data_9JLQ
# 
_entry.id   9JLQ 
# 
_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   9JLQ         pdb_00009jlq 10.2210/pdb9jlq/pdb 
WWPDB D_1300051230 ?            ?                   
# 
_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                        9JLQ 
_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                 3 
_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 ? 
'Yu, F.'     3 ? 
'Wang, Q.S.' 4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   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' 58186.254 4   ? ? ? ? 
2 water   nat water                                                                18.015    160 ? ? ? ? 
# 
_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
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQELEH
HHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQELEH
HHHH
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   LEU n 
1 5   PHE n 
1 6   LEU n 
1 7   VAL n 
1 8   PHE n 
1 9   TRP n 
1 10  TRP n 
1 11  HIS n 
1 12  MET n 
1 13  HIS n 
1 14  GLN n 
1 15  PRO n 
1 16  LEU n 
1 17  TYR n 
1 18  ARG n 
1 19  GLU n 
1 20  PRO n 
1 21  TYR n 
1 22  THR n 
1 23  GLY n 
1 24  GLU n 
1 25  TYR n 
1 26  LEU n 
1 27  LEU n 
1 28  PRO n 
1 29  TRP n 
1 30  THR n 
1 31  PHE n 
1 32  PHE n 
1 33  HIS n 
1 34  ALA n 
1 35  VAL n 
1 36  LYS n 
1 37  ASP n 
1 38  TYR n 
1 39  TYR n 
1 40  ASP n 
1 41  MET n 
1 42  PRO n 
1 43  ALA n 
1 44  TYR n 
1 45  LEU n 
1 46  LYS n 
1 47  ASP n 
1 48  PHE n 
1 49  GLU n 
1 50  ILE n 
1 51  LYS n 
1 52  LEU n 
1 53  ASN n 
1 54  PHE n 
1 55  ASN n 
1 56  LEU n 
1 57  THR n 
1 58  PRO n 
1 59  VAL n 
1 60  LEU n 
1 61  ILE n 
1 62  ASP n 
1 63  GLN n 
1 64  ILE n 
1 65  GLN n 
1 66  GLU n 
1 67  TYR n 
1 68  ALA n 
1 69  GLN n 
1 70  GLY n 
1 71  LYS n 
1 72  ALA n 
1 73  LYS n 
1 74  ASP n 
1 75  VAL n 
1 76  PHE n 
1 77  LEU n 
1 78  GLU n 
1 79  ALA n 
1 80  ILE n 
1 81  ARG n 
1 82  LYS n 
1 83  ASP n 
1 84  PRO n 
1 85  ASP n 
1 86  ASP n 
1 87  LEU n 
1 88  GLU n 
1 89  LYS n 
1 90  GLU n 
1 91  GLU n 
1 92  VAL n 
1 93  GLU n 
1 94  LYS n 
1 95  LEU n 
1 96  ILE n 
1 97  GLU n 
1 98  PHE n 
1 99  THR n 
1 100 LYS n 
1 101 LEU n 
1 102 ASN n 
1 103 TYR n 
1 104 GLU n 
1 105 LYS n 
1 106 PRO n 
1 107 ILE n 
1 108 TYR n 
1 109 ARG n 
1 110 PHE n 
1 111 GLU n 
1 112 ARG n 
1 113 ILE n 
1 114 ARG n 
1 115 GLU n 
1 116 LEU n 
1 117 MET n 
1 118 ASN n 
1 119 LYS n 
1 120 GLU n 
1 121 LYS n 
1 122 LEU n 
1 123 ASN n 
1 124 ARG n 
1 125 GLU n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 ASP n 
1 130 LEU n 
1 131 GLN n 
1 132 THR n 
1 133 LEU n 
1 134 ASN n 
1 135 LEU n 
1 136 LEU n 
1 137 ALA n 
1 138 TRP n 
1 139 CYS n 
1 140 GLY n 
1 141 ARG n 
1 142 THR n 
1 143 LEU n 
1 144 ARG n 
1 145 LYS n 
1 146 ASP n 
1 147 LEU n 
1 148 LYS n 
1 149 ASP n 
1 150 LEU n 
1 151 LEU n 
1 152 ASN n 
1 153 LYS n 
1 154 GLY n 
1 155 ARG n 
1 156 ASN n 
1 157 TYR n 
1 158 THR n 
1 159 GLN n 
1 160 GLU n 
1 161 GLU n 
1 162 LYS n 
1 163 GLU n 
1 164 TYR n 
1 165 VAL n 
1 166 LEU n 
1 167 ASN n 
1 168 LYS n 
1 169 TYR n 
1 170 PHE n 
1 171 GLU n 
1 172 ILE n 
1 173 ILE n 
1 174 LYS n 
1 175 LYS n 
1 176 THR n 
1 177 LEU n 
1 178 SER n 
1 179 ILE n 
1 180 TYR n 
1 181 ARG n 
1 182 GLU n 
1 183 ILE n 
1 184 LYS n 
1 185 GLU n 
1 186 GLU n 
1 187 GLY n 
1 188 LYS n 
1 189 GLY n 
1 190 SER n 
1 191 VAL n 
1 192 SER n 
1 193 THR n 
1 194 SER n 
1 195 PRO n 
1 196 TYR n 
1 197 TYR n 
1 198 HIS n 
1 199 PRO n 
1 200 LEU n 
1 201 ILE n 
1 202 PRO n 
1 203 ILE n 
1 204 LEU n 
1 205 LEU n 
1 206 ASN n 
1 207 PRO n 
1 208 ASN n 
1 209 CYS n 
1 210 VAL n 
1 211 TYR n 
1 212 GLU n 
1 213 THR n 
1 214 THR n 
1 215 PRO n 
1 216 ASN n 
1 217 VAL n 
1 218 LYS n 
1 219 ILE n 
1 220 PRO n 
1 221 ASP n 
1 222 PHE n 
1 223 ALA n 
1 224 VAL n 
1 225 SER n 
1 226 PHE n 
1 227 ARG n 
1 228 GLU n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 HIS n 
1 234 VAL n 
1 235 GLU n 
1 236 LEU n 
1 237 ALA n 
1 238 LYS n 
1 239 GLU n 
1 240 LYS n 
1 241 TYR n 
1 242 PHE n 
1 243 GLU n 
1 244 ILE n 
1 245 PHE n 
1 246 GLY n 
1 247 GLU n 
1 248 HIS n 
1 249 PRO n 
1 250 VAL n 
1 251 TYR n 
1 252 MET n 
1 253 TRP n 
1 254 PRO n 
1 255 PRO n 
1 256 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 ASP n 
1 353 GLY n 
1 354 GLU n 
1 355 ASN n 
1 356 CYS n 
1 357 TRP n 
1 358 GLU n 
1 359 TYR n 
1 360 TYR n 
1 361 GLU n 
1 362 GLU n 
1 363 ASN n 
1 364 GLY n 
1 365 ILE n 
1 366 PRO n 
1 367 PHE n 
1 368 LEU n 
1 369 GLU n 
1 370 LYS n 
1 371 LEU n 
1 372 TYR n 
1 373 SER n 
1 374 THR n 
1 375 LEU n 
1 376 GLU n 
1 377 LYS n 
1 378 GLU n 
1 379 GLU n 
1 380 TRP n 
1 381 ILE n 
1 382 GLU n 
1 383 THR n 
1 384 LEU n 
1 385 THR n 
1 386 LEU n 
1 387 GLU n 
1 388 GLU n 
1 389 ALA n 
1 390 MET n 
1 391 ARG n 
1 392 LYS n 
1 393 GLU n 
1 394 ASP n 
1 395 VAL n 
1 396 LYS n 
1 397 THR n 
1 398 GLU n 
1 399 VAL n 
1 400 ILE n 
1 401 GLU n 
1 402 SER n 
1 403 VAL n 
1 404 LYS n 
1 405 ALA n 
1 406 GLY n 
1 407 THR n 
1 408 TRP n 
1 409 PHE n 
1 410 ASP n 
1 411 GLY n 
1 412 ASN n 
1 413 PHE n 
1 414 LEU n 
1 415 LYS n 
1 416 TRP n 
1 417 ILE n 
1 418 GLY n 
1 419 ASN n 
1 420 LYS n 
1 421 GLU n 
1 422 LYS n 
1 423 ASN n 
1 424 GLU n 
1 425 TYR n 
1 426 TRP n 
1 427 LYS n 
1 428 ILE n 
1 429 LEU n 
1 430 ILE n 
1 431 GLU n 
1 432 ALA n 
1 433 LYS n 
1 434 LYS n 
1 435 LYS n 
1 436 ALA n 
1 437 LYS n 
1 438 ASN n 
1 439 ASP n 
1 440 TYR n 
1 441 ILE n 
1 442 LEU n 
1 443 VAL n 
1 444 ALA n 
1 445 GLU n 
1 446 GLY n 
1 447 SER n 
1 448 ASP n 
1 449 TRP n 
1 450 PHE n 
1 451 TRP n 
1 452 TRP n 
1 453 GLN n 
1 454 GLY n 
1 455 GLU n 
1 456 GLU n 
1 457 LYS n 
1 458 ALA n 
1 459 PRO n 
1 460 PHE n 
1 461 VAL n 
1 462 GLU n 
1 463 VAL n 
1 464 PHE n 
1 465 ASP n 
1 466 LYS n 
1 467 LEU n 
1 468 PHE n 
1 469 ARG n 
1 470 SER n 
1 471 PHE n 
1 472 VAL n 
1 473 ARG n 
1 474 ARG n 
1 475 ALA n 
1 476 GLN n 
1 477 GLU n 
1 478 LEU n 
1 479 GLU n 
1 480 HIS n 
1 481 HIS n 
1 482 HIS n 
1 483 HIS n 
1 484 HIS n 
# 
_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                   484 
_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_
_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 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   PHE 5   5   5   PHE PHE A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   TRP 9   9   9   TRP TRP A . n 
A 1 10  TRP 10  10  10  TRP TRP A . n 
A 1 11  HIS 11  11  11  HIS HIS A . n 
A 1 12  MET 12  12  12  MET MET A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  GLN 14  14  14  GLN GLN A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ARG 18  18  18  ARG ARG A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  THR 22  22  22  THR THR A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  TYR 25  25  25  TYR TYR A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  TRP 29  29  29  TRP TRP A . n 
A 1 30  THR 30  30  30  THR THR A . n 
A 1 31  PHE 31  31  31  PHE PHE A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  ILE 50  50  50  ILE ILE A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  PHE 54  54  54  PHE PHE A . n 
A 1 55  ASN 55  55  55  ASN ASN A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  PRO 58  58  58  PRO PRO A . n 
A 1 59  VAL 59  59  59  VAL VAL A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ILE 61  61  61  ILE ILE A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  GLU 66  66  66  GLU GLU A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ARG 81  81  81  ARG ARG A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  GLU 88  88  88  GLU GLU A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  VAL 92  92  92  VAL VAL A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  LYS 94  94  94  LYS LYS A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 TYR 108 108 108 TYR TYR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 PHE 110 110 110 PHE PHE A . n 
A 1 111 GLU 111 111 111 GLU GLU A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 ARG 114 114 114 ARG ARG A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 ASN 123 123 123 ASN ASN A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 THR 132 132 132 THR THR A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 ARG 144 144 144 ARG ARG A . n 
A 1 145 LYS 145 145 145 LYS LYS A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 ASP 149 149 149 ASP ASP A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 LEU 151 151 151 LEU LEU A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 THR 158 158 158 THR THR A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LYS 162 162 162 LYS LYS A . n 
A 1 163 GLU 163 163 163 GLU GLU A . n 
A 1 164 TYR 164 164 164 TYR TYR A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 LYS 175 175 175 LYS LYS A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 SER 178 178 178 SER SER A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 TYR 180 180 180 TYR TYR A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLU 182 182 182 GLU GLU A . n 
A 1 183 ILE 183 183 183 ILE ILE A . n 
A 1 184 LYS 184 184 184 LYS LYS A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 LYS 188 188 188 LYS LYS A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 SER 190 190 190 SER SER A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 HIS 198 198 198 HIS HIS A . n 
A 1 199 PRO 199 199 199 PRO PRO A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ASN 206 206 206 ASN ASN A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 ASN 208 208 208 ASN ASN A . n 
A 1 209 CYS 209 209 209 CYS CYS A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 TYR 211 211 211 TYR TYR A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 THR 213 213 213 THR THR A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 PRO 215 215 215 PRO PRO A . n 
A 1 216 ASN 216 216 216 ASN ASN A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 PRO 220 220 220 PRO PRO A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 VAL 224 224 224 VAL VAL A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 SER 231 231 231 SER SER A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 LYS 238 238 238 LYS LYS A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 TYR 241 241 241 TYR TYR A . n 
A 1 242 PHE 242 242 242 PHE PHE A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 HIS 248 248 248 HIS HIS A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 TRP 253 253 253 TRP TRP A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 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 ASP 352 352 352 ASP ASP A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 GLU 354 354 354 GLU GLU A . n 
A 1 355 ASN 355 355 355 ASN ASN A . n 
A 1 356 CYS 356 356 356 CYS CYS A . n 
A 1 357 TRP 357 357 357 TRP TRP A . n 
A 1 358 GLU 358 358 358 GLU GLU A . n 
A 1 359 TYR 359 359 359 TYR TYR A . n 
A 1 360 TYR 360 360 360 TYR TYR A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 GLU 362 362 362 GLU GLU A . n 
A 1 363 ASN 363 363 363 ASN ASN A . n 
A 1 364 GLY 364 364 364 GLY GLY A . n 
A 1 365 ILE 365 365 365 ILE ILE A . n 
A 1 366 PRO 366 366 366 PRO PRO A . n 
A 1 367 PHE 367 367 367 PHE PHE A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 GLU 369 369 369 GLU GLU A . n 
A 1 370 LYS 370 370 370 LYS LYS A . n 
A 1 371 LEU 371 371 371 LEU LEU A . n 
A 1 372 TYR 372 372 372 TYR TYR A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 LEU 375 375 375 LEU LEU A . n 
A 1 376 GLU 376 376 376 GLU GLU A . n 
A 1 377 LYS 377 377 377 LYS LYS A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 GLU 379 379 379 GLU GLU A . n 
A 1 380 TRP 380 380 380 TRP TRP A . n 
A 1 381 ILE 381 381 381 ILE ILE A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 THR 383 383 383 THR THR A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 LEU 386 386 386 LEU LEU A . n 
A 1 387 GLU 387 387 387 GLU GLU A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 ALA 389 389 389 ALA ALA A . n 
A 1 390 MET 390 390 390 MET MET A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 LYS 392 392 392 LYS LYS A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 ASP 394 394 394 ASP ASP A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 LYS 396 396 396 LYS LYS A . n 
A 1 397 THR 397 397 397 THR THR A . n 
A 1 398 GLU 398 398 398 GLU GLU A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ILE 400 400 400 ILE ILE A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 SER 402 402 402 SER SER A . n 
A 1 403 VAL 403 403 403 VAL VAL A . n 
A 1 404 LYS 404 404 404 LYS LYS A . n 
A 1 405 ALA 405 405 405 ALA ALA A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 THR 407 407 407 THR THR A . n 
A 1 408 TRP 408 408 408 TRP TRP A . n 
A 1 409 PHE 409 409 409 PHE PHE A . n 
A 1 410 ASP 410 410 410 ASP ASP A . n 
A 1 411 GLY 411 411 411 GLY GLY A . n 
A 1 412 ASN 412 412 412 ASN ASN A . n 
A 1 413 PHE 413 413 413 PHE PHE A . n 
A 1 414 LEU 414 414 414 LEU LEU A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 TRP 416 416 416 TRP TRP A . n 
A 1 417 ILE 417 417 417 ILE ILE A . n 
A 1 418 GLY 418 418 418 GLY GLY A . n 
A 1 419 ASN 419 419 419 ASN ASN A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 GLU 421 421 421 GLU GLU A . n 
A 1 422 LYS 422 422 422 LYS LYS A . n 
A 1 423 ASN 423 423 423 ASN ASN A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 TYR 425 425 425 TYR TYR A . n 
A 1 426 TRP 426 426 426 TRP TRP A . n 
A 1 427 LYS 427 427 427 LYS LYS A . n 
A 1 428 ILE 428 428 428 ILE ILE A . n 
A 1 429 LEU 429 429 429 LEU LEU A . n 
A 1 430 ILE 430 430 430 ILE ILE A . n 
A 1 431 GLU 431 431 431 GLU GLU A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 LYS 433 433 433 LYS LYS A . n 
A 1 434 LYS 434 434 434 LYS LYS A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 ALA 436 436 436 ALA ALA A . n 
A 1 437 LYS 437 437 437 LYS LYS A . n 
A 1 438 ASN 438 438 438 ASN ASN A . n 
A 1 439 ASP 439 439 439 ASP ASP A . n 
A 1 440 TYR 440 440 440 TYR TYR A . n 
A 1 441 ILE 441 441 441 ILE ILE A . n 
A 1 442 LEU 442 442 442 LEU LEU A . n 
A 1 443 VAL 443 443 443 VAL VAL A . n 
A 1 444 ALA 444 444 444 ALA ALA A . n 
A 1 445 GLU 445 445 445 GLU GLU A . n 
A 1 446 GLY 446 446 446 GLY GLY A . n 
A 1 447 SER 447 447 447 SER SER A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 TRP 449 449 449 TRP TRP A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 TRP 451 451 451 TRP TRP A . n 
A 1 452 TRP 452 452 452 TRP TRP A . n 
A 1 453 GLN 453 453 453 GLN GLN A . n 
A 1 454 GLY 454 454 454 GLY GLY A . n 
A 1 455 GLU 455 455 455 GLU GLU A . n 
A 1 456 GLU 456 456 456 GLU GLU A . n 
A 1 457 LYS 457 457 457 LYS LYS A . n 
A 1 458 ALA 458 458 458 ALA ALA A . n 
A 1 459 PRO 459 459 459 PRO PRO A . n 
A 1 460 PHE 460 460 460 PHE PHE A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 GLU 462 462 462 GLU GLU A . n 
A 1 463 VAL 463 463 463 VAL VAL A . n 
A 1 464 PHE 464 464 464 PHE PHE A . n 
A 1 465 ASP 465 465 465 ASP ASP A . n 
A 1 466 LYS 466 466 466 LYS LYS A . n 
A 1 467 LEU 467 467 467 LEU LEU A . n 
A 1 468 PHE 468 468 468 PHE PHE A . n 
A 1 469 ARG 469 469 469 ARG ARG A . n 
A 1 470 SER 470 470 470 SER SER A . n 
A 1 471 PHE 471 471 471 PHE PHE A . n 
A 1 472 VAL 472 472 472 VAL VAL A . n 
A 1 473 ARG 473 473 473 ARG ARG A . n 
A 1 474 ARG 474 474 474 ARG ARG A . n 
A 1 475 ALA 475 475 475 ALA ALA A . n 
A 1 476 GLN 476 476 476 GLN GLN A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
A 1 478 LEU 478 478 ?   ?   ?   A . n 
A 1 479 GLU 479 479 ?   ?   ?   A . n 
A 1 480 HIS 480 480 ?   ?   ?   A . n 
A 1 481 HIS 481 481 ?   ?   ?   A . n 
A 1 482 HIS 482 482 ?   ?   ?   A . n 
A 1 483 HIS 483 483 ?   ?   ?   A . n 
A 1 484 HIS 484 484 ?   ?   ?   A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   LYS 2   2   2   LYS LYS B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   PHE 5   5   5   PHE PHE B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   TRP 9   9   9   TRP TRP B . n 
B 1 10  TRP 10  10  10  TRP TRP B . n 
B 1 11  HIS 11  11  11  HIS HIS B . n 
B 1 12  MET 12  12  12  MET MET B . n 
B 1 13  HIS 13  13  13  HIS HIS B . n 
B 1 14  GLN 14  14  14  GLN GLN B . n 
B 1 15  PRO 15  15  15  PRO PRO B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ARG 18  18  18  ARG ARG B . n 
B 1 19  GLU 19  19  19  GLU GLU B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  THR 22  22  22  THR THR B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  TYR 25  25  25  TYR TYR B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  TRP 29  29  29  TRP TRP B . n 
B 1 30  THR 30  30  30  THR THR B . n 
B 1 31  PHE 31  31  31  PHE PHE B . n 
B 1 32  PHE 32  32  32  PHE PHE B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  ASP 37  37  37  ASP ASP B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  MET 41  41  41  MET MET B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  LEU 45  45  45  LEU LEU B . n 
B 1 46  LYS 46  46  46  LYS LYS B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  ILE 50  50  50  ILE ILE B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  PHE 54  54  54  PHE PHE B . n 
B 1 55  ASN 55  55  55  ASN ASN B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  PRO 58  58  58  PRO PRO B . n 
B 1 59  VAL 59  59  59  VAL VAL B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  ILE 61  61  61  ILE ILE B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  GLU 66  66  66  GLU GLU B . n 
B 1 67  TYR 67  67  67  TYR TYR B . n 
B 1 68  ALA 68  68  68  ALA ALA B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  LYS 73  73  73  LYS LYS B . n 
B 1 74  ASP 74  74  74  ASP ASP B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  LEU 77  77  77  LEU LEU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  ARG 81  81  81  ARG ARG B . n 
B 1 82  LYS 82  82  82  LYS LYS B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  GLU 88  88  88  GLU GLU B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  GLU 90  90  90  GLU GLU B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  VAL 92  92  92  VAL VAL B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  LYS 94  94  94  LYS LYS B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  GLU 97  97  97  GLU GLU B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  THR 99  99  99  THR THR B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ASN 102 102 102 ASN ASN B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 LYS 105 105 105 LYS LYS B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 TYR 108 108 108 TYR TYR B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 PHE 110 110 110 PHE PHE B . n 
B 1 111 GLU 111 111 111 GLU GLU B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 ARG 114 114 114 ARG ARG B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 ASN 118 118 118 ASN ASN B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 ASN 123 123 123 ASN ASN B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 GLU 125 125 125 GLU GLU B . n 
B 1 126 GLU 126 126 126 GLU GLU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 THR 132 132 132 THR THR B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 ALA 137 137 137 ALA ALA B . n 
B 1 138 TRP 138 138 138 TRP TRP B . n 
B 1 139 CYS 139 139 139 CYS CYS B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 ARG 144 144 144 ARG ARG B . n 
B 1 145 LYS 145 145 145 LYS LYS B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 LYS 148 148 148 LYS LYS B . n 
B 1 149 ASP 149 149 149 ASP ASP B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 LEU 151 151 151 LEU LEU B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 GLY 154 154 154 GLY GLY B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
B 1 158 THR 158 158 158 THR THR B . n 
B 1 159 GLN 159 159 159 GLN GLN B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 LYS 162 162 162 LYS LYS B . n 
B 1 163 GLU 163 163 163 GLU GLU B . n 
B 1 164 TYR 164 164 164 TYR TYR B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ASN 167 167 167 ASN ASN B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 TYR 169 169 169 TYR TYR B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 ILE 173 173 173 ILE ILE B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 LYS 175 175 175 LYS LYS B . n 
B 1 176 THR 176 176 176 THR THR B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 SER 178 178 178 SER SER B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 TYR 180 180 180 TYR TYR B . n 
B 1 181 ARG 181 181 181 ARG ARG B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 ILE 183 183 183 ILE ILE B . n 
B 1 184 LYS 184 184 184 LYS LYS B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 LYS 188 188 188 LYS LYS B . n 
B 1 189 GLY 189 189 189 GLY GLY B . n 
B 1 190 SER 190 190 190 SER SER B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 SER 192 192 192 SER SER B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 SER 194 194 194 SER SER B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 TYR 196 196 196 TYR TYR B . n 
B 1 197 TYR 197 197 197 TYR TYR B . n 
B 1 198 HIS 198 198 198 HIS HIS B . n 
B 1 199 PRO 199 199 199 PRO PRO B . n 
B 1 200 LEU 200 200 200 LEU LEU B . n 
B 1 201 ILE 201 201 201 ILE ILE B . n 
B 1 202 PRO 202 202 202 PRO PRO B . n 
B 1 203 ILE 203 203 203 ILE ILE B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ASN 206 206 206 ASN ASN B . n 
B 1 207 PRO 207 207 207 PRO PRO B . n 
B 1 208 ASN 208 208 208 ASN ASN B . n 
B 1 209 CYS 209 209 209 CYS CYS B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 TYR 211 211 211 TYR TYR B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 THR 213 213 213 THR THR B . n 
B 1 214 THR 214 214 214 THR THR B . n 
B 1 215 PRO 215 215 215 PRO PRO B . n 
B 1 216 ASN 216 216 216 ASN ASN B . n 
B 1 217 VAL 217 217 217 VAL VAL B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 ILE 219 219 219 ILE ILE B . n 
B 1 220 PRO 220 220 220 PRO PRO B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 VAL 224 224 224 VAL VAL B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 PHE 226 226 226 PHE PHE B . n 
B 1 227 ARG 227 227 227 ARG ARG B . n 
B 1 228 GLU 228 228 228 GLU GLU B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 SER 231 231 231 SER SER B . n 
B 1 232 LYS 232 232 232 LYS LYS B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 VAL 234 234 234 VAL VAL B . n 
B 1 235 GLU 235 235 235 GLU GLU B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 LYS 238 238 238 LYS LYS B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 TYR 241 241 241 TYR TYR B . n 
B 1 242 PHE 242 242 242 PHE PHE B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 PHE 245 245 245 PHE PHE B . n 
B 1 246 GLY 246 246 246 GLY GLY B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 HIS 248 248 248 HIS HIS B . n 
B 1 249 PRO 249 249 249 PRO PRO B . n 
B 1 250 VAL 250 250 250 VAL VAL B . n 
B 1 251 TYR 251 251 251 TYR TYR B . n 
B 1 252 MET 252 252 252 MET MET B . n 
B 1 253 TRP 253 253 253 TRP TRP B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 PRO 255 255 255 PRO PRO B . n 
B 1 256 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 ASP 352 352 352 ASP ASP B . n 
B 1 353 GLY 353 353 353 GLY GLY B . n 
B 1 354 GLU 354 354 354 GLU GLU B . n 
B 1 355 ASN 355 355 355 ASN ASN B . n 
B 1 356 CYS 356 356 356 CYS CYS B . n 
B 1 357 TRP 357 357 357 TRP TRP B . n 
B 1 358 GLU 358 358 358 GLU GLU B . n 
B 1 359 TYR 359 359 359 TYR TYR B . n 
B 1 360 TYR 360 360 360 TYR TYR B . n 
B 1 361 GLU 361 361 361 GLU GLU B . n 
B 1 362 GLU 362 362 362 GLU GLU B . n 
B 1 363 ASN 363 363 363 ASN ASN B . n 
B 1 364 GLY 364 364 364 GLY GLY B . n 
B 1 365 ILE 365 365 365 ILE ILE B . n 
B 1 366 PRO 366 366 366 PRO PRO B . n 
B 1 367 PHE 367 367 367 PHE PHE B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 GLU 369 369 369 GLU GLU B . n 
B 1 370 LYS 370 370 370 LYS LYS B . n 
B 1 371 LEU 371 371 371 LEU LEU B . n 
B 1 372 TYR 372 372 372 TYR TYR B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 LEU 375 375 375 LEU LEU B . n 
B 1 376 GLU 376 376 376 GLU GLU B . n 
B 1 377 LYS 377 377 377 LYS LYS B . n 
B 1 378 GLU 378 378 378 GLU GLU B . n 
B 1 379 GLU 379 379 379 GLU GLU B . n 
B 1 380 TRP 380 380 380 TRP TRP B . n 
B 1 381 ILE 381 381 381 ILE ILE B . n 
B 1 382 GLU 382 382 382 GLU GLU B . n 
B 1 383 THR 383 383 383 THR THR B . n 
B 1 384 LEU 384 384 384 LEU LEU B . n 
B 1 385 THR 385 385 385 THR THR B . n 
B 1 386 LEU 386 386 386 LEU LEU B . n 
B 1 387 GLU 387 387 387 GLU GLU B . n 
B 1 388 GLU 388 388 388 GLU GLU B . n 
B 1 389 ALA 389 389 389 ALA ALA B . n 
B 1 390 MET 390 390 390 MET MET B . n 
B 1 391 ARG 391 391 391 ARG ARG B . n 
B 1 392 LYS 392 392 392 LYS LYS B . n 
B 1 393 GLU 393 393 393 GLU GLU B . n 
B 1 394 ASP 394 394 394 ASP ASP B . n 
B 1 395 VAL 395 395 395 VAL VAL B . n 
B 1 396 LYS 396 396 396 LYS LYS B . n 
B 1 397 THR 397 397 397 THR THR B . n 
B 1 398 GLU 398 398 398 GLU GLU B . n 
B 1 399 VAL 399 399 399 VAL VAL B . n 
B 1 400 ILE 400 400 400 ILE ILE B . n 
B 1 401 GLU 401 401 401 GLU GLU B . n 
B 1 402 SER 402 402 402 SER SER B . n 
B 1 403 VAL 403 403 403 VAL VAL B . n 
B 1 404 LYS 404 404 404 LYS LYS B . n 
B 1 405 ALA 405 405 405 ALA ALA B . n 
B 1 406 GLY 406 406 406 GLY GLY B . n 
B 1 407 THR 407 407 407 THR THR B . n 
B 1 408 TRP 408 408 408 TRP TRP B . n 
B 1 409 PHE 409 409 409 PHE PHE B . n 
B 1 410 ASP 410 410 410 ASP ASP B . n 
B 1 411 GLY 411 411 411 GLY GLY B . n 
B 1 412 ASN 412 412 412 ASN ASN B . n 
B 1 413 PHE 413 413 413 PHE PHE B . n 
B 1 414 LEU 414 414 414 LEU LEU B . n 
B 1 415 LYS 415 415 415 LYS LYS B . n 
B 1 416 TRP 416 416 416 TRP TRP B . n 
B 1 417 ILE 417 417 417 ILE ILE B . n 
B 1 418 GLY 418 418 418 GLY GLY B . n 
B 1 419 ASN 419 419 419 ASN ASN B . n 
B 1 420 LYS 420 420 420 LYS LYS B . n 
B 1 421 GLU 421 421 421 GLU GLU B . n 
B 1 422 LYS 422 422 422 LYS LYS B . n 
B 1 423 ASN 423 423 423 ASN ASN B . n 
B 1 424 GLU 424 424 424 GLU GLU B . n 
B 1 425 TYR 425 425 425 TYR TYR B . n 
B 1 426 TRP 426 426 426 TRP TRP B . n 
B 1 427 LYS 427 427 427 LYS LYS B . n 
B 1 428 ILE 428 428 428 ILE ILE B . n 
B 1 429 LEU 429 429 429 LEU LEU B . n 
B 1 430 ILE 430 430 430 ILE ILE B . n 
B 1 431 GLU 431 431 431 GLU GLU B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 LYS 433 433 433 LYS LYS B . n 
B 1 434 LYS 434 434 434 LYS LYS B . n 
B 1 435 LYS 435 435 435 LYS LYS B . n 
B 1 436 ALA 436 436 436 ALA ALA B . n 
B 1 437 LYS 437 437 437 LYS LYS B . n 
B 1 438 ASN 438 438 438 ASN ASN B . n 
B 1 439 ASP 439 439 439 ASP ASP B . n 
B 1 440 TYR 440 440 440 TYR TYR B . n 
B 1 441 ILE 441 441 441 ILE ILE B . n 
B 1 442 LEU 442 442 442 LEU LEU B . n 
B 1 443 VAL 443 443 443 VAL VAL B . n 
B 1 444 ALA 444 444 444 ALA ALA B . n 
B 1 445 GLU 445 445 445 GLU GLU B . n 
B 1 446 GLY 446 446 446 GLY GLY B . n 
B 1 447 SER 447 447 447 SER SER B . n 
B 1 448 ASP 448 448 448 ASP ASP B . n 
B 1 449 TRP 449 449 449 TRP TRP B . n 
B 1 450 PHE 450 450 450 PHE PHE B . n 
B 1 451 TRP 451 451 451 TRP TRP B . n 
B 1 452 TRP 452 452 452 TRP TRP B . n 
B 1 453 GLN 453 453 453 GLN GLN B . n 
B 1 454 GLY 454 454 454 GLY GLY B . n 
B 1 455 GLU 455 455 455 GLU GLU B . n 
B 1 456 GLU 456 456 456 GLU GLU B . n 
B 1 457 LYS 457 457 457 LYS LYS B . n 
B 1 458 ALA 458 458 458 ALA ALA B . n 
B 1 459 PRO 459 459 459 PRO PRO B . n 
B 1 460 PHE 460 460 460 PHE PHE B . n 
B 1 461 VAL 461 461 461 VAL VAL B . n 
B 1 462 GLU 462 462 462 GLU GLU B . n 
B 1 463 VAL 463 463 463 VAL VAL B . n 
B 1 464 PHE 464 464 464 PHE PHE B . n 
B 1 465 ASP 465 465 465 ASP ASP B . n 
B 1 466 LYS 466 466 466 LYS LYS B . n 
B 1 467 LEU 467 467 467 LEU LEU B . n 
B 1 468 PHE 468 468 468 PHE PHE B . n 
B 1 469 ARG 469 469 469 ARG ARG B . n 
B 1 470 SER 470 470 470 SER SER B . n 
B 1 471 PHE 471 471 471 PHE PHE B . n 
B 1 472 VAL 472 472 472 VAL VAL B . n 
B 1 473 ARG 473 473 473 ARG ARG B . n 
B 1 474 ARG 474 474 474 ARG ARG B . n 
B 1 475 ALA 475 475 475 ALA ALA B . n 
B 1 476 GLN 476 476 476 GLN GLN B . n 
B 1 477 GLU 477 477 477 GLU GLU B . n 
B 1 478 LEU 478 478 ?   ?   ?   B . n 
B 1 479 GLU 479 479 ?   ?   ?   B . n 
B 1 480 HIS 480 480 ?   ?   ?   B . n 
B 1 481 HIS 481 481 ?   ?   ?   B . n 
B 1 482 HIS 482 482 ?   ?   ?   B . n 
B 1 483 HIS 483 483 ?   ?   ?   B . n 
B 1 484 HIS 484 484 ?   ?   ?   B . n 
C 1 1   MET 1   1   1   MET MET C . n 
C 1 2   LYS 2   2   2   LYS LYS C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   LEU 4   4   4   LEU LEU C . n 
C 1 5   PHE 5   5   5   PHE PHE C . n 
C 1 6   LEU 6   6   6   LEU LEU C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   PHE 8   8   8   PHE PHE C . n 
C 1 9   TRP 9   9   9   TRP TRP C . n 
C 1 10  TRP 10  10  10  TRP TRP C . n 
C 1 11  HIS 11  11  11  HIS HIS C . n 
C 1 12  MET 12  12  12  MET MET C . n 
C 1 13  HIS 13  13  13  HIS HIS C . n 
C 1 14  GLN 14  14  14  GLN GLN C . n 
C 1 15  PRO 15  15  15  PRO PRO C . n 
C 1 16  LEU 16  16  16  LEU LEU C . n 
C 1 17  TYR 17  17  17  TYR TYR C . n 
C 1 18  ARG 18  18  18  ARG ARG C . n 
C 1 19  GLU 19  19  19  GLU GLU C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  TYR 21  21  21  TYR TYR C . n 
C 1 22  THR 22  22  22  THR THR C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  TYR 25  25  25  TYR TYR C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  LEU 27  27  27  LEU LEU C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  TRP 29  29  29  TRP TRP C . n 
C 1 30  THR 30  30  30  THR THR C . n 
C 1 31  PHE 31  31  31  PHE PHE C . n 
C 1 32  PHE 32  32  32  PHE PHE C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  ALA 34  34  34  ALA ALA C . n 
C 1 35  VAL 35  35  35  VAL VAL C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  ASP 37  37  37  ASP ASP C . n 
C 1 38  TYR 38  38  38  TYR TYR C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  MET 41  41  41  MET MET C . n 
C 1 42  PRO 42  42  42  PRO PRO C . n 
C 1 43  ALA 43  43  43  ALA ALA C . n 
C 1 44  TYR 44  44  44  TYR TYR C . n 
C 1 45  LEU 45  45  45  LEU LEU C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  ASP 47  47  47  ASP ASP C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  ILE 50  50  50  ILE ILE C . n 
C 1 51  LYS 51  51  51  LYS LYS C . n 
C 1 52  LEU 52  52  52  LEU LEU C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  PHE 54  54  54  PHE PHE C . n 
C 1 55  ASN 55  55  55  ASN ASN C . n 
C 1 56  LEU 56  56  56  LEU LEU C . n 
C 1 57  THR 57  57  57  THR THR C . n 
C 1 58  PRO 58  58  58  PRO PRO C . n 
C 1 59  VAL 59  59  59  VAL VAL C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  ILE 61  61  61  ILE ILE C . n 
C 1 62  ASP 62  62  62  ASP ASP C . n 
C 1 63  GLN 63  63  63  GLN GLN C . n 
C 1 64  ILE 64  64  64  ILE ILE C . n 
C 1 65  GLN 65  65  65  GLN GLN C . n 
C 1 66  GLU 66  66  66  GLU GLU C . n 
C 1 67  TYR 67  67  67  TYR TYR C . n 
C 1 68  ALA 68  68  68  ALA ALA C . n 
C 1 69  GLN 69  69  69  GLN GLN C . n 
C 1 70  GLY 70  70  70  GLY GLY C . n 
C 1 71  LYS 71  71  71  LYS LYS C . n 
C 1 72  ALA 72  72  72  ALA ALA C . n 
C 1 73  LYS 73  73  73  LYS LYS C . n 
C 1 74  ASP 74  74  74  ASP ASP C . n 
C 1 75  VAL 75  75  75  VAL VAL C . n 
C 1 76  PHE 76  76  76  PHE PHE C . n 
C 1 77  LEU 77  77  77  LEU LEU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ALA 79  79  79  ALA ALA C . n 
C 1 80  ILE 80  80  80  ILE ILE C . n 
C 1 81  ARG 81  81  81  ARG ARG C . n 
C 1 82  LYS 82  82  82  LYS LYS C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  PRO 84  84  84  PRO PRO C . n 
C 1 85  ASP 85  85  85  ASP ASP C . n 
C 1 86  ASP 86  86  86  ASP ASP C . n 
C 1 87  LEU 87  87  87  LEU LEU C . n 
C 1 88  GLU 88  88  88  GLU GLU C . n 
C 1 89  LYS 89  89  89  LYS LYS C . n 
C 1 90  GLU 90  90  90  GLU GLU C . n 
C 1 91  GLU 91  91  91  GLU GLU C . n 
C 1 92  VAL 92  92  92  VAL VAL C . n 
C 1 93  GLU 93  93  93  GLU GLU C . n 
C 1 94  LYS 94  94  94  LYS LYS C . n 
C 1 95  LEU 95  95  95  LEU LEU C . n 
C 1 96  ILE 96  96  96  ILE ILE C . n 
C 1 97  GLU 97  97  97  GLU GLU C . n 
C 1 98  PHE 98  98  98  PHE PHE C . n 
C 1 99  THR 99  99  99  THR THR C . n 
C 1 100 LYS 100 100 100 LYS LYS C . n 
C 1 101 LEU 101 101 101 LEU LEU C . n 
C 1 102 ASN 102 102 102 ASN ASN C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 LYS 105 105 105 LYS LYS C . n 
C 1 106 PRO 106 106 106 PRO PRO C . n 
C 1 107 ILE 107 107 107 ILE ILE C . n 
C 1 108 TYR 108 108 108 TYR TYR C . n 
C 1 109 ARG 109 109 109 ARG ARG C . n 
C 1 110 PHE 110 110 110 PHE PHE C . n 
C 1 111 GLU 111 111 111 GLU GLU C . n 
C 1 112 ARG 112 112 112 ARG ARG C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 ARG 114 114 114 ARG ARG C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 MET 117 117 117 MET MET C . n 
C 1 118 ASN 118 118 118 ASN ASN C . n 
C 1 119 LYS 119 119 119 LYS LYS C . n 
C 1 120 GLU 120 120 120 GLU GLU C . n 
C 1 121 LYS 121 121 121 LYS LYS C . n 
C 1 122 LEU 122 122 122 LEU LEU C . n 
C 1 123 ASN 123 123 123 ASN ASN C . n 
C 1 124 ARG 124 124 124 ARG ARG C . n 
C 1 125 GLU 125 125 125 GLU GLU C . n 
C 1 126 GLU 126 126 126 GLU GLU C . n 
C 1 127 LEU 127 127 127 LEU LEU C . n 
C 1 128 LEU 128 128 128 LEU LEU C . n 
C 1 129 ASP 129 129 129 ASP ASP C . n 
C 1 130 LEU 130 130 130 LEU LEU C . n 
C 1 131 GLN 131 131 131 GLN GLN C . n 
C 1 132 THR 132 132 132 THR THR C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LEU 135 135 135 LEU LEU C . n 
C 1 136 LEU 136 136 136 LEU LEU C . n 
C 1 137 ALA 137 137 137 ALA ALA C . n 
C 1 138 TRP 138 138 138 TRP TRP C . n 
C 1 139 CYS 139 139 139 CYS CYS C . n 
C 1 140 GLY 140 140 140 GLY GLY C . n 
C 1 141 ARG 141 141 141 ARG ARG C . n 
C 1 142 THR 142 142 142 THR THR C . n 
C 1 143 LEU 143 143 143 LEU LEU C . n 
C 1 144 ARG 144 144 144 ARG ARG C . n 
C 1 145 LYS 145 145 145 LYS LYS C . n 
C 1 146 ASP 146 146 146 ASP ASP C . n 
C 1 147 LEU 147 147 147 LEU LEU C . n 
C 1 148 LYS 148 148 148 LYS LYS C . n 
C 1 149 ASP 149 149 149 ASP ASP C . n 
C 1 150 LEU 150 150 150 LEU LEU C . n 
C 1 151 LEU 151 151 151 LEU LEU C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 LYS 153 153 153 LYS LYS C . n 
C 1 154 GLY 154 154 154 GLY GLY C . n 
C 1 155 ARG 155 155 155 ARG ARG C . n 
C 1 156 ASN 156 156 156 ASN ASN C . n 
C 1 157 TYR 157 157 157 TYR TYR C . n 
C 1 158 THR 158 158 158 THR THR C . n 
C 1 159 GLN 159 159 159 GLN GLN C . n 
C 1 160 GLU 160 160 160 GLU GLU C . n 
C 1 161 GLU 161 161 161 GLU GLU C . n 
C 1 162 LYS 162 162 162 LYS LYS C . n 
C 1 163 GLU 163 163 163 GLU GLU C . n 
C 1 164 TYR 164 164 164 TYR TYR C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LEU 166 166 166 LEU LEU C . n 
C 1 167 ASN 167 167 167 ASN ASN C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 TYR 169 169 169 TYR TYR C . n 
C 1 170 PHE 170 170 170 PHE PHE C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ILE 172 172 172 ILE ILE C . n 
C 1 173 ILE 173 173 173 ILE ILE C . n 
C 1 174 LYS 174 174 174 LYS LYS C . n 
C 1 175 LYS 175 175 175 LYS LYS C . n 
C 1 176 THR 176 176 176 THR THR C . n 
C 1 177 LEU 177 177 177 LEU LEU C . n 
C 1 178 SER 178 178 178 SER SER C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 TYR 180 180 180 TYR TYR C . n 
C 1 181 ARG 181 181 181 ARG ARG C . n 
C 1 182 GLU 182 182 182 GLU GLU C . n 
C 1 183 ILE 183 183 183 ILE ILE C . n 
C 1 184 LYS 184 184 184 LYS LYS C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 GLU 186 186 186 GLU GLU C . n 
C 1 187 GLY 187 187 187 GLY GLY C . n 
C 1 188 LYS 188 188 188 LYS LYS C . n 
C 1 189 GLY 189 189 189 GLY GLY C . n 
C 1 190 SER 190 190 190 SER SER C . n 
C 1 191 VAL 191 191 191 VAL VAL C . n 
C 1 192 SER 192 192 192 SER SER C . n 
C 1 193 THR 193 193 193 THR THR C . n 
C 1 194 SER 194 194 194 SER SER C . n 
C 1 195 PRO 195 195 195 PRO PRO C . n 
C 1 196 TYR 196 196 196 TYR TYR C . n 
C 1 197 TYR 197 197 197 TYR TYR C . n 
C 1 198 HIS 198 198 198 HIS HIS C . n 
C 1 199 PRO 199 199 199 PRO PRO C . n 
C 1 200 LEU 200 200 200 LEU LEU C . n 
C 1 201 ILE 201 201 201 ILE ILE C . n 
C 1 202 PRO 202 202 202 PRO PRO C . n 
C 1 203 ILE 203 203 203 ILE ILE C . n 
C 1 204 LEU 204 204 204 LEU LEU C . n 
C 1 205 LEU 205 205 205 LEU LEU C . n 
C 1 206 ASN 206 206 206 ASN ASN C . n 
C 1 207 PRO 207 207 207 PRO PRO C . n 
C 1 208 ASN 208 208 208 ASN ASN C . n 
C 1 209 CYS 209 209 209 CYS CYS C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 TYR 211 211 211 TYR TYR C . n 
C 1 212 GLU 212 212 212 GLU GLU C . n 
C 1 213 THR 213 213 213 THR THR C . n 
C 1 214 THR 214 214 214 THR THR C . n 
C 1 215 PRO 215 215 215 PRO PRO C . n 
C 1 216 ASN 216 216 216 ASN ASN C . n 
C 1 217 VAL 217 217 217 VAL VAL C . n 
C 1 218 LYS 218 218 218 LYS LYS C . n 
C 1 219 ILE 219 219 219 ILE ILE C . n 
C 1 220 PRO 220 220 220 PRO PRO C . n 
C 1 221 ASP 221 221 221 ASP ASP C . n 
C 1 222 PHE 222 222 222 PHE PHE C . n 
C 1 223 ALA 223 223 223 ALA ALA C . n 
C 1 224 VAL 224 224 224 VAL VAL C . n 
C 1 225 SER 225 225 225 SER SER C . n 
C 1 226 PHE 226 226 226 PHE PHE C . n 
C 1 227 ARG 227 227 227 ARG ARG C . n 
C 1 228 GLU 228 228 228 GLU GLU C . n 
C 1 229 ASP 229 229 229 ASP ASP C . n 
C 1 230 ALA 230 230 230 ALA ALA C . n 
C 1 231 SER 231 231 231 SER SER C . n 
C 1 232 LYS 232 232 232 LYS LYS C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 VAL 234 234 234 VAL VAL C . n 
C 1 235 GLU 235 235 235 GLU GLU C . n 
C 1 236 LEU 236 236 236 LEU LEU C . n 
C 1 237 ALA 237 237 237 ALA ALA C . n 
C 1 238 LYS 238 238 238 LYS LYS C . n 
C 1 239 GLU 239 239 239 GLU GLU C . n 
C 1 240 LYS 240 240 240 LYS LYS C . n 
C 1 241 TYR 241 241 241 TYR TYR C . n 
C 1 242 PHE 242 242 242 PHE PHE C . n 
C 1 243 GLU 243 243 243 GLU GLU C . n 
C 1 244 ILE 244 244 244 ILE ILE C . n 
C 1 245 PHE 245 245 245 PHE PHE C . n 
C 1 246 GLY 246 246 246 GLY GLY C . n 
C 1 247 GLU 247 247 247 GLU GLU C . n 
C 1 248 HIS 248 248 248 HIS HIS C . n 
C 1 249 PRO 249 249 249 PRO PRO C . n 
C 1 250 VAL 250 250 250 VAL VAL C . n 
C 1 251 TYR 251 251 251 TYR TYR C . n 
C 1 252 MET 252 252 252 MET MET C . n 
C 1 253 TRP 253 253 253 TRP TRP C . n 
C 1 254 PRO 254 254 254 PRO PRO C . n 
C 1 255 PRO 255 255 255 PRO PRO C . n 
C 1 256 GLU 256 256 256 GLU GLU C . n 
C 1 257 ALA 257 257 257 ALA ALA C . n 
C 1 258 SER 258 258 258 SER SER C . n 
C 1 259 VAL 259 259 259 VAL VAL C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 ASN 261 261 261 ASN ASN C . n 
C 1 262 GLU 262 262 262 GLU GLU C . n 
C 1 263 ALA 263 263 263 ALA ALA C . n 
C 1 264 LEU 264 264 264 LEU LEU C . n 
C 1 265 GLU 265 265 265 GLU GLU C . n 
C 1 266 LEU 266 266 266 LEU LEU C . n 
C 1 267 TYR 267 267 267 TYR TYR C . n 
C 1 268 TYR 268 268 268 TYR TYR C . n 
C 1 269 GLU 269 269 269 GLU GLU C . n 
C 1 270 LYS 270 270 270 LYS LYS C . n 
C 1 271 GLY 271 271 271 GLY GLY C . n 
C 1 272 ILE 272 272 272 ILE ILE C . n 
C 1 273 ASN 273 273 273 ASN ASN C . n 
C 1 274 MET 274 274 274 MET MET C . n 
C 1 275 LEU 275 275 275 LEU LEU C . n 
C 1 276 ALA 276 276 276 ALA ALA C . n 
C 1 277 THR 277 277 277 THR THR C . n 
C 1 278 ASP 278 278 278 ASP ASP C . n 
C 1 279 GLU 279 279 279 GLU GLU C . n 
C 1 280 VAL 280 280 280 VAL VAL C . n 
C 1 281 ILE 281 281 281 ILE ILE C . n 
C 1 282 LEU 282 282 282 LEU LEU C . n 
C 1 283 LYS 283 283 283 LYS LYS C . n 
C 1 284 ASN 284 284 284 ASN ASN C . n 
C 1 285 SER 285 285 285 SER SER C . n 
C 1 286 VAL 286 286 286 VAL VAL C . n 
C 1 287 GLU 287 287 287 GLU GLU C . n 
C 1 288 ARG 288 288 288 ARG ARG C . n 
C 1 289 ALA 289 289 289 ALA ALA C . n 
C 1 290 SER 290 290 290 SER SER C . n 
C 1 291 PRO 291 291 291 PRO PRO C . n 
C 1 292 TYR 292 292 292 TYR TYR C . n 
C 1 293 LEU 293 293 293 LEU LEU C . n 
C 1 294 ARG 294 294 294 ARG ARG C . n 
C 1 295 TYR 295 295 295 TYR TYR C . n 
C 1 296 TYR 296 296 296 TYR TYR C . n 
C 1 297 PHE 297 297 297 PHE PHE C . n 
C 1 298 ARG 298 298 298 ARG ARG C . n 
C 1 299 GLU 299 299 299 GLU GLU C . n 
C 1 300 LEU 300 300 300 LEU LEU C . n 
C 1 301 ILE 301 301 301 ILE ILE C . n 
C 1 302 SER 302 302 302 SER SER C . n 
C 1 303 VAL 303 303 303 VAL VAL C . n 
C 1 304 PHE 304 304 304 PHE PHE C . n 
C 1 305 PHE 305 305 305 PHE PHE C . n 
C 1 306 ARG 306 306 306 ARG ARG C . n 
C 1 307 ASP 307 307 307 ASP ASP C . n 
C 1 308 LYS 308 308 308 LYS LYS C . n 
C 1 309 THR 309 309 309 THR THR C . n 
C 1 310 LEU 310 310 310 LEU LEU C . n 
C 1 311 SER 311 311 311 SER SER C . n 
C 1 312 ASP 312 312 312 ASP ASP C . n 
C 1 313 LEU 313 313 313 LEU LEU C . n 
C 1 314 ILE 314 314 314 ILE ILE C . n 
C 1 315 GLY 315 315 315 GLY GLY C . n 
C 1 316 PHE 316 316 316 PHE PHE C . n 
C 1 317 SER 317 317 317 SER SER C . n 
C 1 318 TYR 318 318 318 TYR TYR C . n 
C 1 319 HIS 319 319 319 HIS HIS C . n 
C 1 320 ALA 320 320 320 ALA ALA C . n 
C 1 321 TRP 321 321 321 TRP TRP C . n 
C 1 322 ASN 322 322 322 ASN ASN C . n 
C 1 323 ALA 323 323 323 ALA ALA C . n 
C 1 324 GLU 324 324 324 GLU GLU C . n 
C 1 325 ASP 325 325 325 ASP ASP C . n 
C 1 326 ALA 326 326 326 ALA ALA C . n 
C 1 327 VAL 327 327 327 VAL VAL C . n 
C 1 328 ARG 328 328 328 ARG ARG C . n 
C 1 329 ASP 329 329 329 ASP ASP C . n 
C 1 330 PHE 330 330 330 PHE PHE C . n 
C 1 331 ILE 331 331 331 ILE ILE C . n 
C 1 332 GLY 332 332 332 GLY GLY C . n 
C 1 333 ARG 333 333 333 ARG ARG C . n 
C 1 334 LEU 334 334 334 LEU LEU C . n 
C 1 335 LYS 335 335 335 LYS LYS C . n 
C 1 336 LYS 336 336 336 LYS LYS C . n 
C 1 337 ILE 337 337 337 ILE ILE C . n 
C 1 338 HIS 338 338 338 HIS HIS C . n 
C 1 339 GLU 339 339 339 GLU GLU C . n 
C 1 340 SER 340 340 340 SER SER C . n 
C 1 341 VAL 341 341 341 VAL VAL C . n 
C 1 342 ASP 342 342 342 ASP ASP C . n 
C 1 343 PHE 343 343 343 PHE PHE C . n 
C 1 344 GLN 344 344 344 GLN GLN C . n 
C 1 345 PRO 345 345 345 PRO PRO C . n 
C 1 346 VAL 346 346 346 VAL VAL C . n 
C 1 347 VAL 347 347 347 VAL VAL C . n 
C 1 348 PHE 348 348 348 PHE PHE C . n 
C 1 349 VAL 349 349 349 VAL VAL C . n 
C 1 350 VAL 350 350 350 VAL VAL C . n 
C 1 351 LEU 351 351 351 LEU LEU C . n 
C 1 352 ASP 352 352 352 ASP ASP C . n 
C 1 353 GLY 353 353 353 GLY GLY C . n 
C 1 354 GLU 354 354 354 GLU GLU C . n 
C 1 355 ASN 355 355 355 ASN ASN C . n 
C 1 356 CYS 356 356 356 CYS CYS C . n 
C 1 357 TRP 357 357 357 TRP TRP C . n 
C 1 358 GLU 358 358 358 GLU GLU C . n 
C 1 359 TYR 359 359 359 TYR TYR C . n 
C 1 360 TYR 360 360 360 TYR TYR C . n 
C 1 361 GLU 361 361 361 GLU GLU C . n 
C 1 362 GLU 362 362 362 GLU GLU C . n 
C 1 363 ASN 363 363 363 ASN ASN C . n 
C 1 364 GLY 364 364 364 GLY GLY C . n 
C 1 365 ILE 365 365 365 ILE ILE C . n 
C 1 366 PRO 366 366 366 PRO PRO C . n 
C 1 367 PHE 367 367 367 PHE PHE C . n 
C 1 368 LEU 368 368 368 LEU LEU C . n 
C 1 369 GLU 369 369 369 GLU GLU C . n 
C 1 370 LYS 370 370 370 LYS LYS C . n 
C 1 371 LEU 371 371 371 LEU LEU C . n 
C 1 372 TYR 372 372 372 TYR TYR C . n 
C 1 373 SER 373 373 373 SER SER C . n 
C 1 374 THR 374 374 374 THR THR C . n 
C 1 375 LEU 375 375 375 LEU LEU C . n 
C 1 376 GLU 376 376 376 GLU GLU C . n 
C 1 377 LYS 377 377 377 LYS LYS C . n 
C 1 378 GLU 378 378 378 GLU GLU C . n 
C 1 379 GLU 379 379 379 GLU GLU C . n 
C 1 380 TRP 380 380 380 TRP TRP C . n 
C 1 381 ILE 381 381 381 ILE ILE C . n 
C 1 382 GLU 382 382 382 GLU GLU C . n 
C 1 383 THR 383 383 383 THR THR C . n 
C 1 384 LEU 384 384 384 LEU LEU C . n 
C 1 385 THR 385 385 385 THR THR C . n 
C 1 386 LEU 386 386 386 LEU LEU C . n 
C 1 387 GLU 387 387 387 GLU GLU C . n 
C 1 388 GLU 388 388 388 GLU GLU C . n 
C 1 389 ALA 389 389 389 ALA ALA C . n 
C 1 390 MET 390 390 390 MET MET C . n 
C 1 391 ARG 391 391 391 ARG ARG C . n 
C 1 392 LYS 392 392 392 LYS LYS C . n 
C 1 393 GLU 393 393 393 GLU GLU C . n 
C 1 394 ASP 394 394 394 ASP ASP C . n 
C 1 395 VAL 395 395 395 VAL VAL C . n 
C 1 396 LYS 396 396 396 LYS LYS C . n 
C 1 397 THR 397 397 397 THR THR C . n 
C 1 398 GLU 398 398 398 GLU GLU C . n 
C 1 399 VAL 399 399 399 VAL VAL C . n 
C 1 400 ILE 400 400 400 ILE ILE C . n 
C 1 401 GLU 401 401 401 GLU GLU C . n 
C 1 402 SER 402 402 402 SER SER C . n 
C 1 403 VAL 403 403 403 VAL VAL C . n 
C 1 404 LYS 404 404 404 LYS LYS C . n 
C 1 405 ALA 405 405 405 ALA ALA C . n 
C 1 406 GLY 406 406 406 GLY GLY C . n 
C 1 407 THR 407 407 407 THR THR C . n 
C 1 408 TRP 408 408 408 TRP TRP C . n 
C 1 409 PHE 409 409 409 PHE PHE C . n 
C 1 410 ASP 410 410 410 ASP ASP C . n 
C 1 411 GLY 411 411 411 GLY GLY C . n 
C 1 412 ASN 412 412 412 ASN ASN C . n 
C 1 413 PHE 413 413 413 PHE PHE C . n 
C 1 414 LEU 414 414 414 LEU LEU C . n 
C 1 415 LYS 415 415 415 LYS LYS C . n 
C 1 416 TRP 416 416 416 TRP TRP C . n 
C 1 417 ILE 417 417 417 ILE ILE C . n 
C 1 418 GLY 418 418 418 GLY GLY C . n 
C 1 419 ASN 419 419 419 ASN ASN C . n 
C 1 420 LYS 420 420 420 LYS LYS C . n 
C 1 421 GLU 421 421 421 GLU GLU C . n 
C 1 422 LYS 422 422 422 LYS LYS C . n 
C 1 423 ASN 423 423 423 ASN ASN C . n 
C 1 424 GLU 424 424 424 GLU GLU C . n 
C 1 425 TYR 425 425 425 TYR TYR C . n 
C 1 426 TRP 426 426 426 TRP TRP C . n 
C 1 427 LYS 427 427 427 LYS LYS C . n 
C 1 428 ILE 428 428 428 ILE ILE C . n 
C 1 429 LEU 429 429 429 LEU LEU C . n 
C 1 430 ILE 430 430 430 ILE ILE C . n 
C 1 431 GLU 431 431 431 GLU GLU C . n 
C 1 432 ALA 432 432 432 ALA ALA C . n 
C 1 433 LYS 433 433 433 LYS LYS C . n 
C 1 434 LYS 434 434 434 LYS LYS C . n 
C 1 435 LYS 435 435 435 LYS LYS C . n 
C 1 436 ALA 436 436 436 ALA ALA C . n 
C 1 437 LYS 437 437 437 LYS LYS C . n 
C 1 438 ASN 438 438 438 ASN ASN C . n 
C 1 439 ASP 439 439 439 ASP ASP C . n 
C 1 440 TYR 440 440 440 TYR TYR C . n 
C 1 441 ILE 441 441 441 ILE ILE C . n 
C 1 442 LEU 442 442 442 LEU LEU C . n 
C 1 443 VAL 443 443 443 VAL VAL C . n 
C 1 444 ALA 444 444 444 ALA ALA C . n 
C 1 445 GLU 445 445 445 GLU GLU C . n 
C 1 446 GLY 446 446 446 GLY GLY C . n 
C 1 447 SER 447 447 447 SER SER C . n 
C 1 448 ASP 448 448 448 ASP ASP C . n 
C 1 449 TRP 449 449 449 TRP TRP C . n 
C 1 450 PHE 450 450 450 PHE PHE C . n 
C 1 451 TRP 451 451 451 TRP TRP C . n 
C 1 452 TRP 452 452 452 TRP TRP C . n 
C 1 453 GLN 453 453 453 GLN GLN C . n 
C 1 454 GLY 454 454 454 GLY GLY C . n 
C 1 455 GLU 455 455 455 GLU GLU C . n 
C 1 456 GLU 456 456 456 GLU GLU C . n 
C 1 457 LYS 457 457 457 LYS LYS C . n 
C 1 458 ALA 458 458 458 ALA ALA C . n 
C 1 459 PRO 459 459 459 PRO PRO C . n 
C 1 460 PHE 460 460 460 PHE PHE C . n 
C 1 461 VAL 461 461 461 VAL VAL C . n 
C 1 462 GLU 462 462 462 GLU GLU C . n 
C 1 463 VAL 463 463 463 VAL VAL C . n 
C 1 464 PHE 464 464 464 PHE PHE C . n 
C 1 465 ASP 465 465 465 ASP ASP C . n 
C 1 466 LYS 466 466 466 LYS LYS C . n 
C 1 467 LEU 467 467 467 LEU LEU C . n 
C 1 468 PHE 468 468 468 PHE PHE C . n 
C 1 469 ARG 469 469 469 ARG ARG C . n 
C 1 470 SER 470 470 470 SER SER C . n 
C 1 471 PHE 471 471 471 PHE PHE C . n 
C 1 472 VAL 472 472 472 VAL VAL C . n 
C 1 473 ARG 473 473 473 ARG ARG C . n 
C 1 474 ARG 474 474 474 ARG ARG C . n 
C 1 475 ALA 475 475 475 ALA ALA C . n 
C 1 476 GLN 476 476 476 GLN GLN C . n 
C 1 477 GLU 477 477 477 GLU GLU C . n 
C 1 478 LEU 478 478 478 LEU LEU C . n 
C 1 479 GLU 479 479 479 GLU GLU C . n 
C 1 480 HIS 480 480 480 HIS HIS C . n 
C 1 481 HIS 481 481 481 HIS HIS C . n 
C 1 482 HIS 482 482 482 HIS HIS C . n 
C 1 483 HIS 483 483 483 HIS HIS C . n 
C 1 484 HIS 484 484 484 HIS HIS C . n 
D 1 1   MET 1   1   1   MET MET D . n 
D 1 2   LYS 2   2   2   LYS LYS D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   LEU 4   4   4   LEU LEU D . n 
D 1 5   PHE 5   5   5   PHE PHE D . n 
D 1 6   LEU 6   6   6   LEU LEU D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   PHE 8   8   8   PHE PHE D . n 
D 1 9   TRP 9   9   9   TRP TRP D . n 
D 1 10  TRP 10  10  10  TRP TRP D . n 
D 1 11  HIS 11  11  11  HIS HIS D . n 
D 1 12  MET 12  12  12  MET MET D . n 
D 1 13  HIS 13  13  13  HIS HIS D . n 
D 1 14  GLN 14  14  14  GLN GLN D . n 
D 1 15  PRO 15  15  15  PRO PRO D . n 
D 1 16  LEU 16  16  16  LEU LEU D . n 
D 1 17  TYR 17  17  17  TYR TYR D . n 
D 1 18  ARG 18  18  18  ARG ARG D . n 
D 1 19  GLU 19  19  19  GLU GLU D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  TYR 21  21  21  TYR TYR D . n 
D 1 22  THR 22  22  22  THR THR D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  TYR 25  25  25  TYR TYR D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  LEU 27  27  27  LEU LEU D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  TRP 29  29  29  TRP TRP D . n 
D 1 30  THR 30  30  30  THR THR D . n 
D 1 31  PHE 31  31  31  PHE PHE D . n 
D 1 32  PHE 32  32  32  PHE PHE D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  ALA 34  34  34  ALA ALA D . n 
D 1 35  VAL 35  35  35  VAL VAL D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  ASP 37  37  37  ASP ASP D . n 
D 1 38  TYR 38  38  38  TYR TYR D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  MET 41  41  41  MET MET D . n 
D 1 42  PRO 42  42  42  PRO PRO D . n 
D 1 43  ALA 43  43  43  ALA ALA D . n 
D 1 44  TYR 44  44  44  TYR TYR D . n 
D 1 45  LEU 45  45  45  LEU LEU D . n 
D 1 46  LYS 46  46  46  LYS LYS D . n 
D 1 47  ASP 47  47  47  ASP ASP D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  ILE 50  50  50  ILE ILE D . n 
D 1 51  LYS 51  51  51  LYS LYS D . n 
D 1 52  LEU 52  52  52  LEU LEU D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  PHE 54  54  54  PHE PHE D . n 
D 1 55  ASN 55  55  55  ASN ASN D . n 
D 1 56  LEU 56  56  56  LEU LEU D . n 
D 1 57  THR 57  57  57  THR THR D . n 
D 1 58  PRO 58  58  58  PRO PRO D . n 
D 1 59  VAL 59  59  59  VAL VAL D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  ILE 61  61  61  ILE ILE D . n 
D 1 62  ASP 62  62  62  ASP ASP D . n 
D 1 63  GLN 63  63  63  GLN GLN D . n 
D 1 64  ILE 64  64  64  ILE ILE D . n 
D 1 65  GLN 65  65  65  GLN GLN D . n 
D 1 66  GLU 66  66  66  GLU GLU D . n 
D 1 67  TYR 67  67  67  TYR TYR D . n 
D 1 68  ALA 68  68  68  ALA ALA D . n 
D 1 69  GLN 69  69  69  GLN GLN D . n 
D 1 70  GLY 70  70  70  GLY GLY D . n 
D 1 71  LYS 71  71  71  LYS LYS D . n 
D 1 72  ALA 72  72  72  ALA ALA D . n 
D 1 73  LYS 73  73  73  LYS LYS D . n 
D 1 74  ASP 74  74  74  ASP ASP D . n 
D 1 75  VAL 75  75  75  VAL VAL D . n 
D 1 76  PHE 76  76  76  PHE PHE D . n 
D 1 77  LEU 77  77  77  LEU LEU D . n 
D 1 78  GLU 78  78  78  GLU GLU D . n 
D 1 79  ALA 79  79  79  ALA ALA D . n 
D 1 80  ILE 80  80  80  ILE ILE D . n 
D 1 81  ARG 81  81  81  ARG ARG D . n 
D 1 82  LYS 82  82  82  LYS LYS D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  PRO 84  84  84  PRO PRO D . n 
D 1 85  ASP 85  85  85  ASP ASP D . n 
D 1 86  ASP 86  86  86  ASP ASP D . n 
D 1 87  LEU 87  87  87  LEU LEU D . n 
D 1 88  GLU 88  88  88  GLU GLU D . n 
D 1 89  LYS 89  89  89  LYS LYS D . n 
D 1 90  GLU 90  90  90  GLU GLU D . n 
D 1 91  GLU 91  91  91  GLU GLU D . n 
D 1 92  VAL 92  92  92  VAL VAL D . n 
D 1 93  GLU 93  93  93  GLU GLU D . n 
D 1 94  LYS 94  94  94  LYS LYS D . n 
D 1 95  LEU 95  95  95  LEU LEU D . n 
D 1 96  ILE 96  96  96  ILE ILE D . n 
D 1 97  GLU 97  97  97  GLU GLU D . n 
D 1 98  PHE 98  98  98  PHE PHE D . n 
D 1 99  THR 99  99  99  THR THR D . n 
D 1 100 LYS 100 100 100 LYS LYS D . n 
D 1 101 LEU 101 101 101 LEU LEU D . n 
D 1 102 ASN 102 102 102 ASN ASN D . n 
D 1 103 TYR 103 103 103 TYR TYR D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 LYS 105 105 105 LYS LYS D . n 
D 1 106 PRO 106 106 106 PRO PRO D . n 
D 1 107 ILE 107 107 107 ILE ILE D . n 
D 1 108 TYR 108 108 108 TYR TYR D . n 
D 1 109 ARG 109 109 109 ARG ARG D . n 
D 1 110 PHE 110 110 110 PHE PHE D . n 
D 1 111 GLU 111 111 111 GLU GLU D . n 
D 1 112 ARG 112 112 112 ARG ARG D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 ARG 114 114 114 ARG ARG D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 MET 117 117 117 MET MET D . n 
D 1 118 ASN 118 118 118 ASN ASN D . n 
D 1 119 LYS 119 119 119 LYS LYS D . n 
D 1 120 GLU 120 120 120 GLU GLU D . n 
D 1 121 LYS 121 121 121 LYS LYS D . n 
D 1 122 LEU 122 122 122 LEU LEU D . n 
D 1 123 ASN 123 123 123 ASN ASN D . n 
D 1 124 ARG 124 124 124 ARG ARG D . n 
D 1 125 GLU 125 125 125 GLU GLU D . n 
D 1 126 GLU 126 126 126 GLU GLU D . n 
D 1 127 LEU 127 127 127 LEU LEU D . n 
D 1 128 LEU 128 128 128 LEU LEU D . n 
D 1 129 ASP 129 129 129 ASP ASP D . n 
D 1 130 LEU 130 130 130 LEU LEU D . n 
D 1 131 GLN 131 131 131 GLN GLN D . n 
D 1 132 THR 132 132 132 THR THR D . n 
D 1 133 LEU 133 133 133 LEU LEU D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LEU 135 135 135 LEU LEU D . n 
D 1 136 LEU 136 136 136 LEU LEU D . n 
D 1 137 ALA 137 137 137 ALA ALA D . n 
D 1 138 TRP 138 138 138 TRP TRP D . n 
D 1 139 CYS 139 139 139 CYS CYS D . n 
D 1 140 GLY 140 140 140 GLY GLY D . n 
D 1 141 ARG 141 141 141 ARG ARG D . n 
D 1 142 THR 142 142 142 THR THR D . n 
D 1 143 LEU 143 143 143 LEU LEU D . n 
D 1 144 ARG 144 144 144 ARG ARG D . n 
D 1 145 LYS 145 145 145 LYS LYS D . n 
D 1 146 ASP 146 146 146 ASP ASP D . n 
D 1 147 LEU 147 147 147 LEU LEU D . n 
D 1 148 LYS 148 148 148 LYS LYS D . n 
D 1 149 ASP 149 149 149 ASP ASP D . n 
D 1 150 LEU 150 150 150 LEU LEU D . n 
D 1 151 LEU 151 151 151 LEU LEU D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 LYS 153 153 153 LYS LYS D . n 
D 1 154 GLY 154 154 154 GLY GLY D . n 
D 1 155 ARG 155 155 155 ARG ARG D . n 
D 1 156 ASN 156 156 156 ASN ASN D . n 
D 1 157 TYR 157 157 157 TYR TYR D . n 
D 1 158 THR 158 158 158 THR THR D . n 
D 1 159 GLN 159 159 159 GLN GLN D . n 
D 1 160 GLU 160 160 160 GLU GLU D . n 
D 1 161 GLU 161 161 161 GLU GLU D . n 
D 1 162 LYS 162 162 162 LYS LYS D . n 
D 1 163 GLU 163 163 163 GLU GLU D . n 
D 1 164 TYR 164 164 164 TYR TYR D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LEU 166 166 166 LEU LEU D . n 
D 1 167 ASN 167 167 167 ASN ASN D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 TYR 169 169 169 TYR TYR D . n 
D 1 170 PHE 170 170 170 PHE PHE D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ILE 172 172 172 ILE ILE D . n 
D 1 173 ILE 173 173 173 ILE ILE D . n 
D 1 174 LYS 174 174 174 LYS LYS D . n 
D 1 175 LYS 175 175 175 LYS LYS D . n 
D 1 176 THR 176 176 176 THR THR D . n 
D 1 177 LEU 177 177 177 LEU LEU D . n 
D 1 178 SER 178 178 178 SER SER D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 TYR 180 180 180 TYR TYR D . n 
D 1 181 ARG 181 181 181 ARG ARG D . n 
D 1 182 GLU 182 182 182 GLU GLU D . n 
D 1 183 ILE 183 183 183 ILE ILE D . n 
D 1 184 LYS 184 184 184 LYS LYS D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 GLU 186 186 186 GLU GLU D . n 
D 1 187 GLY 187 187 187 GLY GLY D . n 
D 1 188 LYS 188 188 188 LYS LYS D . n 
D 1 189 GLY 189 189 189 GLY GLY D . n 
D 1 190 SER 190 190 190 SER SER D . n 
D 1 191 VAL 191 191 191 VAL VAL D . n 
D 1 192 SER 192 192 192 SER SER D . n 
D 1 193 THR 193 193 193 THR THR D . n 
D 1 194 SER 194 194 194 SER SER D . n 
D 1 195 PRO 195 195 195 PRO PRO D . n 
D 1 196 TYR 196 196 196 TYR TYR D . n 
D 1 197 TYR 197 197 197 TYR TYR D . n 
D 1 198 HIS 198 198 198 HIS HIS D . n 
D 1 199 PRO 199 199 199 PRO PRO D . n 
D 1 200 LEU 200 200 200 LEU LEU D . n 
D 1 201 ILE 201 201 201 ILE ILE D . n 
D 1 202 PRO 202 202 202 PRO PRO D . n 
D 1 203 ILE 203 203 203 ILE ILE D . n 
D 1 204 LEU 204 204 204 LEU LEU D . n 
D 1 205 LEU 205 205 205 LEU LEU D . n 
D 1 206 ASN 206 206 206 ASN ASN D . n 
D 1 207 PRO 207 207 207 PRO PRO D . n 
D 1 208 ASN 208 208 208 ASN ASN D . n 
D 1 209 CYS 209 209 209 CYS CYS D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 TYR 211 211 211 TYR TYR D . n 
D 1 212 GLU 212 212 212 GLU GLU D . n 
D 1 213 THR 213 213 213 THR THR D . n 
D 1 214 THR 214 214 214 THR THR D . n 
D 1 215 PRO 215 215 215 PRO PRO D . n 
D 1 216 ASN 216 216 216 ASN ASN D . n 
D 1 217 VAL 217 217 217 VAL VAL D . n 
D 1 218 LYS 218 218 218 LYS LYS D . n 
D 1 219 ILE 219 219 219 ILE ILE D . n 
D 1 220 PRO 220 220 220 PRO PRO D . n 
D 1 221 ASP 221 221 221 ASP ASP D . n 
D 1 222 PHE 222 222 222 PHE PHE D . n 
D 1 223 ALA 223 223 223 ALA ALA D . n 
D 1 224 VAL 224 224 224 VAL VAL D . n 
D 1 225 SER 225 225 225 SER SER D . n 
D 1 226 PHE 226 226 226 PHE PHE D . n 
D 1 227 ARG 227 227 227 ARG ARG D . n 
D 1 228 GLU 228 228 228 GLU GLU D . n 
D 1 229 ASP 229 229 229 ASP ASP D . n 
D 1 230 ALA 230 230 230 ALA ALA D . n 
D 1 231 SER 231 231 231 SER SER D . n 
D 1 232 LYS 232 232 232 LYS LYS D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 VAL 234 234 234 VAL VAL D . n 
D 1 235 GLU 235 235 235 GLU GLU D . n 
D 1 236 LEU 236 236 236 LEU LEU D . n 
D 1 237 ALA 237 237 237 ALA ALA D . n 
D 1 238 LYS 238 238 238 LYS LYS D . n 
D 1 239 GLU 239 239 239 GLU GLU D . n 
D 1 240 LYS 240 240 240 LYS LYS D . n 
D 1 241 TYR 241 241 241 TYR TYR D . n 
D 1 242 PHE 242 242 242 PHE PHE D . n 
D 1 243 GLU 243 243 243 GLU GLU D . n 
D 1 244 ILE 244 244 244 ILE ILE D . n 
D 1 245 PHE 245 245 245 PHE PHE D . n 
D 1 246 GLY 246 246 246 GLY GLY D . n 
D 1 247 GLU 247 247 247 GLU GLU D . n 
D 1 248 HIS 248 248 248 HIS HIS D . n 
D 1 249 PRO 249 249 249 PRO PRO D . n 
D 1 250 VAL 250 250 250 VAL VAL D . n 
D 1 251 TYR 251 251 251 TYR TYR D . n 
D 1 252 MET 252 252 252 MET MET D . n 
D 1 253 TRP 253 253 253 TRP TRP D . n 
D 1 254 PRO 254 254 254 PRO PRO D . n 
D 1 255 PRO 255 255 255 PRO PRO D . n 
D 1 256 GLU 256 256 256 GLU GLU D . n 
D 1 257 ALA 257 257 257 ALA ALA D . n 
D 1 258 SER 258 258 258 SER SER D . n 
D 1 259 VAL 259 259 259 VAL VAL D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 ASN 261 261 261 ASN ASN D . n 
D 1 262 GLU 262 262 262 GLU GLU D . n 
D 1 263 ALA 263 263 263 ALA ALA D . n 
D 1 264 LEU 264 264 264 LEU LEU D . n 
D 1 265 GLU 265 265 265 GLU GLU D . n 
D 1 266 LEU 266 266 266 LEU LEU D . n 
D 1 267 TYR 267 267 267 TYR TYR D . n 
D 1 268 TYR 268 268 268 TYR TYR D . n 
D 1 269 GLU 269 269 269 GLU GLU D . n 
D 1 270 LYS 270 270 270 LYS LYS D . n 
D 1 271 GLY 271 271 271 GLY GLY D . n 
D 1 272 ILE 272 272 272 ILE ILE D . n 
D 1 273 ASN 273 273 273 ASN ASN D . n 
D 1 274 MET 274 274 274 MET MET D . n 
D 1 275 LEU 275 275 275 LEU LEU D . n 
D 1 276 ALA 276 276 276 ALA ALA D . n 
D 1 277 THR 277 277 277 THR THR D . n 
D 1 278 ASP 278 278 278 ASP ASP D . n 
D 1 279 GLU 279 279 279 GLU GLU D . n 
D 1 280 VAL 280 280 280 VAL VAL D . n 
D 1 281 ILE 281 281 281 ILE ILE D . n 
D 1 282 LEU 282 282 282 LEU LEU D . n 
D 1 283 LYS 283 283 283 LYS LYS D . n 
D 1 284 ASN 284 284 284 ASN ASN D . n 
D 1 285 SER 285 285 285 SER SER D . n 
D 1 286 VAL 286 286 286 VAL VAL D . n 
D 1 287 GLU 287 287 287 GLU GLU D . n 
D 1 288 ARG 288 288 288 ARG ARG D . n 
D 1 289 ALA 289 289 289 ALA ALA D . n 
D 1 290 SER 290 290 290 SER SER D . n 
D 1 291 PRO 291 291 291 PRO PRO D . n 
D 1 292 TYR 292 292 292 TYR TYR D . n 
D 1 293 LEU 293 293 293 LEU LEU D . n 
D 1 294 ARG 294 294 294 ARG ARG D . n 
D 1 295 TYR 295 295 295 TYR TYR D . n 
D 1 296 TYR 296 296 296 TYR TYR D . n 
D 1 297 PHE 297 297 297 PHE PHE D . n 
D 1 298 ARG 298 298 298 ARG ARG D . n 
D 1 299 GLU 299 299 299 GLU GLU D . n 
D 1 300 LEU 300 300 300 LEU LEU D . n 
D 1 301 ILE 301 301 301 ILE ILE D . n 
D 1 302 SER 302 302 302 SER SER D . n 
D 1 303 VAL 303 303 303 VAL VAL D . n 
D 1 304 PHE 304 304 304 PHE PHE D . n 
D 1 305 PHE 305 305 305 PHE PHE D . n 
D 1 306 ARG 306 306 306 ARG ARG D . n 
D 1 307 ASP 307 307 307 ASP ASP D . n 
D 1 308 LYS 308 308 308 LYS LYS D . n 
D 1 309 THR 309 309 309 THR THR D . n 
D 1 310 LEU 310 310 310 LEU LEU D . n 
D 1 311 SER 311 311 311 SER SER D . n 
D 1 312 ASP 312 312 312 ASP ASP D . n 
D 1 313 LEU 313 313 313 LEU LEU D . n 
D 1 314 ILE 314 314 314 ILE ILE D . n 
D 1 315 GLY 315 315 315 GLY GLY D . n 
D 1 316 PHE 316 316 316 PHE PHE D . n 
D 1 317 SER 317 317 317 SER SER D . n 
D 1 318 TYR 318 318 318 TYR TYR D . n 
D 1 319 HIS 319 319 319 HIS HIS D . n 
D 1 320 ALA 320 320 320 ALA ALA D . n 
D 1 321 TRP 321 321 321 TRP TRP D . n 
D 1 322 ASN 322 322 322 ASN ASN D . n 
D 1 323 ALA 323 323 323 ALA ALA D . n 
D 1 324 GLU 324 324 324 GLU GLU D . n 
D 1 325 ASP 325 325 325 ASP ASP D . n 
D 1 326 ALA 326 326 326 ALA ALA D . n 
D 1 327 VAL 327 327 327 VAL VAL D . n 
D 1 328 ARG 328 328 328 ARG ARG D . n 
D 1 329 ASP 329 329 329 ASP ASP D . n 
D 1 330 PHE 330 330 330 PHE PHE D . n 
D 1 331 ILE 331 331 331 ILE ILE D . n 
D 1 332 GLY 332 332 332 GLY GLY D . n 
D 1 333 ARG 333 333 333 ARG ARG D . n 
D 1 334 LEU 334 334 334 LEU LEU D . n 
D 1 335 LYS 335 335 335 LYS LYS D . n 
D 1 336 LYS 336 336 336 LYS LYS D . n 
D 1 337 ILE 337 337 337 ILE ILE D . n 
D 1 338 HIS 338 338 338 HIS HIS D . n 
D 1 339 GLU 339 339 339 GLU GLU D . n 
D 1 340 SER 340 340 340 SER SER D . n 
D 1 341 VAL 341 341 341 VAL VAL D . n 
D 1 342 ASP 342 342 342 ASP ASP D . n 
D 1 343 PHE 343 343 343 PHE PHE D . n 
D 1 344 GLN 344 344 344 GLN GLN D . n 
D 1 345 PRO 345 345 345 PRO PRO D . n 
D 1 346 VAL 346 346 346 VAL VAL D . n 
D 1 347 VAL 347 347 347 VAL VAL D . n 
D 1 348 PHE 348 348 348 PHE PHE D . n 
D 1 349 VAL 349 349 349 VAL VAL D . n 
D 1 350 VAL 350 350 350 VAL VAL D . n 
D 1 351 LEU 351 351 351 LEU LEU D . n 
D 1 352 ASP 352 352 352 ASP ASP D . n 
D 1 353 GLY 353 353 353 GLY GLY D . n 
D 1 354 GLU 354 354 354 GLU GLU D . n 
D 1 355 ASN 355 355 355 ASN ASN D . n 
D 1 356 CYS 356 356 356 CYS CYS D . n 
D 1 357 TRP 357 357 357 TRP TRP D . n 
D 1 358 GLU 358 358 358 GLU GLU D . n 
D 1 359 TYR 359 359 359 TYR TYR D . n 
D 1 360 TYR 360 360 360 TYR TYR D . n 
D 1 361 GLU 361 361 361 GLU GLU D . n 
D 1 362 GLU 362 362 362 GLU GLU D . n 
D 1 363 ASN 363 363 363 ASN ASN D . n 
D 1 364 GLY 364 364 364 GLY GLY D . n 
D 1 365 ILE 365 365 365 ILE ILE D . n 
D 1 366 PRO 366 366 366 PRO PRO D . n 
D 1 367 PHE 367 367 367 PHE PHE D . n 
D 1 368 LEU 368 368 368 LEU LEU D . n 
D 1 369 GLU 369 369 369 GLU GLU D . n 
D 1 370 LYS 370 370 370 LYS LYS D . n 
D 1 371 LEU 371 371 371 LEU LEU D . n 
D 1 372 TYR 372 372 372 TYR TYR D . n 
D 1 373 SER 373 373 373 SER SER D . n 
D 1 374 THR 374 374 374 THR THR D . n 
D 1 375 LEU 375 375 375 LEU LEU D . n 
D 1 376 GLU 376 376 376 GLU GLU D . n 
D 1 377 LYS 377 377 377 LYS LYS D . n 
D 1 378 GLU 378 378 378 GLU GLU D . n 
D 1 379 GLU 379 379 379 GLU GLU D . n 
D 1 380 TRP 380 380 380 TRP TRP D . n 
D 1 381 ILE 381 381 381 ILE ILE D . n 
D 1 382 GLU 382 382 382 GLU GLU D . n 
D 1 383 THR 383 383 383 THR THR D . n 
D 1 384 LEU 384 384 384 LEU LEU D . n 
D 1 385 THR 385 385 385 THR THR D . n 
D 1 386 LEU 386 386 386 LEU LEU D . n 
D 1 387 GLU 387 387 387 GLU GLU D . n 
D 1 388 GLU 388 388 388 GLU GLU D . n 
D 1 389 ALA 389 389 389 ALA ALA D . n 
D 1 390 MET 390 390 390 MET MET D . n 
D 1 391 ARG 391 391 391 ARG ARG D . n 
D 1 392 LYS 392 392 392 LYS LYS D . n 
D 1 393 GLU 393 393 393 GLU GLU D . n 
D 1 394 ASP 394 394 394 ASP ASP D . n 
D 1 395 VAL 395 395 395 VAL VAL D . n 
D 1 396 LYS 396 396 396 LYS LYS D . n 
D 1 397 THR 397 397 397 THR THR D . n 
D 1 398 GLU 398 398 398 GLU GLU D . n 
D 1 399 VAL 399 399 399 VAL VAL D . n 
D 1 400 ILE 400 400 400 ILE ILE D . n 
D 1 401 GLU 401 401 401 GLU GLU D . n 
D 1 402 SER 402 402 402 SER SER D . n 
D 1 403 VAL 403 403 403 VAL VAL D . n 
D 1 404 LYS 404 404 404 LYS LYS D . n 
D 1 405 ALA 405 405 405 ALA ALA D . n 
D 1 406 GLY 406 406 406 GLY GLY D . n 
D 1 407 THR 407 407 407 THR THR D . n 
D 1 408 TRP 408 408 408 TRP TRP D . n 
D 1 409 PHE 409 409 409 PHE PHE D . n 
D 1 410 ASP 410 410 410 ASP ASP D . n 
D 1 411 GLY 411 411 411 GLY GLY D . n 
D 1 412 ASN 412 412 412 ASN ASN D . n 
D 1 413 PHE 413 413 413 PHE PHE D . n 
D 1 414 LEU 414 414 414 LEU LEU D . n 
D 1 415 LYS 415 415 415 LYS LYS D . n 
D 1 416 TRP 416 416 416 TRP TRP D . n 
D 1 417 ILE 417 417 417 ILE ILE D . n 
D 1 418 GLY 418 418 418 GLY GLY D . n 
D 1 419 ASN 419 419 419 ASN ASN D . n 
D 1 420 LYS 420 420 420 LYS LYS D . n 
D 1 421 GLU 421 421 421 GLU GLU D . n 
D 1 422 LYS 422 422 422 LYS LYS D . n 
D 1 423 ASN 423 423 423 ASN ASN D . n 
D 1 424 GLU 424 424 424 GLU GLU D . n 
D 1 425 TYR 425 425 425 TYR TYR D . n 
D 1 426 TRP 426 426 426 TRP TRP D . n 
D 1 427 LYS 427 427 427 LYS LYS D . n 
D 1 428 ILE 428 428 428 ILE ILE D . n 
D 1 429 LEU 429 429 429 LEU LEU D . n 
D 1 430 ILE 430 430 430 ILE ILE D . n 
D 1 431 GLU 431 431 431 GLU GLU D . n 
D 1 432 ALA 432 432 432 ALA ALA D . n 
D 1 433 LYS 433 433 433 LYS LYS D . n 
D 1 434 LYS 434 434 434 LYS LYS D . n 
D 1 435 LYS 435 435 435 LYS LYS D . n 
D 1 436 ALA 436 436 436 ALA ALA D . n 
D 1 437 LYS 437 437 437 LYS LYS D . n 
D 1 438 ASN 438 438 438 ASN ASN D . n 
D 1 439 ASP 439 439 439 ASP ASP D . n 
D 1 440 TYR 440 440 440 TYR TYR D . n 
D 1 441 ILE 441 441 441 ILE ILE D . n 
D 1 442 LEU 442 442 442 LEU LEU D . n 
D 1 443 VAL 443 443 443 VAL VAL D . n 
D 1 444 ALA 444 444 444 ALA ALA D . n 
D 1 445 GLU 445 445 445 GLU GLU D . n 
D 1 446 GLY 446 446 446 GLY GLY D . n 
D 1 447 SER 447 447 447 SER SER D . n 
D 1 448 ASP 448 448 448 ASP ASP D . n 
D 1 449 TRP 449 449 449 TRP TRP D . n 
D 1 450 PHE 450 450 450 PHE PHE D . n 
D 1 451 TRP 451 451 451 TRP TRP D . n 
D 1 452 TRP 452 452 452 TRP TRP D . n 
D 1 453 GLN 453 453 453 GLN GLN D . n 
D 1 454 GLY 454 454 454 GLY GLY D . n 
D 1 455 GLU 455 455 455 GLU GLU D . n 
D 1 456 GLU 456 456 456 GLU GLU D . n 
D 1 457 LYS 457 457 457 LYS LYS D . n 
D 1 458 ALA 458 458 458 ALA ALA D . n 
D 1 459 PRO 459 459 459 PRO PRO D . n 
D 1 460 PHE 460 460 460 PHE PHE D . n 
D 1 461 VAL 461 461 461 VAL VAL D . n 
D 1 462 GLU 462 462 462 GLU GLU D . n 
D 1 463 VAL 463 463 463 VAL VAL D . n 
D 1 464 PHE 464 464 464 PHE PHE D . n 
D 1 465 ASP 465 465 465 ASP ASP D . n 
D 1 466 LYS 466 466 466 LYS LYS D . n 
D 1 467 LEU 467 467 467 LEU LEU D . n 
D 1 468 PHE 468 468 468 PHE PHE D . n 
D 1 469 ARG 469 469 469 ARG ARG D . n 
D 1 470 SER 470 470 470 SER SER D . n 
D 1 471 PHE 471 471 471 PHE PHE D . n 
D 1 472 VAL 472 472 472 VAL VAL D . n 
D 1 473 ARG 473 473 473 ARG ARG D . n 
D 1 474 ARG 474 474 474 ARG ARG D . n 
D 1 475 ALA 475 475 475 ALA ALA D . n 
D 1 476 GLN 476 476 476 GLN GLN D . n 
D 1 477 GLU 477 477 477 GLU GLU D . n 
D 1 478 LEU 478 478 478 LEU LEU D . n 
D 1 479 GLU 479 479 479 GLU GLU D . n 
D 1 480 HIS 480 480 480 HIS HIS D . n 
D 1 481 HIS 481 481 481 HIS HIS D . n 
D 1 482 HIS 482 482 482 HIS HIS D . n 
D 1 483 HIS 483 483 483 HIS HIS D . n 
D 1 484 HIS 484 484 ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 HOH 1  501 85  HOH HOH A . 
E 2 HOH 2  502 31  HOH HOH A . 
E 2 HOH 3  503 54  HOH HOH A . 
E 2 HOH 4  504 1   HOH HOH A . 
E 2 HOH 5  505 122 HOH HOH A . 
E 2 HOH 6  506 133 HOH HOH A . 
E 2 HOH 7  507 6   HOH HOH A . 
E 2 HOH 8  508 46  HOH HOH A . 
E 2 HOH 9  509 78  HOH HOH A . 
E 2 HOH 10 510 55  HOH HOH A . 
E 2 HOH 11 511 21  HOH HOH A . 
E 2 HOH 12 512 126 HOH HOH A . 
E 2 HOH 13 513 4   HOH HOH A . 
E 2 HOH 14 514 35  HOH HOH A . 
E 2 HOH 15 515 102 HOH HOH A . 
E 2 HOH 16 516 61  HOH HOH A . 
E 2 HOH 17 517 114 HOH HOH A . 
E 2 HOH 18 518 76  HOH HOH A . 
E 2 HOH 19 519 89  HOH HOH A . 
E 2 HOH 20 520 159 HOH HOH A . 
E 2 HOH 21 521 28  HOH HOH A . 
E 2 HOH 22 522 75  HOH HOH A . 
E 2 HOH 23 523 7   HOH HOH A . 
E 2 HOH 24 524 70  HOH HOH A . 
E 2 HOH 25 525 157 HOH HOH A . 
E 2 HOH 26 526 99  HOH HOH A . 
E 2 HOH 27 527 44  HOH HOH A . 
E 2 HOH 28 528 9   HOH HOH A . 
E 2 HOH 29 529 32  HOH HOH A . 
E 2 HOH 30 530 71  HOH HOH A . 
E 2 HOH 31 531 23  HOH HOH A . 
E 2 HOH 32 532 5   HOH HOH A . 
E 2 HOH 33 533 52  HOH HOH A . 
E 2 HOH 34 534 19  HOH HOH A . 
E 2 HOH 35 535 120 HOH HOH A . 
E 2 HOH 36 536 40  HOH HOH A . 
E 2 HOH 37 537 36  HOH HOH A . 
E 2 HOH 38 538 51  HOH HOH A . 
E 2 HOH 39 539 62  HOH HOH A . 
E 2 HOH 40 540 74  HOH HOH A . 
E 2 HOH 41 541 92  HOH HOH A . 
E 2 HOH 42 542 26  HOH HOH A . 
E 2 HOH 43 543 160 HOH HOH A . 
E 2 HOH 44 544 2   HOH HOH A . 
E 2 HOH 45 545 156 HOH HOH A . 
E 2 HOH 46 546 115 HOH HOH A . 
E 2 HOH 47 547 117 HOH HOH A . 
E 2 HOH 48 548 150 HOH HOH A . 
E 2 HOH 49 549 131 HOH HOH A . 
E 2 HOH 50 550 11  HOH HOH A . 
E 2 HOH 51 551 124 HOH HOH A . 
E 2 HOH 52 552 98  HOH HOH A . 
E 2 HOH 53 553 18  HOH HOH A . 
E 2 HOH 54 554 43  HOH HOH A . 
E 2 HOH 55 555 10  HOH HOH A . 
E 2 HOH 56 556 97  HOH HOH A . 
E 2 HOH 57 557 90  HOH HOH A . 
E 2 HOH 58 558 111 HOH HOH A . 
E 2 HOH 59 559 24  HOH HOH A . 
E 2 HOH 60 560 20  HOH HOH A . 
E 2 HOH 61 561 149 HOH HOH A . 
E 2 HOH 62 562 135 HOH HOH A . 
E 2 HOH 63 563 101 HOH HOH A . 
E 2 HOH 64 564 147 HOH HOH A . 
E 2 HOH 65 565 148 HOH HOH A . 
F 2 HOH 1  501 65  HOH HOH B . 
F 2 HOH 2  502 56  HOH HOH B . 
F 2 HOH 3  503 93  HOH HOH B . 
F 2 HOH 4  504 63  HOH HOH B . 
F 2 HOH 5  505 141 HOH HOH B . 
F 2 HOH 6  506 45  HOH HOH B . 
F 2 HOH 7  507 3   HOH HOH B . 
F 2 HOH 8  508 16  HOH HOH B . 
F 2 HOH 9  509 12  HOH HOH B . 
F 2 HOH 10 510 14  HOH HOH B . 
F 2 HOH 11 511 41  HOH HOH B . 
F 2 HOH 12 512 87  HOH HOH B . 
F 2 HOH 13 513 38  HOH HOH B . 
F 2 HOH 14 514 138 HOH HOH B . 
F 2 HOH 15 515 144 HOH HOH B . 
F 2 HOH 16 516 91  HOH HOH B . 
F 2 HOH 17 517 50  HOH HOH B . 
F 2 HOH 18 518 106 HOH HOH B . 
F 2 HOH 19 519 48  HOH HOH B . 
F 2 HOH 20 520 68  HOH HOH B . 
F 2 HOH 21 521 27  HOH HOH B . 
F 2 HOH 22 522 30  HOH HOH B . 
F 2 HOH 23 523 110 HOH HOH B . 
F 2 HOH 24 524 94  HOH HOH B . 
F 2 HOH 25 525 53  HOH HOH B . 
F 2 HOH 26 526 108 HOH HOH B . 
F 2 HOH 27 527 58  HOH HOH B . 
F 2 HOH 28 528 8   HOH HOH B . 
F 2 HOH 29 529 137 HOH HOH B . 
F 2 HOH 30 530 129 HOH HOH B . 
F 2 HOH 31 531 81  HOH HOH B . 
F 2 HOH 32 532 121 HOH HOH B . 
F 2 HOH 33 533 96  HOH HOH B . 
F 2 HOH 34 534 139 HOH HOH B . 
F 2 HOH 35 535 15  HOH HOH B . 
F 2 HOH 36 536 17  HOH HOH B . 
F 2 HOH 37 537 152 HOH HOH B . 
F 2 HOH 38 538 100 HOH HOH B . 
F 2 HOH 39 539 79  HOH HOH B . 
F 2 HOH 40 540 125 HOH HOH B . 
F 2 HOH 41 541 104 HOH HOH B . 
G 2 HOH 1  501 59  HOH HOH C . 
G 2 HOH 2  502 142 HOH HOH C . 
G 2 HOH 3  503 107 HOH HOH C . 
G 2 HOH 4  504 158 HOH HOH C . 
G 2 HOH 5  505 132 HOH HOH C . 
G 2 HOH 6  506 123 HOH HOH C . 
G 2 HOH 7  507 151 HOH HOH C . 
G 2 HOH 8  508 95  HOH HOH C . 
G 2 HOH 9  509 146 HOH HOH C . 
G 2 HOH 10 510 47  HOH HOH C . 
G 2 HOH 11 511 37  HOH HOH C . 
G 2 HOH 12 512 134 HOH HOH C . 
G 2 HOH 13 513 86  HOH HOH C . 
G 2 HOH 14 514 84  HOH HOH C . 
G 2 HOH 15 515 77  HOH HOH C . 
G 2 HOH 16 516 34  HOH HOH C . 
G 2 HOH 17 517 80  HOH HOH C . 
G 2 HOH 18 518 13  HOH HOH C . 
G 2 HOH 19 519 128 HOH HOH C . 
G 2 HOH 20 520 69  HOH HOH C . 
G 2 HOH 21 521 153 HOH HOH C . 
G 2 HOH 22 522 88  HOH HOH C . 
G 2 HOH 23 523 64  HOH HOH C . 
G 2 HOH 24 524 154 HOH HOH C . 
G 2 HOH 25 525 103 HOH HOH C . 
G 2 HOH 26 526 116 HOH HOH C . 
G 2 HOH 27 527 39  HOH HOH C . 
G 2 HOH 28 528 29  HOH HOH C . 
G 2 HOH 29 529 130 HOH HOH C . 
G 2 HOH 30 530 82  HOH HOH C . 
G 2 HOH 31 531 143 HOH HOH C . 
G 2 HOH 32 532 155 HOH HOH C . 
H 2 HOH 1  501 66  HOH HOH D . 
H 2 HOH 2  502 49  HOH HOH D . 
H 2 HOH 3  503 67  HOH HOH D . 
H 2 HOH 4  504 22  HOH HOH D . 
H 2 HOH 5  505 105 HOH HOH D . 
H 2 HOH 6  506 60  HOH HOH D . 
H 2 HOH 7  507 57  HOH HOH D . 
H 2 HOH 8  508 145 HOH HOH D . 
H 2 HOH 9  509 140 HOH HOH D . 
H 2 HOH 10 510 112 HOH HOH D . 
H 2 HOH 11 511 73  HOH HOH D . 
H 2 HOH 12 512 119 HOH HOH D . 
H 2 HOH 13 513 109 HOH HOH D . 
H 2 HOH 14 514 136 HOH HOH D . 
H 2 HOH 15 515 33  HOH HOH D . 
H 2 HOH 16 516 118 HOH HOH D . 
H 2 HOH 17 517 42  HOH HOH D . 
H 2 HOH 18 518 113 HOH HOH D . 
H 2 HOH 19 519 72  HOH HOH D . 
H 2 HOH 20 520 127 HOH HOH D . 
H 2 HOH 21 521 83  HOH HOH D . 
H 2 HOH 22 522 25  HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.19.2_4158: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   110.31 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JLQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.658 
_cell.length_a_esd                 ? 
_cell.length_b                     166.730 
_cell.length_b_esd                 ? 
_cell.length_c                     99.514 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JLQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JLQ 
_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             2.43 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.36 
_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    '40% MPD, 5% PEG2W, 0.1M MES 6.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-05-23 
_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   0.97915 
_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        0.97915 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JLQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.54 
_reflns.d_resolution_low                               99.330 
_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                                     45539 
_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                           88.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          3.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.905 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.54 
_reflns_shell.d_res_low                                     2.814 
_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                             2275 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.792 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.376 
_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                                  1.47 
_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                                 9JLQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.54 
_refine.ls_d_res_low                             93.33 
_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                     45452 
_refine.ls_number_reflns_R_free                  2259 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    62.26 
_refine.ls_percent_reflns_R_free                 4.97 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2002 
_refine.ls_R_factor_R_free                       0.2426 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1979 
_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                          1.36 
_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                 24.12 
_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.pdbx_number_atoms_protein        16333 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             160 
_refine_hist.number_atoms_total               16493 
_refine_hist.d_res_high                       2.54 
_refine_hist.d_res_low                        93.33 
# 
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' ? 0.003 ? 16794 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.610 ? 22715 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.161 ? 2118  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.042 ? 2355  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 2877  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.54 2.60  . . 2   44   1.00  . . . . 0.2111 . . . . . . . . . . . 0.1036 
'X-RAY DIFFRACTION' 2.60 2.66  . . 17  280  7.00  . . . . 0.2033 . . . . . . . . . . . 0.3374 
'X-RAY DIFFRACTION' 2.66 2.72  . . 36  652  15.00 . . . . 0.2725 . . . . . . . . . . . 0.2832 
'X-RAY DIFFRACTION' 2.72 2.80  . . 54  937  22.00 . . . . 0.2719 . . . . . . . . . . . 0.3250 
'X-RAY DIFFRACTION' 2.80 2.88  . . 51  1197 28.00 . . . . 0.2459 . . . . . . . . . . . 0.3101 
'X-RAY DIFFRACTION' 2.88 2.97  . . 88  1608 38.00 . . . . 0.2576 . . . . . . . . . . . 0.2962 
'X-RAY DIFFRACTION' 2.97 3.08  . . 127 2335 54.00 . . . . 0.2457 . . . . . . . . . . . 0.2854 
'X-RAY DIFFRACTION' 3.08 3.20  . . 127 3005 69.00 . . . . 0.2334 . . . . . . . . . . . 0.2979 
'X-RAY DIFFRACTION' 3.20 3.35  . . 174 3390 78.00 . . . . 0.2383 . . . . . . . . . . . 0.2775 
'X-RAY DIFFRACTION' 3.35 3.52  . . 208 3998 92.00 . . . . 0.2249 . . . . . . . . . . . 0.2737 
'X-RAY DIFFRACTION' 3.52 3.74  . . 244 4297 99.00 . . . . 0.1958 . . . . . . . . . . . 0.2532 
'X-RAY DIFFRACTION' 3.74 4.03  . . 222 4320 99.00 . . . . 0.1872 . . . . . . . . . . . 0.2624 
'X-RAY DIFFRACTION' 4.03 4.44  . . 230 4250 99.00 . . . . 0.1669 . . . . . . . . . . . 0.2166 
'X-RAY DIFFRACTION' 4.44 5.08  . . 198 4278 98.00 . . . . 0.1578 . . . . . . . . . . . 0.2011 
'X-RAY DIFFRACTION' 5.08 6.40  . . 249 4266 99.00 . . . . 0.1914 . . . . . . . . . . . 0.2151 
'X-RAY DIFFRACTION' 6.40 93.33 . . 232 4336 98.00 . . . . 0.1791 . . . . . . . . . . . 0.1920 
# 
_struct.entry_id                     9JLQ 
_struct.title                        'Crystal structure of GH57 family amylopullulanase from Aquifex aeolicus wild type apo' 
_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        9JLQ 
_struct_keywords.text            'GH57 family, amylopullulanase, Aquifex aeolicus, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 2 ? 
# 
_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 9JLQ A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9JLQ B 1 ? 477 ? O66934 1 ? 477 ? 1 477 
3 1 9JLQ C 1 ? 477 ? O66934 1 ? 477 ? 1 477 
4 1 9JLQ D 1 ? 477 ? O66934 1 ? 477 ? 1 477 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9JLQ LEU A 478 ? UNP O66934 ? ? 'expression tag' 478 1  
1 9JLQ GLU A 479 ? UNP O66934 ? ? 'expression tag' 479 2  
1 9JLQ HIS A 480 ? UNP O66934 ? ? 'expression tag' 480 3  
1 9JLQ HIS A 481 ? UNP O66934 ? ? 'expression tag' 481 4  
1 9JLQ HIS A 482 ? UNP O66934 ? ? 'expression tag' 482 5  
1 9JLQ HIS A 483 ? UNP O66934 ? ? 'expression tag' 483 6  
1 9JLQ HIS A 484 ? UNP O66934 ? ? 'expression tag' 484 7  
2 9JLQ LEU B 478 ? UNP O66934 ? ? 'expression tag' 478 8  
2 9JLQ GLU B 479 ? UNP O66934 ? ? 'expression tag' 479 9  
2 9JLQ HIS B 480 ? UNP O66934 ? ? 'expression tag' 480 10 
2 9JLQ HIS B 481 ? UNP O66934 ? ? 'expression tag' 481 11 
2 9JLQ HIS B 482 ? UNP O66934 ? ? 'expression tag' 482 12 
2 9JLQ HIS B 483 ? UNP O66934 ? ? 'expression tag' 483 13 
2 9JLQ HIS B 484 ? UNP O66934 ? ? 'expression tag' 484 14 
3 9JLQ LEU C 478 ? UNP O66934 ? ? 'expression tag' 478 15 
3 9JLQ GLU C 479 ? UNP O66934 ? ? 'expression tag' 479 16 
3 9JLQ HIS C 480 ? UNP O66934 ? ? 'expression tag' 480 17 
3 9JLQ HIS C 481 ? UNP O66934 ? ? 'expression tag' 481 18 
3 9JLQ HIS C 482 ? UNP O66934 ? ? 'expression tag' 482 19 
3 9JLQ HIS C 483 ? UNP O66934 ? ? 'expression tag' 483 20 
3 9JLQ HIS C 484 ? UNP O66934 ? ? 'expression tag' 484 21 
4 9JLQ LEU D 478 ? UNP O66934 ? ? 'expression tag' 478 22 
4 9JLQ GLU D 479 ? UNP O66934 ? ? 'expression tag' 479 23 
4 9JLQ HIS D 480 ? UNP O66934 ? ? 'expression tag' 480 24 
4 9JLQ HIS D 481 ? UNP O66934 ? ? 'expression tag' 481 25 
4 9JLQ HIS D 482 ? UNP O66934 ? ? 'expression tag' 482 26 
4 9JLQ HIS D 483 ? UNP O66934 ? ? 'expression tag' 483 27 
4 9JLQ HIS D 484 ? UNP O66934 ? ? 'expression tag' 484 28 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E 
2 1 B,F 
3 1 C,G 
4 1 D,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  ? PHE A 48  ? TYR A 39  PHE A 48  1 ? 10 
HELX_P HELX_P3   AA3 THR A 57  ? GLN A 69  ? THR A 57  GLN A 69  1 ? 13 
HELX_P HELX_P4   AA4 VAL A 75  ? LYS A 82  ? VAL A 75  LYS A 82  1 ? 8  
HELX_P HELX_P5   AA5 ASP A 83  ? LEU A 87  ? ASP A 83  LEU A 87  5 ? 5  
HELX_P HELX_P6   AA6 GLU A 88  ? ASN A 102 ? GLU A 88  ASN A 102 1 ? 15 
HELX_P HELX_P7   AA7 LYS A 105 ? ARG A 109 ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P8   AA8 PHE A 110 ? LYS A 119 ? PHE A 110 LYS A 119 1 ? 10 
HELX_P HELX_P9   AA9 ASN A 123 ? ALA A 137 ? ASN A 123 ALA A 137 1 ? 15 
HELX_P HELX_P10  AB1 GLY A 140 ? LEU A 147 ? GLY A 140 LEU A 147 1 ? 8  
HELX_P HELX_P11  AB2 LEU A 147 ? GLY A 154 ? LEU A 147 GLY A 154 1 ? 8  
HELX_P HELX_P12  AB3 THR A 158 ? GLU A 186 ? THR A 158 GLU A 186 1 ? 29 
HELX_P HELX_P13  AB4 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P14  AB5 PRO A 207 ? GLU A 212 ? PRO A 207 GLU A 212 5 ? 6  
HELX_P HELX_P15  AB6 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P16  AB7 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P17  AB8 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P18  AB9 GLU A 279 ? VAL A 286 ? GLU A 279 VAL A 286 1 ? 8  
HELX_P HELX_P19  AC1 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P20  AC2 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P21  AC3 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P22  AC4 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P23  AC5 GLY A 364 ? GLU A 378 ? GLY A 364 GLU A 378 1 ? 15 
HELX_P HELX_P24  AC6 THR A 385 ? LYS A 392 ? THR A 385 LYS A 392 1 ? 8  
HELX_P HELX_P25  AC7 ASN A 419 ? LYS A 435 ? ASN A 419 LYS A 435 1 ? 17 
HELX_P HELX_P26  AC8 ASP A 439 ? ALA A 444 ? ASP A 439 ALA A 444 1 ? 6  
HELX_P HELX_P27  AC9 GLY A 446 ? TRP A 452 ? GLY A 446 TRP A 452 1 ? 7  
HELX_P HELX_P28  AD1 PHE A 460 ? GLN A 476 ? PHE A 460 GLN A 476 1 ? 17 
HELX_P HELX_P29  AD2 PRO B 28  ? VAL B 35  ? PRO B 28  VAL B 35  1 ? 8  
HELX_P HELX_P30  AD3 TYR B 39  ? TYR B 44  ? TYR B 39  TYR B 44  1 ? 6  
HELX_P HELX_P31  AD4 LEU B 45  ? ASP B 47  ? LEU B 45  ASP B 47  5 ? 3  
HELX_P HELX_P32  AD5 THR B 57  ? GLY B 70  ? THR B 57  GLY B 70  1 ? 14 
HELX_P HELX_P33  AD6 VAL B 75  ? LYS B 82  ? VAL B 75  LYS B 82  1 ? 8  
HELX_P HELX_P34  AD7 ASP B 83  ? LEU B 87  ? ASP B 83  LEU B 87  5 ? 5  
HELX_P HELX_P35  AD8 GLU B 88  ? ASN B 102 ? GLU B 88  ASN B 102 1 ? 15 
HELX_P HELX_P36  AD9 TYR B 103 ? ARG B 109 ? TYR B 103 ARG B 109 5 ? 7  
HELX_P HELX_P37  AE1 PHE B 110 ? LYS B 119 ? PHE B 110 LYS B 119 1 ? 10 
HELX_P HELX_P38  AE2 ASN B 123 ? ALA B 137 ? ASN B 123 ALA B 137 1 ? 15 
HELX_P HELX_P39  AE3 THR B 142 ? LEU B 147 ? THR B 142 LEU B 147 1 ? 6  
HELX_P HELX_P40  AE4 LEU B 147 ? GLY B 154 ? LEU B 147 GLY B 154 1 ? 8  
HELX_P HELX_P41  AE5 THR B 158 ? LYS B 175 ? THR B 158 LYS B 175 1 ? 18 
HELX_P HELX_P42  AE6 LYS B 175 ? GLU B 186 ? LYS B 175 GLU B 186 1 ? 12 
HELX_P HELX_P43  AE7 LEU B 200 ? ASN B 206 ? LEU B 200 ASN B 206 1 ? 7  
HELX_P HELX_P44  AE8 PRO B 207 ? THR B 213 ? PRO B 207 THR B 213 5 ? 7  
HELX_P HELX_P45  AE9 PHE B 226 ? GLY B 246 ? PHE B 226 GLY B 246 1 ? 21 
HELX_P HELX_P46  AF1 PRO B 254 ? SER B 258 ? PRO B 254 SER B 258 5 ? 5  
HELX_P HELX_P47  AF2 SER B 260 ? LYS B 270 ? SER B 260 LYS B 270 1 ? 11 
HELX_P HELX_P48  AF3 GLU B 279 ? VAL B 286 ? GLU B 279 VAL B 286 1 ? 8  
HELX_P HELX_P49  AF4 ASP B 307 ? SER B 317 ? ASP B 307 SER B 317 1 ? 11 
HELX_P HELX_P50  AF5 TYR B 318 ? TRP B 321 ? TYR B 318 TRP B 321 5 ? 4  
HELX_P HELX_P51  AF6 ASN B 322 ? GLU B 339 ? ASN B 322 GLU B 339 1 ? 18 
HELX_P HELX_P52  AF7 TYR B 360 ? ASN B 363 ? TYR B 360 ASN B 363 5 ? 4  
HELX_P HELX_P53  AF8 GLY B 364 ? GLU B 378 ? GLY B 364 GLU B 378 1 ? 15 
HELX_P HELX_P54  AF9 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P55  AG1 ASN B 419 ? LYS B 435 ? ASN B 419 LYS B 435 1 ? 17 
HELX_P HELX_P56  AG2 ASP B 439 ? ALA B 444 ? ASP B 439 ALA B 444 1 ? 6  
HELX_P HELX_P57  AG3 GLU B 445 ? PHE B 450 ? GLU B 445 PHE B 450 5 ? 6  
HELX_P HELX_P58  AG4 PHE B 460 ? GLN B 476 ? PHE B 460 GLN B 476 1 ? 17 
HELX_P HELX_P59  AG5 PRO C 28  ? ASP C 37  ? PRO C 28  ASP C 37  1 ? 10 
HELX_P HELX_P60  AG6 TYR C 39  ? TYR C 44  ? TYR C 39  TYR C 44  1 ? 6  
HELX_P HELX_P61  AG7 LEU C 45  ? ASP C 47  ? LEU C 45  ASP C 47  5 ? 3  
HELX_P HELX_P62  AG8 THR C 57  ? GLN C 69  ? THR C 57  GLN C 69  1 ? 13 
HELX_P HELX_P63  AG9 LEU C 77  ? LYS C 82  ? LEU C 77  LYS C 82  1 ? 6  
HELX_P HELX_P64  AH1 GLU C 88  ? ASN C 102 ? GLU C 88  ASN C 102 1 ? 15 
HELX_P HELX_P65  AH2 LYS C 105 ? ARG C 109 ? LYS C 105 ARG C 109 5 ? 5  
HELX_P HELX_P66  AH3 PHE C 110 ? MET C 117 ? PHE C 110 MET C 117 1 ? 8  
HELX_P HELX_P67  AH4 ASN C 123 ? TRP C 138 ? ASN C 123 TRP C 138 1 ? 16 
HELX_P HELX_P68  AH5 GLY C 140 ? LYS C 145 ? GLY C 140 LYS C 145 1 ? 6  
HELX_P HELX_P69  AH6 LEU C 147 ? GLY C 154 ? LEU C 147 GLY C 154 1 ? 8  
HELX_P HELX_P70  AH7 THR C 158 ? LYS C 175 ? THR C 158 LYS C 175 1 ? 18 
HELX_P HELX_P71  AH8 LYS C 175 ? GLU C 186 ? LYS C 175 GLU C 186 1 ? 12 
HELX_P HELX_P72  AH9 LEU C 200 ? ASN C 206 ? LEU C 200 ASN C 206 1 ? 7  
HELX_P HELX_P73  AI1 PRO C 207 ? THR C 213 ? PRO C 207 THR C 213 5 ? 7  
HELX_P HELX_P74  AI2 PHE C 226 ? GLY C 246 ? PHE C 226 GLY C 246 1 ? 21 
HELX_P HELX_P75  AI3 PRO C 254 ? SER C 258 ? PRO C 254 SER C 258 5 ? 5  
HELX_P HELX_P76  AI4 SER C 260 ? LYS C 270 ? SER C 260 LYS C 270 1 ? 11 
HELX_P HELX_P77  AI5 GLU C 279 ? ASN C 284 ? GLU C 279 ASN C 284 1 ? 6  
HELX_P HELX_P78  AI6 ASP C 307 ? SER C 317 ? ASP C 307 SER C 317 1 ? 11 
HELX_P HELX_P79  AI7 TYR C 318 ? TRP C 321 ? TYR C 318 TRP C 321 5 ? 4  
HELX_P HELX_P80  AI8 ASN C 322 ? GLU C 339 ? ASN C 322 GLU C 339 1 ? 18 
HELX_P HELX_P81  AI9 TYR C 360 ? ASN C 363 ? TYR C 360 ASN C 363 5 ? 4  
HELX_P HELX_P82  AJ1 GLY C 364 ? GLU C 378 ? GLY C 364 GLU C 378 1 ? 15 
HELX_P HELX_P83  AJ2 THR C 385 ? LYS C 392 ? THR C 385 LYS C 392 1 ? 8  
HELX_P HELX_P84  AJ3 ASN C 419 ? LYS C 435 ? ASN C 419 LYS C 435 1 ? 17 
HELX_P HELX_P85  AJ4 ASP C 439 ? ALA C 444 ? ASP C 439 ALA C 444 1 ? 6  
HELX_P HELX_P86  AJ5 GLY C 446 ? TRP C 452 ? GLY C 446 TRP C 452 1 ? 7  
HELX_P HELX_P87  AJ6 PHE C 460 ? GLN C 476 ? PHE C 460 GLN C 476 1 ? 17 
HELX_P HELX_P88  AJ7 PRO D 28  ? VAL D 35  ? PRO D 28  VAL D 35  1 ? 8  
HELX_P HELX_P89  AJ8 TYR D 39  ? PHE D 48  ? TYR D 39  PHE D 48  1 ? 10 
HELX_P HELX_P90  AJ9 THR D 57  ? GLN D 69  ? THR D 57  GLN D 69  1 ? 13 
HELX_P HELX_P91  AK1 VAL D 75  ? LYS D 82  ? VAL D 75  LYS D 82  1 ? 8  
HELX_P HELX_P92  AK2 GLU D 88  ? ASN D 102 ? GLU D 88  ASN D 102 1 ? 15 
HELX_P HELX_P93  AK3 ILE D 113 ? ASN D 118 ? ILE D 113 ASN D 118 1 ? 6  
HELX_P HELX_P94  AK4 ASN D 123 ? TRP D 138 ? ASN D 123 TRP D 138 1 ? 16 
HELX_P HELX_P95  AK5 GLY D 140 ? ARG D 144 ? GLY D 140 ARG D 144 5 ? 5  
HELX_P HELX_P96  AK6 LEU D 147 ? GLY D 154 ? LEU D 147 GLY D 154 1 ? 8  
HELX_P HELX_P97  AK7 GLN D 159 ? GLU D 186 ? GLN D 159 GLU D 186 1 ? 28 
HELX_P HELX_P98  AK8 LEU D 200 ? ASN D 206 ? LEU D 200 ASN D 206 1 ? 7  
HELX_P HELX_P99  AK9 PRO D 207 ? THR D 213 ? PRO D 207 THR D 213 5 ? 7  
HELX_P HELX_P100 AL1 PHE D 226 ? GLY D 246 ? PHE D 226 GLY D 246 1 ? 21 
HELX_P HELX_P101 AL2 PRO D 254 ? SER D 258 ? PRO D 254 SER D 258 5 ? 5  
HELX_P HELX_P102 AL3 SER D 260 ? LYS D 270 ? SER D 260 LYS D 270 1 ? 11 
HELX_P HELX_P103 AL4 GLU D 279 ? VAL D 286 ? GLU D 279 VAL D 286 1 ? 8  
HELX_P HELX_P104 AL5 ASP D 307 ? SER D 317 ? ASP D 307 SER D 317 1 ? 11 
HELX_P HELX_P105 AL6 ASN D 322 ? VAL D 341 ? ASN D 322 VAL D 341 1 ? 20 
HELX_P HELX_P106 AL7 TYR D 360 ? ASN D 363 ? TYR D 360 ASN D 363 5 ? 4  
HELX_P HELX_P107 AL8 GLY D 364 ? GLU D 378 ? GLY D 364 GLU D 378 1 ? 15 
HELX_P HELX_P108 AL9 THR D 385 ? LYS D 392 ? THR D 385 LYS D 392 1 ? 8  
HELX_P HELX_P109 AM1 GLU D 421 ? LYS D 435 ? GLU D 421 LYS D 435 1 ? 15 
HELX_P HELX_P110 AM2 ASP D 439 ? GLU D 445 ? ASP D 439 GLU D 445 1 ? 7  
HELX_P HELX_P111 AM3 GLY D 446 ? TRP D 452 ? GLY D 446 TRP D 452 1 ? 7  
HELX_P HELX_P112 AM4 PHE D 460 ? ALA D 475 ? PHE D 460 ALA D 475 1 ? 16 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 5 ? 
AB3 ? 4 ? 
AB4 ? 4 ? 
AB5 ? 2 ? 
AB6 ? 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 ? anti-parallel 
AA4 3 4 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? parallel      
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB2 1 2 ? parallel      
AB2 2 3 ? parallel      
AB2 3 4 ? anti-parallel 
AB2 4 5 ? parallel      
AB3 1 2 ? parallel      
AB3 2 3 ? parallel      
AB3 3 4 ? parallel      
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB5 1 2 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? anti-parallel 
AB6 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 ? THR A 193 ? VAL A 191 THR A 193 
AA1 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA1 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA1 4 VAL A 346 ? ASP A 352 ? VAL A 346 ASP A 352 
AA2 1 VAL A 191 ? THR A 193 ? VAL A 191 THR A 193 
AA2 2 ASN A 53  ? LEU A 56  ? ASN A 53  LEU A 56  
AA2 3 LEU A 4   ? MET A 12  ? LEU A 4   MET A 12  
AA2 4 ILE A 381 ? THR A 383 ? ILE A 381 THR A 383 
AA3 1 GLU A 24  ? TYR A 25  ? GLU A 24  TYR A 25  
AA3 2 LYS A 73  ? ASP A 74  ? LYS A 73  ASP A 74  
AA4 1 MET A 274 ? ASP A 278 ? MET A 274 ASP A 278 
AA4 2 ILE A 301 ? ARG A 306 ? ILE A 301 ARG A 306 
AA4 3 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 4 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
AA5 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA5 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA5 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA5 4 VAL B 346 ? ASP B 352 ? VAL B 346 ASP B 352 
AA6 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA6 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA6 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA6 4 ILE B 381 ? THR B 383 ? ILE B 381 THR B 383 
AA7 1 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 ? ASP B 278 ? MET B 274 ASP B 278 
AA8 3 ILE B 301 ? ARG B 306 ? ILE B 301 ARG B 306 
AA8 4 ARG B 294 ? PHE B 297 ? ARG B 294 PHE B 297 
AA8 5 THR B 397 ? ILE B 400 ? THR B 397 ILE B 400 
AA9 1 VAL C 191 ? THR C 193 ? VAL C 191 THR C 193 
AA9 2 ASN C 53  ? LEU C 56  ? ASN C 53  LEU C 56  
AA9 3 LEU C 4   ? MET C 12  ? LEU C 4   MET C 12  
AA9 4 VAL C 346 ? ASP C 352 ? VAL C 346 ASP C 352 
AB1 1 VAL C 191 ? THR C 193 ? VAL C 191 THR C 193 
AB1 2 ASN C 53  ? LEU C 56  ? ASN C 53  LEU C 56  
AB1 3 LEU C 4   ? MET C 12  ? LEU C 4   MET C 12  
AB1 4 ILE C 381 ? LEU C 384 ? ILE C 381 LEU C 384 
AB2 1 TYR C 251 ? MET C 252 ? TYR C 251 MET C 252 
AB2 2 MET C 274 ? ASP C 278 ? MET C 274 ASP C 278 
AB2 3 ILE C 301 ? ARG C 306 ? ILE C 301 ARG C 306 
AB2 4 ARG C 294 ? PHE C 297 ? ARG C 294 PHE C 297 
AB2 5 THR C 397 ? ILE C 400 ? THR C 397 ILE C 400 
AB3 1 GLY D 189 ? SER D 192 ? GLY D 189 SER D 192 
AB3 2 LEU D 52  ? LEU D 56  ? LEU D 52  LEU D 56  
AB3 3 LEU D 4   ? MET D 12  ? LEU D 4   MET D 12  
AB3 4 VAL D 346 ? LEU D 351 ? VAL D 346 LEU D 351 
AB4 1 GLY D 189 ? SER D 192 ? GLY D 189 SER D 192 
AB4 2 LEU D 52  ? LEU D 56  ? LEU D 52  LEU D 56  
AB4 3 LEU D 4   ? MET D 12  ? LEU D 4   MET D 12  
AB4 4 ILE D 381 ? LEU D 384 ? ILE D 381 LEU D 384 
AB5 1 GLU D 24  ? TYR D 25  ? GLU D 24  TYR D 25  
AB5 2 LYS D 73  ? ASP D 74  ? LYS D 73  ASP D 74  
AB6 1 TYR D 251 ? MET D 252 ? TYR D 251 MET D 252 
AB6 2 MET D 274 ? ASP D 278 ? MET D 274 ASP D 278 
AB6 3 ILE D 301 ? ARG D 306 ? ILE D 301 ARG D 306 
AB6 4 ARG D 294 ? PHE D 297 ? ARG D 294 PHE D 297 
AB6 5 THR D 397 ? ILE D 400 ? THR D 397 ILE D 400 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 192 ? O SER A 192 N LEU A 56  ? N LEU A 56  
AA1 2 3 O ASN A 55  ? O ASN A 55  N TRP A 10  ? N TRP A 10  
AA1 3 4 N VAL A 7   ? N VAL A 7   O VAL A 349 ? O VAL A 349 
AA2 1 2 O SER A 192 ? O SER A 192 N LEU A 56  ? N LEU A 56  
AA2 2 3 O ASN A 55  ? O ASN A 55  N TRP A 10  ? N TRP A 10  
AA2 3 4 N LEU A 4   ? N LEU A 4   O GLU A 382 ? O GLU A 382 
AA3 1 2 N TYR A 25  ? N TYR A 25  O LYS A 73  ? O LYS A 73  
AA4 1 2 N THR A 277 ? N THR A 277 O ARG A 306 ? O ARG A 306 
AA4 2 3 O ILE A 301 ? O ILE A 301 N PHE A 297 ? N PHE A 297 
AA4 3 4 N TYR A 296 ? N TYR A 296 O GLU A 398 ? O GLU A 398 
AA5 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA5 2 3 O ASN B 55  ? O ASN B 55  N MET B 12  ? N MET B 12  
AA5 3 4 N VAL B 7   ? N VAL B 7   O VAL B 349 ? O VAL B 349 
AA6 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA6 2 3 O ASN B 55  ? O ASN B 55  N MET B 12  ? N MET B 12  
AA6 3 4 N LEU B 6   ? N LEU B 6   O GLU B 382 ? O GLU B 382 
AA7 1 2 N TYR B 25  ? N TYR B 25  O LYS B 73  ? O LYS B 73  
AA8 1 2 N MET B 252 ? N MET B 252 O MET B 274 ? O MET B 274 
AA8 2 3 N THR B 277 ? N THR B 277 O ARG B 306 ? O ARG B 306 
AA8 3 4 O ILE B 301 ? O ILE B 301 N PHE B 297 ? N PHE B 297 
AA8 4 5 N TYR B 296 ? N TYR B 296 O GLU B 398 ? O GLU B 398 
AA9 1 2 O SER C 192 ? O SER C 192 N PHE C 54  ? N PHE C 54  
AA9 2 3 O ASN C 55  ? O ASN C 55  N MET C 12  ? N MET C 12  
AA9 3 4 N VAL C 7   ? N VAL C 7   O VAL C 349 ? O VAL C 349 
AB1 1 2 O SER C 192 ? O SER C 192 N PHE C 54  ? N PHE C 54  
AB1 2 3 O ASN C 55  ? O ASN C 55  N MET C 12  ? N MET C 12  
AB1 3 4 N LEU C 4   ? N LEU C 4   O GLU C 382 ? O GLU C 382 
AB2 1 2 N MET C 252 ? N MET C 252 O MET C 274 ? O MET C 274 
AB2 2 3 N THR C 277 ? N THR C 277 O ARG C 306 ? O ARG C 306 
AB2 3 4 O VAL C 303 ? O VAL C 303 N TYR C 295 ? N TYR C 295 
AB2 4 5 N TYR C 296 ? N TYR C 296 O ILE C 400 ? O ILE C 400 
AB3 1 2 O SER D 192 ? O SER D 192 N PHE D 54  ? N PHE D 54  
AB3 2 3 O ASN D 55  ? O ASN D 55  N MET D 12  ? N MET D 12  
AB3 3 4 N TRP D 9   ? N TRP D 9   O VAL D 349 ? O VAL D 349 
AB4 1 2 O SER D 192 ? O SER D 192 N PHE D 54  ? N PHE D 54  
AB4 2 3 O ASN D 55  ? O ASN D 55  N MET D 12  ? N MET D 12  
AB4 3 4 N LEU D 6   ? N LEU D 6   O LEU D 384 ? O LEU D 384 
AB5 1 2 N TYR D 25  ? N TYR D 25  O LYS D 73  ? O LYS D 73  
AB6 1 2 N MET D 252 ? N MET D 252 O MET D 274 ? O MET D 274 
AB6 2 3 N THR D 277 ? N THR D 277 O ARG D 306 ? O ARG D 306 
AB6 3 4 O ILE D 301 ? O ILE D 301 N PHE D 297 ? N PHE D 297 
AB6 4 5 N TYR D 296 ? N TYR D 296 O ILE D 400 ? O ILE D 400 
# 
_pdbx_entry_details.entry_id                   9JLQ 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 544 ? ? O   A HOH 554 ? ? 1.83 
2  1 O   B HOH 524 ? ? O   B HOH 540 ? ? 1.88 
3  1 OE1 A GLU 186 ? ? O   A HOH 501 ? ? 1.96 
4  1 O   B HOH 510 ? ? O   B HOH 536 ? ? 2.00 
5  1 O   A CYS 356 ? ? O   A HOH 502 ? ? 2.00 
6  1 O   B ARG 141 ? ? O   B HOH 501 ? ? 2.03 
7  1 O   B PRO 249 ? ? O   B HOH 502 ? ? 2.03 
8  1 NZ  A LYS 335 ? ? O   A HOH 503 ? ? 2.05 
9  1 O   A HOH 515 ? ? O   A HOH 558 ? ? 2.06 
10 1 NE  D ARG 469 ? ? O   D HOH 501 ? ? 2.07 
11 1 OD1 C ASN 216 ? ? O   C HOH 501 ? ? 2.10 
12 1 O   A HOH 511 ? ? O   A HOH 555 ? ? 2.11 
13 1 O   D ILE 314 ? ? OH  D TYR 360 ? ? 2.13 
14 1 OE1 B GLU 185 ? ? O   B HOH 503 ? ? 2.15 
15 1 NH1 D ARG 18  ? ? O   D HOH 502 ? ? 2.15 
16 1 O   D LYS 336 ? ? OG  D SER 340 ? ? 2.17 
17 1 OH  A TYR 25  ? ? OE1 A GLU 66  ? ? 2.17 
18 1 O   C PHE 316 ? ? O   C HOH 502 ? ? 2.17 
19 1 OG1 A THR 385 ? ? O   A HOH 504 ? ? 2.18 
20 1 O   A HOH 531 ? ? O   A HOH 553 ? ? 2.18 
21 1 O   D VAL 191 ? ? OH  D TYR 241 ? ? 2.18 
22 1 NH1 A ARG 155 ? ? O   A HOH 505 ? ? 2.18 
23 1 O   A HOH 555 ? ? O   A HOH 557 ? ? 2.19 
24 1 OE2 C GLU 382 ? ? O   C HOH 503 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 49  ? ? -91.07  58.03   
2  1 TRP A 138 ? ? -98.56  34.57   
3  1 ASN B 216 ? ? -101.74 70.06   
4  1 GLU B 339 ? ? -94.59  31.45   
5  1 ASP B 448 ? ? -69.31  0.77    
6  1 PRO C 15  ? ? -69.04  -178.92 
7  1 ASP C 37  ? ? -133.13 -32.69  
8  1 TRP C 138 ? ? -96.39  32.49   
9  1 LEU C 147 ? ? -99.46  37.23   
10 1 HIS C 248 ? ? 105.21  130.30  
11 1 PHE C 316 ? ? -131.41 -30.41  
12 1 GLU C 455 ? ? 72.62   -13.20  
13 1 GLU C 456 ? ? -172.33 138.51  
14 1 ASP D 37  ? ? -130.02 -35.69  
15 1 PRO D 106 ? ? -69.76  0.09    
16 1 TYR D 108 ? ? -91.64  50.73   
17 1 ILE D 113 ? ? -108.06 -61.33  
18 1 ASN D 156 ? ? 61.98   70.42   
19 1 THR D 158 ? ? -97.68  -87.09  
20 1 GLN D 159 ? ? -139.78 -58.88  
21 1 ASP D 439 ? ? -69.90  4.63    
22 1 HIS D 480 ? ? 61.77   74.02   
# 
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 17.6551  -3.7732  9.9113   0.1360  ? 0.0324  ? -0.0838 ? 0.0750 ? 0.0199  ? 0.0674 ? 1.5797 ? 
0.7528  ? 0.4848  ? 0.8734 ? 0.1438  ? 0.8650 ? -0.1107 ? 0.1091  ? -0.2263 ? 0.1707  ? 0.1242  ? -0.2588 ? 0.0831  ? 0.2451  ? 
-0.0164 ? 
2  'X-RAY DIFFRACTION' ? refined 32.7710  4.0212   15.0413  0.1654  ? -0.0139 ? -0.0202 ? 0.2094 ? -0.0578 ? 0.2111 ? 3.3087 ? 
0.4480  ? 0.3747  ? 1.5488 ? 0.2954  ? 1.2723 ? 0.0463  ? 0.0454  ? 0.2415  ? 0.1883  ? 0.0948  ? -0.3264 ? 0.0926  ? 0.3416  ? 
-0.1122 ? 
3  'X-RAY DIFFRACTION' ? refined 1.1451   -2.9773  -1.1334  0.1371  ? -0.0299 ? -0.0067 ? 0.0980 ? -0.0152 ? 0.1306 ? 1.2628 ? 
0.3713  ? -0.2383 ? 1.3799 ? 0.2729  ? 1.8191 ? -0.1256 ? 0.1935  ? -0.0603 ? -0.1509 ? 0.1110  ? 0.0685  ? 0.1228  ? -0.0987 ? 
-0.0408 ? 
4  'X-RAY DIFFRACTION' ? refined 1.1111   8.1338   17.0331  0.1160  ? -0.0061 ? -0.0348 ? 0.1369 ? -0.0370 ? 0.0961 ? 3.0603 ? 
0.3060  ? 0.0653  ? 1.9149 ? 0.1874  ? 2.2263 ? 0.0220  ? -0.2802 ? 0.3941  ? 0.0308  ? 0.0222  ? 0.2192  ? 0.1091  ? -0.0961 ? 
-0.0223 ? 
5  'X-RAY DIFFRACTION' ? refined 6.5447   1.1049   -11.9226 0.1989  ? -0.0547 ? -0.1515 ? 0.2443 ? 0.0157  ? 0.0437 ? 1.0419 ? 
-0.9432 ? 0.0983  ? 2.5291 ? 1.3616  ? 1.3949 ? -0.0803 ? 0.4231  ? 0.3625  ? -0.7442 ? 0.3125  ? -0.7148 ? -0.2755 ? 0.0516  ? 
-0.0334 ? 
6  'X-RAY DIFFRACTION' ? refined 21.0609  -4.1533  -10.1928 0.1367  ? 0.0070  ? -0.0023 ? 0.3204 ? -0.0382 ? 0.2472 ? 4.2133 ? 
0.4574  ? 0.3333  ? 3.5406 ? -0.2653 ? 3.7414 ? -0.1818 ? 0.2600  ? 0.3373  ? 0.2170  ? 0.1577  ? -0.4843 ? -0.3140 ? 0.3737  ? 
-0.0427 ? 
7  'X-RAY DIFFRACTION' ? refined -25.5939 38.9241  30.4953  0.1436  ? 0.0047  ? 0.0115  ? 0.2985 ? 0.0288  ? 0.2254 ? 2.7722 ? 
0.0390  ? -0.0751 ? 0.7757 ? -0.0546 ? 0.6388 ? 0.0020  ? -0.4180 ? -0.1121 ? 0.0348  ? 0.1053  ? 0.2572  ? 0.0151  ? -0.2395 ? 
-0.0608 ? 
8  'X-RAY DIFFRACTION' ? refined -5.3839  46.0114  11.1226  0.1477  ? -0.0114 ? -0.0395 ? 0.1228 ? 0.0006  ? 0.1546 ? 2.6870 ? 
-0.1892 ? -0.1114 ? 1.4063 ? -0.2765 ? 1.9554 ? -0.0799 ? 0.2625  ? 0.0525  ? -0.2324 ? 0.0534  ? 0.0840  ? -0.1348 ? 0.1068  ? 
-0.0389 ? 
9  'X-RAY DIFFRACTION' ? refined 3.1033   37.9904  20.4443  -0.1140 ? -0.0905 ? 0.0443  ? 0.0430 ? -0.0359 ? 0.2141 ? 1.7190 ? 
0.2418  ? -0.1618 ? 1.0545 ? -0.5806 ? 1.9549 ? 0.1336  ? 0.1129  ? -0.1788 ? -0.0683 ? 0.1443  ? -0.1583 ? 0.5693  ? 0.5592  ? 
0.1159  ? 
10 'X-RAY DIFFRACTION' ? refined -0.5057  31.8923  35.5359  0.1445  ? -0.0450 ? -0.0368 ? 0.2014 ? 0.0280  ? 0.1848 ? 3.1920 ? 
0.0376  ? -0.2009 ? 1.5525 ? -0.4992 ? 2.2494 ? 0.0297  ? -0.4242 ? -0.3642 ? 0.0344  ? -0.0318 ? -0.0284 ? 0.0501  ? 0.1088  ? 
-0.0991 ? 
11 'X-RAY DIFFRACTION' ? refined -6.2352  36.7408  5.6563   0.2392  ? -0.0792 ? -0.0228 ? 0.2368 ? -0.0932 ? 0.1567 ? 2.1483 ? 
-0.2138 ? 0.5744  ? 1.0697 ? -0.5022 ? 2.1599 ? 0.1680  ? 0.2399  ? -0.4427 ? -0.3381 ? 0.0639  ? 0.1641  ? 0.4083  ? -0.4787 ? 
-0.1237 ? 
12 'X-RAY DIFFRACTION' ? refined -20.3399 41.4907  7.4402   0.2363  ? 0.0080  ? -0.0830 ? 0.2624 ? -0.0076 ? 0.1948 ? 5.7703 ? 
0.7736  ? -0.7974 ? 3.4291 ? 1.2106  ? 4.9501 ? -0.1319 ? 0.3313  ? -0.2328 ? 0.2464  ? 0.0724  ? 0.3157  ? 0.5730  ? -0.0263 ? 
0.0895  ? 
13 'X-RAY DIFFRACTION' ? refined 3.3134   -10.5368 47.3238  0.4965  ? -0.0301 ? -0.1941 ? 0.4013 ? -0.0173 ? 0.3388 ? 1.3917 ? 
0.0862  ? -0.1963 ? 2.2023 ? -0.3531 ? 1.5646 ? -0.0557 ? 0.4093  ? -0.1752 ? -0.2669 ? 0.1226  ? 0.5504  ? 0.1010  ? -0.4573 ? 
-0.0582 ? 
14 'X-RAY DIFFRACTION' ? refined 25.6628  -10.1922 65.5463  0.2082  ? 0.0661  ? -0.0940 ? 0.2173 ? -0.0243 ? 0.2060 ? 1.9733 ? 
0.6361  ? -0.1424 ? 1.7302 ? -0.1200 ? 2.9531 ? -0.0373 ? -0.0329 ? 0.0622  ? 0.0259  ? -0.1397 ? -0.1085 ? 0.2817  ? 0.2491  ? 
0.0576  ? 
15 'X-RAY DIFFRACTION' ? refined 31.9889  3.4810   61.6142  0.3014  ? -0.0749 ? -0.0592 ? 0.2968 ? 0.0515  ? 0.2305 ? 2.9135 ? 
0.0595  ? -0.1206 ? 2.4782 ? 0.0075  ? 2.8105 ? -0.1792 ? -0.1010 ? 0.3530  ? -0.4001 ? 0.1026  ? -0.0663 ? -0.2993 ? 0.4670  ? 
0.1065  ? 
16 'X-RAY DIFFRACTION' ? refined 17.5311  10.2119  47.8666  0.5010  ? 0.0287  ? -0.1467 ? 0.3096 ? 0.0669  ? 0.3391 ? 2.3209 ? 
0.5575  ? -0.4046 ? 1.8402 ? 0.2039  ? 1.5733 ? -0.0151 ? 0.2083  ? 0.4019  ? -0.1454 ? 0.0519  ? 0.2336  ? -0.3862 ? -0.0048 ? 
0.0003  ? 
17 'X-RAY DIFFRACTION' ? refined 20.0112  -5.4380  73.0550  0.3116  ? 0.0248  ? -0.0895 ? 0.1693 ? 0.0004  ? 0.1502 ? 1.8531 ? 
0.3664  ? -0.0070 ? 3.7389 ? -0.3206 ? 1.6897 ? 0.1018  ? 0.1494  ? 0.1489  ? 0.3824  ? -0.0576 ? 0.7091  ? 0.0833  ? 0.0532  ? 
-0.1193 ? 
18 'X-RAY DIFFRACTION' ? refined 11.8585  -19.9979 68.6775  0.2924  ? -0.0682 ? -0.0839 ? 0.2907 ? -0.0036 ? 0.2270 ? 1.9035 ? 
0.9997  ? 0.1917  ? 4.2640 ? 0.2046  ? 1.3581 ? -0.1309 ? 0.3960  ? 0.1569  ? -0.1910 ? -0.1108 ? 0.5865  ? -0.3274 ? -0.0173 ? 
0.2564  ? 
19 'X-RAY DIFFRACTION' ? refined 2.5322   47.9679  66.5567  1.1018  ? 0.1523  ? 0.4453  ? 0.5892 ? 0.0556  ? 0.6814 ? 0.8381 ? 
-0.1350 ? -0.3010 ? 1.1378 ? 0.1010  ? 0.9876 ? 0.0288  ? 0.4543  ? -0.2474 ? -0.8557 ? 0.0313  ? -1.0305 ? 0.1825  ? 0.2765  ? 
-0.0176 ? 
20 'X-RAY DIFFRACTION' ? refined -18.9009 47.4421  74.9392  0.8069  ? 0.0715  ? 0.0384  ? 0.4070 ? 0.0047  ? 0.1666 ? 1.9326 ? 
0.0871  ? -0.3173 ? 1.3214 ? 0.1660  ? 0.9149 ? -0.0481 ? 0.6187  ? 0.0398  ? -0.9264 ? -0.0581 ? -0.1403 ? -0.0583 ? -0.3205 ? 
0.0154  ? 
21 'X-RAY DIFFRACTION' ? refined -19.5121 28.5579  77.7741  0.9045  ? 0.0953  ? 0.1942  ? 0.3877 ? -0.1527 ? 0.4460 ? 1.7987 ? 
-0.5480 ? -1.1129 ? 1.0418 ? 0.4534  ? 1.8315 ? -0.0116 ? 0.5445  ? -0.4420 ? -0.4594 ? -0.1112 ? -0.2085 ? 0.6560  ? -0.1924 ? 
0.3701  ? 
22 'X-RAY DIFFRACTION' ? refined -13.7798 26.2516  65.5266  1.3493  ? 0.0999  ? 0.2622  ? 0.7605 ? -0.0907 ? 0.5547 ? 1.5537 ? 
-0.2226 ? -0.0914 ? 1.4454 ? -0.0749 ? 1.3684 ? 0.3787  ? 0.6616  ? -0.4241 ? -0.8851 ? -0.0985 ? -0.4464 ? 0.3806  ? -0.2721 ? 
-0.1783 ? 
23 'X-RAY DIFFRACTION' ? refined -17.9592 36.4792  88.3804  0.2966  ? 0.0538  ? 0.0712  ? 0.3534 ? -0.0122 ? 0.1573 ? 2.8839 ? 
0.2796  ? 0.2934  ? 3.4482 ? 0.2968  ? 2.1878 ? 0.0475  ? 0.2881  ? -0.5058 ? -0.3159 ? -0.1049 ? -0.3916 ? 0.4224  ? 0.0257  ? 
0.0296  ? 
24 'X-RAY DIFFRACTION' ? refined -14.6972 57.1653  90.6732  0.3031  ? 0.1263  ? 0.0522  ? 0.1518 ? -0.0301 ? 0.1836 ? 2.2959 ? 
-1.0442 ? 0.1881  ? 4.6182 ? -1.0471 ? 1.5683 ? -0.1066 ? 0.1142  ? 0.0583  ? 0.0820  ? 0.0136  ? -0.2198 ? 0.0587  ? -0.3110 ? 
0.0281  ? 
25 'X-RAY DIFFRACTION' ? refined -6.5244  57.8659  86.5142  0.4987  ? 0.0857  ? 0.0454  ? 0.3108 ? 0.1121  ? 0.3223 ? 1.5995 ? 
-0.1761 ? -0.7965 ? 3.8979 ? 1.7120  ? 2.2058 ? 0.1282  ? 0.1785  ? 0.0766  ? -0.3371 ? -0.2515 ? -1.0401 ? 0.4179  ? 0.3212  ? 
0.2253  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 81 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 82 through 185 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 186 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 434 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 435 through 477 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1 through 185 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 186 through 245 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 246 through 322 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 323 through 396 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 397 through 435 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 436 through 477 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 1 through 194 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 195 through 260 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 261 through 307 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 308 through 396 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 397 through 435 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 436 through 484 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 1 through 159 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 160 through 273 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 274 through 322 )
;
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 323 through 396 )
;
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 397 through 421 )
;
24 'X-RAY DIFFRACTION' 24 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 422 through 445 )
;
25 'X-RAY DIFFRACTION' 25 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 446 through 483 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 564 ? 6.18 . 
