0239 327 VAL B CA  
6805 C C   . VAL B 327 ? 0.3424 0.2997 0.3531 -0.0695 0.0115  -0.0317 327 VAL B C   
6806 O O   . VAL B 327 ? 0.3738 0.3313 0.3808 -0.0655 0.0118  -0.0365 327 VAL B O   
6807 C CB  . VAL B 327 ? 0.3580 0.3391 0.3744 -0.0702 0.0121  -0.0202 327 VAL B CB  
6808 C CG1 . VAL B 327 ? 0.2896 0.2771 0.3032 -0.0710 0.0105  -0.0257 327 VAL B CG1 
6809 C CG2 . VAL B 327 ? 0.3237 0.3142 0.3405 -0.0643 0.0139  -0.0138 327 VAL B CG2 
6810 N N   . ARG B 328 ? 0.3584 0.3083 0.3702 -0.0765 0.0097  -0.0329 328 ARG B N   
6811 C CA  . ARG B 328 ? 0.4167 0.3561 0.4242 -0.0786 0.0079  -0.0407 328 ARG B CA  
6812 C C   . ARG B 328 ? 0.3769 0.3049 0.3804 -0.0715 0.0099  -0.0444 328 ARG B C   
6813 O O   . ARG B 328 ? 0.3535 0.2790 0.3522 -0.0688 0.0100  -0.0507 328 ARG B O   
6814 C CB  . ARG B 328 ? 0.4285 0.3586 0.4375 -0.0871 0.0050  -0.0407 328 ARG B CB  
6815 C CG  . ARG B 328 ? 0.4883 0.4015 0.4912 -0.0875 0.0032  -0.0485 328 ARG B CG  
6816 C CD  . ARG B 328 ? 0.5266 0.4312 0.5300 -0.0972 -0.0012 -0.0493 328 ARG B CD  
6817 N NE  . ARG B 328 ? 0.6158 0.5280 0.6272 -0.1037 -0.0020 -0.0408 328 ARG B NE  
6818 C CZ  . ARG B 328 ? 0.5778 0.4817 0.5926 -0.1057 -0.0016 -0.0354 328 ARG B CZ  
6819 N NH1 . ARG B 328 ? 0.5326 0.4194 0.5431 -0.1016 -0.0007 -0.0381 328 ARG B NH1 
6820 N NH2 . ARG B 328 ? 0.5349 0.4480 0.5572 -0.1116 -0.0020 -0.0271 328 ARG B NH2 
6821 N N   . ASP B 329 ? 0.4062 0.3280 0.4114 -0.0682 0.0118  -0.0403 329 ASP B N   
6822 C CA  . ASP B 329 ? 0.3761 0.2882 0.3784 -0.0612 0.0136  -0.0430 329 ASP B CA  
6823 C C   . ASP B 329 ? 0.3222 0.2438 0.3234 -0.0546 0.0152  -0.0441 329 ASP B C   
6824 O O   . ASP B 329 ? 0.3179 0.2357 0.3158 -0.0505 0.0161  -0.0490 329 ASP B O   
6825 C CB  . ASP B 329 ? 0.3995 0.3044 0.4044 -0.0590 0.0150  -0.0375 329 ASP B CB  
6826 C CG  . ASP B 329 ? 0.4076 0.3038 0.4101 -0.0512 0.0169  -0.0398 329 ASP B CG  
6827 O OD1 . ASP B 329 ? 0.4770 0.3602 0.4759 -0.0507 0.0166  -0.0446 329 ASP B OD1 
6828 O OD2 . ASP B 329 ? 0.3951 0.2974 0.3991 -0.0454 0.0185  -0.0367 329 ASP B OD2 
6829 N N   . PHE B 330 ? 0.3825 0.3164 0.3863 -0.0534 0.0155  -0.0392 330 PHE B N   
6830 C CA  . PHE B 330 ? 0.3070 0.2495 0.3098 -0.0480 0.0162  -0.0395 330 PHE B CA  
6831 C C   . PHE B 330 ? 0.3787 0.3260 0.3785 -0.0493 0.0154  -0.0450 330 PHE B C   
6832 O O   . PHE B 330 ? 0.3405 0.2881 0.3383 -0.0449 0.0164  -0.0479 330 PHE B O   
6833 C CB  . PHE B 330 ? 0.3347 0.2879 0.3395 -0.0469 0.0159  -0.0335 330 PHE B CB  
6834 C CG  . PHE B 330 ? 0.3384 0.2980 0.3419 -0.0411 0.0158  -0.0327 330 PHE B CG  
6835 C CD1 . PHE B 330 ? 0.3064 0.2623 0.3103 -0.0356 0.0163  -0.0301 330 PHE B CD1 
6836 C CD2 . PHE B 330 ? 0.3686 0.3379 0.3704 -0.0415 0.0146  -0.0341 330 PHE B CD2 
6837 C CE1 . PHE B 330 ? 0.3134 0.2746 0.3163 -0.0310 0.0153  -0.0291 330 PHE B CE1 
6838 C CE2 . PHE B 330 ? 0.3625 0.3367 0.3630 -0.0368 0.0139  -0.0330 330 PHE B CE2 
6839 C CZ  . PHE B 330 ? 0.2879 0.2579 0.2890 -0.0318 0.0140  -0.0305 330 PHE B CZ  
6840 N N   . ILE B 331 ? 0.4052 0.3570 0.4048 -0.0553 0.0137  -0.0461 331 ILE B N   
6841 C CA  . ILE B 331 ? 0.4472 0.4042 0.4434 -0.0566 0.0127  -0.0510 331 ILE B CA  
6842 C C   . ILE B 331 ? 0.3459 0.2922 0.3378 -0.0557 0.0131  -0.0576 331 ILE B C   
6843 O O   . ILE B 331 ? 0.3463 0.2957 0.3349 -0.0527 0.0138  -0.0614 331 ILE B O   
6844 C CB  . ILE B 331 ? 0.5101 0.4746 0.5075 -0.0634 0.0103  -0.0503 331 ILE B CB  
6845 C CG1 . ILE B 331 ? 0.4333 0.4099 0.4340 -0.0626 0.0103  -0.0439 331 ILE B CG1 
6846 C CG2 . ILE B 331 ? 0.5321 0.5007 0.5253 -0.0650 0.0089  -0.0560 331 ILE B CG2 
6847 C CD1 . ILE B 331 ? 0.3897 0.3755 0.3884 -0.0578 0.0106  -0.0435 331 ILE B CD1 
6848 N N   . GLY B 332 ? 0.3669 0.3003 0.3583 -0.0579 0.0126  -0.0589 332 GLY B N   
6849 C CA  . GLY B 332 ? 0.3707 0.2924 0.3567 -0.0557 0.0130  -0.0653 332 GLY B CA  
6850 C C   . GLY B 332 ? 0.3818 0.3032 0.3669 -0.0473 0.0161  -0.0659 332 GLY B C   
6851 O O   . GLY B 332 ? 0.4328 0.3528 0.4133 -0.0439 0.0171  -0.0710 332 GLY B O   
6852 N N   . ARG B 333 ? 0.3095 0.2330 0.2992 -0.0438 0.0175  -0.0605 333 ARG B N   
6853 C CA  . ARG B 333 ? 0.3903 0.3153 0.3804 -0.0364 0.0200  -0.0601 333 ARG B CA  
6854 C C   . ARG B 333 ? 0.3820 0.3200 0.3718 -0.0346 0.0204  -0.0604 333 ARG B C   
6855 O O   . ARG B 333 ? 0.3818 0.3212 0.3700 -0.0299 0.0222  -0.0627 333 ARG B O   
6856 C CB  . ARG B 333 ? 0.4079 0.3325 0.4028 -0.0336 0.0206  -0.0540 333 ARG B CB  
6857 C CG  . ARG B 333 ? 0.3651 0.2757 0.3599 -0.0331 0.0210  -0.0536 333 ARG B CG  
6858 C CD  . ARG B 333 ? 0.3366 0.2481 0.3357 -0.0311 0.0213  -0.0471 333 ARG B CD  
6859 N NE  . ARG B 333 ? 0.4158 0.3149 0.4152 -0.0323 0.0213  -0.0455 333 ARG B NE  
6860 C CZ  . ARG B 333 ? 0.4492 0.3374 0.4474 -0.0278 0.0225  -0.0466 333 ARG B CZ  
6861 N NH1 . ARG B 333 ? 0.4281 0.3171 0.4252 -0.0216 0.0241  -0.0495 333 ARG B NH1 
6862 N NH2 . ARG B 333 ? 0.5710 0.4476 0.5693 -0.0293 0.0222  -0.0446 333 ARG B NH2 
6863 N N   . LEU B 334 ? 0.3497 0.2976 0.3410 -0.0381 0.0187  -0.0578 334 LEU B N   
6864 C CA  . LEU B 334 ? 0.3291 0.2882 0.3193 -0.0371 0.0186  -0.0583 334 LEU B CA  
6865 C C   . LEU B 334 ? 0.3828 0.3410 0.3677 -0.0380 0.0189  -0.0645 334 LEU B C   
6866 O O   . LEU B 334 ? 0.4261 0.3899 0.4093 -0.0347 0.0202  -0.0658 334 LEU B O   
6867 C CB  . LEU B 334 ? 0.2660 0.2344 0.2576 -0.0406 0.0165  -0.0548 334 LEU B CB  
6868 C CG  . LEU B 334 ? 0.3063 0.2773 0.3015 -0.0386 0.0159  -0.0487 334 LEU B CG  
6869 C CD1 . LEU B 334 ? 0.3433 0.3234 0.3384 -0.0412 0.0139  -0.0459 334 LEU B CD1 
6870 C CD2 . LEU B 334 ? 0.3555 0.3285 0.3521 -0.0331 0.0165  -0.0466 334 LEU B CD2 
6871 N N   . LYS B 335 ? 0.3601 0.3112 0.3421 -0.0427 0.0174  -0.0681 335 LYS B N   
6872 C CA  . LYS B 335 ? 0.4193 0.3681 0.3948 -0.0433 0.0170  -0.0746 335 LYS B CA  
6873 C C   . LYS B 335 ? 0.4621 0.4047 0.4342 -0.0367 0.0198  -0.0781 335 LYS B C   
6874 O O   . LYS B 335 ? 0.4569 0.4040 0.4247 -0.0338 0.0211  -0.0812 335 LYS B O   
6875 C CB  . LYS B 335 ? 0.4435 0.3837 0.4167 -0.0498 0.0140  -0.0777 335 LYS B CB  
6876 C CG  . LYS B 335 ? 0.4783 0.4142 0.4437 -0.0510 0.0126  -0.0849 335 LYS B CG  
6877 C CD  . LYS B 335 ? 0.5055 0.4324 0.4695 -0.0585 0.0086  -0.0871 335 LYS B CD  
6878 C CE  . LYS B 335 ? 0.6106 0.5233 0.5655 -0.0575 0.0072  -0.0949 335 LYS B CE  
6879 N NZ  . LYS B 335 ? 0.6940 0.6127 0.6420 -0.0555 0.0071  -0.0999 335 LYS B NZ  
6880 N N   . LYS B 336 ? 0.4166 0.3498 0.3904 -0.0336 0.0211  -0.0770 336 LYS B N   
6881 C CA  . LYS B 336 ? 0.4703 0.3976 0.4408 -0.0266 0.0240  -0.0800 336 LYS B CA  
6882 C C   . LYS B 336 ? 0.4777 0.4172 0.4517 -0.0210 0.0268  -0.0767 336 LYS B C   
6883 O O   . LYS B 336 ? 0.4643 0.4061 0.4346 -0.0160 0.0292  -0.0796 336 LYS B O   
6884 C CB  . LYS B 336 ? 0.4932 0.4070 0.4647 -0.0247 0.0243  -0.0794 336 LYS B CB  
6885 C CG  . LYS B 336 ? 0.6062 0.5067 0.5740 -0.0307 0.0212  -0.0826 336 LYS B CG  
6886 C CD  . LYS B 336 ? 0.7255 0.6122 0.6945 -0.0294 0.0213  -0.0811 336 LYS B CD  
6887 C CE  . LYS B 336 ? 0.7815 0.6554 0.7478 -0.0367 0.0175  -0.0832 336 LYS B CE  
6888 N NZ  . LYS B 336 ? 0.7606 0.6291 0.7325 -0.0394 0.0169  -0.0774 336 LYS B NZ  
6889 N N   . ILE B 337 ? 0.4218 0.3692 0.4027 -0.0217 0.0263  -0.0704 337 ILE B N   
6890 C CA  . ILE B 337 ? 0.3301 0.2897 0.3146 -0.0180 0.0278  -0.0667 337 ILE B CA  
6891 C C   . ILE B 337 ? 0.3651 0.3339 0.3459 -0.0193 0.0278  -0.0688 337 ILE B C   
6892 O O   . ILE B 337 ? 0.3790 0.3547 0.3595 -0.0150 0.0302  -0.0687 337 ILE B O   
6893 C CB  . ILE B 337 ? 0.3060 0.2708 0.2969 -0.0195 0.0259  -0.0601 337 ILE B CB  
6894 C CG1 . ILE B 337 ? 0.3872 0.3437 0.3816 -0.0172 0.0262  -0.0576 337 ILE B CG1 
6895 C CG2 . ILE B 337 ? 0.3813 0.3581 0.3756 -0.0172 0.0262  -0.0562 337 ILE B CG2 
6896 C CD1 . ILE B 337 ? 0.3687 0.3280 0.3673 -0.0192 0.0237  -0.0520 337 ILE B CD1 
6897 N N   . HIS B 338 ? 0.3366 0.3066 0.3150 -0.0250 0.0252  -0.0703 338 HIS B N   
6898 C CA  . HIS B 338 ? 0.3976 0.3762 0.3721 -0.0265 0.0248  -0.0723 338 HIS B CA  
6899 C C   . HIS B 338 ? 0.4742 0.4494 0.4415 -0.0230 0.0270  -0.0783 338 HIS B C   
6900 O O   . HIS B 338 ? 0.4613 0.4452 0.4265 -0.0204 0.0287  -0.0785 338 HIS B O   
6901 C CB  . HIS B 338 ? 0.3800 0.3594 0.3531 -0.0331 0.0214  -0.0730 338 HIS B CB  
6902 C CG  . HIS B 338 ? 0.5303 0.5187 0.4995 -0.0348 0.0205  -0.0746 338 HIS B CG  
6903 N ND1 . HIS B 338 ? 0.5847 0.5711 0.5487 -0.0390 0.0184  -0.0793 338 HIS B ND1 
6904 C CD2 . HIS B 338 ? 0.5512 0.5505 0.5210 -0.0332 0.0211  -0.0718 338 HIS B CD2 
6905 C CE1 . HIS B 338 ? 0.5933 0.5892 0.5544 -0.0393 0.0180  -0.0796 338 HIS B CE1 
6906 N NE2 . HIS B 338 ? 0.5458 0.5495 0.5104 -0.0359 0.0197  -0.0749 338 HIS B NE2 
6907 N N   . GLU B 339 ? 0.5099 0.4720 0.4729 -0.0227 0.0268  -0.0831 339 GLU B N   
6908 C CA  . GLU B 339 ? 0.5604 0.5172 0.5148 -0.0186 0.0284  -0.0896 339 GLU B CA  
6909 C C   . GLU B 339 ? 0.5614 0.5192 0.5164 -0.0100 0.0328  -0.0888 339 GLU B C   
6910 O O   . GLU B 339 ? 0.5856 0.5433 0.5336 -0.0050 0.0351  -0.0930 339 GLU B O   
6911 C CB  . GLU B 339 ? 0.5842 0.5247 0.5327 -0.0213 0.0259  -0.0953 339 GLU B CB  
6912 C CG  . GLU B 339 ? 0.6308 0.5698 0.5793 -0.0301 0.0214  -0.0961 339 GLU B CG  
6913 C CD  . GLU B 339 ? 0.7066 0.6286 0.6518 -0.0334 0.0186  -0.0998 339 GLU B CD  
6914 O OE1 . GLU B 339 ? 0.6779 0.5898 0.6234 -0.0292 0.0202  -0.0999 339 GLU B OE1 
6915 O OE2 . GLU B 339 ? 0.7150 0.6338 0.6577 -0.0402 0.0145  -0.1024 339 GLU B OE2 
6916 N N   . SER B 340 ? 0.5104 0.4695 0.4733 -0.0080 0.0340  -0.0833 340 SER B N   
6917 C CA  . SER B 340 ? 0.5462 0.5058 0.5106 0.0001  0.0378  -0.0822 340 SER B CA  
6918 C C   . SER B 340 ? 0.5463 0.5222 0.5147 0.0037  0.0406  -0.0777 340 SER B C   
6919 O O   . SER B 340 ? 0.5403 0.5194 0.5098 0.0109  0.0443  -0.0767 340 SER B O   
6920 C CB  . SER B 340 ? 0.6084 0.5622 0.5797 0.0007  0.0374  -0.0782 340 SER B CB  
6921 O OG  . SER B 340 ? 0.6907 0.6558 0.6708 -0.0009 0.0368  -0.0710 340 SER B OG  
6922 N N   . VAL B 341 ? 0.5438 0.5304 0.5146 -0.0009 0.0389  -0.0746 341 VAL B N   
6923 C CA  . VAL B 341 ? 0.5105 0.5123 0.4863 0.0013  0.0408  -0.0691 341 VAL B CA  
6924 C C   . VAL B 341 ? 0.4907 0.5001 0.4607 -0.0003 0.0410  -0.0711 341 VAL B C   
6925 O O   . VAL B 341 ? 0.4585 0.4637 0.4233 -0.0052 0.0382  -0.0749 341 VAL B O   
6926 C CB  . VAL B 341 ? 0.5202 0.5280 0.5053 -0.0024 0.0382  -0.0618 341 VAL B CB  
6927 C CG1 . VAL B 341 ? 0.5054 0.5084 0.4967 0.0007  0.0386  -0.0589 341 VAL B CG1 
6928 C CG2 . VAL B 341 ? 0.4670 0.4712 0.4508 -0.0095 0.0339  -0.0625 341 VAL B CG2 
6929 N N   . ASP B 342 ? 0.5007 0.5223 0.4722 0.0038  0.0442  -0.0679 342 ASP B N   
6930 C CA  . ASP B 342 ? 0.5439 0.5747 0.5105 0.0031  0.0448  -0.0685 342 ASP B CA  
6931 C C   . ASP B 342 ? 0.5399 0.5798 0.5117 -0.0027 0.0417  -0.0626 342 ASP B C   
6932 O O   . ASP B 342 ? 0.5806 0.6260 0.5477 -0.0048 0.0411  -0.0634 342 ASP B O   
6933 C CB  . ASP B 342 ? 0.7081 0.7486 0.6738 0.0106  0.0501  -0.0669 342 ASP B CB  
6934 C CG  . ASP B 342 ? 0.8862 0.9349 0.8630 0.0135  0.0519  -0.0592 342 ASP B CG  
6935 O OD1 . ASP B 342 ? 0.9096 0.9503 0.8904 0.0147  0.0514  -0.0591 342 ASP B OD1 
6936 O OD2 . ASP B 342 ? 0.9678 1.0309 0.9494 0.0144  0.0537  -0.0529 342 ASP B OD2 
6937 N N   . PHE B 343 ? 0.4607 0.5015 0.4412 -0.0050 0.0395  -0.0569 343 PHE B N   
6938 C CA  . PHE B 343 ? 0.3919 0.4392 0.3769 -0.0099 0.0360  -0.0512 343 PHE B CA  
6939 C C   . PHE B 343 ? 0.4164 0.4549 0.4009 -0.0149 0.0316  -0.0528 343 PHE B C   
6940 O O   . PHE B 343 ? 0.4822 0.5105 0.4635 -0.0152 0.0315  -0.0577 343 PHE B O   
6941 C CB  . PHE B 343 ? 0.3053 0.3600 0.2998 -0.0086 0.0360  -0.0433 343 PHE B CB  
6942 C CG  . PHE B 343 ? 0.3052 0.3530 0.3050 -0.0064 0.0359  -0.0426 343 PHE B CG  
6943 C CD1 . PHE B 343 ? 0.2938 0.3402 0.2937 -0.0004 0.0402  -0.0446 343 PHE B CD1 
6944 C CD2 . PHE B 343 ? 0.3237 0.3664 0.3275 -0.0097 0.0317  -0.0398 343 PHE B CD2 
6945 C CE1 . PHE B 343 ? 0.3097 0.3496 0.3141 0.0018  0.0400  -0.0438 343 PHE B CE1 
6946 C CE2 . PHE B 343 ? 0.3725 0.4089 0.3807 -0.0075 0.0316  -0.0390 343 PHE B CE2 
6947 C CZ  . PHE B 343 ? 0.2622 0.2973 0.2710 -0.0019 0.0358  -0.0409 343 PHE B CZ  
6948 N N   . GLN B 344 ? 0.3411 0.3834 0.3284 -0.0186 0.0280  -0.0482 344 GLN B N   
6949 C CA  . GLN B 344 ? 0.3593 0.3953 0.3465 -0.0225 0.0241  -0.0485 344 GLN B CA  
6950 C C   . GLN B 344 ? 0.2984 0.3302 0.2919 -0.0216 0.0226  -0.0446 344 GLN B C   
6951 O O   . GLN B 344 ? 0.2655 0.3015 0.2634 -0.0219 0.0203  -0.0389 344 GLN B O   
6952 C CB  . GLN B 344 ? 0.4156 0.4572 0.4008 -0.0259 0.0208  -0.0460 344 GLN B CB  
6953 C CG  . GLN B 344 ? 0.4128 0.4589 0.3913 -0.0269 0.0218  -0.0497 344 GLN B CG  
6954 C CD  . GLN B 344 ? 0.3746 0.4246 0.3509 -0.0302 0.0181  -0.0476 344 GLN B CD  
6955 O OE1 . GLN B 344 ? 0.3150 0.3634 0.2870 -0.0327 0.0166  -0.0512 344 GLN B OE1 
6956 N NE2 . GLN B 344 ? 0.3288 0.3837 0.3082 -0.0303 0.0162  -0.0416 344 GLN B NE2 
6957 N N   . PRO B 345 ? 0.3219 0.3447 0.3157 -0.0207 0.0234  -0.0472 345 PRO B N   
6958 C CA  . PRO B 345 ? 0.3364 0.3553 0.3359 -0.0192 0.0222  -0.0434 345 PRO B CA  
6959 C C   . PRO B 345 ? 0.3096 0.3273 0.3099 -0.0220 0.0178  -0.0401 345 PRO B C   
6960 O O   . PRO B 345 ? 0.3408 0.3578 0.3372 -0.0250 0.0161  -0.0418 345 PRO B O   
6961 C CB  . PRO B 345 ? 0.2916 0.3004 0.2896 -0.0179 0.0242  -0.0477 345 PRO B CB  
6962 C CG  . PRO B 345 ? 0.3138 0.3199 0.3056 -0.0210 0.0241  -0.0530 345 PRO B CG  
6963 C CD  . PRO B 345 ? 0.3348 0.3500 0.3235 -0.0214 0.0248  -0.0536 345 PRO B CD  
6964 N N   . VAL B 346 ? 0.2837 0.3013 0.2889 -0.0206 0.0157  -0.0352 346 VAL B N   
6965 C CA  . VAL B 346 ? 0.2249 0.2390 0.2300 -0.0217 0.0114  -0.0322 346 VAL B CA  
6966 C C   . VAL B 346 ? 0.2048 0.2109 0.2118 -0.0198 0.0119  -0.0322 346 VAL B C   
6967 O O   . VAL B 346 ? 0.3458 0.3509 0.3572 -0.0170 0.0132  -0.0309 346 VAL B O   
6968 C CB  . VAL B 346 ? 0.3030 0.3216 0.3110 -0.0217 0.0076  -0.0266 346 VAL B CB  
6969 C CG1 . VAL B 346 ? 0.3390 0.3523 0.3450 -0.0219 0.0029  -0.0241 346 VAL B CG1 
6970 C CG2 . VAL B 346 ? 0.2766 0.3029 0.2826 -0.0237 0.0073  -0.0261 346 VAL B CG2 
6971 N N   . VAL B 347 ? 0.2731 0.2741 0.2772 -0.0212 0.0108  -0.0333 347 VAL B N   
6972 C CA  . VAL B 347 ? 0.3032 0.2963 0.3084 -0.0198 0.0117  -0.0335 347 VAL B CA  
6973 C C   . VAL B 347 ? 0.2827 0.2734 0.2872 -0.0190 0.0081  -0.0296 347 VAL B C   
6974 O O   . VAL B 347 ? 0.3338 0.3248 0.3347 -0.0207 0.0067  -0.0297 347 VAL B O   
6975 C CB  . VAL B 347 ? 0.3286 0.3174 0.3310 -0.0222 0.0141  -0.0379 347 VAL B CB  
6976 C CG1 . VAL B 347 ? 0.2712 0.2514 0.2749 -0.0210 0.0149  -0.0373 347 VAL B CG1 
6977 C CG2 . VAL B 347 ? 0.3200 0.3101 0.3214 -0.0221 0.0172  -0.0423 347 VAL B CG2 
6978 N N   . PHE B 348 ? 0.2045 0.1930 0.2122 -0.0161 0.0064  -0.0262 348 PHE B N   
6979 C CA  . PHE B 348 ? 0.2322 0.2174 0.2382 -0.0146 0.0025  -0.0228 348 PHE B CA  
6980 C C   . PHE B 348 ? 0.2338 0.2120 0.2394 -0.0132 0.0041  -0.0227 348 PHE B C   
6981 O O   . PHE B 348 ? 0.3094 0.2838 0.3184 -0.0114 0.0061  -0.0228 348 PHE B O   
6982 C CB  . PHE B 348 ? 0.2517 0.2377 0.2606 -0.0125 -0.0012 -0.0189 348 PHE B CB  
6983 C CG  . PHE B 348 ? 0.2569 0.2465 0.2633 -0.0138 -0.0055 -0.0170 348 PHE B CG  
6984 C CD1 . PHE B 348 ? 0.2454 0.2417 0.2522 -0.0163 -0.0044 -0.0182 348 PHE B CD1 
6985 C CD2 . PHE B 348 ? 0.2511 0.2368 0.2538 -0.0121 -0.0109 -0.0141 348 PHE B CD2 
6986 C CE1 . PHE B 348 ? 0.2504 0.2494 0.2548 -0.0176 -0.0086 -0.0161 348 PHE B CE1 
6987 C CE2 . PHE B 348 ? 0.3487 0.3361 0.3483 -0.0131 -0.0153 -0.0125 348 PHE B CE2 
6988 C CZ  . PHE B 348 ? 0.2962 0.2901 0.2968 -0.0161 -0.0143 -0.0133 348 PHE B CZ  
6989 N N   . VAL B 349 ? 0.2542 0.2313 0.2557 -0.0137 0.0032  -0.0220 349 VAL B N   
6990 C CA  . VAL B 349 ? 0.2465 0.2182 0.2473 -0.0125 0.0043  -0.0207 349 VAL B CA  
6991 C C   . VAL B 349 ? 0.2919 0.2618 0.2894 -0.0088 0.0003  -0.0168 349 VAL B C   
6992 O O   . VAL B 349 ? 0.2951 0.2678 0.2880 -0.0084 -0.0020 -0.0159 349 VAL B O   
6993 C CB  . VAL B 349 ? 0.2751 0.2482 0.2741 -0.0158 0.0065  -0.0222 349 VAL B CB  
6994 C CG1 . VAL B 349 ? 0.2731 0.2409 0.2724 -0.0151 0.0081  -0.0201 349 VAL B CG1 
6995 C CG2 . VAL B 349 ? 0.3181 0.2928 0.3188 -0.0195 0.0092  -0.0267 349 VAL B CG2 
6996 N N   . VAL B 350 ? 0.2838 0.2489 0.2831 -0.0056 -0.0009 -0.0146 350 VAL B N   
6997 C CA  . VAL B 350 ? 0.3026 0.2651 0.2983 -0.0017 -0.0056 -0.0113 350 VAL B CA  
6998 C C   . VAL B 350 ? 0.3194 0.2759 0.3145 0.0014  -0.0046 -0.0091 350 VAL B C   
6999 O O   . VAL B 350 ? 0.3288 0.2821 0.3284 0.0020  -0.0027 -0.0091 350 VAL B O   
7000 C CB  . VAL B 350 ? 0.2798 0.2428 0.2782 -0.0008 -0.0096 -0.0102 350 VAL B CB  
7001 C CG1 . VAL B 350 ? 0.2403 0.1991 0.2335 0.0029  -0.0155 -0.0072 350 VAL B CG1 
7002 C CG2 . VAL B 350 ? 0.3031 0.2724 0.3027 -0.0043 -0.0099 -0.0119 350 VAL B CG2 
7003 N N   . LEU B 351 ? 0.2596 0.2148 0.2489 0.0039  -0.0057 -0.0070 351 LEU B N   
7004 C CA  . LEU B 351 ? 0.3076 0.2576 0.2956 0.0073  -0.0048 -0.0042 351 LEU B CA  
7005 C C   . LEU B 351 ? 0.3184 0.2680 0.2983 0.0116  -0.0076 -0.0016 351 LEU B C   
7006 O O   . LEU B 351 ? 0.3554 0.3085 0.3309 0.0117  -0.0098 -0.0023 351 LEU B O   
7007 C CB  . LEU B 351 ? 0.2436 0.1929 0.2350 0.0043  0.0007  -0.0047 351 LEU B CB  
7008 C CG  . LEU B 351 ? 0.3569 0.3115 0.3466 0.0012  0.0030  -0.0049 351 LEU B CG  
7009 C CD1 . LEU B 351 ? 0.3495 0.3017 0.3405 0.0003  0.0066  -0.0025 351 LEU B CD1 
7010 C CD2 . LEU B 351 ? 0.3702 0.3293 0.3632 -0.0042 0.0046  -0.0091 351 LEU B CD2 
7011 N N   . ASN B 352 ? 0.2379 0.1829 0.2151 0.0157  -0.0075 0.0015  352 ASN B N   
7012 C CA  . ASN B 352 ? 0.3004 0.2453 0.2689 0.0207  -0.0094 0.0041  352 ASN B CA  
7013 C C   . ASN B 352 ? 0.3154 0.2673 0.2830 0.0185  -0.0055 0.0045  352 ASN B C   
7014 O O   . ASN B 352 ? 0.3145 0.2691 0.2881 0.0137  -0.0009 0.0040  352 ASN B O   
7015 C CB  . ASN B 352 ? 0.3018 0.2412 0.2676 0.0256  -0.0092 0.0077  352 ASN B CB  
7016 C CG  . ASN B 352 ? 0.4362 0.3694 0.3980 0.0302  -0.0154 0.0082  352 ASN B CG  
7017 O OD1 . ASN B 352 ? 0.4165 0.3467 0.3839 0.0291  -0.0166 0.0076  352 ASN B OD1 
7018 N ND2 . ASN B 352 ? 0.3605 0.2918 0.3122 0.0357  -0.0197 0.0092  352 ASN B ND2 
7019 N N   . GLY B 353 ? 0.2971 0.2519 0.2571 0.0222  -0.0078 0.0052  353 GLY B N   
7020 C CA  . GLY B 353 ? 0.2849 0.2481 0.2439 0.0209  -0.0048 0.0059  353 GLY B CA  
7021 C C   . GLY B 353 ? 0.3059 0.2720 0.2604 0.0253  -0.0023 0.0105  353 GLY B C   
7022 O O   . GLY B 353 ? 0.2826 0.2572 0.2369 0.0244  0.0005  0.0119  353 GLY B O   
7023 N N   . GLU B 354 ? 0.2556 0.2157 0.2066 0.0304  -0.0030 0.0134  354 GLU B N   
7024 C CA  . GLU B 354 ? 0.3114 0.2749 0.2570 0.0357  -0.0005 0.0184  354 GLU B CA  
7025 C C   . GLU B 354 ? 0.2977 0.2585 0.2474 0.0351  0.0031  0.0221  354 GLU B C   
7026 O O   . GLU B 354 ? 0.3676 0.3328 0.3143 0.0386  0.0061  0.0271  354 GLU B O   
7027 C CB  . GLU B 354 ? 0.3731 0.3320 0.3061 0.0453  -0.0055 0.0191  354 GLU B CB  
7028 C CG  . GLU B 354 ? 0.3446 0.2930 0.2746 0.0492  -0.0091 0.0194  354 GLU B CG  
7029 C CD  . GLU B 354 ? 0.3686 0.3103 0.3013 0.0463  -0.0144 0.0151  354 GLU B CD  
7030 O OE1 . GLU B 354 ? 0.3914 0.3268 0.3158 0.0511  -0.0209 0.0138  354 GLU B OE1 
7031 O OE2 . GLU B 354 ? 0.3593 0.3019 0.3021 0.0393  -0.0123 0.0131  354 GLU B OE2 
7032 N N   . ASN B 355 ? 0.2694 0.2238 0.2259 0.0310  0.0033  0.0203  355 ASN B N   
7033 C CA  . ASN B 355 ? 0.2905 0.2399 0.2492 0.0318  0.0057  0.0239  355 ASN B CA  
7034 C C   . ASN B 355 ? 0.2777 0.2295 0.2452 0.0246  0.0110  0.0254  355 ASN B C   
7035 O O   . ASN B 355 ? 0.3375 0.2875 0.3056 0.0255  0.0138  0.0302  355 ASN B O   
7036 C CB  . ASN B 355 ? 0.2953 0.2352 0.2552 0.0330  0.0023  0.0215  355 ASN B CB  
7037 C CG  . ASN B 355 ? 0.3821 0.3180 0.3329 0.0403  -0.0036 0.0213  355 ASN B CG  
7038 O OD1 . ASN B 355 ? 0.3342 0.2714 0.2762 0.0466  -0.0042 0.0243  355 ASN B OD1 
7039 N ND2 . ASN B 355 ? 0.3477 0.2789 0.3001 0.0397  -0.0082 0.0178  355 ASN B ND2 
7040 N N   . CYS B 356 ? 0.2681 0.2229 0.2420 0.0174  0.0121  0.0217  356 CYS B N   
7041 C CA  . CYS B 356 ? 0.2567 0.2110 0.2383 0.0102  0.0160  0.0224  356 CYS B CA  
7042 C C   . CYS B 356 ? 0.3015 0.2654 0.2847 0.0072  0.0192  0.0268  356 CYS B C   
7043 O O   . CYS B 356 ? 0.3741 0.3367 0.3623 0.0026  0.0222  0.0301  356 CYS B O   
7044 C CB  . CYS B 356 ? 0.2792 0.2316 0.2663 0.0040  0.0154  0.0162  356 CYS B CB  
7045 S SG  . CYS B 356 ? 0.3209 0.2815 0.3061 0.0029  0.0130  0.0117  356 CYS B SG  
7046 N N   . TRP B 357 ? 0.3331 0.3064 0.3121 0.0098  0.0186  0.0275  357 TRP B N   
7047 C CA  . TRP B 357 ? 0.2994 0.2841 0.2817 0.0059  0.0215  0.0311  357 TRP B CA  
7048 C C   . TRP B 357 ? 0.3136 0.3015 0.2962 0.0075  0.0250  0.0392  357 TRP B C   
7049 O O   . TRP B 357 ? 0.3537 0.3481 0.3428 0.0012  0.0279  0.0430  357 TRP B O   
7050 C CB  . TRP B 357 ? 0.3240 0.3181 0.3011 0.0096  0.0199  0.0301  357 TRP B CB  
7051 C CG  . TRP B 357 ? 0.3695 0.3594 0.3452 0.0089  0.0162  0.0230  357 TRP B CG  
7052 C CD1 . TRP B 357 ? 0.3527 0.3392 0.3208 0.0155  0.0123  0.0206  357 TRP B CD1 
7053 C CD2 . TRP B 357 ? 0.3894 0.3775 0.3714 0.0013  0.0159  0.0177  357 TRP B CD2 
7054 N NE1 . TRP B 357 ? 0.3250 0.3087 0.2950 0.0119  0.0097  0.0147  357 TRP B NE1 
7055 C CE2 . TRP B 357 ? 0.3471 0.3321 0.3253 0.0037  0.0122  0.0128  357 TRP B CE2 
7056 C CE3 . TRP B 357 ? 0.4199 0.4083 0.4097 -0.0072 0.0181  0.0167  357 TRP B CE3 
7057 C CZ2 . TRP B 357 ? 0.2595 0.2431 0.2417 -0.0017 0.0113  0.0073  357 TRP B CZ2 
7058 C CZ3 . TRP B 357 ? 0.3945 0.3804 0.3873 -0.0121 0.0168  0.0105  357 TRP B CZ3 
7059 C CH2 . TRP B 357 ? 0.3724 0.3565 0.3614 -0.0091 0.0138  0.0061  357 TRP B CH2 
7060 N N   . GLU B 358 ? 0.3321 0.3159 0.3080 0.0156  0.0246  0.0423  358 GLU B N   
7061 C CA  . GLU B 358 ? 0.3141 0.3013 0.2898 0.0178  0.0282  0.0506  358 GLU B CA  
7062 C C   . GLU B 358 ? 0.3271 0.3085 0.3113 0.0100  0.0306  0.0530  358 GLU B C   
7063 O O   . GLU B 358 ? 0.3124 0.2987 0.2989 0.0089  0.0340  0.0606  358 GLU B O   
7064 C CB  . GLU B 358 ? 0.3596 0.3414 0.3255 0.0282  0.0267  0.0526  358 GLU B CB  
7065 C CG  . GLU B 358 ? 0.3349 0.3023 0.3004 0.0290  0.0239  0.0486  358 GLU B CG  
7066 C CD  . GLU B 358 ? 0.4332 0.3957 0.3879 0.0392  0.0200  0.0477  358 GLU B CD  
7067 O OE1 . GLU B 358 ? 0.4734 0.4293 0.4251 0.0435  0.0201  0.0508  358 GLU B OE1 
7068 O OE2 . GLU B 358 ? 0.3654 0.3299 0.3141 0.0429  0.0167  0.0441  358 GLU B OE2 
7069 N N   . TYR B 359 ? 0.2711 0.2420 0.2595 0.0050  0.0289  0.0471  359 TYR B N   
7070 C CA  . TYR B 359 ? 0.3721 0.3356 0.3675 -0.0024 0.0306  0.0485  359 TYR B CA  
7071 C C   . TYR B 359 ? 0.3412 0.3089 0.3441 -0.0124 0.0311  0.0466  359 TYR B C   
7072 O O   . TYR B 359 ? 0.3623 0.3241 0.3709 -0.0193 0.0322  0.0483  359 TYR B O   
7073 C CB  . TYR B 359 ? 0.4225 0.3714 0.4176 -0.0012 0.0286  0.0434  359 TYR B CB  
7074 C CG  . TYR B 359 ? 0.4415 0.3857 0.4297 0.0082  0.0273  0.0451  359 TYR B CG  
7075 C CD1 . TYR B 359 ? 0.4699 0.4107 0.4566 0.0112  0.0293  0.0518  359 TYR B CD1 
7076 C CD2 . TYR B 359 ? 0.4410 0.3840 0.4239 0.0139  0.0237  0.0402  359 TYR B CD2 
7077 C CE1 . TYR B 359 ? 0.5133 0.4496 0.4929 0.0201  0.0277  0.0532  359 TYR B CE1 
7078 C CE2 . TYR B 359 ? 0.4992 0.4374 0.4755 0.0222  0.0217  0.0416  359 TYR B CE2 
7079 C CZ  . TYR B 359 ? 0.5676 0.5025 0.5420 0.0255  0.0237  0.0479  359 TYR B CZ  
7080 O OH  . TYR B 359 ? 0.6534 0.5834 0.6206 0.0339  0.0212  0.0491  359 TYR B OH  
7081 N N   . TYR B 360 ? 0.2901 0.2672 0.2928 -0.0134 0.0300  0.0433  360 TYR B N   
7082 C CA  . TYR B 360 ? 0.3014 0.2841 0.3107 -0.0227 0.0302  0.0420  360 TYR B CA  
7083 C C   . TYR B 360 ? 0.3628 0.3588 0.3758 -0.0253 0.0329  0.0506  360 TYR B C   
7084 O O   . TYR B 360 ? 0.3191 0.3239 0.3279 -0.0183 0.0345  0.0561  360 TYR B O   
7085 C CB  . TYR B 360 ? 0.3281 0.3163 0.3356 -0.0225 0.0279  0.0355  360 TYR B CB  
7086 C CG  . TYR B 360 ? 0.3388 0.3166 0.3454 -0.0232 0.0254  0.0269  360 TYR B CG  
7087 C CD1 . TYR B 360 ? 0.3105 0.2793 0.3126 -0.0168 0.0241  0.0244  360 TYR B CD1 
7088 C CD2 . TYR B 360 ? 0.2935 0.2717 0.3036 -0.0301 0.0243  0.0216  360 TYR B CD2 
7089 C CE1 . TYR B 360 ? 0.3617 0.3232 0.3638 -0.0173 0.0221  0.0173  360 TYR B CE1 
7090 C CE2 . TYR B 360 ? 0.2678 0.2381 0.2769 -0.0302 0.0225  0.0142  360 TYR B CE2 
7091 C CZ  . TYR B 360 ? 0.3307 0.2933 0.3362 -0.0239 0.0216  0.0124  360 TYR B CZ  
7092 O OH  . TYR B 360 ? 0.2943 0.2509 0.2996 -0.0242 0.0202  0.0058  360 TYR B OH  
7093 N N   . GLU B 361 ? 0.2913 0.4198 0.4059 -0.0580 0.0744  0.0010  361 GLU B N   
7094 C CA  . GLU B 361 ? 0.3422 0.4818 0.4653 -0.0577 0.0787  -0.0012 361 GLU B CA  
7095 C C   . GLU B 361 ? 0.3383 0.4820 0.4555 -0.0529 0.0735  -0.0083 361 GLU B C   
7096 O O   . GLU B 361 ? 0.2586 0.3979 0.3729 -0.0521 0.0673  -0.0135 361 GLU B O   
7097 C CB  . GLU B 361 ? 0.3985 0.5416 0.5386 -0.0632 0.0822  -0.0030 361 GLU B CB  
7098 C CG  . GLU B 361 ? 0.5322 0.6707 0.6791 -0.0680 0.0870  0.0037  361 GLU B CG  
7099 C CD  . GLU B 361 ? 0.5975 0.7386 0.7424 -0.0676 0.0938  0.0116  361 GLU B CD  
7100 O OE1 . GLU B 361 ? 0.6416 0.7920 0.7881 -0.0655 0.0973  0.0114  361 GLU B OE1 
7101 O OE2 . GLU B 361 ? 0.5978 0.7321 0.7395 -0.0689 0.0958  0.0180  361 GLU B OE2 
7102 N N   . GLU B 362 ? 0.3475 0.4996 0.4625 -0.0493 0.0761  -0.0083 362 GLU B N   
7103 C CA  . GLU B 362 ? 0.3021 0.4586 0.4105 -0.0439 0.0714  -0.0147 362 GLU B CA  
7104 C C   . GLU B 362 ? 0.3074 0.4540 0.4009 -0.0402 0.0634  -0.0164 362 GLU B C   
7105 O O   . GLU B 362 ? 0.3146 0.4598 0.4043 -0.0377 0.0576  -0.0227 362 GLU B O   
7106 C CB  . GLU B 362 ? 0.3742 0.5367 0.4933 -0.0452 0.0702  -0.0222 362 GLU B CB  
7107 C CG  . GLU B 362 ? 0.5521 0.7279 0.6833 -0.0461 0.0766  -0.0231 362 GLU B CG  
7108 C CD  . GLU B 362 ? 0.6902 0.8713 0.8345 -0.0485 0.0756  -0.0302 362 GLU B CD  
7109 O OE1 . GLU B 362 ? 0.7269 0.9104 0.8673 -0.0445 0.0703  -0.0374 362 GLU B OE1 
7110 O OE2 . GLU B 362 ? 0.7465 0.9289 0.9047 -0.0542 0.0798  -0.0288 362 GLU B OE2 
7111 N N   . ASN B 363 ? 0.3187 0.4579 0.4037 -0.0400 0.0632  -0.0106 363 ASN B N   
7112 C CA  . ASN B 363 ? 0.2708 0.4016 0.3416 -0.0361 0.0561  -0.0115 363 ASN B CA  
7113 C C   . ASN B 363 ? 0.2575 0.3804 0.3273 -0.0376 0.0499  -0.0156 363 ASN B C   
7114 O O   . ASN B 363 ? 0.2606 0.3784 0.3205 -0.0340 0.0433  -0.0189 363 ASN B O   
7115 C CB  . ASN B 363 ? 0.2359 0.3717 0.2980 -0.0294 0.0535  -0.0150 363 ASN B CB  
7116 C CG  . ASN B 363 ? 0.2841 0.4116 0.3318 -0.0253 0.0472  -0.0147 363 ASN B CG  
7117 O OD1 . ASN B 363 ? 0.2817 0.4014 0.3257 -0.0272 0.0465  -0.0103 363 ASN B OD1 
7118 N ND2 . ASN B 363 ? 0.3674 0.4963 0.4071 -0.0197 0.0422  -0.0197 363 ASN B ND2 
7119 N N   . GLY B 364 ? 0.1963 0.3180 0.2762 -0.0427 0.0518  -0.0154 364 GLY B N   
7120 C CA  . GLY B 364 ? 0.2811 0.3959 0.3605 -0.0440 0.0466  -0.0186 364 GLY B CA  
7121 C C   . GLY B 364 ? 0.2674 0.3857 0.3488 -0.0418 0.0430  -0.0262 364 GLY B C   
7122 O O   . GLY B 364 ? 0.2654 0.3787 0.3467 -0.0426 0.0390  -0.0289 364 GLY B O   
7123 N N   . ILE B 365 ? 0.2588 0.3861 0.3419 -0.0388 0.0445  -0.0296 365 ILE B N   
7124 C CA  . ILE B 365 ? 0.2457 0.3768 0.3298 -0.0359 0.0407  -0.0372 365 ILE B CA  
7125 C C   . ILE B 365 ? 0.2767 0.4102 0.3731 -0.0395 0.0417  -0.0405 365 ILE B C   