2 1 O ? A HOH 565 ? 7.30 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A LEU 478 ? A LEU 478 
2  1 Y 1 A GLU 479 ? A GLU 479 
3  1 Y 1 A HIS 480 ? A HIS 480 
4  1 Y 1 A HIS 481 ? A HIS 481 
5  1 Y 1 A HIS 482 ? A HIS 482 
6  1 Y 1 A HIS 483 ? A HIS 483 
7  1 Y 1 A HIS 484 ? A HIS 484 
8  1 Y 1 B LEU 478 ? B LEU 478 
9  1 Y 1 B GLU 479 ? B GLU 479 
10 1 Y 1 B HIS 480 ? B HIS 480 
11 1 Y 1 B HIS 481 ? B HIS 481 
12 1 Y 1 B HIS 482 ? B HIS 482 
13 1 Y 1 B HIS 483 ? B HIS 483 
14 1 Y 1 B HIS 484 ? B HIS 484 
15 1 Y 1 D HIS 484 ? D HIS 484 
# 
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  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JLQ 
_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]   0.013763 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005092 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005998 
_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]   0.010715 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . MET A 1 1   ? -16.097 6.845   26.166  1.00 48.65  ? 1   MET A N   1 
ATOM   2     C CA  . MET A 1 1   ? -14.941 7.597   25.689  1.00 48.10  ? 1   MET A CA  1 
ATOM   3     C C   . MET A 1 1   ? -14.657 7.328   24.219  1.00 41.21  ? 1   MET A C   1 
ATOM   4     O O   . MET A 1 1   ? -14.296 6.213   23.842  1.00 54.23  ? 1   MET A O   1 
ATOM   5     C CB  . MET A 1 1   ? -13.698 7.264   26.522  1.00 43.63  ? 1   MET A CB  1 
ATOM   6     C CG  . MET A 1 1   ? -12.439 7.984   26.054  1.00 39.50  ? 1   MET A CG  1 
ATOM   7     S SD  . MET A 1 1   ? -11.115 8.042   27.283  1.00 61.83  ? 1   MET A SD  1 
ATOM   8     C CE  . MET A 1 1   ? -10.691 6.311   27.442  1.00 42.31  ? 1   MET A CE  1 
ATOM   9     N N   . LYS A 1 2   ? -14.831 8.353   23.389  1.00 27.98  ? 2   LYS A N   1 
ATOM   10    C CA  . LYS A 1 2   ? -14.433 8.246   21.994  1.00 23.26  ? 2   LYS A CA  1 
ATOM   11    C C   . LYS A 1 2   ? -12.915 8.225   21.897  1.00 25.75  ? 2   LYS A C   1 
ATOM   12    O O   . LYS A 1 2   ? -12.223 9.004   22.559  1.00 30.13  ? 2   LYS A O   1 
ATOM   13    C CB  . LYS A 1 2   ? -14.998 9.407   21.180  1.00 29.09  ? 2   LYS A CB  1 
ATOM   14    C CG  . LYS A 1 2   ? -14.614 9.371   19.712  1.00 22.59  ? 2   LYS A CG  1 
ATOM   15    C CD  . LYS A 1 2   ? -15.488 10.301  18.893  1.00 26.22  ? 2   LYS A CD  1 
ATOM   16    C CE  . LYS A 1 2   ? -14.724 10.867  17.712  1.00 23.81  ? 2   LYS A CE  1 
ATOM   17    N NZ  . LYS A 1 2   ? -15.365 12.096  17.167  1.00 24.21  ? 2   LYS A NZ  1 
ATOM   18    N N   . LYS A 1 3   ? -12.394 7.326   21.068  1.00 23.73  ? 3   LYS A N   1 
ATOM   19    C CA  . LYS A 1 3   ? -10.964 7.088   20.988  1.00 23.37  ? 3   LYS A CA  1 
ATOM   20    C C   . LYS A 1 3   ? -10.453 7.297   19.571  1.00 19.57  ? 3   LYS A C   1 
ATOM   21    O O   . LYS A 1 3   ? -11.196 7.173   18.594  1.00 15.08  ? 3   LYS A O   1 
ATOM   22    C CB  . LYS A 1 3   ? -10.608 5.665   21.428  1.00 25.85  ? 3   LYS A CB  1 
ATOM   23    C CG  . LYS A 1 3   ? -10.209 5.524   22.878  1.00 25.00  ? 3   LYS A CG  1 
ATOM   24    C CD  . LYS A 1 3   ? -10.445 4.099   23.349  1.00 27.67  ? 3   LYS A CD  1 
ATOM   25    C CE  . LYS A 1 3   ? -10.261 3.974   24.846  1.00 42.91  ? 3   LYS A CE  1 
ATOM   26    N NZ  . LYS A 1 3   ? -8.864  4.285   25.259  1.00 45.00  ? 3   LYS A NZ  1 
ATOM   27    N N   . LEU A 1 4   ? -9.169  7.616   19.479  1.00 17.36  ? 4   LEU A N   1 
ATOM   28    C CA  . LEU A 1 4   ? -8.415  7.505   18.241  1.00 15.29  ? 4   LEU A CA  1 
ATOM   29    C C   . LEU A 1 4   ? -7.520  6.282   18.353  1.00 19.87  ? 4   LEU A C   1 
ATOM   30    O O   . LEU A 1 4   ? -6.759  6.153   19.319  1.00 19.97  ? 4   LEU A O   1 
ATOM   31    C CB  . LEU A 1 4   ? -7.575  8.757   17.981  1.00 16.39  ? 4   LEU A CB  1 
ATOM   32    C CG  . LEU A 1 4   ? -6.652  8.745   16.755  1.00 10.92  ? 4   LEU A CG  1 
ATOM   33    C CD1 . LEU A 1 4   ? -6.632  10.121  16.114  1.00 23.75  ? 4   LEU A CD1 1 
ATOM   34    C CD2 . LEU A 1 4   ? -5.233  8.307   17.109  1.00 9.30   ? 4   LEU A CD2 1 
ATOM   35    N N   . PHE A 1 5   ? -7.617  5.385   17.380  1.00 18.02  ? 5   PHE A N   1 
ATOM   36    C CA  . PHE A 1 5   ? -6.785  4.191   17.340  1.00 14.36  ? 5   PHE A CA  1 
ATOM   37    C C   . PHE A 1 5   ? -5.586  4.476   16.446  1.00 11.42  ? 5   PHE A C   1 
ATOM   38    O O   . PHE A 1 5   ? -5.748  4.746   15.251  1.00 15.21  ? 5   PHE A O   1 
ATOM   39    C CB  . PHE A 1 5   ? -7.575  2.985   16.834  1.00 17.52  ? 5   PHE A CB  1 
ATOM   40    C CG  . PHE A 1 5   ? -8.823  2.711   17.622  1.00 19.98  ? 5   PHE A CG  1 
ATOM   41    C CD1 . PHE A 1 5   ? -8.746  2.268   18.931  1.00 24.28  ? 5   PHE A CD1 1 
ATOM   42    C CD2 . PHE A 1 5   ? -10.071 2.904   17.057  1.00 22.51  ? 5   PHE A CD2 1 
ATOM   43    C CE1 . PHE A 1 5   ? -9.893  2.020   19.661  1.00 26.00  ? 5   PHE A CE1 1 
ATOM   44    C CE2 . PHE A 1 5   ? -11.220 2.658   17.782  1.00 25.72  ? 5   PHE A CE2 1 
ATOM   45    C CZ  . PHE A 1 5   ? -11.131 2.215   19.087  1.00 28.58  ? 5   PHE A CZ  1 
ATOM   46    N N   . LEU A 1 6   ? -4.394  4.423   17.030  1.00 13.18  ? 6   LEU A N   1 
ATOM   47    C CA  . LEU A 1 6   ? -3.156  4.749   16.340  1.00 10.76  ? 6   LEU A CA  1 
ATOM   48    C C   . LEU A 1 6   ? -2.395  3.465   16.045  1.00 6.31   ? 6   LEU A C   1 
ATOM   49    O O   . LEU A 1 6   ? -2.223  2.624   16.934  1.00 14.14  ? 6   LEU A O   1 
ATOM   50    C CB  . LEU A 1 6   ? -2.298  5.691   17.185  1.00 7.41   ? 6   LEU A CB  1 
ATOM   51    C CG  . LEU A 1 6   ? -1.146  6.399   16.474  1.00 10.58  ? 6   LEU A CG  1 
ATOM   52    C CD1 . LEU A 1 6   ? -1.653  7.126   15.238  1.00 6.88   ? 6   LEU A CD1 1 
ATOM   53    C CD2 . LEU A 1 6   ? -0.450  7.361   17.421  1.00 16.20  ? 6   LEU A CD2 1 
ATOM   54    N N   . VAL A 1 7   ? -1.951  3.307   14.802  1.00 5.92   ? 7   VAL A N   1 
ATOM   55    C CA  . VAL A 1 7   ? -1.147  2.160   14.398  1.00 8.72   ? 7   VAL A CA  1 
ATOM   56    C C   . VAL A 1 7   ? 0.156   2.674   13.806  1.00 14.17  ? 7   VAL A C   1 
ATOM   57    O O   . VAL A 1 7   ? 0.146   3.399   12.802  1.00 13.48  ? 7   VAL A O   1 
ATOM   58    C CB  . VAL A 1 7   ? -1.887  1.260   13.399  1.00 5.54   ? 7   VAL A CB  1 
ATOM   59    C CG1 . VAL A 1 7   ? -1.065  0.017   13.107  1.00 5.45   ? 7   VAL A CG1 1 
ATOM   60    C CG2 . VAL A 1 7   ? -3.252  0.876   13.947  1.00 9.14   ? 7   VAL A CG2 1 
ATOM   61    N N   . PHE A 1 8   ? 1.271   2.305   14.432  1.00 17.76  ? 8   PHE A N   1 
ATOM   62    C CA  . PHE A 1 8   ? 2.606   2.576   13.919  1.00 9.04   ? 8   PHE A CA  1 
ATOM   63    C C   . PHE A 1 8   ? 3.101   1.351   13.168  1.00 6.78   ? 8   PHE A C   1 
ATOM   64    O O   . PHE A 1 8   ? 2.971   0.225   13.658  1.00 10.33  ? 8   PHE A O   1 
ATOM   65    C CB  . PHE A 1 8   ? 3.574   2.916   15.052  1.00 9.74   ? 8   PHE A CB  1 
ATOM   66    C CG  . PHE A 1 8   ? 3.503   4.343   15.511  1.00 16.14  ? 8   PHE A CG  1 
ATOM   67    C CD1 . PHE A 1 8   ? 4.076   5.356   14.759  1.00 17.48  ? 8   PHE A CD1 1 
ATOM   68    C CD2 . PHE A 1 8   ? 2.878   4.669   16.703  1.00 11.89  ? 8   PHE A CD2 1 
ATOM   69    C CE1 . PHE A 1 8   ? 4.021   6.669   15.180  1.00 13.08  ? 8   PHE A CE1 1 
ATOM   70    C CE2 . PHE A 1 8   ? 2.819   5.981   17.130  1.00 14.96  ? 8   PHE A CE2 1 
ATOM   71    C CZ  . PHE A 1 8   ? 3.391   6.983   16.369  1.00 16.47  ? 8   PHE A CZ  1 
ATOM   72    N N   . TRP A 1 9   ? 3.670   1.570   11.985  1.00 18.79  ? 9   TRP A N   1 
ATOM   73    C CA  . TRP A 1 9   ? 4.144   0.469   11.145  1.00 8.15   ? 9   TRP A CA  1 
ATOM   74    C C   . TRP A 1 9   ? 5.463   0.889   10.503  1.00 8.56   ? 9   TRP A C   1 
ATOM   75    O O   . TRP A 1 9   ? 5.476   1.517   9.442   1.00 15.02  ? 9   TRP A O   1 
ATOM   76    C CB  . TRP A 1 9   ? 3.102   0.114   10.105  1.00 10.45  ? 9   TRP A CB  1 
ATOM   77    C CG  . TRP A 1 9   ? 3.251   -1.239  9.532   1.00 10.49  ? 9   TRP A CG  1 
ATOM   78    C CD1 . TRP A 1 9   ? 4.251   -2.133  9.769   1.00 12.51  ? 9   TRP A CD1 1 
ATOM   79    C CD2 . TRP A 1 9   ? 2.367   -1.858  8.601   1.00 10.87  ? 9   TRP A CD2 1 
ATOM   80    N NE1 . TRP A 1 9   ? 4.038   -3.287  9.042   1.00 11.66  ? 9   TRP A NE1 1 
ATOM   81    C CE2 . TRP A 1 9   ? 2.885   -3.137  8.315   1.00 11.15  ? 9   TRP A CE2 1 
ATOM   82    C CE3 . TRP A 1 9   ? 1.182   -1.454  7.979   1.00 13.32  ? 9   TRP A CE3 1 
ATOM   83    C CZ2 . TRP A 1 9   ? 2.254   -4.016  7.432   1.00 10.65  ? 9   TRP A CZ2 1 
ATOM   84    C CZ3 . TRP A 1 9   ? 0.567   -2.322  7.098   1.00 11.98  ? 9   TRP A CZ3 1 
ATOM   85    C CH2 . TRP A 1 9   ? 1.102   -3.592  6.835   1.00 11.33  ? 9   TRP A CH2 1 
ATOM   86    N N   . TRP A 1 10  ? 6.566   0.531   11.153  1.00 11.21  ? 10  TRP A N   1 
ATOM   87    C CA  . TRP A 1 10  ? 7.894   0.813   10.628  1.00 8.41   ? 10  TRP A CA  1 
ATOM   88    C C   . TRP A 1 10  ? 8.299   -0.264  9.628   1.00 11.81  ? 10  TRP A C   1 
ATOM   89    O O   . TRP A 1 10  ? 8.147   -1.460  9.894   1.00 14.87  ? 10  TRP A O   1 
ATOM   90    C CB  . TRP A 1 10  ? 8.915   0.886   11.765  1.00 9.87   ? 10  TRP A CB  1 
ATOM   91    C CG  . TRP A 1 10  ? 8.541   1.776   12.930  1.00 9.37   ? 10  TRP A CG  1 
ATOM   92    C CD1 . TRP A 1 10  ? 8.200   1.371   14.189  1.00 11.35  ? 10  TRP A CD1 1 
ATOM   93    C CD2 . TRP A 1 10  ? 8.513   3.211   12.952  1.00 12.72  ? 10  TRP A CD2 1 
ATOM   94    N NE1 . TRP A 1 10  ? 7.949   2.458   14.989  1.00 10.92  ? 10  TRP A NE1 1 
ATOM   95    C CE2 . TRP A 1 10  ? 8.134   3.601   14.255  1.00 21.16  ? 10  TRP A CE2 1 
ATOM   96    C CE3 . TRP A 1 10  ? 8.764   4.203   11.999  1.00 11.49  ? 10  TRP A CE3 1 
ATOM   97    C CZ2 . TRP A 1 10  ? 7.998   4.940   14.626  1.00 18.75  ? 10  TRP A CZ2 1 
ATOM   98    C CZ3 . TRP A 1 10  ? 8.630   5.533   12.372  1.00 10.70  ? 10  TRP A CZ3 1 
ATOM   99    C CH2 . TRP A 1 10  ? 8.250   5.888   13.671  1.00 14.07  ? 10  TRP A CH2 1 
ATOM   100   N N   . HIS A 1 11  ? 8.821   0.163   8.483   1.00 9.95   ? 11  HIS A N   1 
ATOM   101   C CA  . HIS A 1 11  ? 9.230   -0.734  7.409   1.00 9.55   ? 11  HIS A CA  1 
ATOM   102   C C   . HIS A 1 11  ? 10.751  -0.765  7.340   1.00 10.26  ? 11  HIS A C   1 
ATOM   103   O O   . HIS A 1 11  ? 11.385  0.264   7.089   1.00 26.66  ? 11  HIS A O   1 
ATOM   104   C CB  . HIS A 1 11  ? 8.625   -0.287  6.077   1.00 10.16  ? 11  HIS A CB  1 
ATOM   105   C CG  . HIS A 1 11  ? 9.295   -0.872  4.874   1.00 7.86   ? 11  HIS A CG  1 
ATOM   106   N ND1 . HIS A 1 11  ? 9.171   -2.199  4.522   1.00 12.30  ? 11  HIS A ND1 1 
ATOM   107   C CD2 . HIS A 1 11  ? 10.085  -0.307  3.931   1.00 11.38  ? 11  HIS A CD2 1 
ATOM   108   C CE1 . HIS A 1 11  ? 9.861   -2.428  3.419   1.00 10.14  ? 11  HIS A CE1 1 
ATOM   109   N NE2 . HIS A 1 11  ? 10.426  -1.296  3.040   1.00 6.99   ? 11  HIS A NE2 1 
ATOM   110   N N   . MET A 1 12  ? 11.329  -1.940  7.571   1.00 11.23  ? 12  MET A N   1 
ATOM   111   C CA  . MET A 1 12  ? 12.772  -2.141  7.536   1.00 12.10  ? 12  MET A CA  1 
ATOM   112   C C   . MET A 1 12  ? 13.142  -2.924  6.286   1.00 11.26  ? 12  MET A C   1 
ATOM   113   O O   . MET A 1 12  ? 12.594  -4.005  6.043   1.00 13.68  ? 12  MET A O   1 
ATOM   114   C CB  . MET A 1 12  ? 13.252  -2.893  8.778   1.00 11.84  ? 12  MET A CB  1 
ATOM   115   C CG  . MET A 1 12  ? 12.534  -2.515  10.058  1.00 8.39   ? 12  MET A CG  1 
ATOM   116   S SD  . MET A 1 12  ? 12.936  -0.851  10.618  1.00 18.83  ? 12  MET A SD  1 
ATOM   117   C CE  . MET A 1 12  ? 12.918  -1.098  12.393  1.00 11.79  ? 12  MET A CE  1 
ATOM   118   N N   . HIS A 1 13  ? 14.078  -2.388  5.505   1.00 10.86  ? 13  HIS A N   1 
ATOM   119   C CA  . HIS A 1 13  ? 14.496  -3.059  4.284   1.00 13.54  ? 13  HIS A CA  1 
ATOM   120   C C   . HIS A 1 13  ? 15.870  -2.561  3.865   1.00 15.93  ? 13  HIS A C   1 
ATOM   121   O O   . HIS A 1 13  ? 16.194  -1.382  4.032   1.00 22.82  ? 13  HIS A O   1 
ATOM   122   C CB  . HIS A 1 13  ? 13.492  -2.833  3.146   1.00 14.59  ? 13  HIS A CB  1 
ATOM   123   C CG  . HIS A 1 13  ? 14.053  -3.103  1.785   1.00 19.84  ? 13  HIS A CG  1 
ATOM   124   N ND1 . HIS A 1 13  ? 14.295  -4.378  1.320   1.00 20.14  ? 13  HIS A ND1 1 
ATOM   125   C CD2 . HIS A 1 13  ? 14.421  -2.264  0.788   1.00 20.29  ? 13  HIS A CD2 1 
ATOM   126   C CE1 . HIS A 1 13  ? 14.786  -4.313  0.096   1.00 18.96  ? 13  HIS A CE1 1 
ATOM   127   N NE2 . HIS A 1 13  ? 14.873  -3.042  -0.251  1.00 17.29  ? 13  HIS A NE2 1 
ATOM   128   N N   . GLN A 1 14  ? 16.671  -3.480  3.317   1.00 19.11  ? 14  GLN A N   1 
ATOM   129   C CA  . GLN A 1 14  ? 17.929  -3.158  2.658   1.00 18.07  ? 14  GLN A CA  1 
ATOM   130   C C   . GLN A 1 14  ? 18.044  -4.100  1.466   1.00 21.18  ? 14  GLN A C   1 
ATOM   131   O O   . GLN A 1 14  ? 17.861  -5.320  1.625   1.00 21.30  ? 14  GLN A O   1 
ATOM   132   C CB  . GLN A 1 14  ? 19.157  -3.306  3.566   1.00 15.71  ? 14  GLN A CB  1 
ATOM   133   C CG  . GLN A 1 14  ? 19.229  -2.346  4.744   1.00 19.55  ? 14  GLN A CG  1 
ATOM   134   C CD  . GLN A 1 14  ? 19.394  -0.884  4.348   1.00 17.14  ? 14  GLN A CD  1 
ATOM   135   O OE1 . GLN A 1 14  ? 19.423  -0.539  3.167   1.00 19.78  ? 14  GLN A OE1 1 
ATOM   136   N NE2 . GLN A 1 14  ? 19.523  -0.018  5.347   1.00 17.58  ? 14  GLN A NE2 1 
ATOM   137   N N   . PRO A 1 15  ? 18.346  -3.584  0.278   1.00 15.41  ? 15  PRO A N   1 
ATOM   138   C CA  . PRO A 1 15  ? 18.554  -4.468  -0.872  1.00 15.37  ? 15  PRO A CA  1 
ATOM   139   C C   . PRO A 1 15  ? 19.811  -5.302  -0.690  1.00 20.90  ? 15  PRO A C   1 
ATOM   140   O O   . PRO A 1 15  ? 20.723  -4.950  0.063   1.00 23.10  ? 15  PRO A O   1 
ATOM   141   C CB  . PRO A 1 15  ? 18.690  -3.508  -2.062  1.00 19.87  ? 15  PRO A CB  1 
ATOM   142   C CG  . PRO A 1 15  ? 18.741  -2.123  -1.492  1.00 15.80  ? 15  PRO A CG  1 
ATOM   143   C CD  . PRO A 1 15  ? 18.721  -2.189  -0.001  1.00 15.48  ? 15  PRO A CD  1 
ATOM   144   N N   . LEU A 1 16  ? 19.842  -6.436  -1.388  1.00 18.94  ? 16  LEU A N   1 
ATOM   145   C CA  . LEU A 1 16  ? 20.981  -7.339  -1.297  1.00 14.97  ? 16  LEU A CA  1 
ATOM   146   C C   . LEU A 1 16  ? 22.251  -6.649  -1.782  1.00 15.79  ? 16  LEU A C   1 
ATOM   147   O O   . LEU A 1 16  ? 22.400  -6.373  -2.977  1.00 14.69  ? 16  LEU A O   1 
ATOM   148   C CB  . LEU A 1 16  ? 20.724  -8.615  -2.101  1.00 13.21  ? 16  LEU A CB  1 
ATOM   149   C CG  . LEU A 1 16  ? 21.804  -9.688  -1.968  1.00 14.48  ? 16  LEU A CG  1 
ATOM   150   C CD1 . LEU A 1 16  ? 21.870  -10.190 -0.537  1.00 14.23  ? 16  LEU A CD1 1 
ATOM   151   C CD2 . LEU A 1 16  ? 21.560  -10.836 -2.931  1.00 15.36  ? 16  LEU A CD2 1 
ATOM   152   N N   . TYR A 1 17  ? 23.166  -6.360  -0.860  1.00 21.07  ? 17  TYR A N   1 
ATOM   153   C CA  . TYR A 1 17  ? 24.440  -5.738  -1.189  1.00 21.28  ? 17  TYR A CA  1 
ATOM   154   C C   . TYR A 1 17  ? 25.542  -6.757  -1.448  1.00 15.67  ? 17  TYR A C   1 
ATOM   155   O O   . TYR A 1 17  ? 26.675  -6.363  -1.748  1.00 16.55  ? 17  TYR A O   1 
ATOM   156   C CB  . TYR A 1 17  ? 24.879  -4.796  -0.065  1.00 21.26  ? 17  TYR A CB  1 
ATOM   157   C CG  . TYR A 1 17  ? 23.944  -3.634  0.179   1.00 16.91  ? 17  TYR A CG  1 
ATOM   158   C CD1 . TYR A 1 17  ? 23.704  -2.690  -0.810  1.00 17.86  ? 17  TYR A CD1 1 
ATOM   159   C CD2 . TYR A 1 17  ? 23.318  -3.468  1.406   1.00 21.35  ? 17  TYR A CD2 1 
ATOM   160   C CE1 . TYR A 1 17  ? 22.856  -1.621  -0.589  1.00 18.57  ? 17  TYR A CE1 1 
ATOM   161   C CE2 . TYR A 1 17  ? 22.470  -2.402  1.639   1.00 21.21  ? 17  TYR A CE2 1 
ATOM   162   C CZ  . TYR A 1 17  ? 22.243  -1.481  0.638   1.00 19.72  ? 17  TYR A CZ  1 
ATOM   163   O OH  . TYR A 1 17  ? 21.399  -0.418  0.864   1.00 20.54  ? 17  TYR A OH  1 
ATOM   164   N N   . ARG A 1 18  ? 25.240  -8.047  -1.341  1.00 16.01  ? 18  ARG A N   1 
ATOM   165   C CA  . ARG A 1 18  ? 26.246  -9.095  -1.466  1.00 17.48  ? 18  ARG A CA  1 
ATOM   166   C C   . ARG A 1 18  ? 26.480  -9.399  -2.942  1.00 18.55  ? 18  ARG A C   1 
ATOM   167   O O   . ARG A 1 18  ? 25.618  -9.980  -3.609  1.00 18.49  ? 18  ARG A O   1 
ATOM   168   C CB  . ARG A 1 18  ? 25.793  -10.338 -0.707  1.00 17.50  ? 18  ARG A CB  1 
ATOM   169   C CG  . ARG A 1 18  ? 26.876  -11.371 -0.493  1.00 19.02  ? 18  ARG A CG  1 
ATOM   170   C CD  . ARG A 1 18  ? 26.298  -12.655 0.080   1.00 19.17  ? 18  ARG A CD  1 
ATOM   171   N NE  . ARG A 1 18  ? 27.157  -13.801 -0.190  1.00 20.90  ? 18  ARG A NE  1 
ATOM   172   C CZ  . ARG A 1 18  ? 27.207  -14.433 -1.353  1.00 31.47  ? 18  ARG A CZ  1 
ATOM   173   N NH1 . ARG A 1 18  ? 26.446  -14.066 -2.373  1.00 37.80  ? 18  ARG A NH1 1 
ATOM   174   N NH2 . ARG A 1 18  ? 28.038  -15.462 -1.497  1.00 43.00  ? 18  ARG A NH2 1 
ATOM   175   N N   . GLU A 1 19  ? 27.641  -9.007  -3.452  1.00 22.14  ? 19  GLU A N   1 
ATOM   176   C CA  . GLU A 1 19  ? 27.973  -9.284  -4.844  1.00 20.88  ? 19  GLU A CA  1 
ATOM   177   C C   . GLU A 1 19  ? 28.116  -10.790 -5.041  1.00 26.91  ? 19  GLU A C   1 
ATOM   178   O O   . GLU A 1 19  ? 28.890  -11.430 -4.323  1.00 28.17  ? 19  GLU A O   1 
ATOM   179   C CB  . GLU A 1 19  ? 29.260  -8.565  -5.243  1.00 21.92  ? 19  GLU A CB  1 
ATOM   180   C CG  . GLU A 1 19  ? 29.337  -8.237  -6.724  1.00 28.08  ? 19  GLU A CG  1 
ATOM   181   C CD  . GLU A 1 19  ? 30.059  -9.306  -7.517  1.00 36.39  ? 19  GLU A CD  1 
ATOM   182   O OE1 . GLU A 1 19  ? 31.021  -9.892  -6.980  1.00 36.89  ? 19  GLU A OE1 1 
ATOM   183   O OE2 . GLU A 1 19  ? 29.657  -9.572  -8.670  1.00 41.00  ? 19  GLU A OE2 1 
ATOM   184   N N   . PRO A 1 20  ? 27.390  -11.389 -5.990  1.00 30.85  ? 20  PRO A N   1 
ATOM   185   C CA  . PRO A 1 20  ? 27.339  -12.863 -6.052  1.00 31.01  ? 20  PRO A CA  1 
ATOM   186   C C   . PRO A 1 20  ? 28.678  -13.531 -6.320  1.00 34.85  ? 20  PRO A C   1 
ATOM   187   O O   . PRO A 1 20  ? 28.932  -14.621 -5.793  1.00 38.87  ? 20  PRO A O   1 
ATOM   188   C CB  . PRO A 1 20  ? 26.336  -13.137 -7.184  1.00 23.32  ? 20  PRO A CB  1 
ATOM   189   C CG  . PRO A 1 20  ? 26.241  -11.875 -7.960  1.00 32.45  ? 20  PRO A CG  1 
ATOM   190   C CD  . PRO A 1 20  ? 26.614  -10.741 -7.062  1.00 31.97  ? 20  PRO A CD  1 
ATOM   191   N N   . TYR A 1 21  ? 29.548  -12.918 -7.122  1.00 30.89  ? 21  TYR A N   1 
ATOM   192   C CA  . TYR A 1 21  ? 30.785  -13.592 -7.506  1.00 35.69  ? 21  TYR A CA  1 
ATOM   193   C C   . TYR A 1 21  ? 31.799  -13.580 -6.369  1.00 38.85  ? 21  TYR A C   1 
ATOM   194   O O   . TYR A 1 21  ? 32.217  -14.637 -5.885  1.00 42.80  ? 21  TYR A O   1 
ATOM   195   C CB  . TYR A 1 21  ? 31.359  -12.945 -8.767  1.00 35.36  ? 21  TYR A CB  1 
ATOM   196   C CG  . TYR A 1 21  ? 30.540  -13.264 -9.991  1.00 37.97  ? 21  TYR A CG  1 
ATOM   197   C CD1 . TYR A 1 21  ? 30.498  -14.555 -10.501 1.00 44.94  ? 21  TYR A CD1 1 
ATOM   198   C CD2 . TYR A 1 21  ? 29.783  -12.285 -10.619 1.00 42.39  ? 21  TYR A CD2 1 
ATOM   199   C CE1 . TYR A 1 21  ? 29.740  -14.858 -11.614 1.00 57.44  ? 21  TYR A CE1 1 
ATOM   200   C CE2 . TYR A 1 21  ? 29.023  -12.578 -11.731 1.00 46.93  ? 21  TYR A CE2 1 
ATOM   201   C CZ  . TYR A 1 21  ? 29.005  -13.865 -12.224 1.00 56.41  ? 21  TYR A CZ  1 
ATOM   202   O OH  . TYR A 1 21  ? 28.247  -14.154 -13.332 1.00 59.53  ? 21  TYR A OH  1 
ATOM   203   N N   . THR A 1 22  ? 32.206  -12.391 -5.926  1.00 30.88  ? 22  THR A N   1 
ATOM   204   C CA  . THR A 1 22  ? 33.163  -12.292 -4.832  1.00 28.23  ? 22  THR A CA  1 
ATOM   205   C C   . THR A 1 22  ? 32.532  -12.522 -3.465  1.00 32.97  ? 22  THR A C   1 
ATOM   206   O O   . THR A 1 22  ? 33.260  -12.775 -2.499  1.00 33.23  ? 22  THR A O   1 
ATOM   207   C CB  . THR A 1 22  ? 33.851  -10.927 -4.855  1.00 39.96  ? 22  THR A CB  1 
ATOM   208   O OG1 . THR A 1 22  ? 33.064  -9.977  -4.126  1.00 42.11  ? 22  THR A OG1 1 
ATOM   209   C CG2 . THR A 1 22  ? 34.046  -10.447 -6.287  1.00 45.47  ? 22  THR A CG2 1 
ATOM   210   N N   . GLY A 1 23  ? 31.206  -12.439 -3.355  1.00 28.14  ? 23  GLY A N   1 
ATOM   211   C CA  . GLY A 1 23  ? 30.559  -12.610 -2.068  1.00 36.32  ? 23  GLY A CA  1 
ATOM   212   C C   . GLY A 1 23  ? 30.704  -11.441 -1.123  1.00 34.34  ? 23  GLY A C   1 
ATOM   213   O O   . GLY A 1 23  ? 30.303  -11.548 0.040   1.00 36.21  ? 23  GLY A O   1 
ATOM   214   N N   . GLU A 1 24  ? 31.257  -10.325 -1.587  1.00 35.22  ? 24  GLU A N   1 
ATOM   215   C CA  . GLU A 1 24  ? 31.566  -9.194  -0.726  1.00 26.50  ? 24  GLU A CA  1 
ATOM   216   C C   . GLU A 1 24  ? 30.398  -8.220  -0.665  1.00 22.90  ? 24  GLU A C   1 
ATOM   217   O O   . GLU A 1 24  ? 29.744  -7.947  -1.676  1.00 23.56  ? 24  GLU A O   1 
ATOM   218   C CB  . GLU A 1 24  ? 32.816  -8.470  -1.228  1.00 26.02  ? 24  GLU A CB  1 
ATOM   219   C CG  . GLU A 1 24  ? 34.085  -9.304  -1.161  1.00 45.22  ? 24  GLU A CG  1 
ATOM   220   C CD  . GLU A 1 24  ? 35.288  -8.588  -1.749  1.00 71.40  ? 24  GLU A CD  1 
ATOM   221   O OE1 . GLU A 1 24  ? 36.395  -9.166  -1.731  1.00 68.20  ? 24  GLU A OE1 1 
ATOM   222   O OE2 . GLU A 1 24  ? 35.127  -7.445  -2.228  1.00 74.40  ? 24  GLU A OE2 1 
ATOM   223   N N   . TYR A 1 25  ? 30.144  -7.696  0.532   1.00 21.09  ? 25  TYR A N   1 
ATOM   224   C CA  . TYR A 1 25  ? 29.167  -6.628  0.712   1.00 17.78  ? 25  TYR A CA  1 
ATOM   225   C C   . TYR A 1 25  ? 29.825  -5.310  0.330   1.00 18.00  ? 25  TYR A C   1 
ATOM   226   O O   . TYR A 1 25  ? 30.733  -4.836  1.019   1.00 18.19  ? 25  TYR A O   1 
ATOM   227   C CB  . TYR A 1 25  ? 28.664  -6.596  2.151   1.00 17.25  ? 25  TYR A CB  1 
ATOM   228   C CG  . TYR A 1 25  ? 27.634  -7.656  2.458   1.00 19.09  ? 25  TYR A CG  1 
ATOM   229   C CD1 . TYR A 1 25  ? 27.978  -9.001  2.488   1.00 19.53  ? 25  TYR A CD1 1 
ATOM   230   C CD2 . TYR A 1 25  ? 26.315  -7.311  2.712   1.00 20.27  ? 25  TYR A CD2 1 
ATOM   231   C CE1 . TYR A 1 25  ? 27.037  -9.971  2.767   1.00 17.13  ? 25  TYR A CE1 1 
ATOM   232   C CE2 . TYR A 1 25  ? 25.369  -8.273  2.992   1.00 21.51  ? 25  TYR A CE2 1 
ATOM   233   C CZ  . TYR A 1 25  ? 25.734  -9.601  3.018   1.00 15.75  ? 25  TYR A CZ  1 
ATOM   234   O OH  . TYR A 1 25  ? 24.790  -10.561 3.297   1.00 15.51  ? 25  TYR A OH  1 
ATOM   235   N N   . LEU A 1 26  ? 29.369  -4.715  -0.772  1.00 20.59  ? 26  LEU A N   1 
ATOM   236   C CA  . LEU A 1 26  ? 29.990  -3.504  -1.291  1.00 18.56  ? 26  LEU A CA  1 
ATOM   237   C C   . LEU A 1 26  ? 29.566  -2.246  -0.544  1.00 22.56  ? 26  LEU A C   1 
ATOM   238   O O   . LEU A 1 26  ? 30.213  -1.205  -0.706  1.00 19.43  ? 26  LEU A O   1 
ATOM   239   C CB  . LEU A 1 26  ? 29.668  -3.356  -2.780  1.00 18.37  ? 26  LEU A CB  1 
ATOM   240   C CG  . LEU A 1 26  ? 29.944  -4.587  -3.643  1.00 19.60  ? 26  LEU A CG  1 
ATOM   241   C CD1 . LEU A 1 26  ? 29.646  -4.297  -5.104  1.00 20.08  ? 26  LEU A CD1 1 
ATOM   242   C CD2 . LEU A 1 26  ? 31.381  -5.056  -3.466  1.00 21.07  ? 26  LEU A CD2 1 
ATOM   243   N N   . LEU A 1 27  ? 28.507  -2.313  0.268   1.00 18.67  ? 27  LEU A N   1 
ATOM   244   C CA  . LEU A 1 27  ? 28.034  -1.164  1.028   1.00 14.52  ? 27  LEU A CA  1 
ATOM   245   C C   . LEU A 1 27  ? 27.679  -1.626  2.437   1.00 18.52  ? 27  LEU A C   1 
ATOM   246   O O   . LEU A 1 27  ? 26.969  -2.635  2.596   1.00 27.34  ? 27  LEU A O   1 
ATOM   247   C CB  . LEU A 1 27  ? 26.829  -0.497  0.363   1.00 18.90  ? 27  LEU A CB  1 
ATOM   248   C CG  . LEU A 1 27  ? 27.138  0.416   -0.826  1.00 14.92  ? 27  LEU A CG  1 
ATOM   249   C CD1 . LEU A 1 27  ? 25.858  0.781   -1.555  1.00 16.91  ? 27  LEU A CD1 1 
ATOM   250   C CD2 . LEU A 1 27  ? 27.880  1.667   -0.378  1.00 23.63  ? 27  LEU A CD2 1 
ATOM   251   N N   . PRO A 1 28  ? 28.141  -0.919  3.469   1.00 20.22  ? 28  PRO A N   1 
ATOM   252   C CA  . PRO A 1 28  ? 27.918  -1.378  4.844   1.00 16.23  ? 28  PRO A CA  1 
ATOM   253   C C   . PRO A 1 28  ? 26.571  -0.955  5.405   1.00 20.85  ? 28  PRO A C   1 
ATOM   254   O O   . PRO A 1 28  ? 26.374  -0.971  6.624   1.00 30.03  ? 28  PRO A O   1 
ATOM   255   C CB  . PRO A 1 28  ? 29.070  -0.713  5.602   1.00 19.84  ? 28  PRO A CB  1 
ATOM   256   C CG  . PRO A 1 28  ? 29.177  0.613   4.911   1.00 23.05  ? 28  PRO A CG  1 
ATOM   257   C CD  . PRO A 1 28  ? 28.988  0.288   3.437   1.00 19.55  ? 28  PRO A CD  1 
ATOM   258   N N   . TRP A 1 29  ? 25.643  -0.560  4.530   1.00 18.30  ? 29  TRP A N   1 
ATOM   259   C CA  . TRP A 1 29  ? 24.376  -0.006  4.998   1.00 18.97  ? 29  TRP A CA  1 
ATOM   260   C C   . TRP A 1 29  ? 23.598  -1.010  5.839   1.00 16.35  ? 29  TRP A C   1 
ATOM   261   O O   . TRP A 1 29  ? 22.948  -0.630  6.820   1.00 13.95  ? 29  TRP A O   1 
ATOM   262   C CB  . TRP A 1 29  ? 23.539  0.473   3.811   1.00 21.65  ? 29  TRP A CB  1 
ATOM   263   C CG  . TRP A 1 29  ? 24.145  1.644   3.090   1.00 22.03  ? 29  TRP A CG  1 
ATOM   264   C CD1 . TRP A 1 29  ? 24.371  1.753   1.747   1.00 24.47  ? 29  TRP A CD1 1 
ATOM   265   C CD2 . TRP A 1 29  ? 24.616  2.867   3.675   1.00 23.56  ? 29  TRP A CD2 1 
ATOM   266   N NE1 . TRP A 1 29  ? 24.944  2.968   1.460   1.00 27.97  ? 29  TRP A NE1 1 
ATOM   267   C CE2 . TRP A 1 29  ? 25.106  3.670   2.626   1.00 28.24  ? 29  TRP A CE2 1 
ATOM   268   C CE3 . TRP A 1 29  ? 24.666  3.362   4.983   1.00 26.44  ? 29  TRP A CE3 1 
ATOM   269   C CZ2 . TRP A 1 29  ? 25.641  4.939   2.845   1.00 35.41  ? 29  TRP A CZ2 1 
ATOM   270   C CZ3 . TRP A 1 29  ? 25.198  4.620   5.198   1.00 28.38  ? 29  TRP A CZ3 1 
ATOM   271   C CH2 . TRP A 1 29  ? 25.677  5.395   4.135   1.00 36.37  ? 29  TRP A CH2 1 
ATOM   272   N N   . THR A 1 30  ? 23.655  -2.293  5.477   1.00 19.86  ? 30  THR A N   1 
ATOM   273   C CA  . THR A 1 30  ? 22.969  -3.307  6.270   1.00 18.52  ? 30  THR A CA  1 
ATOM   274   C C   . THR A 1 30  ? 23.511  -3.348  7.693   1.00 20.75  ? 30  THR A C   1 
ATOM   275   O O   . THR A 1 30  ? 22.744  -3.400  8.660   1.00 19.76  ? 30  THR A O   1 
ATOM   276   C CB  . THR A 1 30  ? 23.109  -4.679  5.614   1.00 18.66  ? 30  THR A CB  1 
ATOM   277   O OG1 . THR A 1 30  ? 22.784  -4.587  4.223   1.00 22.91  ? 30  THR A OG1 1 
ATOM   278   C CG2 . THR A 1 30  ? 22.173  -5.668  6.282   1.00 17.55  ? 30  THR A CG2 1 
ATOM   279   N N   . PHE A 1 31  ? 24.837  -3.318  7.836   1.00 21.03  ? 31  PHE A N   1 
ATOM   280   C CA  . PHE A 1 31  ? 25.449  -3.398  9.159   1.00 15.63  ? 31  PHE A CA  1 
ATOM   281   C C   . PHE A 1 31  ? 25.101  -2.182  10.009  1.00 19.31  ? 31  PHE A C   1 
ATOM   282   O O   . PHE A 1 31  ? 24.631  -2.317  11.144  1.00 21.56  ? 31  PHE A O   1 
ATOM   283   C CB  . PHE A 1 31  ? 26.965  -3.538  9.025   1.00 13.45  ? 31  PHE A CB  1 
ATOM   284   C CG  . PHE A 1 31  ? 27.697  -3.435  10.332  1.00 13.24  ? 31  PHE A CG  1 
ATOM   285   C CD1 . PHE A 1 31  ? 27.646  -4.464  11.255  1.00 18.92  ? 31  PHE A CD1 1 
ATOM   286   C CD2 . PHE A 1 31  ? 28.426  -2.302  10.642  1.00 17.43  ? 31  PHE A CD2 1 
ATOM   287   C CE1 . PHE A 1 31  ? 28.318  -4.365  12.463  1.00 17.32  ? 31  PHE A CE1 1 
ATOM   288   C CE2 . PHE A 1 31  ? 29.094  -2.198  11.847  1.00 18.02  ? 31  PHE A CE2 1 
ATOM   289   C CZ  . PHE A 1 31  ? 29.042  -3.232  12.756  1.00 14.25  ? 31  PHE A CZ  1 
ATOM   290   N N   . PHE A 1 32  ? 25.321  -0.982  9.469   1.00 19.66  ? 32  PHE A N   1 
ATOM   291   C CA  . PHE A 1 32  ? 25.220  0.226   10.281  1.00 10.44  ? 32  PHE A CA  1 
ATOM   292   C C   . PHE A 1 32  ? 23.791  0.496   10.731  1.00 13.60  ? 32  PHE A C   1 
ATOM   293   O O   . PHE A 1 32  ? 23.580  1.004   11.839  1.00 19.56  ? 32  PHE A O   1 
ATOM   294   C CB  . PHE A 1 32  ? 25.784  1.418   9.512   1.00 13.16  ? 32  PHE A CB  1 
ATOM   295   C CG  . PHE A 1 32  ? 27.272  1.549   9.631   1.00 15.42  ? 32  PHE A CG  1 
ATOM   296   C CD1 . PHE A 1 32  ? 27.864  1.663   10.878  1.00 16.08  ? 32  PHE A CD1 1 
ATOM   297   C CD2 . PHE A 1 32  ? 28.080  1.534   8.508   1.00 18.83  ? 32  PHE A CD2 1 
ATOM   298   C CE1 . PHE A 1 32  ? 29.233  1.776   11.002  1.00 13.51  ? 32  PHE A CE1 1 
ATOM   299   C CE2 . PHE A 1 32  ? 29.452  1.646   8.625   1.00 22.02  ? 32  PHE A CE2 1 
ATOM   300   C CZ  . PHE A 1 32  ? 30.029  1.767   9.876   1.00 18.63  ? 32  PHE A CZ  1 
ATOM   301   N N   . HIS A 1 33  ? 22.802  0.178   9.900   1.00 10.69  ? 33  HIS A N   1 
ATOM   302   C CA  . HIS A 1 33  ? 21.421  0.303   10.341  1.00 13.41  ? 33  HIS A CA  1 
ATOM   303   C C   . HIS A 1 33  ? 21.009  -0.827  11.278  1.00 18.50  ? 33  HIS A C   1 
ATOM   304   O O   . HIS A 1 33  ? 20.076  -0.647  12.069  1.00 21.76  ? 33  HIS A O   1 
ATOM   305   C CB  . HIS A 1 33  ? 20.488  0.369   9.129   1.00 13.33  ? 33  HIS A CB  1 
ATOM   306   C CG  . HIS A 1 33  ? 20.434  1.723   8.490   1.00 13.99  ? 33  HIS A CG  1 
ATOM   307   N ND1 . HIS A 1 33  ? 19.879  2.818   9.116   1.00 24.02  ? 33  HIS A ND1 1 
ATOM   308   C CD2 . HIS A 1 33  ? 20.876  2.162   7.288   1.00 18.39  ? 33  HIS A CD2 1 
ATOM   309   C CE1 . HIS A 1 33  ? 19.977  3.872   8.325   1.00 24.19  ? 33  HIS A CE1 1 
ATOM   310   N NE2 . HIS A 1 33  ? 20.578  3.500   7.209   1.00 23.69  ? 33  HIS A NE2 1 
ATOM   311   N N   . ALA A 1 34  ? 21.696  -1.973  11.224  1.00 14.29  ? 34  ALA A N   1 
ATOM   312   C CA  . ALA A 1 34  ? 21.373  -3.075  12.125  1.00 12.46  ? 34  ALA A CA  1 
ATOM   313   C C   . ALA A 1 34  ? 21.850  -2.806  13.545  1.00 14.30  ? 34  ALA A C   1 
ATOM   314   O O   . ALA A 1 34  ? 21.189  -3.215  14.506  1.00 17.50  ? 34  ALA A O   1 
ATOM   315   C CB  . ALA A 1 34  ? 21.974  -4.379  11.602  1.00 12.65  ? 34  ALA A CB  1 
ATOM   316   N N   . VAL A 1 35  ? 22.992  -2.135  13.702  1.00 10.33  ? 35  VAL A N   1 
ATOM   317   C CA  . VAL A 1 35  ? 23.477  -1.811  15.037  1.00 10.93  ? 35  VAL A CA  1 
ATOM   318   C C   . VAL A 1 35  ? 22.776  -0.591  15.616  1.00 15.16  ? 35  VAL A C   1 
ATOM   319   O O   . VAL A 1 35  ? 22.743  -0.428  16.843  1.00 18.02  ? 35  VAL A O   1 
ATOM   320   C CB  . VAL A 1 35  ? 24.998  -1.584  15.031  1.00 14.78  ? 35  VAL A CB  1 
ATOM   321   C CG1 . VAL A 1 35  ? 25.723  -2.850  14.600  1.00 19.40  ? 35  VAL A CG1 1 
ATOM   322   C CG2 . VAL A 1 35  ? 25.367  -0.418  14.123  1.00 16.25  ? 35  VAL A CG2 1 
ATOM   323   N N   . LYS A 1 36  ? 22.196  0.260   14.770  1.00 19.38  ? 36  LYS A N   1 
ATOM   324   C CA  . LYS A 1 36  ? 21.606  1.521   15.204  1.00 23.37  ? 36  LYS A CA  1 
ATOM   325   C C   . LYS A 1 36  ? 20.087  1.482   15.293  1.00 24.47  ? 36  LYS A C   1 
ATOM   326   O O   . LYS A 1 36  ? 19.516  2.077   16.212  1.00 21.51  ? 36  LYS A O   1 
ATOM   327   C CB  . LYS A 1 36  ? 22.031  2.651   14.258  1.00 24.26  ? 36  LYS A CB  1 
ATOM   328   C CG  . LYS A 1 36  ? 21.580  4.037   14.691  1.00 24.08  ? 36  LYS A CG  1 
ATOM   329   C CD  . LYS A 1 36  ? 22.039  5.110   13.707  1.00 27.23  ? 36  LYS A CD  1 
ATOM   330   C CE  . LYS A 1 36  ? 21.403  4.942   12.333  1.00 26.16  ? 36  LYS A CE  1 
ATOM   331   N NZ  . LYS A 1 36  ? 20.011  5.472   12.283  1.00 21.62  ? 36  LYS A NZ  1 
ATOM   332   N N   . ASP A 1 37  ? 19.409  0.803   14.369  1.00 21.55  ? 37  ASP A N   1 
ATOM   333   C CA  . ASP A 1 37  ? 17.953  0.874   14.319  1.00 16.88  ? 37  ASP A CA  1 
ATOM   334   C C   . ASP A 1 37  ? 17.250  -0.473  14.383  1.00 20.55  ? 37  ASP A C   1 
ATOM   335   O O   . ASP A 1 37  ? 16.228  -0.588  15.061  1.00 22.57  ? 37  ASP A O   1 
ATOM   336   C CB  . ASP A 1 37  ? 17.512  1.616   13.045  1.00 20.24  ? 37  ASP A CB  1 
ATOM   337   C CG  . ASP A 1 37  ? 17.757  3.111   13.129  1.00 30.41  ? 37  ASP A CG  1 
ATOM   338   O OD1 . ASP A 1 37  ? 17.270  3.745   14.089  1.00 35.54  ? 37  ASP A OD1 1 
ATOM   339   O OD2 . ASP A 1 37  ? 18.430  3.656   12.228  1.00 23.16  ? 37  ASP A OD2 1 
ATOM   340   N N   . TYR A 1 38  ? 17.763  -1.502  13.700  1.00 23.67  ? 38  TYR A N   1 
ATOM   341   C CA  . TYR A 1 38  ? 16.985  -2.729  13.519  1.00 15.16  ? 38  TYR A CA  1 
ATOM   342   C C   . TYR A 1 38  ? 16.691  -3.420  14.844  1.00 19.76  ? 38  TYR A C   1 
ATOM   343   O O   . TYR A 1 38  ? 15.613  -4.000  15.020  1.00 24.01  ? 38  TYR A O   1 
ATOM   344   C CB  . TYR A 1 38  ? 17.705  -3.682  12.567  1.00 11.65  ? 38  TYR A CB  1 
ATOM   345   C CG  . TYR A 1 38  ? 17.715  -3.173  11.152  1.00 11.44  ? 38  TYR A CG  1 
ATOM   346   C CD1 . TYR A 1 38  ? 16.798  -2.220  10.737  1.00 15.60  ? 38  TYR A CD1 1 
ATOM   347   C CD2 . TYR A 1 38  ? 18.641  -3.634  10.233  1.00 18.85  ? 38  TYR A CD2 1 
ATOM   348   C CE1 . TYR A 1 38  ? 16.799  -1.739  9.445   1.00 16.98  ? 38  TYR A CE1 1 
ATOM   349   C CE2 . TYR A 1 38  ? 18.656  -3.163  8.942   1.00 18.48  ? 38  TYR A CE2 1 
ATOM   350   C CZ  . TYR A 1 38  ? 17.731  -2.216  8.553   1.00 15.82  ? 38  TYR A CZ  1 
ATOM   351   O OH  . TYR A 1 38  ? 17.729  -1.736  7.272   1.00 26.42  ? 38  TYR A OH  1 
ATOM   352   N N   . TYR A 1 39  ? 17.629  -3.376  15.785  1.00 17.06  ? 39  TYR A N   1 
ATOM   353   C CA  . TYR A 1 39  ? 17.356  -3.950  17.094  1.00 14.32  ? 39  TYR A CA  1 
ATOM   354   C C   . TYR A 1 39  ? 16.667  -2.962  18.024  1.00 15.80  ? 39  TYR A C   1 
ATOM   355   O O   . TYR A 1 39  ? 15.726  -3.332  18.734  1.00 15.09  ? 39  TYR A O   1 
ATOM   356   C CB  . TYR A 1 39  ? 18.649  -4.439  17.744  1.00 20.87  ? 39  TYR A CB  1 
ATOM   357   C CG  . TYR A 1 39  ? 18.424  -4.989  19.131  1.00 19.34  ? 39  TYR A CG  1 
ATOM   358   C CD1 . TYR A 1 39  ? 18.013  -6.301  19.316  1.00 23.35  ? 39  TYR A CD1 1 
ATOM   359   C CD2 . TYR A 1 39  ? 18.601  -4.193  20.255  1.00 12.88  ? 39  TYR A CD2 1 
ATOM   360   C CE1 . TYR A 1 39  ? 17.799  -6.809  20.576  1.00 25.58  ? 39  TYR A CE1 1 
ATOM   361   C CE2 . TYR A 1 39  ? 18.385  -4.689  21.520  1.00 12.72  ? 39  TYR A CE2 1 
ATOM   362   C CZ  . TYR A 1 39  ? 17.986  -6.000  21.677  1.00 24.89  ? 39  TYR A CZ  1 
ATOM   363   O OH  . TYR A 1 39  ? 17.770  -6.507  22.938  1.00 36.98  ? 39  TYR A OH  1 
ATOM   364   N N   . ASP A 1 40  ? 17.123  -1.710  18.032  1.00 16.66  ? 40  ASP A N   1 
ATOM   365   C CA  . ASP A 1 40  ? 16.659  -0.755  19.030  1.00 19.28  ? 40  ASP A CA  1 
ATOM   366   C C   . ASP A 1 40  ? 15.257  -0.234  18.739  1.00 17.28  ? 40  ASP A C   1 
ATOM   367   O O   . ASP A 1 40  ? 14.531  0.118   19.676  1.00 15.82  ? 40  ASP A O   1 
ATOM   368   C CB  . ASP A 1 40  ? 17.655  0.398   19.133  1.00 22.52  ? 40  ASP A CB  1 
ATOM   369   C CG  . ASP A 1 40  ? 19.091  -0.086  19.198  1.00 35.46  ? 40  ASP A CG  1 
ATOM   370   O OD1 . ASP A 1 40  ? 19.597  -0.586  18.169  1.00 32.90  ? 40  ASP A OD1 1 
ATOM   371   O OD2 . ASP A 1 40  ? 19.708  0.021   20.280  1.00 31.69  ? 40  ASP A OD2 1 
ATOM   372   N N   . MET A 1 41  ? 14.855  -0.170  17.470  1.00 19.24  ? 41  MET A N   1 
ATOM   373   C CA  . MET A 1 41  ? 13.500  0.283   17.158  1.00 15.46  ? 41  MET A CA  1 
ATOM   374   C C   . MET A 1 41  ? 12.432  -0.615  17.771  1.00 18.50  ? 41  MET A C   1 
ATOM   375   O O   . MET A 1 41  ? 11.529  -0.085  18.441  1.00 27.85  ? 41  MET A O   1 
ATOM   376   C CB  . MET A 1 41  ? 13.333  0.423   15.639  1.00 12.82  ? 41  MET A CB  1 
ATOM   377   C CG  . MET A 1 41  ? 12.175  1.308   15.205  1.00 19.84  ? 41  MET A CG  1 
ATOM   378   S SD  . MET A 1 41  ? 12.530  3.078   15.236  1.00 24.04  ? 41  MET A SD  1 
ATOM   379   C CE  . MET A 1 41  ? 14.320  3.094   15.210  1.00 14.85  ? 41  MET A CE  1 
ATOM   380   N N   . PRO A 1 42  ? 12.458  -1.945  17.608  1.00 12.27  ? 42  PRO A N   1 
ATOM   381   C CA  . PRO A 1 42  ? 11.505  -2.777  18.360  1.00 12.02  ? 42  PRO A CA  1 
ATOM   382   C C   . PRO A 1 42  ? 11.790  -2.832  19.850  1.00 20.18  ? 42  PRO A C   1 
ATOM   383   O O   . PRO A 1 42  ? 10.884  -3.174  20.620  1.00 20.76  ? 42  PRO A O   1 
ATOM   384   C CB  . PRO A 1 42  ? 11.649  -4.159  17.710  1.00 12.35  ? 42  PRO A CB  1 
ATOM   385   C CG  . PRO A 1 42  ? 13.013  -4.166  17.147  1.00 13.74  ? 42  PRO A CG  1 
ATOM   386   C CD  . PRO A 1 42  ? 13.276  -2.761  16.691  1.00 16.07  ? 42  PRO A CD  1 
ATOM   387   N N   . ALA A 1 43  ? 13.011  -2.505  20.279  1.00 18.00  ? 43  ALA A N   1 
ATOM   388   C CA  . ALA A 1 43  ? 13.368  -2.620  21.688  1.00 15.82  ? 43  ALA A CA  1 
ATOM   389   C C   . ALA A 1 43  ? 12.702  -1.560  22.557  1.00 18.37  ? 43  ALA A C   1 
ATOM   390   O O   . ALA A 1 43  ? 12.678  -1.717  23.783  1.00 26.05  ? 43  ALA A O   1 
ATOM   391   C CB  . ALA A 1 43  ? 14.886  -2.550  21.854  1.00 17.52  ? 43  ALA A CB  1 
ATOM   392   N N   . TYR A 1 44  ? 12.169  -0.487  21.961  1.00 15.66  ? 44  TYR A N   1 
ATOM   393   C CA  . TYR A 1 44  ? 11.390  0.472   22.739  1.00 13.15  ? 44  TYR A CA  1 
ATOM   394   C C   . TYR A 1 44  ? 10.194  -0.196  23.405  1.00 16.95  ? 44  TYR A C   1 
ATOM   395   O O   . TYR A 1 44  ? 9.741   0.251   24.466  1.00 15.75  ? 44  TYR A O   1 
ATOM   396   C CB  . TYR A 1 44  ? 10.900  1.620   21.854  1.00 15.05  ? 44  TYR A CB  1 
ATOM   397   C CG  . TYR A 1 44  ? 11.953  2.615   21.413  1.00 20.61  ? 44  TYR A CG  1 
ATOM   398   C CD1 . TYR A 1 44  ? 12.649  2.438   20.224  1.00 20.91  ? 44  TYR A CD1 1 
ATOM   399   C CD2 . TYR A 1 44  ? 12.232  3.745   22.172  1.00 14.45  ? 44  TYR A CD2 1 
ATOM   400   C CE1 . TYR A 1 44  ? 13.603  3.349   19.810  1.00 13.87  ? 44  TYR A CE1 1 
ATOM   401   C CE2 . TYR A 1 44  ? 13.184  4.663   21.765  1.00 10.99  ? 44  TYR A CE2 1 
ATOM   402   C CZ  . TYR A 1 44  ? 13.866  4.459   20.583  1.00 9.33   ? 44  TYR A CZ  1 
ATOM   403   O OH  . TYR A 1 44  ? 14.816  5.364   20.169  1.00 13.71  ? 44  TYR A OH  1 
ATOM   404   N N   . LEU A 1 45  ? 9.673   -1.263  22.795  1.00 17.05  ? 45  LEU A N   1 
ATOM   405   C CA  . LEU A 1 45  ? 8.483   -1.931  23.309  1.00 23.33  ? 45  LEU A CA  1 
ATOM   406   C C   . LEU A 1 45  ? 8.707   -2.548  24.683  1.00 19.47  ? 45  LEU A C   1 
ATOM   407   O O   . LEU A 1 45  ? 7.734   -2.818  25.396  1.00 25.78  ? 45  LEU A O   1 
ATOM   408   C CB  . LEU A 1 45  ? 8.027   -2.998  22.314  1.00 18.11  ? 45  LEU A CB  1 
ATOM   409   C CG  . LEU A 1 45  ? 7.377   -2.431  21.050  1.00 17.66  ? 45  LEU A CG  1 
ATOM   410   C CD1 . LEU A 1 45  ? 6.907   -3.534  20.114  1.00 19.41  ? 45  LEU A CD1 1 
ATOM   411   C CD2 . LEU A 1 45  ? 6.226   -1.519  21.428  1.00 13.73  ? 45  LEU A CD2 1 
ATOM   412   N N   . LYS A 1 46  ? 9.960   -2.792  25.066  1.00 15.51  ? 46  LYS A N   1 
ATOM   413   C CA  . LYS A 1 46  ? 10.240  -3.278  26.411  1.00 23.34  ? 46  LYS A CA  1 
ATOM   414   C C   . LYS A 1 46  ? 10.147  -2.167  27.450  1.00 17.21  ? 46  LYS A C   1 
ATOM   415   O O   . LYS A 1 46  ? 9.841   -2.440  28.615  1.00 20.41  ? 46  LYS A O   1 
ATOM   416   C CB  . LYS A 1 46  ? 11.625  -3.927  26.463  1.00 22.15  ? 46  LYS A CB  1 
ATOM   417   C CG  . LYS A 1 46  ? 11.966  -4.775  25.247  1.00 19.68  ? 46  LYS A CG  1 
ATOM   418   C CD  . LYS A 1 46  ? 12.843  -5.956  25.630  1.00 36.84  ? 46  LYS A CD  1 
ATOM   419   C CE  . LYS A 1 46  ? 14.296  -5.701  25.266  1.00 39.49  ? 46  LYS A CE  1 
ATOM   420   N NZ  . LYS A 1 46  ? 15.233  -6.578  26.021  1.00 25.05  ? 46  LYS A NZ  1 
ATOM   421   N N   . ASP A 1 47  ? 10.398  -0.919  27.051  1.00 23.04  ? 47  ASP A N   1 
ATOM   422   C CA  . ASP A 1 47  ? 10.426  0.200   27.984  1.00 18.12  ? 47  ASP A CA  1 
ATOM   423   C C   . ASP A 1 47  ? 9.134   1.003   28.019  1.00 19.32  ? 47  ASP A C   1 
ATOM   424   O O   . ASP A 1 47  ? 8.905   1.730   28.992  1.00 23.72  ? 47  ASP A O   1 
ATOM   425   C CB  . ASP A 1 47  ? 11.587  1.145   27.644  1.00 16.62  ? 47  ASP A CB  1 
ATOM   426   C CG  . ASP A 1 47  ? 12.942  0.499   27.849  1.00 25.57  ? 47  ASP A CG  1 
ATOM   427   O OD1 . ASP A 1 47  ? 13.382  0.401   29.014  1.00 35.02  ? 47  ASP A OD1 1 
ATOM   428   O OD2 . ASP A 1 47  ? 13.566  0.089   26.847  1.00 32.81  ? 47  ASP A OD2 1 
ATOM   429   N N   . PHE A 1 48  ? 8.289   0.896   26.998  1.00 24.13  ? 48  PHE A N   1 
ATOM   430   C CA  . PHE A 1 48  ? 7.065   1.681   26.916  1.00 18.34  ? 48  PHE A CA  1 
ATOM   431   C C   . PHE A 1 48  ? 5.880   0.754   26.695  1.00 22.33  ? 48  PHE A C   1 
ATOM   432   O O   . PHE A 1 48  ? 5.975   -0.225  25.947  1.00 25.75  ? 48  PHE A O   1 
ATOM   433   C CB  . PHE A 1 48  ? 7.150   2.721   25.792  1.00 18.45  ? 48  PHE A CB  1 
ATOM   434   C CG  . PHE A 1 48  ? 8.271   3.708   25.965  1.00 15.54  ? 48  PHE A CG  1 
ATOM   435   C CD1 . PHE A 1 48  ? 9.537   3.435   25.473  1.00 14.41  ? 48  PHE A CD1 1 
ATOM   436   C CD2 . PHE A 1 48  ? 8.061   4.905   26.628  1.00 15.15  ? 48  PHE A CD2 1 
ATOM   437   C CE1 . PHE A 1 48  ? 10.569  4.340   25.636  1.00 13.58  ? 48  PHE A CE1 1 
ATOM   438   C CE2 . PHE A 1 48  ? 9.090   5.813   26.792  1.00 12.09  ? 48  PHE A CE2 1 
ATOM   439   C CZ  . PHE A 1 48  ? 10.346  5.529   26.296  1.00 11.86  ? 48  PHE A CZ  1 
ATOM   440   N N   . GLU A 1 49  ? 4.764   1.067   27.351  1.00 22.74  ? 49  GLU A N   1 
ATOM   441   C CA  . GLU A 1 49  ? 3.573   0.219   27.300  1.00 22.77  ? 49  GLU A CA  1 
ATOM   442   C C   . GLU A 1 49  ? 2.653   0.647   26.157  1.00 21.44  ? 49  GLU A C   1 
ATOM   443   O O   . GLU A 1 49  ? 1.486   0.988   26.344  1.00 27.99  ? 49  GLU A O   1 
ATOM   444   C CB  . GLU A 1 49  ? 2.848   0.248   28.641  1.00 21.74  ? 49  GLU A CB  1 
ATOM   445   C CG  . GLU A 1 49  ? 3.691   -0.259  29.799  1.00 36.19  ? 49  GLU A CG  1 
ATOM   446   C CD  . GLU A 1 49  ? 4.498   -1.496  29.440  1.00 50.93  ? 49  GLU A CD  1 
ATOM   447   O OE1 . GLU A 1 49  ? 3.897   -2.483  28.961  1.00 45.23  ? 49  GLU A OE1 1 
ATOM   448   O OE2 . GLU A 1 49  ? 5.733   -1.481  29.628  1.00 53.18  ? 49  GLU A OE2 1 
ATOM   449   N N   . ILE A 1 50  ? 3.213   0.624   24.948  1.00 16.24  ? 50  ILE A N   1 
ATOM   450   C CA  . ILE A 1 50  ? 2.482   0.932   23.728  1.00 9.86   ? 50  ILE A CA  1 
ATOM   451   C C   . ILE A 1 50  ? 2.665   -0.225  22.754  1.00 14.08  ? 50  ILE A C   1 
ATOM   452   O O   . ILE A 1 50  ? 3.442   -1.150  22.989  1.00 18.19  ? 50  ILE A O   1 
ATOM   453   C CB  . ILE A 1 50  ? 2.937   2.255   23.085  1.00 9.35   ? 50  ILE A CB  1 
ATOM   454   C CG1 . ILE A 1 50  ? 4.353   2.109   22.528  1.00 13.59  ? 50  ILE A CG1 1 
ATOM   455   C CG2 . ILE A 1 50  ? 2.859   3.398   24.090  1.00 19.61  ? 50  ILE A CG2 1 
ATOM   456   C CD1 . ILE A 1 50  ? 4.768   3.245   21.622  1.00 18.39  ? 50  ILE A CD1 1 
ATOM   457   N N   . LYS A 1 51  ? 1.928   -0.162  21.649  1.00 19.16  ? 51  LYS A N   1 
ATOM   458   C CA  . LYS A 1 51  ? 2.003   -1.158  20.592  1.00 11.83  ? 51  LYS A CA  1 
ATOM   459   C C   . LYS A 1 51  ? 2.677   -0.553  19.370  1.00 11.97  ? 51  LYS A C   1 
ATOM   460   O O   . LYS A 1 51  ? 2.415   0.600   19.015  1.00 9.64   ? 51  LYS A O   1 
ATOM   461   C CB  . LYS A 1 51  ? 0.611   -1.679  20.216  1.00 14.31  ? 51  LYS A CB  1 
ATOM   462   C CG  . LYS A 1 51  ? -0.186  -2.243  21.381  1.00 20.04  ? 51  LYS A CG  1 
ATOM   463   C CD  . LYS A 1 51  ? 0.552   -3.380  22.068  1.00 16.03  ? 51  LYS A CD  1 
ATOM   464   C CE  . LYS A 1 51  ? -0.423  -4.323  22.747  1.00 19.52  ? 51  LYS A CE  1 
ATOM   465   N NZ  . LYS A 1 51  ? -1.436  -3.586  23.550  1.00 24.06  ? 51  LYS A NZ  1 
ATOM   466   N N   . LEU A 1 52  ? 3.546   -1.337  18.733  1.00 13.50  ? 52  LEU A N   1 
ATOM   467   C CA  . LEU A 1 52  ? 4.283   -0.896  17.556  1.00 10.25  ? 52  LEU A CA  1 
ATOM   468   C C   . LEU A 1 52  ? 4.441   -2.084  16.620  1.00 9.21   ? 52  LEU A C   1 
ATOM   469   O O   . LEU A 1 52  ? 4.657   -3.207  17.076  1.00 11.51  ? 52  LEU A O   1 
ATOM   470   C CB  . LEU A 1 52  ? 5.659   -0.338  17.933  1.00 16.84  ? 52  LEU A CB  1 
ATOM   471   C CG  . LEU A 1 52  ? 5.732   0.921   18.803  1.00 15.68  ? 52  LEU A CG  1 
ATOM   472   C CD1 . LEU A 1 52  ? 7.179   1.270   19.069  1.00 12.94  ? 52  LEU A CD1 1 
ATOM   473   C CD2 . LEU A 1 52  ? 5.022   2.092   18.154  1.00 16.31  ? 52  LEU A CD2 1 
ATOM   474   N N   . ASN A 1 53  ? 4.355   -1.832  15.316  1.00 14.97  ? 53  ASN A N   1 
ATOM   475   C CA  . ASN A 1 53  ? 4.354   -2.890  14.318  1.00 6.26   ? 53  ASN A CA  1 
ATOM   476   C C   . ASN A 1 53  ? 5.499   -2.697  13.332  1.00 12.35  ? 53  ASN A C   1 
ATOM   477   O O   . ASN A 1 53  ? 5.889   -1.567  13.020  1.00 14.22  ? 53  ASN A O   1 
ATOM   478   C CB  . ASN A 1 53  ? 3.021   -2.929  13.576  1.00 6.80   ? 53  ASN A CB  1 
ATOM   479   C CG  . ASN A 1 53  ? 1.843   -2.992  14.519  1.00 10.30  ? 53  ASN A CG  1 
ATOM   480   O OD1 . ASN A 1 53  ? 1.396   -4.073  14.892  1.00 15.43  ? 53  ASN A OD1 1 
ATOM   481   N ND2 . ASN A 1 53  ? 1.348   -1.830  14.931  1.00 9.72   ? 53  ASN A ND2 1 
ATOM   482   N N   . PHE A 1 54  ? 6.034   -3.815  12.840  1.00 9.48   ? 54  PHE A N   1 
ATOM   483   C CA  . PHE A 1 54  ? 7.235   -3.788  12.022  1.00 8.45   ? 54  PHE A CA  1 
ATOM   484   C C   . PHE A 1 54  ? 7.083   -4.679  10.800  1.00 15.39  ? 54  PHE A C   1 
ATOM   485   O O   . PHE A 1 54  ? 6.494   -5.761  10.869  1.00 10.02  ? 54  PHE A O   1 
ATOM   486   C CB  . PHE A 1 54  ? 8.448   -4.218  12.841  1.00 8.97   ? 54  PHE A CB  1 
ATOM   487   C CG  . PHE A 1 54  ? 8.616   -3.423  14.096  1.00 11.74  ? 54  PHE A CG  1 
ATOM   488   C CD1 . PHE A 1 54  ? 9.215   -2.178  14.062  1.00 11.11  ? 54  PHE A CD1 1 
ATOM   489   C CD2 . PHE A 1 54  ? 8.141   -3.903  15.304  1.00 12.75  ? 54  PHE A CD2 1 
ATOM   490   C CE1 . PHE A 1 54  ? 9.358   -1.437  15.213  1.00 9.61   ? 54  PHE A CE1 1 
ATOM   491   C CE2 . PHE A 1 54  ? 8.280   -3.164  16.457  1.00 9.13   ? 54  PHE A CE2 1 
ATOM   492   C CZ  . PHE A 1 54  ? 8.885   -1.927  16.410  1.00 11.13  ? 54  PHE A CZ  1 
ATOM   493   N N   . ASN A 1 55  ? 7.620   -4.203  9.683   1.00 8.98   ? 55  ASN A N   1 
ATOM   494   C CA  . ASN A 1 55  ? 7.718   -4.963  8.448   1.00 11.28  ? 55  ASN A CA  1 
ATOM   495   C C   . ASN A 1 55  ? 9.180   -5.305  8.199   1.00 13.88  ? 55  ASN A C   1 
ATOM   496   O O   . ASN A 1 55  ? 10.059  -4.451  8.353   1.00 19.18  ? 55  ASN A O   1 
ATOM   497   C CB  . ASN A 1 55  ? 7.147   -4.170  7.270   1.00 11.78  ? 55  ASN A CB  1 
ATOM   498   C CG  . ASN A 1 55  ? 7.071   -4.988  5.997   1.00 12.22  ? 55  ASN A CG  1 
ATOM   499   O OD1 . ASN A 1 55  ? 6.135   -5.762  5.803   1.00 15.21  ? 55  ASN A OD1 1 
ATOM   500   N ND2 . ASN A 1 55  ? 8.053   -4.817  5.120   1.00 11.77  ? 55  ASN A ND2 1 
ATOM   501   N N   . LEU A 1 56  ? 9.437   -6.560  7.838   1.00 11.30  ? 56  LEU A N   1 
ATOM   502   C CA  . LEU A 1 56  ? 10.788  -7.029  7.552   1.00 7.01   ? 56  LEU A CA  1 
ATOM   503   C C   . LEU A 1 56  ? 10.802  -7.682  6.182   1.00 14.18  ? 56  LEU A C   1 
ATOM   504   O O   . LEU A 1 56  ? 10.105  -8.678  5.960   1.00 24.23  ? 56  LEU A O   1 
ATOM   505   C CB  . LEU A 1 56  ? 11.276  -8.016  8.618   1.00 8.31   ? 56  LEU A CB  1 
ATOM   506   C CG  . LEU A 1 56  ? 11.440  -7.497  10.047  1.00 6.50   ? 56  LEU A CG  1 
ATOM   507   C CD1 . LEU A 1 56  ? 11.700  -8.655  10.994  1.00 7.18   ? 56  LEU A CD1 1 
ATOM   508   C CD2 . LEU A 1 56  ? 12.564  -6.475  10.124  1.00 6.54   ? 56  LEU A CD2 1 
ATOM   509   N N   . THR A 1 57  ? 11.586  -7.122  5.267   1.00 10.26  ? 57  THR A N   1 
ATOM   510   C CA  . THR A 1 57  ? 11.754  -7.746  3.969   1.00 12.17  ? 57  THR A CA  1 
ATOM   511   C C   . THR A 1 57  ? 12.626  -8.992  4.104   1.00 16.01  ? 57  THR A C   1 
ATOM   512   O O   . THR A 1 57  ? 13.588  -8.998  4.879   1.00 18.05  ? 57  THR A O   1 
ATOM   513   C CB  . THR A 1 57  ? 12.377  -6.767  2.975   1.00 14.48  ? 57  THR A CB  1 
ATOM   514   O OG1 . THR A 1 57  ? 13.587  -6.226  3.523   1.00 13.57  ? 57  THR A OG1 1 
ATOM   515   C CG2 . THR A 1 57  ? 11.408  -5.633  2.678   1.00 11.09  ? 57  THR A CG2 1 
ATOM   516   N N   . PRO A 1 58  ? 12.308  -10.066 3.378   1.00 12.89  ? 58  PRO A N   1 
ATOM   517   C CA  . PRO A 1 58  ? 13.128  -11.284 3.476   1.00 13.63  ? 58  PRO A CA  1 
ATOM   518   C C   . PRO A 1 58  ? 14.571  -11.080 3.053   1.00 16.96  ? 58  PRO A C   1 
ATOM   519   O O   . PRO A 1 58  ? 15.468  -11.729 3.607   1.00 15.22  ? 58  PRO A O   1 
ATOM   520   C CB  . PRO A 1 58  ? 12.397  -12.272 2.555   1.00 12.51  ? 58  PRO A CB  1 
ATOM   521   C CG  . PRO A 1 58  ? 11.016  -11.704 2.394   1.00 13.07  ? 58  PRO A CG  1 
ATOM   522   C CD  . PRO A 1 58  ? 11.190  -10.226 2.438   1.00 13.33  ? 58  PRO A CD  1 
ATOM   523   N N   . VAL A 1 59  ? 14.824  -10.195 2.088   1.00 18.30  ? 59  VAL A N   1 
ATOM   524   C CA  . VAL A 1 59  ? 16.194  -9.946  1.653   1.00 10.00  ? 59  VAL A CA  1 
ATOM   525   C C   . VAL A 1 59  ? 17.004  -9.318  2.780   1.00 12.84  ? 59  VAL A C   1 
ATOM   526   O O   . VAL A 1 59  ? 18.187  -9.632  2.962   1.00 17.25  ? 59  VAL A O   1 
ATOM   527   C CB  . VAL A 1 59  ? 16.202  -9.077  0.380   1.00 11.53  ? 59  VAL A CB  1 
ATOM   528   C CG1 . VAL A 1 59  ? 15.282  -7.872  0.540   1.00 16.46  ? 59  VAL A CG1 1 
ATOM   529   C CG2 . VAL A 1 59  ? 17.620  -8.646  0.028   1.00 10.41  ? 59  VAL A CG2 1 
ATOM   530   N N   . LEU A 1 60  ? 16.383  -8.431  3.564   1.00 15.78  ? 60  LEU A N   1 
ATOM   531   C CA  . LEU A 1 60  ? 17.075  -7.875  4.723   1.00 15.36  ? 60  LEU A CA  1 
ATOM   532   C C   . LEU A 1 60  ? 17.310  -8.938  5.790   1.00 12.40  ? 60  LEU A C   1 
ATOM   533   O O   . LEU A 1 60  ? 18.354  -8.936  6.453   1.00 21.11  ? 60  LEU A O   1 
ATOM   534   C CB  . LEU A 1 60  ? 16.290  -6.698  5.305   1.00 14.23  ? 60  LEU A CB  1 
ATOM   535   C CG  . LEU A 1 60  ? 16.894  -6.119  6.587   1.00 13.80  ? 60  LEU A CG  1 
ATOM   536   C CD1 . LEU A 1 60  ? 18.286  -5.565  6.323   1.00 15.25  ? 60  LEU A CD1 1 
ATOM   537   C CD2 . LEU A 1 60  ? 15.993  -5.057  7.200   1.00 12.69  ? 60  LEU A CD2 1 
ATOM   538   N N   . ILE A 1 61  ? 16.354  -9.854  5.973   1.00 13.98  ? 61  ILE A N   1 
ATOM   539   C CA  . ILE A 1 61  ? 16.523  -10.916 6.963   1.00 15.88  ? 61  ILE A CA  1 
ATOM   540   C C   . ILE A 1 61  ? 17.714  -11.797 6.602   1.00 18.64  ? 61  ILE A C   1 
ATOM   541   O O   . ILE A 1 61  ? 18.456  -12.255 7.480   1.00 20.07  ? 61  ILE A O   1 
ATOM   542   C CB  . ILE A 1 61  ? 15.226  -11.737 7.098   1.00 13.67  ? 61  ILE A CB  1 
ATOM   543   C CG1 . ILE A 1 61  ? 14.077  -10.858 7.596   1.00 17.34  ? 61  ILE A CG1 1 
ATOM   544   C CG2 . ILE A 1 61  ? 15.425  -12.910 8.039   1.00 13.77  ? 61  ILE A CG2 1 
ATOM   545   C CD1 . ILE A 1 61  ? 12.716  -11.528 7.514   1.00 16.43  ? 61  ILE A CD1 1 
ATOM   546   N N   . ASP A 1 62  ? 17.919  -12.042 5.306   1.00 18.11  ? 62  ASP A N   1 
ATOM   547   C CA  . ASP A 1 62  ? 19.071  -12.829 4.877   1.00 14.99  ? 62  ASP A CA  1 
ATOM   548   C C   . ASP A 1 62  ? 20.379  -12.149 5.263   1.00 18.45  ? 62  ASP A C   1 
ATOM   549   O O   . ASP A 1 62  ? 21.312  -12.805 5.742   1.00 18.79  ? 62  ASP A O   1 
ATOM   550   C CB  . ASP A 1 62  ? 19.018  -13.056 3.365   1.00 17.56  ? 62  ASP A CB  1 
ATOM   551   C CG  . ASP A 1 62  ? 17.900  -13.992 2.953   1.00 26.49  ? 62  ASP A CG  1 
ATOM   552   O OD1 . ASP A 1 62  ? 17.341  -14.672 3.838   1.00 26.06  ? 62  ASP A OD1 1 
ATOM   553   O OD2 . ASP A 1 62  ? 17.582  -14.047 1.745   1.00 29.10  ? 62  ASP A OD2 1 
ATOM   554   N N   . GLN A 1 63  ? 20.463  -10.832 5.066   1.00 18.82  ? 63  GLN A N   1 
ATOM   555   C CA  . GLN A 1 63  ? 21.703  -10.118 5.351   1.00 13.40  ? 63  GLN A CA  1 
ATOM   556   C C   . GLN A 1 63  ? 21.941  -9.993  6.850   1.00 16.27  ? 63  GLN A C   1 
ATOM   557   O O   . GLN A 1 63  ? 23.084  -10.099 7.311   1.00 20.54  ? 63  GLN A O   1 
ATOM   558   C CB  . GLN A 1 63  ? 21.677  -8.743  4.690   1.00 11.90  ? 63  GLN A CB  1 
ATOM   559   C CG  . GLN A 1 63  ? 21.939  -8.772  3.197   1.00 12.39  ? 63  GLN A CG  1 
ATOM   560   C CD  . GLN A 1 63  ? 21.632  -7.449  2.528   1.00 21.68  ? 63  GLN A CD  1 
ATOM   561   O OE1 . GLN A 1 63  ? 22.479  -6.873  1.846   1.00 28.42  ? 63  GLN A OE1 1 
ATOM   562   N NE2 . GLN A 1 63  ? 20.414  -6.955  2.722   1.00 23.99  ? 63  GLN A NE2 1 
ATOM   563   N N   . ILE A 1 64  ? 20.879  -9.763  7.628   1.00 21.81  ? 64  ILE A N   1 
ATOM   564   C CA  . ILE A 1 64  ? 21.023  -9.728  9.082   1.00 15.63  ? 64  ILE A CA  1 
ATOM   565   C C   . ILE A 1 64  ? 21.564  -11.059 9.588   1.00 15.29  ? 64  ILE A C   1 
ATOM   566   O O   . ILE A 1 64  ? 22.439  -11.103 10.462  1.00 16.58  ? 64  ILE A O   1 
ATOM   567   C CB  . ILE A 1 64  ? 19.679  -9.375  9.750   1.00 10.66  ? 64  ILE A CB  1 
ATOM   568   C CG1 . ILE A 1 64  ? 19.367  -7.885  9.594   1.00 9.73   ? 64  ILE A CG1 1 
ATOM   569   C CG2 . ILE A 1 64  ? 19.685  -9.763  11.222  1.00 10.98  ? 64  ILE A CG2 1 
ATOM   570   C CD1 . ILE A 1 64  ? 17.899  -7.550  9.774   1.00 17.95  ? 64  ILE A CD1 1 
ATOM   571   N N   . GLN A 1 65  ? 21.062  -12.163 9.034   1.00 13.15  ? 65  GLN A N   1 
ATOM   572   C CA  . GLN A 1 65  ? 21.518  -13.480 9.458   1.00 16.21  ? 65  GLN A CA  1 
ATOM   573   C C   . GLN A 1 65  ? 22.976  -13.716 9.077   1.00 19.60  ? 65  GLN A C   1 
ATOM   574   O O   . GLN A 1 65  ? 23.732  -14.313 9.851   1.00 23.56  ? 65  GLN A O   1 
ATOM   575   C CB  . GLN A 1 65  ? 20.614  -14.560 8.863   1.00 25.23  ? 65  GLN A CB  1 
ATOM   576   C CG  . GLN A 1 65  ? 19.246  -14.630 9.527   1.00 16.99  ? 65  GLN A CG  1 
ATOM   577   C CD  . GLN A 1 65  ? 18.445  -15.857 9.137   1.00 21.90  ? 65  GLN A CD  1 
ATOM   578   O OE1 . GLN A 1 65  ? 18.126  -16.060 7.966   1.00 25.21  ? 65  GLN A OE1 1 
ATOM   579   N NE2 . GLN A 1 65  ? 18.115  -16.683 10.124  1.00 30.70  ? 65  GLN A NE2 1 
ATOM   580   N N   . GLU A 1 66  ? 23.393  -13.248 7.897   1.00 24.06  ? 66  GLU A N   1 
ATOM   581   C CA  . GLU A 1 66  ? 24.768  -13.482 7.458   1.00 24.13  ? 66  GLU A CA  1 
ATOM   582   C C   . GLU A 1 66  ? 25.771  -12.768 8.356   1.00 21.94  ? 66  GLU A C   1 
ATOM   583   O O   . GLU A 1 66  ? 26.845  -13.308 8.645   1.00 24.70  ? 66  GLU A O   1 
ATOM   584   C CB  . GLU A 1 66  ? 24.940  -13.046 6.003   1.00 23.77  ? 66  GLU A CB  1 
ATOM   585   C CG  . GLU A 1 66  ? 25.651  -14.075 5.135   1.00 28.41  ? 66  GLU A CG  1 
ATOM   586   C CD  . GLU A 1 66  ? 26.155  -13.492 3.831   1.00 26.48  ? 66  GLU A CD  1 
ATOM   587   O OE1 . GLU A 1 66  ? 25.460  -12.625 3.264   1.00 25.99  ? 66  GLU A OE1 1 
ATOM   588   O OE2 . GLU A 1 66  ? 27.242  -13.899 3.371   1.00 30.34  ? 66  GLU A OE2 1 
ATOM   589   N N   . TYR A 1 67  ? 25.447  -11.550 8.798   1.00 23.64  ? 67  TYR A N   1 
ATOM   590   C CA  . TYR A 1 67  ? 26.313  -10.853 9.744   1.00 19.38  ? 67  TYR A CA  1 
ATOM   591   C C   . TYR A 1 67  ? 26.286  -11.521 11.113  1.00 19.88  ? 67  TYR A C   1 
ATOM   592   O O   . TYR A 1 67  ? 27.313  -11.588 11.799  1.00 22.15  ? 67  TYR A O   1 
ATOM   593   C CB  . TYR A 1 67  ? 25.896  -9.388  9.866   1.00 21.49  ? 67  TYR A CB  1 
ATOM   594   C CG  . TYR A 1 67  ? 26.368  -8.512  8.732   1.00 17.06  ? 67  TYR A CG  1 
ATOM   595   C CD1 . TYR A 1 67  ? 25.608  -8.368  7.581   1.00 17.62  ? 67  TYR A CD1 1 
ATOM   596   C CD2 . TYR A 1 67  ? 27.568  -7.820  8.815   1.00 20.67  ? 67  TYR A CD2 1 
ATOM   597   C CE1 . TYR A 1 67  ? 26.029  -7.567  6.542   1.00 15.45  ? 67  TYR A CE1 1 
ATOM   598   C CE2 . TYR A 1 67  ? 27.999  -7.014  7.778   1.00 25.33  ? 67  TYR A CE2 1 
ATOM   599   C CZ  . TYR A 1 67  ? 27.225  -6.892  6.645   1.00 15.36  ? 67  TYR A CZ  1 
ATOM   600   O OH  . TYR A 1 67  ? 27.647  -6.092  5.608   1.00 21.82  ? 67  TYR A OH  1 
ATOM   601   N N   . ALA A 1 68  ? 25.118  -12.015 11.528  1.00 24.01  ? 68  ALA A N   1 
ATOM   602   C CA  . ALA A 1 68  ? 24.986  -12.642 12.835  1.00 19.08  ? 68  ALA A CA  1 
ATOM   603   C C   . ALA A 1 68  ? 25.708  -13.980 12.913  1.00 18.26  ? 68  ALA A C   1 
ATOM   604   O O   . ALA A 1 68  ? 25.987  -14.454 14.020  1.00 30.73  ? 68  ALA A O   1 
ATOM   605   C CB  . ALA A 1 68  ? 23.508  -12.824 13.180  1.00 26.86  ? 68  ALA A CB  1 
ATOM   606   N N   . GLN A 1 69  ? 26.008  -14.600 11.774  1.00 18.73  ? 69  GLN A N   1 
ATOM   607   C CA  . GLN A 1 69  ? 26.786  -15.830 11.729  1.00 20.89  ? 69  GLN A CA  1 
ATOM   608   C C   . GLN A 1 69  ? 28.256  -15.583 11.412  1.00 23.41  ? 69  GLN A C   1 
ATOM   609   O O   . GLN A 1 69  ? 29.009  -16.545 11.232  1.00 31.88  ? 69  GLN A O   1 
ATOM   610   C CB  . GLN A 1 69  ? 26.193  -16.797 10.702  1.00 34.02  ? 69  GLN A CB  1 
ATOM   611   C CG  . GLN A 1 69  ? 24.712  -17.076 10.873  1.00 49.26  ? 69  GLN A CG  1 
ATOM   612   C CD  . GLN A 1 69  ? 24.199  -18.115 9.893   1.00 51.07  ? 69  GLN A CD  1 
ATOM   613   O OE1 . GLN A 1 69  ? 23.226  -17.879 9.177   1.00 38.45  ? 69  GLN A OE1 1 
ATOM   614   N NE2 . GLN A 1 69  ? 24.861  -19.265 9.845   1.00 49.56  ? 69  GLN A NE2 1 
ATOM   615   N N   . GLY A 1 70  ? 28.681  -14.323 11.341  1.00 22.18  ? 70  GLY A N   1 
ATOM   616   C CA  . GLY A 1 70  ? 30.054  -14.004 11.004  1.00 21.71  ? 70  GLY A CA  1 
ATOM   617   C C   . GLY A 1 70  ? 30.443  -14.484 9.622   1.00 25.09  ? 70  GLY A C   1 
ATOM   618   O O   . GLY A 1 70  ? 31.506  -15.086 9.440   1.00 24.05  ? 70  GLY A O   1 
ATOM   619   N N   . LYS A 1 71  ? 29.583  -14.227 8.635   1.00 28.91  ? 71  LYS A N   1 
ATOM   620   C CA  . LYS A 1 71  ? 29.811  -14.679 7.271   1.00 35.00  ? 71  LYS A CA  1 
ATOM   621   C C   . LYS A 1 71  ? 29.921  -13.555 6.253   1.00 35.30  ? 71  LYS A C   1 
ATOM   622   O O   . LYS A 1 71  ? 30.473  -13.785 5.171   1.00 39.70  ? 71  LYS A O   1 
ATOM   623   C CB  . LYS A 1 71  ? 28.689  -15.631 6.827   1.00 31.57  ? 71  LYS A CB  1 
ATOM   624   C CG  . LYS A 1 71  ? 28.727  -16.998 7.491   1.00 29.15  ? 71  LYS A CG  1 
ATOM   625   C CD  . LYS A 1 71  ? 27.494  -17.813 7.130   1.00 32.52  ? 71  LYS A CD  1 
ATOM   626   C CE  . LYS A 1 71  ? 27.688  -19.289 7.440   1.00 32.15  ? 71  LYS A CE  1 
ATOM   627   N NZ  . LYS A 1 71  ? 26.932  -20.161 6.498   1.00 28.58  ? 71  LYS A NZ  1 
ATOM   628   N N   . ALA A 1 72  ? 29.421  -12.360 6.557   1.00 24.58  ? 72  ALA A N   1 
ATOM   629   C CA  . ALA A 1 72  ? 29.457  -11.263 5.599   1.00 27.72  ? 72  ALA A CA  1 
ATOM   630   C C   . ALA A 1 72  ? 30.887  -10.767 5.420   1.00 21.67  ? 72  ALA A C   1 
ATOM   631   O O   . ALA A 1 72  ? 31.541  -10.369 6.390   1.00 32.32  ? 72  ALA A O   1 
ATOM   632   C CB  . ALA A 1 72  ? 28.550  -10.126 6.065   1.00 28.02  ? 72  ALA A CB  1 
ATOM   633   N N   . LYS A 1 73  ? 31.374  -10.798 4.178   1.00 21.92  ? 73  LYS A N   1 
ATOM   634   C CA  . LYS A 1 73  ? 32.695  -10.263 3.848   1.00 29.23  ? 73  LYS A CA  1 
ATOM   635   C C   . LYS A 1 73  ? 32.535  -8.787  3.494   1.00 31.01  ? 73  LYS A C   1 
ATOM   636   O O   . LYS A 1 73  ? 32.598  -8.376  2.334   1.00 33.06  ? 73  LYS A O   1 
ATOM   637   C CB  . LYS A 1 73  ? 33.333  -11.057 2.715   1.00 36.02  ? 73  LYS A CB  1 
ATOM   638   C CG  . LYS A 1 73  ? 33.415  -12.559 2.964   1.00 44.36  ? 73  LYS A CG  1 
ATOM   639   C CD  . LYS A 1 73  ? 33.296  -13.352 1.669   1.00 45.01  ? 73  LYS A CD  1 
ATOM   640   C CE  . LYS A 1 73  ? 32.081  -14.267 1.683   1.00 52.67  ? 73  LYS A CE  1 
ATOM   641   N NZ  . LYS A 1 73  ? 31.957  -15.045 0.419   1.00 40.33  ? 73  LYS A NZ  1 
ATOM   642   N N   . ASP A 1 74  ? 32.324  -7.975  4.529   1.00 32.74  ? 74  ASP A N   1 
ATOM   643   C CA  . ASP A 1 74  ? 32.051  -6.550  4.361   1.00 29.50  ? 74  ASP A CA  1 
ATOM   644   C C   . ASP A 1 74  ? 33.373  -5.810  4.186   1.00 28.26  ? 74  ASP A C   1 
ATOM   645   O O   . ASP A 1 74  ? 34.173  -5.722  5.123   1.00 23.99  ? 74  ASP A O   1 
ATOM   646   C CB  . ASP A 1 74  ? 31.264  -6.023  5.558   1.00 29.23  ? 74  ASP A CB  1 
ATOM   647   C CG  . ASP A 1 74  ? 30.672  -4.645  5.316   1.00 28.18  ? 74  ASP A CG  1 
ATOM   648   O OD1 . ASP A 1 74  ? 31.347  -3.793  4.701   1.00 32.83  ? 74  ASP A OD1 1 
ATOM   649   O OD2 . ASP A 1 74  ? 29.520  -4.414  5.739   1.00 28.13  ? 74  ASP A OD2 1 
ATOM   650   N N   . VAL A 1 75  ? 33.594  -5.267  2.987   1.00 34.99  ? 75  VAL A N   1 
ATOM   651   C CA  . VAL A 1 75  ? 34.896  -4.694  2.655   1.00 33.56  ? 75  VAL A CA  1 
ATOM   652   C C   . VAL A 1 75  ? 35.163  -3.430  3.470   1.00 28.55  ? 75  VAL A C   1 
ATOM   653   O O   . VAL A 1 75  ? 36.298  -3.185  3.895   1.00 26.12  ? 75  VAL A O   1 
ATOM   654   C CB  . VAL A 1 75  ? 35.000  -4.453  1.134   1.00 37.66  ? 75  VAL A CB  1 
ATOM   655   C CG1 . VAL A 1 75  ? 34.249  -5.539  0.381   1.00 24.33  ? 75  VAL A CG1 1 
ATOM   656   C CG2 . VAL A 1 75  ? 34.477  -3.077  0.734   1.00 33.28  ? 75  VAL A CG2 1 
ATOM   657   N N   . PHE A 1 76  ? 34.135  -2.612  3.707   1.00 27.48  ? 76  PHE A N   1 
ATOM   658   C CA  . PHE A 1 76  ? 34.330  -1.407  4.507   1.00 22.80  ? 76  PHE A CA  1 
ATOM   659   C C   . PHE A 1 76  ? 34.481  -1.750  5.982   1.00 24.86  ? 76  PHE A C   1 
ATOM   660   O O   . PHE A 1 76  ? 35.300  -1.146  6.685   1.00 23.81  ? 76  PHE A O   1 
ATOM   661   C CB  . PHE A 1 76  ? 33.167  -0.437  4.296   1.00 25.13  ? 76  PHE A CB  1 
ATOM   662   C CG  . PHE A 1 76  ? 33.283  0.834   5.093   1.00 23.08  ? 76  PHE A CG  1 
ATOM   663   C CD1 . PHE A 1 76  ? 34.050  1.892   4.629   1.00 29.46  ? 76  PHE A CD1 1 
ATOM   664   C CD2 . PHE A 1 76  ? 32.625  0.972   6.305   1.00 28.12  ? 76  PHE A CD2 1 
ATOM   665   C CE1 . PHE A 1 76  ? 34.158  3.064   5.362   1.00 32.10  ? 76  PHE A CE1 1 
ATOM   666   C CE2 . PHE A 1 76  ? 32.730  2.138   7.042   1.00 30.25  ? 76  PHE A CE2 1 
ATOM   667   C CZ  . PHE A 1 76  ? 33.497  3.186   6.570   1.00 28.68  ? 76  PHE A CZ  1 
ATOM   668   N N   . LEU A 1 77  ? 33.698  -2.717  6.465   1.00 35.42  ? 77  LEU A N   1 
ATOM   669   C CA  . LEU A 1 77  ? 33.804  -3.131  7.860   1.00 26.52  ? 77  LEU A CA  1 
ATOM   670   C C   . LEU A 1 77  ? 35.179  -3.710  8.156   1.00 26.21  ? 77  LEU A C   1 
ATOM   671   O O   . LEU A 1 77  ? 35.715  -3.532  9.256   1.00 33.86  ? 77  LEU A O   1 
ATOM   672   C CB  . LEU A 1 77  ? 32.714  -4.148  8.190   1.00 24.14  ? 77  LEU A CB  1 
ATOM   673   C CG  . LEU A 1 77  ? 32.464  -4.361  9.681   1.00 29.92  ? 77  LEU A CG  1 
ATOM   674   C CD1 . LEU A 1 77  ? 32.063  -3.048  10.325  1.00 20.83  ? 77  LEU A CD1 1 
ATOM   675   C CD2 . LEU A 1 77  ? 31.403  -5.428  9.902   1.00 28.70  ? 77  LEU A CD2 1 
ATOM   676   N N   . GLU A 1 78  ? 35.762  -4.416  7.185   1.00 25.44  ? 78  GLU A N   1 
ATOM   677   C CA  . GLU A 1 78  ? 37.111  -4.942  7.357   1.00 25.85  ? 78  GLU A CA  1 
ATOM   678   C C   . GLU A 1 78  ? 38.135  -3.821  7.489   1.00 23.13  ? 78  GLU A C   1 
ATOM   679   O O   . GLU A 1 78  ? 39.153  -3.988  8.169   1.00 24.09  ? 78  GLU A O   1 
ATOM   680   C CB  . GLU A 1 78  ? 37.453  -5.862  6.186   1.00 30.77  ? 78  GLU A CB  1 
ATOM   681   C CG  . GLU A 1 78  ? 38.676  -6.732  6.397   1.00 41.21  ? 78  GLU A CG  1 
ATOM   682   C CD  . GLU A 1 78  ? 39.463  -6.934  5.120   1.00 72.39  ? 78  GLU A CD  1 
ATOM   683   O OE1 . GLU A 1 78  ? 39.049  -7.773  4.292   1.00 76.00  ? 78  GLU A OE1 1 
ATOM   684   O OE2 . GLU A 1 78  ? 40.493  -6.252  4.940   1.00 68.69  ? 78  GLU A OE2 1 
ATOM   685   N N   . ALA A 1 79  ? 37.882  -2.673  6.853   1.00 22.98  ? 79  ALA A N   1 
ATOM   686   C CA  . ALA A 1 79  ? 38.792  -1.540  6.979   1.00 22.73  ? 79  ALA A CA  1 
ATOM   687   C C   . ALA A 1 79  ? 38.742  -0.937  8.377   1.00 22.58  ? 79  ALA A C   1 
ATOM   688   O O   . ALA A 1 79  ? 39.777  -0.538  8.924   1.00 33.92  ? 79  ALA A O   1 
ATOM   689   C CB  . ALA A 1 79  ? 38.466  -0.484  5.925   1.00 22.21  ? 79  ALA A CB  1 
ATOM   690   N N   . ILE A 1 80  ? 37.548  -0.844  8.967   1.00 21.03  ? 80  ILE A N   1 
ATOM   691   C CA  . ILE A 1 80  ? 37.440  -0.372  10.345  1.00 20.35  ? 80  ILE A CA  1 
ATOM   692   C C   . ILE A 1 80  ? 38.140  -1.338  11.291  1.00 21.37  ? 80  ILE A C   1 
ATOM   693   O O   . ILE A 1 80  ? 38.863  -0.924  12.205  1.00 30.46  ? 80  ILE A O   1 
ATOM   694   C CB  . ILE A 1 80  ? 35.963  -0.177  10.736  1.00 18.85  ? 80  ILE A CB  1 
ATOM   695   C CG1 . ILE A 1 80  ? 35.291  0.871   9.847   1.00 17.95  ? 80  ILE A CG1 1 
ATOM   696   C CG2 . ILE A 1 80  ? 35.857  0.236   12.191  1.00 18.55  ? 80  ILE A CG2 1 
ATOM   697   C CD1 . ILE A 1 80  ? 35.819  2.275   10.041  1.00 20.57  ? 80  ILE A CD1 1 
ATOM   698   N N   . ARG A 1 81  ? 37.939  -2.642  11.080  1.00 21.78  ? 81  ARG A N   1 
ATOM   699   C CA  . ARG A 1 81  ? 38.524  -3.652  11.958  1.00 22.86  ? 81  ARG A CA  1 
ATOM   700   C C   . ARG A 1 81  ? 40.046  -3.592  11.942  1.00 24.42  ? 81  ARG A C   1 
ATOM   701   O O   . ARG A 1 81  ? 40.694  -3.809  12.973  1.00 25.22  ? 81  ARG A O   1 
ATOM   702   C CB  . ARG A 1 81  ? 38.039  -5.039  11.538  1.00 23.15  ? 81  ARG A CB  1 
ATOM   703   C CG  . ARG A 1 81  ? 38.376  -6.151  12.515  1.00 30.81  ? 81  ARG A CG  1 
ATOM   704   C CD  . ARG A 1 81  ? 37.400  -7.310  12.375  1.00 36.89  ? 81  ARG A CD  1 
ATOM   705   N NE  . ARG A 1 81  ? 37.025  -7.869  13.669  1.00 47.57  ? 81  ARG A NE  1 
ATOM   706   C CZ  . ARG A 1 81  ? 35.906  -8.542  13.899  1.00 48.30  ? 81  ARG A CZ  1 
ATOM   707   N NH1 . ARG A 1 81  ? 35.025  -8.768  12.938  1.00 54.45  ? 81  ARG A NH1 1 
ATOM   708   N NH2 . ARG A 1 81  ? 35.665  -9.000  15.123  1.00 41.43  ? 81  ARG A NH2 1 
ATOM   709   N N   . LYS A 1 82  ? 40.630  -3.292  10.783  1.00 27.35  ? 82  LYS A N   1 
ATOM   710   C CA  . LYS A 1 82  ? 42.074  -3.358  10.600  1.00 25.51  ? 82  LYS A CA  1 
ATOM   711   C C   . LYS A 1 82  ? 42.808  -2.403  11.533  1.00 28.90  ? 82  LYS A C   1 
ATOM   712   O O   . LYS A 1 82  ? 42.310  -1.330  11.884  1.00 28.70  ? 82  LYS A O   1 
ATOM   713   C CB  . LYS A 1 82  ? 42.437  -3.012  9.156   1.00 25.53  ? 82  LYS A CB  1 
ATOM   714   C CG  . LYS A 1 82  ? 42.807  -4.186  8.280   1.00 26.84  ? 82  LYS A CG  1 
ATOM   715   C CD  . LYS A 1 82  ? 43.351  -3.676  6.959   1.00 27.86  ? 82  LYS A CD  1 
ATOM   716   C CE  . LYS A 1 82  ? 42.928  -4.553  5.803   1.00 33.88  ? 82  LYS A CE  1 
ATOM   717   N NZ  . LYS A 1 82  ? 43.427  -4.037  4.500   1.00 47.45  ? 82  LYS A NZ  1 
ATOM   718   N N   . ASP A 1 83  ? 44.006  -2.810  11.938  1.00 30.54  ? 83  ASP A N   1 
ATOM   719   C CA  . ASP A 1 83  ? 44.938  -1.865  12.528  1.00 28.57  ? 83  ASP A CA  1 
ATOM   720   C C   . ASP A 1 83  ? 45.323  -0.827  11.477  1.00 34.57  ? 83  ASP A C   1 
ATOM   721   O O   . ASP A 1 83  ? 45.585  -1.186  10.322  1.00 41.53  ? 83  ASP A O   1 
ATOM   722   C CB  . ASP A 1 83  ? 46.186  -2.584  13.046  1.00 33.98  ? 83  ASP A CB  1 
ATOM   723   C CG  . ASP A 1 83  ? 47.056  -1.693  13.916  1.00 34.04  ? 83  ASP A CG  1 
ATOM   724   O OD1 . ASP A 1 83  ? 47.771  -0.834  13.360  1.00 40.90  ? 83  ASP A OD1 1 
ATOM   725   O OD2 . ASP A 1 83  ? 47.030  -1.850  15.156  1.00 32.54  ? 83  ASP A OD2 1 
ATOM   726   N N   . PRO A 1 84  ? 45.363  0.460   11.831  1.00 30.89  ? 84  PRO A N   1 
ATOM   727   C CA  . PRO A 1 84  ? 45.624  1.493   10.815  1.00 33.08  ? 84  PRO A CA  1 
ATOM   728   C C   . PRO A 1 84  ? 46.944  1.318   10.089  1.00 34.77  ? 84  PRO A C   1 
ATOM   729   O O   . PRO A 1 84  ? 47.075  1.788   8.950   1.00 35.17  ? 84  PRO A O   1 
ATOM   730   C CB  . PRO A 1 84  ? 45.592  2.795   11.626  1.00 30.63  ? 84  PRO A CB  1 
ATOM   731   C CG  . PRO A 1 84  ? 44.753  2.467   12.822  1.00 29.90  ? 84  PRO A CG  1 
ATOM   732   C CD  . PRO A 1 84  ? 45.098  1.046   13.155  1.00 31.96  ? 84  PRO A CD  1 
ATOM   733   N N   . ASP A 1 85  ? 47.921  0.650   10.705  1.00 32.32  ? 85  ASP A N   1 
ATOM   734   C CA  . ASP A 1 85  ? 49.173  0.352   10.021  1.00 35.30  ? 85  ASP A CA  1 
ATOM   735   C C   . ASP A 1 85  ? 48.969  -0.511  8.782   1.00 33.14  ? 85  ASP A C   1 
ATOM   736   O O   . ASP A 1 85  ? 49.817  -0.490  7.883   1.00 38.49  ? 85  ASP A O   1 
ATOM   737   C CB  . ASP A 1 85  ? 50.134  -0.348  10.987  1.00 38.02  ? 85  ASP A CB  1 
ATOM   738   C CG  . ASP A 1 85  ? 51.013  0.626   11.746  1.00 49.92  ? 85  ASP A CG  1 
ATOM   739   O OD1 . ASP A 1 85  ? 50.831  1.850   11.572  1.00 55.37  ? 85  ASP A OD1 1 
ATOM   740   O OD2 . ASP A 1 85  ? 51.887  0.171   12.517  1.00 52.02  ? 85  ASP A OD2 1 
ATOM   741   N N   . ASP A 1 86  ? 47.872  -1.263  8.715   1.00 31.87  ? 86  ASP A N   1 
ATOM   742   C CA  . ASP A 1 86  ? 47.605  -2.180  7.614   1.00 32.34  ? 86  ASP A CA  1 
ATOM   743   C C   . ASP A 1 86  ? 46.890  -1.530  6.435   1.00 31.79  ? 86  ASP A C   1 
ATOM   744   O O   . ASP A 1 86  ? 46.831  -2.137  5.360   1.00 32.61  ? 86  ASP A O   1 
ATOM   745   C CB  . ASP A 1 86  ? 46.754  -3.358  8.106   1.00 31.46  ? 86  ASP A CB  1 
ATOM   746   C CG  . ASP A 1 86  ? 47.452  -4.190  9.161   1.00 38.09  ? 86  ASP A CG  1 
ATOM   747   O OD1 . ASP A 1 86  ? 48.688  -4.344  9.079   1.00 48.36  ? 86  ASP A OD1 1 
ATOM   748   O OD2 . ASP A 1 86  ? 46.759  -4.696  10.072  1.00 40.79  ? 86  ASP A OD2 1 
ATOM   749   N N   . LEU A 1 87  ? 46.356  -0.323  6.602   1.00 30.64  ? 87  LEU A N   1 
ATOM   750   C CA  . LEU A 1 87  ? 45.433  0.239   5.626   1.00 29.93  ? 87  LEU A CA  1 
ATOM   751   C C   . LEU A 1 87  ? 46.169  0.769   4.403   1.00 31.66  ? 87  LEU A C   1 
ATOM   752   O O   . LEU A 1 87  ? 47.162  1.493   4.524   1.00 32.80  ? 87  LEU A O   1 
ATOM   753   C CB  . LEU A 1 87  ? 44.609  1.357   6.261   1.00 28.34  ? 87  LEU A CB  1 
ATOM   754   C CG  . LEU A 1 87  ? 43.558  0.910   7.276   1.00 26.56  ? 87  LEU A CG  1 
ATOM   755   C CD1 . LEU A 1 87  ? 42.911  2.118   7.930   1.00 26.81  ? 87  LEU A CD1 1 
ATOM   756   C CD2 . LEU A 1 87  ? 42.510  0.026   6.615   1.00 26.00  ? 87  LEU A CD2 1 
ATOM   757   N N   . GLU A 1 88  ? 45.674  0.409   3.223   1.00 33.88  ? 88  GLU A N   1 
ATOM   758   C CA  . GLU A 1 88  ? 46.194  0.961   1.984   1.00 39.15  ? 88  GLU A CA  1 
ATOM   759   C C   . GLU A 1 88  ? 45.633  2.360   1.758   1.00 34.07  ? 88  GLU A C   1 
ATOM   760   O O   . GLU A 1 88  ? 44.623  2.756   2.347   1.00 36.73  ? 88  GLU A O   1 
ATOM   761   C CB  . GLU A 1 88  ? 45.854  0.054   0.801   1.00 34.61  ? 88  GLU A CB  1 
ATOM   762   C CG  . GLU A 1 88  ? 46.191  -1.409  1.036   1.00 35.16  ? 88  GLU A CG  1 
ATOM   763   C CD  . GLU A 1 88  ? 47.675  -1.642  1.247   1.00 46.13  ? 88  GLU A CD  1 
ATOM   764   O OE1 . GLU A 1 88  ? 48.486  -0.870  0.694   1.00 42.64  ? 88  GLU A OE1 1 
ATOM   765   O OE2 . GLU A 1 88  ? 48.031  -2.590  1.978   1.00 43.23  ? 88  GLU A OE2 1 
ATOM   766   N N   . LYS A 1 89  ? 46.308  3.112   0.885   1.00 34.90  ? 89  LYS A N   1 
ATOM   767   C CA  . LYS A 1 89  ? 45.910  4.493   0.634   1.00 39.01  ? 89  LYS A CA  1 
ATOM   768   C C   . LYS A 1 89  ? 44.482  4.585   0.109   1.00 41.52  ? 89  LYS A C   1 
ATOM   769   O O   . LYS A 1 89  ? 43.813  5.604   0.312   1.00 43.60  ? 89  LYS A O   1 
ATOM   770   C CB  . LYS A 1 89  ? 46.886  5.150   -0.344  1.00 52.59  ? 89  LYS A CB  1 
ATOM   771   C CG  . LYS A 1 89  ? 48.331  4.682   -0.195  1.00 53.00  ? 89  LYS A CG  1 
ATOM   772   C CD  . LYS A 1 89  ? 48.980  5.257   1.058   1.00 48.83  ? 89  LYS A CD  1 
ATOM   773   C CE  . LYS A 1 89  ? 50.500  5.163   1.000   1.00 40.87  ? 89  LYS A CE  1 
ATOM   774   N NZ  . LYS A 1 89  ? 51.070  5.879   -0.175  1.00 44.06  ? 89  LYS A NZ  1 
ATOM   775   N N   . GLU A 1 90  ? 43.999  3.539   -0.567  1.00 44.90  ? 90  GLU A N   1 
ATOM   776   C CA  . GLU A 1 90  ? 42.615  3.525   -1.030  1.00 41.24  ? 90  GLU A CA  1 
ATOM   777   C C   . GLU A 1 90  ? 41.637  3.195   0.091   1.00 36.65  ? 90  GLU A C   1 
ATOM   778   O O   . GLU A 1 90  ? 40.492  3.662   0.064   1.00 32.39  ? 90  GLU A O   1 
ATOM   779   C CB  . GLU A 1 90  ? 42.448  2.532   -2.182  1.00 53.55  ? 90  GLU A CB  1 
ATOM   780   C CG  . GLU A 1 90  ? 42.434  1.072   -1.754  1.00 58.93  ? 90  GLU A CG  1 
ATOM   781   C CD  . GLU A 1 90  ? 41.977  0.143   -2.860  1.00 74.57  ? 90  GLU A CD  1 
ATOM   782   O OE1 . GLU A 1 90  ? 41.421  0.636   -3.862  1.00 83.68  ? 90  GLU A OE1 1 
ATOM   783   O OE2 . GLU A 1 90  ? 42.169  -1.083  -2.721  1.00 75.21  ? 90  GLU A OE2 1 
ATOM   784   N N   . GLU A 1 91  ? 42.055  2.390   1.071   1.00 33.21  ? 91  GLU A N   1 
ATOM   785   C CA  . GLU A 1 91  ? 41.191  2.118   2.214   1.00 34.01  ? 91  GLU A CA  1 
ATOM   786   C C   . GLU A 1 91  ? 41.024  3.355   3.086   1.00 31.83  ? 91  GLU A C   1 
ATOM   787   O O   . GLU A 1 91  ? 39.949  3.569   3.661   1.00 28.92  ? 91  GLU A O   1 
ATOM   788   C CB  . GLU A 1 91  ? 41.751  0.957   3.034   1.00 29.50  ? 91  GLU A CB  1 
ATOM   789   C CG  . GLU A 1 91  ? 42.036  -0.296  2.222   1.00 37.43  ? 91  GLU A CG  1 
ATOM   790   C CD  . GLU A 1 91  ? 42.458  -1.469  3.084   1.00 39.71  ? 91  GLU A CD  1 
ATOM   791   O OE1 . GLU A 1 91  ? 41.603  -2.015  3.814   1.00 43.46  ? 91  GLU A OE1 1 
ATOM   792   O OE2 . GLU A 1 91  ? 43.646  -1.848  3.033   1.00 46.86  ? 91  GLU A OE2 1 
ATOM   793   N N   . VAL A 1 92  ? 42.072  4.174   3.199   1.00 27.67  ? 92  VAL A N   1 
ATOM   794   C CA  . VAL A 1 92  ? 41.978  5.411   3.965   1.00 27.17  ? 92  VAL A CA  1 
ATOM   795   C C   . VAL A 1 92  ? 41.097  6.426   3.245   1.00 27.09  ? 92  VAL A C   1 
ATOM   796   O O   . VAL A 1 92  ? 40.251  7.080   3.866   1.00 33.99  ? 92  VAL A O   1 
ATOM   797   C CB  . VAL A 1 92  ? 43.384  5.972   4.242   1.00 28.65  ? 92  VAL A CB  1 
ATOM   798   C CG1 . VAL A 1 92  ? 43.290  7.295   4.984   1.00 28.38  ? 92  VAL A CG1 1 
ATOM   799   C CG2 . VAL A 1 92  ? 44.201  4.969   5.040   1.00 28.79  ? 92  VAL A CG2 1 
ATOM   800   N N   . GLU A 1 93  ? 41.276  6.576   1.929   1.00 28.51  ? 93  GLU A N   1 
ATOM   801   C CA  . GLU A 1 93  ? 40.441  7.512   1.181   1.00 37.62  ? 93  GLU A CA  1 
ATOM   802   C C   . GLU A 1 93  ? 38.974  7.103   1.221   1.00 34.60  ? 93  GLU A C   1 
ATOM   803   O O   . GLU A 1 93  ? 38.088  7.960   1.134   1.00 38.85  ? 93  GLU A O   1 
ATOM   804   C CB  . GLU A 1 93  ? 40.929  7.624   -0.266  1.00 42.38  ? 93  GLU A CB  1 
ATOM   805   C CG  . GLU A 1 93  ? 42.299  8.283   -0.431  1.00 53.33  ? 93  GLU A CG  1 
ATOM   806   C CD  . GLU A 1 93  ? 42.239  9.801   -0.488  1.00 70.35  ? 93  GLU A CD  1 
ATOM   807   O OE1 . GLU A 1 93  ? 41.292  10.389  0.075   1.00 64.15  ? 93  GLU A OE1 1 
ATOM   808   O OE2 . GLU A 1 93  ? 43.145  10.408  -1.100  1.00 84.88  ? 93  GLU A OE2 1 
ATOM   809   N N   . LYS A 1 94  ? 38.700  5.802   1.349   1.00 37.14  ? 94  LYS A N   1 
ATOM   810   C CA  . LYS A 1 94  ? 37.325  5.349   1.526   1.00 24.68  ? 94  LYS A CA  1 
ATOM   811   C C   . LYS A 1 94  ? 36.777  5.764   2.886   1.00 25.85  ? 94  LYS A C   1 
ATOM   812   O O   . LYS A 1 94  ? 35.626  6.204   2.989   1.00 25.02  ? 94  LYS A O   1 
ATOM   813   C CB  . LYS A 1 94  ? 37.249  3.831   1.362   1.00 25.72  ? 94  LYS A CB  1 
ATOM   814   C CG  . LYS A 1 94  ? 37.175  3.363   -0.082  1.00 29.09  ? 94  LYS A CG  1 
ATOM   815   C CD  . LYS A 1 94  ? 37.586  1.900   -0.229  1.00 35.24  ? 94  LYS A CD  1 
ATOM   816   C CE  . LYS A 1 94  ? 36.505  0.945   0.271   1.00 40.15  ? 94  LYS A CE  1 
ATOM   817   N NZ  . LYS A 1 94  ? 36.545  0.737   1.748   1.00 37.88  ? 94  LYS A NZ  1 
ATOM   818   N N   . LEU A 1 95  ? 37.587  5.626   3.941   1.00 33.99  ? 95  LEU A N   1 
ATOM   819   C CA  . LEU A 1 95  ? 37.136  5.980   5.284   1.00 27.73  ? 95  LEU A CA  1 
ATOM   820   C C   . LEU A 1 95  ? 36.903  7.476   5.428   1.00 29.48  ? 95  LEU A C   1 
ATOM   821   O O   . LEU A 1 95  ? 36.072  7.898   6.241   1.00 30.93  ? 95  LEU A O   1 
ATOM   822   C CB  . LEU A 1 95  ? 38.149  5.507   6.325   1.00 27.70  ? 95  LEU A CB  1 
ATOM   823   C CG  . LEU A 1 95  ? 37.708  4.345   7.215   1.00 31.49  ? 95  LEU A CG  1 
ATOM   824   C CD1 . LEU A 1 95  ? 37.675  3.042   6.429   1.00 42.60  ? 95  LEU A CD1 1 
ATOM   825   C CD2 . LEU A 1 95  ? 38.636  4.233   8.403   1.00 24.03  ? 95  LEU A CD2 1 
ATOM   826   N N   . ILE A 1 96  ? 37.640  8.292   4.674   1.00 33.48  ? 96  ILE A N   1 
ATOM   827   C CA  . ILE A 1 96  ? 37.403  9.730   4.683   1.00 30.50  ? 96  ILE A CA  1 
ATOM   828   C C   . ILE A 1 96  ? 36.145  10.074  3.891   1.00 34.39  ? 96  ILE A C   1 
ATOM   829   O O   . ILE A 1 96  ? 35.330  10.894  4.328   1.00 39.17  ? 96  ILE A O   1 
ATOM   830   C CB  . ILE A 1 96  ? 38.643  10.468  4.146   1.00 26.46  ? 96  ILE A CB  1 
ATOM   831   C CG1 . ILE A 1 96  ? 39.742  10.490  5.210   1.00 26.08  ? 96  ILE A CG1 1 
ATOM   832   C CG2 . ILE A 1 96  ? 38.290  11.881  3.725   1.00 34.57  ? 96  ILE A CG2 1 
ATOM   833   C CD1 . ILE A 1 96  ? 41.144  10.490  4.641   1.00 27.87  ? 96  ILE A CD1 1 
ATOM   834   N N   . GLU A 1 97  ? 35.960  9.440   2.729   1.00 34.79  ? 97  GLU A N   1 
ATOM   835   C CA  . GLU A 1 97  ? 34.784  9.706   1.903   1.00 35.09  ? 97  GLU A CA  1 
ATOM   836   C C   . GLU A 1 97  ? 33.496  9.392   2.653   1.00 34.84  ? 97  GLU A C   1 
ATOM   837   O O   . GLU A 1 97  ? 32.511  10.133  2.551   1.00 34.14  ? 97  GLU A O   1 
ATOM   838   C CB  . GLU A 1 97  ? 34.859  8.894   0.611   1.00 38.12  ? 97  GLU A CB  1 
ATOM   839   C CG  . GLU A 1 97  ? 34.547  9.684   -0.647  1.00 48.11  ? 97  GLU A CG  1 
ATOM   840   C CD  . GLU A 1 97  ? 34.311  8.792   -1.849  1.00 62.34  ? 97  GLU A CD  1 
ATOM   841   O OE1 . GLU A 1 97  ? 33.356  7.987   -1.812  1.00 45.37  ? 97  GLU A OE1 1 
ATOM   842   O OE2 . GLU A 1 97  ? 35.078  8.897   -2.830  1.00 78.65  ? 97  GLU A OE2 1 
ATOM   843   N N   . PHE A 1 98  ? 33.484  8.293   3.409   1.00 30.76  ? 98  PHE A N   1 
ATOM   844   C CA  . PHE A 1 98  ? 32.318  7.966   4.222   1.00 27.21  ? 98  PHE A CA  1 
ATOM   845   C C   . PHE A 1 98  ? 32.057  9.046   5.267   1.00 25.05  ? 98  PHE A C   1 
ATOM   846   O O   . PHE A 1 98  ? 30.905  9.431   5.498   1.00 30.50  ? 98  PHE A O   1 
ATOM   847   C CB  . PHE A 1 98  ? 32.520  6.602   4.887   1.00 26.85  ? 98  PHE A CB  1 
ATOM   848   C CG  . PHE A 1 98  ? 31.272  6.028   5.497   1.00 17.30  ? 98  PHE A CG  1 
ATOM   849   C CD1 . PHE A 1 98  ? 30.197  5.670   4.702   1.00 18.66  ? 98  PHE A CD1 1 
ATOM   850   C CD2 . PHE A 1 98  ? 31.181  5.827   6.866   1.00 21.96  ? 98  PHE A CD2 1 
ATOM   851   C CE1 . PHE A 1 98  ? 29.049  5.134   5.258   1.00 19.95  ? 98  PHE A CE1 1 
ATOM   852   C CE2 . PHE A 1 98  ? 30.035  5.290   7.429   1.00 20.23  ? 98  PHE A CE2 1 
ATOM   853   C CZ  . PHE A 1 98  ? 28.969  4.943   6.622   1.00 21.78  ? 98  PHE A CZ  1 
ATOM   854   N N   . THR A 1 99  ? 33.118  9.550   5.905   1.00 19.81  ? 99  THR A N   1 
ATOM   855   C CA  . THR A 1 99  ? 32.951  10.582  6.926   1.00 26.15  ? 99  THR A CA  1 
ATOM   856   C C   . THR A 1 99  ? 32.473  11.900  6.324   1.00 30.67  ? 99  THR A C   1 
ATOM   857   O O   . THR A 1 99  ? 31.663  12.607  6.936   1.00 28.17  ? 99  THR A O   1 
ATOM   858   C CB  . THR A 1 99  ? 34.261  10.783  7.688   1.00 27.81  ? 99  THR A CB  1 
ATOM   859   O OG1 . THR A 1 99  ? 34.797  9.508   8.066   1.00 24.38  ? 99  THR A OG1 1 
ATOM   860   C CG2 . THR A 1 99  ? 34.029  11.619  8.938   1.00 20.24  ? 99  THR A CG2 1 
ATOM   861   N N   . LYS A 1 100 ? 32.972  12.259  5.136   1.00 29.58  ? 100 LYS A N   1 
ATOM   862   C CA  . LYS A 1 100 ? 32.486  13.467  4.473   1.00 23.25  ? 100 LYS A CA  1 
ATOM   863   C C   . LYS A 1 100 ? 31.005  13.359  4.136   1.00 22.69  ? 100 LYS A C   1 
ATOM   864   O O   . LYS A 1 100 ? 30.294  14.370  4.133   1.00 26.75  ? 100 LYS A O   1 
ATOM   865   C CB  . LYS A 1 100 ? 33.291  13.745  3.200   1.00 30.21  ? 100 LYS A CB  1 
ATOM   866   C CG  . LYS A 1 100 ? 34.795  13.866  3.391   1.00 33.31  ? 100 LYS A CG  1 
ATOM   867   C CD  . LYS A 1 100 ? 35.368  14.946  2.483   1.00 42.95  ? 100 LYS A CD  1 
ATOM   868   C CE  . LYS A 1 100 ? 36.752  14.581  1.965   1.00 51.75  ? 100 LYS A CE  1 
ATOM   869   N NZ  . LYS A 1 100 ? 36.736  13.332  1.149   1.00 48.30  ? 100 LYS A NZ  1 
ATOM   870   N N   . LEU A 1 101 ? 30.528  12.148  3.842   1.00 28.41  ? 101 LEU A N   1 
ATOM   871   C CA  . LEU A 1 101 ? 29.121  11.955  3.504   1.00 20.94  ? 101 LEU A CA  1 
ATOM   872   C C   . LEU A 1 101 ? 28.215  12.217  4.701   1.00 19.88  ? 101 LEU A C   1 
ATOM   873   O O   . LEU A 1 101 ? 27.142  12.815  4.556   1.00 23.51  ? 101 LEU A O   1 
ATOM   874   C CB  . LEU A 1 101 ? 28.908  10.540  2.969   1.00 20.86  ? 101 LEU A CB  1 
ATOM   875   C CG  . LEU A 1 101 ? 27.554  10.225  2.337   1.00 29.85  ? 101 LEU A CG  1 
ATOM   876   C CD1 . LEU A 1 101 ? 27.479  10.793  0.930   1.00 36.55  ? 101 LEU A CD1 1 
ATOM   877   C CD2 . LEU A 1 101 ? 27.316  8.723   2.327   1.00 31.89  ? 101 LEU A CD2 1 
ATOM   878   N N   . ASN A 1 102 ? 28.625  11.774  5.889   1.00 25.64  ? 102 ASN A N   1 
ATOM   879   C CA  . ASN A 1 102 ? 27.811  11.866  7.094   1.00 28.45  ? 102 ASN A CA  1 
ATOM   880   C C   . ASN A 1 102 ? 28.164  13.069  7.957   1.00 23.21  ? 102 ASN A C   1 
ATOM   881   O O   . ASN A 1 102 ? 27.657  13.182  9.076   1.00 27.29  ? 102 ASN A O   1 
ATOM   882   C CB  . ASN A 1 102 ? 27.960  10.591  7.924   1.00 17.02  ? 102 ASN A CB  1 
ATOM   883   C CG  . ASN A 1 102 ? 27.869  9.332   7.088   1.00 16.29  ? 102 ASN A CG  1 
ATOM   884   O OD1 . ASN A 1 102 ? 26.903  9.126   6.353   1.00 24.25  ? 102 ASN A OD1 1 
ATOM   885   N ND2 . ASN A 1 102 ? 28.884  8.482   7.193   1.00 17.64  ? 102 ASN A ND2 1 
ATOM   886   N N   . TYR A 1 103 ? 29.014  13.971  7.460   1.00 31.89  ? 103 TYR A N   1 
ATOM   887   C CA  . TYR A 1 103 ? 29.604  15.000  8.313   1.00 30.64  ? 103 TYR A CA  1 
ATOM   888   C C   . TYR A 1 103 ? 28.536  15.876  8.961   1.00 31.11  ? 103 TYR A C   1 
ATOM   889   O O   . TYR A 1 103 ? 28.596  16.159  10.163  1.00 29.92  ? 103 TYR A O   1 
ATOM   890   C CB  . TYR A 1 103 ? 30.573  15.853  7.496   1.00 22.68  ? 103 TYR A CB  1 
ATOM   891   C CG  . TYR A 1 103 ? 31.506  16.685  8.337   1.00 28.13  ? 103 TYR A CG  1 
ATOM   892   C CD1 . TYR A 1 103 ? 32.315  16.096  9.298   1.00 32.40  ? 103 TYR A CD1 1 
ATOM   893   C CD2 . TYR A 1 103 ? 31.579  18.063  8.174   1.00 35.67  ? 103 TYR A CD2 1 
ATOM   894   C CE1 . TYR A 1 103 ? 33.172  16.854  10.073  1.00 43.75  ? 103 TYR A CE1 1 
ATOM   895   C CE2 . TYR A 1 103 ? 32.431  18.829  8.943   1.00 38.73  ? 103 TYR A CE2 1 
ATOM   896   C CZ  . TYR A 1 103 ? 33.225  18.221  9.891   1.00 42.67  ? 103 TYR A CZ  1 
ATOM   897   O OH  . TYR A 1 103 ? 34.075  18.985  10.657  1.00 52.66  ? 103 TYR A OH  1 
ATOM   898   N N   . GLU A 1 104 ? 27.542  16.301  8.184   1.00 40.08  ? 104 GLU A N   1 
ATOM   899   C CA  . GLU A 1 104 ? 26.535  17.230  8.682   1.00 35.17  ? 104 GLU A CA  1 
ATOM   900   C C   . GLU A 1 104 ? 25.426  16.550  9.475   1.00 26.96  ? 104 GLU A C   1 
ATOM   901   O O   . GLU A 1 104 ? 24.571  17.248  10.029  1.00 26.06  ? 104 GLU A O   1 
ATOM   902   C CB  . GLU A 1 104 ? 25.929  18.013  7.515   1.00 34.18  ? 104 GLU A CB  1 
ATOM   903   C CG  . GLU A 1 104 ? 25.751  17.194  6.244   1.00 58.44  ? 104 GLU A CG  1 
ATOM   904   C CD  . GLU A 1 104 ? 24.480  16.363  6.256   1.00 59.48  ? 104 GLU A CD  1 
ATOM   905   O OE1 . GLU A 1 104 ? 24.537  15.178  5.861   1.00 42.43  ? 104 GLU A OE1 1 
ATOM   906   O OE2 . GLU A 1 104 ? 23.424  16.895  6.659   1.00 43.97  ? 104 GLU A OE2 1 
ATOM   907   N N   . LYS A 1 105 ? 25.411  15.224  9.541   1.00 25.19  ? 105 LYS A N   1 
ATOM   908   C CA  . LYS A 1 105 ? 24.375  14.538  10.295  1.00 18.76  ? 105 LYS A CA  1 
ATOM   909   C C   . LYS A 1 105 ? 24.623  14.697  11.794  1.00 18.90  ? 105 LYS A C   1 
ATOM   910   O O   . LYS A 1 105 ? 25.769  14.611  12.247  1.00 24.39  ? 105 LYS A O   1 
ATOM   911   C CB  . LYS A 1 105 ? 24.328  13.059  9.915   1.00 17.35  ? 105 LYS A CB  1 
ATOM   912   C CG  . LYS A 1 105 ? 24.176  12.830  8.421   1.00 20.50  ? 105 LYS A CG  1 
ATOM   913   C CD  . LYS A 1 105 ? 24.235  11.356  8.064   1.00 23.38  ? 105 LYS A CD  1 
ATOM   914   C CE  . LYS A 1 105 ? 23.996  11.146  6.576   1.00 19.09  ? 105 LYS A CE  1 
ATOM   915   N NZ  . LYS A 1 105 ? 24.009  9.703   6.205   1.00 17.35  ? 105 LYS A NZ  1 
ATOM   916   N N   . PRO A 1 106 ? 23.572  14.929  12.586  1.00 18.18  ? 106 PRO A N   1 
ATOM   917   C CA  . PRO A 1 106 ? 23.772  15.164  14.027  1.00 18.44  ? 106 PRO A CA  1 
ATOM   918   C C   . PRO A 1 106 ? 24.398  13.995  14.767  1.00 17.45  ? 106 PRO A C   1 
ATOM   919   O O   . PRO A 1 106 ? 24.936  14.196  15.863  1.00 17.90  ? 106 PRO A O   1 
ATOM   920   C CB  . PRO A 1 106 ? 22.352  15.447  14.533  1.00 18.64  ? 106 PRO A CB  1 
ATOM   921   C CG  . PRO A 1 106 ? 21.628  15.960  13.331  1.00 19.09  ? 106 PRO A CG  1 
ATOM   922   C CD  . PRO A 1 106 ? 22.180  15.178  12.175  1.00 18.32  ? 106 PRO A CD  1 
ATOM   923   N N   . ILE A 1 107 ? 24.345  12.777  14.215  1.00 16.31  ? 107 ILE A N   1 
ATOM   924   C CA  . ILE A 1 107 ? 24.969  11.633  14.877  1.00 20.23  ? 107 ILE A CA  1 
ATOM   925   C C   . ILE A 1 107 ? 26.465  11.557  14.626  1.00 25.26  ? 107 ILE A C   1 
ATOM   926   O O   . ILE A 1 107 ? 27.109  10.595  15.065  1.00 22.52  ? 107 ILE A O   1 
ATOM   927   C CB  . ILE A 1 107 ? 24.305  10.308  14.450  1.00 17.29  ? 107 ILE A CB  1 
ATOM   928   C CG1 . ILE A 1 107 ? 24.546  10.031  12.965  1.00 17.20  ? 107 ILE A CG1 1 
ATOM   929   C CG2 . ILE A 1 107 ? 22.815  10.337  14.756  1.00 17.32  ? 107 ILE A CG2 1 
ATOM   930   C CD1 . ILE A 1 107 ? 24.455  8.561   12.601  1.00 13.83  ? 107 ILE A CD1 1 
ATOM   931   N N   . TYR A 1 108 ? 27.040  12.539  13.933  1.00 21.26  ? 108 TYR A N   1 
ATOM   932   C CA  . TYR A 1 108 ? 28.481  12.628  13.739  1.00 18.62  ? 108 TYR A CA  1 
ATOM   933   C C   . TYR A 1 108 ? 29.079  13.855  14.416  1.00 22.70  ? 108 TYR A C   1 
ATOM   934   O O   . TYR A 1 108 ? 30.210  14.241  14.103  1.00 26.88  ? 108 TYR A O   1 
ATOM   935   C CB  . TYR A 1 108 ? 28.823  12.634  12.249  1.00 19.14  ? 108 TYR A CB  1 
ATOM   936   C CG  . TYR A 1 108 ? 29.049  11.260  11.670  1.00 16.60  ? 108 TYR A CG  1 
ATOM   937   C CD1 . TYR A 1 108 ? 27.991  10.380  11.491  1.00 17.41  ? 108 TYR A CD1 1 
ATOM   938   C CD2 . TYR A 1 108 ? 30.321  10.840  11.309  1.00 19.31  ? 108 TYR A CD2 1 
ATOM   939   C CE1 . TYR A 1 108 ? 28.192  9.119   10.964  1.00 20.00  ? 108 TYR A CE1 1 
ATOM   940   C CE2 . TYR A 1 108 ? 30.534  9.580   10.780  1.00 25.51  ? 108 TYR A CE2 1 
ATOM   941   C CZ  . TYR A 1 108 ? 29.464  8.724   10.609  1.00 23.32  ? 108 TYR A CZ  1 
ATOM   942   O OH  . TYR A 1 108 ? 29.667  7.468   10.084  1.00 21.09  ? 108 TYR A OH  1 
ATOM   943   N N   . ARG A 1 109 ? 28.344  14.482  15.331  1.00 27.02  ? 109 ARG A N   1 
ATOM   944   C CA  . ARG A 1 109 ? 28.835  15.685  16.002  1.00 26.94  ? 109 ARG A CA  1 
ATOM   945   C C   . ARG A 1 109 ? 29.802  15.270  17.101  1.00 28.79  ? 109 ARG A C   1 
ATOM   946   O O   . ARG A 1 109 ? 29.433  15.093  18.264  1.00 20.63  ? 109 ARG A O   1 
ATOM   947   C CB  . ARG A 1 109 ? 27.686  16.520  16.550  1.00 21.03  ? 109 ARG A CB  1 
ATOM   948   C CG  . ARG A 1 109 ? 27.787  17.990  16.168  1.00 26.16  ? 109 ARG A CG  1 
ATOM   949   C CD  . ARG A 1 109 ? 26.909  18.858  17.047  1.00 23.69  ? 109 ARG A CD  1 
ATOM   950   N NE  . ARG A 1 109 ? 25.536  18.372  17.079  1.00 22.82  ? 109 ARG A NE  1 
ATOM   951   C CZ  . ARG A 1 109 ? 24.636  18.611  16.136  1.00 24.86  ? 109 ARG A CZ  1 
ATOM   952   N NH1 . ARG A 1 109 ? 24.928  19.338  15.069  1.00 37.67  ? 109 ARG A NH1 1 
ATOM   953   N NH2 . ARG A 1 109 ? 23.409  18.110  16.267  1.00 23.11  ? 109 ARG A NH2 1 
ATOM   954   N N   . PHE A 1 110 ? 31.061  15.107  16.712  1.00 29.69  ? 110 PHE A N   1 
ATOM   955   C CA  . PHE A 1 110 ? 32.170  14.906  17.628  1.00 23.67  ? 110 PHE A CA  1 
ATOM   956   C C   . PHE A 1 110 ? 33.190  16.004  17.378  1.00 28.00  ? 110 PHE A C   1 
ATOM   957   O O   . PHE A 1 110 ? 33.473  16.344  16.225  1.00 32.53  ? 110 PHE A O   1 
ATOM   958   C CB  . PHE A 1 110 ? 32.824  13.535  17.429  1.00 24.69  ? 110 PHE A CB  1 
ATOM   959   C CG  . PHE A 1 110 ? 31.925  12.378  17.754  1.00 23.51  ? 110 PHE A CG  1 
ATOM   960   C CD1 . PHE A 1 110 ? 31.835  11.894  19.048  1.00 21.20  ? 110 PHE A CD1 1 
ATOM   961   C CD2 . PHE A 1 110 ? 31.171  11.775  16.763  1.00 24.17  ? 110 PHE A CD2 1 
ATOM   962   C CE1 . PHE A 1 110 ? 31.009  10.826  19.346  1.00 20.76  ? 110 PHE A CE1 1 
ATOM   963   C CE2 . PHE A 1 110 ? 30.343  10.710  17.052  1.00 23.05  ? 110 PHE A CE2 1 
ATOM   964   C CZ  . PHE A 1 110 ? 30.262  10.235  18.347  1.00 27.71  ? 110 PHE A CZ  1 
ATOM   965   N N   . GLU A 1 111 ? 33.731  16.575  18.456  1.00 24.13  ? 111 GLU A N   1 
ATOM   966   C CA  . GLU A 1 111 ? 34.785  17.567  18.285  1.00 29.71  ? 111 GLU A CA  1 
ATOM   967   C C   . GLU A 1 111 ? 36.014  16.945  17.640  1.00 33.75  ? 111 GLU A C   1 
ATOM   968   O O   . GLU A 1 111 ? 36.701  17.591  16.840  1.00 37.10  ? 111 GLU A O   1 
ATOM   969   C CB  . GLU A 1 111 ? 35.138  18.207  19.627  1.00 32.03  ? 111 GLU A CB  1 
ATOM   970   C CG  . GLU A 1 111 ? 36.076  19.402  19.510  1.00 41.66  ? 111 GLU A CG  1 
ATOM   971   C CD  . GLU A 1 111 ? 35.486  20.543  18.697  1.00 54.54  ? 111 GLU A CD  1 
ATOM   972   O OE1 . GLU A 1 111 ? 34.245  20.618  18.571  1.00 54.28  ? 111 GLU A OE1 1 
ATOM   973   O OE2 . GLU A 1 111 ? 36.270  21.364  18.176  1.00 52.67  ? 111 GLU A OE2 1 
ATOM   974   N N   . ARG A 1 112 ? 36.304  15.686  17.973  1.00 29.95  ? 112 ARG A N   1 
ATOM   975   C CA  . ARG A 1 112 ? 37.421  14.985  17.348  1.00 30.72  ? 112 ARG A CA  1 
ATOM   976   C C   . ARG A 1 112 ? 37.215  14.862  15.841  1.00 30.05  ? 112 ARG A C   1 
ATOM   977   O O   . ARG A 1 112 ? 38.107  15.198  15.055  1.00 37.03  ? 112 ARG A O   1 
ATOM   978   C CB  . ARG A 1 112 ? 37.594  13.611  18.001  1.00 25.21  ? 112 ARG A CB  1 
ATOM   979   C CG  . ARG A 1 112 ? 38.818  12.819  17.560  1.00 24.00  ? 112 ARG A CG  1 
ATOM   980   C CD  . ARG A 1 112 ? 40.131  13.565  17.765  1.00 32.57  ? 112 ARG A CD  1 
ATOM   981   N NE  . ARG A 1 112 ? 41.277  12.666  17.671  1.00 37.85  ? 112 ARG A NE  1 
ATOM   982   C CZ  . ARG A 1 112 ? 42.499  13.037  17.313  1.00 33.07  ? 112 ARG A CZ  1 
ATOM   983   N NH1 . ARG A 1 112 ? 42.778  14.294  17.008  1.00 32.12  ? 112 ARG A NH1 1 
ATOM   984   N NH2 . ARG A 1 112 ? 43.465  12.123  17.256  1.00 27.72  ? 112 ARG A NH2 1 
ATOM   985   N N   . ILE A 1 113 ? 36.023  14.427  15.417  1.00 22.91  ? 113 ILE A N   1 
ATOM   986   C CA  . ILE A 1 113 ? 35.742  14.293  13.987  1.00 26.65  ? 113 ILE A CA  1 
ATOM   987   C C   . ILE A 1 113 ? 35.906  15.634  13.282  1.00 33.16  ? 113 ILE A C   1 
ATOM   988   O O   . ILE A 1 113 ? 36.406  15.703  12.152  1.00 33.56  ? 113 ILE A O   1 
ATOM   989   C CB  . ILE A 1 113 ? 34.336  13.701  13.762  1.00 21.40  ? 113 ILE A CB  1 
ATOM   990   C CG1 . ILE A 1 113 ? 34.380  12.176  13.823  1.00 25.13  ? 113 ILE A CG1 1 
ATOM   991   C CG2 . ILE A 1 113 ? 33.758  14.140  12.422  1.00 24.69  ? 113 ILE A CG2 1 
ATOM   992   C CD1 . ILE A 1 113 ? 33.015  11.526  13.742  1.00 29.73  ? 113 ILE A CD1 1 
ATOM   993   N N   . ARG A 1 114 ? 35.499  16.722  13.942  1.00 37.18  ? 114 ARG A N   1 
ATOM   994   C CA  . ARG A 1 114 ? 35.736  18.053  13.393  1.00 34.96  ? 114 ARG A CA  1 
ATOM   995   C C   . ARG A 1 114 ? 37.221  18.291  13.149  1.00 36.16  ? 114 ARG A C   1 
ATOM   996   O O   . ARG A 1 114 ? 37.601  18.953  12.175  1.00 43.32  ? 114 ARG A O   1 
ATOM   997   C CB  . ARG A 1 114 ? 35.168  19.113  14.337  1.00 39.07  ? 114 ARG A CB  1 
ATOM   998   C CG  . ARG A 1 114 ? 34.761  20.408  13.653  1.00 38.63  ? 114 ARG A CG  1 
ATOM   999   C CD  . ARG A 1 114 ? 33.350  20.818  14.045  1.00 40.61  ? 114 ARG A CD  1 
ATOM   1000  N NE  . ARG A 1 114 ? 32.363  19.820  13.647  1.00 61.93  ? 114 ARG A NE  1 
ATOM   1001  C CZ  . ARG A 1 114 ? 31.336  19.444  14.396  1.00 57.30  ? 114 ARG A CZ  1 
ATOM   1002  N NH1 . ARG A 1 114 ? 31.125  19.967  15.593  1.00 54.33  ? 114 ARG A NH1 1 
ATOM   1003  N NH2 . ARG A 1 114 ? 30.500  18.518  13.932  1.00 45.92  ? 114 ARG A NH2 1 
ATOM   1004  N N   . GLU A 1 115 ? 38.078  17.753  14.022  1.00 28.80  ? 115 GLU A N   1 
ATOM   1005  C CA  . GLU A 1 115 ? 39.515  17.978  13.897  1.00 30.00  ? 115 GLU A CA  1 
ATOM   1006  C C   . GLU A 1 115 ? 40.149  17.100  12.821  1.00 28.70  ? 115 GLU A C   1 
ATOM   1007  O O   . GLU A 1 115 ? 40.986  17.581  12.050  1.00 33.28  ? 115 GLU A O   1 
ATOM   1008  C CB  . GLU A 1 115 ? 40.202  17.751  15.242  1.00 29.31  ? 115 GLU A CB  1 
ATOM   1009  C CG  . GLU A 1 115 ? 39.772  18.740  16.313  1.00 36.87  ? 115 GLU A CG  1 
ATOM   1010  C CD  . GLU A 1 115 ? 40.159  18.295  17.706  1.00 38.20  ? 115 GLU A CD  1 
ATOM   1011  O OE1 . GLU A 1 115 ? 41.151  17.544  17.835  1.00 46.75  ? 115 GLU A OE1 1 
ATOM   1012  O OE2 . GLU A 1 115 ? 39.473  18.689  18.671  1.00 38.05  ? 115 GLU A OE2 1 
ATOM   1013  N N   . LEU A 1 116 ? 39.778  15.815  12.748  1.00 31.80  ? 116 LEU A N   1 
ATOM   1014  C CA  . LEU A 1 116 ? 40.398  14.937  11.753  1.00 28.84  ? 116 LEU A CA  1 
ATOM   1015  C C   . LEU A 1 116 ? 40.116  15.412  10.334  1.00 33.04  ? 116 LEU A C   1 
ATOM   1016  O O   . LEU A 1 116 ? 41.002  15.374  9.471   1.00 32.43  ? 116 LEU A O   1 
ATOM   1017  C CB  . LEU A 1 116 ? 39.931  13.488  11.897  1.00 25.32  ? 116 LEU A CB  1 
ATOM   1018  C CG  . LEU A 1 116 ? 40.422  12.581  13.030  1.00 30.48  ? 116 LEU A CG  1 
ATOM   1019  C CD1 . LEU A 1 116 ? 41.900  12.802  13.334  1.00 32.14  ? 116 LEU A CD1 1 
ATOM   1020  C CD2 . LEU A 1 116 ? 39.574  12.708  14.262  1.00 29.94  ? 116 LEU A CD2 1 
ATOM   1021  N N   . MET A 1 117 ? 38.883  15.843  10.065  1.00 31.53  ? 117 MET A N   1 
ATOM   1022  C CA  . MET A 1 117 ? 38.540  16.260  8.711   1.00 29.76  ? 117 MET A CA  1 
ATOM   1023  C C   . MET A 1 117 ? 39.290  17.519  8.300   1.00 42.86  ? 117 MET A C   1 
ATOM   1024  O O   . MET A 1 117 ? 39.536  17.729  7.108   1.00 42.36  ? 117 MET A O   1 
ATOM   1025  C CB  . MET A 1 117 ? 37.031  16.462  8.595   1.00 28.32  ? 117 MET A CB  1 
ATOM   1026  C CG  . MET A 1 117 ? 36.231  15.204  8.881   1.00 36.87  ? 117 MET A CG  1 
ATOM   1027  S SD  . MET A 1 117 ? 36.972  13.723  8.159   1.00 37.41  ? 117 MET A SD  1 
ATOM   1028  C CE  . MET A 1 117 ? 36.942  14.117  6.408   1.00 33.68  ? 117 MET A CE  1 
ATOM   1029  N N   . ASN A 1 118 ? 39.663  18.362  9.261   1.00 43.28  ? 118 ASN A N   1 
ATOM   1030  C CA  . ASN A 1 118 ? 40.461  19.544  8.972   1.00 40.26  ? 118 ASN A CA  1 
ATOM   1031  C C   . ASN A 1 118 ? 41.957  19.261  8.950   1.00 38.70  ? 118 ASN A C   1 
ATOM   1032  O O   . ASN A 1 118 ? 42.736  20.157  8.607   1.00 42.82  ? 118 ASN A O   1 
ATOM   1033  C CB  . ASN A 1 118 ? 40.163  20.647  9.993   1.00 40.21  ? 118 ASN A CB  1 
ATOM   1034  C CG  . ASN A 1 118 ? 38.939  21.463  9.627   1.00 45.46  ? 118 ASN A CG  1 
ATOM   1035  O OD1 . ASN A 1 118 ? 37.921  20.920  9.196   1.00 36.21  ? 118 ASN A OD1 1 
ATOM   1036  N ND2 . ASN A 1 118 ? 39.033  22.778  9.791   1.00 49.33  ? 118 ASN A ND2 1 
ATOM   1037  N N   . LYS A 1 119 ? 42.375  18.050  9.302   1.00 40.98  ? 119 LYS A N   1 
ATOM   1038  C CA  . LYS A 1 119 ? 43.785  17.701  9.267   1.00 44.81  ? 119 LYS A CA  1 
ATOM   1039  C C   . LYS A 1 119 ? 44.234  17.412  7.837   1.00 50.85  ? 119 LYS A C   1 
ATOM   1040  O O   . LYS A 1 119 ? 43.428  17.135  6.945   1.00 55.54  ? 119 LYS A O   1 
ATOM   1041  C CB  . LYS A 1 119 ? 44.062  16.492  10.158  1.00 42.95  ? 119 LYS A CB  1 
ATOM   1042  C CG  . LYS A 1 119 ? 45.171  16.718  11.166  1.00 49.71  ? 119 LYS A CG  1 
ATOM   1043  C CD  . LYS A 1 119 ? 45.315  15.530  12.093  1.00 45.19  ? 119 LYS A CD  1 
ATOM   1044  C CE  . LYS A 1 119 ? 44.263  15.551  13.186  1.00 48.15  ? 119 LYS A CE  1 
ATOM   1045  N NZ  . LYS A 1 119 ? 44.480  16.674  14.139  1.00 59.31  ? 119 LYS A NZ  1 
ATOM   1046  N N   . GLU A 1 120 ? 45.549  17.477  7.628   1.00 53.12  ? 120 GLU A N   1 
ATOM   1047  C CA  . GLU A 1 120 ? 46.119  17.255  6.305   1.00 50.66  ? 120 GLU A CA  1 
ATOM   1048  C C   . GLU A 1 120 ? 46.415  15.779  6.050   1.00 43.95  ? 120 GLU A C   1 
ATOM   1049  O O   . GLU A 1 120 ? 45.935  15.215  5.063   1.00 54.04  ? 120 GLU A O   1 
ATOM   1050  C CB  . GLU A 1 120 ? 47.389  18.093  6.135   1.00 60.14  ? 120 GLU A CB  1 
ATOM   1051  C CG  . GLU A 1 120 ? 47.228  19.549  6.548   1.00 80.05  ? 120 GLU A CG  1 
ATOM   1052  C CD  . GLU A 1 120 ? 47.740  19.820  7.949   1.00 92.50  ? 120 GLU A CD  1 
ATOM   1053  O OE1 . GLU A 1 120 ? 47.596  18.933  8.817   1.00 80.80  ? 120 GLU A OE1 1 
ATOM   1054  O OE2 . GLU A 1 120 ? 48.288  20.919  8.181   1.00 89.78  ? 120 GLU A OE2 1 
ATOM   1055  N N   . LYS A 1 121 ? 47.190  15.144  6.929   1.00 36.51  ? 121 LYS A N   1 
ATOM   1056  C CA  . LYS A 1 121 ? 47.520  13.727  6.815   1.00 42.17  ? 121 LYS A CA  1 
ATOM   1057  C C   . LYS A 1 121 ? 47.369  13.075  8.182   1.00 44.37  ? 121 LYS A C   1 
ATOM   1058  O O   . LYS A 1 121 ? 47.861  13.608  9.182   1.00 47.05  ? 121 LYS A O   1 
ATOM   1059  C CB  . LYS A 1 121 ? 48.943  13.529  6.275   1.00 58.95  ? 121 LYS A CB  1 
ATOM   1060  C CG  . LYS A 1 121 ? 49.015  12.811  4.927   1.00 64.88  ? 121 LYS A CG  1 
ATOM   1061  C CD  . LYS A 1 121 ? 48.147  13.500  3.885   1.00 38.67  ? 121 LYS A CD  1 
ATOM   1062  C CE  . LYS A 1 121 ? 48.728  13.401  2.484   1.00 51.41  ? 121 LYS A CE  1 
ATOM   1063  N NZ  . LYS A 1 121 ? 47.647  13.340  1.458   1.00 41.01  ? 121 LYS A NZ  1 
ATOM   1064  N N   . LEU A 1 122 ? 46.704  11.922  8.220   1.00 43.19  ? 122 LEU A N   1 
ATOM   1065  C CA  . LEU A 1 122 ? 46.313  11.273  9.466   1.00 39.84  ? 122 LEU A CA  1 
ATOM   1066  C C   . LEU A 1 122 ? 47.319  10.192  9.848   1.00 35.76  ? 122 LEU A C   1 
ATOM   1067  O O   . LEU A 1 122 ? 47.692  9.363   9.010   1.00 34.73  ? 122 LEU A O   1 
ATOM   1068  C CB  . LEU A 1 122 ? 44.914  10.662  9.340   1.00 38.67  ? 122 LEU A CB  1 
ATOM   1069  C CG  . LEU A 1 122 ? 43.706  11.445  9.866   1.00 31.51  ? 122 LEU A CG  1 
ATOM   1070  C CD1 . LEU A 1 122 ? 43.788  12.919  9.497   1.00 36.74  ? 122 LEU A CD1 1 
ATOM   1071  C CD2 . LEU A 1 122 ? 42.408  10.835  9.353   1.00 26.63  ? 122 LEU A CD2 1 
ATOM   1072  N N   . ASN A 1 123 ? 47.746  10.194  11.113  1.00 37.38  ? 123 ASN A N   1 
ATOM   1073  C CA  . ASN A 1 123 ? 48.668  9.182   11.609  1.00 32.41  ? 123 ASN A CA  1 
ATOM   1074  C C   . ASN A 1 123 ? 47.896  7.992   12.182  1.00 32.15  ? 123 ASN A C   1 
ATOM   1075  O O   . ASN A 1 123 ? 46.663  7.966   12.193  1.00 36.20  ? 123 ASN A O   1 
ATOM   1076  C CB  . ASN A 1 123 ? 49.632  9.777   12.637  1.00 35.79  ? 123 ASN A CB  1 
ATOM   1077  C CG  . ASN A 1 123 ? 48.927  10.379  13.842  1.00 38.96  ? 123 ASN A CG  1 
ATOM   1078  O OD1 . ASN A 1 123 ? 48.053  9.759   14.449  1.00 35.53  ? 123 ASN A OD1 1 
ATOM   1079  N ND2 . ASN A 1 123 ? 49.333  11.588  14.213  1.00 44.26  ? 123 ASN A ND2 1 
ATOM   1080  N N   . ARG A 1 124 ? 48.638  6.994   12.678  1.00 33.47  ? 124 ARG A N   1 
ATOM   1081  C CA  . ARG A 1 124 ? 48.016  5.736   13.086  1.00 30.28  ? 124 ARG A CA  1 
ATOM   1082  C C   . ARG A 1 124 ? 47.011  5.946   14.210  1.00 28.95  ? 124 ARG A C   1 
ATOM   1083  O O   . ARG A 1 124 ? 45.939  5.331   14.217  1.00 34.50  ? 124 ARG A O   1 
ATOM   1084  C CB  . ARG A 1 124 ? 49.078  4.724   13.518  1.00 35.94  ? 124 ARG A CB  1 
ATOM   1085  C CG  . ARG A 1 124 ? 48.495  3.344   13.808  1.00 36.76  ? 124 ARG A CG  1 
ATOM   1086  C CD  . ARG A 1 124 ? 49.278  2.578   14.864  1.00 37.95  ? 124 ARG A CD  1 
ATOM   1087  N NE  . ARG A 1 124 ? 48.521  1.435   15.367  1.00 31.23  ? 124 ARG A NE  1 
ATOM   1088  C CZ  . ARG A 1 124 ? 47.951  1.377   16.563  1.00 30.30  ? 124 ARG A CZ  1 
ATOM   1089  N NH1 . ARG A 1 124 ? 48.055  2.373   17.429  1.00 30.47  ? 124 ARG A NH1 1 
ATOM   1090  N NH2 . ARG A 1 124 ? 47.259  0.291   16.900  1.00 29.70  ? 124 ARG A NH2 1 
ATOM   1091  N N   . GLU A 1 125 ? 47.341  6.802   15.176  1.00 30.78  ? 125 GLU A N   1 
ATOM   1092  C CA  . GLU A 1 125 ? 46.394  7.070   16.251  1.00 37.76  ? 125 GLU A CA  1 
ATOM   1093  C C   . GLU A 1 125 ? 45.230  7.927   15.771  1.00 35.34  ? 125 GLU A C   1 
ATOM   1094  O O   . GLU A 1 125 ? 44.109  7.780   16.270  1.00 34.33  ? 125 GLU A O   1 
ATOM   1095  C CB  . GLU A 1 125 ? 47.111  7.725   17.432  1.00 33.81  ? 125 GLU A CB  1 
ATOM   1096  C CG  . GLU A 1 125 ? 48.459  7.087   17.750  1.00 41.31  ? 125 GLU A CG  1 
ATOM   1097  C CD  . GLU A 1 125 ? 48.380  5.575   17.907  1.00 57.14  ? 125 GLU A CD  1 
ATOM   1098  O OE1 . GLU A 1 125 ? 47.372  5.074   18.451  1.00 61.99  ? 125 GLU A OE1 1 
ATOM   1099  O OE2 . GLU A 1 125 ? 49.327  4.886   17.471  1.00 53.68  ? 125 GLU A OE2 1 
ATOM   1100  N N   . GLU A 1 126 ? 45.467  8.817   14.804  1.00 39.96  ? 126 GLU A N   1 
ATOM   1101  C CA  . GLU A 1 126 ? 44.369  9.586   14.227  1.00 35.03  ? 126 GLU A CA  1 
ATOM   1102  C C   . GLU A 1 126 ? 43.443  8.700   13.400  1.00 25.66  ? 126 GLU A C   1 
ATOM   1103  O O   . GLU A 1 126 ? 42.218  8.860   13.448  1.00 25.73  ? 126 GLU A O   1 
ATOM   1104  C CB  . GLU A 1 126 ? 44.915  10.733  13.379  1.00 33.87  ? 126 GLU A CB  1 
ATOM   1105  C CG  . GLU A 1 126 ? 45.511  11.864  14.196  1.00 42.16  ? 126 GLU A CG  1 
ATOM   1106  C CD  . GLU A 1 126 ? 46.591  12.611  13.448  1.00 50.26  ? 126 GLU A CD  1 
ATOM   1107  O OE1 . GLU A 1 126 ? 46.519  12.668  12.206  1.00 53.88  ? 126 GLU A OE1 1 
ATOM   1108  O OE2 . GLU A 1 126 ? 47.516  13.138  14.100  1.00 54.00  ? 126 GLU A OE2 1 
ATOM   1109  N N   . LEU A 1 127 ? 44.008  7.767   12.630  1.00 26.46  ? 127 LEU A N   1 
ATOM   1110  C CA  . LEU A 1 127 ? 43.174  6.818   11.899  1.00 25.05  ? 127 LEU A CA  1 
ATOM   1111  C C   . LEU A 1 127 ? 42.417  5.899   12.849  1.00 23.75  ? 127 LEU A C   1 
ATOM   1112  O O   . LEU A 1 127 ? 41.297  5.477   12.540  1.00 27.61  ? 127 LEU A O   1 
ATOM   1113  C CB  . LEU A 1 127 ? 44.023  5.996   10.927  1.00 27.83  ? 127 LEU A CB  1 
ATOM   1114  C CG  . LEU A 1 127 ? 44.657  6.751   9.756   1.00 27.80  ? 127 LEU A CG  1 
ATOM   1115  C CD1 . LEU A 1 127 ? 45.812  5.955   9.167   1.00 28.58  ? 127 LEU A CD1 1 
ATOM   1116  C CD2 . LEU A 1 127 ? 43.613  7.058   8.695   1.00 26.49  ? 127 LEU A CD2 1 
ATOM   1117  N N   . LEU A 1 128 ? 43.015  5.573   13.999  1.00 26.83  ? 128 LEU A N   1 
ATOM   1118  C CA  . LEU A 1 128 ? 42.299  4.807   15.013  1.00 24.89  ? 128 LEU A CA  1 
ATOM   1119  C C   . LEU A 1 128 ? 41.090  5.574   15.526  1.00 27.17  ? 128 LEU A C   1 
ATOM   1120  O O   . LEU A 1 128 ? 40.002  5.004   15.685  1.00 22.07  ? 128 LEU A O   1 
ATOM   1121  C CB  . LEU A 1 128 ? 43.241  4.457   16.165  1.00 24.48  ? 128 LEU A CB  1 
ATOM   1122  C CG  . LEU A 1 128 ? 43.610  2.984   16.324  1.00 24.86  ? 128 LEU A CG  1 
ATOM   1123  C CD1 . LEU A 1 128 ? 44.403  2.750   17.602  1.00 26.04  ? 128 LEU A CD1 1 
ATOM   1124  C CD2 . LEU A 1 128 ? 42.358  2.124   16.307  1.00 24.79  ? 128 LEU A CD2 1 
ATOM   1125  N N   . ASP A 1 129 ? 41.260  6.870   15.786  1.00 27.31  ? 129 ASP A N   1 
ATOM   1126  C CA  . ASP A 1 129 ? 40.139  7.687   16.234  1.00 22.11  ? 129 ASP A CA  1 
ATOM   1127  C C   . ASP A 1 129 ? 39.074  7.802   15.150  1.00 21.07  ? 129 ASP A C   1 
ATOM   1128  O O   . ASP A 1 129 ? 37.875  7.835   15.452  1.00 23.38  ? 129 ASP A O   1 
ATOM   1129  C CB  . ASP A 1 129 ? 40.640  9.071   16.653  1.00 23.88  ? 129 ASP A CB  1 
ATOM   1130  C CG  . ASP A 1 129 ? 41.493  9.026   17.907  1.00 36.40  ? 129 ASP A CG  1 
ATOM   1131  O OD1 . ASP A 1 129 ? 42.120  7.978   18.162  1.00 38.43  ? 129 ASP A OD1 1 
ATOM   1132  O OD2 . ASP A 1 129 ? 41.546  10.042  18.631  1.00 33.22  ? 129 ASP A OD2 1 
ATOM   1133  N N   . LEU A 1 130 ? 39.491  7.863   13.883  1.00 24.85  ? 130 LEU A N   1 
ATOM   1134  C CA  . LEU A 1 130 ? 38.523  7.951   12.792  1.00 20.66  ? 130 LEU A CA  1 
ATOM   1135  C C   . LEU A 1 130 ? 37.792  6.630   12.585  1.00 19.60  ? 130 LEU A C   1 
ATOM   1136  O O   . LEU A 1 130 ? 36.577  6.618   12.354  1.00 20.07  ? 130 LEU A O   1 
ATOM   1137  C CB  . LEU A 1 130 ? 39.215  8.386   11.502  1.00 21.64  ? 130 LEU A CB  1 
ATOM   1138  C CG  . LEU A 1 130 ? 38.236  8.746   10.383  1.00 21.22  ? 130 LEU A CG  1 
ATOM   1139  C CD1 . LEU A 1 130 ? 37.329  9.888   10.817  1.00 20.94  ? 130 LEU A CD1 1 
ATOM   1140  C CD2 . LEU A 1 130 ? 38.973  9.096   9.102   1.00 25.39  ? 130 LEU A CD2 1 
ATOM   1141  N N   . GLN A 1 131 ? 38.515  5.509   12.650  1.00 19.92  ? 131 GLN A N   1 
ATOM   1142  C CA  . GLN A 1 131 ? 37.862  4.205   12.580  1.00 19.14  ? 131 GLN A CA  1 
ATOM   1143  C C   . GLN A 1 131 ? 36.827  4.062   13.687  1.00 21.08  ? 131 GLN A C   1 
ATOM   1144  O O   . GLN A 1 131 ? 35.686  3.649   13.443  1.00 20.70  ? 131 GLN A O   1 
ATOM   1145  C CB  . GLN A 1 131 ? 38.899  3.086   12.693  1.00 19.96  ? 131 GLN A CB  1 
ATOM   1146  C CG  . GLN A 1 131 ? 39.745  2.849   11.459  1.00 20.91  ? 131 GLN A CG  1 
ATOM   1147  C CD  . GLN A 1 131 ? 40.825  1.803   11.687  1.00 27.38  ? 131 GLN A CD  1 
ATOM   1148  O OE1 . GLN A 1 131 ? 41.239  1.555   12.821  1.00 24.87  ? 131 GLN A OE1 1 
ATOM   1149  N NE2 . GLN A 1 131 ? 41.282  1.182   10.607  1.00 27.60  ? 131 GLN A NE2 1 
ATOM   1150  N N   . THR A 1 132 ? 37.209  4.418   14.914  1.00 19.79  ? 132 THR A N   1 
ATOM   1151  C CA  . THR A 1 132 ? 36.366  4.144   16.072  1.00 18.09  ? 132 THR A CA  1 
ATOM   1152  C C   . THR A 1 132 ? 35.163  5.078   16.127  1.00 21.76  ? 132 THR A C   1 
ATOM   1153  O O   . THR A 1 132 ? 34.053  4.647   16.461  1.00 27.42  ? 132 THR A O   1 
ATOM   1154  C CB  . THR A 1 132 ? 37.197  4.259   17.348  1.00 19.05  ? 132 THR A CB  1 
ATOM   1155  O OG1 . THR A 1 132 ? 38.391  3.481   17.202  1.00 21.57  ? 132 THR A OG1 1 
ATOM   1156  C CG2 . THR A 1 132 ? 36.411  3.748   18.542  1.00 26.88  ? 132 THR A CG2 1 
ATOM   1157  N N   . LEU A 1 133 ? 35.359  6.361   15.808  1.00 20.80  ? 133 LEU A N   1 
ATOM   1158  C CA  . LEU A 1 133 ? 34.244  7.301   15.855  1.00 19.23  ? 133 LEU A CA  1 
ATOM   1159  C C   . LEU A 1 133 ? 33.202  6.997   14.786  1.00 21.51  ? 133 LEU A C   1 
ATOM   1160  O O   . LEU A 1 133 ? 32.010  7.241   15.001  1.00 24.93  ? 133 LEU A O   1 
ATOM   1161  C CB  . LEU A 1 133 ? 34.757  8.731   15.722  1.00 18.21  ? 133 LEU A CB  1 
ATOM   1162  C CG  . LEU A 1 133 ? 35.292  9.282   17.040  1.00 19.09  ? 133 LEU A CG  1 
ATOM   1163  C CD1 . LEU A 1 133 ? 36.132  10.519  16.808  1.00 23.88  ? 133 LEU A CD1 1 
ATOM   1164  C CD2 . LEU A 1 133 ? 34.144  9.574   17.989  1.00 20.73  ? 133 LEU A CD2 1 
ATOM   1165  N N   . ASN A 1 134 ? 33.629  6.475   13.634  1.00 21.86  ? 134 ASN A N   1 
ATOM   1166  C CA  . ASN A 1 134 ? 32.669  6.021   12.634  1.00 18.99  ? 134 ASN A CA  1 
ATOM   1167  C C   . ASN A 1 134 ? 31.797  4.895   13.172  1.00 20.82  ? 134 ASN A C   1 
ATOM   1168  O O   . ASN A 1 134 ? 30.629  4.777   12.786  1.00 24.79  ? 134 ASN A O   1 
ATOM   1169  C CB  . ASN A 1 134 ? 33.401  5.570   11.368  1.00 18.00  ? 134 ASN A CB  1 
ATOM   1170  C CG  . ASN A 1 134 ? 33.293  6.578   10.241  1.00 21.56  ? 134 ASN A CG  1 
ATOM   1171  O OD1 . ASN A 1 134 ? 32.207  6.823   9.715   1.00 18.21  ? 134 ASN A OD1 1 
ATOM   1172  N ND2 . ASN A 1 134 ? 34.422  7.165   9.859   1.00 27.29  ? 134 ASN A ND2 1 
ATOM   1173  N N   . LEU A 1 135 ? 32.344  4.054   14.052  1.00 17.30  ? 135 LEU A N   1 
ATOM   1174  C CA  . LEU A 1 135 ? 31.543  3.020   14.698  1.00 14.81  ? 135 LEU A CA  1 
ATOM   1175  C C   . LEU A 1 135 ? 30.620  3.613   15.757  1.00 24.19  ? 135 LEU A C   1 
ATOM   1176  O O   . LEU A 1 135 ? 29.427  3.292   15.802  1.00 21.58  ? 135 LEU A O   1 
ATOM   1177  C CB  . LEU A 1 135 ? 32.456  1.966   15.327  1.00 17.13  ? 135 LEU A CB  1 
ATOM   1178  C CG  . LEU A 1 135 ? 33.113  0.963   14.384  1.00 15.49  ? 135 LEU A CG  1 
ATOM   1179  C CD1 . LEU A 1 135 ? 33.810  -0.123  15.186  1.00 16.20  ? 135 LEU A CD1 1 
ATOM   1180  C CD2 . LEU A 1 135 ? 32.086  0.366   13.436  1.00 14.84  ? 135 LEU A CD2 1 
ATOM   1181  N N   . LEU A 1 136 ? 31.159  4.485   16.613  1.00 20.67  ? 136 LEU A N   1 
ATOM   1182  C CA  . LEU A 1 136 ? 30.383  5.040   17.713  1.00 15.30  ? 136 LEU A CA  1 
ATOM   1183  C C   . LEU A 1 136 ? 29.276  5.969   17.235  1.00 16.43  ? 136 LEU A C   1 
ATOM   1184  O O   . LEU A 1 136 ? 28.303  6.182   17.966  1.00 19.28  ? 136 LEU A O   1 
ATOM   1185  C CB  . LEU A 1 136 ? 31.306  5.784   18.677  1.00 26.59  ? 136 LEU A CB  1 
ATOM   1186  C CG  . LEU A 1 136 ? 32.389  4.928   19.335  1.00 22.44  ? 136 LEU A CG  1 
ATOM   1187  C CD1 . LEU A 1 136 ? 33.253  5.776   20.248  1.00 17.75  ? 136 LEU A CD1 1 
ATOM   1188  C CD2 . LEU A 1 136 ? 31.767  3.772   20.098  1.00 20.88  ? 136 LEU A CD2 1 
ATOM   1189  N N   . ALA A 1 137 ? 29.406  6.525   16.030  1.00 22.04  ? 137 ALA A N   1 
ATOM   1190  C CA  . ALA A 1 137 ? 28.376  7.415   15.508  1.00 24.68  ? 137 ALA A CA  1 
ATOM   1191  C C   . ALA A 1 137 ? 27.061  6.681   15.277  1.00 21.09  ? 137 ALA A C   1 
ATOM   1192  O O   . ALA A 1 137 ? 25.987  7.275   15.423  1.00 27.88  ? 137 ALA A O   1 
ATOM   1193  C CB  . ALA A 1 137 ? 28.859  8.065   14.213  1.00 21.75  ? 137 ALA A CB  1 
ATOM   1194  N N   . TRP A 1 138 ? 27.123  5.398   14.929  1.00 15.11  ? 138 TRP A N   1 
ATOM   1195  C CA  . TRP A 1 138 ? 25.940  4.596   14.640  1.00 18.07  ? 138 TRP A CA  1 
ATOM   1196  C C   . TRP A 1 138 ? 25.520  3.747   15.832  1.00 17.73  ? 138 TRP A C   1 
ATOM   1197  O O   . TRP A 1 138 ? 25.032  2.626   15.663  1.00 20.83  ? 138 TRP A O   1 
ATOM   1198  C CB  . TRP A 1 138 ? 26.184  3.726   13.408  1.00 19.14  ? 138 TRP A CB  1 
ATOM   1199  C CG  . TRP A 1 138 ? 26.599  4.534   12.216  1.00 17.97  ? 138 TRP A CG  1 
ATOM   1200  C CD1 . TRP A 1 138 ? 27.818  5.104   12.001  1.00 20.24  ? 138 TRP A CD1 1 
ATOM   1201  C CD2 . TRP A 1 138 ? 25.787  4.887   11.091  1.00 15.91  ? 138 TRP A CD2 1 
ATOM   1202  N NE1 . TRP A 1 138 ? 27.820  5.784   10.808  1.00 13.41  ? 138 TRP A NE1 1 
ATOM   1203  C CE2 . TRP A 1 138 ? 26.584  5.665   10.230  1.00 13.02  ? 138 TRP A CE2 1 
ATOM   1204  C CE3 . TRP A 1 138 ? 24.467  4.615   10.727  1.00 21.60  ? 138 TRP A CE3 1 
ATOM   1205  C CZ2 . TRP A 1 138 ? 26.105  6.174   9.028   1.00 22.04  ? 138 TRP A CZ2 1 
ATOM   1206  C CZ3 . TRP A 1 138 ? 23.992  5.121   9.535   1.00 17.57  ? 138 TRP A CZ3 1 
ATOM   1207  C CH2 . TRP A 1 138 ? 24.809  5.892   8.699   1.00 18.17  ? 138 TRP A CH2 1 
ATOM   1208  N N   . CYS A 1 139 ? 25.705  4.267   17.041  1.00 17.70  ? 139 CYS A N   1 
ATOM   1209  C CA  . CYS A 1 139 ? 25.406  3.527   18.260  1.00 21.68  ? 139 CYS A CA  1 
ATOM   1210  C C   . CYS A 1 139 ? 23.917  3.637   18.574  1.00 25.71  ? 139 CYS A C   1 
ATOM   1211  O O   . CYS A 1 139 ? 23.389  4.743   18.735  1.00 32.78  ? 139 CYS A O   1 
ATOM   1212  C CB  . CYS A 1 139 ? 26.245  4.064   19.417  1.00 21.69  ? 139 CYS A CB  1 
ATOM   1213  S SG  . CYS A 1 139 ? 26.541  2.893   20.759  1.00 24.51  ? 139 CYS A SG  1 
ATOM   1214  N N   . GLY A 1 140 ? 23.245  2.494   18.672  1.00 26.64  ? 140 GLY A N   1 
ATOM   1215  C CA  . GLY A 1 140 ? 21.829  2.482   18.974  1.00 24.64  ? 140 GLY A CA  1 
ATOM   1216  C C   . GLY A 1 140 ? 21.546  2.889   20.406  1.00 21.57  ? 140 GLY A C   1 
ATOM   1217  O O   . GLY A 1 140 ? 22.446  3.083   21.224  1.00 30.45  ? 140 GLY A O   1 
ATOM   1218  N N   . ARG A 1 141 ? 20.252  3.015   20.711  1.00 20.66  ? 141 ARG A N   1 
ATOM   1219  C CA  . ARG A 1 141 ? 19.846  3.481   22.035  1.00 23.86  ? 141 ARG A CA  1 
ATOM   1220  C C   . ARG A 1 141 ? 20.323  2.535   23.130  1.00 26.30  ? 141 ARG A C   1 
ATOM   1221  O O   . ARG A 1 141 ? 20.751  2.979   24.203  1.00 23.47  ? 141 ARG A O   1 
ATOM   1222  C CB  . ARG A 1 141 ? 18.326  3.644   22.098  1.00 18.38  ? 141 ARG A CB  1 
ATOM   1223  C CG  . ARG A 1 141 ? 17.816  4.050   23.472  1.00 25.87  ? 141 ARG A CG  1 
ATOM   1224  C CD  . ARG A 1 141 ? 16.326  4.353   23.470  1.00 20.39  ? 141 ARG A CD  1 
ATOM   1225  N NE  . ARG A 1 141 ? 15.524  3.189   23.824  1.00 19.86  ? 141 ARG A NE  1 
ATOM   1226  C CZ  . ARG A 1 141 ? 14.851  3.060   24.960  1.00 17.71  ? 141 ARG A CZ  1 
ATOM   1227  N NH1 . ARG A 1 141 ? 14.874  4.001   25.888  1.00 24.40  ? 141 ARG A NH1 1 
ATOM   1228  N NH2 . ARG A 1 141 ? 14.136  1.959   25.169  1.00 21.89  ? 141 ARG A NH2 1 
ATOM   1229  N N   . THR A 1 142 ? 20.259  1.226   22.878  1.00 32.10  ? 142 THR A N   1 
ATOM   1230  C CA  . THR A 1 142 ? 20.635  0.252   23.897  1.00 30.78  ? 142 THR A CA  1 
ATOM   1231  C C   . THR A 1 142 ? 22.106  0.385   24.278  1.00 31.75  ? 142 THR A C   1 
ATOM   1232  O O   . THR A 1 142 ? 22.448  0.441   25.465  1.00 41.15  ? 142 THR A O   1 
ATOM   1233  C CB  . THR A 1 142 ? 20.336  -1.163  23.400  1.00 31.76  ? 142 THR A CB  1 
ATOM   1234  O OG1 . THR A 1 142 ? 18.920  -1.333  23.255  1.00 37.97  ? 142 THR A OG1 1 
ATOM   1235  C CG2 . THR A 1 142 ? 20.866  -2.194  24.381  1.00 29.65  ? 142 THR A CG2 1 
ATOM   1236  N N   . LEU A 1 143 ? 22.993  0.448   23.282  1.00 27.09  ? 143 LEU A N   1 
ATOM   1237  C CA  . LEU A 1 143 ? 24.423  0.490   23.561  1.00 22.80  ? 143 LEU A CA  1 
ATOM   1238  C C   . LEU A 1 143 ? 24.925  1.881   23.926  1.00 28.69  ? 143 LEU A C   1 
ATOM   1239  O O   . LEU A 1 143 ? 26.020  1.995   24.486  1.00 34.62  ? 143 LEU A O   1 
ATOM   1240  C CB  . LEU A 1 143 ? 25.217  -0.039  22.366  1.00 34.19  ? 143 LEU A CB  1 
ATOM   1241  C CG  . LEU A 1 143 ? 25.276  -1.561  22.234  1.00 27.35  ? 143 LEU A CG  1 