7126 O O   . ILE B 365 ? 0.2185 0.3483 0.3124 -0.0380 0.0366  -0.0451 365 ILE B O   
7127 C CB  . ILE B 365 ? 0.2387 0.3800 0.3226 -0.0318 0.0425  -0.0400 365 ILE B CB  
7128 C CG1 . ILE B 365 ? 0.2569 0.3948 0.3270 -0.0272 0.0400  -0.0376 365 ILE B CG1 
7129 C CG2 . ILE B 365 ? 0.2980 0.4439 0.3833 -0.0285 0.0387  -0.0483 365 ILE B CG2 
7130 C CD1 . ILE B 365 ? 0.2682 0.4169 0.3382 -0.0234 0.0433  -0.0384 365 ILE B CD1 
7131 N N   . PRO B 366 ? 0.2958 0.4352 0.4055 -0.0440 0.0479  -0.0386 366 PRO B N   
7132 C CA  . PRO B 366 ? 0.2931 0.4340 0.4146 -0.0472 0.0480  -0.0423 366 PRO B CA  
7133 C C   . PRO B 366 ? 0.2867 0.4173 0.4040 -0.0485 0.0440  -0.0413 366 PRO B C   
7134 O O   . PRO B 366 ? 0.3458 0.4759 0.4655 -0.0476 0.0404  -0.0466 366 PRO B O   
7135 C CB  . PRO B 366 ? 0.2572 0.4038 0.3923 -0.0522 0.0555  -0.0386 366 PRO B CB  
7136 C CG  . PRO B 366 ? 0.2959 0.4487 0.4281 -0.0503 0.0595  -0.0355 366 PRO B CG  
7137 C CD  . PRO B 366 ? 0.2952 0.4404 0.4104 -0.0461 0.0550  -0.0333 366 PRO B CD  
7138 N N   . PHE B 367 ? 0.2483 0.3713 0.3594 -0.0502 0.0445  -0.0347 367 PHE B N   
7139 C CA  . PHE B 367 ? 0.2514 0.3653 0.3585 -0.0515 0.0409  -0.0333 367 PHE B CA  
7140 C C   . PHE B 367 ? 0.2689 0.3778 0.3651 -0.0472 0.0341  -0.0371 367 PHE B C   
7141 O O   . PHE B 367 ? 0.2331 0.3399 0.3306 -0.0469 0.0309  -0.0405 367 PHE B O   
7142 C CB  . PHE B 367 ? 0.2296 0.3369 0.3314 -0.0536 0.0426  -0.0257 367 PHE B CB  
7143 C CG  . PHE B 367 ? 0.2552 0.3535 0.3515 -0.0545 0.0387  -0.0240 367 PHE B CG  
7144 C CD1 . PHE B 367 ? 0.2574 0.3545 0.3617 -0.0576 0.0393  -0.0242 367 PHE B CD1 
7145 C CD2 . PHE B 367 ? 0.1915 0.2828 0.2750 -0.0521 0.0342  -0.0223 367 PHE B CD2 
7146 C CE1 . PHE B 367 ? 0.2606 0.3504 0.3598 -0.0581 0.0359  -0.0226 367 PHE B CE1 
7147 C CE2 . PHE B 367 ? 0.2212 0.3050 0.3005 -0.0531 0.0309  -0.0205 367 PHE B CE2 
7148 C CZ  . PHE B 367 ? 0.2767 0.3600 0.3636 -0.0561 0.0319  -0.0204 367 PHE B CZ  
7149 N N   . LEU B 368 ? 0.2177 0.3245 0.3029 -0.0436 0.0317  -0.0365 368 LEU B N   
7150 C CA  . LEU B 368 ? 0.2503 0.3505 0.3245 -0.0399 0.0251  -0.0389 368 LEU B CA  
7151 C C   . LEU B 368 ? 0.2845 0.3892 0.3605 -0.0365 0.0222  -0.0464 368 LEU B C   
7152 O O   . LEU B 368 ? 0.2532 0.3528 0.3247 -0.0348 0.0177  -0.0487 368 LEU B O   
7153 C CB  . LEU B 368 ? 0.2341 0.3308 0.2967 -0.0368 0.0229  -0.0368 368 LEU B CB  
7154 C CG  . LEU B 368 ? 0.2388 0.3274 0.2949 -0.0387 0.0223  -0.0303 368 LEU B CG  
7155 C CD1 . LEU B 368 ? 0.2192 0.3044 0.2637 -0.0346 0.0189  -0.0299 368 LEU B CD1 
7156 C CD2 . LEU B 368 ? 0.2120 0.2925 0.2664 -0.0408 0.0192  -0.0289 368 LEU B CD2 
7157 N N   . GLU B 369 ? 0.2723 0.3869 0.3550 -0.0353 0.0250  -0.0502 369 GLU B N   
7158 C CA  . GLU B 369 ? 0.2951 0.4149 0.3805 -0.0319 0.0224  -0.0579 369 GLU B CA  
7159 C C   . GLU B 369 ? 0.3119 0.4324 0.4063 -0.0341 0.0224  -0.0604 369 GLU B C   
7160 O O   . GLU B 369 ? 0.3295 0.4488 0.4213 -0.0309 0.0180  -0.0654 369 GLU B O   
7161 C CB  . GLU B 369 ? 0.3485 0.4801 0.4406 -0.0305 0.0258  -0.0613 369 GLU B CB  
7162 C CG  . GLU B 369 ? 0.2993 0.4312 0.3810 -0.0263 0.0244  -0.0607 369 GLU B CG  
7163 C CD  . GLU B 369 ? 0.3196 0.4639 0.4069 -0.0237 0.0269  -0.0653 369 GLU B CD  
7164 O OE1 . GLU B 369 ? 0.2974 0.4504 0.3984 -0.0265 0.0310  -0.0676 369 GLU B OE1 
7165 O OE2 . GLU B 369 ? 0.3141 0.4595 0.3925 -0.0188 0.0246  -0.0668 369 GLU B OE2 
7166 N N   . LYS B 370 ? 0.2330 0.3552 0.3377 -0.0393 0.0270  -0.0571 370 LYS B N   
7167 C CA  . LYS B 370 ? 0.2820 0.4044 0.3951 -0.0411 0.0265  -0.0597 370 LYS B CA  
7168 C C   . LYS B 370 ? 0.3155 0.4279 0.4196 -0.0406 0.0224  -0.0573 370 LYS B C   
7169 O O   . LYS B 370 ? 0.3875 0.4992 0.4916 -0.0383 0.0190  -0.0615 370 LYS B O   
7170 C CB  . LYS B 370 ? 0.2757 0.4016 0.4020 -0.0467 0.0322  -0.0567 370 LYS B CB  
7171 C CG  . LYS B 370 ? 0.3910 0.5178 0.5269 -0.0482 0.0314  -0.0603 370 LYS B CG  
7172 C CD  . LYS B 370 ? 0.4571 0.5871 0.6069 -0.0537 0.0369  -0.0577 370 LYS B CD  
7173 C CE  . LYS B 370 ? 0.4451 0.5842 0.6038 -0.0551 0.0417  -0.0585 370 LYS B CE  
7174 N NZ  . LYS B 370 ? 0.4694 0.6168 0.6320 -0.0515 0.0394  -0.0669 370 LYS B NZ  
7175 N N   . LEU B 371 ? 0.2228 0.3278 0.3194 -0.0424 0.0227  -0.0504 371 LEU B N   
7176 C CA  . LEU B 371 ? 0.2368 0.3327 0.3254 -0.0423 0.0191  -0.0476 371 LEU B CA  
7177 C C   . LEU B 371 ? 0.2542 0.3466 0.3329 -0.0372 0.0135  -0.0513 371 LEU B C   
7178 O O   . LEU B 371 ? 0.2634 0.3532 0.3408 -0.0358 0.0107  -0.0531 371 LEU B O   
7179 C CB  . LEU B 371 ? 0.2353 0.3246 0.3174 -0.0447 0.0201  -0.0402 371 LEU B CB  
7180 C CG  . LEU B 371 ? 0.2932 0.3734 0.3670 -0.0449 0.0166  -0.0367 371 LEU B CG  
7181 C CD1 . LEU B 371 ? 0.2688 0.3489 0.3500 -0.0480 0.0182  -0.0353 371 LEU B CD1 
7182 C CD2 . LEU B 371 ? 0.2297 0.3038 0.2952 -0.0459 0.0162  -0.0309 371 LEU B CD2 
7183 N N   . TYR B 372 ? 0.2407 0.3329 0.3120 -0.0341 0.0117  -0.0524 372 TYR B N   
7184 C CA  . TYR B 372 ? 0.2601 0.3477 0.3211 -0.0291 0.0062  -0.0555 372 TYR B CA  
7185 C C   . TYR B 372 ? 0.3061 0.3995 0.3715 -0.0256 0.0045  -0.0628 372 TYR B C   
7186 O O   . TYR B 372 ? 0.2997 0.3884 0.3586 -0.0222 0.0003  -0.0647 372 TYR B O   
7187 C CB  . TYR B 372 ? 0.2834 0.3704 0.3366 -0.0261 0.0046  -0.0558 372 TYR B CB  
7188 C CG  . TYR B 372 ? 0.2231 0.3031 0.2695 -0.0282 0.0046  -0.0493 372 TYR B CG  
7189 C CD1 . TYR B 372 ? 0.2632 0.3366 0.3087 -0.0319 0.0048  -0.0438 372 TYR B CD1 
7190 C CD2 . TYR B 372 ? 0.2712 0.3518 0.3121 -0.0261 0.0042  -0.0490 372 TYR B CD2 
7191 C CE1 . TYR B 372 ? 0.2699 0.3373 0.3095 -0.0336 0.0045  -0.0383 372 TYR B CE1 
7192 C CE2 . TYR B 372 ? 0.2471 0.3215 0.2818 -0.0274 0.0037  -0.0436 372 TYR B CE2 
7193 C CZ  . TYR B 372 ? 0.2624 0.3303 0.2967 -0.0313 0.0039  -0.0384 372 TYR B CZ  
7194 O OH  . TYR B 372 ? 0.2078 0.2701 0.2364 -0.0324 0.0031  -0.0336 372 TYR B OH  
7195 N N   . SER B 373 ? 0.3135 0.4171 0.3899 -0.0261 0.0078  -0.0671 373 SER B N   
7196 C CA  . SER B 373 ? 0.3518 0.4618 0.4335 -0.0227 0.0060  -0.0748 373 SER B CA  
7197 C C   . SER B 373 ? 0.3544 0.4629 0.4406 -0.0237 0.0054  -0.0754 373 SER B C   
7198 O O   . SER B 373 ? 0.3518 0.4607 0.4358 -0.0193 0.0018  -0.0803 373 SER B O   
7199 C CB  . SER B 373 ? 0.3554 0.4772 0.4493 -0.0236 0.0099  -0.0791 373 SER B CB  
7200 O OG  . SER B 373 ? 0.4745 0.6028 0.5766 -0.0215 0.0087  -0.0863 373 SER B OG  
7201 N N   . THR B 374 ? 0.3358 0.4430 0.4281 -0.0289 0.0088  -0.0705 374 THR B N   
7202 C CA  . THR B 374 ? 0.3378 0.4433 0.4337 -0.0297 0.0081  -0.0705 374 THR B CA  
7203 C C   . THR B 374 ? 0.3599 0.4560 0.4431 -0.0273 0.0041  -0.0673 374 THR B C   
7204 O O   . THR B 374 ? 0.3173 0.4132 0.3995 -0.0241 0.0014  -0.0704 374 THR B O   
7205 C CB  . THR B 374 ? 0.2661 0.3718 0.3708 -0.0358 0.0126  -0.0657 374 THR B CB  
7206 O OG1 . THR B 374 ? 0.2628 0.3769 0.3797 -0.0382 0.0166  -0.0682 374 THR B OG1 
7207 C CG2 . THR B 374 ? 0.3652 0.4699 0.4741 -0.0362 0.0117  -0.0663 374 THR B CG2 
7208 N N   . LEU B 375 ? 0.2975 0.3862 0.3715 -0.0287 0.0037  -0.0612 375 LEU B N   
7209 C CA  . LEU B 375 ? 0.2814 0.3609 0.3443 -0.0273 0.0003  -0.0573 375 LEU B CA  
7210 C C   . LEU B 375 ? 0.3090 0.3869 0.3640 -0.0211 -0.0043 -0.0619 375 LEU B C   
7211 O O   . LEU B 375 ? 0.3192 0.3930 0.3692 -0.0188 -0.0067 -0.0612 375 LEU B O   
7212 C CB  . LEU B 375 ? 0.3033 0.3756 0.3586 -0.0298 0.0004  -0.0508 375 LEU B CB  
7213 C CG  . LEU B 375 ? 0.3260 0.3971 0.3858 -0.0354 0.0040  -0.0447 375 LEU B CG  
7214 C CD1 . LEU B 375 ? 0.3067 0.3715 0.3583 -0.0367 0.0033  -0.0396 375 LEU B CD1 
7215 C CD2 . LEU B 375 ? 0.3449 0.4133 0.4059 -0.0370 0.0040  -0.0419 375 LEU B CD2 
7216 N N   . GLU B 376 ? 0.3081 0.3896 0.3618 -0.0179 -0.0054 -0.0666 376 GLU B N   
7217 C CA  . GLU B 376 ? 0.3641 0.4437 0.4097 -0.0116 -0.0099 -0.0711 376 GLU B CA  
7218 C C   . GLU B 376 ? 0.4001 0.4861 0.4515 -0.0081 -0.0108 -0.0774 376 GLU B C   
7219 O O   . GLU B 376 ? 0.4066 0.4909 0.4510 -0.0023 -0.0146 -0.0811 376 GLU B O   
7220 C CB  . GLU B 376 ? 0.3776 0.4595 0.4198 -0.0087 -0.0112 -0.0746 376 GLU B CB  
7221 C CG  . GLU B 376 ? 0.4383 0.5320 0.4921 -0.0091 -0.0081 -0.0802 376 GLU B CG  
7222 C CD  . GLU B 376 ? 0.4874 0.5845 0.5374 -0.0051 -0.0097 -0.0846 376 GLU B CD  
7223 O OE1 . GLU B 376 ? 0.4783 0.5679 0.5168 -0.0028 -0.0129 -0.0824 376 GLU B OE1 
7224 O OE2 . GLU B 376 ? 0.4887 0.5964 0.5478 -0.0042 -0.0079 -0.0903 376 GLU B OE2 
7225 N N   . LYS B 377 ? 0.3696 0.4627 0.4335 -0.0113 -0.0075 -0.0790 377 LYS B N   
7226 C CA  . LYS B 377 ? 0.3603 0.4598 0.4309 -0.0081 -0.0085 -0.0854 377 LYS B CA  
7227 C C   . LYS B 377 ? 0.3868 0.4826 0.4563 -0.0084 -0.0089 -0.0823 377 LYS B C   
7228 O O   . LYS B 377 ? 0.4198 0.5193 0.4911 -0.0040 -0.0110 -0.0874 377 LYS B O   
7229 C CB  . LYS B 377 ? 0.3702 0.4803 0.4565 -0.0109 -0.0050 -0.0901 377 LYS B CB  
7230 C CG  . LYS B 377 ? 0.4288 0.5461 0.5180 -0.0086 -0.0052 -0.0961 377 LYS B CG  
7231 C CD  . LYS B 377 ? 0.5069 0.6342 0.6125 -0.0127 -0.0010 -0.0992 377 LYS B CD  
7232 C CE  . LYS B 377 ? 0.5884 0.7232 0.6967 -0.0109 -0.0004 -0.1040 377 LYS B CE  
7233 N NZ  . LYS B 377 ? 0.6330 0.7620 0.7295 -0.0105 -0.0008 -0.0992 377 LYS B NZ  
7234 N N   . GLU B 378 ? 0.3016 0.3910 0.3683 -0.0129 -0.0072 -0.0744 378 GLU B N   
7235 C CA  . GLU B 378 ? 0.3530 0.4401 0.4196 -0.0134 -0.0073 -0.0714 378 GLU B CA  
7236 C C   . GLU B 378 ? 0.3962 0.4761 0.4497 -0.0089 -0.0108 -0.0689 378 GLU B C   
7237 O O   . GLU B 378 ? 0.3846 0.4564 0.4289 -0.0102 -0.0116 -0.0633 378 GLU B O   
7238 C CB  . GLU B 378 ? 0.3467 0.4307 0.4165 -0.0200 -0.0039 -0.0643 378 GLU B CB  
7239 C CG  . GLU B 378 ? 0.3857 0.4757 0.4678 -0.0247 0.0000  -0.0656 378 GLU B CG  
7240 C CD  . GLU B 378 ? 0.4542 0.5510 0.5486 -0.0252 0.0013  -0.0698 378 GLU B CD  
7241 O OE1 . GLU B 378 ? 0.4607 0.5585 0.5541 -0.0213 -0.0012 -0.0726 378 GLU B OE1 
7242 O OE2 . GLU B 378 ? 0.5046 0.6056 0.6099 -0.0294 0.0046  -0.0703 378 GLU B OE2 
7243 N N   . GLU B 379 ? 0.3906 0.4733 0.4434 -0.0036 -0.0129 -0.0730 379 GLU B N   
7244 C CA  . GLU B 379 ? 0.3537 0.4301 0.3941 0.0012  -0.0160 -0.0706 379 GLU B CA  
7245 C C   . GLU B 379 ? 0.2983 0.3678 0.3339 -0.0022 -0.0149 -0.0617 379 GLU B C   
7246 O O   . GLU B 379 ? 0.4082 0.4701 0.4328 -0.0003 -0.0167 -0.0572 379 GLU B O   
7247 C CB  . GLU B 379 ? 0.3458 0.4279 0.3872 0.0081  -0.0182 -0.0770 379 GLU B CB  
7248 C CG  . GLU B 379 ? 0.4594 0.5472 0.5023 0.0135  -0.0205 -0.0860 379 GLU B CG  
7249 C CD  . GLU B 379 ? 0.5592 0.6526 0.6027 0.0207  -0.0230 -0.0924 379 GLU B CD  
7250 O OE1 . GLU B 379 ? 0.5944 0.6868 0.6361 0.0218  -0.0228 -0.0894 379 GLU B OE1 
7251 O OE2 . GLU B 379 ? 0.5937 0.6931 0.6396 0.0256  -0.0251 -0.1007 379 GLU B OE2 
7252 N N   . TRP B 380 ? 0.3043 0.3764 0.3480 -0.0071 -0.0119 -0.0591 380 TRP B N   
7253 C CA  . TRP B 380 ? 0.2588 0.3259 0.2989 -0.0101 -0.0108 -0.0513 380 TRP B CA  
7254 C C   . TRP B 380 ? 0.2349 0.2954 0.2722 -0.0160 -0.0094 -0.0446 380 TRP B C   
7255 O O   . TRP B 380 ? 0.2833 0.3397 0.3179 -0.0189 -0.0085 -0.0379 380 TRP B O   
7256 C CB  . TRP B 380 ? 0.3007 0.3739 0.3505 -0.0118 -0.0087 -0.0522 380 TRP B CB  
7257 C CG  . TRP B 380 ? 0.3181 0.3962 0.3796 -0.0162 -0.0062 -0.0551 380 TRP B CG  
7258 C CD1 . TRP B 380 ? 0.3891 0.4741 0.4590 -0.0147 -0.0062 -0.0628 380 TRP B CD1 
7259 C CD2 . TRP B 380 ? 0.3155 0.3921 0.3819 -0.0228 -0.0030 -0.0501 380 TRP B CD2 
7260 N NE1 . TRP B 380 ? 0.3294 0.4170 0.4093 -0.0203 -0.0030 -0.0625 380 TRP B NE1 
7261 C CE2 . TRP B 380 ? 0.3416 0.4239 0.4190 -0.0251 -0.0011 -0.0547 380 TRP B CE2 
7262 C CE3 . TRP B 380 ? 0.3776 0.4487 0.4402 -0.0270 -0.0017 -0.0422 380 TRP B CE3 
7263 C CZ2 . TRP B 380 ? 0.3867 0.4689 0.4707 -0.0310 0.0023  -0.0513 380 TRP B CZ2 
7264 C CZ3 . TRP B 380 ? 0.3985 0.4698 0.4676 -0.0326 0.0013  -0.0394 380 TRP B CZ3 
7265 C CH2 . TRP B 380 ? 0.3342 0.4107 0.4135 -0.0344 0.0034  -0.0437 380 TRP B CH2 
7266 N N   . ILE B 381 ? 0.2701 0.3302 0.3083 -0.0176 -0.0092 -0.0463 381 ILE B N   
7267 C CA  . ILE B 381 ? 0.3061 0.3602 0.3409 -0.0222 -0.0086 -0.0408 381 ILE B CA  
7268 C C   . ILE B 381 ? 0.3652 0.4131 0.3900 -0.0191 -0.0119 -0.0411 381 ILE B C   
7269 O O   . ILE B 381 ? 0.3357 0.3865 0.3599 -0.0149 -0.0135 -0.0471 381 ILE B O   
7270 C CB  . ILE B 381 ? 0.3202 0.3788 0.3637 -0.0263 -0.0056 -0.0421 381 ILE B CB  
7271 C CG1 . ILE B 381 ? 0.3349 0.3989 0.3887 -0.0294 -0.0024 -0.0420 381 ILE B CG1 
7272 C CG2 . ILE B 381 ? 0.2714 0.3238 0.3102 -0.0300 -0.0053 -0.0367 381 ILE B CG2 
7273 C CD1 . ILE B 381 ? 0.2836 0.3524 0.3468 -0.0331 0.0009  -0.0435 381 ILE B CD1 
7274 N N   . GLU B 382 ? 0.2937 0.3330 0.3109 -0.0210 -0.0131 -0.0347 382 GLU B N   
7275 C CA  . GLU B 382 ? 0.3281 0.3602 0.3361 -0.0187 -0.0164 -0.0345 382 GLU B CA  
7276 C C   . GLU B 382 ? 0.3063 0.3335 0.3131 -0.0235 -0.0161 -0.0300 382 GLU B C   
7277 O O   . GLU B 382 ? 0.3062 0.3292 0.3123 -0.0274 -0.0154 -0.0238 382 GLU B O   
7278 C CB  . GLU B 382 ? 0.3559 0.3811 0.3549 -0.0156 -0.0191 -0.0314 382 GLU B CB  
7279 C CG  . GLU B 382 ? 0.5081 0.5240 0.4975 -0.0139 -0.0228 -0.0301 382 GLU B CG  
7280 C CD  . GLU B 382 ? 0.6374 0.6470 0.6181 -0.0098 -0.0252 -0.0279 382 GLU B CD  
7281 O OE1 . GLU B 382 ? 0.6629 0.6766 0.6450 -0.0076 -0.0240 -0.0279 382 GLU B OE1 
7282 O OE2 . GLU B 382 ? 0.6806 0.6813 0.6532 -0.0085 -0.0285 -0.0260 382 GLU B OE2 
7283 N N   . THR B 383 ? 0.3064 0.3349 0.3135 -0.0231 -0.0166 -0.0333 383 THR B N   
7284 C CA  . THR B 383 ? 0.2894 0.3132 0.2942 -0.0264 -0.0170 -0.0297 383 THR B CA  
7285 C C   . THR B 383 ? 0.3324 0.3457 0.3270 -0.0248 -0.0214 -0.0270 383 THR B C   