ATOM   1242  C CD1 . LEU A 1 143 ? 25.974  -1.962  20.945  1.00 25.64  ? 143 LEU A CD1 1 
ATOM   1243  C CD2 . LEU A 1 143 ? 25.970  -2.174  23.439  1.00 30.92  ? 143 LEU A CD2 1 
ATOM   1244  N N   . ARG A 1 144 ? 24.162  2.936   23.628  1.00 31.10  ? 144 ARG A N   1 
ATOM   1245  C CA  . ARG A 1 144 ? 24.542  4.265   24.096  1.00 23.64  ? 144 ARG A CA  1 
ATOM   1246  C C   . ARG A 1 144 ? 24.501  4.359   25.615  1.00 33.88  ? 144 ARG A C   1 
ATOM   1247  O O   . ARG A 1 144 ? 25.085  5.286   26.187  1.00 41.31  ? 144 ARG A O   1 
ATOM   1248  C CB  . ARG A 1 144 ? 23.636  5.334   23.476  1.00 27.07  ? 144 ARG A CB  1 
ATOM   1249  C CG  . ARG A 1 144 ? 23.967  5.667   22.027  1.00 32.02  ? 144 ARG A CG  1 
ATOM   1250  C CD  . ARG A 1 144 ? 23.419  7.026   21.622  1.00 33.39  ? 144 ARG A CD  1 
ATOM   1251  N NE  . ARG A 1 144 ? 23.691  7.325   20.220  1.00 41.89  ? 144 ARG A NE  1 
ATOM   1252  C CZ  . ARG A 1 144 ? 23.896  8.543   19.737  1.00 49.43  ? 144 ARG A CZ  1 
ATOM   1253  N NH1 . ARG A 1 144 ? 23.874  9.609   20.521  1.00 59.56  ? 144 ARG A NH1 1 
ATOM   1254  N NH2 . ARG A 1 144 ? 24.127  8.696   18.435  1.00 30.89  ? 144 ARG A NH2 1 
ATOM   1255  N N   . LYS A 1 145 ? 23.818  3.422   26.275  1.00 31.59  ? 145 LYS A N   1 
ATOM   1256  C CA  . LYS A 1 145 ? 23.833  3.333   27.728  1.00 35.24  ? 145 LYS A CA  1 
ATOM   1257  C C   . LYS A 1 145 ? 25.005  2.511   28.247  1.00 30.15  ? 145 LYS A C   1 
ATOM   1258  O O   . LYS A 1 145 ? 25.530  2.808   29.327  1.00 33.84  ? 145 LYS A O   1 
ATOM   1259  C CB  . LYS A 1 145 ? 22.518  2.727   28.228  1.00 38.12  ? 145 LYS A CB  1 
ATOM   1260  C CG  . LYS A 1 145 ? 21.268  3.408   27.683  1.00 41.04  ? 145 LYS A CG  1 
ATOM   1261  C CD  . LYS A 1 145 ? 20.002  2.724   28.185  1.00 33.63  ? 145 LYS A CD  1 
ATOM   1262  C CE  . LYS A 1 145 ? 18.848  2.868   27.201  1.00 33.64  ? 145 LYS A CE  1 
ATOM   1263  N NZ  . LYS A 1 145 ? 18.751  4.245   26.642  1.00 41.23  ? 145 LYS A NZ  1 
ATOM   1264  N N   . ASP A 1 146 ? 25.436  1.497   27.493  1.00 37.87  ? 146 ASP A N   1 
ATOM   1265  C CA  . ASP A 1 146 ? 26.504  0.602   27.924  1.00 41.41  ? 146 ASP A CA  1 
ATOM   1266  C C   . ASP A 1 146 ? 27.898  1.130   27.609  1.00 33.78  ? 146 ASP A C   1 
ATOM   1267  O O   . ASP A 1 146 ? 28.856  0.782   28.309  1.00 28.73  ? 146 ASP A O   1 
ATOM   1268  C CB  . ASP A 1 146 ? 26.328  -0.775  27.276  1.00 40.99  ? 146 ASP A CB  1 
ATOM   1269  C CG  . ASP A 1 146 ? 26.479  -1.911  28.270  1.00 78.60  ? 146 ASP A CG  1 
ATOM   1270  O OD1 . ASP A 1 146 ? 26.424  -1.649  29.490  1.00 79.13  ? 146 ASP A OD1 1 
ATOM   1271  O OD2 . ASP A 1 146 ? 26.646  -3.068  27.830  1.00 76.97  ? 146 ASP A OD2 1 
ATOM   1272  N N   . LEU A 1 147 ? 28.041  1.955   26.572  1.00 33.03  ? 147 LEU A N   1 
ATOM   1273  C CA  . LEU A 1 147 ? 29.334  2.497   26.170  1.00 28.40  ? 147 LEU A CA  1 
ATOM   1274  C C   . LEU A 1 147 ? 29.476  3.968   26.552  1.00 31.44  ? 147 LEU A C   1 
ATOM   1275  O O   . LEU A 1 147 ? 30.144  4.733   25.852  1.00 28.89  ? 147 LEU A O   1 
ATOM   1276  C CB  . LEU A 1 147 ? 29.551  2.317   24.668  1.00 24.67  ? 147 LEU A CB  1 
ATOM   1277  C CG  . LEU A 1 147 ? 29.084  1.013   24.017  1.00 28.47  ? 147 LEU A CG  1 
ATOM   1278  C CD1 . LEU A 1 147 ? 29.482  0.980   22.547  1.00 16.94  ? 147 LEU A CD1 1 
ATOM   1279  C CD2 . LEU A 1 147 ? 29.644  -0.199  24.750  1.00 25.13  ? 147 LEU A CD2 1 
ATOM   1280  N N   . LYS A 1 148 ? 28.854  4.371   27.664  1.00 36.83  ? 148 LYS A N   1 
ATOM   1281  C CA  . LYS A 1 148 ? 28.860  5.777   28.061  1.00 32.71  ? 148 LYS A CA  1 
ATOM   1282  C C   . LYS A 1 148 ? 30.280  6.302   28.235  1.00 33.18  ? 148 LYS A C   1 
ATOM   1283  O O   . LYS A 1 148 ? 30.590  7.423   27.815  1.00 40.36  ? 148 LYS A O   1 
ATOM   1284  C CB  . LYS A 1 148 ? 28.061  5.958   29.352  1.00 36.96  ? 148 LYS A CB  1 
ATOM   1285  C CG  . LYS A 1 148 ? 26.589  6.282   29.144  1.00 51.34  ? 148 LYS A CG  1 
ATOM   1286  C CD  . LYS A 1 148 ? 26.356  7.780   29.023  1.00 60.56  ? 148 LYS A CD  1 
ATOM   1287  C CE  . LYS A 1 148 ? 24.958  8.079   28.504  1.00 58.19  ? 148 LYS A CE  1 
ATOM   1288  N NZ  . LYS A 1 148 ? 24.616  9.524   28.622  1.00 47.47  ? 148 LYS A NZ  1 
ATOM   1289  N N   . ASP A 1 149 ? 31.157  5.509   28.857  1.00 37.80  ? 149 ASP A N   1 
ATOM   1290  C CA  . ASP A 1 149 ? 32.531  5.953   29.069  1.00 37.38  ? 149 ASP A CA  1 
ATOM   1291  C C   . ASP A 1 149 ? 33.298  6.048   27.754  1.00 36.96  ? 149 ASP A C   1 
ATOM   1292  O O   . ASP A 1 149 ? 34.042  7.011   27.534  1.00 34.97  ? 149 ASP A O   1 
ATOM   1293  C CB  . ASP A 1 149 ? 33.239  5.014   30.044  1.00 40.98  ? 149 ASP A CB  1 
ATOM   1294  C CG  . ASP A 1 149 ? 33.954  5.761   31.149  1.00 64.12  ? 149 ASP A CG  1 
ATOM   1295  O OD1 . ASP A 1 149 ? 34.381  6.910   30.906  1.00 63.20  ? 149 ASP A OD1 1 
ATOM   1296  O OD2 . ASP A 1 149 ? 34.087  5.203   32.259  1.00 77.60  ? 149 ASP A OD2 1 
ATOM   1297  N N   . LEU A 1 150 ? 33.134  5.058   26.869  1.00 35.62  ? 150 LEU A N   1 
ATOM   1298  C CA  . LEU A 1 150 ? 33.764  5.130   25.553  1.00 23.62  ? 150 LEU A CA  1 
ATOM   1299  C C   . LEU A 1 150 ? 33.262  6.336   24.772  1.00 25.66  ? 150 LEU A C   1 
ATOM   1300  O O   . LEU A 1 150 ? 34.048  7.048   24.136  1.00 25.22  ? 150 LEU A O   1 
ATOM   1301  C CB  . LEU A 1 150 ? 33.494  3.848   24.764  1.00 20.78  ? 150 LEU A CB  1 
ATOM   1302  C CG  . LEU A 1 150 ? 34.260  2.562   25.079  1.00 21.50  ? 150 LEU A CG  1 
ATOM   1303  C CD1 . LEU A 1 150 ? 33.785  1.453   24.156  1.00 21.57  ? 150 LEU A CD1 1 
ATOM   1304  C CD2 . LEU A 1 150 ? 35.760  2.764   24.945  1.00 22.37  ? 150 LEU A CD2 1 
ATOM   1305  N N   . LEU A 1 151 ? 31.951  6.577   24.809  1.00 29.89  ? 151 LEU A N   1 
ATOM   1306  C CA  . LEU A 1 151 ? 31.379  7.718   24.104  1.00 26.20  ? 151 LEU A CA  1 
ATOM   1307  C C   . LEU A 1 151 ? 31.784  9.039   24.747  1.00 28.22  ? 151 LEU A C   1 
ATOM   1308  O O   . LEU A 1 151 ? 31.890  10.057  24.053  1.00 33.73  ? 151 LEU A O   1 
ATOM   1309  C CB  . LEU A 1 151 ? 29.859  7.580   24.055  1.00 25.67  ? 151 LEU A CB  1 
ATOM   1310  C CG  . LEU A 1 151 ? 29.362  6.459   23.139  1.00 22.91  ? 151 LEU A CG  1 
ATOM   1311  C CD1 . LEU A 1 151 ? 27.883  6.188   23.353  1.00 32.23  ? 151 LEU A CD1 1 
ATOM   1312  C CD2 . LEU A 1 151 ? 29.638  6.803   21.686  1.00 22.49  ? 151 LEU A CD2 1 
ATOM   1313  N N   . ASN A 1 152 ? 32.004  9.045   26.062  1.00 27.93  ? 152 ASN A N   1 
ATOM   1314  C CA  . ASN A 1 152 ? 32.454  10.261  26.730  1.00 30.58  ? 152 ASN A CA  1 
ATOM   1315  C C   . ASN A 1 152 ? 33.914  10.565  26.424  1.00 32.09  ? 152 ASN A C   1 
ATOM   1316  O O   . ASN A 1 152 ? 34.321  11.732  26.450  1.00 37.58  ? 152 ASN A O   1 
ATOM   1317  C CB  . ASN A 1 152 ? 32.244  10.141  28.240  1.00 39.03  ? 152 ASN A CB  1 
ATOM   1318  C CG  . ASN A 1 152 ? 30.995  10.857  28.714  1.00 47.09  ? 152 ASN A CG  1 
ATOM   1319  O OD1 . ASN A 1 152 ? 30.453  11.714  28.017  1.00 50.74  ? 152 ASN A OD1 1 
ATOM   1320  N ND2 . ASN A 1 152 ? 30.531  10.507  29.909  1.00 59.77  ? 152 ASN A ND2 1 
ATOM   1321  N N   . LYS A 1 153 ? 34.713  9.533   26.142  1.00 30.63  ? 153 LYS A N   1 
ATOM   1322  C CA  . LYS A 1 153 ? 36.125  9.740   25.831  1.00 25.02  ? 153 LYS A CA  1 
ATOM   1323  C C   . LYS A 1 153 ? 36.290  10.644  24.616  1.00 30.22  ? 153 LYS A C   1 
ATOM   1324  O O   . LYS A 1 153 ? 37.082  11.593  24.635  1.00 28.33  ? 153 LYS A O   1 
ATOM   1325  C CB  . LYS A 1 153 ? 36.809  8.392   25.595  1.00 32.32  ? 153 LYS A CB  1 
ATOM   1326  C CG  . LYS A 1 153 ? 38.144  8.228   26.303  1.00 27.59  ? 153 LYS A CG  1 
ATOM   1327  C CD  . LYS A 1 153 ? 38.659  6.803   26.169  1.00 26.11  ? 153 LYS A CD  1 
ATOM   1328  C CE  . LYS A 1 153 ? 40.173  6.754   26.276  1.00 32.83  ? 153 LYS A CE  1 
ATOM   1329  N NZ  . LYS A 1 153 ? 40.743  5.582   25.555  1.00 28.36  ? 153 LYS A NZ  1 
ATOM   1330  N N   . GLY A 1 154 ? 35.550  10.361  23.546  1.00 30.88  ? 154 GLY A N   1 
ATOM   1331  C CA  . GLY A 1 154 ? 35.534  11.214  22.375  1.00 25.45  ? 154 GLY A CA  1 
ATOM   1332  C C   . GLY A 1 154 ? 36.769  11.133  21.500  1.00 32.73  ? 154 GLY A C   1 
ATOM   1333  O O   . GLY A 1 154 ? 36.716  11.495  20.322  1.00 24.19  ? 154 GLY A O   1 
ATOM   1334  N N   . ARG A 1 155 ? 37.881  10.656  22.053  1.00 36.08  ? 155 ARG A N   1 
ATOM   1335  C CA  . ARG A 1 155 ? 39.160  10.705  21.357  1.00 26.59  ? 155 ARG A CA  1 
ATOM   1336  C C   . ARG A 1 155 ? 40.120  9.719   22.006  1.00 30.52  ? 155 ARG A C   1 
ATOM   1337  O O   . ARG A 1 155 ? 39.855  9.179   23.082  1.00 33.73  ? 155 ARG A O   1 
ATOM   1338  C CB  . ARG A 1 155 ? 39.747  12.117  21.388  1.00 32.07  ? 155 ARG A CB  1 
ATOM   1339  C CG  . ARG A 1 155 ? 39.926  12.651  22.801  1.00 41.60  ? 155 ARG A CG  1 
ATOM   1340  C CD  . ARG A 1 155 ? 40.007  14.161  22.814  1.00 38.34  ? 155 ARG A CD  1 
ATOM   1341  N NE  . ARG A 1 155 ? 40.483  14.676  21.538  1.00 33.75  ? 155 ARG A NE  1 
ATOM   1342  C CZ  . ARG A 1 155 ? 40.016  15.768  20.952  1.00 39.53  ? 155 ARG A CZ  1 
ATOM   1343  N NH1 . ARG A 1 155 ? 39.064  16.497  21.508  1.00 32.05  ? 155 ARG A NH1 1 
ATOM   1344  N NH2 . ARG A 1 155 ? 40.523  16.142  19.781  1.00 43.18  ? 155 ARG A NH2 1 
ATOM   1345  N N   . ASN A 1 156 ? 41.254  9.507   21.334  1.00 31.87  ? 156 ASN A N   1 
ATOM   1346  C CA  . ASN A 1 156 ? 42.341  8.664   21.831  1.00 30.22  ? 156 ASN A CA  1 
ATOM   1347  C C   . ASN A 1 156 ? 41.864  7.228   22.063  1.00 25.83  ? 156 ASN A C   1 
ATOM   1348  O O   . ASN A 1 156 ? 41.952  6.680   23.164  1.00 26.50  ? 156 ASN A O   1 
ATOM   1349  C CB  . ASN A 1 156 ? 42.954  9.257   23.104  1.00 29.77  ? 156 ASN A CB  1 
ATOM   1350  C CG  . ASN A 1 156 ? 43.501  10.655  22.889  1.00 39.68  ? 156 ASN A CG  1 
ATOM   1351  O OD1 . ASN A 1 156 ? 43.242  11.562  23.680  1.00 42.11  ? 156 ASN A OD1 1 
ATOM   1352  N ND2 . ASN A 1 156 ? 44.265  10.836  21.818  1.00 41.08  ? 156 ASN A ND2 1 
ATOM   1353  N N   . TYR A 1 157 ? 41.360  6.622   20.992  1.00 24.58  ? 157 TYR A N   1 
ATOM   1354  C CA  . TYR A 1 157 ? 40.859  5.256   21.042  1.00 26.00  ? 157 TYR A CA  1 
ATOM   1355  C C   . TYR A 1 157 ? 41.960  4.272   20.669  1.00 28.50  ? 157 TYR A C   1 
ATOM   1356  O O   . TYR A 1 157 ? 42.724  4.501   19.728  1.00 30.62  ? 157 TYR A O   1 
ATOM   1357  C CB  . TYR A 1 157 ? 39.663  5.084   20.105  1.00 22.29  ? 157 TYR A CB  1 
ATOM   1358  C CG  . TYR A 1 157 ? 38.430  5.819   20.571  1.00 24.04  ? 157 TYR A CG  1 
ATOM   1359  C CD1 . TYR A 1 157 ? 37.721  5.386   21.683  1.00 21.57  ? 157 TYR A CD1 1 
ATOM   1360  C CD2 . TYR A 1 157 ? 37.976  6.948   19.903  1.00 28.26  ? 157 TYR A CD2 1 
ATOM   1361  C CE1 . TYR A 1 157 ? 36.594  6.056   22.116  1.00 27.06  ? 157 TYR A CE1 1 
ATOM   1362  C CE2 . TYR A 1 157 ? 36.850  7.626   20.329  1.00 25.88  ? 157 TYR A CE2 1 
ATOM   1363  C CZ  . TYR A 1 157 ? 36.164  7.176   21.436  1.00 28.40  ? 157 TYR A CZ  1 
ATOM   1364  O OH  . TYR A 1 157 ? 35.042  7.849   21.862  1.00 27.03  ? 157 TYR A OH  1 
ATOM   1365  N N   . THR A 1 158 ? 42.035  3.178   21.418  1.00 25.11  ? 158 THR A N   1 
ATOM   1366  C CA  . THR A 1 158 ? 43.017  2.130   21.191  1.00 26.05  ? 158 THR A CA  1 
ATOM   1367  C C   . THR A 1 158 ? 42.398  0.986   20.391  1.00 25.14  ? 158 THR A C   1 
ATOM   1368  O O   . THR A 1 158 ? 41.178  0.881   20.244  1.00 28.92  ? 158 THR A O   1 
ATOM   1369  C CB  . THR A 1 158 ? 43.571  1.616   22.524  1.00 28.33  ? 158 THR A CB  1 
ATOM   1370  O OG1 . THR A 1 158 ? 42.598  0.776   23.154  1.00 31.61  ? 158 THR A OG1 1 
ATOM   1371  C CG2 . THR A 1 158 ? 43.898  2.780   23.447  1.00 28.38  ? 158 THR A CG2 1 
ATOM   1372  N N   . GLN A 1 159 ? 43.268  0.117   19.869  1.00 26.00  ? 159 GLN A N   1 
ATOM   1373  C CA  . GLN A 1 159 ? 42.804  -0.970  19.013  1.00 25.44  ? 159 GLN A CA  1 
ATOM   1374  C C   . GLN A 1 159 ? 41.913  -1.940  19.779  1.00 25.17  ? 159 GLN A C   1 
ATOM   1375  O O   . GLN A 1 159 ? 40.922  -2.444  19.236  1.00 28.65  ? 159 GLN A O   1 
ATOM   1376  C CB  . GLN A 1 159 ? 43.997  -1.700  18.395  1.00 26.78  ? 159 GLN A CB  1 
ATOM   1377  C CG  . GLN A 1 159 ? 43.624  -2.928  17.572  1.00 26.61  ? 159 GLN A CG  1 
ATOM   1378  C CD  . GLN A 1 159 ? 43.089  -2.574  16.197  1.00 25.51  ? 159 GLN A CD  1 
ATOM   1379  O OE1 . GLN A 1 159 ? 43.414  -1.523  15.644  1.00 25.43  ? 159 GLN A OE1 1 
ATOM   1380  N NE2 . GLN A 1 159 ? 42.268  -3.454  15.635  1.00 24.91  ? 159 GLN A NE2 1 
ATOM   1381  N N   . GLU A 1 160 ? 42.246  -2.220  21.042  1.00 26.29  ? 160 GLU A N   1 
ATOM   1382  C CA  . GLU A 1 160 ? 41.397  -3.105  21.835  1.00 31.61  ? 160 GLU A CA  1 
ATOM   1383  C C   . GLU A 1 160 ? 40.052  -2.463  22.146  1.00 25.89  ? 160 GLU A C   1 
ATOM   1384  O O   . GLU A 1 160 ? 39.032  -3.160  22.189  1.00 29.13  ? 160 GLU A O   1 
ATOM   1385  C CB  . GLU A 1 160 ? 42.107  -3.511  23.127  1.00 45.51  ? 160 GLU A CB  1 
ATOM   1386  C CG  . GLU A 1 160 ? 41.374  -4.591  23.916  1.00 57.14  ? 160 GLU A CG  1 
ATOM   1387  C CD  . GLU A 1 160 ? 41.577  -5.979  23.334  1.00 79.16  ? 160 GLU A CD  1 
ATOM   1388  O OE1 . GLU A 1 160 ? 42.646  -6.578  23.577  1.00 76.60  ? 160 GLU A OE1 1 
ATOM   1389  O OE2 . GLU A 1 160 ? 40.669  -6.469  22.630  1.00 66.77  ? 160 GLU A OE2 1 
ATOM   1390  N N   . GLU A 1 161 ? 40.026  -1.146  22.374  1.00 24.52  ? 161 GLU A N   1 
ATOM   1391  C CA  . GLU A 1 161 ? 38.752  -0.457  22.552  1.00 23.29  ? 161 GLU A CA  1 
ATOM   1392  C C   . GLU A 1 161 ? 37.901  -0.542  21.292  1.00 26.04  ? 161 GLU A C   1 
ATOM   1393  O O   . GLU A 1 161 ? 36.691  -0.789  21.365  1.00 23.05  ? 161 GLU A O   1 
ATOM   1394  C CB  . GLU A 1 161 ? 38.985  1.004   22.939  1.00 23.45  ? 161 GLU A CB  1 
ATOM   1395  C CG  . GLU A 1 161 ? 39.601  1.195   24.314  1.00 31.01  ? 161 GLU A CG  1 
ATOM   1396  C CD  . GLU A 1 161 ? 39.890  2.649   24.627  1.00 33.94  ? 161 GLU A CD  1 
ATOM   1397  O OE1 . GLU A 1 161 ? 39.235  3.529   24.030  1.00 34.96  ? 161 GLU A OE1 1 
ATOM   1398  O OE2 . GLU A 1 161 ? 40.779  2.913   25.465  1.00 46.67  ? 161 GLU A OE2 1 
ATOM   1399  N N   . LYS A 1 162 ? 38.518  -0.337  20.125  1.00 23.29  ? 162 LYS A N   1 
ATOM   1400  C CA  . LYS A 1 162 ? 37.787  -0.465  18.869  1.00 20.40  ? 162 LYS A CA  1 
ATOM   1401  C C   . LYS A 1 162 ? 37.266  -1.882  18.679  1.00 20.30  ? 162 LYS A C   1 
ATOM   1402  O O   . LYS A 1 162 ? 36.139  -2.080  18.211  1.00 26.44  ? 162 LYS A O   1 
ATOM   1403  C CB  . LYS A 1 162 ? 38.683  -0.062  17.697  1.00 20.65  ? 162 LYS A CB  1 
ATOM   1404  C CG  . LYS A 1 162 ? 37.990  -0.096  16.345  1.00 19.68  ? 162 LYS A CG  1 
ATOM   1405  C CD  . LYS A 1 162 ? 38.965  0.240   15.233  1.00 20.29  ? 162 LYS A CD  1 
ATOM   1406  C CE  . LYS A 1 162 ? 40.207  -0.630  15.320  1.00 21.68  ? 162 LYS A CE  1 
ATOM   1407  N NZ  . LYS A 1 162 ? 41.188  -0.312  14.248  1.00 22.49  ? 162 LYS A NZ  1 
ATOM   1408  N N   . GLU A 1 163 ? 38.077  -2.883  19.031  1.00 21.53  ? 163 GLU A N   1 
ATOM   1409  C CA  . GLU A 1 163 ? 37.612  -4.264  18.975  1.00 21.76  ? 163 GLU A CA  1 
ATOM   1410  C C   . GLU A 1 163 ? 36.475  -4.502  19.958  1.00 21.41  ? 163 GLU A C   1 
ATOM   1411  O O   . GLU A 1 163 ? 35.540  -5.258  19.666  1.00 20.94  ? 163 GLU A O   1 
ATOM   1412  C CB  . GLU A 1 163 ? 38.768  -5.223  19.253  1.00 23.46  ? 163 GLU A CB  1 
ATOM   1413  C CG  . GLU A 1 163 ? 39.585  -5.580  18.025  1.00 29.98  ? 163 GLU A CG  1 
ATOM   1414  C CD  . GLU A 1 163 ? 40.865  -6.315  18.371  1.00 47.40  ? 163 GLU A CD  1 
ATOM   1415  O OE1 . GLU A 1 163 ? 40.783  -7.390  19.001  1.00 49.37  ? 163 GLU A OE1 1 
ATOM   1416  O OE2 . GLU A 1 163 ? 41.954  -5.820  18.014  1.00 49.65  ? 163 GLU A OE2 1 
ATOM   1417  N N   . TYR A 1 164 ? 36.539  -3.868  21.132  1.00 23.87  ? 164 TYR A N   1 
ATOM   1418  C CA  . TYR A 1 164 ? 35.473  -4.021  22.117  1.00 21.71  ? 164 TYR A CA  1 
ATOM   1419  C C   . TYR A 1 164 ? 34.139  -3.541  21.559  1.00 20.57  ? 164 TYR A C   1 
ATOM   1420  O O   . TYR A 1 164 ? 33.107  -4.202  21.731  1.00 19.88  ? 164 TYR A O   1 
ATOM   1421  C CB  . TYR A 1 164 ? 35.825  -3.262  23.397  1.00 22.57  ? 164 TYR A CB  1 
ATOM   1422  C CG  . TYR A 1 164 ? 34.757  -3.358  24.463  1.00 23.54  ? 164 TYR A CG  1 
ATOM   1423  C CD1 . TYR A 1 164 ? 34.365  -4.590  24.968  1.00 29.50  ? 164 TYR A CD1 1 
ATOM   1424  C CD2 . TYR A 1 164 ? 34.136  -2.219  24.959  1.00 29.46  ? 164 TYR A CD2 1 
ATOM   1425  C CE1 . TYR A 1 164 ? 33.388  -4.686  25.941  1.00 31.49  ? 164 TYR A CE1 1 
ATOM   1426  C CE2 . TYR A 1 164 ? 33.158  -2.306  25.933  1.00 33.86  ? 164 TYR A CE2 1 
ATOM   1427  C CZ  . TYR A 1 164 ? 32.787  -3.542  26.420  1.00 38.49  ? 164 TYR A CZ  1 
ATOM   1428  O OH  . TYR A 1 164 ? 31.815  -3.639  27.389  1.00 44.37  ? 164 TYR A OH  1 
ATOM   1429  N N   . VAL A 1 165 ? 34.144  -2.389  20.884  1.00 21.44  ? 165 VAL A N   1 
ATOM   1430  C CA  . VAL A 1 165 ? 32.922  -1.875  20.272  1.00 17.88  ? 165 VAL A CA  1 
ATOM   1431  C C   . VAL A 1 165 ? 32.377  -2.874  19.261  1.00 17.43  ? 165 VAL A C   1 
ATOM   1432  O O   . VAL A 1 165 ? 31.192  -3.230  19.287  1.00 25.47  ? 165 VAL A O   1 
ATOM   1433  C CB  . VAL A 1 165 ? 33.185  -0.507  19.617  1.00 17.33  ? 165 VAL A CB  1 
ATOM   1434  C CG1 . VAL A 1 165 ? 32.012  -0.105  18.740  1.00 16.11  ? 165 VAL A CG1 1 
ATOM   1435  C CG2 . VAL A 1 165 ? 33.455  0.548   20.670  1.00 17.88  ? 165 VAL A CG2 1 
ATOM   1436  N N   . LEU A 1 166 ? 33.243  -3.351  18.362  1.00 17.70  ? 166 LEU A N   1 
ATOM   1437  C CA  . LEU A 1 166 ? 32.809  -4.269  17.313  1.00 17.43  ? 166 LEU A CA  1 
ATOM   1438  C C   . LEU A 1 166 ? 32.196  -5.532  17.903  1.00 20.85  ? 166 LEU A C   1 
ATOM   1439  O O   . LEU A 1 166 ? 31.238  -6.084  17.349  1.00 32.07  ? 166 LEU A O   1 
ATOM   1440  C CB  . LEU A 1 166 ? 33.990  -4.624  16.410  1.00 18.14  ? 166 LEU A CB  1 
ATOM   1441  C CG  . LEU A 1 166 ? 34.252  -3.764  15.174  1.00 17.65  ? 166 LEU A CG  1 
ATOM   1442  C CD1 . LEU A 1 166 ? 35.694  -3.926  14.717  1.00 18.76  ? 166 LEU A CD1 1 
ATOM   1443  C CD2 . LEU A 1 166 ? 33.293  -4.124  14.053  1.00 16.97  ? 166 LEU A CD2 1 
ATOM   1444  N N   . ASN A 1 167 ? 32.740  -6.012  19.023  1.00 19.44  ? 167 ASN A N   1 
ATOM   1445  C CA  . ASN A 1 167 ? 32.169  -7.187  19.674  1.00 20.84  ? 167 ASN A CA  1 
ATOM   1446  C C   . ASN A 1 167 ? 30.778  -6.894  20.226  1.00 28.50  ? 167 ASN A C   1 
ATOM   1447  O O   . ASN A 1 167 ? 29.877  -7.735  20.125  1.00 23.68  ? 167 ASN A O   1 
ATOM   1448  C CB  . ASN A 1 167 ? 33.098  -7.680  20.782  1.00 21.42  ? 167 ASN A CB  1 
ATOM   1449  C CG  . ASN A 1 167 ? 32.907  -9.151  21.087  1.00 39.45  ? 167 ASN A CG  1 
ATOM   1450  O OD1 . ASN A 1 167 ? 32.169  -9.848  20.392  1.00 33.68  ? 167 ASN A OD1 1 
ATOM   1451  N ND2 . ASN A 1 167 ? 33.571  -9.632  22.132  1.00 45.93  ? 167 ASN A ND2 1 
ATOM   1452  N N   . LYS A 1 168 ? 30.589  -5.714  20.823  1.00 31.04  ? 168 LYS A N   1 
ATOM   1453  C CA  . LYS A 1 168 ? 29.259  -5.323  21.280  1.00 17.98  ? 168 LYS A CA  1 
ATOM   1454  C C   . LYS A 1 168 ? 28.295  -5.202  20.110  1.00 18.03  ? 168 LYS A C   1 
ATOM   1455  O O   . LYS A 1 168 ? 27.135  -5.625  20.201  1.00 20.68  ? 168 LYS A O   1 
ATOM   1456  C CB  . LYS A 1 168 ? 29.329  -4.001  22.046  1.00 17.89  ? 168 LYS A CB  1 
ATOM   1457  C CG  . LYS A 1 168 ? 29.898  -4.113  23.447  1.00 19.32  ? 168 LYS A CG  1 
ATOM   1458  C CD  . LYS A 1 168 ? 28.999  -4.958  24.332  1.00 37.34  ? 168 LYS A CD  1 
ATOM   1459  C CE  . LYS A 1 168 ? 29.067  -4.502  25.779  1.00 42.20  ? 168 LYS A CE  1 
ATOM   1460  N NZ  . LYS A 1 168 ? 27.962  -5.079  26.593  1.00 62.63  ? 168 LYS A NZ  1 
ATOM   1461  N N   . TYR A 1 169 ? 28.761  -4.629  18.999  1.00 17.57  ? 169 TYR A N   1 
ATOM   1462  C CA  . TYR A 1 169 ? 27.901  -4.443  17.836  1.00 16.03  ? 169 TYR A CA  1 
ATOM   1463  C C   . TYR A 1 169 ? 27.450  -5.779  17.266  1.00 16.10  ? 169 TYR A C   1 
ATOM   1464  O O   . TYR A 1 169 ? 26.288  -5.936  16.871  1.00 25.97  ? 169 TYR A O   1 
ATOM   1465  C CB  . TYR A 1 169 ? 28.628  -3.628  16.768  1.00 14.59  ? 169 TYR A CB  1 
ATOM   1466  C CG  . TYR A 1 169 ? 28.618  -2.138  17.021  1.00 14.15  ? 169 TYR A CG  1 
ATOM   1467  C CD1 . TYR A 1 169 ? 28.464  -1.633  18.305  1.00 14.44  ? 169 TYR A CD1 1 
ATOM   1468  C CD2 . TYR A 1 169 ? 28.773  -1.237  15.979  1.00 13.68  ? 169 TYR A CD2 1 
ATOM   1469  C CE1 . TYR A 1 169 ? 28.459  -0.275  18.544  1.00 14.25  ? 169 TYR A CE1 1 
ATOM   1470  C CE2 . TYR A 1 169 ? 28.771  0.126   16.207  1.00 14.80  ? 169 TYR A CE2 1 
ATOM   1471  C CZ  . TYR A 1 169 ? 28.614  0.601   17.492  1.00 13.78  ? 169 TYR A CZ  1 
ATOM   1472  O OH  . TYR A 1 169 ? 28.610  1.956   17.728  1.00 16.36  ? 169 TYR A OH  1 
ATOM   1473  N N   . PHE A 1 170 ? 28.355  -6.757  17.209  1.00 17.27  ? 170 PHE A N   1 
ATOM   1474  C CA  . PHE A 1 170 ? 27.976  -8.048  16.650  1.00 29.39  ? 170 PHE A CA  1 
ATOM   1475  C C   . PHE A 1 170 ? 27.055  -8.818  17.584  1.00 28.93  ? 170 PHE A C   1 
ATOM   1476  O O   . PHE A 1 170 ? 26.175  -9.544  17.112  1.00 25.43  ? 170 PHE A O   1 
ATOM   1477  C CB  . PHE A 1 170 ? 29.221  -8.860  16.301  1.00 25.75  ? 170 PHE A CB  1 
ATOM   1478  C CG  . PHE A 1 170 ? 29.708  -8.617  14.903  1.00 37.69  ? 170 PHE A CG  1 
ATOM   1479  C CD1 . PHE A 1 170 ? 30.400  -7.458  14.590  1.00 35.94  ? 170 PHE A CD1 1 
ATOM   1480  C CD2 . PHE A 1 170 ? 29.437  -9.525  13.895  1.00 40.05  ? 170 PHE A CD2 1 
ATOM   1481  C CE1 . PHE A 1 170 ? 30.836  -7.221  13.299  1.00 38.35  ? 170 PHE A CE1 1 
ATOM   1482  C CE2 . PHE A 1 170 ? 29.869  -9.294  12.601  1.00 43.92  ? 170 PHE A CE2 1 
ATOM   1483  C CZ  . PHE A 1 170 ? 30.570  -8.140  12.303  1.00 42.62  ? 170 PHE A CZ  1 
ATOM   1484  N N   . GLU A 1 171 ? 27.219  -8.661  18.900  1.00 26.41  ? 171 GLU A N   1 
ATOM   1485  C CA  . GLU A 1 171 ? 26.244  -9.229  19.826  1.00 25.21  ? 171 GLU A CA  1 
ATOM   1486  C C   . GLU A 1 171 ? 24.849  -8.678  19.566  1.00 31.41  ? 171 GLU A C   1 
ATOM   1487  O O   . GLU A 1 171 ? 23.855  -9.396  19.727  1.00 31.89  ? 171 GLU A O   1 
ATOM   1488  C CB  . GLU A 1 171 ? 26.659  -8.955  21.272  1.00 30.38  ? 171 GLU A CB  1 
ATOM   1489  C CG  . GLU A 1 171 ? 26.281  -10.058 22.254  1.00 48.10  ? 171 GLU A CG  1 
ATOM   1490  C CD  . GLU A 1 171 ? 26.605  -9.700  23.694  1.00 47.97  ? 171 GLU A CD  1 
ATOM   1491  O OE1 . GLU A 1 171 ? 26.820  -8.503  23.979  1.00 43.50  ? 171 GLU A OE1 1 
ATOM   1492  O OE2 . GLU A 1 171 ? 26.646  -10.618 24.542  1.00 50.84  ? 171 GLU A OE2 1 
ATOM   1493  N N   . ILE A 1 172 ? 24.759  -7.411  19.158  1.00 30.56  ? 172 ILE A N   1 
ATOM   1494  C CA  . ILE A 1 172 ? 23.465  -6.796  18.876  1.00 25.29  ? 172 ILE A CA  1 
ATOM   1495  C C   . ILE A 1 172 ? 22.828  -7.421  17.638  1.00 26.60  ? 172 ILE A C   1 
ATOM   1496  O O   . ILE A 1 172 ? 21.614  -7.653  17.598  1.00 30.41  ? 172 ILE A O   1 
ATOM   1497  C CB  . ILE A 1 172 ? 23.631  -5.271  18.734  1.00 19.79  ? 172 ILE A CB  1 
ATOM   1498  C CG1 . ILE A 1 172 ? 23.740  -4.624  20.115  1.00 19.95  ? 172 ILE A CG1 1 
ATOM   1499  C CG2 . ILE A 1 172 ? 22.483  -4.663  17.948  1.00 17.37  ? 172 ILE A CG2 1 
ATOM   1500  C CD1 . ILE A 1 172 ? 22.463  -4.676  20.917  1.00 30.05  ? 172 ILE A CD1 1 
ATOM   1501  N N   . ILE A 1 173 ? 23.632  -7.709  16.612  1.00 22.90  ? 173 ILE A N   1 
ATOM   1502  C CA  . ILE A 1 173 ? 23.095  -8.307  15.393  1.00 17.66  ? 173 ILE A CA  1 
ATOM   1503  C C   . ILE A 1 173 ? 22.583  -9.720  15.661  1.00 26.76  ? 173 ILE A C   1 
ATOM   1504  O O   . ILE A 1 173 ? 21.532  -10.119 15.144  1.00 31.42  ? 173 ILE A O   1 
ATOM   1505  C CB  . ILE A 1 173 ? 24.152  -8.284  14.276  1.00 21.53  ? 173 ILE A CB  1 
ATOM   1506  C CG1 . ILE A 1 173 ? 24.619  -6.850  14.024  1.00 21.82  ? 173 ILE A CG1 1 
ATOM   1507  C CG2 . ILE A 1 173 ? 23.598  -8.897  12.997  1.00 20.72  ? 173 ILE A CG2 1 
ATOM   1508  C CD1 . ILE A 1 173 ? 25.895  -6.766  13.227  1.00 23.89  ? 173 ILE A CD1 1 
ATOM   1509  N N   . LYS A 1 174 ? 23.311  -10.501 16.466  1.00 27.92  ? 174 LYS A N   1 
ATOM   1510  C CA  . LYS A 1 174 ? 22.827  -11.828 16.839  1.00 25.91  ? 174 LYS A CA  1 
ATOM   1511  C C   . LYS A 1 174 ? 21.534  -11.766 17.644  1.00 24.74  ? 174 LYS A C   1 
ATOM   1512  O O   . LYS A 1 174 ? 20.783  -12.747 17.666  1.00 29.39  ? 174 LYS A O   1 
ATOM   1513  C CB  . LYS A 1 174 ? 23.896  -12.588 17.633  1.00 31.54  ? 174 LYS A CB  1 
ATOM   1514  C CG  . LYS A 1 174 ? 25.317  -12.372 17.142  1.00 37.09  ? 174 LYS A CG  1 
ATOM   1515  C CD  . LYS A 1 174 ? 26.277  -13.431 17.659  1.00 36.33  ? 174 LYS A CD  1 
ATOM   1516  C CE  . LYS A 1 174 ? 27.720  -13.048 17.353  1.00 49.20  ? 174 LYS A CE  1 
ATOM   1517  N NZ  . LYS A 1 174 ? 28.682  -13.621 18.335  1.00 43.91  ? 174 LYS A NZ  1 
ATOM   1518  N N   . LYS A 1 175 ? 21.256  -10.642 18.303  1.00 26.69  ? 175 LYS A N   1 
ATOM   1519  C CA  . LYS A 1 175 ? 20.039  -10.475 19.088  1.00 26.93  ? 175 LYS A CA  1 
ATOM   1520  C C   . LYS A 1 175 ? 18.853  -9.977  18.272  1.00 27.57  ? 175 LYS A C   1 
ATOM   1521  O O   . LYS A 1 175 ? 17.719  -10.051 18.757  1.00 27.76  ? 175 LYS A O   1 
ATOM   1522  C CB  . LYS A 1 175 ? 20.288  -9.492  20.239  1.00 27.95  ? 175 LYS A CB  1 
ATOM   1523  C CG  . LYS A 1 175 ? 19.823  -9.963  21.609  1.00 34.27  ? 175 LYS A CG  1 
ATOM   1524  C CD  . LYS A 1 175 ? 20.656  -9.310  22.705  1.00 43.72  ? 175 LYS A CD  1 
ATOM   1525  C CE  . LYS A 1 175 ? 20.759  -10.187 23.946  1.00 59.94  ? 175 LYS A CE  1 
ATOM   1526  N NZ  . LYS A 1 175 ? 19.451  -10.337 24.646  1.00 46.37  ? 175 LYS A NZ  1 
ATOM   1527  N N   . THR A 1 176 ? 19.082  -9.490  17.049  1.00 24.09  ? 176 THR A N   1 
ATOM   1528  C CA  . THR A 1 176 ? 18.082  -8.666  16.371  1.00 18.07  ? 176 THR A CA  1 
ATOM   1529  C C   . THR A 1 176 ? 16.807  -9.443  16.064  1.00 23.55  ? 176 THR A C   1 
ATOM   1530  O O   . THR A 1 176 ? 15.705  -9.003  16.412  1.00 28.18  ? 176 THR A O   1 
ATOM   1531  C CB  . THR A 1 176 ? 18.671  -8.076  15.088  1.00 17.85  ? 176 THR A CB  1 
ATOM   1532  O OG1 . THR A 1 176 ? 19.602  -7.039  15.424  1.00 24.38  ? 176 THR A OG1 1 
ATOM   1533  C CG2 . THR A 1 176 ? 17.570  -7.485  14.219  1.00 18.18  ? 176 THR A CG2 1 
ATOM   1534  N N   . LEU A 1 177 ? 16.928  -10.601 15.411  1.00 19.58  ? 177 LEU A N   1 
ATOM   1535  C CA  . LEU A 1 177 ? 15.723  -11.306 14.984  1.00 16.17  ? 177 LEU A CA  1 
ATOM   1536  C C   . LEU A 1 177 ? 14.970  -11.908 16.163  1.00 19.30  ? 177 LEU A C   1 
ATOM   1537  O O   . LEU A 1 177 ? 13.747  -12.076 16.091  1.00 17.43  ? 177 LEU A O   1 
ATOM   1538  C CB  . LEU A 1 177 ? 16.073  -12.383 13.960  1.00 16.86  ? 177 LEU A CB  1 
ATOM   1539  C CG  . LEU A 1 177 ? 16.493  -11.822 12.603  1.00 16.11  ? 177 LEU A CG  1 
ATOM   1540  C CD1 . LEU A 1 177 ? 17.481  -12.748 11.925  1.00 19.22  ? 177 LEU A CD1 1 
ATOM   1541  C CD2 . LEU A 1 177 ? 15.279  -11.573 11.718  1.00 15.85  ? 177 LEU A CD2 1 
ATOM   1542  N N   . SER A 1 178 ? 15.673  -12.230 17.250  1.00 18.11  ? 178 SER A N   1 
ATOM   1543  C CA  . SER A 1 178 ? 15.002  -12.770 18.427  1.00 19.10  ? 178 SER A CA  1 
ATOM   1544  C C   . SER A 1 178 ? 14.030  -11.759 19.023  1.00 18.61  ? 178 SER A C   1 
ATOM   1545  O O   . SER A 1 178 ? 12.922  -12.123 19.437  1.00 22.24  ? 178 SER A O   1 
ATOM   1546  C CB  . SER A 1 178 ? 16.033  -13.206 19.468  1.00 20.11  ? 178 SER A CB  1 
ATOM   1547  O OG  . SER A 1 178 ? 16.436  -14.550 19.257  1.00 34.43  ? 178 SER A OG  1 
ATOM   1548  N N   . ILE A 1 179 ? 14.421  -10.481 19.070  1.00 21.22  ? 179 ILE A N   1 
ATOM   1549  C CA  . ILE A 1 179 ? 13.548  -9.466  19.653  1.00 18.20  ? 179 ILE A CA  1 
ATOM   1550  C C   . ILE A 1 179 ? 12.318  -9.222  18.791  1.00 21.77  ? 179 ILE A C   1 
ATOM   1551  O O   . ILE A 1 179 ? 11.317  -8.691  19.285  1.00 26.68  ? 179 ILE A O   1 
ATOM   1552  C CB  . ILE A 1 179 ? 14.301  -8.143  19.897  1.00 16.33  ? 179 ILE A CB  1 
ATOM   1553  C CG1 . ILE A 1 179 ? 13.612  -7.336  20.997  1.00 19.51  ? 179 ILE A CG1 1 
ATOM   1554  C CG2 . ILE A 1 179 ? 14.367  -7.311  18.630  1.00 21.70  ? 179 ILE A CG2 1 
ATOM   1555  C CD1 . ILE A 1 179 ? 14.568  -6.591  21.890  1.00 37.94  ? 179 ILE A CD1 1 
ATOM   1556  N N   . TYR A 1 180 ? 12.363  -9.584  17.507  1.00 26.70  ? 180 TYR A N   1 
ATOM   1557  C CA  . TYR A 1 180 ? 11.150  -9.532  16.699  1.00 24.19  ? 180 TYR A CA  1 
ATOM   1558  C C   . TYR A 1 180 ? 10.219  -10.688 17.037  1.00 21.41  ? 180 TYR A C   1 
ATOM   1559  O O   . TYR A 1 180 ? 8.997   -10.510 17.108  1.00 22.61  ? 180 TYR A O   1 
ATOM   1560  C CB  . TYR A 1 180 ? 11.509  -9.520  15.214  1.00 17.52  ? 180 TYR A CB  1 
ATOM   1561  C CG  . TYR A 1 180 ? 12.001  -8.169  14.759  1.00 14.32  ? 180 TYR A CG  1 
ATOM   1562  C CD1 . TYR A 1 180 ? 11.118  -7.111  14.594  1.00 14.14  ? 180 TYR A CD1 1 
ATOM   1563  C CD2 . TYR A 1 180 ? 13.350  -7.942  14.520  1.00 15.42  ? 180 TYR A CD2 1 
ATOM   1564  C CE1 . TYR A 1 180 ? 11.560  -5.869  14.189  1.00 14.77  ? 180 TYR A CE1 1 
ATOM   1565  C CE2 . TYR A 1 180 ? 13.802  -6.703  14.114  1.00 13.06  ? 180 TYR A CE2 1 
ATOM   1566  C CZ  . TYR A 1 180 ? 12.902  -5.671  13.951  1.00 13.17  ? 180 TYR A CZ  1 
ATOM   1567  O OH  . TYR A 1 180 ? 13.343  -4.433  13.548  1.00 18.51  ? 180 TYR A OH  1 
ATOM   1568  N N   . ARG A 1 181 ? 10.782  -11.876 17.260  1.00 20.85  ? 181 ARG A N   1 
ATOM   1569  C CA  . ARG A 1 181 ? 9.993   -12.989 17.775  1.00 19.94  ? 181 ARG A CA  1 
ATOM   1570  C C   . ARG A 1 181 ? 9.380   -12.643 19.124  1.00 22.27  ? 181 ARG A C   1 
ATOM   1571  O O   . ARG A 1 181 ? 8.187   -12.870 19.356  1.00 22.28  ? 181 ARG A O   1 
ATOM   1572  C CB  . ARG A 1 181 ? 10.869  -14.234 17.904  1.00 21.02  ? 181 ARG A CB  1 
ATOM   1573  C CG  . ARG A 1 181 ? 11.302  -14.858 16.599  1.00 25.25  ? 181 ARG A CG  1 
ATOM   1574  C CD  . ARG A 1 181 ? 11.267  -16.367 16.730  1.00 31.88  ? 181 ARG A CD  1 
ATOM   1575  N NE  . ARG A 1 181 ? 9.988   -16.818 17.267  1.00 34.34  ? 181 ARG A NE  1 
ATOM   1576  C CZ  . ARG A 1 181 ? 9.419   -17.981 16.982  1.00 38.98  ? 181 ARG A CZ  1 
ATOM   1577  N NH1 . ARG A 1 181 ? 10.000  -18.855 16.175  1.00 44.14  ? 181 ARG A NH1 1 
ATOM   1578  N NH2 . ARG A 1 181 ? 8.236   -18.274 17.519  1.00 33.17  ? 181 ARG A NH2 1 
ATOM   1579  N N   . GLU A 1 182 ? 10.188  -12.081 20.025  1.00 20.48  ? 182 GLU A N   1 
ATOM   1580  C CA  . GLU A 1 182 ? 9.741   -11.846 21.394  1.00 23.57  ? 182 GLU A CA  1 
ATOM   1581  C C   . GLU A 1 182 ? 8.565   -10.876 21.445  1.00 31.37  ? 182 GLU A C   1 
ATOM   1582  O O   . GLU A 1 182 ? 7.592   -11.111 22.171  1.00 33.02  ? 182 GLU A O   1 
ATOM   1583  C CB  . GLU A 1 182 ? 10.911  -11.331 22.231  1.00 27.41  ? 182 GLU A CB  1 
ATOM   1584  C CG  . GLU A 1 182 ? 10.577  -11.058 23.686  1.00 42.04  ? 182 GLU A CG  1 
ATOM   1585  C CD  . GLU A 1 182 ? 11.571  -10.118 24.340  1.00 55.39  ? 182 GLU A CD  1 
ATOM   1586  O OE1 . GLU A 1 182 ? 12.782  -10.424 24.321  1.00 55.68  ? 182 GLU A OE1 1 
ATOM   1587  O OE2 . GLU A 1 182 ? 11.142  -9.074  24.875  1.00 60.43  ? 182 GLU A OE2 1 
ATOM   1588  N N   . ILE A 1 183 ? 8.630   -9.784  20.679  1.00 27.91  ? 183 ILE A N   1 
ATOM   1589  C CA  . ILE A 1 183 ? 7.542   -8.809  20.696  1.00 24.09  ? 183 ILE A CA  1 
ATOM   1590  C C   . ILE A 1 183 ? 6.309   -9.313  19.960  1.00 22.89  ? 183 ILE A C   1 
ATOM   1591  O O   . ILE A 1 183 ? 5.194   -8.865  20.257  1.00 30.31  ? 183 ILE A O   1 
ATOM   1592  C CB  . ILE A 1 183 ? 7.982   -7.462  20.096  1.00 18.23  ? 183 ILE A CB  1 
ATOM   1593  C CG1 . ILE A 1 183 ? 8.387   -7.632  18.630  1.00 16.96  ? 183 ILE A CG1 1 
ATOM   1594  C CG2 . ILE A 1 183 ? 9.118   -6.864  20.914  1.00 17.83  ? 183 ILE A CG2 1 
ATOM   1595  C CD1 . ILE A 1 183 ? 7.716   -6.659  17.697  1.00 16.21  ? 183 ILE A CD1 1 
ATOM   1596  N N   . LYS A 1 184 ? 6.476   -10.227 19.002  1.00 21.01  ? 184 LYS A N   1 
ATOM   1597  C CA  . LYS A 1 184 ? 5.321   -10.779 18.303  1.00 20.33  ? 184 LYS A CA  1 
ATOM   1598  C C   . LYS A 1 184 ? 4.551   -11.750 19.191  1.00 22.13  ? 184 LYS A C   1 
ATOM   1599  O O   . LYS A 1 184 ? 3.315   -11.750 19.192  1.00 23.94  ? 184 LYS A O   1 
ATOM   1600  C CB  . LYS A 1 184 ? 5.778   -11.466 17.014  1.00 20.96  ? 184 LYS A CB  1 
ATOM   1601  C CG  . LYS A 1 184 ? 4.651   -11.976 16.133  1.00 20.49  ? 184 LYS A CG  1 
ATOM   1602  C CD  . LYS A 1 184 ? 5.168   -12.983 15.120  1.00 20.67  ? 184 LYS A CD  1 
ATOM   1603  C CE  . LYS A 1 184 ? 4.027   -13.668 14.393  1.00 21.65  ? 184 LYS A CE  1 
ATOM   1604  N NZ  . LYS A 1 184 ? 2.884   -13.942 15.303  1.00 35.06  ? 184 LYS A NZ  1 
ATOM   1605  N N   . GLU A 1 185 ? 5.265   -12.573 19.962  1.00 23.01  ? 185 GLU A N   1 
ATOM   1606  C CA  . GLU A 1 185 ? 4.608   -13.582 20.787  1.00 30.25  ? 185 GLU A CA  1 
ATOM   1607  C C   . GLU A 1 185 ? 4.009   -13.002 22.061  1.00 25.90  ? 185 GLU A C   1 
ATOM   1608  O O   . GLU A 1 185 ? 2.981   -13.499 22.531  1.00 27.47  ? 185 GLU A O   1 
ATOM   1609  C CB  . GLU A 1 185 ? 5.592   -14.702 21.131  1.00 34.27  ? 185 GLU A CB  1 
ATOM   1610  C CG  . GLU A 1 185 ? 6.234   -15.353 19.910  1.00 39.63  ? 185 GLU A CG  1 
ATOM   1611  C CD  . GLU A 1 185 ? 5.222   -15.898 18.911  1.00 60.36  ? 185 GLU A CD  1 
ATOM   1612  O OE1 . GLU A 1 185 ? 5.588   -16.032 17.722  1.00 63.60  ? 185 GLU A OE1 1 
ATOM   1613  O OE2 . GLU A 1 185 ? 4.080   -16.215 19.305  1.00 68.32  ? 185 GLU A OE2 1 
ATOM   1614  N N   . GLU A 1 186 ? 4.624   -11.973 22.637  1.00 23.18  ? 186 GLU A N   1 
ATOM   1615  C CA  . GLU A 1 186 ? 4.077   -11.319 23.816  1.00 33.07  ? 186 GLU A CA  1 
ATOM   1616  C C   . GLU A 1 186 ? 3.058   -10.241 23.467  1.00 32.13  ? 186 GLU A C   1 
ATOM   1617  O O   . GLU A 1 186 ? 2.609   -9.514  24.360  1.00 37.60  ? 186 GLU A O   1 
ATOM   1618  C CB  . GLU A 1 186 ? 5.202   -10.732 24.672  1.00 36.60  ? 186 GLU A CB  1 
ATOM   1619  C CG  . GLU A 1 186 ? 6.272   -11.748 25.047  1.00 43.55  ? 186 GLU A CG  1 
ATOM   1620  C CD  . GLU A 1 186 ? 7.569   -11.101 25.480  1.00 61.83  ? 186 GLU A CD  1 
ATOM   1621  O OE1 . GLU A 1 186 ? 7.826   -9.953  25.065  1.00 56.67  ? 186 GLU A OE1 1 
ATOM   1622  O OE2 . GLU A 1 186 ? 8.336   -11.744 26.230  1.00 53.15  ? 186 GLU A OE2 1 
ATOM   1623  N N   . GLY A 1 187 ? 2.696   -10.116 22.193  1.00 28.28  ? 187 GLY A N   1 
ATOM   1624  C CA  . GLY A 1 187 ? 1.586   -9.280  21.789  1.00 24.28  ? 187 GLY A CA  1 
ATOM   1625  C C   . GLY A 1 187 ? 1.846   -7.793  21.791  1.00 20.44  ? 187 GLY A C   1 
ATOM   1626  O O   . GLY A 1 187 ? 0.894   -7.018  21.653  1.00 24.13  ? 187 GLY A O   1 
ATOM   1627  N N   . LYS A 1 188 ? 3.096   -7.363  21.944  1.00 19.67  ? 188 LYS A N   1 
ATOM   1628  C CA  . LYS A 1 188 ? 3.393   -5.938  21.923  1.00 14.63  ? 188 LYS A CA  1 
ATOM   1629  C C   . LYS A 1 188 ? 3.433   -5.366  20.514  1.00 17.50  ? 188 LYS A C   1 
ATOM   1630  O O   . LYS A 1 188 ? 3.500   -4.140  20.363  1.00 21.48  ? 188 LYS A O   1 
ATOM   1631  C CB  . LYS A 1 188 ? 4.714   -5.672  22.649  1.00 22.76  ? 188 LYS A CB  1 
ATOM   1632  C CG  . LYS A 1 188 ? 4.632   -5.976  24.139  1.00 25.92  ? 188 LYS A CG  1 
ATOM   1633  C CD  . LYS A 1 188 ? 5.998   -6.106  24.786  1.00 29.89  ? 188 LYS A CD  1 
ATOM   1634  C CE  . LYS A 1 188 ? 5.882   -6.027  26.301  1.00 21.01  ? 188 LYS A CE  1 
ATOM   1635  N NZ  . LYS A 1 188 ? 4.700   -6.783  26.806  1.00 26.61  ? 188 LYS A NZ  1 
ATOM   1636  N N   . GLY A 1 189 ? 3.386   -6.211  19.488  1.00 16.97  ? 189 GLY A N   1 
ATOM   1637  C CA  . GLY A 1 189 ? 3.314   -5.722  18.127  1.00 12.25  ? 189 GLY A CA  1 
ATOM   1638  C C   . GLY A 1 189 ? 3.129   -6.851  17.141  1.00 12.23  ? 189 GLY A C   1 
ATOM   1639  O O   . GLY A 1 189 ? 3.321   -8.027  17.464  1.00 12.96  ? 189 GLY A O   1 
ATOM   1640  N N   . SER A 1 190 ? 2.750   -6.472  15.927  1.00 11.50  ? 190 SER A N   1 
ATOM   1641  C CA  . SER A 1 190 ? 2.620   -7.393  14.810  1.00 11.46  ? 190 SER A CA  1 
ATOM   1642  C C   . SER A 1 190 ? 3.828   -7.253  13.893  1.00 12.47  ? 190 SER A C   1 
ATOM   1643  O O   . SER A 1 190 ? 4.452   -6.192  13.822  1.00 15.15  ? 190 SER A O   1 
ATOM   1644  C CB  . SER A 1 190 ? 1.333   -7.122  14.027  1.00 11.08  ? 190 SER A CB  1 
ATOM   1645  O OG  . SER A 1 190 ? 0.191   -7.562  14.739  1.00 16.83  ? 190 SER A OG  1 
ATOM   1646  N N   . VAL A 1 191 ? 4.158   -8.335  13.194  1.00 11.42  ? 191 VAL A N   1 
ATOM   1647  C CA  . VAL A 1 191 ? 5.266   -8.337  12.245  1.00 11.94  ? 191 VAL A CA  1 
ATOM   1648  C C   . VAL A 1 191 ? 4.752   -8.831  10.900  1.00 12.79  ? 191 VAL A C   1 
ATOM   1649  O O   . VAL A 1 191 ? 4.184   -9.925  10.809  1.00 24.85  ? 191 VAL A O   1 
ATOM   1650  C CB  . VAL A 1 191 ? 6.443   -9.201  12.723  1.00 12.07  ? 191 VAL A CB  1 
ATOM   1651  C CG1 . VAL A 1 191 ? 7.610   -9.072  11.759  1.00 11.99  ? 191 VAL A CG1 1 
ATOM   1652  C CG2 . VAL A 1 191 ? 6.867   -8.785  14.122  1.00 12.42  ? 191 VAL A CG2 1 
ATOM   1653  N N   . SER A 1 192 ? 4.956   -8.029  9.864   1.00 10.49  ? 192 SER A N   1 
ATOM   1654  C CA  . SER A 1 192 ? 4.624   -8.380  8.494   1.00 10.42  ? 192 SER A CA  1 
ATOM   1655  C C   . SER A 1 192 ? 5.904   -8.512  7.685   1.00 13.90  ? 192 SER A C   1 
ATOM   1656  O O   . SER A 1 192 ? 6.986   -8.101  8.111   1.00 12.48  ? 192 SER A O   1 
ATOM   1657  C CB  . SER A 1 192 ? 3.713   -7.321  7.863   1.00 10.23  ? 192 SER A CB  1 
ATOM   1658  O OG  . SER A 1 192 ? 4.357   -6.058  7.841   1.00 14.18  ? 192 SER A OG  1 
ATOM   1659  N N   . THR A 1 193 ? 5.766   -9.092  6.502   1.00 15.76  ? 193 THR A N   1 
ATOM   1660  C CA  . THR A 1 193 ? 6.848   -9.177  5.539   1.00 10.94  ? 193 THR A CA  1 
ATOM   1661  C C   . THR A 1 193 ? 6.413   -8.512  4.240   1.00 14.96  ? 193 THR A C   1 
ATOM   1662  O O   . THR A 1 193 ? 5.253   -8.137  4.062   1.00 19.85  ? 193 THR A O   1 
ATOM   1663  C CB  . THR A 1 193 ? 7.259   -10.634 5.289   1.00 11.87  ? 193 THR A CB  1 
ATOM   1664  O OG1 . THR A 1 193 ? 8.490   -10.671 4.557   1.00 24.37  ? 193 THR A OG1 1 
ATOM   1665  C CG2 . THR A 1 193 ? 6.191   -11.356 4.498   1.00 12.10  ? 193 THR A CG2 1 
ATOM   1666  N N   . SER A 1 194 ? 7.368   -8.334  3.349   1.00 16.34  ? 194 SER A N   1 
ATOM   1667  C CA  . SER A 1 194 ? 7.116   -7.887  1.994   1.00 10.57  ? 194 SER A CA  1 
ATOM   1668  C C   . SER A 1 194 ? 7.490   -8.998  1.027   1.00 17.94  ? 194 SER A C   1 
ATOM   1669  O O   . SER A 1 194 ? 8.166   -9.957  1.414   1.00 23.48  ? 194 SER A O   1 
ATOM   1670  C CB  . SER A 1 194 ? 7.925   -6.621  1.682   1.00 14.06  ? 194 SER A CB  1 
ATOM   1671  O OG  . SER A 1 194 ? 7.292   -5.469  2.213   1.00 21.12  ? 194 SER A OG  1 
ATOM   1672  N N   . PRO A 1 195 ? 7.049   -8.924  -0.230  1.00 15.79  ? 195 PRO A N   1 
ATOM   1673  C CA  . PRO A 1 195 ? 7.557   -9.863  -1.236  1.00 16.52  ? 195 PRO A CA  1 
ATOM   1674  C C   . PRO A 1 195 ? 9.080   -9.849  -1.251  1.00 16.18  ? 195 PRO A C   1 
ATOM   1675  O O   . PRO A 1 195 ? 9.711   -8.834  -0.946  1.00 21.37  ? 195 PRO A O   1 
ATOM   1676  C CB  . PRO A 1 195 ? 6.961   -9.337  -2.544  1.00 15.49  ? 195 PRO A CB  1 
ATOM   1677  C CG  . PRO A 1 195 ? 5.694   -8.682  -2.119  1.00 11.67  ? 195 PRO A CG  1 
ATOM   1678  C CD  . PRO A 1 195 ? 5.953   -8.094  -0.757  1.00 11.42  ? 195 PRO A CD  1 
ATOM   1679  N N   . TYR A 1 196 ? 9.661   -10.997 -1.611  1.00 13.65  ? 196 TYR A N   1 
ATOM   1680  C CA  . TYR A 1 196 ? 11.012  -11.345 -1.170  1.00 14.24  ? 196 TYR A CA  1 
ATOM   1681  C C   . TYR A 1 196 ? 12.015  -10.213 -1.370  1.00 17.31  ? 196 TYR A C   1 
ATOM   1682  O O   . TYR A 1 196 ? 12.582  -9.694  -0.402  1.00 20.12  ? 196 TYR A O   1 
ATOM   1683  C CB  . TYR A 1 196 ? 11.491  -12.611 -1.882  1.00 15.48  ? 196 TYR A CB  1 
ATOM   1684  C CG  . TYR A 1 196 ? 12.545  -13.348 -1.088  1.00 16.30  ? 196 TYR A CG  1 
ATOM   1685  C CD1 . TYR A 1 196 ? 13.852  -12.888 -1.052  1.00 16.64  ? 196 TYR A CD1 1 
ATOM   1686  C CD2 . TYR A 1 196 ? 12.230  -14.486 -0.356  1.00 16.88  ? 196 TYR A CD2 1 
ATOM   1687  C CE1 . TYR A 1 196 ? 14.821  -13.542 -0.325  1.00 19.13  ? 196 TYR A CE1 1 
ATOM   1688  C CE2 . TYR A 1 196 ? 13.196  -15.151 0.378   1.00 17.80  ? 196 TYR A CE2 1 
ATOM   1689  C CZ  . TYR A 1 196 ? 14.490  -14.673 0.389   1.00 18.14  ? 196 TYR A CZ  1 
ATOM   1690  O OH  . TYR A 1 196 ? 15.462  -15.323 1.114   1.00 19.22  ? 196 TYR A OH  1 
ATOM   1691  N N   . TYR A 1 197 ? 12.245  -9.807  -2.619  1.00 14.24  ? 197 TYR A N   1 
ATOM   1692  C CA  . TYR A 1 197 ? 13.294  -8.839  -2.920  1.00 14.31  ? 197 TYR A CA  1 
ATOM   1693  C C   . TYR A 1 197 ? 12.747  -7.439  -3.177  1.00 13.64  ? 197 TYR A C   1 
ATOM   1694  O O   . TYR A 1 197 ? 13.355  -6.662  -3.921  1.00 22.17  ? 197 TYR A O   1 
ATOM   1695  C CB  . TYR A 1 197 ? 14.136  -9.318  -4.101  1.00 15.40  ? 197 TYR A CB  1 
ATOM   1696  C CG  . TYR A 1 197 ? 15.045  -10.476 -3.749  1.00 16.46  ? 197 TYR A CG  1 
ATOM   1697  C CD1 . TYR A 1 197 ? 16.163  -10.283 -2.952  1.00 16.79  ? 197 TYR A CD1 1 
ATOM   1698  C CD2 . TYR A 1 197 ? 14.790  -11.759 -4.219  1.00 17.30  ? 197 TYR A CD2 1 
ATOM   1699  C CE1 . TYR A 1 197 ? 16.998  -11.335 -2.625  1.00 17.93  ? 197 TYR A CE1 1 
ATOM   1700  C CE2 . TYR A 1 197 ? 15.622  -12.817 -3.901  1.00 18.44  ? 197 TYR A CE2 1 
ATOM   1701  C CZ  . TYR A 1 197 ? 16.723  -12.600 -3.101  1.00 19.84  ? 197 TYR A CZ  1 
ATOM   1702  O OH  . TYR A 1 197 ? 17.553  -13.650 -2.782  1.00 30.61  ? 197 TYR A OH  1 
ATOM   1703  N N   . HIS A 1 198 ? 11.614  -7.103  -2.559  1.00 16.63  ? 198 HIS A N   1 
ATOM   1704  C CA  . HIS A 1 198 ? 11.014  -5.773  -2.599  1.00 21.02  ? 198 HIS A CA  1 
ATOM   1705  C C   . HIS A 1 198 ? 10.725  -5.278  -4.015  1.00 21.23  ? 198 HIS A C   1 
ATOM   1706  O O   . HIS A 1 198 ? 11.092  -4.143  -4.349  1.00 19.02  ? 198 HIS A O   1 
ATOM   1707  C CB  . HIS A 1 198 ? 11.931  -4.776  -1.885  1.00 16.47  ? 198 HIS A CB  1 
ATOM   1708  C CG  . HIS A 1 198 ? 11.214  -3.597  -1.310  1.00 14.73  ? 198 HIS A CG  1 
ATOM   1709  N ND1 . HIS A 1 198 ? 11.394  -2.316  -1.785  1.00 15.19  ? 198 HIS A ND1 1 
ATOM   1710  C CD2 . HIS A 1 198 ? 10.324  -3.502  -0.294  1.00 16.02  ? 198 HIS A CD2 1 
ATOM   1711  C CE1 . HIS A 1 198 ? 10.642  -1.482  -1.089  1.00 20.46  ? 198 HIS A CE1 1 
ATOM   1712  N NE2 . HIS A 1 198 ? 9.982   -2.176  -0.179  1.00 22.34  ? 198 HIS A NE2 1 
ATOM   1713  N N   . PRO A 1 199 ? 10.062  -6.057  -4.867  1.00 23.11  ? 199 PRO A N   1 
ATOM   1714  C CA  . PRO A 1 199 ? 9.776   -5.588  -6.222  1.00 28.88  ? 199 PRO A CA  1 
ATOM   1715  C C   . PRO A 1 199 ? 8.475   -4.794  -6.282  1.00 30.86  ? 199 PRO A C   1 
ATOM   1716  O O   . PRO A 1 199 ? 7.648   -4.823  -5.370  1.00 24.13  ? 199 PRO A O   1 
ATOM   1717  C CB  . PRO A 1 199 ? 9.657   -6.894  -7.016  1.00 16.92  ? 199 PRO A CB  1 
ATOM   1718  C CG  . PRO A 1 199 ? 9.121   -7.879  -6.026  1.00 13.48  ? 199 PRO A CG  1 
ATOM   1719  C CD  . PRO A 1 199 ? 9.463   -7.384  -4.630  1.00 14.19  ? 199 PRO A CD  1 
ATOM   1720  N N   . LEU A 1 200 ? 8.311   -4.078  -7.391  1.00 25.86  ? 200 LEU A N   1 
ATOM   1721  C CA  . LEU A 1 200 ? 7.057   -3.385  -7.677  1.00 21.40  ? 200 LEU A CA  1 
ATOM   1722  C C   . LEU A 1 200 ? 6.102   -4.399  -8.292  1.00 20.61  ? 200 LEU A C   1 
ATOM   1723  O O   . LEU A 1 200 ? 6.012   -4.550  -9.511  1.00 25.73  ? 200 LEU A O   1 
ATOM   1724  C CB  . LEU A 1 200 ? 7.291   -2.192  -8.593  1.00 19.65  ? 200 LEU A CB  1 
ATOM   1725  C CG  . LEU A 1 200 ? 7.938   -0.995  -7.899  1.00 18.98  ? 200 LEU A CG  1 
ATOM   1726  C CD1 . LEU A 1 200 ? 8.425   0.000   -8.931  1.00 13.10  ? 200 LEU A CD1 1 
ATOM   1727  C CD2 . LEU A 1 200 ? 6.964   -0.345  -6.925  1.00 12.81  ? 200 LEU A CD2 1 
ATOM   1728  N N   . ILE A 1 201 ? 5.380   -5.097  -7.422  1.00 14.77  ? 201 ILE A N   1 
ATOM   1729  C CA  . ILE A 1 201 ? 4.477   -6.185  -7.790  1.00 13.76  ? 201 ILE A CA  1 
ATOM   1730  C C   . ILE A 1 201 ? 3.485   -5.759  -8.873  1.00 23.26  ? 201 ILE A C   1 
ATOM   1731  O O   . ILE A 1 201 ? 3.250   -6.538  -9.810  1.00 25.52  ? 201 ILE A O   1 
ATOM   1732  C CB  . ILE A 1 201 ? 3.762   -6.730  -6.541  1.00 23.73  ? 201 ILE A CB  1 
ATOM   1733  C CG1 . ILE A 1 201 ? 4.735   -7.553  -5.693  1.00 17.29  ? 201 ILE A CG1 1 
ATOM   1734  C CG2 . ILE A 1 201 ? 2.566   -7.576  -6.915  1.00 22.36  ? 201 ILE A CG2 1 
ATOM   1735  C CD1 . ILE A 1 201 ? 5.290   -8.766  -6.410  1.00 21.95  ? 201 ILE A CD1 1 
ATOM   1736  N N   . PRO A 1 202 ? 2.875   -4.562  -8.811  1.00 17.00  ? 202 PRO A N   1 
ATOM   1737  C CA  . PRO A 1 202 ? 1.968   -4.172  -9.910  1.00 15.79  ? 202 PRO A CA  1 
ATOM   1738  C C   . PRO A 1 202 ? 2.613   -4.191  -11.287 1.00 22.20  ? 202 PRO A C   1 
ATOM   1739  O O   . PRO A 1 202 ? 1.985   -4.654  -12.248 1.00 29.18  ? 202 PRO A O   1 
ATOM   1740  C CB  . PRO A 1 202 ? 1.535   -2.755  -9.514  1.00 13.67  ? 202 PRO A CB  1 
ATOM   1741  C CG  . PRO A 1 202 ? 1.625   -2.740  -8.047  1.00 16.36  ? 202 PRO A CG  1 
ATOM   1742  C CD  . PRO A 1 202 ? 2.796   -3.605  -7.690  1.00 14.88  ? 202 PRO A CD  1 
ATOM   1743  N N   . ILE A 1 203 ? 3.852   -3.707  -11.416 1.00 17.83  ? 203 ILE A N   1 
ATOM   1744  C CA  . ILE A 1 203 ? 4.495   -3.700  -12.727 1.00 18.35  ? 203 ILE A CA  1 
ATOM   1745  C C   . ILE A 1 203 ? 4.835   -5.119  -13.164 1.00 18.37  ? 203 ILE A C   1 
ATOM   1746  O O   . ILE A 1 203 ? 4.776   -5.442  -14.358 1.00 20.81  ? 203 ILE A O   1 
ATOM   1747  C CB  . ILE A 1 203 ? 5.737   -2.787  -12.714 1.00 21.35  ? 203 ILE A CB  1 
ATOM   1748  C CG1 . ILE A 1 203 ? 5.325   -1.343  -12.412 1.00 19.26  ? 203 ILE A CG1 1 
ATOM   1749  C CG2 . ILE A 1 203 ? 6.475   -2.845  -14.045 1.00 19.29  ? 203 ILE A CG2 1 
ATOM   1750  C CD1 . ILE A 1 203 ? 6.475   -0.358  -12.422 1.00 20.70  ? 203 ILE A CD1 1 
ATOM   1751  N N   . LEU A 1 204 ? 5.183   -5.991  -12.215 1.00 18.87  ? 204 LEU A N   1 
ATOM   1752  C CA  . LEU A 1 204 ? 5.500   -7.372  -12.560 1.00 23.24  ? 204 LEU A CA  1 
ATOM   1753  C C   . LEU A 1 204 ? 4.281   -8.104  -13.114 1.00 27.59  ? 204 LEU A C   1 
ATOM   1754  O O   . LEU A 1 204 ? 4.415   -8.956  -14.001 1.00 30.73  ? 204 LEU A O   1 
ATOM   1755  C CB  . LEU A 1 204 ? 6.051   -8.103  -11.333 1.00 19.68  ? 204 LEU A CB  1 
ATOM   1756  C CG  . LEU A 1 204 ? 7.430   -7.640  -10.851 1.00 15.81  ? 204 LEU A CG  1 
ATOM   1757  C CD1 . LEU A 1 204 ? 7.994   -8.593  -9.807  1.00 15.63  ? 204 LEU A CD1 1 
ATOM   1758  C CD2 . LEU A 1 204 ? 8.383   -7.508  -12.029 1.00 18.45  ? 204 LEU A CD2 1 
ATOM   1759  N N   . LEU A 1 205 ? 3.084   -7.797  -12.603 1.00 24.45  ? 205 LEU A N   1 
ATOM   1760  C CA  . LEU A 1 205 ? 1.893   -8.518  -13.042 1.00 17.69  ? 205 LEU A CA  1 
ATOM   1761  C C   . LEU A 1 205 ? 1.320   -7.946  -14.330 1.00 23.70  ? 205 LEU A C   1 
ATOM   1762  O O   . LEU A 1 205 ? 0.880   -8.703  -15.204 1.00 28.72  ? 205 LEU A O   1 
ATOM   1763  C CB  . LEU A 1 205 ? 0.825   -8.500  -11.947 1.00 17.00  ? 205 LEU A CB  1 
ATOM   1764  C CG  . LEU A 1 205 ? 1.079   -9.341  -10.698 1.00 16.78  ? 205 LEU A CG  1 
ATOM   1765  C CD1 . LEU A 1 205 ? 0.468   -8.653  -9.502  1.00 16.01  ? 205 LEU A CD1 1 
ATOM   1766  C CD2 . LEU A 1 205 ? 0.494   -10.725 -10.881 1.00 39.12  ? 205 LEU A CD2 1 
ATOM   1767  N N   . ASN A 1 206 ? 1.293   -6.625  -14.456 1.00 28.14  ? 206 ASN A N   1 
ATOM   1768  C CA  . ASN A 1 206 ? 0.808   -5.976  -15.671 1.00 23.00  ? 206 ASN A CA  1 
ATOM   1769  C C   . ASN A 1 206 ? 1.482   -4.620  -15.834 1.00 26.66  ? 206 ASN A C   1 
ATOM   1770  O O   . ASN A 1 206 ? 1.129   -3.665  -15.132 1.00 24.30  ? 206 ASN A O   1 
ATOM   1771  C CB  . ASN A 1 206 ? -0.708  -5.821  -15.629 1.00 23.54  ? 206 ASN A CB  1 
ATOM   1772  C CG  . ASN A 1 206 ? -1.296  -5.504  -16.985 1.00 33.48  ? 206 ASN A CG  1 
ATOM   1773  O OD1 . ASN A 1 206 ? -0.568  -5.329  -17.962 1.00 32.70  ? 206 ASN A OD1 1 
ATOM   1774  N ND2 . ASN A 1 206 ? -2.618  -5.429  -17.055 1.00 36.65  ? 206 ASN A ND2 1 
ATOM   1775  N N   . PRO A 1 207 ? 2.462   -4.498  -16.735 1.00 27.33  ? 207 PRO A N   1 
ATOM   1776  C CA  . PRO A 1 207 ? 3.151   -3.210  -16.908 1.00 26.82  ? 207 PRO A CA  1 
ATOM   1777  C C   . PRO A 1 207 ? 2.253   -2.077  -17.387 1.00 28.82  ? 207 PRO A C   1 
ATOM   1778  O O   . PRO A 1 207 ? 2.676   -0.917  -17.319 1.00 34.86  ? 207 PRO A O   1 
ATOM   1779  C CB  . PRO A 1 207 ? 4.236   -3.531  -17.944 1.00 23.01  ? 207 PRO A CB  1 
ATOM   1780  C CG  . PRO A 1 207 ? 4.490   -4.992  -17.759 1.00 24.02  ? 207 PRO A CG  1 
ATOM   1781  C CD  . PRO A 1 207 ? 3.131   -5.576  -17.481 1.00 20.58  ? 207 PRO A CD  1 
ATOM   1782  N N   . ASN A 1 208 ? 1.045   -2.367  -17.875 1.00 25.69  ? 208 ASN A N   1 
ATOM   1783  C CA  . ASN A 1 208 ? 0.148   -1.309  -18.326 1.00 25.92  ? 208 ASN A CA  1 
ATOM   1784  C C   . ASN A 1 208 ? -0.424  -0.488  -17.177 1.00 28.63  ? 208 ASN A C   1 
ATOM   1785  O O   . ASN A 1 208 ? -1.092  0.520   -17.432 1.00 32.96  ? 208 ASN A O   1 
ATOM   1786  C CB  . ASN A 1 208 ? -0.990  -1.899  -19.158 1.00 28.91  ? 208 ASN A CB  1 
ATOM   1787  C CG  . ASN A 1 208 ? -0.504  -2.506  -20.457 1.00 27.60  ? 208 ASN A CG  1 
ATOM   1788  O OD1 . ASN A 1 208 ? 0.220   -1.864  -21.219 1.00 38.97  ? 208 ASN A OD1 1 
ATOM   1789  N ND2 . ASN A 1 208 ? -0.899  -3.746  -20.718 1.00 33.02  ? 208 ASN A ND2 1 
ATOM   1790  N N   . CYS A 1 209 ? -0.187  -0.898  -15.930 1.00 24.88  ? 209 CYS A N   1 
ATOM   1791  C CA  . CYS A 1 209 ? -0.677  -0.152  -14.778 1.00 23.08  ? 209 CYS A CA  1 
ATOM   1792  C C   . CYS A 1 209 ? 0.009   1.199   -14.623 1.00 29.03  ? 209 CYS A C   1 
ATOM   1793  O O   . CYS A 1 209 ? -0.491  2.054   -13.883 1.00 32.51  ? 209 CYS A O   1 
ATOM   1794  C CB  . CYS A 1 209 ? -0.487  -0.979  -13.507 1.00 19.23  ? 209 CYS A CB  1 
ATOM   1795  S SG  . CYS A 1 209 ? 1.236   -1.257  -13.060 1.00 28.23  ? 209 CYS A SG  1 
ATOM   1796  N N   . VAL A 1 210 ? 1.148   1.408   -15.289 1.00 26.02  ? 210 VAL A N   1 
ATOM   1797  C CA  . VAL A 1 210 ? 1.787   2.716   -15.269 1.00 19.26  ? 210 VAL A CA  1 
ATOM   1798  C C   . VAL A 1 210 ? 0.905   3.767   -15.927 1.00 21.26  ? 210 VAL A C   1 
ATOM   1799  O O   . VAL A 1 210 ? 1.039   4.961   -15.633 1.00 24.45  ? 210 VAL A O   1 
ATOM   1800  C CB  . VAL A 1 210 ? 3.173   2.654   -15.947 1.00 24.60  ? 210 VAL A CB  1 
ATOM   1801  C CG1 . VAL A 1 210 ? 3.940   1.417   -15.499 1.00 22.94  ? 210 VAL A CG1 1 
ATOM   1802  C CG2 . VAL A 1 210 ? 3.028   2.675   -17.462 1.00 24.77  ? 210 VAL A CG2 1 
ATOM   1803  N N   . TYR A 1 211 ? -0.008  3.348   -16.808 1.00 23.99  ? 211 TYR A N   1 
ATOM   1804  C CA  . TYR A 1 211 ? -0.870  4.259   -17.550 1.00 21.90  ? 211 TYR A CA  1 
ATOM   1805  C C   . TYR A 1 211 ? -2.135  4.649   -16.799 1.00 23.94  ? 211 TYR A C   1 
ATOM   1806  O O   . TYR A 1 211 ? -2.875  5.513   -17.278 1.00 29.32  ? 211 TYR A O   1 
ATOM   1807  C CB  . TYR A 1 211 ? -1.257  3.632   -18.889 1.00 23.38  ? 211 TYR A CB  1 
ATOM   1808  C CG  . TYR A 1 211 ? -0.079  3.295   -19.769 1.00 23.67  ? 211 TYR A CG  1 
ATOM   1809  C CD1 . TYR A 1 211 ? 0.755   4.293   -20.254 1.00 24.22  ? 211 TYR A CD1 1 
ATOM   1810  C CD2 . TYR A 1 211 ? 0.204   1.979   -20.108 1.00 23.90  ? 211 TYR A CD2 1 
ATOM   1811  C CE1 . TYR A 1 211 ? 1.836   3.989   -21.056 1.00 24.80  ? 211 TYR A CE1 1 
ATOM   1812  C CE2 . TYR A 1 211 ? 1.284   1.666   -20.908 1.00 24.28  ? 211 TYR A CE2 1 
ATOM   1813  C CZ  . TYR A 1 211 ? 2.097   2.675   -21.381 1.00 25.63  ? 211 TYR A CZ  1 
ATOM   1814  O OH  . TYR A 1 211 ? 3.174   2.369   -22.180 1.00 38.59  ? 211 TYR A OH  1 
ATOM   1815  N N   . GLU A 1 212 ? -2.407  4.034   -15.646 1.00 24.52  ? 212 GLU A N   1 
ATOM   1816  C CA  . GLU A 1 212 ? -3.587  4.412   -14.877 1.00 27.37  ? 212 GLU A CA  1 
ATOM   1817  C C   . GLU A 1 212 ? -3.511  5.871   -14.444 1.00 30.42  ? 212 GLU A C   1 
ATOM   1818  O O   . GLU A 1 212 ? -4.507  6.601   -14.515 1.00 34.11  ? 212 GLU A O   1 
ATOM   1819  C CB  . GLU A 1 212 ? -3.739  3.498   -13.660 1.00 24.53  ? 212 GLU A CB  1 
ATOM   1820  C CG  . GLU A 1 212 ? -3.600  2.013   -13.964 1.00 31.86  ? 212 GLU A CG  1 
ATOM   1821  C CD  . GLU A 1 212 ? -4.836  1.214   -13.598 1.00 38.57  ? 212 GLU A CD  1 
ATOM   1822  O OE1 . GLU A 1 212 ? -5.947  1.782   -13.633 1.00 47.19  ? 212 GLU A OE1 1 
ATOM   1823  O OE2 . GLU A 1 212 ? -4.693  0.016   -13.271 1.00 40.72  ? 212 GLU A OE2 1 
ATOM   1824  N N   . THR A 1 213 ? -2.332  6.318   -14.008 1.00 26.90  ? 213 THR A N   1 
ATOM   1825  C CA  . THR A 1 213 ? -2.155  7.667   -13.495 1.00 26.56  ? 213 THR A CA  1 
ATOM   1826  C C   . THR A 1 213 ? -1.291  8.561   -14.374 1.00 31.84  ? 213 THR A C   1 
ATOM   1827  O O   . THR A 1 213 ? -1.329  9.784   -14.202 1.00 33.06  ? 213 THR A O   1 
ATOM   1828  C CB  . THR A 1 213 ? -1.547  7.620   -12.085 1.00 20.59  ? 213 THR A CB  1 
ATOM   1829  O OG1 . THR A 1 213 ? -0.455  6.694   -12.066 1.00 19.67  ? 213 THR A OG1 1 
ATOM   1830  C CG2 . THR A 1 213 ? -2.594  7.178   -11.073 1.00 17.45  ? 213 THR A CG2 1 
ATOM   1831  N N   . THR A 1 214 ? -0.513  7.995   -15.297 1.00 30.14  ? 214 THR A N   1 
ATOM   1832  C CA  . THR A 1 214 ? 0.342   8.776   -16.191 1.00 31.32  ? 214 THR A CA  1 
ATOM   1833  C C   . THR A 1 214 ? 0.222   8.206   -17.600 1.00 31.90  ? 214 THR A C   1 
ATOM   1834  O O   . THR A 1 214 ? 1.023   7.358   -18.017 1.00 34.51  ? 214 THR A O   1 
ATOM   1835  C CB  . THR A 1 214 ? 1.795   8.773   -15.713 1.00 35.15  ? 214 THR A CB  1 
ATOM   1836  O OG1 . THR A 1 214 ? 2.166   7.448   -15.314 1.00 32.24  ? 214 THR A OG1 1 
ATOM   1837  C CG2 . THR A 1 214 ? 1.975   9.718   -14.528 1.00 29.43  ? 214 THR A CG2 1 
ATOM   1838  N N   . PRO A 1 215 ? -0.768  8.662   -18.371 1.00 25.09  ? 215 PRO A N   1 
ATOM   1839  C CA  . PRO A 1 215 ? -1.152  7.959   -19.605 1.00 25.50  ? 215 PRO A CA  1 
ATOM   1840  C C   . PRO A 1 215 ? -0.261  8.209   -20.814 1.00 29.30  ? 215 PRO A C   1 
ATOM   1841  O O   . PRO A 1 215 ? -0.573  7.696   -21.893 1.00 32.08  ? 215 PRO A O   1 
ATOM   1842  C CB  . PRO A 1 215 ? -2.572  8.495   -19.872 1.00 27.80  ? 215 PRO A CB  1 
ATOM   1843  C CG  . PRO A 1 215 ? -2.994  9.189   -18.603 1.00 26.85  ? 215 PRO A CG  1 
ATOM   1844  C CD  . PRO A 1 215 ? -1.733  9.710   -18.014 1.00 24.84  ? 215 PRO A CD  1 
ATOM   1845  N N   . ASN A 1 216 ? 0.825   8.971   -20.696 1.00 35.56  ? 216 ASN A N   1 
ATOM   1846  C CA  . ASN A 1 216 ? 1.650   9.297   -21.853 1.00 29.22  ? 216 ASN A CA  1 
ATOM   1847  C C   . ASN A 1 216 ? 3.075   8.772   -21.757 1.00 31.31  ? 216 ASN A C   1 
ATOM   1848  O O   . ASN A 1 216 ? 3.880   9.048   -22.653 1.00 30.34  ? 216 ASN A O   1 
ATOM   1849  C CB  . ASN A 1 216 ? 1.687   10.816  -22.070 1.00 30.63  ? 216 ASN A CB  1 
ATOM   1850  C CG  . ASN A 1 216 ? 0.456   11.334  -22.787 1.00 41.31  ? 216 ASN A CG  1 
ATOM   1851  O OD1 . ASN A 1 216 ? -0.516  11.740  -22.154 1.00 42.02  ? 216 ASN A OD1 1 
ATOM   1852  N ND2 . ASN A 1 216 ? 0.495   11.333  -24.113 1.00 53.73  ? 216 ASN A ND2 1 
ATOM   1853  N N   . VAL A 1 217 ? 3.408   8.018   -20.710 1.00 28.40  ? 217 VAL A N   1 
ATOM   1854  C CA  . VAL A 1 217 ? 4.790   7.609   -20.495 1.00 30.09  ? 217 VAL A CA  1 
ATOM   1855  C C   . VAL A 1 217 ? 5.194   6.534   -21.498 1.00 28.68  ? 217 VAL A C   1 
ATOM   1856  O O   . VAL A 1 217 ? 4.362   5.768   -22.006 1.00 33.86  ? 217 VAL A O   1 
ATOM   1857  C CB  . VAL A 1 217 ? 4.989   7.127   -19.048 1.00 27.50  ? 217 VAL A CB  1 
ATOM   1858  C CG1 . VAL A 1 217 ? 4.302   8.075   -18.091 1.00 35.37  ? 217 VAL A CG1 1 
ATOM   1859  C CG2 . VAL A 1 217 ? 4.442   5.725   -18.871 1.00 22.36  ? 217 VAL A CG2 1 
ATOM   1860  N N   . LYS A 1 218 ? 6.493   6.485   -21.796 1.00 35.98  ? 218 LYS A N   1 
ATOM   1861  C CA  . LYS A 1 218 ? 7.071   5.528   -22.739 1.00 32.18  ? 218 LYS A CA  1 
ATOM   1862  C C   . LYS A 1 218 ? 7.821   4.469   -21.937 1.00 29.52  ? 218 LYS A C   1 
ATOM   1863  O O   . LYS A 1 218 ? 8.955   4.694   -21.507 1.00 32.83  ? 218 LYS A O   1 
ATOM   1864  C CB  . LYS A 1 218 ? 8.001   6.236   -23.722 1.00 30.17  ? 218 LYS A CB  1 
ATOM   1865  C CG  . LYS A 1 218 ? 7.317   6.803   -24.956 1.00 30.03  ? 218 LYS A CG  1 
ATOM   1866  C CD  . LYS A 1 218 ? 7.879   6.184   -26.225 1.00 45.06  ? 218 LYS A CD  1 
ATOM   1867  C CE  . LYS A 1 218 ? 7.707   7.106   -27.419 1.00 42.31  ? 218 LYS A CE  1 
ATOM   1868  N NZ  . LYS A 1 218 ? 8.710   6.814   -28.480 1.00 46.47  ? 218 LYS A NZ  1 
ATOM   1869  N N   . ILE A 1 219 ? 7.193   3.313   -21.745 1.00 24.94  ? 219 ILE A N   1 
ATOM   1870  C CA  . ILE A 1 219 ? 7.827   2.208   -21.031 1.00 24.38  ? 219 ILE A CA  1 
ATOM   1871  C C   . ILE A 1 219 ? 8.344   1.209   -22.059 1.00 25.10  ? 219 ILE A C   1 
ATOM   1872  O O   . ILE A 1 219 ? 7.859   1.197   -23.200 1.00 26.45  ? 219 ILE A O   1 
ATOM   1873  C CB  . ILE A 1 219 ? 6.858   1.556   -20.030 1.00 27.90  ? 219 ILE A CB  1 
ATOM   1874  C CG1 . ILE A 1 219 ? 5.848   0.658   -20.744 1.00 27.40  ? 219 ILE A CG1 1 
ATOM   1875  C CG2 . ILE A 1 219 ? 6.159   2.620   -19.205 1.00 31.03  ? 219 ILE A CG2 1 
ATOM   1876  C CD1 . ILE A 1 219 ? 4.866   -0.014  -19.801 1.00 32.93  ? 219 ILE A CD1 1 
ATOM   1877  N N   . PRO A 1 220 ? 9.330   0.365   -21.720 1.00 24.79  ? 220 PRO A N   1 
ATOM   1878  C CA  . PRO A 1 220 ? 9.914   -0.520  -22.736 1.00 26.09  ? 220 PRO A CA  1 
ATOM   1879  C C   . PRO A 1 220 ? 8.960   -1.612  -23.190 1.00 30.14  ? 220 PRO A C   1 
ATOM   1880  O O   . PRO A 1 220 ? 7.849   -1.740  -22.667 1.00 45.44  ? 220 PRO A O   1 
ATOM   1881  C CB  . PRO A 1 220 ? 11.136  -1.108  -22.022 1.00 25.54  ? 220 PRO A CB  1 
ATOM   1882  C CG  . PRO A 1 220 ? 10.764  -1.088  -20.587 1.00 23.80  ? 220 PRO A CG  1 
ATOM   1883  C CD  . PRO A 1 220 ? 9.952   0.163   -20.398 1.00 26.72  ? 220 PRO A CD  1 
ATOM   1884  N N   . ASP A 1 221 ? 9.387   -2.400  -24.170 1.00 36.17  ? 221 ASP A N   1 
ATOM   1885  C CA  . ASP A 1 221 ? 8.588   -3.505  -24.681 1.00 37.30  ? 221 ASP A CA  1 
ATOM   1886  C C   . ASP A 1 221 ? 8.857   -4.743  -23.835 1.00 27.68  ? 221 ASP A C   1 
ATOM   1887  O O   . ASP A 1 221 ? 9.982   -5.256  -23.812 1.00 33.30  ? 221 ASP A O   1 
ATOM   1888  C CB  . ASP A 1 221 ? 8.912   -3.770  -26.151 1.00 32.56  ? 221 ASP A CB  1 
ATOM   1889  C CG  . ASP A 1 221 ? 8.183   -4.977  -26.700 1.00 56.04  ? 221 ASP A CG  1 
ATOM   1890  O OD1 . ASP A 1 221 ? 6.938   -4.926  -26.804 1.00 64.11  ? 221 ASP A OD1 1 
ATOM   1891  O OD2 . ASP A 1 221 ? 8.854   -5.977  -27.032 1.00 60.88  ? 221 ASP A OD2 1 
ATOM   1892  N N   . PHE A 1 222 ? 7.823   -5.221  -23.142 1.00 29.80  ? 222 PHE A N   1 
ATOM   1893  C CA  . PHE A 1 222 ? 7.945   -6.360  -22.231 1.00 29.60  ? 222 PHE A CA  1 
ATOM   1894  C C   . PHE A 1 222 ? 7.694   -7.640  -23.019 1.00 32.11  ? 222 PHE A C   1 
ATOM   1895  O O   . PHE A 1 222 ? 6.571   -8.138  -23.099 1.00 37.66  ? 222 PHE A O   1 
ATOM   1896  C CB  . PHE A 1 222 ? 6.977   -6.218  -21.063 1.00 27.26  ? 222 PHE A CB  1 
ATOM   1897  C CG  . PHE A 1 222 ? 7.456   -5.283  -19.989 1.00 33.43  ? 222 PHE A CG  1 
ATOM   1898  C CD1 . PHE A 1 222 ? 7.526   -3.919  -20.217 1.00 35.55  ? 222 PHE A CD1 1 
ATOM   1899  C CD2 . PHE A 1 222 ? 7.837   -5.772  -18.751 1.00 22.00  ? 222 PHE A CD2 1 
ATOM   1900  C CE1 . PHE A 1 222 ? 7.966   -3.059  -19.229 1.00 36.81  ? 222 PHE A CE1 1 
ATOM   1901  C CE2 . PHE A 1 222 ? 8.277   -4.918  -17.759 1.00 20.86  ? 222 PHE A CE2 1 
ATOM   1902  C CZ  . PHE A 1 222 ? 8.342   -3.561  -17.998 1.00 25.46  ? 222 PHE A CZ  1 
ATOM   1903  N N   . ALA A 1 223 ? 8.761   -8.187  -23.597 1.00 28.36  ? 223 ALA A N   1 
ATOM   1904  C CA  . ALA A 1 223 ? 8.672   -9.392  -24.409 1.00 29.82  ? 223 ALA A CA  1 
ATOM   1905  C C   . ALA A 1 223 ? 8.641   -10.669 -23.578 1.00 29.93  ? 223 ALA A C   1 
ATOM   1906  O O   . ALA A 1 223 ? 8.636   -11.763 -24.151 1.00 48.73  ? 223 ALA A O   1 
ATOM   1907  C CB  . ALA A 1 223 ? 9.840   -9.447  -25.396 1.00 34.14  ? 223 ALA A CB  1 
ATOM   1908  N N   . VAL A 1 224 ? 8.640   -10.559 -22.248 1.00 38.98  ? 224 VAL A N   1 
ATOM   1909  C CA  . VAL A 1 224 ? 8.530   -11.705 -21.353 1.00 41.53  ? 224 VAL A CA  1 
ATOM   1910  C C   . VAL A 1 224 ? 7.474   -11.391 -20.299 1.00 32.12  ? 224 VAL A C   1 
ATOM   1911  O O   . VAL A 1 224 ? 7.102   -10.237 -20.079 1.00 31.12  ? 224 VAL A O   1 
ATOM   1912  C CB  . VAL A 1 224 ? 9.874   -12.071 -20.676 1.00 37.67  ? 224 VAL A CB  1 
ATOM   1913  C CG1 . VAL A 1 224 ? 9.896   -13.543 -20.286 1.00 34.71  ? 224 VAL A CG1 1 
ATOM   1914  C CG2 . VAL A 1 224 ? 11.049  -11.748 -21.585 1.00 36.35  ? 224 VAL A CG2 1 
ATOM   1915  N N   . SER A 1 225 ? 6.983   -12.444 -19.652 1.00 31.79  ? 225 SER A N   1 
ATOM   1916  C CA  . SER A 1 225 ? 5.993   -12.325 -18.590 1.00 25.08  ? 225 SER A CA  1 
ATOM   1917  C C   . SER A 1 225 ? 6.689   -12.427 -17.239 1.00 28.02  ? 225 SER A C   1 
ATOM   1918  O O   . SER A 1 225 ? 7.362   -13.425 -16.956 1.00 30.98  ? 225 SER A O   1 
ATOM   1919  C CB  . SER A 1 225 ? 4.918   -13.402 -18.720 1.00 25.15  ? 225 SER A CB  1 
ATOM   1920  O OG  . SER A 1 225 ? 4.181   -13.533 -17.516 1.00 28.45  ? 225 SER A OG  1 
ATOM   1921  N N   . PHE A 1 226 ? 6.526   -11.396 -16.409 1.00 29.16  ? 226 PHE A N   1 
ATOM   1922  C CA  . PHE A 1 226 ? 7.020   -11.396 -15.039 1.00 28.12  ? 226 PHE A CA  1 
ATOM   1923  C C   . PHE A 1 226 ? 5.966   -11.862 -14.040 1.00 20.19  ? 226 PHE A C   1 
ATOM   1924  O O   . PHE A 1 226 ? 6.079   -11.567 -12.845 1.00 18.96  ? 226 PHE A O   1 
ATOM   1925  C CB  . PHE A 1 226 ? 7.518   -9.999  -14.660 1.00 23.80  ? 226 PHE A CB  1 
ATOM   1926  C CG  . PHE A 1 226 ? 8.789   -9.597  -15.353 1.00 22.95  ? 226 PHE A CG  1 
ATOM   1927  C CD1 . PHE A 1 226 ? 9.994   -10.195 -15.021 1.00 21.63  ? 226 PHE A CD1 1 
ATOM   1928  C CD2 . PHE A 1 226 ? 8.781   -8.616  -16.331 1.00 24.03  ? 226 PHE A CD2 1 
ATOM   1929  C CE1 . PHE A 1 226 ? 11.168  -9.823  -15.654 1.00 22.48  ? 226 PHE A CE1 1 
ATOM   1930  C CE2 . PHE A 1 226 ? 9.952   -8.240  -16.967 1.00 26.37  ? 226 PHE A CE2 1 
ATOM   1931  C CZ  . PHE A 1 226 ? 11.146  -8.844  -16.628 1.00 21.84  ? 226 PHE A CZ  1 
ATOM   1932  N N   . ARG A 1 227 ? 4.943   -12.582 -14.506 1.00 23.80  ? 227 ARG A N   1 
ATOM   1933  C CA  . ARG A 1 227 ? 3.816   -12.933 -13.650 1.00 21.64  ? 227 ARG A CA  1 
ATOM   1934  C C   . ARG A 1 227 ? 4.130   -14.085 -12.703 1.00 22.02  ? 227 ARG A C   1 
ATOM   1935  O O   . ARG A 1 227 ? 3.623   -14.106 -11.577 1.00 24.70  ? 227 ARG A O   1 
ATOM   1936  C CB  . ARG A 1 227 ? 2.601   -13.271 -14.515 1.00 25.91  ? 227 ARG A CB  1 
ATOM   1937  C CG  . ARG A 1 227 ? 2.095   -12.091 -15.332 1.00 28.10  ? 227 ARG A CG  1 
ATOM   1938  C CD  . ARG A 1 227 ? 0.665   -12.305 -15.795 1.00 31.57  ? 227 ARG A CD  1 
ATOM   1939  N NE  . ARG A 1 227 ? -0.211  -12.673 -14.690 1.00 32.86  ? 227 ARG A NE  1 
ATOM   1940  C CZ  . ARG A 1 227 ? -1.319  -12.021 -14.364 1.00 41.09  ? 227 ARG A CZ  1 
ATOM   1941  N NH1 . ARG A 1 227 ? -1.724  -10.962 -15.046 1.00 42.40  ? 227 ARG A NH1 1 
ATOM   1942  N NH2 . ARG A 1 227 ? -2.039  -12.443 -13.327 1.00 49.66  ? 227 ARG A NH2 1 
ATOM   1943  N N   . GLU A 1 228 ? 4.941   -15.054 -13.133 1.00 24.94  ? 228 GLU A N   1 
ATOM   1944  C CA  . GLU A 1 228 ? 5.325   -16.140 -12.236 1.00 22.73  ? 228 GLU A CA  1 
ATOM   1945  C C   . GLU A 1 228 ? 6.373   -15.687 -11.229 1.00 32.89  ? 228 GLU A C   1 
ATOM   1946  O O   . GLU A 1 228 ? 6.344   -16.110 -10.068 1.00 38.23  ? 228 GLU A O   1 
ATOM   1947  C CB  . GLU A 1 228 ? 5.836   -17.336 -13.042 1.00 30.59  ? 228 GLU A CB  1 
ATOM   1948  C CG  . GLU A 1 228 ? 6.257   -18.537 -12.197 1.00 33.37  ? 228 GLU A CG  1 
ATOM   1949  C CD  . GLU A 1 228 ? 5.213   -18.942 -11.171 1.00 46.69  ? 228 GLU A CD  1 
ATOM   1950  O OE1 . GLU A 1 228 ? 4.026   -19.063 -11.543 1.00 54.17  ? 228 GLU A OE1 1 
ATOM   1951  O OE2 . GLU A 1 228 ? 5.581   -19.145 -9.994  1.00 48.19  ? 228 GLU A OE2 1 
ATOM   1952  N N   . ASP A 1 229 ? 7.302   -14.829 -11.656 1.00 26.82  ? 229 ASP A N   1 
ATOM   1953  C CA  . ASP A 1 229 ? 8.314   -14.315 -10.739 1.00 19.66  ? 229 ASP A CA  1 
ATOM   1954  C C   . ASP A 1 229 ? 7.677   -13.499 -9.623  1.00 21.37  ? 229 ASP A C   1 
ATOM   1955  O O   . ASP A 1 229 ? 8.136   -13.535 -8.475  1.00 17.70  ? 229 ASP A O   1 
ATOM   1956  C CB  . ASP A 1 229 ? 9.336   -13.477 -11.508 1.00 19.85  ? 229 ASP A CB  1 
ATOM   1957  C CG  . ASP A 1 229 ? 10.439  -14.319 -12.119 1.00 33.41  ? 229 ASP A CG  1 
ATOM   1958  O OD1 . ASP A 1 229 ? 10.445  -15.547 -11.897 1.00 41.70  ? 229 ASP A OD1 1 
ATOM   1959  O OD2 . ASP A 1 229 ? 11.298  -13.755 -12.831 1.00 30.01  ? 229 ASP A OD2 1 
ATOM   1960  N N   . ALA A 1 230 ? 6.618   -12.750 -9.945  1.00 29.41  ? 230 ALA A N   1 
ATOM   1961  C CA  . ALA A 1 230 ? 5.887   -12.015 -8.918  1.00 17.71  ? 230 ALA A CA  1 
ATOM   1962  C C   . ALA A 1 230 ? 5.257   -12.966 -7.909  1.00 21.84  ? 230 ALA A C   1 
ATOM   1963  O O   . ALA A 1 230 ? 5.222   -12.674 -6.708  1.00 30.90  ? 230 ALA A O   1 
ATOM   1964  C CB  . ALA A 1 230 ? 4.820   -11.127 -9.558  1.00 16.35  ? 230 ALA A CB  1 
ATOM   1965  N N   . SER A 1 231 ? 4.745   -14.106 -8.380  1.00 22.90  ? 231 SER A N   1 
ATOM   1966  C CA  . SER A 1 231 ? 4.227   -15.117 -7.463  1.00 23.25  ? 231 SER A CA  1 
ATOM   1967  C C   . SER A 1 231 ? 5.335   -15.678 -6.582  1.00 20.39  ? 231 SER A C   1 
ATOM   1968  O O   . SER A 1 231 ? 5.120   -15.937 -5.392  1.00 20.23  ? 231 SER A O   1 
ATOM   1969  C CB  . SER A 1 231 ? 3.544   -16.241 -8.240  1.00 25.91  ? 231 SER A CB  1 
ATOM   1970  O OG  . SER A 1 231 ? 2.267   -15.837 -8.704  1.00 35.98  ? 231 SER A OG  1 
ATOM   1971  N N   . LYS A 1 232 ? 6.528   -15.878 -7.150  1.00 18.44  ? 232 LYS A N   1 
ATOM   1972  C CA  . LYS A 1 232 ? 7.646   -16.385 -6.361  1.00 19.32  ? 232 LYS A CA  1 
ATOM   1973  C C   . LYS A 1 232 ? 8.034   -15.409 -5.257  1.00 18.00  ? 232 LYS A C   1 
ATOM   1974  O O   . LYS A 1 232 ? 8.405   -15.826 -4.154  1.00 17.55  ? 232 LYS A O   1 
ATOM   1975  C CB  . LYS A 1 232 ? 8.841   -16.673 -7.271  1.00 20.41  ? 232 LYS A CB  1 
ATOM   1976  C CG  . LYS A 1 232 ? 8.806   -18.051 -7.911  1.00 24.14  ? 232 LYS A CG  1 
ATOM   1977  C CD  . LYS A 1 232 ? 9.829   -18.179 -9.025  1.00 22.64  ? 232 LYS A CD  1 
ATOM   1978  C CE  . LYS A 1 232 ? 9.249   -18.914 -10.220 1.00 35.22  ? 232 LYS A CE  1 
ATOM   1979  N NZ  . LYS A 1 232 ? 9.596   -18.251 -11.506 1.00 42.55  ? 232 LYS A NZ  1 
ATOM   1980  N N   . HIS A 1 233 ? 7.952   -14.105 -5.532  1.00 23.06  ? 233 HIS A N   1 
ATOM   1981  C CA  . HIS A 1 233 ? 8.308   -13.115 -4.521  1.00 15.59  ? 233 HIS A CA  1 
ATOM   1982  C C   . HIS A 1 233 ? 7.416   -13.238 -3.291  1.00 17.74  ? 233 HIS A C   1 
ATOM   1983  O O   . HIS A 1 233 ? 7.900   -13.152 -2.156  1.00 20.93  ? 233 HIS A O   1 
ATOM   1984  C CB  . HIS A 1 233 ? 8.228   -11.708 -5.114  1.00 14.88  ? 233 HIS A CB  1 
ATOM   1985  C CG  . HIS A 1 233 ? 9.452   -11.304 -5.878  1.00 15.30  ? 233 HIS A CG  1 
ATOM   1986  N ND1 . HIS A 1 233 ? 10.609  -10.880 -5.260  1.00 15.16  ? 233 HIS A ND1 1 
ATOM   1987  C CD2 . HIS A 1 233 ? 9.695   -11.246 -7.210  1.00 15.97  ? 233 HIS A CD2 1 
ATOM   1988  C CE1 . HIS A 1 233 ? 11.514  -10.588 -6.176  1.00 15.74  ? 233 HIS A CE1 1 
ATOM   1989  N NE2 . HIS A 1 233 ? 10.985  -10.800 -7.367  1.00 16.23  ? 233 HIS A NE2 1 
ATOM   1990  N N   . VAL A 1 234 ? 6.112   -13.438 -3.492  1.00 17.66  ? 234 VAL A N   1 
ATOM   1991  C CA  . VAL A 1 234 ? 5.216   -13.658 -2.359  1.00 20.41  ? 234 VAL A CA  1 
ATOM   1992  C C   . VAL A 1 234 ? 5.441   -15.041 -1.761  1.00 16.58  ? 234 VAL A C   1 
ATOM   1993  O O   . VAL A 1 234 ? 5.570   -15.194 -0.540  1.00 22.13  ? 234 VAL A O   1 
ATOM   1994  C CB  . VAL A 1 234 ? 3.748   -13.464 -2.783  1.00 17.04  ? 234 VAL A CB  1 
ATOM   1995  C CG1 . VAL A 1 234 ? 2.851   -13.349 -1.556  1.00 14.06  ? 234 VAL A CG1 1 
ATOM   1996  C CG2 . VAL A 1 234 ? 3.604   -12.238 -3.670  1.00 14.03  ? 234 VAL A CG2 1 
ATOM   1997  N N   . GLU A 1 235 ? 5.502   -16.066 -2.617  1.00 18.94  ? 235 GLU A N   1 
ATOM   1998  C CA  . GLU A 1 235 ? 5.554   -17.443 -2.135  1.00 19.97  ? 235 GLU A CA  1 
ATOM   1999  C C   . GLU A 1 235 ? 6.798   -17.692 -1.295  1.00 20.68  ? 235 GLU A C   1 
ATOM   2000  O O   . GLU A 1 235 ? 6.734   -18.369 -0.261  1.00 21.19  ? 235 GLU A O   1 
ATOM   2001  C CB  . GLU A 1 235 ? 5.505   -18.409 -3.319  1.00 24.58  ? 235 GLU A CB  1 
ATOM   2002  C CG  . GLU A 1 235 ? 4.139   -19.025 -3.577  1.00 31.64  ? 235 GLU A CG  1 
ATOM   2003  C CD  . GLU A 1 235 ? 4.081   -19.770 -4.897  1.00 59.70  ? 235 GLU A CD  1 
ATOM   2004  O OE1 . GLU A 1 235 ? 5.102   -20.377 -5.288  1.00 66.42  ? 235 GLU A OE1 1 
ATOM   2005  O OE2 . GLU A 1 235 ? 3.015   -19.749 -5.547  1.00 66.25  ? 235 GLU A OE2 1 
ATOM   2006  N N   . LEU A 1 236 ? 7.941   -17.155 -1.723  1.00 17.83  ? 236 LEU A N   1 
ATOM   2007  C CA  . LEU A 1 236 ? 9.168   -17.318 -0.956  1.00 18.18  ? 236 LEU A CA  1 
ATOM   2008  C C   . LEU A 1 236 ? 9.211   -16.394 0.253   1.00 17.13  ? 236 LEU A C   1 
ATOM   2009  O O   . LEU A 1 236 ? 9.828   -16.738 1.267   1.00 18.53  ? 236 LEU A O   1 
ATOM   2010  C CB  . LEU A 1 236 ? 10.380  -17.082 -1.855  1.00 18.63  ? 236 LEU A CB  1 
ATOM   2011  C CG  . LEU A 1 236 ? 10.433  -18.001 -3.077  1.00 19.84  ? 236 LEU A CG  1 
ATOM   2012  C CD1 . LEU A 1 236 ? 11.363  -17.441 -4.142  1.00 20.05  ? 236 LEU A CD1 1 
ATOM   2013  C CD2 . LEU A 1 236 ? 10.838  -19.412 -2.679  1.00 21.30  ? 236 LEU A CD2 1 
ATOM   2014  N N   . ALA A 1 237 ? 8.568   -15.227 0.170   1.00 16.11  ? 237 ALA A N   1 
ATOM   2015  C CA  . ALA A 1 237 ? 8.486   -14.352 1.334   1.00 15.62  ? 237 ALA A CA  1 
ATOM   2016  C C   . ALA A 1 237 ? 7.739   -15.029 2.473   1.00 19.13  ? 237 ALA A C   1 
ATOM   2017  O O   . ALA A 1 237 ? 8.098   -14.868 3.645   1.00 19.02  ? 237 ALA A O   1 
ATOM   2018  C CB  . ALA A 1 237 ? 7.803   -13.037 0.962   1.00 16.95  ? 237 ALA A CB  1 
ATOM   2019  N N   . LYS A 1 238 ? 6.694   -15.791 2.145   1.00 18.99  ? 238 LYS A N   1 
ATOM   2020  C CA  . LYS A 1 238 ? 5.925   -16.477 3.176   1.00 16.00  ? 238 LYS A CA  1 
ATOM   2021  C C   . LYS A 1 238 ? 6.745   -17.574 3.845   1.00 21.77  ? 238 LYS A C   1 
ATOM   2022  O O   . LYS A 1 238 ? 6.610   -17.809 5.051   1.00 28.46  ? 238 LYS A O   1 
ATOM   2023  C CB  . LYS A 1 238 ? 4.639   -17.045 2.577   1.00 16.35  ? 238 LYS A CB  1 
ATOM   2024  C CG  . LYS A 1 238 ? 3.612   -15.980 2.220   1.00 15.36  ? 238 LYS A CG  1 
ATOM   2025  C CD  . LYS A 1 238 ? 2.436   -16.563 1.457   1.00 15.93  ? 238 LYS A CD  1 
ATOM   2026  C CE  . LYS A 1 238 ? 1.687   -17.583 2.297   1.00 23.27  ? 238 LYS A CE  1 
ATOM   2027  N NZ  . LYS A 1 238 ? 0.975   -18.572 1.440   1.00 23.42  ? 238 LYS A NZ  1 
ATOM   2028  N N   . GLU A 1 239 ? 7.599   -18.262 3.082   1.00 18.06  ? 239 GLU A N   1 
ATOM   2029  C CA  . GLU A 1 239 ? 8.390   -19.339 3.668   1.00 19.38  ? 239 GLU A CA  1 
ATOM   2030  C C   . GLU A 1 239 ? 9.564   -18.810 4.489   1.00 20.73  ? 239 GLU A C   1 
ATOM   2031  O O   . GLU A 1 239 ? 9.900   -19.388 5.529   1.00 24.04  ? 239 GLU A O   1 
ATOM   2032  C CB  . GLU A 1 239 ? 8.873   -20.292 2.575   1.00 30.09  ? 239 GLU A CB  1 
ATOM   2033  C CG  . GLU A 1 239 ? 7.746   -21.096 1.940   1.00 42.73  ? 239 GLU A CG  1 
ATOM   2034  C CD  . GLU A 1 239 ? 6.962   -21.907 2.958   1.00 48.33  ? 239 GLU A CD  1 
ATOM   2035  O OE1 . GLU A 1 239 ? 7.534   -22.851 3.544   1.00 55.38  ? 239 GLU A OE1 1 
ATOM   2036  O OE2 . GLU A 1 239 ? 5.773   -21.592 3.179   1.00 38.15  ? 239 GLU A OE2 1 
ATOM   2037  N N   . LYS A 1 240 ? 10.206  -17.726 4.044   1.00 18.70  ? 240 LYS A N   1 
ATOM   2038  C CA  . LYS A 1 240 ? 11.256  -17.120 4.860   1.00 18.33  ? 240 LYS A CA  1 
ATOM   2039  C C   . LYS A 1 240 ? 10.686  -16.589 6.167   1.00 17.65  ? 240 LYS A C   1 
ATOM   2040  O O   . LYS A 1 240 ? 11.295  -16.746 7.232   1.00 24.00  ? 240 LYS A O   1 
ATOM   2041  C CB  . LYS A 1 240 ? 11.954  -15.997 4.092   1.00 18.84  ? 240 LYS A CB  1 
ATOM   2042  C CG  . LYS A 1 240 ? 13.080  -15.337 4.879   1.00 17.64  ? 240 LYS A CG  1 
ATOM   2043  C CD  . LYS A 1 240 ? 14.369  -16.130 4.746   1.00 34.09  ? 240 LYS A CD  1 
ATOM   2044  C CE  . LYS A 1 240 ? 15.210  -16.059 6.008   1.00 25.41  ? 240 LYS A CE  1 
ATOM   2045  N NZ  . LYS A 1 240 ? 16.345  -17.023 5.950   1.00 21.39  ? 240 LYS A NZ  1 
ATOM   2046  N N   . TYR A 1 241 ? 9.511   -15.959 6.101   1.00 16.59  ? 241 TYR A N   1 
ATOM   2047  C CA  . TYR A 1 241 ? 8.818   -15.530 7.310   1.00 16.08  ? 241 TYR A CA  1 
ATOM   2048  C C   . TYR A 1 241 ? 8.461   -16.726 8.182   1.00 17.17  ? 241 TYR A C   1 
ATOM   2049  O O   . TYR A 1 241 ? 8.514   -16.645 9.415   1.00 25.37  ? 241 TYR A O   1 
ATOM   2050  C CB  . TYR A 1 241 ? 7.566   -14.741 6.925   1.00 14.98  ? 241 TYR A CB  1 
ATOM   2051  C CG  . TYR A 1 241 ? 6.781   -14.158 8.080   1.00 14.45  ? 241 TYR A CG  1 
ATOM   2052  C CD1 . TYR A 1 241 ? 5.804   -14.901 8.729   1.00 18.77  ? 241 TYR A CD1 1 
ATOM   2053  C CD2 . TYR A 1 241 ? 6.996   -12.852 8.500   1.00 13.57  ? 241 TYR A CD2 1 
ATOM   2054  C CE1 . TYR A 1 241 ? 5.075   -14.369 9.775   1.00 19.83  ? 241 TYR A CE1 1 
ATOM   2055  C CE2 . TYR A 1 241 ? 6.270   -12.309 9.544   1.00 13.20  ? 241 TYR A CE2 1 
ATOM   2056  C CZ  . TYR A 1 241 ? 5.312   -13.073 10.178  1.00 15.01  ? 241 TYR A CZ  1 
ATOM   2057  O OH  . TYR A 1 241 ? 4.588   -12.539 11.220  1.00 19.33  ? 241 TYR A OH  1 
ATOM   2058  N N   . PHE A 1 242 ? 8.092   -17.848 7.557   1.00 20.29  ? 242 PHE A N   1 
ATOM   2059  C CA  . PHE A 1 242 ? 7.811   -19.063 8.315   1.00 19.28  ? 242 PHE A CA  1 
ATOM   2060  C C   . PHE A 1 242 ? 9.052   -19.554 9.046   1.00 22.82  ? 242 PHE A C   1 
ATOM   2061  O O   . PHE A 1 242 ? 8.959   -20.065 10.168  1.00 25.60  ? 242 PHE A O   1 
ATOM   2062  C CB  . PHE A 1 242 ? 7.273   -20.157 7.392   1.00 20.14  ? 242 PHE A CB  1 
ATOM   2063  C CG  . PHE A 1 242 ? 6.884   -21.418 8.114   1.00 21.56  ? 242 PHE A CG  1 
ATOM   2064  C CD1 . PHE A 1 242 ? 7.813   -22.419 8.352   1.00 23.08  ? 242 PHE A CD1 1 
ATOM   2065  C CD2 . PHE A 1 242 ? 5.590   -21.592 8.573   1.00 21.51  ? 242 PHE A CD2 1 
ATOM   2066  C CE1 . PHE A 1 242 ? 7.453   -23.570 9.028   1.00 29.17  ? 242 PHE A CE1 1 
ATOM   2067  C CE2 . PHE A 1 242 ? 5.225   -22.741 9.248   1.00 22.94  ? 242 PHE A CE2 1 
ATOM   2068  C CZ  . PHE A 1 242 ? 6.157   -23.730 9.476   1.00 27.46  ? 242 PHE A CZ  1 
ATOM   2069  N N   . GLU A 1 243 ? 10.223  -19.425 8.418   1.00 20.61  ? 243 GLU A N   1 
ATOM   2070  C CA  . GLU A 1 243 ? 11.448  -19.911 9.043   1.00 21.86  ? 243 GLU A CA  1 
ATOM   2071  C C   . GLU A 1 243 ? 11.715  -19.199 10.363  1.00 21.56  ? 243 GLU A C   1 
ATOM   2072  O O   . GLU A 1 243 ? 12.072  -19.838 11.360  1.00 30.66  ? 243 GLU A O   1 
ATOM   2073  C CB  . GLU A 1 243 ? 12.631  -19.734 8.090   1.00 22.11  ? 243 GLU A CB  1 
ATOM   2074  C CG  . GLU A 1 243 ? 13.930  -20.351 8.589   1.00 26.22  ? 243 GLU A CG  1 
ATOM   2075  C CD  . GLU A 1 243 ? 15.153  -19.795 7.883   1.00 31.15  ? 243 GLU A CD  1 
ATOM   2076  O OE1 . GLU A 1 243 ? 15.072  -19.534 6.664   1.00 23.19  ? 243 GLU A OE1 1 
ATOM   2077  O OE2 . GLU A 1 243 ? 16.196  -19.621 8.549   1.00 36.32  ? 243 GLU A OE2 1 
ATOM   2078  N N   . ILE A 1 244 ? 11.536  -17.880 10.394  1.00 25.15  ? 244 ILE A N   1 
ATOM   2079  C CA  . ILE A 1 244 ? 11.847  -17.119 11.599  1.00 23.12  ? 244 ILE A CA  1 
ATOM   2080  C C   . ILE A 1 244 ? 10.724  -17.234 12.623  1.00 19.76  ? 244 ILE A C   1 
ATOM   2081  O O   . ILE A 1 244 ? 10.968  -17.500 13.804  1.00 22.09  ? 244 ILE A O   1 
ATOM   2082  C CB  . ILE A 1 244 ? 12.135  -15.647 11.244  1.00 18.50  ? 244 ILE A CB  1 
ATOM   2083  C CG1 . ILE A 1 244 ? 13.014  -15.556 9.994   1.00 18.55  ? 244 ILE A CG1 1 
ATOM   2084  C CG2 . ILE A 1 244 ? 12.791  -14.937 12.418  1.00 23.63  ? 244 ILE A CG2 1 
ATOM   2085  C CD1 . ILE A 1 244 ? 14.484  -15.823 10.249  1.00 19.76  ? 244 ILE A CD1 1 
ATOM   2086  N N   . PHE A 1 245 ? 9.479   -17.044 12.191  1.00 18.87  ? 245 PHE A N   1 
ATOM   2087  C CA  . PHE A 1 245 ? 8.362   -16.899 13.115  1.00 18.63  ? 245 PHE A CA  1 
ATOM   2088  C C   . PHE A 1 245 ? 7.500   -18.149 13.241  1.00 24.98  ? 245 PHE A C   1 
ATOM   2089  O O   . PHE A 1 245 ? 6.553   -18.149 14.035  1.00 35.08  ? 245 PHE A O   1 
ATOM   2090  C CB  . PHE A 1 245 ? 7.498   -15.703 12.699  1.00 20.42  ? 245 PHE A CB  1 
ATOM   2091  C CG  . PHE A 1 245 ? 8.252   -14.403 12.659  1.00 21.17  ? 245 PHE A CG  1 
ATOM   2092  C CD1 . PHE A 1 245 ? 8.656   -13.784 13.831  1.00 20.75  ? 245 PHE A CD1 1 
ATOM   2093  C CD2 . PHE A 1 245 ? 8.571   -13.808 11.453  1.00 19.15  ? 245 PHE A CD2 1 
ATOM   2094  C CE1 . PHE A 1 245 ? 9.356   -12.589 13.797  1.00 19.82  ? 245 PHE A CE1 1 
ATOM   2095  C CE2 . PHE A 1 245 ? 9.269   -12.614 11.412  1.00 16.92  ? 245 PHE A CE2 1 
ATOM   2096  C CZ  . PHE A 1 245 ? 9.663   -12.005 12.585  1.00 14.80  ? 245 PHE A CZ  1 
ATOM   2097  N N   . GLY A 1 246 ? 7.795   -19.207 12.489  1.00 28.59  ? 246 GLY A N   1 
ATOM   2098  C CA  . GLY A 1 246 ? 7.098   -20.467 12.677  1.00 27.64  ? 246 GLY A CA  1 
ATOM   2099  C C   . GLY A 1 246 ? 5.646   -20.477 12.259  1.00 24.05  ? 246 GLY A C   1 
ATOM   2100  O O   . GLY A 1 246 ? 4.889   -21.338 12.711  1.00 23.18  ? 246 GLY A O   1 
ATOM   2101  N N   . GLU A 1 247 ? 5.233   -19.543 11.408  1.00 29.16  ? 247 GLU A N   1 
ATOM   2102  C CA  . GLU A 1 247 ? 3.864   -19.493 10.917  1.00 29.28  ? 247 GLU A CA  1 
ATOM   2103  C C   . GLU A 1 247 ? 3.830   -18.614 9.677   1.00 28.38  ? 247 GLU A C   1 
ATOM   2104  O O   . GLU A 1 247 ? 4.681   -17.740 9.498   1.00 34.65  ? 247 GLU A O   1 
ATOM   2105  C CB  . GLU A 1 247 ? 2.901   -18.955 11.984  1.00 30.97  ? 247 GLU A CB  1 
ATOM   2106  C CG  . GLU A 1 247 ? 3.380   -17.680 12.661  1.00 33.40  ? 247 GLU A CG  1 
ATOM   2107  C CD  . GLU A 1 247 ? 2.576   -17.343 13.900  1.00 42.09  ? 247 GLU A CD  1 
ATOM   2108  O OE1 . GLU A 1 247 ? 1.541   -16.655 13.767  1.00 41.23  ? 247 GLU A OE1 1 
ATOM   2109  O OE2 . GLU A 1 247 ? 2.981   -17.760 15.006  1.00 47.85  ? 247 GLU A OE2 1 
ATOM   2110  N N   . HIS A 1 248 ? 2.842   -18.861 8.822   1.00 21.72  ? 248 HIS A N   1 
ATOM   2111  C CA  . HIS A 1 248 ? 2.682   -18.044 7.633   1.00 20.09  ? 248 HIS A CA  1 
ATOM   2112  C C   . HIS A 1 248 ? 2.298   -16.620 8.027   1.00 20.82  ? 248 HIS A C   1 
ATOM   2113  O O   . HIS A 1 248 ? 1.580   -16.411 9.008   1.00 28.91  ? 248 HIS A O   1 
ATOM   2114  C CB  . HIS A 1 248 ? 1.611   -18.626 6.715   1.00 25.07  ? 248 HIS A CB  1 
ATOM   2115  C CG  . HIS A 1 248 ? 2.146   -19.558 5.673   1.00 31.50  ? 248 HIS A CG  1 
ATOM   2116  N ND1 . HIS A 1 248 ? 1.336   -20.190 4.755   1.00 35.49  ? 248 HIS A ND1 1 
ATOM   2117  C CD2 . HIS A 1 248 ? 3.408   -19.968 5.408   1.00 27.77  ? 248 HIS A CD2 1 
ATOM   2118  C CE1 . HIS A 1 248 ? 2.076   -20.947 3.965   1.00 25.78  ? 248 HIS A CE1 1 
ATOM   2119  N NE2 . HIS A 1 248 ? 3.337   -20.832 4.341   1.00 25.55  ? 248 HIS A NE2 1 
ATOM   2120  N N   . PRO A 1 249 ? 2.770   -15.622 7.287   1.00 17.68  ? 249 PRO A N   1 
ATOM   2121  C CA  . PRO A 1 249 ? 2.276   -14.264 7.502   1.00 14.68  ? 249 PRO A CA  1 
ATOM   2122  C C   . PRO A 1 249 ? 0.903   -14.092 6.878   1.00 17.64  ? 249 PRO A C   1 
ATOM   2123  O O   . PRO A 1 249 ? 0.578   -14.688 5.849   1.00 18.49  ? 249 PRO A O   1 
ATOM   2124  C CB  . PRO A 1 249 ? 3.321   -13.390 6.800   1.00 13.23  ? 249 PRO A CB  1 
ATOM   2125  C CG  . PRO A 1 249 ? 3.877   -14.262 5.720   1.00 13.86  ? 249 PRO A CG  1 
ATOM   2126  C CD  . PRO A 1 249 ? 3.638   -15.710 6.100   1.00 22.42  ? 249 PRO A CD  1 
ATOM   2127  N N   . VAL A 1 250 ? 0.082   -13.280 7.537   1.00 15.64  ? 250 VAL A N   1 
ATOM   2128  C CA  . VAL A 1 250 ? -1.198  -12.866 6.976   1.00 22.32  ? 250 VAL A CA  1 
ATOM   2129  C C   . VAL A 1 250 ? -1.240  -11.377 6.692   1.00 16.13  ? 250 VAL A C   1 
ATOM   2130  O O   . VAL A 1 250 ? -2.146  -10.923 5.975   1.00 17.51  ? 250 VAL A O   1 
ATOM   2131  C CB  . VAL A 1 250 ? -2.373  -13.269 7.891   1.00 16.66  ? 250 VAL A CB  1 
ATOM   2132  C CG1 . VAL A 1 250 ? -2.592  -14.775 7.829   1.00 16.29  ? 250 VAL A CG1 1 
ATOM   2133  C CG2 . VAL A 1 250 ? -2.109  -12.820 9.317   1.00 13.58  ? 250 VAL A CG2 1 
ATOM   2134  N N   . TYR A 1 251 ? -0.289  -10.610 7.210   1.00 11.62  ? 251 TYR A N   1 
ATOM   2135  C CA  . TYR A 1 251 ? -0.170  -9.187  6.944   1.00 11.55  ? 251 TYR A CA  1 
ATOM   2136  C C   . TYR A 1 251 ? 1.092   -8.947  6.131   1.00 12.00  ? 251 TYR A C   1 
ATOM   2137  O O   . TYR A 1 251 ? 2.135   -9.554  6.394   1.00 17.78  ? 251 TYR A O   1 
ATOM   2138  C CB  . TYR A 1 251 ? -0.127  -8.392  8.249   1.00 12.86  ? 251 TYR A CB  1 
ATOM   2139  C CG  . TYR A 1 251 ? -1.212  -8.794  9.219   1.00 13.21  ? 251 TYR A CG  1 
ATOM   2140  C CD1 . TYR A 1 251 ? -2.533  -8.882  8.806   1.00 13.01  ? 251 TYR A CD1 1 
ATOM   2141  C CD2 . TYR A 1 251 ? -0.914  -9.106  10.541  1.00 14.45  ? 251 TYR A CD2 1 
ATOM   2142  C CE1 . TYR A 1 251 ? -3.529  -9.257  9.679   1.00 24.42  ? 251 TYR A CE1 1 
ATOM   2143  C CE2 . TYR A 1 251 ? -1.907  -9.483  11.428  1.00 12.74  ? 251 TYR A CE2 1 
ATOM   2144  C CZ  . TYR A 1 251 ? -3.214  -9.556  10.990  1.00 22.59  ? 251 TYR A CZ  1 
ATOM   2145  O OH  . TYR A 1 251 ? -4.209  -9.930  11.862  1.00 34.83  ? 251 TYR A OH  1 
ATOM   2146  N N   . MET A 1 252 ? 0.987   -8.087  5.124   1.00 10.13  ? 252 MET A N   1 
ATOM   2147  C CA  . MET A 1 252 ? 2.103   -7.809  4.235   1.00 9.96   ? 252 MET A CA  1 
ATOM   2148  C C   . MET A 1 252 ? 2.087   -6.336  3.863   1.00 10.37  ? 252 MET A C   1 
ATOM   2149  O O   . MET A 1 252 ? 1.019   -5.757  3.652   1.00 11.02  ? 252 MET A O   1 
ATOM   2150  C CB  . MET A 1 252 ? 2.034   -8.673  2.969   1.00 10.47  ? 252 MET A CB  1 
ATOM   2151  C CG  . MET A 1 252 ? 2.990   -9.859  2.959   1.00 11.04  ? 252 MET A CG  1 
ATOM   2152  S SD  . MET A 1 252 ? 3.095   -10.662 1.347   1.00 33.41  ? 252 MET A SD  1 
ATOM   2153  C CE  . MET A 1 252 ? 4.063   -12.115 1.740   1.00 15.38  ? 252 MET A CE  1 
ATOM   2154  N N   . TRP A 1 253 ? 3.272   -5.729  3.793   1.00 15.09  ? 253 TRP A N   1 
ATOM   2155  C CA  . TRP A 1 253 ? 3.396   -4.353  3.331   1.00 14.47  ? 253 TRP A CA  1 
ATOM   2156  C C   . TRP A 1 253 ? 3.821   -4.356  1.875   1.00 12.64  ? 253 TRP A C   1 
ATOM   2157  O O   . TRP A 1 253 ? 4.924   -4.834  1.567   1.00 21.58  ? 253 TRP A O   1 
ATOM   2158  C CB  . TRP A 1 253 ? 4.408   -3.582  4.170   1.00 11.58  ? 253 TRP A CB  1 
ATOM   2159  C CG  . TRP A 1 253 ? 4.832   -2.297  3.536   1.00 9.02   ? 253 TRP A CG  1 
ATOM   2160  C CD1 . TRP A 1 253 ? 6.031   -2.030  2.943   1.00 8.72   ? 253 TRP A CD1 1 
ATOM   2161  C CD2 . TRP A 1 253 ? 4.054   -1.100  3.426   1.00 10.07  ? 253 TRP A CD2 1 
ATOM   2162  N NE1 . TRP A 1 253 ? 6.049   -0.740  2.471   1.00 9.91   ? 253 TRP A NE1 1 
ATOM   2163  C CE2 . TRP A 1 253 ? 4.846   -0.147  2.755   1.00 8.20   ? 253 TRP A CE2 1 
ATOM   2164  C CE3 . TRP A 1 253 ? 2.764   -0.740  3.830   1.00 11.34  ? 253 TRP A CE3 1 
ATOM   2165  C CZ2 . TRP A 1 253 ? 4.392   1.140   2.478   1.00 8.16   ? 253 TRP A CZ2 1 
ATOM   2166  C CZ3 . TRP A 1 253 ? 2.314   0.539   3.554   1.00 11.63  ? 253 TRP A CZ3 1 
ATOM   2167  C CH2 . TRP A 1 253 ? 3.127   1.464   2.887   1.00 9.50   ? 253 TRP A CH2 1 
ATOM   2168  N N   . PRO A 1 254 ? 3.004   -3.856  0.954   1.00 9.45   ? 254 PRO A N   1 
ATOM   2169  C CA  . PRO A 1 254 ? 3.395   -3.856  -0.456  1.00 11.39  ? 254 PRO A CA  1 
ATOM   2170  C C   . PRO A 1 254 ? 4.567   -2.921  -0.678  1.00 10.96  ? 254 PRO A C   1 
ATOM   2171  O O   . PRO A 1 254 ? 4.549   -1.774  -0.207  1.00 10.96  ? 254 PRO A O   1 
ATOM   2172  C CB  . PRO A 1 254 ? 2.135   -3.356  -1.174  1.00 12.08  ? 254 PRO A CB  1 
ATOM   2173  C CG  . PRO A 1 254 ? 1.431   -2.546  -0.160  1.00 10.82  ? 254 PRO A CG  1 
ATOM   2174  C CD  . PRO A 1 254 ? 1.716   -3.178  1.173   1.00 8.97   ? 254 PRO A CD  1 
ATOM   2175  N N   . PRO A 1 255 ? 5.602   -3.369  -1.354  1.00 10.66  ? 255 PRO A N   1 
ATOM   2176  C CA  . PRO A 1 255 ? 6.769   -2.549  -1.580  1.00 11.51  ? 255 PRO A CA  1 
ATOM   2177  C C   . PRO A 1 255 ? 6.484   -1.204  -2.145  1.00 9.63   ? 255 PRO A C   1 
ATOM   2178  O O   . PRO A 1 255 ? 5.875   -1.104  -3.136  1.00 21.22  ? 255 PRO A O   1 
ATOM   2179  C CB  . PRO A 1 255 ? 7.535   -3.376  -2.556  1.00 15.50  ? 255 PRO A CB  1 
ATOM   2180  C CG  . PRO A 1 255 ? 7.283   -4.737  -2.118  1.00 10.54  ? 255 PRO A CG  1 
ATOM   2181  C CD  . PRO A 1 255 ? 5.909   -4.773  -1.602  1.00 13.62  ? 255 PRO A CD  1 
ATOM   2182  N N   . GLU A 1 256 ? 6.935   -0.171  -1.491  1.00 12.68  ? 256 GLU A N   1 
ATOM   2183  C CA  . GLU A 1 256 ? 6.668   1.174   -1.940  1.00 20.51  ? 256 GLU A CA  1 
ATOM   2184  C C   . GLU A 1 256 ? 5.169   1.544   -1.918  1.00 11.89  ? 256 GLU A C   1 
ATOM   2185  O O   . GLU A 1 256 ? 4.784   2.507   -2.470  1.00 11.74  ? 256 GLU A O   1 
ATOM   2186  C CB  . GLU A 1 256 ? 7.299   1.410   -3.308  1.00 12.91  ? 256 GLU A CB  1 
ATOM   2187  C CG  . GLU A 1 256 ? 8.721   0.893   -3.440  1.00 15.39  ? 256 GLU A CG  1 
ATOM   2188  C CD  . GLU A 1 256 ? 9.775   1.842   -2.910  1.00 25.34  ? 256 GLU A CD  1 
ATOM   2189  O OE1 . GLU A 1 256 ? 9.425   2.792   -2.248  1.00 20.54  ? 256 GLU A OE1 1 
ATOM   2190  O OE2 . GLU A 1 256 ? 10.954  1.676   -3.144  1.00 28.39  ? 256 GLU A OE2 1 
ATOM   2191  N N   . ALA A 1 257 ? 4.386   0.733   -1.235  1.00 9.44   ? 257 ALA A N   1 
ATOM   2192  C CA  . ALA A 1 257 ? 2.954   0.836   -1.068  1.00 9.07   ? 257 ALA A CA  1 
ATOM   2193  C C   . ALA A 1 257 ? 2.222   0.638   -2.364  1.00 11.19  ? 257 ALA A C   1 
ATOM   2194  O O   . ALA A 1 257 ? 1.087   0.942   -2.468  1.00 11.45  ? 257 ALA A O   1 
ATOM   2195  C CB  . ALA A 1 257 ? 2.578   2.155   -0.410  1.00 8.99   ? 257 ALA A CB  1 
ATOM   2196  N N   . SER A 1 258 ? 2.902   0.095   -3.348  1.00 10.83  ? 258 SER A N   1 
ATOM   2197  C CA  . SER A 1 258 ? 2.318   -0.015  -4.677  1.00 10.59  ? 258 SER A CA  1 
ATOM   2198  C C   . SER A 1 258 ? 1.219   -1.067  -4.690  1.00 10.80  ? 258 SER A C   1 
ATOM   2199  O O   . SER A 1 258 ? 1.411   -2.194  -4.225  1.00 10.66  ? 258 SER A O   1 
ATOM   2200  C CB  . SER A 1 258 ? 3.393   -0.356  -5.709  1.00 15.07  ? 258 SER A CB  1 
ATOM   2201  O OG  . SER A 1 258 ? 4.137   -1.498  -5.328  1.00 26.00  ? 258 SER A OG  1 
ATOM   2202  N N   . VAL A 1 259 ? 0.061   -0.694  -5.233  1.00 11.29  ? 259 VAL A N   1 
ATOM   2203  C CA  . VAL A 1 259 ? -1.096  -1.573  -5.296  1.00 11.67  ? 259 VAL A CA  1 
ATOM   2204  C C   . VAL A 1 259 ? -1.694  -1.511  -6.694  1.00 13.33  ? 259 VAL A C   1 
ATOM   2205  O O   . VAL A 1 259 ? -1.421  -0.601  -7.479  1.00 15.66  ? 259 VAL A O   1 
ATOM   2206  C CB  . VAL A 1 259 ? -2.170  -1.210  -4.248  1.00 11.60  ? 259 VAL A CB  1 
ATOM   2207  C CG1 . VAL A 1 259 ? -1.816  -1.800  -2.895  1.00 20.13  ? 259 VAL A CG1 1 
ATOM   2208  C CG2 . VAL A 1 259 ? -2.335  0.301   -4.159  1.00 11.49  ? 259 VAL A CG2 1 
ATOM   2209  N N   . SER A 1 260 ? -2.514  -2.513  -6.995  1.00 13.14  ? 260 SER A N   1 
ATOM   2210  C CA  . SER A 1 260 ? -3.352  -2.525  -8.183  1.00 14.19  ? 260 SER A CA  1 
ATOM   2211  C C   . SER A 1 260 ? -4.410  -3.595  -7.980  1.00 20.92  ? 260 SER A C   1 
ATOM   2212  O O   . SER A 1 260 ? -4.285  -4.453  -7.101  1.00 20.13  ? 260 SER A O   1 
ATOM   2213  C CB  . SER A 1 260 ? -2.539  -2.787  -9.457  1.00 20.51  ? 260 SER A CB  1 
ATOM   2214  O OG  . SER A 1 260 ? -2.082  -4.127  -9.508  1.00 25.26  ? 260 SER A OG  1 
ATOM   2215  N N   . ASN A 1 261 ? -5.466  -3.526  -8.794  1.00 27.24  ? 261 ASN A N   1 
ATOM   2216  C CA  . ASN A 1 261 ? -6.479  -4.574  -8.755  1.00 16.36  ? 261 ASN A CA  1 
ATOM   2217  C C   . ASN A 1 261 ? -5.868  -5.942  -9.011  1.00 25.29  ? 261 ASN A C   1 
ATOM   2218  O O   . ASN A 1 261 ? -6.331  -6.944  -8.456  1.00 32.72  ? 261 ASN A O   1 
ATOM   2219  C CB  . ASN A 1 261 ? -7.577  -4.289  -9.778  1.00 22.87  ? 261 ASN A CB  1 
ATOM   2220  C CG  . ASN A 1 261 ? -8.079  -2.867  -9.710  1.00 19.93  ? 261 ASN A CG  1 
ATOM   2221  O OD1 . ASN A 1 261 ? -9.093  -2.598  -9.076  1.00 18.38  ? 261 ASN A OD1 1 
ATOM   2222  N ND2 . ASN A 1 261 ? -7.378  -1.950  -10.367 1.00 18.35  ? 261 ASN A ND2 1 
ATOM   2223  N N   . GLU A 1 262 ? -4.826  -6.000  -9.840  1.00 24.46  ? 262 GLU A N   1 
ATOM   2224  C CA  . GLU A 1 262 ? -4.163  -7.266  -10.125 1.00 19.23  ? 262 GLU A CA  1 
ATOM   2225  C C   . GLU A 1 262 ? -3.258  -7.701  -8.978  1.00 17.63  ? 262 GLU A C   1 
ATOM   2226  O O   . GLU A 1 262 ? -3.147  -8.899  -8.695  1.00 26.25  ? 262 GLU A O   1 
ATOM   2227  C CB  . GLU A 1 262 ? -3.372  -7.151  -11.425 1.00 24.31  ? 262 GLU A CB  1 
ATOM   2228  C CG  . GLU A 1 262 ? -4.253  -7.182  -12.662 1.00 34.61  ? 262 GLU A CG  1 
ATOM   2229  C CD  . GLU A 1 262 ? -4.315  -5.846  -13.378 1.00 44.58  ? 262 GLU A CD  1 
ATOM   2230  O OE1 . GLU A 1 262 ? -3.762  -5.748  -14.493 1.00 38.77  ? 262 GLU A OE1 1 
ATOM   2231  O OE2 . GLU A 1 262 ? -4.916  -4.894  -12.833 1.00 50.29  ? 262 GLU A OE2 1 
ATOM   2232  N N   . ALA A 1 263 ? -2.602  -6.748  -8.309  1.00 16.53  ? 263 ALA A N   1 
ATOM   2233  C CA  . ALA A 1 263 ? -1.753  -7.100  -7.174  1.00 21.14  ? 263 ALA A CA  1 
ATOM   2234  C C   . ALA A 1 263 ? -2.586  -7.466  -5.953  1.00 17.08  ? 263 ALA A C   1 
ATOM   2235  O O   . ALA A 1 263 ? -2.267  -8.427  -5.243  1.00 25.30  ? 263 ALA A O   1 
ATOM   2236  C CB  . ALA A 1 263 ? -0.798  -5.953  -6.850  1.00 13.60  ? 263 ALA A CB  1 
ATOM   2237  N N   . LEU A 1 264 ? -3.659  -6.713  -5.693  1.00 13.83  ? 264 LEU A N   1 
ATOM   2238  C CA  . LEU A 1 264 ? -4.550  -7.055  -4.589  1.00 15.18  ? 264 LEU A CA  1 
ATOM   2239  C C   . LEU A 1 264 ? -5.188  -8.423  -4.793  1.00 25.17  ? 264 LEU A C   1 
ATOM   2240  O O   . LEU A 1 264 ? -5.442  -9.142  -3.820  1.00 21.06  ? 264 LEU A O   1 
ATOM   2241  C CB  . LEU A 1 264 ? -5.626  -5.979  -4.428  1.00 18.70  ? 264 LEU A CB  1 
ATOM   2242  C CG  . LEU A 1 264 ? -5.187  -4.627  -3.860  1.00 21.01  ? 264 LEU A CG  1 
ATOM   2243  C CD1 . LEU A 1 264 ? -6.004  -3.504  -4.471  1.00 21.44  ? 264 LEU A CD1 1 
ATOM   2244  C CD2 . LEU A 1 264 ? -5.299  -4.601  -2.343  1.00 15.81  ? 264 LEU A CD2 1 
ATOM   2245  N N   . GLU A 1 265 ? -5.464  -8.794  -6.044  1.00 30.36  ? 265 GLU A N   1 
ATOM   2246  C CA  . GLU A 1 265 ? -5.910  -10.153 -6.331  1.00 20.18  ? 265 GLU A CA  1 
ATOM   2247  C C   . GLU A 1 265 ? -4.832  -11.168 -5.966  1.00 22.30  ? 265 GLU A C   1 
ATOM   2248  O O   . GLU A 1 265 ? -5.117  -12.199 -5.345  1.00 22.81  ? 265 GLU A O   1 
ATOM   2249  C CB  . GLU A 1 265 ? -6.285  -10.283 -7.809  1.00 24.55  ? 265 GLU A CB  1 
ATOM   2250  C CG  . GLU A 1 265 ? -7.669  -9.768  -8.169  1.00 37.15  ? 265 GLU A CG  1 
ATOM   2251  C CD  . GLU A 1 265 ? -7.906  -9.749  -9.672  1.00 45.37  ? 265 GLU A CD  1 
ATOM   2252  O OE1 . GLU A 1 265 ? -6.944  -9.979  -10.433 1.00 34.59  ? 265 GLU A OE1 1 
ATOM   2253  O OE2 . GLU A 1 265 ? -9.054  -9.495  -10.093 1.00 43.97  ? 265 GLU A OE2 1 
ATOM   2254  N N   . LEU A 1 266 ? -3.582  -10.885 -6.340  1.00 24.46  ? 266 LEU A N   1 
ATOM   2255  C CA  . LEU A 1 266 ? -2.497  -11.836 -6.111  1.00 19.50  ? 266 LEU A CA  1 
ATOM   2256  C C   . LEU A 1 266 ? -2.243  -12.047 -4.623  1.00 15.39  ? 266 LEU A C   1 
ATOM   2257  O O   . LEU A 1 266 ? -1.995  -13.177 -4.184  1.00 22.63  ? 266 LEU A O   1 
ATOM   2258  C CB  . LEU A 1 266 ? -1.226  -11.360 -6.816  1.00 17.83  ? 266 LEU A CB  1 
ATOM   2259  C CG  . LEU A 1 266 ? 0.082   -12.057 -6.433  1.00 15.41  ? 266 LEU A CG  1 
ATOM   2260  C CD1 . LEU A 1 266 ? 0.324   -13.277 -7.305  1.00 19.28  ? 266 LEU A CD1 1 
ATOM   2261  C CD2 . LEU A 1 266 ? 1.249   -11.090 -6.536  1.00 14.74  ? 266 LEU A CD2 1 
ATOM   2262  N N   . TYR A 1 267 ? -2.297  -10.974 -3.832  1.00 14.17  ? 267 TYR A N   1 
ATOM   2263  C CA  . TYR A 1 267 ? -2.090  -11.106 -2.394  1.00 17.03  ? 267 TYR A CA  1 
ATOM   2264  C C   . TYR A 1 267 ? -3.161  -11.987 -1.764  1.00 15.30  ? 267 TYR A C   1 
ATOM   2265  O O   . TYR A 1 267 ? -2.864  -12.823 -0.902  1.00 14.51  ? 267 TYR A O   1 
ATOM   2266  C CB  . TYR A 1 267 ? -2.083  -9.723  -1.742  1.00 15.96  ? 267 TYR A CB  1 
ATOM   2267  C CG  . TYR A 1 267 ? -0.866  -8.891  -2.084  1.00 18.53  ? 267 TYR A CG  1 
ATOM   2268  C CD1 . TYR A 1 267 ? 0.410   -9.434  -2.025  1.00 15.81  ? 267 TYR A CD1 1 
ATOM   2269  C CD2 . TYR A 1 267 ? -0.995  -7.565  -2.476  1.00 11.75  ? 267 TYR A CD2 1 
ATOM   2270  C CE1 . TYR A 1 267 ? 1.525   -8.679  -2.339  1.00 11.73  ? 267 TYR A CE1 1 
ATOM   2271  C CE2 . TYR A 1 267 ? 0.113   -6.802  -2.791  1.00 14.37  ? 267 TYR A CE2 1 
ATOM   2272  C CZ  . TYR A 1 267 ? 1.370   -7.365  -2.722  1.00 16.85  ? 267 TYR A CZ  1 
ATOM   2273  O OH  . TYR A 1 267 ? 2.478   -6.611  -3.036  1.00 26.52  ? 267 TYR A OH  1 
ATOM   2274  N N   . TYR A 1 268 ? -4.414  -11.817 -2.191  1.00 16.14  ? 268 TYR A N   1 
ATOM   2275  C CA  . TYR A 1 268 ? -5.510  -12.611 -1.646  1.00 15.83  ? 268 TYR A CA  1 
ATOM   2276  C C   . TYR A 1 268 ? -5.347  -14.088 -1.980  1.00 17.20  ? 268 TYR A C   1 
ATOM   2277  O O   . TYR A 1 268 ? -5.631  -14.955 -1.145  1.00 21.10  ? 268 TYR A O   1 
ATOM   2278  C CB  . TYR A 1 268 ? -6.841  -12.074 -2.172  1.00 24.50  ? 268 TYR A CB  1 
ATOM   2279  C CG  . TYR A 1 268 ? -8.018  -13.002 -1.988  1.00 18.85  ? 268 TYR A CG  1 
ATOM   2280  C CD1 . TYR A 1 268 ? -8.500  -13.306 -0.722  1.00 17.15  ? 268 TYR A CD1 1 
ATOM   2281  C CD2 . TYR A 1 268 ? -8.656  -13.565 -3.085  1.00 18.21  ? 268 TYR A CD2 1 
ATOM   2282  C CE1 . TYR A 1 268 ? -9.582  -14.150 -0.555  1.00 19.58  ? 268 TYR A CE1 1 
ATOM   2283  C CE2 . TYR A 1 268 ? -9.736  -14.409 -2.928  1.00 19.36  ? 268 TYR A CE2 1 
ATOM   2284  C CZ  . TYR A 1 268 ? -10.195 -14.698 -1.661  1.00 19.41  ? 268 TYR A CZ  1 
ATOM   2285  O OH  . TYR A 1 268 ? -11.272 -15.539 -1.501  1.00 29.78  ? 268 TYR A OH  1 
ATOM   2286  N N   . GLU A 1 269 ? -4.878  -14.395 -3.191  1.00 19.15  ? 269 GLU A N   1 
ATOM   2287  C CA  . GLU A 1 269 ? -4.682  -15.781 -3.600  1.00 17.98  ? 269 GLU A CA  1 
ATOM   2288  C C   . GLU A 1 269 ? -3.530  -16.460 -2.870  1.00 17.83  ? 269 GLU A C   1 
ATOM   2289  O O   . GLU A 1 269 ? -3.381  -17.680 -2.985  1.00 24.88  ? 269 GLU A O   1 
ATOM   2290  C CB  . GLU A 1 269 ? -4.445  -15.852 -5.109  1.00 21.60  ? 269 GLU A CB  1 
ATOM   2291  C CG  . GLU A 1 269 ? -5.717  -15.903 -5.937  1.00 31.65  ? 269 GLU A CG  1 
ATOM   2292  C CD  . GLU A 1 269 ? -5.622  -15.060 -7.195  1.00 50.72  ? 269 GLU A CD  1 
ATOM   2293  O OE1 . GLU A 1 269 ? -4.698  -15.299 -8.003  1.00 47.63  ? 269 GLU A OE1 1 
ATOM   2294  O OE2 . GLU A 1 269 ? -6.471  -14.163 -7.379  1.00 41.70  ? 269 GLU A OE2 1 
ATOM   2295  N N   . LYS A 1 270 ? -2.713  -15.706 -2.137  1.00 16.75  ? 270 LYS A N   1 
ATOM   2296  C CA  . LYS A 1 270 ? -1.610  -16.258 -1.362  1.00 16.68  ? 270 LYS A CA  1 
ATOM   2297  C C   . LYS A 1 270 ? -1.905  -16.295 0.132   1.00 16.40  ? 270 LYS A C   1 
ATOM   2298  O O   . LYS A 1 270 ? -1.003  -16.584 0.923   1.00 16.31  ? 270 LYS A O   1 
ATOM   2299  C CB  . LYS A 1 270 ? -0.330  -15.462 -1.625  1.00 15.88  ? 270 LYS A CB  1 
ATOM   2300  C CG  . LYS A 1 270 ? 0.065   -15.424 -3.091  1.00 16.26  ? 270 LYS A CG  1 
ATOM   2301  C CD  . LYS A 1 270 ? 1.111   -16.482 -3.407  1.00 25.58  ? 270 LYS A CD  1 
ATOM   2302  C CE  . LYS A 1 270 ? 1.222   -16.718 -4.905  1.00 25.94  ? 270 LYS A CE  1 
ATOM   2303  N NZ  . LYS A 1 270 ? 0.650   -18.038 -5.298  1.00 38.48  ? 270 LYS A NZ  1 
ATOM   2304  N N   . GLY A 1 271 ? -3.138  -16.012 0.538   1.00 16.41  ? 271 GLY A N   1 
ATOM   2305  C CA  . GLY A 1 271 ? -3.500  -16.051 1.940   1.00 16.30  ? 271 GLY A CA  1 
ATOM   2306  C C   . GLY A 1 271 ? -3.214  -14.793 2.723   1.00 15.14  ? 271 GLY A C   1 
ATOM   2307  O O   . GLY A 1 271 ? -3.170  -14.849 3.958   1.00 17.97  ? 271 GLY A O   1 
ATOM   2308  N N   . ILE A 1 272 ? -3.015  -13.662 2.054   1.00 14.37  ? 272 ILE A N   1 
ATOM   2309  C CA  . ILE A 1 272 ? -2.808  -12.389 2.736   1.00 13.38  ? 272 ILE A CA  1 
ATOM   2310  C C   . ILE A 1 272 ? -4.171  -11.797 3.071   1.00 13.41  ? 272 ILE A C   1 
ATOM   2311  O O   . ILE A 1 272 ? -4.993  -11.562 2.179   1.00 13.72  ? 272 ILE A O   1 
ATOM   2312  C CB  . ILE A 1 272 ? -1.982  -11.426 1.872   1.00 12.70  ? 272 ILE A CB  1 
ATOM   2313  C CG1 . ILE A 1 272 ? -0.607  -12.022 1.558   1.00 12.81  ? 272 ILE A CG1 1 
ATOM   2314  C CG2 . ILE A 1 272 ? -1.841  -10.080 2.562   1.00 11.82  ? 272 ILE A CG2 1 
ATOM   2315  C CD1 . ILE A 1 272 ? 0.170   -12.454 2.782   1.00 12.79  ? 272 ILE A CD1 1 
ATOM   2316  N N   . ASN A 1 273 ? -4.419  -11.565 4.360   1.00 13.25  ? 273 ASN A N   1 
ATOM   2317  C CA  . ASN A 1 273 ? -5.699  -11.027 4.798   1.00 13.43  ? 273 ASN A CA  1 
ATOM   2318  C C   . ASN A 1 273 ? -5.742  -9.510  4.792   1.00 14.13  ? 273 ASN A C   1 
ATOM   2319  O O   . ASN A 1 273 ? -6.834  -8.933  4.716   1.00 17.35  ? 273 ASN A O   1 
ATOM   2320  C CB  . ASN A 1 273 ? -6.036  -11.524 6.208   1.00 13.82  ? 273 ASN A CB  1 
ATOM   2321  C CG  . ASN A 1 273 ? -5.890  -13.024 6.349   1.00 20.74  ? 273 ASN A CG  1 
ATOM   2322  O OD1 . ASN A 1 273 ? -5.951  -13.761 5.367   1.00 23.19  ? 273 ASN A OD1 1 
ATOM   2323  N ND2 . ASN A 1 273 ? -5.710  -13.486 7.579   1.00 29.27  ? 273 ASN A ND2 1 
ATOM   2324  N N   . MET A 1 274 ? -4.591  -8.852  4.860   1.00 14.71  ? 274 MET A N   1 
ATOM   2325  C CA  . MET A 1 274 ? -4.595  -7.412  5.013   1.00 11.44  ? 274 MET A CA  1 
ATOM   2326  C C   . MET A 1 274 ? -3.305  -6.832  4.444   1.00 10.62  ? 274 MET A C   1 
ATOM   2327  O O   . MET A 1 274 ? -2.244  -7.459  4.497   1.00 15.36  ? 274 MET A O   1 
ATOM   2328  C CB  . MET A 1 274 ? -4.770  -7.054  6.490   1.00 22.16  ? 274 MET A CB  1 
ATOM   2329  C CG  . MET A 1 274 ? -4.332  -5.670  6.850   1.00 16.44  ? 274 MET A CG  1 
ATOM   2330  S SD  . MET A 1 274 ? -2.688  -5.610  7.547   1.00 28.89  ? 274 MET A SD  1 
ATOM   2331  C CE  . MET A 1 274 ? -2.378  -3.889  7.279   1.00 13.94  ? 274 MET A CE  1 
ATOM   2332  N N   . LEU A 1 275 ? -3.418  -5.636  3.871   1.00 10.33  ? 275 LEU A N   1 
ATOM   2333  C CA  . LEU A 1 275 ? -2.265  -4.834  3.490   1.00 11.19  ? 275 LEU A CA  1 
ATOM   2334  C C   . LEU A 1 275 ? -2.669  -3.370  3.594   1.00 11.77  ? 275 LEU A C   1 
ATOM   2335  O O   . LEU A 1 275 ? -3.835  -3.045  3.824   1.00 14.98  ? 275 LEU A O   1 
ATOM   2336  C CB  . LEU A 1 275 ? -1.765  -5.192  2.086   1.00 9.94   ? 275 LEU A CB  1 
ATOM   2337  C CG  . LEU A 1 275 ? -2.722  -4.952  0.923   1.00 18.55  ? 275 LEU A CG  1 
ATOM   2338  C CD1 . LEU A 1 275 ? -2.277  -3.750  0.106   1.00 16.09  ? 275 LEU A CD1 1 
ATOM   2339  C CD2 . LEU A 1 275 ? -2.812  -6.194  0.065   1.00 20.25  ? 275 LEU A CD2 1 
ATOM   2340  N N   . ALA A 1 276 ? -1.691  -2.485  3.446   1.00 10.13  ? 276 ALA A N   1 
ATOM   2341  C CA  . ALA A 1 276 ? -1.923  -1.051  3.531   1.00 13.51  ? 276 ALA A CA  1 
ATOM   2342  C C   . ALA A 1 276 ? -1.284  -0.363  2.334   1.00 14.14  ? 276 ALA A C   1 
ATOM   2343  O O   . ALA A 1 276 ? -0.476  -0.952  1.613   1.00 12.87  ? 276 ALA A O   1 
ATOM   2344  C CB  . ALA A 1 276 ? -1.372  -0.463  4.837   1.00 10.82  ? 276 ALA A CB  1 
ATOM   2345  N N   . THR A 1 277 ? -1.653  0.897   2.122   1.00 9.14   ? 277 THR A N   1 
ATOM   2346  C CA  . THR A 1 277 ? -1.053  1.690   1.055   1.00 13.64  ? 277 THR A CA  1 
ATOM   2347  C C   . THR A 1 277 ? -1.268  3.168   1.359   1.00 15.25  ? 277 THR A C   1 
ATOM   2348  O O   . THR A 1 277 ? -1.794  3.536   2.413   1.00 15.21  ? 277 THR A O   1 
ATOM   2349  C CB  . THR A 1 277 ? -1.617  1.306   -0.317  1.00 9.78   ? 277 THR A CB  1 
ATOM   2350  O OG1 . THR A 1 277 ? -1.027  2.137   -1.323  1.00 11.87  ? 277 THR A OG1 1 
ATOM   2351  C CG2 . THR A 1 277 ? -3.121  1.474   -0.347  1.00 10.34  ? 277 THR A CG2 1 
ATOM   2352  N N   . ASP A 1 278 ? -0.843  4.013   0.424   1.00 22.36  ? 278 ASP A N   1 
ATOM   2353  C CA  . ASP A 1 278 ? -0.866  5.457   0.601   1.00 20.40  ? 278 ASP A CA  1 
ATOM   2354  C C   . ASP A 1 278 ? -2.284  6.000   0.482   1.00 16.34  ? 278 ASP A C   1 
ATOM   2355  O O   . ASP A 1 278 ? -3.145  5.407   -0.172  1.00 18.28  ? 278 ASP A O   1 
ATOM   2356  C CB  . ASP A 1 278 ? 0.035   6.121   -0.440  1.00 20.47  ? 278 ASP A CB  1 
ATOM   2357  C CG  . ASP A 1 278 ? 0.605   7.437   0.034   1.00 26.81  ? 278 ASP A CG  1 
ATOM   2358  O OD1 . ASP A 1 278 ? 0.948   7.538   1.232   1.00 22.56  ? 278 ASP A OD1 1 
ATOM   2359  O OD2 . ASP A 1 278 ? 0.733   8.362   -0.792  1.00 36.13  ? 278 ASP A OD2 1 
ATOM   2360  N N   . GLU A 1 279 ? -2.525  7.147   1.123   1.00 15.70  ? 279 GLU A N   1 
ATOM   2361  C CA  . GLU A 1 279 ? -3.828  7.788   0.987   1.00 17.37  ? 279 GLU A CA  1 
ATOM   2362  C C   . GLU A 1 279 ? -3.937  8.631   -0.275  1.00 18.60  ? 279 GLU A C   1 
ATOM   2363  O O   . GLU A 1 279 ? -5.053  9.002   -0.655  1.00 19.44  ? 279 GLU A O   1 
ATOM   2364  C CB  . GLU A 1 279 ? -4.153  8.649   2.214   1.00 16.55  ? 279 GLU A CB  1 
ATOM   2365  C CG  . GLU A 1 279 ? -3.291  9.880   2.408   1.00 18.51  ? 279 GLU A CG  1 
ATOM   2366  C CD  . GLU A 1 279 ? -3.934  10.882  3.354   1.00 30.17  ? 279 GLU A CD  1 
ATOM   2367  O OE1 . GLU A 1 279 ? -5.059  11.339  3.058   1.00 27.13  ? 279 GLU A OE1 1 
ATOM   2368  O OE2 . GLU A 1 279 ? -3.326  11.205  4.397   1.00 30.78  ? 279 GLU A OE2 1 
ATOM   2369  N N   . VAL A 1 280 ? -2.816  8.941   -0.930  1.00 20.19  ? 280 VAL A N   1 
ATOM   2370  C CA  . VAL A 1 280 ? -2.883  9.498   -2.279  1.00 20.73  ? 280 VAL A CA  1 
ATOM   2371  C C   . VAL A 1 280 ? -3.532  8.490   -3.220  1.00 21.77  ? 280 VAL A C   1 
ATOM   2372  O O   . VAL A 1 280 ? -4.328  8.853   -4.095  1.00 17.14  ? 280 VAL A O   1 
ATOM   2373  C CB  . VAL A 1 280 ? -1.479  9.915   -2.760  1.00 18.54  ? 280 VAL A CB  1 
ATOM   2374  C CG1 . VAL A 1 280 ? -1.393  9.905   -4.285  1.00 16.89  ? 280 VAL A CG1 1 
ATOM   2375  C CG2 . VAL A 1 280 ? -1.111  11.288  -2.213  1.00 26.83  ? 280 VAL A CG2 1 
ATOM   2376  N N   . ILE A 1 281 ? -3.219  7.205   -3.034  1.00 18.06  ? 281 ILE A N   1 
ATOM   2377  C CA  . ILE A 1 281 ? -3.869  6.146   -3.801  1.00 12.99  ? 281 ILE A CA  1 
ATOM   2378  C C   . ILE A 1 281 ? -5.367  6.137   -3.528  1.00 15.01  ? 281 ILE A C   1 
ATOM   2379  O O   . ILE A 1 281 ? -6.180  5.937   -4.440  1.00 15.96  ? 281 ILE A O   1 
ATOM   2380  C CB  . ILE A 1 281 ? -3.229  4.783   -3.471  1.00 15.05  ? 281 ILE A CB  1 
ATOM   2381  C CG1 . ILE A 1 281 ? -1.730  4.784   -3.795  1.00 12.86  ? 281 ILE A CG1 1 
ATOM   2382  C CG2 . ILE A 1 281 ? -3.934  3.663   -4.224  1.00 16.15  ? 281 ILE A CG2 1 
ATOM   2383  C CD1 . ILE A 1 281 ? -1.367  5.521   -5.062  1.00 19.57  ? 281 ILE A CD1 1 
ATOM   2384  N N   . LEU A 1 282 ? -5.755  6.355   -2.268  1.00 17.99  ? 282 LEU A N   1 
ATOM   2385  C CA  . LEU A 1 282 ? -7.170  6.396   -1.913  1.00 14.05  ? 282 LEU A CA  1 
ATOM   2386  C C   . LEU A 1 282 ? -7.886  7.535   -2.627  1.00 15.34  ? 282 LEU A C   1 
ATOM   2387  O O   . LEU A 1 282 ? -9.012  7.363   -3.112  1.00 20.72  ? 282 LEU A O   1 
ATOM   2388  C CB  . LEU A 1 282 ? -7.320  6.531   -0.397  1.00 14.47  ? 282 LEU A CB  1 
ATOM   2389  C CG  . LEU A 1 282 ? -8.721  6.736   0.177   1.00 14.42  ? 282 LEU A CG  1 
ATOM   2390  C CD1 . LEU A 1 282 ? -9.593  5.525   -0.107  1.00 14.75  ? 282 LEU A CD1 1 
ATOM   2391  C CD2 . LEU A 1 282 ? -8.631  7.001   1.670   1.00 13.99  ? 282 LEU A CD2 1 
ATOM   2392  N N   . LYS A 1 283 ? -7.249  8.705   -2.705  1.00 15.39  ? 283 LYS A N   1 
ATOM   2393  C CA  . LYS A 1 283 ? -7.864  9.836   -3.395  1.00 18.30  ? 283 LYS A CA  1 
ATOM   2394  C C   . LYS A 1 283 ? -8.031  9.550   -4.884  1.00 17.47  ? 283 LYS A C   1 
ATOM   2395  O O   . LYS A 1 283 ? -9.041  9.929   -5.486  1.00 18.77  ? 283 LYS A O   1 
ATOM   2396  C CB  . LYS A 1 283 ? -7.032  11.103  -3.178  1.00 26.56  ? 283 LYS A CB  1 
ATOM   2397  C CG  . LYS A 1 283 ? -6.790  11.501  -1.714  1.00 23.08  ? 283 LYS A CG  1 
ATOM   2398  C CD  . LYS A 1 283 ? -7.929  11.094  -0.782  1.00 25.12  ? 283 LYS A CD  1 
ATOM   2399  C CE  . LYS A 1 283 ? -8.082  12.071  0.377   1.00 25.98  ? 283 LYS A CE  1 
ATOM   2400  N NZ  . LYS A 1 283 ? -7.381  11.608  1.608   1.00 15.64  ? 283 LYS A NZ  1 
ATOM   2401  N N   . ASN A 1 284 ? -7.048  8.885   -5.494  1.00 16.81  ? 284 ASN A N   1 
ATOM   2402  C CA  . ASN A 1 284 ? -7.143  8.539   -6.909  1.00 17.58  ? 284 ASN A CA  1 
ATOM   2403  C C   . ASN A 1 284 ? -8.213  7.485   -7.171  1.00 18.29  ? 284 ASN A C   1 
ATOM   2404  O O   . ASN A 1 284 ? -8.807  7.467   -8.255  1.00 22.87  ? 284 ASN A O   1 
ATOM   2405  C CB  . ASN A 1 284 ? -5.786  8.039   -7.415  1.00 16.96  ? 284 ASN A CB  1 
ATOM   2406  C CG  . ASN A 1 284 ? -4.764  9.152   -7.555  1.00 23.99  ? 284 ASN A CG  1 
ATOM   2407  O OD1 . ASN A 1 284 ? -5.033  10.307  -7.231  1.00 29.29  ? 284 ASN A OD1 1 
ATOM   2408  N ND2 . ASN A 1 284 ? -3.573  8.801   -8.034  1.00 18.57  ? 284 ASN A ND2 1 
ATOM   2409  N N   . SER A 1 285 ? -8.472  6.607   -6.203  1.00 20.40  ? 285 SER A N   1 
ATOM   2410  C CA  . SER A 1 285 ? -9.323  5.441   -6.415  1.00 17.57  ? 285 SER A CA  1 
ATOM   2411  C C   . SER A 1 285 ? -10.785 5.708   -6.071  1.00 20.88  ? 285 SER A C   1 
ATOM   2412  O O   . SER A 1 285 ? -11.668 5.503   -6.908  1.00 34.56  ? 285 SER A O   1 
ATOM   2413  C CB  . SER A 1 285 ? -8.798  4.259   -5.594  1.00 17.62  ? 285 SER A CB  1 
ATOM   2414  O OG  . SER A 1 285 ? -7.434  4.012   -5.883  1.00 18.94  ? 285 SER A OG  1 
ATOM   2415  N N   . VAL A 1 286 ? -11.057 6.162   -4.851  1.00 21.20  ? 286 VAL A N   1 
ATOM   2416  C CA  . VAL A 1 286 ? -12.421 6.362   -4.380  1.00 21.32  ? 286 VAL A CA  1 
ATOM   2417  C C   . VAL A 1 286 ? -12.711 7.860   -4.359  1.00 28.73  ? 286 VAL A C   1 
ATOM   2418  O O   . VAL A 1 286 ? -11.805 8.698   -4.373  1.00 34.12  ? 286 VAL A O   1 
ATOM   2419  C CB  . VAL A 1 286 ? -12.644 5.710   -2.998  1.00 18.57  ? 286 VAL A CB  1 
ATOM   2420  C CG1 . VAL A 1 286 ? -14.127 5.497   -2.720  1.00 26.77  ? 286 VAL A CG1 1 
ATOM   2421  C CG2 . VAL A 1 286 ? -11.900 4.385   -2.927  1.00 20.29  ? 286 VAL A CG2 1 
ATOM   2422  N N   . GLU A 1 287 ? -14.002 8.195   -4.313  1.00 34.41  ? 287 GLU A N   1 
ATOM   2423  C CA  . GLU A 1 287 ? -14.457 9.531   -4.702  1.00 42.06  ? 287 GLU A CA  1 
ATOM   2424  C C   . GLU A 1 287 ? -14.215 10.581  -3.619  1.00 50.15  ? 287 GLU A C   1 
ATOM   2425  O O   . GLU A 1 287 ? -13.402 11.494  -3.797  1.00 68.57  ? 287 GLU A O   1 
ATOM   2426  C CB  . GLU A 1 287 ? -15.942 9.462   -5.066  1.00 45.45  ? 287 GLU A CB  1 
ATOM   2427  C CG  . GLU A 1 287 ? -16.569 10.781  -5.449  1.00 57.25  ? 287 GLU A CG  1 
ATOM   2428  C CD  . GLU A 1 287 ? -17.984 10.914  -4.921  1.00 66.32  ? 287 GLU A CD  1 
ATOM   2429  O OE1 . GLU A 1 287 ? -18.301 10.281  -3.892  1.00 64.20  ? 287 GLU A OE1 1 
ATOM   2430  O OE2 . GLU A 1 287 ? -18.782 11.648  -5.540  1.00 56.57  ? 287 GLU A OE2 1 
ATOM   2431  N N   . ARG A 1 288 ? -14.908 10.465  -2.484  1.00 38.22  ? 288 ARG A N   1 
ATOM   2432  C CA  . ARG A 1 288 ? -14.733 11.380  -1.351  1.00 36.12  ? 288 ARG A CA  1 
ATOM   2433  C C   . ARG A 1 288 ? -14.534 10.506  -0.120  1.00 34.54  ? 288 ARG A C   1 
ATOM   2434  O O   . ARG A 1 288 ? -15.476 10.231  0.627   1.00 36.15  ? 288 ARG A O   1 
ATOM   2435  C CB  . ARG A 1 288 ? -15.924 12.328  -1.194  1.00 47.81  ? 288 ARG A CB  1 
ATOM   2436  C CG  . ARG A 1 288 ? -16.027 13.397  -2.270  1.00 46.23  ? 288 ARG A CG  1 
ATOM   2437  C CD  . ARG A 1 288 ? -17.443 13.478  -2.815  1.00 50.66  ? 288 ARG A CD  1 
ATOM   2438  N NE  . ARG A 1 288 ? -17.812 14.834  -3.204  1.00 63.51  ? 288 ARG A NE  1 
ATOM   2439  C CZ  . ARG A 1 288 ? -17.518 15.385  -4.374  1.00 62.23  ? 288 ARG A CZ  1 
ATOM   2440  N NH1 . ARG A 1 288 ? -16.843 14.723  -5.301  1.00 59.22  ? 288 ARG A NH1 1 
ATOM   2441  N NH2 . ARG A 1 288 ? -17.911 16.631  -4.620  1.00 61.00  ? 288 ARG A NH2 1 
ATOM   2442  N N   . ALA A 1 289 ? -13.296 10.088  0.101   1.00 29.32  ? 289 ALA A N   1 
ATOM   2443  C CA  . ALA A 1 289 ? -12.985 9.082   1.099   1.00 21.60  ? 289 ALA A CA  1 
ATOM   2444  C C   . ALA A 1 289 ? -12.202 9.688   2.253   1.00 22.39  ? 289 ALA A C   1 
ATOM   2445  O O   . ALA A 1 289 ? -11.639 10.782  2.155   1.00 28.08  ? 289 ALA A O   1 
ATOM   2446  C CB  . ALA A 1 289 ? -12.190 7.927   0.483   1.00 18.65  ? 289 ALA A CB  1 
ATOM   2447  N N   . SER A 1 290 ? -12.179 8.949   3.355   1.00 18.14  ? 290 SER A N   1 
ATOM   2448  C CA  . SER A 1 290 ? -11.408 9.295   4.527   1.00 16.48  ? 290 SER A CA  1 
ATOM   2449  C C   . SER A 1 290 ? -10.429 8.168   4.822   1.00 17.03  ? 290 SER A C   1 
ATOM   2450  O O   . SER A 1 290 ? -10.827 6.995   4.815   1.00 19.02  ? 290 SER A O   1 
ATOM   2451  C CB  . SER A 1 290 ? -12.323 9.529   5.738   1.00 20.97  ? 290 SER A CB  1 
ATOM   2452  O OG  . SER A 1 290 ? -11.568 9.659   6.930   1.00 20.15  ? 290 SER A OG  1 
ATOM   2453  N N   . PRO A 1 291 ? -9.155  8.470   5.086   1.00 14.24  ? 291 PRO A N   1 
ATOM   2454  C CA  . PRO A 1 291 ? -8.189  7.400   5.369   1.00 13.10  ? 291 PRO A CA  1 
ATOM   2455  C C   . PRO A 1 291 ? -8.356  6.781   6.741   1.00 16.19  ? 291 PRO A C   1 
ATOM   2456  O O   . PRO A 1 291 ? -7.581  5.888   7.099   1.00 13.65  ? 291 PRO A O   1 
ATOM   2457  C CB  . PRO A 1 291 ? -6.831  8.107   5.245   1.00 21.52  ? 291 PRO A CB  1 
ATOM   2458  C CG  . PRO A 1 291 ? -7.124  9.592   5.267   1.00 30.27  ? 291 PRO A CG  1 
ATOM   2459  C CD  . PRO A 1 291 ? -8.603  9.805   5.360   1.00 16.07  ? 291 PRO A CD  1 
ATOM   2460  N N   . TYR A 1 292 ? -9.342  7.228   7.516   1.00 23.87  ? 292 TYR A N   1 
ATOM   2461  C CA  . TYR A 1 292 ? -9.530  6.791   8.892   1.00 21.02  ? 292 TYR A CA  1 
ATOM   2462  C C   . TYR A 1 292 ? -10.538 5.655   9.015   1.00 17.08  ? 292 TYR A C   1 
ATOM   2463  O O   . TYR A 1 292 ? -11.200 5.521   10.052  1.00 14.58  ? 292 TYR A O   1 
ATOM   2464  C CB  . TYR A 1 292 ? -9.927  7.991   9.749   1.00 19.14  ? 292 TYR A CB  1 
ATOM   2465  C CG  . TYR A 1 292 ? -9.017  9.175   9.501   1.00 19.64  ? 292 TYR A CG  1 
ATOM   2466  C CD1 . TYR A 1 292 ? -7.634  9.022   9.509   1.00 23.47  ? 292 TYR A CD1 1 
ATOM   2467  C CD2 . TYR A 1 292 ? -9.533  10.437  9.239   1.00 19.41  ? 292 TYR A CD2 1 
ATOM   2468  C CE1 . TYR A 1 292 ? -6.792  10.093  9.274   1.00 27.32  ? 292 TYR A CE1 1 
ATOM   2469  C CE2 . TYR A 1 292 ? -8.699  11.515  9.005   1.00 17.79  ? 292 TYR A CE2 1 
ATOM   2470  C CZ  . TYR A 1 292 ? -7.330  11.338  9.023   1.00 24.14  ? 292 TYR A CZ  1 
ATOM   2471  O OH  . TYR A 1 292 ? -6.499  12.409  8.790   1.00 27.97  ? 292 TYR A OH  1 
ATOM   2472  N N   . LEU A 1 293 ? -10.650 4.820   7.984   1.00 17.45  ? 293 LEU A N   1 
ATOM   2473  C CA  . LEU A 1 293 ? -11.603 3.724   7.938   1.00 14.92  ? 293 LEU A CA  1 
ATOM   2474  C C   . LEU A 1 293 ? -10.877 2.425   7.621   1.00 13.62  ? 293 LEU A C   1 
ATOM   2475  O O   . LEU A 1 293 ? -9.785  2.421   7.049   1.00 17.22  ? 293 LEU A O   1 
ATOM   2476  C CB  . LEU A 1 293 ? -12.684 3.961   6.873   1.00 16.17  ? 293 LEU A CB  1 
ATOM   2477  C CG  . LEU A 1 293 ? -13.980 4.672   7.251   1.00 16.73  ? 293 LEU A CG  1 
ATOM   2478  C CD1 . LEU A 1 293 ? -13.767 6.169   7.232   1.00 24.90  ? 293 LEU A CD1 1 
ATOM   2479  C CD2 . LEU A 1 293 ? -15.083 4.273   6.286   1.00 17.77  ? 293 LEU A CD2 1 
ATOM   2480  N N   . ARG A 1 294 ? -11.502 1.317   8.008   1.00 13.99  ? 294 ARG A N   1 
ATOM   2481  C CA  . ARG A 1 294 ? -11.121 0.002   7.516   1.00 13.63  ? 294 ARG A CA  1 
ATOM   2482  C C   . ARG A 1 294 ? -11.843 -0.249  6.200   1.00 14.25  ? 294 ARG A C   1 
ATOM   2483  O O   . ARG A 1 294 ? -13.046 -0.002  6.093   1.00 15.27  ? 294 ARG A O   1 
ATOM   2484  C CB  . ARG A 1 294 ? -11.475 -1.080  8.536   1.00 13.93  ? 294 ARG A CB  1 
ATOM   2485  C CG  . ARG A 1 294 ? -10.885 -2.442  8.232   1.00 13.58  ? 294 ARG A CG  1 
ATOM   2486  C CD  . ARG A 1 294 ? -11.742 -3.546  8.823   1.00 21.09  ? 294 ARG A CD  1 
ATOM   2487  N NE  . ARG A 1 294 ? -11.297 -3.929  10.157  1.00 26.60  ? 294 ARG A NE  1 
ATOM   2488  C CZ  . ARG A 1 294 ? -11.820 -3.459  11.281  1.00 28.85  ? 294 ARG A CZ  1 
ATOM   2489  N NH1 . ARG A 1 294 ? -12.793 -2.563  11.268  1.00 24.09  ? 294 ARG A NH1 1 
ATOM   2490  N NH2 . ARG A 1 294 ? -11.350 -3.893  12.446  1.00 38.48  ? 294 ARG A NH2 1 
ATOM   2491  N N   . TYR A 1 295 ? -11.115 -0.717  5.195   1.00 13.76  ? 295 TYR A N   1 
ATOM   2492  C CA  . TYR A 1 295 ? -11.695 -0.910  3.877   1.00 14.40  ? 295 TYR A CA  1 
ATOM   2493  C C   . TYR A 1 295 ? -11.676 -2.381  3.500   1.00 14.51  ? 295 TYR A C   1 
ATOM   2494  O O   . TYR A 1 295 ? -10.680 -3.079  3.718   1.00 13.78  ? 295 TYR A O   1 
ATOM   2495  C CB  . TYR A 1 295 ? -10.962 -0.079  2.819   1.00 14.02  ? 295 TYR A CB  1 
ATOM   2496  C CG  . TYR A 1 295 ? -11.354 1.382   2.843   1.00 14.42  ? 295 TYR A CG  1 
ATOM   2497  C CD1 . TYR A 1 295 ? -12.480 1.832   2.167   1.00 15.58  ? 295 TYR A CD1 1 
ATOM   2498  C CD2 . TYR A 1 295 ? -10.608 2.309   3.557   1.00 13.81  ? 295 TYR A CD2 1 
ATOM   2499  C CE1 . TYR A 1 295 ? -12.846 3.164   2.194   1.00 16.12  ? 295 TYR A CE1 1 
ATOM   2500  C CE2 . TYR A 1 295 ? -10.966 3.643   3.588   1.00 14.32  ? 295 TYR A CE2 1 
ATOM   2501  C CZ  . TYR A 1 295 ? -12.085 4.064   2.906   1.00 15.48  ? 295 TYR A CZ  1 
ATOM   2502  O OH  . TYR A 1 295 ? -12.441 5.391   2.938   1.00 21.04  ? 295 TYR A OH  1 
ATOM   2503  N N   . TYR A 1 296 ? -12.794 -2.846  2.951   1.00 15.58  ? 296 TYR A N   1 
ATOM   2504  C CA  . TYR A 1 296 ? -12.909 -4.183  2.382   1.00 15.97  ? 296 TYR A CA  1 
ATOM   2505  C C   . TYR A 1 296 ? -12.774 -4.056  0.871   1.00 16.21  ? 296 TYR A C   1 
ATOM   2506  O O   . TYR A 1 296 ? -13.671 -3.533  0.205   1.00 17.12  ? 296 TYR A O   1 
ATOM   2507  C CB  . TYR A 1 296 ? -14.244 -4.824  2.747   1.00 17.18  ? 296 TYR A CB  1 
ATOM   2508  C CG  . TYR A 1 296 ? -14.292 -5.453  4.116   1.00 17.12  ? 296 TYR A CG  1 
ATOM   2509  C CD1 . TYR A 1 296 ? -13.125 -5.763  4.803   1.00 16.64  ? 296 TYR A CD1 1 
ATOM   2510  C CD2 . TYR A 1 296 ? -15.507 -5.747  4.718   1.00 18.25  ? 296 TYR A CD2 1 
ATOM   2511  C CE1 . TYR A 1 296 ? -13.170 -6.343  6.055   1.00 16.17  ? 296 TYR A CE1 1 
ATOM   2512  C CE2 . TYR A 1 296 ? -15.562 -6.326  5.967   1.00 18.33  ? 296 TYR A CE2 1 
ATOM   2513  C CZ  . TYR A 1 296 ? -14.393 -6.622  6.631   1.00 17.29  ? 296 TYR A CZ  1 
ATOM   2514  O OH  . TYR A 1 296 ? -14.450 -7.199  7.876   1.00 22.72  ? 296 TYR A OH  1 
ATOM   2515  N N   . PHE A 1 297 ? -11.659 -4.531  0.326   1.00 15.52  ? 297 PHE A N   1 
ATOM   2516  C CA  . PHE A 1 297 ? -11.485 -4.526  -1.120  1.00 15.85  ? 297 PHE A CA  1 
ATOM   2517  C C   . PHE A 1 297 ? -12.219 -5.724  -1.706  1.00 17.73  ? 297 PHE A C   1 
ATOM   2518  O O   . PHE A 1 297 ? -11.753 -6.861  -1.594  1.00 16.76  ? 297 PHE A O   1 
ATOM   2519  C CB  . PHE A 1 297 ? -10.010 -4.556  -1.500  1.00 14.88  ? 297 PHE A CB  1 
ATOM   2520  C CG  . PHE A 1 297 ? -9.780  -4.550  -2.982  1.00 15.31  ? 297 PHE A CG  1 
ATOM   2521  C CD1 . PHE A 1 297 ? -9.840  -3.366  -3.695  1.00 15.50  ? 297 PHE A CD1 1 
ATOM   2522  C CD2 . PHE A 1 297 ? -9.531  -5.729  -3.666  1.00 15.67  ? 297 PHE A CD2 1 
ATOM   2523  C CE1 . PHE A 1 297 ? -9.643  -3.353  -5.059  1.00 18.15  ? 297 PHE A CE1 1 
ATOM   2524  C CE2 . PHE A 1 297 ? -9.333  -5.723  -5.032  1.00 16.19  ? 297 PHE A CE2 1 
ATOM   2525  C CZ  . PHE A 1 297 ? -9.389  -4.535  -5.729  1.00 16.91  ? 297 PHE A CZ  1 
ATOM   2526  N N   . ARG A 1 298 ? -13.373 -5.469  -2.323  1.00 18.92  ? 298 ARG A N   1 
ATOM   2527  C CA  . ARG A 1 298 ? -14.168 -6.477  -3.022  1.00 19.32  ? 298 ARG A CA  1 
ATOM   2528  C C   . ARG A 1 298 ? -14.524 -7.665  -2.134  1.00 19.60  ? 298 ARG A C   1 
ATOM   2529  O O   . ARG A 1 298 ? -14.782 -8.763  -2.639  1.00 29.93  ? 298 ARG A O   1 
ATOM   2530  C CB  . ARG A 1 298 ? -13.451 -6.964  -4.289  1.00 19.38  ? 298 ARG A CB  1 
ATOM   2531  C CG  . ARG A 1 298 ? -13.012 -5.847  -5.226  1.00 19.20  ? 298 ARG A CG  1 
ATOM   2532  C CD  . ARG A 1 298 ? -13.244 -6.222  -6.682  1.00 22.36  ? 298 ARG A CD  1 
ATOM   2533  N NE  . ARG A 1 298 ? -12.109 -6.919  -7.275  1.00 21.54  ? 298 ARG A NE  1 
ATOM   2534  C CZ  . ARG A 1 298 ? -11.299 -6.389  -8.182  1.00 26.21  ? 298 ARG A CZ  1 
ATOM   2535  N NH1 . ARG A 1 298 ? -11.457 -5.146  -8.608  1.00 20.52  ? 298 ARG A NH1 1 
ATOM   2536  N NH2 . ARG A 1 298 ? -10.305 -7.126  -8.676  1.00 21.86  ? 298 ARG A NH2 1 
ATOM   2537  N N   . GLU A 1 299 ? -14.536 -7.465  -0.814  1.00 19.06  ? 299 GLU A N   1 
ATOM   2538  C CA  . GLU A 1 299 ? -14.834 -8.524  0.152   1.00 28.50  ? 299 GLU A CA  1 
ATOM   2539  C C   . GLU A 1 299 ? -13.866 -9.700  0.030   1.00 24.36  ? 299 GLU A C   1 
ATOM   2540  O O   . GLU A 1 299 ? -14.220 -10.844 0.324   1.00 25.40  ? 299 GLU A O   1 
ATOM   2541  C CB  . GLU A 1 299 ? -16.285 -9.001  0.028   1.00 32.49  ? 299 GLU A CB  1 
ATOM   2542  C CG  . GLU A 1 299 ? -17.294 -7.863  0.034   1.00 36.11  ? 299 GLU A CG  1 
ATOM   2543  C CD  . GLU A 1 299 ? -18.727 -8.346  -0.068  1.00 41.54  ? 299 GLU A CD  1 
ATOM   2544  O OE1 . GLU A 1 299 ? -18.934 -9.553  -0.320  1.00 43.20  ? 299 GLU A OE1 1 
ATOM   2545  O OE2 . GLU A 1 299 ? -19.646 -7.517  0.099   1.00 44.98  ? 299 GLU A OE2 1 
ATOM   2546  N N   . LEU A 1 300 ? -12.638 -9.424  -0.409  1.00 18.69  ? 300 LEU A N   1 
ATOM   2547  C CA  . LEU A 1 300 ? -11.553 -10.398 -0.422  1.00 17.53  ? 300 LEU A CA  1 
ATOM   2548  C C   . LEU A 1 300 ? -10.482 -10.086 0.611   1.00 19.46  ? 300 LEU A C   1 
ATOM   2549  O O   . LEU A 1 300 ? -10.096 -10.956 1.397   1.00 20.20  ? 300 LEU A O   1 
ATOM   2550  C CB  . LEU A 1 300 ? -10.903 -10.461 -1.814  1.00 17.54  ? 300 LEU A CB  1 
ATOM   2551  C CG  . LEU A 1 300 ? -11.784 -10.566 -3.055  1.00 18.73  ? 300 LEU A CG  1 
ATOM   2552  C CD1 . LEU A 1 300 ? -10.931 -10.485 -4.316  1.00 18.60  ? 300 LEU A CD1 1 
ATOM   2553  C CD2 . LEU A 1 300 ? -12.580 -11.858 -3.026  1.00 24.07  ? 300 LEU A CD2 1 
ATOM   2554  N N   . ILE A 1 301 ? -10.001 -8.845  0.630   1.00 19.09  ? 301 ILE A N   1 
ATOM   2555  C CA  . ILE A 1 301 ? -8.861  -8.442  1.437   1.00 14.35  ? 301 ILE A CA  1 
ATOM   2556  C C   . ILE A 1 301 ? -9.229  -7.168  2.187   1.00 13.97  ? 301 ILE A C   1 
ATOM   2557  O O   . ILE A 1 301 ? -10.192 -6.475  1.850   1.00 14.48  ? 301 ILE A O   1 
ATOM   2558  C CB  . ILE A 1 301 ? -7.600  -8.224  0.568   1.00 13.72  ? 301 ILE A CB  1 
ATOM   2559  C CG1 . ILE A 1 301 ? -6.323  -8.389  1.390   1.00 17.79  ? 301 ILE A CG1 1 
ATOM   2560  C CG2 . ILE A 1 301 ? -7.635  -6.859  -0.098  1.00 13.45  ? 301 ILE A CG2 1 
ATOM   2561  C CD1 . ILE A 1 301 ? -5.147  -8.871  0.570   1.00 24.91  ? 301 ILE A CD1 1 
ATOM   2562  N N   . SER A 1 302 ? -8.456  -6.874  3.226   1.00 13.21  ? 302 SER A N   1 
ATOM   2563  C CA  . SER A 1 302 ? -8.612  -5.655  4.007   1.00 12.84  ? 302 SER A CA  1 
ATOM   2564  C C   . SER A 1 302 ? -7.465  -4.709  3.687   1.00 11.97  ? 302 SER A C   1 
ATOM   2565  O O   . SER A 1 302 ? -6.300  -5.119  3.685   1.00 15.49  ? 302 SER A O   1 
ATOM   2566  C CB  . SER A 1 302 ? -8.650  -5.963  5.505   1.00 12.81  ? 302 SER A CB  1 
ATOM   2567  O OG  . SER A 1 302 ? -9.931  -6.426  5.895   1.00 15.26  ? 302 SER A OG  1 
ATOM   2568  N N   . VAL A 1 303 ? -7.794  -3.451  3.408   1.00 11.96  ? 303 VAL A N   1 
ATOM   2569  C CA  . VAL A 1 303 ? -6.808  -2.436  3.060   1.00 11.32  ? 303 VAL A CA  1 
ATOM   2570  C C   . VAL A 1 303 ? -6.926  -1.275  4.037   1.00 11.13  ? 303 VAL A C   1 
ATOM   2571  O O   . VAL A 1 303 ? -8.030  -0.914  4.458   1.00 11.79  ? 303 VAL A O   1 
ATOM   2572  C CB  . VAL A 1 303 ? -6.975  -1.943  1.607   1.00 11.66  ? 303 VAL A CB  1 
ATOM   2573  C CG1 . VAL A 1 303 ? -5.726  -1.204  1.150   1.00 11.05  ? 303 VAL A CG1 1 
ATOM   2574  C CG2 . VAL A 1 303 ? -7.273  -3.109  0.677   1.00 12.19  ? 303 VAL A CG2 1 
ATOM   2575  N N   . PHE A 1 304 ? -5.782  -0.707  4.409   1.00 10.45  ? 304 PHE A N   1 
ATOM   2576  C CA  . PHE A 1 304 ? -5.712  0.523   5.183   1.00 11.43  ? 304 PHE A CA  1 
ATOM   2577  C C   . PHE A 1 304 ? -4.884  1.547   4.418   1.00 11.79  ? 304 PHE A C   1 
ATOM   2578  O O   . PHE A 1 304 ? -3.966  1.196   3.675   1.00 12.22  ? 304 PHE A O   1 
ATOM   2579  C CB  . PHE A 1 304 ? -5.091  0.292   6.566   1.00 16.09  ? 304 PHE A CB  1 
ATOM   2580  C CG  . PHE A 1 304 ? -5.950  -0.517  7.493   1.00 10.37  ? 304 PHE A CG  1 
ATOM   2581  C CD1 . PHE A 1 304 ? -6.918  0.092   8.272   1.00 10.88  ? 304 PHE A CD1 1 
ATOM   2582  C CD2 . PHE A 1 304 ? -5.777  -1.886  7.599   1.00 10.39  ? 304 PHE A CD2 1 
ATOM   2583  C CE1 . PHE A 1 304 ? -7.706  -0.651  9.128   1.00 11.56  ? 304 PHE A CE1 1 
ATOM   2584  C CE2 . PHE A 1 304 ? -6.562  -2.634  8.457   1.00 12.63  ? 304 PHE A CE2 1 
ATOM   2585  C CZ  . PHE A 1 304 ? -7.526  -2.014  9.220   1.00 11.40  ? 304 PHE A CZ  1 
ATOM   2586  N N   . PHE A 1 305 ? -5.219  2.819   4.593   1.00 10.31  ? 305 PHE A N   1 
ATOM   2587  C CA  . PHE A 1 305 ? -4.517  3.903   3.918   1.00 10.24  ? 305 PHE A CA  1 
ATOM   2588  C C   . PHE A 1 305 ? -3.837  4.772   4.966   1.00 11.90  ? 305 PHE A C   1 
ATOM   2589  O O   . PHE A 1 305 ? -4.499  5.295   5.868   1.00 15.97  ? 305 PHE A O   1 
ATOM   2590  C CB  . PHE A 1 305 ? -5.481  4.714   3.050   1.00 11.04  ? 305 PHE A CB  1 
ATOM   2591  C CG  . PHE A 1 305 ? -6.175  3.892   1.996   1.00 11.47  ? 305 PHE A CG  1 
ATOM   2592  C CD1 . PHE A 1 305 ? -5.610  3.723   0.745   1.00 11.46  ? 305 PHE A CD1 1 
ATOM   2593  C CD2 . PHE A 1 305 ? -7.385  3.277   2.262   1.00 12.00  ? 305 PHE A CD2 1 
ATOM   2594  C CE1 . PHE A 1 305 ? -6.245  2.968   -0.223  1.00 11.98  ? 305 PHE A CE1 1 
ATOM   2595  C CE2 . PHE A 1 305 ? -8.021  2.520   1.297   1.00 12.52  ? 305 PHE A CE2 1 
ATOM   2596  C CZ  . PHE A 1 305 ? -7.449  2.365   0.054   1.00 12.51  ? 305 PHE A CZ  1 
ATOM   2597  N N   . ARG A 1 306 ? -2.518  4.914   4.852   1.00 9.49   ? 306 ARG A N   1 
ATOM   2598  C CA  . ARG A 1 306 ? -1.760  5.665   5.840   1.00 9.31   ? 306 ARG A CA  1 
ATOM   2599  C C   . ARG A 1 306 ? -2.087  7.149   5.749   1.00 16.99  ? 306 ARG A C   1 
ATOM   2600  O O   . ARG A 1 306 ? -2.452  7.666   4.690   1.00 19.81  ? 306 ARG A O   1 
ATOM   2601  C CB  . ARG A 1 306 ? -0.254  5.453   5.651   1.00 9.44   ? 306 ARG A CB  1 
ATOM   2602  C CG  . ARG A 1 306 ? 0.336   6.138   4.423   1.00 17.28  ? 306 ARG A CG  1 
ATOM   2603  C CD  . ARG A 1 306 ? 1.863   6.077   4.419   1.00 12.36  ? 306 ARG A CD  1 
ATOM   2604  N NE  . ARG A 1 306 ? 2.429   6.686   3.219   1.00 17.01  ? 306 ARG A NE  1 
ATOM   2605  C CZ  . ARG A 1 306 ? 3.155   7.796   3.203   1.00 19.51  ? 306 ARG A CZ  1 
ATOM   2606  N NH1 . ARG A 1 306 ? 3.458   8.442   4.314   1.00 29.57  ? 306 ARG A NH1 1 
ATOM   2607  N NH2 . ARG A 1 306 ? 3.587   8.271   2.038   1.00 22.80  ? 306 ARG A NH2 1 
ATOM   2608  N N   . ASP A 1 307 ? -1.963  7.833   6.884   1.00 20.01  ? 307 ASP A N   1 
ATOM   2609  C CA  . ASP A 1 307 ? -2.131  9.283   6.944   1.00 21.22  ? 307 ASP A CA  1 
ATOM   2610  C C   . ASP A 1 307 ? -0.844  9.912   6.425   1.00 25.44  ? 307 ASP A C   1 
ATOM   2611  O O   . ASP A 1 307 ? 0.145   10.023  7.153   1.00 25.60  ? 307 ASP A O   1 
ATOM   2612  C CB  . ASP A 1 307 ? -2.447  9.724   8.369   1.00 22.26  ? 307 ASP A CB  1 
ATOM   2613  C CG  . ASP A 1 307 ? -2.837  11.185  8.456   1.00 33.94  ? 307 ASP A CG  1 
ATOM   2614  O OD1 . ASP A 1 307 ? -1.955  12.050  8.267   1.00 29.40  ? 307 ASP A OD1 1 
ATOM   2615  O OD2 . ASP A 1 307 ? -4.025  11.467  8.725   1.00 26.71  ? 307 ASP A OD2 1 
ATOM   2616  N N   . LYS A 1 308 ? -0.859  10.330  5.156   1.00 27.98  ? 308 LYS A N   1 
ATOM   2617  C CA  . LYS A 1 308 ? 0.381   10.674  4.463   1.00 22.90  ? 308 LYS A CA  1 
ATOM   2618  C C   . LYS A 1 308 ? 1.114   11.819  5.152   1.00 26.24  ? 308 LYS A C   1 
ATOM   2619  O O   . LYS A 1 308 ? 2.336   11.765  5.334   1.00 28.90  ? 308 LYS A O   1 
ATOM   2620  C CB  . LYS A 1 308 ? 0.088   11.029  3.005   1.00 25.50  ? 308 LYS A CB  1 
ATOM   2621  C CG  . LYS A 1 308 ? 1.321   11.458  2.221   1.00 29.84  ? 308 LYS A CG  1 
ATOM   2622  C CD  . LYS A 1 308 ? 1.052   12.701  1.390   1.00 29.56  ? 308 LYS A CD  1 
ATOM   2623  C CE  . LYS A 1 308 ? 2.021   12.798  0.224   1.00 41.98  ? 308 LYS A CE  1 
ATOM   2624  N NZ  . LYS A 1 308 ? 3.402   12.403  0.620   1.00 37.74  ? 308 LYS A NZ  1 
ATOM   2625  N N   . THR A 1 309 ? 0.384   12.870  5.539   1.00 24.26  ? 309 THR A N   1 
ATOM   2626  C CA  . THR A 1 309 ? 1.035   14.041  6.119   1.00 21.27  ? 309 THR A CA  1 
ATOM   2627  C C   . THR A 1 309 ? 1.680   13.716  7.462   1.00 24.28  ? 309 THR A C   1 
ATOM   2628  O O   . THR A 1 309 ? 2.786   14.186  7.752   1.00 26.42  ? 309 THR A O   1 
ATOM   2629  C CB  . THR A 1 309 ? 0.036   15.188  6.265   1.00 14.36  ? 309 THR A CB  1 
ATOM   2630  O OG1 . THR A 1 309 ? -0.629  15.090  7.530   1.00 34.59  ? 309 THR A OG1 1 
ATOM   2631  C CG2 . THR A 1 309 ? -0.994  15.144  5.145   1.00 13.67  ? 309 THR A CG2 1 
ATOM   2632  N N   . LEU A 1 310 ? 1.007   12.917  8.294   1.00 19.24  ? 310 LEU A N   1 
ATOM   2633  C CA  . LEU A 1 310 ? 1.575   12.560  9.592   1.00 19.53  ? 310 LEU A CA  1 
ATOM   2634  C C   . LEU A 1 310 ? 2.833   11.715  9.435   1.00 17.71  ? 310 LEU A C   1 
ATOM   2635  O O   . LEU A 1 310 ? 3.843   11.961  10.105  1.00 25.58  ? 310 LEU A O   1 
ATOM   2636  C CB  . LEU A 1 310 ? 0.537   11.828  10.441  1.00 18.62  ? 310 LEU A CB  1 
ATOM   2637  C CG  . LEU A 1 310 ? -0.487  12.727  11.132  1.00 16.89  ? 310 LEU A CG  1 
ATOM   2638  C CD1 . LEU A 1 310 ? -1.376  11.906  12.044  1.00 21.78  ? 310 LEU A CD1 1 
ATOM   2639  C CD2 . LEU A 1 310 ? 0.216   13.832  11.903  1.00 12.66  ? 310 LEU A CD2 1 
ATOM   2640  N N   . SER A 1 311 ? 2.793   10.710  8.556   1.00 15.42  ? 311 SER A N   1 
ATOM   2641  C CA  . SER A 1 311 ? 3.973   9.881   8.339   1.00 16.59  ? 311 SER A CA  1 
ATOM   2642  C C   . SER A 1 311 ? 5.099   10.681  7.696   1.00 17.93  ? 311 SER A C   1 
ATOM   2643  O O   . SER A 1 311 ? 6.275   10.468  8.011   1.00 18.97  ? 311 SER A O   1 
ATOM   2644  C CB  . SER A 1 311 ? 3.612   8.669   7.479   1.00 16.92  ? 311 SER A CB  1 
ATOM   2645  O OG  . SER A 1 311 ? 2.533   7.941   8.044   1.00 20.47  ? 311 SER A OG  1 
ATOM   2646  N N   . ASP A 1 312 ? 4.760   11.609  6.799   1.00 25.08  ? 312 ASP A N   1 
ATOM   2647  C CA  . ASP A 1 312 ? 5.783   12.446  6.182   1.00 19.37  ? 312 ASP A CA  1 
ATOM   2648  C C   . ASP A 1 312 ? 6.435   13.374  7.198   1.00 15.93  ? 312 ASP A C   1 
ATOM   2649  O O   . ASP A 1 312 ? 7.634   13.654  7.095   1.00 18.03  ? 312 ASP A O   1 
ATOM   2650  C CB  . ASP A 1 312 ? 5.178   13.249  5.031   1.00 23.48  ? 312 ASP A CB  1 
ATOM   2651  C CG  . ASP A 1 312 ? 5.317   12.545  3.695   1.00 31.17  ? 312 ASP A CG  1 
ATOM   2652  O OD1 . ASP A 1 312 ? 5.319   11.296  3.681   1.00 28.28  ? 312 ASP A OD1 1 
ATOM   2653  O OD2 . ASP A 1 312 ? 5.420   13.238  2.660   1.00 41.94  ? 312 ASP A OD2 1 
ATOM   2654  N N   . LEU A 1 313 ? 5.668   13.859  8.180   1.00 19.24  ? 313 LEU A N   1 
ATOM   2655  C CA  . LEU A 1 313 ? 6.225   14.758  9.186   1.00 15.08  ? 313 LEU A CA  1 
ATOM   2656  C C   . LEU A 1 313 ? 7.356   14.090  9.959   1.00 15.12  ? 313 LEU A C   1 
ATOM   2657  O O   . LEU A 1 313 ? 8.408   14.696  10.192  1.00 16.75  ? 313 LEU A O   1 
ATOM   2658  C CB  . LEU A 1 313 ? 5.127   15.225  10.142  1.00 12.51  ? 313 LEU A CB  1 
ATOM   2659  C CG  . LEU A 1 313 ? 4.195   16.338  9.658   1.00 15.24  ? 313 LEU A CG  1 
ATOM   2660  C CD1 . LEU A 1 313 ? 2.882   16.306  10.427  1.00 16.18  ? 313 LEU A CD1 1 
ATOM   2661  C CD2 . LEU A 1 313 ? 4.863   17.696  9.784   1.00 17.16  ? 313 LEU A CD2 1 
ATOM   2662  N N   . ILE A 1 314 ? 7.157   12.837  10.369  1.00 11.21  ? 314 ILE A N   1 
ATOM   2663  C CA  . ILE A 1 314 ? 8.198   12.121  11.100  1.00 12.15  ? 314 ILE A CA  1 
ATOM   2664  C C   . ILE A 1 314 ? 9.399   11.863  10.199  1.00 13.39  ? 314 ILE A C   1 
ATOM   2665  O O   . ILE A 1 314 ? 10.547  12.137  10.571  1.00 17.93  ? 314 ILE A O   1 
ATOM   2666  C CB  . ILE A 1 314 ? 7.639   10.809  11.682  1.00 11.96  ? 314 ILE A CB  1 
ATOM   2667  C CG1 . ILE A 1 314 ? 6.747   11.092  12.891  1.00 10.79  ? 314 ILE A CG1 1 
ATOM   2668  C CG2 . ILE A 1 314 ? 8.771   9.868   12.064  1.00 14.50  ? 314 ILE A CG2 1 
ATOM   2669  C CD1 . ILE A 1 314 ? 5.653   10.068  13.086  1.00 10.33  ? 314 ILE A CD1 1 
ATOM   2670  N N   . GLY A 1 315 ? 9.153   11.351  8.990   1.00 16.00  ? 315 GLY A N   1 
ATOM   2671  C CA  . GLY A 1 315 ? 10.239  10.922  8.129   1.00 11.81  ? 315 GLY A CA  1 
ATOM   2672  C C   . GLY A 1 315 ? 11.022  12.037  7.472   1.00 14.38  ? 315 GLY A C   1 
ATOM   2673  O O   . GLY A 1 315 ? 12.165  11.811  7.060   1.00 22.20  ? 315 GLY A O   1 
ATOM   2674  N N   . PHE A 1 316 ? 10.443  13.233  7.356   1.00 11.82  ? 316 PHE A N   1 
ATOM   2675  C CA  . PHE A 1 316 ? 11.115  14.302  6.629   1.00 12.62  ? 316 PHE A CA  1 
ATOM   2676  C C   . PHE A 1 316 ? 11.076  15.668  7.300   1.00 13.45  ? 316 PHE A C   1 
ATOM   2677  O O   . PHE A 1 316 ? 11.767  16.570  6.819   1.00 23.77  ? 316 PHE A O   1 
ATOM   2678  C CB  . PHE A 1 316 ? 10.523  14.440  5.216   1.00 13.33  ? 316 PHE A CB  1 
ATOM   2679  C CG  . PHE A 1 316 ? 10.579  13.174  4.401   1.00 17.11  ? 316 PHE A CG  1 
ATOM   2680  C CD1 . PHE A 1 316 ? 11.734  12.817  3.723   1.00 16.57  ? 316 PHE A CD1 1 
ATOM   2681  C CD2 . PHE A 1 316 ? 9.471   12.345  4.303   1.00 21.68  ? 316 PHE A CD2 1 
ATOM   2682  C CE1 . PHE A 1 316 ? 11.788  11.654  2.971   1.00 19.70  ? 316 PHE A CE1 1 
ATOM   2683  C CE2 . PHE A 1 316 ? 9.518   11.181  3.552   1.00 27.42  ? 316 PHE A CE2 1 
ATOM   2684  C CZ  . PHE A 1 316 ? 10.678  10.836  2.885   1.00 19.39  ? 316 PHE A CZ  1 
ATOM   2685  N N   . SER A 1 317 ? 10.309  15.872  8.372   1.00 15.47  ? 317 SER A N   1 
ATOM   2686  C CA  . SER A 1 317 ? 10.088  17.218  8.892   1.00 17.11  ? 317 SER A CA  1 
ATOM   2687  C C   . SER A 1 317 ? 10.551  17.414  10.329  1.00 20.84  ? 317 SER A C   1 
ATOM   2688  O O   . SER A 1 317 ? 11.243  18.399  10.618  1.00 17.43  ? 317 SER A O   1 
ATOM   2689  C CB  . SER A 1 317 ? 8.600   17.581  8.776   1.00 20.00  ? 317 SER A CB  1 
ATOM   2690  O OG  . SER A 1 317 ? 8.383   18.942  9.110   1.00 39.33  ? 317 SER A OG  1 
ATOM   2691  N N   . TYR A 1 318 ? 10.189  16.512  11.246  1.00 15.74  ? 318 TYR A N   1 
ATOM   2692  C CA  . TYR A 1 318 ? 10.396  16.772  12.670  1.00 14.59  ? 318 TYR A CA  1 
ATOM   2693  C C   . TYR A 1 318 ? 11.864  16.790  13.080  1.00 15.13  ? 318 TYR A C   1 
ATOM   2694  O O   . TYR A 1 318 ? 12.162  17.206  14.206  1.00 15.81  ? 318 TYR A O   1 
ATOM   2695  C CB  . TYR A 1 318 ? 9.657   15.737  13.522  1.00 13.92  ? 318 TYR A CB  1 
ATOM   2696  C CG  . TYR A 1 318 ? 8.162   15.951  13.632  1.00 13.81  ? 318 TYR A CG  1 
ATOM   2697  C CD1 . TYR A 1 318 ? 7.610   17.218  13.520  1.00 15.73  ? 318 TYR A CD1 1 
ATOM   2698  C CD2 . TYR A 1 318 ? 7.305   14.884  13.873  1.00 16.62  ? 318 TYR A CD2 1 
ATOM   2699  C CE1 . TYR A 1 318 ? 6.245   17.414  13.628  1.00 14.65  ? 318 TYR A CE1 1 
ATOM   2700  C CE2 . TYR A 1 318 ? 5.941   15.071  13.984  1.00 13.12  ? 318 TYR A CE2 1 
ATOM   2701  C CZ  . TYR A 1 318 ? 5.417   16.336  13.861  1.00 13.91  ? 318 TYR A CZ  1 
ATOM   2702  O OH  . TYR A 1 318 ? 4.059   16.522  13.971  1.00 17.72  ? 318 TYR A OH  1 
ATOM   2703  N N   . HIS A 1 319 ? 12.781  16.351  12.212  1.00 14.97  ? 319 HIS A N   1 
ATOM   2704  C CA  . HIS A 1 319 ? 14.192  16.309  12.587  1.00 15.61  ? 319 HIS A CA  1 
ATOM   2705  C C   . HIS A 1 319 ? 14.719  17.699  12.923  1.00 16.88  ? 319 HIS A C   1 
ATOM   2706  O O   . HIS A 1 319 ? 15.560  17.854  13.816  1.00 17.64  ? 319 HIS A O   1 
ATOM   2707  C CB  . HIS A 1 319 ? 15.021  15.680  11.466  1.00 15.37  ? 319 HIS A CB  1 
ATOM   2708  C CG  . HIS A 1 319 ? 14.896  16.383  10.150  1.00 15.55  ? 319 HIS A CG  1 
ATOM   2709  N ND1 . HIS A 1 319 ? 15.586  17.540  9.859   1.00 16.64  ? 319 HIS A ND1 1 
ATOM   2710  C CD2 . HIS A 1 319 ? 14.173  16.089  9.044   1.00 15.00  ? 319 HIS A CD2 1 
ATOM   2711  C CE1 . HIS A 1 319 ? 15.287  17.933  8.634   1.00 16.67  ? 319 HIS A CE1 1 
ATOM   2712  N NE2 . HIS A 1 319 ? 14.432  17.069  8.117   1.00 17.68  ? 319 HIS A NE2 1 
ATOM   2713  N N   . ALA A 1 320 ? 14.230  18.722  12.227  1.00 17.57  ? 320 ALA A N   1 
ATOM   2714  C CA  . ALA A 1 320 ? 14.652  20.096  12.461  1.00 24.51  ? 320 ALA A CA  1 
ATOM   2715  C C   . ALA A 1 320 ? 13.913  20.757  13.621  1.00 19.10  ? 320 ALA A C   1 
ATOM   2716  O O   . ALA A 1 320 ? 14.090  21.959  13.842  1.00 20.88  ? 320 ALA A O   1 
ATOM   2717  C CB  . ALA A 1 320 ? 14.473  20.927  11.187  1.00 18.99  ? 320 ALA A CB  1 
ATOM   2718  N N   . TRP A 1 321 ? 13.096  20.009  14.357  1.00 18.34  ? 321 TRP A N   1 
ATOM   2719  C CA  . TRP A 1 321 ? 12.327  20.528  15.477  1.00 25.34  ? 321 TRP A CA  1 
ATOM   2720  C C   . TRP A 1 321 ? 12.914  20.044  16.796  1.00 29.63  ? 321 TRP A C   1 
ATOM   2721  O O   . TRP A 1 321 ? 13.576  19.004  16.861  1.00 37.11  ? 321 TRP A O   1 
ATOM   2722  C CB  . TRP A 1 321 ? 10.861  20.081  15.414  1.00 20.14  ? 321 TRP A CB  1 
ATOM   2723  C CG  . TRP A 1 321 ? 10.071  20.471  14.201  1.00 22.62  ? 321 TRP A CG  1 
ATOM   2724  C CD1 . TRP A 1 321 ? 10.501  20.516  12.907  1.00 23.72  ? 321 TRP A CD1 1 
ATOM   2725  C CD2 . TRP A 1 321 ? 8.687   20.838  14.176  1.00 20.77  ? 321 TRP A CD2 1 
ATOM   2726  N NE1 . TRP A 1 321 ? 9.472   20.902  12.080  1.00 25.39  ? 321 TRP A NE1 1 
ATOM   2727  C CE2 . TRP A 1 321 ? 8.347   21.105  12.836  1.00 19.35  ? 321 TRP A CE2 1 
ATOM   2728  C CE3 . TRP A 1 321 ? 7.702   20.973  15.162  1.00 18.10  ? 321 TRP A CE3 1 
ATOM   2729  C CZ2 . TRP A 1 321 ? 7.067   21.499  12.455  1.00 17.90  ? 321 TRP A CZ2 1 
ATOM   2730  C CZ3 . TRP A 1 321 ? 6.433   21.364  14.782  1.00 20.28  ? 321 TRP A CZ3 1 
ATOM   2731  C CH2 . TRP A 1 321 ? 6.126   21.623  13.441  1.00 19.90  ? 321 TRP A CH2 1 
ATOM   2732  N N   . ASN A 1 322 ? 12.640  20.805  17.855  1.00 23.74  ? 322 ASN A N   1 
ATOM   2733  C CA  . ASN A 1 322 ? 12.825  20.286  19.203  1.00 26.86  ? 322 ASN A CA  1 
ATOM   2734  C C   . ASN A 1 322 ? 11.895  19.099  19.428  1.00 28.03  ? 322 ASN A C   1 
ATOM   2735  O O   . ASN A 1 322 ? 10.790  19.035  18.882  1.00 28.02  ? 322 ASN A O   1 
ATOM   2736  C CB  . ASN A 1 322 ? 12.552  21.368  20.248  1.00 23.66  ? 322 ASN A CB  1 
ATOM   2737  C CG  . ASN A 1 322 ? 13.622  22.444  20.277  1.00 38.39  ? 322 ASN A CG  1 
ATOM   2738  O OD1 . ASN A 1 322 ? 14.758  22.223  19.858  1.00 44.61  ? 322 ASN A OD1 1 
ATOM   2739  N ND2 . ASN A 1 322 ? 13.262  23.618  20.783  1.00 40.29  ? 322 ASN A ND2 1 
ATOM   2740  N N   . ALA A 1 323 ? 12.355  18.144  20.241  1.00 24.14  ? 323 ALA A N   1 
ATOM   2741  C CA  . ALA A 1 323 ? 11.575  16.931  20.471  1.00 16.25  ? 323 ALA A CA  1 
ATOM   2742  C C   . ALA A 1 323 ? 10.225  17.250  21.100  1.00 17.15  ? 323 ALA A C   1 
ATOM   2743  O O   . ALA A 1 323 ? 9.196   16.699  20.690  1.00 20.27  ? 323 ALA A O   1 
ATOM   2744  C CB  . ALA A 1 323 ? 12.360  15.963  21.353  1.00 16.32  ? 323 ALA A CB  1 
ATOM   2745  N N   . GLU A 1 324 ? 10.208  18.138  22.097  1.00 27.06  ? 324 GLU A N   1 
ATOM   2746  C CA  . GLU A 1 324 ? 8.952   18.512  22.739  1.00 31.42  ? 324 GLU A CA  1 
ATOM   2747  C C   . GLU A 1 324 ? 7.985   19.130  21.737  1.00 30.88  ? 324 GLU A C   1 
ATOM   2748  O O   . GLU A 1 324 ? 6.805   18.764  21.688  1.00 28.88  ? 324 GLU A O   1 
ATOM   2749  C CB  . GLU A 1 324 ? 9.222   19.481  23.891  1.00 36.11  ? 324 GLU A CB  1 
ATOM   2750  C CG  . GLU A 1 324 ? 8.240   19.371  25.045  1.00 45.30  ? 324 GLU A CG  1 
ATOM   2751  C CD  . GLU A 1 324 ? 8.918   19.430  26.400  1.00 61.72  ? 324 GLU A CD  1 
ATOM   2752  O OE1 . GLU A 1 324 ? 10.117  19.778  26.456  1.00 63.40  ? 324 GLU A OE1 1 
ATOM   2753  O OE2 . GLU A 1 324 ? 8.251   19.129  27.412  1.00 66.19  ? 324 GLU A OE2 1 
ATOM   2754  N N   . ASP A 1 325 ? 8.475   20.068  20.921  1.00 33.14  ? 325 ASP A N   1 
ATOM   2755  C CA  . ASP A 1 325 ? 7.622   20.698  19.917  1.00 24.63  ? 325 ASP A CA  1 
ATOM   2756  C C   . ASP A 1 325 ? 7.121   19.681  18.901  1.00 22.91  ? 325 ASP A C   1 
ATOM   2757  O O   . ASP A 1 325 ? 5.954   19.722  18.492  1.00 18.99  ? 325 ASP A O   1 
ATOM   2758  C CB  . ASP A 1 325 ? 8.381   21.824  19.212  1.00 32.41  ? 325 ASP A CB  1 
ATOM   2759  C CG  . ASP A 1 325 ? 9.032   22.786  20.183  1.00 43.13  ? 325 ASP A CG  1 
ATOM   2760  O OD1 . ASP A 1 325 ? 8.453   23.023  21.264  1.00 43.58  ? 325 ASP A OD1 1 
ATOM   2761  O OD2 . ASP A 1 325 ? 10.119  23.313  19.860  1.00 41.01  ? 325 ASP A OD2 1 
ATOM   2762  N N   . ALA A 1 326 ? 7.991   18.762  18.478  1.00 24.96  ? 326 ALA A N   1 
ATOM   2763  C CA  . ALA A 1 326 ? 7.593   17.761  17.494  1.00 21.59  ? 326 ALA A CA  1 
ATOM   2764  C C   . ALA A 1 326 ? 6.470   16.876  18.023  1.00 20.51  ? 326 ALA A C   1 
ATOM   2765  O O   . ALA A 1 326 ? 5.500   16.598  17.308  1.00 24.91  ? 326 ALA A O   1 
ATOM   2766  C CB  . ALA A 1 326 ? 8.800   16.915  17.091  1.00 15.52  ? 326 ALA A CB  1 
ATOM   2767  N N   . VAL A 1 327 ? 6.582   16.426  19.274  1.00 18.87  ? 327 VAL A N   1 
ATOM   2768  C CA  . VAL A 1 327 ? 5.539   15.588  19.857  1.00 14.62  ? 327 VAL A CA  1 
ATOM   2769  C C   . VAL A 1 327 ? 4.271   16.400  20.095  1.00 20.44  ? 327 VAL A C   1 
ATOM   2770  O O   . VAL A 1 327 ? 3.157   15.919  19.858  1.00 18.28  ? 327 VAL A O   1 
ATOM   2771  C CB  . VAL A 1 327 ? 6.048   14.930  21.153  1.00 16.64  ? 327 VAL A CB  1 
ATOM   2772  C CG1 . VAL A 1 327 ? 4.911   14.227  21.883  1.00 13.83  ? 327 VAL A CG1 1 
ATOM   2773  C CG2 . VAL A 1 327 ? 7.177   13.958  20.844  1.00 17.94  ? 327 VAL A CG2 1 
ATOM   2774  N N   . ARG A 1 328 ? 4.419   17.648  20.554  1.00 20.68  ? 328 ARG A N   1 
ATOM   2775  C CA  . ARG A 1 328 ? 3.253   18.495  20.793  1.00 17.38  ? 328 ARG A CA  1 
ATOM   2776  C C   . ARG A 1 328 ? 2.472   18.743  19.508  1.00 17.20  ? 328 ARG A C   1 
ATOM   2777  O O   . ARG A 1 328 ? 1.239   18.661  19.501  1.00 17.46  ? 328 ARG A O   1 
ATOM   2778  C CB  . ARG A 1 328 ? 3.675   19.823  21.424  1.00 19.22  ? 328 ARG A CB  1 
ATOM   2779  C CG  . ARG A 1 328 ? 3.785   19.799  22.943  1.00 20.17  ? 328 ARG A CG  1 
ATOM   2780  C CD  . ARG A 1 328 ? 3.658   21.205  23.531  1.00 29.08  ? 328 ARG A CD  1 
ATOM   2781  N NE  . ARG A 1 328 ? 4.903   21.954  23.401  1.00 44.35  ? 328 ARG A NE  1 
ATOM   2782  C CZ  . ARG A 1 328 ? 5.070   23.016  22.622  1.00 47.89  ? 328 ARG A CZ  1 
ATOM   2783  N NH1 . ARG A 1 328 ? 4.089   23.481  21.864  1.00 43.04  ? 328 ARG A NH1 1 
ATOM   2784  N NH2 . ARG A 1 328 ? 6.255   23.619  22.590  1.00 42.67  ? 328 ARG A NH2 1 
ATOM   2785  N N   . ASP A 1 329 ? 3.170   19.046  18.409  1.00 16.94  ? 329 ASP A N   1 
ATOM   2786  C CA  . ASP A 1 329 ? 2.487   19.201  17.129  1.00 16.89  ? 329 ASP A CA  1 
ATOM   2787  C C   . ASP A 1 329 ? 1.817   17.898  16.715  1.00 15.48  ? 329 ASP A C   1 
ATOM   2788  O O   . ASP A 1 329 ? 0.656   17.891  16.294  1.00 15.77  ? 329 ASP A O   1 
ATOM   2789  C CB  . ASP A 1 329 ? 3.473   19.660  16.055  1.00 17.00  ? 329 ASP A CB  1 
ATOM   2790  C CG  . ASP A 1 329 ? 2.836   19.753  14.680  1.00 21.67  ? 329 ASP A CG  1 
ATOM   2791  O OD1 . ASP A 1 329 ? 2.081   20.719  14.440  1.00 24.23  ? 329 ASP A OD1 1 
ATOM   2792  O OD2 . ASP A 1 329 ? 3.088   18.862  13.840  1.00 20.41  ? 329 ASP A OD2 1 
ATOM   2793  N N   . PHE A 1 330 ? 2.534   16.780  16.855  1.00 14.17  ? 330 PHE A N   1 
ATOM   2794  C CA  . PHE A 1 330 ? 1.996   15.479  16.466  1.00 13.00  ? 330 PHE A CA  1 
ATOM   2795  C C   . PHE A 1 330 ? 0.690   15.177  17.193  1.00 15.02  ? 330 PHE A C   1 
ATOM   2796  O O   . PHE A 1 330 ? -0.307  14.793  16.569  1.00 15.60  ? 330 PHE A O   1 
ATOM   2797  C CB  . PHE A 1 330 ? 3.035   14.394  16.748  1.00 11.92  ? 330 PHE A CB  1 
ATOM   2798  C CG  . PHE A 1 330 ? 2.694   13.054  16.166  1.00 10.88  ? 330 PHE A CG  1 
ATOM   2799  C CD1 . PHE A 1 330 ? 2.955   12.776  14.836  1.00 10.45  ? 330 PHE A CD1 1 
ATOM   2800  C CD2 . PHE A 1 330 ? 2.120   12.068  16.952  1.00 10.57  ? 330 PHE A CD2 1 
ATOM   2801  C CE1 . PHE A 1 330 ? 2.645   11.541  14.297  1.00 9.73   ? 330 PHE A CE1 1 
ATOM   2802  C CE2 . PHE A 1 330 ? 1.808   10.831  16.420  1.00 9.85   ? 330 PHE A CE2 1 
ATOM   2803  C CZ  . PHE A 1 330 ? 2.071   10.567  15.090  1.00 9.43   ? 330 PHE A CZ  1 
ATOM   2804  N N   . ILE A 1 331 ? 0.677   15.347  18.517  1.00 13.91  ? 331 ILE A N   1 
ATOM   2805  C CA  . ILE A 1 331 ? -0.540  15.093  19.282  1.00 14.49  ? 331 ILE A CA  1 
ATOM   2806  C C   . ILE A 1 331 ? -1.621  16.104  18.922  1.00 16.84  ? 331 ILE A C   1 
ATOM   2807  O O   . ILE A 1 331 ? -2.812  15.772  18.904  1.00 22.07  ? 331 ILE A O   1 
ATOM   2808  C CB  . ILE A 1 331 ? -0.238  15.091  20.793  1.00 16.34  ? 331 ILE A CB  1 
ATOM   2809  C CG1 . ILE A 1 331 ? 0.876   14.094  21.114  1.00 20.59  ? 331 ILE A CG1 1 
ATOM   2810  C CG2 . ILE A 1 331 ? -1.484  14.743  21.589  1.00 15.89  ? 331 ILE A CG2 1 
ATOM   2811  C CD1 . ILE A 1 331 ? 0.677   12.725  20.492  1.00 17.84  ? 331 ILE A CD1 1 
ATOM   2812  N N   . GLY A 1 332 ? -1.231  17.348  18.635  1.00 16.68  ? 332 GLY A N   1 
ATOM   2813  C CA  . GLY A 1 332 ? -2.206  18.334  18.199  1.00 18.11  ? 332 GLY A CA  1 
ATOM   2814  C C   . GLY A 1 332 ? -2.884  17.947  16.898  1.00 17.68  ? 332 GLY A C   1 
ATOM   2815  O O   . GLY A 1 332 ? -4.074  18.207  16.706  1.00 18.69  ? 332 GLY A O   1 
ATOM   2816  N N   . ARG A 1 333 ? -2.131  17.332  15.980  1.00 16.38  ? 333 ARG A N   1 
ATOM   2817  C CA  . ARG A 1 333 ? -2.736  16.822  14.753  1.00 16.04  ? 333 ARG A CA  1 
ATOM   2818  C C   . ARG A 1 333 ? -3.705  15.686  15.050  1.00 16.63  ? 333 ARG A C   1 
ATOM   2819  O O   . ARG A 1 333 ? -4.793  15.621  14.466  1.00 27.62  ? 333 ARG A O   1 
ATOM   2820  C CB  . ARG A 1 333 ? -1.651  16.354  13.784  1.00 14.93  ? 333 ARG A CB  1 
ATOM   2821  C CG  . ARG A 1 333 ? -0.534  17.356  13.596  1.00 15.42  ? 333 ARG A CG  1 
ATOM   2822  C CD  . ARG A 1 333 ? -0.350  17.786  12.158  1.00 15.91  ? 333 ARG A CD  1 
ATOM   2823  N NE  . ARG A 1 333 ? 0.846   18.606  12.018  1.00 16.40  ? 333 ARG A NE  1 
ATOM   2824  C CZ  . ARG A 1 333 ? 1.174   19.274  10.921  1.00 30.51  ? 333 ARG A CZ  1 
ATOM   2825  N NH1 . ARG A 1 333 ? 0.426   19.220  9.831   1.00 24.26  ? 333 ARG A NH1 1 
ATOM   2826  N NH2 . ARG A 1 333 ? 2.282   20.012  10.917  1.00 32.58  ? 333 ARG A NH2 1 
ATOM   2827  N N   . LEU A 1 334 ? -3.322  14.779  15.952  1.00 14.63  ? 334 LEU A N   1 
ATOM   2828  C CA  . LEU A 1 334 ? -4.200  13.670  16.312  1.00 18.17  ? 334 LEU A CA  1 
ATOM   2829  C C   . LEU A 1 334 ? -5.482  14.168  16.967  1.00 26.41  ? 334 LEU A C   1 
ATOM   2830  O O   . LEU A 1 334 ? -6.558  13.593  16.760  1.00 22.24  ? 334 LEU A O   1 
ATOM   2831  C CB  . LEU A 1 334 ? -3.464  12.700  17.235  1.00 16.59  ? 334 LEU A CB  1 
ATOM   2832  C CG  . LEU A 1 334 ? -2.245  12.011  16.623  1.00 13.00  ? 334 LEU A CG  1 
ATOM   2833  C CD1 . LEU A 1 334 ? -1.648  10.995  17.587  1.00 11.54  ? 334 LEU A CD1 1 
ATOM   2834  C CD2 . LEU A 1 334 ? -2.633  11.347  15.316  1.00 11.71  ? 334 LEU A CD2 1 
ATOM   2835  N N   . LYS A 1 335 ? -5.385  15.231  17.769  1.00 29.40  ? 335 LYS A N   1 
ATOM   2836  C CA  . LYS A 1 335 ? -6.581  15.814  18.367  1.00 26.48  ? 335 LYS A CA  1 
ATOM   2837  C C   . LYS A 1 335 ? -7.542  16.310  17.295  1.00 20.12  ? 335 LYS A C   1 
ATOM   2838  O O   . LYS A 1 335 ? -8.758  16.122  17.408  1.00 24.42  ? 335 LYS A O   1 
ATOM   2839  C CB  . LYS A 1 335 ? -6.195  16.953  19.313  1.00 23.30  ? 335 LYS A CB  1 
ATOM   2840  C CG  . LYS A 1 335 ? -6.531  16.703  20.773  1.00 20.58  ? 335 LYS A CG  1 
ATOM   2841  C CD  . LYS A 1 335 ? -8.020  16.487  20.977  1.00 35.80  ? 335 LYS A CD  1 
ATOM   2842  C CE  . LYS A 1 335 ? -8.330  16.200  22.435  1.00 47.97  ? 335 LYS A CE  1 
ATOM   2843  N NZ  . LYS A 1 335 ? -9.579  15.409  22.590  1.00 36.00  ? 335 LYS A NZ  1 
ATOM   2844  N N   . LYS A 1 336 ? -7.015  16.934  16.238  1.00 19.48  ? 336 LYS A N   1 
ATOM   2845  C CA  . LYS A 1 336 ? -7.878  17.450  15.181  1.00 27.31  ? 336 LYS A CA  1 
ATOM   2846  C C   . LYS A 1 336 ? -8.519  16.330  14.370  1.00 31.86  ? 336 LYS A C   1 
ATOM   2847  O O   . LYS A 1 336 ? -9.637  16.494  13.872  1.00 35.11  ? 336 LYS A O   1 
ATOM   2848  C CB  . LYS A 1 336 ? -7.089  18.400  14.277  1.00 25.85  ? 336 LYS A CB  1 
ATOM   2849  C CG  . LYS A 1 336 ? -6.782  19.734  14.951  1.00 31.31  ? 336 LYS A CG  1 
ATOM   2850  C CD  . LYS A 1 336 ? -6.408  20.834  13.965  1.00 48.38  ? 336 LYS A CD  1 
ATOM   2851  C CE  . LYS A 1 336 ? -4.900  20.937  13.770  1.00 39.15  ? 336 LYS A CE  1 
ATOM   2852  N NZ  . LYS A 1 336 ? -4.541  21.117  12.334  1.00 42.95  ? 336 LYS A NZ  1 
ATOM   2853  N N   . ILE A 1 337 ? -7.833  15.194  14.224  1.00 26.08  ? 337 ILE A N   1 
ATOM   2854  C CA  . ILE A 1 337 ? -8.453  14.031  13.594  1.00 17.80  ? 337 ILE A CA  1 
ATOM   2855  C C   . ILE A 1 337 ? -9.578  13.491  14.469  1.00 19.08  ? 337 ILE A C   1 
ATOM   2856  O O   . ILE A 1 337 ? -10.635 13.085  13.970  1.00 25.27  ? 337 ILE A O   1 
ATOM   2857  C CB  . ILE A 1 337 ? -7.398  12.948  13.304  1.00 16.01  ? 337 ILE A CB  1 
ATOM   2858  C CG1 . ILE A 1 337 ? -6.268  13.514  12.444  1.00 15.53  ? 337 ILE A CG1 1 
ATOM   2859  C CG2 . ILE A 1 337 ? -8.036  11.747  12.621  1.00 15.80  ? 337 ILE A CG2 1 
ATOM   2860  C CD1 . ILE A 1 337 ? -4.973  12.742  12.566  1.00 14.32  ? 337 ILE A CD1 1 
ATOM   2861  N N   . HIS A 1 338 ? -9.365  13.475  15.788  1.00 22.49  ? 338 HIS A N   1 
ATOM   2862  C CA  . HIS A 1 338 ? -10.359 12.938  16.714  1.00 25.01  ? 338 HIS A CA  1 
ATOM   2863  C C   . HIS A 1 338 ? -11.668 13.719  16.670  1.00 32.53  ? 338 HIS A C   1 
ATOM   2864  O O   . HIS A 1 338 ? -12.734 13.149  16.927  1.00 32.12  ? 338 HIS A O   1 
ATOM   2865  C CB  . HIS A 1 338 ? -9.783  12.932  18.133  1.00 23.90  ? 338 HIS A CB  1 
ATOM   2866  C CG  . HIS A 1 338 ? -10.702 12.359  19.167  1.00 21.23  ? 338 HIS A CG  1 
ATOM   2867  N ND1 . HIS A 1 338 ? -11.483 13.147  19.985  1.00 28.31  ? 338 HIS A ND1 1 
ATOM   2868  C CD2 . HIS A 1 338 ? -10.957 11.078  19.524  1.00 27.17  ? 338 HIS A CD2 1 
ATOM   2869  C CE1 . HIS A 1 338 ? -12.183 12.376  20.798  1.00 29.17  ? 338 HIS A CE1 1 
ATOM   2870  N NE2 . HIS A 1 338 ? -11.883 11.116  20.539  1.00 27.32  ? 338 HIS A NE2 1 
ATOM   2871  N N   . GLU A 1 339 ? -11.617 15.014  16.350  1.00 32.50  ? 339 GLU A N   1 
ATOM   2872  C CA  . GLU A 1 339 ? -12.826 15.827  16.316  1.00 26.72  ? 339 GLU A CA  1 
ATOM   2873  C C   . GLU A 1 339 ? -13.370 16.053  14.912  1.00 29.29  ? 339 GLU A C   1 
ATOM   2874  O O   . GLU A 1 339 ? -14.544 16.414  14.775  1.00 31.47  ? 339 GLU A O   1 
ATOM   2875  C CB  . GLU A 1 339 ? -12.578 17.192  16.973  1.00 29.82  ? 339 GLU A CB  1 
ATOM   2876  C CG  . GLU A 1 339 ? -11.208 17.783  16.680  1.00 42.35  ? 339 GLU A CG  1 
ATOM   2877  C CD  . GLU A 1 339 ? -10.671 18.620  17.830  1.00 68.02  ? 339 GLU A CD  1 
ATOM   2878  O OE1 . GLU A 1 339 ? -10.693 18.135  18.982  1.00 68.76  ? 339 GLU A OE1 1 
ATOM   2879  O OE2 . GLU A 1 339 ? -10.215 19.758  17.583  1.00 65.61  ? 339 GLU A OE2 1 
ATOM   2880  N N   . SER A 1 340 ? -12.554 15.860  13.874  1.00 28.11  ? 340 SER A N   1 
ATOM   2881  C CA  . SER A 1 340 ? -13.018 16.097  12.511  1.00 29.75  ? 340 SER A CA  1 
ATOM   2882  C C   . SER A 1 340 ? -14.006 15.040  12.037  1.00 30.85  ? 340 SER A C   1 
ATOM   2883  O O   . SER A 1 340 ? -14.795 15.315  11.126  1.00 31.28  ? 340 SER A O   1 
ATOM   2884  C CB  . SER A 1 340 ? -11.831 16.153  11.550  1.00 28.54  ? 340 SER A CB  1 
ATOM   2885  O OG  . SER A 1 340 ? -11.587 14.881  10.974  1.00 24.02  ? 340 SER A OG  1 
ATOM   2886  N N   . VAL A 1 341 ? -13.978 13.847  12.624  1.00 28.22  ? 341 VAL A N   1 
ATOM   2887  C CA  . VAL A 1 341 ? -14.855 12.756  12.224  1.00 26.94  ? 341 VAL A CA  1 
ATOM   2888  C C   . VAL A 1 341 ? -15.850 12.477  13.345  1.00 32.98  ? 341 VAL A C   1 
ATOM   2889  O O   . VAL A 1 341 ? -15.629 12.810  14.513  1.00 39.32  ? 341 VAL A O   1 
ATOM   2890  C CB  . VAL A 1 341 ? -14.060 11.486  11.858  1.00 23.04  ? 341 VAL A CB  1 
ATOM   2891  C CG1 . VAL A 1 341 ? -13.025 11.800  10.787  1.00 21.45  ? 341 VAL A CG1 1 
ATOM   2892  C CG2 . VAL A 1 341 ? -13.388 10.908  13.093  1.00 26.95  ? 341 VAL A CG2 1 
ATOM   2893  N N   . ASP A 1 342 ? -16.968 11.858  12.973  1.00 34.48  ? 342 ASP A N   1 
ATOM   2894  C CA  . ASP A 1 342 ? -18.041 11.548  13.907  1.00 35.49  ? 342 ASP A CA  1 
ATOM   2895  C C   . ASP A 1 342 ? -17.961 10.130  14.456  1.00 36.77  ? 342 ASP A C   1 
ATOM   2896  O O   . ASP A 1 342 ? -18.801 9.749   15.279  1.00 45.10  ? 342 ASP A O   1 
ATOM   2897  C CB  . ASP A 1 342 ? -19.399 11.767  13.230  1.00 50.94  ? 342 ASP A CB  1 
ATOM   2898  C CG  . ASP A 1 342 ? -19.400 11.330  11.774  1.00 57.41  ? 342 ASP A CG  1 
ATOM   2899  O OD1 . ASP A 1 342 ? -18.516 11.781  11.016  1.00 54.58  ? 342 ASP A OD1 1 
ATOM   2900  O OD2 . ASP A 1 342 ? -20.281 10.537  11.385  1.00 53.06  ? 342 ASP A OD2 1 
ATOM   2901  N N   . PHE A 1 343 ? -16.979 9.347   14.026  1.00 30.67  ? 343 PHE A N   1 
ATOM   2902  C CA  . PHE A 1 343 ? -16.786 7.966   14.449  1.00 28.28  ? 343 PHE A CA  1 
ATOM   2903  C C   . PHE A 1 343 ? -15.439 7.842   15.154  1.00 22.55  ? 343 PHE A C   1 
ATOM   2904  O O   . PHE A 1 343 ? -14.697 8.816   15.290  1.00 27.62  ? 343 PHE A O   1 
ATOM   2905  C CB  . PHE A 1 343 ? -16.867 7.020   13.247  1.00 27.84  ? 343 PHE A CB  1 
ATOM   2906  C CG  . PHE A 1 343 ? -15.964 7.410   12.113  1.00 23.05  ? 343 PHE A CG  1 
ATOM   2907  C CD1 . PHE A 1 343 ? -16.404 8.272   11.122  1.00 24.09  ? 343 PHE A CD1 1 
ATOM   2908  C CD2 . PHE A 1 343 ? -14.671 6.924   12.045  1.00 21.15  ? 343 PHE A CD2 1 
ATOM   2909  C CE1 . PHE A 1 343 ? -15.573 8.637   10.084  1.00 23.27  ? 343 PHE A CE1 1 
ATOM   2910  C CE2 . PHE A 1 343 ? -13.836 7.285   11.009  1.00 23.15  ? 343 PHE A CE2 1 
ATOM   2911  C CZ  . PHE A 1 343 ? -14.288 8.144   10.028  1.00 21.37  ? 343 PHE A CZ  1 
ATOM   2912  N N   . GLN A 1 344 ? -15.126 6.627   15.604  1.00 21.87  ? 344 GLN A N   1 
ATOM   2913  C CA  . GLN A 1 344 ? -13.819 6.349   16.191  1.00 20.87  ? 344 GLN A CA  1 
ATOM   2914  C C   . GLN A 1 344 ? -12.824 6.049   15.076  1.00 18.72  ? 344 GLN A C   1 
ATOM   2915  O O   . GLN A 1 344 ? -12.823 4.942   14.525  1.00 22.71  ? 344 GLN A O   1 
ATOM   2916  C CB  . GLN A 1 344 ? -13.896 5.179   17.175  1.00 22.03  ? 344 GLN A CB  1 
ATOM   2917  C CG  . GLN A 1 344 ? -14.536 5.526   18.514  1.00 22.69  ? 344 GLN A CG  1 
ATOM   2918  C CD  . GLN A 1 344 ? -14.285 4.471   19.578  1.00 23.51  ? 344 GLN A CD  1 
ATOM   2919  O OE1 . GLN A 1 344 ? -13.371 4.597   20.390  1.00 27.34  ? 344 GLN A OE1 1 
ATOM   2920  N NE2 . GLN A 1 344 ? -15.106 3.428   19.581  1.00 23.01  ? 344 GLN A NE2 1 
ATOM   2921  N N   . PRO A 1 345 ? -11.970 6.999   14.713  1.00 17.85  ? 345 PRO A N   1 
ATOM   2922  C CA  . PRO A 1 345 ? -11.102 6.807   13.552  1.00 16.75  ? 345 PRO A CA  1 
ATOM   2923  C C   . PRO A 1 345 ? -9.914  5.910   13.865  1.00 17.45  ? 345 PRO A C   1 
ATOM   2924  O O   . PRO A 1 345 ? -9.546  5.686   15.019  1.00 33.74  ? 345 PRO A O   1 
ATOM   2925  C CB  . PRO A 1 345 ? -10.642 8.232   13.234  1.00 16.65  ? 345 PRO A CB  1 
ATOM   2926  C CG  . PRO A 1 345 ? -10.563 8.870   14.576  1.00 16.87  ? 345 PRO A CG  1 
ATOM   2927  C CD  . PRO A 1 345 ? -11.693 8.277   15.392  1.00 18.00  ? 345 PRO A CD  1 
ATOM   2928  N N   . VAL A 1 346 ? -9.315  5.393   12.797  1.00 21.53  ? 346 VAL A N   1 
ATOM   2929  C CA  . VAL A 1 346 ? -8.043  4.688   12.862  1.00 15.30  ? 346 VAL A CA  1 
ATOM   2930  C C   . VAL A 1 346 ? -7.030  5.489   12.054  1.00 19.04  ? 346 VAL A C   1 
ATOM   2931  O O   . VAL A 1 346 ? -7.358  6.037   10.996  1.00 23.83  ? 346 VAL A O   1 
ATOM   2932  C CB  . VAL A 1 346 ? -8.154  3.231   12.356  1.00 16.53  ? 346 VAL A CB  1 
ATOM   2933  C CG1 . VAL A 1 346 ? -8.180  3.161   10.831  1.00 17.96  ? 346 VAL A CG1 1 
ATOM   2934  C CG2 . VAL A 1 346 ? -7.018  2.390   12.914  1.00 17.23  ? 346 VAL A CG2 1 
ATOM   2935  N N   . VAL A 1 347 ? -5.818  5.611   12.584  1.00 18.06  ? 347 VAL A N   1 
ATOM   2936  C CA  . VAL A 1 347 ? -4.773  6.420   11.966  1.00 11.63  ? 347 VAL A CA  1 
ATOM   2937  C C   . VAL A 1 347 ? -3.556  5.532   11.766  1.00 15.50  ? 347 VAL A C   1 
ATOM   2938  O O   . VAL A 1 347 ? -2.898  5.144   12.739  1.00 15.33  ? 347 VAL A O   1 
ATOM   2939  C CB  . VAL A 1 347 ? -4.419  7.654   12.803  1.00 11.15  ? 347 VAL A CB  1 
ATOM   2940  C CG1 . VAL A 1 347 ? -3.440  8.533   12.049  1.00 14.01  ? 347 VAL A CG1 1 
ATOM   2941  C CG2 . VAL A 1 347 ? -5.675  8.432   13.141  1.00 12.24  ? 347 VAL A CG2 1 
ATOM   2942  N N   . PHE A 1 348 ? -3.253  5.212   10.512  1.00 13.91  ? 348 PHE A N   1 
ATOM   2943  C CA  . PHE A 1 348 ? -2.074  4.426   10.185  1.00 9.81   ? 348 PHE A CA  1 
ATOM   2944  C C   . PHE A 1 348 ? -0.889  5.345   9.925   1.00 13.41  ? 348 PHE A C   1 
ATOM   2945  O O   . PHE A 1 348 ? -0.969  6.263   9.102   1.00 10.36  ? 348 PHE A O   1 
ATOM   2946  C CB  . PHE A 1 348 ? -2.331  3.530   8.973   1.00 10.38  ? 348 PHE A CB  1 
ATOM   2947  C CG  . PHE A 1 348 ? -2.627  2.105   9.334   1.00 13.18  ? 348 PHE A CG  1 
ATOM   2948  C CD1 . PHE A 1 348 ? -3.749  1.785   10.082  1.00 15.00  ? 348 PHE A CD1 1 
ATOM   2949  C CD2 . PHE A 1 348 ? -1.773  1.088   8.944   1.00 14.23  ? 348 PHE A CD2 1 
ATOM   2950  C CE1 . PHE A 1 348 ? -4.023  0.472   10.423  1.00 11.50  ? 348 PHE A CE1 1 
ATOM   2951  C CE2 . PHE A 1 348 ? -2.038  -0.226  9.283   1.00 14.79  ? 348 PHE A CE2 1 
ATOM   2952  C CZ  . PHE A 1 348 ? -3.164  -0.534  10.023  1.00 11.51  ? 348 PHE A CZ  1 
ATOM   2953  N N   . VAL A 1 349 ? 0.203   5.098   10.640  1.00 13.04  ? 349 VAL A N   1 
ATOM   2954  C CA  . VAL A 1 349 ? 1.467   5.793   10.442  1.00 11.41  ? 349 VAL A CA  1 
ATOM   2955  C C   . VAL A 1 349 ? 2.455   4.762   9.919   1.00 11.62  ? 349 VAL A C   1 
ATOM   2956  O O   . VAL A 1 349 ? 2.928   3.907   10.678  1.00 15.50  ? 349 VAL A O   1 
ATOM   2957  C CB  . VAL A 1 349 ? 1.970   6.444   11.738  1.00 11.58  ? 349 VAL A CB  1 
ATOM   2958  C CG1 . VAL A 1 349 ? 3.237   7.244   11.476  1.00 17.98  ? 349 VAL A CG1 1 
ATOM   2959  C CG2 . VAL A 1 349 ? 0.889   7.323   12.352  1.00 8.83   ? 349 VAL A CG2 1 
ATOM   2960  N N   . VAL A 1 350 ? 2.756   4.824   8.624   1.00 8.77   ? 350 VAL A N   1 
ATOM   2961  C CA  . VAL A 1 350 ? 3.672   3.891   7.977   1.00 12.11  ? 350 VAL A CA  1 
ATOM   2962  C C   . VAL A 1 350 ? 4.790   4.686   7.319   1.00 10.93  ? 350 VAL A C   1 
ATOM   2963  O O   . VAL A 1 350 ? 4.523   5.641   6.581   1.00 18.99  ? 350 VAL A O   1 
ATOM   2964  C CB  . VAL A 1 350 ? 2.956   3.013   6.934   1.00 11.76  ? 350 VAL A CB  1 
ATOM   2965  C CG1 . VAL A 1 350 ? 3.887   1.913   6.446   1.00 15.84  ? 350 VAL A CG1 1 
ATOM   2966  C CG2 . VAL A 1 350 ? 1.679   2.426   7.511   1.00 13.87  ? 350 VAL A CG2 1 
ATOM   2967  N N   . LEU A 1 351 ? 6.033   4.288   7.581   1.00 9.08   ? 351 LEU A N   1 
ATOM   2968  C CA  . LEU A 1 351 ? 7.196   4.903   6.954   1.00 14.16  ? 351 LEU A CA  1 
ATOM   2969  C C   . LEU A 1 351 ? 8.413   4.038   7.252   1.00 11.13  ? 351 LEU A C   1 
ATOM   2970  O O   . LEU A 1 351 ? 8.388   3.186   8.145   1.00 11.14  ? 351 LEU A O   1 
ATOM   2971  C CB  . LEU A 1 351 ? 7.417   6.341   7.435   1.00 13.42  ? 351 LEU A CB  1 
ATOM   2972  C CG  . LEU A 1 351 ? 7.770   6.570   8.905   1.00 18.00  ? 351 LEU A CG  1 
ATOM   2973  C CD1 . LEU A 1 351 ? 8.584   7.840   9.041   1.00 20.25  ? 351 LEU A CD1 1 
ATOM   2974  C CD2 . LEU A 1 351 ? 6.516   6.648   9.767   1.00 16.89  ? 351 LEU A CD2 1 
ATOM   2975  N N   . ASP A 1 352 ? 9.483   4.274   6.493   1.00 14.13  ? 352 ASP A N   1 
ATOM   2976  C CA  . ASP A 1 352 ? 10.739  3.568   6.721   1.00 11.41  ? 352 ASP A CA  1 
ATOM   2977  C C   . ASP A 1 352 ? 11.257  3.863   8.124   1.00 12.66  ? 352 ASP A C   1 
ATOM   2978  O O   . ASP A 1 352 ? 11.408  5.024   8.515   1.00 12.50  ? 352 ASP A O   1 
ATOM   2979  C CB  . ASP A 1 352 ? 11.774  3.979   5.674   1.00 15.34  ? 352 ASP A CB  1 
ATOM   2980  C CG  . ASP A 1 352 ? 11.343  3.637   4.256   1.00 24.08  ? 352 ASP A CG  1 
ATOM   2981  O OD1 . ASP A 1 352 ? 10.452  2.778   4.092   1.00 24.82  ? 352 ASP A OD1 1 
ATOM   2982  O OD2 . ASP A 1 352 ? 11.897  4.227   3.304   1.00 25.54  ? 352 ASP A OD2 1 
ATOM   2983  N N   . GLY A 1 353 ? 11.547  2.803   8.874   1.00 10.14  ? 353 GLY A N   1 
ATOM   2984  C CA  . GLY A 1 353 ? 11.880  2.937   10.277  1.00 9.84   ? 353 GLY A CA  1 
ATOM   2985  C C   . GLY A 1 353 ? 13.363  2.932   10.578  1.00 16.98  ? 353 GLY A C   1 
ATOM   2986  O O   . GLY A 1 353 ? 13.770  2.592   11.692  1.00 34.05  ? 353 GLY A O   1 
ATOM   2987  N N   . GLU A 1 354 ? 14.189  3.292   9.595   1.00 11.19  ? 354 GLU A N   1 
ATOM   2988  C CA  . GLU A 1 354 ? 15.628  3.381   9.836   1.00 12.04  ? 354 GLU A CA  1 
ATOM   2989  C C   . GLU A 1 354 ? 16.287  4.634   9.279   1.00 16.20  ? 354 GLU A C   1 
ATOM   2990  O O   . GLU A 1 354 ? 17.325  5.040   9.811   1.00 15.95  ? 354 GLU A O   1 
ATOM   2991  C CB  . GLU A 1 354 ? 16.347  2.159   9.241   1.00 13.38  ? 354 GLU A CB  1 
ATOM   2992  C CG  . GLU A 1 354 ? 16.223  2.066   7.728   1.00 19.74  ? 354 GLU A CG  1 
ATOM   2993  C CD  . GLU A 1 354 ? 15.269  0.986   7.275   1.00 33.14  ? 354 GLU A CD  1 
ATOM   2994  O OE1 . GLU A 1 354 ? 15.737  -0.131  6.978   1.00 67.66  ? 354 GLU A OE1 1 
ATOM   2995  O OE2 . GLU A 1 354 ? 14.045  1.244   7.258   1.00 30.50  ? 354 GLU A OE2 1 
ATOM   2996  N N   . ASN A 1 355 ? 15.737  5.266   8.245   1.00 21.78  ? 355 ASN A N   1 
ATOM   2997  C CA  . ASN A 1 355 ? 16.483  6.249   7.471   1.00 14.90  ? 355 ASN A CA  1 
ATOM   2998  C C   . ASN A 1 355 ? 16.324  7.679   7.969   1.00 16.64  ? 355 ASN A C   1 
ATOM   2999  O O   . ASN A 1 355 ? 17.139  8.536   7.608   1.00 14.48  ? 355 ASN A O   1 
ATOM   3000  C CB  . ASN A 1 355 ? 16.066  6.176   5.997   1.00 13.88  ? 355 ASN A CB  1 
ATOM   3001  C CG  . ASN A 1 355 ? 16.338  4.817   5.383   1.00 19.36  ? 355 ASN A CG  1 
ATOM   3002  O OD1 . ASN A 1 355 ? 17.446  4.287   5.485   1.00 20.37  ? 355 ASN A OD1 1 
ATOM   3003  N ND2 . ASN A 1 355 ? 15.326  4.240   4.746   1.00 36.65  ? 355 ASN A ND2 1 
ATOM   3004  N N   . CYS A 1 356 ? 15.312  7.961   8.784   1.00 13.12  ? 356 CYS A N   1 
ATOM   3005  C CA  . CYS A 1 356 ? 15.056  9.335   9.195   1.00 12.70  ? 356 CYS A CA  1 
ATOM   3006  C C   . CYS A 1 356 ? 15.781  9.736   10.473  1.00 18.14  ? 356 CYS A C   1 
ATOM   3007  O O   . CYS A 1 356 ? 15.941  10.936  10.720  1.00 23.54  ? 356 CYS A O   1 
ATOM   3008  C CB  . CYS A 1 356 ? 13.549  9.560   9.373   1.00 14.91  ? 356 CYS A CB  1 
ATOM   3009  S SG  . CYS A 1 356 ? 12.714  8.374   10.456  1.00 27.93  ? 356 CYS A SG  1 
ATOM   3010  N N   . TRP A 1 357 ? 16.231  8.777   11.282  1.00 15.77  ? 357 TRP A N   1 
ATOM   3011  C CA  . TRP A 1 357 ? 16.730  9.115   12.611  1.00 12.58  ? 357 TRP A CA  1 
ATOM   3012  C C   . TRP A 1 357 ? 18.158  9.644   12.599  1.00 17.24  ? 357 TRP A C   1 
ATOM   3013  O O   . TRP A 1 357 ? 18.543  10.376  13.517  1.00 21.10  ? 357 TRP A O   1 
ATOM   3014  C CB  . TRP A 1 357 ? 16.627  7.896   13.524  1.00 12.18  ? 357 TRP A CB  1 
ATOM   3015  C CG  . TRP A 1 357 ? 15.337  7.185   13.355  1.00 11.17  ? 357 TRP A CG  1 
ATOM   3016  C CD1 . TRP A 1 357 ? 15.143  5.964   12.786  1.00 13.49  ? 357 TRP A CD1 1 
ATOM   3017  C CD2 . TRP A 1 357 ? 14.042  7.665   13.734  1.00 13.94  ? 357 TRP A CD2 1 
ATOM   3018  N NE1 . TRP A 1 357 ? 13.807  5.644   12.800  1.00 20.43  ? 357 TRP A NE1 1 
ATOM   3019  C CE2 . TRP A 1 357 ? 13.110  6.672   13.379  1.00 14.14  ? 357 TRP A CE2 1 
ATOM   3020  C CE3 . TRP A 1 357 ? 13.583  8.833   14.349  1.00 23.04  ? 357 TRP A CE3 1 
ATOM   3021  C CZ2 . TRP A 1 357 ? 11.743  6.813   13.614  1.00 11.16  ? 357 TRP A CZ2 1 
ATOM   3022  C CZ3 . TRP A 1 357 ? 12.226  8.972   14.583  1.00 13.59  ? 357 TRP A CZ3 1 
ATOM   3023  C CH2 . TRP A 1 357 ? 11.323  7.967   14.215  1.00 9.20   ? 357 TRP A CH2 1 
ATOM   3024  N N   . GLU A 1 358 ? 18.957  9.290   11.590  1.00 20.57  ? 358 GLU A N   1 
ATOM   3025  C CA  . GLU A 1 358 ? 20.327  9.789   11.540  1.00 16.04  ? 358 GLU A CA  1 
ATOM   3026  C C   . GLU A 1 358 ? 20.380  11.306  11.420  1.00 18.58  ? 358 GLU A C   1 
ATOM   3027  O O   . GLU A 1 358 ? 21.400  11.910  11.767  1.00 32.15  ? 358 GLU A O   1 
ATOM   3028  C CB  . GLU A 1 358 ? 21.084  9.149   10.378  1.00 16.97  ? 358 GLU A CB  1 
ATOM   3029  C CG  . GLU A 1 358 ? 20.368  9.233   9.044   1.00 25.30  ? 358 GLU A CG  1 
ATOM   3030  C CD  . GLU A 1 358 ? 20.921  8.252   8.032   1.00 32.25  ? 358 GLU A CD  1 
ATOM   3031  O OE1 . GLU A 1 358 ? 22.040  8.486   7.529   1.00 36.54  ? 358 GLU A OE1 1 
ATOM   3032  O OE2 . GLU A 1 358 ? 20.243  7.244   7.745   1.00 36.91  ? 358 GLU A OE2 1 
ATOM   3033  N N   . TYR A 1 359 ? 19.307  11.930  10.944  1.00 17.62  ? 359 TYR A N   1 
ATOM   3034  C CA  . TYR A 1 359 ? 19.203  13.379  10.867  1.00 16.85  ? 359 TYR A CA  1 
ATOM   3035  C C   . TYR A 1 359 ? 18.564  13.989  12.108  1.00 16.46  ? 359 TYR A C   1 
ATOM   3036  O O   . TYR A 1 359 ? 18.386  15.211  12.159  1.00 17.21  ? 359 TYR A O   1 
ATOM   3037  C CB  . TYR A 1 359 ? 18.403  13.786  9.624   1.00 21.24  ? 359 TYR A CB  1 
ATOM   3038  C CG  . TYR A 1 359 ? 18.933  13.195  8.338   1.00 17.36  ? 359 TYR A CG  1 
ATOM   3039  C CD1 . TYR A 1 359 ? 19.960  13.814  7.640   1.00 19.03  ? 359 TYR A CD1 1 
ATOM   3040  C CD2 . TYR A 1 359 ? 18.402  12.021  7.819   1.00 16.64  ? 359 TYR A CD2 1 
ATOM   3041  C CE1 . TYR A 1 359 ? 20.449  13.277  6.466   1.00 26.31  ? 359 TYR A CE1 1 
ATOM   3042  C CE2 . TYR A 1 359 ? 18.884  11.477  6.643   1.00 18.61  ? 359 TYR A CE2 1 
ATOM   3043  C CZ  . TYR A 1 359 ? 19.907  12.109  5.971   1.00 18.88  ? 359 TYR A CZ  1 
ATOM   3044  O OH  . TYR A 1 359 ? 20.391  11.573  4.800   1.00 24.77  ? 359 TYR A OH  1 
ATOM   3045  N N   . TYR A 1 360 ? 18.220  13.176  13.103  1.00 15.54  ? 360 TYR A N   1 
ATOM   3046  C CA  . TYR A 1 360 ? 17.604  13.647  14.334  1.00 15.33  ? 360 TYR A CA  1 
ATOM   3047  C C   . TYR A 1 360 ? 18.664  13.917  15.396  1.00 16.46  ? 360 TYR A C   1 
ATOM   3048  O O   . TYR A 1 360 ? 19.765  13.364  15.365  1.00 17.08  ? 360 TYR A O   1 
ATOM   3049  C CB  . TYR A 1 360 ? 16.615  12.614  14.870  1.00 13.99  ? 360 TYR A CB  1 
ATOM   3050  C CG  . TYR A 1 360 ? 15.187  12.750  14.404  1.00 13.08  ? 360 TYR A CG  1 
ATOM   3051  C CD1 . TYR A 1 360 ? 14.831  12.457  13.097  1.00 12.69  ? 360 TYR A CD1 1 
ATOM   3052  C CD2 . TYR A 1 360 ? 14.186  13.135  15.284  1.00 12.79  ? 360 TYR A CD2 1 
ATOM   3053  C CE1 . TYR A 1 360 ? 13.521  12.564  12.671  1.00 12.37  ? 360 TYR A CE1 1 
ATOM   3054  C CE2 . TYR A 1 360 ? 12.873  13.246  14.869  1.00 16.51  ? 360 TYR A CE2 1 
ATOM   3055  C CZ  . TYR A 1 360 ? 12.546  12.959  13.560  1.00 13.67  ? 360 TYR A CZ  1 
ATOM   3056  O OH  . TYR A 1 360 ? 11.241  13.065  13.138  1.00 11.33  ? 360 TYR A OH  1 
ATOM   3057  N N   . GLU A 1 361 ? 18.310  14.776  16.350  1.00 16.92  ? 361 GLU A N   1 
ATOM   3058  C CA  . GLU A 1 361 ? 19.156  14.979  17.520  1.00 18.07  ? 361 GLU A CA  1 
ATOM   3059  C C   . GLU A 1 361 ? 19.242  13.684  18.316  1.00 17.99  ? 361 GLU A C   1 
ATOM   3060  O O   . GLU A 1 361 ? 18.217  13.084  18.649  1.00 20.06  ? 361 GLU A O   1 
ATOM   3061  C CB  . GLU A 1 361 ? 18.593  16.099  18.398  1.00 27.18  ? 361 GLU A CB  1 
ATOM   3062  C CG  . GLU A 1 361 ? 18.704  17.502  17.815  1.00 45.28  ? 361 GLU A CG  1 
ATOM   3063  C CD  . GLU A 1 361 ? 20.122  17.867  17.417  1.00 56.41  ? 361 GLU A CD  1 
ATOM   3064  O OE1 . GLU A 1 361 ? 21.062  17.486  18.145  1.00 45.62  ? 361 GLU A OE1 1 
ATOM   3065  O OE2 . GLU A 1 361 ? 20.292  18.535  16.375  1.00 56.70  ? 361 GLU A OE2 1 
ATOM   3066  N N   . GLU A 1 362 ? 20.471  13.251  18.612  1.00 18.48  ? 362 GLU A N   1 
ATOM   3067  C CA  . GLU A 1 362 ? 20.716  12.025  19.376  1.00 18.37  ? 362 GLU A CA  1 
ATOM   3068  C C   . GLU A 1 362 ? 20.048  10.812  18.727  1.00 16.91  ? 362 GLU A C   1 
ATOM   3069  O O   . GLU A 1 362 ? 19.545  9.921   19.413  1.00 25.92  ? 362 GLU A O   1 
ATOM   3070  C CB  . GLU A 1 362 ? 20.263  12.183  20.829  1.00 18.80  ? 362 GLU A CB  1 
ATOM   3071  C CG  . GLU A 1 362 ? 21.284  11.743  21.866  1.00 38.66  ? 362 GLU A CG  1 
ATOM   3072  C CD  . GLU A 1 362 ? 20.642  11.374  23.191  1.00 57.68  ? 362 GLU A CD  1 
ATOM   3073  O OE1 . GLU A 1 362 ? 19.819  12.168  23.692  1.00 47.13  ? 362 GLU A OE1 1 
ATOM   3074  O OE2 . GLU A 1 362 ? 20.962  10.295  23.733  1.00 50.62  ? 362 GLU A OE2 1 
ATOM   3075  N N   . ASN A 1 363 ? 20.038  10.785  17.392  1.00 16.44  ? 363 ASN A N   1 
ATOM   3076  C CA  . ASN A 1 363 ? 19.495  9.667   16.616  1.00 15.99  ? 363 ASN A CA  1 
ATOM   3077  C C   . ASN A 1 363 ? 18.013  9.430   16.910  1.00 14.04  ? 363 ASN A C   1 
ATOM   3078  O O   . ASN A 1 363 ? 17.529  8.296   16.874  1.00 13.37  ? 363 ASN A O   1 
ATOM   3079  C CB  . ASN A 1 363 ? 20.311  8.388   16.849  1.00 15.87  ? 363 ASN A CB  1 
ATOM   3080  C CG  . ASN A 1 363 ? 19.990  7.293   15.847  1.00 16.48  ? 363 ASN A CG  1 
ATOM   3081  O OD1 . ASN A 1 363 ? 20.055  7.502   14.634  1.00 19.97  ? 363 ASN A OD1 1 
ATOM   3082  N ND2 . ASN A 1 363 ? 19.639  6.117   16.353  1.00 24.14  ? 363 ASN A ND2 1 
ATOM   3083  N N   . GLY A 1 364 ? 17.274  10.495  17.208  1.00 14.75  ? 364 GLY A N   1 
ATOM   3084  C CA  . GLY A 1 364 ? 15.844  10.392  17.420  1.00 13.51  ? 364 GLY A CA  1 
ATOM   3085  C C   . GLY A 1 364 ? 15.430  9.846   18.766  1.00 15.71  ? 364 GLY A C   1 
ATOM   3086  O O   . GLY A 1 364 ? 14.227  9.675   18.999  1.00 20.24  ? 364 GLY A O   1 
ATOM   3087  N N   . ILE A 1 365 ? 16.383  9.564   19.655  1.00 13.83  ? 365 ILE A N   1 
ATOM   3088  C CA  . ILE A 1 365 ? 16.037  9.022   20.969  1.00 14.13  ? 365 ILE A CA  1 
ATOM   3089  C C   . ILE A 1 365 ? 15.198  9.997   21.793  1.00 16.43  ? 365 ILE A C   1 
ATOM   3090  O O   . ILE A 1 365 ? 14.196  9.564   22.382  1.00 25.72  ? 365 ILE A O   1 
ATOM   3091  C CB  . ILE A 1 365 ? 17.305  8.550   21.693  1.00 15.40  ? 365 ILE A CB  1 
ATOM   3092  C CG1 . ILE A 1 365 ? 18.042  7.526   20.827  1.00 15.30  ? 365 ILE A CG1 1 
ATOM   3093  C CG2 . ILE A 1 365 ? 16.966  7.962   23.050  1.00 15.97  ? 365 ILE A CG2 1 
ATOM   3094  C CD1 . ILE A 1 365 ? 19.389  7.107   21.373  1.00 16.77  ? 365 ILE A CD1 1 
ATOM   3095  N N   . PRO A 1 366 ? 15.540  11.290  21.897  1.00 15.16  ? 366 PRO A N   1 
ATOM   3096  C CA  . PRO A 1 366 ? 14.639  12.201  22.629  1.00 15.54  ? 366 PRO A CA  1 
ATOM   3097  C C   . PRO A 1 366 ? 13.242  12.285  22.038  1.00 14.43  ? 366 PRO A C   1 
ATOM   3098  O O   . PRO A 1 366 ? 12.260  12.268  22.789  1.00 16.60  ? 366 PRO A O   1 
ATOM   3099  C CB  . PRO A 1 366 ? 15.369  13.548  22.554  1.00 16.71  ? 366 PRO A CB  1 
ATOM   3100  C CG  . PRO A 1 366 ? 16.789  13.196  22.355  1.00 17.31  ? 366 PRO A CG  1 
ATOM   3101  C CD  . PRO A 1 366 ? 16.782  11.972  21.498  1.00 16.08  ? 366 PRO A CD  1 
ATOM   3102  N N   . PHE A 1 367 ? 13.118  12.367  20.712  1.00 13.61  ? 367 PHE A N   1 
ATOM   3103  C CA  . PHE A 1 367 ? 11.795  12.460  20.101  1.00 12.76  ? 367 PHE A CA  1 
ATOM   3104  C C   . PHE A 1 367 ? 10.990  11.189  20.338  1.00 16.59  ? 367 PHE A C   1 
ATOM   3105  O O   . PHE A 1 367 ? 9.823   11.245  20.743  1.00 17.26  ? 367 PHE A O   1 
ATOM   3106  C CB  . PHE A 1 367 ? 11.920  12.736  18.603  1.00 12.30  ? 367 PHE A CB  1 
ATOM   3107  C CG  . PHE A 1 367 ? 10.635  12.546  17.843  1.00 11.45  ? 367 PHE A CG  1 
ATOM   3108  C CD1 . PHE A 1 367 ? 9.631   13.499  17.909  1.00 12.65  ? 367 PHE A CD1 1 
ATOM   3109  C CD2 . PHE A 1 367 ? 10.425  11.412  17.073  1.00 14.06  ? 367 PHE A CD2 1 
ATOM   3110  C CE1 . PHE A 1 367 ? 8.447   13.330  17.218  1.00 12.07  ? 367 PHE A CE1 1 
ATOM   3111  C CE2 . PHE A 1 367 ? 9.240   11.236  16.379  1.00 10.40  ? 367 PHE A CE2 1 
ATOM   3112  C CZ  . PHE A 1 367 ? 8.250   12.198  16.452  1.00 10.96  ? 367 PHE A CZ  1 
ATOM   3113  N N   . LEU A 1 368 ? 11.600  10.029  20.081  1.00 16.90  ? 368 LEU A N   1 
ATOM   3114  C CA  . LEU A 1 368 ? 10.882  8.764   20.208  1.00 13.58  ? 368 LEU A CA  1 
ATOM   3115  C C   . LEU A 1 368 ? 10.470  8.493   21.651  1.00 13.64  ? 368 LEU A C   1 
ATOM   3116  O O   . LEU A 1 368 ? 9.340   8.061   21.907  1.00 11.33  ? 368 LEU A O   1 
ATOM   3117  C CB  . LEU A 1 368 ? 11.742  7.622   19.671  1.00 11.07  ? 368 LEU A CB  1 
ATOM   3118  C CG  . LEU A 1 368 ? 11.738  7.464   18.153  1.00 14.96  ? 368 LEU A CG  1 
ATOM   3119  C CD1 . LEU A 1 368 ? 12.454  6.186   17.750  1.00 16.61  ? 368 LEU A CD1 1 
ATOM   3120  C CD2 . LEU A 1 368 ? 10.312  7.476   17.625  1.00 14.53  ? 368 LEU A CD2 1 
ATOM   3121  N N   . GLU A 1 369 ? 11.372  8.731   22.605  1.00 16.63  ? 369 GLU A N   1 
ATOM   3122  C CA  . GLU A 1 369 ? 11.025  8.531   24.008  1.00 13.52  ? 369 GLU A CA  1 
ATOM   3123  C C   . GLU A 1 369 ? 9.950   9.514   24.458  1.00 14.81  ? 369 GLU A C   1 
ATOM   3124  O O   . GLU A 1 369 ? 9.035   9.146   25.203  1.00 20.12  ? 369 GLU A O   1 
ATOM   3125  C CB  . GLU A 1 369 ? 12.271  8.656   24.883  1.00 16.51  ? 369 GLU A CB  1 
ATOM   3126  C CG  . GLU A 1 369 ? 13.270  7.527   24.700  1.00 14.92  ? 369 GLU A CG  1 
ATOM   3127  C CD  . GLU A 1 369 ? 14.436  7.626   25.660  1.00 24.13  ? 369 GLU A CD  1 
ATOM   3128  O OE1 . GLU A 1 369 ? 14.653  8.722   26.221  1.00 25.30  ? 369 GLU A OE1 1 
ATOM   3129  O OE2 . GLU A 1 369 ? 15.137  6.610   25.855  1.00 31.62  ? 369 GLU A OE2 1 
ATOM   3130  N N   . LYS A 1 370 ? 10.050  10.773  24.026  1.00 13.95  ? 370 LYS A N   1 
ATOM   3131  C CA  . LYS A 1 370 ? 9.019   11.748  24.363  1.00 17.21  ? 370 LYS A CA  1 
ATOM   3132  C C   . LYS A 1 370 ? 7.674   11.355  23.765  1.00 21.66  ? 370 LYS A C   1 
ATOM   3133  O O   . LYS A 1 370 ? 6.638   11.450  24.433  1.00 23.76  ? 370 LYS A O   1 
ATOM   3134  C CB  . LYS A 1 370 ? 9.431   13.139  23.883  1.00 20.31  ? 370 LYS A CB  1 
ATOM   3135  C CG  . LYS A 1 370 ? 8.945   14.279  24.766  1.00 22.46  ? 370 LYS A CG  1 
ATOM   3136  C CD  . LYS A 1 370 ? 9.601   14.243  26.139  1.00 33.87  ? 370 LYS A CD  1 
ATOM   3137  C CE  . LYS A 1 370 ? 8.579   14.435  27.250  1.00 33.41  ? 370 LYS A CE  1 
ATOM   3138  N NZ  . LYS A 1 370 ? 9.185   14.263  28.600  1.00 26.83  ? 370 LYS A NZ  1 
ATOM   3139  N N   . LEU A 1 371 ? 7.671   10.908  22.507  1.00 15.78  ? 371 LEU A N   1 
ATOM   3140  C CA  . LEU A 1 371 ? 6.418   10.544  21.851  1.00 13.82  ? 371 LEU A CA  1 
ATOM   3141  C C   . LEU A 1 371 ? 5.780   9.326   22.507  1.00 18.36  ? 371 LEU A C   1 
ATOM   3142  O O   . LEU A 1 371 ? 4.579   9.325   22.803  1.00 20.65  ? 371 LEU A O   1 
ATOM   3143  C CB  . LEU A 1 371 ? 6.660   10.292  20.362  1.00 12.18  ? 371 LEU A CB  1 
ATOM   3144  C CG  . LEU A 1 371 ? 5.539   9.605   19.578  1.00 9.96   ? 371 LEU A CG  1 
ATOM   3145  C CD1 . LEU A 1 371 ? 4.307   10.493  19.491  1.00 12.02  ? 371 LEU A CD1 1 
ATOM   3146  C CD2 . LEU A 1 371 ? 6.018   9.216   18.189  1.00 10.57  ? 371 LEU A CD2 1 
ATOM   3147  N N   . TYR A 1 372 ? 6.571   8.279   22.752  1.00 17.72  ? 372 TYR A N   1 
ATOM   3148  C CA  . TYR A 1 372 ? 6.012   7.048   23.302  1.00 18.44  ? 372 TYR A CA  1 
ATOM   3149  C C   . TYR A 1 372 ? 5.521   7.252   24.729  1.00 21.22  ? 372 TYR A C   1 
ATOM   3150  O O   . TYR A 1 372 ? 4.480   6.708   25.117  1.00 30.40  ? 372 TYR A O   1 
ATOM   3151  C CB  . TYR A 1 372 ? 7.047   5.924   23.236  1.00 17.53  ? 372 TYR A CB  1 
ATOM   3152  C CG  . TYR A 1 372 ? 7.405   5.491   21.828  1.00 10.66  ? 372 TYR A CG  1 
ATOM   3153  C CD1 . TYR A 1 372 ? 6.747   6.017   20.723  1.00 17.34  ? 372 TYR A CD1 1 
ATOM   3154  C CD2 . TYR A 1 372 ? 8.400   4.549   21.608  1.00 12.25  ? 372 TYR A CD2 1 
ATOM   3155  C CE1 . TYR A 1 372 ? 7.073   5.621   19.440  1.00 18.37  ? 372 TYR A CE1 1 
ATOM   3156  C CE2 . TYR A 1 372 ? 8.733   4.147   20.330  1.00 11.25  ? 372 TYR A CE2 1 
ATOM   3157  C CZ  . TYR A 1 372 ? 8.067   4.685   19.250  1.00 10.43  ? 372 TYR A CZ  1 
ATOM   3158  O OH  . TYR A 1 372 ? 8.398   4.283   17.978  1.00 11.92  ? 372 TYR A OH  1 
ATOM   3159  N N   . SER A 1 373 ? 6.257   8.026   25.528  1.00 17.16  ? 373 SER A N   1 
ATOM   3160  C CA  . SER A 1 373 ? 5.779   8.359   26.865  1.00 22.59  ? 373 SER A CA  1 
ATOM   3161  C C   . SER A 1 373 ? 4.523   9.219   26.798  1.00 28.18  ? 373 SER A C   1 
ATOM   3162  O O   . SER A 1 373 ? 3.617   9.074   27.626  1.00 35.87  ? 373 SER A O   1 
ATOM   3163  C CB  . SER A 1 373 ? 6.879   9.062   27.661  1.00 17.61  ? 373 SER A CB  1 
ATOM   3164  O OG  . SER A 1 373 ? 7.486   10.099  26.908  1.00 23.96  ? 373 SER A OG  1 
ATOM   3165  N N   . THR A 1 374 ? 4.449   10.120  25.815  1.00 28.62  ? 374 THR A N   1 
ATOM   3166  C CA  . THR A 1 374 ? 3.267   10.965  25.665  1.00 28.01  ? 374 THR A CA  1 
ATOM   3167  C C   . THR A 1 374 ? 2.042   10.141  25.288  1.00 28.37  ? 374 THR A C   1 
ATOM   3168  O O   . THR A 1 374 ? 0.965   10.309  25.873  1.00 27.84  ? 374 THR A O   1 
ATOM   3169  C CB  . THR A 1 374 ? 3.524   12.048  24.615  1.00 25.58  ? 374 THR A CB  1 
ATOM   3170  O OG1 . THR A 1 374 ? 4.599   12.890  25.048  1.00 28.78  ? 374 THR A OG1 1 
ATOM   3171  C CG2 . THR A 1 374 ? 2.278   12.895  24.408  1.00 26.81  ? 374 THR A CG2 1 
ATOM   3172  N N   . LEU A 1 375 ? 2.188   9.243   24.309  1.00 28.28  ? 375 LEU A N   1 
ATOM   3173  C CA  . LEU A 1 375 ? 1.065   8.404   23.896  1.00 27.64  ? 375 LEU A CA  1 
ATOM   3174  C C   . LEU A 1 375 ? 0.591   7.526   25.044  1.00 25.69  ? 375 LEU A C   1 
ATOM   3175  O O   . LEU A 1 375 ? -0.615  7.305   25.214  1.00 27.45  ? 375 LEU A O   1 
ATOM   3176  C CB  . LEU A 1 375 ? 1.465   7.544   22.698  1.00 22.97  ? 375 LEU A CB  1 
ATOM   3177  C CG  . LEU A 1 375 ? 1.692   8.277   21.377  1.00 18.17  ? 375 LEU A CG  1 
ATOM   3178  C CD1 . LEU A 1 375 ? 2.046   7.287   20.282  1.00 23.24  ? 375 LEU A CD1 1 
ATOM   3179  C CD2 . LEU A 1 375 ? 0.464   9.088   20.993  1.00 11.43  ? 375 LEU A CD2 1 
ATOM   3180  N N   . GLU A 1 376 ? 1.532   7.011   25.836  1.00 22.86  ? 376 GLU A N   1 
ATOM   3181  C CA  . GLU A 1 376 ? 1.184   6.250   27.030  1.00 28.17  ? 376 GLU A CA  1 
ATOM   3182  C C   . GLU A 1 376 ? 0.320   7.074   27.977  1.00 33.67  ? 376 GLU A C   1 
ATOM   3183  O O   . GLU A 1 376 ? -0.606  6.548   28.605  1.00 32.22  ? 376 GLU A O   1 
ATOM   3184  C CB  . GLU A 1 376 ? 2.464   5.798   27.731  1.00 28.38  ? 376 GLU A CB  1 
ATOM   3185  C CG  . GLU A 1 376 ? 2.449   4.391   28.283  1.00 28.17  ? 376 GLU A CG  1 
ATOM   3186  C CD  . GLU A 1 376 ? 3.645   4.131   29.177  1.00 41.09  ? 376 GLU A CD  1 
ATOM   3187  O OE1 . GLU A 1 376 ? 3.942   4.991   30.033  1.00 66.37  ? 376 GLU A OE1 1 
ATOM   3188  O OE2 . GLU A 1 376 ? 4.297   3.077   29.021  1.00 42.63  ? 376 GLU A OE2 1 
ATOM   3189  N N   . LYS A 1 377 ? 0.609   8.372   28.090  1.00 33.74  ? 377 LYS A N   1 
ATOM   3190  C CA  . LYS A 1 377 ? -0.127  9.229   29.011  1.00 28.44  ? 377 LYS A CA  1 
ATOM   3191  C C   . LYS A 1 377 ? -1.522  9.572   28.501  1.00 26.86  ? 377 LYS A C   1 
ATOM   3192  O O   . LYS A 1 377 ? -2.434  9.783   29.310  1.00 28.43  ? 377 LYS A O   1 
ATOM   3193  C CB  . LYS A 1 377 ? 0.648   10.523  29.273  1.00 37.46  ? 377 LYS A CB  1 
ATOM   3194  C CG  . LYS A 1 377 ? 1.989   10.359  29.981  1.00 31.44  ? 377 LYS A CG  1 
ATOM   3195  C CD  . LYS A 1 377 ? 2.027   9.153   30.906  1.00 43.29  ? 377 LYS A CD  1 
ATOM   3196  C CE  . LYS A 1 377 ? 3.408   8.516   30.906  1.00 45.53  ? 377 LYS A CE  1 
ATOM   3197  N NZ  . LYS A 1 377 ? 3.368   7.086   31.314  1.00 49.19  ? 377 LYS A NZ  1 
ATOM   3198  N N   . GLU A 1 378 ? -1.714  9.633   27.184  1.00 30.05  ? 378 GLU A N   1 
ATOM   3199  C CA  . GLU A 1 378 ? -2.976  10.093  26.613  1.00 29.45  ? 378 GLU A CA  1 
ATOM   3200  C C   . GLU A 1 378 ? -4.017  8.983   26.707  1.00 31.01  ? 378 GLU A C   1 
ATOM   3201  O O   . GLU A 1 378 ? -3.897  7.946   26.046  1.00 31.94  ? 378 GLU A O   1 
ATOM   3202  C CB  . GLU A 1 378 ? -2.777  10.552  25.172  1.00 20.55  ? 378 GLU A CB  1 
ATOM   3203  C CG  . GLU A 1 378 ? -1.934  11.813  25.047  1.00 27.66  ? 378 GLU A CG  1 
ATOM   3204  C CD  . GLU A 1 378 ? -2.420  12.931  25.951  1.00 37.45  ? 378 GLU A CD  1 
ATOM   3205  O OE1 . GLU A 1 378 ? -3.542  13.432  25.726  1.00 38.63  ? 378 GLU A OE1 1 
ATOM   3206  O OE2 . GLU A 1 378 ? -1.682  13.307  26.887  1.00 38.32  ? 378 GLU A OE2 1 
ATOM   3207  N N   . GLU A 1 379 ? -5.046  9.213   27.526  1.00 23.06  ? 379 GLU A N   1 
ATOM   3208  C CA  . GLU A 1 379 ? -6.085  8.212   27.743  1.00 21.37  ? 379 GLU A CA  1 
ATOM   3209  C C   . GLU A 1 379 ? -6.851  7.913   26.461  1.00 32.03  ? 379 GLU A C   1 
ATOM   3210  O O   . GLU A 1 379 ? -7.226  6.763   26.205  1.00 38.71  ? 379 GLU A O   1 
ATOM   3211  C CB  . GLU A 1 379 ? -7.041  8.702   28.832  1.00 47.10  ? 379 GLU A CB  1 
ATOM   3212  C CG  . GLU A 1 379 ? -7.605  10.094  28.552  1.00 43.54  ? 379 GLU A CG  1 
ATOM   3213  C CD  . GLU A 1 379 ? -8.007  10.843  29.806  1.00 59.17  ? 379 GLU A CD  1 
ATOM   3214  O OE1 . GLU A 1 379 ? -8.030  10.228  30.892  1.00 62.22  ? 379 GLU A OE1 1 
ATOM   3215  O OE2 . GLU A 1 379 ? -8.296  12.055  29.702  1.00 53.41  ? 379 GLU A OE2 1 
ATOM   3216  N N   . TRP A 1 380 ? -7.095  8.938   25.647  1.00 31.77  ? 380 TRP A N   1 
ATOM   3217  C CA  . TRP A 1 380 ? -7.972  8.846   24.488  1.00 20.04  ? 380 TRP A CA  1 
ATOM   3218  C C   . TRP A 1 380 ? -7.293  8.253   23.260  1.00 25.75  ? 380 TRP A C   1 
ATOM   3219  O O   . TRP A 1 380 ? -7.967  8.037   22.248  1.00 32.72  ? 380 TRP A O   1 
ATOM   3220  C CB  . TRP A 1 380 ? -8.516  10.236  24.158  1.00 19.98  ? 380 TRP A CB  1 
ATOM   3221  C CG  . TRP A 1 380 ? -7.436  11.197  23.792  1.00 24.53  ? 380 TRP A CG  1 
ATOM   3222  C CD1 . TRP A 1 380 ? -6.642  11.906  24.646  1.00 19.62  ? 380 TRP A CD1 1 
ATOM   3223  C CD2 . TRP A 1 380 ? -7.026  11.559  22.469  1.00 30.30  ? 380 TRP A CD2 1 
ATOM   3224  N NE1 . TRP A 1 380 ? -5.761  12.686  23.937  1.00 24.92  ? 380 TRP A NE1 1 
ATOM   3225  C CE2 . TRP A 1 380 ? -5.978  12.492  22.597  1.00 28.45  ? 380 TRP A CE2 1 
ATOM   3226  C CE3 . TRP A 1 380 ? -7.445  11.186  21.188  1.00 35.94  ? 380 TRP A CE3 1 
ATOM   3227  C CZ2 . TRP A 1 380 ? -5.343  13.058  21.492  1.00 31.75  ? 380 TRP A CZ2 1 
ATOM   3228  C CZ3 . TRP A 1 380 ? -6.812  11.747  20.092  1.00 38.00  ? 380 TRP A CZ3 1 
ATOM   3229  C CH2 . TRP A 1 380 ? -5.772  12.672  20.251  1.00 31.88  ? 380 TRP A CH2 1 
ATOM   3230  N N   . ILE A 1 381 ? -5.990  7.992   23.314  1.00 28.90  ? 381 ILE A N   1 
ATOM   3231  C CA  . ILE A 1 381 ? -5.250  7.401   22.205  1.00 15.22  ? 381 ILE A CA  1 
ATOM   3232  C C   . ILE A 1 381 ? -4.936  5.958   22.571  1.00 14.83  ? 381 ILE A C   1 
ATOM   3233  O O   . ILE A 1 381 ? -4.283  5.695   23.589  1.00 24.20  ? 381 ILE A O   1 
ATOM   3234  C CB  . ILE A 1 381 ? -3.961  8.180   21.902  1.00 16.88  ? 381 ILE A CB  1 
ATOM   3235  C CG1 . ILE A 1 381 ? -4.286  9.560   21.329  1.00 17.81  ? 381 ILE A CG1 1 
ATOM   3236  C CG2 . ILE A 1 381 ? -3.082  7.404   20.936  1.00 13.16  ? 381 ILE A CG2 1 
ATOM   3237  C CD1 . ILE A 1 381 ? -3.069  10.442  21.166  1.00 22.24  ? 381 ILE A CD1 1 
ATOM   3238  N N   . GLU A 1 382 ? -5.399  5.025   21.747  1.00 14.28  ? 382 GLU A N   1 
ATOM   3239  C CA  . GLU A 1 382 ? -5.148  3.602   21.946  1.00 17.07  ? 382 GLU A CA  1 
ATOM   3240  C C   . GLU A 1 382 ? -4.303  3.091   20.787  1.00 22.06  ? 382 GLU A C   1 
ATOM   3241  O O   . GLU A 1 382 ? -4.799  2.947   19.664  1.00 22.28  ? 382 GLU A O   1 
ATOM   3242  C CB  . GLU A 1 382 ? -6.456  2.821   22.058  1.00 20.68  ? 382 GLU A CB  1 
ATOM   3243  C CG  . GLU A 1 382 ? -6.308  1.488   22.773  1.00 35.74  ? 382 GLU A CG  1 
ATOM   3244  C CD  . GLU A 1 382 ? -7.608  0.709   22.837  1.00 55.94  ? 382 GLU A CD  1 
ATOM   3245  O OE1 . GLU A 1 382 ? -7.589  -0.441  23.328  1.00 60.01  ? 382 GLU A OE1 1 
ATOM   3246  O OE2 . GLU A 1 382 ? -8.645  1.243   22.398  1.00 61.07  ? 382 GLU A OE2 1 
ATOM   3247  N N   . THR A 1 383 ? -3.028  2.827   21.057  1.00 18.16  ? 383 THR A N   1 
ATOM   3248  C CA  . THR A 1 383 ? -2.166  2.228   20.051  1.00 12.60  ? 383 THR A CA  1 
ATOM   3249  C C   . THR A 1 383 ? -2.523  0.760   19.871  1.00 16.72  ? 383 THR A C   1 
ATOM   3250  O O   . THR A 1 383 ? -2.819  0.052   20.838  1.00 22.75  ? 383 THR A O   1 
ATOM   3251  C CB  . THR A 1 383 ? -0.697  2.374   20.444  1.00 12.36  ? 383 THR A CB  1 
ATOM   3252  O OG1 . THR A 1 383 ? -0.543  2.086   21.839  1.00 13.31  ? 383 THR A OG1 1 
ATOM   3253  C CG2 . THR A 1 383 ? -0.215  3.791   20.164  1.00 10.59  ? 383 THR A CG2 1 
ATOM   3254  N N   . LEU A 1 384 ? -2.499  0.303   18.622  1.00 11.67  ? 384 LEU A N   1 
ATOM   3255  C CA  . LEU A 1 384 ? -2.929  -1.041  18.276  1.00 12.66  ? 384 LEU A CA  1 
ATOM   3256  C C   . LEU A 1 384 ? -1.833  -1.760  17.508  1.00 12.80  ? 384 LEU A C   1 
ATOM   3257  O O   . LEU A 1 384 ? -0.957  -1.140  16.898  1.00 11.96  ? 384 LEU A O   1 
ATOM   3258  C CB  . LEU A 1 384 ? -4.202  -1.037  17.419  1.00 12.72  ? 384 LEU A CB  1 
ATOM   3259  C CG  . LEU A 1 384 ? -5.518  -0.490  17.963  1.00 13.51  ? 384 LEU A CG  1 
ATOM   3260  C CD1 . LEU A 1 384 ? -6.569  -0.532  16.866  1.00 13.90  ? 384 LEU A CD1 1 
ATOM   3261  C CD2 . LEU A 1 384 ? -5.979  -1.281  19.174  1.00 14.74  ? 384 LEU A CD2 1 
ATOM   3262  N N   . THR A 1 385 ? -1.895  -3.083  17.552  1.00 13.46  ? 385 THR A N   1 
ATOM   3263  C CA  . THR A 1 385 ? -1.141  -3.902  16.622  1.00 12.74  ? 385 THR A CA  1 
ATOM   3264  C C   . THR A 1 385 ? -1.951  -4.081  15.341  1.00 12.89  ? 385 THR A C   1 
ATOM   3265  O O   . THR A 1 385 ? -3.136  -3.749  15.276  1.00 21.17  ? 385 THR A O   1 
ATOM   3266  C CB  . THR A 1 385 ? -0.805  -5.261  17.237  1.00 13.90  ? 385 THR A CB  1 
ATOM   3267  O OG1 . THR A 1 385 ? -1.907  -6.155  17.056  1.00 16.88  ? 385 THR A OG1 1 
ATOM   3268  C CG2 . THR A 1 385 ? -0.530  -5.117  18.720  1.00 15.46  ? 385 THR A CG2 1 
ATOM   3269  N N   . LEU A 1 386 ? -1.294  -4.607  14.305  1.00 12.87  ? 386 LEU A N   1 
ATOM   3270  C CA  . LEU A 1 386 ? -2.004  -4.884  13.061  1.00 13.31  ? 386 LEU A CA  1 
ATOM   3271  C C   . LEU A 1 386 ? -3.120  -5.894  13.286  1.00 18.31  ? 386 LEU A C   1 
ATOM   3272  O O   . LEU A 1 386 ? -4.220  -5.748  12.740  1.00 22.34  ? 386 LEU A O   1 
ATOM   3273  C CB  . LEU A 1 386 ? -1.032  -5.386  11.993  1.00 13.38  ? 386 LEU A CB  1 
ATOM   3274  C CG  . LEU A 1 386 ? 0.139   -4.470  11.640  1.00 12.28  ? 386 LEU A CG  1 
ATOM   3275  C CD1 . LEU A 1 386 ? 1.019   -5.113  10.580  1.00 12.74  ? 386 LEU A CD1 1 
ATOM   3276  C CD2 . LEU A 1 386 ? -0.369  -3.118  11.174  1.00 15.39  ? 386 LEU A CD2 1 
ATOM   3277  N N   . GLU A 1 387 ? -2.857  -6.924  14.093  1.00 25.44  ? 387 GLU A N   1 
ATOM   3278  C CA  . GLU A 1 387 ? -3.894  -7.902  14.408  1.00 23.80  ? 387 GLU A CA  1 
ATOM   3279  C C   . GLU A 1 387 ? -5.026  -7.275  15.212  1.00 17.29  ? 387 GLU A C   1 
ATOM   3280  O O   . GLU A 1 387 ? -6.201  -7.582  14.983  1.00 18.34  ? 387 GLU A O   1 
ATOM   3281  C CB  . GLU A 1 387 ? -3.290  -9.083  15.166  1.00 20.55  ? 387 GLU A CB  1 
ATOM   3282  C CG  . GLU A 1 387 ? -4.328  -10.012 15.767  1.00 33.63  ? 387 GLU A CG  1 
ATOM   3283  C CD  . GLU A 1 387 ? -3.874  -11.452 15.792  1.00 56.46  ? 387 GLU A CD  1 
ATOM   3284  O OE1 . GLU A 1 387 ? -2.646  -11.689 15.772  1.00 40.86  ? 387 GLU A OE1 1 
ATOM   3285  O OE2 . GLU A 1 387 ? -4.747  -12.346 15.822  1.00 57.88  ? 387 GLU A OE2 1 
ATOM   3286  N N   . GLU A 1 388 ? -4.693  -6.403  16.167  1.00 18.39  ? 388 GLU A N   1 
ATOM   3287  C CA  . GLU A 1 388 ? -5.733  -5.729  16.938  1.00 19.13  ? 388 GLU A CA  1 
ATOM   3288  C C   . GLU A 1 388 ? -6.608  -4.869  16.035  1.00 16.60  ? 388 GLU A C   1 
ATOM   3289  O O   . GLU A 1 388 ? -7.840  -4.906  16.128  1.00 26.32  ? 388 GLU A O   1 
ATOM   3290  C CB  . GLU A 1 388 ? -5.104  -4.891  18.053  1.00 17.30  ? 388 GLU A CB  1 
ATOM   3291  C CG  . GLU A 1 388 ? -5.259  -5.495  19.443  1.00 28.94  ? 388 GLU A CG  1 
ATOM   3292  C CD  . GLU A 1 388 ? -4.164  -5.059  20.397  1.00 36.64  ? 388 GLU A CD  1 
ATOM   3293  O OE1 . GLU A 1 388 ? -3.873  -3.845  20.462  1.00 41.40  ? 388 GLU A OE1 1 
ATOM   3294  O OE2 . GLU A 1 388 ? -3.597  -5.929  21.090  1.00 29.05  ? 388 GLU A OE2 1 
ATOM   3295  N N   . ALA A 1 389 ? -5.984  -4.098  15.139  1.00 15.24  ? 389 ALA A N   1 
ATOM   3296  C CA  . ALA A 1 389 ? -6.749  -3.303  14.185  1.00 15.01  ? 389 ALA A CA  1 
ATOM   3297  C C   . ALA A 1 389 ? -7.601  -4.183  13.282  1.00 18.45  ? 389 ALA A C   1 
ATOM   3298  O O   . ALA A 1 389 ? -8.666  -3.754  12.821  1.00 24.47  ? 389 ALA A O   1 
ATOM   3299  C CB  . ALA A 1 389 ? -5.811  -2.433  13.349  1.00 13.73  ? 389 ALA A CB  1 
ATOM   3300  N N   . MET A 1 390 ? -7.147  -5.407  13.006  1.00 16.82  ? 390 MET A N   1 
ATOM   3301  C CA  . MET A 1 390 ? -7.947  -6.330  12.210  1.00 18.27  ? 390 MET A CA  1 
ATOM   3302  C C   . MET A 1 390 ? -9.211  -6.750  12.950  1.00 19.72  ? 390 MET A C   1 
ATOM   3303  O O   . MET A 1 390 ? -10.290 -6.822  12.352  1.00 24.97  ? 390 MET A O   1 
ATOM   3304  C CB  . MET A 1 390 ? -7.113  -7.553  11.835  1.00 20.75  ? 390 MET A CB  1 
ATOM   3305  C CG  . MET A 1 390 ? -6.132  -7.290  10.715  1.00 17.97  ? 390 MET A CG  1 
ATOM   3306  S SD  . MET A 1 390 ? -6.971  -7.029  9.145   1.00 26.13  ? 390 MET A SD  1 
ATOM   3307  C CE  . MET A 1 390 ? -7.439  -8.707  8.727   1.00 20.88  ? 390 MET A CE  1 
ATOM   3308  N N   . ARG A 1 391 ? -9.102  -7.023  14.249  1.00 19.97  ? 391 ARG A N   1 
ATOM   3309  C CA  . ARG A 1 391 ? -10.236 -7.488  15.036  1.00 22.56  ? 391 ARG A CA  1 
ATOM   3310  C C   . ARG A 1 391 ? -11.084 -6.355  15.599  1.00 21.49  ? 391 ARG A C   1 
ATOM   3311  O O   . ARG A 1 391 ? -12.163 -6.623  16.137  1.00 23.01  ? 391 ARG A O   1 
ATOM   3312  C CB  . ARG A 1 391 ? -9.757  -8.365  16.201  1.00 26.34  ? 391 ARG A CB  1 
ATOM   3313  C CG  . ARG A 1 391 ? -8.856  -9.526  15.809  1.00 27.67  ? 391 ARG A CG  1 
ATOM   3314  C CD  . ARG A 1 391 ? -9.513  -10.440 14.794  1.00 25.33  ? 391 ARG A CD  1 
ATOM   3315  N NE  . ARG A 1 391 ? -8.537  -10.962 13.847  1.00 26.86  ? 391 ARG A NE  1 
ATOM   3316  C CZ  . ARG A 1 391 ? -8.700  -10.976 12.532  1.00 41.87  ? 391 ARG A CZ  1 
ATOM   3317  N NH1 . ARG A 1 391 ? -9.810  -10.524 11.969  1.00 35.88  ? 391 ARG A NH1 1 
ATOM   3318  N NH2 . ARG A 1 391 ? -7.724  -11.454 11.762  1.00 53.77  ? 391 ARG A NH2 1 
ATOM   3319  N N   . LYS A 1 392 ? -10.637 -5.108  15.483  1.00 19.95  ? 392 LYS A N   1 
ATOM   3320  C CA  . LYS A 1 392 ? -11.282 -4.006  16.190  1.00 28.09  ? 392 LYS A CA  1 
ATOM   3321  C C   . LYS A 1 392 ? -12.651 -3.708  15.589  1.00 34.75  ? 392 LYS A C   1 
ATOM   3322  O O   . LYS A 1 392 ? -12.755 -3.329  14.417  1.00 45.22  ? 392 LYS A O   1 
ATOM   3323  C CB  . LYS A 1 392 ? -10.394 -2.765  16.145  1.00 23.24  ? 392 LYS A CB  1 
ATOM   3324  C CG  . LYS A 1 392 ? -11.051 -1.517  16.706  1.00 23.76  ? 392 LYS A CG  1 
ATOM   3325  C CD  . LYS A 1 392 ? -11.374 -1.675  18.180  1.00 26.52  ? 392 LYS A CD  1 
ATOM   3326  C CE  . LYS A 1 392 ? -10.109 -1.804  19.007  1.00 23.27  ? 392 LYS A CE  1 
ATOM   3327  N NZ  . LYS A 1 392 ? -10.417 -1.907  20.460  1.00 27.97  ? 392 LYS A NZ  1 
ATOM   3328  N N   . GLU A 1 393 ? -13.699 -3.869  16.399  1.00 32.41  ? 393 GLU A N   1 
ATOM   3329  C CA  . GLU A 1 393 ? -15.067 -3.629  15.961  1.00 31.19  ? 393 GLU A CA  1 
ATOM   3330  C C   . GLU A 1 393 ? -15.520 -2.187  16.163  1.00 36.85  ? 393 GLU A C   1 
ATOM   3331  O O   . GLU A 1 393 ? -16.606 -1.827  15.698  1.00 36.33  ? 393 GLU A O   1 
ATOM   3332  C CB  . GLU A 1 393 ? -16.029 -4.571  16.690  1.00 35.26  ? 393 GLU A CB  1 
ATOM   3333  C CG  . GLU A 1 393 ? -15.595 -6.029  16.684  1.00 45.13  ? 393 GLU A CG  1 
ATOM   3334  C CD  . GLU A 1 393 ? -15.129 -6.506  18.048  1.00 52.43  ? 393 GLU A CD  1 
ATOM   3335  O OE1 . GLU A 1 393 ? -15.786 -6.164  19.053  1.00 75.62  ? 393 GLU A OE1 1 
ATOM   3336  O OE2 . GLU A 1 393 ? -14.109 -7.223  18.116  1.00 50.86  ? 393 GLU A OE2 1 
ATOM   3337  N N   . ASP A 1 394 ? -14.727 -1.358  16.846  1.00 41.15  ? 394 ASP A N   1 
ATOM   3338  C CA  . ASP A 1 394 ? -15.042 0.061   16.962  1.00 31.38  ? 394 ASP A CA  1 
ATOM   3339  C C   . ASP A 1 394 ? -14.758 0.831   15.681  1.00 25.78  ? 394 ASP A C   1 
ATOM   3340  O O   . ASP A 1 394 ? -15.173 1.989   15.569  1.00 24.45  ? 394 ASP A O   1 
ATOM   3341  C CB  . ASP A 1 394 ? -14.247 0.692   18.110  1.00 33.04  ? 394 ASP A CB  1 
ATOM   3342  C CG  . ASP A 1 394 ? -14.495 0.011   19.440  1.00 47.88  ? 394 ASP A CG  1 
ATOM   3343  O OD1 . ASP A 1 394 ? -14.440 -1.236  19.495  1.00 51.75  ? 394 ASP A OD1 1 
ATOM   3344  O OD2 . ASP A 1 394 ? -14.739 0.728   20.435  1.00 55.23  ? 394 ASP A OD2 1 
ATOM   3345  N N   . VAL A 1 395 ? -14.066 0.221   14.727  1.00 28.05  ? 395 VAL A N   1 
ATOM   3346  C CA  . VAL A 1 395 ? -13.629 0.895   13.511  1.00 26.73  ? 395 VAL A CA  1 
ATOM   3347  C C   . VAL A 1 395 ? -14.662 0.668   12.416  1.00 25.77  ? 395 VAL A C   1 
ATOM   3348  O O   . VAL A 1 395 ? -15.123 -0.461  12.204  1.00 22.18  ? 395 VAL A O   1 
ATOM   3349  C CB  . VAL A 1 395 ? -12.239 0.394   13.084  1.00 26.63  ? 395 VAL A CB  1 
ATOM   3350  C CG1 . VAL A 1 395 ? -11.893 0.881   11.691  1.00 21.19  ? 395 VAL A CG1 1 
ATOM   3351  C CG2 . VAL A 1 395 ? -11.192 0.864   14.082  1.00 23.65  ? 395 VAL A CG2 1 
ATOM   3352  N N   . LYS A 1 396 ? -15.041 1.746   11.733  1.00 21.49  ? 396 LYS A N   1 
ATOM   3353  C CA  . LYS A 1 396 ? -16.020 1.668   10.659  1.00 22.99  ? 396 LYS A CA  1 
ATOM   3354  C C   . LYS A 1 396 ? -15.381 1.078   9.407   1.00 22.53  ? 396 LYS A C   1 
ATOM   3355  O O   . LYS A 1 396 ? -14.278 1.474   9.017   1.00 21.12  ? 396 LYS A O   1 
ATOM   3356  C CB  . LYS A 1 396 ? -16.592 3.054   10.364  1.00 23.69  ? 396 LYS A CB  1 
ATOM   3357  C CG  . LYS A 1 396 ? -18.019 3.275   10.855  1.00 37.16  ? 396 LYS A CG  1 
ATOM   3358  C CD  . LYS A 1 396 ? -18.175 3.008   12.349  1.00 38.51  ? 396 LYS A CD  1 
ATOM   3359  C CE  . LYS A 1 396 ? -19.372 3.769   12.914  1.00 41.80  ? 396 LYS A CE  1 
ATOM   3360  N NZ  . LYS A 1 396 ? -19.859 3.210   14.208  1.00 40.84  ? 396 LYS A NZ  1 
ATOM   3361  N N   . THR A 1 397 ? -16.075 0.134   8.778   1.00 18.14  ? 397 THR A N   1 
ATOM   3362  C CA  . THR A 1 397 ? -15.577 -0.562  7.599   1.00 14.84  ? 397 THR A CA  1 
ATOM   3363  C C   . THR A 1 397 ? -16.406 -0.192  6.376   1.00 16.73  ? 397 THR A C   1 
ATOM   3364  O O   . THR A 1 397 ? -17.626 -0.024  6.468   1.00 25.43  ? 397 THR A O   1 
ATOM   3365  C CB  . THR A 1 397 ? -15.601 -2.082  7.797   1.00 17.11  ? 397 THR A CB  1 
ATOM   3366  O OG1 . THR A 1 397 ? -15.175 -2.403  9.126   1.00 18.79  ? 397 THR A OG1 1 
ATOM   3367  C CG2 . THR A 1 397 ? -14.685 -2.768  6.792   1.00 15.93  ? 397 THR A CG2 1 
ATOM   3368  N N   . GLU A 1 398 ? -15.740 -0.065  5.230   1.00 15.20  ? 398 GLU A N   1 
ATOM   3369  C CA  . GLU A 1 398 ? -16.420 0.212   3.974   1.00 16.84  ? 398 GLU A CA  1 
ATOM   3370  C C   . GLU A 1 398 ? -15.850 -0.668  2.871   1.00 15.28  ? 398 GLU A C   1 
ATOM   3371  O O   . GLU A 1 398 ? -14.693 -1.090  2.922   1.00 15.83  ? 398 GLU A O   1 
ATOM   3372  C CB  . GLU A 1 398 ? -16.313 1.690   3.580   1.00 21.11  ? 398 GLU A CB  1 
ATOM   3373  C CG  . GLU A 1 398 ? -17.457 2.529   4.118   1.00 32.93  ? 398 GLU A CG  1 
ATOM   3374  C CD  . GLU A 1 398 ? -17.549 3.889   3.465   1.00 38.69  ? 398 GLU A CD  1 
ATOM   3375  O OE1 . GLU A 1 398 ? -16.510 4.391   2.985   1.00 50.25  ? 398 GLU A OE1 1 
ATOM   3376  O OE2 . GLU A 1 398 ? -18.664 4.453   3.426   1.00 33.05  ? 398 GLU A OE2 1 
ATOM   3377  N N   . VAL A 1 399 ? -16.680 -0.944  1.871   1.00 16.01  ? 399 VAL A N   1 
ATOM   3378  C CA  . VAL A 1 399 ? -16.308 -1.785  0.739   1.00 15.95  ? 399 VAL A CA  1 
ATOM   3379  C C   . VAL A 1 399 ? -15.997 -0.898  -0.455  1.00 16.39  ? 399 VAL A C   1 
ATOM   3380  O O   . VAL A 1 399 ? -16.693 0.094   -0.707  1.00 19.24  ? 399 VAL A O   1 
ATOM   3381  C CB  . VAL A 1 399 ? -17.422 -2.791  0.395   1.00 23.36  ? 399 VAL A CB  1 
ATOM   3382  C CG1 . VAL A 1 399 ? -16.876 -3.908  -0.487  1.00 19.08  ? 399 VAL A CG1 1 
ATOM   3383  C CG2 . VAL A 1 399 ? -18.043 -3.357  1.663   1.00 21.20  ? 399 VAL A CG2 1 
ATOM   3384  N N   . ILE A 1 400 ? -14.932 -1.242  -1.180  1.00 15.91  ? 400 ILE A N   1 
ATOM   3385  C CA  . ILE A 1 400 ? -14.581 -0.593  -2.434  1.00 16.38  ? 400 ILE A CA  1 
ATOM   3386  C C   . ILE A 1 400 ? -14.272 -1.686  -3.447  1.00 18.95  ? 400 ILE A C   1 
ATOM   3387  O O   . ILE A 1 400 ? -13.940 -2.819  -3.092  1.00 20.82  ? 400 ILE A O   1 
ATOM   3388  C CB  . ILE A 1 400 ? -13.388 0.375   -2.291  1.00 15.83  ? 400 ILE A CB  1 
ATOM   3389  C CG1 . ILE A 1 400 ? -12.215 -0.316  -1.596  1.00 14.70  ? 400 ILE A CG1 1 
ATOM   3390  C CG2 . ILE A 1 400 ? -13.806 1.614   -1.518  1.00 23.24  ? 400 ILE A CG2 1 
ATOM   3391  C CD1 . ILE A 1 400 ? -10.877 0.338   -1.861  1.00 14.27  ? 400 ILE A CD1 1 
ATOM   3392  N N   . GLU A 1 401 ? -14.389 -1.334  -4.728  1.00 19.84  ? 401 GLU A N   1 
ATOM   3393  C CA  . GLU A 1 401 ? -14.325 -2.318  -5.796  1.00 22.73  ? 401 GLU A CA  1 
ATOM   3394  C C   . GLU A 1 401 ? -13.084 -2.220  -6.672  1.00 24.11  ? 401 GLU A C   1 
ATOM   3395  O O   . GLU A 1 401 ? -12.816 -3.157  -7.435  1.00 19.05  ? 401 GLU A O   1 
ATOM   3396  C CB  . GLU A 1 401 ? -15.578 -2.222  -6.678  1.00 29.76  ? 401 GLU A CB  1 
ATOM   3397  C CG  . GLU A 1 401 ? -16.884 -2.313  -5.898  1.00 41.86  ? 401 GLU A CG  1 
ATOM   3398  C CD  . GLU A 1 401 ? -17.228 -3.742  -5.515  1.00 48.76  ? 401 GLU A CD  1 
ATOM   3399  O OE1 . GLU A 1 401 ? -18.212 -3.951  -4.776  1.00 46.65  ? 401 GLU A OE1 1 
ATOM   3400  O OE2 . GLU A 1 401 ? -16.506 -4.662  -5.954  1.00 46.50  ? 401 GLU A OE2 1 
ATOM   3401  N N   . SER A 1 402 ? -12.327 -1.127  -6.598  1.00 20.94  ? 402 SER A N   1 
ATOM   3402  C CA  . SER A 1 402 ? -11.150 -0.989  -7.444  1.00 16.86  ? 402 SER A CA  1 
ATOM   3403  C C   . SER A 1 402 ? -10.185 0.007   -6.819  1.00 18.64  ? 402 SER A C   1 
ATOM   3404  O O   . SER A 1 402 ? -10.550 0.774   -5.925  1.00 26.21  ? 402 SER A O   1 
ATOM   3405  C CB  . SER A 1 402 ? -11.527 -0.550  -8.862  1.00 18.16  ? 402 SER A CB  1 
ATOM   3406  O OG  . SER A 1 402 ? -11.995 0.784   -8.869  1.00 18.86  ? 402 SER A OG  1 
ATOM   3407  N N   . VAL A 1 403 ? -8.937  -0.032  -7.292  1.00 15.84  ? 403 VAL A N   1 
ATOM   3408  C CA  . VAL A 1 403 ? -7.930  0.962   -6.940  1.00 15.35  ? 403 VAL A CA  1 
ATOM   3409  C C   . VAL A 1 403 ? -7.166  1.361   -8.196  1.00 23.38  ? 403 VAL A C   1 
ATOM   3410  O O   . VAL A 1 403 ? -7.010  0.572   -9.134  1.00 33.72  ? 403 VAL A O   1 
ATOM   3411  C CB  . VAL A 1 403 ? -6.945  0.466   -5.850  1.00 14.19  ? 403 VAL A CB  1 
ATOM   3412  C CG1 . VAL A 1 403 ? -7.689  -0.175  -4.684  1.00 18.40  ? 403 VAL A CG1 1 
ATOM   3413  C CG2 . VAL A 1 403 ? -5.921  -0.491  -6.438  1.00 16.82  ? 403 VAL A CG2 1 
ATOM   3414  N N   . LYS A 1 404 ? -6.705  2.609   -8.215  1.00 16.03  ? 404 LYS A N   1 
ATOM   3415  C CA  . LYS A 1 404 ? -5.794  3.068   -9.254  1.00 17.52  ? 404 LYS A CA  1 
ATOM   3416  C C   . LYS A 1 404 ? -4.379  2.627   -8.908  1.00 18.37  ? 404 LYS A C   1 
ATOM   3417  O O   . LYS A 1 404 ? -3.939  2.766   -7.763  1.00 23.46  ? 404 LYS A O   1 
ATOM   3418  C CB  . LYS A 1 404 ? -5.859  4.589   -9.393  1.00 17.25  ? 404 LYS A CB  1 
ATOM   3419  C CG  . LYS A 1 404 ? -7.197  5.123   -9.877  1.00 29.50  ? 404 LYS A CG  1 
ATOM   3420  C CD  . LYS A 1 404 ? -7.092  5.682   -11.287 1.00 34.85  ? 404 LYS A CD  1 
ATOM   3421  C CE  . LYS A 1 404 ? -8.425  6.241   -11.762 1.00 52.67  ? 404 LYS A CE  1 
ATOM   3422  N NZ  . LYS A 1 404 ? -8.449  7.730   -11.700 1.00 56.67  ? 404 LYS A NZ  1 
ATOM   3423  N N   . ALA A 1 405 ? -3.669  2.090   -9.894  1.00 21.10  ? 405 ALA A N   1 
ATOM   3424  C CA  . ALA A 1 405 ? -2.331  1.574   -9.645  1.00 24.04  ? 405 ALA A CA  1 
ATOM   3425  C C   . ALA A 1 405 ? -1.342  2.717   -9.455  1.00 14.68  ? 405 ALA A C   1 
ATOM   3426  O O   . ALA A 1 405 ? -1.268  3.633   -10.279 1.00 25.36  ? 405 ALA A O   1 
ATOM   3427  C CB  . ALA A 1 405 ? -1.886  0.678   -10.796 1.00 31.19  ? 405 ALA A CB  1 
ATOM   3428  N N   . GLY A 1 406 ? -0.579  2.653   -8.372  1.00 13.80  ? 406 GLY A N   1 
ATOM   3429  C CA  . GLY A 1 406 ? 0.403   3.679   -8.078  1.00 15.05  ? 406 GLY A CA  1 
ATOM   3430  C C   . GLY A 1 406 ? 1.152   3.328   -6.813  1.00 16.63  ? 406 GLY A C   1 
ATOM   3431  O O   . GLY A 1 406 ? 0.905   2.295   -6.183  1.00 21.05  ? 406 GLY A O   1 
ATOM   3432  N N   . THR A 1 407 ? 2.076   4.207   -6.448  1.00 12.81  ? 407 THR A N   1 
ATOM   3433  C CA  . THR A 1 407 ? 2.903   4.060   -5.256  1.00 12.30  ? 407 THR A CA  1 
ATOM   3434  C C   . THR A 1 407 ? 2.657   5.242   -4.325  1.00 14.96  ? 407 THR A C   1 
ATOM   3435  O O   . THR A 1 407 ? 1.884   6.149   -4.634  1.00 12.89  ? 407 THR A O   1 
ATOM   3436  C CB  . THR A 1 407 ? 4.387   3.961   -5.627  1.00 14.63  ? 407 THR A CB  1 
ATOM   3437  O OG1 . THR A 1 407 ? 4.862   5.248   -6.045  1.00 20.84  ? 407 THR A OG1 1 
ATOM   3438  C CG2 . THR A 1 407 ? 4.590   2.964   -6.756  1.00 13.71  ? 407 THR A CG2 1 
ATOM   3439  N N   . TRP A 1 408 ? 3.324   5.236   -3.172  1.00 20.44  ? 408 TRP A N   1 
ATOM   3440  C CA  . TRP A 1 408 ? 3.232   6.389   -2.285  1.00 17.14  ? 408 TRP A CA  1 
ATOM   3441  C C   . TRP A 1 408 ? 4.102   7.550   -2.748  1.00 19.90  ? 408 TRP A C   1 
ATOM   3442  O O   . TRP A 1 408 ? 4.181   8.567   -2.050  1.00 20.36  ? 408 TRP A O   1 
ATOM   3443  C CB  . TRP A 1 408 ? 3.573   5.995   -0.839  1.00 15.93  ? 408 TRP A CB  1 
ATOM   3444  C CG  . TRP A 1 408 ? 4.972   5.506   -0.574  1.00 15.02  ? 408 TRP A CG  1 
ATOM   3445  C CD1 . TRP A 1 408 ? 6.020   5.461   -1.449  1.00 18.32  ? 408 TRP A CD1 1 
ATOM   3446  C CD2 . TRP A 1 408 ? 5.467   4.991   0.668   1.00 14.89  ? 408 TRP A CD2 1 
ATOM   3447  N NE1 . TRP A 1 408 ? 7.135   4.951   -0.826  1.00 12.56  ? 408 TRP A NE1 1 
ATOM   3448  C CE2 . TRP A 1 408 ? 6.820   4.655   0.474   1.00 14.02  ? 408 TRP A CE2 1 
ATOM   3449  C CE3 . TRP A 1 408 ? 4.893   4.783   1.926   1.00 12.68  ? 408 TRP A CE3 1 
ATOM   3450  C CZ2 . TRP A 1 408 ? 7.609   4.121   1.490   1.00 17.41  ? 408 TRP A CZ2 1 
ATOM   3451  C CZ3 . TRP A 1 408 ? 5.676   4.255   2.932   1.00 14.79  ? 408 TRP A CZ3 1 
ATOM   3452  C CH2 . TRP A 1 408 ? 7.019   3.929   2.709   1.00 15.66  ? 408 TRP A CH2 1 
ATOM   3453  N N   . PHE A 1 409 ? 4.745   7.418   -3.905  1.00 18.92  ? 409 PHE A N   1 
ATOM   3454  C CA  . PHE A 1 409 ? 5.519   8.491   -4.524  1.00 19.95  ? 409 PHE A CA  1 
ATOM   3455  C C   . PHE A 1 409 ? 4.669   9.069   -5.653  1.00 24.34  ? 409 PHE A C   1 
ATOM   3456  O O   . PHE A 1 409 ? 4.712   8.599   -6.790  1.00 26.87  ? 409 PHE A O   1 
ATOM   3457  C CB  . PHE A 1 409 ? 6.857   7.966   -5.030  1.00 24.34  ? 409 PHE A CB  1 
ATOM   3458  C CG  . PHE A 1 409 ? 7.967   8.970   -4.959  1.00 37.74  ? 409 PHE A CG  1 
ATOM   3459  C CD1 . PHE A 1 409 ? 7.987   10.061  -5.814  1.00 40.93  ? 409 PHE A CD1 1 
ATOM   3460  C CD2 . PHE A 1 409 ? 8.993   8.824   -4.039  1.00 33.11  ? 409 PHE A CD2 1 
ATOM   3461  C CE1 . PHE A 1 409 ? 9.009   10.992  -5.753  1.00 38.16  ? 409 PHE A CE1 1 
ATOM   3462  C CE2 . PHE A 1 409 ? 10.019  9.750   -3.973  1.00 36.55  ? 409 PHE A CE2 1 
ATOM   3463  C CZ  . PHE A 1 409 ? 10.027  10.837  -4.831  1.00 36.49  ? 409 PHE A CZ  1 
ATOM   3464  N N   . ASP A 1 410 ? 3.875   10.089  -5.320  1.00 22.95  ? 410 ASP A N   1 
ATOM   3465  C CA  . ASP A 1 410 ? 3.000   10.819  -6.236  1.00 21.37  ? 410 ASP A CA  1 
ATOM   3466  C C   . ASP A 1 410 ? 1.868   9.972   -6.801  1.00 21.32  ? 410 ASP A C   1 
ATOM   3467  O O   . ASP A 1 410 ? 1.149   10.433  -7.695  1.00 22.61  ? 410 ASP A O   1 
ATOM   3468  C CB  . ASP A 1 410 ? 3.780   11.442  -7.400  1.00 27.91  ? 410 ASP A CB  1 
ATOM   3469  C CG  . ASP A 1 410 ? 4.594   12.645  -6.978  1.00 45.95  ? 410 ASP A CG  1 
ATOM   3470  O OD1 . ASP A 1 410 ? 4.086   13.456  -6.175  1.00 57.49  ? 410 ASP A OD1 1 
ATOM   3471  O OD2 . ASP A 1 410 ? 5.741   12.782  -7.450  1.00 56.83  ? 410 ASP A OD2 1 
ATOM   3472  N N   . GLY A 1 411 ? 1.678   8.752   -6.310  1.00 28.36  ? 411 GLY A N   1 
ATOM   3473  C CA  . GLY A 1 411 ? 0.609   7.917   -6.812  1.00 22.26  ? 411 GLY A CA  1 
ATOM   3474  C C   . GLY A 1 411 ? 0.870   7.269   -8.151  1.00 17.12  ? 411 GLY A C   1 
ATOM   3475  O O   . GLY A 1 411 ? -0.074  6.760   -8.767  1.00 22.93  ? 411 GLY A O   1 
ATOM   3476  N N   . ASN A 1 412 ? 2.114   7.274   -8.628  1.00 14.83  ? 412 ASN A N   1 
ATOM   3477  C CA  . ASN A 1 412 ? 2.457   6.683   -9.913  1.00 16.29  ? 412 ASN A CA  1 
ATOM   3478  C C   . ASN A 1 412 ? 3.827   6.027   -9.803  1.00 14.94  ? 412 ASN A C   1 
ATOM   3479  O O   . ASN A 1 412 ? 4.486   6.082   -8.761  1.00 17.13  ? 412 ASN A O   1 
ATOM   3480  C CB  . ASN A 1 412 ? 2.428   7.730   -11.034 1.00 22.51  ? 412 ASN A CB  1 
ATOM   3481  C CG  . ASN A 1 412 ? 3.210   8.983   -10.688 1.00 19.69  ? 412 ASN A CG  1 
ATOM   3482  O OD1 . ASN A 1 412 ? 4.374   8.916   -10.292 1.00 19.77  ? 412 ASN A OD1 1 
ATOM   3483  N ND2 . ASN A 1 412 ? 2.570   10.135  -10.837 1.00 27.30  ? 412 ASN A ND2 1 
ATOM   3484  N N   . PHE A 1 413 ? 4.260   5.408   -10.901 1.00 14.97  ? 413 PHE A N   1 
ATOM   3485  C CA  . PHE A 1 413 ? 5.510   4.664   -10.951 1.00 14.54  ? 413 PHE A CA  1 
ATOM   3486  C C   . PHE A 1 413 ? 6.622   5.437   -11.652 1.00 18.00  ? 413 PHE A C   1 
ATOM   3487  O O   . PHE A 1 413 ? 7.593   4.828   -12.115 1.00 19.28  ? 413 PHE A O   1 
ATOM   3488  C CB  . PHE A 1 413 ? 5.290   3.316   -11.641 1.00 14.60  ? 413 PHE A CB  1 
ATOM   3489  C CG  . PHE A 1 413 ? 4.186   2.498   -11.034 1.00 14.18  ? 413 PHE A CG  1 
ATOM   3490  C CD1 . PHE A 1 413 ? 2.875   2.649   -11.457 1.00 16.75  ? 413 PHE A CD1 1 
ATOM   3491  C CD2 . PHE A 1 413 ? 4.460   1.578   -10.040 1.00 14.62  ? 413 PHE A CD2 1 
ATOM   3492  C CE1 . PHE A 1 413 ? 1.859   1.899   -10.896 1.00 16.33  ? 413 PHE A CE1 1 
ATOM   3493  C CE2 . PHE A 1 413 ? 3.448   0.824   -9.477  1.00 18.90  ? 413 PHE A CE2 1 
ATOM   3494  C CZ  . PHE A 1 413 ? 2.147   0.985   -9.905  1.00 19.14  ? 413 PHE A CZ  1 
ATOM   3495  N N   . LEU A 1 414 ? 6.499   6.765   -11.735 1.00 22.05  ? 414 LEU A N   1 
ATOM   3496  C CA  . LEU A 1 414 ? 7.471   7.561   -12.479 1.00 18.87  ? 414 LEU A CA  1 
ATOM   3497  C C   . LEU A 1 414 ? 8.873   7.453   -11.891 1.00 19.32  ? 414 LEU A C   1 
ATOM   3498  O O   . LEU A 1 414 ? 9.860   7.559   -12.629 1.00 23.46  ? 414 LEU A O   1 
ATOM   3499  C CB  . LEU A 1 414 ? 7.023   9.024   -12.523 1.00 19.84  ? 414 LEU A CB  1 
ATOM   3500  C CG  . LEU A 1 414 ? 6.061   9.438   -13.640 1.00 20.90  ? 414 LEU A CG  1 
ATOM   3501  C CD1 . LEU A 1 414 ? 6.216   10.917  -13.954 1.00 25.86  ? 414 LEU A CD1 1 
ATOM   3502  C CD2 . LEU A 1 414 ? 6.279   8.602   -14.895 1.00 24.96  ? 414 LEU A CD2 1 
ATOM   3503  N N   . LYS A 1 415 ? 8.989   7.235   -10.579 1.00 17.70  ? 415 LYS A N   1 
ATOM   3504  C CA  . LYS A 1 415 ? 10.300  7.169   -9.941  1.00 20.44  ? 415 LYS A CA  1 
ATOM   3505  C C   . LYS A 1 415 ? 11.076  5.911   -10.313 1.00 23.93  ? 415 LYS A C   1 
ATOM   3506  O O   . LYS A 1 415 ? 12.276  5.833   -10.026 1.00 26.61  ? 415 LYS A O   1 
ATOM   3507  C CB  . LYS A 1 415 ? 10.144  7.263   -8.418  1.00 16.92  ? 415 LYS A CB  1 
ATOM   3508  C CG  . LYS A 1 415 ? 11.446  7.429   -7.640  1.00 24.94  ? 415 LYS A CG  1 
ATOM   3509  C CD  . LYS A 1 415 ? 11.642  8.867   -7.197  1.00 36.12  ? 415 LYS A CD  1 
ATOM   3510  C CE  . LYS A 1 415 ? 13.087  9.147   -6.806  1.00 47.73  ? 415 LYS A CE  1 
ATOM   3511  N NZ  . LYS A 1 415 ? 14.047  8.885   -7.918  1.00 39.84  ? 415 LYS A NZ  1 
ATOM   3512  N N   . TRP A 1 416 ? 10.436  4.931   -10.948 1.00 22.64  ? 416 TRP A N   1 
ATOM   3513  C CA  . TRP A 1 416 ? 11.103  3.687   -11.300 1.00 20.15  ? 416 TRP A CA  1 
ATOM   3514  C C   . TRP A 1 416 ? 11.098  3.384   -12.787 1.00 23.02  ? 416 TRP A C   1 
ATOM   3515  O O   . TRP A 1 416 ? 11.936  2.597   -13.239 1.00 23.37  ? 416 TRP A O   1 
ATOM   3516  C CB  . TRP A 1 416 ? 10.454  2.509   -10.559 1.00 15.53  ? 416 TRP A CB  1 
ATOM   3517  C CG  . TRP A 1 416 ? 10.570  2.628   -9.081  1.00 16.93  ? 416 TRP A CG  1 
ATOM   3518  C CD1 . TRP A 1 416 ? 11.575  2.147   -8.295  1.00 20.47  ? 416 TRP A CD1 1 
ATOM   3519  C CD2 . TRP A 1 416 ? 9.656   3.293   -8.202  1.00 15.98  ? 416 TRP A CD2 1 
ATOM   3520  N NE1 . TRP A 1 416 ? 11.339  2.462   -6.979  1.00 20.95  ? 416 TRP A NE1 1 
ATOM   3521  C CE2 . TRP A 1 416 ? 10.167  3.167   -6.896  1.00 18.25  ? 416 TRP A CE2 1 
ATOM   3522  C CE3 . TRP A 1 416 ? 8.453   3.980   -8.393  1.00 16.46  ? 416 TRP A CE3 1 
ATOM   3523  C CZ2 . TRP A 1 416 ? 9.517   3.701   -5.786  1.00 13.31  ? 416 TRP A CZ2 1 
ATOM   3524  C CZ3 . TRP A 1 416 ? 7.809   4.509   -7.290  1.00 16.87  ? 416 TRP A CZ3 1 
ATOM   3525  C CH2 . TRP A 1 416 ? 8.342   4.367   -6.003  1.00 17.72  ? 416 TRP A CH2 1 
ATOM   3526  N N   . ILE A 1 417 ? 10.191  3.986   -13.555 1.00 29.51  ? 417 ILE A N   1 
ATOM   3527  C CA  . ILE A 1 417 ? 10.028  3.668   -14.967 1.00 22.93  ? 417 ILE A CA  1 
ATOM   3528  C C   . ILE A 1 417 ? 9.466   4.915   -15.635 1.00 22.53  ? 417 ILE A C   1 
ATOM   3529  O O   . ILE A 1 417 ? 8.944   5.810   -14.968 1.00 21.90  ? 417 ILE A O   1 
ATOM   3530  C CB  . ILE A 1 417 ? 9.111   2.430   -15.145 1.00 19.55  ? 417 ILE A CB  1 
ATOM   3531  C CG1 . ILE A 1 417 ? 9.308   1.780   -16.516 1.00 25.03  ? 417 ILE A CG1 1 
ATOM   3532  C CG2 . ILE A 1 417 ? 7.657   2.796   -14.903 1.00 18.28  ? 417 ILE A CG2 1 
ATOM   3533  C CD1 . ILE A 1 417 ? 8.600   0.451   -16.659 1.00 19.67  ? 417 ILE A CD1 1 
ATOM   3534  N N   . GLY A 1 418 ? 9.559   4.975   -16.961 1.00 24.97  ? 418 GLY A N   1 
ATOM   3535  C CA  . GLY A 1 418 ? 9.308   6.238   -17.631 1.00 30.22  ? 418 GLY A CA  1 
ATOM   3536  C C   . GLY A 1 418 ? 10.384  6.638   -18.620 1.00 39.60  ? 418 GLY A C   1 
ATOM   3537  O O   . GLY A 1 418 ? 10.494  6.039   -19.693 1.00 44.92  ? 418 GLY A O   1 
ATOM   3538  N N   . ASN A 1 419 ? 11.163  7.670   -18.289 1.00 37.29  ? 419 ASN A N   1 
ATOM   3539  C CA  . ASN A 1 419 ? 12.139  8.236   -19.216 1.00 46.53  ? 419 ASN A CA  1 
ATOM   3540  C C   . ASN A 1 419 ? 13.195  7.214   -19.626 1.00 46.07  ? 419 ASN A C   1 
ATOM   3541  O O   . ASN A 1 419 ? 13.193  6.077   -19.139 1.00 45.52  ? 419 ASN A O   1 
ATOM   3542  C CB  . ASN A 1 419 ? 12.815  9.459   -18.589 1.00 52.73  ? 419 ASN A CB  1 
ATOM   3543  C CG  . ASN A 1 419 ? 13.110  9.266   -17.114 1.00 59.34  ? 419 ASN A CG  1 
ATOM   3544  O OD1 . ASN A 1 419 ? 13.395  8.155   -16.672 1.00 55.63  ? 419 ASN A OD1 1 
ATOM   3545  N ND2 . ASN A 1 419 ? 13.049  10.348  -16.346 1.00 62.02  ? 419 ASN A ND2 1 
ATOM   3546  N N   . LYS A 1 420 ? 14.102  7.609   -20.524 1.00 48.53  ? 420 LYS A N   1 
ATOM   3547  C CA  . LYS A 1 420 ? 15.041  6.648   -21.095 1.00 51.97  ? 420 LYS A CA  1 
ATOM   3548  C C   . LYS A 1 420 ? 15.950  6.046   -20.030 1.00 48.82  ? 420 LYS A C   1 
ATOM   3549  O O   . LYS A 1 420 ? 16.295  4.859   -20.101 1.00 49.96  ? 420 LYS A O   1 
ATOM   3550  C CB  . LYS A 1 420 ? 15.878  7.307   -22.195 1.00 51.87  ? 420 LYS A CB  1 
ATOM   3551  C CG  . LYS A 1 420 ? 16.878  6.352   -22.839 1.00 56.25  ? 420 LYS A CG  1 
ATOM   3552  C CD  . LYS A 1 420 ? 17.785  7.044   -23.841 1.00 61.59  ? 420 LYS A CD  1 
ATOM   3553  C CE  . LYS A 1 420 ? 19.251  6.821   -23.498 1.00 59.60  ? 420 LYS A CE  1 
ATOM   3554  N NZ  . LYS A 1 420 ? 20.133  6.939   -24.692 1.00 57.08  ? 420 LYS A NZ  1 
ATOM   3555  N N   . GLU A 1 421 ? 16.356  6.843   -19.038 1.00 37.69  ? 421 GLU A N   1 
ATOM   3556  C CA  . GLU A 1 421 ? 17.293  6.342   -18.036 1.00 45.71  ? 421 GLU A CA  1 
ATOM   3557  C C   . GLU A 1 421 ? 16.670  5.237   -17.189 1.00 48.72  ? 421 GLU A C   1 
ATOM   3558  O O   . GLU A 1 421 ? 17.260  4.162   -17.027 1.00 43.30  ? 421 GLU A O   1 
ATOM   3559  C CB  . GLU A 1 421 ? 17.791  7.484   -17.150 1.00 53.78  ? 421 GLU A CB  1 
ATOM   3560  C CG  . GLU A 1 421 ? 16.783  8.592   -16.911 1.00 54.01  ? 421 GLU A CG  1 
ATOM   3561  C CD  . GLU A 1 421 ? 17.426  9.826   -16.308 1.00 59.31  ? 421 GLU A CD  1 
ATOM   3562  O OE1 . GLU A 1 421 ? 18.513  10.224  -16.781 1.00 52.34  ? 421 GLU A OE1 1 
ATOM   3563  O OE2 . GLU A 1 421 ? 16.848  10.396  -15.360 1.00 65.76  ? 421 GLU A OE2 1 
ATOM   3564  N N   . LYS A 1 422 ? 15.475  5.479   -16.643 1.00 44.94  ? 422 LYS A N   1 
ATOM   3565  C CA  . LYS A 1 422 ? 14.813  4.447   -15.849 1.00 34.95  ? 422 LYS A CA  1 
ATOM   3566  C C   . LYS A 1 422 ? 14.485  3.222   -16.692 1.00 29.16  ? 422 LYS A C   1 
ATOM   3567  O O   . LYS A 1 422 ? 14.397  2.109   -16.163 1.00 31.79  ? 422 LYS A O   1 
ATOM   3568  C CB  . LYS A 1 422 ? 13.535  5.001   -15.215 1.00 37.31  ? 422 LYS A CB  1 
ATOM   3569  C CG  . LYS A 1 422 ? 13.744  6.223   -14.336 1.00 36.59  ? 422 LYS A CG  1 
ATOM   3570  C CD  . LYS A 1 422 ? 13.994  5.874   -12.883 1.00 32.19  ? 422 LYS A CD  1 
ATOM   3571  C CE  . LYS A 1 422 ? 14.165  7.143   -12.061 1.00 28.15  ? 422 LYS A CE  1 
ATOM   3572  N NZ  . LYS A 1 422 ? 15.083  6.951   -10.906 1.00 32.97  ? 422 LYS A NZ  1 
ATOM   3573  N N   . ASN A 1 423 ? 14.304  3.407   -18.000 1.00 31.03  ? 423 ASN A N   1 
ATOM   3574  C CA  . ASN A 1 423 ? 13.916  2.313   -18.880 1.00 38.20  ? 423 ASN A CA  1 
ATOM   3575  C C   . ASN A 1 423 ? 15.092  1.455   -19.330 1.00 39.32  ? 423 ASN A C   1 
ATOM   3576  O O   . ASN A 1 423 ? 14.882  0.295   -19.702 1.00 31.20  ? 423 ASN A O   1 
ATOM   3577  C CB  . ASN A 1 423 ? 13.186  2.863   -20.108 1.00 35.60  ? 423 ASN A CB  1 
ATOM   3578  C CG  . ASN A 1 423 ? 11.756  3.263   -19.803 1.00 33.92  ? 423 ASN A CG  1 
ATOM   3579  O OD1 . ASN A 1 423 ? 11.348  3.322   -18.643 1.00 27.36  ? 423 ASN A OD1 1 
ATOM   3580  N ND2 . ASN A 1 423 ? 10.984  3.536   -20.848 1.00 30.65  ? 423 ASN A ND2 1 
ATOM   3581  N N   . GLU A 1 424 ? 16.316  1.991   -19.312 1.00 37.17  ? 424 GLU A N   1 
ATOM   3582  C CA  . GLU A 1 424 ? 17.469  1.200   -19.734 1.00 34.61  ? 424 GLU A CA  1 
ATOM   3583  C C   . GLU A 1 424 ? 17.658  -0.018  -18.838 1.00 32.44  ? 424 GLU A C   1 
ATOM   3584  O O   . GLU A 1 424 ? 17.930  -1.120  -19.328 1.00 32.60  ? 424 GLU A O   1 
ATOM   3585  C CB  . GLU A 1 424 ? 18.731  2.063   -19.740 1.00 39.58  ? 424 GLU A CB  1 
ATOM   3586  C CG  . GLU A 1 424 ? 19.775  1.657   -20.781 1.00 70.24  ? 424 GLU A CG  1 
ATOM   3587  C CD  . GLU A 1 424 ? 19.164  1.046   -22.032 1.00 67.47  ? 424 GLU A CD  1 
ATOM   3588  O OE1 . GLU A 1 424 ? 18.645  1.807   -22.877 1.00 72.06  ? 424 GLU A OE1 1 
ATOM   3589  O OE2 . GLU A 1 424 ? 19.215  -0.195  -22.176 1.00 53.17  ? 424 GLU A OE2 1 
ATOM   3590  N N   . TYR A 1 425 ? 17.506  0.158   -17.523 1.00 30.50  ? 425 TYR A N   1 
ATOM   3591  C CA  . TYR A 1 425 ? 17.626  -0.972  -16.607 1.00 30.35  ? 425 TYR A CA  1 
ATOM   3592  C C   . TYR A 1 425 ? 16.544  -2.015  -16.865 1.00 28.16  ? 425 TYR A C   1 
ATOM   3593  O O   . TYR A 1 425 ? 16.811  -3.222  -16.813 1.00 26.79  ? 425 TYR A O   1 
ATOM   3594  C CB  . TYR A 1 425 ? 17.563  -0.483  -15.161 1.00 31.61  ? 425 TYR A CB  1 
ATOM   3595  C CG  . TYR A 1 425 ? 18.904  -0.147  -14.549 1.00 31.27  ? 425 TYR A CG  1 
ATOM   3596  C CD1 . TYR A 1 425 ? 19.998  0.165   -15.346 1.00 31.34  ? 425 TYR A CD1 1 
ATOM   3597  C CD2 . TYR A 1 425 ? 19.073  -0.139  -13.169 1.00 29.72  ? 425 TYR A CD2 1 
ATOM   3598  C CE1 . TYR A 1 425 ? 21.225  0.474   -14.786 1.00 40.72  ? 425 TYR A CE1 1 
ATOM   3599  C CE2 . TYR A 1 425 ? 20.293  0.170   -12.601 1.00 36.03  ? 425 TYR A CE2 1 
ATOM   3600  C CZ  . TYR A 1 425 ? 21.365  0.477   -13.412 1.00 42.73  ? 425 TYR A CZ  1 
ATOM   3601  O OH  . TYR A 1 425 ? 22.581  0.784   -12.846 1.00 37.28  ? 425 TYR A OH  1 
ATOM   3602  N N   . TRP A 1 426 ? 15.313  -1.570  -17.135 1.00 27.11  ? 426 TRP A N   1 
ATOM   3603  C CA  . TRP A 1 426 ? 14.226  -2.510  -17.398 1.00 24.97  ? 426 TRP A CA  1 
ATOM   3604  C C   . TRP A 1 426 ? 14.495  -3.334  -18.652 1.00 26.40  ? 426 TRP A C   1 
ATOM   3605  O O   . TRP A 1 426 ? 14.224  -4.540  -18.681 1.00 28.59  ? 426 TRP A O   1 
ATOM   3606  C CB  . TRP A 1 426 ? 12.898  -1.760  -17.523 1.00 23.49  ? 426 TRP A CB  1 
ATOM   3607  C CG  . TRP A 1 426 ? 12.268  -1.412  -16.204 1.00 30.46  ? 426 TRP A CG  1 
ATOM   3608  C CD1 . TRP A 1 426 ? 12.240  -0.183  -15.609 1.00 35.02  ? 426 TRP A CD1 1 
ATOM   3609  C CD2 . TRP A 1 426 ? 11.571  -2.300  -15.320 1.00 23.86  ? 426 TRP A CD2 1 
ATOM   3610  N NE1 . TRP A 1 426 ? 11.571  -0.252  -14.410 1.00 30.19  ? 426 TRP A NE1 1 
ATOM   3611  C CE2 . TRP A 1 426 ? 11.150  -1.540  -14.210 1.00 27.92  ? 426 TRP A CE2 1 
ATOM   3612  C CE3 . TRP A 1 426 ? 11.263  -3.664  -15.360 1.00 26.88  ? 426 TRP A CE3 1 
ATOM   3613  C CZ2 . TRP A 1 426 ? 10.438  -2.098  -13.149 1.00 31.24  ? 426 TRP A CZ2 1 
ATOM   3614  C CZ3 . TRP A 1 426 ? 10.555  -4.216  -14.305 1.00 31.86  ? 426 TRP A CZ3 1 
ATOM   3615  C CH2 . TRP A 1 426 ? 10.151  -3.434  -13.216 1.00 27.13  ? 426 TRP A CH2 1 
ATOM   3616  N N   . LYS A 1 427 ? 15.019  -2.697  -19.703 1.00 28.14  ? 427 LYS A N   1 
ATOM   3617  C CA  . LYS A 1 427 ? 15.372  -3.438  -20.911 1.00 29.80  ? 427 LYS A CA  1 
ATOM   3618  C C   . LYS A 1 427 ? 16.463  -4.462  -20.626 1.00 29.98  ? 427 LYS A C   1 
ATOM   3619  O O   . LYS A 1 427 ? 16.409  -5.592  -21.126 1.00 29.87  ? 427 LYS A O   1 
ATOM   3620  C CB  . LYS A 1 427 ? 15.814  -2.478  -22.014 1.00 32.79  ? 427 LYS A CB  1 
ATOM   3621  C CG  . LYS A 1 427 ? 14.679  -1.704  -22.659 1.00 33.08  ? 427 LYS A CG  1 
ATOM   3622  C CD  . LYS A 1 427 ? 15.202  -0.584  -23.543 1.00 37.74  ? 427 LYS A CD  1 
ATOM   3623  C CE  . LYS A 1 427 ? 14.298  0.637   -23.485 1.00 51.68  ? 427 LYS A CE  1 
ATOM   3624  N NZ  . LYS A 1 427 ? 15.080  1.903   -23.526 1.00 61.14  ? 427 LYS A NZ  1 
ATOM   3625  N N   . ILE A 1 428 ? 17.464  -4.083  -19.828 1.00 30.39  ? 428 ILE A N   1 
ATOM   3626  C CA  . ILE A 1 428 ? 18.490  -5.036  -19.412 1.00 30.52  ? 428 ILE A CA  1 
ATOM   3627  C C   . ILE A 1 428 ? 17.859  -6.192  -18.649 1.00 27.88  ? 428 ILE A C   1 
ATOM   3628  O O   . ILE A 1 428 ? 18.232  -7.357  -18.833 1.00 27.91  ? 428 ILE A O   1 
ATOM   3629  C CB  . ILE A 1 428 ? 19.571  -4.328  -18.573 1.00 31.39  ? 428 ILE A CB  1 
ATOM   3630  C CG1 . ILE A 1 428 ? 20.221  -3.196  -19.373 1.00 34.32  ? 428 ILE A CG1 1 
ATOM   3631  C CG2 . ILE A 1 428 ? 20.618  -5.325  -18.098 1.00 31.61  ? 428 ILE A CG2 1 
ATOM   3632  C CD1 . ILE A 1 428 ? 21.494  -2.657  -18.754 1.00 35.85  ? 428 ILE A CD1 1 
ATOM   3633  N N   . LEU A 1 429 ? 16.892  -5.888  -17.780 1.00 25.70  ? 429 LEU A N   1 
ATOM   3634  C CA  . LEU A 1 429 ? 16.227  -6.934  -17.010 1.00 24.36  ? 429 LEU A CA  1 
ATOM   3635  C C   . LEU A 1 429 ? 15.464  -7.896  -17.914 1.00 23.71  ? 429 LEU A C   1 
ATOM   3636  O O   . LEU A 1 429 ? 15.525  -9.116  -17.724 1.00 23.31  ? 429 LEU A O   1 
ATOM   3637  C CB  . LEU A 1 429 ? 15.289  -6.305  -15.981 1.00 21.35  ? 429 LEU A CB  1 
ATOM   3638  C CG  . LEU A 1 429 ? 14.553  -7.269  -15.048 1.00 19.02  ? 429 LEU A CG  1 
ATOM   3639  C CD1 . LEU A 1 429 ? 15.520  -8.272  -14.442 1.00 19.83  ? 429 LEU A CD1 1 
ATOM   3640  C CD2 . LEU A 1 429 ? 13.815  -6.509  -13.959 1.00 21.23  ? 429 LEU A CD2 1 
ATOM   3641  N N   . ILE A 1 430 ? 14.742  -7.367  -18.904 1.00 27.48  ? 430 ILE A N   1 
ATOM   3642  C CA  . ILE A 1 430 ? 13.888  -8.212  -19.735 1.00 23.51  ? 430 ILE A CA  1 
ATOM   3643  C C   . ILE A 1 430 ? 14.729  -9.168  -20.572 1.00 27.89  ? 430 ILE A C   1 
ATOM   3644  O O   . ILE A 1 430 ? 14.443  -10.370 -20.646 1.00 35.45  ? 430 ILE A O   1 
ATOM   3645  C CB  . ILE A 1 430 ? 12.967  -7.348  -20.614 1.00 24.22  ? 430 ILE A CB  1 
ATOM   3646  C CG1 . ILE A 1 430 ? 11.884  -6.689  -19.758 1.00 22.35  ? 430 ILE A CG1 1 
ATOM   3647  C CG2 . ILE A 1 430 ? 12.336  -8.190  -21.713 1.00 24.72  ? 430 ILE A CG2 1 
ATOM   3648  C CD1 . ILE A 1 430 ? 11.382  -5.372  -20.311 1.00 23.39  ? 430 ILE A CD1 1 
ATOM   3649  N N   . GLU A 1 431 ? 15.780  -8.653  -21.215 1.00 27.37  ? 431 GLU A N   1 
ATOM   3650  C CA  . GLU A 1 431 ? 16.638  -9.519  -22.016 1.00 29.04  ? 431 GLU A CA  1 
ATOM   3651  C C   . GLU A 1 431 ? 17.351  -10.549 -21.152 1.00 36.86  ? 431 GLU A C   1 
ATOM   3652  O O   . GLU A 1 431 ? 17.606  -11.671 -21.606 1.00 42.74  ? 431 GLU A O   1 
ATOM   3653  C CB  . GLU A 1 431 ? 17.646  -8.684  -22.806 1.00 31.93  ? 431 GLU A CB  1 
ATOM   3654  C CG  . GLU A 1 431 ? 17.152  -8.272  -24.186 1.00 34.78  ? 431 GLU A CG  1 
ATOM   3655  C CD  . GLU A 1 431 ? 16.543  -9.427  -24.959 1.00 53.64  ? 431 GLU A CD  1 
ATOM   3656  O OE1 . GLU A 1 431 ? 17.191  -10.490 -25.058 1.00 49.33  ? 431 GLU A OE1 1 
ATOM   3657  O OE2 . GLU A 1 431 ? 15.411  -9.272  -25.464 1.00 55.87  ? 431 GLU A OE2 1 
ATOM   3658  N N   . ALA A 1 432 ? 17.687  -10.187 -19.911 1.00 27.10  ? 432 ALA A N   1 
ATOM   3659  C CA  . ALA A 1 432 ? 18.215  -11.172 -18.973 1.00 26.12  ? 432 ALA A CA  1 
ATOM   3660  C C   . ALA A 1 432 ? 17.153  -12.190 -18.589 1.00 28.75  ? 432 ALA A C   1 
ATOM   3661  O O   . ALA A 1 432 ? 17.432  -13.393 -18.518 1.00 35.94  ? 432 ALA A O   1 
ATOM   3662  C CB  . ALA A 1 432 ? 18.750  -10.479 -17.726 1.00 25.62  ? 432 ALA A CB  1 
ATOM   3663  N N   . LYS A 1 433 ? 15.930  -11.722 -18.328 1.00 29.84  ? 433 LYS A N   1 
ATOM   3664  C CA  . LYS A 1 433 ? 14.830  -12.633 -18.035 1.00 28.36  ? 433 LYS A CA  1 
ATOM   3665  C C   . LYS A 1 433 ? 14.605  -13.617 -19.175 1.00 29.34  ? 433 LYS A C   1 
ATOM   3666  O O   . LYS A 1 433 ? 14.230  -14.771 -18.936 1.00 31.30  ? 433 LYS A O   1 
ATOM   3667  C CB  . LYS A 1 433 ? 13.557  -11.832 -17.758 1.00 25.59  ? 433 LYS A CB  1 
ATOM   3668  C CG  . LYS A 1 433 ? 12.310  -12.675 -17.592 1.00 21.42  ? 433 LYS A CG  1 
ATOM   3669  C CD  . LYS A 1 433 ? 12.266  -13.331 -16.227 1.00 20.20  ? 433 LYS A CD  1 
ATOM   3670  C CE  . LYS A 1 433 ? 10.975  -14.105 -16.051 1.00 27.76  ? 433 LYS A CE  1 
ATOM   3671  N NZ  . LYS A 1 433 ? 9.846   -13.421 -16.741 1.00 32.87  ? 433 LYS A NZ  1 
ATOM   3672  N N   . LYS A 1 434 ? 14.847  -13.184 -20.414 1.00 31.52  ? 434 LYS A N   1 
ATOM   3673  C CA  . LYS A 1 434 ? 14.697  -14.068 -21.564 1.00 33.23  ? 434 LYS A CA  1 
ATOM   3674  C C   . LYS A 1 434 ? 15.634  -15.266 -21.467 1.00 40.97  ? 434 LYS A C   1 
ATOM   3675  O O   . LYS A 1 434 ? 15.240  -16.400 -21.766 1.00 44.72  ? 434 LYS A O   1 
ATOM   3676  C CB  . LYS A 1 434 ? 14.955  -13.286 -22.850 1.00 32.23  ? 434 LYS A CB  1 
ATOM   3677  C CG  . LYS A 1 434 ? 14.344  -13.894 -24.099 1.00 46.05  ? 434 LYS A CG  1 
ATOM   3678  C CD  . LYS A 1 434 ? 15.222  -13.630 -25.314 1.00 55.20  ? 434 LYS A CD  1 
ATOM   3679  C CE  . LYS A 1 434 ? 14.581  -14.143 -26.596 1.00 39.91  ? 434 LYS A CE  1 
ATOM   3680  N NZ  . LYS A 1 434 ? 14.723  -15.616 -26.756 1.00 31.25  ? 434 LYS A NZ  1 
ATOM   3681  N N   . LYS A 1 435 ? 16.879  -15.035 -21.049 1.00 37.67  ? 435 LYS A N   1 
ATOM   3682  C CA  . LYS A 1 435 ? 17.884  -16.085 -20.940 1.00 39.64  ? 435 LYS A CA  1 
ATOM   3683  C C   . LYS A 1 435 ? 18.175  -16.460 -19.490 1.00 38.60  ? 435 LYS A C   1 
ATOM   3684  O O   . LYS A 1 435 ? 19.235  -17.025 -19.198 1.00 39.77  ? 435 LYS A O   1 
ATOM   3685  C CB  . LYS A 1 435 ? 19.164  -15.657 -21.659 1.00 38.91  ? 435 LYS A CB  1 
ATOM   3686  C CG  . LYS A 1 435 ? 18.921  -15.236 -23.105 1.00 44.42  ? 435 LYS A CG  1 
ATOM   3687  C CD  . LYS A 1 435 ? 20.165  -14.674 -23.782 1.00 46.16  ? 435 LYS A CD  1 
ATOM   3688  C CE  . LYS A 1 435 ? 20.635  -13.385 -23.130 1.00 57.08  ? 435 LYS A CE  1 
ATOM   3689  N NZ  . LYS A 1 435 ? 22.041  -13.496 -22.653 1.00 53.51  ? 435 LYS A NZ  1 
ATOM   3690  N N   . ALA A 1 436 ? 17.248  -16.165 -18.579 1.00 30.01  ? 436 ALA A N   1 
ATOM   3691  C CA  . ALA A 1 436 ? 17.463  -16.437 -17.164 1.00 26.56  ? 436 ALA A CA  1 
ATOM   3692  C C   . ALA A 1 436 ? 17.407  -17.934 -16.878 1.00 25.75  ? 436 ALA A C   1 
ATOM   3693  O O   . ALA A 1 436 ? 16.609  -18.667 -17.468 1.00 26.16  ? 436 ALA A O   1 
ATOM   3694  C CB  . ALA A 1 436 ? 16.420  -15.706 -16.323 1.00 20.07  ? 436 ALA A CB  1 
ATOM   3695  N N   . LYS A 1 437 ? 18.261  -18.383 -15.962 1.00 27.15  ? 437 LYS A N   1 
ATOM   3696  C CA  . LYS A 1 437 ? 18.310  -19.782 -15.551 1.00 26.29  ? 437 LYS A CA  1 
ATOM   3697  C C   . LYS A 1 437 ? 18.036  -19.987 -14.070 1.00 24.13  ? 437 LYS A C   1 
ATOM   3698  O O   . LYS A 1 437 ? 17.269  -20.884 -13.711 1.00 26.43  ? 437 LYS A O   1 
ATOM   3699  C CB  . LYS A 1 437 ? 19.674  -20.391 -15.904 1.00 32.27  ? 437 LYS A CB  1 
ATOM   3700  C CG  . LYS A 1 437 ? 20.175  -20.021 -17.288 1.00 29.33  ? 437 LYS A CG  1 
ATOM   3701  C CD  . LYS A 1 437 ? 20.682  -21.243 -18.032 1.00 31.28  ? 437 LYS A CD  1 
ATOM   3702  C CE  . LYS A 1 437 ? 19.533  -22.031 -18.638 1.00 39.26  ? 437 LYS A CE  1 
ATOM   3703  N NZ  . LYS A 1 437 ? 18.929  -21.322 -19.801 1.00 33.00  ? 437 LYS A NZ  1 
ATOM   3704  N N   . ASN A 1 438 ? 18.639  -19.186 -13.197 1.00 22.95  ? 438 ASN A N   1 
ATOM   3705  C CA  . ASN A 1 438 ? 18.483  -19.335 -11.758 1.00 22.51  ? 438 ASN A CA  1 
ATOM   3706  C C   . ASN A 1 438 ? 17.647  -18.186 -11.202 1.00 28.25  ? 438 ASN A C   1 
ATOM   3707  O O   . ASN A 1 438 ? 17.149  -17.328 -11.935 1.00 31.74  ? 438 ASN A O   1 
ATOM   3708  C CB  . ASN A 1 438 ? 19.847  -19.408 -11.067 1.00 23.37  ? 438 ASN A CB  1 
ATOM   3709  C CG  . ASN A 1 438 ? 20.831  -18.395 -11.612 1.00 30.24  ? 438 ASN A CG  1 
ATOM   3710  O OD1 . ASN A 1 438 ? 20.928  -17.277 -11.111 1.00 28.64  ? 438 ASN A OD1 1 
ATOM   3711  N ND2 . ASN A 1 438 ? 21.581  -18.789 -12.635 1.00 37.59  ? 438 ASN A ND2 1 
ATOM   3712  N N   . ASP A 1 439 ? 17.511  -18.171 -9.877  1.00 28.14  ? 439 ASP A N   1 
ATOM   3713  C CA  . ASP A 1 439 ? 16.630  -17.230 -9.199  1.00 24.90  ? 439 ASP A CA  1 
ATOM   3714  C C   . ASP A 1 439 ? 17.261  -15.864 -8.978  1.00 21.53  ? 439 ASP A C   1 
ATOM   3715  O O   . ASP A 1 439 ? 16.611  -14.992 -8.393  1.00 22.03  ? 439 ASP A O   1 
ATOM   3716  C CB  . ASP A 1 439 ? 16.177  -17.809 -7.854  1.00 26.78  ? 439 ASP A CB  1 
ATOM   3717  C CG  . ASP A 1 439 ? 14.907  -18.622 -7.971  1.00 48.16  ? 439 ASP A CG  1 
ATOM   3718  O OD1 . ASP A 1 439 ? 14.155  -18.410 -8.946  1.00 46.05  ? 439 ASP A OD1 1 
ATOM   3719  O OD2 . ASP A 1 439 ? 14.659  -19.473 -7.091  1.00 60.94  ? 439 ASP A OD2 1 
ATOM   3720  N N   . TYR A 1 440 ? 18.501  -15.651 -9.419  1.00 24.71  ? 440 TYR A N   1 
ATOM   3721  C CA  . TYR A 1 440 ? 19.096  -14.325 -9.294  1.00 19.89  ? 440 TYR A CA  1 
ATOM   3722  C C   . TYR A 1 440 ? 18.348  -13.282 -10.108 1.00 16.49  ? 440 TYR A C   1 
ATOM   3723  O O   . TYR A 1 440 ? 18.513  -12.084 -9.856  1.00 22.28  ? 440 TYR A O   1 
ATOM   3724  C CB  . TYR A 1 440 ? 20.568  -14.362 -9.702  1.00 21.07  ? 440 TYR A CB  1 
ATOM   3725  C CG  . TYR A 1 440 ? 21.500  -14.481 -8.524  1.00 23.06  ? 440 TYR A CG  1 
ATOM   3726  C CD1 . TYR A 1 440 ? 21.798  -13.377 -7.739  1.00 20.96  ? 440 TYR A CD1 1 
ATOM   3727  C CD2 . TYR A 1 440 ? 22.066  -15.701 -8.183  1.00 27.67  ? 440 TYR A CD2 1 
ATOM   3728  C CE1 . TYR A 1 440 ? 22.644  -13.480 -6.657  1.00 20.47  ? 440 TYR A CE1 1 
ATOM   3729  C CE2 . TYR A 1 440 ? 22.915  -15.814 -7.102  1.00 26.82  ? 440 TYR A CE2 1 
ATOM   3730  C CZ  . TYR A 1 440 ? 23.200  -14.701 -6.341  1.00 25.30  ? 440 TYR A CZ  1 
ATOM   3731  O OH  . TYR A 1 440 ? 24.045  -14.810 -5.262  1.00 39.39  ? 440 TYR A OH  1 
ATOM   3732  N N   . ILE A 1 441 ? 17.528  -13.707 -11.074 1.00 17.69  ? 441 ILE A N   1 
ATOM   3733  C CA  . ILE A 1 441 ? 16.658  -12.765 -11.767 1.00 15.73  ? 441 ILE A CA  1 
ATOM   3734  C C   . ILE A 1 441 ? 15.640  -12.176 -10.807 1.00 15.91  ? 441 ILE A C   1 
ATOM   3735  O O   . ILE A 1 441 ? 15.161  -11.060 -11.025 1.00 21.87  ? 441 ILE A O   1 
ATOM   3736  C CB  . ILE A 1 441 ? 15.974  -13.432 -12.982 1.00 16.26  ? 441 ILE A CB  1 
ATOM   3737  C CG1 . ILE A 1 441 ? 15.688  -12.391 -14.064 1.00 16.17  ? 441 ILE A CG1 1 
ATOM   3738  C CG2 . ILE A 1 441 ? 14.685  -14.132 -12.577 1.00 24.32  ? 441 ILE A CG2 1 
ATOM   3739  C CD1 . ILE A 1 441 ? 16.935  -11.741 -14.624 1.00 16.62  ? 441 ILE A CD1 1 
ATOM   3740  N N   . LEU A 1 442 ? 15.306  -12.895 -9.732  1.00 15.30  ? 442 LEU A N   1 
ATOM   3741  C CA  . LEU A 1 442 ? 14.425  -12.337 -8.711  1.00 16.16  ? 442 LEU A CA  1 
ATOM   3742  C C   . LEU A 1 442 ? 15.091  -11.179 -7.981  1.00 17.76  ? 442 LEU A C   1 
ATOM   3743  O O   . LEU A 1 442 ? 14.431  -10.192 -7.636  1.00 16.67  ? 442 LEU A O   1 
ATOM   3744  C CB  . LEU A 1 442 ? 14.010  -13.425 -7.720  1.00 15.61  ? 442 LEU A CB  1 