7286 O O   . THR B 383 ? 0.3183 0.3287 0.3070 -0.0201 -0.0243 -0.0297 383 THR B O   
7287 C CB  . THR B 383 ? 0.2923 0.3213 0.3000 -0.0257 -0.0160 -0.0340 383 THR B CB  
7288 O OG1 . THR B 383 ? 0.3041 0.3341 0.3078 -0.0202 -0.0188 -0.0398 383 THR B OG1 
7289 C CG2 . THR B 383 ? 0.2866 0.3253 0.3053 -0.0282 -0.0113 -0.0357 383 THR B CG2 
7290 N N   . LEU B 384 ? 0.3031 0.3104 0.2959 -0.0288 -0.0219 -0.0217 384 LEU B N   
7291 C CA  . LEU B 384 ? 0.2988 0.2954 0.2836 -0.0286 -0.0259 -0.0182 384 LEU B CA  
7292 C C   . LEU B 384 ? 0.3250 0.3174 0.3073 -0.0299 -0.0281 -0.0177 384 LEU B C   
7293 O O   . LEU B 384 ? 0.3039 0.3006 0.2909 -0.0328 -0.0256 -0.0171 384 LEU B O   
7294 C CB  . LEU B 384 ? 0.3221 0.3151 0.3076 -0.0324 -0.0250 -0.0115 384 LEU B CB  
7295 C CG  . LEU B 384 ? 0.3507 0.3480 0.3386 -0.0313 -0.0227 -0.0109 384 LEU B CG  
7296 C CD1 . LEU B 384 ? 0.2295 0.2230 0.2174 -0.0351 -0.0219 -0.0038 384 LEU B CD1 
7297 C CD2 . LEU B 384 ? 0.2489 0.2445 0.2309 -0.0252 -0.0252 -0.0146 384 LEU B CD2 
7298 N N   . THR B 385 ? 0.2858 0.2696 0.2604 -0.0274 -0.0328 -0.0180 385 THR B N   
7299 C CA  . THR B 385 ? 0.2970 0.2747 0.2687 -0.0291 -0.0357 -0.0165 385 THR B CA  
7300 C C   . THR B 385 ? 0.2740 0.2470 0.2477 -0.0345 -0.0353 -0.0097 385 THR B C   
7301 O O   . THR B 385 ? 0.2487 0.2214 0.2239 -0.0361 -0.0336 -0.0062 385 THR B O   
7302 C CB  . THR B 385 ? 0.3593 0.3283 0.3226 -0.0248 -0.0414 -0.0188 385 THR B CB  
7303 O OG1 . THR B 385 ? 0.3288 0.2895 0.2881 -0.0249 -0.0434 -0.0151 385 THR B OG1 
7304 C CG2 . THR B 385 ? 0.3410 0.3151 0.3021 -0.0190 -0.0420 -0.0257 385 THR B CG2 
7305 N N   . LEU B 386 ? 0.2912 0.2610 0.2648 -0.0369 -0.0370 -0.0082 386 LEU B N   
7306 C CA  . LEU B 386 ? 0.2992 0.2642 0.2746 -0.0419 -0.0373 -0.0023 386 LEU B CA  
7307 C C   . LEU B 386 ? 0.3396 0.2953 0.3107 -0.0419 -0.0404 0.0009  386 LEU B C   
7308 O O   . LEU B 386 ? 0.3635 0.3180 0.3372 -0.0454 -0.0387 0.0062  386 LEU B O   
7309 C CB  . LEU B 386 ? 0.3089 0.2714 0.2841 -0.0434 -0.0397 -0.0022 386 LEU B CB  
7310 C CG  . LEU B 386 ? 0.3159 0.2871 0.2947 -0.0432 -0.0365 -0.0045 386 LEU B CG  
7311 C CD1 . LEU B 386 ? 0.3474 0.3149 0.3239 -0.0432 -0.0401 -0.0051 386 LEU B CD1 
7312 C CD2 . LEU B 386 ? 0.2775 0.2557 0.2634 -0.0472 -0.0311 -0.0012 386 LEU B CD2 
7313 N N   . GLU B 387 ? 0.3660 0.3151 0.3305 -0.0377 -0.0447 -0.0021 387 GLU B N   
7314 C CA  . GLU B 387 ? 0.4259 0.3651 0.3855 -0.0371 -0.0477 0.0011  387 GLU B CA  
7315 C C   . GLU B 387 ? 0.3944 0.3371 0.3550 -0.0368 -0.0440 0.0037  387 GLU B C   
7316 O O   . GLU B 387 ? 0.3718 0.3099 0.3325 -0.0395 -0.0437 0.0094  387 GLU B O   
7317 C CB  . GLU B 387 ? 0.4559 0.3885 0.4078 -0.0315 -0.0527 -0.0036 387 GLU B CB  
7318 C CG  . GLU B 387 ? 0.5795 0.5014 0.5257 -0.0302 -0.0557 -0.0005 387 GLU B CG  
7319 C CD  . GLU B 387 ? 0.7627 0.6738 0.7088 -0.0343 -0.0594 0.0041  387 GLU B CD  
7320 O OE1 . GLU B 387 ? 0.8275 0.7394 0.7771 -0.0373 -0.0605 0.0037  387 GLU B OE1 
7321 O OE2 . GLU B 387 ? 0.8571 0.7590 0.7997 -0.0344 -0.0614 0.0080  387 GLU B OE2 
7322 N N   . GLU B 388 ? 0.3418 0.2931 0.3034 -0.0332 -0.0413 -0.0007 388 GLU B N   
7323 C CA  . GLU B 388 ? 0.3023 0.2578 0.2649 -0.0320 -0.0382 0.0008  388 GLU B CA  
7324 C C   . GLU B 388 ? 0.3107 0.2713 0.2800 -0.0372 -0.0340 0.0058  388 GLU B C   
7325 O O   . GLU B 388 ? 0.3612 0.3210 0.3303 -0.0378 -0.0325 0.0102  388 GLU B O   
7326 C CB  . GLU B 388 ? 0.3227 0.2867 0.2859 -0.0272 -0.0366 -0.0058 388 GLU B CB  
7327 C CG  . GLU B 388 ? 0.3787 0.3383 0.3345 -0.0211 -0.0406 -0.0106 388 GLU B CG  
7328 C CD  . GLU B 388 ? 0.4469 0.4161 0.4048 -0.0169 -0.0393 -0.0180 388 GLU B CD  
7329 O OE1 . GLU B 388 ? 0.3656 0.3432 0.3305 -0.0193 -0.0361 -0.0197 388 GLU B OE1 
7330 O OE2 . GLU B 388 ? 0.5196 0.4878 0.4723 -0.0112 -0.0414 -0.0219 388 GLU B OE2 
7331 N N   . ALA B 389 ? 0.3308 0.2971 0.3061 -0.0405 -0.0319 0.0051  389 ALA B N   
7332 C CA  . ALA B 389 ? 0.2602 0.2313 0.2418 -0.0452 -0.0282 0.0096  389 ALA B CA  
7333 C C   . ALA B 389 ? 0.3573 0.3213 0.3384 -0.0493 -0.0296 0.0162  389 ALA B C   
7334 O O   . ALA B 389 ? 0.3297 0.2961 0.3136 -0.0516 -0.0270 0.0208  389 ALA B O   
7335 C CB  . ALA B 389 ? 0.2811 0.2584 0.2682 -0.0475 -0.0262 0.0077  389 ALA B CB  
7336 N N   . MET B 390 ? 0.3693 0.3247 0.3471 -0.0502 -0.0338 0.0166  390 MET B N   
7337 C CA  . MET B 390 ? 0.3892 0.3376 0.3676 -0.0545 -0.0355 0.0225  390 MET B CA  
7338 C C   . MET B 390 ? 0.3781 0.3213 0.3530 -0.0536 -0.0357 0.0269  390 MET B C   
7339 O O   . MET B 390 ? 0.3444 0.2858 0.3219 -0.0576 -0.0347 0.0330  390 MET B O   
7340 C CB  . MET B 390 ? 0.3738 0.3141 0.3498 -0.0550 -0.0406 0.0209  390 MET B CB  
7341 C CG  . MET B 390 ? 0.4640 0.3958 0.4410 -0.0595 -0.0434 0.0262  390 MET B CG  
7342 S SD  . MET B 390 ? 0.5315 0.4531 0.5050 -0.0587 -0.0504 0.0228  390 MET B SD  
7343 C CE  . MET B 390 ? 0.4689 0.3823 0.4335 -0.0528 -0.0538 0.0203  390 MET B CE  
7344 N N   . ARG B 391 ? 0.3732 0.3142 0.3421 -0.0482 -0.0368 0.0240  391 ARG B N   
7345 C CA  . ARG B 391 ? 0.4419 0.3763 0.4058 -0.0464 -0.0376 0.0280  391 ARG B CA  
7346 C C   . ARG B 391 ? 0.4128 0.3544 0.3759 -0.0428 -0.0339 0.0281  391 ARG B C   
7347 O O   . ARG B 391 ? 0.4137 0.3510 0.3725 -0.0410 -0.0337 0.0322  391 ARG B O   
7348 C CB  . ARG B 391 ? 0.5588 0.4831 0.5150 -0.0424 -0.0426 0.0251  391 ARG B CB  
7349 C CG  . ARG B 391 ? 0.6479 0.5637 0.6041 -0.0453 -0.0473 0.0250  391 ARG B CG  
7350 C CD  . ARG B 391 ? 0.7838 0.6880 0.7322 -0.0413 -0.0526 0.0234  391 ARG B CD  
7351 N NE  . ARG B 391 ? 0.8781 0.7721 0.8273 -0.0451 -0.0570 0.0256  391 ARG B NE  
7352 C CZ  . ARG B 391 ? 0.9343 0.8213 0.8856 -0.0497 -0.0573 0.0327  391 ARG B CZ  
7353 N NH1 . ARG B 391 ? 0.9153 0.8047 0.8673 -0.0507 -0.0531 0.0385  391 ARG B NH1 
7354 N NH2 . ARG B 391 ? 0.9607 0.8388 0.9136 -0.0531 -0.0618 0.0338  391 ARG B NH2 
7355 N N   . LYS B 392 ? 0.3930 0.3452 0.3601 -0.0415 -0.0309 0.0237  392 LYS B N   
7356 C CA  . LYS B 392 ? 0.3927 0.3520 0.3593 -0.0373 -0.0280 0.0224  392 LYS B CA  
7357 C C   . LYS B 392 ? 0.3665 0.3273 0.3344 -0.0392 -0.0252 0.0294  392 LYS B C   
7358 O O   . LYS B 392 ? 0.4376 0.4016 0.4113 -0.0444 -0.0230 0.0332  392 LYS B O   
7359 C CB  . LYS B 392 ? 0.3881 0.3583 0.3608 -0.0369 -0.0254 0.0169  392 LYS B CB  
7360 C CG  . LYS B 392 ? 0.4378 0.4157 0.4106 -0.0319 -0.0233 0.0136  392 LYS B CG  
7361 C CD  . LYS B 392 ? 0.5136 0.4973 0.4885 -0.0289 -0.0235 0.0055  392 LYS B CD  
7362 C CE  . LYS B 392 ? 0.5287 0.5084 0.4964 -0.0228 -0.0268 0.0011  392 LYS B CE  
7363 N NZ  . LYS B 392 ? 0.5370 0.5194 0.5015 -0.0175 -0.0261 0.0007  392 LYS B NZ  
7364 N N   . GLU B 393 ? 0.3499 0.3090 0.3122 -0.0346 -0.0250 0.0310  393 GLU B N   
7365 C CA  . GLU B 393 ? 0.4590 0.4191 0.4213 -0.0358 -0.0222 0.0383  393 GLU B CA  
7366 C C   . GLU B 393 ? 0.4510 0.4233 0.4183 -0.0347 -0.0182 0.0373  393 GLU B C   
7367 O O   . GLU B 393 ? 0.5209 0.4968 0.4920 -0.0381 -0.0155 0.0429  393 GLU B O   
7368 C CB  . GLU B 393 ? 0.5390 0.4922 0.4926 -0.0307 -0.0235 0.0410  393 GLU B CB  
7369 C CG  . GLU B 393 ? 0.6698 0.6097 0.6186 -0.0321 -0.0275 0.0433  393 GLU B CG  
7370 C CD  . GLU B 393 ? 0.8208 0.7533 0.7610 -0.0274 -0.0282 0.0472  393 GLU B CD  
7371 O OE1 . GLU B 393 ? 0.8894 0.8278 0.8271 -0.0228 -0.0255 0.0482  393 GLU B OE1 
7372 O OE2 . GLU B 393 ? 0.8899 0.8105 0.8257 -0.0281 -0.0317 0.0493  393 GLU B OE2 
7373 N N   . ASP B 394 ? 0.4052 0.3841 0.3729 -0.0300 -0.0180 0.0301  394 ASP B N   
7374 C CA  . ASP B 394 ? 0.4115 0.4014 0.3831 -0.0275 -0.0149 0.0284  394 ASP B CA  
7375 C C   . ASP B 394 ? 0.3426 0.3396 0.3232 -0.0319 -0.0130 0.0260  394 ASP B C   
7376 O O   . ASP B 394 ? 0.4260 0.4301 0.4104 -0.0297 -0.0123 0.0198  394 ASP B O   
7377 C CB  . ASP B 394 ? 0.4320 0.4253 0.3998 -0.0198 -0.0159 0.0217  394 ASP B CB  
7378 C CG  . ASP B 394 ? 0.6151 0.6061 0.5823 -0.0185 -0.0187 0.0146  394 ASP B CG  
7379 O OD1 . ASP B 394 ? 0.6767 0.6600 0.6424 -0.0219 -0.0208 0.0160  394 ASP B OD1 
7380 O OD2 . ASP B 394 ? 0.6121 0.6095 0.5806 -0.0138 -0.0189 0.0074  394 ASP B OD2 
7381 N N   . VAL B 395 ? 0.3782 0.3730 0.3622 -0.0383 -0.0122 0.0312  395 VAL B N   
7382 C CA  . VAL B 395 ? 0.3368 0.3375 0.3287 -0.0426 -0.0104 0.0302  395 VAL B CA  
7383 C C   . VAL B 395 ? 0.3803 0.3826 0.3752 -0.0470 -0.0082 0.0373  395 VAL B C   
7384 O O   . VAL B 395 ? 0.3877 0.3848 0.3792 -0.0481 -0.0086 0.0434  395 VAL B O   
7385 C CB  . VAL B 395 ? 0.4283 0.4249 0.4218 -0.0460 -0.0123 0.0275  395 VAL B CB  
7386 C CG1 . VAL B 395 ? 0.4492 0.4462 0.4408 -0.0416 -0.0140 0.0200  395 VAL B CG1 
7387 C CG2 . VAL B 395 ? 0.4472 0.4337 0.4371 -0.0492 -0.0149 0.0323  395 VAL B CG2 
7388 N N   . LYS B 396 ? 0.3571 0.3666 0.3587 -0.0494 -0.0060 0.0367  396 LYS B N   
7389 C CA  . LYS B 396 ? 0.3235 0.3357 0.3286 -0.0536 -0.0040 0.0428  396 LYS B CA  
7390 C C   . LYS B 396 ? 0.3346 0.3412 0.3417 -0.0596 -0.0054 0.0456  396 LYS B C   
7391 O O   . LYS B 396 ? 0.3597 0.3643 0.3682 -0.0609 -0.0067 0.0417  396 LYS B O   
7392 C CB  . LYS B 396 ? 0.3198 0.3418 0.3309 -0.0532 -0.0013 0.0406  396 LYS B CB  
7393 C CG  . LYS B 396 ? 0.3260 0.3525 0.3403 -0.0561 0.0010  0.0466  396 LYS B CG  
7394 C CD  . LYS B 396 ? 0.3751 0.4112 0.3931 -0.0531 0.0032  0.0441  396 LYS B CD  
7395 C CE  . LYS B 396 ? 0.3860 0.4274 0.4083 -0.0564 0.0053  0.0488  396 LYS B CE  
7396 N NZ  . LYS B 396 ? 0.4452 0.4953 0.4718 -0.0536 0.0068  0.0449  396 LYS B NZ  
7397 N N   . THR B 397 ? 0.2736 0.3028 0.2969 0.0070  0.0238  -0.0183 397 THR B N   
7398 C CA  . THR B 397 ? 0.2773 0.3204 0.3041 -0.0005 0.0221  -0.0140 397 THR B CA  
7399 C C   . THR B 397 ? 0.3248 0.3904 0.3554 0.0064  0.0225  -0.0089 397 THR B C   
7400 O O   . THR B 397 ? 0.3619 0.4352 0.3930 0.0152  0.0245  -0.0082 397 THR B O   
7401 C CB  . THR B 397 ? 0.3032 0.3520 0.3322 -0.0131 0.0214  -0.0129 397 THR B CB  
7402 O OG1 . THR B 397 ? 0.3322 0.3934 0.3634 -0.0112 0.0234  -0.0114 397 THR B OG1 
7403 C CG2 . THR B 397 ? 0.2647 0.2915 0.2897 -0.0205 0.0208  -0.0178 397 THR B CG2 
7404 N N   . GLU B 398 ? 0.3157 0.3919 0.3490 0.0023  0.0205  -0.0053 398 GLU B N   
7405 C CA  . GLU B 398 ? 0.2957 0.3939 0.3333 0.0077  0.0206  -0.0001 398 GLU B CA  
7406 C C   . GLU B 398 ? 0.2657 0.3769 0.3073 -0.0018 0.0180  0.0041  398 GLU B C   
7407 O O   . GLU B 398 ? 0.2707 0.3714 0.3103 -0.0083 0.0158  0.0027  398 GLU B O   
7408 C CB  . GLU B 398 ? 0.2953 0.3899 0.3307 0.0193  0.0208  -0.0006 398 GLU B CB  
7409 C CG  . GLU B 398 ? 0.3434 0.4611 0.3831 0.0255  0.0209  0.0048  398 GLU B CG  
7410 C CD  . GLU B 398 ? 0.5137 0.6279 0.5510 0.0375  0.0211  0.0041  398 GLU B CD  
7411 O OE1 . GLU B 398 ? 0.5139 0.6092 0.5465 0.0430  0.0217  -0.0004 398 GLU B OE1 
7412 O OE2 . GLU B 398 ? 0.5872 0.7172 0.6274 0.0413  0.0205  0.0082  398 GLU B OE2 
7413 N N   . VAL B 399 ? 0.2279 0.3618 0.2751 -0.0023 0.0181  0.0092  399 VAL B N   
7414 C CA  . VAL B 399 ? 0.3281 0.4762 0.3800 -0.0105 0.0152  0.0136  399 VAL B CA  
7415 C C   . VAL B 399 ? 0.3725 0.5303 0.4257 -0.0032 0.0143  0.0166  399 VAL B C   
7416 O O   . VAL B 399 ? 0.4486 0.6161 0.5030 0.0071  0.0164  0.0182  399 VAL B O   
7417 C CB  . VAL B 399 ? 0.3683 0.5363 0.4265 -0.0159 0.0155  0.0181  399 VAL B CB  
7418 C CG1 . VAL B 399 ? 0.3511 0.5351 0.4148 -0.0232 0.0121  0.0231  399 VAL B CG1 
7419 C CG2 . VAL B 399 ? 0.3686 0.5265 0.4253 -0.0241 0.0161  0.0152  399 VAL B CG2 
7420 N N   . ILE B 400 ? 0.3454 0.5007 0.3981 -0.0085 0.0113  0.0172  400 ILE B N   
7421 C CA  . ILE B 400 ? 0.3547 0.5202 0.4091 -0.0030 0.0099  0.0203  400 ILE B CA  
7422 C C   . ILE B 400 ? 0.2843 0.4650 0.3436 -0.0120 0.0065  0.0249  400 ILE B C   
7423 O O   . ILE B 400 ? 0.3130 0.4888 0.3722 -0.0229 0.0042  0.0243  400 ILE B O   
7424 C CB  . ILE B 400 ? 0.4038 0.5505 0.4521 0.0013  0.0094  0.0167  400 ILE B CB  
7425 C CG1 . ILE B 400 ? 0.4848 0.6138 0.5292 -0.0087 0.0075  0.0136  400 ILE B CG1 
7426 C CG2 . ILE B 400 ? 0.3810 0.5160 0.4255 0.0122  0.0125  0.0131  400 ILE B CG2 
7427 C CD1 . ILE B 400 ? 0.5518 0.6635 0.5909 -0.0054 0.0069  0.0108  400 ILE B CD1 
7428 N N   . GLU B 401 ? 0.2678 0.4671 0.3317 -0.0072 0.0058  0.0295  401 GLU B N   
7429 C CA  . GLU B 401 ? 0.2269 0.4432 0.2967 -0.0148 0.0023  0.0345  401 GLU B CA  
7430 C C   . GLU B 401 ? 0.2513 0.4666 0.3196 -0.0145 -0.0009 0.0354  401 GLU B C   
7431 O O   . GLU B 401 ? 0.2889 0.5148 0.3612 -0.0219 -0.0046 0.0388  401 GLU B O   
7432 C CB  . GLU B 401 ? 0.3351 0.5765 0.4128 -0.0111 0.0036  0.0401  401 GLU B CB  
7433 C CG  . GLU B 401 ? 0.4528 0.6977 0.5325 -0.0113 0.0067  0.0401  401 GLU B CG  
7434 C CD  . GLU B 401 ? 0.5113 0.7566 0.5936 -0.0244 0.0048  0.0406  401 GLU B CD  
7435 O OE1 . GLU B 401 ? 0.5403 0.7827 0.6224 -0.0256 0.0073  0.0392  401 GLU B OE1 
7436 O OE2 . GLU B 401 ? 0.4730 0.7212 0.5574 -0.0332 0.0006  0.0425  401 GLU B OE2 
7437 N N   . SER B 402 ? 0.2297 0.4328 0.2927 -0.0063 0.0002  0.0325  402 SER B N   
7438 C CA  . SER B 402 ? 0.2645 0.4680 0.3262 -0.0049 -0.0025 0.0337  402 SER B CA  
7439 C C   . SER B 402 ? 0.3201 0.5022 0.3743 0.0012  -0.0013 0.0291  402 SER B C   
7440 O O   . SER B 402 ? 0.2962 0.4707 0.3480 0.0093  0.0020  0.0265  402 SER B O   
7441 C CB  . SER B 402 ? 0.2091 0.4345 0.2764 0.0022  -0.0026 0.0386  402 SER B CB  
7442 O OG  . SER B 402 ? 0.2885 0.5146 0.3545 0.0035  -0.0054 0.0398  402 SER B OG  
7443 N N   . VAL B 403 ? 0.3322 0.5046 0.3826 -0.0026 -0.0040 0.0282  403 VAL B N   
7444 C CA  . VAL B 403 ? 0.3309 0.4849 0.3750 0.0033  -0.0031 0.0248  403 VAL B CA  
7445 C C   . VAL B 403 ? 0.3340 0.4952 0.3780 0.0067  -0.0055 0.0275  403 VAL B C   
7446 O O   . VAL B 403 ? 0.3721 0.5467 0.4197 0.0011  -0.0087 0.0310  403 VAL B O   