ATOM   3745  C CG  . LEU A 1 442 ? 13.058  -14.503 -8.242  1.00 16.15  ? 442 LEU A CG  1 
ATOM   3746  C CD1 . LEU A 1 442 ? 12.777  -15.542 -7.167  1.00 17.21  ? 442 LEU A CD1 1 
ATOM   3747  C CD2 . LEU A 1 442 ? 11.765  -13.874 -8.734  1.00 16.85  ? 442 LEU A CD2 1 
ATOM   3748  N N   . VAL A 1 443 ? 16.398  -11.287 -7.728  1.00 16.21  ? 443 VAL A N   1 
ATOM   3749  C CA  . VAL A 1 443 ? 17.122  -10.212 -7.057  1.00 15.35  ? 443 VAL A CA  1 
ATOM   3750  C C   . VAL A 1 443 ? 17.157  -8.964  -7.930  1.00 17.01  ? 443 VAL A C   1 
ATOM   3751  O O   . VAL A 1 443 ? 17.058  -7.837  -7.429  1.00 25.54  ? 443 VAL A O   1 
ATOM   3752  C CB  . VAL A 1 443 ? 18.541  -10.676 -6.678  1.00 16.19  ? 443 VAL A CB  1 
ATOM   3753  C CG1 . VAL A 1 443 ? 19.224  -9.639  -5.802  1.00 19.02  ? 443 VAL A CG1 1 
ATOM   3754  C CG2 . VAL A 1 443 ? 18.490  -12.023 -5.979  1.00 18.23  ? 443 VAL A CG2 1 
ATOM   3755  N N   . ALA A 1 444 ? 17.291  -9.143  -9.246  1.00 16.46  ? 444 ALA A N   1 
ATOM   3756  C CA  . ALA A 1 444 ? 17.346  -8.015  -10.168 1.00 15.54  ? 444 ALA A CA  1 
ATOM   3757  C C   . ALA A 1 444 ? 16.007  -7.308  -10.331 1.00 16.35  ? 444 ALA A C   1 
ATOM   3758  O O   . ALA A 1 444 ? 15.969  -6.221  -10.916 1.00 22.66  ? 444 ALA A O   1 
ATOM   3759  C CB  . ALA A 1 444 ? 17.853  -8.481  -11.533 1.00 15.28  ? 444 ALA A CB  1 
ATOM   3760  N N   . GLU A 1 445 ? 14.917  -7.886  -9.833  1.00 16.80  ? 445 GLU A N   1 
ATOM   3761  C CA  . GLU A 1 445 ? 13.602  -7.264  -9.902  1.00 16.46  ? 445 GLU A CA  1 
ATOM   3762  C C   . GLU A 1 445 ? 13.313  -6.360  -8.711  1.00 14.95  ? 445 GLU A C   1 
ATOM   3763  O O   . GLU A 1 445 ? 12.191  -5.864  -8.586  1.00 20.90  ? 445 GLU A O   1 
ATOM   3764  C CB  . GLU A 1 445 ? 12.515  -8.339  -10.017 1.00 23.67  ? 445 GLU A CB  1 
ATOM   3765  C CG  . GLU A 1 445 ? 12.698  -9.269  -11.204 1.00 18.02  ? 445 GLU A CG  1 
ATOM   3766  C CD  . GLU A 1 445 ? 11.660  -10.376 -11.261 1.00 17.49  ? 445 GLU A CD  1 
ATOM   3767  O OE1 . GLU A 1 445 ? 11.030  -10.661 -10.222 1.00 19.98  ? 445 GLU A OE1 1 
ATOM   3768  O OE2 . GLU A 1 445 ? 11.483  -10.970 -12.345 1.00 25.37  ? 445 GLU A OE2 1 
ATOM   3769  N N   . GLY A 1 446 ? 14.292  -6.143  -7.837  1.00 18.94  ? 446 GLY A N   1 
ATOM   3770  C CA  . GLY A 1 446 ? 14.086  -5.253  -6.708  1.00 17.46  ? 446 GLY A CA  1 
ATOM   3771  C C   . GLY A 1 446 ? 13.928  -3.807  -7.151  1.00 19.88  ? 446 GLY A C   1 
ATOM   3772  O O   . GLY A 1 446 ? 14.574  -3.346  -8.093  1.00 21.87  ? 446 GLY A O   1 
ATOM   3773  N N   . SER A 1 447 ? 13.060  -3.081  -6.443  1.00 17.65  ? 447 SER A N   1 
ATOM   3774  C CA  . SER A 1 447 ? 12.779  -1.695  -6.799  1.00 21.13  ? 447 SER A CA  1 
ATOM   3775  C C   . SER A 1 447 ? 13.992  -0.792  -6.625  1.00 19.62  ? 447 SER A C   1 
ATOM   3776  O O   . SER A 1 447 ? 14.084  0.240   -7.299  1.00 21.05  ? 447 SER A O   1 
ATOM   3777  C CB  . SER A 1 447 ? 11.615  -1.163  -5.959  1.00 21.53  ? 447 SER A CB  1 
ATOM   3778  O OG  . SER A 1 447 ? 11.852  -1.355  -4.575  1.00 25.50  ? 447 SER A OG  1 
ATOM   3779  N N   . ASP A 1 448 ? 14.927  -1.159  -5.747  1.00 19.65  ? 448 ASP A N   1 
ATOM   3780  C CA  . ASP A 1 448 ? 16.021  -0.262  -5.400  1.00 20.93  ? 448 ASP A CA  1 
ATOM   3781  C C   . ASP A 1 448 ? 16.986  -0.032  -6.556  1.00 20.79  ? 448 ASP A C   1 
ATOM   3782  O O   . ASP A 1 448 ? 17.651  1.008   -6.591  1.00 22.25  ? 448 ASP A O   1 
ATOM   3783  C CB  . ASP A 1 448 ? 16.772  -0.807  -4.185  1.00 21.28  ? 448 ASP A CB  1 
ATOM   3784  C CG  . ASP A 1 448 ? 15.855  -1.056  -3.004  1.00 23.49  ? 448 ASP A CG  1 
ATOM   3785  O OD1 . ASP A 1 448 ? 15.281  -2.163  -2.919  1.00 23.06  ? 448 ASP A OD1 1 
ATOM   3786  O OD2 . ASP A 1 448 ? 15.701  -0.143  -2.165  1.00 27.53  ? 448 ASP A OD2 1 
ATOM   3787  N N   . TRP A 1 449 ? 17.080  -0.966  -7.502  1.00 24.60  ? 449 TRP A N   1 
ATOM   3788  C CA  . TRP A 1 449 ? 17.987  -0.764  -8.628  1.00 23.63  ? 449 TRP A CA  1 
ATOM   3789  C C   . TRP A 1 449 ? 17.440  0.257   -9.616  1.00 22.07  ? 449 TRP A C   1 
ATOM   3790  O O   . TRP A 1 449 ? 18.216  0.935   -10.298 1.00 28.69  ? 449 TRP A O   1 
ATOM   3791  C CB  . TRP A 1 449 ? 18.265  -2.095  -9.326  1.00 20.27  ? 449 TRP A CB  1 
ATOM   3792  C CG  . TRP A 1 449 ? 18.476  -3.223  -8.368  1.00 20.13  ? 449 TRP A CG  1 
ATOM   3793  C CD1 . TRP A 1 449 ? 17.678  -4.316  -8.197  1.00 18.73  ? 449 TRP A CD1 1 
ATOM   3794  C CD2 . TRP A 1 449 ? 19.552  -3.362  -7.433  1.00 25.82  ? 449 TRP A CD2 1 
ATOM   3795  N NE1 . TRP A 1 449 ? 18.194  -5.132  -7.218  1.00 17.75  ? 449 TRP A NE1 1 
ATOM   3796  C CE2 . TRP A 1 449 ? 19.345  -4.568  -6.733  1.00 20.40  ? 449 TRP A CE2 1 
ATOM   3797  C CE3 . TRP A 1 449 ? 20.673  -2.586  -7.122  1.00 26.30  ? 449 TRP A CE3 1 
ATOM   3798  C CZ2 . TRP A 1 449 ? 20.215  -5.013  -5.742  1.00 19.49  ? 449 TRP A CZ2 1 
ATOM   3799  C CZ3 . TRP A 1 449 ? 21.536  -3.032  -6.138  1.00 25.60  ? 449 TRP A CZ3 1 
ATOM   3800  C CH2 . TRP A 1 449 ? 21.303  -4.234  -5.461  1.00 23.61  ? 449 TRP A CH2 1 
ATOM   3801  N N   . PHE A 1 450 ? 16.117  0.382   -9.705  1.00 20.27  ? 450 PHE A N   1 
ATOM   3802  C CA  . PHE A 1 450 ? 15.491  1.309   -10.638 1.00 21.36  ? 450 PHE A CA  1 
ATOM   3803  C C   . PHE A 1 450 ? 15.180  2.660   -10.011 1.00 23.25  ? 450 PHE A C   1 
ATOM   3804  O O   . PHE A 1 450 ? 14.965  3.635   -10.739 1.00 24.78  ? 450 PHE A O   1 
ATOM   3805  C CB  . PHE A 1 450 ? 14.213  0.686   -11.200 1.00 20.55  ? 450 PHE A CB  1 
ATOM   3806  C CG  . PHE A 1 450 ? 14.415  -0.700  -11.740 1.00 19.00  ? 450 PHE A CG  1 
ATOM   3807  C CD1 . PHE A 1 450 ? 14.849  -0.894  -13.039 1.00 19.15  ? 450 PHE A CD1 1 
ATOM   3808  C CD2 . PHE A 1 450 ? 14.199  -1.810  -10.942 1.00 17.77  ? 450 PHE A CD2 1 
ATOM   3809  C CE1 . PHE A 1 450 ? 15.047  -2.166  -13.535 1.00 18.12  ? 450 PHE A CE1 1 
ATOM   3810  C CE2 . PHE A 1 450 ? 14.397  -3.084  -11.432 1.00 19.73  ? 450 PHE A CE2 1 
ATOM   3811  C CZ  . PHE A 1 450 ? 14.823  -3.261  -12.732 1.00 19.44  ? 450 PHE A CZ  1 
ATOM   3812  N N   . TRP A 1 451 ? 15.144  2.735   -8.680  1.00 23.89  ? 451 TRP A N   1 
ATOM   3813  C CA  . TRP A 1 451 ? 14.998  4.019   -8.004  1.00 29.47  ? 451 TRP A CA  1 
ATOM   3814  C C   . TRP A 1 451 ? 16.224  4.897   -8.223  1.00 30.87  ? 451 TRP A C   1 
ATOM   3815  O O   . TRP A 1 451 ? 16.098  6.098   -8.490  1.00 29.50  ? 451 TRP A O   1 
ATOM   3816  C CB  . TRP A 1 451 ? 14.762  3.784   -6.508  1.00 28.64  ? 451 TRP A CB  1 
ATOM   3817  C CG  . TRP A 1 451 ? 14.343  5.000   -5.736  1.00 29.53  ? 451 TRP A CG  1 
ATOM   3818  C CD1 . TRP A 1 451 ? 13.074  5.327   -5.354  1.00 35.73  ? 451 TRP A CD1 1 
ATOM   3819  C CD2 . TRP A 1 451 ? 15.194  6.035   -5.225  1.00 34.63  ? 451 TRP A CD2 1 
ATOM   3820  N NE1 . TRP A 1 451 ? 13.079  6.507   -4.651  1.00 37.72  ? 451 TRP A NE1 1 
ATOM   3821  C CE2 . TRP A 1 451 ? 14.368  6.961   -4.556  1.00 34.35  ? 451 TRP A CE2 1 
ATOM   3822  C CE3 . TRP A 1 451 ? 16.572  6.272   -5.272  1.00 46.41  ? 451 TRP A CE3 1 
ATOM   3823  C CZ2 . TRP A 1 451 ? 14.874  8.105   -3.942  1.00 38.98  ? 451 TRP A CZ2 1 
ATOM   3824  C CZ3 . TRP A 1 451 ? 17.071  7.411   -4.662  1.00 47.75  ? 451 TRP A CZ3 1 
ATOM   3825  C CH2 . TRP A 1 451 ? 16.224  8.311   -4.006  1.00 40.99  ? 451 TRP A CH2 1 
ATOM   3826  N N   . TRP A 1 452 ? 17.416  4.305   -8.141  1.00 39.58  ? 452 TRP A N   1 
ATOM   3827  C CA  . TRP A 1 452 ? 18.674  5.037   -8.114  1.00 40.30  ? 452 TRP A CA  1 
ATOM   3828  C C   . TRP A 1 452 ? 19.203  5.367   -9.505  1.00 43.08  ? 452 TRP A C   1 
ATOM   3829  O O   . TRP A 1 452 ? 20.380  5.720   -9.636  1.00 53.95  ? 452 TRP A O   1 
ATOM   3830  C CB  . TRP A 1 452 ? 19.728  4.234   -7.344  1.00 43.72  ? 452 TRP A CB  1 
ATOM   3831  C CG  . TRP A 1 452 ? 19.511  4.200   -5.861  1.00 48.38  ? 452 TRP A CG  1 
ATOM   3832  C CD1 . TRP A 1 452 ? 18.907  3.209   -5.146  1.00 51.78  ? 452 TRP A CD1 1 
ATOM   3833  C CD2 . TRP A 1 452 ? 19.908  5.194   -4.910  1.00 50.93  ? 452 TRP A CD2 1 
ATOM   3834  N NE1 . TRP A 1 452 ? 18.895  3.525   -3.810  1.00 48.44  ? 452 TRP A NE1 1 
ATOM   3835  C CE2 . TRP A 1 452 ? 19.505  4.739   -3.638  1.00 48.31  ? 452 TRP A CE2 1 
ATOM   3836  C CE3 . TRP A 1 452 ? 20.562  6.423   -5.008  1.00 53.74  ? 452 TRP A CE3 1 
ATOM   3837  C CZ2 . TRP A 1 452 ? 19.735  5.470   -2.476  1.00 50.71  ? 452 TRP A CZ2 1 
ATOM   3838  C CZ3 . TRP A 1 452 ? 20.788  7.145   -3.852  1.00 60.35  ? 452 TRP A CZ3 1 
ATOM   3839  C CH2 . TRP A 1 452 ? 20.377  6.668   -2.605  1.00 48.37  ? 452 TRP A CH2 1 
ATOM   3840  N N   . GLN A 1 453 ? 18.376  5.260   -10.541 1.00 39.01  ? 453 GLN A N   1 
ATOM   3841  C CA  . GLN A 1 453 ? 18.852  5.448   -11.911 1.00 41.69  ? 453 GLN A CA  1 
ATOM   3842  C C   . GLN A 1 453 ? 18.697  6.910   -12.316 1.00 47.41  ? 453 GLN A C   1 
ATOM   3843  O O   . GLN A 1 453 ? 17.594  7.372   -12.621 1.00 45.95  ? 453 GLN A O   1 
ATOM   3844  C CB  . GLN A 1 453 ? 18.111  4.530   -12.879 1.00 40.50  ? 453 GLN A CB  1 
ATOM   3845  C CG  . GLN A 1 453 ? 19.020  3.597   -13.694 1.00 49.96  ? 453 GLN A CG  1 
ATOM   3846  C CD  . GLN A 1 453 ? 20.023  4.319   -14.602 1.00 62.42  ? 453 GLN A CD  1 
ATOM   3847  O OE1 . GLN A 1 453 ? 20.101  5.547   -14.634 1.00 68.79  ? 453 GLN A OE1 1 
ATOM   3848  N NE2 . GLN A 1 453 ? 20.797  3.539   -15.347 1.00 50.26  ? 453 GLN A NE2 1 
ATOM   3849  N N   . GLY A 1 454 ? 19.809  7.641   -12.294 1.00 55.87  ? 454 GLY A N   1 
ATOM   3850  C CA  . GLY A 1 454 ? 19.973  8.868   -13.053 1.00 68.18  ? 454 GLY A CA  1 
ATOM   3851  C C   . GLY A 1 454 ? 19.069  10.048  -12.755 1.00 77.56  ? 454 GLY A C   1 
ATOM   3852  O O   . GLY A 1 454 ? 19.023  10.992  -13.552 1.00 69.04  ? 454 GLY A O   1 
ATOM   3853  N N   . GLU A 1 455 ? 18.348  10.031  -11.633 1.00 75.89  ? 455 GLU A N   1 
ATOM   3854  C CA  . GLU A 1 455 ? 17.492  11.172  -11.322 1.00 81.34  ? 455 GLU A CA  1 
ATOM   3855  C C   . GLU A 1 455 ? 18.312  12.367  -10.846 1.00 82.76  ? 455 GLU A C   1 
ATOM   3856  O O   . GLU A 1 455 ? 18.058  13.506  -11.256 1.00 79.98  ? 455 GLU A O   1 
ATOM   3857  C CB  . GLU A 1 455 ? 16.446  10.782  -10.277 1.00 70.64  ? 455 GLU A CB  1 
ATOM   3858  C CG  . GLU A 1 455 ? 15.666  11.961  -9.698  1.00 80.25  ? 455 GLU A CG  1 
ATOM   3859  C CD  . GLU A 1 455 ? 14.657  12.554  -10.673 1.00 89.09  ? 455 GLU A CD  1 
ATOM   3860  O OE1 . GLU A 1 455 ? 15.070  13.059  -11.739 1.00 80.75  ? 455 GLU A OE1 1 
ATOM   3861  O OE2 . GLU A 1 455 ? 13.446  12.511  -10.373 1.00 78.42  ? 455 GLU A OE2 1 
ATOM   3862  N N   . GLU A 1 456 ? 19.303  12.122  -9.995  1.00 83.06  ? 456 GLU A N   1 
ATOM   3863  C CA  . GLU A 1 456 ? 20.186  13.161  -9.481  1.00 77.18  ? 456 GLU A CA  1 
ATOM   3864  C C   . GLU A 1 456 ? 21.387  12.469  -8.857  1.00 73.43  ? 456 GLU A C   1 
ATOM   3865  O O   . GLU A 1 456 ? 21.223  11.474  -8.146  1.00 78.54  ? 456 GLU A O   1 
ATOM   3866  C CB  . GLU A 1 456 ? 19.475  14.051  -8.454  1.00 74.96  ? 456 GLU A CB  1 
ATOM   3867  C CG  . GLU A 1 456 ? 20.343  15.142  -7.838  1.00 85.17  ? 456 GLU A CG  1 
ATOM   3868  C CD  . GLU A 1 456 ? 20.568  16.320  -8.772  1.00 84.97  ? 456 GLU A CD  1 
ATOM   3869  O OE1 . GLU A 1 456 ? 19.579  16.992  -9.135  1.00 68.05  ? 456 GLU A OE1 1 
ATOM   3870  O OE2 . GLU A 1 456 ? 21.735  16.583  -9.131  1.00 81.13  ? 456 GLU A OE2 1 
ATOM   3871  N N   . LYS A 1 457 ? 22.586  12.990  -9.133  1.00 58.38  ? 457 LYS A N   1 
ATOM   3872  C CA  . LYS A 1 457 ? 23.808  12.332  -8.687  1.00 66.06  ? 457 LYS A CA  1 
ATOM   3873  C C   . LYS A 1 457 ? 23.778  12.124  -7.179  1.00 65.76  ? 457 LYS A C   1 
ATOM   3874  O O   . LYS A 1 457 ? 23.619  13.076  -6.407  1.00 65.18  ? 457 LYS A O   1 
ATOM   3875  C CB  . LYS A 1 457 ? 25.040  13.139  -9.096  1.00 68.96  ? 457 LYS A CB  1 
ATOM   3876  C CG  . LYS A 1 457 ? 26.347  12.520  -8.616  1.00 70.04  ? 457 LYS A CG  1 
ATOM   3877  C CD  . LYS A 1 457 ? 27.429  12.580  -9.683  1.00 63.11  ? 457 LYS A CD  1 
ATOM   3878  C CE  . LYS A 1 457 ? 28.806  12.327  -9.088  1.00 67.74  ? 457 LYS A CE  1 
ATOM   3879  N NZ  . LYS A 1 457 ? 28.956  12.947  -7.743  1.00 60.58  ? 457 LYS A NZ  1 
ATOM   3880  N N   . ALA A 1 458 ? 23.940  10.876  -6.772  1.00 70.58  ? 458 ALA A N   1 
ATOM   3881  C CA  . ALA A 1 458 ? 23.624  10.385  -5.440  1.00 61.95  ? 458 ALA A CA  1 
ATOM   3882  C C   . ALA A 1 458 ? 24.783  9.537   -4.945  1.00 61.19  ? 458 ALA A C   1 
ATOM   3883  O O   . ALA A 1 458 ? 25.653  9.147   -5.730  1.00 64.01  ? 458 ALA A O   1 
ATOM   3884  C CB  . ALA A 1 458 ? 22.315  9.581   -5.509  1.00 47.65  ? 458 ALA A CB  1 
ATOM   3885  N N   . PRO A 1 459 ? 24.851  9.248   -3.640  1.00 58.62  ? 459 PRO A N   1 
ATOM   3886  C CA  . PRO A 1 459 ? 26.051  8.581   -3.118  1.00 48.31  ? 459 PRO A CA  1 
ATOM   3887  C C   . PRO A 1 459 ? 26.122  7.113   -3.511  1.00 45.28  ? 459 PRO A C   1 
ATOM   3888  O O   . PRO A 1 459 ? 25.133  6.378   -3.447  1.00 49.85  ? 459 PRO A O   1 
ATOM   3889  C CB  . PRO A 1 459 ? 25.922  8.740   -1.596  1.00 46.10  ? 459 PRO A CB  1 
ATOM   3890  C CG  . PRO A 1 459 ? 24.503  9.097   -1.329  1.00 52.78  ? 459 PRO A CG  1 
ATOM   3891  C CD  . PRO A 1 459 ? 23.782  9.301   -2.623  1.00 53.64  ? 459 PRO A CD  1 
ATOM   3892  N N   . PHE A 1 460 ? 27.323  6.697   -3.913  1.00 47.72  ? 460 PHE A N   1 
ATOM   3893  C CA  . PHE A 1 460 ? 27.622  5.307   -4.258  1.00 39.12  ? 460 PHE A CA  1 
ATOM   3894  C C   . PHE A 1 460 ? 26.666  4.775   -5.325  1.00 36.16  ? 460 PHE A C   1 
ATOM   3895  O O   . PHE A 1 460 ? 26.140  3.665   -5.224  1.00 36.94  ? 460 PHE A O   1 
ATOM   3896  C CB  . PHE A 1 460 ? 27.607  4.417   -3.014  1.00 38.53  ? 460 PHE A CB  1 
ATOM   3897  C CG  . PHE A 1 460 ? 28.569  4.846   -1.939  1.00 47.80  ? 460 PHE A CG  1 
ATOM   3898  C CD1 . PHE A 1 460 ? 28.190  5.772   -0.980  1.00 46.97  ? 460 PHE A CD1 1 
ATOM   3899  C CD2 . PHE A 1 460 ? 29.846  4.309   -1.879  1.00 49.63  ? 460 PHE A CD2 1 
ATOM   3900  C CE1 . PHE A 1 460 ? 29.071  6.166   0.014   1.00 47.04  ? 460 PHE A CE1 1 
ATOM   3901  C CE2 . PHE A 1 460 ? 30.734  4.699   -0.889  1.00 50.55  ? 460 PHE A CE2 1 
ATOM   3902  C CZ  . PHE A 1 460 ? 30.346  5.628   0.059   1.00 54.67  ? 460 PHE A CZ  1 
ATOM   3903  N N   . VAL A 1 461 ? 26.432  5.587   -6.357  1.00 45.50  ? 461 VAL A N   1 
ATOM   3904  C CA  . VAL A 1 461 ? 25.644  5.123   -7.495  1.00 40.53  ? 461 VAL A CA  1 
ATOM   3905  C C   . VAL A 1 461 ? 26.412  4.062   -8.274  1.00 40.49  ? 461 VAL A C   1 
ATOM   3906  O O   . VAL A 1 461 ? 25.829  3.086   -8.763  1.00 38.59  ? 461 VAL A O   1 
ATOM   3907  C CB  . VAL A 1 461 ? 25.238  6.309   -8.388  1.00 36.58  ? 461 VAL A CB  1 
ATOM   3908  C CG1 . VAL A 1 461 ? 24.756  5.820   -9.747  1.00 34.29  ? 461 VAL A CG1 1 
ATOM   3909  C CG2 . VAL A 1 461 ? 24.153  7.131   -7.710  1.00 36.51  ? 461 VAL A CG2 1 
ATOM   3910  N N   . GLU A 1 462 ? 27.734  4.227   -8.388  1.00 35.61  ? 462 GLU A N   1 
ATOM   3911  C CA  . GLU A 1 462 ? 28.556  3.242   -9.084  1.00 35.25  ? 462 GLU A CA  1 
ATOM   3912  C C   . GLU A 1 462 ? 28.414  1.855   -8.472  1.00 33.15  ? 462 GLU A C   1 
ATOM   3913  O O   . GLU A 1 462 ? 28.536  0.848   -9.179  1.00 32.01  ? 462 GLU A O   1 
ATOM   3914  C CB  . GLU A 1 462 ? 30.022  3.680   -9.063  1.00 42.15  ? 462 GLU A CB  1 
ATOM   3915  C CG  . GLU A 1 462 ? 30.269  5.070   -9.628  1.00 66.12  ? 462 GLU A CG  1 
ATOM   3916  C CD  . GLU A 1 462 ? 31.502  5.730   -9.038  1.00 88.52  ? 462 GLU A CD  1 
ATOM   3917  O OE1 . GLU A 1 462 ? 31.590  6.975   -9.080  1.00 97.54  ? 462 GLU A OE1 1 
ATOM   3918  O OE2 . GLU A 1 462 ? 32.383  5.006   -8.530  1.00 81.52  ? 462 GLU A OE2 1 
ATOM   3919  N N   . VAL A 1 463 ? 28.160  1.781   -7.165  1.00 32.97  ? 463 VAL A N   1 
ATOM   3920  C CA  . VAL A 1 463 ? 28.001  0.488   -6.508  1.00 31.37  ? 463 VAL A CA  1 
ATOM   3921  C C   . VAL A 1 463 ? 26.652  -0.135  -6.848  1.00 28.55  ? 463 VAL A C   1 
ATOM   3922  O O   . VAL A 1 463 ? 26.565  -1.337  -7.123  1.00 27.13  ? 463 VAL A O   1 
ATOM   3923  C CB  . VAL A 1 463 ? 28.194  0.640   -4.989  1.00 32.59  ? 463 VAL A CB  1 
ATOM   3924  C CG1 . VAL A 1 463 ? 27.738  -0.617  -4.269  1.00 30.97  ? 463 VAL A CG1 1 
ATOM   3925  C CG2 . VAL A 1 463 ? 29.651  0.945   -4.671  1.00 35.54  ? 463 VAL A CG2 1 
ATOM   3926  N N   . PHE A 1 464 ? 25.578  0.660   -6.835  1.00 28.04  ? 464 PHE A N   1 
ATOM   3927  C CA  . PHE A 1 464 ? 24.269  0.119   -7.185  1.00 25.73  ? 464 PHE A CA  1 
ATOM   3928  C C   . PHE A 1 464 ? 24.211  -0.304  -8.647  1.00 26.78  ? 464 PHE A C   1 
ATOM   3929  O O   . PHE A 1 464 ? 23.456  -1.219  -8.996  1.00 27.58  ? 464 PHE A O   1 
ATOM   3930  C CB  . PHE A 1 464 ? 23.169  1.137   -6.879  1.00 29.56  ? 464 PHE A CB  1 
ATOM   3931  C CG  . PHE A 1 464 ? 22.834  1.244   -5.418  1.00 29.30  ? 464 PHE A CG  1 
ATOM   3932  C CD1 . PHE A 1 464 ? 23.501  2.145   -4.604  1.00 35.48  ? 464 PHE A CD1 1 
ATOM   3933  C CD2 . PHE A 1 464 ? 21.862  0.432   -4.857  1.00 25.21  ? 464 PHE A CD2 1 
ATOM   3934  C CE1 . PHE A 1 464 ? 23.198  2.243   -3.259  1.00 33.94  ? 464 PHE A CE1 1 
ATOM   3935  C CE2 . PHE A 1 464 ? 21.557  0.523   -3.512  1.00 36.00  ? 464 PHE A CE2 1 
ATOM   3936  C CZ  . PHE A 1 464 ? 22.226  1.429   -2.712  1.00 37.77  ? 464 PHE A CZ  1 
ATOM   3937  N N   . ASP A 1 465 ? 24.988  0.350   -9.512  1.00 31.37  ? 465 ASP A N   1 
ATOM   3938  C CA  . ASP A 1 465 ? 25.096  -0.107  -10.893 1.00 26.81  ? 465 ASP A CA  1 
ATOM   3939  C C   . ASP A 1 465 ? 25.871  -1.416  -10.974 1.00 25.78  ? 465 ASP A C   1 
ATOM   3940  O O   . ASP A 1 465 ? 25.434  -2.369  -11.629 1.00 26.54  ? 465 ASP A O   1 
ATOM   3941  C CB  . ASP A 1 465 ? 25.761  0.968   -11.752 1.00 30.81  ? 465 ASP A CB  1 
ATOM   3942  C CG  . ASP A 1 465 ? 25.929  0.539   -13.194 1.00 36.51  ? 465 ASP A CG  1 
ATOM   3943  O OD1 . ASP A 1 465 ? 24.947  0.638   -13.961 1.00 30.78  ? 465 ASP A OD1 1 
ATOM   3944  O OD2 . ASP A 1 465 ? 27.044  0.108   -13.562 1.00 39.67  ? 465 ASP A OD2 1 
ATOM   3945  N N   . LYS A 1 466 ? 27.025  -1.484  -10.301 1.00 28.62  ? 466 LYS A N   1 
ATOM   3946  C CA  . LYS A 1 466 ? 27.842  -2.694  -10.340 1.00 27.51  ? 466 LYS A CA  1 
ATOM   3947  C C   . LYS A 1 466 ? 27.080  -3.894  -9.794  1.00 29.33  ? 466 LYS A C   1 
ATOM   3948  O O   . LYS A 1 466 ? 27.232  -5.015  -10.295 1.00 34.57  ? 466 LYS A O   1 
ATOM   3949  C CB  . LYS A 1 466 ? 29.138  -2.473  -9.555  1.00 29.77  ? 466 LYS A CB  1 
ATOM   3950  C CG  . LYS A 1 466 ? 30.007  -3.715  -9.414  1.00 34.36  ? 466 LYS A CG  1 
ATOM   3951  C CD  . LYS A 1 466 ? 31.463  -3.353  -9.160  1.00 42.42  ? 466 LYS A CD  1 
ATOM   3952  C CE  . LYS A 1 466 ? 32.387  -4.520  -9.475  1.00 44.85  ? 466 LYS A CE  1 
ATOM   3953  N NZ  . LYS A 1 466 ? 32.972  -5.123  -8.243  1.00 38.45  ? 466 LYS A NZ  1 
ATOM   3954  N N   . LEU A 1 467 ? 26.254  -3.680  -8.768  1.00 28.31  ? 467 LEU A N   1 
ATOM   3955  C CA  . LEU A 1 467 ? 25.511  -4.788  -8.176  1.00 22.98  ? 467 LEU A CA  1 
ATOM   3956  C C   . LEU A 1 467 ? 24.371  -5.247  -9.077  1.00 21.24  ? 467 LEU A C   1 
ATOM   3957  O O   . LEU A 1 467 ? 24.168  -6.454  -9.256  1.00 28.76  ? 467 LEU A O   1 
ATOM   3958  C CB  . LEU A 1 467 ? 24.983  -4.389  -6.798  1.00 22.90  ? 467 LEU A CB  1 
ATOM   3959  C CG  . LEU A 1 467 ? 25.942  -4.661  -5.636  1.00 24.48  ? 467 LEU A CG  1 
ATOM   3960  C CD1 . LEU A 1 467 ? 25.498  -3.933  -4.378  1.00 25.05  ? 467 LEU A CD1 1 
ATOM   3961  C CD2 . LEU A 1 467 ? 26.058  -6.155  -5.383  1.00 24.14  ? 467 LEU A CD2 1 
ATOM   3962  N N   . PHE A 1 468 ? 23.608  -4.308  -9.647  1.00 22.89  ? 468 PHE A N   1 
ATOM   3963  C CA  . PHE A 1 468 ? 22.481  -4.701  -10.490 1.00 22.22  ? 468 PHE A CA  1 
ATOM   3964  C C   . PHE A 1 468 ? 22.952  -5.443  -11.733 1.00 27.61  ? 468 PHE A C   1 
ATOM   3965  O O   . PHE A 1 468 ? 22.357  -6.455  -12.123 1.00 27.02  ? 468 PHE A O   1 
ATOM   3966  C CB  . PHE A 1 468 ? 21.647  -3.483  -10.885 1.00 25.39  ? 468 PHE A CB  1 
ATOM   3967  C CG  . PHE A 1 468 ? 20.560  -3.795  -11.881 1.00 30.23  ? 468 PHE A CG  1 
ATOM   3968  C CD1 . PHE A 1 468 ? 19.460  -4.551  -11.508 1.00 29.54  ? 468 PHE A CD1 1 
ATOM   3969  C CD2 . PHE A 1 468 ? 20.637  -3.335  -13.186 1.00 32.82  ? 468 PHE A CD2 1 
ATOM   3970  C CE1 . PHE A 1 468 ? 18.459  -4.844  -12.416 1.00 22.00  ? 468 PHE A CE1 1 
ATOM   3971  C CE2 . PHE A 1 468 ? 19.636  -3.624  -14.100 1.00 25.32  ? 468 PHE A CE2 1 
ATOM   3972  C CZ  . PHE A 1 468 ? 18.547  -4.379  -13.713 1.00 25.29  ? 468 PHE A CZ  1 
ATOM   3973  N N   . ARG A 1 469 ? 24.021  -4.960  -12.370 1.00 21.68  ? 469 ARG A N   1 
ATOM   3974  C CA  . ARG A 1 469 ? 24.581  -5.676  -13.508 1.00 22.21  ? 469 ARG A CA  1 
ATOM   3975  C C   . ARG A 1 469 ? 25.178  -7.017  -13.101 1.00 22.41  ? 469 ARG A C   1 
ATOM   3976  O O   . ARG A 1 469 ? 25.297  -7.910  -13.946 1.00 31.90  ? 469 ARG A O   1 
ATOM   3977  C CB  . ARG A 1 469 ? 25.630  -4.811  -14.206 1.00 24.28  ? 469 ARG A CB  1 
ATOM   3978  C CG  . ARG A 1 469 ? 25.120  -3.423  -14.548 1.00 26.16  ? 469 ARG A CG  1 
ATOM   3979  C CD  . ARG A 1 469 ? 26.099  -2.628  -15.388 1.00 26.98  ? 469 ARG A CD  1 
ATOM   3980  N NE  . ARG A 1 469 ? 25.445  -1.465  -15.975 1.00 28.64  ? 469 ARG A NE  1 
ATOM   3981  C CZ  . ARG A 1 469 ? 24.859  -1.457  -17.164 1.00 27.73  ? 469 ARG A CZ  1 
ATOM   3982  N NH1 . ARG A 1 469 ? 24.855  -2.529  -17.940 1.00 27.60  ? 469 ARG A NH1 1 
ATOM   3983  N NH2 . ARG A 1 469 ? 24.257  -0.347  -17.583 1.00 28.45  ? 469 ARG A NH2 1 
ATOM   3984  N N   . SER A 1 470 ? 25.550  -7.179  -11.830 1.00 23.23  ? 470 SER A N   1 
ATOM   3985  C CA  . SER A 1 470 ? 26.062  -8.464  -11.363 1.00 26.70  ? 470 SER A CA  1 
ATOM   3986  C C   . SER A 1 470 ? 24.956  -9.511  -11.298 1.00 22.19  ? 470 SER A C   1 
ATOM   3987  O O   . SER A 1 470 ? 25.098  -10.612 -11.843 1.00 34.17  ? 470 SER A O   1 
ATOM   3988  C CB  . SER A 1 470 ? 26.725  -8.299  -9.995  1.00 27.55  ? 470 SER A CB  1 
ATOM   3989  O OG  . SER A 1 470 ? 28.115  -8.061  -10.128 1.00 41.34  ? 470 SER A OG  1 
ATOM   3990  N N   . PHE A 1 471 ? 23.842  -9.185  -10.634 1.00 22.44  ? 471 PHE A N   1 
ATOM   3991  C CA  . PHE A 1 471 ? 22.745  -10.141 -10.515 1.00 25.06  ? 471 PHE A CA  1 
ATOM   3992  C C   . PHE A 1 471 ? 22.178  -10.497 -11.882 1.00 28.64  ? 471 PHE A C   1 
ATOM   3993  O O   . PHE A 1 471 ? 21.830  -11.656 -12.139 1.00 27.37  ? 471 PHE A O   1 
ATOM   3994  C CB  . PHE A 1 471 ? 21.645  -9.575  -9.616  1.00 17.65  ? 471 PHE A CB  1 
ATOM   3995  C CG  . PHE A 1 471 ? 22.112  -9.215  -8.236  1.00 20.47  ? 471 PHE A CG  1 
ATOM   3996  C CD1 . PHE A 1 471 ? 22.856  -10.108 -7.488  1.00 23.72  ? 471 PHE A CD1 1 
ATOM   3997  C CD2 . PHE A 1 471 ? 21.796  -7.985  -7.681  1.00 22.90  ? 471 PHE A CD2 1 
ATOM   3998  C CE1 . PHE A 1 471 ? 23.283  -9.782  -6.213  1.00 21.23  ? 471 PHE A CE1 1 
ATOM   3999  C CE2 . PHE A 1 471 ? 22.220  -7.654  -6.406  1.00 18.91  ? 471 PHE A CE2 1 
ATOM   4000  C CZ  . PHE A 1 471 ? 22.964  -8.553  -5.672  1.00 19.87  ? 471 PHE A CZ  1 
ATOM   4001  N N   . VAL A 1 472 ? 22.079  -9.507  -12.770 1.00 32.73  ? 472 VAL A N   1 
ATOM   4002  C CA  . VAL A 1 472 ? 21.562  -9.733  -14.116 1.00 26.67  ? 472 VAL A CA  1 
ATOM   4003  C C   . VAL A 1 472 ? 22.428  -10.736 -14.868 1.00 27.55  ? 472 VAL A C   1 
ATOM   4004  O O   . VAL A 1 472 ? 21.916  -11.642 -15.537 1.00 28.43  ? 472 VAL A O   1 
ATOM   4005  C CB  . VAL A 1 472 ? 21.457  -8.389  -14.861 1.00 28.08  ? 472 VAL A CB  1 
ATOM   4006  C CG1 . VAL A 1 472 ? 21.257  -8.604  -16.343 1.00 26.25  ? 472 VAL A CG1 1 
ATOM   4007  C CG2 . VAL A 1 472 ? 20.311  -7.565  -14.288 1.00 29.01  ? 472 VAL A CG2 1 
ATOM   4008  N N   . ARG A 1 473 ? 23.751  -10.598 -14.769 1.00 33.44  ? 473 ARG A N   1 
ATOM   4009  C CA  . ARG A 1 473 ? 24.644  -11.526 -15.455 1.00 36.00  ? 473 ARG A CA  1 
ATOM   4010  C C   . ARG A 1 473 ? 24.713  -12.873 -14.742 1.00 33.92  ? 473 ARG A C   1 
ATOM   4011  O O   . ARG A 1 473 ? 24.790  -13.920 -15.396 1.00 34.41  ? 473 ARG A O   1 
ATOM   4012  C CB  . ARG A 1 473 ? 26.038  -10.909 -15.584 1.00 38.34  ? 473 ARG A CB  1 
ATOM   4013  C CG  . ARG A 1 473 ? 26.482  -10.682 -17.021 1.00 43.27  ? 473 ARG A CG  1 
ATOM   4014  C CD  . ARG A 1 473 ? 25.422  -9.941  -17.828 1.00 43.14  ? 473 ARG A CD  1 
ATOM   4015  N NE  . ARG A 1 473 ? 25.207  -8.578  -17.355 1.00 56.64  ? 473 ARG A NE  1 
ATOM   4016  C CZ  . ARG A 1 473 ? 24.612  -7.627  -18.062 1.00 66.54  ? 473 ARG A CZ  1 
ATOM   4017  N NH1 . ARG A 1 473 ? 24.160  -7.855  -19.285 1.00 55.81  ? 473 ARG A NH1 1 
ATOM   4018  N NH2 . ARG A 1 473 ? 24.466  -6.416  -17.528 1.00 52.80  ? 473 ARG A NH2 1 
ATOM   4019  N N   . ARG A 1 474 ? 24.690  -12.867 -13.406 1.00 33.81  ? 474 ARG A N   1 
ATOM   4020  C CA  . ARG A 1 474 ? 24.691  -14.119 -12.653 1.00 34.96  ? 474 ARG A CA  1 
ATOM   4021  C C   . ARG A 1 474 ? 23.433  -14.937 -12.921 1.00 36.90  ? 474 ARG A C   1 
ATOM   4022  O O   . ARG A 1 474 ? 23.475  -16.173 -12.887 1.00 36.76  ? 474 ARG A O   1 
ATOM   4023  C CB  . ARG A 1 474 ? 24.834  -13.821 -11.159 1.00 30.05  ? 474 ARG A CB  1 
ATOM   4024  C CG  . ARG A 1 474 ? 24.721  -15.027 -10.233 1.00 25.74  ? 474 ARG A CG  1 
ATOM   4025  C CD  . ARG A 1 474 ? 25.935  -15.939 -10.306 1.00 35.14  ? 474 ARG A CD  1 
ATOM   4026  N NE  . ARG A 1 474 ? 25.671  -17.230 -9.681  1.00 34.98  ? 474 ARG A NE  1 
ATOM   4027  C CZ  . ARG A 1 474 ? 25.335  -18.330 -10.340 1.00 38.57  ? 474 ARG A CZ  1 
ATOM   4028  N NH1 . ARG A 1 474 ? 25.216  -18.338 -11.658 1.00 42.69  ? 474 ARG A NH1 1 
ATOM   4029  N NH2 . ARG A 1 474 ? 25.115  -19.452 -9.661  1.00 37.09  ? 474 ARG A NH2 1 
ATOM   4030  N N   . ALA A 1 475 ? 22.311  -14.270 -13.195 1.00 36.83  ? 475 ALA A N   1 
ATOM   4031  C CA  . ALA A 1 475 ? 21.060  -14.974 -13.447 1.00 27.60  ? 475 ALA A CA  1 
ATOM   4032  C C   . ALA A 1 475 ? 21.040  -15.673 -14.799 1.00 27.67  ? 475 ALA A C   1 
ATOM   4033  O O   . ALA A 1 475 ? 20.226  -16.581 -15.000 1.00 26.18  ? 475 ALA A O   1 
ATOM   4034  C CB  . ALA A 1 475 ? 19.885  -14.001 -13.354 1.00 25.12  ? 475 ALA A CB  1 
ATOM   4035  N N   . GLN A 1 476 ? 21.904  -15.272 -15.729 1.00 27.28  ? 476 GLN A N   1 
ATOM   4036  C CA  . GLN A 1 476 ? 21.954  -15.892 -17.045 1.00 35.07  ? 476 GLN A CA  1 
ATOM   4037  C C   . GLN A 1 476 ? 22.934  -17.055 -17.120 1.00 36.06  ? 476 GLN A C   1 
ATOM   4038  O O   . GLN A 1 476 ? 22.999  -17.724 -18.158 1.00 32.55  ? 476 GLN A O   1 
ATOM   4039  C CB  . GLN A 1 476 ? 22.307  -14.840 -18.101 1.00 35.54  ? 476 GLN A CB  1 
ATOM   4040  C CG  . GLN A 1 476 ? 21.346  -13.660 -18.111 1.00 29.21  ? 476 GLN A CG  1 
ATOM   4041  C CD  . GLN A 1 476 ? 21.759  -12.570 -19.077 1.00 40.49  ? 476 GLN A CD  1 
ATOM   4042  O OE1 . GLN A 1 476 ? 21.678  -12.739 -20.292 1.00 48.89  ? 476 GLN A OE1 1 
ATOM   4043  N NE2 . GLN A 1 476 ? 22.206  -11.441 -18.541 1.00 44.77  ? 476 GLN A NE2 1 
ATOM   4044  N N   . GLU A 1 477 ? 23.689  -17.309 -16.057 1.00 30.64  ? 477 GLU A N   1 
ATOM   4045  C CA  . GLU A 1 477 ? 24.558  -18.477 -15.992 1.00 29.67  ? 477 GLU A CA  1 
ATOM   4046  C C   . GLU A 1 477 ? 23.961  -19.529 -15.065 1.00 29.58  ? 477 GLU A C   1 
ATOM   4047  O O   . GLU A 1 477 ? 23.823  -20.693 -15.438 1.00 40.61  ? 477 GLU A O   1 
ATOM   4048  C CB  . GLU A 1 477 ? 25.957  -18.093 -15.514 1.00 30.77  ? 477 GLU A CB  1 
ATOM   4049  C CG  . GLU A 1 477 ? 26.402  -16.699 -15.915 1.00 45.46  ? 477 GLU A CG  1 
ATOM   4050  C CD  . GLU A 1 477 ? 27.712  -16.303 -15.265 1.00 58.78  ? 477 GLU A CD  1 
ATOM   4051  O OE1 . GLU A 1 477 ? 28.277  -17.128 -14.516 1.00 56.74  ? 477 GLU A OE1 1 
ATOM   4052  O OE2 . GLU A 1 477 ? 28.179  -15.168 -15.497 1.00 62.38  ? 477 GLU A OE2 1 
ATOM   4053  N N   . MET B 1 1   ? 16.502  34.548  44.435  1.00 46.09  ? 1   MET B N   1 
ATOM   4054  C CA  . MET B 1 1   ? 15.894  33.323  43.928  1.00 52.23  ? 1   MET B CA  1 
ATOM   4055  C C   . MET B 1 1   ? 15.435  33.491  42.482  1.00 35.84  ? 1   MET B C   1 
ATOM   4056  O O   . MET B 1 1   ? 14.911  34.541  42.102  1.00 41.23  ? 1   MET B O   1 
ATOM   4057  C CB  . MET B 1 1   ? 14.720  32.900  44.823  1.00 59.00  ? 1   MET B CB  1 
ATOM   4058  C CG  . MET B 1 1   ? 13.491  33.799  44.732  1.00 52.72  ? 1   MET B CG  1 
ATOM   4059  S SD  . MET B 1 1   ? 12.021  33.099  45.512  1.00 64.64  ? 1   MET B SD  1 
ATOM   4060  C CE  . MET B 1 1   ? 12.303  31.347  45.273  1.00 56.41  ? 1   MET B CE  1 
ATOM   4061  N N   . LYS B 1 2   ? 15.659  32.459  41.671  1.00 33.08  ? 2   LYS B N   1 
ATOM   4062  C CA  . LYS B 1 2   ? 15.164  32.474  40.303  1.00 27.11  ? 2   LYS B CA  1 
ATOM   4063  C C   . LYS B 1 2   ? 13.643  32.438  40.309  1.00 26.87  ? 2   LYS B C   1 
ATOM   4064  O O   . LYS B 1 2   ? 13.026  31.666  41.046  1.00 35.27  ? 2   LYS B O   1 
ATOM   4065  C CB  . LYS B 1 2   ? 15.721  31.289  39.515  1.00 27.21  ? 2   LYS B CB  1 
ATOM   4066  C CG  . LYS B 1 2   ? 15.702  31.490  38.006  1.00 25.83  ? 2   LYS B CG  1 
ATOM   4067  C CD  . LYS B 1 2   ? 15.178  30.265  37.275  1.00 34.26  ? 2   LYS B CD  1 
ATOM   4068  C CE  . LYS B 1 2   ? 16.254  29.201  37.134  1.00 38.54  ? 2   LYS B CE  1 
ATOM   4069  N NZ  . LYS B 1 2   ? 15.735  27.966  36.485  1.00 30.83  ? 2   LYS B NZ  1 
ATOM   4070  N N   . LYS B 1 3   ? 13.038  33.286  39.487  1.00 29.08  ? 3   LYS B N   1 
ATOM   4071  C CA  . LYS B 1 3   ? 11.597  33.471  39.479  1.00 24.25  ? 3   LYS B CA  1 
ATOM   4072  C C   . LYS B 1 3   ? 11.024  33.044  38.134  1.00 22.97  ? 3   LYS B C   1 
ATOM   4073  O O   . LYS B 1 3   ? 11.751  32.727  37.190  1.00 30.22  ? 3   LYS B O   1 
ATOM   4074  C CB  . LYS B 1 3   ? 11.234  34.932  39.765  1.00 23.82  ? 3   LYS B CB  1 
ATOM   4075  C CG  . LYS B 1 3   ? 11.399  35.337  41.217  1.00 26.86  ? 3   LYS B CG  1 
ATOM   4076  C CD  . LYS B 1 3   ? 10.841  36.727  41.469  1.00 31.39  ? 3   LYS B CD  1 
ATOM   4077  C CE  . LYS B 1 3   ? 10.682  36.998  42.955  1.00 35.96  ? 3   LYS B CE  1 
ATOM   4078  N NZ  . LYS B 1 3   ? 10.114  38.350  43.210  1.00 46.80  ? 3   LYS B NZ  1 
ATOM   4079  N N   . LEU B 1 4   ? 9.696   33.030  38.063  1.00 22.42  ? 4   LEU B N   1 
ATOM   4080  C CA  . LEU B 1 4   ? 8.971   32.881  36.809  1.00 21.17  ? 4   LEU B CA  1 
ATOM   4081  C C   . LEU B 1 4   ? 8.040   34.075  36.670  1.00 23.89  ? 4   LEU B C   1 
ATOM   4082  O O   . LEU B 1 4   ? 7.211   34.324  37.551  1.00 28.06  ? 4   LEU B O   1 
ATOM   4083  C CB  . LEU B 1 4   ? 8.186   31.568  36.758  1.00 21.52  ? 4   LEU B CB  1 
ATOM   4084  C CG  . LEU B 1 4   ? 7.339   31.371  35.496  1.00 20.39  ? 4   LEU B CG  1 
ATOM   4085  C CD1 . LEU B 1 4   ? 7.524   29.970  34.940  1.00 22.23  ? 4   LEU B CD1 1 
ATOM   4086  C CD2 . LEU B 1 4   ? 5.863   31.653  35.756  1.00 20.01  ? 4   LEU B CD2 1 
ATOM   4087  N N   . PHE B 1 5   ? 8.182   34.810  35.572  1.00 21.28  ? 5   PHE B N   1 
ATOM   4088  C CA  . PHE B 1 5   ? 7.401   36.018  35.337  1.00 18.35  ? 5   PHE B CA  1 
ATOM   4089  C C   . PHE B 1 5   ? 6.180   35.649  34.504  1.00 19.35  ? 5   PHE B C   1 
ATOM   4090  O O   . PHE B 1 5   ? 6.290   35.402  33.298  1.00 17.96  ? 5   PHE B O   1 
ATOM   4091  C CB  . PHE B 1 5   ? 8.258   37.077  34.650  1.00 20.31  ? 5   PHE B CB  1 
ATOM   4092  C CG  . PHE B 1 5   ? 9.386   37.583  35.505  1.00 18.72  ? 5   PHE B CG  1 
ATOM   4093  C CD1 . PHE B 1 5   ? 9.142   38.054  36.782  1.00 19.54  ? 5   PHE B CD1 1 
ATOM   4094  C CD2 . PHE B 1 5   ? 10.688  37.579  35.033  1.00 18.84  ? 5   PHE B CD2 1 
ATOM   4095  C CE1 . PHE B 1 5   ? 10.174  38.516  37.572  1.00 20.49  ? 5   PHE B CE1 1 
ATOM   4096  C CE2 . PHE B 1 5   ? 11.723  38.041  35.821  1.00 20.51  ? 5   PHE B CE2 1 
ATOM   4097  C CZ  . PHE B 1 5   ? 11.466  38.510  37.091  1.00 20.57  ? 5   PHE B CZ  1 
ATOM   4098  N N   . LEU B 1 6   ? 5.018   35.605  35.152  1.00 22.15  ? 6   LEU B N   1 
ATOM   4099  C CA  . LEU B 1 6   ? 3.775   35.181  34.524  1.00 21.11  ? 6   LEU B CA  1 
ATOM   4100  C C   . LEU B 1 6   ? 2.951   36.406  34.147  1.00 16.31  ? 6   LEU B C   1 
ATOM   4101  O O   . LEU B 1 6   ? 2.721   37.286  34.981  1.00 17.37  ? 6   LEU B O   1 
ATOM   4102  C CB  . LEU B 1 6   ? 2.984   34.275  35.466  1.00 17.93  ? 6   LEU B CB  1 
ATOM   4103  C CG  . LEU B 1 6   ? 1.697   33.668  34.915  1.00 17.54  ? 6   LEU B CG  1 
ATOM   4104  C CD1 . LEU B 1 6   ? 2.006   32.713  33.775  1.00 17.26  ? 6   LEU B CD1 1 
ATOM   4105  C CD2 . LEU B 1 6   ? 0.943   32.958  36.023  1.00 18.53  ? 6   LEU B CD2 1 
ATOM   4106  N N   . VAL B 1 7   ? 2.516   36.468  32.891  1.00 15.43  ? 7   VAL B N   1 
ATOM   4107  C CA  . VAL B 1 7   ? 1.760   37.605  32.381  1.00 14.74  ? 7   VAL B CA  1 
ATOM   4108  C C   . VAL B 1 7   ? 0.468   37.088  31.763  1.00 15.78  ? 7   VAL B C   1 
ATOM   4109  O O   . VAL B 1 7   ? 0.501   36.349  30.773  1.00 15.26  ? 7   VAL B O   1 
ATOM   4110  C CB  . VAL B 1 7   ? 2.565   38.417  31.354  1.00 14.19  ? 7   VAL B CB  1 
ATOM   4111  C CG1 . VAL B 1 7   ? 1.771   39.630  30.900  1.00 13.68  ? 7   VAL B CG1 1 
ATOM   4112  C CG2 . VAL B 1 7   ? 3.904   38.843  31.942  1.00 14.70  ? 7   VAL B CG2 1 
ATOM   4113  N N   . PHE B 1 8   ? -0.665  37.475  32.348  1.00 14.41  ? 8   PHE B N   1 
ATOM   4114  C CA  . PHE B 1 8   ? -1.979  37.201  31.781  1.00 14.04  ? 8   PHE B CA  1 
ATOM   4115  C C   . PHE B 1 8   ? -2.410  38.376  30.916  1.00 16.67  ? 8   PHE B C   1 
ATOM   4116  O O   . PHE B 1 8   ? -2.098  39.530  31.223  1.00 13.38  ? 8   PHE B O   1 
ATOM   4117  C CB  . PHE B 1 8   ? -3.014  36.969  32.882  1.00 14.62  ? 8   PHE B CB  1 
ATOM   4118  C CG  . PHE B 1 8   ? -2.845  35.676  33.622  1.00 15.43  ? 8   PHE B CG  1 
ATOM   4119  C CD1 . PHE B 1 8   ? -3.208  34.474  33.039  1.00 17.62  ? 8   PHE B CD1 1 
ATOM   4120  C CD2 . PHE B 1 8   ? -2.330  35.665  34.906  1.00 16.31  ? 8   PHE B CD2 1 
ATOM   4121  C CE1 . PHE B 1 8   ? -3.057  33.283  33.728  1.00 23.19  ? 8   PHE B CE1 1 
ATOM   4122  C CE2 . PHE B 1 8   ? -2.178  34.482  35.598  1.00 17.21  ? 8   PHE B CE2 1 
ATOM   4123  C CZ  . PHE B 1 8   ? -2.540  33.288  35.009  1.00 17.24  ? 8   PHE B CZ  1 
ATOM   4124  N N   . TRP B 1 9   ? -3.124  38.080  29.827  1.00 12.89  ? 9   TRP B N   1 
ATOM   4125  C CA  . TRP B 1 9   ? -3.536  39.135  28.898  1.00 12.36  ? 9   TRP B CA  1 
ATOM   4126  C C   . TRP B 1 9   ? -4.834  38.690  28.221  1.00 16.57  ? 9   TRP B C   1 
ATOM   4127  O O   . TRP B 1 9   ? -4.808  37.994  27.205  1.00 17.96  ? 9   TRP B O   1 
ATOM   4128  C CB  . TRP B 1 9   ? -2.435  39.418  27.887  1.00 12.06  ? 9   TRP B CB  1 
ATOM   4129  C CG  . TRP B 1 9   ? -2.580  40.709  27.164  1.00 12.60  ? 9   TRP B CG  1 
ATOM   4130  C CD1 . TRP B 1 9   ? -3.601  41.604  27.274  1.00 18.79  ? 9   TRP B CD1 1 
ATOM   4131  C CD2 . TRP B 1 9   ? -1.661  41.261  26.217  1.00 17.47  ? 9   TRP B CD2 1 
ATOM   4132  N NE1 . TRP B 1 9   ? -3.378  42.680  26.446  1.00 20.57  ? 9   TRP B NE1 1 
ATOM   4133  C CE2 . TRP B 1 9   ? -2.191  42.492  25.787  1.00 17.68  ? 9   TRP B CE2 1 
ATOM   4134  C CE3 . TRP B 1 9   ? -0.441  40.832  25.687  1.00 15.28  ? 9   TRP B CE3 1 
ATOM   4135  C CZ2 . TRP B 1 9   ? -1.543  43.296  24.855  1.00 11.65  ? 9   TRP B CZ2 1 
ATOM   4136  C CZ3 . TRP B 1 9   ? 0.199   41.636  24.764  1.00 11.54  ? 9   TRP B CZ3 1 
ATOM   4137  C CH2 . TRP B 1 9   ? -0.354  42.851  24.357  1.00 15.27  ? 9   TRP B CH2 1 
ATOM   4138  N N   . TRP B 1 10  ? -5.962  39.121  28.784  1.00 17.40  ? 10  TRP B N   1 
ATOM   4139  C CA  . TRP B 1 10  ? -7.275  38.698  28.309  1.00 15.43  ? 10  TRP B CA  1 
ATOM   4140  C C   . TRP B 1 10  ? -7.750  39.598  27.175  1.00 15.08  ? 10  TRP B C   1 
ATOM   4141  O O   . TRP B 1 10  ? -7.695  40.827  27.282  1.00 15.59  ? 10  TRP B O   1 
ATOM   4142  C CB  . TRP B 1 10  ? -8.297  38.713  29.446  1.00 17.19  ? 10  TRP B CB  1 
ATOM   4143  C CG  . TRP B 1 10  ? -7.841  38.012  30.687  1.00 13.26  ? 10  TRP B CG  1 
ATOM   4144  C CD1 . TRP B 1 10  ? -7.284  38.582  31.792  1.00 13.68  ? 10  TRP B CD1 1 
ATOM   4145  C CD2 . TRP B 1 10  ? -7.902  36.606  30.947  1.00 13.74  ? 10  TRP B CD2 1 
ATOM   4146  N NE1 . TRP B 1 10  ? -6.997  37.618  32.728  1.00 14.34  ? 10  TRP B NE1 1 
ATOM   4147  C CE2 . TRP B 1 10  ? -7.365  36.395  32.232  1.00 15.17  ? 10  TRP B CE2 1 
ATOM   4148  C CE3 . TRP B 1 10  ? -8.358  35.504  30.218  1.00 16.96  ? 10  TRP B CE3 1 
ATOM   4149  C CZ2 . TRP B 1 10  ? -7.272  35.128  32.804  1.00 15.52  ? 10  TRP B CZ2 1 
ATOM   4150  C CZ3 . TRP B 1 10  ? -8.265  34.246  30.787  1.00 21.73  ? 10  TRP B CZ3 1 
ATOM   4151  C CH2 . TRP B 1 10  ? -7.727  34.069  32.067  1.00 21.98  ? 10  TRP B CH2 1 
ATOM   4152  N N   . HIS B 1 11  ? -8.230  38.979  26.098  1.00 15.16  ? 11  HIS B N   1 
ATOM   4153  C CA  . HIS B 1 11  ? -8.721  39.691  24.926  1.00 11.46  ? 11  HIS B CA  1 
ATOM   4154  C C   . HIS B 1 11  ? -10.240 39.793  24.998  1.00 15.18  ? 11  HIS B C   1 
ATOM   4155  O O   . HIS B 1 11  ? -10.934 38.772  24.980  1.00 18.28  ? 11  HIS B O   1 
ATOM   4156  C CB  . HIS B 1 11  ? -8.291  38.978  23.644  1.00 12.22  ? 11  HIS B CB  1 
ATOM   4157  C CG  . HIS B 1 11  ? -8.790  39.630  22.393  1.00 15.42  ? 11  HIS B CG  1 
ATOM   4158  N ND1 . HIS B 1 11  ? -8.761  40.994  22.204  1.00 19.44  ? 11  HIS B ND1 1 
ATOM   4159  C CD2 . HIS B 1 11  ? -9.325  39.105  21.266  1.00 18.65  ? 11  HIS B CD2 1 
ATOM   4160  C CE1 . HIS B 1 11  ? -9.257  41.284  21.015  1.00 17.35  ? 11  HIS B CE1 1 
ATOM   4161  N NE2 . HIS B 1 11  ? -9.607  40.155  20.424  1.00 20.30  ? 11  HIS B NE2 1 
ATOM   4162  N N   . MET B 1 12  ? -10.748 41.021  25.078  1.00 13.71  ? 12  MET B N   1 
ATOM   4163  C CA  . MET B 1 12  ? -12.180 41.297  25.096  1.00 11.83  ? 12  MET B CA  1 
ATOM   4164  C C   . MET B 1 12  ? -12.570 41.932  23.772  1.00 11.79  ? 12  MET B C   1 
ATOM   4165  O O   . MET B 1 12  ? -12.111 43.034  23.455  1.00 12.85  ? 12  MET B O   1 
ATOM   4166  C CB  . MET B 1 12  ? -12.544 42.222  26.255  1.00 12.10  ? 12  MET B CB  1 
ATOM   4167  C CG  . MET B 1 12  ? -11.941 41.799  27.566  1.00 12.29  ? 12  MET B CG  1 
ATOM   4168  S SD  . MET B 1 12  ? -12.373 40.089  27.916  1.00 21.71  ? 12  MET B SD  1 
ATOM   4169  C CE  . MET B 1 12  ? -12.273 40.089  29.698  1.00 13.07  ? 12  MET B CE  1 
ATOM   4170  N N   . HIS B 1 13  ? -13.414 41.248  23.002  1.00 13.86  ? 13  HIS B N   1 
ATOM   4171  C CA  . HIS B 1 13  ? -13.815 41.788  21.714  1.00 14.10  ? 13  HIS B CA  1 
ATOM   4172  C C   . HIS B 1 13  ? -15.201 41.290  21.326  1.00 22.87  ? 13  HIS B C   1 
ATOM   4173  O O   . HIS B 1 13  ? -15.623 40.192  21.705  1.00 17.73  ? 13  HIS B O   1 
ATOM   4174  C CB  . HIS B 1 13  ? -12.807 41.433  20.615  1.00 11.94  ? 13  HIS B CB  1 
ATOM   4175  C CG  . HIS B 1 13  ? -13.296 41.748  19.238  1.00 12.26  ? 13  HIS B CG  1 
ATOM   4176  N ND1 . HIS B 1 13  ? -13.655 43.022  18.854  1.00 12.49  ? 13  HIS B ND1 1 
ATOM   4177  C CD2 . HIS B 1 13  ? -13.510 40.956  18.162  1.00 12.56  ? 13  HIS B CD2 1 
ATOM   4178  C CE1 . HIS B 1 13  ? -14.062 43.002  17.598  1.00 13.44  ? 13  HIS B CE1 1 
ATOM   4179  N NE2 . HIS B 1 13  ? -13.981 41.761  17.154  1.00 17.13  ? 13  HIS B NE2 1 
ATOM   4180  N N   . GLN B 1 14  ? -15.894 42.120  20.542  1.00 24.29  ? 14  GLN B N   1 
ATOM   4181  C CA  . GLN B 1 14  ? -17.228 41.879  20.014  1.00 16.80  ? 14  GLN B CA  1 
ATOM   4182  C C   . GLN B 1 14  ? -17.415 42.692  18.738  1.00 13.41  ? 14  GLN B C   1 
ATOM   4183  O O   . GLN B 1 14  ? -17.246 43.918  18.761  1.00 20.99  ? 14  GLN B O   1 
ATOM   4184  C CB  . GLN B 1 14  ? -18.287 42.265  21.044  1.00 20.62  ? 14  GLN B CB  1 
ATOM   4185  C CG  . GLN B 1 14  ? -19.450 41.308  21.134  1.00 20.81  ? 14  GLN B CG  1 
ATOM   4186  C CD  . GLN B 1 14  ? -19.060 39.990  21.757  1.00 15.57  ? 14  GLN B CD  1 
ATOM   4187  O OE1 . GLN B 1 14  ? -18.586 39.944  22.892  1.00 22.75  ? 14  GLN B OE1 1 
ATOM   4188  N NE2 . GLN B 1 14  ? -19.261 38.904  21.021  1.00 22.89  ? 14  GLN B NE2 1 
ATOM   4189  N N   . PRO B 1 15  ? -17.759 42.067  17.615  1.00 13.78  ? 15  PRO B N   1 
ATOM   4190  C CA  . PRO B 1 15  ? -18.031 42.840  16.398  1.00 14.62  ? 15  PRO B CA  1 
ATOM   4191  C C   . PRO B 1 15  ? -19.318 43.640  16.536  1.00 17.51  ? 15  PRO B C   1 
ATOM   4192  O O   . PRO B 1 15  ? -20.119 43.444  17.452  1.00 24.66  ? 15  PRO B O   1 
ATOM   4193  C CB  . PRO B 1 15  ? -18.141 41.769  15.309  1.00 14.74  ? 15  PRO B CB  1 
ATOM   4194  C CG  . PRO B 1 15  ? -18.587 40.558  16.031  1.00 14.59  ? 15  PRO B CG  1 
ATOM   4195  C CD  . PRO B 1 15  ? -17.976 40.625  17.410  1.00 18.00  ? 15  PRO B CD  1 
ATOM   4196  N N   . LEU B 1 16  ? -19.502 44.569  15.603  1.00 21.39  ? 16  LEU B N   1 
ATOM   4197  C CA  . LEU B 1 16  ? -20.631 45.496  15.645  1.00 15.90  ? 16  LEU B CA  1 
ATOM   4198  C C   . LEU B 1 16  ? -21.894 44.770  15.203  1.00 16.42  ? 16  LEU B C   1 
ATOM   4199  O O   . LEU B 1 16  ? -22.136 44.590  14.008  1.00 20.71  ? 16  LEU B O   1 
ATOM   4200  C CB  . LEU B 1 16  ? -20.359 46.711  14.766  1.00 16.50  ? 16  LEU B CB  1 
ATOM   4201  C CG  . LEU B 1 16  ? -21.371 47.852  14.876  1.00 18.32  ? 16  LEU B CG  1 
ATOM   4202  C CD1 . LEU B 1 16  ? -21.600 48.228  16.334  1.00 18.35  ? 16  LEU B CD1 1 
ATOM   4203  C CD2 . LEU B 1 16  ? -20.913 49.062  14.070  1.00 17.88  ? 16  LEU B CD2 1 
ATOM   4204  N N   . TYR B 1 17  ? -22.714 44.359  16.170  1.00 20.33  ? 17  TYR B N   1 
ATOM   4205  C CA  . TYR B 1 17  ? -24.007 43.747  15.883  1.00 17.13  ? 17  TYR B CA  1 
ATOM   4206  C C   . TYR B 1 17  ? -25.091 44.774  15.594  1.00 17.62  ? 17  TYR B C   1 
ATOM   4207  O O   . TYR B 1 17  ? -26.233 44.387  15.325  1.00 18.22  ? 17  TYR B O   1 
ATOM   4208  C CB  . TYR B 1 17  ? -24.455 42.871  17.055  1.00 18.90  ? 17  TYR B CB  1 
ATOM   4209  C CG  . TYR B 1 17  ? -23.471 41.801  17.464  1.00 18.68  ? 17  TYR B CG  1 
ATOM   4210  C CD1 . TYR B 1 17  ? -22.877 40.972  16.521  1.00 16.72  ? 17  TYR B CD1 1 
ATOM   4211  C CD2 . TYR B 1 17  ? -23.142 41.617  18.800  1.00 18.18  ? 17  TYR B CD2 1 
ATOM   4212  C CE1 . TYR B 1 17  ? -21.979 39.989  16.900  1.00 21.74  ? 17  TYR B CE1 1 
ATOM   4213  C CE2 . TYR B 1 17  ? -22.248 40.640  19.187  1.00 21.58  ? 17  TYR B CE2 1 
ATOM   4214  C CZ  . TYR B 1 17  ? -21.668 39.829  18.235  1.00 21.01  ? 17  TYR B CZ  1 
ATOM   4215  O OH  . TYR B 1 17  ? -20.775 38.855  18.624  1.00 17.10  ? 17  TYR B OH  1 
ATOM   4216  N N   . ARG B 1 18  ? -24.767 46.062  15.653  1.00 18.16  ? 18  ARG B N   1 
ATOM   4217  C CA  . ARG B 1 18  ? -25.760 47.116  15.510  1.00 18.57  ? 18  ARG B CA  1 
ATOM   4218  C C   . ARG B 1 18  ? -26.020 47.389  14.032  1.00 19.48  ? 18  ARG B C   1 
ATOM   4219  O O   . ARG B 1 18  ? -25.119 47.823  13.306  1.00 19.59  ? 18  ARG B O   1 
ATOM   4220  C CB  . ARG B 1 18  ? -25.279 48.376  16.222  1.00 19.20  ? 18  ARG B CB  1 
ATOM   4221  C CG  . ARG B 1 18  ? -26.291 49.491  16.258  1.00 23.44  ? 18  ARG B CG  1 
ATOM   4222  C CD  . ARG B 1 18  ? -25.729 50.699  16.978  1.00 19.48  ? 18  ARG B CD  1 
ATOM   4223  N NE  . ARG B 1 18  ? -26.567 51.870  16.767  1.00 20.61  ? 18  ARG B NE  1 
ATOM   4224  C CZ  . ARG B 1 18  ? -26.570 52.595  15.657  1.00 26.62  ? 18  ARG B CZ  1 
ATOM   4225  N NH1 . ARG B 1 18  ? -25.759 52.317  14.649  1.00 25.05  ? 18  ARG B NH1 1 
ATOM   4226  N NH2 . ARG B 1 18  ? -27.409 53.623  15.555  1.00 37.49  ? 18  ARG B NH2 1 
ATOM   4227  N N   . GLU B 1 19  ? -27.249 47.144  13.594  1.00 25.12  ? 19  GLU B N   1 
ATOM   4228  C CA  . GLU B 1 19  ? -27.595 47.301  12.185  1.00 21.81  ? 19  GLU B CA  1 
ATOM   4229  C C   . GLU B 1 19  ? -27.477 48.765  11.775  1.00 26.89  ? 19  GLU B C   1 
ATOM   4230  O O   . GLU B 1 19  ? -28.002 49.642  12.470  1.00 28.48  ? 19  GLU B O   1 
ATOM   4231  C CB  . GLU B 1 19  ? -29.011 46.793  11.929  1.00 25.83  ? 19  GLU B CB  1 
ATOM   4232  C CG  . GLU B 1 19  ? -29.193 46.081  10.597  1.00 32.11  ? 19  GLU B CG  1 
ATOM   4233  C CD  . GLU B 1 19  ? -29.795 46.980  9.534   1.00 41.87  ? 19  GLU B CD  1 
ATOM   4234  O OE1 . GLU B 1 19  ? -30.393 48.011  9.901   1.00 39.33  ? 19  GLU B OE1 1 
ATOM   4235  O OE2 . GLU B 1 19  ? -29.677 46.653  8.334   1.00 44.07  ? 19  GLU B OE2 1 
ATOM   4236  N N   . PRO B 1 20  ? -26.800 49.071  10.663  1.00 31.18  ? 20  PRO B N   1 
ATOM   4237  C CA  . PRO B 1 20  ? -26.573 50.486  10.314  1.00 26.73  ? 20  PRO B CA  1 
ATOM   4238  C C   . PRO B 1 20  ? -27.846 51.267  10.030  1.00 33.70  ? 20  PRO B C   1 
ATOM   4239  O O   . PRO B 1 20  ? -27.944 52.439  10.412  1.00 40.36  ? 20  PRO B O   1 
ATOM   4240  C CB  . PRO B 1 20  ? -25.674 50.406  9.072   1.00 25.98  ? 20  PRO B CB  1 
ATOM   4241  C CG  . PRO B 1 20  ? -25.836 49.030  8.537   1.00 30.63  ? 20  PRO B CG  1 
ATOM   4242  C CD  . PRO B 1 20  ? -26.301 48.136  9.641   1.00 31.60  ? 20  PRO B CD  1 
ATOM   4243  N N   . TYR B 1 21  ? -28.830 50.651  9.375   1.00 33.04  ? 21  TYR B N   1 
ATOM   4244  C CA  . TYR B 1 21  ? -30.010 51.397  8.950   1.00 31.50  ? 21  TYR B CA  1 
ATOM   4245  C C   . TYR B 1 21  ? -31.002 51.589  10.092  1.00 32.01  ? 21  TYR B C   1 
ATOM   4246  O O   . TYR B 1 21  ? -31.445 52.713  10.355  1.00 38.34  ? 21  TYR B O   1 
ATOM   4247  C CB  . TYR B 1 21  ? -30.673 50.690  7.765   1.00 27.77  ? 21  TYR B CB  1 
ATOM   4248  C CG  . TYR B 1 21  ? -29.820 50.700  6.515   1.00 30.96  ? 21  TYR B CG  1 
ATOM   4249  C CD1 . TYR B 1 21  ? -29.717 51.841  5.731   1.00 34.07  ? 21  TYR B CD1 1 
ATOM   4250  C CD2 . TYR B 1 21  ? -29.108 49.573  6.126   1.00 40.76  ? 21  TYR B CD2 1 
ATOM   4251  C CE1 . TYR B 1 21  ? -28.935 51.858  4.591   1.00 34.93  ? 21  TYR B CE1 1 
ATOM   4252  C CE2 . TYR B 1 21  ? -28.323 49.581  4.987   1.00 40.73  ? 21  TYR B CE2 1 
ATOM   4253  C CZ  . TYR B 1 21  ? -28.241 50.726  4.224   1.00 29.82  ? 21  TYR B CZ  1 
ATOM   4254  O OH  . TYR B 1 21  ? -27.462 50.742  3.090   1.00 30.65  ? 21  TYR B OH  1 
ATOM   4255  N N   . THR B 1 22  ? -31.360 50.508  10.783  1.00 28.04  ? 22  THR B N   1 
ATOM   4256  C CA  . THR B 1 22  ? -32.347 50.570  11.853  1.00 27.05  ? 22  THR B CA  1 
ATOM   4257  C C   . THR B 1 22  ? -31.741 50.795  13.232  1.00 31.64  ? 22  THR B C   1 
ATOM   4258  O O   . THR B 1 22  ? -32.484 51.103  14.171  1.00 34.27  ? 22  THR B O   1 
ATOM   4259  C CB  . THR B 1 22  ? -33.185 49.288  11.873  1.00 32.80  ? 22  THR B CB  1 
ATOM   4260  O OG1 . THR B 1 22  ? -32.525 48.296  12.668  1.00 42.36  ? 22  THR B OG1 1 
ATOM   4261  C CG2 . THR B 1 22  ? -33.398 48.760  10.461  1.00 44.58  ? 22  THR B CG2 1 
ATOM   4262  N N   . GLY B 1 23  ? -30.426 50.644  13.384  1.00 26.27  ? 23  GLY B N   1 
ATOM   4263  C CA  . GLY B 1 23  ? -29.804 50.854  14.677  1.00 25.49  ? 23  GLY B CA  1 
ATOM   4264  C C   . GLY B 1 23  ? -30.027 49.750  15.683  1.00 25.08  ? 23  GLY B C   1 
ATOM   4265  O O   . GLY B 1 23  ? -29.641 49.904  16.846  1.00 21.22  ? 23  GLY B O   1 
ATOM   4266  N N   . GLU B 1 24  ? -30.630 48.638  15.277  1.00 31.93  ? 24  GLU B N   1 
ATOM   4267  C CA  . GLU B 1 24  ? -30.986 47.574  16.202  1.00 31.73  ? 24  GLU B CA  1 
ATOM   4268  C C   . GLU B 1 24  ? -29.831 46.597  16.378  1.00 28.65  ? 24  GLU B C   1 
ATOM   4269  O O   . GLU B 1 24  ? -29.051 46.348  15.454  1.00 23.82  ? 24  GLU B O   1 
ATOM   4270  C CB  . GLU B 1 24  ? -32.233 46.836  15.714  1.00 26.28  ? 24  GLU B CB  1 
ATOM   4271  C CG  . GLU B 1 24  ? -33.442 47.747  15.545  1.00 33.24  ? 24  GLU B CG  1 
ATOM   4272  C CD  . GLU B 1 24  ? -34.725 46.986  15.280  1.00 48.63  ? 24  GLU B CD  1 
ATOM   4273  O OE1 . GLU B 1 24  ? -34.937 46.571  14.122  1.00 55.10  ? 24  GLU B OE1 1 
ATOM   4274  O OE2 . GLU B 1 24  ? -35.531 46.817  16.221  1.00 55.33  ? 24  GLU B OE2 1 
ATOM   4275  N N   . TYR B 1 25  ? -29.729 46.049  17.588  1.00 25.50  ? 25  TYR B N   1 
ATOM   4276  C CA  . TYR B 1 25  ? -28.701 45.068  17.930  1.00 20.24  ? 25  TYR B CA  1 
ATOM   4277  C C   . TYR B 1 25  ? -29.252 43.677  17.645  1.00 22.18  ? 25  TYR B C   1 
ATOM   4278  O O   . TYR B 1 25  ? -30.048 43.140  18.418  1.00 27.84  ? 25  TYR B O   1 
ATOM   4279  C CB  . TYR B 1 25  ? -28.279 45.219  19.386  1.00 26.00  ? 25  TYR B CB  1 
ATOM   4280  C CG  . TYR B 1 25  ? -27.177 46.231  19.580  1.00 21.51  ? 25  TYR B CG  1 
ATOM   4281  C CD1 . TYR B 1 25  ? -27.465 47.579  19.726  1.00 26.35  ? 25  TYR B CD1 1 
ATOM   4282  C CD2 . TYR B 1 25  ? -25.847 45.838  19.600  1.00 22.25  ? 25  TYR B CD2 1 
ATOM   4283  C CE1 . TYR B 1 25  ? -26.460 48.507  19.898  1.00 25.69  ? 25  TYR B CE1 1 
ATOM   4284  C CE2 . TYR B 1 25  ? -24.834 46.758  19.771  1.00 28.61  ? 25  TYR B CE2 1 
ATOM   4285  C CZ  . TYR B 1 25  ? -25.147 48.092  19.919  1.00 22.07  ? 25  TYR B CZ  1 
ATOM   4286  O OH  . TYR B 1 25  ? -24.146 49.018  20.090  1.00 21.64  ? 25  TYR B OH  1 
ATOM   4287  N N   . LEU B 1 26  ? -28.815 43.085  16.533  1.00 19.35  ? 26  LEU B N   1 
ATOM   4288  C CA  . LEU B 1 26  ? -29.365 41.804  16.109  1.00 19.28  ? 26  LEU B CA  1 
ATOM   4289  C C   . LEU B 1 26  ? -28.950 40.656  17.021  1.00 18.70  ? 26  LEU B C   1 
ATOM   4290  O O   . LEU B 1 26  ? -29.654 39.643  17.076  1.00 33.13  ? 26  LEU B O   1 
ATOM   4291  C CB  . LEU B 1 26  ? -28.951 41.507  14.668  1.00 19.68  ? 26  LEU B CB  1 
ATOM   4292  C CG  . LEU B 1 26  ? -29.215 42.602  13.628  1.00 20.41  ? 26  LEU B CG  1 
ATOM   4293  C CD1 . LEU B 1 26  ? -29.135 42.028  12.224  1.00 21.16  ? 26  LEU B CD1 1 
ATOM   4294  C CD2 . LEU B 1 26  ? -30.565 43.272  13.853  1.00 21.13  ? 26  LEU B CD2 1 
ATOM   4295  N N   . LEU B 1 27  ? -27.835 40.787  17.739  1.00 18.74  ? 27  LEU B N   1 
ATOM   4296  C CA  . LEU B 1 27  ? -27.363 39.748  18.643  1.00 23.19  ? 27  LEU B CA  1 
ATOM   4297  C C   . LEU B 1 27  ? -27.043 40.372  19.997  1.00 25.76  ? 27  LEU B C   1 
ATOM   4298  O O   . LEU B 1 27  ? -26.352 41.404  20.056  1.00 27.88  ? 27  LEU B O   1 
ATOM   4299  C CB  . LEU B 1 27  ? -26.126 39.038  18.078  1.00 24.09  ? 27  LEU B CB  1 
ATOM   4300  C CG  . LEU B 1 27  ? -26.284 38.343  16.725  1.00 17.65  ? 27  LEU B CG  1 
ATOM   4301  C CD1 . LEU B 1 27  ? -24.931 37.905  16.186  1.00 23.56  ? 27  LEU B CD1 1 
ATOM   4302  C CD2 . LEU B 1 27  ? -27.237 37.158  16.820  1.00 20.75  ? 27  LEU B CD2 1 
ATOM   4303  N N   . PRO B 1 28  ? -27.502 39.778  21.100  1.00 24.38  ? 28  PRO B N   1 
ATOM   4304  C CA  . PRO B 1 28  ? -27.266 40.359  22.425  1.00 23.14  ? 28  PRO B CA  1 
ATOM   4305  C C   . PRO B 1 28  ? -25.914 40.022  23.034  1.00 23.25  ? 28  PRO B C   1 
ATOM   4306  O O   . PRO B 1 28  ? -25.720 40.266  24.228  1.00 20.92  ? 28  PRO B O   1 
ATOM   4307  C CB  . PRO B 1 28  ? -28.398 39.739  23.255  1.00 17.36  ? 28  PRO B CB  1 
ATOM   4308  C CG  . PRO B 1 28  ? -28.572 38.377  22.650  1.00 17.62  ? 28  PRO B CG  1 
ATOM   4309  C CD  . PRO B 1 28  ? -28.204 38.484  21.183  1.00 20.34  ? 28  PRO B CD  1 
ATOM   4310  N N   . TRP B 1 29  ? -24.980 39.477  22.251  1.00 25.42  ? 29  TRP B N   1 
ATOM   4311  C CA  . TRP B 1 29  ? -23.751 38.927  22.812  1.00 18.48  ? 29  TRP B CA  1 
ATOM   4312  C C   . TRP B 1 29  ? -22.887 39.976  23.494  1.00 22.24  ? 29  TRP B C   1 
ATOM   4313  O O   . TRP B 1 29  ? -22.083 39.625  24.364  1.00 23.96  ? 29  TRP B O   1 
ATOM   4314  C CB  . TRP B 1 29  ? -22.953 38.222  21.716  1.00 22.68  ? 29  TRP B CB  1 
ATOM   4315  C CG  . TRP B 1 29  ? -23.634 37.005  21.174  1.00 25.60  ? 29  TRP B CG  1 
ATOM   4316  C CD1 . TRP B 1 29  ? -23.825 36.699  19.861  1.00 26.78  ? 29  TRP B CD1 1 
ATOM   4317  C CD2 . TRP B 1 29  ? -24.198 35.920  21.927  1.00 32.21  ? 29  TRP B CD2 1 
ATOM   4318  N NE1 . TRP B 1 29  ? -24.480 35.497  19.746  1.00 33.49  ? 29  TRP B NE1 1 
ATOM   4319  C CE2 . TRP B 1 29  ? -24.719 34.998  20.999  1.00 35.58  ? 29  TRP B CE2 1 
ATOM   4320  C CE3 . TRP B 1 29  ? -24.314 35.641  23.293  1.00 33.14  ? 29  TRP B CE3 1 
ATOM   4321  C CZ2 . TRP B 1 29  ? -25.349 33.818  21.394  1.00 44.28  ? 29  TRP B CZ2 1 
ATOM   4322  C CZ3 . TRP B 1 29  ? -24.938 34.471  23.682  1.00 31.69  ? 29  TRP B CZ3 1 
ATOM   4323  C CH2 . TRP B 1 29  ? -25.441 33.570  22.736  1.00 39.99  ? 29  TRP B CH2 1 
ATOM   4324  N N   . THR B 1 30  ? -23.014 41.249  23.118  1.00 21.18  ? 30  THR B N   1 
ATOM   4325  C CA  . THR B 1 30  ? -22.321 42.284  23.876  1.00 18.87  ? 30  THR B CA  1 
ATOM   4326  C C   . THR B 1 30  ? -22.935 42.447  25.261  1.00 17.71  ? 30  THR B C   1 
ATOM   4327  O O   . THR B 1 30  ? -22.210 42.604  26.251  1.00 20.50  ? 30  THR B O   1 
ATOM   4328  C CB  . THR B 1 30  ? -22.340 43.612  23.116  1.00 23.14  ? 30  THR B CB  1 
ATOM   4329  O OG1 . THR B 1 30  ? -21.787 43.424  21.808  1.00 21.97  ? 30  THR B OG1 1 
ATOM   4330  C CG2 . THR B 1 30  ? -21.516 44.652  23.859  1.00 14.53  ? 30  THR B CG2 1 
ATOM   4331  N N   . PHE B 1 31  ? -24.266 42.395  25.355  1.00 15.49  ? 31  PHE B N   1 
ATOM   4332  C CA  . PHE B 1 31  ? -24.924 42.550  26.649  1.00 16.01  ? 31  PHE B CA  1 
ATOM   4333  C C   . PHE B 1 31  ? -24.568 41.406  27.590  1.00 16.81  ? 31  PHE B C   1 
ATOM   4334  O O   . PHE B 1 31  ? -24.146 41.632  28.729  1.00 19.74  ? 31  PHE B O   1 
ATOM   4335  C CB  . PHE B 1 31  ? -26.440 42.634  26.468  1.00 19.19  ? 31  PHE B CB  1 
ATOM   4336  C CG  . PHE B 1 31  ? -27.190 42.848  27.756  1.00 17.36  ? 31  PHE B CG  1 
ATOM   4337  C CD1 . PHE B 1 31  ? -27.350 44.122  28.276  1.00 17.75  ? 31  PHE B CD1 1 
ATOM   4338  C CD2 . PHE B 1 31  ? -27.733 41.776  28.449  1.00 18.95  ? 31  PHE B CD2 1 
ATOM   4339  C CE1 . PHE B 1 31  ? -28.036 44.325  29.462  1.00 18.56  ? 31  PHE B CE1 1 
ATOM   4340  C CE2 . PHE B 1 31  ? -28.420 41.972  29.635  1.00 18.52  ? 31  PHE B CE2 1 
ATOM   4341  C CZ  . PHE B 1 31  ? -28.572 43.248  30.142  1.00 18.90  ? 31  PHE B CZ  1 
ATOM   4342  N N   . PHE B 1 32  ? -24.725 40.165  27.124  1.00 22.58  ? 32  PHE B N   1 
ATOM   4343  C CA  . PHE B 1 32  ? -24.619 39.022  28.025  1.00 22.92  ? 32  PHE B CA  1 
ATOM   4344  C C   . PHE B 1 32  ? -23.196 38.815  28.526  1.00 21.91  ? 32  PHE B C   1 
ATOM   4345  O O   . PHE B 1 32  ? -23.002 38.260  29.613  1.00 22.50  ? 32  PHE B O   1 
ATOM   4346  C CB  . PHE B 1 32  ? -25.144 37.762  27.338  1.00 18.94  ? 32  PHE B CB  1 
ATOM   4347  C CG  . PHE B 1 32  ? -26.631 37.602  27.445  1.00 17.26  ? 32  PHE B CG  1 
ATOM   4348  C CD1 . PHE B 1 32  ? -27.259 37.707  28.674  1.00 17.88  ? 32  PHE B CD1 1 
ATOM   4349  C CD2 . PHE B 1 32  ? -27.402 37.362  26.323  1.00 23.68  ? 32  PHE B CD2 1 
ATOM   4350  C CE1 . PHE B 1 32  ? -28.628 37.568  28.785  1.00 18.64  ? 32  PHE B CE1 1 
ATOM   4351  C CE2 . PHE B 1 32  ? -28.773 37.221  26.426  1.00 20.80  ? 32  PHE B CE2 1 
ATOM   4352  C CZ  . PHE B 1 32  ? -29.386 37.325  27.660  1.00 19.85  ? 32  PHE B CZ  1 
ATOM   4353  N N   . HIS B 1 33  ? -22.194 39.246  27.762  1.00 15.18  ? 33  HIS B N   1 
ATOM   4354  C CA  . HIS B 1 33  ? -20.821 39.169  28.241  1.00 14.81  ? 33  HIS B CA  1 
ATOM   4355  C C   . HIS B 1 33  ? -20.385 40.421  28.987  1.00 19.87  ? 33  HIS B C   1 
ATOM   4356  O O   . HIS B 1 33  ? -19.403 40.367  29.739  1.00 21.70  ? 33  HIS B O   1 
ATOM   4357  C CB  . HIS B 1 33  ? -19.870 38.893  27.072  1.00 14.22  ? 33  HIS B CB  1 
ATOM   4358  C CG  . HIS B 1 33  ? -19.922 37.480  26.580  1.00 17.38  ? 33  HIS B CG  1 
ATOM   4359  N ND1 . HIS B 1 33  ? -19.544 36.408  27.360  1.00 21.59  ? 33  HIS B ND1 1 
ATOM   4360  C CD2 . HIS B 1 33  ? -20.316 36.961  25.393  1.00 16.24  ? 33  HIS B CD2 1 
ATOM   4361  C CE1 . HIS B 1 33  ? -19.699 35.290  26.673  1.00 19.78  ? 33  HIS B CE1 1 
ATOM   4362  N NE2 . HIS B 1 33  ? -20.166 35.598  25.476  1.00 18.54  ? 33  HIS B NE2 1 
ATOM   4363  N N   . ALA B 1 34  ? -21.090 41.541  28.802  1.00 15.62  ? 34  ALA B N   1 
ATOM   4364  C CA  . ALA B 1 34  ? -20.827 42.717  29.625  1.00 15.24  ? 34  ALA B CA  1 
ATOM   4365  C C   . ALA B 1 34  ? -21.317 42.505  31.052  1.00 19.27  ? 34  ALA B C   1 
ATOM   4366  O O   . ALA B 1 34  ? -20.663 42.937  32.010  1.00 22.82  ? 34  ALA B O   1 
ATOM   4367  C CB  . ALA B 1 34  ? -21.480 43.954  29.012  1.00 15.41  ? 34  ALA B CB  1 
ATOM   4368  N N   . VAL B 1 35  ? -22.463 41.836  31.212  1.00 16.45  ? 35  VAL B N   1 
ATOM   4369  C CA  . VAL B 1 35  ? -23.005 41.564  32.541  1.00 25.09  ? 35  VAL B CA  1 
ATOM   4370  C C   . VAL B 1 35  ? -22.352 40.368  33.208  1.00 27.00  ? 35  VAL B C   1 
ATOM   4371  O O   . VAL B 1 35  ? -22.593 40.124  34.398  1.00 33.60  ? 35  VAL B O   1 
ATOM   4372  C CB  . VAL B 1 35  ? -24.526 41.324  32.490  1.00 17.92  ? 35  VAL B CB  1 
ATOM   4373  C CG1 . VAL B 1 35  ? -25.248 42.580  32.028  1.00 18.69  ? 35  VAL B CG1 1 
ATOM   4374  C CG2 . VAL B 1 35  ? -24.846 40.148  31.583  1.00 22.78  ? 35  VAL B CG2 1 
ATOM   4375  N N   . LYS B 1 36  ? -21.532 39.615  32.482  1.00 18.21  ? 36  LYS B N   1 
ATOM   4376  C CA  . LYS B 1 36  ? -20.893 38.421  33.018  1.00 25.56  ? 36  LYS B CA  1 
ATOM   4377  C C   . LYS B 1 36  ? -19.380 38.530  33.113  1.00 27.14  ? 36  LYS B C   1 
ATOM   4378  O O   . LYS B 1 36  ? -18.800 38.085  34.106  1.00 35.40  ? 36  LYS B O   1 
ATOM   4379  C CB  . LYS B 1 36  ? -21.256 37.203  32.161  1.00 27.08  ? 36  LYS B CB  1 
ATOM   4380  C CG  . LYS B 1 36  ? -21.337 35.896  32.933  1.00 23.39  ? 36  LYS B CG  1 
ATOM   4381  C CD  . LYS B 1 36  ? -21.732 34.745  32.019  1.00 26.50  ? 36  LYS B CD  1 
ATOM   4382  C CE  . LYS B 1 36  ? -20.693 34.503  30.934  1.00 23.57  ? 36  LYS B CE  1 
ATOM   4383  N NZ  . LYS B 1 36  ? -19.307 34.648  31.452  1.00 30.81  ? 36  LYS B NZ  1 
ATOM   4384  N N   . ASP B 1 37  ? -18.720 39.116  32.115  1.00 19.12  ? 37  ASP B N   1 
ATOM   4385  C CA  . ASP B 1 37  ? -17.264 39.059  32.047  1.00 20.13  ? 37  ASP B CA  1 
ATOM   4386  C C   . ASP B 1 37  ? -16.583 40.417  31.975  1.00 17.50  ? 37  ASP B C   1 
ATOM   4387  O O   . ASP B 1 37  ? -15.567 40.620  32.643  1.00 24.02  ? 37  ASP B O   1 
ATOM   4388  C CB  . ASP B 1 37  ? -16.837 38.218  30.839  1.00 25.91  ? 37  ASP B CB  1 
ATOM   4389  C CG  . ASP B 1 37  ? -17.190 36.755  30.998  1.00 29.56  ? 37  ASP B CG  1 
ATOM   4390  O OD1 . ASP B 1 37  ? -16.687 36.123  31.949  1.00 30.96  ? 37  ASP B OD1 1 
ATOM   4391  O OD2 . ASP B 1 37  ? -17.980 36.239  30.179  1.00 26.90  ? 37  ASP B OD2 1 
ATOM   4392  N N   . TYR B 1 38  ? -17.107 41.360  31.186  1.00 15.04  ? 38  TYR B N   1 
ATOM   4393  C CA  . TYR B 1 38  ? -16.373 42.598  30.945  1.00 17.50  ? 38  TYR B CA  1 
ATOM   4394  C C   . TYR B 1 38  ? -16.211 43.443  32.201  1.00 22.99  ? 38  TYR B C   1 
ATOM   4395  O O   . TYR B 1 38  ? -15.278 44.247  32.268  1.00 22.12  ? 38  TYR B O   1 
ATOM   4396  C CB  . TYR B 1 38  ? -17.050 43.413  29.840  1.00 20.95  ? 38  TYR B CB  1 
ATOM   4397  C CG  . TYR B 1 38  ? -17.048 42.702  28.511  1.00 13.68  ? 38  TYR B CG  1 
ATOM   4398  C CD1 . TYR B 1 38  ? -16.050 41.794  28.200  1.00 15.86  ? 38  TYR B CD1 1 
ATOM   4399  C CD2 . TYR B 1 38  ? -18.036 42.938  27.567  1.00 15.03  ? 38  TYR B CD2 1 
ATOM   4400  C CE1 . TYR B 1 38  ? -16.037 41.137  26.999  1.00 16.96  ? 38  TYR B CE1 1 
ATOM   4401  C CE2 . TYR B 1 38  ? -18.032 42.281  26.353  1.00 13.96  ? 38  TYR B CE2 1 
ATOM   4402  C CZ  . TYR B 1 38  ? -17.029 41.381  26.072  1.00 18.63  ? 38  TYR B CZ  1 
ATOM   4403  O OH  . TYR B 1 38  ? -17.015 40.722  24.864  1.00 15.66  ? 38  TYR B OH  1 
ATOM   4404  N N   . TYR B 1 39  ? -17.079 43.283  33.196  1.00 18.86  ? 39  TYR B N   1 
ATOM   4405  C CA  . TYR B 1 39  ? -16.814 43.923  34.478  1.00 16.87  ? 39  TYR B CA  1 
ATOM   4406  C C   . TYR B 1 39  ? -16.124 42.984  35.457  1.00 20.88  ? 39  TYR B C   1 
ATOM   4407  O O   . TYR B 1 39  ? -15.239 43.411  36.206  1.00 20.18  ? 39  TYR B O   1 
ATOM   4408  C CB  . TYR B 1 39  ? -18.107 44.438  35.110  1.00 21.31  ? 39  TYR B CB  1 
ATOM   4409  C CG  . TYR B 1 39  ? -17.879 45.052  36.473  1.00 19.83  ? 39  TYR B CG  1 
ATOM   4410  C CD1 . TYR B 1 39  ? -17.345 46.327  36.598  1.00 26.33  ? 39  TYR B CD1 1 
ATOM   4411  C CD2 . TYR B 1 39  ? -18.169 44.347  37.636  1.00 25.87  ? 39  TYR B CD2 1 
ATOM   4412  C CE1 . TYR B 1 39  ? -17.119 46.891  37.839  1.00 36.21  ? 39  TYR B CE1 1 
ATOM   4413  C CE2 . TYR B 1 39  ? -17.945 44.901  38.884  1.00 21.06  ? 39  TYR B CE2 1 
ATOM   4414  C CZ  . TYR B 1 39  ? -17.420 46.175  38.979  1.00 33.57  ? 39  TYR B CZ  1 
ATOM   4415  O OH  . TYR B 1 39  ? -17.196 46.736  40.215  1.00 42.99  ? 39  TYR B OH  1 
ATOM   4416  N N   . ASP B 1 40  ? -16.512 41.707  35.459  1.00 25.37  ? 40  ASP B N   1 
ATOM   4417  C CA  . ASP B 1 40  ? -16.030 40.788  36.483  1.00 20.31  ? 40  ASP B CA  1 
ATOM   4418  C C   . ASP B 1 40  ? -14.578 40.389  36.261  1.00 26.23  ? 40  ASP B C   1 
ATOM   4419  O O   . ASP B 1 40  ? -13.848 40.160  37.234  1.00 33.33  ? 40  ASP B O   1 
ATOM   4420  C CB  . ASP B 1 40  ? -16.922 39.548  36.532  1.00 18.01  ? 40  ASP B CB  1 
ATOM   4421  C CG  . ASP B 1 40  ? -18.163 39.765  37.366  1.00 32.23  ? 40  ASP B CG  1 
ATOM   4422  O OD1 . ASP B 1 40  ? -18.033 39.913  38.600  1.00 36.98  ? 40  ASP B OD1 1 
ATOM   4423  O OD2 . ASP B 1 40  ? -19.269 39.801  36.786  1.00 38.44  ? 40  ASP B OD2 1 
ATOM   4424  N N   . MET B 1 41  ? -14.142 40.295  35.003  1.00 19.57  ? 41  MET B N   1 
ATOM   4425  C CA  . MET B 1 41  ? -12.767 39.876  34.733  1.00 22.07  ? 41  MET B CA  1 
ATOM   4426  C C   . MET B 1 41  ? -11.731 40.800  35.362  1.00 23.22  ? 41  MET B C   1 
ATOM   4427  O O   . MET B 1 41  ? -10.826 40.292  36.046  1.00 25.86  ? 41  MET B O   1 
ATOM   4428  C CB  . MET B 1 41  ? -12.551 39.736  33.221  1.00 22.57  ? 41  MET B CB  1 
ATOM   4429  C CG  . MET B 1 41  ? -11.648 38.583  32.838  1.00 30.03  ? 41  MET B CG  1 
ATOM   4430  S SD  . MET B 1 41  ? -12.122 37.034  33.622  1.00 25.29  ? 41  MET B SD  1 
ATOM   4431  C CE  . MET B 1 41  ? -11.083 35.901  32.712  1.00 22.27  ? 41  MET B CE  1 
ATOM   4432  N N   . PRO B 1 42  ? -11.788 42.129  35.197  1.00 17.97  ? 42  PRO B N   1 
ATOM   4433  C CA  . PRO B 1 42  ? -10.831 42.987  35.910  1.00 16.44  ? 42  PRO B CA  1 
ATOM   4434  C C   . PRO B 1 42  ? -11.162 43.197  37.377  1.00 20.66  ? 42  PRO B C   1 
ATOM   4435  O O   . PRO B 1 42  ? -10.315 43.723  38.111  1.00 18.35  ? 42  PRO B O   1 
ATOM   4436  C CB  . PRO B 1 42  ? -10.907 44.307  35.133  1.00 16.07  ? 42  PRO B CB  1 
ATOM   4437  C CG  . PRO B 1 42  ? -12.291 44.344  34.630  1.00 19.31  ? 42  PRO B CG  1 
ATOM   4438  C CD  . PRO B 1 42  ? -12.642 42.921  34.291  1.00 22.94  ? 42  PRO B CD  1 
ATOM   4439  N N   . ALA B 1 43  ? -12.354 42.804  37.828  1.00 20.60  ? 43  ALA B N   1 
ATOM   4440  C CA  . ALA B 1 43  ? -12.725 42.991  39.225  1.00 19.48  ? 43  ALA B CA  1 
ATOM   4441  C C   . ALA B 1 43  ? -12.049 41.990  40.151  1.00 21.29  ? 43  ALA B C   1 
ATOM   4442  O O   . ALA B 1 43  ? -12.025 42.213  41.367  1.00 24.55  ? 43  ALA B O   1 
ATOM   4443  C CB  . ALA B 1 43  ? -14.243 42.907  39.389  1.00 19.89  ? 43  ALA B CB  1 
ATOM   4444  N N   . TYR B 1 44  ? -11.503 40.897  39.608  1.00 25.04  ? 44  TYR B N   1 
ATOM   4445  C CA  . TYR B 1 44  ? -10.689 39.997  40.419  1.00 21.52  ? 44  TYR B CA  1 
ATOM   4446  C C   . TYR B 1 44  ? -9.512  40.730  41.047  1.00 26.49  ? 44  TYR B C   1 
ATOM   4447  O O   . TYR B 1 44  ? -9.040  40.343  42.124  1.00 30.46  ? 44  TYR B O   1 
ATOM   4448  C CB  . TYR B 1 44  ? -10.174 38.831  39.571  1.00 19.53  ? 44  TYR B CB  1 
ATOM   4449  C CG  . TYR B 1 44  ? -11.165 37.711  39.354  1.00 19.60  ? 44  TYR B CG  1 
ATOM   4450  C CD1 . TYR B 1 44  ? -12.018 37.714  38.259  1.00 20.45  ? 44  TYR B CD1 1 
ATOM   4451  C CD2 . TYR B 1 44  ? -11.236 36.641  40.236  1.00 20.68  ? 44  TYR B CD2 1 
ATOM   4452  C CE1 . TYR B 1 44  ? -12.920 36.688  38.052  1.00 18.89  ? 44  TYR B CE1 1 
ATOM   4453  C CE2 . TYR B 1 44  ? -12.134 35.610  40.038  1.00 20.88  ? 44  TYR B CE2 1 
ATOM   4454  C CZ  . TYR B 1 44  ? -12.974 35.638  38.945  1.00 19.97  ? 44  TYR B CZ  1 
ATOM   4455  O OH  . TYR B 1 44  ? -13.871 34.615  38.745  1.00 24.07  ? 44  TYR B OH  1 
ATOM   4456  N N   . LEU B 1 45  ? -9.027  41.785  40.387  1.00 22.90  ? 45  LEU B N   1 
ATOM   4457  C CA  . LEU B 1 45  ? -7.874  42.533  40.875  1.00 27.95  ? 45  LEU B CA  1 
ATOM   4458  C C   . LEU B 1 45  ? -8.138  43.217  42.211  1.00 35.57  ? 45  LEU B C   1 
ATOM   4459  O O   . LEU B 1 45  ? -7.183  43.525  42.934  1.00 36.45  ? 45  LEU B O   1 
ATOM   4460  C CB  . LEU B 1 45  ? -7.451  43.561  39.825  1.00 19.61  ? 45  LEU B CB  1 
ATOM   4461  C CG  . LEU B 1 45  ? -6.894  42.939  38.546  1.00 18.33  ? 45  LEU B CG  1 
ATOM   4462  C CD1 . LEU B 1 45  ? -7.109  43.844  37.343  1.00 17.69  ? 45  LEU B CD1 1 
ATOM   4463  C CD2 . LEU B 1 45  ? -5.419  42.622  38.721  1.00 21.16  ? 45  LEU B CD2 1 
ATOM   4464  N N   . LYS B 1 46  ? -9.403  43.470  42.553  1.00 28.48  ? 46  LYS B N   1 
ATOM   4465  C CA  . LYS B 1 46  ? -9.714  44.084  43.837  1.00 30.97  ? 46  LYS B CA  1 
ATOM   4466  C C   . LYS B 1 46  ? -9.775  43.079  44.980  1.00 25.45  ? 46  LYS B C   1 
ATOM   4467  O O   . LYS B 1 46  ? -9.799  43.492  46.143  1.00 36.85  ? 46  LYS B O   1 
ATOM   4468  C CB  . LYS B 1 46  ? -11.036 44.850  43.748  1.00 27.31  ? 46  LYS B CB  1 
ATOM   4469  C CG  . LYS B 1 46  ? -11.130 45.776  42.544  1.00 37.18  ? 46  LYS B CG  1 
ATOM   4470  C CD  . LYS B 1 46  ? -12.377 46.644  42.598  1.00 51.19  ? 46  LYS B CD  1 
ATOM   4471  C CE  . LYS B 1 46  ? -13.634 45.805  42.760  1.00 35.84  ? 46  LYS B CE  1 
ATOM   4472  N NZ  . LYS B 1 46  ? -14.786 46.410  42.040  1.00 30.72  ? 46  LYS B NZ  1 
ATOM   4473  N N   . ASP B 1 47  ? -9.801  41.780  44.685  1.00 27.48  ? 47  ASP B N   1 
ATOM   4474  C CA  . ASP B 1 47  ? -9.833  40.741  45.706  1.00 26.27  ? 47  ASP B CA  1 
ATOM   4475  C C   . ASP B 1 47  ? -8.583  39.870  45.719  1.00 30.76  ? 47  ASP B C   1 
ATOM   4476  O O   . ASP B 1 47  ? -8.481  38.968  46.560  1.00 27.43  ? 47  ASP B O   1 
ATOM   4477  C CB  . ASP B 1 47  ? -11.070 39.851  45.525  1.00 28.75  ? 47  ASP B CB  1 
ATOM   4478  C CG  . ASP B 1 47  ? -12.370 40.639  45.513  1.00 52.95  ? 47  ASP B CG  1 
ATOM   4479  O OD1 . ASP B 1 47  ? -12.329 41.885  45.535  1.00 68.47  ? 47  ASP B OD1 1 
ATOM   4480  O OD2 . ASP B 1 47  ? -13.444 40.001  45.483  1.00 71.66  ? 47  ASP B OD2 1 
ATOM   4481  N N   . PHE B 1 48  ? -7.632  40.105  44.816  1.00 32.42  ? 48  PHE B N   1 
ATOM   4482  C CA  . PHE B 1 48  ? -6.421  39.299  44.737  1.00 24.97  ? 48  PHE B CA  1 
ATOM   4483  C C   . PHE B 1 48  ? -5.251  40.205  44.392  1.00 25.52  ? 48  PHE B C   1 
ATOM   4484  O O   . PHE B 1 48  ? -5.307  40.939  43.401  1.00 30.75  ? 48  PHE B O   1 
ATOM   4485  C CB  . PHE B 1 48  ? -6.567  38.186  43.693  1.00 26.41  ? 48  PHE B CB  1 
ATOM   4486  C CG  . PHE B 1 48  ? -7.599  37.153  44.052  1.00 30.81  ? 48  PHE B CG  1 
ATOM   4487  C CD1 . PHE B 1 48  ? -7.280  36.096  44.889  1.00 27.49  ? 48  PHE B CD1 1 
ATOM   4488  C CD2 . PHE B 1 48  ? -8.891  37.246  43.562  1.00 27.56  ? 48  PHE B CD2 1 
ATOM   4489  C CE1 . PHE B 1 48  ? -8.230  35.145  45.222  1.00 32.07  ? 48  PHE B CE1 1 
ATOM   4490  C CE2 . PHE B 1 48  ? -9.846  36.300  43.893  1.00 26.89  ? 48  PHE B CE2 1 
ATOM   4491  C CZ  . PHE B 1 48  ? -9.515  35.248  44.724  1.00 25.91  ? 48  PHE B CZ  1 
ATOM   4492  N N   . GLU B 1 49  ? -4.194  40.148  45.202  1.00 32.36  ? 49  GLU B N   1 
ATOM   4493  C CA  . GLU B 1 49  ? -3.053  41.038  45.024  1.00 30.07  ? 49  GLU B CA  1 
ATOM   4494  C C   . GLU B 1 49  ? -2.101  40.516  43.956  1.00 29.72  ? 49  GLU B C   1 
ATOM   4495  O O   . GLU B 1 49  ? -0.905  40.345  44.211  1.00 34.46  ? 49  GLU B O   1 
ATOM   4496  C CB  . GLU B 1 49  ? -2.310  41.233  46.348  1.00 39.01  ? 49  GLU B CB  1 
ATOM   4497  C CG  . GLU B 1 49  ? -1.736  42.637  46.544  1.00 59.73  ? 49  GLU B CG  1 
ATOM   4498  C CD  . GLU B 1 49  ? -2.787  43.732  46.458  1.00 61.23  ? 49  GLU B CD  1 
ATOM   4499  O OE1 . GLU B 1 49  ? -3.966  43.465  46.778  1.00 64.36  ? 49  GLU B OE1 1 
ATOM   4500  O OE2 . GLU B 1 49  ? -2.432  44.864  46.060  1.00 57.65  ? 49  GLU B OE2 1 
ATOM   4501  N N   . ILE B 1 50  ? -2.628  40.265  42.758  1.00 30.68  ? 50  ILE B N   1 
ATOM   4502  C CA  . ILE B 1 50  ? -1.829  39.863  41.608  1.00 21.74  ? 50  ILE B CA  1 
ATOM   4503  C C   . ILE B 1 50  ? -2.087  40.855  40.484  1.00 20.91  ? 50  ILE B C   1 
ATOM   4504  O O   . ILE B 1 50  ? -2.926  41.753  40.616  1.00 21.81  ? 50  ILE B O   1 
ATOM   4505  C CB  . ILE B 1 50  ? -2.154  38.425  41.165  1.00 21.15  ? 50  ILE B CB  1 
ATOM   4506  C CG1 . ILE B 1 50  ? -3.605  38.328  40.694  1.00 20.57  ? 50  ILE B CG1 1 
ATOM   4507  C CG2 . ILE B 1 50  ? -1.897  37.444  42.298  1.00 23.40  ? 50  ILE B CG2 1 
ATOM   4508  C CD1 . ILE B 1 50  ? -3.801  37.420  39.501  1.00 19.54  ? 50  ILE B CD1 1 
ATOM   4509  N N   . LYS B 1 51  ? -1.377  40.701  39.373  1.00 19.49  ? 51  LYS B N   1 
ATOM   4510  C CA  . LYS B 1 51  ? -1.529  41.578  38.223  1.00 19.83  ? 51  LYS B CA  1 
ATOM   4511  C C   . LYS B 1 51  ? -2.182  40.824  37.072  1.00 17.11  ? 51  LYS B C   1 
ATOM   4512  O O   . LYS B 1 51  ? -1.854  39.661  36.813  1.00 19.28  ? 51  LYS B O   1 
ATOM   4513  C CB  . LYS B 1 51  ? -0.175  42.144  37.785  1.00 21.43  ? 51  LYS B CB  1 
ATOM   4514  C CG  . LYS B 1 51  ? 0.271   43.377  38.561  1.00 21.34  ? 51  LYS B CG  1 
ATOM   4515  C CD  . LYS B 1 51  ? 1.241   43.035  39.676  1.00 22.76  ? 51  LYS B CD  1 
ATOM   4516  C CE  . LYS B 1 51  ? 1.604   44.273  40.482  1.00 32.12  ? 51  LYS B CE  1 
ATOM   4517  N NZ  . LYS B 1 51  ? 0.645   44.525  41.592  1.00 37.87  ? 51  LYS B NZ  1 
ATOM   4518  N N   . LEU B 1 52  ? -3.117  41.489  36.394  1.00 18.32  ? 52  LEU B N   1 
ATOM   4519  C CA  . LEU B 1 52  ? -3.795  40.938  35.228  1.00 15.60  ? 52  LEU B CA  1 
ATOM   4520  C C   . LEU B 1 52  ? -3.951  42.032  34.184  1.00 14.89  ? 52  LEU B C   1 
ATOM   4521  O O   . LEU B 1 52  ? -4.210  43.188  34.525  1.00 15.19  ? 52  LEU B O   1 
ATOM   4522  C CB  . LEU B 1 52  ? -5.174  40.368  35.585  1.00 17.38  ? 52  LEU B CB  1 
ATOM   4523  C CG  . LEU B 1 52  ? -5.258  39.201  36.568  1.00 16.67  ? 52  LEU B CG  1 
ATOM   4524  C CD1 . LEU B 1 52  ? -6.697  39.001  37.000  1.00 17.04  ? 52  LEU B CD1 1 
ATOM   4525  C CD2 . LEU B 1 52  ? -4.712  37.934  35.944  1.00 16.38  ? 52  LEU B CD2 1 
ATOM   4526  N N   . ASN B 1 53  ? -3.812  41.664  32.916  1.00 14.10  ? 53  ASN B N   1 
ATOM   4527  C CA  . ASN B 1 53  ? -3.857  42.622  31.824  1.00 13.54  ? 53  ASN B CA  1 
ATOM   4528  C C   . ASN B 1 53  ? -5.027  42.312  30.901  1.00 14.22  ? 53  ASN B C   1 
ATOM   4529  O O   . ASN B 1 53  ? -5.517  41.180  30.840  1.00 17.03  ? 53  ASN B O   1 
ATOM   4530  C CB  . ASN B 1 53  ? -2.541  42.613  31.042  1.00 13.96  ? 53  ASN B CB  1 
ATOM   4531  C CG  . ASN B 1 53  ? -1.334  42.733  31.945  1.00 14.05  ? 53  ASN B CG  1 
ATOM   4532  O OD1 . ASN B 1 53  ? -1.020  43.815  32.437  1.00 16.83  ? 53  ASN B OD1 1 
ATOM   4533  N ND2 . ASN B 1 53  ? -0.656  41.617  32.178  1.00 15.11  ? 53  ASN B ND2 1 
ATOM   4534  N N   . PHE B 1 54  ? -5.479  43.338  30.182  1.00 12.80  ? 54  PHE B N   1 
ATOM   4535  C CA  . PHE B 1 54  ? -6.691  43.240  29.385  1.00 12.49  ? 54  PHE B CA  1 
ATOM   4536  C C   . PHE B 1 54  ? -6.542  44.038  28.099  1.00 12.15  ? 54  PHE B C   1 
ATOM   4537  O O   . PHE B 1 54  ? -5.898  45.089  28.071  1.00 13.73  ? 54  PHE B O   1 
ATOM   4538  C CB  . PHE B 1 54  ? -7.910  43.731  30.173  1.00 13.96  ? 54  PHE B CB  1 
ATOM   4539  C CG  . PHE B 1 54  ? -8.062  43.067  31.506  1.00 15.76  ? 54  PHE B CG  1 
ATOM   4540  C CD1 . PHE B 1 54  ? -8.767  41.883  31.625  1.00 13.76  ? 54  PHE B CD1 1 
ATOM   4541  C CD2 . PHE B 1 54  ? -7.479  43.614  32.638  1.00 14.89  ? 54  PHE B CD2 1 
ATOM   4542  C CE1 . PHE B 1 54  ? -8.901  41.260  32.849  1.00 15.66  ? 54  PHE B CE1 1 
ATOM   4543  C CE2 . PHE B 1 54  ? -7.606  42.996  33.863  1.00 16.96  ? 54  PHE B CE2 1 
ATOM   4544  C CZ  . PHE B 1 54  ? -8.317  41.814  33.968  1.00 16.66  ? 54  PHE B CZ  1 
ATOM   4545  N N   . ASN B 1 55  ? -7.145  43.520  27.033  1.00 12.79  ? 55  ASN B N   1 
ATOM   4546  C CA  . ASN B 1 55  ? -7.208  44.190  25.743  1.00 11.63  ? 55  ASN B CA  1 
ATOM   4547  C C   . ASN B 1 55  ? -8.665  44.459  25.403  1.00 12.66  ? 55  ASN B C   1 
ATOM   4548  O O   . ASN B 1 55  ? -9.489  43.539  25.427  1.00 17.41  ? 55  ASN B O   1 
ATOM   4549  C CB  . ASN B 1 55  ? -6.565  43.340  24.648  1.00 11.34  ? 55  ASN B CB  1 
ATOM   4550  C CG  . ASN B 1 55  ? -6.603  44.017  23.295  1.00 14.15  ? 55  ASN B CG  1 
ATOM   4551  O OD1 . ASN B 1 55  ? -6.142  45.141  23.147  1.00 18.71  ? 55  ASN B OD1 1 
ATOM   4552  N ND2 . ASN B 1 55  ? -7.165  43.340  22.304  1.00 11.49  ? 55  ASN B ND2 1 
ATOM   4553  N N   . LEU B 1 56  ? -8.979  45.712  25.083  1.00 13.19  ? 56  LEU B N   1 
ATOM   4554  C CA  . LEU B 1 56  ? -10.329 46.112  24.701  1.00 12.15  ? 56  LEU B CA  1 
ATOM   4555  C C   . LEU B 1 56  ? -10.289 46.701  23.299  1.00 12.21  ? 56  LEU B C   1 
ATOM   4556  O O   . LEU B 1 56  ? -9.615  47.710  23.066  1.00 16.07  ? 56  LEU B O   1 
ATOM   4557  C CB  . LEU B 1 56  ? -10.911 47.124  25.690  1.00 12.66  ? 56  LEU B CB  1 
ATOM   4558  C CG  . LEU B 1 56  ? -10.664 46.882  27.177  1.00 13.15  ? 56  LEU B CG  1 
ATOM   4559  C CD1 . LEU B 1 56  ? -11.061 48.110  27.982  1.00 15.88  ? 56  LEU B CD1 1 
ATOM   4560  C CD2 . LEU B 1 56  ? -11.426 45.654  27.653  1.00 17.05  ? 56  LEU B CD2 1 
ATOM   4561  N N   . THR B 1 57  ? -11.002 46.071  22.374  1.00 13.51  ? 57  THR B N   1 
ATOM   4562  C CA  . THR B 1 57  ? -11.108 46.614  21.030  1.00 12.37  ? 57  THR B CA  1 
ATOM   4563  C C   . THR B 1 57  ? -12.036 47.827  21.040  1.00 16.04  ? 57  THR B C   1 
ATOM   4564  O O   . THR B 1 57  ? -13.064 47.815  21.724  1.00 19.84  ? 57  THR B O   1 
ATOM   4565  C CB  . THR B 1 57  ? -11.632 45.558  20.057  1.00 12.30  ? 57  THR B CB  1 
ATOM   4566  O OG1 . THR B 1 57  ? -12.896 45.064  20.518  1.00 13.69  ? 57  THR B OG1 1 
ATOM   4567  C CG2 . THR B 1 57  ? -10.653 44.399  19.959  1.00 13.24  ? 57  THR B CG2 1 
ATOM   4568  N N   . PRO B 1 58  ? -11.696 48.890  20.306  1.00 13.88  ? 58  PRO B N   1 
ATOM   4569  C CA  . PRO B 1 58  ? -12.522 50.109  20.356  1.00 14.01  ? 58  PRO B CA  1 
ATOM   4570  C C   . PRO B 1 58  ? -13.961 49.894  19.918  1.00 16.15  ? 58  PRO B C   1 
ATOM   4571  O O   . PRO B 1 58  ? -14.852 50.619  20.376  1.00 18.79  ? 58  PRO B O   1 
ATOM   4572  C CB  . PRO B 1 58  ? -11.781 51.067  19.414  1.00 14.52  ? 58  PRO B CB  1 
ATOM   4573  C CG  . PRO B 1 58  ? -10.376 50.564  19.391  1.00 14.05  ? 58  PRO B CG  1 
ATOM   4574  C CD  . PRO B 1 58  ? -10.486 49.074  19.489  1.00 13.37  ? 58  PRO B CD  1 
ATOM   4575  N N   . VAL B 1 59  ? -14.222 48.925  19.039  1.00 17.81  ? 59  VAL B N   1 
ATOM   4576  C CA  . VAL B 1 59  ? -15.597 48.655  18.636  1.00 14.98  ? 59  VAL B CA  1 
ATOM   4577  C C   . VAL B 1 59  ? -16.379 47.990  19.762  1.00 14.07  ? 59  VAL B C   1 
ATOM   4578  O O   . VAL B 1 59  ? -17.610 48.096  19.803  1.00 14.64  ? 59  VAL B O   1 
ATOM   4579  C CB  . VAL B 1 59  ? -15.625 47.803  17.349  1.00 17.69  ? 59  VAL B CB  1 
ATOM   4580  C CG1 . VAL B 1 59  ? -15.100 46.397  17.611  1.00 13.75  ? 59  VAL B CG1 1 
ATOM   4581  C CG2 . VAL B 1 59  ? -17.029 47.767  16.754  1.00 15.34  ? 59  VAL B CG2 1 
ATOM   4582  N N   . LEU B 1 60  ? -15.696 47.302  20.681  1.00 15.86  ? 60  LEU B N   1 
ATOM   4583  C CA  . LEU B 1 60  ? -16.370 46.793  21.871  1.00 13.42  ? 60  LEU B CA  1 
ATOM   4584  C C   . LEU B 1 60  ? -16.623 47.908  22.878  1.00 13.83  ? 60  LEU B C   1 
ATOM   4585  O O   . LEU B 1 60  ? -17.655 47.911  23.558  1.00 17.39  ? 60  LEU B O   1 
ATOM   4586  C CB  . LEU B 1 60  ? -15.550 45.674  22.513  1.00 12.89  ? 60  LEU B CB  1 
ATOM   4587  C CG  . LEU B 1 60  ? -16.053 45.220  23.883  1.00 12.94  ? 60  LEU B CG  1 
ATOM   4588  C CD1 . LEU B 1 60  ? -17.382 44.502  23.745  1.00 13.14  ? 60  LEU B CD1 1 
ATOM   4589  C CD2 . LEU B 1 60  ? -15.031 44.342  24.585  1.00 13.55  ? 60  LEU B CD2 1 
ATOM   4590  N N   . ILE B 1 61  ? -15.693 48.861  22.984  1.00 13.96  ? 61  ILE B N   1 
ATOM   4591  C CA  . ILE B 1 61  ? -15.901 50.007  23.862  1.00 14.56  ? 61  ILE B CA  1 
ATOM   4592  C C   . ILE B 1 61  ? -17.064 50.852  23.363  1.00 18.81  ? 61  ILE B C   1 
ATOM   4593  O O   . ILE B 1 61  ? -17.826 51.414  24.160  1.00 24.78  ? 61  ILE B O   1 
ATOM   4594  C CB  . ILE B 1 61  ? -14.602 50.826  23.987  1.00 14.67  ? 61  ILE B CB  1 
ATOM   4595  C CG1 . ILE B 1 61  ? -13.522 49.999  24.683  1.00 14.09  ? 61  ILE B CG1 1 
ATOM   4596  C CG2 . ILE B 1 61  ? -14.843 52.109  24.759  1.00 15.51  ? 61  ILE B CG2 1 
ATOM   4597  C CD1 . ILE B 1 61  ? -12.134 50.579  24.565  1.00 14.11  ? 61  ILE B CD1 1 
ATOM   4598  N N   . ASP B 1 62  ? -17.229 50.948  22.041  1.00 19.32  ? 62  ASP B N   1 
ATOM   4599  C CA  . ASP B 1 62  ? -18.377 51.661  21.491  1.00 18.57  ? 62  ASP B CA  1 
ATOM   4600  C C   . ASP B 1 62  ? -19.687 51.015  21.924  1.00 18.98  ? 62  ASP B C   1 
ATOM   4601  O O   . ASP B 1 62  ? -20.636 51.710  22.309  1.00 21.37  ? 62  ASP B O   1 
ATOM   4602  C CB  . ASP B 1 62  ? -18.291 51.701  19.965  1.00 19.74  ? 62  ASP B CB  1 
ATOM   4603  C CG  . ASP B 1 62  ? -17.295 52.724  19.464  1.00 39.91  ? 62  ASP B CG  1 
ATOM   4604  O OD1 . ASP B 1 62  ? -17.113 53.760  20.137  1.00 49.40  ? 62  ASP B OD1 1 
ATOM   4605  O OD2 . ASP B 1 62  ? -16.690 52.491  18.394  1.00 43.15  ? 62  ASP B OD2 1 
ATOM   4606  N N   . GLN B 1 63  ? -19.757 49.684  21.872  1.00 21.05  ? 63  GLN B N   1 
ATOM   4607  C CA  . GLN B 1 63  ? -20.999 48.999  22.208  1.00 15.67  ? 63  GLN B CA  1 
ATOM   4608  C C   . GLN B 1 63  ? -21.295 49.074  23.701  1.00 15.81  ? 63  GLN B C   1 
ATOM   4609  O O   . GLN B 1 63  ? -22.446 49.293  24.094  1.00 26.38  ? 63  GLN B O   1 
ATOM   4610  C CB  . GLN B 1 63  ? -20.943 47.548  21.727  1.00 15.12  ? 63  GLN B CB  1 
ATOM   4611  C CG  . GLN B 1 63  ? -20.756 47.428  20.222  1.00 15.18  ? 63  GLN B CG  1 
ATOM   4612  C CD  . GLN B 1 63  ? -20.757 45.995  19.732  1.00 19.57  ? 63  GLN B CD  1 
ATOM   4613  O OE1 . GLN B 1 63  ? -21.812 45.418  19.466  1.00 19.11  ? 63  GLN B OE1 1 
ATOM   4614  N NE2 . GLN B 1 63  ? -19.571 45.414  19.598  1.00 20.74  ? 63  GLN B NE2 1 
ATOM   4615  N N   . ILE B 1 64  ? -20.274 48.909  24.550  1.00 15.43  ? 64  ILE B N   1 
ATOM   4616  C CA  . ILE B 1 64  ? -20.497 48.993  25.993  1.00 17.72  ? 64  ILE B CA  1 
ATOM   4617  C C   . ILE B 1 64  ? -21.053 50.364  26.362  1.00 19.00  ? 64  ILE B C   1 
ATOM   4618  O O   . ILE B 1 64  ? -21.953 50.481  27.203  1.00 23.86  ? 64  ILE B O   1 
ATOM   4619  C CB  . ILE B 1 64  ? -19.199 48.686  26.768  1.00 18.78  ? 64  ILE B CB  1 
ATOM   4620  C CG1 . ILE B 1 64  ? -18.891 47.189  26.759  1.00 17.13  ? 64  ILE B CG1 1 
ATOM   4621  C CG2 . ILE B 1 64  ? -19.304 49.157  28.214  1.00 19.23  ? 64  ILE B CG2 1 
ATOM   4622  C CD1 . ILE B 1 64  ? -17.403 46.882  26.835  1.00 24.16  ? 64  ILE B CD1 1 
ATOM   4623  N N   . GLN B 1 65  ? -20.536 51.419  25.725  1.00 21.77  ? 65  GLN B N   1 
ATOM   4624  C CA  . GLN B 1 65  ? -21.036 52.765  25.986  1.00 27.32  ? 65  GLN B CA  1 
ATOM   4625  C C   . GLN B 1 65  ? -22.502 52.904  25.599  1.00 28.33  ? 65  GLN B C   1 
ATOM   4626  O O   . GLN B 1 65  ? -23.289 53.508  26.337  1.00 29.00  ? 65  GLN B O   1 
ATOM   4627  C CB  . GLN B 1 65  ? -20.197 53.795  25.232  1.00 27.21  ? 65  GLN B CB  1 
ATOM   4628  C CG  . GLN B 1 65  ? -18.810 54.014  25.797  1.00 27.70  ? 65  GLN B CG  1 
ATOM   4629  C CD  . GLN B 1 65  ? -17.991 54.961  24.945  1.00 30.55  ? 65  GLN B CD  1 
ATOM   4630  O OE1 . GLN B 1 65  ? -17.903 54.798  23.730  1.00 28.76  ? 65  GLN B OE1 1 
ATOM   4631  N NE2 . GLN B 1 65  ? -17.391 55.961  25.580  1.00 25.70  ? 65  GLN B NE2 1 
ATOM   4632  N N   . GLU B 1 66  ? -22.889 52.352  24.446  1.00 22.57  ? 66  GLU B N   1 
ATOM   4633  C CA  . GLU B 1 66  ? -24.259 52.519  23.970  1.00 18.84  ? 66  GLU B CA  1 
ATOM   4634  C C   . GLU B 1 66  ? -25.262 51.920  24.947  1.00 20.32  ? 66  GLU B C   1 
ATOM   4635  O O   . GLU B 1 66  ? -26.347 52.476  25.152  1.00 30.79  ? 66  GLU B O   1 
ATOM   4636  C CB  . GLU B 1 66  ? -24.421 51.897  22.584  1.00 18.51  ? 66  GLU B CB  1 
ATOM   4637  C CG  . GLU B 1 66  ? -25.182 52.783  21.610  1.00 26.00  ? 66  GLU B CG  1 
ATOM   4638  C CD  . GLU B 1 66  ? -25.414 52.121  20.269  1.00 27.49  ? 66  GLU B CD  1 
ATOM   4639  O OE1 . GLU B 1 66  ? -24.707 51.141  19.963  1.00 27.67  ? 66  GLU B OE1 1 
ATOM   4640  O OE2 . GLU B 1 66  ? -26.309 52.575  19.525  1.00 30.08  ? 66  GLU B OE2 1 
ATOM   4641  N N   . TYR B 1 67  ? -24.922 50.781  25.553  1.00 19.83  ? 67  TYR B N   1 
ATOM   4642  C CA  . TYR B 1 67  ? -25.788 50.206  26.576  1.00 24.02  ? 67  TYR B CA  1 
ATOM   4643  C C   . TYR B 1 67  ? -25.798 51.064  27.834  1.00 27.63  ? 67  TYR B C   1 
ATOM   4644  O O   . TYR B 1 67  ? -26.841 51.215  28.481  1.00 30.61  ? 67  TYR B O   1 
ATOM   4645  C CB  . TYR B 1 67  ? -25.338 48.782  26.897  1.00 19.37  ? 67  TYR B CB  1 
ATOM   4646  C CG  . TYR B 1 67  ? -25.696 47.783  25.822  1.00 17.37  ? 67  TYR B CG  1 
ATOM   4647  C CD1 . TYR B 1 67  ? -24.975 47.724  24.640  1.00 19.41  ? 67  TYR B CD1 1 
ATOM   4648  C CD2 . TYR B 1 67  ? -26.755 46.904  25.987  1.00 27.54  ? 67  TYR B CD2 1 
ATOM   4649  C CE1 . TYR B 1 67  ? -25.293 46.818  23.652  1.00 25.58  ? 67  TYR B CE1 1 
ATOM   4650  C CE2 . TYR B 1 67  ? -27.081 45.993  25.006  1.00 26.54  ? 67  TYR B CE2 1 
ATOM   4651  C CZ  . TYR B 1 67  ? -26.346 45.954  23.839  1.00 25.63  ? 67  TYR B CZ  1 
ATOM   4652  O OH  . TYR B 1 67  ? -26.666 45.048  22.854  1.00 28.98  ? 67  TYR B OH  1 
ATOM   4653  N N   . ALA B 1 68  ? -24.645 51.634  28.196  1.00 23.56  ? 68  ALA B N   1 
ATOM   4654  C CA  . ALA B 1 68  ? -24.551 52.415  29.427  1.00 28.22  ? 68  ALA B CA  1 
ATOM   4655  C C   . ALA B 1 68  ? -25.421 53.665  29.361  1.00 30.60  ? 68  ALA B C   1 
ATOM   4656  O O   . ALA B 1 68  ? -26.064 54.037  30.351  1.00 31.00  ? 68  ALA B O   1 
ATOM   4657  C CB  . ALA B 1 68  ? -23.095 52.784  29.704  1.00 25.88  ? 68  ALA B CB  1 
ATOM   4658  N N   . GLN B 1 69  ? -25.452 54.329  28.206  1.00 21.49  ? 69  GLN B N   1 
ATOM   4659  C CA  . GLN B 1 69  ? -26.300 55.501  28.030  1.00 28.47  ? 69  GLN B CA  1 
ATOM   4660  C C   . GLN B 1 69  ? -27.767 55.144  27.837  1.00 34.62  ? 69  GLN B C   1 
ATOM   4661  O O   . GLN B 1 69  ? -28.623 56.028  27.952  1.00 29.35  ? 69  GLN B O   1 
ATOM   4662  C CB  . GLN B 1 69  ? -25.809 56.328  26.839  1.00 27.62  ? 69  GLN B CB  1 
ATOM   4663  C CG  . GLN B 1 69  ? -24.305 56.555  26.837  1.00 46.83  ? 69  GLN B CG  1 
ATOM   4664  C CD  . GLN B 1 69  ? -23.759 56.843  25.452  1.00 53.91  ? 69  GLN B CD  1 
ATOM   4665  O OE1 . GLN B 1 69  ? -24.489 56.795  24.462  1.00 49.64  ? 69  GLN B OE1 1 
ATOM   4666  N NE2 . GLN B 1 69  ? -22.462 57.121  25.372  1.00 39.04  ? 69  GLN B NE2 1 
ATOM   4667  N N   . GLY B 1 70  ? -28.075 53.881  27.556  1.00 27.26  ? 70  GLY B N   1 
ATOM   4668  C CA  . GLY B 1 70  ? -29.443 53.465  27.333  1.00 24.65  ? 70  GLY B CA  1 
ATOM   4669  C C   . GLY B 1 70  ? -29.938 53.611  25.914  1.00 22.64  ? 70  GLY B C   1 
ATOM   4670  O O   . GLY B 1 70  ? -31.154 53.597  25.696  1.00 23.98  ? 70  GLY B O   1 
ATOM   4671  N N   . LYS B 1 71  ? -29.040 53.744  24.939  1.00 22.10  ? 71  LYS B N   1 
ATOM   4672  C CA  . LYS B 1 71  ? -29.410 53.966  23.548  1.00 22.36  ? 71  LYS B CA  1 
ATOM   4673  C C   . LYS B 1 71  ? -29.318 52.699  22.702  1.00 30.06  ? 71  LYS B C   1 
ATOM   4674  O O   . LYS B 1 71  ? -29.272 52.789  21.471  1.00 32.65  ? 71  LYS B O   1 
ATOM   4675  C CB  . LYS B 1 71  ? -28.532 55.061  22.939  1.00 24.64  ? 71  LYS B CB  1 
ATOM   4676  C CG  . LYS B 1 71  ? -28.796 56.457  23.478  1.00 30.39  ? 71  LYS B CG  1 
ATOM   4677  C CD  . LYS B 1 71  ? -27.550 57.325  23.380  1.00 35.42  ? 71  LYS B CD  1 
ATOM   4678  C CE  . LYS B 1 71  ? -27.744 58.661  24.080  1.00 47.13  ? 71  LYS B CE  1 
ATOM   4679  N NZ  . LYS B 1 71  ? -27.007 59.762  23.398  1.00 43.74  ? 71  LYS B NZ  1 
ATOM   4680  N N   . ALA B 1 72  ? -29.292 51.525  23.331  1.00 29.16  ? 72  ALA B N   1 
ATOM   4681  C CA  . ALA B 1 72  ? -29.104 50.270  22.615  1.00 19.97  ? 72  ALA B CA  1 
ATOM   4682  C C   . ALA B 1 72  ? -30.450 49.655  22.255  1.00 28.57  ? 72  ALA B C   1 
ATOM   4683  O O   . ALA B 1 72  ? -31.296 49.439  23.129  1.00 36.89  ? 72  ALA B O   1 
ATOM   4684  C CB  . ALA B 1 72  ? -28.284 49.289  23.453  1.00 19.96  ? 72  ALA B CB  1 
ATOM   4685  N N   . LYS B 1 73  ? -30.638 49.372  20.968  1.00 30.42  ? 73  LYS B N   1 
ATOM   4686  C CA  . LYS B 1 73  ? -31.866 48.748  20.473  1.00 36.32  ? 73  LYS B CA  1 
ATOM   4687  C C   . LYS B 1 73  ? -31.666 47.235  20.370  1.00 41.82  ? 73  LYS B C   1 
ATOM   4688  O O   . LYS B 1 73  ? -31.530 46.659  19.291  1.00 39.92  ? 73  LYS B O   1 
ATOM   4689  C CB  . LYS B 1 73  ? -32.263 49.360  19.131  1.00 37.53  ? 73  LYS B CB  1 
ATOM   4690  C CG  . LYS B 1 73  ? -33.568 50.139  19.150  1.00 39.32  ? 73  LYS B CG  1 
ATOM   4691  C CD  . LYS B 1 73  ? -33.428 51.447  19.912  1.00 50.88  ? 73  LYS B CD  1 
ATOM   4692  C CE  . LYS B 1 73  ? -32.661 52.486  19.107  1.00 55.06  ? 73  LYS B CE  1 
ATOM   4693  N NZ  . LYS B 1 73  ? -32.291 53.668  19.938  1.00 46.38  ? 73  LYS B NZ  1 
ATOM   4694  N N   . ASP B 1 74  ? -31.649 46.593  21.537  1.00 37.58  ? 74  ASP B N   1 
ATOM   4695  C CA  . ASP B 1 74  ? -31.404 45.154  21.641  1.00 37.24  ? 74  ASP B CA  1 
ATOM   4696  C C   . ASP B 1 74  ? -32.729 44.413  21.503  1.00 34.37  ? 74  ASP B C   1 
ATOM   4697  O O   . ASP B 1 74  ? -33.471 44.264  22.476  1.00 39.25  ? 74  ASP B O   1 
ATOM   4698  C CB  . ASP B 1 74  ? -30.722 44.818  22.962  1.00 37.99  ? 74  ASP B CB  1 
ATOM   4699  C CG  . ASP B 1 74  ? -29.648 43.760  22.809  1.00 39.16  ? 74  ASP B CG  1 
ATOM   4700  O OD1 . ASP B 1 74  ? -29.926 42.717  22.183  1.00 43.43  ? 74  ASP B OD1 1 
ATOM   4701  O OD2 . ASP B 1 74  ? -28.534 43.958  23.332  1.00 33.58  ? 74  ASP B OD2 1 
ATOM   4702  N N   . VAL B 1 75  ? -33.009 43.913  20.295  1.00 27.34  ? 75  VAL B N   1 
ATOM   4703  C CA  . VAL B 1 75  ? -34.304 43.290  20.021  1.00 36.42  ? 75  VAL B CA  1 
ATOM   4704  C C   . VAL B 1 75  ? -34.537 42.100  20.945  1.00 35.24  ? 75  VAL B C   1 
ATOM   4705  O O   . VAL B 1 75  ? -35.612 41.955  21.540  1.00 36.15  ? 75  VAL B O   1 
ATOM   4706  C CB  . VAL B 1 75  ? -34.400 42.878  18.540  1.00 40.57  ? 75  VAL B CB  1 
ATOM   4707  C CG1 . VAL B 1 75  ? -34.776 44.070  17.680  1.00 36.20  ? 75  VAL B CG1 1 
ATOM   4708  C CG2 . VAL B 1 75  ? -33.089 42.268  18.065  1.00 29.80  ? 75  VAL B CG2 1 
ATOM   4709  N N   . PHE B 1 76  ? -33.532 41.233  21.081  1.00 35.23  ? 76  PHE B N   1 
ATOM   4710  C CA  . PHE B 1 76  ? -33.688 40.056  21.930  1.00 26.70  ? 76  PHE B CA  1 
ATOM   4711  C C   . PHE B 1 76  ? -33.859 40.444  23.393  1.00 30.46  ? 76  PHE B C   1 
ATOM   4712  O O   . PHE B 1 76  ? -34.653 39.828  24.114  1.00 26.52  ? 76  PHE B O   1 
ATOM   4713  C CB  . PHE B 1 76  ? -32.492 39.119  21.756  1.00 23.59  ? 76  PHE B CB  1 
ATOM   4714  C CG  . PHE B 1 76  ? -32.502 37.947  22.694  1.00 19.95  ? 76  PHE B CG  1 
ATOM   4715  C CD1 . PHE B 1 76  ? -33.184 36.789  22.364  1.00 20.64  ? 76  PHE B CD1 1 
ATOM   4716  C CD2 . PHE B 1 76  ? -31.826 37.999  23.903  1.00 26.08  ? 76  PHE B CD2 1 
ATOM   4717  C CE1 . PHE B 1 76  ? -33.196 35.707  23.224  1.00 25.20  ? 76  PHE B CE1 1 
ATOM   4718  C CE2 . PHE B 1 76  ? -31.834 36.920  24.765  1.00 20.69  ? 76  PHE B CE2 1 
ATOM   4719  C CZ  . PHE B 1 76  ? -32.522 35.775  24.426  1.00 20.49  ? 76  PHE B CZ  1 
ATOM   4720  N N   . LEU B 1 77  ? -33.111 41.449  23.857  1.00 33.92  ? 77  LEU B N   1 
ATOM   4721  C CA  . LEU B 1 77  ? -33.207 41.850  25.257  1.00 30.05  ? 77  LEU B CA  1 
ATOM   4722  C C   . LEU B 1 77  ? -34.552 42.498  25.560  1.00 30.26  ? 77  LEU B C   1 
ATOM   4723  O O   . LEU B 1 77  ? -35.139 42.254  26.621  1.00 35.07  ? 77  LEU B O   1 
ATOM   4724  C CB  . LEU B 1 77  ? -32.070 42.801  25.621  1.00 26.00  ? 77  LEU B CB  1 
ATOM   4725  C CG  . LEU B 1 77  ? -32.164 43.337  27.050  1.00 24.11  ? 77  LEU B CG  1 
ATOM   4726  C CD1 . LEU B 1 77  ? -31.748 42.266  28.047  1.00 25.81  ? 77  LEU B CD1 1 
ATOM   4727  C CD2 . LEU B 1 77  ? -31.331 44.595  27.224  1.00 32.53  ? 77  LEU B CD2 1 
ATOM   4728  N N   . GLU B 1 78  ? -35.057 43.327  24.644  1.00 28.78  ? 78  GLU B N   1 
ATOM   4729  C CA  . GLU B 1 78  ? -36.358 43.946  24.858  1.00 27.87  ? 78  GLU B CA  1 
ATOM   4730  C C   . GLU B 1 78  ? -37.483 42.921  24.846  1.00 29.06  ? 78  GLU B C   1 
ATOM   4731  O O   . GLU B 1 78  ? -38.577 43.216  25.339  1.00 38.59  ? 78  GLU B O   1 
ATOM   4732  C CB  . GLU B 1 78  ? -36.608 45.041  23.813  1.00 38.09  ? 78  GLU B CB  1 
ATOM   4733  C CG  . GLU B 1 78  ? -36.288 46.447  24.326  1.00 58.95  ? 78  GLU B CG  1 
ATOM   4734  C CD  . GLU B 1 78  ? -34.857 46.893  24.042  1.00 77.18  ? 78  GLU B CD  1 
ATOM   4735  O OE1 . GLU B 1 78  ? -34.365 46.669  22.916  1.00 82.41  ? 78  GLU B OE1 1 
ATOM   4736  O OE2 . GLU B 1 78  ? -34.215 47.457  24.956  1.00 66.32  ? 78  GLU B OE2 1 
ATOM   4737  N N   . ALA B 1 79  ? -37.239 41.728  24.296  1.00 34.48  ? 79  ALA B N   1 
ATOM   4738  C CA  . ALA B 1 79  ? -38.193 40.632  24.427  1.00 24.39  ? 79  ALA B CA  1 
ATOM   4739  C C   . ALA B 1 79  ? -38.160 40.015  25.820  1.00 23.75  ? 79  ALA B C   1 
ATOM   4740  O O   . ALA B 1 79  ? -39.195 39.555  26.314  1.00 31.56  ? 79  ALA B O   1 
ATOM   4741  C CB  . ALA B 1 79  ? -37.917 39.561  23.373  1.00 23.44  ? 79  ALA B CB  1 
ATOM   4742  N N   . ILE B 1 80  ? -36.987 39.978  26.459  1.00 29.58  ? 80  ILE B N   1 
ATOM   4743  C CA  . ILE B 1 80  ? -36.911 39.522  27.843  1.00 25.39  ? 80  ILE B CA  1 
ATOM   4744  C C   . ILE B 1 80  ? -37.571 40.531  28.775  1.00 27.09  ? 80  ILE B C   1 
ATOM   4745  O O   . ILE B 1 80  ? -38.227 40.155  29.753  1.00 27.41  ? 80  ILE B O   1 
ATOM   4746  C CB  . ILE B 1 80  ? -35.449 39.260  28.248  1.00 24.64  ? 80  ILE B CB  1 
ATOM   4747  C CG1 . ILE B 1 80  ? -34.755 38.345  27.238  1.00 23.70  ? 80  ILE B CG1 1 
ATOM   4748  C CG2 . ILE B 1 80  ? -35.383 38.657  29.644  1.00 22.83  ? 80  ILE B CG2 1 
ATOM   4749  C CD1 . ILE B 1 80  ? -33.386 37.886  27.690  1.00 21.04  ? 80  ILE B CD1 1 
ATOM   4750  N N   . ARG B 1 81  ? -37.404 41.825  28.491  1.00 23.76  ? 81  ARG B N   1 
ATOM   4751  C CA  . ARG B 1 81  ? -37.873 42.863  29.404  1.00 24.47  ? 81  ARG B CA  1 
ATOM   4752  C C   . ARG B 1 81  ? -39.392 42.862  29.533  1.00 33.33  ? 81  ARG B C   1 
ATOM   4753  O O   . ARG B 1 81  ? -39.930 42.909  30.645  1.00 36.03  ? 81  ARG B O   1 
ATOM   4754  C CB  . ARG B 1 81  ? -37.379 44.230  28.930  1.00 24.14  ? 81  ARG B CB  1 
ATOM   4755  C CG  . ARG B 1 81  ? -37.691 45.372  29.883  1.00 24.94  ? 81  ARG B CG  1 
ATOM   4756  C CD  . ARG B 1 81  ? -38.074 46.639  29.132  1.00 34.08  ? 81  ARG B CD  1 
ATOM   4757  N NE  . ARG B 1 81  ? -39.472 46.633  28.713  1.00 62.33  ? 81  ARG B NE  1 
ATOM   4758  C CZ  . ARG B 1 81  ? -40.495 46.935  29.502  1.00 62.20  ? 81  ARG B CZ  1 
ATOM   4759  N NH1 . ARG B 1 81  ? -40.315 47.271  30.770  1.00 57.21  ? 81  ARG B NH1 1 
ATOM   4760  N NH2 . ARG B 1 81  ? -41.730 46.898  29.008  1.00 46.66  ? 81  ARG B NH2 1 
ATOM   4761  N N   . LYS B 1 82  ? -40.099 42.798  28.408  1.00 32.27  ? 82  LYS B N   1 
ATOM   4762  C CA  . LYS B 1 82  ? -41.528 43.071  28.396  1.00 27.35  ? 82  LYS B CA  1 
ATOM   4763  C C   . LYS B 1 82  ? -42.315 41.942  29.063  1.00 27.78  ? 82  LYS B C   1 
ATOM   4764  O O   . LYS B 1 82  ? -41.792 40.866  29.367  1.00 27.42  ? 82  LYS B O   1 
ATOM   4765  C CB  . LYS B 1 82  ? -42.020 43.282  26.964  1.00 27.12  ? 82  LYS B CB  1 
ATOM   4766  C CG  . LYS B 1 82  ? -41.799 42.091  26.053  1.00 26.67  ? 82  LYS B CG  1 
ATOM   4767  C CD  . LYS B 1 82  ? -42.524 42.278  24.733  1.00 27.28  ? 82  LYS B CD  1 
ATOM   4768  C CE  . LYS B 1 82  ? -41.973 43.469  23.968  1.00 26.76  ? 82  LYS B CE  1 
ATOM   4769  N NZ  . LYS B 1 82  ? -42.396 43.451  22.542  1.00 28.57  ? 82  LYS B NZ  1 
ATOM   4770  N N   . ASP B 1 83  ? -43.595 42.217  29.299  1.00 28.97  ? 83  ASP B N   1 
ATOM   4771  C CA  . ASP B 1 83  ? -44.487 41.239  29.903  1.00 29.92  ? 83  ASP B CA  1 
ATOM   4772  C C   . ASP B 1 83  ? -44.722 40.076  28.941  1.00 33.84  ? 83  ASP B C   1 
ATOM   4773  O O   . ASP B 1 83  ? -44.838 40.287  27.730  1.00 36.35  ? 83  ASP B O   1 
ATOM   4774  C CB  . ASP B 1 83  ? -45.817 41.901  30.269  1.00 31.37  ? 83  ASP B CB  1 
ATOM   4775  C CG  . ASP B 1 83  ? -46.653 41.061  31.215  1.00 44.38  ? 83  ASP B CG  1 
ATOM   4776  O OD1 . ASP B 1 83  ? -47.312 40.113  30.742  1.00 47.73  ? 83  ASP B OD1 1 
ATOM   4777  O OD2 . ASP B 1 83  ? -46.656 41.352  32.430  1.00 49.13  ? 83  ASP B OD2 1 
ATOM   4778  N N   . PRO B 1 84  ? -44.797 38.841  29.445  1.00 30.14  ? 84  PRO B N   1 
ATOM   4779  C CA  . PRO B 1 84  ? -45.057 37.699  28.552  1.00 30.26  ? 84  PRO B CA  1 
ATOM   4780  C C   . PRO B 1 84  ? -46.383 37.788  27.819  1.00 36.09  ? 84  PRO B C   1 
ATOM   4781  O O   . PRO B 1 84  ? -46.524 37.175  26.753  1.00 44.34  ? 84  PRO B O   1 
ATOM   4782  C CB  . PRO B 1 84  ? -45.017 36.491  29.500  1.00 30.77  ? 84  PRO B CB  1 
ATOM   4783  C CG  . PRO B 1 84  ? -44.263 36.970  30.700  1.00 35.48  ? 84  PRO B CG  1 
ATOM   4784  C CD  . PRO B 1 84  ? -44.606 38.416  30.840  1.00 34.75  ? 84  PRO B CD  1 
ATOM   4785  N N   . ASP B 1 85  ? -47.361 38.521  28.356  1.00 32.22  ? 85  ASP B N   1 
ATOM   4786  C CA  . ASP B 1 85  ? -48.602 38.749  27.623  1.00 33.21  ? 85  ASP B CA  1 
ATOM   4787  C C   . ASP B 1 85  ? -48.359 39.571  26.363  1.00 33.25  ? 85  ASP B C   1 
ATOM   4788  O O   . ASP B 1 85  ? -49.067 39.401  25.364  1.00 41.01  ? 85  ASP B O   1 
ATOM   4789  C CB  . ASP B 1 85  ? -49.624 39.450  28.519  1.00 34.38  ? 85  ASP B CB  1 
ATOM   4790  C CG  . ASP B 1 85  ? -49.941 38.663  29.777  1.00 44.65  ? 85  ASP B CG  1 
ATOM   4791  O OD1 . ASP B 1 85  ? -50.093 37.426  29.685  1.00 41.33  ? 85  ASP B OD1 1 
ATOM   4792  O OD2 . ASP B 1 85  ? -50.043 39.284  30.858  1.00 43.34  ? 85  ASP B OD2 1 
ATOM   4793  N N   . ASP B 1 86  ? -47.368 40.462  26.390  1.00 31.66  ? 86  ASP B N   1 
ATOM   4794  C CA  . ASP B 1 86  ? -47.048 41.313  25.251  1.00 31.21  ? 86  ASP B CA  1 
ATOM   4795  C C   . ASP B 1 86  ? -46.135 40.636  24.240  1.00 30.29  ? 86  ASP B C   1 
ATOM   4796  O O   . ASP B 1 86  ? -45.820 41.244  23.211  1.00 35.25  ? 86  ASP B O   1 
ATOM   4797  C CB  . ASP B 1 86  ? -46.394 42.613  25.727  1.00 31.11  ? 86  ASP B CB  1 
ATOM   4798  C CG  . ASP B 1 86  ? -47.404 43.629  26.213  1.00 36.08  ? 86  ASP B CG  1 
ATOM   4799  O OD1 . ASP B 1 86  ? -48.548 43.615  25.714  1.00 32.91  ? 86  ASP B OD1 1 
ATOM   4800  O OD2 . ASP B 1 86  ? -47.046 44.453  27.080  1.00 46.56  ? 86  ASP B OD2 1 
ATOM   4801  N N   . LEU B 1 87  ? -45.700 39.409  24.503  1.00 31.37  ? 87  LEU B N   1 
ATOM   4802  C CA  . LEU B 1 87  ? -44.790 38.717  23.603  1.00 29.91  ? 87  LEU B CA  1 
ATOM   4803  C C   . LEU B 1 87  ? -45.540 38.206  22.381  1.00 36.27  ? 87  LEU B C   1 
ATOM   4804  O O   . LEU B 1 87  ? -46.605 37.594  22.504  1.00 37.61  ? 87  LEU B O   1 
ATOM   4805  C CB  . LEU B 1 87  ? -44.110 37.555  24.325  1.00 28.76  ? 87  LEU B CB  1 
ATOM   4806  C CG  . LEU B 1 87  ? -42.872 37.907  25.143  1.00 27.68  ? 87  LEU B CG  1 
ATOM   4807  C CD1 . LEU B 1 87  ? -42.223 36.641  25.661  1.00 27.44  ? 87  LEU B CD1 1 
ATOM   4808  C CD2 . LEU B 1 87  ? -41.889 38.716  24.312  1.00 26.68  ? 87  LEU B CD2 1 
ATOM   4809  N N   . GLU B 1 88  ? -44.985 38.461  21.202  1.00 34.21  ? 88  GLU B N   1 
ATOM   4810  C CA  . GLU B 1 88  ? -45.509 37.848  19.997  1.00 34.94  ? 88  GLU B CA  1 
ATOM   4811  C C   . GLU B 1 88  ? -44.922 36.453  19.831  1.00 39.95  ? 88  GLU B C   1 
ATOM   4812  O O   . GLU B 1 88  ? -43.875 36.121  20.394  1.00 37.91  ? 88  GLU B O   1 
ATOM   4813  C CB  . GLU B 1 88  ? -45.198 38.704  18.768  1.00 38.10  ? 88  GLU B CB  1 
ATOM   4814  C CG  . GLU B 1 88  ? -45.677 40.137  18.881  1.00 42.54  ? 88  GLU B CG  1 
ATOM   4815  C CD  . GLU B 1 88  ? -47.116 40.232  19.349  1.00 44.75  ? 88  GLU B CD  1 
ATOM   4816  O OE1 . GLU B 1 88  ? -47.985 39.565  18.749  1.00 40.87  ? 88  GLU B OE1 1 
ATOM   4817  O OE2 . GLU B 1 88  ? -47.377 40.970  20.322  1.00 44.56  ? 88  GLU B OE2 1 
ATOM   4818  N N   . LYS B 1 89  ? -45.619 35.627  19.048  1.00 41.68  ? 89  LYS B N   1 
ATOM   4819  C CA  . LYS B 1 89  ? -45.131 34.277  18.804  1.00 47.10  ? 89  LYS B CA  1 
ATOM   4820  C C   . LYS B 1 89  ? -43.774 34.280  18.112  1.00 39.40  ? 89  LYS B C   1 
ATOM   4821  O O   . LYS B 1 89  ? -43.023 33.313  18.250  1.00 35.74  ? 89  LYS B O   1 
ATOM   4822  C CB  . LYS B 1 89  ? -46.159 33.486  17.994  1.00 50.84  ? 89  LYS B CB  1 
ATOM   4823  C CG  . LYS B 1 89  ? -47.444 33.205  18.770  1.00 43.92  ? 89  LYS B CG  1 
ATOM   4824  C CD  . LYS B 1 89  ? -48.571 32.731  17.868  1.00 44.28  ? 89  LYS B CD  1 
ATOM   4825  C CE  . LYS B 1 89  ? -49.899 32.723  18.613  1.00 39.97  ? 89  LYS B CE  1 
ATOM   4826  N NZ  . LYS B 1 89  ? -51.026 33.189  17.758  1.00 46.45  ? 89  LYS B NZ  1 
ATOM   4827  N N   . GLU B 1 90  ? -43.432 35.352  17.395  1.00 37.12  ? 90  GLU B N   1 
ATOM   4828  C CA  . GLU B 1 90  ? -42.086 35.468  16.844  1.00 38.83  ? 90  GLU B CA  1 
ATOM   4829  C C   . GLU B 1 90  ? -41.049 35.658  17.946  1.00 41.15  ? 90  GLU B C   1 
ATOM   4830  O O   . GLU B 1 90  ? -39.944 35.109  17.868  1.00 50.09  ? 90  GLU B O   1 
ATOM   4831  C CB  . GLU B 1 90  ? -42.026 36.622  15.842  1.00 50.59  ? 90  GLU B CB  1 
ATOM   4832  C CG  . GLU B 1 90  ? -42.450 37.967  16.415  1.00 61.22  ? 90  GLU B CG  1 
ATOM   4833  C CD  . GLU B 1 90  ? -42.292 39.103  15.426  1.00 71.51  ? 90  GLU B CD  1 
ATOM   4834  O OE1 . GLU B 1 90  ? -42.202 38.827  14.212  1.00 92.01  ? 90  GLU B OE1 1 
ATOM   4835  O OE2 . GLU B 1 90  ? -42.256 40.273  15.864  1.00 53.86  ? 90  GLU B OE2 1 
ATOM   4836  N N   . GLU B 1 91  ? -41.385 36.435  18.980  1.00 41.24  ? 91  GLU B N   1 
ATOM   4837  C CA  . GLU B 1 91  ? -40.437 36.690  20.060  1.00 33.66  ? 91  GLU B CA  1 
ATOM   4838  C C   . GLU B 1 91  ? -40.250 35.461  20.940  1.00 29.40  ? 91  GLU B C   1 
ATOM   4839  O O   . GLU B 1 91  ? -39.132 35.170  21.379  1.00 25.37  ? 91  GLU B O   1 
ATOM   4840  C CB  . GLU B 1 91  ? -40.907 37.875  20.902  1.00 33.10  ? 91  GLU B CB  1 
ATOM   4841  C CG  . GLU B 1 91  ? -41.008 39.186  20.146  1.00 38.13  ? 91  GLU B CG  1 
ATOM   4842  C CD  . GLU B 1 91  ? -41.599 40.296  20.994  1.00 35.92  ? 91  GLU B CD  1 
ATOM   4843  O OE1 . GLU B 1 91  ? -42.808 40.230  21.297  1.00 40.55  ? 91  GLU B OE1 1 
ATOM   4844  O OE2 . GLU B 1 91  ? -40.855 41.229  21.364  1.00 37.20  ? 91  GLU B OE2 1 
ATOM   4845  N N   . VAL B 1 92  ? -41.336 34.738  21.221  1.00 27.29  ? 92  VAL B N   1 
ATOM   4846  C CA  . VAL B 1 92  ? -41.239 33.553  22.069  1.00 27.56  ? 92  VAL B CA  1 
ATOM   4847  C C   . VAL B 1 92  ? -40.375 32.492  21.401  1.00 36.15  ? 92  VAL B C   1 
ATOM   4848  O O   . VAL B 1 92  ? -39.571 31.822  22.060  1.00 40.43  ? 92  VAL B O   1 
ATOM   4849  C CB  . VAL B 1 92  ? -42.642 33.020  22.414  1.00 28.93  ? 92  VAL B CB  1 
ATOM   4850  C CG1 . VAL B 1 92  ? -42.544 31.695  23.154  1.00 29.43  ? 92  VAL B CG1 1 
ATOM   4851  C CG2 . VAL B 1 92  ? -43.401 34.039  23.249  1.00 29.13  ? 92  VAL B CG2 1 
ATOM   4852  N N   . GLU B 1 93  ? -40.517 32.329  20.082  1.00 35.28  ? 93  GLU B N   1 
ATOM   4853  C CA  . GLU B 1 93  ? -39.638 31.413  19.359  1.00 29.22  ? 93  GLU B CA  1 
ATOM   4854  C C   . GLU B 1 93  ? -38.179 31.815  19.527  1.00 30.45  ? 93  GLU B C   1 
ATOM   4855  O O   . GLU B 1 93  ? -37.298 30.952  19.617  1.00 35.55  ? 93  GLU B O   1 
ATOM   4856  C CB  . GLU B 1 93  ? -40.013 31.365  17.876  1.00 42.65  ? 93  GLU B CB  1 
ATOM   4857  C CG  . GLU B 1 93  ? -41.443 30.915  17.608  1.00 64.39  ? 93  GLU B CG  1 
ATOM   4858  C CD  . GLU B 1 93  ? -41.549 29.829  16.558  1.00 76.03  ? 93  GLU B CD  1 
ATOM   4859  O OE1 . GLU B 1 93  ? -40.737 29.835  15.609  1.00 83.86  ? 93  GLU B OE1 1 
ATOM   4860  O OE2 . GLU B 1 93  ? -42.463 28.984  16.672  1.00 60.54  ? 93  GLU B OE2 1 
ATOM   4861  N N   . LYS B 1 94  ? -37.904 33.121  19.573  1.00 33.18  ? 94  LYS B N   1 
ATOM   4862  C CA  . LYS B 1 94  ? -36.542 33.579  19.833  1.00 35.45  ? 94  LYS B CA  1 
ATOM   4863  C C   . LYS B 1 94  ? -36.082 33.180  21.230  1.00 35.20  ? 94  LYS B C   1 
ATOM   4864  O O   . LYS B 1 94  ? -34.941 32.736  21.410  1.00 39.09  ? 94  LYS B O   1 
ATOM   4865  C CB  . LYS B 1 94  ? -36.453 35.095  19.651  1.00 37.17  ? 94  LYS B CB  1 
ATOM   4866  C CG  . LYS B 1 94  ? -35.813 35.534  18.347  1.00 39.76  ? 94  LYS B CG  1 
ATOM   4867  C CD  . LYS B 1 94  ? -36.787 35.419  17.189  1.00 45.27  ? 94  LYS B CD  1 
ATOM   4868  C CE  . LYS B 1 94  ? -36.554 36.514  16.163  1.00 48.87  ? 94  LYS B CE  1 
ATOM   4869  N NZ  . LYS B 1 94  ? -37.764 36.765  15.332  1.00 44.19  ? 94  LYS B NZ  1 
ATOM   4870  N N   . LEU B 1 95  ? -36.952 33.335  22.232  1.00 29.36  ? 95  LEU B N   1 
ATOM   4871  C CA  . LEU B 1 95  ? -36.584 32.958  23.593  1.00 24.19  ? 95  LEU B CA  1 
ATOM   4872  C C   . LEU B 1 95  ? -36.297 31.468  23.694  1.00 24.71  ? 95  LEU B C   1 
ATOM   4873  O O   . LEU B 1 95  ? -35.334 31.058  24.353  1.00 32.77  ? 95  LEU B O   1 
ATOM   4874  C CB  . LEU B 1 95  ? -37.687 33.357  24.573  1.00 29.31  ? 95  LEU B CB  1 
ATOM   4875  C CG  . LEU B 1 95  ? -37.596 34.765  25.167  1.00 40.48  ? 95  LEU B CG  1 
ATOM   4876  C CD1 . LEU B 1 95  ? -38.945 35.210  25.701  1.00 31.65  ? 95  LEU B CD1 1 
ATOM   4877  C CD2 . LEU B 1 95  ? -36.540 34.822  26.260  1.00 29.77  ? 95  LEU B CD2 1 
ATOM   4878  N N   . ILE B 1 96  ? -37.122 30.642  23.051  1.00 30.93  ? 96  ILE B N   1 
ATOM   4879  C CA  . ILE B 1 96  ? -36.873 29.206  23.037  1.00 26.50  ? 96  ILE B CA  1 
ATOM   4880  C C   . ILE B 1 96  ? -35.620 28.890  22.231  1.00 30.93  ? 96  ILE B C   1 
ATOM   4881  O O   . ILE B 1 96  ? -34.809 28.044  22.628  1.00 27.11  ? 96  ILE B O   1 
ATOM   4882  C CB  . ILE B 1 96  ? -38.104 28.461  22.492  1.00 27.87  ? 96  ILE B CB  1 
ATOM   4883  C CG1 . ILE B 1 96  ? -39.372 28.909  23.220  1.00 28.50  ? 96  ILE B CG1 1 
ATOM   4884  C CG2 . ILE B 1 96  ? -37.923 26.967  22.655  1.00 32.78  ? 96  ILE B CG2 1 
ATOM   4885  C CD1 . ILE B 1 96  ? -39.402 28.550  24.683  1.00 28.79  ? 96  ILE B CD1 1 
ATOM   4886  N N   . GLU B 1 97  ? -35.443 29.564  21.090  1.00 38.49  ? 97  GLU B N   1 
ATOM   4887  C CA  . GLU B 1 97  ? -34.246 29.370  20.274  1.00 32.45  ? 97  GLU B CA  1 
ATOM   4888  C C   . GLU B 1 97  ? -32.978 29.626  21.078  1.00 27.07  ? 97  GLU B C   1 
ATOM   4889  O O   . GLU B 1 97  ? -32.005 28.870  20.982  1.00 30.58  ? 97  GLU B O   1 
ATOM   4890  C CB  . GLU B 1 97  ? -34.296 30.298  19.058  1.00 43.60  ? 97  GLU B CB  1 
ATOM   4891  C CG  . GLU B 1 97  ? -33.810 29.692  17.754  1.00 55.40  ? 97  GLU B CG  1 
ATOM   4892  C CD  . GLU B 1 97  ? -33.733 30.721  16.643  1.00 70.81  ? 97  GLU B CD  1 
ATOM   4893  O OE1 . GLU B 1 97  ? -33.021 30.477  15.645  1.00 56.59  ? 97  GLU B OE1 1 
ATOM   4894  O OE2 . GLU B 1 97  ? -34.385 31.778  16.772  1.00 73.50  ? 97  GLU B OE2 1 
ATOM   4895  N N   . PHE B 1 98  ? -32.977 30.688  21.885  1.00 23.00  ? 98  PHE B N   1 
ATOM   4896  C CA  . PHE B 1 98  ? -31.800 31.032  22.674  1.00 22.59  ? 98  PHE B CA  1 
ATOM   4897  C C   . PHE B 1 98  ? -31.533 30.007  23.769  1.00 22.45  ? 98  PHE B C   1 
ATOM   4898  O O   . PHE B 1 98  ? -30.374 29.671  24.041  1.00 24.66  ? 98  PHE B O   1 
ATOM   4899  C CB  . PHE B 1 98  ? -31.978 32.419  23.284  1.00 28.57  ? 98  PHE B CB  1 
ATOM   4900  C CG  . PHE B 1 98  ? -30.694 33.073  23.679  1.00 23.83  ? 98  PHE B CG  1 
ATOM   4901  C CD1 . PHE B 1 98  ? -29.791 33.496  22.718  1.00 23.17  ? 98  PHE B CD1 1 
ATOM   4902  C CD2 . PHE B 1 98  ? -30.382 33.254  25.014  1.00 27.74  ? 98  PHE B CD2 1 
ATOM   4903  C CE1 . PHE B 1 98  ? -28.608 34.103  23.081  1.00 23.43  ? 98  PHE B CE1 1 
ATOM   4904  C CE2 . PHE B 1 98  ? -29.198 33.857  25.387  1.00 20.04  ? 98  PHE B CE2 1 
ATOM   4905  C CZ  . PHE B 1 98  ? -28.308 34.281  24.418  1.00 22.55  ? 98  PHE B CZ  1 
ATOM   4906  N N   . THR B 1 99  ? -32.588 29.514  24.423  1.00 23.42  ? 99  THR B N   1 
ATOM   4907  C CA  . THR B 1 99  ? -32.398 28.576  25.526  1.00 24.89  ? 99  THR B CA  1 
ATOM   4908  C C   . THR B 1 99  ? -31.940 27.212  25.022  1.00 32.16  ? 99  THR B C   1 
ATOM   4909  O O   . THR B 1 99  ? -31.031 26.606  25.602  1.00 32.19  ? 99  THR B O   1 
ATOM   4910  C CB  . THR B 1 99  ? -33.684 28.448  26.342  1.00 25.02  ? 99  THR B CB  1 
ATOM   4911  O OG1 . THR B 1 99  ? -34.032 29.729  26.881  1.00 24.50  ? 99  THR B OG1 1 
ATOM   4912  C CG2 . THR B 1 99  ? -33.492 27.474  27.489  1.00 25.81  ? 99  THR B CG2 1 
ATOM   4913  N N   . LYS B 1 100 ? -32.550 26.715  23.940  1.00 34.16  ? 100 LYS B N   1 
ATOM   4914  C CA  . LYS B 1 100 ? -32.070 25.475  23.337  1.00 26.08  ? 100 LYS B CA  1 
ATOM   4915  C C   . LYS B 1 100 ? -30.620 25.601  22.889  1.00 25.76  ? 100 LYS B C   1 
ATOM   4916  O O   . LYS B 1 100 ? -29.905 24.596  22.808  1.00 33.94  ? 100 LYS B O   1 
ATOM   4917  C CB  . LYS B 1 100 ? -32.939 25.066  22.144  1.00 27.02  ? 100 LYS B CB  1 
ATOM   4918  C CG  . LYS B 1 100 ? -34.426 24.925  22.429  1.00 37.22  ? 100 LYS B CG  1 
ATOM   4919  C CD  . LYS B 1 100 ? -35.059 23.908  21.488  1.00 35.73  ? 100 LYS B CD  1 
ATOM   4920  C CE  . LYS B 1 100 ? -36.569 24.077  21.395  1.00 44.95  ? 100 LYS B CE  1 
ATOM   4921  N NZ  . LYS B 1 100 ? -36.948 24.953  20.254  1.00 59.91  ? 100 LYS B NZ  1 
ATOM   4922  N N   . LEU B 1 101 ? -30.170 26.822  22.586  1.00 27.17  ? 101 LEU B N   1 
ATOM   4923  C CA  . LEU B 1 101 ? -28.789 27.020  22.157  1.00 30.04  ? 101 LEU B CA  1 
ATOM   4924  C C   . LEU B 1 101 ? -27.817 26.831  23.315  1.00 26.70  ? 101 LEU B C   1 
ATOM   4925  O O   . LEU B 1 101 ? -26.885 26.023  23.230  1.00 35.10  ? 101 LEU B O   1 
ATOM   4926  C CB  . LEU B 1 101 ? -28.626 28.407  21.543  1.00 23.26  ? 101 LEU B CB  1 
ATOM   4927  C CG  . LEU B 1 101 ? -27.373 28.548  20.680  1.00 24.77  ? 101 LEU B CG  1 
ATOM   4928  C CD1 . LEU B 1 101 ? -27.612 27.965  19.293  1.00 27.10  ? 101 LEU B CD1 1 
ATOM   4929  C CD2 . LEU B 1 101 ? -26.925 29.998  20.599  1.00 30.80  ? 101 LEU B CD2 1 
ATOM   4930  N N   . ASN B 1 102 ? -28.016 27.570  24.405  1.00 22.17  ? 102 ASN B N   1 
ATOM   4931  C CA  . ASN B 1 102 ? -27.156 27.495  25.578  1.00 21.91  ? 102 ASN B CA  1 
ATOM   4932  C C   . ASN B 1 102 ? -27.571 26.386  26.538  1.00 23.79  ? 102 ASN B C   1 
ATOM   4933  O O   . ASN B 1 102 ? -27.186 26.419  27.712  1.00 26.30  ? 102 ASN B O   1 
ATOM   4934  C CB  . ASN B 1 102 ? -27.145 28.837  26.313  1.00 21.06  ? 102 ASN B CB  1 
ATOM   4935  C CG  . ASN B 1 102 ? -27.047 30.019  25.371  1.00 21.79  ? 102 ASN B CG  1 
ATOM   4936  O OD1 . ASN B 1 102 ? -25.953 30.438  24.990  1.00 24.22  ? 102 ASN B OD1 1 
ATOM   4937  N ND2 . ASN B 1 102 ? -28.195 30.567  24.991  1.00 23.76  ? 102 ASN B ND2 1 
ATOM   4938  N N   . TYR B 1 103 ? -28.342 25.408  26.060  1.00 31.03  ? 103 TYR B N   1 
ATOM   4939  C CA  . TYR B 1 103 ? -28.880 24.375  26.940  1.00 32.62  ? 103 TYR B CA  1 
ATOM   4940  C C   . TYR B 1 103 ? -27.770 23.550  27.582  1.00 35.14  ? 103 TYR B C   1 
ATOM   4941  O O   . TYR B 1 103 ? -27.834 23.231  28.775  1.00 35.02  ? 103 TYR B O   1 
ATOM   4942  C CB  . TYR B 1 103 ? -29.833 23.478  26.149  1.00 29.91  ? 103 TYR B CB  1 
ATOM   4943  C CG  . TYR B 1 103 ? -30.748 22.629  26.997  1.00 34.27  ? 103 TYR B CG  1 
ATOM   4944  C CD1 . TYR B 1 103 ? -31.574 23.202  27.953  1.00 28.42  ? 103 TYR B CD1 1 
ATOM   4945  C CD2 . TYR B 1 103 ? -30.790 21.249  26.836  1.00 59.58  ? 103 TYR B CD2 1 
ATOM   4946  C CE1 . TYR B 1 103 ? -32.414 22.425  28.728  1.00 39.21  ? 103 TYR B CE1 1 
ATOM   4947  C CE2 . TYR B 1 103 ? -31.627 20.464  27.606  1.00 56.85  ? 103 TYR B CE2 1 
ATOM   4948  C CZ  . TYR B 1 103 ? -32.436 21.056  28.551  1.00 51.82  ? 103 TYR B CZ  1 
ATOM   4949  O OH  . TYR B 1 103 ? -33.270 20.274  29.318  1.00 42.20  ? 103 TYR B OH  1 
ATOM   4950  N N   . GLU B 1 104 ? -26.739 23.204  26.813  1.00 38.49  ? 104 GLU B N   1 
ATOM   4951  C CA  . GLU B 1 104 ? -25.691 22.329  27.323  1.00 40.19  ? 104 GLU B CA  1 
ATOM   4952  C C   . GLU B 1 104 ? -24.659 23.059  28.174  1.00 38.62  ? 104 GLU B C   1 
ATOM   4953  O O   . GLU B 1 104 ? -23.888 22.400  28.882  1.00 36.03  ? 104 GLU B O   1 
ATOM   4954  C CB  . GLU B 1 104 ? -24.991 21.618  26.162  1.00 50.81  ? 104 GLU B CB  1 
ATOM   4955  C CG  . GLU B 1 104 ? -25.931 21.142  25.058  1.00 59.65  ? 104 GLU B CG  1 
ATOM   4956  C CD  . GLU B 1 104 ? -26.692 19.874  25.419  1.00 76.78  ? 104 GLU B CD  1 
ATOM   4957  O OE1 . GLU B 1 104 ? -27.185 19.201  24.489  1.00 84.37  ? 104 GLU B OE1 1 
ATOM   4958  O OE2 . GLU B 1 104 ? -26.802 19.546  26.620  1.00 79.54  ? 104 GLU B OE2 1 
ATOM   4959  N N   . LYS B 1 105 ? -24.624 24.384  28.128  1.00 30.41  ? 105 LYS B N   1 
ATOM   4960  C CA  . LYS B 1 105 ? -23.633 25.124  28.901  1.00 22.98  ? 105 LYS B CA  1 
ATOM   4961  C C   . LYS B 1 105 ? -23.965 25.052  30.389  1.00 23.97  ? 105 LYS B C   1 
ATOM   4962  O O   . LYS B 1 105 ? -25.118 25.277  30.774  1.00 37.43  ? 105 LYS B O   1 
ATOM   4963  C CB  . LYS B 1 105 ? -23.571 26.572  28.427  1.00 21.60  ? 105 LYS B CB  1 
ATOM   4964  C CG  . LYS B 1 105 ? -22.880 26.728  27.080  1.00 20.86  ? 105 LYS B CG  1 
ATOM   4965  C CD  . LYS B 1 105 ? -23.394 27.930  26.306  1.00 20.01  ? 105 LYS B CD  1 
ATOM   4966  C CE  . LYS B 1 105 ? -22.748 28.006  24.929  1.00 19.52  ? 105 LYS B CE  1 
ATOM   4967  N NZ  . LYS B 1 105 ? -23.543 28.830  23.977  1.00 23.80  ? 105 LYS B NZ  1 
ATOM   4968  N N   . PRO B 1 106 ? -22.993 24.734  31.250  1.00 23.97  ? 106 PRO B N   1 
ATOM   4969  C CA  . PRO B 1 106 ? -23.302 24.538  32.678  1.00 26.75  ? 106 PRO B CA  1 
ATOM   4970  C C   . PRO B 1 106 ? -23.880 25.761  33.367  1.00 24.73  ? 106 PRO B C   1 
ATOM   4971  O O   . PRO B 1 106 ? -24.517 25.609  34.416  1.00 27.88  ? 106 PRO B O   1 
ATOM   4972  C CB  . PRO B 1 106 ? -21.949 24.150  33.294  1.00 25.31  ? 106 PRO B CB  1 
ATOM   4973  C CG  . PRO B 1 106 ? -20.958 24.101  32.175  1.00 32.47  ? 106 PRO B CG  1 
ATOM   4974  C CD  . PRO B 1 106 ? -21.673 24.204  30.875  1.00 30.51  ? 106 PRO B CD  1 
ATOM   4975  N N   . ILE B 1 107 ? -23.674 26.968  32.832  1.00 28.23  ? 107 ILE B N   1 
ATOM   4976  C CA  . ILE B 1 107 ? -24.281 28.147  33.440  1.00 33.98  ? 107 ILE B CA  1 
ATOM   4977  C C   . ILE B 1 107 ? -25.797 28.128  33.302  1.00 36.25  ? 107 ILE B C   1 
ATOM   4978  O O   . ILE B 1 107 ? -26.489 28.883  33.994  1.00 35.26  ? 107 ILE B O   1 
ATOM   4979  C CB  . ILE B 1 107 ? -23.697 29.438  32.836  1.00 21.44  ? 107 ILE B CB  1 
ATOM   4980  C CG1 . ILE B 1 107 ? -23.847 29.435  31.315  1.00 20.74  ? 107 ILE B CG1 1 
ATOM   4981  C CG2 . ILE B 1 107 ? -22.239 29.603  33.240  1.00 23.10  ? 107 ILE B CG2 1 
ATOM   4982  C CD1 . ILE B 1 107 ? -23.834 30.818  30.701  1.00 20.83  ? 107 ILE B CD1 1 
ATOM   4983  N N   . TYR B 1 108 ? -26.333 27.279  32.425  1.00 33.73  ? 108 TYR B N   1 
ATOM   4984  C CA  . TYR B 1 108 ? -27.767 27.102  32.256  1.00 28.99  ? 108 TYR B CA  1 
ATOM   4985  C C   . TYR B 1 108 ? -28.295 25.883  33.003  1.00 30.10  ? 108 TYR B C   1 
ATOM   4986  O O   . TYR B 1 108 ? -29.383 25.391  32.684  1.00 27.89  ? 108 TYR B O   1 
ATOM   4987  C CB  . TYR B 1 108 ? -28.112 26.993  30.771  1.00 24.17  ? 108 TYR B CB  1 
ATOM   4988  C CG  . TYR B 1 108 ? -28.499 28.304  30.130  1.00 27.61  ? 108 TYR B CG  1 
ATOM   4989  C CD1 . TYR B 1 108 ? -27.550 29.290  29.894  1.00 30.34  ? 108 TYR B CD1 1 
ATOM   4990  C CD2 . TYR B 1 108 ? -29.811 28.551  29.751  1.00 28.71  ? 108 TYR B CD2 1 
ATOM   4991  C CE1 . TYR B 1 108 ? -27.900 30.491  29.303  1.00 31.56  ? 108 TYR B CE1 1 
ATOM   4992  C CE2 . TYR B 1 108 ? -30.170 29.746  29.160  1.00 29.02  ? 108 TYR B CE2 1 
ATOM   4993  C CZ  . TYR B 1 108 ? -29.211 30.714  28.938  1.00 31.89  ? 108 TYR B CZ  1 
ATOM   4994  O OH  . TYR B 1 108 ? -29.566 31.906  28.349  1.00 31.53  ? 108 TYR B OH  1 
ATOM   4995  N N   . ARG B 1 109 ? -27.546 25.376  33.983  1.00 30.88  ? 109 ARG B N   1 
ATOM   4996  C CA  . ARG B 1 109 ? -27.969 24.187  34.722  1.00 35.25  ? 109 ARG B CA  1 
ATOM   4997  C C   . ARG B 1 109 ? -28.906 24.600  35.859  1.00 37.05  ? 109 ARG B C   1 
ATOM   4998  O O   . ARG B 1 109 ? -28.573 24.556  37.046  1.00 32.08  ? 109 ARG B O   1 
ATOM   4999  C CB  . ARG B 1 109 ? -26.768 23.402  35.231  1.00 29.05  ? 109 ARG B CB  1 
ATOM   5000  C CG  . ARG B 1 109 ? -27.067 21.922  35.443  1.00 33.93  ? 109 ARG B CG  1 
ATOM   5001  C CD  . ARG B 1 109 ? -25.795 21.098  35.560  1.00 34.01  ? 109 ARG B CD  1 
ATOM   5002  N NE  . ARG B 1 109 ? -24.901 21.627  36.582  1.00 44.45  ? 109 ARG B NE  1 
ATOM   5003  C CZ  . ARG B 1 109 ? -23.595 21.790  36.422  1.00 47.41  ? 109 ARG B CZ  1 
ATOM   5004  N NH1 . ARG B 1 109 ? -22.990 21.458  35.292  1.00 38.59  ? 109 ARG B NH1 1 
ATOM   5005  N NH2 . ARG B 1 109 ? -22.878 22.296  37.422  1.00 47.37  ? 109 ARG B NH2 1 
ATOM   5006  N N   . PHE B 1 110 ? -30.100 25.028  35.460  1.00 39.10  ? 110 PHE B N   1 
ATOM   5007  C CA  . PHE B 1 110 ? -31.247 25.164  36.344  1.00 31.12  ? 110 PHE B CA  1 
ATOM   5008  C C   . PHE B 1 110 ? -32.207 24.019  36.053  1.00 40.24  ? 110 PHE B C   1 
ATOM   5009  O O   . PHE B 1 110 ? -32.365 23.617  34.896  1.00 54.88  ? 110 PHE B O   1 
ATOM   5010  C CB  . PHE B 1 110 ? -31.974 26.498  36.136  1.00 31.66  ? 110 PHE B CB  1 
ATOM   5011  C CG  . PHE B 1 110 ? -31.145 27.718  36.443  1.00 32.80  ? 110 PHE B CG  1 
ATOM   5012  C CD1 . PHE B 1 110 ? -30.316 28.272  35.479  1.00 38.80  ? 110 PHE B CD1 1 
ATOM   5013  C CD2 . PHE B 1 110 ? -31.227 28.336  37.681  1.00 30.99  ? 110 PHE B CD2 1 
ATOM   5014  C CE1 . PHE B 1 110 ? -29.565 29.405  35.751  1.00 33.05  ? 110 PHE B CE1 1 
ATOM   5015  C CE2 . PHE B 1 110 ? -30.480 29.469  37.960  1.00 39.68  ? 110 PHE B CE2 1 
ATOM   5016  C CZ  . PHE B 1 110 ? -29.648 30.004  36.993  1.00 39.06  ? 110 PHE B CZ  1 
ATOM   5017  N N   . GLU B 1 111 ? -32.846 23.488  37.096  1.00 47.09  ? 111 GLU B N   1 
ATOM   5018  C CA  . GLU B 1 111 ? -33.825 22.430  36.864  1.00 51.81  ? 111 GLU B CA  1 
ATOM   5019  C C   . GLU B 1 111 ? -35.115 22.980  36.269  1.00 49.76  ? 111 GLU B C   1 
ATOM   5020  O O   . GLU B 1 111 ? -35.803 22.271  35.526  1.00 57.07  ? 111 GLU B O   1 
ATOM   5021  C CB  . GLU B 1 111 ? -34.116 21.674  38.159  1.00 64.28  ? 111 GLU B CB  1 
ATOM   5022  C CG  . GLU B 1 111 ? -34.941 20.408  37.953  1.00 68.41  ? 111 GLU B CG  1 
ATOM   5023  C CD  . GLU B 1 111 ? -34.147 19.280  37.318  1.00 80.10  ? 111 GLU B CD  1 
ATOM   5024  O OE1 . GLU B 1 111 ? -32.900 19.317  37.378  1.00 80.38  ? 111 GLU B OE1 1 
ATOM   5025  O OE2 . GLU B 1 111 ? -34.772 18.357  36.753  1.00 67.32  ? 111 GLU B OE2 1 
ATOM   5026  N N   . ARG B 1 112 ? -35.455 24.234  36.576  1.00 42.30  ? 112 ARG B N   1 
ATOM   5027  C CA  . ARG B 1 112 ? -36.639 24.848  35.983  1.00 45.30  ? 112 ARG B CA  1 
ATOM   5028  C C   . ARG B 1 112 ? -36.516 24.928  34.466  1.00 43.57  ? 112 ARG B C   1 
ATOM   5029  O O   . ARG B 1 112 ? -37.504 24.746  33.743  1.00 37.39  ? 112 ARG B O   1 
ATOM   5030  C CB  . ARG B 1 112 ? -36.858 26.238  36.580  1.00 46.37  ? 112 ARG B CB  1 
ATOM   5031  C CG  . ARG B 1 112 ? -38.055 26.995  36.022  1.00 40.54  ? 112 ARG B CG  1 
ATOM   5032  C CD  . ARG B 1 112 ? -39.369 26.339  36.410  1.00 37.77  ? 112 ARG B CD  1 
ATOM   5033  N NE  . ARG B 1 112 ? -40.493 27.250  36.233  1.00 35.46  ? 112 ARG B NE  1 
ATOM   5034  C CZ  . ARG B 1 112 ? -41.739 26.866  35.997  1.00 44.64  ? 112 ARG B CZ  1 
ATOM   5035  N NH1 . ARG B 1 112 ? -42.062 25.586  35.909  1.00 56.20  ? 112 ARG B NH1 1 
ATOM   5036  N NH2 . ARG B 1 112 ? -42.686 27.789  35.847  1.00 45.14  ? 112 ARG B NH2 1 
ATOM   5037  N N   . ILE B 1 113 ? -35.307 25.197  33.967  1.00 45.91  ? 113 ILE B N   1 
ATOM   5038  C CA  . ILE B 1 113 ? -35.078 25.260  32.526  1.00 39.68  ? 113 ILE B CA  1 
ATOM   5039  C C   . ILE B 1 113 ? -35.276 23.891  31.884  1.00 40.33  ? 113 ILE B C   1 
ATOM   5040  O O   . ILE B 1 113 ? -35.751 23.793  30.745  1.00 41.36  ? 113 ILE B O   1 
ATOM   5041  C CB  . ILE B 1 113 ? -33.675 25.834  32.249  1.00 31.12  ? 113 ILE B CB  1 
ATOM   5042  C CG1 . ILE B 1 113 ? -33.618 27.304  32.675  1.00 34.72  ? 113 ILE B CG1 1 
ATOM   5043  C CG2 . ILE B 1 113 ? -33.301 25.682  30.781  1.00 42.06  ? 113 ILE B CG2 1 
ATOM   5044  C CD1 . ILE B 1 113 ? -32.464 28.080  32.082  1.00 31.10  ? 113 ILE B CD1 1 
ATOM   5045  N N   . ARG B 1 114 ? -34.927 22.816  32.597  1.00 42.44  ? 114 ARG B N   1 
ATOM   5046  C CA  . ARG B 1 114 ? -35.130 21.472  32.063  1.00 47.47  ? 114 ARG B CA  1 
ATOM   5047  C C   . ARG B 1 114 ? -36.610 21.184  31.836  1.00 46.39  ? 114 ARG B C   1 
ATOM   5048  O O   . ARG B 1 114 ? -36.979 20.524  30.857  1.00 41.47  ? 114 ARG B O   1 
ATOM   5049  C CB  . ARG B 1 114 ? -34.520 20.436  33.009  1.00 47.37  ? 114 ARG B CB  1 
ATOM   5050  C CG  . ARG B 1 114 ? -33.913 19.224  32.313  1.00 47.05  ? 114 ARG B CG  1 
ATOM   5051  C CD  . ARG B 1 114 ? -34.948 18.137  32.068  1.00 59.46  ? 114 ARG B CD  1 
ATOM   5052  N NE  . ARG B 1 114 ? -35.949 18.082  33.127  1.00 66.16  ? 114 ARG B NE  1 
ATOM   5053  C CZ  . ARG B 1 114 ? -36.957 17.221  33.162  1.00 64.93  ? 114 ARG B CZ  1 
ATOM   5054  N NH1 . ARG B 1 114 ? -37.124 16.314  32.213  1.00 59.99  ? 114 ARG B NH1 1 
ATOM   5055  N NH2 . ARG B 1 114 ? -37.818 17.271  34.176  1.00 62.26  ? 114 ARG B NH2 1 
ATOM   5056  N N   . GLU B 1 115 ? -37.472 21.666  32.735  1.00 52.05  ? 115 GLU B N   1 
ATOM   5057  C CA  . GLU B 1 115 ? -38.907 21.433  32.589  1.00 52.54  ? 115 GLU B CA  1 
ATOM   5058  C C   . GLU B 1 115 ? -39.485 22.220  31.419  1.00 47.46  ? 115 GLU B C   1 
ATOM   5059  O O   . GLU B 1 115 ? -40.301 21.694  30.653  1.00 42.43  ? 115 GLU B O   1 
ATOM   5060  C CB  . GLU B 1 115 ? -39.633 21.804  33.881  1.00 51.00  ? 115 GLU B CB  1 
ATOM   5061  C CG  . GLU B 1 115 ? -38.854 21.499  35.146  1.00 61.76  ? 115 GLU B CG  1 
ATOM   5062  C CD  . GLU B 1 115 ? -39.459 22.159  36.368  1.00 68.94  ? 115 GLU B CD  1 
ATOM   5063  O OE1 . GLU B 1 115 ? -40.618 22.618  36.283  1.00 68.04  ? 115 GLU B OE1 1 
ATOM   5064  O OE2 . GLU B 1 115 ? -38.776 22.225  37.412  1.00 62.74  ? 115 GLU B OE2 1 
ATOM   5065  N N   . LEU B 1 116 ? -39.078 23.483  31.271  1.00 45.08  ? 116 LEU B N   1 
ATOM   5066  C CA  . LEU B 1 116 ? -39.652 24.333  30.233  1.00 39.17  ? 116 LEU B CA  1 
ATOM   5067  C C   . LEU B 1 116 ? -39.289 23.846  28.836  1.00 44.45  ? 116 LEU B C   1 
ATOM   5068  O O   . LEU B 1 116 ? -40.100 23.967  27.909  1.00 46.26  ? 116 LEU B O   1 
ATOM   5069  C CB  . LEU B 1 116 ? -39.197 25.779  30.435  1.00 32.00  ? 116 LEU B CB  1 
ATOM   5070  C CG  . LEU B 1 116 ? -39.584 26.410  31.776  1.00 32.35  ? 116 LEU B CG  1 
ATOM   5071  C CD1 . LEU B 1 116 ? -39.396 27.917  31.745  1.00 31.06  ? 116 LEU B CD1 1 
ATOM   5072  C CD2 . LEU B 1 116 ? -41.020 26.059  32.146  1.00 40.74  ? 116 LEU B CD2 1 
ATOM   5073  N N   . MET B 1 117 ? -38.087 23.294  28.663  1.00 39.15  ? 117 MET B N   1 
ATOM   5074  C CA  . MET B 1 117 ? -37.673 22.805  27.356  1.00 33.64  ? 117 MET B CA  1 
ATOM   5075  C C   . MET B 1 117 ? -38.321 21.477  26.990  1.00 45.60  ? 117 MET B C   1 
ATOM   5076  O O   . MET B 1 117 ? -38.352 21.125  25.806  1.00 51.03  ? 117 MET B O   1 
ATOM   5077  C CB  . MET B 1 117 ? -36.151 22.677  27.302  1.00 47.57  ? 117 MET B CB  1 
ATOM   5078  C CG  . MET B 1 117 ? -35.451 23.992  27.017  1.00 48.02  ? 117 MET B CG  1 
ATOM   5079  S SD  . MET B 1 117 ? -36.109 24.789  25.540  1.00 59.49  ? 117 MET B SD  1 
ATOM   5080  C CE  . MET B 1 117 ? -36.940 26.209  26.246  1.00 32.91  ? 117 MET B CE  1 
ATOM   5081  N N   . ASN B 1 118 ? -38.826 20.731  27.971  1.00 53.49  ? 118 ASN B N   1 
ATOM   5082  C CA  . ASN B 1 118 ? -39.640 19.554  27.699  1.00 58.42  ? 118 ASN B CA  1 
ATOM   5083  C C   . ASN B 1 118 ? -41.122 19.884  27.600  1.00 56.28  ? 118 ASN B C   1 
ATOM   5084  O O   . ASN B 1 118 ? -41.914 19.015  27.217  1.00 54.22  ? 118 ASN B O   1 
ATOM   5085  C CB  . ASN B 1 118 ? -39.423 18.496  28.786  1.00 51.59  ? 118 ASN B CB  1 
ATOM   5086  C CG  . ASN B 1 118 ? -38.399 17.452  28.386  1.00 60.57  ? 118 ASN B CG  1 
ATOM   5087  O OD1 . ASN B 1 118 ? -38.747 16.318  28.057  1.00 68.63  ? 118 ASN B OD1 1 
ATOM   5088  N ND2 . ASN B 1 118 ? -37.126 17.833  28.407  1.00 48.44  ? 118 ASN B ND2 1 
ATOM   5089  N N   . LYS B 1 119 ? -41.506 21.115  27.929  1.00 50.47  ? 119 LYS B N   1 
ATOM   5090  C CA  . LYS B 1 119 ? -42.898 21.533  27.890  1.00 48.66  ? 119 LYS B CA  1 
ATOM   5091  C C   . LYS B 1 119 ? -43.305 21.899  26.468  1.00 52.49  ? 119 LYS B C   1 
ATOM   5092  O O   . LYS B 1 119 ? -42.506 22.437  25.697  1.00 47.98  ? 119 LYS B O   1 
ATOM   5093  C CB  . LYS B 1 119 ? -43.107 22.724  28.826  1.00 48.46  ? 119 LYS B CB  1 
ATOM   5094  C CG  . LYS B 1 119 ? -44.552 23.092  29.077  1.00 47.27  ? 119 LYS B CG  1 
ATOM   5095  C CD  . LYS B 1 119 ? -44.885 23.020  30.554  1.00 42.70  ? 119 LYS B CD  1 
ATOM   5096  C CE  . LYS B 1 119 ? -46.386 23.011  30.766  1.00 57.78  ? 119 LYS B CE  1 
ATOM   5097  N NZ  . LYS B 1 119 ? -47.026 21.879  30.045  1.00 46.45  ? 119 LYS B NZ  1 
ATOM   5098  N N   . GLU B 1 120 ? -44.558 21.602  26.122  1.00 55.09  ? 120 GLU B N   1 
ATOM   5099  C CA  . GLU B 1 120 ? -45.055 21.879  24.780  1.00 49.74  ? 120 GLU B CA  1 
ATOM   5100  C C   . GLU B 1 120 ? -45.776 23.216  24.678  1.00 47.58  ? 120 GLU B C   1 
ATOM   5101  O O   . GLU B 1 120 ? -45.696 23.874  23.634  1.00 42.80  ? 120 GLU B O   1 
ATOM   5102  C CB  . GLU B 1 120 ? -45.985 20.753  24.320  1.00 52.11  ? 120 GLU B CB  1 
ATOM   5103  C CG  . GLU B 1 120 ? -45.249 19.493  23.890  1.00 64.81  ? 120 GLU B CG  1 
ATOM   5104  C CD  . GLU B 1 120 ? -44.932 18.574  25.054  1.00 71.12  ? 120 GLU B CD  1 
ATOM   5105  O OE1 . GLU B 1 120 ? -45.760 18.487  25.985  1.00 79.64  ? 120 GLU B OE1 1 
ATOM   5106  O OE2 . GLU B 1 120 ? -43.852 17.945  25.043  1.00 61.59  ? 120 GLU B OE2 1 
ATOM   5107  N N   . LYS B 1 121 ? -46.484 23.629  25.728  1.00 46.00  ? 121 LYS B N   1 
ATOM   5108  C CA  . LYS B 1 121 ? -47.145 24.928  25.775  1.00 40.85  ? 121 LYS B CA  1 
ATOM   5109  C C   . LYS B 1 121 ? -46.741 25.640  27.057  1.00 44.24  ? 121 LYS B C   1 
ATOM   5110  O O   . LYS B 1 121 ? -46.816 25.057  28.143  1.00 45.04  ? 121 LYS B O   1 
ATOM   5111  C CB  . LYS B 1 121 ? -48.669 24.784  25.705  1.00 39.91  ? 121 LYS B CB  1 
ATOM   5112  C CG  . LYS B 1 121 ? -49.427 26.098  25.838  1.00 40.47  ? 121 LYS B CG  1 
ATOM   5113  C CD  . LYS B 1 121 ? -49.137 27.028  24.669  1.00 38.45  ? 121 LYS B CD  1 
ATOM   5114  C CE  . LYS B 1 121 ? -50.353 27.871  24.316  1.00 39.04  ? 121 LYS B CE  1 
ATOM   5115  N NZ  . LYS B 1 121 ? -51.297 27.146  23.419  1.00 40.54  ? 121 LYS B NZ  1 
ATOM   5116  N N   . LEU B 1 122 ? -46.322 26.897  26.931  1.00 37.13  ? 122 LEU B N   1 
ATOM   5117  C CA  . LEU B 1 122 ? -45.875 27.697  28.063  1.00 35.34  ? 122 LEU B CA  1 
ATOM   5118  C C   . LEU B 1 122 ? -46.851 28.840  28.298  1.00 35.52  ? 122 LEU B C   1 
ATOM   5119  O O   . LEU B 1 122 ? -47.257 29.519  27.350  1.00 39.69  ? 122 LEU B O   1 
ATOM   5120  C CB  . LEU B 1 122 ? -44.469 28.250  27.821  1.00 33.64  ? 122 LEU B CB  1 
ATOM   5121  C CG  . LEU B 1 122 ? -43.406 27.279  27.308  1.00 33.30  ? 122 LEU B CG  1 
ATOM   5122  C CD1 . LEU B 1 122 ? -42.397 28.027  26.463  1.00 31.75  ? 122 LEU B CD1 1 
ATOM   5123  C CD2 . LEU B 1 122 ? -42.716 26.571  28.462  1.00 33.53  ? 122 LEU B CD2 1 
ATOM   5124  N N   . ASN B 1 123 ? -47.221 29.052  29.559  1.00 36.09  ? 123 ASN B N   1 
ATOM   5125  C CA  . ASN B 1 123 ? -48.118 30.130  29.940  1.00 36.42  ? 123 ASN B CA  1 
ATOM   5126  C C   . ASN B 1 123 ? -47.304 31.346  30.385  1.00 35.13  ? 123 ASN B C   1 
ATOM   5127  O O   . ASN B 1 123 ? -46.083 31.406  30.204  1.00 33.90  ? 123 ASN B O   1 
ATOM   5128  C CB  . ASN B 1 123 ? -49.100 29.651  31.015  1.00 38.06  ? 123 ASN B CB  1 
ATOM   5129  C CG  . ASN B 1 123 ? -48.411 29.195  32.284  1.00 38.24  ? 123 ASN B CG  1 
ATOM   5130  O OD1 . ASN B 1 123 ? -47.804 29.993  32.997  1.00 37.53  ? 123 ASN B OD1 1 
ATOM   5131  N ND2 . ASN B 1 123 ? -48.512 27.904  32.578  1.00 41.71  ? 123 ASN B ND2 1 
ATOM   5132  N N   . ARG B 1 124 ? -47.989 32.338  30.962  1.00 35.52  ? 124 ARG B N   1 
ATOM   5133  C CA  . ARG B 1 124 ? -47.342 33.613  31.261  1.00 34.49  ? 124 ARG B CA  1 
ATOM   5134  C C   . ARG B 1 124 ? -46.276 33.472  32.341  1.00 34.05  ? 124 ARG B C   1 
ATOM   5135  O O   . ARG B 1 124 ? -45.204 34.080  32.244  1.00 34.51  ? 124 ARG B O   1 
ATOM   5136  C CB  . ARG B 1 124 ? -48.382 34.648  31.685  1.00 35.29  ? 124 ARG B CB  1 
ATOM   5137  C CG  . ARG B 1 124 ? -47.781 36.022  31.927  1.00 34.42  ? 124 ARG B CG  1 
ATOM   5138  C CD  . ARG B 1 124 ? -48.711 36.935  32.700  1.00 36.95  ? 124 ARG B CD  1 
ATOM   5139  N NE  . ARG B 1 124 ? -48.021 38.144  33.134  1.00 42.25  ? 124 ARG B NE  1 
ATOM   5140  C CZ  . ARG B 1 124 ? -47.382 38.267  34.290  1.00 39.96  ? 124 ARG B CZ  1 
ATOM   5141  N NH1 . ARG B 1 124 ? -47.342 37.277  35.166  1.00 35.54  ? 124 ARG B NH1 1 
ATOM   5142  N NH2 . ARG B 1 124 ? -46.768 39.413  34.572  1.00 36.49  ? 124 ARG B NH2 1 
ATOM   5143  N N   . GLU B 1 125 ? -46.553 32.693  33.388  1.00 35.17  ? 125 GLU B N   1 
ATOM   5144  C CA  . GLU B 1 125 ? -45.592 32.570  34.480  1.00 34.99  ? 125 GLU B CA  1 
ATOM   5145  C C   . GLU B 1 125 ? -44.372 31.765  34.050  1.00 35.10  ? 125 GLU B C   1 
ATOM   5146  O O   . GLU B 1 125 ? -43.246 32.062  34.466  1.00 33.16  ? 125 GLU B O   1 
ATOM   5147  C CB  . GLU B 1 125 ? -46.258 31.937  35.702  1.00 36.68  ? 125 GLU B CB  1 
ATOM   5148  C CG  . GLU B 1 125 ? -47.235 32.851  36.454  1.00 40.55  ? 125 GLU B CG  1 
ATOM   5149  C CD  . GLU B 1 125 ? -48.404 33.322  35.601  1.00 52.21  ? 125 GLU B CD  1 
ATOM   5150  O OE1 . GLU B 1 125 ? -48.767 32.613  34.639  1.00 54.09  ? 125 GLU B OE1 1 
ATOM   5151  O OE2 . GLU B 1 125 ? -48.959 34.404  35.893  1.00 38.34  ? 125 GLU B OE2 1 
ATOM   5152  N N   . GLU B 1 126 ? -44.577 30.742  33.219  1.00 35.84  ? 126 GLU B N   1 
ATOM   5153  C CA  . GLU B 1 126 ? -43.454 29.944  32.739  1.00 33.50  ? 126 GLU B CA  1 
ATOM   5154  C C   . GLU B 1 126 ? -42.600 30.729  31.751  1.00 31.85  ? 126 GLU B C   1 
ATOM   5155  O O   . GLU B 1 126 ? -41.371 30.590  31.742  1.00 42.39  ? 126 GLU B O   1 
ATOM   5156  C CB  . GLU B 1 126 ? -43.972 28.644  32.125  1.00 34.65  ? 126 GLU B CB  1 
ATOM   5157  C CG  . GLU B 1 126 ? -45.073 27.997  32.965  1.00 53.14  ? 126 GLU B CG  1 
ATOM   5158  C CD  . GLU B 1 126 ? -45.500 26.636  32.449  1.00 63.50  ? 126 GLU B CD  1 
ATOM   5159  O OE1 . GLU B 1 126 ? -45.820 26.525  31.247  1.00 66.06  ? 126 GLU B OE1 1 
ATOM   5160  O OE2 . GLU B 1 126 ? -45.524 25.678  33.252  1.00 59.66  ? 126 GLU B OE2 1 
ATOM   5161  N N   . LEU B 1 127 ? -43.227 31.555  30.907  1.00 31.57  ? 127 LEU B N   1 
ATOM   5162  C CA  . LEU B 1 127 ? -42.451 32.458  30.061  1.00 30.15  ? 127 LEU B CA  1 
ATOM   5163  C C   . LEU B 1 127 ? -41.765 33.532  30.889  1.00 29.44  ? 127 LEU B C   1 
ATOM   5164  O O   . LEU B 1 127 ? -40.674 33.991  30.529  1.00 30.84  ? 127 LEU B O   1 
ATOM   5165  C CB  . LEU B 1 127 ? -43.340 33.101  28.998  1.00 30.26  ? 127 LEU B CB  1 
ATOM   5166  C CG  . LEU B 1 127 ? -43.743 32.201  27.831  1.00 31.07  ? 127 LEU B CG  1 
ATOM   5167  C CD1 . LEU B 1 127 ? -44.889 32.818  27.042  1.00 31.26  ? 127 LEU B CD1 1 
ATOM   5168  C CD2 . LEU B 1 127 ? -42.543 31.932  26.935  1.00 29.61  ? 127 LEU B CD2 1 
ATOM   5169  N N   . LEU B 1 128 ? -42.390 33.952  31.990  1.00 30.29  ? 128 LEU B N   1 
ATOM   5170  C CA  . LEU B 1 128 ? -41.707 34.823  32.937  1.00 29.89  ? 128 LEU B CA  1 
ATOM   5171  C C   . LEU B 1 128 ? -40.508 34.109  33.546  1.00 30.14  ? 128 LEU B C   1 
ATOM   5172  O O   . LEU B 1 128 ? -39.459 34.722  33.779  1.00 28.62  ? 128 LEU B O   1 
ATOM   5173  C CB  . LEU B 1 128 ? -42.679 35.274  34.026  1.00 36.71  ? 128 LEU B CB  1 
ATOM   5174  C CG  . LEU B 1 128 ? -42.496 36.687  34.584  1.00 30.98  ? 128 LEU B CG  1 
ATOM   5175  C CD1 . LEU B 1 128 ? -43.769 37.160  35.279  1.00 32.41  ? 128 LEU B CD1 1 
ATOM   5176  C CD2 . LEU B 1 128 ? -41.298 36.762  35.511  1.00 50.70  ? 128 LEU B CD2 1 
ATOM   5177  N N   . ASP B 1 129 ? -40.647 32.808  33.812  1.00 30.37  ? 129 ASP B N   1 
ATOM   5178  C CA  . ASP B 1 129 ? -39.529 32.035  34.341  1.00 30.11  ? 129 ASP B CA  1 
ATOM   5179  C C   . ASP B 1 129 ? -38.447 31.832  33.287  1.00 32.69  ? 129 ASP B C   1 
ATOM   5180  O O   . ASP B 1 129 ? -37.255 31.807  33.614  1.00 35.09  ? 129 ASP B O   1 
ATOM   5181  C CB  . ASP B 1 129 ? -40.027 30.689  34.870  1.00 37.35  ? 129 ASP B CB  1 
ATOM   5182  C CG  . ASP B 1 129 ? -40.647 30.798  36.249  1.00 46.20  ? 129 ASP B CG  1 
ATOM   5183  O OD1 . ASP B 1 129 ? -41.162 31.884  36.586  1.00 48.57  ? 129 ASP B OD1 1 
ATOM   5184  O OD2 . ASP B 1 129 ? -40.621 29.796  36.996  1.00 43.09  ? 129 ASP B OD2 1 
ATOM   5185  N N   . LEU B 1 130 ? -38.837 31.675  32.019  1.00 30.42  ? 130 LEU B N   1 
ATOM   5186  C CA  . LEU B 1 130 ? -37.840 31.539  30.962  1.00 27.35  ? 130 LEU B CA  1 
ATOM   5187  C C   . LEU B 1 130 ? -37.086 32.845  30.742  1.00 26.09  ? 130 LEU B C   1 
ATOM   5188  O O   . LEU B 1 130 ? -35.880 32.832  30.472  1.00 28.24  ? 130 LEU B O   1 
ATOM   5189  C CB  . LEU B 1 130 ? -38.496 31.073  29.664  1.00 27.58  ? 130 LEU B CB  1 
ATOM   5190  C CG  . LEU B 1 130 ? -37.501 30.564  28.619  1.00 26.80  ? 130 LEU B CG  1 
ATOM   5191  C CD1 . LEU B 1 130 ? -37.077 29.132  28.916  1.00 27.45  ? 130 LEU B CD1 1 
ATOM   5192  C CD2 . LEU B 1 130 ? -38.073 30.680  27.219  1.00 26.80  ? 130 LEU B CD2 1 
ATOM   5193  N N   . GLN B 1 131 ? -37.780 33.981  30.843  1.00 26.16  ? 131 GLN B N   1 
ATOM   5194  C CA  . GLN B 1 131 ? -37.115 35.272  30.691  1.00 25.18  ? 131 GLN B CA  1 
ATOM   5195  C C   . GLN B 1 131 ? -36.099 35.501  31.803  1.00 26.91  ? 131 GLN B C   1 
ATOM   5196  O O   . GLN B 1 131 ? -34.949 35.875  31.545  1.00 29.66  ? 131 GLN B O   1 
ATOM   5197  C CB  . GLN B 1 131 ? -38.147 36.400  30.684  1.00 25.61  ? 131 GLN B CB  1 
ATOM   5198  C CG  . GLN B 1 131 ? -38.840 36.634  29.357  1.00 25.58  ? 131 GLN B CG  1 
ATOM   5199  C CD  . GLN B 1 131 ? -40.070 37.507  29.505  1.00 26.39  ? 131 GLN B CD  1 
ATOM   5200  O OE1 . GLN B 1 131 ? -40.397 37.957  30.604  1.00 26.98  ? 131 GLN B OE1 1 
ATOM   5201  N NE2 . GLN B 1 131 ? -40.756 37.755  28.398  1.00 26.55  ? 131 GLN B NE2 1 
ATOM   5202  N N   . THR B 1 132 ? -36.510 35.279  33.054  1.00 25.87  ? 132 THR B N   1 
ATOM   5203  C CA  . THR B 1 132 ? -35.651 35.614  34.185  1.00 25.84  ? 132 THR B CA  1 
ATOM   5204  C C   . THR B 1 132 ? -34.498 34.627  34.323  1.00 25.47  ? 132 THR B C   1 
ATOM   5205  O O   . THR B 1 132 ? -33.356 35.031  34.570  1.00 24.76  ? 132 THR B O   1 
ATOM   5206  C CB  . THR B 1 132 ? -36.475 35.666  35.472  1.00 27.22  ? 132 THR B CB  1 
ATOM   5207  O OG1 . THR B 1 132 ? -37.605 36.527  35.281  1.00 27.67  ? 132 THR B OG1 1 
ATOM   5208  C CG2 . THR B 1 132 ? -35.633 36.196  36.622  1.00 27.32  ? 132 THR B CG2 1 
ATOM   5209  N N   . LEU B 1 133 ? -34.773 33.330  34.167  1.00 26.04  ? 133 LEU B N   1 
ATOM   5210  C CA  . LEU B 1 133 ? -33.704 32.342  34.279  1.00 28.37  ? 133 LEU B CA  1 
ATOM   5211  C C   . LEU B 1 133 ? -32.724 32.442  33.117  1.00 26.43  ? 133 LEU B C   1 
ATOM   5212  O O   . LEU B 1 133 ? -31.554 32.074  33.264  1.00 32.48  ? 133 LEU B O   1 
ATOM   5213  C CB  . LEU B 1 133 ? -34.291 30.935  34.371  1.00 30.48  ? 133 LEU B CB  1 
ATOM   5214  C CG  . LEU B 1 133 ? -34.587 30.442  35.790  1.00 29.37  ? 133 LEU B CG  1 
ATOM   5215  C CD1 . LEU B 1 133 ? -34.657 28.928  35.831  1.00 33.85  ? 133 LEU B CD1 1 
ATOM   5216  C CD2 . LEU B 1 133 ? -33.548 30.955  36.777  1.00 28.18  ? 133 LEU B CD2 1 
ATOM   5217  N N   . ASN B 1 134 ? -33.181 32.923  31.958  1.00 23.99  ? 134 ASN B N   1 
ATOM   5218  C CA  . ASN B 1 134 ? -32.250 33.258  30.885  1.00 22.79  ? 134 ASN B CA  1 
ATOM   5219  C C   . ASN B 1 134 ? -31.324 34.390  31.308  1.00 21.98  ? 134 ASN B C   1 
ATOM   5220  O O   . ASN B 1 134 ? -30.118 34.351  31.039  1.00 34.07  ? 134 ASN B O   1 
ATOM   5221  C CB  . ASN B 1 134 ? -33.015 33.640  29.621  1.00 22.61  ? 134 ASN B CB  1 
ATOM   5222  C CG  . ASN B 1 134 ? -32.984 32.552  28.567  1.00 22.72  ? 134 ASN B CG  1 
ATOM   5223  O OD1 . ASN B 1 134 ? -31.918 32.063  28.195  1.00 24.53  ? 134 ASN B OD1 1 
ATOM   5224  N ND2 . ASN B 1 134 ? -34.155 32.176  28.071  1.00 23.50  ? 134 ASN B ND2 1 
ATOM   5225  N N   . LEU B 1 135 ? -31.874 35.411  31.968  1.00 25.80  ? 135 LEU B N   1 
ATOM   5226  C CA  . LEU B 1 135 ? -31.047 36.501  32.476  1.00 26.97  ? 135 LEU B CA  1 
ATOM   5227  C C   . LEU B 1 135 ? -30.082 36.009  33.548  1.00 24.82  ? 135 LEU B C   1 
ATOM   5228  O O   . LEU B 1 135 ? -28.872 36.252  33.471  1.00 23.59  ? 135 LEU B O   1 
ATOM   5229  C CB  . LEU B 1 135 ? -31.933 37.615  33.034  1.00 23.73  ? 135 LEU B CB  1 
ATOM   5230  C CG  . LEU B 1 135 ? -32.344 38.731  32.076  1.00 23.38  ? 135 LEU B CG  1 
ATOM   5231  C CD1 . LEU B 1 135 ? -33.313 39.689  32.757  1.00 22.76  ? 135 LEU B CD1 1 
ATOM   5232  C CD2 . LEU B 1 135 ? -31.118 39.473  31.570  1.00 20.85  ? 135 LEU B CD2 1 
ATOM   5233  N N   . LEU B 1 136 ? -30.605 35.306  34.556  1.00 23.03  ? 136 LEU B N   1 
ATOM   5234  C CA  . LEU B 1 136 ? -29.791 34.934  35.710  1.00 26.10  ? 136 LEU B CA  1 
ATOM   5235  C C   . LEU B 1 136 ? -28.662 33.986  35.334  1.00 30.22  ? 136 LEU B C   1 
ATOM   5236  O O   . LEU B 1 136 ? -27.604 34.000  35.974  1.00 41.14  ? 136 LEU B O   1 
ATOM   5237  C CB  . LEU B 1 136 ? -30.671 34.304  36.789  1.00 25.97  ? 136 LEU B CB  1 
ATOM   5238  C CG  . LEU B 1 136 ? -31.752 35.208  37.382  1.00 26.73  ? 136 LEU B CG  1 
ATOM   5239  C CD1 . LEU B 1 136 ? -32.787 34.382  38.126  1.00 29.62  ? 136 LEU B CD1 1 
ATOM   5240  C CD2 . LEU B 1 136 ? -31.141 36.258  38.294  1.00 25.85  ? 136 LEU B CD2 1 
ATOM   5241  N N   . ALA B 1 137 ? -28.859 33.159  34.305  1.00 31.45  ? 137 ALA B N   1 
ATOM   5242  C CA  . ALA B 1 137 ? -27.827 32.211  33.902  1.00 25.93  ? 137 ALA B CA  1 
ATOM   5243  C C   . ALA B 1 137 ? -26.551 32.908  33.450  1.00 29.83  ? 137 ALA B C   1 
ATOM   5244  O O   . ALA B 1 137 ? -25.495 32.268  33.387  1.00 38.91  ? 137 ALA B O   1 
ATOM   5245  C CB  . ALA B 1 137 ? -28.350 31.301  32.788  1.00 26.94  ? 137 ALA B CB  1 
ATOM   5246  N N   . TRP B 1 138 ? -26.625 34.201  33.135  1.00 28.70  ? 138 TRP B N   1 
ATOM   5247  C CA  . TRP B 1 138 ? -25.468 34.991  32.735  1.00 25.54  ? 138 TRP B CA  1 
ATOM   5248  C C   . TRP B 1 138 ? -25.000 35.917  33.854  1.00 22.74  ? 138 TRP B C   1 
ATOM   5249  O O   . TRP B 1 138 ? -24.490 37.009  33.592  1.00 23.25  ? 138 TRP B O   1 
ATOM   5250  C CB  . TRP B 1 138 ? -25.790 35.793  31.476  1.00 26.91  ? 138 TRP B CB  1 
ATOM   5251  C CG  . TRP B 1 138 ? -26.085 34.924  30.298  1.00 28.60  ? 138 TRP B CG  1 
ATOM   5252  C CD1 . TRP B 1 138 ? -27.258 34.285  30.021  1.00 22.48  ? 138 TRP B CD1 1 
ATOM   5253  C CD2 . TRP B 1 138 ? -25.181 34.580  29.245  1.00 26.50  ? 138 TRP B CD2 1 
ATOM   5254  N NE1 . TRP B 1 138 ? -27.142 33.570  28.854  1.00 22.29  ? 138 TRP B NE1 1 
ATOM   5255  C CE2 . TRP B 1 138 ? -25.876 33.734  28.358  1.00 28.99  ? 138 TRP B CE2 1 
ATOM   5256  C CE3 . TRP B 1 138 ? -23.852 34.909  28.963  1.00 17.54  ? 138 TRP B CE3 1 
ATOM   5257  C CZ2 . TRP B 1 138 ? -25.286 33.213  27.209  1.00 30.44  ? 138 TRP B CZ2 1 
ATOM   5258  C CZ3 . TRP B 1 138 ? -23.269 34.391  27.824  1.00 27.46  ? 138 TRP B CZ3 1 
ATOM   5259  C CH2 . TRP B 1 138 ? -23.985 33.552  26.960  1.00 30.22  ? 138 TRP B CH2 1 
ATOM   5260  N N   . CYS B 1 139 ? -25.173 35.496  35.103  1.00 29.03  ? 139 CYS B N   1 
ATOM   5261  C CA  . CYS B 1 139 ? -24.790 36.317  36.242  1.00 38.50  ? 139 CYS B CA  1 
ATOM   5262  C C   . CYS B 1 139 ? -23.297 36.197  36.517  1.00 37.35  ? 139 CYS B C   1 
ATOM   5263  O O   . CYS B 1 139 ? -22.690 35.136  36.335  1.00 35.95  ? 139 CYS B O   1 
ATOM   5264  C CB  . CYS B 1 139 ? -25.583 35.918  37.487  1.00 39.23  ? 139 CYS B CB  1 
ATOM   5265  S SG  . CYS B 1 139 ? -25.514 37.118  38.836  1.00 42.54  ? 139 CYS B SG  1 
ATOM   5266  N N   . GLY B 1 140 ? -22.705 37.306  36.966  1.00 31.65  ? 140 GLY B N   1 
ATOM   5267  C CA  . GLY B 1 140 ? -21.278 37.375  37.185  1.00 35.58  ? 140 GLY B CA  1 
ATOM   5268  C C   . GLY B 1 140 ? -20.880 37.092  38.625  1.00 35.53  ? 140 GLY B C   1 
ATOM   5269  O O   . GLY B 1 140 ? -21.703 36.821  39.497  1.00 40.48  ? 140 GLY B O   1 
ATOM   5270  N N   . ARG B 1 141 ? -19.565 37.156  38.857  1.00 31.35  ? 141 ARG B N   1 
ATOM   5271  C CA  . ARG B 1 141 ? -19.022 36.935  40.194  1.00 27.63  ? 141 ARG B CA  1 
ATOM   5272  C C   . ARG B 1 141 ? -19.517 37.988  41.178  1.00 36.76  ? 141 ARG B C   1 
ATOM   5273  O O   . ARG B 1 141 ? -19.827 37.673  42.334  1.00 39.39  ? 141 ARG B O   1 
ATOM   5274  C CB  . ARG B 1 141 ? -17.495 36.933  40.135  1.00 22.11  ? 141 ARG B CB  1 
ATOM   5275  C CG  . ARG B 1 141 ? -16.811 36.684  41.466  1.00 22.93  ? 141 ARG B CG  1 
ATOM   5276  C CD  . ARG B 1 141 ? -15.309 36.560  41.281  1.00 22.87  ? 141 ARG B CD  1 
ATOM   5277  N NE  . ARG B 1 141 ? -14.592 36.604  42.550  1.00 31.83  ? 141 ARG B NE  1 
ATOM   5278  C CZ  . ARG B 1 141 ? -14.203 37.720  43.150  1.00 31.01  ? 141 ARG B CZ  1 
ATOM   5279  N NH1 . ARG B 1 141 ? -14.459 38.911  42.630  1.00 27.67  ? 141 ARG B NH1 1 
ATOM   5280  N NH2 . ARG B 1 141 ? -13.543 37.641  44.302  1.00 34.79  ? 141 ARG B NH2 1 
ATOM   5281  N N   . THR B 1 142 ? -19.590 39.247  40.741  1.00 37.28  ? 142 THR B N   1 
ATOM   5282  C CA  . THR B 1 142 ? -19.994 40.324  41.640  1.00 28.75  ? 142 THR B CA  1 
ATOM   5283  C C   . THR B 1 142 ? -21.450 40.172  42.067  1.00 35.92  ? 142 THR B C   1 
ATOM   5284  O O   . THR B 1 142 ? -21.773 40.286  43.255  1.00 38.72  ? 142 THR B O   1 
ATOM   5285  C CB  . THR B 1 142 ? -19.774 41.679  40.967  1.00 32.06  ? 142 THR B CB  1 
ATOM   5286  O OG1 . THR B 1 142 ? -18.456 41.723  40.406  1.00 33.74  ? 142 THR B OG1 1 
ATOM   5287  C CG2 . THR B 1 142 ? -19.924 42.807  41.979  1.00 26.70  ? 142 THR B CG2 1 
ATOM   5288  N N   . LEU B 1 143 ? -22.344 39.905  41.113  1.00 39.83  ? 143 LEU B N   1 
ATOM   5289  C CA  . LEU B 1 143 ? -23.772 39.912  41.403  1.00 39.67  ? 143 LEU B CA  1 
ATOM   5290  C C   . LEU B 1 143 ? -24.288 38.591  41.953  1.00 38.33  ? 143 LEU B C   1 
ATOM   5291  O O   . LEU B 1 143 ? -25.402 38.558  42.489  1.00 42.98  ? 143 LEU B O   1 
ATOM   5292  C CB  . LEU B 1 143 ? -24.565 40.281  40.150  1.00 29.06  ? 143 LEU B CB  1 
ATOM   5293  C CG  . LEU B 1 143 ? -24.557 41.770  39.816  1.00 23.38  ? 143 LEU B CG  1 
ATOM   5294  C CD1 . LEU B 1 143 ? -25.047 41.987  38.398  1.00 29.53  ? 143 LEU B CD1 1 
ATOM   5295  C CD2 . LEU B 1 143 ? -25.411 42.533  40.813  1.00 24.77  ? 143 LEU B CD2 1 
ATOM   5296  N N   . ARG B 1 144 ? -23.516 37.506  41.845  1.00 31.71  ? 144 ARG B N   1 
ATOM   5297  C CA  . ARG B 1 144 ? -23.933 36.253  42.462  1.00 34.75  ? 144 ARG B CA  1 
ATOM   5298  C C   . ARG B 1 144 ? -24.018 36.364  43.979  1.00 42.47  ? 144 ARG B C   1 
ATOM   5299  O O   . ARG B 1 144 ? -24.614 35.490  44.619  1.00 47.33  ? 144 ARG B O   1 
ATOM   5300  C CB  . ARG B 1 144 ? -22.980 35.123  42.061  1.00 36.61  ? 144 ARG B CB  1 
ATOM   5301  C CG  . ARG B 1 144 ? -23.433 34.346  40.828  1.00 40.12  ? 144 ARG B CG  1 
ATOM   5302  C CD  . ARG B 1 144 ? -22.344 33.413  40.317  1.00 47.11  ? 144 ARG B CD  1 
ATOM   5303  N NE  . ARG B 1 144 ? -22.883 32.170  39.774  1.00 42.57  ? 144 ARG B NE  1 
ATOM   5304  C CZ  . ARG B 1 144 ? -23.053 31.926  38.482  1.00 37.46  ? 144 ARG B CZ  1 
ATOM   5305  N NH1 . ARG B 1 144 ? -22.740 32.822  37.561  1.00 32.52  ? 144 ARG B NH1 1 
ATOM   5306  N NH2 . ARG B 1 144 ? -23.549 30.751  38.103  1.00 46.01  ? 144 ARG B NH2 1 
ATOM   5307  N N   . LYS B 1 145 ? -23.434 37.412  44.561  1.00 51.07  ? 145 LYS B N   1 
ATOM   5308  C CA  . LYS B 1 145 ? -23.565 37.717  45.980  1.00 40.66  ? 145 LYS B CA  1 
ATOM   5309  C C   . LYS B 1 145 ? -24.804 38.558  46.274  1.00 50.05  ? 145 LYS B C   1 
ATOM   5310  O O   . LYS B 1 145 ? -25.521 38.285  47.242  1.00 57.19  ? 145 LYS B O   1 
ATOM   5311  C CB  . LYS B 1 145 ? -22.307 38.442  46.468  1.00 44.77  ? 145 LYS B CB  1 
ATOM   5312  C CG  . LYS B 1 145 ? -21.035 37.983  45.765  1.00 50.01  ? 145 LYS B CG  1 
ATOM   5313  C CD  . LYS B 1 145 ? -19.886 38.961  45.960  1.00 52.59  ? 145 LYS B CD  1 
ATOM   5314  C CE  . LYS B 1 145 ? -18.572 38.362  45.474  1.00 55.83  ? 145 LYS B CE  1 
ATOM   5315  N NZ  . LYS B 1 145 ? -17.475 39.368  45.396  1.00 55.94  ? 145 LYS B NZ  1 
ATOM   5316  N N   . ASP B 1 146 ? -25.071 39.581  45.456  1.00 57.02  ? 146 ASP B N   1 
ATOM   5317  C CA  . ASP B 1 146 ? -26.248 40.420  45.672  1.00 55.67  ? 146 ASP B CA  1 
ATOM   5318  C C   . ASP B 1 146 ? -27.530 39.682  45.306  1.00 44.94  ? 146 ASP B C   1 
ATOM   5319  O O   . ASP B 1 146 ? -28.508 39.701  46.063  1.00 50.35  ? 146 ASP B O   1 
ATOM   5320  C CB  . ASP B 1 146 ? -26.131 41.716  44.867  1.00 57.44  ? 146 ASP B CB  1 
ATOM   5321  C CG  . ASP B 1 146 ? -25.036 42.628  45.382  1.00 72.76  ? 146 ASP B CG  1 
ATOM   5322  O OD1 . ASP B 1 146 ? -24.600 42.445  46.540  1.00 67.30  ? 146 ASP B OD1 1 
ATOM   5323  O OD2 . ASP B 1 146 ? -24.616 43.534  44.632  1.00 73.38  ? 146 ASP B OD2 1 
ATOM   5324  N N   . LEU B 1 147 ? -27.541 39.014  44.150  1.00 45.13  ? 147 LEU B N   1 
ATOM   5325  C CA  . LEU B 1 147 ? -28.716 38.304  43.657  1.00 35.74  ? 147 LEU B CA  1 
ATOM   5326  C C   . LEU B 1 147 ? -28.765 36.856  44.125  1.00 45.29  ? 147 LEU B C   1 
ATOM   5327  O O   . LEU B 1 147 ? -29.348 36.006  43.438  1.00 42.67  ? 147 LEU B O   1 
ATOM   5328  C CB  . LEU B 1 147 ? -28.773 38.366  42.130  1.00 27.85  ? 147 LEU B CB  1 
ATOM   5329  C CG  . LEU B 1 147 ? -28.828 39.740  41.458  1.00 35.79  ? 147 LEU B CG  1 
ATOM   5330  C CD1 . LEU B 1 147 ? -28.735 39.594  39.947  1.00 27.50  ? 147 LEU B CD1 1 
ATOM   5331  C CD2 . LEU B 1 147 ? -30.096 40.483  41.846  1.00 28.59  ? 147 LEU B CD2 1 
ATOM   5332  N N   . LYS B 1 148 ? -28.158 36.551  45.275  1.00 43.62  ? 148 LYS B N   1 
ATOM   5333  C CA  . LYS B 1 148 ? -28.151 35.178  45.771  1.00 44.66  ? 148 LYS B CA  1 
ATOM   5334  C C   . LYS B 1 148 ? -29.564 34.690  46.066  1.00 48.31  ? 148 LYS B C   1 
ATOM   5335  O O   . LYS B 1 148 ? -29.883 33.517  45.836  1.00 50.82  ? 148 LYS B O   1 
ATOM   5336  C CB  . LYS B 1 148 ? -27.271 35.081  47.018  1.00 42.50  ? 148 LYS B CB  1 
ATOM   5337  C CG  . LYS B 1 148 ? -27.252 33.706  47.669  1.00 46.12  ? 148 LYS B CG  1 
ATOM   5338  C CD  . LYS B 1 148 ? -26.570 33.745  49.028  1.00 40.96  ? 148 LYS B CD  1 
ATOM   5339  C CE  . LYS B 1 148 ? -26.132 32.356  49.466  1.00 41.16  ? 148 LYS B CE  1 
ATOM   5340  N NZ  . LYS B 1 148 ? -26.211 32.188  50.944  1.00 47.40  ? 148 LYS B NZ  1 
ATOM   5341  N N   . ASP B 1 149 ? -30.425 35.576  46.571  1.00 51.29  ? 149 ASP B N   1 
ATOM   5342  C CA  . ASP B 1 149 ? -31.786 35.178  46.921  1.00 47.52  ? 149 ASP B CA  1 
ATOM   5343  C C   . ASP B 1 149 ? -32.563 34.713  45.694  1.00 47.90  ? 149 ASP B C   1 
ATOM   5344  O O   . ASP B 1 149 ? -33.193 33.648  45.712  1.00 47.57  ? 149 ASP B O   1 
ATOM   5345  C CB  . ASP B 1 149 ? -32.511 36.337  47.607  1.00 37.03  ? 149 ASP B CB  1 
ATOM   5346  C CG  . ASP B 1 149 ? -32.681 36.118  49.096  1.00 58.98  ? 149 ASP B CG  1 
ATOM   5347  O OD1 . ASP B 1 149 ? -32.096 35.150  49.627  1.00 56.34  ? 149 ASP B OD1 1 
ATOM   5348  O OD2 . ASP B 1 149 ? -33.404 36.911  49.735  1.00 71.11  ? 149 ASP B OD2 1 
ATOM   5349  N N   . LEU B 1 150 ? -32.530 35.500  44.614  1.00 39.40  ? 150 LEU B N   1 
ATOM   5350  C CA  . LEU B 1 150 ? -33.249 35.119  43.401  1.00 33.52  ? 150 LEU B CA  1 
ATOM   5351  C C   . LEU B 1 150 ? -32.618 33.910  42.726  1.00 37.38  ? 150 LEU B C   1 
ATOM   5352  O O   . LEU B 1 150 ? -33.330 33.084  42.145  1.00 42.71  ? 150 LEU B O   1 
ATOM   5353  C CB  . LEU B 1 150 ? -33.305 36.293  42.424  1.00 35.64  ? 150 LEU B CB  1 
ATOM   5354  C CG  . LEU B 1 150 ? -34.094 37.527  42.855  1.00 31.82  ? 150 LEU B CG  1 
ATOM   5355  C CD1 . LEU B 1 150 ? -33.777 38.700  41.943  1.00 30.46  ? 150 LEU B CD1 1 
ATOM   5356  C CD2 . LEU B 1 150 ? -35.586 37.232  42.855  1.00 32.85  ? 150 LEU B CD2 1 
ATOM   5357  N N   . LEU B 1 151 ? -31.289 33.792  42.784  1.00 38.00  ? 151 LEU B N   1 
ATOM   5358  C CA  . LEU B 1 151 ? -30.618 32.671  42.137  1.00 36.03  ? 151 LEU B CA  1 
ATOM   5359  C C   . LEU B 1 151 ? -31.038 31.340  42.745  1.00 39.36  ? 151 LEU B C   1 
ATOM   5360  O O   . LEU B 1 151 ? -31.139 30.337  42.030  1.00 44.45  ? 151 LEU B O   1 
ATOM   5361  C CB  . LEU B 1 151 ? -29.102 32.847  42.224  1.00 38.66  ? 151 LEU B CB  1 
ATOM   5362  C CG  . LEU B 1 151 ? -28.502 33.804  41.192  1.00 44.59  ? 151 LEU B CG  1 
ATOM   5363  C CD1 . LEU B 1 151 ? -27.008 33.976  41.413  1.00 46.99  ? 151 LEU B CD1 1 
ATOM   5364  C CD2 . LEU B 1 151 ? -28.788 33.314  39.783  1.00 43.87  ? 151 LEU B CD2 1 
ATOM   5365  N N   . ASN B 1 152 ? -31.289 31.308  44.053  1.00 46.71  ? 152 ASN B N   1 
ATOM   5366  C CA  . ASN B 1 152 ? -31.745 30.097  44.720  1.00 49.39  ? 152 ASN B CA  1 
ATOM   5367  C C   . ASN B 1 152 ? -33.262 30.007  44.834  1.00 45.89  ? 152 ASN B C   1 
ATOM   5368  O O   . ASN B 1 152 ? -33.771 28.972  45.280  1.00 48.38  ? 152 ASN B O   1 
ATOM   5369  C CB  . ASN B 1 152 ? -31.109 29.994  46.112  1.00 38.43  ? 152 ASN B CB  1 
ATOM   5370  C CG  . ASN B 1 152 ? -29.617 29.721  46.045  1.00 51.47  ? 152 ASN B CG  1 
ATOM   5371  O OD1 . ASN B 1 152 ? -29.143 29.029  45.144  1.00 59.23  ? 152 ASN B OD1 1 
ATOM   5372  N ND2 . ASN B 1 152 ? -28.870 30.262  47.001  1.00 55.87  ? 152 ASN B ND2 1 
ATOM   5373  N N   . LYS B 1 153 ? -33.992 31.058  44.452  1.00 41.63  ? 153 LYS B N   1 
ATOM   5374  C CA  . LYS B 1 153 ? -35.445 30.950  44.359  1.00 39.09  ? 153 LYS B CA  1 
ATOM   5375  C C   . LYS B 1 153 ? -35.849 29.976  43.263  1.00 46.40  ? 153 LYS B C   1 
ATOM   5376  O O   . LYS B 1 153 ? -36.876 29.295  43.379  1.00 52.02  ? 153 LYS B O   1 
ATOM   5377  C CB  . LYS B 1 153 ? -36.060 32.329  44.108  1.00 37.63  ? 153 LYS B CB  1 
ATOM   5378  C CG  . LYS B 1 153 ? -37.563 32.394  44.317  1.00 37.44  ? 153 LYS B CG  1 
ATOM   5379  C CD  . LYS B 1 153 ? -38.131 33.679  43.744  1.00 42.47  ? 153 LYS B CD  1 
ATOM   5380  C CE  . LYS B 1 153 ? -39.477 34.014  44.357  1.00 44.72  ? 153 LYS B CE  1 
ATOM   5381  N NZ  . LYS B 1 153 ? -39.564 35.454  44.715  1.00 51.48  ? 153 LYS B NZ  1 
ATOM   5382  N N   . GLY B 1 154 ? -35.054 29.898  42.202  1.00 34.84  ? 154 GLY B N   1 
ATOM   5383  C CA  . GLY B 1 154 ? -35.183 28.852  41.204  1.00 37.57  ? 154 GLY B CA  1 
ATOM   5384  C C   . GLY B 1 154 ? -36.304 29.038  40.209  1.00 39.21  ? 154 GLY B C   1 
ATOM   5385  O O   . GLY B 1 154 ? -36.076 28.966  38.999  1.00 40.84  ? 154 GLY B O   1 
ATOM   5386  N N   . ARG B 1 155 ? -37.517 29.280  40.699  1.00 38.40  ? 155 ARG B N   1 
ATOM   5387  C CA  . ARG B 1 155 ? -38.687 29.394  39.837  1.00 38.73  ? 155 ARG B CA  1 
ATOM   5388  C C   . ARG B 1 155 ? -39.602 30.475  40.406  1.00 44.45  ? 155 ARG B C   1 
ATOM   5389  O O   . ARG B 1 155 ? -39.251 31.174  41.364  1.00 38.84  ? 155 ARG B O   1 
ATOM   5390  C CB  . ARG B 1 155 ? -39.398 28.039  39.714  1.00 36.46  ? 155 ARG B CB  1 
ATOM   5391  C CG  . ARG B 1 155 ? -39.544 27.292  41.033  1.00 38.36  ? 155 ARG B CG  1 
ATOM   5392  C CD  . ARG B 1 155 ? -40.213 25.935  40.843  1.00 49.99  ? 155 ARG B CD  1 
ATOM   5393  N NE  . ARG B 1 155 ? -39.528 25.106  39.857  1.00 61.60  ? 155 ARG B NE  1 
ATOM   5394  C CZ  . ARG B 1 155 ? -38.486 24.329  40.125  1.00 56.82  ? 155 ARG B CZ  1 
ATOM   5395  N NH1 . ARG B 1 155 ? -37.967 24.264  41.339  1.00 48.45  ? 155 ARG B NH1 1 
ATOM   5396  N NH2 . ARG B 1 155 ? -37.949 23.604  39.148  1.00 52.16  ? 155 ARG B NH2 1 
ATOM   5397  N N   . ASN B 1 156 ? -40.783 30.609  39.805  1.00 44.33  ? 156 ASN B N   1 
ATOM   5398  C CA  . ASN B 1 156 ? -41.809 31.552  40.246  1.00 40.74  ? 156 ASN B CA  1 
ATOM   5399  C C   . ASN B 1 156 ? -41.248 32.970  40.348  1.00 46.73  ? 156 ASN B C   1 
ATOM   5400  O O   . ASN B 1 156 ? -41.167 33.566  41.422  1.00 48.51  ? 156 ASN B O   1 
ATOM   5401  C CB  . ASN B 1 156 ? -42.426 31.107  41.573  1.00 38.76  ? 156 ASN B CB  1 
ATOM   5402  C CG  . ASN B 1 156 ? -43.376 29.942  41.410  1.00 46.14  ? 156 ASN B CG  1 
ATOM   5403  O OD1 . ASN B 1 156 ? -43.276 29.175  40.452  1.00 50.22  ? 156 ASN B OD1 1 
ATOM   5404  N ND2 . ASN B 1 156 ? -44.315 29.808  42.339  1.00 57.26  ? 156 ASN B ND2 1 
ATOM   5405  N N   . TYR B 1 157 ? -40.848 33.499  39.199  1.00 43.35  ? 157 TYR B N   1 
ATOM   5406  C CA  . TYR B 1 157 ? -40.312 34.847  39.123  1.00 36.75  ? 157 TYR B CA  1 
ATOM   5407  C C   . TYR B 1 157 ? -41.409 35.847  38.775  1.00 33.42  ? 157 TYR B C   1 
ATOM   5408  O O   . TYR B 1 157 ? -42.491 35.488  38.308  1.00 36.73  ? 157 TYR B O   1 
ATOM   5409  C CB  . TYR B 1 157 ? -39.167 34.913  38.112  1.00 33.51  ? 157 TYR B CB  1 
ATOM   5410  C CG  . TYR B 1 157 ? -37.908 34.279  38.650  1.00 31.13  ? 157 TYR B CG  1 
ATOM   5411  C CD1 . TYR B 1 157 ? -37.211 34.865  39.698  1.00 31.37  ? 157 TYR B CD1 1 
ATOM   5412  C CD2 . TYR B 1 157 ? -37.434 33.079  38.138  1.00 30.83  ? 157 TYR B CD2 1 
ATOM   5413  C CE1 . TYR B 1 157 ? -36.067 34.287  40.207  1.00 36.21  ? 157 TYR B CE1 1 
ATOM   5414  C CE2 . TYR B 1 157 ? -36.288 32.492  38.641  1.00 34.88  ? 157 TYR B CE2 1 
ATOM   5415  C CZ  . TYR B 1 157 ? -35.609 33.100  39.677  1.00 38.07  ? 157 TYR B CZ  1 
ATOM   5416  O OH  . TYR B 1 157 ? -34.467 32.524  40.186  1.00 46.79  ? 157 TYR B OH  1 
ATOM   5417  N N   . THR B 1 158 ? -41.111 37.117  39.025  1.00 33.11  ? 158 THR B N   1 
ATOM   5418  C CA  . THR B 1 158 ? -42.084 38.195  38.964  1.00 33.66  ? 158 THR B CA  1 
ATOM   5419  C C   . THR B 1 158 ? -41.557 39.290  38.044  1.00 35.55  ? 158 THR B C   1 
ATOM   5420  O O   . THR B 1 158 ? -40.344 39.479  37.917  1.00 34.89  ? 158 THR B O   1 
ATOM   5421  C CB  . THR B 1 158 ? -42.354 38.739  40.383  1.00 35.12  ? 158 THR B CB  1 
ATOM   5422  O OG1 . THR B 1 158 ? -43.050 37.746  41.146  1.00 41.78  ? 158 THR B OG1 1 
ATOM   5423  C CG2 . THR B 1 158 ? -43.198 39.999  40.362  1.00 40.61  ? 158 THR B CG2 1 
ATOM   5424  N N   . GLN B 1 159 ? -42.480 39.992  37.376  1.00 32.50  ? 159 GLN B N   1 
ATOM   5425  C CA  . GLN B 1 159 ? -42.091 41.138  36.558  1.00 31.54  ? 159 GLN B CA  1 
ATOM   5426  C C   . GLN B 1 159 ? -41.313 42.164  37.373  1.00 32.55  ? 159 GLN B C   1 
ATOM   5427  O O   . GLN B 1 159 ? -40.430 42.844  36.839  1.00 33.65  ? 159 GLN B O   1 
ATOM   5428  C CB  . GLN B 1 159 ? -43.327 41.783  35.932  1.00 32.15  ? 159 GLN B CB  1 
ATOM   5429  C CG  . GLN B 1 159 ? -43.025 42.944  34.999  1.00 31.36  ? 159 GLN B CG  1 
ATOM   5430  C CD  . GLN B 1 159 ? -42.571 42.484  33.630  1.00 30.08  ? 159 GLN B CD  1 
ATOM   5431  O OE1 . GLN B 1 159 ? -42.809 41.342  33.236  1.00 33.81  ? 159 GLN B OE1 1 
ATOM   5432  N NE2 . GLN B 1 159 ? -41.907 43.370  32.898  1.00 29.22  ? 159 GLN B NE2 1 
ATOM   5433  N N   . GLU B 1 160 ? -41.628 42.290  38.663  1.00 32.91  ? 160 GLU B N   1 
ATOM   5434  C CA  . GLU B 1 160 ? -40.844 43.154  39.538  1.00 33.16  ? 160 GLU B CA  1 
ATOM   5435  C C   . GLU B 1 160 ? -39.470 42.558  39.818  1.00 32.28  ? 160 GLU B C   1 
ATOM   5436  O O   . GLU B 1 160 ? -38.472 43.287  39.874  1.00 31.67  ? 160 GLU B O   1 
ATOM   5437  C CB  . GLU B 1 160 ? -41.604 43.402  40.842  1.00 42.58  ? 160 GLU B CB  1 
ATOM   5438  C CG  . GLU B 1 160 ? -42.716 44.452  40.753  1.00 54.52  ? 160 GLU B CG  1 
ATOM   5439  C CD  . GLU B 1 160 ? -43.814 44.100  39.756  1.00 56.34  ? 160 GLU B CD  1 
ATOM   5440  O OE1 . GLU B 1 160 ? -43.961 42.910  39.407  1.00 52.06  ? 160 GLU B OE1 1 
ATOM   5441  O OE2 . GLU B 1 160 ? -44.537 45.022  39.322  1.00 63.61  ? 160 GLU B OE2 1 
ATOM   5442  N N   . GLU B 1 161 ? -39.396 41.236  40.004  1.00 33.39  ? 161 GLU B N   1 
ATOM   5443  C CA  . GLU B 1 161 ? -38.104 40.596  40.242  1.00 31.57  ? 161 GLU B CA  1 
ATOM   5444  C C   . GLU B 1 161 ? -37.249 40.577  38.982  1.00 29.79  ? 161 GLU B C   1 
ATOM   5445  O O   . GLU B 1 161 ? -36.036 40.806  39.049  1.00 29.00  ? 161 GLU B O   1 
ATOM   5446  C CB  . GLU B 1 161 ? -38.301 39.175  40.768  1.00 32.29  ? 161 GLU B CB  1 
ATOM   5447  C CG  . GLU B 1 161 ? -39.170 39.085  42.006  1.00 45.96  ? 161 GLU B CG  1 
ATOM   5448  C CD  . GLU B 1 161 ? -39.397 37.655  42.449  1.00 43.26  ? 161 GLU B CD  1 
ATOM   5449  O OE1 . GLU B 1 161 ? -39.167 36.739  41.633  1.00 43.77  ? 161 GLU B OE1 1 
ATOM   5450  O OE2 . GLU B 1 161 ? -39.806 37.448  43.611  1.00 42.81  ? 161 GLU B OE2 1 
ATOM   5451  N N   . LYS B 1 162 ? -37.855 40.291  37.826  1.00 29.25  ? 162 LYS B N   1 
ATOM   5452  C CA  . LYS B 1 162 ? -37.096 40.301  36.579  1.00 27.72  ? 162 LYS B CA  1 
ATOM   5453  C C   . LYS B 1 162 ? -36.560 41.693  36.274  1.00 28.59  ? 162 LYS B C   1 
ATOM   5454  O O   . LYS B 1 162 ? -35.411 41.844  35.842  1.00 27.68  ? 162 LYS B O   1 
ATOM   5455  C CB  . LYS B 1 162 ? -37.957 39.802  35.422  1.00 27.54  ? 162 LYS B CB  1 
ATOM   5456  C CG  . LYS B 1 162 ? -37.194 39.700  34.107  1.00 26.14  ? 162 LYS B CG  1 
ATOM   5457  C CD  . LYS B 1 162 ? -38.015 40.172  32.917  1.00 26.03  ? 162 LYS B CD  1 
ATOM   5458  C CE  . LYS B 1 162 ? -39.495 39.856  33.077  1.00 32.32  ? 162 LYS B CE  1 
ATOM   5459  N NZ  . LYS B 1 162 ? -40.338 40.774  32.258  1.00 27.45  ? 162 LYS B NZ  1 
ATOM   5460  N N   . GLU B 1 163 ? -37.382 42.725  36.482  1.00 30.51  ? 163 GLU B N   1 
ATOM   5461  C CA  . GLU B 1 163 ? -36.914 44.087  36.256  1.00 27.64  ? 163 GLU B CA  1 
ATOM   5462  C C   . GLU B 1 163 ? -35.864 44.493  37.283  1.00 29.74  ? 163 GLU B C   1 
ATOM   5463  O O   . GLU B 1 163 ? -35.023 45.353  36.997  1.00 31.99  ? 163 GLU B O   1 
ATOM   5464  C CB  . GLU B 1 163 ? -38.096 45.058  36.271  1.00 28.70  ? 163 GLU B CB  1 
ATOM   5465  C CG  . GLU B 1 163 ? -38.844 45.114  34.945  1.00 41.15  ? 163 GLU B CG  1 
ATOM   5466  C CD  . GLU B 1 163 ? -40.115 45.939  35.012  1.00 56.49  ? 163 GLU B CD  1 
ATOM   5467  O OE1 . GLU B 1 163 ? -40.142 46.929  35.769  1.00 61.28  ? 163 GLU B OE1 1 
ATOM   5468  O OE2 . GLU B 1 163 ? -41.085 45.602  34.299  1.00 57.70  ? 163 GLU B OE2 1 
ATOM   5469  N N   . TYR B 1 164 ? -35.894 43.892  38.478  1.00 29.31  ? 164 TYR B N   1 
ATOM   5470  C CA  . TYR B 1 164 ? -34.833 44.135  39.450  1.00 28.86  ? 164 TYR B CA  1 
ATOM   5471  C C   . TYR B 1 164 ? -33.495 43.604  38.951  1.00 27.46  ? 164 TYR B C   1 
ATOM   5472  O O   . TYR B 1 164 ? -32.462 44.265  39.108  1.00 27.08  ? 164 TYR B O   1 
ATOM   5473  C CB  . TYR B 1 164 ? -35.192 43.505  40.794  1.00 31.64  ? 164 TYR B CB  1 
ATOM   5474  C CG  . TYR B 1 164 ? -34.149 43.753  41.861  1.00 30.73  ? 164 TYR B CG  1 
ATOM   5475  C CD1 . TYR B 1 164 ? -33.860 45.041  42.289  1.00 39.52  ? 164 TYR B CD1 1 
ATOM   5476  C CD2 . TYR B 1 164 ? -33.444 42.700  42.430  1.00 30.76  ? 164 TYR B CD2 1 
ATOM   5477  C CE1 . TYR B 1 164 ? -32.904 45.276  43.259  1.00 38.87  ? 164 TYR B CE1 1 
ATOM   5478  C CE2 . TYR B 1 164 ? -32.487 42.923  43.400  1.00 36.09  ? 164 TYR B CE2 1 
ATOM   5479  C CZ  . TYR B 1 164 ? -32.221 44.213  43.812  1.00 37.27  ? 164 TYR B CZ  1 
ATOM   5480  O OH  . TYR B 1 164 ? -31.268 44.441  44.779  1.00 49.36  ? 164 TYR B OH  1 
ATOM   5481  N N   . VAL B 1 165 ? -33.493 42.411  38.353  1.00 26.80  ? 165 VAL B N   1 
ATOM   5482  C CA  . VAL B 1 165 ? -32.269 41.874  37.764  1.00 25.51  ? 165 VAL B CA  1 
ATOM   5483  C C   . VAL B 1 165 ? -31.803 42.758  36.615  1.00 24.39  ? 165 VAL B C   1 
ATOM   5484  O O   . VAL B 1 165 ? -30.599 42.966  36.417  1.00 29.15  ? 165 VAL B O   1 
ATOM   5485  C CB  . VAL B 1 165 ? -32.493 40.421  37.304  1.00 25.25  ? 165 VAL B CB  1 
ATOM   5486  C CG1 . VAL B 1 165 ? -31.223 39.846  36.688  1.00 24.04  ? 165 VAL B CG1 1 
ATOM   5487  C CG2 . VAL B 1 165 ? -32.959 39.561  38.466  1.00 26.54  ? 165 VAL B CG2 1 
ATOM   5488  N N   . LEU B 1 166 ? -32.749 43.295  35.842  1.00 28.91  ? 166 LEU B N   1 
ATOM   5489  C CA  . LEU B 1 166 ? -32.390 44.098  34.677  1.00 28.47  ? 166 LEU B CA  1 
ATOM   5490  C C   . LEU B 1 166 ? -31.656 45.374  35.075  1.00 32.44  ? 166 LEU B C   1 
ATOM   5491  O O   . LEU B 1 166 ? -30.680 45.758  34.421  1.00 31.17  ? 166 LEU B O   1 
ATOM   5492  C CB  . LEU B 1 166 ? -33.641 44.425  33.862  1.00 32.20  ? 166 LEU B CB  1 
ATOM   5493  C CG  . LEU B 1 166 ? -34.014 43.393  32.792  1.00 29.18  ? 166 LEU B CG  1 
ATOM   5494  C CD1 . LEU B 1 166 ? -35.457 43.571  32.337  1.00 24.10  ? 166 LEU B CD1 1 
ATOM   5495  C CD2 . LEU B 1 166 ? -33.057 43.471  31.610  1.00 22.15  ? 166 LEU B CD2 1 
ATOM   5496  N N   . ASN B 1 167 ? -32.105 46.047  36.137  1.00 30.37  ? 167 ASN B N   1 
ATOM   5497  C CA  . ASN B 1 167 ? -31.453 47.291  36.537  1.00 31.85  ? 167 ASN B CA  1 
ATOM   5498  C C   . ASN B 1 167 ? -30.033 47.041  37.033  1.00 31.25  ? 167 ASN B C   1 
ATOM   5499  O O   . ASN B 1 167 ? -29.089 47.715  36.604  1.00 33.18  ? 167 ASN B O   1 
ATOM   5500  C CB  . ASN B 1 167 ? -32.270 48.009  37.611  1.00 28.17  ? 167 ASN B CB  1 
ATOM   5501  C CG  . ASN B 1 167 ? -31.614 49.302  38.064  1.00 38.22  ? 167 ASN B CG  1 
ATOM   5502  O OD1 . ASN B 1 167 ? -31.595 50.291  37.331  1.00 39.25  ? 167 ASN B OD1 1 
ATOM   5503  N ND2 . ASN B 1 167 ? -31.064 49.297  39.275  1.00 37.72  ? 167 ASN B ND2 1 
ATOM   5504  N N   . LYS B 1 168 ? -29.864 46.074  37.942  1.00 26.53  ? 168 LYS B N   1 
ATOM   5505  C CA  . LYS B 1 168 ? -28.531 45.755  38.441  1.00 24.62  ? 168 LYS B CA  1 
ATOM   5506  C C   . LYS B 1 168 ? -27.611 45.306  37.315  1.00 25.95  ? 168 LYS B C   1 
ATOM   5507  O O   . LYS B 1 168 ? -26.398 45.536  37.374  1.00 35.06  ? 168 LYS B O   1 
ATOM   5508  C CB  . LYS B 1 168 ? -28.610 44.680  39.525  1.00 25.38  ? 168 LYS B CB  1 
ATOM   5509  C CG  . LYS B 1 168 ? -29.615 44.974  40.627  1.00 27.03  ? 168 LYS B CG  1 
ATOM   5510  C CD  . LYS B 1 168 ? -28.941 45.037  41.987  1.00 28.10  ? 168 LYS B CD  1 
ATOM   5511  C CE  . LYS B 1 168 ? -28.237 46.369  42.192  1.00 39.05  ? 168 LYS B CE  1 
ATOM   5512  N NZ  . LYS B 1 168 ? -27.463 46.410  43.466  1.00 42.00  ? 168 LYS B NZ  1 
ATOM   5513  N N   . TYR B 1 169 ? -28.169 44.672  36.280  1.00 25.23  ? 169 TYR B N   1 
ATOM   5514  C CA  . TYR B 1 169 ? -27.365 44.305  35.122  1.00 26.00  ? 169 TYR B CA  1 
ATOM   5515  C C   . TYR B 1 169 ? -26.875 45.535  34.370  1.00 29.79  ? 169 TYR B C   1 
ATOM   5516  O O   . TYR B 1 169 ? -25.787 45.506  33.780  1.00 33.39  ? 169 TYR B O   1 
ATOM   5517  C CB  . TYR B 1 169 ? -28.166 43.393  34.193  1.00 21.01  ? 169 TYR B CB  1 
ATOM   5518  C CG  . TYR B 1 169 ? -28.095 41.930  34.565  1.00 20.84  ? 169 TYR B CG  1 
ATOM   5519  C CD1 . TYR B 1 169 ? -27.775 41.538  35.858  1.00 21.55  ? 169 TYR B CD1 1 
ATOM   5520  C CD2 . TYR B 1 169 ? -28.350 40.941  33.624  1.00 20.37  ? 169 TYR B CD2 1 
ATOM   5521  C CE1 . TYR B 1 169 ? -27.710 40.204  36.203  1.00 23.36  ? 169 TYR B CE1 1 
ATOM   5522  C CE2 . TYR B 1 169 ? -28.287 39.603  33.961  1.00 20.59  ? 169 TYR B CE2 1 
ATOM   5523  C CZ  . TYR B 1 169 ? -27.967 39.239  35.252  1.00 24.40  ? 169 TYR B CZ  1 
ATOM   5524  O OH  . TYR B 1 169 ? -27.902 37.906  35.593  1.00 31.37  ? 169 TYR B OH  1 
ATOM   5525  N N   . PHE B 1 170 ? -27.652 46.620  34.381  1.00 29.43  ? 170 PHE B N   1 
ATOM   5526  C CA  . PHE B 1 170 ? -27.211 47.846  33.728  1.00 37.19  ? 170 PHE B CA  1 
ATOM   5527  C C   . PHE B 1 170 ? -26.313 48.685  34.625  1.00 35.18  ? 170 PHE B C   1 
ATOM   5528  O O   . PHE B 1 170 ? -25.467 49.431  34.118  1.00 32.07  ? 170 PHE B O   1 
ATOM   5529  C CB  . PHE B 1 170 ? -28.419 48.663  33.268  1.00 34.34  ? 170 PHE B CB  1 
ATOM   5530  C CG  . PHE B 1 170 ? -28.988 48.197  31.961  1.00 31.01  ? 170 PHE B CG  1 
ATOM   5531  C CD1 . PHE B 1 170 ? -28.413 48.585  30.763  1.00 34.96  ? 170 PHE B CD1 1 
ATOM   5532  C CD2 . PHE B 1 170 ? -30.096 47.365  31.931  1.00 29.67  ? 170 PHE B CD2 1 
ATOM   5533  C CE1 . PHE B 1 170 ? -28.933 48.154  29.556  1.00 36.45  ? 170 PHE B CE1 1 
ATOM   5534  C CE2 . PHE B 1 170 ? -30.622 46.931  30.728  1.00 41.75  ? 170 PHE B CE2 1 
ATOM   5535  C CZ  . PHE B 1 170 ? -30.040 47.326  29.538  1.00 36.23  ? 170 PHE B CZ  1 
ATOM   5536  N N   . GLU B 1 171 ? -26.474 48.580  35.947  1.00 33.39  ? 171 GLU B N   1 
ATOM   5537  C CA  . GLU B 1 171 ? -25.525 49.218  36.854  1.00 34.18  ? 171 GLU B CA  1 
ATOM   5538  C C   . GLU B 1 171 ? -24.115 48.705  36.606  1.00 31.23  ? 171 GLU B C   1 
ATOM   5539  O O   . GLU B 1 171 ? -23.158 49.487  36.556  1.00 30.04  ? 171 GLU B O   1 
ATOM   5540  C CB  . GLU B 1 171 ? -25.935 48.969  38.306  1.00 37.21  ? 171 GLU B CB  1 
ATOM   5541  C CG  . GLU B 1 171 ? -25.593 50.098  39.265  1.00 56.09  ? 171 GLU B CG  1 
ATOM   5542  C CD  . GLU B 1 171 ? -25.313 49.601  40.673  1.00 68.05  ? 171 GLU B CD  1 
ATOM   5543  O OE1 . GLU B 1 171 ? -24.781 48.480  40.816  1.00 71.52  ? 171 GLU B OE1 1 
ATOM   5544  O OE2 . GLU B 1 171 ? -25.628 50.331  41.637  1.00 70.65  ? 171 GLU B OE2 1 
ATOM   5545  N N   . ILE B 1 172 ? -23.974 47.391  36.435  1.00 29.57  ? 172 ILE B N   1 
ATOM   5546  C CA  . ILE B 1 172 ? -22.673 46.796  36.151  1.00 26.77  ? 172 ILE B CA  1 
ATOM   5547  C C   . ILE B 1 172 ? -22.144 47.284  34.808  1.00 28.12  ? 172 ILE B C   1 
ATOM   5548  O O   . ILE B 1 172 ? -20.956 47.606  34.670  1.00 21.01  ? 172 ILE B O   1 
ATOM   5549  C CB  . ILE B 1 172 ? -22.781 45.261  36.204  1.00 34.20  ? 172 ILE B CB  1 
ATOM   5550  C CG1 . ILE B 1 172 ? -22.995 44.799  37.649  1.00 30.36  ? 172 ILE B CG1 1 
ATOM   5551  C CG2 . ILE B 1 172 ? -21.561 44.607  35.579  1.00 33.43  ? 172 ILE B CG2 1 
ATOM   5552  C CD1 . ILE B 1 172 ? -21.716 44.470  38.392  1.00 43.00  ? 172 ILE B CD1 1 
ATOM   5553  N N   . ILE B 1 173 ? -23.015 47.345  33.797  1.00 27.94  ? 173 ILE B N   1 
ATOM   5554  C CA  . ILE B 1 173 ? -22.611 47.857  32.489  1.00 29.14  ? 173 ILE B CA  1 
ATOM   5555  C C   . ILE B 1 173 ? -22.154 49.306  32.602  1.00 31.52  ? 173 ILE B C   1 
ATOM   5556  O O   . ILE B 1 173 ? -21.132 49.701  32.025  1.00 28.56  ? 173 ILE B O   1 
ATOM   5557  C CB  . ILE B 1 173 ? -23.763 47.710  31.476  1.00 21.14  ? 173 ILE B CB  1 
ATOM   5558  C CG1 . ILE B 1 173 ? -23.906 46.256  31.030  1.00 17.67  ? 173 ILE B CG1 1 
ATOM   5559  C CG2 . ILE B 1 173 ? -23.544 48.621  30.276  1.00 18.01  ? 173 ILE B CG2 1 
ATOM   5560  C CD1 . ILE B 1 173 ? -24.957 46.056  29.967  1.00 17.62  ? 173 ILE B CD1 1 
ATOM   5561  N N   . LYS B 1 174 ? -22.899 50.119  33.355  1.00 31.61  ? 174 LYS B N   1 
ATOM   5562  C CA  . LYS B 1 174 ? -22.595 51.542  33.466  1.00 29.44  ? 174 LYS B CA  1 
ATOM   5563  C C   . LYS B 1 174 ? -21.245 51.809  34.123  1.00 31.85  ? 174 LYS B C   1 
ATOM   5564  O O   . LYS B 1 174 ? -20.723 52.923  33.999  1.00 33.44  ? 174 LYS B O   1 
ATOM   5565  C CB  . LYS B 1 174 ? -23.704 52.249  34.248  1.00 28.92  ? 174 LYS B CB  1 
ATOM   5566  C CG  . LYS B 1 174 ? -25.001 52.423  33.471  1.00 26.86  ? 174 LYS B CG  1 
ATOM   5567  C CD  . LYS B 1 174 ? -25.832 53.569  34.022  1.00 33.28  ? 174 LYS B CD  1 
ATOM   5568  C CE  . LYS B 1 174 ? -27.054 53.049  34.768  1.00 50.27  ? 174 LYS B CE  1 
ATOM   5569  N NZ  . LYS B 1 174 ? -28.130 52.590  33.841  1.00 46.11  ? 174 LYS B NZ  1 
ATOM   5570  N N   . LYS B 1 175 ? -20.665 50.825  34.815  1.00 22.86  ? 175 LYS B N   1 
ATOM   5571  C CA  . LYS B 1 175 ? -19.381 51.013  35.482  1.00 20.90  ? 175 LYS B CA  1 
ATOM   5572  C C   . LYS B 1 175 ? -18.301 50.077  34.948  1.00 27.10  ? 175 LYS B C   1 
ATOM   5573  O O   . LYS B 1 175 ? -17.301 49.840  35.634  1.00 26.57  ? 175 LYS B O   1 
ATOM   5574  C CB  . LYS B 1 175 ? -19.530 50.839  36.997  1.00 22.52  ? 175 LYS B CB  1 
ATOM   5575  C CG  . LYS B 1 175 ? -20.047 49.478  37.440  1.00 21.66  ? 175 LYS B CG  1 
ATOM   5576  C CD  . LYS B 1 175 ? -20.571 49.540  38.869  1.00 37.50  ? 175 LYS B CD  1 
ATOM   5577  C CE  . LYS B 1 175 ? -20.301 48.248  39.629  1.00 50.30  ? 175 LYS B CE  1 
ATOM   5578  N NZ  . LYS B 1 175 ? -21.022 48.219  40.935  1.00 46.70  ? 175 LYS B NZ  1 
ATOM   5579  N N   . THR B 1 176 ? -18.475 49.536  33.739  1.00 28.71  ? 176 THR B N   1 
ATOM   5580  C CA  . THR B 1 176 ? -17.456 48.650  33.182  1.00 17.38  ? 176 THR B CA  1 
ATOM   5581  C C   . THR B 1 176 ? -16.204 49.424  32.784  1.00 25.10  ? 176 THR B C   1 
ATOM   5582  O O   . THR B 1 176 ? -15.084 49.038  33.138  1.00 34.94  ? 176 THR B O   1 
ATOM   5583  C CB  . THR B 1 176 ? -18.015 47.880  31.985  1.00 20.91  ? 176 THR B CB  1 
ATOM   5584  O OG1 . THR B 1 176 ? -18.978 46.922  32.438  1.00 29.31  ? 176 THR B OG1 1 
ATOM   5585  C CG2 . THR B 1 176 ? -16.897 47.149  31.252  1.00 18.43  ? 176 THR B CG2 1 
ATOM   5586  N N   . LEU B 1 177 ? -16.368 50.525  32.047  1.00 29.42  ? 177 LEU B N   1 
ATOM   5587  C CA  . LEU B 1 177 ? -15.198 51.287  31.621  1.00 25.40  ? 177 LEU B CA  1 
ATOM   5588  C C   . LEU B 1 177 ? -14.527 51.992  32.793  1.00 21.30  ? 177 LEU B C   1 
ATOM   5589  O O   . LEU B 1 177 ? -13.321 52.255  32.746  1.00 26.62  ? 177 LEU B O   1 
ATOM   5590  C CB  . LEU B 1 177 ? -15.586 52.293  30.536  1.00 21.73  ? 177 LEU B CB  1 
ATOM   5591  C CG  . LEU B 1 177 ? -16.067 51.668  29.225  1.00 16.61  ? 177 LEU B CG  1 
ATOM   5592  C CD1 . LEU B 1 177 ? -16.347 52.739  28.183  1.00 16.98  ? 177 LEU B CD1 1 
ATOM   5593  C CD2 . LEU B 1 177 ? -15.047 50.663  28.710  1.00 15.64  ? 177 LEU B CD2 1 
ATOM   5594  N N   . SER B 1 178 ? -15.285 52.304  33.846  1.00 19.51  ? 178 SER B N   1 
ATOM   5595  C CA  . SER B 1 178 ? -14.694 52.933  35.023  1.00 22.05  ? 178 SER B CA  1 
ATOM   5596  C C   . SER B 1 178 ? -13.704 52.005  35.718  1.00 28.08  ? 178 SER B C   1 
ATOM   5597  O O   . SER B 1 178 ? -12.627 52.444  36.136  1.00 33.45  ? 178 SER B O   1 
ATOM   5598  C CB  . SER B 1 178 ? -15.793 53.370  35.993  1.00 25.58  ? 178 SER B CB  1 
ATOM   5599  O OG  . SER B 1 178 ? -16.752 54.192  35.344  1.00 33.33  ? 178 SER B OG  1 
ATOM   5600  N N   . ILE B 1 179 ? -14.048 50.721  35.854  1.00 34.53  ? 179 ILE B N   1 
ATOM   5601  C CA  . ILE B 1 179 ? -13.167 49.808  36.578  1.00 29.78  ? 179 ILE B CA  1 
ATOM   5602  C C   . ILE B 1 179 ? -11.885 49.541  35.793  1.00 26.16  ? 179 ILE B C   1 
ATOM   5603  O O   . ILE B 1 179 ? -10.810 49.393  36.388  1.00 34.55  ? 179 ILE B O   1 
ATOM   5604  C CB  . ILE B 1 179 ? -13.901 48.502  36.944  1.00 29.29  ? 179 ILE B CB  1 
ATOM   5605  C CG1 . ILE B 1 179 ? -13.079 47.705  37.958  1.00 33.43  ? 179 ILE B CG1 1 
ATOM   5606  C CG2 . ILE B 1 179 ? -14.173 47.649  35.719  1.00 30.42  ? 179 ILE B CG2 1 
ATOM   5607  C CD1 . ILE B 1 179 ? -13.605 46.319  38.205  1.00 30.15  ? 179 ILE B CD1 1 
ATOM   5608  N N   . TYR B 1 180 ? -11.967 49.468  34.460  1.00 25.32  ? 180 TYR B N   1 
ATOM   5609  C CA  . TYR B 1 180 ? -10.754 49.342  33.657  1.00 25.11  ? 180 TYR B CA  1 
ATOM   5610  C C   . TYR B 1 180 ? -9.871  50.567  33.823  1.00 23.57  ? 180 TYR B C   1 
ATOM   5611  O O   . TYR B 1 180 ? -8.643  50.452  33.918  1.00 19.25  ? 180 TYR B O   1 
ATOM   5612  C CB  . TYR B 1 180 ? -11.112 49.144  32.186  1.00 23.58  ? 180 TYR B CB  1 
ATOM   5613  C CG  . TYR B 1 180 ? -11.486 47.730  31.832  1.00 21.26  ? 180 TYR B CG  1 
ATOM   5614  C CD1 . TYR B 1 180 ? -10.512 46.780  31.554  1.00 21.82  ? 180 TYR B CD1 1 
ATOM   5615  C CD2 . TYR B 1 180 ? -12.813 47.346  31.766  1.00 22.78  ? 180 TYR B CD2 1 
ATOM   5616  C CE1 . TYR B 1 180 ? -10.855 45.483  31.228  1.00 20.11  ? 180 TYR B CE1 1 
ATOM   5617  C CE2 . TYR B 1 180 ? -13.162 46.060  31.438  1.00 25.44  ? 180 TYR B CE2 1 
ATOM   5618  C CZ  . TYR B 1 180 ? -12.185 45.129  31.172  1.00 19.07  ? 180 TYR B CZ  1 
ATOM   5619  O OH  . TYR B 1 180 ? -12.548 43.842  30.846  1.00 13.75  ? 180 TYR B OH  1 
ATOM   5620  N N   . ARG B 1 181 ? -10.490 51.747  33.850  1.00 24.68  ? 181 ARG B N   1 
ATOM   5621  C CA  . ARG B 1 181 ? -9.775  52.971  34.186  1.00 21.69  ? 181 ARG B CA  1 
ATOM   5622  C C   . ARG B 1 181 ? -9.113  52.858  35.552  1.00 31.66  ? 181 ARG B C   1 
ATOM   5623  O O   . ARG B 1 181 ? -8.002  53.361  35.757  1.00 30.58  ? 181 ARG B O   1 
ATOM   5624  C CB  . ARG B 1 181 ? -10.748 54.150  34.155  1.00 22.39  ? 181 ARG B CB  1 
ATOM   5625  C CG  . ARG B 1 181 ? -10.158 55.463  33.698  1.00 25.72  ? 181 ARG B CG  1 
ATOM   5626  C CD  . ARG B 1 181 ? -11.221 56.557  33.677  1.00 31.78  ? 181 ARG B CD  1 
ATOM   5627  N NE  . ARG B 1 181 ? -11.870 56.679  32.376  1.00 32.89  ? 181 ARG B NE  1 
ATOM   5628  C CZ  . ARG B 1 181 ? -13.078 56.209  32.088  1.00 27.95  ? 181 ARG B CZ  1 
ATOM   5629  N NH1 . ARG B 1 181 ? -13.805 55.570  32.991  1.00 23.40  ? 181 ARG B NH1 1 
ATOM   5630  N NH2 . ARG B 1 181 ? -13.565 56.380  30.862  1.00 27.85  ? 181 ARG B NH2 1 
ATOM   5631  N N   . GLU B 1 182 ? -9.778  52.188  36.494  1.00 34.87  ? 182 GLU B N   1 
ATOM   5632  C CA  . GLU B 1 182 ? -9.283  52.108  37.864  1.00 31.76  ? 182 GLU B CA  1 
ATOM   5633  C C   . GLU B 1 182 ? -8.007  51.279  37.950  1.00 31.88  ? 182 GLU B C   1 
ATOM   5634  O O   . GLU B 1 182 ? -6.961  51.771  38.391  1.00 37.60  ? 182 GLU B O   1 
ATOM   5635  C CB  . GLU B 1 182 ? -10.372 51.526  38.769  1.00 29.26  ? 182 GLU B CB  1 
ATOM   5636  C CG  . GLU B 1 182 ? -10.069 51.602  40.253  1.00 46.61  ? 182 GLU B CG  1 
ATOM   5637  C CD  . GLU B 1 182 ? -10.781 50.525  41.048  1.00 59.25  ? 182 GLU B CD  1 
ATOM   5638  O OE1 . GLU B 1 182 ? -12.022 50.599  41.167  1.00 68.76  ? 182 GLU B OE1 1 
ATOM   5639  O OE2 . GLU B 1 182 ? -10.101 49.609  41.558  1.00 55.66  ? 182 GLU B OE2 1 
ATOM   5640  N N   . ILE B 1 183 ? -8.073  50.013  37.528  1.00 25.81  ? 183 ILE B N   1 
ATOM   5641  C CA  . ILE B 1 183 ? -6.937  49.110  37.702  1.00 25.68  ? 183 ILE B CA  1 
ATOM   5642  C C   . ILE B 1 183 ? -5.724  49.587  36.913  1.00 31.15  ? 183 ILE B C   1 
ATOM   5643  O O   . ILE B 1 183 ? -4.582  49.273  37.269  1.00 26.16  ? 183 ILE B O   1 
ATOM   5644  C CB  . ILE B 1 183 ? -7.336  47.668  37.317  1.00 18.35  ? 183 ILE B CB  1 
ATOM   5645  C CG1 . ILE B 1 183 ? -7.778  47.594  35.854  1.00 22.95  ? 183 ILE B CG1 1 
ATOM   5646  C CG2 . ILE B 1 183 ? -8.430  47.154  38.240  1.00 24.90  ? 183 ILE B CG2 1 
ATOM   5647  C CD1 . ILE B 1 183 ? -6.818  46.834  34.967  1.00 16.25  ? 183 ILE B CD1 1 
ATOM   5648  N N   . LYS B 1 184 ? -5.943  50.343  35.834  1.00 34.02  ? 184 LYS B N   1 
ATOM   5649  C CA  . LYS B 1 184 ? -4.823  50.909  35.090  1.00 24.35  ? 184 LYS B CA  1 
ATOM   5650  C C   . LYS B 1 184 ? -4.093  51.966  35.911  1.00 26.18  ? 184 LYS B C   1 
ATOM   5651  O O   . LYS B 1 184 ? -2.865  51.921  36.049  1.00 32.38  ? 184 LYS B O   1 
ATOM   5652  C CB  . LYS B 1 184 ? -5.320  51.496  33.769  1.00 23.52  ? 184 LYS B CB  1 
ATOM   5653  C CG  . LYS B 1 184 ? -4.229  52.140  32.939  1.00 24.42  ? 184 LYS B CG  1 
ATOM   5654  C CD  . LYS B 1 184 ? -4.472  51.930  31.458  1.00 25.15  ? 184 LYS B CD  1 
ATOM   5655  C CE  . LYS B 1 184 ? -4.229  53.215  30.690  1.00 25.06  ? 184 LYS B CE  1 
ATOM   5656  N NZ  . LYS B 1 184 ? -3.151  54.026  31.318  1.00 34.67  ? 184 LYS B NZ  1 
ATOM   5657  N N   . GLU B 1 185 ? -4.835  52.930  36.466  1.00 32.01  ? 185 GLU B N   1 
ATOM   5658  C CA  . GLU B 1 185 ? -4.210  53.972  37.275  1.00 32.93  ? 185 GLU B CA  1 
ATOM   5659  C C   . GLU B 1 185 ? -3.683  53.420  38.590  1.00 31.33  ? 185 GLU B C   1 
ATOM   5660  O O   . GLU B 1 185 ? -2.662  53.897  39.099  1.00 30.25  ? 185 GLU B O   1 
ATOM   5661  C CB  . GLU B 1 185 ? -5.202  55.104  37.542  1.00 31.64  ? 185 GLU B CB  1 
ATOM   5662  C CG  . GLU B 1 185 ? -4.919  56.373  36.755  1.00 41.24  ? 185 GLU B CG  1 
ATOM   5663  C CD  . GLU B 1 185 ? -5.302  56.247  35.295  1.00 58.37  ? 185 GLU B CD  1 
ATOM   5664  O OE1 . GLU B 1 185 ? -6.335  55.607  35.003  1.00 63.61  ? 185 GLU B OE1 1 
ATOM   5665  O OE2 . GLU B 1 185 ? -4.572  56.786  34.435  1.00 64.64  ? 185 GLU B OE2 1 
ATOM   5666  N N   . GLU B 1 186 ? -4.362  52.419  39.152  1.00 33.09  ? 186 GLU B N   1 
ATOM   5667  C CA  . GLU B 1 186 ? -3.938  51.801  40.402  1.00 29.19  ? 186 GLU B CA  1 
ATOM   5668  C C   . GLU B 1 186 ? -2.686  50.950  40.246  1.00 29.62  ? 186 GLU B C   1 
ATOM   5669  O O   . GLU B 1 186 ? -2.146  50.488  41.256  1.00 33.74  ? 186 GLU B O   1 
ATOM   5670  C CB  . GLU B 1 186 ? -5.070  50.942  40.964  1.00 35.99  ? 186 GLU B CB  1 
ATOM   5671  C CG  . GLU B 1 186 ? -5.914  51.624  42.025  1.00 40.21  ? 186 GLU B CG  1 
ATOM   5672  C CD  . GLU B 1 186 ? -6.750  50.638  42.814  1.00 62.55  ? 186 GLU B CD  1 
ATOM   5673  O OE1 . GLU B 1 186 ? -7.924  50.952  43.107  1.00 50.37  ? 186 GLU B OE1 1 
ATOM   5674  O OE2 . GLU B 1 186 ? -6.236  49.546  43.137  1.00 70.69  ? 186 GLU B OE2 1 
ATOM   5675  N N   . GLY B 1 187 ? -2.226  50.716  39.019  1.00 31.46  ? 187 GLY B N   1 
ATOM   5676  C CA  . GLY B 1 187 ? -1.061  49.887  38.799  1.00 28.40  ? 187 GLY B CA  1 
ATOM   5677  C C   . GLY B 1 187 ? -1.304  48.404  38.935  1.00 27.29  ? 187 GLY B C   1 
ATOM   5678  O O   . GLY B 1 187 ? -0.336  47.635  38.985  1.00 25.64  ? 187 GLY B O   1 
ATOM   5679  N N   . LYS B 1 188 ? -2.563  47.976  39.003  1.00 29.27  ? 188 LYS B N   1 
ATOM   5680  C CA  . LYS B 1 188 ? -2.891  46.564  39.132  1.00 27.46  ? 188 LYS B CA  1 
ATOM   5681  C C   . LYS B 1 188 ? -2.909  45.833  37.799  1.00 22.70  ? 188 LYS B C   1 
ATOM   5682  O O   . LYS B 1 188 ? -2.826  44.599  37.785  1.00 25.31  ? 188 LYS B O   1 
ATOM   5683  C CB  . LYS B 1 188 ? -4.253  46.401  39.812  1.00 30.72  ? 188 LYS B CB  1 
ATOM   5684  C CG  . LYS B 1 188 ? -4.282  46.863  41.256  1.00 33.56  ? 188 LYS B CG  1 
ATOM   5685  C CD  . LYS B 1 188 ? -4.981  45.846  42.135  1.00 37.64  ? 188 LYS B CD  1 
ATOM   5686  C CE  . LYS B 1 188 ? -4.059  44.690  42.472  1.00 43.60  ? 188 LYS B CE  1 
ATOM   5687  N NZ  . LYS B 1 188 ? -4.773  43.623  43.222  1.00 38.35  ? 188 LYS B NZ  1 
ATOM   5688  N N   . GLY B 1 189 ? -3.016  46.552  36.690  1.00 21.49  ? 189 GLY B N   1 
ATOM   5689  C CA  . GLY B 1 189 ? -3.036  45.907  35.394  1.00 19.76  ? 189 GLY B CA  1 
ATOM   5690  C C   . GLY B 1 189 ? -2.853  46.906  34.277  1.00 18.87  ? 189 GLY B C   1 
ATOM   5691  O O   . GLY B 1 189 ? -3.123  48.102  34.432  1.00 19.45  ? 189 GLY B O   1 
ATOM   5692  N N   . SER B 1 190 ? -2.381  46.394  33.148  1.00 17.63  ? 190 SER B N   1 
ATOM   5693  C CA  . SER B 1 190 ? -2.224  47.174  31.933  1.00 16.76  ? 190 SER B CA  1 
ATOM   5694  C C   . SER B 1 190 ? -3.453  47.002  31.052  1.00 15.67  ? 190 SER B C   1 
ATOM   5695  O O   . SER B 1 190 ? -4.170  46.003  31.139  1.00 15.39  ? 190 SER B O   1 
ATOM   5696  C CB  . SER B 1 190 ? -0.965  46.746  31.172  1.00 16.27  ? 190 SER B CB  1 
ATOM   5697  O OG  . SER B 1 190 ? 0.210   47.199  31.819  1.00 17.60  ? 190 SER B OG  1 
ATOM   5698  N N   . VAL B 1 191 ? -3.699  47.999  30.208  1.00 15.30  ? 191 VAL B N   1 
ATOM   5699  C CA  . VAL B 1 191 ? -4.785  47.947  29.237  1.00 14.40  ? 191 VAL B CA  1 
ATOM   5700  C C   . VAL B 1 191 ? -4.217  48.277  27.864  1.00 16.30  ? 191 VAL B C   1 
ATOM   5701  O O   . VAL B 1 191 ? -3.641  49.354  27.666  1.00 22.99  ? 191 VAL B O   1 
ATOM   5702  C CB  . VAL B 1 191 ? -5.936  48.902  29.594  1.00 15.01  ? 191 VAL B CB  1 
ATOM   5703  C CG1 . VAL B 1 191 ? -7.074  48.736  28.603  1.00 14.20  ? 191 VAL B CG1 1 
ATOM   5704  C CG2 . VAL B 1 191 ? -6.423  48.635  31.010  1.00 16.03  ? 191 VAL B CG2 1 
ATOM   5705  N N   . SER B 1 192 ? -4.376  47.354  26.925  1.00 12.67  ? 192 SER B N   1 
ATOM   5706  C CA  . SER B 1 192 ? -4.002  47.539  25.533  1.00 12.02  ? 192 SER B CA  1 
ATOM   5707  C C   . SER B 1 192 ? -5.261  47.654  24.685  1.00 14.73  ? 192 SER B C   1 
ATOM   5708  O O   . SER B 1 192 ? -6.376  47.399  25.145  1.00 17.60  ? 192 SER B O   1 
ATOM   5709  C CB  . SER B 1 192 ? -3.136  46.375  25.047  1.00 13.49  ? 192 SER B CB  1 
ATOM   5710  O OG  . SER B 1 192 ? -3.795  45.141  25.273  1.00 21.55  ? 192 SER B OG  1 
ATOM   5711  N N   . THR B 1 193 ? -5.075  48.042  23.430  1.00 14.03  ? 193 THR B N   1 
ATOM   5712  C CA  . THR B 1 193 ? -6.172  48.106  22.476  1.00 14.15  ? 193 THR B CA  1 
ATOM   5713  C C   . THR B 1 193 ? -5.736  47.432  21.179  1.00 14.00  ? 193 THR B C   1 
ATOM   5714  O O   . THR B 1 193 ? -4.622  46.914  21.068  1.00 14.94  ? 193 THR B O   1 
ATOM   5715  C CB  . THR B 1 193 ? -6.634  49.553  22.253  1.00 11.42  ? 193 THR B CB  1 
ATOM   5716  O OG1 . THR B 1 193 ? -7.867  49.556  21.522  1.00 13.83  ? 193 THR B OG1 1 
ATOM   5717  C CG2 . THR B 1 193 ? -5.587  50.351  21.505  1.00 11.65  ? 193 THR B CG2 1 
ATOM   5718  N N   . SER B 1 194 ? -6.636  47.406  20.208  1.00 17.15  ? 194 SER B N   1 
ATOM   5719  C CA  . SER B 1 194 ? -6.423  46.773  18.916  1.00 14.42  ? 194 SER B CA  1 
ATOM   5720  C C   . SER B 1 194 ? -6.864  47.736  17.830  1.00 12.67  ? 194 SER B C   1 
ATOM   5721  O O   . SER B 1 194 ? -7.607  48.684  18.102  1.00 15.52  ? 194 SER B O   1 
ATOM   5722  C CB  . SER B 1 194 ? -7.216  45.462  18.797  1.00 12.69  ? 194 SER B CB  1 
ATOM   5723  O OG  . SER B 1 194 ? -6.699  44.464  19.658  1.00 15.57  ? 194 SER B OG  1 
ATOM   5724  N N   . PRO B 1 195 ? -6.411  47.537  16.591  1.00 15.52  ? 195 PRO B N   1 
ATOM   5725  C CA  . PRO B 1 195 ? -6.992  48.283  15.469  1.00 15.47  ? 195 PRO B CA  1 
ATOM   5726  C C   . PRO B 1 195 ? -8.512  48.197  15.501  1.00 19.59  ? 195 PRO B C   1 
ATOM   5727  O O   . PRO B 1 195 ? -9.085  47.160  15.843  1.00 26.20  ? 195 PRO B O   1 
ATOM   5728  C CB  . PRO B 1 195 ? -6.398  47.585  14.243  1.00 18.81  ? 195 PRO B CB  1 
ATOM   5729  C CG  . PRO B 1 195 ? -5.062  47.113  14.722  1.00 13.81  ? 195 PRO B CG  1 
ATOM   5730  C CD  . PRO B 1 195 ? -5.237  46.744  16.177  1.00 13.40  ? 195 PRO B CD  1 
ATOM   5731  N N   . TYR B 1 196 ? -9.155  49.305  15.123  1.00 19.47  ? 196 TYR B N   1 
ATOM   5732  C CA  . TYR B 1 196 ? -10.494 49.636  15.611  1.00 12.36  ? 196 TYR B CA  1 
ATOM   5733  C C   . TYR B 1 196 ? -11.479 48.477  15.487  1.00 14.39  ? 196 TYR B C   1 
ATOM   5734  O O   . TYR B 1 196 ? -12.033 48.007  16.487  1.00 19.61  ? 196 TYR B O   1 
ATOM   5735  C CB  . TYR B 1 196 ? -11.026 50.870  14.882  1.00 14.15  ? 196 TYR B CB  1 
ATOM   5736  C CG  . TYR B 1 196 ? -12.027 51.651  15.704  1.00 14.04  ? 196 TYR B CG  1 
ATOM   5737  C CD1 . TYR B 1 196 ? -13.266 51.110  16.014  1.00 19.11  ? 196 TYR B CD1 1 
ATOM   5738  C CD2 . TYR B 1 196 ? -11.729 52.919  16.181  1.00 18.70  ? 196 TYR B CD2 1 
ATOM   5739  C CE1 . TYR B 1 196 ? -14.183 51.812  16.765  1.00 23.71  ? 196 TYR B CE1 1 
ATOM   5740  C CE2 . TYR B 1 196 ? -12.643 53.632  16.935  1.00 18.08  ? 196 TYR B CE2 1 
ATOM   5741  C CZ  . TYR B 1 196 ? -13.869 53.073  17.225  1.00 19.99  ? 196 TYR B CZ  1 
ATOM   5742  O OH  . TYR B 1 196 ? -14.789 53.771  17.975  1.00 26.26  ? 196 TYR B OH  1 
ATOM   5743  N N   . TYR B 1 197 ? -11.730 48.011  14.266  1.00 12.22  ? 197 TYR B N   1 
ATOM   5744  C CA  . TYR B 1 197 ? -12.766 47.015  14.038  1.00 12.06  ? 197 TYR B CA  1 
ATOM   5745  C C   . TYR B 1 197 ? -12.212 45.600  13.955  1.00 11.83  ? 197 TYR B C   1 
ATOM   5746  O O   . TYR B 1 197 ? -12.862 44.720  13.379  1.00 18.18  ? 197 TYR B O   1 
ATOM   5747  C CB  . TYR B 1 197 ? -13.558 47.373  12.783  1.00 12.41  ? 197 TYR B CB  1 
ATOM   5748  C CG  . TYR B 1 197 ? -14.384 48.614  12.988  1.00 13.57  ? 197 TYR B CG  1 
ATOM   5749  C CD1 . TYR B 1 197 ? -15.626 48.550  13.604  1.00 13.46  ? 197 TYR B CD1 1 
ATOM   5750  C CD2 . TYR B 1 197 ? -13.906 49.859  12.604  1.00 18.10  ? 197 TYR B CD2 1 
ATOM   5751  C CE1 . TYR B 1 197 ? -16.380 49.685  13.807  1.00 14.24  ? 197 TYR B CE1 1 
ATOM   5752  C CE2 . TYR B 1 197 ? -14.653 51.001  12.803  1.00 15.54  ? 197 TYR B CE2 1 
ATOM   5753  C CZ  . TYR B 1 197 ? -15.890 50.909  13.406  1.00 14.96  ? 197 TYR B CZ  1 
ATOM   5754  O OH  . TYR B 1 197 ? -16.640 52.044  13.608  1.00 19.32  ? 197 TYR B OH  1 
ATOM   5755  N N   . HIS B 1 198 ? -11.032 45.367  14.531  1.00 10.63  ? 198 HIS B N   1 
ATOM   5756  C CA  . HIS B 1 198 ? -10.427 44.045  14.639  1.00 12.92  ? 198 HIS B CA  1 
ATOM   5757  C C   . HIS B 1 198 ? -10.161 43.440  13.262  1.00 11.65  ? 198 HIS B C   1 
ATOM   5758  O O   . HIS B 1 198 ? -10.665 42.350  12.962  1.00 14.70  ? 198 HIS B O   1 
ATOM   5759  C CB  . HIS B 1 198 ? -11.338 43.143  15.473  1.00 14.91  ? 198 HIS B CB  1 
ATOM   5760  C CG  . HIS B 1 198 ? -10.656 41.955  16.070  1.00 13.49  ? 198 HIS B CG  1 
ATOM   5761  N ND1 . HIS B 1 198 ? -10.737 40.697  15.515  1.00 19.77  ? 198 HIS B ND1 1 
ATOM   5762  C CD2 . HIS B 1 198 ? -9.900  41.826  17.185  1.00 17.40  ? 198 HIS B CD2 1 
ATOM   5763  C CE1 . HIS B 1 198 ? -10.053 39.845  16.256  1.00 20.38  ? 198 HIS B CE1 1 
ATOM   5764  N NE2 . HIS B 1 198 ? -9.534  40.505  17.276  1.00 16.83  ? 198 HIS B NE2 1 
ATOM   5765  N N   . PRO B 1 199 ? -9.389  44.101  12.397  1.00 11.89  ? 199 PRO B N   1 
ATOM   5766  C CA  . PRO B 1 199 ? -9.147  43.566  11.057  1.00 15.45  ? 199 PRO B CA  1 
ATOM   5767  C C   . PRO B 1 199 ? -7.862  42.753  10.969  1.00 25.04  ? 199 PRO B C   1 
ATOM   5768  O O   . PRO B 1 199 ? -6.969  42.852  11.812  1.00 35.56  ? 199 PRO B O   1 
ATOM   5769  C CB  . PRO B 1 199 ? -9.048  44.838  10.208  1.00 11.86  ? 199 PRO B CB  1 
ATOM   5770  C CG  . PRO B 1 199 ? -8.411  45.829  11.131  1.00 11.34  ? 199 PRO B CG  1 
ATOM   5771  C CD  . PRO B 1 199 ? -8.727  45.406  12.561  1.00 18.05  ? 199 PRO B CD  1 
ATOM   5772  N N   . LEU B 1 200 ? -7.784  41.942  9.915   1.00 20.14  ? 200 LEU B N   1 
ATOM   5773  C CA  . LEU B 1 200 ? -6.536  41.261  9.603   1.00 14.10  ? 200 LEU B CA  1 
ATOM   5774  C C   . LEU B 1 200 ? -5.559  42.255  8.987   1.00 15.50  ? 200 LEU B C   1 
ATOM   5775  O O   . LEU B 1 200 ? -5.496  42.411  7.762   1.00 19.34  ? 200 LEU B O   1 
ATOM   5776  C CB  . LEU B 1 200 ? -6.782  40.068  8.677   1.00 15.42  ? 200 LEU B CB  1 
ATOM   5777  C CG  . LEU B 1 200 ? -7.385  38.833  9.348   1.00 14.14  ? 200 LEU B CG  1 
ATOM   5778  C CD1 . LEU B 1 200 ? -6.923  37.571  8.643   1.00 23.41  ? 200 LEU B CD1 1 
ATOM   5779  C CD2 . LEU B 1 200 ? -7.012  38.783  10.824  1.00 19.43  ? 200 LEU B CD2 1 
ATOM   5780  N N   . ILE B 1 201 ? -4.810  42.945  9.852   1.00 12.71  ? 201 ILE B N   1 
ATOM   5781  C CA  . ILE B 1 201 ? -3.936  44.023  9.384   1.00 13.81  ? 201 ILE B CA  1 
ATOM   5782  C C   . ILE B 1 201 ? -2.918  43.541  8.359   1.00 19.89  ? 201 ILE B C   1 
ATOM   5783  O O   . ILE B 1 201 ? -2.687  44.255  7.371   1.00 15.71  ? 201 ILE B O   1 
ATOM   5784  C CB  . ILE B 1 201 ? -3.303  44.744  10.582  1.00 18.31  ? 201 ILE B CB  1 
ATOM   5785  C CG1 . ILE B 1 201 ? -4.332  45.667  11.242  1.00 13.46  ? 201 ILE B CG1 1 
ATOM   5786  C CG2 . ILE B 1 201 ? -2.079  45.531  10.168  1.00 15.56  ? 201 ILE B CG2 1 
ATOM   5787  C CD1 . ILE B 1 201 ? -4.648  46.902  10.429  1.00 14.68  ? 201 ILE B CD1 1 
ATOM   5788  N N   . PRO B 1 202 ? -2.272  42.373  8.509   1.00 18.39  ? 202 PRO B N   1 
ATOM   5789  C CA  . PRO B 1 202 ? -1.355  41.923  7.447   1.00 14.87  ? 202 PRO B CA  1 
ATOM   5790  C C   . PRO B 1 202 ? -1.998  41.838  6.072   1.00 16.68  ? 202 PRO B C   1 
ATOM   5791  O O   . PRO B 1 202 ? -1.356  42.193  5.075   1.00 22.24  ? 202 PRO B O   1 
ATOM   5792  C CB  . PRO B 1 202 ? -0.905  40.546  7.949   1.00 13.75  ? 202 PRO B CB  1 
ATOM   5793  C CG  . PRO B 1 202 ? -0.929  40.691  9.419   1.00 12.78  ? 202 PRO B CG  1 
ATOM   5794  C CD  . PRO B 1 202 ? -2.168  41.502  9.695   1.00 13.29  ? 202 PRO B CD  1 
ATOM   5795  N N   . ILE B 1 203 ? -3.249  41.383  5.985   1.00 15.09  ? 203 ILE B N   1 
ATOM   5796  C CA  . ILE B 1 203 ? -3.885  41.247  4.677   1.00 21.96  ? 203 ILE B CA  1 
ATOM   5797  C C   . ILE B 1 203 ? -4.205  42.616  4.085   1.00 20.51  ? 203 ILE B C   1 
ATOM   5798  O O   . ILE B 1 203 ? -3.969  42.859  2.895   1.00 23.04  ? 203 ILE B O   1 
ATOM   5799  C CB  . ILE B 1 203 ? -5.139  40.359  4.772   1.00 20.52  ? 203 ILE B CB  1 
ATOM   5800  C CG1 . ILE B 1 203 ? -4.734  38.892  4.918   1.00 20.02  ? 203 ILE B CG1 1 
ATOM   5801  C CG2 . ILE B 1 203 ? -5.998  40.529  3.533   1.00 16.91  ? 203 ILE B CG2 1 
ATOM   5802  C CD1 . ILE B 1 203 ? -5.863  37.913  4.664   1.00 19.98  ? 203 ILE B CD1 1 
ATOM   5803  N N   . LEU B 1 204 ? -4.743  43.530  4.900   1.00 19.22  ? 204 LEU B N   1 
ATOM   5804  C CA  . LEU B 1 204 ? -5.052  44.869  4.403   1.00 16.14  ? 204 LEU B CA  1 
ATOM   5805  C C   . LEU B 1 204 ? -3.808  45.549  3.849   1.00 20.71  ? 204 LEU B C   1 
ATOM   5806  O O   . LEU B 1 204 ? -3.852  46.161  2.774   1.00 17.37  ? 204 LEU B O   1 
ATOM   5807  C CB  . LEU B 1 204 ? -5.665  45.729  5.511   1.00 14.74  ? 204 LEU B CB  1 
ATOM   5808  C CG  . LEU B 1 204 ? -7.024  45.371  6.115   1.00 16.26  ? 204 LEU B CG  1 
ATOM   5809  C CD1 . LEU B 1 204 ? -7.276  46.228  7.344   1.00 13.48  ? 204 LEU B CD1 1 
ATOM   5810  C CD2 . LEU B 1 204 ? -8.147  45.548  5.106   1.00 17.39  ? 204 LEU B CD2 1 
ATOM   5811  N N   . LEU B 1 205 ? -2.688  45.454  4.569   1.00 25.63  ? 205 LEU B N   1 
ATOM   5812  C CA  . LEU B 1 205 ? -1.452  46.079  4.111   1.00 17.48  ? 205 LEU B CA  1 
ATOM   5813  C C   . LEU B 1 205 ? -0.956  45.437  2.821   1.00 24.83  ? 205 LEU B C   1 
ATOM   5814  O O   . LEU B 1 205 ? -0.618  46.133  1.856   1.00 30.79  ? 205 LEU B O   1 
ATOM   5815  C CB  . LEU B 1 205 ? -0.384  45.988  5.202   1.00 15.76  ? 205 LEU B CB  1 
ATOM   5816  C CG  . LEU B 1 205 ? -0.491  46.980  6.360   1.00 15.00  ? 205 LEU B CG  1 
ATOM   5817  C CD1 . LEU B 1 205 ? 0.160   46.400  7.596   1.00 14.19  ? 205 LEU B CD1 1 
ATOM   5818  C CD2 . LEU B 1 205 ? 0.148   48.306  5.996   1.00 24.20  ? 205 LEU B CD2 1 
ATOM   5819  N N   . ASN B 1 206 ? -0.898  44.105  2.790   1.00 28.55  ? 206 ASN B N   1 
ATOM   5820  C CA  . ASN B 1 206 ? -0.394  43.377  1.631   1.00 25.57  ? 206 ASN B CA  1 
ATOM   5821  C C   . ASN B 1 206 ? -0.993  41.975  1.589   1.00 22.83  ? 206 ASN B C   1 
ATOM   5822  O O   . ASN B 1 206 ? -0.629  41.123  2.410   1.00 35.97  ? 206 ASN B O   1 
ATOM   5823  C CB  . ASN B 1 206 ? 1.134   43.307  1.667   1.00 19.89  ? 206 ASN B CB  1 
ATOM   5824  C CG  . ASN B 1 206 ? 1.735   42.874  0.344   1.00 30.79  ? 206 ASN B CG  1 
ATOM   5825  O OD1 . ASN B 1 206 ? 1.066   42.265  -0.490  1.00 26.55  ? 206 ASN B OD1 1 
ATOM   5826  N ND2 . ASN B 1 206 ? 3.010   43.187  0.147   1.00 49.55  ? 206 ASN B ND2 1 
ATOM   5827  N N   . PRO B 1 207 ? -1.905  41.693  0.653   1.00 19.99  ? 207 PRO B N   1 
ATOM   5828  C CA  . PRO B 1 207 ? -2.486  40.343  0.569   1.00 20.31  ? 207 PRO B CA  1 
ATOM   5829  C C   . PRO B 1 207 ? -1.488  39.256  0.194   1.00 24.26  ? 207 PRO B C   1 
ATOM   5830  O O   . PRO B 1 207 ? -1.818  38.072  0.331   1.00 21.54  ? 207 PRO B O   1 
ATOM   5831  C CB  . PRO B 1 207 ? -3.568  40.494  -0.510  1.00 26.93  ? 207 PRO B CB  1 
ATOM   5832  C CG  . PRO B 1 207 ? -3.869  41.956  -0.544  1.00 25.40  ? 207 PRO B CG  1 
ATOM   5833  C CD  . PRO B 1 207 ? -2.562  42.631  -0.271  1.00 25.32  ? 207 PRO B CD  1 
ATOM   5834  N N   . ASN B 1 208 ? -0.289  39.608  -0.275  1.00 30.98  ? 208 ASN B N   1 
ATOM   5835  C CA  . ASN B 1 208 ? 0.726   38.603  -0.571  1.00 27.04  ? 208 ASN B CA  1 
ATOM   5836  C C   . ASN B 1 208 ? 1.308   37.966  0.686   1.00 21.97  ? 208 ASN B C   1 
ATOM   5837  O O   . ASN B 1 208 ? 2.096   37.021  0.570   1.00 22.85  ? 208 ASN B O   1 
ATOM   5838  C CB  . ASN B 1 208 ? 1.850   39.216  -1.410  1.00 25.35  ? 208 ASN B CB  1 
ATOM   5839  C CG  . ASN B 1 208 ? 1.480   39.339  -2.877  1.00 27.37  ? 208 ASN B CG  1 
ATOM   5840  O OD1 . ASN B 1 208 ? 0.840   38.453  -3.443  1.00 29.70  ? 208 ASN B OD1 1 
ATOM   5841  N ND2 . ASN B 1 208 ? 1.894   40.434  -3.504  1.00 30.92  ? 208 ASN B ND2 1 
ATOM   5842  N N   . CYS B 1 209 ? 0.953   38.470  1.871   1.00 21.88  ? 209 CYS B N   1 
ATOM   5843  C CA  . CYS B 1 209 ? 1.451   37.895  3.117   1.00 19.41  ? 209 CYS B CA  1 
ATOM   5844  C C   . CYS B 1 209 ? 0.957   36.469  3.325   1.00 26.53  ? 209 CYS B C   1 
ATOM   5845  O O   . CYS B 1 209 ? 1.651   35.660  3.953   1.00 32.00  ? 209 CYS B O   1 
ATOM   5846  C CB  . CYS B 1 209 ? 1.030   38.771  4.296   1.00 19.19  ? 209 CYS B CB  1 
ATOM   5847  S SG  . CYS B 1 209 ? -0.756  38.757  4.613   1.00 34.10  ? 209 CYS B SG  1 
ATOM   5848  N N   . VAL B 1 210 ? -0.233  36.140  2.812   1.00 25.86  ? 210 VAL B N   1 
ATOM   5849  C CA  . VAL B 1 210 ? -0.821  34.832  3.080   1.00 23.46  ? 210 VAL B CA  1 
ATOM   5850  C C   . VAL B 1 210 ? -0.023  33.703  2.443   1.00 27.77  ? 210 VAL B C   1 
ATOM   5851  O O   . VAL B 1 210 ? -0.208  32.537  2.811   1.00 34.40  ? 210 VAL B O   1 
ATOM   5852  C CB  . VAL B 1 210 ? -2.283  34.786  2.585   1.00 22.93  ? 210 VAL B CB  1 
ATOM   5853  C CG1 . VAL B 1 210 ? -3.141  35.763  3.370   1.00 28.66  ? 210 VAL B CG1 1 
ATOM   5854  C CG2 . VAL B 1 210 ? -2.347  35.067  1.098   1.00 26.24  ? 210 VAL B CG2 1 
ATOM   5855  N N   . TYR B 1 211 ? 0.861   34.014  1.497   1.00 23.26  ? 211 TYR B N   1 
ATOM   5856  C CA  . TYR B 1 211 ? 1.611   32.983  0.794   1.00 25.12  ? 211 TYR B CA  1 
ATOM   5857  C C   . TYR B 1 211 ? 2.832   32.500  1.559   1.00 25.10  ? 211 TYR B C   1 
ATOM   5858  O O   . TYR B 1 211 ? 3.442   31.503  1.153   1.00 31.24  ? 211 TYR B O   1 
ATOM   5859  C CB  . TYR B 1 211 ? 2.047   33.499  -0.577  1.00 26.53  ? 211 TYR B CB  1 
ATOM   5860  C CG  . TYR B 1 211 ? 0.911   33.614  -1.558  1.00 27.34  ? 211 TYR B CG  1 
ATOM   5861  C CD1 . TYR B 1 211 ? 0.249   32.485  -2.006  1.00 28.70  ? 211 TYR B CD1 1 
ATOM   5862  C CD2 . TYR B 1 211 ? 0.499   34.850  -2.033  1.00 26.94  ? 211 TYR B CD2 1 
ATOM   5863  C CE1 . TYR B 1 211 ? -0.787  32.576  -2.902  1.00 29.63  ? 211 TYR B CE1 1 
ATOM   5864  C CE2 . TYR B 1 211 ? -0.542  34.953  -2.930  1.00 27.85  ? 211 TYR B CE2 1 
ATOM   5865  C CZ  . TYR B 1 211 ? -1.181  33.812  -3.362  1.00 29.19  ? 211 TYR B CZ  1 
ATOM   5866  O OH  . TYR B 1 211 ? -2.217  33.899  -4.258  1.00 42.75  ? 211 TYR B OH  1 
ATOM   5867  N N   . GLU B 1 212 ? 3.201   33.166  2.652   1.00 23.51  ? 212 GLU B N   1 
ATOM   5868  C CA  . GLU B 1 212 ? 4.424   32.806  3.354   1.00 27.79  ? 212 GLU B CA  1 
ATOM   5869  C C   . GLU B 1 212 ? 4.291   31.493  4.116   1.00 25.50  ? 212 GLU B C   1 
ATOM   5870  O O   . GLU B 1 212 ? 5.310   30.888  4.464   1.00 30.95  ? 212 GLU B O   1 
ATOM   5871  C CB  . GLU B 1 212 ? 4.831   33.941  4.295   1.00 31.17  ? 212 GLU B CB  1 
ATOM   5872  C CG  . GLU B 1 212 ? 5.490   35.102  3.563   1.00 39.87  ? 212 GLU B CG  1 
ATOM   5873  C CD  . GLU B 1 212 ? 5.293   36.434  4.258   1.00 39.76  ? 212 GLU B CD  1 
ATOM   5874  O OE1 . GLU B 1 212 ? 5.211   36.450  5.504   1.00 42.44  ? 212 GLU B OE1 1 
ATOM   5875  O OE2 . GLU B 1 212 ? 5.214   37.465  3.556   1.00 35.47  ? 212 GLU B OE2 1 
ATOM   5876  N N   . THR B 1 213 ? 3.065   31.035  4.369   1.00 24.59  ? 213 THR B N   1 
ATOM   5877  C CA  . THR B 1 213 ? 2.834   29.748  5.007   1.00 26.48  ? 213 THR B CA  1 
ATOM   5878  C C   . THR B 1 213 ? 1.916   28.828  4.215   1.00 31.73  ? 213 THR B C   1 
ATOM   5879  O O   . THR B 1 213 ? 1.814   27.646  4.563   1.00 32.03  ? 213 THR B O   1 
ATOM   5880  C CB  . THR B 1 213 ? 2.245   29.939  6.413   1.00 29.90  ? 213 THR B CB  1 
ATOM   5881  O OG1 . THR B 1 213 ? 1.159   30.871  6.356   1.00 31.53  ? 213 THR B OG1 1 
ATOM   5882  C CG2 . THR B 1 213 ? 3.306   30.460  7.371   1.00 29.67  ? 213 THR B CG2 1 
ATOM   5883  N N   . THR B 1 214 ? 1.238   29.327  3.182   1.00 31.17  ? 214 THR B N   1 
ATOM   5884  C CA  . THR B 1 214 ? 0.353   28.519  2.340   1.00 29.10  ? 214 THR B CA  1 
ATOM   5885  C C   . THR B 1 214 ? 0.586   28.915  0.888   1.00 35.94  ? 214 THR B C   1 
ATOM   5886  O O   . THR B 1 214 ? -0.225  29.624  0.280   1.00 39.44  ? 214 THR B O   1 
ATOM   5887  C CB  . THR B 1 214 ? -1.112  28.712  2.739   1.00 33.49  ? 214 THR B CB  1 
ATOM   5888  O OG1 . THR B 1 214 ? -1.375  30.110  2.920   1.00 28.57  ? 214 THR B OG1 1 
ATOM   5889  C CG2 . THR B 1 214 ? -1.410  27.978  4.037   1.00 29.52  ? 214 THR B CG2 1 
ATOM   5890  N N   . PRO B 1 215 ? 1.701   28.471  0.297   1.00 30.22  ? 215 PRO B N   1 
ATOM   5891  C CA  . PRO B 1 215 ? 2.122   29.036  -1.000  1.00 31.37  ? 215 PRO B CA  1 
ATOM   5892  C C   . PRO B 1 215 ? 1.124   28.866  -2.138  1.00 38.19  ? 215 PRO B C   1 
ATOM   5893  O O   . PRO B 1 215 ? 0.981   29.784  -2.954  1.00 37.76  ? 215 PRO B O   1 
ATOM   5894  C CB  . PRO B 1 215 ? 3.434   28.290  -1.279  1.00 34.76  ? 215 PRO B CB  1 
ATOM   5895  C CG  . PRO B 1 215 ? 3.939   27.918  0.084   1.00 32.01  ? 215 PRO B CG  1 
ATOM   5896  C CD  . PRO B 1 215 ? 2.698   27.528  0.829   1.00 31.06  ? 215 PRO B CD  1 
ATOM   5897  N N   . ASN B 1 216 ? 0.456   27.721  -2.252  1.00 43.21  ? 216 ASN B N   1 
ATOM   5898  C CA  . ASN B 1 216 ? -0.512  27.516  -3.333  1.00 47.44  ? 216 ASN B CA  1 
ATOM   5899  C C   . ASN B 1 216 ? -1.941  27.686  -2.815  1.00 41.10  ? 216 ASN B C   1 
ATOM   5900  O O   . ASN B 1 216 ? -2.721  26.739  -2.716  1.00 52.30  ? 216 ASN B O   1 
ATOM   5901  C CB  . ASN B 1 216 ? -0.304  26.153  -3.990  1.00 56.13  ? 216 ASN B CB  1 
ATOM   5902  C CG  . ASN B 1 216 ? -0.058  25.047  -2.985  1.00 63.31  ? 216 ASN B CG  1 
ATOM   5903  O OD1 . ASN B 1 216 ? -0.994  24.507  -2.396  1.00 71.04  ? 216 ASN B OD1 1 
ATOM   5904  N ND2 . ASN B 1 216 ? 1.207   24.690  -2.798  1.00 48.49  ? 216 ASN B ND2 1 
ATOM   5905  N N   . VAL B 1 217 ? -2.283  28.931  -2.494  1.00 32.51  ? 217 VAL B N   1 
ATOM   5906  C CA  . VAL B 1 217 ? -3.627  29.266  -2.037  1.00 35.11  ? 217 VAL B CA  1 
ATOM   5907  C C   . VAL B 1 217 ? -4.283  30.199  -3.048  1.00 41.81  ? 217 VAL B C   1 
ATOM   5908  O O   . VAL B 1 217 ? -3.619  30.914  -3.806  1.00 32.17  ? 217 VAL B O   1 
ATOM   5909  C CB  . VAL B 1 217 ? -3.627  29.890  -0.622  1.00 28.79  ? 217 VAL B CB  1 
ATOM   5910  C CG1 . VAL B 1 217 ? -3.375  31.388  -0.690  1.00 30.96  ? 217 VAL B CG1 1 
ATOM   5911  C CG2 . VAL B 1 217 ? -4.941  29.598  0.085   1.00 28.20  ? 217 VAL B CG2 1 
ATOM   5912  N N   . LYS B 1 218 ? -5.618  30.178  -3.056  1.00 45.69  ? 218 LYS B N   1 
ATOM   5913  C CA  . LYS B 1 218 ? -6.434  30.945  -3.999  1.00 36.89  ? 218 LYS B CA  1 
ATOM   5914  C C   . LYS B 1 218 ? -6.923  32.216  -3.312  1.00 39.93  ? 218 LYS B C   1 
ATOM   5915  O O   . LYS B 1 218 ? -7.911  32.189  -2.575  1.00 41.98  ? 218 LYS B O   1 
ATOM   5916  C CB  . LYS B 1 218 ? -7.622  30.117  -4.486  1.00 39.54  ? 218 LYS B CB  1 
ATOM   5917  C CG  . LYS B 1 218 ? -7.291  28.853  -5.265  1.00 47.88  ? 218 LYS B CG  1 
ATOM   5918  C CD  . LYS B 1 218 ? -6.441  29.149  -6.477  1.00 47.20  ? 218 LYS B CD  1 
ATOM   5919  C CE  . LYS B 1 218 ? -7.102  30.159  -7.407  1.00 64.09  ? 218 LYS B CE  1 
ATOM   5920  N NZ  . LYS B 1 218 ? -6.209  30.517  -8.545  1.00 67.69  ? 218 LYS B NZ  1 
ATOM   5921  N N   . ILE B 1 219 ? -6.250  33.334  -3.562  1.00 45.52  ? 219 ILE B N   1 
ATOM   5922  C CA  . ILE B 1 219 ? -6.761  34.618  -3.084  1.00 46.40  ? 219 ILE B CA  1 
ATOM   5923  C C   . ILE B 1 219 ? -7.264  35.410  -4.286  1.00 45.14  ? 219 ILE B C   1 
ATOM   5924  O O   . ILE B 1 219 ? -6.645  35.370  -5.360  1.00 40.05  ? 219 ILE B O   1 
ATOM   5925  C CB  . ILE B 1 219 ? -5.703  35.404  -2.289  1.00 38.15  ? 219 ILE B CB  1 
ATOM   5926  C CG1 . ILE B 1 219 ? -4.464  35.682  -3.141  1.00 37.60  ? 219 ILE B CG1 1 
ATOM   5927  C CG2 . ILE B 1 219 ? -5.331  34.654  -1.018  1.00 36.62  ? 219 ILE B CG2 1 
ATOM   5928  C CD1 . ILE B 1 219 ? -3.921  37.087  -2.999  1.00 37.24  ? 219 ILE B CD1 1 
ATOM   5929  N N   . PRO B 1 220 ? -8.380  36.122  -4.160  1.00 42.88  ? 220 PRO B N   1 
ATOM   5930  C CA  . PRO B 1 220 ? -8.901  36.892  -5.295  1.00 42.77  ? 220 PRO B CA  1 
ATOM   5931  C C   . PRO B 1 220 ? -7.998  38.069  -5.628  1.00 44.75  ? 220 PRO B C   1 
ATOM   5932  O O   . PRO B 1 220 ? -7.059  38.406  -4.905  1.00 44.43  ? 220 PRO B O   1 
ATOM   5933  C CB  . PRO B 1 220 ? -10.278 37.362  -4.813  1.00 39.29  ? 220 PRO B CB  1 
ATOM   5934  C CG  . PRO B 1 220 ? -10.211 37.300  -3.324  1.00 27.66  ? 220 PRO B CG  1 
ATOM   5935  C CD  . PRO B 1 220 ? -9.259  36.193  -2.980  1.00 36.91  ? 220 PRO B CD  1 
ATOM   5936  N N   . ASP B 1 221 ? -8.296  38.696  -6.763  1.00 58.38  ? 221 ASP B N   1 
ATOM   5937  C CA  . ASP B 1 221 ? -7.547  39.867  -7.200  1.00 52.60  ? 221 ASP B CA  1 
ATOM   5938  C C   . ASP B 1 221 ? -7.858  41.049  -6.288  1.00 41.40  ? 221 ASP B C   1 
ATOM   5939  O O   . ASP B 1 221 ? -9.016  41.462  -6.170  1.00 44.57  ? 221 ASP B O   1 
ATOM   5940  C CB  . ASP B 1 221 ? -7.896  40.202  -8.648  1.00 48.78  ? 221 ASP B CB  1 
ATOM   5941  C CG  . ASP B 1 221 ? -7.402  39.154  -9.626  1.00 55.68  ? 221 ASP B CG  1 
ATOM   5942  O OD1 . ASP B 1 221 ? -6.916  38.096  -9.177  1.00 72.80  ? 221 ASP B OD1 1 
ATOM   5943  O OD2 . ASP B 1 221 ? -7.510  39.388  -10.849 1.00 52.66  ? 221 ASP B OD2 1 
ATOM   5944  N N   . PHE B 1 222 ? -6.828  41.590  -5.643  1.00 35.76  ? 222 PHE B N   1 
ATOM   5945  C CA  . PHE B 1 222 ? -6.981  42.779  -4.807  1.00 35.73  ? 222 PHE B CA  1 
ATOM   5946  C C   . PHE B 1 222 ? -6.628  44.020  -5.625  1.00 45.55  ? 222 PHE B C   1 
ATOM   5947  O O   . PHE B 1 222 ? -5.592  44.662  -5.443  1.00 48.68  ? 222 PHE B O   1 
ATOM   5948  C CB  . PHE B 1 222 ? -6.120  42.662  -3.551  1.00 34.86  ? 222 PHE B CB  1 
ATOM   5949  C CG  . PHE B 1 222 ? -6.733  41.816  -2.467  1.00 33.33  ? 222 PHE B CG  1 
ATOM   5950  C CD1 . PHE B 1 222 ? -6.674  40.434  -2.530  1.00 33.74  ? 222 PHE B CD1 1 
ATOM   5951  C CD2 . PHE B 1 222 ? -7.367  42.406  -1.385  1.00 32.07  ? 222 PHE B CD2 1 
ATOM   5952  C CE1 . PHE B 1 222 ? -7.234  39.654  -1.533  1.00 32.19  ? 222 PHE B CE1 1 
ATOM   5953  C CE2 . PHE B 1 222 ? -7.929  41.632  -0.386  1.00 33.98  ? 222 PHE B CE2 1 
ATOM   5954  C CZ  . PHE B 1 222 ? -7.863  40.254  -0.460  1.00 34.54  ? 222 PHE B CZ  1 
ATOM   5955  N N   . ALA B 1 223 ? -7.533  44.352  -6.548  1.00 47.82  ? 223 ALA B N   1 
ATOM   5956  C CA  . ALA B 1 223 ? -7.338  45.482  -7.450  1.00 48.20  ? 223 ALA B CA  1 
ATOM   5957  C C   . ALA B 1 223 ? -7.500  46.831  -6.763  1.00 50.56  ? 223 ALA B C   1 
ATOM   5958  O O   . ALA B 1 223 ? -7.419  47.863  -7.440  1.00 59.84  ? 223 ALA B O   1 
ATOM   5959  C CB  . ALA B 1 223 ? -8.306  45.381  -8.630  1.00 50.72  ? 223 ALA B CB  1 
ATOM   5960  N N   . VAL B 1 224 ? -7.730  46.850  -5.450  1.00 40.93  ? 224 VAL B N   1 
ATOM   5961  C CA  . VAL B 1 224 ? -7.859  48.077  -4.681  1.00 35.55  ? 224 VAL B CA  1 
ATOM   5962  C C   . VAL B 1 224 ? -6.906  47.984  -3.496  1.00 25.27  ? 224 VAL B C   1 
ATOM   5963  O O   . VAL B 1 224 ? -6.488  46.897  -3.091  1.00 28.17  ? 224 VAL B O   1 
ATOM   5964  C CB  . VAL B 1 224 ? -9.312  48.313  -4.209  1.00 33.86  ? 224 VAL B CB  1 
ATOM   5965  C CG1 . VAL B 1 224 ? -9.609  47.509  -2.949  1.00 24.82  ? 224 VAL B CG1 1 
ATOM   5966  C CG2 . VAL B 1 224 ? -9.581  49.797  -3.995  1.00 39.66  ? 224 VAL B CG2 1 
ATOM   5967  N N   . SER B 1 225 ? -6.549  49.141  -2.947  1.00 27.38  ? 225 SER B N   1 
ATOM   5968  C CA  . SER B 1 225 ? -5.605  49.204  -1.840  1.00 24.31  ? 225 SER B CA  1 
ATOM   5969  C C   . SER B 1 225 ? -6.339  49.377  -0.518  1.00 21.77  ? 225 SER B C   1 
ATOM   5970  O O   . SER B 1 225 ? -7.328  50.112  -0.431  1.00 22.27  ? 225 SER B O   1 
ATOM   5971  C CB  . SER B 1 225 ? -4.605  50.346  -2.020  1.00 24.05  ? 225 SER B CB  1 
ATOM   5972  O OG  . SER B 1 225 ? -3.959  50.636  -0.791  1.00 22.69  ? 225 SER B OG  1 
ATOM   5973  N N   . PHE B 1 226 ? -5.840  48.692  0.510   1.00 21.13  ? 226 PHE B N   1 
ATOM   5974  C CA  . PHE B 1 226 ? -6.362  48.792  1.867   1.00 20.31  ? 226 PHE B CA  1 
ATOM   5975  C C   . PHE B 1 226 ? -5.317  49.336  2.833   1.00 20.51  ? 226 PHE B C   1 
ATOM   5976  O O   . PHE B 1 226 ? -5.443  49.151  4.048   1.00 21.68  ? 226 PHE B O   1 
ATOM   5977  C CB  . PHE B 1 226 ? -6.862  47.430  2.348   1.00 19.57  ? 226 PHE B CB  1 
ATOM   5978  C CG  . PHE B 1 226 ? -8.208  47.050  1.805   1.00 18.65  ? 226 PHE B CG  1 
ATOM   5979  C CD1 . PHE B 1 226 ? -9.346  47.739  2.190   1.00 24.24  ? 226 PHE B CD1 1 
ATOM   5980  C CD2 . PHE B 1 226 ? -8.334  46.001  0.908   1.00 19.48  ? 226 PHE B CD2 1 
ATOM   5981  C CE1 . PHE B 1 226 ? -10.587 47.387  1.693   1.00 26.96  ? 226 PHE B CE1 1 
ATOM   5982  C CE2 . PHE B 1 226 ? -9.571  45.646  0.405   1.00 21.10  ? 226 PHE B CE2 1 
ATOM   5983  C CZ  . PHE B 1 226 ? -10.699 46.339  0.796   1.00 26.35  ? 226 PHE B CZ  1 
ATOM   5984  N N   . ARG B 1 227 ? -4.275  49.991  2.315   1.00 18.91  ? 227 ARG B N   1 
ATOM   5985  C CA  . ARG B 1 227 ? -3.206  50.476  3.181   1.00 18.40  ? 227 ARG B CA  1 
ATOM   5986  C C   . ARG B 1 227 ? -3.677  51.635  4.051   1.00 23.39  ? 227 ARG B C   1 
ATOM   5987  O O   . ARG B 1 227 ? -3.362  51.688  5.246   1.00 28.89  ? 227 ARG B O   1 
ATOM   5988  C CB  . ARG B 1 227 ? -1.996  50.877  2.340   1.00 19.62  ? 227 ARG B CB  1 
ATOM   5989  C CG  . ARG B 1 227 ? -1.316  49.696  1.661   1.00 28.54  ? 227 ARG B CG  1 
ATOM   5990  C CD  . ARG B 1 227 ? -0.129  50.127  0.813   1.00 37.01  ? 227 ARG B CD  1 
ATOM   5991  N NE  . ARG B 1 227 ? 0.934   50.717  1.618   1.00 45.03  ? 227 ARG B NE  1 
ATOM   5992  C CZ  . ARG B 1 227 ? 1.914   50.027  2.185   1.00 53.35  ? 227 ARG B CZ  1 
ATOM   5993  N NH1 . ARG B 1 227 ? 1.994   48.712  2.062   1.00 51.36  ? 227 ARG B NH1 1 
ATOM   5994  N NH2 . ARG B 1 227 ? 2.836   50.672  2.895   1.00 58.75  ? 227 ARG B NH2 1 
ATOM   5995  N N   . GLU B 1 228 ? -4.434  52.571  3.475   1.00 26.35  ? 228 GLU B N   1 
ATOM   5996  C CA  . GLU B 1 228 ? -4.961  53.678  4.267   1.00 29.06  ? 228 GLU B CA  1 
ATOM   5997  C C   . GLU B 1 228 ? -5.963  53.189  5.306   1.00 36.53  ? 228 GLU B C   1 
ATOM   5998  O O   . GLU B 1 228 ? -6.021  53.726  6.419   1.00 44.57  ? 228 GLU B O   1 
ATOM   5999  C CB  . GLU B 1 228 ? -5.596  54.728  3.353   1.00 36.68  ? 228 GLU B CB  1 
ATOM   6000  C CG  . GLU B 1 228 ? -4.708  55.180  2.200   1.00 35.98  ? 228 GLU B CG  1 
ATOM   6001  C CD  . GLU B 1 228 ? -3.334  55.648  2.648   1.00 51.94  ? 228 GLU B CD  1 
ATOM   6002  O OE1 . GLU B 1 228 ? -3.220  56.209  3.759   1.00 65.19  ? 228 GLU B OE1 1 
ATOM   6003  O OE2 . GLU B 1 228 ? -2.365  55.457  1.883   1.00 57.54  ? 228 GLU B OE2 1 
ATOM   6004  N N   . ASP B 1 229 ? -6.767  52.179  4.960   1.00 25.10  ? 229 ASP B N   1 
ATOM   6005  C CA  . ASP B 1 229 ? -7.697  51.609  5.931   1.00 26.32  ? 229 ASP B CA  1 
ATOM   6006  C C   . ASP B 1 229 ? -6.954  50.950  7.088   1.00 24.42  ? 229 ASP B C   1 
ATOM   6007  O O   . ASP B 1 229 ? -7.347  51.095  8.252   1.00 21.36  ? 229 ASP B O   1 
ATOM   6008  C CB  . ASP B 1 229 ? -8.619  50.600  5.245   1.00 34.06  ? 229 ASP B CB  1 
ATOM   6009  C CG  . ASP B 1 229 ? -9.469  51.232  4.162   1.00 42.37  ? 229 ASP B CG  1 
ATOM   6010  O OD1 . ASP B 1 229 ? -8.913  51.964  3.316   1.00 66.43  ? 229 ASP B OD1 1 
ATOM   6011  O OD2 . ASP B 1 229 ? -10.697 50.998  4.161   1.00 35.27  ? 229 ASP B OD2 1 
ATOM   6012  N N   . ALA B 1 230 ? -5.874  50.225  6.787   1.00 22.36  ? 230 ALA B N   1 
ATOM   6013  C CA  . ALA B 1 230 ? -5.095  49.589  7.843   1.00 16.46  ? 230 ALA B CA  1 
ATOM   6014  C C   . ALA B 1 230 ? -4.451  50.622  8.756   1.00 16.26  ? 230 ALA B C   1 
ATOM   6015  O O   . ALA B 1 230 ? -4.267  50.366  9.951   1.00 13.27  ? 230 ALA B O   1 
ATOM   6016  C CB  . ALA B 1 230 ? -4.032  48.674  7.235   1.00 19.59  ? 230 ALA B CB  1 
ATOM   6017  N N   . SER B 1 231 ? -4.091  51.786  8.211   1.00 29.07  ? 231 SER B N   1 
ATOM   6018  C CA  . SER B 1 231 ? -3.557  52.866  9.035   1.00 20.45  ? 231 SER B CA  1 
ATOM   6019  C C   . SER B 1 231 ? -4.663  53.596  9.790   1.00 24.48  ? 231 SER B C   1 
ATOM   6020  O O   . SER B 1 231 ? -4.465  54.005  10.937  1.00 30.77  ? 231 SER B O   1 
ATOM   6021  C CB  . SER B 1 231 ? -2.762  53.844  8.170   1.00 16.96  ? 231 SER B CB  1 
ATOM   6022  O OG  . SER B 1 231 ? -2.021  54.745  8.974   1.00 34.58  ? 231 SER B OG  1 
ATOM   6023  N N   . LYS B 1 232 ? -5.830  53.776  9.166   1.00 21.60  ? 232 LYS B N   1 
ATOM   6024  C CA  . LYS B 1 232 ? -6.944  54.410  9.865   1.00 15.84  ? 232 LYS B CA  1 
ATOM   6025  C C   . LYS B 1 232 ? -7.375  53.584  11.069  1.00 24.30  ? 232 LYS B C   1 
ATOM   6026  O O   . LYS B 1 232 ? -7.712  54.137  12.124  1.00 20.74  ? 232 LYS B O   1 
ATOM   6027  C CB  . LYS B 1 232 ? -8.115  54.626  8.908   1.00 17.18  ? 232 LYS B CB  1 
ATOM   6028  C CG  . LYS B 1 232 ? -7.942  55.808  7.967   1.00 27.68  ? 232 LYS B CG  1 
ATOM   6029  C CD  . LYS B 1 232 ? -9.160  55.985  7.076   1.00 33.24  ? 232 LYS B CD  1 
ATOM   6030  C CE  . LYS B 1 232 ? -10.369 56.444  7.873   1.00 35.43  ? 232 LYS B CE  1 
ATOM   6031  N NZ  . LYS B 1 232 ? -10.296 57.893  8.210   1.00 36.16  ? 232 LYS B NZ  1 
ATOM   6032  N N   . HIS B 1 233 ? -7.359  52.255  10.933  1.00 24.78  ? 233 HIS B N   1 
ATOM   6033  C CA  . HIS B 1 233 ? -7.746  51.384  12.039  1.00 17.61  ? 233 HIS B CA  1 
ATOM   6034  C C   . HIS B 1 233 ? -6.855  51.600  13.256  1.00 17.47  ? 233 HIS B C   1 
ATOM   6035  O O   . HIS B 1 233 ? -7.349  51.690  14.386  1.00 20.85  ? 233 HIS B O   1 
ATOM   6036  C CB  . HIS B 1 233 ? -7.691  49.920  11.599  1.00 18.84  ? 233 HIS B CB  1 
ATOM   6037  C CG  . HIS B 1 233 ? -8.951  49.429  10.959  1.00 15.95  ? 233 HIS B CG  1 
ATOM   6038  N ND1 . HIS B 1 233 ? -10.130 49.279  11.657  1.00 16.00  ? 233 HIS B ND1 1 
ATOM   6039  C CD2 . HIS B 1 233 ? -9.211  49.032  9.691   1.00 13.04  ? 233 HIS B CD2 1 
ATOM   6040  C CE1 . HIS B 1 233 ? -11.066 48.822  10.843  1.00 18.31  ? 233 HIS B CE1 1 
ATOM   6041  N NE2 . HIS B 1 233 ? -10.534 48.663  9.644   1.00 16.37  ? 233 HIS B NE2 1 
ATOM   6042  N N   . VAL B 1 234 ? -5.540  51.696  13.048  1.00 18.59  ? 234 VAL B N   1 
ATOM   6043  C CA  . VAL B 1 234 ? -4.628  51.862  14.176  1.00 22.30  ? 234 VAL B CA  1 
ATOM   6044  C C   . VAL B 1 234 ? -4.581  53.301  14.671  1.00 22.37  ? 234 VAL B C   1 
ATOM   6045  O O   . VAL B 1 234 ? -4.110  53.547  15.788  1.00 26.58  ? 234 VAL B O   1 
ATOM   6046  C CB  . VAL B 1 234 ? -3.203  51.397  13.825  1.00 17.68  ? 234 VAL B CB  1 
ATOM   6047  C CG1 . VAL B 1 234 ? -3.188  49.910  13.514  1.00 21.23  ? 234 VAL B CG1 1 
ATOM   6048  C CG2 . VAL B 1 234 ? -2.643  52.195  12.665  1.00 24.97  ? 234 VAL B CG2 1 
ATOM   6049  N N   . GLU B 1 235 ? -5.058  54.261  13.880  1.00 24.35  ? 235 GLU B N   1 
ATOM   6050  C CA  . GLU B 1 235 ? -5.100  55.644  14.338  1.00 26.17  ? 235 GLU B CA  1 
ATOM   6051  C C   . GLU B 1 235 ? -6.401  55.971  15.059  1.00 21.47  ? 235 GLU B C   1 
ATOM   6052  O O   . GLU B 1 235 ? -6.380  56.648  16.093  1.00 31.39  ? 235 GLU B O   1 
ATOM   6053  C CB  . GLU B 1 235 ? -4.883  56.602  13.163  1.00 28.21  ? 235 GLU B CB  1 
ATOM   6054  C CG  . GLU B 1 235 ? -3.514  56.447  12.514  1.00 31.72  ? 235 GLU B CG  1 
ATOM   6055  C CD  . GLU B 1 235 ? -3.297  57.384  11.342  1.00 46.74  ? 235 GLU B CD  1 
ATOM   6056  O OE1 . GLU B 1 235 ? -4.274  57.676  10.621  1.00 57.59  ? 235 GLU B OE1 1 
ATOM   6057  O OE2 . GLU B 1 235 ? -2.143  57.816  11.133  1.00 54.46  ? 235 GLU B OE2 1 
ATOM   6058  N N   . LEU B 1 236 ? -7.538  55.499  14.540  1.00 15.16  ? 236 LEU B N   1 
ATOM   6059  C CA  . LEU B 1 236 ? -8.798  55.691  15.252  1.00 16.83  ? 236 LEU B CA  1 
ATOM   6060  C C   . LEU B 1 236 ? -8.834  54.889  16.545  1.00 15.25  ? 236 LEU B C   1 
ATOM   6061  O O   . LEU B 1 236 ? -9.490  55.298  17.510  1.00 18.43  ? 236 LEU B O   1 
ATOM   6062  C CB  . LEU B 1 236 ? -9.974  55.316  14.353  1.00 16.43  ? 236 LEU B CB  1 
ATOM   6063  C CG  . LEU B 1 236 ? -10.109 56.135  13.068  1.00 16.42  ? 236 LEU B CG  1 
ATOM   6064  C CD1 . LEU B 1 236 ? -11.182 55.552  12.163  1.00 18.10  ? 236 LEU B CD1 1 
ATOM   6065  C CD2 . LEU B 1 236 ? -10.403 57.591  13.394  1.00 17.80  ? 236 LEU B CD2 1 
ATOM   6066  N N   . ALA B 1 237 ? -8.144  53.747  16.581  1.00 13.49  ? 237 ALA B N   1 
ATOM   6067  C CA  . ALA B 1 237 ? -8.031  52.986  17.820  1.00 12.88  ? 237 ALA B CA  1 
ATOM   6068  C C   . ALA B 1 237 ? -7.269  53.768  18.879  1.00 20.62  ? 237 ALA B C   1 
ATOM   6069  O O   . ALA B 1 237 ? -7.648  53.763  20.056  1.00 22.34  ? 237 ALA B O   1 
ATOM   6070  C CB  . ALA B 1 237 ? -7.343  51.651  17.556  1.00 12.50  ? 237 ALA B CB  1 
ATOM   6071  N N   . LYS B 1 238 ? -6.187  54.439  18.478  1.00 24.69  ? 238 LYS B N   1 
ATOM   6072  C CA  . LYS B 1 238 ? -5.435  55.264  19.417  1.00 16.24  ? 238 LYS B CA  1 
ATOM   6073  C C   . LYS B 1 238 ? -6.300  56.390  19.967  1.00 19.06  ? 238 LYS B C   1 
ATOM   6074  O O   . LYS B 1 238 ? -6.252  56.693  21.165  1.00 30.98  ? 238 LYS B O   1 
ATOM   6075  C CB  . LYS B 1 238 ? -4.190  55.828  18.733  1.00 15.35  ? 238 LYS B CB  1 
ATOM   6076  C CG  . LYS B 1 238 ? -3.035  54.847  18.627  1.00 14.64  ? 238 LYS B CG  1 
ATOM   6077  C CD  . LYS B 1 238 ? -1.804  55.520  18.046  1.00 19.35  ? 238 LYS B CD  1 
ATOM   6078  C CE  . LYS B 1 238 ? -0.988  56.199  19.130  1.00 28.60  ? 238 LYS B CE  1 
ATOM   6079  N NZ  . LYS B 1 238 ? 0.227   56.856  18.577  1.00 30.68  ? 238 LYS B NZ  1 
ATOM   6080  N N   . GLU B 1 239 ? -7.097  57.022  19.103  1.00 21.22  ? 239 GLU B N   1 
ATOM   6081  C CA  . GLU B 1 239 ? -7.945  58.128  19.536  1.00 22.91  ? 239 GLU B CA  1 
ATOM   6082  C C   . GLU B 1 239 ? -8.991  57.664  20.541  1.00 24.84  ? 239 GLU B C   1 
ATOM   6083  O O   . GLU B 1 239 ? -9.169  58.282  21.598  1.00 27.25  ? 239 GLU B O   1 
ATOM   6084  C CB  . GLU B 1 239 ? -8.613  58.774  18.324  1.00 19.36  ? 239 GLU B CB  1 
ATOM   6085  C CG  . GLU B 1 239 ? -9.258  60.114  18.617  1.00 35.17  ? 239 GLU B CG  1 
ATOM   6086  C CD  . GLU B 1 239 ? -9.125  61.085  17.463  1.00 65.80  ? 239 GLU B CD  1 
ATOM   6087  O OE1 . GLU B 1 239 ? -9.037  62.305  17.715  1.00 70.01  ? 239 GLU B OE1 1 
ATOM   6088  O OE2 . GLU B 1 239 ? -9.110  60.627  16.300  1.00 74.89  ? 239 GLU B OE2 1 
ATOM   6089  N N   . LYS B 1 240 ? -9.695  56.574  20.228  1.00 21.56  ? 240 LYS B N   1 
ATOM   6090  C CA  . LYS B 1 240 ? -10.741 56.087  21.121  1.00 20.76  ? 240 LYS B CA  1 
ATOM   6091  C C   . LYS B 1 240 ? -10.166 55.708  22.478  1.00 23.61  ? 240 LYS B C   1 
ATOM   6092  O O   . LYS B 1 240 ? -10.775 55.979  23.520  1.00 28.55  ? 240 LYS B O   1 
ATOM   6093  C CB  . LYS B 1 240 ? -11.461 54.896  20.487  1.00 19.52  ? 240 LYS B CB  1 
ATOM   6094  C CG  . LYS B 1 240 ? -12.609 54.347  21.317  1.00 15.30  ? 240 LYS B CG  1 
ATOM   6095  C CD  . LYS B 1 240 ? -13.773 55.319  21.336  1.00 23.57  ? 240 LYS B CD  1 
ATOM   6096  C CE  . LYS B 1 240 ? -14.806 54.931  22.379  1.00 26.37  ? 240 LYS B CE  1 
ATOM   6097  N NZ  . LYS B 1 240 ? -16.110 55.617  22.151  1.00 33.97  ? 240 LYS B NZ  1 
ATOM   6098  N N   . TYR B 1 241 ? -8.984  55.089  22.482  1.00 19.96  ? 241 TYR B N   1 
ATOM   6099  C CA  . TYR B 1 241 ? -8.306  54.760  23.730  1.00 15.65  ? 241 TYR B CA  1 
ATOM   6100  C C   . TYR B 1 241 ? -7.963  56.021  24.517  1.00 23.33  ? 241 TYR B C   1 
ATOM   6101  O O   . TYR B 1 241 ? -8.000  56.021  25.753  1.00 20.36  ? 241 TYR B O   1 
ATOM   6102  C CB  . TYR B 1 241 ? -7.052  53.943  23.414  1.00 17.94  ? 241 TYR B CB  1 
ATOM   6103  C CG  . TYR B 1 241 ? -6.308  53.377  24.603  1.00 22.68  ? 241 TYR B CG  1 
ATOM   6104  C CD1 . TYR B 1 241 ? -5.271  54.085  25.196  1.00 21.30  ? 241 TYR B CD1 1 
ATOM   6105  C CD2 . TYR B 1 241 ? -6.615  52.119  25.105  1.00 15.56  ? 241 TYR B CD2 1 
ATOM   6106  C CE1 . TYR B 1 241 ? -4.575  53.567  26.269  1.00 17.64  ? 241 TYR B CE1 1 
ATOM   6107  C CE2 . TYR B 1 241 ? -5.924  51.592  26.179  1.00 17.41  ? 241 TYR B CE2 1 
ATOM   6108  C CZ  . TYR B 1 241 ? -4.905  52.322  26.755  1.00 15.77  ? 241 TYR B CZ  1 
ATOM   6109  O OH  . TYR B 1 241 ? -4.213  51.804  27.824  1.00 17.24  ? 241 TYR B OH  1 
ATOM   6110  N N   . PHE B 1 242 ? -7.624  57.107  23.814  1.00 21.20  ? 242 PHE B N   1 
ATOM   6111  C CA  . PHE B 1 242 ? -7.372  58.384  24.475  1.00 19.47  ? 242 PHE B CA  1 
ATOM   6112  C C   . PHE B 1 242 ? -8.644  58.959  25.088  1.00 20.52  ? 242 PHE B C   1 
ATOM   6113  O O   . PHE B 1 242 ? -8.582  59.646  26.113  1.00 22.24  ? 242 PHE B O   1 
ATOM   6114  C CB  . PHE B 1 242 ? -6.761  59.371  23.475  1.00 30.79  ? 242 PHE B CB  1 
ATOM   6115  C CG  . PHE B 1 242 ? -6.284  60.659  24.091  1.00 31.56  ? 242 PHE B CG  1 
ATOM   6116  C CD1 . PHE B 1 242 ? -7.143  61.737  24.235  1.00 24.81  ? 242 PHE B CD1 1 
ATOM   6117  C CD2 . PHE B 1 242 ? -4.969  60.797  24.505  1.00 29.42  ? 242 PHE B CD2 1 
ATOM   6118  C CE1 . PHE B 1 242 ? -6.705  62.923  24.795  1.00 25.61  ? 242 PHE B CE1 1 
ATOM   6119  C CE2 . PHE B 1 242 ? -4.524  61.980  25.065  1.00 24.97  ? 242 PHE B CE2 1 
ATOM   6120  C CZ  . PHE B 1 242 ? -5.394  63.045  25.210  1.00 26.09  ? 242 PHE B CZ  1 
ATOM   6121  N N   . GLU B 1 243 ? -9.799  58.694  24.474  1.00 23.75  ? 243 GLU B N   1 
ATOM   6122  C CA  . GLU B 1 243 ? -11.065 59.168  25.024  1.00 25.73  ? 243 GLU B CA  1 
ATOM   6123  C C   . GLU B 1 243 ? -11.407 58.465  26.333  1.00 25.67  ? 243 GLU B C   1 
ATOM   6124  O O   . GLU B 1 243 ? -12.076 59.048  27.194  1.00 22.47  ? 243 GLU B O   1 
ATOM   6125  C CB  . GLU B 1 243 ? -12.178 58.970  23.989  1.00 25.98  ? 243 GLU B CB  1 
ATOM   6126  C CG  . GLU B 1 243 ? -13.597 59.208  24.492  1.00 33.98  ? 243 GLU B CG  1 
ATOM   6127  C CD  . GLU B 1 243 ? -14.653 58.692  23.528  1.00 37.11  ? 243 GLU B CD  1 
ATOM   6128  O OE1 . GLU B 1 243 ? -14.320 58.470  22.344  1.00 39.35  ? 243 GLU B OE1 1 
ATOM   6129  O OE2 . GLU B 1 243 ? -15.814 58.506  23.952  1.00 25.93  ? 243 GLU B OE2 1 
ATOM   6130  N N   . ILE B 1 244 ? -10.943 57.227  26.507  1.00 29.42  ? 244 ILE B N   1 
ATOM   6131  C CA  . ILE B 1 244 ? -11.302 56.427  27.672  1.00 26.87  ? 244 ILE B CA  1 
ATOM   6132  C C   . ILE B 1 244 ? -10.201 56.371  28.729  1.00 27.87  ? 244 ILE B C   1 
ATOM   6133  O O   . ILE B 1 244 ? -10.493 56.052  29.892  1.00 27.01  ? 244 ILE B O   1 
ATOM   6134  C CB  . ILE B 1 244 ? -11.694 54.998  27.237  1.00 27.74  ? 244 ILE B CB  1 
ATOM   6135  C CG1 . ILE B 1 244 ? -12.545 55.055  25.968  1.00 19.04  ? 244 ILE B CG1 1 
ATOM   6136  C CG2 . ILE B 1 244 ? -12.437 54.267  28.348  1.00 30.53  ? 244 ILE B CG2 1 
ATOM   6137  C CD1 . ILE B 1 244 ? -14.019 55.300  26.230  1.00 27.20  ? 244 ILE B CD1 1 
ATOM   6138  N N   . PHE B 1 245 ? -8.954  56.687  28.374  1.00 29.06  ? 245 PHE B N   1 
ATOM   6139  C CA  . PHE B 1 245 ? -7.845  56.526  29.305  1.00 22.45  ? 245 PHE B CA  1 
ATOM   6140  C C   . PHE B 1 245 ? -6.969  57.768  29.420  1.00 23.02  ? 245 PHE B C   1 
ATOM   6141  O O   . PHE B 1 245 ? -5.921  57.711  30.077  1.00 27.54  ? 245 PHE B O   1 
ATOM   6142  C CB  . PHE B 1 245 ? -7.001  55.312  28.904  1.00 20.38  ? 245 PHE B CB  1 
ATOM   6143  C CG  . PHE B 1 245 ? -7.737  54.007  29.029  1.00 28.35  ? 245 PHE B CG  1 
ATOM   6144  C CD1 . PHE B 1 245 ? -7.896  53.402  30.264  1.00 27.47  ? 245 PHE B CD1 1 
ATOM   6145  C CD2 . PHE B 1 245 ? -8.293  53.400  27.916  1.00 23.77  ? 245 PHE B CD2 1 
ATOM   6146  C CE1 . PHE B 1 245 ? -8.580  52.206  30.386  1.00 19.33  ? 245 PHE B CE1 1 
ATOM   6147  C CE2 . PHE B 1 245 ? -8.979  52.204  28.031  1.00 17.85  ? 245 PHE B CE2 1 
ATOM   6148  C CZ  . PHE B 1 245 ? -9.123  51.607  29.268  1.00 18.70  ? 245 PHE B CZ  1 
ATOM   6149  N N   . GLY B 1 246 ? -7.359  58.880  28.800  1.00 19.25  ? 246 GLY B N   1 
ATOM   6150  C CA  . GLY B 1 246 ? -6.666  60.143  28.974  1.00 20.74  ? 246 GLY B CA  1 
ATOM   6151  C C   . GLY B 1 246 ? -5.241  60.150  28.464  1.00 23.67  ? 246 GLY B C   1 
ATOM   6152  O O   . GLY B 1 246 ? -4.481  61.082  28.743  1.00 23.11  ? 246 GLY B O   1 
ATOM   6153  N N   . GLU B 1 247 ? -4.870  59.118  27.711  1.00 30.69  ? 247 GLU B N   1 
ATOM   6154  C CA  . GLU B 1 247 ? -3.521  59.000  27.175  1.00 30.14  ? 247 GLU B CA  1 
ATOM   6155  C C   . GLU B 1 247 ? -3.544  57.983  26.043  1.00 23.66  ? 247 GLU B C   1 
ATOM   6156  O O   . GLU B 1 247 ? -4.513  57.242  25.862  1.00 19.65  ? 247 GLU B O   1 
ATOM   6157  C CB  . GLU B 1 247 ? -2.515  58.612  28.264  1.00 28.45  ? 247 GLU B CB  1 
ATOM   6158  C CG  . GLU B 1 247 ? -2.644  57.188  28.774  1.00 30.56  ? 247 GLU B CG  1 
ATOM   6159  C CD  . GLU B 1 247 ? -1.853  56.958  30.049  1.00 46.19  ? 247 GLU B CD  1 
ATOM   6160  O OE1 . GLU B 1 247 ? -1.479  57.952  30.707  1.00 54.14  ? 247 GLU B OE1 1 
ATOM   6161  O OE2 . GLU B 1 247 ? -1.603  55.784  30.394  1.00 53.21  ? 247 GLU B OE2 1 
ATOM   6162  N N   . HIS B 1 248 ? -2.465  57.970  25.272  1.00 27.86  ? 248 HIS B N   1 
ATOM   6163  C CA  . HIS B 1 248 ? -2.362  57.101  24.115  1.00 21.64  ? 248 HIS B CA  1 
ATOM   6164  C C   . HIS B 1 248 ? -1.912  55.701  24.525  1.00 17.94  ? 248 HIS B C   1 
ATOM   6165  O O   . HIS B 1 248 ? -1.303  55.517  25.582  1.00 22.45  ? 248 HIS B O   1 
ATOM   6166  C CB  . HIS B 1 248 ? -1.383  57.696  23.109  1.00 26.49  ? 248 HIS B CB  1 
ATOM   6167  C CG  . HIS B 1 248 ? -2.030  58.582  22.092  1.00 31.41  ? 248 HIS B CG  1 
ATOM   6168  N ND1 . HIS B 1 248 ? -1.330  59.159  21.054  1.00 36.86  ? 248 HIS B ND1 1 
ATOM   6169  C CD2 . HIS B 1 248 ? -3.314  58.990  21.953  1.00 31.58  ? 248 HIS B CD2 1 
ATOM   6170  C CE1 . HIS B 1 248 ? -2.154  59.885  20.321  1.00 38.62  ? 248 HIS B CE1 1 
ATOM   6171  N NE2 . HIS B 1 248 ? -3.364  59.799  20.845  1.00 38.34  ? 248 HIS B NE2 1 
ATOM   6172  N N   . PRO B 1 249 ? -2.210  54.692  23.710  1.00 21.64  ? 249 PRO B N   1 
ATOM   6173  C CA  . PRO B 1 249 ? -1.709  53.347  23.994  1.00 17.27  ? 249 PRO B CA  1 
ATOM   6174  C C   . PRO B 1 249 ? -0.299  53.148  23.466  1.00 12.71  ? 249 PRO B C   1 
ATOM   6175  O O   . PRO B 1 249 ? 0.088   53.689  22.429  1.00 16.67  ? 249 PRO B O   1 
ATOM   6176  C CB  . PRO B 1 249 ? -2.702  52.446  23.253  1.00 13.60  ? 249 PRO B CB  1 
ATOM   6177  C CG  . PRO B 1 249 ? -3.086  53.261  22.060  1.00 12.83  ? 249 PRO B CG  1 
ATOM   6178  C CD  . PRO B 1 249 ? -3.067  54.712  22.508  1.00 23.45  ? 249 PRO B CD  1 
ATOM   6179  N N   . VAL B 1 250 ? 0.473   52.353  24.200  1.00 10.08  ? 250 VAL B N   1 
ATOM   6180  C CA  . VAL B 1 250 ? 1.777   51.898  23.728  1.00 11.67  ? 250 VAL B CA  1 
ATOM   6181  C C   . VAL B 1 250 ? 1.832   50.393  23.539  1.00 15.89  ? 250 VAL B C   1 
ATOM   6182  O O   . VAL B 1 250 ? 2.836   49.885  23.013  1.00 15.56  ? 250 VAL B O   1 
ATOM   6183  C CB  . VAL B 1 250 ? 2.917   52.355  24.664  1.00 11.34  ? 250 VAL B CB  1 
ATOM   6184  C CG1 . VAL B 1 250 ? 3.296   53.794  24.358  1.00 13.84  ? 250 VAL B CG1 1 
ATOM   6185  C CG2 . VAL B 1 250 ? 2.511   52.198  26.117  1.00 12.67  ? 250 VAL B CG2 1 
ATOM   6186  N N   . TYR B 1 251 ? 0.795   49.666  23.940  1.00 15.00  ? 251 TYR B N   1 
ATOM   6187  C CA  . TYR B 1 251 ? 0.701   48.230  23.730  1.00 14.79  ? 251 TYR B CA  1 
ATOM   6188  C C   . TYR B 1 251 ? -0.541  47.937  22.905  1.00 13.91  ? 251 TYR B C   1 
ATOM   6189  O O   . TYR B 1 251 ? -1.622  48.460  23.194  1.00 14.89  ? 251 TYR B O   1 
ATOM   6190  C CB  . TYR B 1 251 ? 0.661   47.484  25.064  1.00 15.53  ? 251 TYR B CB  1 
ATOM   6191  C CG  . TYR B 1 251 ? 1.604   48.065  26.091  1.00 16.70  ? 251 TYR B CG  1 
ATOM   6192  C CD1 . TYR B 1 251 ? 2.968   48.145  25.840  1.00 25.41  ? 251 TYR B CD1 1 
ATOM   6193  C CD2 . TYR B 1 251 ? 1.130   48.546  27.304  1.00 16.73  ? 251 TYR B CD2 1 
ATOM   6194  C CE1 . TYR B 1 251 ? 3.836   48.682  26.772  1.00 27.21  ? 251 TYR B CE1 1 
ATOM   6195  C CE2 . TYR B 1 251 ? 1.990   49.084  28.241  1.00 20.41  ? 251 TYR B CE2 1 
ATOM   6196  C CZ  . TYR B 1 251 ? 3.341   49.150  27.971  1.00 19.68  ? 251 TYR B CZ  1 
ATOM   6197  O OH  . TYR B 1 251 ? 4.198   49.686  28.904  1.00 23.21  ? 251 TYR B OH  1 
ATOM   6198  N N   . MET B 1 252 ? -0.376  47.119  21.874  1.00 10.48  ? 252 MET B N   1 
ATOM   6199  C CA  . MET B 1 252 ? -1.467  46.704  21.011  1.00 11.45  ? 252 MET B CA  1 
ATOM   6200  C C   . MET B 1 252 ? -1.479  45.186  20.964  1.00 11.79  ? 252 MET B C   1 
ATOM   6201  O O   . MET B 1 252 ? -0.422  44.554  20.992  1.00 9.38   ? 252 MET B O   1 
ATOM   6202  C CB  . MET B 1 252 ? -1.312  47.279  19.590  1.00 11.18  ? 252 MET B CB  1 
ATOM   6203  C CG  . MET B 1 252 ? -2.616  47.596  18.864  1.00 20.69  ? 252 MET B CG  1 
ATOM   6204  S SD  . MET B 1 252 ? -2.538  49.082  17.837  1.00 29.32  ? 252 MET B SD  1 
ATOM   6205  C CE  . MET B 1 252 ? -3.249  50.321  18.917  1.00 8.84   ? 252 MET B CE  1 
ATOM   6206  N N   . TRP B 1 253 ? -2.671  44.601  20.916  1.00 19.34  ? 253 TRP B N   1 
ATOM   6207  C CA  . TRP B 1 253 ? -2.783  43.179  20.637  1.00 15.94  ? 253 TRP B CA  1 
ATOM   6208  C C   . TRP B 1 253 ? -3.270  43.028  19.208  1.00 16.20  ? 253 TRP B C   1 
ATOM   6209  O O   . TRP B 1 253 ? -4.421  43.387  18.918  1.00 16.84  ? 253 TRP B O   1 
ATOM   6210  C CB  . TRP B 1 253 ? -3.742  42.491  21.605  1.00 12.19  ? 253 TRP B CB  1 
ATOM   6211  C CG  . TRP B 1 253 ? -4.170  41.125  21.146  1.00 15.38  ? 253 TRP B CG  1 
ATOM   6212  C CD1 . TRP B 1 253 ? -5.403  40.761  20.688  1.00 12.71  ? 253 TRP B CD1 1 
ATOM   6213  C CD2 . TRP B 1 253 ? -3.361  39.941  21.096  1.00 11.93  ? 253 TRP B CD2 1 
ATOM   6214  N NE1 . TRP B 1 253 ? -5.413  39.428  20.360  1.00 15.97  ? 253 TRP B NE1 1 
ATOM   6215  C CE2 . TRP B 1 253 ? -4.172  38.901  20.601  1.00 10.73  ? 253 TRP B CE2 1 
ATOM   6216  C CE3 . TRP B 1 253 ? -2.029  39.659  21.424  1.00 15.21  ? 253 TRP B CE3 1 
ATOM   6217  C CZ2 . TRP B 1 253 ? -3.696  37.601  20.424  1.00 8.38   ? 253 TRP B CZ2 1 
ATOM   6218  C CZ3 . TRP B 1 253 ? -1.560  38.368  21.248  1.00 14.59  ? 253 TRP B CZ3 1 
ATOM   6219  C CH2 . TRP B 1 253 ? -2.391  37.356  20.755  1.00 9.02   ? 253 TRP B CH2 1 
ATOM   6220  N N   . PRO B 1 254 ? -2.451  42.529  18.289  1.00 11.20  ? 254 PRO B N   1 
ATOM   6221  C CA  . PRO B 1 254 ? -2.883  42.421  16.897  1.00 9.24   ? 254 PRO B CA  1 
ATOM   6222  C C   . PRO B 1 254 ? -4.028  41.435  16.778  1.00 12.25  ? 254 PRO B C   1 
ATOM   6223  O O   . PRO B 1 254 ? -3.976  40.345  17.368  1.00 15.56  ? 254 PRO B O   1 
ATOM   6224  C CB  . PRO B 1 254 ? -1.631  41.916  16.168  1.00 15.17  ? 254 PRO B CB  1 
ATOM   6225  C CG  . PRO B 1 254 ? -0.794  41.280  17.211  1.00 12.46  ? 254 PRO B CG  1 
ATOM   6226  C CD  . PRO B 1 254 ? -1.164  41.860  18.542  1.00 9.20   ? 254 PRO B CD  1 
ATOM   6227  N N   . PRO B 1 255 ? -5.084  41.790  16.045  1.00 11.42  ? 255 PRO B N   1 
ATOM   6228  C CA  . PRO B 1 255 ? -6.247  40.901  15.947  1.00 14.06  ? 255 PRO B CA  1 
ATOM   6229  C C   . PRO B 1 255 ? -5.846  39.530  15.425  1.00 15.88  ? 255 PRO B C   1 
ATOM   6230  O O   . PRO B 1 255 ? -5.117  39.412  14.438  1.00 16.88  ? 255 PRO B O   1 
ATOM   6231  C CB  . PRO B 1 255 ? -7.168  41.640  14.970  1.00 8.25   ? 255 PRO B CB  1 
ATOM   6232  C CG  . PRO B 1 255 ? -6.804  43.082  15.157  1.00 10.56  ? 255 PRO B CG  1 
ATOM   6233  C CD  . PRO B 1 255 ? -5.312  43.071  15.356  1.00 13.15  ? 255 PRO B CD  1 
ATOM   6234  N N   . GLU B 1 256 ? -6.316  38.490  16.116  1.00 13.95  ? 256 GLU B N   1 
ATOM   6235  C CA  . GLU B 1 256 ? -5.984  37.100  15.809  1.00 13.99  ? 256 GLU B CA  1 
ATOM   6236  C C   . GLU B 1 256 ? -4.488  36.826  15.903  1.00 14.65  ? 256 GLU B C   1 
ATOM   6237  O O   . GLU B 1 256 ? -3.987  35.887  15.274  1.00 17.62  ? 256 GLU B O   1 
ATOM   6238  C CB  . GLU B 1 256 ? -6.507  36.702  14.426  1.00 19.37  ? 256 GLU B CB  1 
ATOM   6239  C CG  . GLU B 1 256 ? -7.991  36.933  14.260  1.00 21.34  ? 256 GLU B CG  1 
ATOM   6240  C CD  . GLU B 1 256 ? -8.804  36.058  15.184  1.00 30.98  ? 256 GLU B CD  1 
ATOM   6241  O OE1 . GLU B 1 256 ? -8.401  34.896  15.398  1.00 27.48  ? 256 GLU B OE1 1 
ATOM   6242  O OE2 . GLU B 1 256 ? -9.839  36.529  15.700  1.00 34.78  ? 256 GLU B OE2 1 
ATOM   6243  N N   . ALA B 1 257 ? -3.767  37.636  16.682  1.00 13.67  ? 257 ALA B N   1 
ATOM   6244  C CA  . ALA B 1 257 ? -2.310  37.573  16.793  1.00 9.42   ? 257 ALA B CA  1 
ATOM   6245  C C   . ALA B 1 257 ? -1.627  37.677  15.435  1.00 12.87  ? 257 ALA B C   1 
ATOM   6246  O O   . ALA B 1 257 ? -0.487  37.228  15.273  1.00 12.93  ? 257 ALA B O   1 
ATOM   6247  C CB  . ALA B 1 257 ? -1.857  36.301  17.517  1.00 11.37  ? 257 ALA B CB  1 