7447 C CB  . VAL B 403 ? 0.3426 0.4744 0.3809 -0.0038 -0.0036 0.0207  403 VAL B CB  
7448 C CG1 . VAL B 403 ? 0.2554 0.3794 0.2935 -0.0074 -0.0014 0.0179  403 VAL B CG1 
7449 C CG2 . VAL B 403 ? 0.3427 0.4763 0.3806 -0.0139 -0.0077 0.0224  403 VAL B CG2 
7450 N N   . LYS B 404 ? 0.2705 0.4226 0.3108 0.0159  -0.0040 0.0258  404 LYS B N   
7451 C CA  . LYS B 404 ? 0.2970 0.4520 0.3360 0.0195  -0.0060 0.0276  404 LYS B CA  
7452 C C   . LYS B 404 ? 0.3019 0.4375 0.3347 0.0149  -0.0075 0.0251  404 LYS B C   
7453 O O   . LYS B 404 ? 0.3147 0.4311 0.3430 0.0166  -0.0053 0.0213  404 LYS B O   
7454 C CB  . LYS B 404 ? 0.3492 0.5059 0.3876 0.0323  -0.0038 0.0276  404 LYS B CB  
7455 C CG  . LYS B 404 ? 0.5249 0.7046 0.5696 0.0374  -0.0032 0.0313  404 LYS B CG  
7456 C CD  . LYS B 404 ? 0.6101 0.8084 0.6591 0.0338  -0.0066 0.0360  404 LYS B CD  
7457 C CE  . LYS B 404 ? 0.6329 0.8457 0.6880 0.0244  -0.0082 0.0389  404 LYS B CE  
7458 N NZ  . LYS B 404 ? 0.6451 0.8824 0.7072 0.0258  -0.0099 0.0443  404 LYS B NZ  
7459 N N   . ALA B 405 ? 0.2549 0.3952 0.2874 0.0093  -0.0111 0.0273  405 ALA B N   
7460 C CA  . ALA B 405 ? 0.2806 0.4036 0.3070 0.0037  -0.0128 0.0252  405 ALA B CA  
7461 C C   . ALA B 405 ? 0.2641 0.3708 0.2851 0.0117  -0.0107 0.0229  405 ALA B C   
7462 O O   . ALA B 405 ? 0.2487 0.3612 0.2703 0.0204  -0.0102 0.0242  405 ALA B O   
7463 C CB  . ALA B 405 ? 0.2897 0.4220 0.3166 -0.0023 -0.0174 0.0282  405 ALA B CB  
7464 N N   . GLY B 406 ? 0.2982 0.3844 0.3141 0.0086  -0.0097 0.0196  406 GLY B N   
7465 C CA  . GLY B 406 ? 0.2588 0.3284 0.2700 0.0154  -0.0077 0.0176  406 GLY B CA  
7466 C C   . GLY B 406 ? 0.3143 0.3627 0.3204 0.0098  -0.0070 0.0146  406 GLY B C   
7467 O O   . GLY B 406 ? 0.2710 0.3178 0.2766 0.0004  -0.0085 0.0141  406 GLY B O   
7468 N N   . THR B 407 ? 0.2531 0.2853 0.2556 0.0158  -0.0049 0.0128  407 THR B N   
7469 C CA  . THR B 407 ? 0.2667 0.2774 0.2648 0.0124  -0.0035 0.0100  407 THR B CA  
7470 C C   . THR B 407 ? 0.2710 0.2699 0.2696 0.0200  -0.0001 0.0075  407 THR B C   
7471 O O   . THR B 407 ? 0.2381 0.2455 0.2399 0.0276  0.0009  0.0079  407 THR B O   
7472 C CB  . THR B 407 ? 0.3169 0.3176 0.3095 0.0120  -0.0046 0.0108  407 THR B CB  
7473 O OG1 . THR B 407 ? 0.3064 0.3051 0.2986 0.0221  -0.0032 0.0116  407 THR B OG1 
7474 C CG2 . THR B 407 ? 0.2667 0.2801 0.2586 0.0060  -0.0086 0.0135  407 THR B CG2 
7475 N N   . TRP B 408 ? 0.2718 0.2506 0.2673 0.0182  0.0016  0.0050  408 TRP B N   
7476 C CA  . TRP B 408 ? 0.2571 0.2230 0.2532 0.0255  0.0044  0.0028  408 TRP B CA  
7477 C C   . TRP B 408 ? 0.3371 0.2970 0.3314 0.0341  0.0050  0.0039  408 TRP B C   
7478 O O   . TRP B 408 ? 0.3618 0.3109 0.3568 0.0410  0.0070  0.0024  408 TRP B O   
7479 C CB  . TRP B 408 ? 0.2766 0.2235 0.2708 0.0202  0.0059  -0.0003 408 TRP B CB  
7480 C CG  . TRP B 408 ? 0.2852 0.2190 0.2747 0.0146  0.0055  -0.0001 408 TRP B CG  
7481 C CD1 . TRP B 408 ? 0.3089 0.2448 0.2950 0.0141  0.0040  0.0023  408 TRP B CD1 
7482 C CD2 . TRP B 408 ? 0.3281 0.2444 0.3154 0.0089  0.0067  -0.0025 408 TRP B CD2 
7483 N NE1 . TRP B 408 ? 0.4198 0.3406 0.4014 0.0087  0.0042  0.0016  408 TRP B NE1 
7484 C CE2 . TRP B 408 ? 0.3410 0.2497 0.3234 0.0053  0.0060  -0.0012 408 TRP B CE2 
7485 C CE3 . TRP B 408 ? 0.2685 0.1746 0.2572 0.0065  0.0084  -0.0056 408 TRP B CE3 
7486 C CZ2 . TRP B 408 ? 0.3568 0.2485 0.3359 -0.0003 0.0070  -0.0028 408 TRP B CZ2 
7487 C CZ3 . TRP B 408 ? 0.3067 0.1961 0.2925 0.0007  0.0092  -0.0073 408 TRP B CZ3 
7488 C CH2 . TRP B 408 ? 0.3028 0.1852 0.2838 -0.0027 0.0086  -0.0058 408 TRP B CH2 
7489 N N   . PHE B 409 ? 0.2862 0.2529 0.2784 0.0342  0.0032  0.0066  409 PHE B N   
7490 C CA  . PHE B 409 ? 0.4319 0.3970 0.4230 0.0431  0.0036  0.0081  409 PHE B CA  
7491 C C   . PHE B 409 ? 0.3708 0.3551 0.3656 0.0495  0.0028  0.0098  409 PHE B C   
7492 O O   . PHE B 409 ? 0.3949 0.3949 0.3902 0.0480  0.0006  0.0122  409 PHE B O   
7493 C CB  . PHE B 409 ? 0.5488 0.5110 0.5353 0.0405  0.0022  0.0101  409 PHE B CB  
7494 C CG  . PHE B 409 ? 0.6518 0.6131 0.6370 0.0494  0.0025  0.0119  409 PHE B CG  
7495 C CD1 . PHE B 409 ? 0.6104 0.5540 0.5938 0.0543  0.0048  0.0112  409 PHE B CD1 
7496 C CD2 . PHE B 409 ? 0.6876 0.6659 0.6736 0.0529  0.0005  0.0144  409 PHE B CD2 
7497 C CE1 . PHE B 409 ? 0.6587 0.6013 0.6409 0.0625  0.0051  0.0129  409 PHE B CE1 
7498 C CE2 . PHE B 409 ? 0.7291 0.7064 0.7136 0.0612  0.0008  0.0160  409 PHE B CE2 
7499 C CZ  . PHE B 409 ? 0.7215 0.6810 0.7040 0.0660  0.0031  0.0152  409 PHE B CZ  
7500 N N   . ASP B 410 ? 0.3725 0.3553 0.3698 0.0570  0.0045  0.0084  410 ASP B N   
7501 C CA  . ASP B 410 ? 0.4502 0.4491 0.4507 0.0648  0.0042  0.0097  410 ASP B CA  
7502 C C   . ASP B 410 ? 0.4223 0.4418 0.4261 0.0603  0.0027  0.0112  410 ASP B C   
7503 O O   . ASP B 410 ? 0.3850 0.4210 0.3912 0.0655  0.0020  0.0134  410 ASP B O   
7504 C CB  . ASP B 410 ? 0.5179 0.5208 0.5169 0.0717  0.0034  0.0121  410 ASP B CB  
7505 C CG  . ASP B 410 ? 0.6473 0.6314 0.6438 0.0773  0.0049  0.0111  410 ASP B CG  
7506 O OD1 . ASP B 410 ? 0.6814 0.6520 0.6786 0.0792  0.0066  0.0085  410 ASP B OD1 
7507 O OD2 . ASP B 410 ? 0.6801 0.6627 0.6740 0.0800  0.0043  0.0129  410 ASP B OD2 
7508 N N   . GLY B 411 ? 0.2833 0.3025 0.2875 0.0507  0.0023  0.0104  411 GLY B N   
7509 C CA  . GLY B 411 ? 0.2532 0.2919 0.2610 0.0457  0.0007  0.0123  411 GLY B CA  
7510 C C   . GLY B 411 ? 0.2946 0.3479 0.3027 0.0431  -0.0022 0.0158  411 GLY B C   
7511 O O   . GLY B 411 ? 0.3953 0.4675 0.4076 0.0416  -0.0035 0.0180  411 GLY B O   
7512 N N   . ASN B 412 ? 0.3555 0.4009 0.3595 0.0428  -0.0033 0.0164  412 ASN B N   
7513 C CA  . ASN B 412 ? 0.3263 0.3848 0.3302 0.0407  -0.0064 0.0196  412 ASN B CA  
7514 C C   . ASN B 412 ? 0.3450 0.3910 0.3435 0.0343  -0.0080 0.0193  412 ASN B C   
7515 O O   . ASN B 412 ? 0.3797 0.4079 0.3749 0.0314  -0.0064 0.0169  412 ASN B O   
7516 C CB  . ASN B 412 ? 0.3489 0.4158 0.3535 0.0508  -0.0064 0.0215  412 ASN B CB  
7517 C CG  . ASN B 412 ? 0.3599 0.4095 0.3602 0.0577  -0.0046 0.0201  412 ASN B CG  
7518 O OD1 . ASN B 412 ? 0.3859 0.4215 0.3816 0.0546  -0.0048 0.0196  412 ASN B OD1 
7519 N ND2 . ASN B 412 ? 0.3730 0.4239 0.3749 0.0675  -0.0029 0.0198  412 ASN B ND2 
7520 N N   . PHE B 413 ? 0.2906 0.3460 0.2881 0.0324  -0.0112 0.0219  413 PHE B N   
7521 C CA  . PHE B 413 ? 0.3851 0.4309 0.3771 0.0261  -0.0133 0.0220  413 PHE B CA  
7522 C C   . PHE B 413 ? 0.4047 0.4428 0.3919 0.0324  -0.0133 0.0229  413 PHE B C   
7523 O O   . PHE B 413 ? 0.3441 0.3763 0.3263 0.0284  -0.0154 0.0235  413 PHE B O   
7524 C CB  . PHE B 413 ? 0.4087 0.4694 0.4024 0.0182  -0.0176 0.0242  413 PHE B CB  
7525 C CG  . PHE B 413 ? 0.3645 0.4317 0.3626 0.0108  -0.0179 0.0236  413 PHE B CG  
7526 C CD1 . PHE B 413 ? 0.3237 0.3787 0.3189 0.0024  -0.0181 0.0215  413 PHE B CD1 
7527 C CD2 . PHE B 413 ? 0.2970 0.3825 0.3020 0.0125  -0.0178 0.0251  413 PHE B CD2 
7528 C CE1 . PHE B 413 ? 0.2711 0.3319 0.2703 -0.0044 -0.0183 0.0209  413 PHE B CE1 
7529 C CE2 . PHE B 413 ? 0.3026 0.3942 0.3117 0.0059  -0.0178 0.0248  413 PHE B CE2 
7530 C CZ  . PHE B 413 ? 0.2746 0.3538 0.2808 -0.0026 -0.0181 0.0226  413 PHE B CZ  
7531 N N   . LEU B 414 ? 0.2575 0.2950 0.2456 0.0423  -0.0110 0.0230  414 LEU B N   
7532 C CA  . LEU B 414 ? 0.4212 0.4536 0.4053 0.0485  -0.0111 0.0242  414 LEU B CA  
7533 C C   . LEU B 414 ? 0.4120 0.4229 0.3898 0.0470  -0.0098 0.0229  414 LEU B C   
7534 O O   . LEU B 414 ? 0.4308 0.4370 0.4044 0.0507  -0.0102 0.0242  414 LEU B O   
7535 C CB  . LEU B 414 ? 0.4501 0.4854 0.4366 0.0595  -0.0090 0.0244  414 LEU B CB  
7536 C CG  . LEU B 414 ? 0.4321 0.4897 0.4242 0.0625  -0.0104 0.0262  414 LEU B CG  
7537 C CD1 . LEU B 414 ? 0.4433 0.5031 0.4364 0.0739  -0.0087 0.0266  414 LEU B CD1 
7538 C CD2 . LEU B 414 ? 0.4248 0.4965 0.4168 0.0581  -0.0145 0.0290  414 LEU B CD2 
7539 N N   . LYS B 415 ? 0.4494 0.4475 0.4265 0.0417  -0.0081 0.0206  415 LYS B N   
7540 C CA  . LYS B 415 ? 0.4428 0.4207 0.4142 0.0402  -0.0065 0.0197  415 LYS B CA  
7541 C C   . LYS B 415 ? 0.4145 0.3908 0.3807 0.0327  -0.0095 0.0206  415 LYS B C   
7542 O O   . LYS B 415 ? 0.3952 0.3564 0.3557 0.0325  -0.0086 0.0206  415 LYS B O   
7543 C CB  . LYS B 415 ? 0.4981 0.4626 0.4709 0.0377  -0.0036 0.0169  415 LYS B CB  
7544 C CG  . LYS B 415 ? 0.6252 0.5684 0.5931 0.0361  -0.0016 0.0159  415 LYS B CG  
7545 C CD  . LYS B 415 ? 0.7445 0.6773 0.7113 0.0453  0.0009  0.0167  415 LYS B CD  
7546 C CE  . LYS B 415 ? 0.8117 0.7295 0.7720 0.0440  0.0016  0.0177  415 LYS B CE  
7547 N NZ  . LYS B 415 ? 0.8436 0.7491 0.8036 0.0525  0.0045  0.0184  415 LYS B NZ  
7548 N N   . TRP B 416 ? 0.3062 0.2976 0.2741 0.0267  -0.0132 0.0215  416 TRP B N   
7549 C CA  . TRP B 416 ? 0.3292 0.3192 0.2922 0.0192  -0.0167 0.0222  416 TRP B CA  
7550 C C   . TRP B 416 ? 0.3778 0.3842 0.3410 0.0193  -0.0211 0.0248  416 TRP B C   
7551 O O   . TRP B 416 ? 0.3626 0.3686 0.3215 0.0137  -0.0247 0.0255  416 TRP B O   
7552 C CB  . TRP B 416 ? 0.2964 0.2860 0.2606 0.0092  -0.0177 0.0206  416 TRP B CB  
7553 C CG  . TRP B 416 ? 0.3816 0.3557 0.3461 0.0085  -0.0137 0.0178  416 TRP B CG  
7554 C CD1 . TRP B 416 ? 0.3990 0.3549 0.3581 0.0047  -0.0124 0.0163  416 TRP B CD1 
7555 C CD2 . TRP B 416 ? 0.3993 0.3746 0.3694 0.0118  -0.0106 0.0163  416 TRP B CD2 
7556 N NE1 . TRP B 416 ? 0.3383 0.2841 0.3000 0.0052  -0.0087 0.0140  416 TRP B NE1 
7557 C CE2 . TRP B 416 ? 0.4078 0.3649 0.3760 0.0095  -0.0077 0.0138  416 TRP B CE2 
7558 C CE3 . TRP B 416 ? 0.3571 0.3469 0.3335 0.0166  -0.0101 0.0168  416 TRP B CE3 
7559 C CZ2 . TRP B 416 ? 0.4292 0.3819 0.4016 0.0120  -0.0046 0.0117  416 TRP B CZ2 
7560 C CZ3 . TRP B 416 ? 0.3486 0.3339 0.3287 0.0193  -0.0069 0.0147  416 TRP B CZ3 
7561 C CH2 . TRP B 416 ? 0.4212 0.3880 0.3994 0.0169  -0.0043 0.0121  416 TRP B CH2 
7562 N N   . ILE B 417 ? 0.3281 0.3489 0.2963 0.0257  -0.0211 0.0263  417 ILE B N   
7563 C CA  . ILE B 417 ? 0.3748 0.4126 0.3443 0.0260  -0.0252 0.0289  417 ILE B CA  
7564 C C   . ILE B 417 ? 0.4306 0.4781 0.4041 0.0358  -0.0236 0.0301  417 ILE B C   
7565 O O   . ILE B 417 ? 0.4045 0.4496 0.3812 0.0404  -0.0199 0.0288  417 ILE B O   
7566 C CB  . ILE B 417 ? 0.3838 0.4367 0.3583 0.0174  -0.0288 0.0296  417 ILE B CB  
7567 C CG1 . ILE B 417 ? 0.4250 0.4918 0.3995 0.0157  -0.0341 0.0324  417 ILE B CG1 
7568 C CG2 . ILE B 417 ? 0.4297 0.4947 0.4123 0.0193  -0.0266 0.0295  417 ILE B CG2 
7569 C CD1 . ILE B 417 ? 0.3760 0.4526 0.3535 0.0054  -0.0384 0.0331  417 ILE B CD1 
7570 N N   . GLY B 418 ? 0.4647 0.5228 0.4376 0.0391  -0.0264 0.0324  418 GLY B N   
7571 C CA  . GLY B 418 ? 0.4814 0.5516 0.4585 0.0479  -0.0255 0.0338  418 GLY B CA  
7572 C C   . GLY B 418 ? 0.5314 0.5941 0.5037 0.0565  -0.0245 0.0345  418 GLY B C   
7573 O O   . GLY B 418 ? 0.5357 0.6095 0.5109 0.0638  -0.0244 0.0359  418 GLY B O   
7574 N N   . ASN B 419 ? 0.5666 0.6113 0.5318 0.0565  -0.0234 0.0336  419 ASN B N   
7575 C CA  . ASN B 419 ? 0.6229 0.6616 0.5833 0.0643  -0.0229 0.0347  419 ASN B CA  
7576 C C   . ASN B 419 ? 0.6366 0.6707 0.5901 0.0604  -0.0263 0.0357  419 ASN B C   
7577 O O   . ASN B 419 ? 0.6399 0.6724 0.5917 0.0518  -0.0287 0.0352  419 ASN B O   
7578 C CB  . ASN B 419 ? 0.6646 0.6854 0.6230 0.0702  -0.0180 0.0333  419 ASN B CB  
7579 C CG  . ASN B 419 ? 0.6996 0.7012 0.6528 0.0649  -0.0164 0.0319  419 ASN B CG  
7580 O OD1 . ASN B 419 ? 0.7769 0.7778 0.7277 0.0568  -0.0189 0.0317  419 ASN B OD1 
7581 N ND2 . ASN B 419 ? 0.6963 0.6822 0.6482 0.0697  -0.0123 0.0311  419 ASN B ND2 
7582 N N   . LYS B 420 ? 0.5546 0.5861 0.5036 0.0671  -0.0266 0.0371  420 LYS B N   
7583 C CA  . LYS B 420 ? 0.5325 0.5625 0.4748 0.0647  -0.0305 0.0383  420 LYS B CA  
7584 C C   . LYS B 420 ? 0.5607 0.5742 0.4966 0.0582  -0.0304 0.0371  420 LYS B C   
7585 O O   . LYS B 420 ? 0.5318 0.5478 0.4647 0.0515  -0.0348 0.0374  420 LYS B O   
7586 C CB  . LYS B 420 ? 0.4790 0.5055 0.4169 0.0739  -0.0298 0.0397  420 LYS B CB  
7587 C CG  . LYS B 420 ? 0.5832 0.6080 0.5136 0.0725  -0.0340 0.0410  420 LYS B CG  
7588 C CD  . LYS B 420 ? 0.6784 0.6940 0.6029 0.0814  -0.0321 0.0421  420 LYS B CD  
7589 C CE  . LYS B 420 ? 0.7508 0.7544 0.6654 0.0794  -0.0342 0.0425  420 LYS B CE  
7590 N NZ  . LYS B 420 ? 0.7869 0.7921 0.6965 0.0864  -0.0359 0.0443  420 LYS B NZ  
7591 N N   . GLU B 421 ? 0.5927 0.5894 0.5266 0.0601  -0.0257 0.0358  421 GLU B N   
7592 C CA  . GLU B 421 ? 0.6447 0.6246 0.5721 0.0547  -0.0251 0.0348  421 GLU B CA  
7593 C C   . GLU B 421 ? 0.5990 0.5824 0.5293 0.0447  -0.0269 0.0333  421 GLU B C   
7594 O O   . GLU B 421 ? 0.5764 0.5567 0.5018 0.0381  -0.0302 0.0332  421 GLU B O   
7595 C CB  . GLU B 421 ? 0.7709 0.7330 0.6970 0.0595  -0.0193 0.0341  421 GLU B CB  
7596 C CG  . GLU B 421 ? 0.8574 0.8180 0.7836 0.0702  -0.0167 0.0355  421 GLU B CG  
7597 C CD  . GLU B 421 ? 0.9218 0.8946 0.8564 0.0748  -0.0155 0.0351  421 GLU B CD  
7598 O OE1 . GLU B 421 ? 0.9490 0.9393 0.8882 0.0724  -0.0187 0.0353  421 GLU B OE1 
7599 O OE2 . GLU B 421 ? 0.9552 0.9203 0.8920 0.0811  -0.0116 0.0348  421 GLU B OE2 
7600 N N   . LYS B 422 ? 0.5637 0.5532 0.5016 0.0436  -0.0249 0.0321  422 LYS B N   
7601 C CA  . LYS B 422 ? 0.4712 0.4636 0.4121 0.0343  -0.0263 0.0307  422 LYS B CA  
7602 C C   . LYS B 422 ? 0.4674 0.4764 0.4100 0.0286  -0.0321 0.0319  422 LYS B C   
7603 O O   . LYS B 422 ? 0.4856 0.4935 0.4268 0.0200  -0.0348 0.0312  422 LYS B O   
7604 C CB  . LYS B 422 ? 0.4850 0.4810 0.4336 0.0352  -0.0229 0.0292  422 LYS B CB  
7605 C CG  . LYS B 422 ? 0.5029 0.4811 0.4504 0.0391  -0.0176 0.0277  422 LYS B CG  
7606 C CD  . LYS B 422 ? 0.4694 0.4527 0.4244 0.0424  -0.0148 0.0265  422 LYS B CD  
7607 C CE  . LYS B 422 ? 0.4722 0.4387 0.4267 0.0482  -0.0100 0.0254  422 LYS B CE  
7608 N NZ  . LYS B 422 ? 0.4732 0.4214 0.4231 0.0430  -0.0084 0.0241  422 LYS B NZ  
7609 N N   . ASN B 423 ? 0.4207 0.4451 0.3666 0.0332  -0.0343 0.0339  423 ASN B N   
7610 C CA  . ASN B 423 ? 0.3778 0.4185 0.3261 0.0281  -0.0401 0.0355  423 ASN B CA  
7611 C C   . ASN B 423 ? 0.4545 0.4878 0.3944 0.0241  -0.0444 0.0358  423 ASN B C   
7612 O O   . ASN B 423 ? 0.4793 0.5181 0.4196 0.0160  -0.0490 0.0360  423 ASN B O   
7613 C CB  . ASN B 423 ? 0.3619 0.4197 0.3151 0.0348  -0.0412 0.0376  423 ASN B CB  
7614 C CG  . ASN B 423 ? 0.3902 0.4604 0.3526 0.0365  -0.0387 0.0375  423 ASN B CG  
7615 O OD1 . ASN B 423 ? 0.3307 0.3982 0.2962 0.0318  -0.0367 0.0360  423 ASN B OD1 
7616 N ND2 . ASN B 423 ? 0.3866 0.4703 0.3533 0.0434  -0.0387 0.0392  423 ASN B ND2 
7617 N N   . GLU B 424 ? 0.5084 0.5284 0.4404 0.0297  -0.0430 0.0360  424 GLU B N   
7618 C CA  . GLU B 424 ? 0.5521 0.5643 0.4752 0.0268  -0.0470 0.0364  424 GLU B CA  
7619 C C   . GLU B 424 ? 0.5049 0.5063 0.4244 0.0180  -0.0478 0.0347  424 GLU B C   
7620 O O   . GLU B 424 ? 0.5264 0.5291 0.4421 0.0120  -0.0532 0.0349  424 GLU B O   
7621 C CB  . GLU B 424 ? 0.6858 0.6846 0.6011 0.0350  -0.0444 0.0369  424 GLU B CB  
7622 C CG  . GLU B 424 ? 0.8532 0.8566 0.7631 0.0379  -0.0492 0.0387  424 GLU B CG  
7623 C CD  . GLU B 424 ? 0.9533 0.9496 0.8553 0.0314  -0.0541 0.0384  424 GLU B CD  
7624 O OE1 . GLU B 424 ? 0.9820 0.9885 0.8833 0.0291  -0.0603 0.0396  424 GLU B OE1 
7625 O OE2 . GLU B 424 ? 0.9929 0.9729 0.8890 0.0287  -0.0519 0.0371  424 GLU B OE2 
7626 N N   . TYR B 425 ? 0.4422 0.4330 0.3630 0.0171  -0.0428 0.0329  425 TYR B N   
7627 C CA  . TYR B 425 ? 0.4876 0.4687 0.4057 0.0086  -0.0433 0.0311  425 TYR B CA  
7628 C C   . TYR B 425 ? 0.4618 0.4576 0.3858 -0.0001 -0.0479 0.0311  425 TYR B C   
7629 O O   . TYR B 425 ? 0.4306 0.4235 0.3504 -0.0074 -0.0522 0.0307  425 TYR B O   
7630 C CB  . TYR B 425 ? 0.5023 0.4711 0.4222 0.0096  -0.0369 0.0292  425 TYR B CB  
7631 C CG  . TYR B 425 ? 0.4625 0.4102 0.3737 0.0118  -0.0338 0.0287  425 TYR B CG  
7632 C CD1 . TYR B 425 ? 0.3830 0.3245 0.2874 0.0185  -0.0338 0.0303  425 TYR B CD1 
7633 C CD2 . TYR B 425 ? 0.4401 0.3743 0.3500 0.0074  -0.0309 0.0268  425 TYR B CD2 
7634 C CE1 . TYR B 425 ? 0.4557 0.3782 0.3523 0.0208  -0.0306 0.0302  425 TYR B CE1 
7635 C CE2 . TYR B 425 ? 0.4385 0.3538 0.3409 0.0095  -0.0278 0.0267  425 TYR B CE2 
7636 C CZ  . TYR B 425 ? 0.5116 0.4214 0.4075 0.0162  -0.0276 0.0285  425 TYR B CZ  
7637 O OH  . TYR B 425 ? 0.6141 0.5052 0.5027 0.0186  -0.0243 0.0287  425 TYR B OH  
7638 N N   . TRP B 426 ? 0.3459 0.3576 0.2796 0.0008  -0.0472 0.0317  426 TRP B N   
7639 C CA  . TRP B 426 ? 0.3867 0.4141 0.3269 -0.0069 -0.0515 0.0323  426 TRP B CA  
7640 C C   . TRP B 426 ? 0.4221 0.4586 0.3601 -0.0093 -0.0586 0.0342  426 TRP B C   
7641 O O   . TRP B 426 ? 0.3953 0.4353 0.3334 -0.0177 -0.0634 0.0343  426 TRP B O   
7642 C CB  . TRP B 426 ? 0.3559 0.3992 0.3066 -0.0040 -0.0492 0.0330  426 TRP B CB  
7643 C CG  . TRP B 426 ? 0.3005 0.3360 0.2540 -0.0039 -0.0435 0.0308  426 TRP B CG  
7644 C CD1 . TRP B 426 ? 0.3707 0.3984 0.3246 0.0039  -0.0379 0.0299  426 TRP B CD1 
7645 C CD2 . TRP B 426 ? 0.3530 0.3871 0.3094 -0.0120 -0.0431 0.0292  426 TRP B CD2 
7646 N NE1 . TRP B 426 ? 0.3687 0.3901 0.3254 0.0013  -0.0343 0.0277  426 TRP B NE1 
7647 C CE2 . TRP B 426 ? 0.3813 0.4065 0.3394 -0.0084 -0.0372 0.0272  426 TRP B CE2 
7648 C CE3 . TRP B 426 ? 0.3677 0.4070 0.3254 -0.0218 -0.0474 0.0292  426 TRP B CE3 
7649 C CZ2 . TRP B 426 ? 0.3797 0.4011 0.3406 -0.0142 -0.0354 0.0252  426 TRP B CZ2 
7650 C CZ3 . TRP B 426 ? 0.3780 0.4135 0.3383 -0.0277 -0.0454 0.0273  426 TRP B CZ3 
7651 C CH2 . TRP B 426 ? 0.3846 0.4112 0.3464 -0.0238 -0.0394 0.0252  426 TRP B CH2 
7652 N N   . LYS B 427 ? 0.4592 0.4991 0.3951 -0.0019 -0.0594 0.0358  427 LYS B N   
7653 C CA  . LYS B 427 ? 0.4782 0.5246 0.4109 -0.0034 -0.0662 0.0376  427 LYS B CA  
7654 C C   . LYS B 427 ? 0.4968 0.5283 0.4195 -0.0088 -0.0696 0.0364  427 LYS B C   
7655 O O   . LYS B 427 ? 0.5110 0.5485 0.4336 -0.0156 -0.0760 0.0370  427 LYS B O   
7656 C CB  . LYS B 427 ? 0.4964 0.5452 0.4269 0.0063  -0.0656 0.0391  427 LYS B CB  
7657 C CG  . LYS B 427 ? 0.5237 0.5856 0.4546 0.0057  -0.0727 0.0413  427 LYS B CG  
7658 C CD  . LYS B 427 ? 0.6149 0.6793 0.5440 0.0157  -0.0715 0.0426  427 LYS B CD  
7659 C CE  . LYS B 427 ? 0.6980 0.7454 0.6148 0.0193  -0.0722 0.0421  427 LYS B CE  
7660 N NZ  . LYS B 427 ? 0.7075 0.7564 0.6216 0.0289  -0.0715 0.0435  427 LYS B NZ  
7661 N N   . ILE B 428 ? 0.5331 0.5452 0.4477 -0.0058 -0.0653 0.0349  428 ILE B N   
7662 C CA  . ILE B 428 ? 0.5046 0.5016 0.4092 -0.0106 -0.0680 0.0337  428 ILE B CA  
7663 C C   . ILE B 428 ? 0.4517 0.4500 0.3594 -0.0209 -0.0701 0.0324  428 ILE B C   
7664 O O   . ILE B 428 ? 0.4685 0.4657 0.3720 -0.0273 -0.0761 0.0323  428 ILE B O   
7665 C CB  . ILE B 428 ? 0.5061 0.4824 0.4025 -0.0053 -0.0621 0.0325  428 ILE B CB  
7666 C CG1 . ILE B 428 ? 0.4946 0.4683 0.3865 0.0045  -0.0607 0.0340  428 ILE B CG1 
7667 C CG2 . ILE B 428 ? 0.4869 0.4475 0.3738 -0.0110 -0.0640 0.0311  428 ILE B CG2 
7668 C CD1 . ILE B 428 ? 0.5258 0.4864 0.4163 0.0112  -0.0531 0.0335  428 ILE B CD1 
7669 N N   . LEU B 429 ? 0.4503 0.4507 0.3652 -0.0226 -0.0654 0.0313  429 LEU B N   
7670 C CA  . LEU B 429 ? 0.4858 0.4879 0.4042 -0.0322 -0.0670 0.0300  429 LEU B CA  
7671 C C   . LEU B 429 ? 0.4404 0.4606 0.3647 -0.0384 -0.0741 0.0318  429 LEU B C   
7672 O O   . LEU B 429 ? 0.4333 0.4518 0.3554 -0.0466 -0.0789 0.0313  429 LEU B O   
7673 C CB  . LEU B 429 ? 0.4060 0.4091 0.3318 -0.0318 -0.0608 0.0288  429 LEU B CB  
7674 C CG  . LEU B 429 ? 0.4445 0.4462 0.3731 -0.0413 -0.0612 0.0271  429 LEU B CG  
7675 C CD1 . LEU B 429 ? 0.5468 0.5277 0.4658 -0.0444 -0.0601 0.0248  429 LEU B CD1 
7676 C CD2 . LEU B 429 ? 0.3930 0.4008 0.3306 -0.0404 -0.0561 0.0263  429 LEU B CD2 
7677 N N   . ILE B 430 ? 0.4793 0.5170 0.4114 -0.0344 -0.0749 0.0340  430 ILE B N   
7678 C CA  . ILE B 430 ? 0.4161 0.4723 0.3551 -0.0399 -0.0815 0.0362  430 ILE B CA  
7679 C C   . ILE B 430 ? 0.4727 0.5254 0.4042 -0.0429 -0.0890 0.0368  430 ILE B C   
7680 O O   . ILE B 430 ? 0.4839 0.5412 0.4169 -0.0514 -0.0950 0.0372  430 ILE B O   
7681 C CB  . ILE B 430 ? 0.4145 0.4894 0.3626 -0.0339 -0.0805 0.0387  430 ILE B CB  
7682 C CG1 . ILE B 430 ? 0.4124 0.4947 0.3697 -0.0337 -0.0749 0.0383  430 ILE B CG1 
7683 C CG2 . ILE B 430 ? 0.3981 0.4907 0.3517 -0.0378 -0.0880 0.0415  430 ILE B CG2 
7684 C CD1 . ILE B 430 ? 0.4470 0.5372 0.4088 -0.0239 -0.0704 0.0394  430 ILE B CD1 
7685 N N   . GLU B 431 ? 0.4866 0.5302 0.4096 -0.0359 -0.0890 0.0369  431 GLU B N   
7686 C CA  . GLU B 431 ? 0.5028 0.5430 0.4181 -0.0378 -0.0964 0.0375  431 GLU B CA  
7687 C C   . GLU B 431 ? 0.4619 0.4860 0.3684 -0.0445 -0.0987 0.0354  431 GLU B C   
7688 O O   . GLU B 431 ? 0.5081 0.5339 0.4121 -0.0506 -0.1063 0.0358  431 GLU B O   
7689 C CB  . GLU B 431 ? 0.6128 0.6466 0.5206 -0.0281 -0.0954 0.0381  431 GLU B CB  
7690 C CG  . GLU B 431 ? 0.7362 0.7880 0.6514 -0.0229 -0.0970 0.0407  431 GLU B CG  
7691 C CD  . GLU B 431 ? 0.8897 0.9599 0.8132 -0.0298 -0.1044 0.0427  431 GLU B CD  
7692 O OE1 . GLU B 431 ? 0.9456 1.0126 0.8643 -0.0355 -0.1116 0.0427  431 GLU B OE1 
7693 O OE2 . GLU B 431 ? 0.9472 1.0351 0.8821 -0.0294 -0.1033 0.0445  431 GLU B OE2 
7694 N N   . ALA B 432 ? 0.3408 0.3491 0.2426 -0.0435 -0.0923 0.0332  432 ALA B N   
7695 C CA  . ALA B 432 ? 0.3864 0.3793 0.2801 -0.0498 -0.0939 0.0311  432 ALA B CA  
7696 C C   . ALA B 432 ? 0.4528 0.4537 0.3534 -0.0601 -0.0970 0.0307  432 ALA B C   
7697 O O   . ALA B 432 ? 0.4798 0.4740 0.3749 -0.0670 -0.1021 0.0297  432 ALA B O   
7698 C CB  . ALA B 432 ? 0.4156 0.3903 0.3035 -0.0458 -0.0860 0.0291  432 ALA B CB  
7699 N N   . LYS B 433 ? 0.4546 0.4695 0.3671 -0.0612 -0.0939 0.0313  433 LYS B N   
7700 C CA  . LYS B 433 ? 0.4456 0.4693 0.3655 -0.0708 -0.0966 0.0313  433 LYS B CA  
7701 C C   . LYS B 433 ? 0.4921 0.5267 0.4137 -0.0770 -0.1061 0.0332  433 LYS B C   
7702 O O   . LYS B 433 ? 0.4745 0.5082 0.3962 -0.0859 -0.1104 0.0325  433 LYS B O   
7703 C CB  . LYS B 433 ? 0.4351 0.4733 0.3674 -0.0696 -0.0917 0.0321  433 LYS B CB  
7704 C CG  . LYS B 433 ? 0.4206 0.4715 0.3621 -0.0788 -0.0946 0.0328  433 LYS B CG  
7705 C CD  . LYS B 433 ? 0.3884 0.4261 0.3262 -0.0858 -0.0930 0.0300  433 LYS B CD  
7706 C CE  . LYS B 433 ? 0.4916 0.5424 0.4383 -0.0953 -0.0968 0.0310  433 LYS B CE  
7707 N NZ  . LYS B 433 ? 0.5156 0.5543 0.4592 -0.1023 -0.0953 0.0282  433 LYS B NZ  
7708 N N   . LYS B 434 ? 0.5058 0.5503 0.4286 -0.0723 -0.1099 0.0355  434 LYS B N   
7709 C CA  . LYS B 434 ? 0.5612 0.6161 0.4859 -0.0777 -0.1194 0.0375  434 LYS B CA  
7710 C C   . LYS B 434 ? 0.5896 0.6290 0.5024 -0.0821 -0.1254 0.0359  434 LYS B C   
7711 O O   . LYS B 434 ? 0.6055 0.6513 0.5201 -0.0891 -0.1336 0.0370  434 LYS B O   
7712 C CB  . LYS B 434 ? 0.5877 0.6539 0.5147 -0.0708 -0.1218 0.0400  434 LYS B CB  
7713 C CG  . LYS B 434 ? 0.5634 0.6446 0.5012 -0.0653 -0.1161 0.0417  434 LYS B CG  
7714 C CD  . LYS B 434 ? 0.6301 0.7209 0.5690 -0.0579 -0.1182 0.0440  434 LYS B CD  
7715 C CE  . LYS B 434 ? 0.6871 0.7958 0.6382 -0.0539 -0.1137 0.0460  434 LYS B CE  
7716 N NZ  . LYS B 434 ? 0.7662 0.8806 0.7169 -0.0446 -0.1133 0.0476  434 LYS B NZ  
7717 N N   . LYS B 435 ? 0.6218 0.6413 0.5226 -0.0779 -0.1217 0.0335  435 LYS B N   
7718 C CA  . LYS B 435 ? 0.6432 0.6466 0.5313 -0.0809 -0.1268 0.0319  435 LYS B CA  
7719 C C   . LYS B 435 ? 0.6346 0.6211 0.5167 -0.0841 -0.1220 0.0290  435 LYS B C   
7720 O O   . LYS B 435 ? 0.6430 0.6126 0.5128 -0.0840 -0.1236 0.0274  435 LYS B O   
7721 C CB  . LYS B 435 ? 0.6907 0.6847 0.5680 -0.0724 -0.1277 0.0322  435 LYS B CB  
7722 C CG  . LYS B 435 ? 0.7607 0.7705 0.6434 -0.0683 -0.1321 0.0349  435 LYS B CG  
7723 C CD  . LYS B 435 ? 0.8172 0.8168 0.6889 -0.0590 -0.1319 0.0350  435 LYS B CD  
7724 C CE  . LYS B 435 ? 0.8452 0.8290 0.7028 -0.0609 -0.1381 0.0336  435 LYS B CE  
7725 N NZ  . LYS B 435 ? 0.8554 0.8361 0.7048 -0.0535 -0.1419 0.0346  435 LYS B NZ  
7726 N N   . ALA B 436 ? 0.6082 0.6556 0.4019 -0.0155 -0.0676 -0.0110 436 ALA B N   
7727 C CA  . ALA B 436 ? 0.6297 0.6611 0.4305 -0.0181 -0.0666 -0.0139 436 ALA B CA  
7728 C C   . ALA B 436 ? 0.5675 0.5969 0.3683 -0.0256 -0.0699 -0.0214 436 ALA B C   
7729 O O   . ALA B 436 ? 0.5853 0.6214 0.3849 -0.0295 -0.0737 -0.0242 436 ALA B O   
7730 C CB  . ALA B 436 ? 0.6500 0.6711 0.4582 -0.0178 -0.0675 -0.0113 436 ALA B CB  
7731 N N   . LYS B 437 ? 0.5119 0.5315 0.3157 -0.0270 -0.0677 -0.0245 437 LYS B N   
7732 C CA  . LYS B 437 ? 0.5334 0.5498 0.3375 -0.0338 -0.0701 -0.0316 437 LYS B CA  
7733 C C   . LYS B 437 ? 0.5699 0.5697 0.3819 -0.0364 -0.0696 -0.0339 437 LYS B C   
7734 O O   . LYS B 437 ? 0.5826 0.5780 0.3954 -0.0419 -0.0711 -0.0396 437 LYS B O   
7735 C CB  . LYS B 437 ? 0.5778 0.6015 0.3757 -0.0337 -0.0681 -0.0344 437 LYS B CB  
7736 C CG  . LYS B 437 ? 0.6884 0.7301 0.4781 -0.0320 -0.0691 -0.0333 437 LYS B CG  
7737 C CD  . LYS B 437 ? 0.7665 0.8153 0.5507 -0.0276 -0.0652 -0.0323 437 LYS B CD  
7738 C CE  . LYS B 437 ? 0.7921 0.8553 0.5724 -0.0232 -0.0647 -0.0293 437 LYS B CE  
7739 N NZ  . LYS B 437 ? 0.7531 0.8199 0.5323 -0.0169 -0.0631 -0.0216 437 LYS B NZ  
7740 N N   . ASN B 438 ? 0.5378 0.5284 0.3555 -0.0327 -0.0676 -0.0297 438 ASN B N   
7741 C CA  . ASN B 438 ? 0.5546 0.5301 0.3801 -0.0347 -0.0671 -0.0317 438 ASN B CA  
7742 C C   . ASN B 438 ? 0.5522 0.5215 0.3836 -0.0313 -0.0667 -0.0269 438 ASN B C   
7743 O O   . ASN B 438 ? 0.6063 0.5828 0.4356 -0.0276 -0.0666 -0.0223 438 ASN B O   
7744 C CB  . ASN B 438 ? 0.5158 0.4848 0.3421 -0.0333 -0.0630 -0.0331 438 ASN B CB  
7745 C CG  . ASN B 438 ? 0.5432 0.5153 0.3676 -0.0262 -0.0582 -0.0277 438 ASN B CG  
7746 O OD1 . ASN B 438 ? 0.5212 0.4877 0.3504 -0.0222 -0.0561 -0.0233 438 ASN B OD1 
7747 N ND2 . ASN B 438 ? 0.5559 0.5373 0.3735 -0.0245 -0.0564 -0.0280 438 ASN B ND2 
7748 N N   . ASP B 439 ? 0.5254 0.4816 0.3643 -0.0326 -0.0663 -0.0282 439 ASP B N   
7749 C CA  . ASP B 439 ? 0.4797 0.4293 0.3250 -0.0303 -0.0663 -0.0248 439 ASP B CA  
7750 C C   . ASP B 439 ? 0.4715 0.4182 0.3189 -0.0239 -0.0613 -0.0198 439 ASP B C   
7751 O O   . ASP B 439 ? 0.4875 0.4280 0.3408 -0.0219 -0.0608 -0.0172 439 ASP B O   
7752 C CB  . ASP B 439 ? 0.4694 0.4067 0.3219 -0.0343 -0.0681 -0.0284 439 ASP B CB  
7753 C CG  . ASP B 439 ? 0.5650 0.5046 0.4170 -0.0398 -0.0733 -0.0316 439 ASP B CG  
7754 O OD1 . ASP B 439 ? 0.5515 0.5017 0.3984 -0.0402 -0.0756 -0.0305 439 ASP B OD1 
7755 O OD2 . ASP B 439 ? 0.6444 0.5753 0.5010 -0.0437 -0.0749 -0.0352 439 ASP B OD2 
7756 N N   . TYR B 440 ? 0.4969 0.4479 0.3399 -0.0205 -0.0574 -0.0183 440 TYR B N   
7757 C CA  . TYR B 440 ? 0.4928 0.4418 0.3377 -0.0140 -0.0525 -0.0130 440 TYR B CA  
7758 C C   . TYR B 440 ? 0.5065 0.4631 0.3493 -0.0103 -0.0528 -0.0078 440 TYR B C   
7759 O O   . TYR B 440 ? 0.4695 0.4224 0.3158 -0.0054 -0.0493 -0.0033 440 TYR B O   
7760 C CB  . TYR B 440 ? 0.5531 0.5053 0.3936 -0.0109 -0.0481 -0.0123 440 TYR B CB  
7761 C CG  . TYR B 440 ? 0.5475 0.4879 0.3933 -0.0115 -0.0451 -0.0147 440 TYR B CG  
7762 C CD1 . TYR B 440 ? 0.5535 0.4844 0.4064 -0.0080 -0.0414 -0.0118 440 TYR B CD1 
7763 C CD2 . TYR B 440 ? 0.5259 0.4647 0.3700 -0.0156 -0.0460 -0.0199 440 TYR B CD2 
7764 C CE1 . TYR B 440 ? 0.5944 0.5147 0.4524 -0.0086 -0.0387 -0.0140 440 TYR B CE1 
7765 C CE2 . TYR B 440 ? 0.5181 0.4461 0.3670 -0.0160 -0.0433 -0.0220 440 TYR B CE2 
7766 C CZ  . TYR B 440 ? 0.5897 0.5087 0.4456 -0.0125 -0.0398 -0.0190 440 TYR B CZ  
7767 O OH  . TYR B 440 ? 0.6028 0.5115 0.4636 -0.0130 -0.0371 -0.0211 440 TYR B OH  