ATOM   6248  N N   . SER B 1 258 ? -2.306  38.268  14.454  1.00 15.47  ? 258 SER B N   1 
ATOM   6249  C CA  . SER B 1 258 ? -1.779  38.309  13.097  1.00 13.57  ? 258 SER B CA  1 
ATOM   6250  C C   . SER B 1 258 ? -0.630  39.299  13.010  1.00 16.72  ? 258 SER B C   1 
ATOM   6251  O O   . SER B 1 258 ? -0.750  40.448  13.443  1.00 12.44  ? 258 SER B O   1 
ATOM   6252  C CB  . SER B 1 258 ? -2.878  38.687  12.104  1.00 17.88  ? 258 SER B CB  1 
ATOM   6253  O OG  . SER B 1 258 ? -3.758  39.648  12.664  1.00 28.21  ? 258 SER B OG  1 
ATOM   6254  N N   . VAL B 1 259 ? 0.489   38.846  12.451  1.00 21.86  ? 259 VAL B N   1 
ATOM   6255  C CA  . VAL B 1 259 ? 1.668   39.680  12.288  1.00 17.93  ? 259 VAL B CA  1 
ATOM   6256  C C   . VAL B 1 259 ? 2.225   39.482  10.887  1.00 16.75  ? 259 VAL B C   1 
ATOM   6257  O O   . VAL B 1 259 ? 1.935   38.498  10.202  1.00 15.27  ? 259 VAL B O   1 
ATOM   6258  C CB  . VAL B 1 259 ? 2.764   39.380  13.335  1.00 9.96   ? 259 VAL B CB  1 
ATOM   6259  C CG1 . VAL B 1 259 ? 2.218   39.518  14.749  1.00 14.59  ? 259 VAL B CG1 1 
ATOM   6260  C CG2 . VAL B 1 259 ? 3.346   37.996  13.110  1.00 9.57   ? 259 VAL B CG2 1 
ATOM   6261  N N   . SER B 1 260 ? 3.015   40.462  10.464  1.00 12.53  ? 260 SER B N   1 
ATOM   6262  C CA  . SER B 1 260 ? 3.893   40.356  9.309   1.00 16.86  ? 260 SER B CA  1 
ATOM   6263  C C   . SER B 1 260 ? 4.971   41.414  9.488   1.00 18.28  ? 260 SER B C   1 
ATOM   6264  O O   . SER B 1 260 ? 4.866   42.284  10.357  1.00 20.62  ? 260 SER B O   1 
ATOM   6265  C CB  . SER B 1 260 ? 3.133   40.530  7.989   1.00 21.22  ? 260 SER B CB  1 
ATOM   6266  O OG  . SER B 1 260 ? 2.533   41.810  7.901   1.00 28.30  ? 260 SER B OG  1 
ATOM   6267  N N   . ASN B 1 261 ? 6.028   41.315  8.679   1.00 13.84  ? 261 ASN B N   1 
ATOM   6268  C CA  . ASN B 1 261 ? 7.080   42.325  8.729   1.00 13.64  ? 261 ASN B CA  1 
ATOM   6269  C C   . ASN B 1 261 ? 6.497   43.719  8.542   1.00 13.51  ? 261 ASN B C   1 
ATOM   6270  O O   . ASN B 1 261 ? 6.732   44.622  9.352   1.00 16.64  ? 261 ASN B O   1 
ATOM   6271  C CB  . ASN B 1 261 ? 8.140   42.042  7.662   1.00 22.71  ? 261 ASN B CB  1 
ATOM   6272  C CG  . ASN B 1 261 ? 8.868   40.733  7.891   1.00 18.40  ? 261 ASN B CG  1 
ATOM   6273  O OD1 . ASN B 1 261 ? 8.886   40.203  9.001   1.00 24.65  ? 261 ASN B OD1 1 
ATOM   6274  N ND2 . ASN B 1 261 ? 9.481   40.207  6.837   1.00 21.86  ? 261 ASN B ND2 1 
ATOM   6275  N N   . GLU B 1 262 ? 5.701   43.899  7.488   1.00 13.56  ? 262 GLU B N   1 
ATOM   6276  C CA  . GLU B 1 262 ? 5.082   45.194  7.235   1.00 16.46  ? 262 GLU B CA  1 
ATOM   6277  C C   . GLU B 1 262 ? 4.113   45.572  8.349   1.00 20.31  ? 262 GLU B C   1 
ATOM   6278  O O   . GLU B 1 262 ? 4.041   46.742  8.744   1.00 23.33  ? 262 GLU B O   1 
ATOM   6279  C CB  . GLU B 1 262 ? 4.384   45.175  5.877   1.00 19.45  ? 262 GLU B CB  1 
ATOM   6280  C CG  . GLU B 1 262 ? 5.149   44.377  4.827   1.00 22.87  ? 262 GLU B CG  1 
ATOM   6281  C CD  . GLU B 1 262 ? 4.681   44.656  3.412   1.00 42.27  ? 262 GLU B CD  1 
ATOM   6282  O OE1 . GLU B 1 262 ? 4.458   45.839  3.081   1.00 50.05  ? 262 GLU B OE1 1 
ATOM   6283  O OE2 . GLU B 1 262 ? 4.545   43.694  2.625   1.00 43.23  ? 262 GLU B OE2 1 
ATOM   6284  N N   . ALA B 1 263 ? 3.363   44.597  8.872   1.00 20.82  ? 263 ALA B N   1 
ATOM   6285  C CA  . ALA B 1 263 ? 2.426   44.884  9.956   1.00 15.30  ? 263 ALA B CA  1 
ATOM   6286  C C   . ALA B 1 263 ? 3.149   45.446  11.174  1.00 15.46  ? 263 ALA B C   1 
ATOM   6287  O O   . ALA B 1 263 ? 2.727   46.456  11.748  1.00 15.59  ? 263 ALA B O   1 
ATOM   6288  C CB  . ALA B 1 263 ? 1.645   43.623  10.329  1.00 17.11  ? 263 ALA B CB  1 
ATOM   6289  N N   . LEU B 1 264 ? 4.256   44.812  11.571  1.00 15.41  ? 264 LEU B N   1 
ATOM   6290  C CA  . LEU B 1 264 ? 5.014   45.294  12.722  1.00 14.51  ? 264 LEU B CA  1 
ATOM   6291  C C   . LEU B 1 264 ? 5.605   46.673  12.467  1.00 16.54  ? 264 LEU B C   1 
ATOM   6292  O O   . LEU B 1 264 ? 5.767   47.462  13.406  1.00 12.76  ? 264 LEU B O   1 
ATOM   6293  C CB  . LEU B 1 264 ? 6.123   44.302  13.077  1.00 14.32  ? 264 LEU B CB  1 
ATOM   6294  C CG  . LEU B 1 264 ? 5.674   42.922  13.565  1.00 14.57  ? 264 LEU B CG  1 
ATOM   6295  C CD1 . LEU B 1 264 ? 6.874   42.046  13.891  1.00 20.72  ? 264 LEU B CD1 1 
ATOM   6296  C CD2 . LEU B 1 264 ? 4.766   43.060  14.767  1.00 10.05  ? 264 LEU B CD2 1 
ATOM   6297  N N   . GLU B 1 265 ? 5.936   46.981  11.211  1.00 18.81  ? 265 GLU B N   1 
ATOM   6298  C CA  . GLU B 1 265 ? 6.435   48.313  10.890  1.00 17.58  ? 265 GLU B CA  1 
ATOM   6299  C C   . GLU B 1 265 ? 5.347   49.369  11.040  1.00 18.39  ? 265 GLU B C   1 
ATOM   6300  O O   . GLU B 1 265 ? 5.637   50.499  11.450  1.00 13.78  ? 265 GLU B O   1 
ATOM   6301  C CB  . GLU B 1 265 ? 7.018   48.330  9.476   1.00 15.30  ? 265 GLU B CB  1 
ATOM   6302  C CG  . GLU B 1 265 ? 8.292   47.509  9.341   1.00 25.59  ? 265 GLU B CG  1 
ATOM   6303  C CD  . GLU B 1 265 ? 8.821   47.456  7.920   1.00 37.32  ? 265 GLU B CD  1 
ATOM   6304  O OE1 . GLU B 1 265 ? 8.789   48.495  7.229   1.00 53.54  ? 265 GLU B OE1 1 
ATOM   6305  O OE2 . GLU B 1 265 ? 9.274   46.371  7.496   1.00 26.53  ? 265 GLU B OE2 1 
ATOM   6306  N N   . LEU B 1 266 ? 4.099   49.023  10.715  1.00 20.56  ? 266 LEU B N   1 
ATOM   6307  C CA  . LEU B 1 266 ? 2.998   49.969  10.874  1.00 12.42  ? 266 LEU B CA  1 
ATOM   6308  C C   . LEU B 1 266 ? 2.750   50.298  12.342  1.00 13.27  ? 266 LEU B C   1 
ATOM   6309  O O   . LEU B 1 266 ? 2.508   51.460  12.688  1.00 15.70  ? 266 LEU B O   1 
ATOM   6310  C CB  . LEU B 1 266 ? 1.730   49.413  10.222  1.00 11.99  ? 266 LEU B CB  1 
ATOM   6311  C CG  . LEU B 1 266 ? 0.409   50.138  10.495  1.00 11.76  ? 266 LEU B CG  1 
ATOM   6312  C CD1 . LEU B 1 266 ? 0.460   51.573  10.000  1.00 12.58  ? 266 LEU B CD1 1 
ATOM   6313  C CD2 . LEU B 1 266 ? -0.751  49.395  9.850   1.00 11.47  ? 266 LEU B CD2 1 
ATOM   6314  N N   . TYR B 1 267 ? 2.803   49.292  13.219  1.00 11.24  ? 267 TYR B N   1 
ATOM   6315  C CA  . TYR B 1 267 ? 2.612   49.547  14.645  1.00 10.84  ? 267 TYR B CA  1 
ATOM   6316  C C   . TYR B 1 267 ? 3.713   50.444  15.197  1.00 13.41  ? 267 TYR B C   1 
ATOM   6317  O O   . TYR B 1 267 ? 3.448   51.336  16.012  1.00 13.36  ? 267 TYR B O   1 
ATOM   6318  C CB  . TYR B 1 267 ? 2.561   48.229  15.417  1.00 10.14  ? 267 TYR B CB  1 
ATOM   6319  C CG  . TYR B 1 267 ? 1.341   47.385  15.125  1.00 17.94  ? 267 TYR B CG  1 
ATOM   6320  C CD1 . TYR B 1 267 ? 0.077   47.785  15.543  1.00 13.75  ? 267 TYR B CD1 1 
ATOM   6321  C CD2 . TYR B 1 267 ? 1.453   46.184  14.437  1.00 20.55  ? 267 TYR B CD2 1 
ATOM   6322  C CE1 . TYR B 1 267 ? -1.040  47.012  15.278  1.00 15.12  ? 267 TYR B CE1 1 
ATOM   6323  C CE2 . TYR B 1 267 ? 0.344   45.407  14.168  1.00 21.81  ? 267 TYR B CE2 1 
ATOM   6324  C CZ  . TYR B 1 267 ? -0.900  45.823  14.590  1.00 21.20  ? 267 TYR B CZ  1 
ATOM   6325  O OH  . TYR B 1 267 ? -2.007  45.049  14.323  1.00 26.22  ? 267 TYR B OH  1 
ATOM   6326  N N   . TYR B 1 268 ? 4.956   50.217  14.768  1.00 12.14  ? 268 TYR B N   1 
ATOM   6327  C CA  . TYR B 1 268 ? 6.059   51.066  15.207  1.00 14.66  ? 268 TYR B CA  1 
ATOM   6328  C C   . TYR B 1 268 ? 5.861   52.509  14.757  1.00 23.17  ? 268 TYR B C   1 
ATOM   6329  O O   . TYR B 1 268 ? 6.070   53.446  15.538  1.00 21.94  ? 268 TYR B O   1 
ATOM   6330  C CB  . TYR B 1 268 ? 7.384   50.512  14.681  1.00 19.22  ? 268 TYR B CB  1 
ATOM   6331  C CG  . TYR B 1 268 ? 8.545   51.481  14.769  1.00 14.90  ? 268 TYR B CG  1 
ATOM   6332  C CD1 . TYR B 1 268 ? 9.128   51.785  15.990  1.00 20.35  ? 268 TYR B CD1 1 
ATOM   6333  C CD2 . TYR B 1 268 ? 9.066   52.076  13.629  1.00 15.88  ? 268 TYR B CD2 1 
ATOM   6334  C CE1 . TYR B 1 268 ? 10.194  52.665  16.076  1.00 19.30  ? 268 TYR B CE1 1 
ATOM   6335  C CE2 . TYR B 1 268 ? 10.131  52.956  13.704  1.00 20.81  ? 268 TYR B CE2 1 
ATOM   6336  C CZ  . TYR B 1 268 ? 10.692  53.247  14.930  1.00 23.08  ? 268 TYR B CZ  1 
ATOM   6337  O OH  . TYR B 1 268 ? 11.751  54.122  15.009  1.00 35.63  ? 268 TYR B OH  1 
ATOM   6338  N N   . GLU B 1 269 ? 5.445   52.705  13.503  1.00 25.94  ? 269 GLU B N   1 
ATOM   6339  C CA  . GLU B 1 269 ? 5.279   54.057  12.977  1.00 21.37  ? 269 GLU B CA  1 
ATOM   6340  C C   . GLU B 1 269 ? 4.221   54.839  13.745  1.00 17.94  ? 269 GLU B C   1 
ATOM   6341  O O   . GLU B 1 269 ? 4.316   56.067  13.854  1.00 23.03  ? 269 GLU B O   1 
ATOM   6342  C CB  . GLU B 1 269 ? 4.926   53.998  11.487  1.00 22.26  ? 269 GLU B CB  1 
ATOM   6343  C CG  . GLU B 1 269 ? 6.137   53.867  10.574  1.00 34.52  ? 269 GLU B CG  1 
ATOM   6344  C CD  . GLU B 1 269 ? 5.837   53.089  9.308   1.00 47.91  ? 269 GLU B CD  1 
ATOM   6345  O OE1 . GLU B 1 269 ? 4.667   53.092  8.869   1.00 46.08  ? 269 GLU B OE1 1 
ATOM   6346  O OE2 . GLU B 1 269 ? 6.769   52.467  8.756   1.00 51.47  ? 269 GLU B OE2 1 
ATOM   6347  N N   . LYS B 1 270 ? 3.214   54.153  14.288  1.00 13.36  ? 270 LYS B N   1 
ATOM   6348  C CA  . LYS B 1 270 ? 2.166   54.791  15.070  1.00 13.05  ? 270 LYS B CA  1 
ATOM   6349  C C   . LYS B 1 270 ? 2.466   54.795  16.565  1.00 13.34  ? 270 LYS B C   1 
ATOM   6350  O O   . LYS B 1 270 ? 1.546   54.973  17.373  1.00 17.68  ? 270 LYS B O   1 
ATOM   6351  C CB  . LYS B 1 270 ? 0.822   54.112  14.803  1.00 12.29  ? 270 LYS B CB  1 
ATOM   6352  C CG  . LYS B 1 270 ? 0.527   53.881  13.331  1.00 12.50  ? 270 LYS B CG  1 
ATOM   6353  C CD  . LYS B 1 270 ? 0.003   55.138  12.660  1.00 14.61  ? 270 LYS B CD  1 
ATOM   6354  C CE  . LYS B 1 270 ? 0.238   55.088  11.160  1.00 20.44  ? 270 LYS B CE  1 
ATOM   6355  N NZ  . LYS B 1 270 ? 0.446   56.443  10.578  1.00 30.81  ? 270 LYS B NZ  1 
ATOM   6356  N N   . GLY B 1 271 ? 3.725   54.609  16.947  1.00 13.17  ? 271 GLY B N   1 
ATOM   6357  C CA  . GLY B 1 271 ? 4.113   54.669  18.346  1.00 13.14  ? 271 GLY B CA  1 
ATOM   6358  C C   . GLY B 1 271 ? 3.599   53.550  19.229  1.00 12.15  ? 271 GLY B C   1 
ATOM   6359  O O   . GLY B 1 271 ? 3.099   53.816  20.331  1.00 11.95  ? 271 GLY B O   1 
ATOM   6360  N N   . ILE B 1 272 ? 3.706   52.304  18.777  1.00 14.84  ? 272 ILE B N   1 
ATOM   6361  C CA  . ILE B 1 272 ? 3.370   51.134  19.582  1.00 10.82  ? 272 ILE B CA  1 
ATOM   6362  C C   . ILE B 1 272 ? 4.679   50.466  19.980  1.00 13.27  ? 272 ILE B C   1 
ATOM   6363  O O   . ILE B 1 272 ? 5.386   49.906  19.133  1.00 17.70  ? 272 ILE B O   1 
ATOM   6364  C CB  . ILE B 1 272 ? 2.451   50.164  18.827  1.00 10.13  ? 272 ILE B CB  1 
ATOM   6365  C CG1 . ILE B 1 272 ? 1.064   50.783  18.627  1.00 11.18  ? 272 ILE B CG1 1 
ATOM   6366  C CG2 . ILE B 1 272 ? 2.343   48.841  19.570  1.00 9.48   ? 272 ILE B CG2 1 
ATOM   6367  C CD1 . ILE B 1 272 ? 0.514   51.477  19.852  1.00 9.91   ? 272 ILE B CD1 1 
ATOM   6368  N N   . ASN B 1 273 ? 5.006   50.523  21.272  1.00 14.97  ? 273 ASN B N   1 
ATOM   6369  C CA  . ASN B 1 273 ? 6.285   50.004  21.744  1.00 11.67  ? 273 ASN B CA  1 
ATOM   6370  C C   . ASN B 1 273 ? 6.304   48.484  21.833  1.00 13.47  ? 273 ASN B C   1 
ATOM   6371  O O   . ASN B 1 273 ? 7.352   47.872  21.604  1.00 18.08  ? 273 ASN B O   1 
ATOM   6372  C CB  . ASN B 1 273 ? 6.626   50.602  23.109  1.00 12.08  ? 273 ASN B CB  1 
ATOM   6373  C CG  . ASN B 1 273 ? 6.620   52.114  23.102  1.00 22.80  ? 273 ASN B CG  1 
ATOM   6374  O OD1 . ASN B 1 273 ? 6.806   52.740  22.060  1.00 23.39  ? 273 ASN B OD1 1 
ATOM   6375  N ND2 . ASN B 1 273 ? 6.412   52.711  24.269  1.00 23.84  ? 273 ASN B ND2 1 
ATOM   6376  N N   . MET B 1 274 ? 5.178   47.859  22.171  1.00 17.03  ? 274 MET B N   1 
ATOM   6377  C CA  . MET B 1 274 ? 5.143   46.420  22.385  1.00 17.34  ? 274 MET B CA  1 
ATOM   6378  C C   . MET B 1 274 ? 3.852   45.833  21.841  1.00 13.85  ? 274 MET B C   1 
ATOM   6379  O O   . MET B 1 274 ? 2.797   46.467  21.901  1.00 18.58  ? 274 MET B O   1 
ATOM   6380  C CB  . MET B 1 274 ? 5.265   46.070  23.875  1.00 19.41  ? 274 MET B CB  1 
ATOM   6381  C CG  . MET B 1 274 ? 5.314   44.574  24.168  1.00 18.42  ? 274 MET B CG  1 
ATOM   6382  S SD  . MET B 1 274 ? 3.685   43.869  24.501  1.00 23.68  ? 274 MET B SD  1 
ATOM   6383  C CE  . MET B 1 274 ? 3.538   44.132  26.266  1.00 21.56  ? 274 MET B CE  1 
ATOM   6384  N N   . LEU B 1 275 ? 3.950   44.616  21.310  1.00 8.88   ? 275 LEU B N   1 
ATOM   6385  C CA  . LEU B 1 275 ? 2.789   43.795  21.008  1.00 8.67   ? 275 LEU B CA  1 
ATOM   6386  C C   . LEU B 1 275 ? 3.178   42.337  21.214  1.00 15.25  ? 275 LEU B C   1 
ATOM   6387  O O   . LEU B 1 275 ? 4.345   42.014  21.446  1.00 17.97  ? 275 LEU B O   1 
ATOM   6388  C CB  . LEU B 1 275 ? 2.266   44.042  19.590  1.00 8.15   ? 275 LEU B CB  1 
ATOM   6389  C CG  . LEU B 1 275 ? 3.228   43.884  18.421  1.00 8.70   ? 275 LEU B CG  1 
ATOM   6390  C CD1 . LEU B 1 275 ? 3.208   42.456  17.895  1.00 20.76  ? 275 LEU B CD1 1 
ATOM   6391  C CD2 . LEU B 1 275 ? 2.863   44.866  17.325  1.00 9.97   ? 275 LEU B CD2 1 
ATOM   6392  N N   . ALA B 1 276 ? 2.187   41.456  21.131  1.00 18.72  ? 276 ALA B N   1 
ATOM   6393  C CA  . ALA B 1 276 ? 2.397   40.032  21.330  1.00 12.74  ? 276 ALA B CA  1 
ATOM   6394  C C   . ALA B 1 276 ? 1.846   39.256  20.143  1.00 13.18  ? 276 ALA B C   1 
ATOM   6395  O O   . ALA B 1 276 ? 1.157   39.804  19.278  1.00 14.66  ? 276 ALA B O   1 
ATOM   6396  C CB  . ALA B 1 276 ? 1.748   39.539  22.630  1.00 8.88   ? 276 ALA B CB  1 
ATOM   6397  N N   . THR B 1 277 ? 2.161   37.965  20.107  1.00 10.04  ? 277 THR B N   1 
ATOM   6398  C CA  . THR B 1 277 ? 1.635   37.071  19.083  1.00 12.37  ? 277 THR B CA  1 
ATOM   6399  C C   . THR B 1 277 ? 1.808   35.631  19.551  1.00 14.35  ? 277 THR B C   1 
ATOM   6400  O O   . THR B 1 277 ? 2.236   35.368  20.679  1.00 17.49  ? 277 THR B O   1 
ATOM   6401  C CB  . THR B 1 277 ? 2.312   37.306  17.731  1.00 9.48   ? 277 THR B CB  1 
ATOM   6402  O OG1 . THR B 1 277 ? 1.973   36.238  16.837  1.00 12.23  ? 277 THR B OG1 1 
ATOM   6403  C CG2 . THR B 1 277 ? 3.812   37.376  17.892  1.00 8.58   ? 277 THR B CG2 1 
ATOM   6404  N N   . ASP B 1 278 ? 1.457   34.696  18.674  1.00 18.76  ? 278 ASP B N   1 
ATOM   6405  C CA  . ASP B 1 278 ? 1.461   33.287  19.023  1.00 17.25  ? 278 ASP B CA  1 
ATOM   6406  C C   . ASP B 1 278 ? 2.848   32.691  18.818  1.00 19.24  ? 278 ASP B C   1 
ATOM   6407  O O   . ASP B 1 278 ? 3.649   33.178  18.014  1.00 21.91  ? 278 ASP B O   1 
ATOM   6408  C CB  . ASP B 1 278 ? 0.415   32.540  18.192  1.00 19.31  ? 278 ASP B CB  1 
ATOM   6409  C CG  . ASP B 1 278 ? 0.158   31.133  18.693  1.00 23.57  ? 278 ASP B CG  1 
ATOM   6410  O OD1 . ASP B 1 278 ? 0.818   30.706  19.664  1.00 25.81  ? 278 ASP B OD1 1 
ATOM   6411  O OD2 . ASP B 1 278 ? -0.751  30.471  18.151  1.00 26.44  ? 278 ASP B OD2 1 
ATOM   6412  N N   . GLU B 1 279 ? 3.137   31.634  19.576  1.00 19.72  ? 279 GLU B N   1 
ATOM   6413  C CA  . GLU B 1 279 ? 4.430   30.975  19.454  1.00 19.78  ? 279 GLU B CA  1 
ATOM   6414  C C   . GLU B 1 279 ? 4.521   30.060  18.237  1.00 18.48  ? 279 GLU B C   1 
ATOM   6415  O O   . GLU B 1 279 ? 5.625   29.613  17.910  1.00 19.68  ? 279 GLU B O   1 
ATOM   6416  C CB  . GLU B 1 279 ? 4.755   30.193  20.733  1.00 18.42  ? 279 GLU B CB  1 
ATOM   6417  C CG  . GLU B 1 279 ? 4.038   28.866  20.910  1.00 20.58  ? 279 GLU B CG  1 
ATOM   6418  C CD  . GLU B 1 279 ? 4.734   27.969  21.925  1.00 29.42  ? 279 GLU B CD  1 
ATOM   6419  O OE1 . GLU B 1 279 ? 5.897   27.581  21.682  1.00 32.89  ? 279 GLU B OE1 1 
ATOM   6420  O OE2 . GLU B 1 279 ? 4.123   27.659  22.970  1.00 32.30  ? 279 GLU B OE2 1 
ATOM   6421  N N   . VAL B 1 280 ? 3.407   29.772  17.555  1.00 17.04  ? 280 VAL B N   1 
ATOM   6422  C CA  . VAL B 1 280 ? 3.524   29.080  16.272  1.00 20.39  ? 280 VAL B CA  1 
ATOM   6423  C C   . VAL B 1 280 ? 4.158   30.004  15.242  1.00 14.80  ? 280 VAL B C   1 
ATOM   6424  O O   . VAL B 1 280 ? 4.905   29.554  14.363  1.00 16.60  ? 280 VAL B O   1 
ATOM   6425  C CB  . VAL B 1 280 ? 2.160   28.557  15.780  1.00 19.37  ? 280 VAL B CB  1 
ATOM   6426  C CG1 . VAL B 1 280 ? 1.111   29.656  15.821  1.00 26.57  ? 280 VAL B CG1 1 
ATOM   6427  C CG2 . VAL B 1 280 ? 2.291   27.931  14.384  1.00 22.05  ? 280 VAL B CG2 1 
ATOM   6428  N N   . ILE B 1 281 ? 3.866   31.304  15.323  1.00 14.01  ? 281 ILE B N   1 
ATOM   6429  C CA  . ILE B 1 281 ? 4.530   32.265  14.452  1.00 12.60  ? 281 ILE B CA  1 
ATOM   6430  C C   . ILE B 1 281 ? 6.011   32.357  14.800  1.00 16.68  ? 281 ILE B C   1 
ATOM   6431  O O   . ILE B 1 281 ? 6.862   32.493  13.913  1.00 18.19  ? 281 ILE B O   1 
ATOM   6432  C CB  . ILE B 1 281 ? 3.833   33.635  14.532  1.00 9.83   ? 281 ILE B CB  1 
ATOM   6433  C CG1 . ILE B 1 281 ? 2.478   33.595  13.821  1.00 9.73   ? 281 ILE B CG1 1 
ATOM   6434  C CG2 . ILE B 1 281 ? 4.704   34.720  13.922  1.00 15.36  ? 281 ILE B CG2 1 
ATOM   6435  C CD1 . ILE B 1 281 ? 1.302   33.773  14.745  1.00 12.83  ? 281 ILE B CD1 1 
ATOM   6436  N N   . LEU B 1 282 ? 6.346   32.262  16.091  1.00 18.36  ? 282 LEU B N   1 
ATOM   6437  C CA  . LEU B 1 282 ? 7.748   32.284  16.502  1.00 13.50  ? 282 LEU B CA  1 
ATOM   6438  C C   . LEU B 1 282 ? 8.498   31.070  15.974  1.00 20.25  ? 282 LEU B C   1 
ATOM   6439  O O   . LEU B 1 282 ? 9.616   31.196  15.460  1.00 24.20  ? 282 LEU B O   1 
ATOM   6440  C CB  . LEU B 1 282 ? 7.848   32.341  18.025  1.00 19.33  ? 282 LEU B CB  1 
ATOM   6441  C CG  . LEU B 1 282 ? 9.180   31.970  18.678  1.00 16.10  ? 282 LEU B CG  1 
ATOM   6442  C CD1 . LEU B 1 282 ? 10.182  33.097  18.501  1.00 17.38  ? 282 LEU B CD1 1 
ATOM   6443  C CD2 . LEU B 1 282 ? 8.974   31.667  20.151  1.00 14.20  ? 282 LEU B CD2 1 
ATOM   6444  N N   . LYS B 1 283 ? 7.900   29.884  16.096  1.00 16.56  ? 283 LYS B N   1 
ATOM   6445  C CA  . LYS B 1 283 ? 8.565   28.671  15.639  1.00 18.91  ? 283 LYS B CA  1 
ATOM   6446  C C   . LYS B 1 283 ? 8.694   28.640  14.121  1.00 22.96  ? 283 LYS B C   1 
ATOM   6447  O O   . LYS B 1 283 ? 9.636   28.039  13.594  1.00 24.27  ? 283 LYS B O   1 
ATOM   6448  C CB  . LYS B 1 283 ? 7.810   27.442  16.143  1.00 21.51  ? 283 LYS B CB  1 
ATOM   6449  C CG  . LYS B 1 283 ? 7.871   27.256  17.652  1.00 19.31  ? 283 LYS B CG  1 
ATOM   6450  C CD  . LYS B 1 283 ? 9.304   27.293  18.162  1.00 20.45  ? 283 LYS B CD  1 
ATOM   6451  C CE  . LYS B 1 283 ? 9.438   26.560  19.486  1.00 21.16  ? 283 LYS B CE  1 
ATOM   6452  N NZ  . LYS B 1 283 ? 8.315   26.873  20.410  1.00 19.37  ? 283 LYS B NZ  1 
ATOM   6453  N N   . ASN B 1 284 ? 7.759   29.272  13.407  1.00 26.13  ? 284 ASN B N   1 
ATOM   6454  C CA  . ASN B 1 284 ? 7.874   29.372  11.956  1.00 19.32  ? 284 ASN B CA  1 
ATOM   6455  C C   . ASN B 1 284 ? 8.972   30.345  11.541  1.00 24.65  ? 284 ASN B C   1 
ATOM   6456  O O   . ASN B 1 284 ? 9.563   30.188  10.467  1.00 33.05  ? 284 ASN B O   1 
ATOM   6457  C CB  . ASN B 1 284 ? 6.540   29.808  11.348  1.00 19.27  ? 284 ASN B CB  1 
ATOM   6458  C CG  . ASN B 1 284 ? 5.549   28.668  11.225  1.00 28.74  ? 284 ASN B CG  1 
ATOM   6459  O OD1 . ASN B 1 284 ? 5.905   27.500  11.370  1.00 43.07  ? 284 ASN B OD1 1 
ATOM   6460  N ND2 . ASN B 1 284 ? 4.293   29.006  10.955  1.00 24.72  ? 284 ASN B ND2 1 
ATOM   6461  N N   . SER B 1 285 ? 9.258   31.348  12.372  1.00 21.56  ? 285 SER B N   1 
ATOM   6462  C CA  . SER B 1 285 ? 10.127  32.456  11.990  1.00 24.16  ? 285 SER B CA  1 
ATOM   6463  C C   . SER B 1 285 ? 11.582  32.231  12.393  1.00 28.95  ? 285 SER B C   1 
ATOM   6464  O O   . SER B 1 285 ? 12.487  32.410  11.572  1.00 44.88  ? 285 SER B O   1 
ATOM   6465  C CB  . SER B 1 285 ? 9.603   33.758  12.601  1.00 23.49  ? 285 SER B CB  1 
ATOM   6466  O OG  . SER B 1 285 ? 8.202   33.871  12.422  1.00 22.51  ? 285 SER B OG  1 
ATOM   6467  N N   . VAL B 1 286 ? 11.824  31.859  13.647  1.00 27.66  ? 286 VAL B N   1 
ATOM   6468  C CA  . VAL B 1 286 ? 13.165  31.563  14.122  1.00 33.76  ? 286 VAL B CA  1 
ATOM   6469  C C   . VAL B 1 286 ? 13.325  30.050  14.218  1.00 37.64  ? 286 VAL B C   1 
ATOM   6470  O O   . VAL B 1 286 ? 12.352  29.302  14.346  1.00 43.55  ? 286 VAL B O   1 
ATOM   6471  C CB  . VAL B 1 286 ? 13.462  32.250  15.474  1.00 29.40  ? 286 VAL B CB  1 
ATOM   6472  C CG1 . VAL B 1 286 ? 13.053  33.719  15.425  1.00 24.48  ? 286 VAL B CG1 1 
ATOM   6473  C CG2 . VAL B 1 286 ? 12.742  31.534  16.592  1.00 35.57  ? 286 VAL B CG2 1 
ATOM   6474  N N   . GLU B 1 287 ? 14.576  29.588  14.146  1.00 40.80  ? 287 GLU B N   1 
ATOM   6475  C CA  . GLU B 1 287 ? 14.848  28.163  13.992  1.00 45.00  ? 287 GLU B CA  1 
ATOM   6476  C C   . GLU B 1 287 ? 14.325  27.348  15.170  1.00 60.77  ? 287 GLU B C   1 
ATOM   6477  O O   . GLU B 1 287 ? 13.395  26.552  15.011  1.00 64.34  ? 287 GLU B O   1 
ATOM   6478  C CB  . GLU B 1 287 ? 16.348  27.920  13.812  1.00 46.55  ? 287 GLU B CB  1 
ATOM   6479  C CG  . GLU B 1 287 ? 16.669  26.639  13.057  1.00 56.78  ? 287 GLU B CG  1 
ATOM   6480  C CD  . GLU B 1 287 ? 17.898  25.929  13.588  1.00 66.95  ? 287 GLU B CD  1 
ATOM   6481  O OE1 . GLU B 1 287 ? 18.938  26.594  13.781  1.00 58.45  ? 287 GLU B OE1 1 
ATOM   6482  O OE2 . GLU B 1 287 ? 17.824  24.702  13.812  1.00 58.31  ? 287 GLU B OE2 1 
ATOM   6483  N N   . ARG B 1 288 ? 14.905  27.540  16.356  1.00 55.58  ? 288 ARG B N   1 
ATOM   6484  C CA  . ARG B 1 288 ? 14.387  26.900  17.567  1.00 52.20  ? 288 ARG B CA  1 
ATOM   6485  C C   . ARG B 1 288 ? 14.716  27.811  18.748  1.00 54.56  ? 288 ARG B C   1 
ATOM   6486  O O   . ARG B 1 288 ? 15.823  27.764  19.292  1.00 51.65  ? 288 ARG B O   1 
ATOM   6487  C CB  . ARG B 1 288 ? 14.947  25.490  17.742  1.00 45.39  ? 288 ARG B CB  1 
ATOM   6488  C CG  . ARG B 1 288 ? 16.464  25.361  17.723  1.00 52.48  ? 288 ARG B CG  1 
ATOM   6489  C CD  . ARG B 1 288 ? 16.928  24.198  16.863  1.00 60.19  ? 288 ARG B CD  1 
ATOM   6490  N NE  . ARG B 1 288 ? 16.610  22.902  17.451  1.00 65.66  ? 288 ARG B NE  1 
ATOM   6491  C CZ  . ARG B 1 288 ? 16.959  21.737  16.921  1.00 59.85  ? 288 ARG B CZ  1 
ATOM   6492  N NH1 . ARG B 1 288 ? 17.653  21.671  15.796  1.00 65.91  ? 288 ARG B NH1 1 
ATOM   6493  N NH2 . ARG B 1 288 ? 16.600  20.612  17.532  1.00 52.69  ? 288 ARG B NH2 1 
ATOM   6494  N N   . ALA B 1 289 ? 13.752  28.643  19.133  1.00 46.58  ? 289 ALA B N   1 
ATOM   6495  C CA  . ALA B 1 289 ? 13.941  29.568  20.237  1.00 51.40  ? 289 ALA B CA  1 
ATOM   6496  C C   . ALA B 1 289 ? 12.722  29.537  21.147  1.00 37.79  ? 289 ALA B C   1 
ATOM   6497  O O   . ALA B 1 289 ? 11.610  29.202  20.729  1.00 32.15  ? 289 ALA B O   1 
ATOM   6498  C CB  . ALA B 1 289 ? 14.200  30.996  19.743  1.00 46.84  ? 289 ALA B CB  1 
ATOM   6499  N N   . SER B 1 290 ? 12.956  29.896  22.405  1.00 31.13  ? 290 SER B N   1 
ATOM   6500  C CA  . SER B 1 290 ? 11.919  29.811  23.417  1.00 25.76  ? 290 SER B CA  1 
ATOM   6501  C C   . SER B 1 290 ? 10.880  30.916  23.232  1.00 22.12  ? 290 SER B C   1 
ATOM   6502  O O   . SER B 1 290 ? 11.198  32.009  22.756  1.00 25.77  ? 290 SER B O   1 
ATOM   6503  C CB  . SER B 1 290 ? 12.530  29.914  24.812  1.00 19.37  ? 290 SER B CB  1 
ATOM   6504  O OG  . SER B 1 290 ? 12.296  28.738  25.565  1.00 28.95  ? 290 SER B OG  1 
ATOM   6505  N N   . PRO B 1 291 ? 9.626   30.652  23.596  1.00 15.44  ? 291 PRO B N   1 
ATOM   6506  C CA  . PRO B 1 291 ? 8.655   31.734  23.781  1.00 13.30  ? 291 PRO B CA  1 
ATOM   6507  C C   . PRO B 1 291 ? 8.811   32.483  25.094  1.00 17.56  ? 291 PRO B C   1 
ATOM   6508  O O   . PRO B 1 291 ? 7.994   33.359  25.391  1.00 24.34  ? 291 PRO B O   1 
ATOM   6509  C CB  . PRO B 1 291 ? 7.314   30.987  23.741  1.00 13.60  ? 291 PRO B CB  1 
ATOM   6510  C CG  . PRO B 1 291 ? 7.630   29.641  24.291  1.00 16.07  ? 291 PRO B CG  1 
ATOM   6511  C CD  . PRO B 1 291 ? 9.043   29.326  23.866  1.00 16.98  ? 291 PRO B CD  1 
ATOM   6512  N N   . TYR B 1 292 ? 9.842   32.155  25.871  1.00 17.56  ? 292 TYR B N   1 
ATOM   6513  C CA  . TYR B 1 292 ? 10.033  32.681  27.213  1.00 20.62  ? 292 TYR B CA  1 
ATOM   6514  C C   . TYR B 1 292 ? 11.029  33.829  27.267  1.00 21.44  ? 292 TYR B C   1 
ATOM   6515  O O   . TYR B 1 292 ? 11.281  34.365  28.351  1.00 20.64  ? 292 TYR B O   1 
ATOM   6516  C CB  . TYR B 1 292 ? 10.472  31.554  28.150  1.00 20.28  ? 292 TYR B CB  1 
ATOM   6517  C CG  . TYR B 1 292 ? 9.532   30.374  28.103  1.00 18.15  ? 292 TYR B CG  1 
ATOM   6518  C CD1 . TYR B 1 292 ? 8.211   30.505  28.510  1.00 18.26  ? 292 TYR B CD1 1 
ATOM   6519  C CD2 . TYR B 1 292 ? 9.956   29.135  27.639  1.00 19.32  ? 292 TYR B CD2 1 
ATOM   6520  C CE1 . TYR B 1 292 ? 7.340   29.436  28.465  1.00 21.41  ? 292 TYR B CE1 1 
ATOM   6521  C CE2 . TYR B 1 292 ? 9.091   28.057  27.590  1.00 18.28  ? 292 TYR B CE2 1 
ATOM   6522  C CZ  . TYR B 1 292 ? 7.784   28.214  28.005  1.00 24.06  ? 292 TYR B CZ  1 
ATOM   6523  O OH  . TYR B 1 292 ? 6.914   27.149  27.962  1.00 35.52  ? 292 TYR B OH  1 
ATOM   6524  N N   . LEU B 1 293 ? 11.603  34.212  26.136  1.00 19.79  ? 293 LEU B N   1 
ATOM   6525  C CA  . LEU B 1 293 ? 12.412  35.414  26.055  1.00 15.68  ? 293 LEU B CA  1 
ATOM   6526  C C   . LEU B 1 293 ? 11.538  36.599  25.664  1.00 14.32  ? 293 LEU B C   1 
ATOM   6527  O O   . LEU B 1 293 ? 10.425  36.443  25.156  1.00 22.62  ? 293 LEU B O   1 
ATOM   6528  C CB  . LEU B 1 293 ? 13.539  35.250  25.032  1.00 17.08  ? 293 LEU B CB  1 
ATOM   6529  C CG  . LEU B 1 293 ? 14.861  34.579  25.409  1.00 19.07  ? 293 LEU B CG  1 
ATOM   6530  C CD1 . LEU B 1 293 ? 14.636  33.189  25.955  1.00 22.85  ? 293 LEU B CD1 1 
ATOM   6531  C CD2 . LEU B 1 293 ? 15.779  34.527  24.199  1.00 20.34  ? 293 LEU B CD2 1 
ATOM   6532  N N   . ARG B 1 294 ? 12.050  37.796  25.921  1.00 14.64  ? 294 ARG B N   1 
ATOM   6533  C CA  . ARG B 1 294 ? 11.524  38.988  25.279  1.00 13.89  ? 294 ARG B CA  1 
ATOM   6534  C C   . ARG B 1 294 ? 12.260  39.166  23.961  1.00 14.63  ? 294 ARG B C   1 
ATOM   6535  O O   . ARG B 1 294 ? 13.478  38.983  23.891  1.00 16.02  ? 294 ARG B O   1 
ATOM   6536  C CB  . ARG B 1 294 ? 11.702  40.222  26.164  1.00 14.04  ? 294 ARG B CB  1 
ATOM   6537  C CG  . ARG B 1 294 ? 11.438  41.545  25.454  1.00 14.46  ? 294 ARG B CG  1 
ATOM   6538  C CD  . ARG B 1 294 ? 11.626  42.723  26.392  1.00 16.21  ? 294 ARG B CD  1 
ATOM   6539  N NE  . ARG B 1 294 ? 12.881  42.627  27.126  1.00 22.53  ? 294 ARG B NE  1 
ATOM   6540  C CZ  . ARG B 1 294 ? 12.978  42.641  28.448  1.00 20.93  ? 294 ARG B CZ  1 
ATOM   6541  N NH1 . ARG B 1 294 ? 11.908  42.762  29.218  1.00 20.06  ? 294 ARG B NH1 1 
ATOM   6542  N NH2 . ARG B 1 294 ? 14.179  42.533  29.012  1.00 19.34  ? 294 ARG B NH2 1 
ATOM   6543  N N   . TYR B 1 295 ? 11.520  39.492  22.908  1.00 13.84  ? 295 TYR B N   1 
ATOM   6544  C CA  . TYR B 1 295 ? 12.098  39.618  21.580  1.00 14.51  ? 295 TYR B CA  1 
ATOM   6545  C C   . TYR B 1 295 ? 12.073  41.068  21.124  1.00 14.45  ? 295 TYR B C   1 
ATOM   6546  O O   . TYR B 1 295 ? 11.054  41.752  21.255  1.00 13.43  ? 295 TYR B O   1 
ATOM   6547  C CB  . TYR B 1 295 ? 11.375  38.717  20.579  1.00 13.94  ? 295 TYR B CB  1 
ATOM   6548  C CG  . TYR B 1 295 ? 11.753  37.268  20.762  1.00 14.58  ? 295 TYR B CG  1 
ATOM   6549  C CD1 . TYR B 1 295 ? 11.039  36.447  21.622  1.00 13.90  ? 295 TYR B CD1 1 
ATOM   6550  C CD2 . TYR B 1 295 ? 12.860  36.735  20.118  1.00 16.07  ? 295 TYR B CD2 1 
ATOM   6551  C CE1 . TYR B 1 295 ? 11.393  35.129  21.808  1.00 14.68  ? 295 TYR B CE1 1 
ATOM   6552  C CE2 . TYR B 1 295 ? 13.224  35.418  20.300  1.00 16.94  ? 295 TYR B CE2 1 
ATOM   6553  C CZ  . TYR B 1 295 ? 12.485  34.620  21.147  1.00 16.25  ? 295 TYR B CZ  1 
ATOM   6554  O OH  . TYR B 1 295 ? 12.831  33.306  21.343  1.00 17.31  ? 295 TYR B OH  1 
ATOM   6555  N N   . TYR B 1 296 ? 13.209  41.527  20.610  1.00 15.71  ? 296 TYR B N   1 
ATOM   6556  C CA  . TYR B 1 296 ? 13.348  42.850  20.018  1.00 15.95  ? 296 TYR B CA  1 
ATOM   6557  C C   . TYR B 1 296 ? 13.232  42.689  18.508  1.00 16.04  ? 296 TYR B C   1 
ATOM   6558  O O   . TYR B 1 296 ? 14.122  42.115  17.874  1.00 17.14  ? 296 TYR B O   1 
ATOM   6559  C CB  . TYR B 1 296 ? 14.693  43.472  20.377  1.00 17.44  ? 296 TYR B CB  1 
ATOM   6560  C CG  . TYR B 1 296 ? 14.759  44.183  21.705  1.00 17.45  ? 296 TYR B CG  1 
ATOM   6561  C CD1 . TYR B 1 296 ? 13.616  44.666  22.323  1.00 16.21  ? 296 TYR B CD1 1 
ATOM   6562  C CD2 . TYR B 1 296 ? 15.979  44.383  22.336  1.00 18.87  ? 296 TYR B CD2 1 
ATOM   6563  C CE1 . TYR B 1 296 ? 13.689  45.322  23.538  1.00 20.60  ? 296 TYR B CE1 1 
ATOM   6564  C CE2 . TYR B 1 296 ? 16.062  45.038  23.544  1.00 19.01  ? 296 TYR B CE2 1 
ATOM   6565  C CZ  . TYR B 1 296 ? 14.917  45.504  24.143  1.00 17.74  ? 296 TYR B CZ  1 
ATOM   6566  O OH  . TYR B 1 296 ? 15.003  46.156  25.351  1.00 18.00  ? 296 TYR B OH  1 
ATOM   6567  N N   . PHE B 1 297 ? 12.148  43.191  17.929  1.00 15.04  ? 297 PHE B N   1 
ATOM   6568  C CA  . PHE B 1 297 ? 12.013  43.150  16.479  1.00 15.21  ? 297 PHE B CA  1 
ATOM   6569  C C   . PHE B 1 297 ? 12.846  44.274  15.880  1.00 17.69  ? 297 PHE B C   1 
ATOM   6570  O O   . PHE B 1 297 ? 12.470  45.447  15.962  1.00 18.58  ? 297 PHE B O   1 
ATOM   6571  C CB  . PHE B 1 297 ? 10.555  43.264  16.047  1.00 13.92  ? 297 PHE B CB  1 
ATOM   6572  C CG  . PHE B 1 297 ? 10.361  43.111  14.564  1.00 15.20  ? 297 PHE B CG  1 
ATOM   6573  C CD1 . PHE B 1 297 ? 10.491  41.869  13.966  1.00 14.36  ? 297 PHE B CD1 1 
ATOM   6574  C CD2 . PHE B 1 297 ? 10.071  44.207  13.766  1.00 17.08  ? 297 PHE B CD2 1 
ATOM   6575  C CE1 . PHE B 1 297 ? 10.325  41.720  12.604  1.00 16.17  ? 297 PHE B CE1 1 
ATOM   6576  C CE2 . PHE B 1 297 ? 9.903   44.062  12.399  1.00 14.55  ? 297 PHE B CE2 1 
ATOM   6577  C CZ  . PHE B 1 297 ? 10.031  42.818  11.819  1.00 15.46  ? 297 PHE B CZ  1 
ATOM   6578  N N   . ARG B 1 298 ? 13.995  43.913  15.303  1.00 20.88  ? 298 ARG B N   1 
ATOM   6579  C CA  . ARG B 1 298 ? 14.820  44.819  14.501  1.00 18.91  ? 298 ARG B CA  1 
ATOM   6580  C C   . ARG B 1 298 ? 15.228  46.073  15.262  1.00 22.07  ? 298 ARG B C   1 
ATOM   6581  O O   . ARG B 1 298 ? 15.492  47.114  14.651  1.00 32.41  ? 298 ARG B O   1 
ATOM   6582  C CB  . ARG B 1 298 ? 14.106  45.216  13.207  1.00 18.57  ? 298 ARG B CB  1 
ATOM   6583  C CG  . ARG B 1 298 ? 13.843  44.071  12.263  1.00 19.96  ? 298 ARG B CG  1 
ATOM   6584  C CD  . ARG B 1 298 ? 14.078  44.515  10.839  1.00 29.07  ? 298 ARG B CD  1 
ATOM   6585  N NE  . ARG B 1 298 ? 12.970  45.324  10.353  1.00 21.23  ? 298 ARG B NE  1 
ATOM   6586  C CZ  . ARG B 1 298 ? 12.075  44.908  9.470   1.00 19.20  ? 298 ARG B CZ  1 
ATOM   6587  N NH1 . ARG B 1 298 ? 12.128  43.690  8.954   1.00 18.19  ? 298 ARG B NH1 1 
ATOM   6588  N NH2 . ARG B 1 298 ? 11.103  45.733  9.095   1.00 21.56  ? 298 ARG B NH2 1 
ATOM   6589  N N   . GLU B 1 299 ? 15.292  45.988  16.589  1.00 19.04  ? 299 GLU B N   1 
ATOM   6590  C CA  . GLU B 1 299 ? 15.593  47.145  17.427  1.00 22.31  ? 299 GLU B CA  1 
ATOM   6591  C C   . GLU B 1 299 ? 14.650  48.304  17.103  1.00 23.51  ? 299 GLU B C   1 
ATOM   6592  O O   . GLU B 1 299 ? 15.066  49.446  16.907  1.00 24.14  ? 299 GLU B O   1 
ATOM   6593  C CB  . GLU B 1 299 ? 17.060  47.560  17.280  1.00 31.06  ? 299 GLU B CB  1 
ATOM   6594  C CG  . GLU B 1 299 ? 18.028  46.382  17.346  1.00 42.99  ? 299 GLU B CG  1 
ATOM   6595  C CD  . GLU B 1 299 ? 19.360  46.660  16.672  1.00 59.68  ? 299 GLU B CD  1 
ATOM   6596  O OE1 . GLU B 1 299 ? 19.644  47.836  16.363  1.00 65.72  ? 299 GLU B OE1 1 
ATOM   6597  O OE2 . GLU B 1 299 ? 20.127  45.698  16.456  1.00 48.92  ? 299 GLU B OE2 1 
ATOM   6598  N N   . LEU B 1 300 ? 13.366  47.982  16.998  1.00 23.21  ? 300 LEU B N   1 
ATOM   6599  C CA  . LEU B 1 300 ? 12.298  48.956  16.793  1.00 20.72  ? 300 LEU B CA  1 
ATOM   6600  C C   . LEU B 1 300 ? 11.155  48.797  17.783  1.00 20.35  ? 300 LEU B C   1 
ATOM   6601  O O   . LEU B 1 300 ? 10.556  49.795  18.189  1.00 20.47  ? 300 LEU B O   1 
ATOM   6602  C CB  . LEU B 1 300 ? 11.730  48.856  15.364  1.00 24.70  ? 300 LEU B CB  1 
ATOM   6603  C CG  . LEU B 1 300 ? 12.616  49.093  14.141  1.00 23.90  ? 300 LEU B CG  1 
ATOM   6604  C CD1 . LEU B 1 300 ? 11.844  48.759  12.869  1.00 21.94  ? 300 LEU B CD1 1 
ATOM   6605  C CD2 . LEU B 1 300 ? 13.113  50.527  14.105  1.00 27.66  ? 300 LEU B CD2 1 
ATOM   6606  N N   . ILE B 1 301 ? 10.836  47.568  18.176  1.00 14.56  ? 301 ILE B N   1 
ATOM   6607  C CA  . ILE B 1 301 ? 9.609   47.282  18.908  1.00 16.24  ? 301 ILE B CA  1 
ATOM   6608  C C   . ILE B 1 301 ? 9.781   45.937  19.603  1.00 13.04  ? 301 ILE B C   1 
ATOM   6609  O O   . ILE B 1 301 ? 10.417  45.024  19.068  1.00 16.77  ? 301 ILE B O   1 
ATOM   6610  C CB  . ILE B 1 301 ? 8.391   47.298  17.950  1.00 15.26  ? 301 ILE B CB  1 
ATOM   6611  C CG1 . ILE B 1 301 ? 7.117   46.821  18.647  1.00 13.20  ? 301 ILE B CG1 1 
ATOM   6612  C CG2 . ILE B 1 301 ? 8.674   46.448  16.719  1.00 20.22  ? 301 ILE B CG2 1 
ATOM   6613  C CD1 . ILE B 1 301 ? 5.906   46.797  17.740  1.00 10.81  ? 301 ILE B CD1 1 
ATOM   6614  N N   . SER B 1 302 ? 9.225   45.825  20.808  1.00 12.43  ? 302 SER B N   1 
ATOM   6615  C CA  . SER B 1 302 ? 9.273   44.583  21.565  1.00 12.15  ? 302 SER B CA  1 
ATOM   6616  C C   . SER B 1 302 ? 8.117   43.675  21.165  1.00 11.13  ? 302 SER B C   1 
ATOM   6617  O O   . SER B 1 302 ? 7.009   44.142  20.885  1.00 10.84  ? 302 SER B O   1 
ATOM   6618  C CB  . SER B 1 302 ? 9.228   44.854  23.069  1.00 12.11  ? 302 SER B CB  1 
ATOM   6619  O OG  . SER B 1 302 ? 10.317  45.660  23.479  1.00 13.18  ? 302 SER B OG  1 
ATOM   6620  N N   . VAL B 1 303 ? 8.390   42.372  21.129  1.00 11.17  ? 303 VAL B N   1 
ATOM   6621  C CA  . VAL B 1 303 ? 7.399   41.352  20.807  1.00 10.37  ? 303 VAL B CA  1 
ATOM   6622  C C   . VAL B 1 303 ? 7.515   40.226  21.825  1.00 10.31  ? 303 VAL B C   1 
ATOM   6623  O O   . VAL B 1 303 ? 8.622   39.772  22.134  1.00 11.16  ? 303 VAL B O   1 
ATOM   6624  C CB  . VAL B 1 303 ? 7.576   40.810  19.374  1.00 10.63  ? 303 VAL B CB  1 
ATOM   6625  C CG1 . VAL B 1 303 ? 6.536   39.744  19.075  1.00 9.90   ? 303 VAL B CG1 1 
ATOM   6626  C CG2 . VAL B 1 303 ? 7.473   41.940  18.358  1.00 10.79  ? 303 VAL B CG2 1 
ATOM   6627  N N   . PHE B 1 304 ? 6.376   39.789  22.356  1.00 9.90   ? 304 PHE B N   1 
ATOM   6628  C CA  . PHE B 1 304 ? 6.297   38.628  23.231  1.00 12.95  ? 304 PHE B CA  1 
ATOM   6629  C C   . PHE B 1 304 ? 5.436   37.562  22.569  1.00 11.99  ? 304 PHE B C   1 
ATOM   6630  O O   . PHE B 1 304 ? 4.378   37.863  22.017  1.00 14.77  ? 304 PHE B O   1 
ATOM   6631  C CB  . PHE B 1 304 ? 5.707   38.990  24.597  1.00 18.93  ? 304 PHE B CB  1 
ATOM   6632  C CG  . PHE B 1 304 ? 6.577   39.896  25.417  1.00 13.06  ? 304 PHE B CG  1 
ATOM   6633  C CD1 . PHE B 1 304 ? 7.539   39.372  26.263  1.00 12.44  ? 304 PHE B CD1 1 
ATOM   6634  C CD2 . PHE B 1 304 ? 6.432   41.270  25.345  1.00 12.76  ? 304 PHE B CD2 1 
ATOM   6635  C CE1 . PHE B 1 304 ? 8.339   40.203  27.023  1.00 12.83  ? 304 PHE B CE1 1 
ATOM   6636  C CE2 . PHE B 1 304 ? 7.230   42.105  26.103  1.00 20.27  ? 304 PHE B CE2 1 
ATOM   6637  C CZ  . PHE B 1 304 ? 8.186   41.569  26.942  1.00 13.09  ? 304 PHE B CZ  1 
ATOM   6638  N N   . PHE B 1 305 ? 5.888   36.318  22.620  1.00 16.93  ? 305 PHE B N   1 
ATOM   6639  C CA  . PHE B 1 305 ? 5.168   35.209  22.013  1.00 13.58  ? 305 PHE B CA  1 
ATOM   6640  C C   . PHE B 1 305 ? 4.520   34.391  23.122  1.00 16.01  ? 305 PHE B C   1 
ATOM   6641  O O   . PHE B 1 305 ? 5.215   33.877  24.005  1.00 16.65  ? 305 PHE B O   1 
ATOM   6642  C CB  . PHE B 1 305 ? 6.105   34.352  21.163  1.00 16.76  ? 305 PHE B CB  1 
ATOM   6643  C CG  . PHE B 1 305 ? 6.760   35.106  20.037  1.00 11.74  ? 305 PHE B CG  1 
ATOM   6644  C CD1 . PHE B 1 305 ? 7.914   35.841  20.255  1.00 12.88  ? 305 PHE B CD1 1 
ATOM   6645  C CD2 . PHE B 1 305 ? 6.213   35.093  18.764  1.00 13.61  ? 305 PHE B CD2 1 
ATOM   6646  C CE1 . PHE B 1 305 ? 8.515   36.540  19.222  1.00 12.44  ? 305 PHE B CE1 1 
ATOM   6647  C CE2 . PHE B 1 305 ? 6.815   35.784  17.725  1.00 13.13  ? 305 PHE B CE2 1 
ATOM   6648  C CZ  . PHE B 1 305 ? 7.964   36.512  17.955  1.00 11.37  ? 305 PHE B CZ  1 
ATOM   6649  N N   . ARG B 1 306 ? 3.195   34.282  23.078  1.00 19.01  ? 306 ARG B N   1 
ATOM   6650  C CA  . ARG B 1 306 ? 2.460   33.606  24.137  1.00 16.78  ? 306 ARG B CA  1 
ATOM   6651  C C   . ARG B 1 306 ? 2.777   32.116  24.147  1.00 16.89  ? 306 ARG B C   1 
ATOM   6652  O O   . ARG B 1 306 ? 3.156   31.530  23.130  1.00 19.77  ? 306 ARG B O   1 
ATOM   6653  C CB  . ARG B 1 306 ? 0.951   33.816  23.965  1.00 14.20  ? 306 ARG B CB  1 
ATOM   6654  C CG  . ARG B 1 306 ? 0.368   33.202  22.697  1.00 10.91  ? 306 ARG B CG  1 
ATOM   6655  C CD  . ARG B 1 306 ? -1.075  32.740  22.896  1.00 9.63   ? 306 ARG B CD  1 
ATOM   6656  N NE  . ARG B 1 306 ? -1.474  31.752  21.899  1.00 14.04  ? 306 ARG B NE  1 
ATOM   6657  C CZ  . ARG B 1 306 ? -2.697  31.251  21.779  1.00 9.48   ? 306 ARG B CZ  1 
ATOM   6658  N NH1 . ARG B 1 306 ? -3.682  31.632  22.577  1.00 9.30   ? 306 ARG B NH1 1 
ATOM   6659  N NH2 . ARG B 1 306 ? -2.937  30.345  20.834  1.00 12.38  ? 306 ARG B NH2 1 
ATOM   6660  N N   . ASP B 1 307 ? 2.629   31.503  25.320  1.00 22.67  ? 307 ASP B N   1 
ATOM   6661  C CA  . ASP B 1 307 ? 2.763   30.056  25.452  1.00 20.40  ? 307 ASP B CA  1 
ATOM   6662  C C   . ASP B 1 307 ? 1.459   29.421  24.985  1.00 17.83  ? 307 ASP B C   1 
ATOM   6663  O O   . ASP B 1 307 ? 0.446   29.473  25.689  1.00 19.77  ? 307 ASP B O   1 
ATOM   6664  C CB  . ASP B 1 307 ? 3.084   29.679  26.896  1.00 22.10  ? 307 ASP B CB  1 
ATOM   6665  C CG  . ASP B 1 307 ? 3.577   28.249  27.037  1.00 33.48  ? 307 ASP B CG  1 
ATOM   6666  O OD1 . ASP B 1 307 ? 3.018   27.346  26.374  1.00 40.11  ? 307 ASP B OD1 1 
ATOM   6667  O OD2 . ASP B 1 307 ? 4.527   28.025  27.816  1.00 33.11  ? 307 ASP B OD2 1 
ATOM   6668  N N   . LYS B 1 308 ? 1.480   28.827  23.789  1.00 15.82  ? 308 LYS B N   1 
ATOM   6669  C CA  . LYS B 1 308 ? 0.247   28.324  23.190  1.00 14.28  ? 308 LYS B CA  1 
ATOM   6670  C C   . LYS B 1 308 ? -0.364  27.211  24.032  1.00 20.66  ? 308 LYS B C   1 
ATOM   6671  O O   . LYS B 1 308 ? -1.591  27.125  24.165  1.00 27.11  ? 308 LYS B O   1 
ATOM   6672  C CB  . LYS B 1 308 ? 0.516   27.850  21.761  1.00 12.27  ? 308 LYS B CB  1 
ATOM   6673  C CG  . LYS B 1 308 ? -0.437  26.777  21.244  1.00 14.31  ? 308 LYS B CG  1 
ATOM   6674  C CD  . LYS B 1 308 ? -0.555  26.832  19.723  1.00 20.17  ? 308 LYS B CD  1 
ATOM   6675  C CE  . LYS B 1 308 ? -1.659  25.921  19.201  1.00 15.18  ? 308 LYS B CE  1 
ATOM   6676  N NZ  . LYS B 1 308 ? -3.020  26.365  19.614  1.00 14.60  ? 308 LYS B NZ  1 
ATOM   6677  N N   . THR B 1 309 ? 0.476   26.355  24.618  1.00 23.85  ? 309 THR B N   1 
ATOM   6678  C CA  . THR B 1 309 ? -0.037  25.229  25.394  1.00 21.82  ? 309 THR B CA  1 
ATOM   6679  C C   . THR B 1 309 ? -0.772  25.702  26.643  1.00 16.58  ? 309 THR B C   1 
ATOM   6680  O O   . THR B 1 309 ? -1.889  25.253  26.925  1.00 26.17  ? 309 THR B O   1 
ATOM   6681  C CB  . THR B 1 309 ? 1.105   24.284  25.773  1.00 25.45  ? 309 THR B CB  1 
ATOM   6682  O OG1 . THR B 1 309 ? 1.967   24.093  24.644  1.00 22.28  ? 309 THR B OG1 1 
ATOM   6683  C CG2 . THR B 1 309 ? 0.554   22.937  26.216  1.00 23.81  ? 309 THR B CG2 1 
ATOM   6684  N N   . LEU B 1 310 ? -0.160  26.609  27.407  1.00 18.38  ? 310 LEU B N   1 
ATOM   6685  C CA  . LEU B 1 310 ? -0.789  27.073  28.640  1.00 22.17  ? 310 LEU B CA  1 
ATOM   6686  C C   . LEU B 1 310 ? -2.073  27.842  28.357  1.00 18.05  ? 310 LEU B C   1 
ATOM   6687  O O   . LEU B 1 310 ? -3.072  27.676  29.066  1.00 19.78  ? 310 LEU B O   1 
ATOM   6688  C CB  . LEU B 1 310 ? 0.188   27.938  29.435  1.00 19.75  ? 310 LEU B CB  1 
ATOM   6689  C CG  . LEU B 1 310 ? 1.294   27.176  30.167  1.00 13.19  ? 310 LEU B CG  1 
ATOM   6690  C CD1 . LEU B 1 310 ? 2.377   28.125  30.618  1.00 12.57  ? 310 LEU B CD1 1 
ATOM   6691  C CD2 . LEU B 1 310 ? 0.728   26.413  31.353  1.00 17.71  ? 310 LEU B CD2 1 
ATOM   6692  N N   . SER B 1 311 ? -2.064  28.688  27.324  1.00 17.85  ? 311 SER B N   1 
ATOM   6693  C CA  . SER B 1 311 ? -3.225  29.521  27.035  1.00 14.75  ? 311 SER B CA  1 
ATOM   6694  C C   . SER B 1 311 ? -4.402  28.691  26.536  1.00 16.94  ? 311 SER B C   1 
ATOM   6695  O O   . SER B 1 311 ? -5.550  28.936  26.927  1.00 18.01  ? 311 SER B O   1 
ATOM   6696  C CB  . SER B 1 311 ? -2.851  30.597  26.018  1.00 12.66  ? 311 SER B CB  1 
ATOM   6697  O OG  . SER B 1 311 ? -1.702  31.313  26.439  1.00 13.43  ? 311 SER B OG  1 
ATOM   6698  N N   . ASP B 1 312 ? -4.144  27.711  25.669  1.00 22.46  ? 312 ASP B N   1 
ATOM   6699  C CA  . ASP B 1 312 ? -5.217  26.871  25.150  1.00 23.75  ? 312 ASP B CA  1 
ATOM   6700  C C   . ASP B 1 312 ? -5.680  25.818  26.146  1.00 20.86  ? 312 ASP B C   1 
ATOM   6701  O O   . ASP B 1 312 ? -6.742  25.220  25.940  1.00 23.94  ? 312 ASP B O   1 
ATOM   6702  C CB  . ASP B 1 312 ? -4.778  26.198  23.847  1.00 23.30  ? 312 ASP B CB  1 
ATOM   6703  C CG  . ASP B 1 312 ? -4.825  27.143  22.665  1.00 32.08  ? 312 ASP B CG  1 
ATOM   6704  O OD1 . ASP B 1 312 ? -5.316  28.279  22.836  1.00 35.83  ? 312 ASP B OD1 1 
ATOM   6705  O OD2 . ASP B 1 312 ? -4.375  26.754  21.566  1.00 31.24  ? 312 ASP B OD2 1 
ATOM   6706  N N   . LEU B 1 313 ? -4.916  25.570  27.211  1.00 20.99  ? 313 LEU B N   1 
ATOM   6707  C CA  . LEU B 1 313 ? -5.404  24.697  28.275  1.00 23.01  ? 313 LEU B CA  1 
ATOM   6708  C C   . LEU B 1 313 ? -6.505  25.379  29.077  1.00 22.80  ? 313 LEU B C   1 
ATOM   6709  O O   . LEU B 1 313 ? -7.508  24.748  29.430  1.00 23.18  ? 313 LEU B O   1 
ATOM   6710  C CB  . LEU B 1 313 ? -4.249  24.281  29.185  1.00 23.41  ? 313 LEU B CB  1 
ATOM   6711  C CG  . LEU B 1 313 ? -3.521  22.994  28.790  1.00 26.93  ? 313 LEU B CG  1 
ATOM   6712  C CD1 . LEU B 1 313 ? -2.120  22.965  29.373  1.00 27.08  ? 313 LEU B CD1 1 
ATOM   6713  C CD2 . LEU B 1 313 ? -4.310  21.777  29.240  1.00 26.78  ? 313 LEU B CD2 1 
ATOM   6714  N N   . ILE B 1 314 ? -6.331  26.667  29.375  1.00 18.74  ? 314 ILE B N   1 
ATOM   6715  C CA  . ILE B 1 314 ? -7.388  27.435  30.024  1.00 17.15  ? 314 ILE B CA  1 
ATOM   6716  C C   . ILE B 1 314 ? -8.594  27.565  29.105  1.00 17.04  ? 314 ILE B C   1 
ATOM   6717  O O   . ILE B 1 314 ? -9.742  27.396  29.533  1.00 16.59  ? 314 ILE B O   1 
ATOM   6718  C CB  . ILE B 1 314 ? -6.857  28.816  30.454  1.00 15.75  ? 314 ILE B CB  1 
ATOM   6719  C CG1 . ILE B 1 314 ? -5.666  28.663  31.401  1.00 17.97  ? 314 ILE B CG1 1 
ATOM   6720  C CG2 . ILE B 1 314 ? -7.962  29.637  31.101  1.00 13.07  ? 314 ILE B CG2 1 
ATOM   6721  C CD1 . ILE B 1 314 ? -5.161  29.975  31.962  1.00 17.77  ? 314 ILE B CD1 1 
ATOM   6722  N N   . GLY B 1 315 ? -8.356  27.860  27.827  1.00 16.31  ? 315 GLY B N   1 
ATOM   6723  C CA  . GLY B 1 315 ? -9.452  28.167  26.929  1.00 13.37  ? 315 GLY B CA  1 
ATOM   6724  C C   . GLY B 1 315 ? -10.248 26.961  26.482  1.00 19.46  ? 315 GLY B C   1 
ATOM   6725  O O   . GLY B 1 315 ? -11.441 27.082  26.186  1.00 26.72  ? 315 GLY B O   1 
ATOM   6726  N N   . PHE B 1 316 ? -9.621  25.783  26.433  1.00 16.10  ? 316 PHE B N   1 
ATOM   6727  C CA  . PHE B 1 316 ? -10.239 24.639  25.776  1.00 19.39  ? 316 PHE B CA  1 
ATOM   6728  C C   . PHE B 1 316 ? -10.213 23.335  26.565  1.00 20.77  ? 316 PHE B C   1 
ATOM   6729  O O   . PHE B 1 316 ? -10.938 22.407  26.190  1.00 25.36  ? 316 PHE B O   1 
ATOM   6730  C CB  . PHE B 1 316 ? -9.574  24.393  24.413  1.00 17.63  ? 316 PHE B CB  1 
ATOM   6731  C CG  . PHE B 1 316 ? -9.638  25.572  23.487  1.00 16.37  ? 316 PHE B CG  1 
ATOM   6732  C CD1 . PHE B 1 316 ? -10.754 25.789  22.698  1.00 16.65  ? 316 PHE B CD1 1 
ATOM   6733  C CD2 . PHE B 1 316 ? -8.586  26.471  23.416  1.00 24.45  ? 316 PHE B CD2 1 
ATOM   6734  C CE1 . PHE B 1 316 ? -10.817 26.878  21.845  1.00 19.64  ? 316 PHE B CE1 1 
ATOM   6735  C CE2 . PHE B 1 316 ? -8.643  27.561  22.568  1.00 28.25  ? 316 PHE B CE2 1 
ATOM   6736  C CZ  . PHE B 1 316 ? -9.759  27.764  21.781  1.00 25.87  ? 316 PHE B CZ  1 
ATOM   6737  N N   . SER B 1 317 ? -9.425  23.226  27.632  1.00 19.28  ? 317 SER B N   1 
ATOM   6738  C CA  . SER B 1 317 ? -9.253  21.956  28.326  1.00 20.47  ? 317 SER B CA  1 
ATOM   6739  C C   . SER B 1 317 ? -9.795  21.960  29.747  1.00 21.31  ? 317 SER B C   1 
ATOM   6740  O O   . SER B 1 317 ? -10.543 21.054  30.124  1.00 29.53  ? 317 SER B O   1 
ATOM   6741  C CB  . SER B 1 317 ? -7.767  21.570  28.347  1.00 23.94  ? 317 SER B CB  1 
ATOM   6742  O OG  . SER B 1 317 ? -7.157  21.798  27.088  1.00 35.58  ? 317 SER B OG  1 
ATOM   6743  N N   . TYR B 1 318 ? -9.444  22.967  30.548  1.00 19.23  ? 318 TYR B N   1 
ATOM   6744  C CA  . TYR B 1 318 ? -9.690  22.918  31.984  1.00 19.50  ? 318 TYR B CA  1 
ATOM   6745  C C   . TYR B 1 318 ? -11.167 22.990  32.350  1.00 25.29  ? 318 TYR B C   1 
ATOM   6746  O O   . TYR B 1 318 ? -11.501 22.775  33.521  1.00 26.90  ? 318 TYR B O   1 
ATOM   6747  C CB  . TYR B 1 318 ? -8.930  24.046  32.682  1.00 20.09  ? 318 TYR B CB  1 
ATOM   6748  C CG  . TYR B 1 318 ? -7.456  23.764  32.866  1.00 21.19  ? 318 TYR B CG  1 
ATOM   6749  C CD1 . TYR B 1 318 ? -6.953  22.478  32.721  1.00 26.94  ? 318 TYR B CD1 1 
ATOM   6750  C CD2 . TYR B 1 318 ? -6.570  24.782  33.193  1.00 22.19  ? 318 TYR B CD2 1 
ATOM   6751  C CE1 . TYR B 1 318 ? -5.606  22.214  32.891  1.00 24.77  ? 318 TYR B CE1 1 
ATOM   6752  C CE2 . TYR B 1 318 ? -5.222  24.528  33.366  1.00 24.57  ? 318 TYR B CE2 1 
ATOM   6753  C CZ  . TYR B 1 318 ? -4.746  23.242  33.214  1.00 27.29  ? 318 TYR B CZ  1 
ATOM   6754  O OH  . TYR B 1 318 ? -3.404  22.986  33.386  1.00 29.11  ? 318 TYR B OH  1 
ATOM   6755  N N   . HIS B 1 319 ? -12.052 23.292  31.397  1.00 25.27  ? 319 HIS B N   1 
ATOM   6756  C CA  . HIS B 1 319 ? -13.479 23.306  31.703  1.00 23.13  ? 319 HIS B CA  1 
ATOM   6757  C C   . HIS B 1 319 ? -13.977 21.925  32.111  1.00 25.26  ? 319 HIS B C   1 
ATOM   6758  O O   . HIS B 1 319 ? -14.907 21.813  32.918  1.00 33.42  ? 319 HIS B O   1 
ATOM   6759  C CB  . HIS B 1 319 ? -14.278 23.818  30.503  1.00 28.05  ? 319 HIS B CB  1 
ATOM   6760  C CG  . HIS B 1 319 ? -14.324 22.857  29.355  1.00 31.17  ? 319 HIS B CG  1 
ATOM   6761  N ND1 . HIS B 1 319 ? -15.382 22.000  29.144  1.00 28.56  ? 319 HIS B ND1 1 
ATOM   6762  C CD2 . HIS B 1 319 ? -13.443 22.620  28.355  1.00 28.83  ? 319 HIS B CD2 1 
ATOM   6763  C CE1 . HIS B 1 319 ? -15.151 21.275  28.064  1.00 29.27  ? 319 HIS B CE1 1 
ATOM   6764  N NE2 . HIS B 1 319 ? -13.981 21.632  27.566  1.00 25.69  ? 319 HIS B NE2 1 
ATOM   6765  N N   . ALA B 1 320 ? -13.378 20.865  31.564  1.00 24.42  ? 320 ALA B N   1 
ATOM   6766  C CA  . ALA B 1 320 ? -13.794 19.506  31.888  1.00 26.29  ? 320 ALA B CA  1 
ATOM   6767  C C   . ALA B 1 320 ? -13.167 18.987  33.174  1.00 26.51  ? 320 ALA B C   1 
ATOM   6768  O O   . ALA B 1 320 ? -13.634 17.977  33.712  1.00 28.36  ? 320 ALA B O   1 
ATOM   6769  C CB  . ALA B 1 320 ? -13.449 18.561  30.735  1.00 27.07  ? 320 ALA B CB  1 
ATOM   6770  N N   . TRP B 1 321 ? -12.132 19.652  33.678  1.00 25.16  ? 321 TRP B N   1 
ATOM   6771  C CA  . TRP B 1 321 ? -11.429 19.198  34.867  1.00 25.78  ? 321 TRP B CA  1 
ATOM   6772  C C   . TRP B 1 321 ? -12.199 19.590  36.124  1.00 25.75  ? 321 TRP B C   1 
ATOM   6773  O O   . TRP B 1 321 ? -13.230 20.266  36.077  1.00 33.87  ? 321 TRP B O   1 
ATOM   6774  C CB  . TRP B 1 321 ? -10.023 19.792  34.915  1.00 29.67  ? 321 TRP B CB  1 
ATOM   6775  C CG  . TRP B 1 321 ? -9.089  19.288  33.860  1.00 24.75  ? 321 TRP B CG  1 
ATOM   6776  C CD1 . TRP B 1 321 ? -9.354  19.131  32.531  1.00 24.89  ? 321 TRP B CD1 1 
ATOM   6777  C CD2 . TRP B 1 321 ? -7.727  18.891  34.047  1.00 25.11  ? 321 TRP B CD2 1 
ATOM   6778  N NE1 . TRP B 1 321 ? -8.245  18.653  31.881  1.00 25.32  ? 321 TRP B NE1 1 
ATOM   6779  C CE2 . TRP B 1 321 ? -7.231  18.498  32.789  1.00 25.48  ? 321 TRP B CE2 1 
ATOM   6780  C CE3 . TRP B 1 321 ? -6.879  18.827  35.157  1.00 25.28  ? 321 TRP B CE3 1 
ATOM   6781  C CZ2 . TRP B 1 321 ? -5.927  18.046  32.610  1.00 26.06  ? 321 TRP B CZ2 1 
ATOM   6782  C CZ3 . TRP B 1 321 ? -5.586  18.378  34.977  1.00 27.29  ? 321 TRP B CZ3 1 
ATOM   6783  C CH2 . TRP B 1 321 ? -5.122  17.994  33.713  1.00 26.25  ? 321 TRP B CH2 1 
ATOM   6784  N N   . ASN B 1 322 ? -11.686 19.154  37.268  1.00 29.72  ? 322 ASN B N   1 
ATOM   6785  C CA  . ASN B 1 322 ? -12.094 19.710  38.547  1.00 33.72  ? 322 ASN B CA  1 
ATOM   6786  C C   . ASN B 1 322 ? -11.268 20.960  38.818  1.00 35.29  ? 322 ASN B C   1 
ATOM   6787  O O   . ASN B 1 322 ? -10.112 21.062  38.398  1.00 39.94  ? 322 ASN B O   1 
ATOM   6788  C CB  . ASN B 1 322 ? -11.911 18.692  39.674  1.00 36.39  ? 322 ASN B CB  1 
ATOM   6789  C CG  . ASN B 1 322 ? -12.164 19.288  41.047  1.00 45.55  ? 322 ASN B CG  1 
ATOM   6790  O OD1 . ASN B 1 322 ? -11.285 19.916  41.639  1.00 48.64  ? 322 ASN B OD1 1 
ATOM   6791  N ND2 . ASN B 1 322 ? -13.374 19.097  41.557  1.00 52.95  ? 322 ASN B ND2 1 
ATOM   6792  N N   . ALA B 1 323 ? -11.878 21.918  39.518  1.00 35.67  ? 323 ALA B N   1 
ATOM   6793  C CA  . ALA B 1 323 ? -11.220 23.203  39.737  1.00 35.03  ? 323 ALA B CA  1 
ATOM   6794  C C   . ALA B 1 323 ? -9.890  23.030  40.460  1.00 40.02  ? 323 ALA B C   1 
ATOM   6795  O O   . ALA B 1 323 ? -8.897  23.679  40.111  1.00 34.24  ? 323 ALA B O   1 
ATOM   6796  C CB  . ALA B 1 323 ? -12.143 24.136  40.519  1.00 35.16  ? 323 ALA B CB  1 
ATOM   6797  N N   . GLU B 1 324 ? -9.848  22.153  41.464  1.00 49.21  ? 324 GLU B N   1 
ATOM   6798  C CA  . GLU B 1 324 ? -8.611  21.941  42.208  1.00 47.63  ? 324 GLU B CA  1 
ATOM   6799  C C   . GLU B 1 324 ? -7.567  21.224  41.360  1.00 45.02  ? 324 GLU B C   1 
ATOM   6800  O O   . GLU B 1 324 ? -6.371  21.523  41.455  1.00 46.09  ? 324 GLU B O   1 
ATOM   6801  C CB  . GLU B 1 324 ? -8.897  21.157  43.487  1.00 48.87  ? 324 GLU B CB  1 
ATOM   6802  C CG  . GLU B 1 324 ? -9.912  21.824  44.400  1.00 56.75  ? 324 GLU B CG  1 
ATOM   6803  C CD  . GLU B 1 324 ? -9.397  21.994  45.814  1.00 74.82  ? 324 GLU B CD  1 
ATOM   6804  O OE1 . GLU B 1 324 ? -8.184  21.788  46.033  1.00 77.98  ? 324 GLU B OE1 1 
ATOM   6805  O OE2 . GLU B 1 324 ? -10.203 22.335  46.706  1.00 66.96  ? 324 GLU B OE2 1 
ATOM   6806  N N   . ASP B 1 325 ? -7.996  20.267  40.533  1.00 42.06  ? 325 ASP B N   1 
ATOM   6807  C CA  . ASP B 1 325 ? -7.047  19.546  39.691  1.00 41.38  ? 325 ASP B CA  1 
ATOM   6808  C C   . ASP B 1 325 ? -6.438  20.457  38.630  1.00 34.25  ? 325 ASP B C   1 
ATOM   6809  O O   . ASP B 1 325 ? -5.241  20.362  38.334  1.00 30.54  ? 325 ASP B O   1 
ATOM   6810  C CB  . ASP B 1 325 ? -7.727  18.344  39.036  1.00 50.42  ? 325 ASP B CB  1 
ATOM   6811  C CG  . ASP B 1 325 ? -8.357  17.405  40.047  1.00 61.30  ? 325 ASP B CG  1 
ATOM   6812  O OD1 . ASP B 1 325 ? -7.811  17.282  41.165  1.00 64.79  ? 325 ASP B OD1 1 
ATOM   6813  O OD2 . ASP B 1 325 ? -9.392  16.784  39.724  1.00 62.67  ? 325 ASP B OD2 1 
ATOM   6814  N N   . ALA B 1 326 ? -7.247  21.344  38.044  1.00 32.52  ? 326 ALA B N   1 
ATOM   6815  C CA  . ALA B 1 326 ? -6.765  22.178  36.946  1.00 39.79  ? 326 ALA B CA  1 
ATOM   6816  C C   . ALA B 1 326 ? -5.755  23.217  37.423  1.00 39.21  ? 326 ALA B C   1 
ATOM   6817  O O   . ALA B 1 326 ? -4.789  23.521  36.714  1.00 33.29  ? 326 ALA B O   1 
ATOM   6818  C CB  . ALA B 1 326 ? -7.944  22.853  36.246  1.00 35.37  ? 326 ALA B CB  1 
ATOM   6819  N N   . VAL B 1 327 ? -5.970  23.789  38.609  1.00 38.00  ? 327 VAL B N   1 
ATOM   6820  C CA  . VAL B 1 327 ? -4.991  24.725  39.152  1.00 32.42  ? 327 VAL B CA  1 
ATOM   6821  C C   . VAL B 1 327 ? -3.715  23.992  39.548  1.00 26.68  ? 327 VAL B C   1 
ATOM   6822  O O   . VAL B 1 327 ? -2.613  24.543  39.438  1.00 24.04  ? 327 VAL B O   1 
ATOM   6823  C CB  . VAL B 1 327 ? -5.590  25.510  40.334  1.00 31.55  ? 327 VAL B CB  1 
ATOM   6824  C CG1 . VAL B 1 327 ? -4.605  26.554  40.832  1.00 22.73  ? 327 VAL B CG1 1 
ATOM   6825  C CG2 . VAL B 1 327 ? -6.896  26.168  39.918  1.00 27.53  ? 327 VAL B CG2 1 
ATOM   6826  N N   . ARG B 1 328 ? -3.839  22.747  40.015  1.00 28.66  ? 328 ARG B N   1 
ATOM   6827  C CA  . ARG B 1 328 ? -2.658  21.942  40.309  1.00 28.11  ? 328 ARG B CA  1 
ATOM   6828  C C   . ARG B 1 328 ? -1.857  21.661  39.046  1.00 25.81  ? 328 ARG B C   1 
ATOM   6829  O O   . ARG B 1 328 ? -0.621  21.699  39.063  1.00 24.80  ? 328 ARG B O   1 
ATOM   6830  C CB  . ARG B 1 328 ? -3.067  20.631  40.978  1.00 32.45  ? 328 ARG B CB  1 
ATOM   6831  C CG  . ARG B 1 328 ? -2.398  20.366  42.316  1.00 33.94  ? 328 ARG B CG  1 
ATOM   6832  C CD  . ARG B 1 328 ? -3.356  19.648  43.246  1.00 47.21  ? 328 ARG B CD  1 
ATOM   6833  N NE  . ARG B 1 328 ? -3.866  18.424  42.640  1.00 55.27  ? 328 ARG B NE  1 
ATOM   6834  C CZ  . ARG B 1 328 ? -5.069  17.917  42.873  1.00 63.39  ? 328 ARG B CZ  1 
ATOM   6835  N NH1 . ARG B 1 328 ? -5.919  18.507  43.697  1.00 63.77  ? 328 ARG B NH1 1 
ATOM   6836  N NH2 . ARG B 1 328 ? -5.429  16.792  42.261  1.00 65.68  ? 328 ARG B NH2 1 
ATOM   6837  N N   . ASP B 1 329 ? -2.545  21.362  37.940  1.00 24.76  ? 329 ASP B N   1 
ATOM   6838  C CA  . ASP B 1 329 ? -1.853  21.094  36.684  1.00 23.47  ? 329 ASP B CA  1 
ATOM   6839  C C   . ASP B 1 329 ? -1.213  22.357  36.120  1.00 25.12  ? 329 ASP B C   1 
ATOM   6840  O O   . ASP B 1 329 ? -0.122  22.300  35.542  1.00 32.29  ? 329 ASP B O   1 
ATOM   6841  C CB  . ASP B 1 329 ? -2.821  20.486  35.672  1.00 23.89  ? 329 ASP B CB  1 
ATOM   6842  C CG  . ASP B 1 329 ? -2.158  20.173  34.347  1.00 29.68  ? 329 ASP B CG  1 
ATOM   6843  O OD1 . ASP B 1 329 ? -2.119  21.068  33.476  1.00 27.48  ? 329 ASP B OD1 1 
ATOM   6844  O OD2 . ASP B 1 329 ? -1.675  19.034  34.176  1.00 31.23  ? 329 ASP B OD2 1 
ATOM   6845  N N   . PHE B 1 330 ? -1.884  23.502  36.263  1.00 27.98  ? 330 PHE B N   1 
ATOM   6846  C CA  . PHE B 1 330 ? -1.330  24.756  35.760  1.00 27.95  ? 330 PHE B CA  1 
ATOM   6847  C C   . PHE B 1 330 ? -0.019  25.095  36.459  1.00 29.05  ? 330 PHE B C   1 
ATOM   6848  O O   . PHE B 1 330 ? 0.991   25.386  35.806  1.00 23.82  ? 330 PHE B O   1 
ATOM   6849  C CB  . PHE B 1 330 ? -2.341  25.887  35.940  1.00 20.37  ? 330 PHE B CB  1 
ATOM   6850  C CG  . PHE B 1 330 ? -2.032  27.105  35.122  1.00 21.76  ? 330 PHE B CG  1 
ATOM   6851  C CD1 . PHE B 1 330 ? -2.323  27.138  33.768  1.00 18.67  ? 330 PHE B CD1 1 
ATOM   6852  C CD2 . PHE B 1 330 ? -1.433  28.211  35.702  1.00 20.74  ? 330 PHE B CD2 1 
ATOM   6853  C CE1 . PHE B 1 330 ? -2.033  28.259  33.009  1.00 25.87  ? 330 PHE B CE1 1 
ATOM   6854  C CE2 . PHE B 1 330 ? -1.139  29.335  34.949  1.00 18.79  ? 330 PHE B CE2 1 
ATOM   6855  C CZ  . PHE B 1 330 ? -1.439  29.360  33.601  1.00 17.73  ? 330 PHE B CZ  1 
ATOM   6856  N N   . ILE B 1 331 ? -0.018  25.062  37.792  1.00 27.94  ? 331 ILE B N   1 
ATOM   6857  C CA  . ILE B 1 331 ? 1.192   25.379  38.543  1.00 20.08  ? 331 ILE B CA  1 
ATOM   6858  C C   . ILE B 1 331 ? 2.268   24.334  38.282  1.00 21.24  ? 331 ILE B C   1 
ATOM   6859  O O   . ILE B 1 331 ? 3.451   24.665  38.135  1.00 27.69  ? 331 ILE B O   1 
ATOM   6860  C CB  . ILE B 1 331 ? 0.872   25.506  40.045  1.00 22.96  ? 331 ILE B CB  1 
ATOM   6861  C CG1 . ILE B 1 331 ? -0.177  26.594  40.287  1.00 19.92  ? 331 ILE B CG1 1 
ATOM   6862  C CG2 . ILE B 1 331 ? 2.138   25.806  40.833  1.00 26.29  ? 331 ILE B CG2 1 
ATOM   6863  C CD1 . ILE B 1 331 ? 0.015   27.848  39.455  1.00 18.41  ? 331 ILE B CD1 1 
ATOM   6864  N N   . GLY B 1 332 ? 1.878   23.060  38.216  1.00 22.45  ? 332 GLY B N   1 
ATOM   6865  C CA  . GLY B 1 332 ? 2.847   22.018  37.922  1.00 23.82  ? 332 GLY B CA  1 
ATOM   6866  C C   . GLY B 1 332 ? 3.530   22.221  36.583  1.00 23.17  ? 332 GLY B C   1 
ATOM   6867  O O   . GLY B 1 332 ? 4.728   21.963  36.442  1.00 30.68  ? 332 GLY B O   1 
ATOM   6868  N N   . ARG B 1 333 ? 2.779   22.687  35.583  1.00 21.95  ? 333 ARG B N   1 
ATOM   6869  C CA  . ARG B 1 333 ? 3.376   22.979  34.284  1.00 21.40  ? 333 ARG B CA  1 
ATOM   6870  C C   . ARG B 1 333 ? 4.305   24.183  34.361  1.00 22.14  ? 333 ARG B C   1 
ATOM   6871  O O   . ARG B 1 333 ? 5.404   24.162  33.795  1.00 20.81  ? 333 ARG B O   1 
ATOM   6872  C CB  . ARG B 1 333 ? 2.283   23.203  33.241  1.00 20.55  ? 333 ARG B CB  1 
ATOM   6873  C CG  . ARG B 1 333 ? 1.780   21.915  32.619  1.00 21.88  ? 333 ARG B CG  1 
ATOM   6874  C CD  . ARG B 1 333 ? 0.573   22.152  31.737  1.00 21.22  ? 333 ARG B CD  1 
ATOM   6875  N NE  . ARG B 1 333 ? 0.706   21.452  30.466  1.00 29.93  ? 333 ARG B NE  1 
ATOM   6876  C CZ  . ARG B 1 333 ? 0.169   20.268  30.205  1.00 23.71  ? 333 ARG B CZ  1 
ATOM   6877  N NH1 . ARG B 1 333 ? -0.554  19.624  31.107  1.00 27.41  ? 333 ARG B NH1 1 
ATOM   6878  N NH2 . ARG B 1 333 ? 0.369   19.714  29.013  1.00 24.70  ? 333 ARG B NH2 1 
ATOM   6879  N N   . LEU B 1 334 ? 3.877   25.243  35.056  1.00 24.96  ? 334 LEU B N   1 
ATOM   6880  C CA  . LEU B 1 334 ? 4.753   26.391  35.275  1.00 24.23  ? 334 LEU B CA  1 
ATOM   6881  C C   . LEU B 1 334 ? 6.046   25.967  35.959  1.00 24.28  ? 334 LEU B C   1 
ATOM   6882  O O   . LEU B 1 334 ? 7.130   26.459  35.621  1.00 21.60  ? 334 LEU B O   1 
ATOM   6883  C CB  . LEU B 1 334 ? 4.035   27.448  36.114  1.00 18.14  ? 334 LEU B CB  1 
ATOM   6884  C CG  . LEU B 1 334 ? 2.984   28.328  35.440  1.00 21.77  ? 334 LEU B CG  1 
ATOM   6885  C CD1 . LEU B 1 334 ? 2.571   29.457  36.374  1.00 16.60  ? 334 LEU B CD1 1 
ATOM   6886  C CD2 . LEU B 1 334 ? 3.499   28.881  34.121  1.00 20.77  ? 334 LEU B CD2 1 
ATOM   6887  N N   . LYS B 1 335 ? 5.943   25.050  36.924  1.00 26.49  ? 335 LYS B N   1 
ATOM   6888  C CA  . LYS B 1 335 ? 7.121   24.520  37.602  1.00 23.00  ? 335 LYS B CA  1 
ATOM   6889  C C   . LYS B 1 335 ? 8.116   23.945  36.605  1.00 24.50  ? 335 LYS B C   1 
ATOM   6890  O O   . LYS B 1 335 ? 9.320   24.215  36.681  1.00 26.62  ? 335 LYS B O   1 
ATOM   6891  C CB  . LYS B 1 335 ? 6.697   23.447  38.607  1.00 26.90  ? 335 LYS B CB  1 
ATOM   6892  C CG  . LYS B 1 335 ? 6.800   23.861  40.060  1.00 34.92  ? 335 LYS B CG  1 
ATOM   6893  C CD  . LYS B 1 335 ? 5.957   22.956  40.942  1.00 35.23  ? 335 LYS B CD  1 
ATOM   6894  C CE  . LYS B 1 335 ? 5.491   23.688  42.190  1.00 37.73  ? 335 LYS B CE  1 
ATOM   6895  N NZ  . LYS B 1 335 ? 4.598   22.847  43.034  1.00 43.92  ? 335 LYS B NZ  1 
ATOM   6896  N N   . LYS B 1 336 ? 7.625   23.149  35.655  1.00 28.45  ? 336 LYS B N   1 
ATOM   6897  C CA  . LYS B 1 336 ? 8.519   22.482  34.718  1.00 30.30  ? 336 LYS B CA  1 
ATOM   6898  C C   . LYS B 1 336 ? 9.105   23.451  33.701  1.00 29.77  ? 336 LYS B C   1 
ATOM   6899  O O   . LYS B 1 336 ? 10.192  23.200  33.172  1.00 33.14  ? 336 LYS B O   1 
ATOM   6900  C CB  . LYS B 1 336 ? 7.784   21.328  34.036  1.00 30.63  ? 336 LYS B CB  1 
ATOM   6901  C CG  . LYS B 1 336 ? 7.640   20.119  34.950  1.00 37.80  ? 336 LYS B CG  1 
ATOM   6902  C CD  . LYS B 1 336 ? 6.575   19.147  34.483  1.00 28.06  ? 336 LYS B CD  1 
ATOM   6903  C CE  . LYS B 1 336 ? 6.635   17.864  35.298  1.00 47.31  ? 336 LYS B CE  1 
ATOM   6904  N NZ  . LYS B 1 336 ? 5.305   17.462  35.831  1.00 53.63  ? 336 LYS B NZ  1 
ATOM   6905  N N   . ILE B 1 337 ? 8.413   24.555  33.415  1.00 25.94  ? 337 ILE B N   1 
ATOM   6906  C CA  . ILE B 1 337 ? 9.037   25.639  32.663  1.00 21.23  ? 337 ILE B CA  1 
ATOM   6907  C C   . ILE B 1 337 ? 10.158  26.263  33.481  1.00 21.66  ? 337 ILE B C   1 
ATOM   6908  O O   . ILE B 1 337 ? 11.237  26.569  32.959  1.00 26.09  ? 337 ILE B O   1 
ATOM   6909  C CB  . ILE B 1 337 ? 7.986   26.690  32.261  1.00 19.50  ? 337 ILE B CB  1 
ATOM   6910  C CG1 . ILE B 1 337 ? 6.917   26.071  31.363  1.00 19.30  ? 337 ILE B CG1 1 
ATOM   6911  C CG2 . ILE B 1 337 ? 8.651   27.876  31.568  1.00 18.87  ? 337 ILE B CG2 1 
ATOM   6912  C CD1 . ILE B 1 337 ? 5.642   26.870  31.316  1.00 17.91  ? 337 ILE B CD1 1 
ATOM   6913  N N   . HIS B 1 338 ? 9.916   26.452  34.780  1.00 21.71  ? 338 HIS B N   1 
ATOM   6914  C CA  . HIS B 1 338 ? 10.869  27.139  35.646  1.00 23.03  ? 338 HIS B CA  1 
ATOM   6915  C C   . HIS B 1 338 ? 12.181  26.371  35.748  1.00 29.19  ? 338 HIS B C   1 
ATOM   6916  O O   . HIS B 1 338 ? 13.265  26.952  35.610  1.00 31.55  ? 338 HIS B O   1 
ATOM   6917  C CB  . HIS B 1 338 ? 10.238  27.337  37.024  1.00 24.96  ? 338 HIS B CB  1 
ATOM   6918  C CG  . HIS B 1 338 ? 11.118  28.041  38.008  1.00 28.49  ? 338 HIS B CG  1 
ATOM   6919  N ND1 . HIS B 1 338 ? 12.034  27.377  38.796  1.00 27.33  ? 338 HIS B ND1 1 
ATOM   6920  C CD2 . HIS B 1 338 ? 11.210  29.350  38.347  1.00 27.75  ? 338 HIS B CD2 1 
ATOM   6921  C CE1 . HIS B 1 338 ? 12.658  28.247  39.570  1.00 25.28  ? 338 HIS B CE1 1 
ATOM   6922  N NE2 . HIS B 1 338 ? 12.177  29.451  39.318  1.00 31.24  ? 338 HIS B NE2 1 
ATOM   6923  N N   . GLU B 1 339 ? 12.106  25.059  35.972  1.00 31.03  ? 339 GLU B N   1 
ATOM   6924  C CA  . GLU B 1 339 ? 13.294  24.222  36.088  1.00 27.30  ? 339 GLU B CA  1 
ATOM   6925  C C   . GLU B 1 339 ? 13.669  23.565  34.764  1.00 27.86  ? 339 GLU B C   1 
ATOM   6926  O O   . GLU B 1 339 ? 14.203  22.452  34.751  1.00 44.25  ? 339 GLU B O   1 
ATOM   6927  C CB  . GLU B 1 339 ? 13.108  23.169  37.183  1.00 36.89  ? 339 GLU B CB  1 
ATOM   6928  C CG  . GLU B 1 339 ? 11.871  22.295  37.051  1.00 51.18  ? 339 GLU B CG  1 
ATOM   6929  C CD  . GLU B 1 339 ? 11.290  21.909  38.403  1.00 58.61  ? 339 GLU B CD  1 
ATOM   6930  O OE1 . GLU B 1 339 ? 11.586  22.599  39.403  1.00 50.97  ? 339 GLU B OE1 1 
ATOM   6931  O OE2 . GLU B 1 339 ? 10.546  20.908  38.468  1.00 49.42  ? 339 GLU B OE2 1 
ATOM   6932  N N   . SER B 1 340 ? 13.387  24.236  33.645  1.00 29.33  ? 340 SER B N   1 
ATOM   6933  C CA  . SER B 1 340 ? 13.834  23.802  32.328  1.00 31.51  ? 340 SER B CA  1 
ATOM   6934  C C   . SER B 1 340 ? 14.723  24.812  31.621  1.00 32.16  ? 340 SER B C   1 
ATOM   6935  O O   . SER B 1 340 ? 15.235  24.502  30.539  1.00 37.98  ? 340 SER B O   1 
ATOM   6936  C CB  . SER B 1 340 ? 12.635  23.494  31.417  1.00 32.02  ? 340 SER B CB  1 
ATOM   6937  O OG  . SER B 1 340 ? 12.225  24.656  30.713  1.00 25.55  ? 340 SER B OG  1 
ATOM   6938  N N   . VAL B 1 341 ? 14.910  26.005  32.180  1.00 33.95  ? 341 VAL B N   1 
ATOM   6939  C CA  . VAL B 1 341 ? 15.738  27.039  31.575  1.00 30.05  ? 341 VAL B CA  1 
ATOM   6940  C C   . VAL B 1 341 ? 16.706  27.563  32.625  1.00 34.14  ? 341 VAL B C   1 
ATOM   6941  O O   . VAL B 1 341 ? 16.452  27.478  33.831  1.00 41.36  ? 341 VAL B O   1 
ATOM   6942  C CB  . VAL B 1 341 ? 14.887  28.192  30.991  1.00 23.98  ? 341 VAL B CB  1 
ATOM   6943  C CG1 . VAL B 1 341 ? 13.954  27.672  29.906  1.00 23.35  ? 341 VAL B CG1 1 
ATOM   6944  C CG2 . VAL B 1 341 ? 14.097  28.877  32.092  1.00 26.36  ? 341 VAL B CG2 1 
ATOM   6945  N N   . ASP B 1 342 ? 17.832  28.101  32.158  1.00 37.14  ? 342 ASP B N   1 
ATOM   6946  C CA  . ASP B 1 342 ? 18.839  28.647  33.059  1.00 36.95  ? 342 ASP B CA  1 
ATOM   6947  C C   . ASP B 1 342 ? 18.580  30.104  33.410  1.00 36.96  ? 342 ASP B C   1 
ATOM   6948  O O   . ASP B 1 342 ? 19.021  30.570  34.468  1.00 44.77  ? 342 ASP B O   1 
ATOM   6949  C CB  . ASP B 1 342 ? 20.230  28.500  32.440  1.00 35.96  ? 342 ASP B CB  1 
ATOM   6950  C CG  . ASP B 1 342 ? 20.649  27.049  32.301  1.00 48.50  ? 342 ASP B CG  1 
ATOM   6951  O OD1 . ASP B 1 342 ? 20.348  26.255  33.217  1.00 50.92  ? 342 ASP B OD1 1 
ATOM   6952  O OD2 . ASP B 1 342 ? 21.276  26.701  31.279  1.00 59.87  ? 342 ASP B OD2 1 
ATOM   6953  N N   . PHE B 1 343 ? 17.875  30.828  32.548  1.00 29.87  ? 343 PHE B N   1 
ATOM   6954  C CA  . PHE B 1 343 ? 17.501  32.210  32.791  1.00 24.97  ? 343 PHE B CA  1 
ATOM   6955  C C   . PHE B 1 343 ? 16.172  32.261  33.539  1.00 28.03  ? 343 PHE B C   1 
ATOM   6956  O O   . PHE B 1 343 ? 15.579  31.234  33.877  1.00 29.39  ? 343 PHE B O   1 
ATOM   6957  C CB  . PHE B 1 343 ? 17.410  32.975  31.472  1.00 24.29  ? 343 PHE B CB  1 
ATOM   6958  C CG  . PHE B 1 343 ? 16.563  32.287  30.436  1.00 24.30  ? 343 PHE B CG  1 
ATOM   6959  C CD1 . PHE B 1 343 ? 17.099  31.299  29.626  1.00 24.42  ? 343 PHE B CD1 1 
ATOM   6960  C CD2 . PHE B 1 343 ? 15.227  32.617  30.284  1.00 25.91  ? 343 PHE B CD2 1 
ATOM   6961  C CE1 . PHE B 1 343 ? 16.323  30.661  28.680  1.00 23.87  ? 343 PHE B CE1 1 
ATOM   6962  C CE2 . PHE B 1 343 ? 14.448  31.981  29.337  1.00 27.67  ? 343 PHE B CE2 1 
ATOM   6963  C CZ  . PHE B 1 343 ? 14.997  31.000  28.537  1.00 22.25  ? 343 PHE B CZ  1 
ATOM   6964  N N   . GLN B 1 344 ? 15.691  33.474  33.798  1.00 30.03  ? 344 GLN B N   1 
ATOM   6965  C CA  . GLN B 1 344 ? 14.363  33.652  34.367  1.00 24.06  ? 344 GLN B CA  1 
ATOM   6966  C C   . GLN B 1 344 ? 13.360  33.808  33.235  1.00 24.39  ? 344 GLN B C   1 
ATOM   6967  O O   . GLN B 1 344 ? 13.431  34.795  32.495  1.00 26.89  ? 344 GLN B O   1 
ATOM   6968  C CB  . GLN B 1 344 ? 14.330  34.861  35.287  1.00 21.66  ? 344 GLN B CB  1 
ATOM   6969  C CG  . GLN B 1 344 ? 15.166  34.670  36.544  1.00 29.16  ? 344 GLN B CG  1 
ATOM   6970  C CD  . GLN B 1 344 ? 15.023  35.800  37.543  1.00 31.60  ? 344 GLN B CD  1 
ATOM   6971  O OE1 . GLN B 1 344 ? 14.233  35.719  38.482  1.00 32.28  ? 344 GLN B OE1 1 
ATOM   6972  N NE2 . GLN B 1 344 ? 15.810  36.851  37.361  1.00 30.62  ? 344 GLN B NE2 1 
ATOM   6973  N N   . PRO B 1 345 ? 12.435  32.872  33.055  1.00 21.16  ? 345 PRO B N   1 
ATOM   6974  C CA  . PRO B 1 345 ? 11.536  32.936  31.902  1.00 18.35  ? 345 PRO B CA  1 
ATOM   6975  C C   . PRO B 1 345 ? 10.378  33.889  32.131  1.00 19.44  ? 345 PRO B C   1 
ATOM   6976  O O   . PRO B 1 345 ? 9.946   34.131  33.260  1.00 19.20  ? 345 PRO B O   1 
ATOM   6977  C CB  . PRO B 1 345 ? 11.036  31.493  31.767  1.00 18.47  ? 345 PRO B CB  1 
ATOM   6978  C CG  . PRO B 1 345 ? 11.093  30.945  33.159  1.00 19.08  ? 345 PRO B CG  1 
ATOM   6979  C CD  . PRO B 1 345 ? 12.137  31.724  33.931  1.00 19.86  ? 345 PRO B CD  1 
ATOM   6980  N N   . VAL B 1 346 ? 9.873   34.430  31.026  1.00 19.73  ? 346 VAL B N   1 
ATOM   6981  C CA  . VAL B 1 346 ? 8.630   35.190  31.014  1.00 15.49  ? 346 VAL B CA  1 
ATOM   6982  C C   . VAL B 1 346 ? 7.592   34.365  30.263  1.00 16.06  ? 346 VAL B C   1 
ATOM   6983  O O   . VAL B 1 346 ? 7.848   33.884  29.152  1.00 21.18  ? 346 VAL B O   1 
ATOM   6984  C CB  . VAL B 1 346 ? 8.823   36.599  30.414  1.00 15.44  ? 346 VAL B CB  1 
ATOM   6985  C CG1 . VAL B 1 346 ? 8.936   36.579  28.891  1.00 17.07  ? 346 VAL B CG1 1 
ATOM   6986  C CG2 . VAL B 1 346 ? 7.697   37.521  30.856  1.00 14.79  ? 346 VAL B CG2 1 
ATOM   6987  N N   . VAL B 1 347 ? 6.450   34.137  30.900  1.00 16.00  ? 347 VAL B N   1 
ATOM   6988  C CA  . VAL B 1 347 ? 5.407   33.284  30.350  1.00 14.15  ? 347 VAL B CA  1 
ATOM   6989  C C   . VAL B 1 347 ? 4.185   34.148  30.091  1.00 14.86  ? 347 VAL B C   1 
ATOM   6990  O O   . VAL B 1 347 ? 3.597   34.702  31.028  1.00 14.57  ? 347 VAL B O   1 
ATOM   6991  C CB  . VAL B 1 347 ? 5.071   32.117  31.289  1.00 14.35  ? 347 VAL B CB  1 
ATOM   6992  C CG1 . VAL B 1 347 ? 4.092   31.182  30.620  1.00 16.26  ? 347 VAL B CG1 1 
ATOM   6993  C CG2 . VAL B 1 347 ? 6.337   31.372  31.682  1.00 16.33  ? 347 VAL B CG2 1 
ATOM   6994  N N   . PHE B 1 348 ? 3.802   34.256  28.823  1.00 18.44  ? 348 PHE B N   1 
ATOM   6995  C CA  . PHE B 1 348 ? 2.670   35.070  28.406  1.00 15.34  ? 348 PHE B CA  1 
ATOM   6996  C C   . PHE B 1 348 ? 1.467   34.171  28.156  1.00 16.03  ? 348 PHE B C   1 
ATOM   6997  O O   . PHE B 1 348 ? 1.554   33.211  27.385  1.00 17.62  ? 348 PHE B O   1 
ATOM   6998  C CB  . PHE B 1 348 ? 3.013   35.868  27.148  1.00 12.74  ? 348 PHE B CB  1 
ATOM   6999  C CG  . PHE B 1 348 ? 3.312   37.314  27.416  1.00 12.74  ? 348 PHE B CG  1 
ATOM   7000  C CD1 . PHE B 1 348 ? 4.525   37.696  27.964  1.00 17.24  ? 348 PHE B CD1 1 
ATOM   7001  C CD2 . PHE B 1 348 ? 2.382   38.292  27.118  1.00 17.30  ? 348 PHE B CD2 1 
ATOM   7002  C CE1 . PHE B 1 348 ? 4.798   39.027  28.214  1.00 21.54  ? 348 PHE B CE1 1 
ATOM   7003  C CE2 . PHE B 1 348 ? 2.651   39.623  27.362  1.00 15.52  ? 348 PHE B CE2 1 
ATOM   7004  C CZ  . PHE B 1 348 ? 3.859   39.992  27.910  1.00 14.31  ? 348 PHE B CZ  1 
ATOM   7005  N N   . VAL B 1 349 ? 0.355   34.482  28.813  1.00 14.10  ? 349 VAL B N   1 
ATOM   7006  C CA  . VAL B 1 349 ? -0.882  33.718  28.696  1.00 13.03  ? 349 VAL B CA  1 
ATOM   7007  C C   . VAL B 1 349 ? -1.916  34.652  28.082  1.00 15.21  ? 349 VAL B C   1 
ATOM   7008  O O   . VAL B 1 349 ? -2.512  35.483  28.780  1.00 17.18  ? 349 VAL B O   1 
ATOM   7009  C CB  . VAL B 1 349 ? -1.350  33.167  30.047  1.00 15.41  ? 349 VAL B CB  1 
ATOM   7010  C CG1 . VAL B 1 349 ? -2.575  32.284  29.868  1.00 14.27  ? 349 VAL B CG1 1 
ATOM   7011  C CG2 . VAL B 1 349 ? -0.225  32.396  30.717  1.00 19.43  ? 349 VAL B CG2 1 
ATOM   7012  N N   . VAL B 1 350 ? -2.131  34.522  26.776  1.00 12.24  ? 350 VAL B N   1 
ATOM   7013  C CA  . VAL B 1 350 ? -3.021  35.396  26.020  1.00 12.30  ? 350 VAL B CA  1 
ATOM   7014  C C   . VAL B 1 350 ? -4.122  34.538  25.412  1.00 12.75  ? 350 VAL B C   1 
ATOM   7015  O O   . VAL B 1 350 ? -3.838  33.598  24.659  1.00 13.25  ? 350 VAL B O   1 
ATOM   7016  C CB  . VAL B 1 350 ? -2.268  36.166  24.923  1.00 12.53  ? 350 VAL B CB  1 
ATOM   7017  C CG1 . VAL B 1 350 ? -3.188  37.179  24.256  1.00 12.77  ? 350 VAL B CG1 1 
ATOM   7018  C CG2 . VAL B 1 350 ? -1.028  36.841  25.495  1.00 12.32  ? 350 VAL B CG2 1 
ATOM   7019  N N   . LEU B 1 351 ? -5.370  34.865  25.729  1.00 12.79  ? 351 LEU B N   1 
ATOM   7020  C CA  . LEU B 1 351 ? -6.511  34.168  25.153  1.00 13.42  ? 351 LEU B CA  1 
ATOM   7021  C C   . LEU B 1 351 ? -7.751  35.029  25.338  1.00 16.14  ? 351 LEU B C   1 
ATOM   7022  O O   . LEU B 1 351 ? -7.757  35.983  26.121  1.00 13.16  ? 351 LEU B O   1 
ATOM   7023  C CB  . LEU B 1 351 ? -6.703  32.782  25.779  1.00 15.94  ? 351 LEU B CB  1 
ATOM   7024  C CG  . LEU B 1 351 ? -7.295  32.725  27.187  1.00 18.45  ? 351 LEU B CG  1 
ATOM   7025  C CD1 . LEU B 1 351 ? -8.190  31.508  27.328  1.00 17.49  ? 351 LEU B CD1 1 
ATOM   7026  C CD2 . LEU B 1 351 ? -6.194  32.706  28.236  1.00 13.00  ? 351 LEU B CD2 1 
ATOM   7027  N N   . ASP B 1 352 ? -8.805  34.676  24.602  1.00 26.32  ? 352 ASP B N   1 
ATOM   7028  C CA  . ASP B 1 352 ? -10.064 35.404  24.694  1.00 25.46  ? 352 ASP B CA  1 
ATOM   7029  C C   . ASP B 1 352 ? -10.575 35.373  26.125  1.00 25.82  ? 352 ASP B C   1 
ATOM   7030  O O   . ASP B 1 352 ? -10.741 34.303  26.719  1.00 28.42  ? 352 ASP B O   1 
ATOM   7031  C CB  . ASP B 1 352 ? -11.098 34.798  23.745  1.00 28.92  ? 352 ASP B CB  1 
ATOM   7032  C CG  . ASP B 1 352 ? -10.684 34.898  22.290  1.00 39.86  ? 352 ASP B CG  1 
ATOM   7033  O OD1 . ASP B 1 352 ? -9.912  34.032  21.826  1.00 50.77  ? 352 ASP B OD1 1 
ATOM   7034  O OD2 . ASP B 1 352 ? -11.135 35.843  21.608  1.00 46.05  ? 352 ASP B OD2 1 
ATOM   7035  N N   . GLY B 1 353 ? -10.829 36.550  26.677  1.00 16.40  ? 353 GLY B N   1 
ATOM   7036  C CA  . GLY B 1 353 ? -11.117 36.630  28.093  1.00 18.99  ? 353 GLY B CA  1 
ATOM   7037  C C   . GLY B 1 353 ? -12.532 36.327  28.518  1.00 25.58  ? 353 GLY B C   1 
ATOM   7038  O O   . GLY B 1 353 ? -12.810 36.375  29.726  1.00 28.91  ? 353 GLY B O   1 
ATOM   7039  N N   . GLU B 1 354 ? -13.439 36.013  27.585  1.00 25.78  ? 354 GLU B N   1 
ATOM   7040  C CA  . GLU B 1 354 ? -14.843 35.843  27.953  1.00 21.92  ? 354 GLU B CA  1 
ATOM   7041  C C   . GLU B 1 354 ? -15.562 34.659  27.312  1.00 23.96  ? 354 GLU B C   1 
ATOM   7042  O O   . GLU B 1 354 ? -16.747 34.477  27.582  1.00 30.41  ? 354 GLU B O   1 
ATOM   7043  C CB  . GLU B 1 354 ? -15.618 37.134  27.646  1.00 25.02  ? 354 GLU B CB  1 
ATOM   7044  C CG  . GLU B 1 354 ? -16.037 37.342  26.186  1.00 26.60  ? 354 GLU B CG  1 
ATOM   7045  C CD  . GLU B 1 354 ? -14.934 38.017  25.388  1.00 26.48  ? 354 GLU B CD  1 
ATOM   7046  O OE1 . GLU B 1 354 ? -13.930 37.358  25.084  1.00 32.48  ? 354 GLU B OE1 1 
ATOM   7047  O OE2 . GLU B 1 354 ? -15.060 39.228  25.089  1.00 20.80  ? 354 GLU B OE2 1 
ATOM   7048  N N   . ASN B 1 355 ? -14.901 33.853  26.478  1.00 25.80  ? 355 ASN B N   1 
ATOM   7049  C CA  . ASN B 1 355 ? -15.591 32.769  25.785  1.00 26.56  ? 355 ASN B CA  1 
ATOM   7050  C C   . ASN B 1 355 ? -15.607 31.463  26.574  1.00 29.43  ? 355 ASN B C   1 
ATOM   7051  O O   . ASN B 1 355 ? -16.543 30.664  26.428  1.00 25.38  ? 355 ASN B O   1 
ATOM   7052  C CB  . ASN B 1 355 ? -14.948 32.505  24.427  1.00 26.18  ? 355 ASN B CB  1 
ATOM   7053  C CG  . ASN B 1 355 ? -15.330 33.536  23.394  1.00 31.28  ? 355 ASN B CG  1 
ATOM   7054  O OD1 . ASN B 1 355 ? -16.489 33.911  23.274  1.00 36.60  ? 355 ASN B OD1 1 
ATOM   7055  N ND2 . ASN B 1 355 ? -14.347 33.976  22.607  1.00 42.19  ? 355 ASN B ND2 1 
ATOM   7056  N N   . CYS B 1 356 ? -14.574 31.204  27.377  1.00 31.16  ? 356 CYS B N   1 
ATOM   7057  C CA  . CYS B 1 356 ? -14.382 29.871  27.939  1.00 27.95  ? 356 CYS B CA  1 
ATOM   7058  C C   . CYS B 1 356 ? -15.265 29.610  29.152  1.00 20.74  ? 356 CYS B C   1 
ATOM   7059  O O   . CYS B 1 356 ? -15.637 28.459  29.405  1.00 30.90  ? 356 CYS B O   1 
ATOM   7060  C CB  . CYS B 1 356 ? -12.910 29.681  28.303  1.00 22.49  ? 356 CYS B CB  1 
ATOM   7061  S SG  . CYS B 1 356 ? -12.065 31.204  28.809  1.00 28.33  ? 356 CYS B SG  1 
ATOM   7062  N N   . TRP B 1 357 ? -15.616 30.653  29.903  1.00 18.71  ? 357 TRP B N   1 
ATOM   7063  C CA  . TRP B 1 357 ? -16.181 30.462  31.232  1.00 19.26  ? 357 TRP B CA  1 
ATOM   7064  C C   . TRP B 1 357 ? -17.633 30.004  31.222  1.00 25.67  ? 357 TRP B C   1 
ATOM   7065  O O   . TRP B 1 357 ? -18.102 29.478  32.236  1.00 32.57  ? 357 TRP B O   1 
ATOM   7066  C CB  . TRP B 1 357 ? -16.032 31.751  32.039  1.00 18.58  ? 357 TRP B CB  1 
ATOM   7067  C CG  . TRP B 1 357 ? -14.693 32.389  31.832  1.00 18.24  ? 357 TRP B CG  1 
ATOM   7068  C CD1 . TRP B 1 357 ? -14.436 33.583  31.224  1.00 18.78  ? 357 TRP B CD1 1 
ATOM   7069  C CD2 . TRP B 1 357 ? -13.420 31.846  32.208  1.00 21.27  ? 357 TRP B CD2 1 
ATOM   7070  N NE1 . TRP B 1 357 ? -13.082 33.823  31.209  1.00 20.97  ? 357 TRP B NE1 1 
ATOM   7071  C CE2 . TRP B 1 357 ? -12.437 32.772  31.808  1.00 24.19  ? 357 TRP B CE2 1 
ATOM   7072  C CE3 . TRP B 1 357 ? -13.018 30.671  32.850  1.00 24.00  ? 357 TRP B CE3 1 
ATOM   7073  C CZ2 . TRP B 1 357 ? -11.074 32.555  32.028  1.00 16.51  ? 357 TRP B CZ2 1 
ATOM   7074  C CZ3 . TRP B 1 357 ? -11.667 30.459  33.069  1.00 16.29  ? 357 TRP B CZ3 1 
ATOM   7075  C CH2 . TRP B 1 357 ? -10.712 31.397  32.660  1.00 15.26  ? 357 TRP B CH2 1 
ATOM   7076  N N   . GLU B 1 358 ? -18.358 30.177  30.115  1.00 27.80  ? 358 GLU B N   1 
ATOM   7077  C CA  . GLU B 1 358 ? -19.705 29.618  30.052  1.00 25.31  ? 358 GLU B CA  1 
ATOM   7078  C C   . GLU B 1 358 ? -19.687 28.097  30.089  1.00 24.13  ? 358 GLU B C   1 
ATOM   7079  O O   . GLU B 1 358 ? -20.682 27.485  30.488  1.00 25.65  ? 358 GLU B O   1 
ATOM   7080  C CB  . GLU B 1 358 ? -20.440 30.104  28.799  1.00 25.38  ? 358 GLU B CB  1 
ATOM   7081  C CG  . GLU B 1 358 ? -19.569 30.264  27.567  1.00 30.35  ? 358 GLU B CG  1 
ATOM   7082  C CD  . GLU B 1 358 ? -19.196 31.708  27.314  1.00 36.50  ? 358 GLU B CD  1 
ATOM   7083  O OE1 . GLU B 1 358 ? -19.087 32.097  26.133  1.00 45.98  ? 358 GLU B OE1 1 
ATOM   7084  O OE2 . GLU B 1 358 ? -19.010 32.454  28.301  1.00 24.32  ? 358 GLU B OE2 1 
ATOM   7085  N N   . TYR B 1 359 ? -18.579 27.477  29.686  1.00 24.73  ? 359 TYR B N   1 
ATOM   7086  C CA  . TYR B 1 359 ? -18.437 26.029  29.724  1.00 24.62  ? 359 TYR B CA  1 
ATOM   7087  C C   . TYR B 1 359 ? -17.833 25.522  31.026  1.00 24.42  ? 359 TYR B C   1 
ATOM   7088  O O   . TYR B 1 359 ? -17.892 24.318  31.289  1.00 32.22  ? 359 TYR B O   1 
ATOM   7089  C CB  . TYR B 1 359 ? -17.582 25.560  28.545  1.00 24.45  ? 359 TYR B CB  1 
ATOM   7090  C CG  . TYR B 1 359 ? -18.111 26.032  27.214  1.00 24.85  ? 359 TYR B CG  1 
ATOM   7091  C CD1 . TYR B 1 359 ? -19.215 25.428  26.632  1.00 26.75  ? 359 TYR B CD1 1 
ATOM   7092  C CD2 . TYR B 1 359 ? -17.521 27.101  26.552  1.00 26.43  ? 359 TYR B CD2 1 
ATOM   7093  C CE1 . TYR B 1 359 ? -19.709 25.863  25.420  1.00 27.34  ? 359 TYR B CE1 1 
ATOM   7094  C CE2 . TYR B 1 359 ? -18.008 27.545  25.339  1.00 24.12  ? 359 TYR B CE2 1 
ATOM   7095  C CZ  . TYR B 1 359 ? -19.102 26.922  24.778  1.00 26.02  ? 359 TYR B CZ  1 
ATOM   7096  O OH  . TYR B 1 359 ? -19.590 27.361  23.570  1.00 34.17  ? 359 TYR B OH  1 
ATOM   7097  N N   . TYR B 1 360 ? -17.255 26.401  31.838  1.00 23.08  ? 360 TYR B N   1 
ATOM   7098  C CA  . TYR B 1 360 ? -16.783 26.008  33.154  1.00 23.13  ? 360 TYR B CA  1 
ATOM   7099  C C   . TYR B 1 360 ? -17.957 25.889  34.117  1.00 24.47  ? 360 TYR B C   1 
ATOM   7100  O O   . TYR B 1 360 ? -19.020 26.486  33.923  1.00 24.94  ? 360 TYR B O   1 
ATOM   7101  C CB  . TYR B 1 360 ? -15.787 27.025  33.712  1.00 27.70  ? 360 TYR B CB  1 
ATOM   7102  C CG  . TYR B 1 360 ? -14.372 26.908  33.195  1.00 23.84  ? 360 TYR B CG  1 
ATOM   7103  C CD1 . TYR B 1 360 ? -14.063 27.237  31.883  1.00 23.59  ? 360 TYR B CD1 1 
ATOM   7104  C CD2 . TYR B 1 360 ? -13.342 26.489  34.026  1.00 20.24  ? 360 TYR B CD2 1 
ATOM   7105  C CE1 . TYR B 1 360 ? -12.770 27.142  31.407  1.00 19.29  ? 360 TYR B CE1 1 
ATOM   7106  C CE2 . TYR B 1 360 ? -12.045 26.390  33.559  1.00 21.13  ? 360 TYR B CE2 1 
ATOM   7107  C CZ  . TYR B 1 360 ? -11.765 26.718  32.249  1.00 19.30  ? 360 TYR B CZ  1 
ATOM   7108  O OH  . TYR B 1 360 ? -10.478 26.625  31.773  1.00 18.16  ? 360 TYR B OH  1 
ATOM   7109  N N   . GLU B 1 361 ? -17.754 25.105  35.171  1.00 25.27  ? 361 GLU B N   1 
ATOM   7110  C CA  . GLU B 1 361 ? -18.711 25.079  36.266  1.00 26.56  ? 361 GLU B CA  1 
ATOM   7111  C C   . GLU B 1 361 ? -18.716 26.429  36.972  1.00 25.64  ? 361 GLU B C   1 
ATOM   7112  O O   . GLU B 1 361 ? -17.656 26.979  37.285  1.00 24.33  ? 361 GLU B O   1 
ATOM   7113  C CB  . GLU B 1 361 ? -18.369 23.963  37.251  1.00 32.96  ? 361 GLU B CB  1 
ATOM   7114  C CG  . GLU B 1 361 ? -18.292 22.587  36.616  1.00 44.77  ? 361 GLU B CG  1 
ATOM   7115  C CD  . GLU B 1 361 ? -19.657 21.955  36.447  1.00 48.73  ? 361 GLU B CD  1 
ATOM   7116  O OE1 . GLU B 1 361 ? -20.472 22.051  37.388  1.00 46.05  ? 361 GLU B OE1 1 
ATOM   7117  O OE2 . GLU B 1 361 ? -19.918 21.374  35.373  1.00 57.51  ? 361 GLU B OE2 1 
ATOM   7118  N N   . GLU B 1 362 ? -19.914 26.963  37.213  1.00 31.23  ? 362 GLU B N   1 
ATOM   7119  C CA  . GLU B 1 362 ? -20.093 28.240  37.907  1.00 26.11  ? 362 GLU B CA  1 
ATOM   7120  C C   . GLU B 1 362 ? -19.287 29.360  37.253  1.00 24.26  ? 362 GLU B C   1 
ATOM   7121  O O   . GLU B 1 362 ? -18.637 30.159  37.930  1.00 26.74  ? 362 GLU B O   1 
ATOM   7122  C CB  . GLU B 1 362 ? -19.739 28.115  39.390  1.00 26.67  ? 362 GLU B CB  1 
ATOM   7123  C CG  . GLU B 1 362 ? -20.665 27.209  40.181  1.00 40.99  ? 362 GLU B CG  1 
ATOM   7124  C CD  . GLU B 1 362 ? -19.954 25.992  40.738  1.00 59.67  ? 362 GLU B CD  1 
ATOM   7125  O OE1 . GLU B 1 362 ? -19.655 25.066  39.954  1.00 53.81  ? 362 GLU B OE1 1 
ATOM   7126  O OE2 . GLU B 1 362 ? -19.691 25.964  41.959  1.00 54.97  ? 362 GLU B OE2 1 
ATOM   7127  N N   . ASN B 1 363 ? -19.319 29.406  35.918  1.00 23.71  ? 363 ASN B N   1 
ATOM   7128  C CA  . ASN B 1 363 ? -18.745 30.510  35.143  1.00 22.27  ? 363 ASN B CA  1 
ATOM   7129  C C   . ASN B 1 363 ? -17.244 30.665  35.388  1.00 25.65  ? 363 ASN B C   1 
ATOM   7130  O O   . ASN B 1 363 ? -16.697 31.767  35.300  1.00 29.34  ? 363 ASN B O   1 
ATOM   7131  C CB  . ASN B 1 363 ? -19.480 31.823  35.437  1.00 22.54  ? 363 ASN B CB  1 
ATOM   7132  C CG  . ASN B 1 363 ? -19.189 32.904  34.414  1.00 24.00  ? 363 ASN B CG  1 
ATOM   7133  O OD1 . ASN B 1 363 ? -19.180 32.651  33.208  1.00 23.77  ? 363 ASN B OD1 1 
ATOM   7134  N ND2 . ASN B 1 363 ? -18.945 34.118  34.892  1.00 24.45  ? 363 ASN B ND2 1 
ATOM   7135  N N   . GLY B 1 364 ? -16.561 29.565  35.704  1.00 25.16  ? 364 GLY B N   1 
ATOM   7136  C CA  . GLY B 1 364 ? -15.141 29.605  35.985  1.00 23.07  ? 364 GLY B CA  1 
ATOM   7137  C C   . GLY B 1 364 ? -14.764 30.227  37.308  1.00 24.15  ? 364 GLY B C   1 
ATOM   7138  O O   . GLY B 1 364 ? -13.582 30.195  37.669  1.00 29.06  ? 364 GLY B O   1 
ATOM   7139  N N   . ILE B 1 365 ? -15.731 30.783  38.047  1.00 20.73  ? 365 ILE B N   1 
ATOM   7140  C CA  . ILE B 1 365 ? -15.407 31.468  39.303  1.00 20.96  ? 365 ILE B CA  1 
ATOM   7141  C C   . ILE B 1 365 ? -14.653 30.573  40.271  1.00 21.43  ? 365 ILE B C   1 
ATOM   7142  O O   . ILE B 1 365 ? -13.661 31.035  40.860  1.00 22.57  ? 365 ILE B O   1 
ATOM   7143  C CB  . ILE B 1 365 ? -16.675 32.082  39.909  1.00 22.18  ? 365 ILE B CB  1 
ATOM   7144  C CG1 . ILE B 1 365 ? -17.383 32.970  38.883  1.00 22.17  ? 365 ILE B CG1 1 
ATOM   7145  C CG2 . ILE B 1 365 ? -16.340 32.878  41.159  1.00 22.62  ? 365 ILE B CG2 1 
ATOM   7146  C CD1 . ILE B 1 365 ? -18.823 33.264  39.225  1.00 23.36  ? 365 ILE B CD1 1 
ATOM   7147  N N   . PRO B 1 366 ? -15.042 29.310  40.511  1.00 22.53  ? 366 PRO B N   1 
ATOM   7148  C CA  . PRO B 1 366 ? -14.208 28.466  41.386  1.00 23.10  ? 366 PRO B CA  1 
ATOM   7149  C C   . PRO B 1 366 ? -12.796 28.270  40.863  1.00 21.91  ? 366 PRO B C   1 
ATOM   7150  O O   . PRO B 1 366 ? -11.846 28.236  41.655  1.00 30.05  ? 366 PRO B O   1 
ATOM   7151  C CB  . PRO B 1 366 ? -14.982 27.141  41.445  1.00 24.60  ? 366 PRO B CB  1 
ATOM   7152  C CG  . PRO B 1 366 ? -16.373 27.485  41.061  1.00 25.14  ? 366 PRO B CG  1 
ATOM   7153  C CD  . PRO B 1 366 ? -16.263 28.604  40.079  1.00 23.59  ? 366 PRO B CD  1 
ATOM   7154  N N   . PHE B 1 367 ? -12.631 28.142  39.545  1.00 21.30  ? 367 PHE B N   1 
ATOM   7155  C CA  . PHE B 1 367 ? -11.303 27.928  38.979  1.00 20.05  ? 367 PHE B CA  1 
ATOM   7156  C C   . PHE B 1 367 ? -10.448 29.186  39.080  1.00 23.84  ? 367 PHE B C   1 
ATOM   7157  O O   . PHE B 1 367 ? -9.289  29.128  39.510  1.00 31.86  ? 367 PHE B O   1 
ATOM   7158  C CB  . PHE B 1 367 ? -11.425 27.471  37.525  1.00 24.82  ? 367 PHE B CB  1 
ATOM   7159  C CG  . PHE B 1 367 ? -10.136 27.535  36.757  1.00 18.53  ? 367 PHE B CG  1 
ATOM   7160  C CD1 . PHE B 1 367 ? -9.203  26.518  36.861  1.00 19.30  ? 367 PHE B CD1 1 
ATOM   7161  C CD2 . PHE B 1 367 ? -9.862  28.604  35.920  1.00 17.31  ? 367 PHE B CD2 1 
ATOM   7162  C CE1 . PHE B 1 367 ? -8.016  26.568  36.153  1.00 18.21  ? 367 PHE B CE1 1 
ATOM   7163  C CE2 . PHE B 1 367 ? -8.677  28.661  35.210  1.00 16.96  ? 367 PHE B CE2 1 
ATOM   7164  C CZ  . PHE B 1 367 ? -7.754  27.641  35.326  1.00 16.97  ? 367 PHE B CZ  1 
ATOM   7165  N N   . LEU B 1 368 ? -11.000 30.333  38.679  1.00 20.51  ? 368 LEU B N   1 
ATOM   7166  C CA  . LEU B 1 368 ? -10.225 31.570  38.695  1.00 17.35  ? 368 LEU B CA  1 
ATOM   7167  C C   . LEU B 1 368 ? -9.874  31.989  40.116  1.00 18.02  ? 368 LEU B C   1 
ATOM   7168  O O   . LEU B 1 368 ? -8.751  32.438  40.379  1.00 18.81  ? 368 LEU B O   1 
ATOM   7169  C CB  . LEU B 1 368 ? -10.991 32.684  37.981  1.00 16.92  ? 368 LEU B CB  1 
ATOM   7170  C CG  . LEU B 1 368 ? -11.113 32.523  36.465  1.00 16.24  ? 368 LEU B CG  1 
ATOM   7171  C CD1 . LEU B 1 368 ? -12.324 33.275  35.936  1.00 18.74  ? 368 LEU B CD1 1 
ATOM   7172  C CD2 . LEU B 1 368 ? -9.841  32.992  35.781  1.00 15.19  ? 368 LEU B CD2 1 
ATOM   7173  N N   . GLU B 1 369 ? -10.819 31.850  41.048  1.00 20.71  ? 369 GLU B N   1 
ATOM   7174  C CA  . GLU B 1 369 ? -10.542 32.206  42.435  1.00 20.61  ? 369 GLU B CA  1 
ATOM   7175  C C   . GLU B 1 369 ? -9.420  31.345  43.000  1.00 24.88  ? 369 GLU B C   1 
ATOM   7176  O O   . GLU B 1 369 ? -8.501  31.853  43.652  1.00 20.64  ? 369 GLU B O   1 
ATOM   7177  C CB  . GLU B 1 369 ? -11.814 32.074  43.276  1.00 21.64  ? 369 GLU B CB  1 
ATOM   7178  C CG  . GLU B 1 369 ? -12.760 33.263  43.149  1.00 28.68  ? 369 GLU B CG  1 
ATOM   7179  C CD  . GLU B 1 369 ? -14.002 33.134  44.013  1.00 32.65  ? 369 GLU B CD  1 
ATOM   7180  O OE1 . GLU B 1 369 ? -14.273 32.023  44.515  1.00 33.36  ? 369 GLU B OE1 1 
ATOM   7181  O OE2 . GLU B 1 369 ? -14.710 34.150  44.189  1.00 28.46  ? 369 GLU B OE2 1 
ATOM   7182  N N   . LYS B 1 370 ? -9.470  30.036  42.743  1.00 29.86  ? 370 LYS B N   1 
ATOM   7183  C CA  . LYS B 1 370 ? -8.412  29.145  43.211  1.00 28.55  ? 370 LYS B CA  1 
ATOM   7184  C C   . LYS B 1 370 ? -7.080  29.464  42.541  1.00 27.29  ? 370 LYS B C   1 
ATOM   7185  O O   . LYS B 1 370 ? -6.036  29.507  43.201  1.00 35.85  ? 370 LYS B O   1 
ATOM   7186  C CB  . LYS B 1 370 ? -8.804  27.687  42.958  1.00 27.70  ? 370 LYS B CB  1 
ATOM   7187  C CG  . LYS B 1 370 ? -7.793  26.673  43.474  1.00 30.88  ? 370 LYS B CG  1 
ATOM   7188  C CD  . LYS B 1 370 ? -8.478  25.547  44.232  1.00 45.33  ? 370 LYS B CD  1 
ATOM   7189  C CE  . LYS B 1 370 ? -9.027  26.031  45.566  1.00 35.22  ? 370 LYS B CE  1 
ATOM   7190  N NZ  . LYS B 1 370 ? -8.026  26.853  46.306  1.00 42.26  ? 370 LYS B NZ  1 
ATOM   7191  N N   . LEU B 1 371 ? -7.099  29.686  41.225  1.00 24.96  ? 371 LEU B N   1 
ATOM   7192  C CA  . LEU B 1 371 ? -5.863  29.951  40.492  1.00 19.11  ? 371 LEU B CA  1 
ATOM   7193  C C   . LEU B 1 371 ? -5.194  31.229  40.984  1.00 28.54  ? 371 LEU B C   1 
ATOM   7194  O O   . LEU B 1 371 ? -4.005  31.229  41.323  1.00 31.24  ? 371 LEU B O   1 
ATOM   7195  C CB  . LEU B 1 371 ? -6.155  30.028  38.992  1.00 16.88  ? 371 LEU B CB  1 
ATOM   7196  C CG  . LEU B 1 371 ? -5.083  30.599  38.057  1.00 15.83  ? 371 LEU B CG  1 
ATOM   7197  C CD1 . LEU B 1 371 ? -3.822  29.750  38.077  1.00 16.14  ? 371 LEU B CD1 1 
ATOM   7198  C CD2 . LEU B 1 371 ? -5.627  30.715  36.641  1.00 15.11  ? 371 LEU B CD2 1 
ATOM   7199  N N   . TYR B 1 372 ? -5.950  32.330  41.040  1.00 33.80  ? 372 TYR B N   1 
ATOM   7200  C CA  . TYR B 1 372 ? -5.380  33.597  41.489  1.00 26.12  ? 372 TYR B CA  1 
ATOM   7201  C C   . TYR B 1 372 ? -4.942  33.531  42.947  1.00 28.65  ? 372 TYR B C   1 
ATOM   7202  O O   . TYR B 1 372 ? -3.968  34.189  43.332  1.00 37.15  ? 372 TYR B O   1 
ATOM   7203  C CB  . TYR B 1 372 ? -6.387  34.732  41.298  1.00 21.80  ? 372 TYR B CB  1 
ATOM   7204  C CG  . TYR B 1 372 ? -6.762  35.026  39.860  1.00 20.06  ? 372 TYR B CG  1 
ATOM   7205  C CD1 . TYR B 1 372 ? -5.972  34.593  38.803  1.00 16.98  ? 372 TYR B CD1 1 
ATOM   7206  C CD2 . TYR B 1 372 ? -7.903  35.758  39.565  1.00 19.72  ? 372 TYR B CD2 1 
ATOM   7207  C CE1 . TYR B 1 372 ? -6.320  34.872  37.490  1.00 14.51  ? 372 TYR B CE1 1 
ATOM   7208  C CE2 . TYR B 1 372 ? -8.256  36.042  38.262  1.00 15.47  ? 372 TYR B CE2 1 
ATOM   7209  C CZ  . TYR B 1 372 ? -7.462  35.598  37.228  1.00 14.61  ? 372 TYR B CZ  1 
ATOM   7210  O OH  . TYR B 1 372 ? -7.818  35.884  35.930  1.00 14.05  ? 372 TYR B OH  1 
ATOM   7211  N N   . SER B 1 373 ? -5.647  32.750  43.772  1.00 27.45  ? 373 SER B N   1 
ATOM   7212  C CA  . SER B 1 373 ? -5.267  32.623  45.176  1.00 28.35  ? 373 SER B CA  1 
ATOM   7213  C C   . SER B 1 373 ? -4.007  31.786  45.345  1.00 34.31  ? 373 SER B C   1 
ATOM   7214  O O   . SER B 1 373 ? -3.265  31.977  46.314  1.00 38.16  ? 373 SER B O   1 
ATOM   7215  C CB  . SER B 1 373 ? -6.412  32.011  45.981  1.00 39.39  ? 373 SER B CB  1 
ATOM   7216  O OG  . SER B 1 373 ? -6.352  30.594  45.954  1.00 39.36  ? 373 SER B OG  1 
ATOM   7217  N N   . THR B 1 374 ? -3.764  30.842  44.437  1.00 34.14  ? 374 THR B N   1 
ATOM   7218  C CA  . THR B 1 374 ? -2.537  30.056  44.494  1.00 28.31  ? 374 THR B CA  1 
ATOM   7219  C C   . THR B 1 374 ? -1.344  30.857  43.984  1.00 26.94  ? 374 THR B C   1 
ATOM   7220  O O   . THR B 1 374 ? -0.240  30.751  44.532  1.00 25.52  ? 374 THR B O   1 
ATOM   7221  C CB  . THR B 1 374 ? -2.713  28.763  43.694  1.00 21.16  ? 374 THR B CB  1 
ATOM   7222  O OG1 . THR B 1 374 ? -3.461  27.824  44.476  1.00 25.09  ? 374 THR B OG1 1 
ATOM   7223  C CG2 . THR B 1 374 ? -1.369  28.152  43.335  1.00 21.26  ? 374 THR B CG2 1 
ATOM   7224  N N   . LEU B 1 375 ? -1.555  31.685  42.957  1.00 20.92  ? 375 LEU B N   1 
ATOM   7225  C CA  . LEU B 1 375 ? -0.460  32.468  42.395  1.00 18.48  ? 375 LEU B CA  1 
ATOM   7226  C C   . LEU B 1 375 ? 0.152   33.408  43.424  1.00 27.32  ? 375 LEU B C   1 
ATOM   7227  O O   . LEU B 1 375 ? 1.361   33.663  43.387  1.00 32.19  ? 375 LEU B O   1 
ATOM   7228  C CB  . LEU B 1 375 ? -0.947  33.260  41.181  1.00 17.13  ? 375 LEU B CB  1 
ATOM   7229  C CG  . LEU B 1 375 ? -1.318  32.445  39.942  1.00 16.29  ? 375 LEU B CG  1 
ATOM   7230  C CD1 . LEU B 1 375 ? -1.936  33.337  38.881  1.00 15.43  ? 375 LEU B CD1 1 
ATOM   7231  C CD2 . LEU B 1 375 ? -0.103  31.719  39.390  1.00 20.63  ? 375 LEU B CD2 1 
ATOM   7232  N N   . GLU B 1 376 ? -0.658  33.941  44.345  1.00 28.03  ? 376 GLU B N   1 
ATOM   7233  C CA  . GLU B 1 376 ? -0.105  34.825  45.366  1.00 33.67  ? 376 GLU B CA  1 
ATOM   7234  C C   . GLU B 1 376 ? 0.680   34.050  46.418  1.00 26.32  ? 376 GLU B C   1 
ATOM   7235  O O   . GLU B 1 376 ? 1.662   34.570  46.959  1.00 27.44  ? 376 GLU B O   1 
ATOM   7236  C CB  . GLU B 1 376 ? -1.218  35.650  46.021  1.00 27.55  ? 376 GLU B CB  1 
ATOM   7237  C CG  . GLU B 1 376 ? -2.245  34.839  46.791  1.00 41.31  ? 376 GLU B CG  1 
ATOM   7238  C CD  . GLU B 1 376 ? -3.571  35.560  46.940  1.00 49.05  ? 376 GLU B CD  1 
ATOM   7239  O OE1 . GLU B 1 376 ? -3.772  36.582  46.252  1.00 45.39  ? 376 GLU B OE1 1 
ATOM   7240  O OE2 . GLU B 1 376 ? -4.411  35.104  47.747  1.00 51.45  ? 376 GLU B OE2 1 
ATOM   7241  N N   . LYS B 1 377 ? 0.268   32.816  46.727  1.00 28.38  ? 377 LYS B N   1 
ATOM   7242  C CA  . LYS B 1 377 ? 1.044   31.994  47.652  1.00 30.90  ? 377 LYS B CA  1 
ATOM   7243  C C   . LYS B 1 377 ? 2.390   31.603  47.053  1.00 34.73  ? 377 LYS B C   1 
ATOM   7244  O O   . LYS B 1 377 ? 3.408   31.600  47.754  1.00 42.67  ? 377 LYS B O   1 
ATOM   7245  C CB  . LYS B 1 377 ? 0.260   30.742  48.051  1.00 33.00  ? 377 LYS B CB  1 
ATOM   7246  C CG  . LYS B 1 377 ? -1.013  31.008  48.835  1.00 35.16  ? 377 LYS B CG  1 
ATOM   7247  C CD  . LYS B 1 377 ? -1.943  29.805  48.790  1.00 40.31  ? 377 LYS B CD  1 
ATOM   7248  C CE  . LYS B 1 377 ? -3.390  30.204  49.028  1.00 52.41  ? 377 LYS B CE  1 
ATOM   7249  N NZ  . LYS B 1 377 ? -4.338  29.206  48.457  1.00 42.78  ? 377 LYS B NZ  1 
ATOM   7250  N N   . GLU B 1 378 ? 2.416   31.272  45.764  1.00 38.99  ? 378 GLU B N   1 
ATOM   7251  C CA  . GLU B 1 378 ? 3.640   30.809  45.112  1.00 29.98  ? 378 GLU B CA  1 
ATOM   7252  C C   . GLU B 1 378 ? 4.587   31.989  44.932  1.00 26.54  ? 378 GLU B C   1 
ATOM   7253  O O   . GLU B 1 378 ? 4.419   32.815  44.034  1.00 32.29  ? 378 GLU B O   1 
ATOM   7254  C CB  . GLU B 1 378 ? 3.313   30.136  43.784  1.00 27.80  ? 378 GLU B CB  1 
ATOM   7255  C CG  . GLU B 1 378 ? 2.376   28.939  43.929  1.00 36.49  ? 378 GLU B CG  1 
ATOM   7256  C CD  . GLU B 1 378 ? 3.077   27.688  44.440  1.00 46.44  ? 378 GLU B CD  1 
ATOM   7257  O OE1 . GLU B 1 378 ? 2.427   26.620  44.489  1.00 39.69  ? 378 GLU B OE1 1 
ATOM   7258  O OE2 . GLU B 1 378 ? 4.275   27.765  44.787  1.00 41.59  ? 378 GLU B OE2 1 
ATOM   7259  N N   . GLU B 1 379 ? 5.597   32.058  45.798  1.00 29.64  ? 379 GLU B N   1 
ATOM   7260  C CA  . GLU B 1 379 ? 6.506   33.196  45.836  1.00 31.44  ? 379 GLU B CA  1 
ATOM   7261  C C   . GLU B 1 379 ? 7.450   33.235  44.642  1.00 33.01  ? 379 GLU B C   1 
ATOM   7262  O O   . GLU B 1 379 ? 7.989   34.302  44.330  1.00 30.31  ? 379 GLU B O   1 
ATOM   7263  C CB  . GLU B 1 379 ? 7.310   33.165  47.138  1.00 41.38  ? 379 GLU B CB  1 
ATOM   7264  C CG  . GLU B 1 379 ? 8.407   32.094  47.184  1.00 57.60  ? 379 GLU B CG  1 
ATOM   7265  C CD  . GLU B 1 379 ? 7.868   30.672  47.291  1.00 56.36  ? 379 GLU B CD  1 
ATOM   7266  O OE1 . GLU B 1 379 ? 8.692   29.730  47.245  1.00 53.20  ? 379 GLU B OE1 1 
ATOM   7267  O OE2 . GLU B 1 379 ? 6.640   30.491  47.423  1.00 58.50  ? 379 GLU B OE2 1 
ATOM   7268  N N   . TRP B 1 380 ? 7.665   32.105  43.973  1.00 32.49  ? 380 TRP B N   1 
ATOM   7269  C CA  . TRP B 1 380 ? 8.553   32.051  42.821  1.00 22.86  ? 380 TRP B CA  1 
ATOM   7270  C C   . TRP B 1 380 ? 7.874   32.493  41.532  1.00 25.14  ? 380 TRP B C   1 
ATOM   7271  O O   . TRP B 1 380 ? 8.535   32.545  40.489  1.00 30.17  ? 380 TRP B O   1 
ATOM   7272  C CB  . TRP B 1 380 ? 9.111   30.633  42.653  1.00 28.63  ? 380 TRP B CB  1 
ATOM   7273  C CG  . TRP B 1 380 ? 8.060   29.568  42.686  1.00 23.44  ? 380 TRP B CG  1 
ATOM   7274  C CD1 . TRP B 1 380 ? 7.428   29.069  43.789  1.00 29.06  ? 380 TRP B CD1 1 
ATOM   7275  C CD2 . TRP B 1 380 ? 7.511   28.873  41.562  1.00 23.01  ? 380 TRP B CD2 1 
ATOM   7276  N NE1 . TRP B 1 380 ? 6.519   28.107  43.420  1.00 24.07  ? 380 TRP B NE1 1 
ATOM   7277  C CE2 . TRP B 1 380 ? 6.552   27.967  42.057  1.00 22.87  ? 380 TRP B CE2 1 
ATOM   7278  C CE3 . TRP B 1 380 ? 7.740   28.926  40.184  1.00 26.60  ? 380 TRP B CE3 1 
ATOM   7279  C CZ2 . TRP B 1 380 ? 5.823   27.124  41.223  1.00 29.92  ? 380 TRP B CZ2 1 
ATOM   7280  C CZ3 . TRP B 1 380 ? 7.014   28.090  39.358  1.00 23.25  ? 380 TRP B CZ3 1 
ATOM   7281  C CH2 . TRP B 1 380 ? 6.067   27.202  39.880  1.00 29.45  ? 380 TRP B CH2 1 
ATOM   7282  N N   . ILE B 1 381 ? 6.583   32.810  41.577  1.00 30.43  ? 381 ILE B N   1 
ATOM   7283  C CA  . ILE B 1 381 ? 5.825   33.246  40.410  1.00 24.60  ? 381 ILE B CA  1 
ATOM   7284  C C   . ILE B 1 381 ? 5.463   34.709  40.629  1.00 24.66  ? 381 ILE B C   1 
ATOM   7285  O O   . ILE B 1 381 ? 4.573   35.029  41.423  1.00 25.74  ? 381 ILE B O   1 
ATOM   7286  C CB  . ILE B 1 381 ? 4.572   32.395  40.182  1.00 20.21  ? 381 ILE B CB  1 
ATOM   7287  C CG1 . ILE B 1 381 ? 4.950   30.942  39.901  1.00 26.70  ? 381 ILE B CG1 1 
ATOM   7288  C CG2 . ILE B 1 381 ? 3.751   32.951  39.029  1.00 31.61  ? 381 ILE B CG2 1 
ATOM   7289  C CD1 . ILE B 1 381 ? 3.837   29.961  40.192  1.00 24.39  ? 381 ILE B CD1 1 
ATOM   7290  N N   . GLU B 1 382 ? 6.147   35.604  39.922  1.00 21.68  ? 382 GLU B N   1 
ATOM   7291  C CA  . GLU B 1 382 ? 5.799   37.018  39.925  1.00 22.55  ? 382 GLU B CA  1 
ATOM   7292  C C   . GLU B 1 382 ? 4.908   37.310  38.725  1.00 24.86  ? 382 GLU B C   1 
ATOM   7293  O O   . GLU B 1 382 ? 5.273   37.002  37.587  1.00 30.00  ? 382 GLU B O   1 
ATOM   7294  C CB  . GLU B 1 382 ? 7.057   37.888  39.883  1.00 22.22  ? 382 GLU B CB  1 
ATOM   7295  C CG  . GLU B 1 382 ? 6.837   39.344  40.287  1.00 29.30  ? 382 GLU B CG  1 
ATOM   7296  C CD  . GLU B 1 382 ? 8.119   40.160  40.261  1.00 40.95  ? 382 GLU B CD  1 
ATOM   7297  O OE1 . GLU B 1 382 ? 9.139   39.684  40.805  1.00 43.73  ? 382 GLU B OE1 1 
ATOM   7298  O OE2 . GLU B 1 382 ? 8.106   41.280  39.708  1.00 39.29  ? 382 GLU B OE2 1 
ATOM   7299  N N   . THR B 1 383 ? 3.735   37.882  38.982  1.00 16.95  ? 383 THR B N   1 
ATOM   7300  C CA  . THR B 1 383 ? 2.855   38.329  37.913  1.00 18.85  ? 383 THR B CA  1 
ATOM   7301  C C   . THR B 1 383 ? 3.126   39.798  37.622  1.00 19.59  ? 383 THR B C   1 
ATOM   7302  O O   . THR B 1 383 ? 3.410   40.581  38.533  1.00 20.55  ? 383 THR B O   1 
ATOM   7303  C CB  . THR B 1 383 ? 1.382   38.123  38.272  1.00 16.66  ? 383 THR B CB  1 
ATOM   7304  O OG1 . THR B 1 383 ? 0.957   39.143  39.184  1.00 26.91  ? 383 THR B OG1 1 
ATOM   7305  C CG2 . THR B 1 383 ? 1.168   36.755  38.902  1.00 18.01  ? 383 THR B CG2 1 
ATOM   7306  N N   . LEU B 1 384 ? 3.044   40.168  36.344  1.00 15.05  ? 384 LEU B N   1 
ATOM   7307  C CA  . LEU B 1 384 ? 3.448   41.495  35.907  1.00 16.26  ? 384 LEU B CA  1 
ATOM   7308  C C   . LEU B 1 384 ? 2.376   42.148  35.048  1.00 16.54  ? 384 LEU B C   1 
ATOM   7309  O O   . LEU B 1 384 ? 1.627   41.477  34.332  1.00 19.15  ? 384 LEU B O   1 
ATOM   7310  C CB  . LEU B 1 384 ? 4.758   41.446  35.112  1.00 15.67  ? 384 LEU B CB  1 
ATOM   7311  C CG  . LEU B 1 384 ? 5.860   40.521  35.619  1.00 19.45  ? 384 LEU B CG  1 
ATOM   7312  C CD1 . LEU B 1 384 ? 6.959   40.399  34.578  1.00 19.12  ? 384 LEU B CD1 1 
ATOM   7313  C CD2 . LEU B 1 384 ? 6.413   41.043  36.931  1.00 17.23  ? 384 LEU B CD2 1 
ATOM   7314  N N   . THR B 1 385 ? 2.315   43.474  35.136  1.00 19.51  ? 385 THR B N   1 
ATOM   7315  C CA  . THR B 1 385 ? 1.643   44.274  34.128  1.00 20.43  ? 385 THR B CA  1 
ATOM   7316  C C   . THR B 1 385 ? 2.513   44.352  32.879  1.00 24.44  ? 385 THR B C   1 
ATOM   7317  O O   . THR B 1 385 ? 3.731   44.163  32.930  1.00 27.29  ? 385 THR B O   1 
ATOM   7318  C CB  . THR B 1 385 ? 1.354   45.688  34.641  1.00 17.96  ? 385 THR B CB  1 
ATOM   7319  O OG1 . THR B 1 385 ? 2.581   46.422  34.746  1.00 17.89  ? 385 THR B OG1 1 
ATOM   7320  C CG2 . THR B 1 385 ? 0.681   45.645  35.999  1.00 17.47  ? 385 THR B CG2 1 
ATOM   7321  N N   . LEU B 1 386 ? 1.869   44.632  31.741  1.00 24.97  ? 386 LEU B N   1 
ATOM   7322  C CA  . LEU B 1 386 ? 2.616   44.788  30.496  1.00 15.71  ? 386 LEU B CA  1 
ATOM   7323  C C   . LEU B 1 386 ? 3.667   45.882  30.617  1.00 24.18  ? 386 LEU B C   1 
ATOM   7324  O O   . LEU B 1 386 ? 4.706   45.821  29.951  1.00 30.64  ? 386 LEU B O   1 
ATOM   7325  C CB  . LEU B 1 386 ? 1.661   45.085  29.340  1.00 22.35  ? 386 LEU B CB  1 
ATOM   7326  C CG  . LEU B 1 386 ? 0.493   44.108  29.164  1.00 18.20  ? 386 LEU B CG  1 
ATOM   7327  C CD1 . LEU B 1 386 ? -0.503  44.630  28.137  1.00 14.71  ? 386 LEU B CD1 1 
ATOM   7328  C CD2 . LEU B 1 386 ? 0.995   42.723  28.781  1.00 15.92  ? 386 LEU B CD2 1 
ATOM   7329  N N   . GLU B 1 387 ? 3.417   46.884  31.465  1.00 29.59  ? 387 GLU B N   1 
ATOM   7330  C CA  . GLU B 1 387 ? 4.447   47.865  31.789  1.00 27.80  ? 387 GLU B CA  1 
ATOM   7331  C C   . GLU B 1 387 ? 5.631   47.201  32.478  1.00 27.06  ? 387 GLU B C   1 
ATOM   7332  O O   . GLU B 1 387 ? 6.787   47.403  32.088  1.00 31.53  ? 387 GLU B O   1 
ATOM   7333  C CB  . GLU B 1 387 ? 3.864   48.955  32.688  1.00 32.94  ? 387 GLU B CB  1 
ATOM   7334  C CG  . GLU B 1 387 ? 4.243   50.371  32.308  1.00 28.64  ? 387 GLU B CG  1 
ATOM   7335  C CD  . GLU B 1 387 ? 3.453   51.397  33.093  1.00 47.30  ? 387 GLU B CD  1 
ATOM   7336  O OE1 . GLU B 1 387 ? 3.279   51.198  34.314  1.00 65.94  ? 387 GLU B OE1 1 
ATOM   7337  O OE2 . GLU B 1 387 ? 3.002   52.395  32.496  1.00 51.64  ? 387 GLU B OE2 1 
ATOM   7338  N N   . GLU B 1 388 ? 5.357   46.399  33.509  1.00 25.53  ? 388 GLU B N   1 
ATOM   7339  C CA  . GLU B 1 388 ? 6.432   45.804  34.298  1.00 34.60  ? 388 GLU B CA  1 
ATOM   7340  C C   . GLU B 1 388 ? 7.293   44.872  33.454  1.00 31.55  ? 388 GLU B C   1 
ATOM   7341  O O   . GLU B 1 388 ? 8.525   44.890  33.558  1.00 36.41  ? 388 GLU B O   1 
ATOM   7342  C CB  . GLU B 1 388 ? 5.843   45.070  35.503  1.00 34.18  ? 388 GLU B CB  1 
ATOM   7343  C CG  . GLU B 1 388 ? 5.244   46.007  36.549  1.00 34.07  ? 388 GLU B CG  1 
ATOM   7344  C CD  . GLU B 1 388 ? 4.591   45.280  37.712  1.00 31.60  ? 388 GLU B CD  1 
ATOM   7345  O OE1 . GLU B 1 388 ? 4.276   44.080  37.574  1.00 30.10  ? 388 GLU B OE1 1 
ATOM   7346  O OE2 . GLU B 1 388 ? 4.387   45.914  38.768  1.00 29.30  ? 388 GLU B OE2 1 
ATOM   7347  N N   . ALA B 1 389 ? 6.663   44.054  32.607  1.00 29.91  ? 389 ALA B N   1 
ATOM   7348  C CA  . ALA B 1 389 ? 7.423   43.166  31.733  1.00 21.46  ? 389 ALA B CA  1 
ATOM   7349  C C   . ALA B 1 389 ? 8.268   43.949  30.737  1.00 26.88  ? 389 ALA B C   1 
ATOM   7350  O O   . ALA B 1 389 ? 9.311   43.459  30.287  1.00 30.50  ? 389 ALA B O   1 
ATOM   7351  C CB  . ALA B 1 389 ? 6.480   42.214  30.998  1.00 16.32  ? 389 ALA B CB  1 
ATOM   7352  N N   . MET B 1 390 ? 7.833   45.159  30.376  1.00 25.07  ? 390 MET B N   1 
ATOM   7353  C CA  . MET B 1 390 ? 8.602   45.986  29.453  1.00 25.61  ? 390 MET B CA  1 
ATOM   7354  C C   . MET B 1 390 ? 9.796   46.654  30.128  1.00 32.13  ? 390 MET B C   1 
ATOM   7355  O O   . MET B 1 390 ? 10.784  46.966  29.454  1.00 28.06  ? 390 MET B O   1 
ATOM   7356  C CB  . MET B 1 390 ? 7.696   47.039  28.814  1.00 24.46  ? 390 MET B CB  1 
ATOM   7357  C CG  . MET B 1 390 ? 6.902   46.518  27.626  1.00 32.89  ? 390 MET B CG  1 
ATOM   7358  S SD  . MET B 1 390 ? 7.940   46.312  26.166  1.00 29.45  ? 390 MET B SD  1 
ATOM   7359  C CE  . MET B 1 390 ? 8.138   48.015  25.647  1.00 33.35  ? 390 MET B CE  1 
ATOM   7360  N N   . ARG B 1 391 ? 9.726   46.894  31.439  1.00 33.28  ? 391 ARG B N   1 
ATOM   7361  C CA  . ARG B 1 391 ? 10.820  47.517  32.173  1.00 28.48  ? 391 ARG B CA  1 
ATOM   7362  C C   . ARG B 1 391 ? 11.720  46.518  32.887  1.00 32.04  ? 391 ARG B C   1 
ATOM   7363  O O   . ARG B 1 391 ? 12.745  46.925  33.446  1.00 39.53  ? 391 ARG B O   1 
ATOM   7364  C CB  . ARG B 1 391 ? 10.269  48.509  33.206  1.00 30.09  ? 391 ARG B CB  1 
ATOM   7365  C CG  . ARG B 1 391 ? 9.211   49.443  32.663  1.00 33.22  ? 391 ARG B CG  1 
ATOM   7366  C CD  . ARG B 1 391 ? 9.785   50.824  32.396  1.00 36.62  ? 391 ARG B CD  1 
ATOM   7367  N NE  . ARG B 1 391 ? 10.298  50.968  31.037  1.00 49.41  ? 391 ARG B NE  1 
ATOM   7368  C CZ  . ARG B 1 391 ? 9.574   50.865  29.928  1.00 47.65  ? 391 ARG B CZ  1 
ATOM   7369  N NH1 . ARG B 1 391 ? 8.267   50.653  29.967  1.00 44.44  ? 391 ARG B NH1 1 
ATOM   7370  N NH2 . ARG B 1 391 ? 10.176  50.995  28.748  1.00 49.50  ? 391 ARG B NH2 1 
ATOM   7371  N N   . LYS B 1 392 ? 11.369  45.234  32.882  1.00 23.29  ? 392 LYS B N   1 
ATOM   7372  C CA  . LYS B 1 392 ? 12.054  44.263  33.726  1.00 21.35  ? 392 LYS B CA  1 
ATOM   7373  C C   . LYS B 1 392 ? 13.487  44.034  33.258  1.00 37.24  ? 392 LYS B C   1 
ATOM   7374  O O   . LYS B 1 392 ? 13.733  43.754  32.082  1.00 42.05  ? 392 LYS B O   1 
ATOM   7375  C CB  . LYS B 1 392 ? 11.284  42.945  33.736  1.00 21.84  ? 392 LYS B CB  1 
ATOM   7376  C CG  . LYS B 1 392 ? 10.483  42.713  35.006  1.00 32.56  ? 392 LYS B CG  1 
ATOM   7377  C CD  . LYS B 1 392 ? 11.400  42.472  36.192  1.00 22.31  ? 392 LYS B CD  1 
ATOM   7378  C CE  . LYS B 1 392 ? 10.613  42.045  37.420  1.00 33.16  ? 392 LYS B CE  1 
ATOM   7379  N NZ  . LYS B 1 392 ? 11.405  42.214  38.670  1.00 45.52  ? 392 LYS B NZ  1 
ATOM   7380  N N   . GLU B 1 393 ? 14.433  44.139  34.196  1.00 37.62  ? 393 GLU B N   1 
ATOM   7381  C CA  . GLU B 1 393 ? 15.846  43.932  33.900  1.00 29.97  ? 393 GLU B CA  1 
ATOM   7382  C C   . GLU B 1 393 ? 16.238  42.461  33.855  1.00 36.86  ? 393 GLU B C   1 
ATOM   7383  O O   . GLU B 1 393 ? 17.213  42.113  33.179  1.00 46.02  ? 393 GLU B O   1 
ATOM   7384  C CB  . GLU B 1 393 ? 16.707  44.642  34.947  1.00 31.19  ? 393 GLU B CB  1 
ATOM   7385  C CG  . GLU B 1 393 ? 16.879  46.134  34.734  1.00 41.28  ? 393 GLU B CG  1 
ATOM   7386  C CD  . GLU B 1 393 ? 17.779  46.764  35.782  1.00 58.99  ? 393 GLU B CD  1 
ATOM   7387  O OE1 . GLU B 1 393 ? 17.521  46.558  36.987  1.00 64.33  ? 393 GLU B OE1 1 
ATOM   7388  O OE2 . GLU B 1 393 ? 18.747  47.458  35.405  1.00 45.70  ? 393 GLU B OE2 1 
ATOM   7389  N N   . ASP B 1 394 ? 15.507  41.595  34.553  1.00 27.28  ? 394 ASP B N   1 
ATOM   7390  C CA  . ASP B 1 394 ? 15.905  40.207  34.748  1.00 25.13  ? 394 ASP B CA  1 
ATOM   7391  C C   . ASP B 1 394 ? 15.593  39.310  33.557  1.00 31.83  ? 394 ASP B C   1 
ATOM   7392  O O   . ASP B 1 394 ? 15.975  38.135  33.574  1.00 28.25  ? 394 ASP B O   1 
ATOM   7393  C CB  . ASP B 1 394 ? 15.215  39.645  35.994  1.00 33.90  ? 394 ASP B CB  1 
ATOM   7394  C CG  . ASP B 1 394 ? 15.703  40.292  37.273  1.00 47.22  ? 394 ASP B CG  1 
ATOM   7395  O OD1 . ASP B 1 394 ? 15.161  41.353  37.648  1.00 42.30  ? 394 ASP B OD1 1 
ATOM   7396  O OD2 . ASP B 1 394 ? 16.625  39.735  37.906  1.00 61.53  ? 394 ASP B OD2 1 
ATOM   7397  N N   . VAL B 1 395 ? 14.923  39.820  32.536  1.00 34.03  ? 395 VAL B N   1 
ATOM   7398  C CA  . VAL B 1 395 ? 14.433  39.002  31.432  1.00 20.57  ? 395 VAL B CA  1 
ATOM   7399  C C   . VAL B 1 395 ? 15.495  38.924  30.343  1.00 21.48  ? 395 VAL B C   1 
ATOM   7400  O O   . VAL B 1 395 ? 16.219  39.893  30.087  1.00 26.73  ? 395 VAL B O   1 
ATOM   7401  C CB  . VAL B 1 395 ? 13.108  39.574  30.892  1.00 19.30  ? 395 VAL B CB  1 
ATOM   7402  C CG1 . VAL B 1 395 ? 12.641  38.810  29.663  1.00 18.56  ? 395 VAL B CG1 1 
ATOM   7403  C CG2 . VAL B 1 395 ? 12.044  39.543  31.979  1.00 19.43  ? 395 VAL B CG2 1 
ATOM   7404  N N   . LYS B 1 396 ? 15.598  37.757  29.709  1.00 21.38  ? 396 LYS B N   1 
ATOM   7405  C CA  . LYS B 1 396 ? 16.519  37.557  28.599  1.00 22.35  ? 396 LYS B CA  1 
ATOM   7406  C C   . LYS B 1 396 ? 15.910  38.121  27.322  1.00 21.78  ? 396 LYS B C   1 
ATOM   7407  O O   . LYS B 1 396 ? 14.745  37.854  27.012  1.00 20.56  ? 396 LYS B O   1 
ATOM   7408  C CB  . LYS B 1 396 ? 16.824  36.068  28.430  1.00 22.73  ? 396 LYS B CB  1 
ATOM   7409  C CG  . LYS B 1 396 ? 17.981  35.754  27.497  1.00 24.75  ? 396 LYS B CG  1 
ATOM   7410  C CD  . LYS B 1 396 ? 18.283  34.259  27.487  1.00 27.04  ? 396 LYS B CD  1 
ATOM   7411  C CE  . LYS B 1 396 ? 19.619  33.964  26.819  1.00 39.43  ? 396 LYS B CE  1 
ATOM   7412  N NZ  . LYS B 1 396 ? 19.527  32.825  25.864  1.00 39.02  ? 396 LYS B NZ  1 
ATOM   7413  N N   . THR B 1 397 ? 16.694  38.898  26.578  1.00 14.52  ? 397 THR B N   1 
ATOM   7414  C CA  . THR B 1 397 ? 16.218  39.534  25.359  1.00 10.67  ? 397 THR B CA  1 
ATOM   7415  C C   . THR B 1 397 ? 16.989  39.024  24.151  1.00 14.52  ? 397 THR B C   1 
ATOM   7416  O O   . THR B 1 397 ? 18.211  38.846  24.208  1.00 17.26  ? 397 THR B O   1 
ATOM   7417  C CB  . THR B 1 397 ? 16.340  41.058  25.432  1.00 14.82  ? 397 THR B CB  1 
ATOM   7418  O OG1 . THR B 1 397 ? 16.033  41.503  26.757  1.00 26.70  ? 397 THR B OG1 1 
ATOM   7419  C CG2 . THR B 1 397 ? 15.370  41.702  24.459  1.00 13.69  ? 397 THR B CG2 1 
ATOM   7420  N N   . GLU B 1 398 ? 16.262  38.796  23.059  1.00 10.72  ? 398 GLU B N   1 
ATOM   7421  C CA  . GLU B 1 398 ? 16.838  38.395  21.787  1.00 13.95  ? 398 GLU B CA  1 
ATOM   7422  C C   . GLU B 1 398 ? 16.311  39.322  20.701  1.00 14.50  ? 398 GLU B C   1 
ATOM   7423  O O   . GLU B 1 398 ? 15.165  39.774  20.756  1.00 15.30  ? 398 GLU B O   1 
ATOM   7424  C CB  . GLU B 1 398 ? 16.499  36.931  21.456  1.00 14.09  ? 398 GLU B CB  1 
ATOM   7425  C CG  . GLU B 1 398 ? 16.859  36.501  20.041  1.00 24.85  ? 398 GLU B CG  1 
ATOM   7426  C CD  . GLU B 1 398 ? 17.471  35.117  19.995  1.00 41.42  ? 398 GLU B CD  1 
ATOM   7427  O OE1 . GLU B 1 398 ? 18.083  34.710  21.004  1.00 35.65  ? 398 GLU B OE1 1 
ATOM   7428  O OE2 . GLU B 1 398 ? 17.346  34.440  18.952  1.00 57.78  ? 398 GLU B OE2 1 
ATOM   7429  N N   . VAL B 1 399 ? 17.160  39.615  19.720  1.00 12.69  ? 399 VAL B N   1 
ATOM   7430  C CA  . VAL B 1 399 ? 16.797  40.459  18.589  1.00 13.30  ? 399 VAL B CA  1 
ATOM   7431  C C   . VAL B 1 399 ? 16.595  39.571  17.370  1.00 11.12  ? 399 VAL B C   1 
ATOM   7432  O O   . VAL B 1 399 ? 17.459  38.747  17.044  1.00 14.72  ? 399 VAL B O   1 
ATOM   7433  C CB  . VAL B 1 399 ? 17.872  41.524  18.320  1.00 17.12  ? 399 VAL B CB  1 
ATOM   7434  C CG1 . VAL B 1 399 ? 17.522  42.330  17.076  1.00 17.31  ? 399 VAL B CG1 1 
ATOM   7435  C CG2 . VAL B 1 399 ? 18.023  42.430  19.523  1.00 12.98  ? 399 VAL B CG2 1 
ATOM   7436  N N   . ILE B 1 400 ? 15.453  39.727  16.703  1.00 9.56   ? 400 ILE B N   1 
ATOM   7437  C CA  . ILE B 1 400 ? 15.165  39.000  15.476  1.00 14.94  ? 400 ILE B CA  1 
ATOM   7438  C C   . ILE B 1 400 ? 14.825  40.005  14.383  1.00 16.45  ? 400 ILE B C   1 
ATOM   7439  O O   . ILE B 1 400 ? 14.407  41.135  14.648  1.00 11.62  ? 400 ILE B O   1 
ATOM   7440  C CB  . ILE B 1 400 ? 14.034  37.962  15.649  1.00 12.09  ? 400 ILE B CB  1 
ATOM   7441  C CG1 . ILE B 1 400 ? 12.664  38.640  15.685  1.00 10.04  ? 400 ILE B CG1 1 
ATOM   7442  C CG2 . ILE B 1 400 ? 14.261  37.129  16.900  1.00 11.55  ? 400 ILE B CG2 1 
ATOM   7443  C CD1 . ILE B 1 400 ? 11.550  37.721  16.135  1.00 9.30   ? 400 ILE B CD1 1 
ATOM   7444  N N   . GLU B 1 401 ? 15.018  39.575  13.137  1.00 23.41  ? 401 GLU B N   1 
ATOM   7445  C CA  . GLU B 1 401 ? 14.938  40.463  11.983  1.00 15.31  ? 401 GLU B CA  1 
ATOM   7446  C C   . GLU B 1 401 ? 13.613  40.395  11.241  1.00 14.70  ? 401 GLU B C   1 
ATOM   7447  O O   . GLU B 1 401 ? 13.229  41.382  10.605  1.00 14.26  ? 401 GLU B O   1 
ATOM   7448  C CB  . GLU B 1 401 ? 16.069  40.145  10.999  1.00 19.90  ? 401 GLU B CB  1 
ATOM   7449  C CG  . GLU B 1 401 ? 17.442  40.576  11.473  1.00 25.81  ? 401 GLU B CG  1 
ATOM   7450  C CD  . GLU B 1 401 ? 17.546  42.076  11.649  1.00 30.68  ? 401 GLU B CD  1 
ATOM   7451  O OE1 . GLU B 1 401 ? 17.004  42.813  10.799  1.00 39.12  ? 401 GLU B OE1 1 
ATOM   7452  O OE2 . GLU B 1 401 ? 18.170  42.517  12.636  1.00 36.38  ? 401 GLU B OE2 1 
ATOM   7453  N N   . SER B 1 402 ? 12.908  39.267  11.294  1.00 11.60  ? 402 SER B N   1 
ATOM   7454  C CA  . SER B 1 402 ? 11.712  39.106  10.479  1.00 15.63  ? 402 SER B CA  1 
ATOM   7455  C C   . SER B 1 402 ? 10.824  38.028  11.081  1.00 15.99  ? 402 SER B C   1 
ATOM   7456  O O   . SER B 1 402 ? 11.263  37.226  11.909  1.00 18.79  ? 402 SER B O   1 
ATOM   7457  C CB  . SER B 1 402 ? 12.071  38.754  9.031   1.00 19.44  ? 402 SER B CB  1 
ATOM   7458  O OG  . SER B 1 402 ? 12.619  37.448  8.950   1.00 24.20  ? 402 SER B OG  1 
ATOM   7459  N N   . VAL B 1 403 ? 9.562   38.024  10.651  1.00 18.04  ? 403 VAL B N   1 
ATOM   7460  C CA  . VAL B 1 403 ? 8.585   37.021  11.056  1.00 17.94  ? 403 VAL B CA  1 
ATOM   7461  C C   . VAL B 1 403 ? 7.849   36.527  9.818   1.00 20.06  ? 403 VAL B C   1 
ATOM   7462  O O   . VAL B 1 403 ? 7.559   37.304  8.900   1.00 18.86  ? 403 VAL B O   1 
ATOM   7463  C CB  . VAL B 1 403 ? 7.585   37.570  12.100  1.00 14.91  ? 403 VAL B CB  1 
ATOM   7464  C CG1 . VAL B 1 403 ? 8.299   37.904  13.401  1.00 12.18  ? 403 VAL B CG1 1 
ATOM   7465  C CG2 . VAL B 1 403 ? 6.847   38.788  11.560  1.00 16.40  ? 403 VAL B CG2 1 
ATOM   7466  N N   . LYS B 1 404 ? 7.567   35.227  9.784   1.00 23.52  ? 404 LYS B N   1 
ATOM   7467  C CA  . LYS B 1 404 ? 6.722   34.649  8.747   1.00 16.91  ? 404 LYS B CA  1 
ATOM   7468  C C   . LYS B 1 404 ? 5.266   34.926  9.099   1.00 21.24  ? 404 LYS B C   1 
ATOM   7469  O O   . LYS B 1 404 ? 4.787   34.493  10.153  1.00 21.16  ? 404 LYS B O   1 
ATOM   7470  C CB  . LYS B 1 404 ? 6.979   33.148  8.623   1.00 21.30  ? 404 LYS B CB  1 
ATOM   7471  C CG  . LYS B 1 404 ? 7.479   32.698  7.258   1.00 25.23  ? 404 LYS B CG  1 
ATOM   7472  C CD  . LYS B 1 404 ? 7.306   31.195  7.080   1.00 31.73  ? 404 LYS B CD  1 
ATOM   7473  C CE  . LYS B 1 404 ? 8.643   30.490  6.898   1.00 30.40  ? 404 LYS B CE  1 
ATOM   7474  N NZ  . LYS B 1 404 ? 8.483   29.008  6.870   1.00 27.33  ? 404 LYS B NZ  1 
ATOM   7475  N N   . ALA B 1 405 ? 4.566   35.637  8.218   1.00 17.52  ? 405 ALA B N   1 
ATOM   7476  C CA  . ALA B 1 405 ? 3.236   36.141  8.538   1.00 15.62  ? 405 ALA B CA  1 
ATOM   7477  C C   . ALA B 1 405 ? 2.257   35.004  8.820   1.00 15.95  ? 405 ALA B C   1 
ATOM   7478  O O   . ALA B 1 405 ? 2.323   33.926  8.221   1.00 26.80  ? 405 ALA B O   1 
ATOM   7479  C CB  . ALA B 1 405 ? 2.706   37.005  7.395   1.00 23.05  ? 405 ALA B CB  1 
ATOM   7480  N N   . GLY B 1 406 ? 1.341   35.258  9.745   1.00 12.79  ? 406 GLY B N   1 
ATOM   7481  C CA  . GLY B 1 406 ? 0.343   34.270  10.102  1.00 19.62  ? 406 GLY B CA  1 
ATOM   7482  C C   . GLY B 1 406 ? -0.531  34.775  11.228  1.00 15.51  ? 406 GLY B C   1 
ATOM   7483  O O   . GLY B 1 406 ? -0.436  35.930  11.642  1.00 19.25  ? 406 GLY B O   1 
ATOM   7484  N N   . THR B 1 407 ? -1.398  33.887  11.711  1.00 14.19  ? 407 THR B N   1 
ATOM   7485  C CA  . THR B 1 407 ? -2.277  34.147  12.844  1.00 17.49  ? 407 THR B CA  1 
ATOM   7486  C C   . THR B 1 407 ? -2.074  33.044  13.876  1.00 19.60  ? 407 THR B C   1 
ATOM   7487  O O   . THR B 1 407 ? -1.293  32.112  13.666  1.00 23.58  ? 407 THR B O   1 
ATOM   7488  C CB  . THR B 1 407 ? -3.748  34.220  12.411  1.00 18.81  ? 407 THR B CB  1 
ATOM   7489  O OG1 . THR B 1 407 ? -4.182  32.924  11.977  1.00 24.41  ? 407 THR B OG1 1 
ATOM   7490  C CG2 . THR B 1 407 ? -3.922  35.218  11.273  1.00 18.70  ? 407 THR B CG2 1 
ATOM   7491  N N   . TRP B 1 408 ? -2.786  33.137  15.001  1.00 21.34  ? 408 TRP B N   1 
ATOM   7492  C CA  . TRP B 1 408 ? -2.672  32.079  15.997  1.00 25.36  ? 408 TRP B CA  1 
ATOM   7493  C C   . TRP B 1 408 ? -3.504  30.852  15.643  1.00 20.22  ? 408 TRP B C   1 
ATOM   7494  O O   . TRP B 1 408 ? -3.454  29.858  16.375  1.00 23.11  ? 408 TRP B O   1 
ATOM   7495  C CB  . TRP B 1 408 ? -3.032  32.590  17.403  1.00 17.80  ? 408 TRP B CB  1 
ATOM   7496  C CG  . TRP B 1 408 ? -4.408  33.162  17.609  1.00 20.66  ? 408 TRP B CG  1 
ATOM   7497  C CD1 . TRP B 1 408 ? -5.428  33.222  16.706  1.00 22.03  ? 408 TRP B CD1 1 
ATOM   7498  C CD2 . TRP B 1 408 ? -4.911  33.745  18.821  1.00 17.57  ? 408 TRP B CD2 1 