7768 N N   . ILE B 441 ? 0.4830 0.4498 0.3206 -0.0125 -0.0569 -0.0084 441 ILE B N   
7769 C CA  . ILE B 441 ? 0.5011 0.4745 0.3373 -0.0095 -0.0579 -0.0038 441 ILE B CA  
7770 C C   . ILE B 441 ? 0.4678 0.4316 0.3120 -0.0099 -0.0591 -0.0029 441 ILE B C   
7771 O O   . ILE B 441 ? 0.4426 0.4073 0.2882 -0.0057 -0.0575 0.0019  441 ILE B O   
7772 C CB  . ILE B 441 ? 0.5134 0.4996 0.3428 -0.0125 -0.0624 -0.0052 441 ILE B CB  
7773 C CG1 . ILE B 441 ? 0.5136 0.5091 0.3397 -0.0079 -0.0622 0.0005  441 ILE B CG1 
7774 C CG2 . ILE B 441 ? 0.4584 0.4408 0.2908 -0.0192 -0.0678 -0.0100 441 ILE B CG2 
7775 C CD1 . ILE B 441 ? 0.4755 0.4777 0.2970 -0.0013 -0.0571 0.0053  441 ILE B CD1 
7776 N N   . LEU B 442 ? 0.4325 0.3871 0.2821 -0.0148 -0.0616 -0.0075 442 LEU B N   
7777 C CA  . LEU B 442 ? 0.4356 0.3813 0.2930 -0.0150 -0.0626 -0.0068 442 LEU B CA  
7778 C C   . LEU B 442 ? 0.4009 0.3378 0.2641 -0.0105 -0.0574 -0.0041 442 LEU B C   
7779 O O   . LEU B 442 ? 0.4310 0.3642 0.2990 -0.0080 -0.0567 -0.0013 442 LEU B O   
7780 C CB  . LEU B 442 ? 0.4277 0.3663 0.2893 -0.0211 -0.0665 -0.0123 442 LEU B CB  
7781 C CG  . LEU B 442 ? 0.4752 0.4210 0.3321 -0.0261 -0.0716 -0.0155 442 LEU B CG  
7782 C CD1 . LEU B 442 ? 0.5044 0.4418 0.3654 -0.0317 -0.0742 -0.0209 442 LEU B CD1 
7783 C CD2 . LEU B 442 ? 0.5054 0.4575 0.3612 -0.0256 -0.0747 -0.0127 442 LEU B CD2 
7784 N N   . VAL B 443 ? 0.4210 0.3542 0.2841 -0.0096 -0.0537 -0.0052 443 VAL B N   
7785 C CA  . VAL B 443 ? 0.4095 0.3348 0.2781 -0.0053 -0.0483 -0.0026 443 VAL B CA  
7786 C C   . VAL B 443 ? 0.4342 0.3649 0.3006 0.0008  -0.0449 0.0037  443 VAL B C   
7787 O O   . VAL B 443 ? 0.4369 0.3615 0.3093 0.0038  -0.0422 0.0064  443 VAL B O   
7788 C CB  . VAL B 443 ? 0.3827 0.3047 0.2503 -0.0050 -0.0448 -0.0044 443 VAL B CB  
7789 C CG1 . VAL B 443 ? 0.3438 0.2575 0.2174 -0.0005 -0.0389 -0.0015 443 VAL B CG1 
7790 C CG2 . VAL B 443 ? 0.4155 0.3319 0.2851 -0.0109 -0.0479 -0.0105 443 VAL B CG2 
7791 N N   . ALA B 444 ? 0.4527 0.3952 0.3107 0.0027  -0.0449 0.0059  444 ALA B N   
7792 C CA  . ALA B 444 ? 0.4372 0.3862 0.2921 0.0088  -0.0415 0.0121  444 ALA B CA  
7793 C C   . ALA B 444 ? 0.4263 0.3769 0.2831 0.0093  -0.0440 0.0145  444 ALA B C   
7794 O O   . ALA B 444 ? 0.4211 0.3742 0.2775 0.0146  -0.0407 0.0198  444 ALA B O   
7795 C CB  . ALA B 444 ? 0.4140 0.3763 0.2592 0.0104  -0.0412 0.0134  444 ALA B CB  
7796 N N   . GLU B 445 ? 0.4256 0.3744 0.2847 0.0042  -0.0495 0.0108  445 GLU B N   
7797 C CA  . GLU B 445 ? 0.4579 0.4074 0.3193 0.0045  -0.0520 0.0129  445 GLU B CA  
7798 C C   . GLU B 445 ? 0.4160 0.3538 0.2870 0.0055  -0.0502 0.0131  445 GLU B C   
7799 O O   . GLU B 445 ? 0.4274 0.3648 0.3010 0.0059  -0.0520 0.0146  445 GLU B O   
7800 C CB  . GLU B 445 ? 0.4764 0.4302 0.3358 -0.0011 -0.0586 0.0091  445 GLU B CB  
7801 C CG  . GLU B 445 ? 0.4656 0.4329 0.3155 -0.0018 -0.0607 0.0093  445 GLU B CG  
7802 C CD  . GLU B 445 ? 0.5202 0.4901 0.3684 -0.0084 -0.0664 0.0041  445 GLU B CD  
7803 O OE1 . GLU B 445 ? 0.4756 0.4371 0.3297 -0.0122 -0.0690 0.0008  445 GLU B OE1 
7804 O OE2 . GLU B 445 ? 0.4740 0.4546 0.3150 -0.0098 -0.0682 0.0032  445 GLU B OE2 
7805 N N   . GLY B 446 ? 0.4514 0.3799 0.3275 0.0059  -0.0466 0.0117  446 GLY B N   
7806 C CA  . GLY B 446 ? 0.3245 0.2425 0.2097 0.0071  -0.0444 0.0120  446 GLY B CA  
7807 C C   . GLY B 446 ? 0.4156 0.3351 0.3016 0.0128  -0.0405 0.0177  446 GLY B C   
7808 O O   . GLY B 446 ? 0.3831 0.3088 0.2636 0.0172  -0.0368 0.0219  446 GLY B O   
7809 N N   . SER B 447 ? 0.4156 0.3293 0.3083 0.0129  -0.0411 0.0178  447 SER B N   
7810 C CA  . SER B 447 ? 0.3418 0.2565 0.2357 0.0180  -0.0376 0.0230  447 SER B CA  
7811 C C   . SER B 447 ? 0.3261 0.2362 0.2223 0.0229  -0.0300 0.0261  447 SER B C   
7812 O O   . SER B 447 ? 0.3538 0.2671 0.2480 0.0280  -0.0260 0.0313  447 SER B O   
7813 C CB  . SER B 447 ? 0.3133 0.2221 0.2147 0.0167  -0.0398 0.0217  447 SER B CB  
7814 O OG  . SER B 447 ? 0.3939 0.2916 0.3042 0.0156  -0.0377 0.0187  447 SER B OG  
7815 N N   . ASP B 448 ? 0.3497 0.2522 0.2501 0.0215  -0.0279 0.0231  448 ASP B N   
7816 C CA  . ASP B 448 ? 0.3902 0.2866 0.2947 0.0258  -0.0206 0.0258  448 ASP B CA  
7817 C C   . ASP B 448 ? 0.4072 0.3112 0.3040 0.0309  -0.0161 0.0309  448 ASP B C   
7818 O O   . ASP B 448 ? 0.3713 0.2733 0.2700 0.0361  -0.0100 0.0354  448 ASP B O   
7819 C CB  . ASP B 448 ? 0.3753 0.2631 0.2850 0.0229  -0.0197 0.0213  448 ASP B CB  
7820 C CG  . ASP B 448 ? 0.4133 0.2943 0.3303 0.0180  -0.0242 0.0162  448 ASP B CG  
7821 O OD1 . ASP B 448 ? 0.4153 0.2996 0.3293 0.0136  -0.0303 0.0129  448 ASP B OD1 
7822 O OD2 . ASP B 448 ? 0.4665 0.3390 0.3922 0.0186  -0.0216 0.0154  448 ASP B OD2 
7823 N N   . TRP B 449 ? 0.3803 0.2933 0.2686 0.0295  -0.0190 0.0303  449 TRP B N   
7824 C CA  . TRP B 449 ? 0.3061 0.2274 0.1867 0.0344  -0.0150 0.0349  449 TRP B CA  
7825 C C   . TRP B 449 ? 0.3484 0.2755 0.2264 0.0394  -0.0128 0.0409  449 TRP B C   
7826 O O   . TRP B 449 ? 0.3121 0.2408 0.1881 0.0453  -0.0066 0.0460  449 TRP B O   
7827 C CB  . TRP B 449 ? 0.4020 0.3328 0.2741 0.0314  -0.0193 0.0324  449 TRP B CB  
7828 C CG  . TRP B 449 ? 0.4409 0.3662 0.3156 0.0254  -0.0229 0.0259  449 TRP B CG  
7829 C CD1 . TRP B 449 ? 0.4318 0.3596 0.3047 0.0196  -0.0295 0.0212  449 TRP B CD1 
7830 C CD2 . TRP B 449 ? 0.4604 0.3764 0.3401 0.0247  -0.0196 0.0235  449 TRP B CD2 
7831 N NE1 . TRP B 449 ? 0.4656 0.3863 0.3420 0.0155  -0.0305 0.0162  449 TRP B NE1 
7832 C CE2 . TRP B 449 ? 0.4738 0.3873 0.3544 0.0186  -0.0247 0.0174  449 TRP B CE2 
7833 C CE3 . TRP B 449 ? 0.4230 0.3326 0.3067 0.0289  -0.0128 0.0260  449 TRP B CE3 
7834 C CZ2 . TRP B 449 ? 0.4584 0.3634 0.3434 0.0165  -0.0232 0.0138  449 TRP B CZ2 
7835 C CZ3 . TRP B 449 ? 0.4070 0.3081 0.2953 0.0266  -0.0115 0.0223  449 TRP B CZ3 
7836 C CH2 . TRP B 449 ? 0.4160 0.3150 0.3048 0.0205  -0.0167 0.0163  449 TRP B CH2 
7837 N N   . PHE B 450 ? 0.3722 0.3025 0.2499 0.0375  -0.0176 0.0404  450 PHE B N   
7838 C CA  . PHE B 450 ? 0.4081 0.3442 0.2831 0.0419  -0.0162 0.0459  450 PHE B CA  
7839 C C   . PHE B 450 ? 0.4762 0.4029 0.3595 0.0450  -0.0114 0.0483  450 PHE B C   
7840 O O   . PHE B 450 ? 0.4964 0.4257 0.3782 0.0505  -0.0070 0.0539  450 PHE B O   
7841 C CB  . PHE B 450 ? 0.3838 0.3269 0.2555 0.0384  -0.0233 0.0444  450 PHE B CB  
7842 C CG  . PHE B 450 ? 0.4429 0.3947 0.3074 0.0346  -0.0282 0.0412  450 PHE B CG  
7843 C CD1 . PHE B 450 ? 0.4179 0.3824 0.2731 0.0373  -0.0281 0.0445  450 PHE B CD1 
7844 C CD2 . PHE B 450 ? 0.4124 0.3598 0.2795 0.0283  -0.0328 0.0350  450 PHE B CD2 
7845 C CE1 . PHE B 450 ? 0.4134 0.3862 0.2622 0.0335  -0.0325 0.0412  450 PHE B CE1 
7846 C CE2 . PHE B 450 ? 0.3819 0.3369 0.2426 0.0246  -0.0370 0.0318  450 PHE B CE2 
7847 C CZ  . PHE B 450 ? 0.3983 0.3660 0.2499 0.0271  -0.0368 0.0348  450 PHE B CZ  
7848 N N   . TRP B 451 ? 0.4070 0.3227 0.2991 0.0415  -0.0121 0.0439  451 TRP B N   
7849 C CA  . TRP B 451 ? 0.4345 0.3409 0.3354 0.0439  -0.0076 0.0453  451 TRP B CA  
7850 C C   . TRP B 451 ? 0.4695 0.3733 0.3708 0.0498  0.0009  0.0500  451 TRP B C   
7851 O O   . TRP B 451 ? 0.4320 0.3343 0.3355 0.0544  0.0056  0.0545  451 TRP B O   
7852 C CB  . TRP B 451 ? 0.3957 0.2916 0.3057 0.0390  -0.0098 0.0393  451 TRP B CB  
7853 C CG  . TRP B 451 ? 0.5336 0.4214 0.4528 0.0395  -0.0081 0.0389  451 TRP B CG  
7854 C CD1 . TRP B 451 ? 0.6265 0.5142 0.5485 0.0371  -0.0128 0.0371  451 TRP B CD1 
7855 C CD2 . TRP B 451 ? 0.5732 0.4517 0.5003 0.0422  -0.0013 0.0399  451 TRP B CD2 
7856 N NE1 . TRP B 451 ? 0.6043 0.4835 0.5353 0.0382  -0.0094 0.0368  451 TRP B NE1 
7857 C CE2 . TRP B 451 ? 0.6053 0.4786 0.5398 0.0413  -0.0023 0.0385  451 TRP B CE2 
7858 C CE3 . TRP B 451 ? 0.6150 0.4891 0.5439 0.0454  0.0056  0.0419  451 TRP B CE3 
7859 C CZ2 . TRP B 451 ? 0.6015 0.4657 0.5451 0.0432  0.0034  0.0387  451 TRP B CZ2 
7860 C CZ3 . TRP B 451 ? 0.6197 0.4845 0.5577 0.0474  0.0114  0.0423  451 TRP B CZ3 
7861 C CH2 . TRP B 451 ? 0.6419 0.5018 0.5872 0.0462  0.0103  0.0406  451 TRP B CH2 
7862 N N   . TRP B 452 ? 0.4218 0.3251 0.3213 0.0499  0.0032  0.0492  452 TRP B N   
7863 C CA  . TRP B 452 ? 0.5334 0.4330 0.4343 0.0553  0.0116  0.0533  452 TRP B CA  
7864 C C   . TRP B 452 ? 0.6467 0.5566 0.5386 0.0612  0.0150  0.0597  452 TRP B C   
7865 O O   . TRP B 452 ? 0.4817 0.3891 0.3748 0.0669  0.0225  0.0646  452 TRP B O   
7866 C CB  . TRP B 452 ? 0.5300 0.4245 0.4328 0.0531  0.0128  0.0497  452 TRP B CB  
7867 C CG  . TRP B 452 ? 0.4998 0.3833 0.4126 0.0485  0.0111  0.0442  452 TRP B CG  
7868 C CD1 . TRP B 452 ? 0.4752 0.3571 0.3893 0.0423  0.0048  0.0381  452 TRP B CD1 
7869 C CD2 . TRP B 452 ? 0.5089 0.3817 0.4318 0.0497  0.0160  0.0442  452 TRP B CD2 
7870 N NE1 . TRP B 452 ? 0.4416 0.3129 0.3659 0.0398  0.0052  0.0344  452 TRP B NE1 
7871 C CE2 . TRP B 452 ? 0.4574 0.3231 0.3873 0.0441  0.0120  0.0379  452 TRP B CE2 
7872 C CE3 . TRP B 452 ? 0.5954 0.4641 0.5223 0.0550  0.0235  0.0489  452 TRP B CE3 
7873 C CZ2 . TRP B 452 ? 0.5172 0.3725 0.4579 0.0436  0.0150  0.0359  452 TRP B CZ2 
7874 C CZ3 . TRP B 452 ? 0.5940 0.4518 0.5319 0.0542  0.0267  0.0468  452 TRP B CZ3 
7875 C CH2 . TRP B 452 ? 0.5610 0.4125 0.5056 0.0485  0.0223  0.0403  452 TRP B CH2 
7876 N N   . GLN B 453 ? 0.9268 0.8482 0.8098 0.0602  0.0100  0.0599  453 GLN B N   
7877 C CA  . GLN B 453 ? 1.0137 0.9462 0.8873 0.0655  0.0127  0.0654  453 GLN B CA  
7878 C C   . GLN B 453 ? 1.0508 0.9898 0.9212 0.0690  0.0127  0.0702  453 GLN B C   
7879 O O   . GLN B 453 ? 1.1250 1.0746 0.9885 0.0679  0.0076  0.0703  453 GLN B O   
7880 C CB  . GLN B 453 ? 1.0862 1.0278 0.9519 0.0622  0.0077  0.0622  453 GLN B CB  
7881 C CG  . GLN B 453 ? 1.1438 1.0791 1.0121 0.0597  0.0088  0.0582  453 GLN B CG  
7882 C CD  . GLN B 453 ? 1.1666 1.1027 1.0326 0.0656  0.0163  0.0626  453 GLN B CD  
7883 O OE1 . GLN B 453 ? 1.1920 1.1376 1.0508 0.0709  0.0190  0.0679  453 GLN B OE1 
7884 N NE2 . GLN B 453 ? 1.1391 1.0655 1.0109 0.0648  0.0197  0.0605  453 GLN B NE2 
7885 N N   . GLY B 454 ? 1.0210 0.9533 0.8969 0.0734  0.0187  0.0742  454 GLY B N   
7886 C CA  . GLY B 454 ? 1.0741 1.0112 0.9477 0.0777  0.0203  0.0795  454 GLY B CA  
7887 C C   . GLY B 454 ? 1.1207 1.0468 1.0031 0.0807  0.0264  0.0819  454 GLY B C   
7888 O O   . GLY B 454 ? 1.1228 1.0489 1.0068 0.0817  0.0259  0.0837  454 GLY B O   
7889 N N   . GLU B 455 ? 1.1444 1.0613 1.0327 0.0820  0.0325  0.0818  455 GLU B N   
7890 C CA  . GLU B 455 ? 1.1618 1.0667 1.0600 0.0835  0.0380  0.0824  455 GLU B CA  
7891 C C   . GLU B 455 ? 1.2380 1.1377 1.1386 0.0885  0.0471  0.0861  455 GLU B C   
7892 O O   . GLU B 455 ? 1.2614 1.1672 1.1553 0.0913  0.0492  0.0886  455 GLU B O   
7893 C CB  . GLU B 455 ? 1.1097 1.0052 1.0171 0.0767  0.0335  0.0750  455 GLU B CB  
7894 C CG  . GLU B 455 ? 1.1025 0.9968 1.0133 0.0742  0.0291  0.0733  455 GLU B CG  
7895 C CD  . GLU B 455 ? 1.1286 1.0314 1.0336 0.0695  0.0198  0.0700  455 GLU B CD  
7896 O OE1 . GLU B 455 ? 1.1294 1.0327 1.0361 0.0676  0.0156  0.0688  455 GLU B OE1 
7897 O OE2 . GLU B 455 ? 1.1548 1.0635 1.0536 0.0676  0.0166  0.0684  455 GLU B OE2 
7898 N N   . GLU B 456 ? 1.2783 1.1666 1.1885 0.0896  0.0527  0.0864  456 GLU B N   
7899 C CA  . GLU B 456 ? 1.3131 1.1941 1.2276 0.0936  0.0616  0.0891  456 GLU B CA  
7900 C C   . GLU B 456 ? 1.2878 1.1671 1.2022 0.0906  0.0604  0.0852  456 GLU B C   
7901 O O   . GLU B 456 ? 1.2615 1.1357 1.1812 0.0843  0.0555  0.0785  456 GLU B O   
7902 C CB  . GLU B 456 ? 1.3451 1.2135 1.2716 0.0932  0.0661  0.0878  456 GLU B CB  
7903 C CG  . GLU B 456 ? 1.3640 1.2328 1.2912 0.0962  0.0679  0.0915  456 GLU B CG  
7904 C CD  . GLU B 456 ? 1.3949 1.2666 1.3179 0.1045  0.0765  0.1000  456 GLU B CD  
7905 O OE1 . GLU B 456 ? 1.4067 1.2834 1.3260 0.1078  0.0768  0.1042  456 GLU B OE1 
7906 O OE2 . GLU B 456 ? 1.4064 1.2754 1.3298 0.1079  0.0830  0.1026  456 GLU B OE2 
7907 N N   . LYS B 457 ? 1.2781 1.1620 1.1866 0.0952  0.0652  0.0894  457 LYS B N   
7908 C CA  . LYS B 457 ? 1.2322 1.1168 1.1386 0.0929  0.0637  0.0863  457 LYS B CA  
7909 C C   . LYS B 457 ? 1.2118 1.0835 1.1286 0.0915  0.0685  0.0835  457 LYS B C   
7910 O O   . LYS B 457 ? 1.2444 1.1102 1.1653 0.0964  0.0771  0.0878  457 LYS B O   
7911 C CB  . LYS B 457 ? 1.1978 1.0924 1.0942 0.0988  0.0673  0.0919  457 LYS B CB  
7912 C CG  . LYS B 457 ? 1.1343 1.0414 1.0215 0.1023  0.0654  0.0966  457 LYS B CG  
7913 C CD  . LYS B 457 ? 1.0703 0.9891 0.9467 0.1066  0.0667  0.1005  457 LYS B CD  
7914 C CE  . LYS B 457 ? 1.0258 0.9586 0.8925 0.1082  0.0623  0.1032  457 LYS B CE  
7915 N NZ  . LYS B 457 ? 0.9934 0.9244 0.8634 0.1069  0.0598  0.1033  457 LYS B NZ  
7916 N N   . ALA B 458 ? 1.1520 1.0193 1.0728 0.0850  0.0630  0.0765  458 ALA B N   
7917 C CA  . ALA B 458 ? 1.0981 0.9534 1.0292 0.0824  0.0659  0.0726  458 ALA B CA  
7918 C C   . ALA B 458 ? 1.0759 0.9314 1.0045 0.0821  0.0671  0.0714  458 ALA B C   
7919 O O   . ALA B 458 ? 1.0516 0.9167 0.9705 0.0826  0.0642  0.0722  458 ALA B O   
7920 C CB  . ALA B 458 ? 1.0612 0.9116 0.9989 0.0753  0.0588  0.0655  458 ALA B CB  
7921 N N   . PRO B 459 ? 1.0850 0.9302 1.0222 0.0813  0.0716  0.0693  459 PRO B N   
7922 C CA  . PRO B 459 ? 1.0773 0.9223 1.0121 0.0820  0.0740  0.0689  459 PRO B CA  
7923 C C   . PRO B 459 ? 1.0626 0.9122 0.9923 0.0767  0.0663  0.0635  459 PRO B C   
7924 O O   . PRO B 459 ? 1.0952 0.9449 1.0227 0.0775  0.0684  0.0633  459 PRO B O   
7925 C CB  . PRO B 459 ? 1.0782 0.9103 1.0250 0.0813  0.0796  0.0670  459 PRO B CB  
7926 C CG  . PRO B 459 ? 1.0874 0.9147 1.0404 0.0837  0.0839  0.0697  459 PRO B CG  
7927 C CD  . PRO B 459 ? 1.0953 0.9292 1.0441 0.0816  0.0768  0.0689  459 PRO B CD  
7928 N N   . PHE B 460 ? 0.9733 0.8264 0.9012 0.0716  0.0578  0.0592  460 PHE B N   
7929 C CA  . PHE B 460 ? 0.8264 0.6839 0.7493 0.0668  0.0511  0.0543  460 PHE B CA  
7930 C C   . PHE B 460 ? 0.7349 0.6030 0.6493 0.0646  0.0435  0.0535  460 PHE B C   
7931 O O   . PHE B 460 ? 0.7462 0.6173 0.6572 0.0598  0.0374  0.0488  460 PHE B O   
7932 C CB  . PHE B 460 ? 0.8055 0.6536 0.7370 0.0606  0.0478  0.0474  460 PHE B CB  
7933 C CG  . PHE B 460 ? 0.8201 0.6594 0.7583 0.0618  0.0540  0.0470  460 PHE B CG  
7934 C CD1 . PHE B 460 ? 0.8071 0.6489 0.7401 0.0642  0.0571  0.0486  460 PHE B CD1 
7935 C CD2 . PHE B 460 ? 0.8295 0.6582 0.7792 0.0604  0.0567  0.0449  460 PHE B CD2 
7936 C CE1 . PHE B 460 ? 0.7492 0.5829 0.6885 0.0653  0.0630  0.0483  460 PHE B CE1 
7937 C CE2 . PHE B 460 ? 0.8087 0.6293 0.7648 0.0614  0.0625  0.0445  460 PHE B CE2 
7938 C CZ  . PHE B 460 ? 0.7651 0.5881 0.7159 0.0639  0.0657  0.0463  460 PHE B CZ  
7939 N N   . VAL B 461 ? 0.6844 0.5581 0.5955 0.0678  0.0440  0.0579  461 VAL B N   
7940 C CA  . VAL B 461 ? 0.7127 0.5972 0.6156 0.0660  0.0371  0.0575  461 VAL B CA  
7941 C C   . VAL B 461 ? 0.7282 0.6233 0.6204 0.0675  0.0362  0.0587  461 VAL B C   
7942 O O   . VAL B 461 ? 0.7930 0.6969 0.6785 0.0645  0.0297  0.0566  461 VAL B O   
7943 C CB  . VAL B 461 ? 0.7496 0.6373 0.6519 0.0696  0.0383  0.0622  461 VAL B CB  
7944 C CG1 . VAL B 461 ? 0.7963 0.6860 0.6961 0.0775  0.0469  0.0697  461 VAL B CG1 
7945 C CG2 . VAL B 461 ? 0.7088 0.6074 0.6031 0.0675  0.0311  0.0617  461 VAL B CG2 
7946 N N   . GLU B 462 ? 0.6884 0.5833 0.5790 0.0721  0.0427  0.0620  462 GLU B N   
7947 C CA  . GLU B 462 ? 0.6702 0.5746 0.5513 0.0732  0.0419  0.0624  462 GLU B CA  
7948 C C   . GLU B 462 ? 0.6096 0.5137 0.4900 0.0661  0.0351  0.0551  462 GLU B C   
7949 O O   . GLU B 462 ? 0.5658 0.4799 0.4377 0.0647  0.0309  0.0536  462 GLU B O   
7950 C CB  . GLU B 462 ? 0.7802 0.6825 0.6612 0.0790  0.0503  0.0667  462 GLU B CB  
7951 C CG  . GLU B 462 ? 0.9201 0.8120 0.8078 0.0761  0.0520  0.0625  462 GLU B CG  
7952 C CD  . GLU B 462 ? 1.0300 0.9192 0.9183 0.0821  0.0609  0.0671  462 GLU B CD  
7953 O OE1 . GLU B 462 ? 1.0628 0.9447 0.9578 0.0858  0.0673  0.0708  462 GLU B OE1 
7954 O OE2 . GLU B 462 ? 1.0516 0.9459 0.9339 0.0832  0.0614  0.0669  462 GLU B OE2 
7955 N N   . VAL B 463 ? 0.5600 0.4527 0.4493 0.0618  0.0342  0.0504  463 VAL B N   
7956 C CA  . VAL B 463 ? 0.5308 0.4222 0.4200 0.0553  0.0282  0.0435  463 VAL B CA  
7957 C C   . VAL B 463 ? 0.4866 0.3833 0.3729 0.0504  0.0201  0.0402  463 VAL B C   
7958 O O   . VAL B 463 ? 0.4775 0.3798 0.3583 0.0465  0.0149  0.0364  463 VAL B O   
7959 C CB  . VAL B 463 ? 0.5223 0.4004 0.4220 0.0523  0.0297  0.0397  463 VAL B CB  
7960 C CG1 . VAL B 463 ? 0.4961 0.3729 0.3952 0.0460  0.0240  0.0330  463 VAL B CG1 
7961 C CG2 . VAL B 463 ? 0.5502 0.4230 0.4529 0.0573  0.0382  0.0432  463 VAL B CG2 
7962 N N   . PHE B 464 ? 0.4961 0.3911 0.3862 0.0505  0.0189  0.0416  464 PHE B N   
7963 C CA  . PHE B 464 ? 0.4992 0.3997 0.3866 0.0463  0.0114  0.0391  464 PHE B CA  
7964 C C   . PHE B 464 ? 0.4287 0.3432 0.3049 0.0479  0.0091  0.0413  464 PHE B C   
7965 O O   . PHE B 464 ? 0.3977 0.3179 0.2696 0.0433  0.0027  0.0375  464 PHE B O   
7966 C CB  . PHE B 464 ? 0.5029 0.3997 0.3961 0.0471  0.0114  0.0409  464 PHE B CB  
7967 C CG  . PHE B 464 ? 0.5012 0.3858 0.4052 0.0437  0.0111  0.0369  464 PHE B CG  
7968 C CD1 . PHE B 464 ? 0.4752 0.3574 0.3816 0.0374  0.0043  0.0310  464 PHE B CD1 
7969 C CD2 . PHE B 464 ? 0.5786 0.4543 0.4904 0.0469  0.0177  0.0390  464 PHE B CD2 
7970 C CE1 . PHE B 464 ? 0.5254 0.3970 0.4418 0.0345  0.0039  0.0273  464 PHE B CE1 
7971 C CE2 . PHE B 464 ? 0.5714 0.4365 0.4935 0.0437  0.0173  0.0350  464 PHE B CE2 
7972 C CZ  . PHE B 464 ? 0.5298 0.3932 0.4540 0.0376  0.0103  0.0292  464 PHE B CZ  
7973 N N   . ASP B 465 ? 0.4749 0.3953 0.3463 0.0544  0.0146  0.0474  465 ASP B N   
7974 C CA  . ASP B 465 ? 0.4773 0.4119 0.3379 0.0564  0.0128  0.0496  465 ASP B CA  
7975 C C   . ASP B 465 ? 0.4585 0.3972 0.3138 0.0539  0.0110  0.0458  465 ASP B C   
7976 O O   . ASP B 465 ? 0.4432 0.3920 0.2914 0.0512  0.0058  0.0436  465 ASP B O   
7977 C CB  . ASP B 465 ? 0.4819 0.4217 0.3391 0.0645  0.0195  0.0574  465 ASP B CB  
7978 C CG  . ASP B 465 ? 0.5536 0.5091 0.3994 0.0671  0.0179  0.0600  465 ASP B CG  
7979 O OD1 . ASP B 465 ? 0.4881 0.4510 0.3303 0.0657  0.0132  0.0601  465 ASP B OD1 
7980 O OD2 . ASP B 465 ? 0.5843 0.5451 0.4249 0.0705  0.0214  0.0618  465 ASP B OD2 
7981 N N   . LYS B 466 ? 0.4186 0.3499 0.2775 0.0546  0.0152  0.0449  466 LYS B N   
7982 C CA  . LYS B 466 ? 0.5392 0.4734 0.3938 0.0520  0.0137  0.0409  466 LYS B CA  
7983 C C   . LYS B 466 ? 0.4891 0.4219 0.3443 0.0441  0.0060  0.0338  466 LYS B C   
7984 O O   . LYS B 466 ? 0.4418 0.3828 0.2901 0.0414  0.0022  0.0308  466 LYS B O   
7985 C CB  . LYS B 466 ? 0.6304 0.5551 0.4900 0.0539  0.0196  0.0410  466 LYS B CB  
7986 C CG  . LYS B 466 ? 0.7428 0.6688 0.5987 0.0510  0.0181  0.0365  466 LYS B CG  
7987 C CD  . LYS B 466 ? 0.8308 0.7700 0.6762 0.0551  0.0197  0.0394  466 LYS B CD  
7988 C CE  . LYS B 466 ? 0.8657 0.8122 0.7048 0.0499  0.0137  0.0336  466 LYS B CE  
7989 N NZ  . LYS B 466 ? 0.8518 0.8103 0.6842 0.0485  0.0084  0.0336  466 LYS B NZ  
7990 N N   . LEU B 467 ? 0.4872 0.4100 0.3508 0.0403  0.0038  0.0310  467 LEU B N   
7991 C CA  . LEU B 467 ? 0.3992 0.3199 0.2642 0.0331  -0.0031 0.0245  467 LEU B CA  
7992 C C   . LEU B 467 ? 0.4579 0.3893 0.3165 0.0309  -0.0090 0.0240  467 LEU B C   
7993 O O   . LEU B 467 ? 0.4993 0.4359 0.3533 0.0265  -0.0137 0.0197  467 LEU B O   
7994 C CB  . LEU B 467 ? 0.3931 0.3013 0.2687 0.0304  -0.0038 0.0222  467 LEU B CB  
7995 C CG  . LEU B 467 ? 0.3563 0.2530 0.2392 0.0307  0.0007  0.0209  467 LEU B CG  
7996 C CD1 . LEU B 467 ? 0.4130 0.2996 0.3061 0.0311  0.0025  0.0216  467 LEU B CD1 
7997 C CD2 . LEU B 467 ? 0.3761 0.2692 0.2596 0.0250  -0.0031 0.0145  467 LEU B CD2 
7998 N N   . PHE B 468 ? 0.4500 0.3849 0.3086 0.0339  -0.0087 0.0283  468 PHE B N   
7999 C CA  . PHE B 468 ? 0.4268 0.3722 0.2794 0.0320  -0.0141 0.0282  468 PHE B CA  
8000 C C   . PHE B 468 ? 0.4273 0.3858 0.2698 0.0329  -0.0149 0.0284  468 PHE B C   
8001 O O   . PHE B 468 ? 0.4830 0.4478 0.3212 0.0282  -0.0205 0.0244  468 PHE B O   
8002 C CB  . PHE B 468 ? 0.4046 0.3520 0.2582 0.0362  -0.0125 0.0336  468 PHE B CB  
8003 C CG  . PHE B 468 ? 0.3886 0.3476 0.2358 0.0352  -0.0175 0.0343  468 PHE B CG  
8004 C CD1 . PHE B 468 ? 0.3720 0.3301 0.2212 0.0295  -0.0239 0.0303  468 PHE B CD1 
8005 C CD2 . PHE B 468 ? 0.4191 0.3903 0.2583 0.0401  -0.0155 0.0391  468 PHE B CD2 
8006 C CE1 . PHE B 468 ? 0.4683 0.4372 0.3117 0.0286  -0.0283 0.0310  468 PHE B CE1 
8007 C CE2 . PHE B 468 ? 0.3876 0.3700 0.2210 0.0392  -0.0201 0.0397  468 PHE B CE2 
8008 C CZ  . PHE B 468 ? 0.3796 0.3606 0.2151 0.0333  -0.0265 0.0356  468 PHE B CZ  
8009 N N   . ARG B 469 ? 0.3903 0.3530 0.2288 0.0389  -0.0092 0.0329  469 ARG B N   
8010 C CA  . ARG B 469 ? 0.5415 0.5172 0.3704 0.0402  -0.0096 0.0330  469 ARG B CA  
8011 C C   . ARG B 469 ? 0.5370 0.5114 0.3647 0.0347  -0.0124 0.0264  469 ARG B C   
8012 O O   . ARG B 469 ? 0.5003 0.4851 0.3208 0.0323  -0.0160 0.0237  469 ARG B O   
8013 C CB  . ARG B 469 ? 0.4486 0.4279 0.2743 0.0480  -0.0023 0.0392  469 ARG B CB  
8014 C CG  . ARG B 469 ? 0.4964 0.4790 0.3218 0.0540  0.0009  0.0462  469 ARG B CG  
8015 C CD  . ARG B 469 ? 0.5612 0.5501 0.3816 0.0619  0.0077  0.0523  469 ARG B CD  
8016 N NE  . ARG B 469 ? 0.5920 0.5698 0.4182 0.0648  0.0142  0.0537  469 ARG B NE  
8017 C CZ  . ARG B 469 ? 0.6457 0.6221 0.4706 0.0644  0.0161  0.0514  469 ARG B CZ  
8018 N NH1 . ARG B 469 ? 0.6116 0.5967 0.4298 0.0612  0.0120  0.0473  469 ARG B NH1 
8019 N NH2 . ARG B 469 ? 0.6962 0.6623 0.5269 0.0672  0.0222  0.0532  469 ARG B NH2 
8020 N N   . SER B 470 ? 0.5052 0.4669 0.3398 0.0329  -0.0106 0.0237  470 SER B N   
8021 C CA  . SER B 470 ? 0.5167 0.4757 0.3508 0.0277  -0.0130 0.0175  470 SER B CA  
8022 C C   . SER B 470 ? 0.4635 0.4234 0.2976 0.0205  -0.0202 0.0119  470 SER B C   
8023 O O   . SER B 470 ? 0.4576 0.4238 0.2864 0.0168  -0.0235 0.0077  470 SER B O   
8024 C CB  . SER B 470 ? 0.5718 0.5166 0.4141 0.0275  -0.0094 0.0162  470 SER B CB  
8025 O OG  . SER B 470 ? 0.6845 0.6294 0.5255 0.0333  -0.0028 0.0201  470 SER B OG  
8026 N N   . PHE B 471 ? 0.4157 0.3691 0.2560 0.0185  -0.0227 0.0118  471 PHE B N   
8027 C CA  . PHE B 471 ? 0.4666 0.4205 0.3073 0.0120  -0.0294 0.0071  471 PHE B CA  
8028 C C   . PHE B 471 ? 0.4668 0.4352 0.2992 0.0115  -0.0330 0.0076  471 PHE B C   
8029 O O   . PHE B 471 ? 0.4416 0.4139 0.2710 0.0061  -0.0378 0.0027  471 PHE B O   
8030 C CB  . PHE B 471 ? 0.4158 0.3607 0.2647 0.0109  -0.0308 0.0075  471 PHE B CB  
8031 C CG  . PHE B 471 ? 0.4412 0.3722 0.2989 0.0106  -0.0280 0.0062  471 PHE B CG  
8032 C CD1 . PHE B 471 ? 0.4395 0.3648 0.2985 0.0074  -0.0279 0.0017  471 PHE B CD1 
8033 C CD2 . PHE B 471 ? 0.4883 0.4119 0.3530 0.0135  -0.0253 0.0094  471 PHE B CD2 
8034 C CE1 . PHE B 471 ? 0.4374 0.3502 0.3046 0.0072  -0.0252 0.0005  471 PHE B CE1 
8035 C CE2 . PHE B 471 ? 0.3691 0.2804 0.2422 0.0131  -0.0227 0.0080  471 PHE B CE2 
8036 C CZ  . PHE B 471 ? 0.4306 0.3367 0.3050 0.0100  -0.0227 0.0035  471 PHE B CZ  
8037 N N   . VAL B 472 ? 0.5092 0.4856 0.3379 0.0171  -0.0306 0.0134  472 VAL B N   
8038 C CA  . VAL B 472 ? 0.5445 0.5355 0.3652 0.0170  -0.0339 0.0143  472 VAL B CA  
8039 C C   . VAL B 472 ? 0.5038 0.5044 0.3170 0.0161  -0.0341 0.0115  472 VAL B C   
8040 O O   . VAL B 472 ? 0.5224 0.5321 0.3305 0.0122  -0.0388 0.0082  472 VAL B O   
8041 C CB  . VAL B 472 ? 0.5137 0.5109 0.3324 0.0238  -0.0307 0.0216  472 VAL B CB  
8042 C CG1 . VAL B 472 ? 0.5503 0.5644 0.3592 0.0258  -0.0319 0.0233  472 VAL B CG1 
8043 C CG2 . VAL B 472 ? 0.4473 0.4394 0.2714 0.0229  -0.0331 0.0230  472 VAL B CG2 
8044 N N   . ARG B 473 ? 0.5594 0.5580 0.3716 0.0197  -0.0291 0.0127  473 ARG B N   
8045 C CA  . ARG B 473 ? 0.5678 0.5753 0.3730 0.0190  -0.0291 0.0099  473 ARG B CA  
8046 C C   . ARG B 473 ? 0.4920 0.4945 0.2988 0.0113  -0.0333 0.0021  473 ARG B C   
8047 O O   . ARG B 473 ? 0.4883 0.5000 0.2893 0.0076  -0.0369 -0.0019 473 ARG B O   
8048 C CB  . ARG B 473 ? 0.6336 0.6395 0.4378 0.0250  -0.0225 0.0133  473 ARG B CB  
8049 C CG  . ARG B 473 ? 0.7327 0.7446 0.5312 0.0237  -0.0222 0.0094  473 ARG B CG  
8050 C CD  . ARG B 473 ? 0.8079 0.8231 0.6032 0.0311  -0.0156 0.0144  473 ARG B CD  
8051 N NE  . ARG B 473 ? 0.8652 0.8697 0.6644 0.0309  -0.0122 0.0123  473 ARG B NE  
8052 C CZ  . ARG B 473 ? 0.8352 0.8420 0.6308 0.0284  -0.0126 0.0076  473 ARG B CZ  
8053 N NH1 . ARG B 473 ? 0.8721 0.8916 0.6603 0.0257  -0.0164 0.0041  473 ARG B NH1 
8054 N NH2 . ARG B 473 ? 0.7272 0.7237 0.5268 0.0286  -0.0093 0.0063  473 ARG B NH2 
8055 N N   . ARG B 474 ? 0.4243 0.4121 0.2389 0.0089  -0.0326 -0.0001 474 ARG B N   
8056 C CA  . ARG B 474 ? 0.4910 0.4728 0.3077 0.0020  -0.0361 -0.0071 474 ARG B CA  
8057 C C   . ARG B 474 ? 0.5465 0.5323 0.3624 -0.0039 -0.0424 -0.0106 474 ARG B C   
8058 O O   . ARG B 474 ? 0.5714 0.5596 0.3846 -0.0092 -0.0456 -0.0163 474 ARG B O   
8059 C CB  . ARG B 474 ? 0.5071 0.4727 0.3330 0.0011  -0.0341 -0.0080 474 ARG B CB  
8060 C CG  . ARG B 474 ? 0.5584 0.5165 0.3872 -0.0057 -0.0373 -0.0148 474 ARG B CG  
8061 C CD  . ARG B 474 ? 0.7075 0.6655 0.5333 -0.0061 -0.0349 -0.0178 474 ARG B CD  
8062 N NE  . ARG B 474 ? 0.8277 0.7767 0.6572 -0.0122 -0.0373 -0.0240 474 ARG B NE  
8063 C CZ  . ARG B 474 ? 0.8696 0.8223 0.6961 -0.0180 -0.0417 -0.0293 474 ARG B CZ  
8064 N NH1 . ARG B 474 ? 0.8106 0.7762 0.6303 -0.0188 -0.0444 -0.0294 474 ARG B NH1 
8065 N NH2 . ARG B 474 ? 0.9094 0.8529 0.7397 -0.0231 -0.0433 -0.0344 474 ARG B NH2 
8066 N N   . ALA B 475 ? 0.5630 0.5496 0.3810 -0.0029 -0.0442 -0.0074 475 ALA B N   
8067 C CA  . ALA B 475 ? 0.5887 0.5785 0.4064 -0.0082 -0.0500 -0.0103 475 ALA B CA  
8068 C C   . ALA B 475 ? 0.5889 0.5936 0.3980 -0.0101 -0.0528 -0.0125 475 ALA B C   
8069 O O   . ALA B 475 ? 0.5521 0.5591 0.3606 -0.0158 -0.0577 -0.0166 475 ALA B O   
8070 C CB  . ALA B 475 ? 0.6042 0.5932 0.4252 -0.0058 -0.0509 -0.0058 475 ALA B CB  
8071 N N   . GLN B 476 ? 0.5505 0.5654 0.3532 -0.0055 -0.0498 -0.0098 476 GLN B N   
8072 C CA  . GLN B 476 ? 0.6114 0.6417 0.4056 -0.0067 -0.0521 -0.0117 476 GLN B CA  
8073 C C   . GLN B 476 ? 0.6746 0.7064 0.4655 -0.0094 -0.0515 -0.0170 476 GLN B C   
8074 O O   . GLN B 476 ? 0.6271 0.6721 0.4109 -0.0104 -0.0529 -0.0192 476 GLN B O   
8075 C CB  . GLN B 476 ? 0.5865 0.6290 0.3751 0.0005  -0.0493 -0.0052 476 GLN B CB  
8076 C CG  . GLN B 476 ? 0.6287 0.6704 0.4201 0.0036  -0.0496 0.0003  476 GLN B CG  
8077 C CD  . GLN B 476 ? 0.7442 0.7946 0.5313 0.0118  -0.0453 0.0075  476 GLN B CD  
8078 O OE1 . GLN B 476 ? 0.8042 0.8685 0.5852 0.0135  -0.0469 0.0096  476 GLN B OE1 
8079 N NE2 . GLN B 476 ? 0.7554 0.7977 0.5458 0.0170  -0.0397 0.0115  476 GLN B NE2 
8080 N N   . GLU B 477 ? 0.6948 0.7138 0.4907 -0.0107 -0.0494 -0.0193 477 GLU B N   
8081 C CA  . GLU B 477 ? 0.7734 0.7925 0.5665 -0.0133 -0.0485 -0.0245 477 GLU B CA  
8082 C C   . GLU B 477 ? 0.7940 0.8026 0.5919 -0.0207 -0.0516 -0.0310 477 GLU B C   
8083 O O   . GLU B 477 ? 0.8119 0.8232 0.6094 -0.0260 -0.0562 -0.0344 477 GLU B O   
8084 C CB  . GLU B 477 ? 0.8248 0.8387 0.6188 -0.0078 -0.0427 -0.0215 477 GLU B CB  
8085 C CG  . GLU B 477 ? 0.8808 0.9068 0.6684 -0.0006 -0.0391 -0.0160 477 GLU B CG  
8086 C CD  . GLU B 477 ? 0.9354 0.9545 0.7252 0.0052  -0.0329 -0.0122 477 GLU B CD  
8087 O OE1 . GLU B 477 ? 0.9337 0.9388 0.7302 0.0035  -0.0315 -0.0138 477 GLU B OE1 
8088 O OE2 . GLU B 477 ? 0.9628 0.9908 0.7477 0.0116  -0.0293 -0.0073 477 GLU B OE2 
# 