ATOM   7499  N NE1 . TRP B 1 408 ? -6.532  33.813  17.277  1.00 20.86  ? 408 TRP B NE1 1 
ATOM   7500  C CE2 . TRP B 1 408 ? -6.239  34.141  18.575  1.00 16.78  ? 408 TRP B CE2 1 
ATOM   7501  C CE3 . TRP B 1 408 ? -4.363  33.971  20.088  1.00 15.19  ? 408 TRP B CE3 1 
ATOM   7502  C CZ2 . TRP B 1 408 ? -7.028  34.752  19.550  1.00 16.63  ? 408 TRP B CZ2 1 
ATOM   7503  C CZ3 . TRP B 1 408 ? -5.147  34.577  21.054  1.00 15.40  ? 408 TRP B CZ3 1 
ATOM   7504  C CH2 . TRP B 1 408 ? -6.465  34.961  20.779  1.00 16.89  ? 408 TRP B CH2 1 
ATOM   7505  N N   . PHE B 1 409 ? -4.257  30.898  14.543  1.00 20.88  ? 409 PHE B N   1 
ATOM   7506  C CA  . PHE B 1 409 ? -4.919  29.718  13.987  1.00 23.45  ? 409 PHE B CA  1 
ATOM   7507  C C   . PHE B 1 409 ? -3.975  29.068  12.984  1.00 33.09  ? 409 PHE B C   1 
ATOM   7508  O O   . PHE B 1 409 ? -3.952  29.421  11.803  1.00 35.61  ? 409 PHE B O   1 
ATOM   7509  C CB  . PHE B 1 409 ? -6.242  30.089  13.329  1.00 20.42  ? 409 PHE B CB  1 
ATOM   7510  C CG  . PHE B 1 409 ? -7.352  30.365  14.297  1.00 28.07  ? 409 PHE B CG  1 
ATOM   7511  C CD1 . PHE B 1 409 ? -8.154  29.336  14.759  1.00 33.51  ? 409 PHE B CD1 1 
ATOM   7512  C CD2 . PHE B 1 409 ? -7.607  31.656  14.732  1.00 29.29  ? 409 PHE B CD2 1 
ATOM   7513  C CE1 . PHE B 1 409 ? -9.182  29.586  15.645  1.00 42.56  ? 409 PHE B CE1 1 
ATOM   7514  C CE2 . PHE B 1 409 ? -8.634  31.909  15.620  1.00 28.01  ? 409 PHE B CE2 1 
ATOM   7515  C CZ  . PHE B 1 409 ? -9.423  30.875  16.073  1.00 33.95  ? 409 PHE B CZ  1 
ATOM   7516  N N   . ASP B 1 410 ? -3.174  28.116  13.466  1.00 32.80  ? 410 ASP B N   1 
ATOM   7517  C CA  . ASP B 1 410 ? -2.316  27.269  12.637  1.00 24.98  ? 410 ASP B CA  1 
ATOM   7518  C C   . ASP B 1 410 ? -1.231  28.050  11.901  1.00 27.67  ? 410 ASP B C   1 
ATOM   7519  O O   . ASP B 1 410 ? -0.661  27.547  10.927  1.00 26.51  ? 410 ASP B O   1 
ATOM   7520  C CB  . ASP B 1 410 ? -3.144  26.461  11.631  1.00 25.97  ? 410 ASP B CB  1 
ATOM   7521  C CG  . ASP B 1 410 ? -4.273  25.694  12.289  1.00 43.21  ? 410 ASP B CG  1 
ATOM   7522  O OD1 . ASP B 1 410 ? -4.395  25.762  13.533  1.00 47.28  ? 410 ASP B OD1 1 
ATOM   7523  O OD2 . ASP B 1 410 ? -5.042  25.029  11.564  1.00 47.62  ? 410 ASP B OD2 1 
ATOM   7524  N N   . GLY B 1 411 ? -0.937  29.276  12.330  1.00 21.31  ? 411 GLY B N   1 
ATOM   7525  C CA  . GLY B 1 411 ? 0.159   30.024  11.748  1.00 17.63  ? 411 GLY B CA  1 
ATOM   7526  C C   . GLY B 1 411 ? -0.077  30.567  10.357  1.00 23.61  ? 411 GLY B C   1 
ATOM   7527  O O   . GLY B 1 411 ? 0.874   31.042  9.729   1.00 29.17  ? 411 GLY B O   1 
ATOM   7528  N N   . ASN B 1 412 ? -1.308  30.522  9.853   1.00 21.01  ? 412 ASN B N   1 
ATOM   7529  C CA  . ASN B 1 412 ? -1.604  30.990  8.504   1.00 22.59  ? 412 ASN B CA  1 
ATOM   7530  C C   . ASN B 1 412 ? -2.930  31.745  8.528   1.00 23.25  ? 412 ASN B C   1 
ATOM   7531  O O   . ASN B 1 412 ? -3.472  32.062  9.592   1.00 19.39  ? 412 ASN B O   1 
ATOM   7532  C CB  . ASN B 1 412 ? -1.621  29.823  7.505   1.00 28.31  ? 412 ASN B CB  1 
ATOM   7533  C CG  . ASN B 1 412 ? -2.573  28.710  7.910   1.00 26.10  ? 412 ASN B CG  1 
ATOM   7534  O OD1 . ASN B 1 412 ? -3.726  28.953  8.269   1.00 31.18  ? 412 ASN B OD1 1 
ATOM   7535  N ND2 . ASN B 1 412 ? -2.095  27.475  7.835   1.00 23.45  ? 412 ASN B ND2 1 
ATOM   7536  N N   . PHE B 1 413 ? -3.453  32.029  7.333   1.00 20.56  ? 413 PHE B N   1 
ATOM   7537  C CA  . PHE B 1 413 ? -4.679  32.798  7.157   1.00 18.59  ? 413 PHE B CA  1 
ATOM   7538  C C   . PHE B 1 413 ? -5.806  31.972  6.548   1.00 20.42  ? 413 PHE B C   1 
ATOM   7539  O O   . PHE B 1 413 ? -6.793  32.540  6.071   1.00 20.66  ? 413 PHE B O   1 
ATOM   7540  C CB  . PHE B 1 413 ? -4.424  34.029  6.285   1.00 17.68  ? 413 PHE B CB  1 
ATOM   7541  C CG  . PHE B 1 413 ? -3.405  34.982  6.840   1.00 24.22  ? 413 PHE B CG  1 
ATOM   7542  C CD1 . PHE B 1 413 ? -2.048  34.734  6.691   1.00 23.17  ? 413 PHE B CD1 1 
ATOM   7543  C CD2 . PHE B 1 413 ? -3.804  36.135  7.494   1.00 19.84  ? 413 PHE B CD2 1 
ATOM   7544  C CE1 . PHE B 1 413 ? -1.112  35.615  7.195   1.00 18.62  ? 413 PHE B CE1 1 
ATOM   7545  C CE2 . PHE B 1 413 ? -2.872  37.019  8.000   1.00 17.86  ? 413 PHE B CE2 1 
ATOM   7546  C CZ  . PHE B 1 413 ? -1.523  36.758  7.851   1.00 17.21  ? 413 PHE B CZ  1 
ATOM   7547  N N   . LEU B 1 414 ? -5.688  30.644  6.559   1.00 21.87  ? 414 LEU B N   1 
ATOM   7548  C CA  . LEU B 1 414 ? -6.688  29.803  5.911   1.00 23.87  ? 414 LEU B CA  1 
ATOM   7549  C C   . LEU B 1 414 ? -8.056  29.906  6.570   1.00 24.31  ? 414 LEU B C   1 
ATOM   7550  O O   . LEU B 1 414 ? -9.043  29.447  5.986   1.00 25.94  ? 414 LEU B O   1 
ATOM   7551  C CB  . LEU B 1 414 ? -6.224  28.345  5.904   1.00 25.50  ? 414 LEU B CB  1 
ATOM   7552  C CG  . LEU B 1 414 ? -4.926  28.056  5.147   1.00 25.60  ? 414 LEU B CG  1 
ATOM   7553  C CD1 . LEU B 1 414 ? -4.571  26.577  5.225   1.00 30.94  ? 414 LEU B CD1 1 
ATOM   7554  C CD2 . LEU B 1 414 ? -5.027  28.517  3.701   1.00 26.00  ? 414 LEU B CD2 1 
ATOM   7555  N N   . LYS B 1 415 ? -8.133  30.493  7.763   1.00 27.04  ? 415 LYS B N   1 
ATOM   7556  C CA  . LYS B 1 415 ? -9.393  30.643  8.476   1.00 26.03  ? 415 LYS B CA  1 
ATOM   7557  C C   . LYS B 1 415 ? -10.262 31.770  7.930   1.00 26.16  ? 415 LYS B C   1 
ATOM   7558  O O   . LYS B 1 415 ? -11.461 31.801  8.224   1.00 31.48  ? 415 LYS B O   1 
ATOM   7559  C CB  . LYS B 1 415 ? -9.111  30.886  9.962   1.00 32.84  ? 415 LYS B CB  1 
ATOM   7560  C CG  . LYS B 1 415 ? -10.210 30.436  10.893  1.00 38.68  ? 415 LYS B CG  1 
ATOM   7561  C CD  . LYS B 1 415 ? -10.575 29.000  10.613  1.00 55.85  ? 415 LYS B CD  1 
ATOM   7562  C CE  . LYS B 1 415 ? -9.865  28.041  11.555  1.00 68.28  ? 415 LYS B CE  1 
ATOM   7563  N NZ  . LYS B 1 415 ? -9.787  26.669  10.976  1.00 76.02  ? 415 LYS B NZ  1 
ATOM   7564  N N   . TRP B 1 416 ? -9.695  32.695  7.149   1.00 22.04  ? 416 TRP B N   1 
ATOM   7565  C CA  . TRP B 1 416 ? -10.439 33.849  6.656   1.00 21.69  ? 416 TRP B CA  1 
ATOM   7566  C C   . TRP B 1 416 ? -10.408 34.011  5.145   1.00 27.10  ? 416 TRP B C   1 
ATOM   7567  O O   . TRP B 1 416 ? -11.211 34.785  4.610   1.00 31.53  ? 416 TRP B O   1 
ATOM   7568  C CB  . TRP B 1 416 ? -9.909  35.143  7.291   1.00 19.76  ? 416 TRP B CB  1 
ATOM   7569  C CG  . TRP B 1 416 ? -9.907  35.111  8.776   1.00 19.21  ? 416 TRP B CG  1 
ATOM   7570  C CD1 . TRP B 1 416 ? -10.878 35.585  9.607   1.00 21.73  ? 416 TRP B CD1 1 
ATOM   7571  C CD2 . TRP B 1 416 ? -8.884  34.573  9.619   1.00 20.12  ? 416 TRP B CD2 1 
ATOM   7572  N NE1 . TRP B 1 416 ? -10.523 35.376  10.917  1.00 18.88  ? 416 TRP B NE1 1 
ATOM   7573  C CE2 . TRP B 1 416 ? -9.302  34.756  10.951  1.00 18.39  ? 416 TRP B CE2 1 
ATOM   7574  C CE3 . TRP B 1 416 ? -7.652  33.957  9.377   1.00 23.61  ? 416 TRP B CE3 1 
ATOM   7575  C CZ2 . TRP B 1 416 ? -8.536  34.342  12.036  1.00 25.47  ? 416 TRP B CZ2 1 
ATOM   7576  C CZ3 . TRP B 1 416 ? -6.893  33.547  10.456  1.00 23.64  ? 416 TRP B CZ3 1 
ATOM   7577  C CH2 . TRP B 1 416 ? -7.336  33.742  11.769  1.00 27.34  ? 416 TRP B CH2 1 
ATOM   7578  N N   . ILE B 1 417 ? -9.511  33.323  4.445   1.00 22.66  ? 417 ILE B N   1 
ATOM   7579  C CA  . ILE B 1 417 ? -9.359  33.483  3.008   1.00 23.28  ? 417 ILE B CA  1 
ATOM   7580  C C   . ILE B 1 417 ? -8.802  32.182  2.453   1.00 25.05  ? 417 ILE B C   1 
ATOM   7581  O O   . ILE B 1 417 ? -8.144  31.418  3.164   1.00 26.31  ? 417 ILE B O   1 
ATOM   7582  C CB  . ILE B 1 417 ? -8.445  34.690  2.674   1.00 28.45  ? 417 ILE B CB  1 
ATOM   7583  C CG1 . ILE B 1 417 ? -8.761  35.258  1.290   1.00 30.84  ? 417 ILE B CG1 1 
ATOM   7584  C CG2 . ILE B 1 417 ? -6.973  34.308  2.783   1.00 27.81  ? 417 ILE B CG2 1 
ATOM   7585  C CD1 . ILE B 1 417 ? -8.286  36.690  1.102   1.00 20.88  ? 417 ILE B CD1 1 
ATOM   7586  N N   . GLY B 1 418 ? -9.091  31.914  1.184   1.00 27.23  ? 418 GLY B N   1 
ATOM   7587  C CA  . GLY B 1 418 ? -8.494  30.804  0.474   1.00 32.34  ? 418 GLY B CA  1 
ATOM   7588  C C   . GLY B 1 418 ? -9.455  29.728  0.013   1.00 35.69  ? 418 GLY B C   1 
ATOM   7589  O O   . GLY B 1 418 ? -9.133  29.004  -0.938  1.00 42.90  ? 418 GLY B O   1 
ATOM   7590  N N   . ASN B 1 419 ? -10.614 29.578  0.648   1.00 40.78  ? 419 ASN B N   1 
ATOM   7591  C CA  . ASN B 1 419 ? -11.578 28.589  0.187   1.00 39.47  ? 419 ASN B CA  1 
ATOM   7592  C C   . ASN B 1 419 ? -12.691 29.264  -0.611  1.00 41.31  ? 419 ASN B C   1 
ATOM   7593  O O   . ASN B 1 419 ? -12.809 30.492  -0.649  1.00 39.82  ? 419 ASN B O   1 
ATOM   7594  C CB  . ASN B 1 419 ? -12.113 27.737  1.360   1.00 37.53  ? 419 ASN B CB  1 
ATOM   7595  C CG  . ASN B 1 419 ? -13.223 28.408  2.183   1.00 46.69  ? 419 ASN B CG  1 
ATOM   7596  O OD1 . ASN B 1 419 ? -13.893 29.344  1.757   1.00 38.99  ? 419 ASN B OD1 1 
ATOM   7597  N ND2 . ASN B 1 419 ? -13.418 27.894  3.393   1.00 57.69  ? 419 ASN B ND2 1 
ATOM   7598  N N   . LYS B 1 420 ? -13.509 28.429  -1.254  1.00 45.26  ? 420 LYS B N   1 
ATOM   7599  C CA  . LYS B 1 420 ? -14.501 28.912  -2.210  1.00 41.17  ? 420 LYS B CA  1 
ATOM   7600  C C   . LYS B 1 420 ? -15.426 29.958  -1.593  1.00 46.73  ? 420 LYS B C   1 
ATOM   7601  O O   . LYS B 1 420 ? -15.586 31.060  -2.131  1.00 46.72  ? 420 LYS B O   1 
ATOM   7602  C CB  . LYS B 1 420 ? -15.300 27.725  -2.749  1.00 40.46  ? 420 LYS B CB  1 
ATOM   7603  C CG  . LYS B 1 420 ? -16.574 28.080  -3.486  1.00 47.32  ? 420 LYS B CG  1 
ATOM   7604  C CD  . LYS B 1 420 ? -17.267 26.816  -3.966  1.00 45.14  ? 420 LYS B CD  1 
ATOM   7605  C CE  . LYS B 1 420 ? -18.342 26.373  -2.988  1.00 46.12  ? 420 LYS B CE  1 
ATOM   7606  N NZ  . LYS B 1 420 ? -19.710 26.683  -3.486  1.00 61.82  ? 420 LYS B NZ  1 
ATOM   7607  N N   . GLU B 1 421 ? -16.036 29.634  -0.451  1.00 47.52  ? 421 GLU B N   1 
ATOM   7608  C CA  . GLU B 1 421 ? -17.016 30.541  0.142   1.00 50.10  ? 421 GLU B CA  1 
ATOM   7609  C C   . GLU B 1 421 ? -16.348 31.736  0.813   1.00 50.35  ? 421 GLU B C   1 
ATOM   7610  O O   . GLU B 1 421 ? -16.867 32.857  0.750   1.00 45.91  ? 421 GLU B O   1 
ATOM   7611  C CB  . GLU B 1 421 ? -17.897 29.785  1.133   1.00 50.99  ? 421 GLU B CB  1 
ATOM   7612  C CG  . GLU B 1 421 ? -18.374 28.436  0.620   1.00 53.90  ? 421 GLU B CG  1 
ATOM   7613  C CD  . GLU B 1 421 ? -19.827 28.463  0.186   1.00 74.72  ? 421 GLU B CD  1 
ATOM   7614  O OE1 . GLU B 1 421 ? -20.557 29.384  0.610   1.00 80.65  ? 421 GLU B OE1 1 
ATOM   7615  O OE2 . GLU B 1 421 ? -20.237 27.570  -0.584  1.00 79.08  ? 421 GLU B OE2 1 
ATOM   7616  N N   . LYS B 1 422 ? -15.204 31.519  1.469   1.00 49.39  ? 422 LYS B N   1 
ATOM   7617  C CA  . LYS B 1 422 ? -14.515 32.622  2.132   1.00 37.05  ? 422 LYS B CA  1 
ATOM   7618  C C   . LYS B 1 422 ? -14.009 33.652  1.133   1.00 35.80  ? 422 LYS B C   1 
ATOM   7619  O O   . LYS B 1 422 ? -13.947 34.844  1.451   1.00 33.28  ? 422 LYS B O   1 
ATOM   7620  C CB  . LYS B 1 422 ? -13.350 32.093  2.970   1.00 35.63  ? 422 LYS B CB  1 
ATOM   7621  C CG  . LYS B 1 422 ? -13.750 31.548  4.327   1.00 31.95  ? 422 LYS B CG  1 
ATOM   7622  C CD  . LYS B 1 422 ? -12.570 30.914  5.047   1.00 30.89  ? 422 LYS B CD  1 
ATOM   7623  C CE  . LYS B 1 422 ? -13.033 30.006  6.177   1.00 36.60  ? 422 LYS B CE  1 
ATOM   7624  N NZ  . LYS B 1 422 ? -14.005 30.688  7.078   1.00 28.29  ? 422 LYS B NZ  1 
ATOM   7625  N N   . ASN B 1 423 ? -13.647 33.214  -0.074  1.00 43.07  ? 423 ASN B N   1 
ATOM   7626  C CA  . ASN B 1 423 ? -13.058 34.124  -1.050  1.00 39.55  ? 423 ASN B CA  1 
ATOM   7627  C C   . ASN B 1 423 ? -14.080 35.104  -1.610  1.00 41.66  ? 423 ASN B C   1 
ATOM   7628  O O   . ASN B 1 423 ? -13.710 36.209  -2.023  1.00 41.23  ? 423 ASN B O   1 
ATOM   7629  C CB  . ASN B 1 423 ? -12.415 33.327  -2.184  1.00 43.08  ? 423 ASN B CB  1 
ATOM   7630  C CG  . ASN B 1 423 ? -10.972 32.969  -1.896  1.00 41.41  ? 423 ASN B CG  1 
ATOM   7631  O OD1 . ASN B 1 423 ? -10.417 33.364  -0.872  1.00 39.61  ? 423 ASN B OD1 1 
ATOM   7632  N ND2 . ASN B 1 423 ? -10.359 32.209  -2.797  1.00 42.81  ? 423 ASN B ND2 1 
ATOM   7633  N N   . GLU B 1 424 ? -15.359 34.724  -1.642  1.00 39.82  ? 424 GLU B N   1 
ATOM   7634  C CA  . GLU B 1 424 ? -16.362 35.603  -2.234  1.00 39.33  ? 424 GLU B CA  1 
ATOM   7635  C C   . GLU B 1 424 ? -16.678 36.791  -1.335  1.00 34.79  ? 424 GLU B C   1 
ATOM   7636  O O   . GLU B 1 424 ? -16.952 37.885  -1.840  1.00 33.56  ? 424 GLU B O   1 
ATOM   7637  C CB  . GLU B 1 424 ? -17.634 34.818  -2.552  1.00 43.20  ? 424 GLU B CB  1 
ATOM   7638  C CG  . GLU B 1 424 ? -18.190 35.085  -3.948  1.00 55.63  ? 424 GLU B CG  1 
ATOM   7639  C CD  . GLU B 1 424 ? -17.160 34.874  -5.048  1.00 60.59  ? 424 GLU B CD  1 
ATOM   7640  O OE1 . GLU B 1 424 ? -16.315 33.962  -4.914  1.00 64.46  ? 424 GLU B OE1 1 
ATOM   7641  O OE2 . GLU B 1 424 ? -17.195 35.620  -6.050  1.00 51.55  ? 424 GLU B OE2 1 
ATOM   7642  N N   . TYR B 1 425 ? -16.637 36.605  -0.014  1.00 39.25  ? 425 TYR B N   1 
ATOM   7643  C CA  . TYR B 1 425 ? -16.853 37.730  0.893   1.00 30.99  ? 425 TYR B CA  1 
ATOM   7644  C C   . TYR B 1 425 ? -15.786 38.799  0.701   1.00 26.65  ? 425 TYR B C   1 
ATOM   7645  O O   . TYR B 1 425 ? -16.085 39.998  0.728   1.00 27.01  ? 425 TYR B O   1 
ATOM   7646  C CB  . TYR B 1 425 ? -16.872 37.247  2.341   1.00 34.74  ? 425 TYR B CB  1 
ATOM   7647  C CG  . TYR B 1 425 ? -18.261 37.033  2.900   1.00 41.45  ? 425 TYR B CG  1 
ATOM   7648  C CD1 . TYR B 1 425 ? -19.301 36.613  2.082   1.00 45.87  ? 425 TYR B CD1 1 
ATOM   7649  C CD2 . TYR B 1 425 ? -18.531 37.248  4.246   1.00 34.90  ? 425 TYR B CD2 1 
ATOM   7650  C CE1 . TYR B 1 425 ? -20.572 36.413  2.589   1.00 50.14  ? 425 TYR B CE1 1 
ATOM   7651  C CE2 . TYR B 1 425 ? -19.796 37.051  4.761   1.00 34.65  ? 425 TYR B CE2 1 
ATOM   7652  C CZ  . TYR B 1 425 ? -20.814 36.633  3.929   1.00 42.24  ? 425 TYR B CZ  1 
ATOM   7653  O OH  . TYR B 1 425 ? -22.076 36.436  4.441   1.00 48.18  ? 425 TYR B OH  1 
ATOM   7654  N N   . TRP B 1 426 ? -14.534 38.380  0.506   1.00 27.57  ? 426 TRP B N   1 
ATOM   7655  C CA  . TRP B 1 426 ? -13.477 39.334  0.188   1.00 23.75  ? 426 TRP B CA  1 
ATOM   7656  C C   . TRP B 1 426 ? -13.761 40.044  -1.128  1.00 28.92  ? 426 TRP B C   1 
ATOM   7657  O O   . TRP B 1 426 ? -13.514 41.249  -1.257  1.00 32.84  ? 426 TRP B O   1 
ATOM   7658  C CB  . TRP B 1 426 ? -12.125 38.624  0.138   1.00 23.30  ? 426 TRP B CB  1 
ATOM   7659  C CG  . TRP B 1 426 ? -11.511 38.449  1.484   1.00 25.31  ? 426 TRP B CG  1 
ATOM   7660  C CD1 . TRP B 1 426 ? -11.546 37.330  2.262   1.00 32.71  ? 426 TRP B CD1 1 
ATOM   7661  C CD2 . TRP B 1 426 ? -10.780 39.431  2.223   1.00 23.13  ? 426 TRP B CD2 1 
ATOM   7662  N NE1 . TRP B 1 426 ? -10.874 37.553  3.441   1.00 21.83  ? 426 TRP B NE1 1 
ATOM   7663  C CE2 . TRP B 1 426 ? -10.396 38.836  3.441   1.00 19.22  ? 426 TRP B CE2 1 
ATOM   7664  C CE3 . TRP B 1 426 ? -10.411 40.756  1.973   1.00 40.27  ? 426 TRP B CE3 1 
ATOM   7665  C CZ2 . TRP B 1 426 ? -9.661  39.519  4.404   1.00 29.94  ? 426 TRP B CZ2 1 
ATOM   7666  C CZ3 . TRP B 1 426 ? -9.681  41.433  2.931   1.00 43.35  ? 426 TRP B CZ3 1 
ATOM   7667  C CH2 . TRP B 1 426 ? -9.318  40.815  4.132   1.00 31.57  ? 426 TRP B CH2 1 
ATOM   7668  N N   . LYS B 1 427 ? -14.284 39.314  -2.116  1.00 27.29  ? 427 LYS B N   1 
ATOM   7669  C CA  . LYS B 1 427 ? -14.636 39.935  -3.389  1.00 27.18  ? 427 LYS B CA  1 
ATOM   7670  C C   . LYS B 1 427 ? -15.695 41.016  -3.202  1.00 34.12  ? 427 LYS B C   1 
ATOM   7671  O O   . LYS B 1 427 ? -15.594 42.101  -3.786  1.00 31.62  ? 427 LYS B O   1 
ATOM   7672  C CB  . LYS B 1 427 ? -15.119 38.872  -4.376  1.00 29.30  ? 427 LYS B CB  1 
ATOM   7673  C CG  . LYS B 1 427 ? -14.587 39.049  -5.788  1.00 30.13  ? 427 LYS B CG  1 
ATOM   7674  C CD  . LYS B 1 427 ? -14.640 37.744  -6.560  1.00 46.82  ? 427 LYS B CD  1 
ATOM   7675  C CE  . LYS B 1 427 ? -13.803 36.672  -5.883  1.00 41.48  ? 427 LYS B CE  1 
ATOM   7676  N NZ  . LYS B 1 427 ? -14.173 35.308  -6.350  1.00 47.85  ? 427 LYS B NZ  1 
ATOM   7677  N N   . ILE B 1 428 ? -16.717 40.739  -2.387  1.00 35.85  ? 428 ILE B N   1 
ATOM   7678  C CA  . ILE B 1 428 ? -17.720 41.756  -2.079  1.00 28.12  ? 428 ILE B CA  1 
ATOM   7679  C C   . ILE B 1 428 ? -17.067 42.960  -1.413  1.00 31.33  ? 428 ILE B C   1 
ATOM   7680  O O   . ILE B 1 428 ? -17.377 44.113  -1.737  1.00 36.76  ? 428 ILE B O   1 
ATOM   7681  C CB  . ILE B 1 428 ? -18.839 41.166  -1.200  1.00 29.05  ? 428 ILE B CB  1 
ATOM   7682  C CG1 . ILE B 1 428 ? -19.336 39.836  -1.770  1.00 30.89  ? 428 ILE B CG1 1 
ATOM   7683  C CG2 . ILE B 1 428 ? -19.988 42.150  -1.064  1.00 38.43  ? 428 ILE B CG2 1 
ATOM   7684  C CD1 . ILE B 1 428 ? -20.296 39.101  -0.855  1.00 31.89  ? 428 ILE B CD1 1 
ATOM   7685  N N   . LEU B 1 429 ? -16.150 42.711  -0.473  1.00 24.78  ? 429 LEU B N   1 
ATOM   7686  C CA  . LEU B 1 429 ? -15.459 43.805  0.201   1.00 23.17  ? 429 LEU B CA  1 
ATOM   7687  C C   . LEU B 1 429 ? -14.599 44.602  -0.772  1.00 22.74  ? 429 LEU B C   1 
ATOM   7688  O O   . LEU B 1 429 ? -14.507 45.831  -0.666  1.00 29.83  ? 429 LEU B O   1 
ATOM   7689  C CB  . LEU B 1 429 ? -14.611 43.257  1.350   1.00 21.81  ? 429 LEU B CB  1 
ATOM   7690  C CG  . LEU B 1 429 ? -13.743 44.262  2.107   1.00 20.17  ? 429 LEU B CG  1 
ATOM   7691  C CD1 . LEU B 1 429 ? -14.592 45.078  3.056   1.00 20.22  ? 429 LEU B CD1 1 
ATOM   7692  C CD2 . LEU B 1 429 ? -12.632 43.552  2.864   1.00 18.98  ? 429 LEU B CD2 1 
ATOM   7693  N N   . ILE B 1 430 ? -13.960 43.923  -1.727  1.00 25.80  ? 430 ILE B N   1 
ATOM   7694  C CA  . ILE B 1 430 ? -13.095 44.615  -2.678  1.00 29.12  ? 430 ILE B CA  1 
ATOM   7695  C C   . ILE B 1 430 ? -13.913 45.516  -3.599  1.00 30.28  ? 430 ILE B C   1 
ATOM   7696  O O   . ILE B 1 430 ? -13.528 46.660  -3.868  1.00 33.32  ? 430 ILE B O   1 
ATOM   7697  C CB  . ILE B 1 430 ? -12.252 43.598  -3.470  1.00 29.12  ? 430 ILE B CB  1 
ATOM   7698  C CG1 . ILE B 1 430 ? -11.190 42.970  -2.564  1.00 22.27  ? 430 ILE B CG1 1 
ATOM   7699  C CG2 . ILE B 1 430 ? -11.589 44.261  -4.671  1.00 24.15  ? 430 ILE B CG2 1 
ATOM   7700  C CD1 . ILE B 1 430 ? -10.724 41.604  -3.018  1.00 24.42  ? 430 ILE B CD1 1 
ATOM   7701  N N   . GLU B 1 431 ? -15.054 45.025  -4.090  1.00 29.16  ? 431 GLU B N   1 
ATOM   7702  C CA  . GLU B 1 431 ? -15.890 45.851  -4.957  1.00 27.03  ? 431 GLU B CA  1 
ATOM   7703  C C   . GLU B 1 431 ? -16.497 47.021  -4.191  1.00 27.45  ? 431 GLU B C   1 
ATOM   7704  O O   . GLU B 1 431 ? -16.621 48.126  -4.733  1.00 31.37  ? 431 GLU B O   1 
ATOM   7705  C CB  . GLU B 1 431 ? -16.984 45.003  -5.605  1.00 28.97  ? 431 GLU B CB  1 
ATOM   7706  C CG  . GLU B 1 431 ? -16.772 44.767  -7.094  1.00 37.70  ? 431 GLU B CG  1 
ATOM   7707  C CD  . GLU B 1 431 ? -16.833 46.050  -7.905  1.00 51.76  ? 431 GLU B CD  1 
ATOM   7708  O OE1 . GLU B 1 431 ? -17.706 46.897  -7.621  1.00 48.50  ? 431 GLU B OE1 1 
ATOM   7709  O OE2 . GLU B 1 431 ? -16.003 46.211  -8.825  1.00 52.38  ? 431 GLU B OE2 1 
ATOM   7710  N N   . ALA B 1 432 ? -16.887 46.797  -2.935  1.00 26.18  ? 432 ALA B N   1 
ATOM   7711  C CA  . ALA B 1 432 ? -17.419 47.885  -2.121  1.00 25.83  ? 432 ALA B CA  1 
ATOM   7712  C C   . ALA B 1 432 ? -16.366 48.959  -1.875  1.00 27.72  ? 432 ALA B C   1 
ATOM   7713  O O   . ALA B 1 432 ? -16.657 50.156  -1.973  1.00 36.33  ? 432 ALA B O   1 
ATOM   7714  C CB  . ALA B 1 432 ? -17.951 47.340  -0.797  1.00 25.55  ? 432 ALA B CB  1 
ATOM   7715  N N   . LYS B 1 433 ? -15.134 48.550  -1.557  1.00 25.40  ? 433 LYS B N   1 
ATOM   7716  C CA  . LYS B 1 433 ? -14.071 49.520  -1.316  1.00 26.94  ? 433 LYS B CA  1 
ATOM   7717  C C   . LYS B 1 433 ? -13.780 50.354  -2.557  1.00 30.59  ? 433 LYS B C   1 
ATOM   7718  O O   . LYS B 1 433 ? -13.353 51.509  -2.445  1.00 33.96  ? 433 LYS B O   1 
ATOM   7719  C CB  . LYS B 1 433 ? -12.808 48.798  -0.848  1.00 24.24  ? 433 LYS B CB  1 
ATOM   7720  C CG  . LYS B 1 433 ? -11.616 49.698  -0.617  1.00 27.64  ? 433 LYS B CG  1 
ATOM   7721  C CD  . LYS B 1 433 ? -11.899 50.717  0.459   1.00 31.11  ? 433 LYS B CD  1 
ATOM   7722  C CE  . LYS B 1 433 ? -10.834 51.791  0.468   1.00 33.46  ? 433 LYS B CE  1 
ATOM   7723  N NZ  . LYS B 1 433 ? -11.179 52.866  1.421   1.00 27.69  ? 433 LYS B NZ  1 
ATOM   7724  N N   . LYS B 1 434 ? -14.003 49.789  -3.745  1.00 35.97  ? 434 LYS B N   1 
ATOM   7725  C CA  . LYS B 1 434 ? -13.880 50.571  -4.971  1.00 24.73  ? 434 LYS B CA  1 
ATOM   7726  C C   . LYS B 1 434 ? -14.894 51.706  -5.010  1.00 29.56  ? 434 LYS B C   1 
ATOM   7727  O O   . LYS B 1 434 ? -14.599 52.786  -5.535  1.00 28.70  ? 434 LYS B O   1 
ATOM   7728  C CB  . LYS B 1 434 ? -14.053 49.669  -6.192  1.00 26.00  ? 434 LYS B CB  1 
ATOM   7729  C CG  . LYS B 1 434 ? -12.883 48.737  -6.468  1.00 28.57  ? 434 LYS B CG  1 
ATOM   7730  C CD  . LYS B 1 434 ? -13.379 47.383  -6.952  1.00 36.12  ? 434 LYS B CD  1 
ATOM   7731  C CE  . LYS B 1 434 ? -12.473 46.787  -8.014  1.00 34.45  ? 434 LYS B CE  1 
ATOM   7732  N NZ  . LYS B 1 434 ? -13.262 46.210  -9.139  1.00 32.41  ? 434 LYS B NZ  1 
ATOM   7733  N N   . LYS B 1 435 ? -16.091 51.482  -4.465  1.00 37.61  ? 435 LYS B N   1 
ATOM   7734  C CA  . LYS B 1 435 ? -17.166 52.467  -4.473  1.00 34.57  ? 435 LYS B CA  1 
ATOM   7735  C C   . LYS B 1 435 ? -17.504 52.979  -3.076  1.00 35.60  ? 435 LYS B C   1 
ATOM   7736  O O   . LYS B 1 435 ? -18.589 53.533  -2.875  1.00 44.86  ? 435 LYS B O   1 
ATOM   7737  C CB  . LYS B 1 435 ? -18.421 51.881  -5.124  1.00 31.07  ? 435 LYS B CB  1 
ATOM   7738  C CG  . LYS B 1 435 ? -18.224 51.359  -6.536  1.00 35.23  ? 435 LYS B CG  1 
ATOM   7739  C CD  . LYS B 1 435 ? -19.559 50.983  -7.163  1.00 32.69  ? 435 LYS B CD  1 
ATOM   7740  C CE  . LYS B 1 435 ? -20.419 52.214  -7.407  1.00 33.90  ? 435 LYS B CE  1 
ATOM   7741  N NZ  . LYS B 1 435 ? -21.699 51.874  -8.086  1.00 35.79  ? 435 LYS B NZ  1 
ATOM   7742  N N   . ALA B 1 436 ? -16.613 52.797  -2.105  1.00 29.21  ? 436 ALA B N   1 
ATOM   7743  C CA  . ALA B 1 436 ? -16.905 53.221  -0.742  1.00 27.69  ? 436 ALA B CA  1 
ATOM   7744  C C   . ALA B 1 436 ? -16.928 54.743  -0.636  1.00 35.82  ? 436 ALA B C   1 
ATOM   7745  O O   . ALA B 1 436 ? -16.221 55.451  -1.358  1.00 46.32  ? 436 ALA B O   1 
ATOM   7746  C CB  . ALA B 1 436 ? -15.877 52.646  0.231   1.00 25.55  ? 436 ALA B CB  1 
ATOM   7747  N N   . LYS B 1 437 ? -17.762 55.245  0.279   1.00 30.75  ? 437 LYS B N   1 
ATOM   7748  C CA  . LYS B 1 437 ? -17.878 56.677  0.514   1.00 31.91  ? 437 LYS B CA  1 
ATOM   7749  C C   . LYS B 1 437 ? -17.852 57.085  1.979   1.00 31.69  ? 437 LYS B C   1 
ATOM   7750  O O   . LYS B 1 437 ? -17.812 58.289  2.257   1.00 39.41  ? 437 LYS B O   1 
ATOM   7751  C CB  . LYS B 1 437 ? -19.161 57.236  -0.119  1.00 34.40  ? 437 LYS B CB  1 
ATOM   7752  C CG  . LYS B 1 437 ? -18.954 57.809  -1.510  1.00 37.75  ? 437 LYS B CG  1 
ATOM   7753  C CD  . LYS B 1 437 ? -20.141 57.549  -2.422  1.00 44.87  ? 437 LYS B CD  1 
ATOM   7754  C CE  . LYS B 1 437 ? -20.003 56.226  -3.146  1.00 52.87  ? 437 LYS B CE  1 
ATOM   7755  N NZ  . LYS B 1 437 ? -18.738 56.126  -3.923  1.00 59.03  ? 437 LYS B NZ  1 
ATOM   7756  N N   . ASN B 1 438 ? -17.876 56.144  2.918   1.00 30.69  ? 438 ASN B N   1 
ATOM   7757  C CA  . ASN B 1 438 ? -17.832 56.484  4.333   1.00 32.12  ? 438 ASN B CA  1 
ATOM   7758  C C   . ASN B 1 438 ? -17.192 55.333  5.099   1.00 33.00  ? 438 ASN B C   1 
ATOM   7759  O O   . ASN B 1 438 ? -16.991 54.238  4.567   1.00 32.61  ? 438 ASN B O   1 
ATOM   7760  C CB  . ASN B 1 438 ? -19.230 56.819  4.874   1.00 36.27  ? 438 ASN B CB  1 
ATOM   7761  C CG  . ASN B 1 438 ? -20.145 55.610  4.934   1.00 36.02  ? 438 ASN B CG  1 
ATOM   7762  O OD1 . ASN B 1 438 ? -20.027 54.773  5.827   1.00 37.99  ? 438 ASN B OD1 1 
ATOM   7763  N ND2 . ASN B 1 438 ? -21.071 55.519  3.985   1.00 31.87  ? 438 ASN B ND2 1 
ATOM   7764  N N   . ASP B 1 439 ? -16.876 55.597  6.362   1.00 27.10  ? 439 ASP B N   1 
ATOM   7765  C CA  . ASP B 1 439 ? -16.085 54.676  7.175   1.00 32.45  ? 439 ASP B CA  1 
ATOM   7766  C C   . ASP B 1 439 ? -16.830 53.405  7.563   1.00 29.65  ? 439 ASP B C   1 
ATOM   7767  O O   . ASP B 1 439 ? -16.265 52.637  8.355   1.00 29.51  ? 439 ASP B O   1 
ATOM   7768  C CB  . ASP B 1 439 ? -15.585 55.392  8.429   1.00 39.35  ? 439 ASP B CB  1 
ATOM   7769  C CG  . ASP B 1 439 ? -14.302 56.158  8.183   1.00 57.86  ? 439 ASP B CG  1 
ATOM   7770  O OD1 . ASP B 1 439 ? -13.443 55.643  7.436   1.00 52.06  ? 439 ASP B OD1 1 
ATOM   7771  O OD2 . ASP B 1 439 ? -14.146 57.269  8.735   1.00 64.35  ? 439 ASP B OD2 1 
ATOM   7772  N N   . TYR B 1 440 ? -18.044 53.127  7.081   1.00 25.41  ? 440 TYR B N   1 
ATOM   7773  C CA  . TYR B 1 440 ? -18.608 51.798  7.273   1.00 19.24  ? 440 TYR B CA  1 
ATOM   7774  C C   . TYR B 1 440 ? -17.840 50.732  6.505   1.00 20.48  ? 440 TYR B C   1 
ATOM   7775  O O   . TYR B 1 440 ? -18.018 49.542  6.787   1.00 32.13  ? 440 TYR B O   1 
ATOM   7776  C CB  . TYR B 1 440 ? -20.082 51.770  6.866   1.00 21.67  ? 440 TYR B CB  1 
ATOM   7777  C CG  . TYR B 1 440 ? -21.035 52.016  8.014   1.00 20.18  ? 440 TYR B CG  1 
ATOM   7778  C CD1 . TYR B 1 440 ? -21.288 51.026  8.952   1.00 19.23  ? 440 TYR B CD1 1 
ATOM   7779  C CD2 . TYR B 1 440 ? -21.684 53.235  8.157   1.00 23.12  ? 440 TYR B CD2 1 
ATOM   7780  C CE1 . TYR B 1 440 ? -22.158 51.241  10.005  1.00 19.96  ? 440 TYR B CE1 1 
ATOM   7781  C CE2 . TYR B 1 440 ? -22.557 53.461  9.206   1.00 28.40  ? 440 TYR B CE2 1 
ATOM   7782  C CZ  . TYR B 1 440 ? -22.790 52.461  10.127  1.00 27.46  ? 440 TYR B CZ  1 
ATOM   7783  O OH  . TYR B 1 440 ? -23.659 52.687  11.171  1.00 22.75  ? 440 TYR B OH  1 
ATOM   7784  N N   . ILE B 1 441 ? -17.002 51.127  5.543   1.00 19.09  ? 441 ILE B N   1 
ATOM   7785  C CA  . ILE B 1 441 ? -16.113 50.166  4.900   1.00 20.65  ? 441 ILE B CA  1 
ATOM   7786  C C   . ILE B 1 441 ? -15.098 49.634  5.905   1.00 20.01  ? 441 ILE B C   1 
ATOM   7787  O O   . ILE B 1 441 ? -14.679 48.473  5.820   1.00 20.68  ? 441 ILE B O   1 
ATOM   7788  C CB  . ILE B 1 441 ? -15.440 50.799  3.662   1.00 22.83  ? 441 ILE B CB  1 
ATOM   7789  C CG1 . ILE B 1 441 ? -15.233 49.748  2.571   1.00 20.22  ? 441 ILE B CG1 1 
ATOM   7790  C CG2 . ILE B 1 441 ? -14.116 51.473  4.014   1.00 20.83  ? 441 ILE B CG2 1 
ATOM   7791  C CD1 . ILE B 1 441 ? -16.512 49.098  2.108   1.00 20.05  ? 441 ILE B CD1 1 
ATOM   7792  N N   . LEU B 1 442 ? -14.694 50.462  6.876   1.00 22.60  ? 442 LEU B N   1 
ATOM   7793  C CA  . LEU B 1 442 ? -13.819 49.989  7.943   1.00 20.28  ? 442 LEU B CA  1 
ATOM   7794  C C   . LEU B 1 442 ? -14.501 48.908  8.770   1.00 23.69  ? 442 LEU B C   1 
ATOM   7795  O O   . LEU B 1 442 ? -13.860 47.938  9.191   1.00 21.63  ? 442 LEU B O   1 
ATOM   7796  C CB  . LEU B 1 442 ? -13.395 51.156  8.834   1.00 19.25  ? 442 LEU B CB  1 
ATOM   7797  C CG  . LEU B 1 442 ? -12.400 52.158  8.254   1.00 20.73  ? 442 LEU B CG  1 
ATOM   7798  C CD1 . LEU B 1 442 ? -12.083 53.239  9.275   1.00 22.08  ? 442 LEU B CD1 1 
ATOM   7799  C CD2 . LEU B 1 442 ? -11.130 51.449  7.813   1.00 22.28  ? 442 LEU B CD2 1 
ATOM   7800  N N   . VAL B 1 443 ? -15.802 49.065  9.019   1.00 17.03  ? 443 VAL B N   1 
ATOM   7801  C CA  . VAL B 1 443 ? -16.551 48.057  9.764   1.00 16.60  ? 443 VAL B CA  1 
ATOM   7802  C C   . VAL B 1 443 ? -16.560 46.737  9.007   1.00 16.24  ? 443 VAL B C   1 
ATOM   7803  O O   . VAL B 1 443 ? -16.484 45.658  9.607   1.00 20.81  ? 443 VAL B O   1 
ATOM   7804  C CB  . VAL B 1 443 ? -17.980 48.557  10.047  1.00 22.19  ? 443 VAL B CB  1 
ATOM   7805  C CG1 . VAL B 1 443 ? -18.672 47.652  11.054  1.00 22.09  ? 443 VAL B CG1 1 
ATOM   7806  C CG2 . VAL B 1 443 ? -17.950 49.996  10.537  1.00 24.67  ? 443 VAL B CG2 1 
ATOM   7807  N N   . ALA B 1 444 ? -16.642 46.802  7.677   1.00 17.88  ? 444 ALA B N   1 
ATOM   7808  C CA  . ALA B 1 444 ? -16.696 45.597  6.859   1.00 19.97  ? 444 ALA B CA  1 
ATOM   7809  C C   . ALA B 1 444 ? -15.388 44.817  6.860   1.00 21.18  ? 444 ALA B C   1 
ATOM   7810  O O   . ALA B 1 444 ? -15.364 43.686  6.363   1.00 21.40  ? 444 ALA B O   1 
ATOM   7811  C CB  . ALA B 1 444 ? -17.083 45.960  5.426   1.00 16.72  ? 444 ALA B CB  1 
ATOM   7812  N N   . GLU B 1 445 ? -14.311 45.382  7.402   1.00 17.07  ? 445 GLU B N   1 
ATOM   7813  C CA  . GLU B 1 445 ? -13.014 44.722  7.428   1.00 17.77  ? 445 GLU B CA  1 
ATOM   7814  C C   . GLU B 1 445 ? -12.742 43.998  8.738   1.00 20.83  ? 445 GLU B C   1 
ATOM   7815  O O   . GLU B 1 445 ? -11.612 43.559  8.965   1.00 19.40  ? 445 GLU B O   1 
ATOM   7816  C CB  . GLU B 1 445 ? -11.902 45.732  7.148   1.00 18.37  ? 445 GLU B CB  1 
ATOM   7817  C CG  . GLU B 1 445 ? -11.921 46.264  5.731   1.00 19.21  ? 445 GLU B CG  1 
ATOM   7818  C CD  . GLU B 1 445 ? -11.361 47.665  5.629   1.00 29.82  ? 445 GLU B CD  1 
ATOM   7819  O OE1 . GLU B 1 445 ? -10.454 48.003  6.417   1.00 31.80  ? 445 GLU B OE1 1 
ATOM   7820  O OE2 . GLU B 1 445 ? -11.831 48.431  4.764   1.00 33.90  ? 445 GLU B OE2 1 
ATOM   7821  N N   . GLY B 1 446 ? -13.740 43.874  9.607   1.00 20.23  ? 446 GLY B N   1 
ATOM   7822  C CA  . GLY B 1 446 ? -13.574 43.033  10.778  1.00 18.89  ? 446 GLY B CA  1 
ATOM   7823  C C   . GLY B 1 446 ? -13.361 41.585  10.377  1.00 21.36  ? 446 GLY B C   1 
ATOM   7824  O O   . GLY B 1 446 ? -14.000 41.074  9.454   1.00 21.99  ? 446 GLY B O   1 
ATOM   7825  N N   . SER B 1 447 ? -12.432 40.920  11.069  1.00 24.35  ? 447 SER B N   1 
ATOM   7826  C CA  . SER B 1 447 ? -12.184 39.511  10.794  1.00 23.21  ? 447 SER B CA  1 
ATOM   7827  C C   . SER B 1 447 ? -13.372 38.640  11.171  1.00 23.65  ? 447 SER B C   1 
ATOM   7828  O O   . SER B 1 447 ? -13.510 37.535  10.636  1.00 24.88  ? 447 SER B O   1 
ATOM   7829  C CB  . SER B 1 447 ? -10.938 39.031  11.539  1.00 25.47  ? 447 SER B CB  1 
ATOM   7830  O OG  . SER B 1 447 ? -11.148 39.044  12.941  1.00 26.36  ? 447 SER B OG  1 
ATOM   7831  N N   . ASP B 1 448 ? -14.240 39.122  12.061  1.00 23.04  ? 448 ASP B N   1 
ATOM   7832  C CA  . ASP B 1 448 ? -15.383 38.353  12.529  1.00 23.85  ? 448 ASP B CA  1 
ATOM   7833  C C   . ASP B 1 448 ? -16.447 38.147  11.457  1.00 22.98  ? 448 ASP B C   1 
ATOM   7834  O O   . ASP B 1 448 ? -17.473 37.521  11.746  1.00 27.83  ? 448 ASP B O   1 
ATOM   7835  C CB  . ASP B 1 448 ? -15.992 39.033  13.757  1.00 23.73  ? 448 ASP B CB  1 
ATOM   7836  C CG  . ASP B 1 448 ? -14.937 39.489  14.752  1.00 24.64  ? 448 ASP B CG  1 
ATOM   7837  O OD1 . ASP B 1 448 ? -14.458 40.637  14.631  1.00 23.40  ? 448 ASP B OD1 1 
ATOM   7838  O OD2 . ASP B 1 448 ? -14.580 38.697  15.650  1.00 27.24  ? 448 ASP B OD2 1 
ATOM   7839  N N   . TRP B 1 449 ? -16.241 38.650  10.240  1.00 22.88  ? 449 TRP B N   1 
ATOM   7840  C CA  . TRP B 1 449 ? -17.159 38.406  9.133   1.00 21.41  ? 449 TRP B CA  1 
ATOM   7841  C C   . TRP B 1 449 ? -16.702 37.291  8.207   1.00 23.07  ? 449 TRP B C   1 
ATOM   7842  O O   . TRP B 1 449 ? -17.542 36.638  7.581   1.00 36.63  ? 449 TRP B O   1 
ATOM   7843  C CB  . TRP B 1 449 ? -17.351 39.678  8.299   1.00 19.66  ? 449 TRP B CB  1 
ATOM   7844  C CG  . TRP B 1 449 ? -17.707 40.893  9.092   1.00 18.99  ? 449 TRP B CG  1 
ATOM   7845  C CD1 . TRP B 1 449 ? -17.059 42.092  9.087   1.00 19.98  ? 449 TRP B CD1 1 
ATOM   7846  C CD2 . TRP B 1 449 ? -18.807 41.035  9.999   1.00 18.65  ? 449 TRP B CD2 1 
ATOM   7847  N NE1 . TRP B 1 449 ? -17.683 42.971  9.939   1.00 21.60  ? 449 TRP B NE1 1 
ATOM   7848  C CE2 . TRP B 1 449 ? -18.759 42.346  10.510  1.00 17.80  ? 449 TRP B CE2 1 
ATOM   7849  C CE3 . TRP B 1 449 ? -19.827 40.181  10.429  1.00 20.82  ? 449 TRP B CE3 1 
ATOM   7850  C CZ2 . TRP B 1 449 ? -19.687 42.822  11.428  1.00 18.02  ? 449 TRP B CZ2 1 
ATOM   7851  C CZ3 . TRP B 1 449 ? -20.748 40.655  11.341  1.00 25.72  ? 449 TRP B CZ3 1 
ATOM   7852  C CH2 . TRP B 1 449 ? -20.672 41.965  11.831  1.00 26.57  ? 449 TRP B CH2 1 
ATOM   7853  N N   . PHE B 1 450 ? -15.397 37.061  8.103   1.00 23.66  ? 450 PHE B N   1 
ATOM   7854  C CA  . PHE B 1 450 ? -14.843 36.112  7.150   1.00 25.37  ? 450 PHE B CA  1 
ATOM   7855  C C   . PHE B 1 450 ? -14.501 34.766  7.777   1.00 28.11  ? 450 PHE B C   1 
ATOM   7856  O O   . PHE B 1 450 ? -14.055 33.863  7.065   1.00 34.79  ? 450 PHE B O   1 
ATOM   7857  C CB  . PHE B 1 450 ? -13.595 36.709  6.486   1.00 25.07  ? 450 PHE B CB  1 
ATOM   7858  C CG  . PHE B 1 450 ? -13.828 38.058  5.858   1.00 24.20  ? 450 PHE B CG  1 
ATOM   7859  C CD1 . PHE B 1 450 ? -13.723 39.219  6.610   1.00 21.44  ? 450 PHE B CD1 1 
ATOM   7860  C CD2 . PHE B 1 450 ? -14.162 38.163  4.517   1.00 26.10  ? 450 PHE B CD2 1 
ATOM   7861  C CE1 . PHE B 1 450 ? -13.943 40.457  6.036   1.00 20.04  ? 450 PHE B CE1 1 
ATOM   7862  C CE2 . PHE B 1 450 ? -14.383 39.399  3.936   1.00 21.61  ? 450 PHE B CE2 1 
ATOM   7863  C CZ  . PHE B 1 450 ? -14.273 40.548  4.698   1.00 20.17  ? 450 PHE B CZ  1 
ATOM   7864  N N   . TRP B 1 451 ? -14.710 34.605  9.084   1.00 28.68  ? 451 TRP B N   1 
ATOM   7865  C CA  . TRP B 1 451 ? -14.369 33.362  9.765   1.00 31.83  ? 451 TRP B CA  1 
ATOM   7866  C C   . TRP B 1 451 ? -15.500 32.342  9.730   1.00 39.56  ? 451 TRP B C   1 
ATOM   7867  O O   . TRP B 1 451 ? -15.232 31.135  9.691   1.00 49.44  ? 451 TRP B O   1 
ATOM   7868  C CB  . TRP B 1 451 ? -13.948 33.668  11.214  1.00 32.30  ? 451 TRP B CB  1 
ATOM   7869  C CG  . TRP B 1 451 ? -14.627 32.871  12.311  1.00 48.37  ? 451 TRP B CG  1 
ATOM   7870  C CD1 . TRP B 1 451 ? -15.947 32.897  12.653  1.00 47.74  ? 451 TRP B CD1 1 
ATOM   7871  C CD2 . TRP B 1 451 ? -13.997 31.970  13.234  1.00 52.10  ? 451 TRP B CD2 1 
ATOM   7872  N NE1 . TRP B 1 451 ? -16.185 32.050  13.708  1.00 51.69  ? 451 TRP B NE1 1 
ATOM   7873  C CE2 . TRP B 1 451 ? -15.003 31.471  14.086  1.00 53.86  ? 451 TRP B CE2 1 
ATOM   7874  C CE3 . TRP B 1 451 ? -12.682 31.530  13.415  1.00 45.45  ? 451 TRP B CE3 1 
ATOM   7875  C CZ2 . TRP B 1 451 ? -14.736 30.555  15.103  1.00 43.64  ? 451 TRP B CZ2 1 
ATOM   7876  C CZ3 . TRP B 1 451 ? -12.420 30.620  14.426  1.00 44.49  ? 451 TRP B CZ3 1 
ATOM   7877  C CH2 . TRP B 1 451 ? -13.442 30.143  15.256  1.00 46.03  ? 451 TRP B CH2 1 
ATOM   7878  N N   . TRP B 1 452 ? -16.758 32.791  9.744   1.00 44.71  ? 452 TRP B N   1 
ATOM   7879  C CA  . TRP B 1 452 ? -17.882 31.856  9.773   1.00 49.77  ? 452 TRP B CA  1 
ATOM   7880  C C   . TRP B 1 452 ? -18.146 31.231  8.412   1.00 53.48  ? 452 TRP B C   1 
ATOM   7881  O O   . TRP B 1 452 ? -18.494 30.049  8.326   1.00 60.54  ? 452 TRP B O   1 
ATOM   7882  C CB  . TRP B 1 452 ? -19.144 32.564  10.271  1.00 50.04  ? 452 TRP B CB  1 
ATOM   7883  C CG  . TRP B 1 452 ? -18.930 33.362  11.512  1.00 60.28  ? 452 TRP B CG  1 
ATOM   7884  C CD1 . TRP B 1 452 ? -18.581 34.679  11.591  1.00 53.41  ? 452 TRP B CD1 1 
ATOM   7885  C CD2 . TRP B 1 452 ? -19.050 32.896  12.862  1.00 60.58  ? 452 TRP B CD2 1 
ATOM   7886  N NE1 . TRP B 1 452 ? -18.474 35.062  12.909  1.00 57.67  ? 452 TRP B NE1 1 
ATOM   7887  C CE2 . TRP B 1 452 ? -18.756 33.985  13.708  1.00 57.44  ? 452 TRP B CE2 1 
ATOM   7888  C CE3 . TRP B 1 452 ? -19.368 31.662  13.437  1.00 50.89  ? 452 TRP B CE3 1 
ATOM   7889  C CZ2 . TRP B 1 452 ? -18.776 33.877  15.096  1.00 68.42  ? 452 TRP B CZ2 1 
ATOM   7890  C CZ3 . TRP B 1 452 ? -19.388 31.558  14.818  1.00 54.90  ? 452 TRP B CZ3 1 
ATOM   7891  C CH2 . TRP B 1 452 ? -19.094 32.659  15.631  1.00 59.61  ? 452 TRP B CH2 1 
ATOM   7892  N N   . GLN B 1 453 ? -17.998 32.010  7.345   1.00 54.77  ? 453 GLN B N   1 
ATOM   7893  C CA  . GLN B 1 453 ? -18.301 31.529  6.002   1.00 51.00  ? 453 GLN B CA  1 
ATOM   7894  C C   . GLN B 1 453 ? -17.326 30.440  5.588   1.00 48.99  ? 453 GLN B C   1 
ATOM   7895  O O   . GLN B 1 453 ? -16.151 30.487  5.933   1.00 48.48  ? 453 GLN B O   1 
ATOM   7896  C CB  . GLN B 1 453 ? -18.262 32.693  5.003   1.00 44.37  ? 453 GLN B CB  1 
ATOM   7897  C CG  . GLN B 1 453 ? -19.584 33.448  4.827   1.00 51.30  ? 453 GLN B CG  1 
ATOM   7898  C CD  . GLN B 1 453 ? -20.320 33.676  6.130   1.00 61.94  ? 453 GLN B CD  1 
ATOM   7899  O OE1 . GLN B 1 453 ? -21.479 33.300  6.277   1.00 53.05  ? 453 GLN B OE1 1 
ATOM   7900  N NE2 . GLN B 1 453 ? -19.648 34.318  7.085   1.00 45.66  ? 453 GLN B NE2 1 
ATOM   7901  N N   . GLY B 1 454 ? -17.821 29.450  4.860   1.00 49.16  ? 454 GLY B N   1 
ATOM   7902  C CA  . GLY B 1 454 ? -16.996 28.360  4.387   1.00 56.39  ? 454 GLY B CA  1 
ATOM   7903  C C   . GLY B 1 454 ? -17.075 27.080  5.202   1.00 80.42  ? 454 GLY B C   1 
ATOM   7904  O O   . GLY B 1 454 ? -18.163 26.603  5.536   1.00 88.83  ? 454 GLY B O   1 
ATOM   7905  N N   . GLU B 1 455 ? -15.909 26.516  5.532   1.00 88.59  ? 455 GLU B N   1 
ATOM   7906  C CA  . GLU B 1 455 ? -15.830 25.213  6.177   1.00 96.17  ? 455 GLU B CA  1 
ATOM   7907  C C   . GLU B 1 455 ? -16.322 25.227  7.619   1.00 101.28 ? 455 GLU B C   1 
ATOM   7908  O O   . GLU B 1 455 ? -16.398 24.158  8.235   1.00 106.13 ? 455 GLU B O   1 
ATOM   7909  C CB  . GLU B 1 455 ? -14.388 24.697  6.132   1.00 77.66  ? 455 GLU B CB  1 
ATOM   7910  C CG  . GLU B 1 455 ? -14.262 23.187  5.985   1.00 99.19  ? 455 GLU B CG  1 
ATOM   7911  C CD  . GLU B 1 455 ? -14.344 22.721  4.542   1.00 103.43 ? 455 GLU B CD  1 
ATOM   7912  O OE1 . GLU B 1 455 ? -14.565 23.567  3.649   1.00 93.95  ? 455 GLU B OE1 1 
ATOM   7913  O OE2 . GLU B 1 455 ? -14.170 21.507  4.301   1.00 103.20 ? 455 GLU B OE2 1 
ATOM   7914  N N   . GLU B 1 456 ? -16.643 26.391  8.175   1.00 88.69  ? 456 GLU B N   1 
ATOM   7915  C CA  . GLU B 1 456 ? -17.046 26.496  9.570   1.00 86.23  ? 456 GLU B CA  1 
ATOM   7916  C C   . GLU B 1 456 ? -18.560 26.409  9.709   1.00 90.44  ? 456 GLU B C   1 
ATOM   7917  O O   . GLU B 1 456 ? -19.306 27.027  8.944   1.00 75.87  ? 456 GLU B O   1 
ATOM   7918  C CB  . GLU B 1 456 ? -16.526 27.802  10.175  1.00 76.98  ? 456 GLU B CB  1 
ATOM   7919  C CG  . GLU B 1 456 ? -15.250 27.605  10.972  1.00 72.48  ? 456 GLU B CG  1 
ATOM   7920  C CD  . GLU B 1 456 ? -14.035 27.390  10.089  1.00 89.46  ? 456 GLU B CD  1 
ATOM   7921  O OE1 . GLU B 1 456 ? -14.174 27.409  8.847   1.00 88.95  ? 456 GLU B OE1 1 
ATOM   7922  O OE2 . GLU B 1 456 ? -12.945 27.153  10.642  1.00 99.07  ? 456 GLU B OE2 1 
ATOM   7923  N N   . LYS B 1 457 ? -19.006 25.636  10.699  1.00 91.48  ? 457 LYS B N   1 
ATOM   7924  C CA  . LYS B 1 457 ? -20.423 25.388  10.934  1.00 82.34  ? 457 LYS B CA  1 
ATOM   7925  C C   . LYS B 1 457 ? -20.763 25.803  12.359  1.00 83.58  ? 457 LYS B C   1 
ATOM   7926  O O   . LYS B 1 457 ? -20.150 25.314  13.314  1.00 85.01  ? 457 LYS B O   1 
ATOM   7927  C CB  . LYS B 1 457 ? -20.757 23.917  10.686  1.00 72.93  ? 457 LYS B CB  1 
ATOM   7928  C CG  . LYS B 1 457 ? -20.313 23.441  9.312   1.00 70.27  ? 457 LYS B CG  1 
ATOM   7929  C CD  . LYS B 1 457 ? -19.349 22.269  9.393   1.00 65.11  ? 457 LYS B CD  1 
ATOM   7930  C CE  . LYS B 1 457 ? -20.059 20.993  9.802   1.00 70.70  ? 457 LYS B CE  1 
ATOM   7931  N NZ  . LYS B 1 457 ? -19.265 19.791  9.429   1.00 75.82  ? 457 LYS B NZ  1 
ATOM   7932  N N   . ALA B 1 458 ? -21.751 26.692  12.498  1.00 92.09  ? 458 ALA B N   1 
ATOM   7933  C CA  . ALA B 1 458 ? -22.027 27.392  13.749  1.00 85.63  ? 458 ALA B CA  1 
ATOM   7934  C C   . ALA B 1 458 ? -23.427 28.001  13.679  1.00 76.92  ? 458 ALA B C   1 
ATOM   7935  O O   . ALA B 1 458 ? -24.051 27.955  12.613  1.00 66.85  ? 458 ALA B O   1 
ATOM   7936  C CB  . ALA B 1 458 ? -20.946 28.448  13.982  1.00 73.28  ? 458 ALA B CB  1 
ATOM   7937  N N   . PRO B 1 459 ? -23.975 28.554  14.763  1.00 67.32  ? 459 PRO B N   1 
ATOM   7938  C CA  . PRO B 1 459 ? -25.317 29.134  14.691  1.00 64.91  ? 459 PRO B CA  1 
ATOM   7939  C C   . PRO B 1 459 ? -25.294 30.624  14.361  1.00 64.37  ? 459 PRO B C   1 
ATOM   7940  O O   . PRO B 1 459 ? -24.259 31.290  14.415  1.00 55.59  ? 459 PRO B O   1 
ATOM   7941  C CB  . PRO B 1 459 ? -25.885 28.898  16.103  1.00 60.88  ? 459 PRO B CB  1 
ATOM   7942  C CG  . PRO B 1 459 ? -24.703 28.578  16.985  1.00 60.84  ? 459 PRO B CG  1 
ATOM   7943  C CD  . PRO B 1 459 ? -23.458 28.591  16.143  1.00 69.80  ? 459 PRO B CD  1 
ATOM   7944  N N   . PHE B 1 460 ? -26.477 31.133  14.004  1.00 62.96  ? 460 PHE B N   1 
ATOM   7945  C CA  . PHE B 1 460 ? -26.698 32.552  13.717  1.00 48.87  ? 460 PHE B CA  1 
ATOM   7946  C C   . PHE B 1 460 ? -25.774 33.078  12.621  1.00 46.51  ? 460 PHE B C   1 
ATOM   7947  O O   . PHE B 1 460 ? -25.466 34.272  12.582  1.00 42.61  ? 460 PHE B O   1 
ATOM   7948  C CB  . PHE B 1 460 ? -26.557 33.407  14.979  1.00 39.92  ? 460 PHE B CB  1 
ATOM   7949  C CG  . PHE B 1 460 ? -27.543 33.064  16.059  1.00 47.52  ? 460 PHE B CG  1 
ATOM   7950  C CD1 . PHE B 1 460 ? -28.904 33.075  15.804  1.00 48.75  ? 460 PHE B CD1 1 
ATOM   7951  C CD2 . PHE B 1 460 ? -27.108 32.742  17.333  1.00 51.69  ? 460 PHE B CD2 1 
ATOM   7952  C CE1 . PHE B 1 460 ? -29.812 32.762  16.797  1.00 49.86  ? 460 PHE B CE1 1 
ATOM   7953  C CE2 . PHE B 1 460 ? -28.011 32.431  18.331  1.00 46.26  ? 460 PHE B CE2 1 
ATOM   7954  C CZ  . PHE B 1 460 ? -29.364 32.440  18.063  1.00 47.42  ? 460 PHE B CZ  1 
ATOM   7955  N N   . VAL B 1 461 ? -25.321 32.201  11.722  1.00 45.00  ? 461 VAL B N   1 
ATOM   7956  C CA  . VAL B 1 461 ? -24.498 32.659  10.606  1.00 41.44  ? 461 VAL B CA  1 
ATOM   7957  C C   . VAL B 1 461 ? -25.310 33.545  9.672   1.00 41.18  ? 461 VAL B C   1 
ATOM   7958  O O   . VAL B 1 461 ? -24.753 34.414  8.988   1.00 40.87  ? 461 VAL B O   1 
ATOM   7959  C CB  . VAL B 1 461 ? -23.869 31.465  9.858   1.00 36.42  ? 461 VAL B CB  1 
ATOM   7960  C CG1 . VAL B 1 461 ? -23.283 30.469  10.843  1.00 46.11  ? 461 VAL B CG1 1 
ATOM   7961  C CG2 . VAL B 1 461 ? -24.887 30.788  8.950   1.00 38.51  ? 461 VAL B CG2 1 
ATOM   7962  N N   . GLU B 1 462 ? -26.631 33.351  9.629   1.00 38.32  ? 462 GLU B N   1 
ATOM   7963  C CA  . GLU B 1 462 ? -27.481 34.201  8.801   1.00 41.23  ? 462 GLU B CA  1 
ATOM   7964  C C   . GLU B 1 462 ? -27.463 35.643  9.289   1.00 33.30  ? 462 GLU B C   1 
ATOM   7965  O O   . GLU B 1 462 ? -27.485 36.580  8.482   1.00 29.20  ? 462 GLU B O   1 
ATOM   7966  C CB  . GLU B 1 462 ? -28.909 33.655  8.783   1.00 41.08  ? 462 GLU B CB  1 
ATOM   7967  C CG  . GLU B 1 462 ? -29.167 32.642  7.677   1.00 59.00  ? 462 GLU B CG  1 
ATOM   7968  C CD  . GLU B 1 462 ? -29.140 31.210  8.176   1.00 76.55  ? 462 GLU B CD  1 
ATOM   7969  O OE1 . GLU B 1 462 ? -30.152 30.498  8.002   1.00 83.93  ? 462 GLU B OE1 1 
ATOM   7970  O OE2 . GLU B 1 462 ? -28.107 30.797  8.744   1.00 80.16  ? 462 GLU B OE2 1 
ATOM   7971  N N   . VAL B 1 463 ? -27.432 35.844  10.609  1.00 35.18  ? 463 VAL B N   1 
ATOM   7972  C CA  . VAL B 1 463 ? -27.373 37.200  11.147  1.00 28.87  ? 463 VAL B CA  1 
ATOM   7973  C C   . VAL B 1 463 ? -26.029 37.843  10.826  1.00 26.38  ? 463 VAL B C   1 
ATOM   7974  O O   . VAL B 1 463 ? -25.959 39.034  10.498  1.00 26.25  ? 463 VAL B O   1 
ATOM   7975  C CB  . VAL B 1 463 ? -27.659 37.190  12.659  1.00 30.08  ? 463 VAL B CB  1 
ATOM   7976  C CG1 . VAL B 1 463 ? -27.224 38.501  13.291  1.00 28.22  ? 463 VAL B CG1 1 
ATOM   7977  C CG2 . VAL B 1 463 ? -29.137 36.944  12.915  1.00 32.51  ? 463 VAL B CG2 1 
ATOM   7978  N N   . PHE B 1 464 ? -24.943 37.070  10.909  1.00 28.83  ? 464 PHE B N   1 
ATOM   7979  C CA  . PHE B 1 464 ? -23.638 37.589  10.512  1.00 26.56  ? 464 PHE B CA  1 
ATOM   7980  C C   . PHE B 1 464 ? -23.651 38.015  9.052   1.00 25.83  ? 464 PHE B C   1 
ATOM   7981  O O   . PHE B 1 464 ? -23.159 39.094  8.702   1.00 24.12  ? 464 PHE B O   1 
ATOM   7982  C CB  . PHE B 1 464 ? -22.554 36.538  10.751  1.00 29.89  ? 464 PHE B CB  1 
ATOM   7983  C CG  . PHE B 1 464 ? -22.194 36.354  12.192  1.00 29.07  ? 464 PHE B CG  1 
ATOM   7984  C CD1 . PHE B 1 464 ? -21.593 37.377  12.905  1.00 25.31  ? 464 PHE B CD1 1 
ATOM   7985  C CD2 . PHE B 1 464 ? -22.454 35.155  12.836  1.00 41.93  ? 464 PHE B CD2 1 
ATOM   7986  C CE1 . PHE B 1 464 ? -21.261 37.208  14.235  1.00 38.66  ? 464 PHE B CE1 1 
ATOM   7987  C CE2 . PHE B 1 464 ? -22.125 34.979  14.166  1.00 45.51  ? 464 PHE B CE2 1 
ATOM   7988  C CZ  . PHE B 1 464 ? -21.527 36.007  14.867  1.00 45.53  ? 464 PHE B CZ  1 
ATOM   7989  N N   . ASP B 1 465 ? -24.221 37.176  8.184   1.00 29.61  ? 465 ASP B N   1 
ATOM   7990  C CA  . ASP B 1 465 ? -24.353 37.531  6.775   1.00 24.75  ? 465 ASP B CA  1 
ATOM   7991  C C   . ASP B 1 465 ? -25.159 38.810  6.605   1.00 23.89  ? 465 ASP B C   1 
ATOM   7992  O O   . ASP B 1 465 ? -24.747 39.724  5.883   1.00 27.81  ? 465 ASP B O   1 
ATOM   7993  C CB  . ASP B 1 465 ? -25.006 36.384  6.003   1.00 27.11  ? 465 ASP B CB  1 
ATOM   7994  C CG  . ASP B 1 465 ? -25.254 36.730  4.549   1.00 33.26  ? 465 ASP B CG  1 
ATOM   7995  O OD1 . ASP B 1 465 ? -24.271 36.919  3.800   1.00 35.19  ? 465 ASP B OD1 1 
ATOM   7996  O OD2 . ASP B 1 465 ? -26.436 36.826  4.158   1.00 32.02  ? 465 ASP B OD2 1 
ATOM   7997  N N   . LYS B 1 466 ? -26.311 38.897  7.277   1.00 24.85  ? 466 LYS B N   1 
ATOM   7998  C CA  . LYS B 1 466 ? -27.160 40.078  7.146   1.00 24.67  ? 466 LYS B CA  1 
ATOM   7999  C C   . LYS B 1 466 ? -26.424 41.341  7.577   1.00 22.73  ? 466 LYS B C   1 
ATOM   8000  O O   . LYS B 1 466 ? -26.601 42.407  6.977   1.00 23.11  ? 466 LYS B O   1 
ATOM   8001  C CB  . LYS B 1 466 ? -28.440 39.898  7.961   1.00 26.38  ? 466 LYS B CB  1 
ATOM   8002  C CG  . LYS B 1 466 ? -29.395 41.081  7.885   1.00 26.81  ? 466 LYS B CG  1 
ATOM   8003  C CD  . LYS B 1 466 ? -30.418 41.049  9.010   1.00 32.30  ? 466 LYS B CD  1 
ATOM   8004  C CE  . LYS B 1 466 ? -31.732 41.692  8.591   1.00 39.76  ? 466 LYS B CE  1 
ATOM   8005  N NZ  . LYS B 1 466 ? -32.854 41.312  9.495   1.00 32.64  ? 466 LYS B NZ  1 
ATOM   8006  N N   . LEU B 1 467 ? -25.585 41.239  8.611   1.00 28.61  ? 467 LEU B N   1 
ATOM   8007  C CA  . LEU B 1 467 ? -24.863 42.410  9.098   1.00 20.44  ? 467 LEU B CA  1 
ATOM   8008  C C   . LEU B 1 467 ? -23.769 42.834  8.125   1.00 25.24  ? 467 LEU B C   1 
ATOM   8009  O O   . LEU B 1 467 ? -23.625 44.024  7.822   1.00 29.65  ? 467 LEU B O   1 
ATOM   8010  C CB  . LEU B 1 467 ? -24.274 42.131  10.480  1.00 20.37  ? 467 LEU B CB  1 
ATOM   8011  C CG  . LEU B 1 467 ? -25.221 42.327  11.664  1.00 21.53  ? 467 LEU B CG  1 
ATOM   8012  C CD1 . LEU B 1 467 ? -24.832 41.412  12.814  1.00 22.48  ? 467 LEU B CD1 1 
ATOM   8013  C CD2 . LEU B 1 467 ? -25.229 43.781  12.107  1.00 21.03  ? 467 LEU B CD2 1 
ATOM   8014  N N   . PHE B 1 468 ? -22.983 41.875  7.625   1.00 22.02  ? 468 PHE B N   1 
ATOM   8015  C CA  . PHE B 1 468 ? -21.894 42.213  6.711   1.00 18.78  ? 468 PHE B CA  1 
ATOM   8016  C C   . PHE B 1 468 ? -22.423 42.917  5.470   1.00 22.44  ? 468 PHE B C   1 
ATOM   8017  O O   . PHE B 1 468 ? -21.909 43.967  5.069   1.00 26.73  ? 468 PHE B O   1 
ATOM   8018  C CB  . PHE B 1 468 ? -21.115 40.954  6.324   1.00 21.00  ? 468 PHE B CB  1 
ATOM   8019  C CG  . PHE B 1 468 ? -20.042 41.197  5.295   1.00 18.88  ? 468 PHE B CG  1 
ATOM   8020  C CD1 . PHE B 1 468 ? -18.842 41.786  5.654   1.00 18.07  ? 468 PHE B CD1 1 
ATOM   8021  C CD2 . PHE B 1 468 ? -20.232 40.836  3.970   1.00 24.20  ? 468 PHE B CD2 1 
ATOM   8022  C CE1 . PHE B 1 468 ? -17.853 42.011  4.712   1.00 18.21  ? 468 PHE B CE1 1 
ATOM   8023  C CE2 . PHE B 1 468 ? -19.244 41.060  3.023   1.00 20.01  ? 468 PHE B CE2 1 
ATOM   8024  C CZ  . PHE B 1 468 ? -18.056 41.647  3.395   1.00 19.18  ? 468 PHE B CZ  1 
ATOM   8025  N N   . ARG B 1 469 ? -23.464 42.355  4.856   1.00 21.13  ? 469 ARG B N   1 
ATOM   8026  C CA  . ARG B 1 469 ? -24.031 42.960  3.659   1.00 21.13  ? 469 ARG B CA  1 
ATOM   8027  C C   . ARG B 1 469 ? -24.676 44.305  3.964   1.00 25.04  ? 469 ARG B C   1 
ATOM   8028  O O   . ARG B 1 469 ? -24.686 45.195  3.107   1.00 32.86  ? 469 ARG B O   1 
ATOM   8029  C CB  . ARG B 1 469 ? -25.033 42.001  3.022   1.00 22.97  ? 469 ARG B CB  1 
ATOM   8030  C CG  . ARG B 1 469 ? -24.484 40.590  2.911   1.00 28.40  ? 469 ARG B CG  1 
ATOM   8031  C CD  . ARG B 1 469 ? -25.437 39.636  2.226   1.00 34.20  ? 469 ARG B CD  1 
ATOM   8032  N NE  . ARG B 1 469 ? -24.712 38.523  1.625   1.00 27.88  ? 469 ARG B NE  1 
ATOM   8033  C CZ  . ARG B 1 469 ? -24.054 38.593  0.476   1.00 32.65  ? 469 ARG B CZ  1 
ATOM   8034  N NH1 . ARG B 1 469 ? -24.038 39.703  -0.245  1.00 34.50  ? 469 ARG B NH1 1 
ATOM   8035  N NH2 . ARG B 1 469 ? -23.390 37.526  0.042   1.00 34.62  ? 469 ARG B NH2 1 
ATOM   8036  N N   . SER B 1 470 ? -25.214 44.475  5.173   1.00 34.60  ? 470 SER B N   1 
ATOM   8037  C CA  . SER B 1 470 ? -25.746 45.776  5.562   1.00 29.12  ? 470 SER B CA  1 
ATOM   8038  C C   . SER B 1 470 ? -24.636 46.815  5.660   1.00 29.59  ? 470 SER B C   1 
ATOM   8039  O O   . SER B 1 470 ? -24.824 47.970  5.259   1.00 34.65  ? 470 SER B O   1 
ATOM   8040  C CB  . SER B 1 470 ? -26.501 45.666  6.888   1.00 28.53  ? 470 SER B CB  1 
ATOM   8041  O OG  . SER B 1 470 ? -27.858 46.045  6.733   1.00 25.63  ? 470 SER B OG  1 
ATOM   8042  N N   . PHE B 1 471 ? -23.471 46.425  6.191   1.00 28.00  ? 471 PHE B N   1 
ATOM   8043  C CA  . PHE B 1 471 ? -22.352 47.361  6.282   1.00 25.02  ? 471 PHE B CA  1 
ATOM   8044  C C   . PHE B 1 471 ? -21.774 47.673  4.906   1.00 24.12  ? 471 PHE B C   1 
ATOM   8045  O O   . PHE B 1 471 ? -21.405 48.820  4.628   1.00 27.16  ? 471 PHE B O   1 
ATOM   8046  C CB  . PHE B 1 471 ? -21.267 46.805  7.204   1.00 19.95  ? 471 PHE B CB  1 
ATOM   8047  C CG  . PHE B 1 471 ? -21.681 46.721  8.647   1.00 20.01  ? 471 PHE B CG  1 
ATOM   8048  C CD1 . PHE B 1 471 ? -22.298 47.794  9.268   1.00 21.40  ? 471 PHE B CD1 1 
ATOM   8049  C CD2 . PHE B 1 471 ? -21.443 45.576  9.386   1.00 24.17  ? 471 PHE B CD2 1 
ATOM   8050  C CE1 . PHE B 1 471 ? -22.678 47.721  10.594  1.00 24.52  ? 471 PHE B CE1 1 
ATOM   8051  C CE2 . PHE B 1 471 ? -21.821 45.498  10.714  1.00 23.13  ? 471 PHE B CE2 1 
ATOM   8052  C CZ  . PHE B 1 471 ? -22.439 46.572  11.317  1.00 18.37  ? 471 PHE B CZ  1 
ATOM   8053  N N   . VAL B 1 472 ? -21.676 46.664  4.036   1.00 26.64  ? 472 VAL B N   1 
ATOM   8054  C CA  . VAL B 1 472 ? -21.194 46.897  2.677   1.00 23.03  ? 472 VAL B CA  1 
ATOM   8055  C C   . VAL B 1 472 ? -22.163 47.794  1.913   1.00 30.09  ? 472 VAL B C   1 
ATOM   8056  O O   . VAL B 1 472 ? -21.748 48.711  1.192   1.00 27.10  ? 472 VAL B O   1 
ATOM   8057  C CB  . VAL B 1 472 ? -20.965 45.553  1.960   1.00 21.95  ? 472 VAL B CB  1 
ATOM   8058  C CG1 . VAL B 1 472 ? -21.117 45.704  0.453   1.00 25.28  ? 472 VAL B CG1 1 
ATOM   8059  C CG2 . VAL B 1 472 ? -19.595 44.991  2.310   1.00 30.35  ? 472 VAL B CG2 1 
ATOM   8060  N N   . ARG B 1 473 ? -23.466 47.542  2.057   1.00 38.81  ? 473 ARG B N   1 
ATOM   8061  C CA  . ARG B 1 473 ? -24.467 48.401  1.433   1.00 30.36  ? 473 ARG B CA  1 
ATOM   8062  C C   . ARG B 1 473 ? -24.400 49.821  1.986   1.00 27.21  ? 473 ARG B C   1 
ATOM   8063  O O   . ARG B 1 473 ? -24.472 50.796  1.229   1.00 36.41  ? 473 ARG B O   1 
ATOM   8064  C CB  . ARG B 1 473 ? -25.861 47.808  1.644   1.00 28.89  ? 473 ARG B CB  1 
ATOM   8065  C CG  . ARG B 1 473 ? -26.886 48.177  0.585   1.00 43.20  ? 473 ARG B CG  1 
ATOM   8066  C CD  . ARG B 1 473 ? -28.293 47.825  1.048   1.00 51.58  ? 473 ARG B CD  1 
ATOM   8067  N NE  . ARG B 1 473 ? -29.209 48.955  0.946   1.00 56.97  ? 473 ARG B NE  1 
ATOM   8068  C CZ  . ARG B 1 473 ? -30.484 48.922  1.311   1.00 56.24  ? 473 ARG B CZ  1 
ATOM   8069  N NH1 . ARG B 1 473 ? -31.030 47.829  1.817   1.00 67.11  ? 473 ARG B NH1 1 
ATOM   8070  N NH2 . ARG B 1 473 ? -31.229 50.014  1.163   1.00 47.42  ? 473 ARG B NH2 1 
ATOM   8071  N N   . ARG B 1 474 ? -24.252 49.956  3.306   1.00 25.75  ? 474 ARG B N   1 
ATOM   8072  C CA  . ARG B 1 474 ? -24.260 51.276  3.930   1.00 32.32  ? 474 ARG B CA  1 
ATOM   8073  C C   . ARG B 1 474 ? -23.003 52.075  3.600   1.00 31.65  ? 474 ARG B C   1 
ATOM   8074  O O   . ARG B 1 474 ? -23.057 53.308  3.528   1.00 38.30  ? 474 ARG B O   1 
ATOM   8075  C CB  . ARG B 1 474 ? -24.419 51.132  5.445   1.00 33.48  ? 474 ARG B CB  1 
ATOM   8076  C CG  . ARG B 1 474 ? -24.576 52.444  6.197   1.00 39.12  ? 474 ARG B CG  1 
ATOM   8077  C CD  . ARG B 1 474 ? -25.868 53.157  5.823   1.00 37.72  ? 474 ARG B CD  1 
ATOM   8078  N NE  . ARG B 1 474 ? -25.616 54.373  5.059   1.00 42.42  ? 474 ARG B NE  1 
ATOM   8079  C CZ  . ARG B 1 474 ? -25.160 55.505  5.578   1.00 44.40  ? 474 ARG B CZ  1 
ATOM   8080  N NH1 . ARG B 1 474 ? -24.910 55.622  6.872   1.00 37.72  ? 474 ARG B NH1 1 
ATOM   8081  N NH2 . ARG B 1 474 ? -24.953 56.548  4.779   1.00 50.13  ? 474 ARG B NH2 1 
ATOM   8082  N N   . ALA B 1 475 ? -21.870 51.400  3.399   1.00 27.06  ? 475 ALA B N   1 
ATOM   8083  C CA  . ALA B 1 475 ? -20.613 52.101  3.171   1.00 24.62  ? 475 ALA B CA  1 
ATOM   8084  C C   . ALA B 1 475 ? -20.585 52.858  1.849   1.00 33.37  ? 475 ALA B C   1 
ATOM   8085  O O   . ALA B 1 475 ? -19.768 53.772  1.694   1.00 37.14  ? 475 ALA B O   1 
ATOM   8086  C CB  . ALA B 1 475 ? -19.445 51.116  3.221   1.00 21.69  ? 475 ALA B CB  1 
ATOM   8087  N N   . GLN B 1 476 ? -21.448 52.505  0.897   1.00 32.25  ? 476 GLN B N   1 
ATOM   8088  C CA  . GLN B 1 476 ? -21.437 53.139  -0.415  1.00 33.69  ? 476 GLN B CA  1 
ATOM   8089  C C   . GLN B 1 476 ? -22.430 54.287  -0.543  1.00 42.21  ? 476 GLN B C   1 
ATOM   8090  O O   . GLN B 1 476 ? -22.362 55.032  -1.526  1.00 51.02  ? 476 GLN B O   1 
ATOM   8091  C CB  . GLN B 1 476 ? -21.725 52.105  -1.508  1.00 29.43  ? 476 GLN B CB  1 
ATOM   8092  C CG  . GLN B 1 476 ? -20.591 51.129  -1.761  1.00 27.93  ? 476 GLN B CG  1 
ATOM   8093  C CD  . GLN B 1 476 ? -21.087 49.766  -2.198  1.00 27.85  ? 476 GLN B CD  1 
ATOM   8094  O OE1 . GLN B 1 476 ? -21.267 49.512  -3.390  1.00 32.17  ? 476 GLN B OE1 1 
ATOM   8095  N NE2 . GLN B 1 476 ? -21.322 48.884  -1.234  1.00 30.58  ? 476 GLN B NE2 1 
ATOM   8096  N N   . GLU B 1 477 ? -23.344 54.450  0.405   1.00 45.56  ? 477 GLU B N   1 
ATOM   8097  C CA  . GLU B 1 477 ? -24.355 55.494  0.289   1.00 44.06  ? 477 GLU B CA  1 
ATOM   8098  C C   . GLU B 1 477 ? -23.844 56.829  0.821   1.00 51.47  ? 477 GLU B C   1 
ATOM   8099  O O   . GLU B 1 477 ? -24.139 57.885  0.260   1.00 45.34  ? 477 GLU B O   1 
ATOM   8100  C CB  . GLU B 1 477 ? -25.630 55.081  1.022   1.00 42.90  ? 477 GLU B CB  1 
ATOM   8101  C CG  . GLU B 1 477 ? -26.184 53.739  0.577   1.00 39.37  ? 477 GLU B CG  1 
ATOM   8102  C CD  . GLU B 1 477 ? -27.546 53.450  1.172   1.00 48.75  ? 477 GLU B CD  1 
ATOM   8103  O OE1 . GLU B 1 477 ? -28.145 54.374  1.761   1.00 53.81  ? 477 GLU B OE1 1 
ATOM   8104  O OE2 . GLU B 1 477 ? -28.017 52.299  1.054   1.00 48.12  ? 477 GLU B OE2 1 
ATOM   8105  N N   . MET C 1 1   ? 33.218  20.595  39.696  1.00 60.60  ? 1   MET C N   1 
ATOM   8106  C CA  . MET C 1 1   ? 34.113  19.696  40.415  1.00 59.55  ? 1   MET C CA  1 
ATOM   8107  C C   . MET C 1 1   ? 33.376  18.986  41.546  1.00 54.87  ? 1   MET C C   1 
ATOM   8108  O O   . MET C 1 1   ? 33.368  17.755  41.618  1.00 59.32  ? 1   MET C O   1 
ATOM   8109  C CB  . MET C 1 1   ? 35.315  20.467  40.969  1.00 55.27  ? 1   MET C CB  1 
ATOM   8110  C CG  . MET C 1 1   ? 36.561  19.618  41.196  1.00 50.86  ? 1   MET C CG  1 
ATOM   8111  S SD  . MET C 1 1   ? 36.466  18.505  42.612  1.00 64.22  ? 1   MET C SD  1 
ATOM   8112  C CE  . MET C 1 1   ? 37.717  19.219  43.673  1.00 50.10  ? 1   MET C CE  1 
ATOM   8113  N N   . LYS C 1 2   ? 32.758  19.769  42.427  1.00 46.75  ? 2   LYS C N   1 
ATOM   8114  C CA  . LYS C 1 2   ? 32.056  19.216  43.580  1.00 44.89  ? 2   LYS C CA  1 
ATOM   8115  C C   . LYS C 1 2   ? 30.838  18.434  43.106  1.00 44.29  ? 2   LYS C C   1 
ATOM   8116  O O   . LYS C 1 2   ? 29.856  19.019  42.637  1.00 46.19  ? 2   LYS C O   1 
ATOM   8117  C CB  . LYS C 1 2   ? 31.646  20.330  44.541  1.00 53.00  ? 2   LYS C CB  1 
ATOM   8118  C CG  . LYS C 1 2   ? 31.634  19.909  46.005  1.00 44.88  ? 2   LYS C CG  1 
ATOM   8119  C CD  . LYS C 1 2   ? 30.712  20.790  46.840  1.00 48.13  ? 2   LYS C CD  1 
ATOM   8120  C CE  . LYS C 1 2   ? 31.209  22.226  46.918  1.00 54.44  ? 2   LYS C CE  1 
ATOM   8121  N NZ  . LYS C 1 2   ? 32.669  22.299  47.196  1.00 51.64  ? 2   LYS C NZ  1 
ATOM   8122  N N   . LYS C 1 3   ? 30.907  17.112  43.218  1.00 42.07  ? 3   LYS C N   1 
ATOM   8123  C CA  . LYS C 1 3   ? 29.789  16.226  42.924  1.00 42.72  ? 3   LYS C CA  1 
ATOM   8124  C C   . LYS C 1 3   ? 29.302  15.606  44.226  1.00 53.02  ? 3   LYS C C   1 
ATOM   8125  O O   . LYS C 1 3   ? 30.105  15.068  44.996  1.00 52.71  ? 3   LYS C O   1 
ATOM   8126  C CB  . LYS C 1 3   ? 30.201  15.131  41.934  1.00 43.67  ? 3   LYS C CB  1 
ATOM   8127  C CG  . LYS C 1 3   ? 29.434  15.134  40.616  1.00 45.05  ? 3   LYS C CG  1 
ATOM   8128  C CD  . LYS C 1 3   ? 30.012  14.119  39.634  1.00 41.35  ? 3   LYS C CD  1 
ATOM   8129  C CE  . LYS C 1 3   ? 28.971  13.663  38.623  1.00 41.24  ? 3   LYS C CE  1 
ATOM   8130  N NZ  . LYS C 1 3   ? 29.561  12.873  37.506  1.00 42.01  ? 3   LYS C NZ  1 
ATOM   8131  N N   . LEU C 1 4   ? 27.998  15.696  44.477  1.00 51.18  ? 4   LEU C N   1 
ATOM   8132  C CA  . LEU C 1 4   ? 27.412  15.044  45.641  1.00 48.84  ? 4   LEU C CA  1 
ATOM   8133  C C   . LEU C 1 4   ? 27.203  13.566  45.341  1.00 46.44  ? 4   LEU C C   1 
ATOM   8134  O O   . LEU C 1 4   ? 26.674  13.206  44.285  1.00 50.74  ? 4   LEU C O   1 
ATOM   8135  C CB  . LEU C 1 4   ? 26.089  15.704  46.031  1.00 40.06  ? 4   LEU C CB  1 
ATOM   8136  C CG  . LEU C 1 4   ? 25.498  15.286  47.380  1.00 35.30  ? 4   LEU C CG  1 
ATOM   8137  C CD1 . LEU C 1 4   ? 24.891  16.483  48.093  1.00 36.87  ? 4   LEU C CD1 1 
ATOM   8138  C CD2 . LEU C 1 4   ? 24.458  14.186  47.206  1.00 34.01  ? 4   LEU C CD2 1 
ATOM   8139  N N   . PHE C 1 5   ? 27.617  12.713  46.270  1.00 36.30  ? 5   PHE C N   1 
ATOM   8140  C CA  . PHE C 1 5   ? 27.578  11.271  46.076  1.00 35.14  ? 5   PHE C CA  1 
ATOM   8141  C C   . PHE C 1 5   ? 26.415  10.675  46.853  1.00 32.82  ? 5   PHE C C   1 
ATOM   8142  O O   . PHE C 1 5   ? 26.274  10.919  48.056  1.00 38.05  ? 5   PHE C O   1 
ATOM   8143  C CB  . PHE C 1 5   ? 28.901  10.637  46.503  1.00 34.96  ? 5   PHE C CB  1 
ATOM   8144  C CG  . PHE C 1 5   ? 30.064  11.052  45.650  1.00 42.93  ? 5   PHE C CG  1 
ATOM   8145  C CD1 . PHE C 1 5   ? 30.055  10.815  44.286  1.00 48.37  ? 5   PHE C CD1 1 
ATOM   8146  C CD2 . PHE C 1 5   ? 31.157  11.698  46.206  1.00 43.10  ? 5   PHE C CD2 1 
ATOM   8147  C CE1 . PHE C 1 5   ? 31.118  11.200  43.491  1.00 48.27  ? 5   PHE C CE1 1 
ATOM   8148  C CE2 . PHE C 1 5   ? 32.226  12.085  45.417  1.00 45.64  ? 5   PHE C CE2 1 
ATOM   8149  C CZ  . PHE C 1 5   ? 32.207  11.836  44.058  1.00 48.30  ? 5   PHE C CZ  1 
ATOM   8150  N N   . LEU C 1 6   ? 25.585  9.898   46.162  1.00 34.14  ? 6   LEU C N   1 
ATOM   8151  C CA  . LEU C 1 6   ? 24.345  9.365   46.714  1.00 30.47  ? 6   LEU C CA  1 
ATOM   8152  C C   . LEU C 1 6   ? 24.419  7.844   46.724  1.00 33.03  ? 6   LEU C C   1 
ATOM   8153  O O   . LEU C 1 6   ? 24.476  7.213   45.663  1.00 43.88  ? 6   LEU C O   1 
ATOM   8154  C CB  . LEU C 1 6   ? 23.143  9.843   45.902  1.00 30.86  ? 6   LEU C CB  1 
ATOM   8155  C CG  . LEU C 1 6   ? 21.777  9.627   46.553  1.00 34.03  ? 6   LEU C CG  1 
ATOM   8156  C CD1 . LEU C 1 6   ? 21.849  9.920   48.040  1.00 31.57  ? 6   LEU C CD1 1 
ATOM   8157  C CD2 . LEU C 1 6   ? 20.726  10.495  45.885  1.00 35.04  ? 6   LEU C CD2 1 
ATOM   8158  N N   . VAL C 1 7   ? 24.403  7.254   47.914  1.00 28.66  ? 7   VAL C N   1 
ATOM   8159  C CA  . VAL C 1 7   ? 24.422  5.806   48.079  1.00 27.83  ? 7   VAL C CA  1 
ATOM   8160  C C   . VAL C 1 7   ? 23.068  5.381   48.627  1.00 32.46  ? 7   VAL C C   1 
ATOM   8161  O O   . VAL C 1 7   ? 22.649  5.844   49.696  1.00 31.36  ? 7   VAL C O   1 
ATOM   8162  C CB  . VAL C 1 7   ? 25.563  5.354   49.003  1.00 27.66  ? 7   VAL C CB  1 
ATOM   8163  C CG1 . VAL C 1 7   ? 25.618  3.836   49.073  1.00 26.99  ? 7   VAL C CG1 1 
ATOM   8164  C CG2 . VAL C 1 7   ? 26.890  5.917   48.523  1.00 29.22  ? 7   VAL C CG2 1 
ATOM   8165  N N   . PHE C 1 8   ? 22.382  4.509   47.896  1.00 38.93  ? 8   PHE C N   1 
ATOM   8166  C CA  . PHE C 1 8   ? 21.106  3.953   48.324  1.00 28.86  ? 8   PHE C CA  1 
ATOM   8167  C C   . PHE C 1 8   ? 21.311  2.520   48.795  1.00 30.77  ? 8   PHE C C   1 
ATOM   8168  O O   . PHE C 1 8   ? 21.867  1.694   48.065  1.00 26.22  ? 8   PHE C O   1 
ATOM   8169  C CB  . PHE C 1 8   ? 20.079  3.986   47.193  1.00 30.87  ? 8   PHE C CB  1 
ATOM   8170  C CG  . PHE C 1 8   ? 19.377  5.304   47.044  1.00 38.03  ? 8   PHE C CG  1 
ATOM   8171  C CD1 . PHE C 1 8   ? 18.331  5.643   47.884  1.00 38.62  ? 8   PHE C CD1 1 
ATOM   8172  C CD2 . PHE C 1 8   ? 19.750  6.195   46.052  1.00 41.34  ? 8   PHE C CD2 1 
ATOM   8173  C CE1 . PHE C 1 8   ? 17.677  6.852   47.746  1.00 45.32  ? 8   PHE C CE1 1 
ATOM   8174  C CE2 . PHE C 1 8   ? 19.098  7.404   45.907  1.00 37.37  ? 8   PHE C CE2 1 
ATOM   8175  C CZ  . PHE C 1 8   ? 18.061  7.734   46.755  1.00 41.50  ? 8   PHE C CZ  1 
ATOM   8176  N N   . TRP C 1 9   ? 20.851  2.230   50.009  1.00 31.34  ? 9   TRP C N   1 
ATOM   8177  C CA  . TRP C 1 9   ? 20.983  0.905   50.609  1.00 31.79  ? 9   TRP C CA  1 
ATOM   8178  C C   . TRP C 1 9   ? 19.613  0.486   51.132  1.00 30.17  ? 9   TRP C C   1 
ATOM   8179  O O   . TRP C 1 9   ? 19.166  0.976   52.174  1.00 24.83  ? 9   TRP C O   1 
ATOM   8180  C CB  . TRP C 1 9   ? 22.024  0.917   51.722  1.00 30.37  ? 9   TRP C CB  1 
ATOM   8181  C CG  . TRP C 1 9   ? 22.734  -0.381  51.934  1.00 29.00  ? 9   TRP C CG  1 
ATOM   8182  C CD1 . TRP C 1 9   ? 22.347  -1.615  51.501  1.00 23.62  ? 9   TRP C CD1 1 
ATOM   8183  C CD2 . TRP C 1 9   ? 23.952  -0.577  52.663  1.00 36.05  ? 9   TRP C CD2 1 
ATOM   8184  N NE1 . TRP C 1 9   ? 23.255  -2.566  51.905  1.00 23.61  ? 9   TRP C NE1 1 
ATOM   8185  C CE2 . TRP C 1 9   ? 24.249  -1.953  52.621  1.00 29.27  ? 9   TRP C CE2 1 
ATOM   8186  C CE3 . TRP C 1 9   ? 24.823  0.280   53.342  1.00 34.89  ? 9   TRP C CE3 1 
ATOM   8187  C CZ2 . TRP C 1 9   ? 25.378  -2.491  53.233  1.00 27.26  ? 9   TRP C CZ2 1 
ATOM   8188  C CZ3 . TRP C 1 9   ? 25.944  -0.258  53.946  1.00 33.16  ? 9   TRP C CZ3 1 
ATOM   8189  C CH2 . TRP C 1 9   ? 26.211  -1.629  53.889  1.00 31.44  ? 9   TRP C CH2 1 
ATOM   8190  N N   . TRP C 1 10  ? 18.946  -0.414  50.413  1.00 25.00  ? 10  TRP C N   1 
ATOM   8191  C CA  . TRP C 1 10  ? 17.661  -0.946  50.843  1.00 30.41  ? 10  TRP C CA  1 
ATOM   8192  C C   . TRP C 1 10  ? 17.887  -2.254  51.595  1.00 23.20  ? 10  TRP C C   1 
ATOM   8193  O O   . TRP C 1 10  ? 18.617  -3.132  51.121  1.00 23.11  ? 10  TRP C O   1 
ATOM   8194  C CB  . TRP C 1 10  ? 16.729  -1.163  49.650  1.00 30.38  ? 10  TRP C CB  1 
ATOM   8195  C CG  . TRP C 1 10  ? 16.533  0.050   48.771  1.00 28.42  ? 10  TRP C CG  1 
ATOM   8196  C CD1 . TRP C 1 10  ? 17.072  0.257   47.535  1.00 38.34  ? 10  TRP C CD1 1 
ATOM   8197  C CD2 . TRP C 1 10  ? 15.730  1.208   49.055  1.00 29.11  ? 10  TRP C CD2 1 
ATOM   8198  N NE1 . TRP C 1 10  ? 16.663  1.471   47.034  1.00 36.99  ? 10  TRP C NE1 1 
ATOM   8199  C CE2 . TRP C 1 10  ? 15.839  2.074   47.947  1.00 35.96  ? 10  TRP C CE2 1 
ATOM   8200  C CE3 . TRP C 1 10  ? 14.935  1.597   50.138  1.00 27.78  ? 10  TRP C CE3 1 
ATOM   8201  C CZ2 . TRP C 1 10  ? 15.183  3.305   47.891  1.00 26.33  ? 10  TRP C CZ2 1 
ATOM   8202  C CZ3 . TRP C 1 10  ? 14.283  2.821   50.079  1.00 33.74  ? 10  TRP C CZ3 1 
ATOM   8203  C CH2 . TRP C 1 10  ? 14.412  3.659   48.964  1.00 26.19  ? 10  TRP C CH2 1 
ATOM   8204  N N   . HIS C 1 11  ? 17.269  -2.374  52.770  1.00 23.02  ? 11  HIS C N   1 
ATOM   8205  C CA  . HIS C 1 11  ? 17.487  -3.500  53.674  1.00 22.49  ? 11  HIS C CA  1 
ATOM   8206  C C   . HIS C 1 11  ? 16.346  -4.498  53.513  1.00 22.55  ? 11  HIS C C   1 
ATOM   8207  O O   . HIS C 1 11  ? 15.213  -4.225  53.923  1.00 22.68  ? 11  HIS C O   1 
ATOM   8208  C CB  . HIS C 1 11  ? 17.595  -3.007  55.117  1.00 32.12  ? 11  HIS C CB  1 
ATOM   8209  C CG  . HIS C 1 11  ? 17.500  -4.094  56.144  1.00 24.59  ? 11  HIS C CG  1 
ATOM   8210  N ND1 . HIS C 1 11  ? 18.412  -5.124  56.225  1.00 22.11  ? 11  HIS C ND1 1 
ATOM   8211  C CD2 . HIS C 1 11  ? 16.608  -4.302  57.141  1.00 22.23  ? 11  HIS C CD2 1 
ATOM   8212  C CE1 . HIS C 1 11  ? 18.083  -5.923  57.225  1.00 24.08  ? 11  HIS C CE1 1 
ATOM   8213  N NE2 . HIS C 1 11  ? 16.991  -5.446  57.796  1.00 25.35  ? 11  HIS C NE2 1 
ATOM   8214  N N   . MET C 1 12  ? 16.648  -5.657  52.928  1.00 26.41  ? 12  MET C N   1 
ATOM   8215  C CA  . MET C 1 12  ? 15.662  -6.706  52.681  1.00 32.56  ? 12  MET C CA  1 
ATOM   8216  C C   . MET C 1 12  ? 15.847  -7.813  53.714  1.00 26.68  ? 12  MET C C   1 
ATOM   8217  O O   . MET C 1 12  ? 16.861  -8.520  53.704  1.00 22.65  ? 12  MET C O   1 
ATOM   8218  C CB  . MET C 1 12  ? 15.798  -7.255  51.261  1.00 25.21  ? 12  MET C CB  1 
ATOM   8219  C CG  . MET C 1 12  ? 15.947  -6.185  50.194  1.00 24.78  ? 12  MET C CG  1 
ATOM   8220  S SD  . MET C 1 12  ? 14.572  -5.020  50.215  1.00 39.65  ? 12  MET C SD  1 
ATOM   8221  C CE  . MET C 1 12  ? 14.125  -4.997  48.482  1.00 24.70  ? 12  MET C CE  1 
ATOM   8222  N N   . HIS C 1 13  ? 14.864  -7.968  54.597  1.00 26.21  ? 13  HIS C N   1 
ATOM   8223  C CA  . HIS C 1 13  ? 14.938  -8.982  55.637  1.00 22.70  ? 13  HIS C CA  1 
ATOM   8224  C C   . HIS C 1 13  ? 13.533  -9.320  56.112  1.00 23.06  ? 13  HIS C C   1 
ATOM   8225  O O   . HIS C 1 13  ? 12.657  -8.455  56.169  1.00 23.20  ? 13  HIS C O   1 
ATOM   8226  C CB  . HIS C 1 13  ? 15.800  -8.514  56.815  1.00 22.42  ? 13  HIS C CB  1 
ATOM   8227  C CG  . HIS C 1 13  ? 15.556  -9.272  58.081  1.00 22.57  ? 13  HIS C CG  1 
ATOM   8228  N ND1 . HIS C 1 13  ? 15.773  -10.628 58.189  1.00 22.79  ? 13  HIS C ND1 1 
ATOM   8229  C CD2 . HIS C 1 13  ? 15.117  -8.862  59.294  1.00 22.69  ? 13  HIS C CD2 1 
ATOM   8230  C CE1 . HIS C 1 13  ? 15.473  -11.023 59.414  1.00 24.74  ? 13  HIS C CE1 1 
ATOM   8231  N NE2 . HIS C 1 13  ? 15.074  -9.971  60.104  1.00 22.97  ? 13  HIS C NE2 1 
ATOM   8232  N N   . GLN C 1 14  ? 13.336  -10.593 56.453  1.00 23.33  ? 14  GLN C N   1 
ATOM   8233  C CA  . GLN C 1 14  ? 12.099  -11.083 57.015  1.00 23.82  ? 14  GLN C CA  1 
ATOM   8234  C C   . GLN C 1 14  ? 12.469  -12.282 57.877  1.00 28.07  ? 14  GLN C C   1 
ATOM   8235  O O   . GLN C 1 14  ? 13.219  -13.153 57.408  1.00 33.81  ? 14  GLN C O   1 
ATOM   8236  C CB  . GLN C 1 14  ? 11.089  -11.487 55.942  1.00 24.40  ? 14  GLN C CB  1 
ATOM   8237  C CG  . GLN C 1 14  ? 9.639   -11.293 56.346  1.00 28.98  ? 14  GLN C CG  1 
ATOM   8238  C CD  . GLN C 1 14  ? 9.084   -9.943  55.936  1.00 32.40  ? 14  GLN C CD  1 
ATOM   8239  O OE1 . GLN C 1 14  ? 9.120   -9.573  54.763  1.00 29.76  ? 14  GLN C OE1 1 
ATOM   8240  N NE2 . GLN C 1 14  ? 8.559   -9.201  56.905  1.00 27.16  ? 14  GLN C NE2 1 
ATOM   8241  N N   . PRO C 1 15  ? 11.978  -12.362 59.117  1.00 24.24  ? 15  PRO C N   1 
ATOM   8242  C CA  . PRO C 1 15  ? 12.367  -13.479 59.990  1.00 24.53  ? 15  PRO C CA  1 
ATOM   8243  C C   . PRO C 1 15  ? 11.796  -14.808 59.521  1.00 28.42  ? 15  PRO C C   1 
ATOM   8244  O O   . PRO C 1 15  ? 11.109  -14.871 58.497  1.00 31.83  ? 15  PRO C O   1 
ATOM   8245  C CB  . PRO C 1 15  ? 11.804  -13.073 61.358  1.00 24.82  ? 15  PRO C CB  1 
ATOM   8246  C CG  . PRO C 1 15  ? 10.689  -12.149 61.052  1.00 24.94  ? 15  PRO C CG  1 
ATOM   8247  C CD  . PRO C 1 15  ? 11.038  -11.439 59.776  1.00 24.42  ? 15  PRO C CD  1 
ATOM   8248  N N   . LEU C 1 16  ? 12.076  -15.877 60.262  1.00 25.60  ? 16  LEU C N   1 
ATOM   8249  C CA  . LEU C 1 16  ? 11.666  -17.221 59.874  1.00 26.35  ? 16  LEU C CA  1 
ATOM   8250  C C   . LEU C 1 16  ? 10.249  -17.476 60.374  1.00 27.12  ? 16  LEU C C   1 
ATOM   8251  O O   . LEU C 1 16  ? 10.018  -17.588 61.583  1.00 27.46  ? 16  LEU C O   1 
ATOM   8252  C CB  . LEU C 1 16  ? 12.641  -18.259 60.422  1.00 26.63  ? 16  LEU C CB  1 
ATOM   8253  C CG  . LEU C 1 16  ? 12.536  -19.643 59.782  1.00 27.42  ? 16  LEU C CG  1 
ATOM   8254  C CD1 . LEU C 1 16  ? 12.635  -19.530 58.270  1.00 27.27  ? 16  LEU C CD1 1 
ATOM   8255  C CD2 . LEU C 1 16  ? 13.606  -20.573 60.324  1.00 27.77  ? 16  LEU C CD2 1 
ATOM   8256  N N   . TYR C 1 17  ? 9.301   -17.568 59.443  1.00 27.55  ? 17  TYR C N   1 
ATOM   8257  C CA  . TYR C 1 17  ? 7.923   -17.907 59.766  1.00 28.52  ? 17  TYR C CA  1 
ATOM   8258  C C   . TYR C 1 17  ? 7.642   -19.399 59.646  1.00 29.54  ? 17  TYR C C   1 
ATOM   8259  O O   . TYR C 1 17  ? 6.491   -19.813 59.818  1.00 30.55  ? 17  TYR C O   1 
ATOM   8260  C CB  . TYR C 1 17  ? 6.959   -17.130 58.864  1.00 28.68  ? 17  TYR C CB  1 
ATOM   8261  C CG  . TYR C 1 17  ? 7.124   -15.627 58.924  1.00 28.27  ? 17  TYR C CG  1 
ATOM   8262  C CD1 . TYR C 1 17  ? 6.871   -14.924 60.094  1.00 27.82  ? 17  TYR C CD1 1 
ATOM   8263  C CD2 . TYR C 1 17  ? 7.523   -14.910 57.805  1.00 31.91  ? 17  TYR C CD2 1 
ATOM   8264  C CE1 . TYR C 1 17  ? 7.019   -13.549 60.150  1.00 27.23  ? 17  TYR C CE1 1 
ATOM   8265  C CE2 . TYR C 1 17  ? 7.670   -13.538 57.851  1.00 28.85  ? 17  TYR C CE2 1 
ATOM   8266  C CZ  . TYR C 1 17  ? 7.418   -12.861 59.025  1.00 29.03  ? 17  TYR C CZ  1 
ATOM   8267  O OH  . TYR C 1 17  ? 7.566   -11.493 59.073  1.00 30.06  ? 17  TYR C OH  1 
ATOM   8268  N N   . ARG C 1 18  ? 8.658   -20.208 59.353  1.00 29.45  ? 18  ARG C N   1 
ATOM   8269  C CA  . ARG C 1 18  ? 8.499   -21.649 59.182  1.00 30.52  ? 18  ARG C CA  1 
ATOM   8270  C C   . ARG C 1 18  ? 8.628   -22.335 60.537  1.00 31.02  ? 18  ARG C C   1 
ATOM   8271  O O   . ARG C 1 18  ? 9.720   -22.389 61.112  1.00 30.56  ? 18  ARG C O   1 
ATOM   8272  C CB  . ARG C 1 18  ? 9.532   -22.187 58.197  1.00 30.38  ? 18  ARG C CB  1 
ATOM   8273  C CG  . ARG C 1 18  ? 9.037   -23.339 57.351  1.00 31.59  ? 18  ARG C CG  1 
ATOM   8274  C CD  . ARG C 1 18  ? 10.185  -24.214 56.883  1.00 31.80  ? 18  ARG C CD  1 
ATOM   8275  N NE  . ARG C 1 18  ? 10.289  -25.429 57.681  1.00 40.62  ? 18  ARG C NE  1 
ATOM   8276  C CZ  . ARG C 1 18  ? 10.731  -26.592 57.223  1.00 33.69  ? 18  ARG C CZ  1 
ATOM   8277  N NH1 . ARG C 1 18  ? 11.132  -26.734 55.971  1.00 33.86  ? 18  ARG C NH1 1 
ATOM   8278  N NH2 . ARG C 1 18  ? 10.765  -27.640 58.041  1.00 34.64  ? 18  ARG C NH2 1 
ATOM   8279  N N   . GLU C 1 19  ? 7.518   -22.865 61.040  1.00 32.11  ? 19  GLU C N   1 
ATOM   8280  C CA  . GLU C 1 19  ? 7.542   -23.572 62.310  1.00 32.84  ? 19  GLU C CA  1 
ATOM   8281  C C   . GLU C 1 19  ? 8.428   -24.812 62.196  1.00 33.33  ? 19  GLU C C   1 
ATOM   8282  O O   . GLU C 1 19  ? 8.420   -25.487 61.159  1.00 33.77  ? 19  GLU C O   1 
ATOM   8283  C CB  . GLU C 1 19  ? 6.122   -23.966 62.719  1.00 38.87  ? 19  GLU C CB  1 
ATOM   8284  C CG  . GLU C 1 19  ? 5.917   -24.140 64.212  1.00 48.65  ? 19  GLU C CG  1 
ATOM   8285  C CD  . GLU C 1 19  ? 5.786   -25.596 64.594  1.00 57.61  ? 19  GLU C CD  1 
ATOM   8286  O OE1 . GLU C 1 19  ? 6.289   -26.441 63.829  1.00 55.97  ? 19  GLU C OE1 1 
ATOM   8287  O OE2 . GLU C 1 19  ? 5.196   -25.898 65.653  1.00 58.80  ? 19  GLU C OE2 1 
ATOM   8288  N N   . PRO C 1 20  ? 9.206   -25.140 63.234  1.00 34.09  ? 20  PRO C N   1 
ATOM   8289  C CA  . PRO C 1 20  ? 10.177  -26.238 63.104  1.00 37.86  ? 20  PRO C CA  1 
ATOM   8290  C C   . PRO C 1 20  ? 9.588   -27.631 63.246  1.00 44.37  ? 20  PRO C C   1 
ATOM   8291  O O   . PRO C 1 20  ? 10.229  -28.593 62.799  1.00 47.28  ? 20  PRO C O   1 
ATOM   8292  C CB  . PRO C 1 20  ? 11.182  -25.958 64.236  1.00 33.53  ? 20  PRO C CB  1 
ATOM   8293  C CG  . PRO C 1 20  ? 10.815  -24.609 64.790  1.00 32.67  ? 20  PRO C CG  1 
ATOM   8294  C CD  . PRO C 1 20  ? 9.369   -24.420 64.504  1.00 34.85  ? 20  PRO C CD  1 
ATOM   8295  N N   . TYR C 1 21  ? 8.413   -27.784 63.852  1.00 40.01  ? 21  TYR C N   1 
ATOM   8296  C CA  . TYR C 1 21  ? 7.806   -29.096 64.042  1.00 42.98  ? 21  TYR C CA  1 
ATOM   8297  C C   . TYR C 1 21  ? 6.771   -29.435 62.977  1.00 43.35  ? 21  TYR C C   1 
ATOM   8298  O O   . TYR C 1 21  ? 6.243   -30.552 62.979  1.00 51.85  ? 21  TYR C O   1 
ATOM   8299  C CB  . TYR C 1 21  ? 7.164   -29.182 65.431  1.00 43.52  ? 21  TYR C CB  1 
ATOM   8300  C CG  . TYR C 1 21  ? 8.172   -29.257 66.554  1.00 41.26  ? 21  TYR C CG  1 
ATOM   8301  C CD1 . TYR C 1 21  ? 8.856   -30.435 66.821  1.00 43.93  ? 21  TYR C CD1 1 
ATOM   8302  C CD2 . TYR C 1 21  ? 8.445   -28.147 67.343  1.00 37.97  ? 21  TYR C CD2 1 
ATOM   8303  C CE1 . TYR C 1 21  ? 9.780   -30.509 67.844  1.00 40.01  ? 21  TYR C CE1 1 
ATOM   8304  C CE2 . TYR C 1 21  ? 9.368   -28.212 68.369  1.00 38.37  ? 21  TYR C CE2 1 
ATOM   8305  C CZ  . TYR C 1 21  ? 10.033  -29.395 68.615  1.00 39.09  ? 21  TYR C CZ  1 
ATOM   8306  O OH  . TYR C 1 21  ? 10.953  -29.466 69.634  1.00 43.00  ? 21  TYR C OH  1 
ATOM   8307  N N   . THR C 1 22  ? 6.459   -28.502 62.078  1.00 42.15  ? 22  THR C N   1 
ATOM   8308  C CA  . THR C 1 22  ? 5.506   -28.752 61.003  1.00 38.78  ? 22  THR C CA  1 
ATOM   8309  C C   . THR C 1 22  ? 5.976   -28.285 59.634  1.00 40.15  ? 22  THR C C   1 
ATOM   8310  O O   . THR C 1 22  ? 5.438   -28.765 58.628  1.00 40.26  ? 22  THR C O   1 
ATOM   8311  C CB  . THR C 1 22  ? 4.157   -28.080 61.307  1.00 40.79  ? 22  THR C CB  1 
ATOM   8312  O OG1 . THR C 1 22  ? 4.370   -26.702 61.640  1.00 48.73  ? 22  THR C OG1 1 
ATOM   8313  C CG2 . THR C 1 22  ? 3.458   -28.777 62.465  1.00 40.57  ? 22  THR C CG2 1 
ATOM   8314  N N   . GLY C 1 23  ? 6.948   -27.379 59.552  1.00 42.30  ? 23  GLY C N   1 
ATOM   8315  C CA  . GLY C 1 23  ? 7.354   -26.835 58.272  1.00 40.14  ? 23  GLY C CA  1 
ATOM   8316  C C   . GLY C 1 23  ? 6.387   -25.843 57.672  1.00 37.37  ? 23  GLY C C   1 
ATOM   8317  O O   . GLY C 1 23  ? 6.547   -25.467 56.507  1.00 37.94  ? 23  GLY C O   1 
ATOM   8318  N N   . GLU C 1 24  ? 5.394   -25.396 58.434  1.00 35.59  ? 24  GLU C N   1 
ATOM   8319  C CA  . GLU C 1 24  ? 4.371   -24.495 57.928  1.00 37.57  ? 24  GLU C CA  1 
ATOM   8320  C C   . GLU C 1 24  ? 4.763   -23.046 58.176  1.00 46.12  ? 24  GLU C C   1 
ATOM   8321  O O   . GLU C 1 24  ? 5.333   -22.716 59.219  1.00 50.31  ? 24  GLU C O   1 
ATOM   8322  C CB  . GLU C 1 24  ? 3.026   -24.802 58.590  1.00 37.30  ? 24  GLU C CB  1 
ATOM   8323  C CG  . GLU C 1 24  ? 2.488   -26.186 58.267  1.00 51.96  ? 24  GLU C CG  1 
ATOM   8324  C CD  . GLU C 1 24  ? 1.122   -26.442 58.872  1.00 67.72  ? 24  GLU C CD  1 
ATOM   8325  O OE1 . GLU C 1 24  ? 0.645   -25.590 59.650  1.00 69.93  ? 24  GLU C OE1 1 
ATOM   8326  O OE2 . GLU C 1 24  ? 0.523   -27.497 58.570  1.00 82.09  ? 24  GLU C OE2 1 
ATOM   8327  N N   . TYR C 1 25  ? 4.466   -22.188 57.204  1.00 42.82  ? 25  TYR C N   1 
ATOM   8328  C CA  . TYR C 1 25  ? 4.671   -20.750 57.341  1.00 32.56  ? 25  TYR C CA  1 
ATOM   8329  C C   . TYR C 1 25  ? 3.411   -20.150 57.958  1.00 33.16  ? 25  TYR C C   1 
ATOM   8330  O O   . TYR C 1 25  ? 2.349   -20.135 57.328  1.00 44.48  ? 25  TYR C O   1 
ATOM   8331  C CB  . TYR C 1 25  ? 4.977   -20.111 55.987  1.00 36.31  ? 25  TYR C CB  1 
ATOM   8332  C CG  . TYR C 1 25  ? 6.383   -20.348 55.472  1.00 32.31  ? 25  TYR C CG  1 
ATOM   8333  C CD1 . TYR C 1 25  ? 6.773   -21.594 55.003  1.00 33.36  ? 25  TYR C CD1 1 
ATOM   8334  C CD2 . TYR C 1 25  ? 7.318   -19.319 55.448  1.00 32.17  ? 25  TYR C CD2 1 
ATOM   8335  C CE1 . TYR C 1 25  ? 8.051   -21.810 54.524  1.00 31.45  ? 25  TYR C CE1 1 
ATOM   8336  C CE2 . TYR C 1 25  ? 8.601   -19.528 54.976  1.00 31.28  ? 25  TYR C CE2 1 
ATOM   8337  C CZ  . TYR C 1 25  ? 8.961   -20.778 54.517  1.00 30.18  ? 25  TYR C CZ  1 
ATOM   8338  O OH  . TYR C 1 25  ? 10.234  -20.997 54.044  1.00 31.24  ? 25  TYR C OH  1 
ATOM   8339  N N   . LEU C 1 26  ? 3.527   -19.652 59.188  1.00 32.72  ? 26  LEU C N   1 
ATOM   8340  C CA  . LEU C 1 26  ? 2.377   -19.145 59.925  1.00 33.71  ? 26  LEU C CA  1 
ATOM   8341  C C   . LEU C 1 26  ? 2.050   -17.694 59.599  1.00 32.95  ? 26  LEU C C   1 
ATOM   8342  O O   . LEU C 1 26  ? 1.070   -17.160 60.132  1.00 33.67  ? 26  LEU C O   1 
ATOM   8343  C CB  . LEU C 1 26  ? 2.589   -19.284 61.440  1.00 37.17  ? 26  LEU C CB  1 
ATOM   8344  C CG  . LEU C 1 26  ? 2.797   -20.666 62.076  1.00 34.26  ? 26  LEU C CG  1 
ATOM   8345  C CD1 . LEU C 1 26  ? 1.649   -21.605 61.715  1.00 35.91  ? 26  LEU C CD1 1 
ATOM   8346  C CD2 . LEU C 1 26  ? 4.151   -21.281 61.763  1.00 33.64  ? 26  LEU C CD2 1 
ATOM   8347  N N   . LEU C 1 27  ? 2.844   -17.043 58.747  1.00 35.70  ? 27  LEU C N   1 
ATOM   8348  C CA  . LEU C 1 27  ? 2.588   -15.682 58.317  1.00 38.47  ? 27  LEU C CA  1 
ATOM   8349  C C   . LEU C 1 27  ? 3.041   -15.582 56.866  1.00 41.31  ? 27  LEU C C   1 
ATOM   8350  O O   . LEU C 1 27  ? 4.143   -16.053 56.541  1.00 46.21  ? 27  LEU C O   1 
ATOM   8351  C CB  . LEU C 1 27  ? 3.318   -14.643 59.167  1.00 32.36  ? 27  LEU C CB  1 
ATOM   8352  C CG  . LEU C 1 27  ? 2.750   -14.358 60.558  1.00 30.90  ? 27  LEU C CG  1 
ATOM   8353  C CD1 . LEU C 1 27  ? 3.740   -13.546 61.383  1.00 29.88  ? 27  LEU C CD1 1 
ATOM   8354  C CD2 . LEU C 1 27  ? 1.404   -13.656 60.478  1.00 31.94  ? 27  LEU C CD2 1 
ATOM   8355  N N   . PRO C 1 28  ? 2.238   -14.988 55.986  1.00 34.54  ? 28  PRO C N   1 
ATOM   8356  C CA  . PRO C 1 28  ? 2.577   -14.941 54.557  1.00 37.53  ? 28  PRO C CA  1 
ATOM   8357  C C   . PRO C 1 28  ? 3.433   -13.756 54.133  1.00 39.35  ? 28  PRO C C   1 
ATOM   8358  O O   . PRO C 1 28  ? 3.541   -13.510 52.928  1.00 38.72  ? 28  PRO C O   1 
ATOM   8359  C CB  . PRO C 1 28  ? 1.192   -14.850 53.907  1.00 33.12  ? 28  PRO C CB  1 
ATOM   8360  C CG  . PRO C 1 28  ? 0.395   -14.041 54.890  1.00 33.40  ? 28  PRO C CG  1 
ATOM   8361  C CD  . PRO C 1 28  ? 0.960   -14.312 56.268  1.00 32.67  ? 28  PRO C CD  1 
ATOM   8362  N N   . TRP C 1 29  ? 4.044   -13.032 55.075  1.00 31.70  ? 29  TRP C N   1 
ATOM   8363  C CA  . TRP C 1 29  ? 4.689   -11.766 54.739  1.00 32.22  ? 29  TRP C CA  1 
ATOM   8364  C C   . TRP C 1 29  ? 5.853   -11.951 53.772  1.00 30.12  ? 29  TRP C C   1 
ATOM   8365  O O   . TRP C 1 29  ? 6.115   -11.068 52.946  1.00 33.88  ? 29  TRP C O   1 
ATOM   8366  C CB  . TRP C 1 29  ? 5.159   -11.062 56.011  1.00 32.76  ? 29  TRP C CB  1 
ATOM   8367  C CG  . TRP C 1 29  ? 4.035   -10.646 56.916  1.00 36.47  ? 29  TRP C CG  1 
ATOM   8368  C CD1 . TRP C 1 29  ? 3.785   -11.103 58.178  1.00 33.79  ? 29  TRP C CD1 1 
ATOM   8369  C CD2 . TRP C 1 29  ? 3.003   -9.696  56.621  1.00 44.78  ? 29  TRP C CD2 1 
ATOM   8370  N NE1 . TRP C 1 29  ? 2.665   -10.490 58.690  1.00 35.47  ? 29  TRP C NE1 1 
ATOM   8371  C CE2 . TRP C 1 29  ? 2.166   -9.623  57.754  1.00 46.47  ? 29  TRP C CE2 1 
ATOM   8372  C CE3 . TRP C 1 29  ? 2.708   -8.898  55.512  1.00 49.42  ? 29  TRP C CE3 1 
ATOM   8373  C CZ2 . TRP C 1 29  ? 1.053   -8.784  57.806  1.00 52.71  ? 29  TRP C CZ2 1 
ATOM   8374  C CZ3 . TRP C 1 29  ? 1.601   -8.065  55.566  1.00 48.00  ? 29  TRP C CZ3 1 
ATOM   8375  C CH2 . TRP C 1 29  ? 0.789   -8.015  56.705  1.00 42.87  ? 29  TRP C CH2 1 
ATOM   8376  N N   . THR C 1 30  ? 6.565   -13.076 53.858  1.00 33.73  ? 30  THR C N   1 
ATOM   8377  C CA  . THR C 1 30  ? 7.663   -13.317 52.926  1.00 36.65  ? 30  THR C CA  1 
ATOM   8378  C C   . THR C 1 30  ? 7.159   -13.415 51.492  1.00 32.20  ? 30  THR C C   1 
ATOM   8379  O O   . THR C 1 30  ? 7.761   -12.848 50.572  1.00 36.94  ? 30  THR C O   1 
ATOM   8380  C CB  . THR C 1 30  ? 8.414   -14.592 53.308  1.00 34.50  ? 30  THR C CB  1 
ATOM   8381  O OG1 . THR C 1 30  ? 8.322   -14.798 54.723  1.00 33.10  ? 30  THR C OG1 1 
ATOM   8382  C CG2 . THR C 1 30  ? 9.876   -14.481 52.911  1.00 30.83  ? 30  THR C CG2 1 
ATOM   8383  N N   . PHE C 1 31  ? 6.053   -14.131 51.285  1.00 34.26  ? 31  PHE C N   1 
ATOM   8384  C CA  . PHE C 1 31  ? 5.499   -14.293 49.943  1.00 32.07  ? 31  PHE C CA  1 
ATOM   8385  C C   . PHE C 1 31  ? 5.049   -12.956 49.365  1.00 31.45  ? 31  PHE C C   1 
ATOM   8386  O O   . PHE C 1 31  ? 5.358   -12.627 48.214  1.00 30.88  ? 31  PHE C O   1 
ATOM   8387  C CB  . PHE C 1 31  ? 4.336   -15.286 49.987  1.00 31.86  ? 31  PHE C CB  1 
ATOM   8388  C CG  . PHE C 1 31  ? 3.563   -15.385 48.702  1.00 43.78  ? 31  PHE C CG  1 
ATOM   8389  C CD1 . PHE C 1 31  ? 4.103   -16.020 47.596  1.00 40.58  ? 31  PHE C CD1 1 
ATOM   8390  C CD2 . PHE C 1 31  ? 2.288   -14.851 48.605  1.00 42.02  ? 31  PHE C CD2 1 
ATOM   8391  C CE1 . PHE C 1 31  ? 3.387   -16.116 46.414  1.00 36.32  ? 31  PHE C CE1 1 
ATOM   8392  C CE2 . PHE C 1 31  ? 1.569   -14.941 47.427  1.00 35.75  ? 31  PHE C CE2 1 
ATOM   8393  C CZ  . PHE C 1 31  ? 2.119   -15.576 46.331  1.00 39.65  ? 31  PHE C CZ  1 
ATOM   8394  N N   . PHE C 1 32  ? 4.328   -12.165 50.161  1.00 30.57  ? 32  PHE C N   1 
ATOM   8395  C CA  . PHE C 1 32  ? 3.704   -10.953 49.642  1.00 36.01  ? 32  PHE C CA  1 
ATOM   8396  C C   . PHE C 1 32  ? 4.737   -9.903  49.257  1.00 34.72  ? 32  PHE C C   1 
ATOM   8397  O O   . PHE C 1 32  ? 4.601   -9.246  48.218  1.00 38.18  ? 32  PHE C O   1 
ATOM   8398  C CB  . PHE C 1 32  ? 2.725   -10.399 50.674  1.00 39.67  ? 32  PHE C CB  1 
ATOM   8399  C CG  . PHE C 1 32  ? 1.439   -11.157 50.737  1.00 32.73  ? 32  PHE C CG  1 
ATOM   8400  C CD1 . PHE C 1 32  ? 0.920   -11.747 49.597  1.00 46.81  ? 32  PHE C CD1 1 
ATOM   8401  C CD2 . PHE C 1 32  ? 0.769   -11.316 51.934  1.00 33.00  ? 32  PHE C CD2 1 
ATOM   8402  C CE1 . PHE C 1 32  ? -0.261  -12.460 49.644  1.00 57.83  ? 32  PHE C CE1 1 
ATOM   8403  C CE2 . PHE C 1 32  ? -0.410  -12.035 51.987  1.00 50.42  ? 32  PHE C CE2 1 
ATOM   8404  C CZ  . PHE C 1 32  ? -0.927  -12.604 50.841  1.00 57.46  ? 32  PHE C CZ  1 
ATOM   8405  N N   . HIS C 1 33  ? 5.772   -9.723  50.076  1.00 32.51  ? 33  HIS C N   1 
ATOM   8406  C CA  . HIS C 1 33  ? 6.767   -8.705  49.769  1.00 32.87  ? 33  HIS C CA  1 
ATOM   8407  C C   . HIS C 1 33  ? 7.679   -9.117  48.620  1.00 33.89  ? 33  HIS C C   1 
ATOM   8408  O O   . HIS C 1 33  ? 8.256   -8.245  47.961  1.00 41.49  ? 33  HIS C O   1 
ATOM   8409  C CB  . HIS C 1 33  ? 7.582   -8.377  51.021  1.00 38.93  ? 33  HIS C CB  1 
ATOM   8410  C CG  . HIS C 1 33  ? 6.868   -7.475  51.978  1.00 31.02  ? 33  HIS C CG  1 
ATOM   8411  N ND1 . HIS C 1 33  ? 6.291   -7.931  53.144  1.00 36.16  ? 33  HIS C ND1 1 
ATOM   8412  C CD2 . HIS C 1 33  ? 6.616   -6.145  51.930  1.00 29.18  ? 33  HIS C CD2 1 
ATOM   8413  C CE1 . HIS C 1 33  ? 5.726   -6.920  53.779  1.00 32.96  ? 33  HIS C CE1 1 
ATOM   8414  N NE2 . HIS C 1 33  ? 5.909   -5.825  53.063  1.00 30.06  ? 33  HIS C NE2 1 
ATOM   8415  N N   . ALA C 1 34  ? 7.812   -10.419 48.358  1.00 28.36  ? 34  ALA C N   1 
ATOM   8416  C CA  . ALA C 1 34  ? 8.594   -10.865 47.210  1.00 30.13  ? 34  ALA C CA  1 
ATOM   8417  C C   . ALA C 1 34  ? 7.906   -10.501 45.901  1.00 32.60  ? 34  ALA C C   1 
ATOM   8418  O O   . ALA C 1 34  ? 8.537   -9.965  44.983  1.00 40.26  ? 34  ALA C O   1 
ATOM   8419  C CB  . ALA C 1 34  ? 8.834   -12.373 47.293  1.00 37.42  ? 34  ALA C CB  1 
ATOM   8420  N N   . VAL C 1 35  ? 6.604   -10.782 45.799  1.00 30.98  ? 35  VAL C N   1 
ATOM   8421  C CA  . VAL C 1 35  ? 5.856   -10.442 44.596  1.00 34.77  ? 35  VAL C CA  1 
ATOM   8422  C C   . VAL C 1 35  ? 5.592   -8.950  44.477  1.00 37.88  ? 35  VAL C C   1 
ATOM   8423  O O   . VAL C 1 35  ? 5.183   -8.488  43.406  1.00 50.12  ? 35  VAL C O   1 
ATOM   8424  C CB  . VAL C 1 35  ? 4.522   -11.216 44.543  1.00 33.60  ? 35  VAL C CB  1 
ATOM   8425  C CG1 . VAL C 1 35  ? 4.769   -12.711 44.687  1.00 33.79  ? 35  VAL C CG1 1 
ATOM   8426  C CG2 . VAL C 1 35  ? 3.570   -10.723 45.623  1.00 36.42  ? 35  VAL C CG2 1 
ATOM   8427  N N   . LYS C 1 36  ? 5.818   -8.183  45.544  1.00 33.86  ? 36  LYS C N   1 
ATOM   8428  C CA  . LYS C 1 36  ? 5.587   -6.745  45.530  1.00 34.60  ? 36  LYS C CA  1 
ATOM   8429  C C   . LYS C 1 36  ? 6.859   -5.913  45.549  1.00 43.60  ? 36  LYS C C   1 
ATOM   8430  O O   . LYS C 1 36  ? 6.866   -4.819  44.979  1.00 49.87  ? 36  LYS C O   1 
ATOM   8431  C CB  . LYS C 1 36  ? 4.707   -6.333  46.721  1.00 31.02  ? 36  LYS C CB  1 
ATOM   8432  C CG  . LYS C 1 36  ? 4.254   -4.874  46.695  1.00 33.96  ? 36  LYS C CG  1 
ATOM   8433  C CD  . LYS C 1 36  ? 3.149   -4.595  47.708  1.00 38.15  ? 36  LYS C CD  1 
ATOM   8434  C CE  . LYS C 1 36  ? 3.702   -4.201  49.072  1.00 47.08  ? 36  LYS C CE  1 
ATOM   8435  N NZ  . LYS C 1 36  ? 5.025   -3.539  48.988  1.00 40.93  ? 36  LYS C NZ  1 
ATOM   8436  N N   . ASP C 1 37  ? 7.928   -6.378  46.198  1.00 37.15  ? 37  ASP C N   1 
ATOM   8437  C CA  . ASP C 1 37  ? 9.110   -5.531  46.331  1.00 33.34  ? 37  ASP C CA  1 
ATOM   8438  C C   . ASP C 1 37  ? 10.442  -6.206  46.006  1.00 37.17  ? 37  ASP C C   1 
ATOM   8439  O O   . ASP C 1 37  ? 11.359  -5.547  45.505  1.00 41.53  ? 37  ASP C O   1 
ATOM   8440  C CB  . ASP C 1 37  ? 9.165   -4.961  47.750  1.00 36.00  ? 37  ASP C CB  1 
ATOM   8441  C CG  . ASP C 1 37  ? 7.828   -4.418  48.209  1.00 39.43  ? 37  ASP C CG  1 
ATOM   8442  O OD1 . ASP C 1 37  ? 7.478   -3.286  47.811  1.00 50.70  ? 37  ASP C OD1 1 
ATOM   8443  O OD2 . ASP C 1 37  ? 7.116   -5.127  48.954  1.00 28.58  ? 37  ASP C OD2 1 
ATOM   8444  N N   . TYR C 1 38  ? 10.572  -7.507  46.280  1.00 30.56  ? 38  TYR C N   1 
ATOM   8445  C CA  . TYR C 1 38  ? 11.905  -8.111  46.279  1.00 28.68  ? 38  TYR C CA  1 
ATOM   8446  C C   . TYR C 1 38  ? 12.468  -8.282  44.874  1.00 35.07  ? 38  TYR C C   1 
ATOM   8447  O O   . TYR C 1 38  ? 13.685  -8.170  44.681  1.00 32.14  ? 38  TYR C O   1 
ATOM   8448  C CB  . TYR C 1 38  ? 11.886  -9.445  47.025  1.00 32.64  ? 38  TYR C CB  1 
ATOM   8449  C CG  . TYR C 1 38  ? 11.698  -9.282  48.518  1.00 35.87  ? 38  TYR C CG  1 
ATOM   8450  C CD1 . TYR C 1 38  ? 12.042  -8.094  49.154  1.00 33.08  ? 38  TYR C CD1 1 
ATOM   8451  C CD2 . TYR C 1 38  ? 11.182  -10.312 49.291  1.00 32.33  ? 38  TYR C CD2 1 
ATOM   8452  C CE1 . TYR C 1 38  ? 11.870  -7.938  50.516  1.00 31.80  ? 38  TYR C CE1 1 
ATOM   8453  C CE2 . TYR C 1 38  ? 11.003  -10.163 50.650  1.00 30.75  ? 38  TYR C CE2 1 
ATOM   8454  C CZ  . TYR C 1 38  ? 11.352  -8.977  51.259  1.00 33.99  ? 38  TYR C CZ  1 
ATOM   8455  O OH  . TYR C 1 38  ? 11.179  -8.831  52.616  1.00 38.23  ? 38  TYR C OH  1 
ATOM   8456  N N   . TYR C 1 39  ? 11.619  -8.567  43.888  1.00 47.75  ? 39  TYR C N   1 
ATOM   8457  C CA  . TYR C 1 39  ? 12.084  -8.544  42.506  1.00 35.69  ? 39  TYR C CA  1 
ATOM   8458  C C   . TYR C 1 39  ? 12.048  -7.132  41.939  1.00 38.28  ? 39  TYR C C   1 
ATOM   8459  O O   . TYR C 1 39  ? 12.934  -6.746  41.169  1.00 46.21  ? 39  TYR C O   1 
ATOM   8460  C CB  . TYR C 1 39  ? 11.241  -9.486  41.642  1.00 37.02  ? 39  TYR C CB  1 
ATOM   8461  C CG  . TYR C 1 39  ? 11.508  -9.394  40.151  1.00 42.88  ? 39  TYR C CG  1 
ATOM   8462  C CD1 . TYR C 1 39  ? 12.523  -10.136 39.558  1.00 47.67  ? 39  TYR C CD1 1 
ATOM   8463  C CD2 . TYR C 1 39  ? 10.735  -8.575  39.335  1.00 38.08  ? 39  TYR C CD2 1 
ATOM   8464  C CE1 . TYR C 1 39  ? 12.765  -10.059 38.194  1.00 38.15  ? 39  TYR C CE1 1 
ATOM   8465  C CE2 . TYR C 1 39  ? 10.971  -8.491  37.973  1.00 35.96  ? 39  TYR C CE2 1 
ATOM   8466  C CZ  . TYR C 1 39  ? 11.986  -9.236  37.409  1.00 42.48  ? 39  TYR C CZ  1 
ATOM   8467  O OH  . TYR C 1 39  ? 12.221  -9.155  36.054  1.00 43.43  ? 39  TYR C OH  1 
ATOM   8468  N N   . ASP C 1 40  ? 11.042  -6.346  42.327  1.00 40.73  ? 40  ASP C N   1 
ATOM   8469  C CA  . ASP C 1 40  ? 10.779  -5.065  41.680  1.00 42.32  ? 40  ASP C CA  1 
ATOM   8470  C C   . ASP C 1 40  ? 11.788  -3.990  42.074  1.00 37.38  ? 40  ASP C C   1 
ATOM   8471  O O   . ASP C 1 40  ? 12.214  -3.206  41.221  1.00 43.84  ? 40  ASP C O   1 
ATOM   8472  C CB  . ASP C 1 40  ? 9.356   -4.608  42.000  1.00 42.65  ? 40  ASP C CB  1 
ATOM   8473  C CG  . ASP C 1 40  ? 8.332   -5.702  41.766  1.00 60.37  ? 40  ASP C CG  1 
ATOM   8474  O OD1 . ASP C 1 40  ? 8.127   -6.082  40.595  1.00 56.28  ? 40  ASP C OD1 1 
ATOM   8475  O OD2 . ASP C 1 40  ? 7.740   -6.192  42.748  1.00 65.67  ? 40  ASP C OD2 1 
ATOM   8476  N N   . MET C 1 41  ? 12.174  -3.923  43.348  1.00 40.10  ? 41  MET C N   1 
ATOM   8477  C CA  . MET C 1 41  ? 13.084  -2.863  43.780  1.00 36.56  ? 41  MET C CA  1 
ATOM   8478  C C   . MET C 1 41  ? 14.433  -2.916  43.077  1.00 38.08  ? 41  MET C C   1 
ATOM   8479  O O   . MET C 1 41  ? 14.914  -1.856  42.640  1.00 46.37  ? 41  MET C O   1 
ATOM   8480  C CB  . MET C 1 41  ? 13.223  -2.892  45.309  1.00 31.96  ? 41  MET C CB  1 
ATOM   8481  C CG  . MET C 1 41  ? 12.049  -2.276  46.061  1.00 40.36  ? 41  MET C CG  1 
ATOM   8482  S SD  . MET C 1 41  ? 12.026  -0.472  46.098  1.00 31.84  ? 41  MET C SD  1 
ATOM   8483  C CE  . MET C 1 41  ? 13.778  -0.086  46.068  1.00 38.38  ? 41  MET C CE  1 
ATOM   8484  N N   . PRO C 1 42  ? 15.101  -4.068  42.942  1.00 34.72  ? 42  PRO C N   1 
ATOM   8485  C CA  . PRO C 1 42  ? 16.309  -4.112  42.099  1.00 45.27  ? 42  PRO C CA  1 
ATOM   8486  C C   . PRO C 1 42  ? 16.020  -4.079  40.609  1.00 40.40  ? 42  PRO C C   1 
ATOM   8487  O O   . PRO C 1 42  ? 16.917  -3.731  39.829  1.00 41.59  ? 42  PRO C O   1 
ATOM   8488  C CB  . PRO C 1 42  ? 16.988  -5.434  42.490  1.00 42.60  ? 42  PRO C CB  1 
ATOM   8489  C CG  . PRO C 1 42  ? 15.942  -6.234  43.158  1.00 43.60  ? 42  PRO C CG  1 
ATOM   8490  C CD  . PRO C 1 42  ? 14.917  -5.309  43.709  1.00 30.47  ? 42  PRO C CD  1 
ATOM   8491  N N   . ALA C 1 43  ? 14.805  -4.439  40.189  1.00 36.51  ? 43  ALA C N   1 
ATOM   8492  C CA  . ALA C 1 43  ? 14.440  -4.353  38.784  1.00 36.27  ? 43  ALA C CA  1 
ATOM   8493  C C   . ALA C 1 43  ? 14.286  -2.917  38.312  1.00 37.85  ? 43  ALA C C   1 
ATOM   8494  O O   . ALA C 1 43  ? 14.188  -2.690  37.101  1.00 36.97  ? 43  ALA C O   1 
ATOM   8495  C CB  . ALA C 1 43  ? 13.146  -5.131  38.519  1.00 32.77  ? 43  ALA C CB  1 
ATOM   8496  N N   . TYR C 1 44  ? 14.262  -1.952  39.235  1.00 34.22  ? 44  TYR C N   1 
ATOM   8497  C CA  . TYR C 1 44  ? 14.286  -0.546  38.851  1.00 35.33  ? 44  TYR C CA  1 
ATOM   8498  C C   . TYR C 1 44  ? 15.555  -0.202  38.080  1.00 33.31  ? 44  TYR C C   1 
ATOM   8499  O O   . TYR C 1 44  ? 15.539  0.683   37.216  1.00 33.88  ? 44  TYR C O   1 
ATOM   8500  C CB  . TYR C 1 44  ? 14.176  0.340   40.094  1.00 31.24  ? 44  TYR C CB  1 
ATOM   8501  C CG  . TYR C 1 44  ? 12.762  0.685   40.508  1.00 35.32  ? 44  TYR C CG  1 
ATOM   8502  C CD1 . TYR C 1 44  ? 12.050  -0.139  41.371  1.00 30.76  ? 44  TYR C CD1 1 
ATOM   8503  C CD2 . TYR C 1 44  ? 12.147  1.844   40.054  1.00 37.93  ? 44  TYR C CD2 1 
ATOM   8504  C CE1 . TYR C 1 44  ? 10.760  0.174   41.760  1.00 31.10  ? 44  TYR C CE1 1 
ATOM   8505  C CE2 . TYR C 1 44  ? 10.859  2.167   40.438  1.00 37.31  ? 44  TYR C CE2 1 
ATOM   8506  C CZ  . TYR C 1 44  ? 10.170  1.329   41.290  1.00 32.09  ? 44  TYR C CZ  1 
ATOM   8507  O OH  . TYR C 1 44  ? 8.887   1.652   41.671  1.00 32.60  ? 44  TYR C OH  1 
ATOM   8508  N N   . LEU C 1 45  ? 16.660  -0.894  38.377  1.00 32.14  ? 45  LEU C N   1 
ATOM   8509  C CA  . LEU C 1 45  ? 17.952  -0.578  37.777  1.00 32.84  ? 45  LEU C CA  1 
ATOM   8510  C C   . LEU C 1 45  ? 17.998  -0.871  36.283  1.00 38.29  ? 45  LEU C C   1 
ATOM   8511  O O   . LEU C 1 45  ? 18.859  -0.324  35.586  1.00 46.68  ? 45  LEU C O   1 
ATOM   8512  C CB  . LEU C 1 45  ? 19.061  -1.357  38.487  1.00 32.67  ? 45  LEU C CB  1 
ATOM   8513  C CG  . LEU C 1 45  ? 19.558  -0.810  39.828  1.00 35.52  ? 45  LEU C CG  1 
ATOM   8514  C CD1 . LEU C 1 45  ? 20.366  -1.864  40.569  1.00 36.32  ? 45  LEU C CD1 1 
ATOM   8515  C CD2 . LEU C 1 45  ? 20.379  0.450   39.627  1.00 35.11  ? 45  LEU C CD2 1 
ATOM   8516  N N   . LYS C 1 46  ? 17.109  -1.728  35.777  1.00 35.93  ? 46  LYS C N   1 
ATOM   8517  C CA  . LYS C 1 46  ? 17.099  -2.038  34.354  1.00 36.63  ? 46  LYS C CA  1 
ATOM   8518  C C   . LYS C 1 46  ? 16.416  -0.962  33.520  1.00 46.07  ? 46  LYS C C   1 
ATOM   8519  O O   . LYS C 1 46  ? 16.606  -0.930  32.299  1.00 56.33  ? 46  LYS C O   1 
ATOM   8520  C CB  . LYS C 1 46  ? 16.418  -3.387  34.112  1.00 42.41  ? 46  LYS C CB  1 
ATOM   8521  C CG  . LYS C 1 46  ? 17.238  -4.583  34.568  1.00 40.61  ? 46  LYS C CG  1 
ATOM   8522  C CD  . LYS C 1 46  ? 16.676  -5.884  34.019  1.00 53.42  ? 46  LYS C CD  1 
ATOM   8523  C CE  . LYS C 1 46  ? 15.217  -6.065  34.408  1.00 42.93  ? 46  LYS C CE  1 
ATOM   8524  N NZ  . LYS C 1 46  ? 14.772  -7.478  34.253  1.00 37.64  ? 46  LYS C NZ  1 
ATOM   8525  N N   . ASP C 1 47  ? 15.629  -0.088  34.145  1.00 47.96  ? 47  ASP C N   1 
ATOM   8526  C CA  . ASP C 1 47  ? 14.941  0.985   33.443  1.00 51.61  ? 47  ASP C CA  1 
ATOM   8527  C C   . ASP C 1 47  ? 15.514  2.361   33.747  1.00 53.70  ? 47  ASP C C   1 
ATOM   8528  O O   . ASP C 1 47  ? 15.057  3.350   33.161  1.00 47.76  ? 47  ASP C O   1 
ATOM   8529  C CB  . ASP C 1 47  ? 13.444  0.968   33.779  1.00 51.29  ? 47  ASP C CB  1 
ATOM   8530  C CG  . ASP C 1 47  ? 12.831  -0.415  33.665  1.00 61.20  ? 47  ASP C CG  1 
ATOM   8531  O OD1 . ASP C 1 47  ? 13.498  -1.403  34.037  1.00 73.98  ? 47  ASP C OD1 1 
ATOM   8532  O OD2 . ASP C 1 47  ? 11.675  -0.516  33.201  1.00 75.65  ? 47  ASP C OD2 1 
ATOM   8533  N N   . PHE C 1 48  ? 16.498  2.457   34.640  1.00 58.61  ? 48  PHE C N   1 
ATOM   8534  C CA  . PHE C 1 48  ? 17.068  3.740   35.025  1.00 50.49  ? 48  PHE C CA  1 
ATOM   8535  C C   . PHE C 1 48  ? 18.578  3.616   35.145  1.00 52.43  ? 48  PHE C C   1 
ATOM   8536  O O   . PHE C 1 48  ? 19.088  2.632   35.687  1.00 49.20  ? 48  PHE C O   1 
ATOM   8537  C CB  . PHE C 1 48  ? 16.472  4.236   36.347  1.00 35.66  ? 48  PHE C CB  1 
ATOM   8538  C CG  . PHE C 1 48  ? 15.024  4.616   36.250  1.00 36.25  ? 48  PHE C CG  1 
ATOM   8539  C CD1 . PHE C 1 48  ? 14.654  5.872   35.795  1.00 39.12  ? 48  PHE C CD1 1 
ATOM   8540  C CD2 . PHE C 1 48  ? 14.031  3.717   36.604  1.00 37.13  ? 48  PHE C CD2 1 
ATOM   8541  C CE1 . PHE C 1 48  ? 13.322  6.227   35.701  1.00 44.12  ? 48  PHE C CE1 1 
ATOM   8542  C CE2 . PHE C 1 48  ? 12.696  4.066   36.511  1.00 43.55  ? 48  PHE C CE2 1 
ATOM   8543  C CZ  . PHE C 1 48  ? 12.341  5.323   36.060  1.00 42.96  ? 48  PHE C CZ  1 
ATOM   8544  N N   . GLU C 1 49  ? 19.288  4.627   34.641  1.00 51.77  ? 49  GLU C N   1 
ATOM   8545  C CA  . GLU C 1 49  ? 20.750  4.639   34.666  1.00 49.73  ? 49  GLU C CA  1 
ATOM   8546  C C   . GLU C 1 49  ? 21.222  5.321   35.947  1.00 46.08  ? 49  GLU C C   1 
ATOM   8547  O O   . GLU C 1 49  ? 21.670  6.469   35.960  1.00 44.87  ? 49  GLU C O   1 
ATOM   8548  C CB  . GLU C 1 49  ? 21.302  5.322   33.421  1.00 52.12  ? 49  GLU C CB  1 
ATOM   8549  C CG  . GLU C 1 49  ? 21.290  4.439   32.186  1.00 53.33  ? 49  GLU C CG  1 
ATOM   8550  C CD  . GLU C 1 49  ? 22.403  3.412   32.197  1.00 66.59  ? 49  GLU C CD  1 
ATOM   8551  O OE1 . GLU C 1 49  ? 23.527  3.746   31.764  1.00 66.48  ? 49  GLU C OE1 1 
ATOM   8552  O OE2 . GLU C 1 49  ? 22.156  2.271   32.643  1.00 72.78  ? 49  GLU C OE2 1 
ATOM   8553  N N   . ILE C 1 50  ? 21.105  4.586   37.049  1.00 38.49  ? 50  ILE C N   1 
ATOM   8554  C CA  . ILE C 1 50  ? 21.598  4.993   38.357  1.00 38.94  ? 50  ILE C CA  1 
ATOM   8555  C C   . ILE C 1 50  ? 22.211  3.772   39.033  1.00 36.48  ? 50  ILE C C   1 
ATOM   8556  O O   . ILE C 1 50  ? 22.298  2.690   38.447  1.00 41.37  ? 50  ILE C O   1 
ATOM   8557  C CB  . ILE C 1 50  ? 20.494  5.608   39.241  1.00 32.98  ? 50  ILE C CB  1 
ATOM   8558  C CG1 . ILE C 1 50  ? 19.251  4.719   39.223  1.00 32.58  ? 50  ILE C CG1 1 
ATOM   8559  C CG2 . ILE C 1 50  ? 20.171  7.026   38.790  1.00 42.82  ? 50  ILE C CG2 1 
ATOM   8560  C CD1 . ILE C 1 50  ? 18.444  4.791   40.484  1.00 31.48  ? 50  ILE C CD1 1 
ATOM   8561  N N   . LYS C 1 51  ? 22.653  3.954   40.274  1.00 31.75  ? 51  LYS C N   1 
ATOM   8562  C CA  . LYS C 1 51  ? 23.227  2.879   41.070  1.00 30.72  ? 51  LYS C CA  1 
ATOM   8563  C C   . LYS C 1 51  ? 22.450  2.753   42.371  1.00 29.64  ? 51  LYS C C   1 
ATOM   8564  O O   . LYS C 1 51  ? 22.250  3.748   43.075  1.00 36.16  ? 51  LYS C O   1 
ATOM   8565  C CB  . LYS C 1 51  ? 24.706  3.140   41.365  1.00 34.79  ? 51  LYS C CB  1 
ATOM   8566  C CG  . LYS C 1 51  ? 25.550  3.456   40.143  1.00 36.29  ? 51  LYS C CG  1 
ATOM   8567  C CD  . LYS C 1 51  ? 25.454  2.364   39.091  1.00 33.03  ? 51  LYS C CD  1 
ATOM   8568  C CE  . LYS C 1 51  ? 26.541  2.530   38.043  1.00 34.53  ? 51  LYS C CE  1 
ATOM   8569  N NZ  . LYS C 1 51  ? 27.841  1.972   38.508  1.00 36.14  ? 51  LYS C NZ  1 
ATOM   8570  N N   . LEU C 1 52  ? 22.012  1.536   42.688  1.00 32.40  ? 52  LEU C N   1 
ATOM   8571  C CA  . LEU C 1 52  ? 21.359  1.249   43.956  1.00 31.63  ? 52  LEU C CA  1 
ATOM   8572  C C   . LEU C 1 52  ? 21.939  -0.023  44.556  1.00 31.54  ? 52  LEU C C   1 
ATOM   8573  O O   . LEU C 1 52  ? 22.286  -0.966  43.840  1.00 27.46  ? 52  LEU C O   1 
ATOM   8574  C CB  . LEU C 1 52  ? 19.841  1.094   43.805  1.00 30.59  ? 52  LEU C CB  1 
ATOM   8575  C CG  . LEU C 1 52  ? 19.102  2.179   43.026  1.00 31.20  ? 52  LEU C CG  1 
ATOM   8576  C CD1 . LEU C 1 52  ? 17.712  1.693   42.667  1.00 33.22  ? 52  LEU C CD1 1 
ATOM   8577  C CD2 . LEU C 1 52  ? 19.039  3.469   43.825  1.00 28.32  ? 52  LEU C CD2 1 
ATOM   8578  N N   . ASN C 1 53  ? 22.022  -0.045  45.882  1.00 31.90  ? 53  ASN C N   1 
ATOM   8579  C CA  . ASN C 1 53  ? 22.599  -1.159  46.614  1.00 25.75  ? 53  ASN C CA  1 
ATOM   8580  C C   . ASN C 1 53  ? 21.544  -1.786  47.510  1.00 30.22  ? 53  ASN C C   1 
ATOM   8581  O O   . ASN C 1 53  ? 20.628  -1.109  47.988  1.00 33.58  ? 53  ASN C O   1 
ATOM   8582  C CB  . ASN C 1 53  ? 23.797  -0.707  47.448  1.00 25.71  ? 53  ASN C CB  1 
ATOM   8583  C CG  . ASN C 1 53  ? 24.777  0.109   46.643  1.00 27.82  ? 53  ASN C CG  1 
ATOM   8584  O OD1 . ASN C 1 53  ? 25.551  -0.434  45.859  1.00 33.03  ? 53  ASN C OD1 1 
ATOM   8585  N ND2 . ASN C 1 53  ? 24.739  1.426   46.818  1.00 26.83  ? 53  ASN C ND2 1 
ATOM   8586  N N   . PHE C 1 54  ? 21.678  -3.091  47.728  1.00 24.76  ? 54  PHE C N   1 
ATOM   8587  C CA  . PHE C 1 54  ? 20.682  -3.859  48.454  1.00 24.21  ? 54  PHE C CA  1 
ATOM   8588  C C   . PHE C 1 54  ? 21.365  -4.747  49.480  1.00 23.84  ? 54  PHE C C   1 
ATOM   8589  O O   . PHE C 1 54  ? 22.444  -5.286  49.227  1.00 24.16  ? 54  PHE C O   1 
ATOM   8590  C CB  . PHE C 1 54  ? 19.838  -4.703  47.490  1.00 24.60  ? 54  PHE C CB  1 
ATOM   8591  C CG  . PHE C 1 54  ? 19.198  -3.898  46.399  1.00 29.79  ? 54  PHE C CG  1 
ATOM   8592  C CD1 . PHE C 1 54  ? 19.887  -3.615  45.230  1.00 29.73  ? 54  PHE C CD1 1 
ATOM   8593  C CD2 . PHE C 1 54  ? 17.918  -3.396  46.557  1.00 28.83  ? 54  PHE C CD2 1 
ATOM   8594  C CE1 . PHE C 1 54  ? 19.305  -2.860  44.232  1.00 30.02  ? 54  PHE C CE1 1 
ATOM   8595  C CE2 . PHE C 1 54  ? 17.330  -2.641  45.563  1.00 32.28  ? 54  PHE C CE2 1 
ATOM   8596  C CZ  . PHE C 1 54  ? 18.028  -2.369  44.401  1.00 32.61  ? 54  PHE C CZ  1 
ATOM   8597  N N   . ASN C 1 55  ? 20.740  -4.882  50.644  1.00 23.31  ? 55  ASN C N   1 
ATOM   8598  C CA  . ASN C 1 55  ? 21.172  -5.829  51.659  1.00 23.06  ? 55  ASN C CA  1 
ATOM   8599  C C   . ASN C 1 55  ? 20.109  -6.905  51.815  1.00 23.70  ? 55  ASN C C   1 
ATOM   8600  O O   . ASN C 1 55  ? 18.929  -6.596  52.011  1.00 23.42  ? 55  ASN C O   1 
ATOM   8601  C CB  . ASN C 1 55  ? 21.423  -5.144  53.002  1.00 22.77  ? 55  ASN C CB  1 
ATOM   8602  C CG  . ASN C 1 55  ? 21.847  -6.123  54.079  1.00 22.67  ? 55  ASN C CG  1 
ATOM   8603  O OD1 . ASN C 1 55  ? 22.998  -6.559  54.122  1.00 26.09  ? 55  ASN C OD1 1 
ATOM   8604  N ND2 . ASN C 1 55  ? 20.911  -6.489  54.947  1.00 22.40  ? 55  ASN C ND2 1 
ATOM   8605  N N   . LEU C 1 56  ? 20.530  -8.162  51.721  1.00 23.15  ? 56  LEU C N   1 
ATOM   8606  C CA  . LEU C 1 56  ? 19.646  -9.306  51.875  1.00 23.21  ? 56  LEU C CA  1 
ATOM   8607  C C   . LEU C 1 56  ? 20.122  -10.133 53.057  1.00 23.98  ? 56  LEU C C   1 
ATOM   8608  O O   . LEU C 1 56  ? 21.291  -10.531 53.106  1.00 27.98  ? 56  LEU C O   1 
ATOM   8609  C CB  . LEU C 1 56  ? 19.630  -10.161 50.606  1.00 23.82  ? 56  LEU C CB  1 
ATOM   8610  C CG  . LEU C 1 56  ? 18.738  -9.710  49.452  1.00 24.16  ? 56  LEU C CG  1 
ATOM   8611  C CD1 . LEU C 1 56  ? 19.526  -8.827  48.504  1.00 24.45  ? 56  LEU C CD1 1 
ATOM   8612  C CD2 . LEU C 1 56  ? 18.171  -10.913 48.718  1.00 24.81  ? 56  LEU C CD2 1 
ATOM   8613  N N   . THR C 1 57  ? 19.231  -10.378 54.009  1.00 22.89  ? 57  THR C N   1 
ATOM   8614  C CA  . THR C 1 57  ? 19.632  -11.280 55.077  1.00 22.98  ? 57  THR C CA  1 
ATOM   8615  C C   . THR C 1 57  ? 19.456  -12.728 54.625  1.00 23.47  ? 57  THR C C   1 
ATOM   8616  O O   . THR C 1 57  ? 18.508  -13.042 53.901  1.00 23.67  ? 57  THR C O   1 
ATOM   8617  C CB  . THR C 1 57  ? 18.820  -11.026 56.343  1.00 22.75  ? 57  THR C CB  1 
ATOM   8618  O OG1 . THR C 1 57  ? 17.424  -11.186 56.061  1.00 25.53  ? 57  THR C OG1 1 
ATOM   8619  C CG2 . THR C 1 57  ? 19.081  -9.620  56.860  1.00 26.96  ? 57  THR C CG2 1 
ATOM   8620  N N   . PRO C 1 58  ? 20.365  -13.620 55.021  1.00 23.82  ? 58  PRO C N   1 
ATOM   8621  C CA  . PRO C 1 58  ? 20.266  -15.018 54.573  1.00 24.46  ? 58  PRO C CA  1 
ATOM   8622  C C   . PRO C 1 58  ? 18.991  -15.716 55.011  1.00 24.60  ? 58  PRO C C   1 
ATOM   8623  O O   . PRO C 1 58  ? 18.594  -16.697 54.369  1.00 25.19  ? 58  PRO C O   1 
ATOM   8624  C CB  . PRO C 1 58  ? 21.504  -15.672 55.200  1.00 29.64  ? 58  PRO C CB  1 
ATOM   8625  C CG  . PRO C 1 58  ? 22.462  -14.536 55.417  1.00 25.07  ? 58  PRO C CG  1 
ATOM   8626  C CD  . PRO C 1 58  ? 21.600  -13.366 55.781  1.00 23.85  ? 58  PRO C CD  1 
ATOM   8627  N N   . VAL C 1 59  ? 18.341  -15.257 56.083  1.00 24.23  ? 59  VAL C N   1 
ATOM   8628  C CA  . VAL C 1 59  ? 17.088  -15.876 56.507  1.00 24.50  ? 59  VAL C CA  1 
ATOM   8629  C C   . VAL C 1 59  ? 15.981  -15.587 55.498  1.00 24.77  ? 59  VAL C C   1 
ATOM   8630  O O   . VAL C 1 59  ? 15.114  -16.433 55.249  1.00 30.57  ? 59  VAL C O   1 
ATOM   8631  C CB  . VAL C 1 59  ? 16.714  -15.418 57.930  1.00 24.26  ? 59  VAL C CB  1 
ATOM   8632  C CG1 . VAL C 1 59  ? 16.487  -13.915 57.976  1.00 24.20  ? 59  VAL C CG1 1 
ATOM   8633  C CG2 . VAL C 1 59  ? 15.488  -16.169 58.433  1.00 24.75  ? 59  VAL C CG2 1 
ATOM   8634  N N   . LEU C 1 60  ? 15.986  -14.389 54.908  1.00 25.59  ? 60  LEU C N   1 
ATOM   8635  C CA  . LEU C 1 60  ? 15.039  -14.082 53.839  1.00 28.91  ? 60  LEU C CA  1 
ATOM   8636  C C   . LEU C 1 60  ? 15.324  -14.917 52.597  1.00 25.40  ? 60  LEU C C   1 
ATOM   8637  O O   . LEU C 1 60  ? 14.410  -15.508 52.009  1.00 28.85  ? 60  LEU C O   1 
ATOM   8638  C CB  . LEU C 1 60  ? 15.092  -12.590 53.508  1.00 28.92  ? 60  LEU C CB  1 
ATOM   8639  C CG  . LEU C 1 60  ? 14.206  -12.103 52.360  1.00 24.25  ? 60  LEU C CG  1 
ATOM   8640  C CD1 . LEU C 1 60  ? 12.751  -12.195 52.760  1.00 28.12  ? 60  LEU C CD1 1 
ATOM   8641  C CD2 . LEU C 1 60  ? 14.565  -10.679 51.963  1.00 23.89  ? 60  LEU C CD2 1 
ATOM   8642  N N   . ILE C 1 61  ? 16.595  -14.984 52.194  1.00 30.91  ? 61  ILE C N   1 
ATOM   8643  C CA  . ILE C 1 61  ? 16.981  -15.732 51.001  1.00 25.74  ? 61  ILE C CA  1 
ATOM   8644  C C   . ILE C 1 61  ? 16.631  -17.206 51.159  1.00 26.50  ? 61  ILE C C   1 
ATOM   8645  O O   . ILE C 1 61  ? 16.233  -17.872 50.196  1.00 27.70  ? 61  ILE C O   1 
ATOM   8646  C CB  . ILE C 1 61  ? 18.480  -15.528 50.717  1.00 25.70  ? 61  ILE C CB  1 
ATOM   8647  C CG1 . ILE C 1 61  ? 18.758  -14.064 50.369  1.00 25.18  ? 61  ILE C CG1 1 
ATOM   8648  C CG2 . ILE C 1 61  ? 18.947  -16.440 49.601  1.00 26.67  ? 61  ILE C CG2 1 
ATOM   8649  C CD1 . ILE C 1 61  ? 20.188  -13.649 50.615  1.00 25.00  ? 61  ILE C CD1 1 
ATOM   8650  N N   . ASP C 1 62  ? 16.776  -17.737 52.374  1.00 26.35  ? 62  ASP C N   1 
ATOM   8651  C CA  . ASP C 1 62  ? 16.351  -19.107 52.640  1.00 27.15  ? 62  ASP C CA  1 
ATOM   8652  C C   . ASP C 1 62  ? 14.864  -19.281 52.361  1.00 33.20  ? 62  ASP C C   1 
ATOM   8653  O O   . ASP C 1 62  ? 14.442  -20.304 51.804  1.00 37.87  ? 62  ASP C O   1 
ATOM   8654  C CB  . ASP C 1 62  ? 16.671  -19.476 54.088  1.00 28.07  ? 62  ASP C CB  1 
ATOM   8655  C CG  . ASP C 1 62  ? 18.031  -20.121 54.240  1.00 41.32  ? 62  ASP C CG  1 
ATOM   8656  O OD1 . ASP C 1 62  ? 18.671  -20.404 53.206  1.00 44.74  ? 62  ASP C OD1 1 
ATOM   8657  O OD2 . ASP C 1 62  ? 18.463  -20.336 55.394  1.00 37.30  ? 62  ASP C OD2 1 
ATOM   8658  N N   . GLN C 1 63  ? 14.052  -18.291 52.739  1.00 27.02  ? 63  GLN C N   1 
ATOM   8659  C CA  . GLN C 1 63  ? 12.613  -18.398 52.531  1.00 29.67  ? 63  GLN C CA  1 
ATOM   8660  C C   . GLN C 1 63  ? 12.241  -18.197 51.066  1.00 37.94  ? 63  GLN C C   1 
ATOM   8661  O O   . GLN C 1 63  ? 11.345  -18.877 50.553  1.00 43.66  ? 63  GLN C O   1 
ATOM   8662  C CB  . GLN C 1 63  ? 11.886  -17.394 53.425  1.00 40.41  ? 63  GLN C CB  1 
ATOM   8663  C CG  . GLN C 1 63  ? 12.041  -17.689 54.910  1.00 34.71  ? 63  GLN C CG  1 
ATOM   8664  C CD  . GLN C 1 63  ? 11.606  -16.534 55.789  1.00 30.79  ? 63  GLN C CD  1 
ATOM   8665  O OE1 . GLN C 1 63  ? 10.458  -16.470 56.224  1.00 31.15  ? 63  GLN C OE1 1 
ATOM   8666  N NE2 . GLN C 1 63  ? 12.527  -15.614 56.058  1.00 28.66  ? 63  GLN C NE2 1 
ATOM   8667  N N   . ILE C 1 64  ? 12.916  -17.275 50.374  1.00 35.46  ? 64  ILE C N   1 
ATOM   8668  C CA  . ILE C 1 64  ? 12.641  -17.081 48.952  1.00 31.48  ? 64  ILE C CA  1 
ATOM   8669  C C   . ILE C 1 64  ? 12.967  -18.350 48.176  1.00 29.43  ? 64  ILE C C   1 
ATOM   8670  O O   . ILE C 1 64  ? 12.251  -18.725 47.240  1.00 33.15  ? 64  ILE C O   1 
ATOM   8671  C CB  . ILE C 1 64  ? 13.417  -15.868 48.403  1.00 33.12  ? 64  ILE C CB  1 
ATOM   8672  C CG1 . ILE C 1 64  ? 12.933  -14.571 49.047  1.00 34.28  ? 64  ILE C CG1 1 
ATOM   8673  C CG2 . ILE C 1 64  ? 13.238  -15.759 46.902  1.00 31.41  ? 64  ILE C CG2 1 
ATOM   8674  C CD1 . ILE C 1 64  ? 13.959  -13.459 48.996  1.00 29.92  ? 64  ILE C CD1 1 
ATOM   8675  N N   . GLN C 1 65  ? 14.049  -19.034 48.557  1.00 31.95  ? 65  GLN C N   1 
ATOM   8676  C CA  . GLN C 1 65  ? 14.408  -20.285 47.898  1.00 30.51  ? 65  GLN C CA  1 
ATOM   8677  C C   . GLN C 1 65  ? 13.345  -21.355 48.116  1.00 31.47  ? 65  GLN C C   1 
ATOM   8678  O O   . GLN C 1 65  ? 13.039  -22.129 47.202  1.00 32.76  ? 65  GLN C O   1 
ATOM   8679  C CB  . GLN C 1 65  ? 15.768  -20.770 48.398  1.00 30.75  ? 65  GLN C CB  1 
ATOM   8680  C CG  . GLN C 1 65  ? 16.951  -20.186 47.647  1.00 30.36  ? 65  GLN C CG  1 
ATOM   8681  C CD  . GLN C 1 65  ? 18.279  -20.711 48.153  1.00 32.99  ? 65  GLN C CD  1 
ATOM   8682  O OE1 . GLN C 1 65  ? 18.417  -21.056 49.327  1.00 33.33  ? 65  GLN C OE1 1 
ATOM   8683  N NE2 . GLN C 1 65  ? 19.265  -20.781 47.265  1.00 36.52  ? 65  GLN C NE2 1 
ATOM   8684  N N   . GLU C 1 66  ? 12.777  -21.424 49.325  1.00 33.54  ? 66  GLU C N   1 
ATOM   8685  C CA  . GLU C 1 66  ? 11.755  -22.431 49.598  1.00 39.42  ? 66  GLU C CA  1 
ATOM   8686  C C   . GLU C 1 66  ? 10.510  -22.206 48.747  1.00 38.20  ? 66  GLU C C   1 
ATOM   8687  O O   . GLU C 1 66  ? 9.937   -23.161 48.210  1.00 47.83  ? 66  GLU C O   1 
ATOM   8688  C CB  . GLU C 1 66  ? 11.396  -22.436 51.084  1.00 35.40  ? 66  GLU C CB  1 
ATOM   8689  C CG  . GLU C 1 66  ? 10.455  -23.571 51.468  1.00 43.71  ? 66  GLU C CG  1 
ATOM   8690  C CD  . GLU C 1 66  ? 10.495  -23.913 52.945  1.00 46.34  ? 66  GLU C CD  1 
ATOM   8691  O OE1 . GLU C 1 66  ? 11.050  -23.117 53.731  1.00 44.53  ? 66  GLU C OE1 1 
ATOM   8692  O OE2 . GLU C 1 66  ? 9.969   -24.982 53.321  1.00 43.10  ? 66  GLU C OE2 1 
ATOM   8693  N N   . TYR C 1 67  ? 10.071  -20.951 48.617  1.00 32.17  ? 67  TYR C N   1 
ATOM   8694  C CA  . TYR C 1 67  ? 8.925   -20.657 47.762  1.00 33.09  ? 67  TYR C CA  1 
ATOM   8695  C C   . TYR C 1 67  ? 9.246   -20.926 46.295  1.00 34.11  ? 67  TYR C C   1 
ATOM   8696  O O   . TYR C 1 67  ? 8.409   -21.461 45.559  1.00 35.56  ? 67  TYR C O   1 
ATOM   8697  C CB  . TYR C 1 67  ? 8.480   -19.205 47.955  1.00 33.49  ? 67  TYR C CB  1 
ATOM   8698  C CG  . TYR C 1 67  ? 7.676   -18.960 49.214  1.00 31.81  ? 67  TYR C CG  1 
ATOM   8699  C CD1 . TYR C 1 67  ? 8.308   -18.685 50.418  1.00 34.26  ? 67  TYR C CD1 1 
ATOM   8700  C CD2 . TYR C 1 67  ? 6.286   -18.990 49.197  1.00 32.80  ? 67  TYR C CD2 1 
ATOM   8701  C CE1 . TYR C 1 67  ? 7.585   -18.458 51.571  1.00 33.27  ? 67  TYR C CE1 1 
ATOM   8702  C CE2 . TYR C 1 67  ? 5.552   -18.765 50.349  1.00 32.61  ? 67  TYR C CE2 1 
ATOM   8703  C CZ  . TYR C 1 67  ? 6.209   -18.499 51.532  1.00 31.42  ? 67  TYR C CZ  1 
ATOM   8704  O OH  . TYR C 1 67  ? 5.492   -18.272 52.684  1.00 34.26  ? 67  TYR C OH  1 
ATOM   8705  N N   . ALA C 1 68  ? 10.455  -20.570 45.856  1.00 34.05  ? 68  ALA C N   1 
ATOM   8706  C CA  . ALA C 1 68  ? 10.817  -20.655 44.448  1.00 34.52  ? 68  ALA C CA  1 
ATOM   8707  C C   . ALA C 1 68  ? 11.025  -22.086 43.971  1.00 35.96  ? 68  ALA C C   1 
ATOM   8708  O O   . ALA C 1 68  ? 11.216  -22.293 42.765  1.00 40.97  ? 68  ALA C O   1 
ATOM   8709  C CB  . ALA C 1 68  ? 12.076  -19.825 44.180  1.00 36.98  ? 68  ALA C CB  1 
ATOM   8710  N N   . GLN C 1 69  ? 11.000  -23.072 44.875  1.00 36.06  ? 69  GLN C N   1 
ATOM   8711  C CA  . GLN C 1 69  ? 11.085  -24.471 44.469  1.00 53.06  ? 69  GLN C CA  1 
ATOM   8712  C C   . GLN C 1 69  ? 9.916   -25.280 45.047  1.00 46.62  ? 69  GLN C C   1 
ATOM   8713  O O   . GLN C 1 69  ? 9.943   -26.518 45.046  1.00 44.02  ? 69  GLN C O   1 
ATOM   8714  C CB  . GLN C 1 69  ? 12.467  -25.043 44.853  1.00 51.45  ? 69  GLN C CB  1 
ATOM   8715  C CG  . GLN C 1 69  ? 12.705  -26.573 44.661  1.00 73.25  ? 69  GLN C CG  1 
ATOM   8716  C CD  . GLN C 1 69  ? 14.062  -26.930 44.069  1.00 80.63  ? 69  GLN C CD  1 
ATOM   8717  O OE1 . GLN C 1 69  ? 14.145  -27.771 43.177  1.00 77.76  ? 69  GLN C OE1 1 
ATOM   8718  N NE2 . GLN C 1 69  ? 15.130  -26.318 44.585  1.00 87.26  ? 69  GLN C NE2 1 
ATOM   8719  N N   . GLY C 1 70  ? 8.866   -24.606 45.531  1.00 40.75  ? 70  GLY C N   1 
ATOM   8720  C CA  . GLY C 1 70  ? 7.604   -25.274 45.796  1.00 39.23  ? 70  GLY C CA  1 
ATOM   8721  C C   . GLY C 1 70  ? 7.465   -25.960 47.136  1.00 44.47  ? 70  GLY C C   1 
ATOM   8722  O O   . GLY C 1 70  ? 6.421   -26.574 47.380  1.00 42.63  ? 70  GLY C O   1 
ATOM   8723  N N   . LYS C 1 71  ? 8.474   -25.898 48.006  1.00 39.43  ? 71  LYS C N   1 
ATOM   8724  C CA  . LYS C 1 71  ? 8.348   -26.542 49.307  1.00 44.69  ? 71  LYS C CA  1 
ATOM   8725  C C   . LYS C 1 71  ? 7.653   -25.675 50.345  1.00 52.29  ? 71  LYS C C   1 
ATOM   8726  O O   . LYS C 1 71  ? 7.361   -26.171 51.437  1.00 66.04  ? 71  LYS C O   1 
ATOM   8727  C CB  . LYS C 1 71  ? 9.717   -26.953 49.861  1.00 42.94  ? 71  LYS C CB  1 
ATOM   8728  C CG  . LYS C 1 71  ? 10.683  -27.514 48.850  1.00 44.37  ? 71  LYS C CG  1 
ATOM   8729  C CD  . LYS C 1 71  ? 12.104  -27.387 49.362  1.00 50.89  ? 71  LYS C CD  1 
ATOM   8730  C CE  . LYS C 1 71  ? 13.090  -27.265 48.225  1.00 65.37  ? 71  LYS C CE  1 
ATOM   8731  N NZ  . LYS C 1 71  ? 13.197  -25.845 47.807  1.00 55.82  ? 71  LYS C NZ  1 
ATOM   8732  N N   . ALA C 1 72  ? 7.388   -24.405 50.046  1.00 44.67  ? 72  ALA C N   1 
ATOM   8733  C CA  . ALA C 1 72  ? 6.749   -23.537 51.025  1.00 34.95  ? 72  ALA C CA  1 
ATOM   8734  C C   . ALA C 1 72  ? 5.329   -24.013 51.306  1.00 40.72  ? 72  ALA C C   1 
ATOM   8735  O O   . ALA C 1 72  ? 4.526   -24.196 50.386  1.00 42.17  ? 72  ALA C O   1 
ATOM   8736  C CB  . ALA C 1 72  ? 6.743   -22.094 50.535  1.00 37.11  ? 72  ALA C CB  1 
ATOM   8737  N N   . LYS C 1 73  ? 5.019   -24.202 52.585  1.00 40.99  ? 73  LYS C N   1 
ATOM   8738  C CA  . LYS C 1 73  ? 3.750   -24.766 53.029  1.00 41.69  ? 73  LYS C CA  1 
ATOM   8739  C C   . LYS C 1 73  ? 2.909   -23.719 53.752  1.00 41.56  ? 73  LYS C C   1 
ATOM   8740  O O   . LYS C 1 73  ? 2.296   -23.995 54.785  1.00 40.37  ? 73  LYS C O   1 
ATOM   8741  C CB  . LYS C 1 73  ? 3.983   -25.984 53.918  1.00 38.12  ? 73  LYS C CB  1 
ATOM   8742  C CG  . LYS C 1 73  ? 4.742   -27.110 53.227  1.00 47.25  ? 73  LYS C CG  1 
ATOM   8743  C CD  . LYS C 1 73  ? 5.046   -28.264 54.174  1.00 48.08  ? 73  LYS C CD  1 
ATOM   8744  C CE  . LYS C 1 73  ? 6.421   -28.125 54.807  1.00 49.49  ? 73  LYS C CE  1 
ATOM   8745  N NZ  . LYS C 1 73  ? 6.657   -29.146 55.865  1.00 43.39  ? 73  LYS C NZ  1 
ATOM   8746  N N   . ASP C 1 74  ? 2.888   -22.503 53.208  1.00 38.51  ? 74  ASP C N   1 
ATOM   8747  C CA  . ASP C 1 74  ? 2.166   -21.385 53.806  1.00 39.50  ? 74  ASP C CA  1 
ATOM   8748  C C   . ASP C 1 74  ? 0.699   -21.735 54.018  1.00 45.10  ? 74  ASP C C   1 
ATOM   8749  O O   . ASP C 1 74  ? -0.035  -21.990 53.057  1.00 52.75  ? 74  ASP C O   1 
ATOM   8750  C CB  . ASP C 1 74  ? 2.293   -20.156 52.906  1.00 41.13  ? 74  ASP C CB  1 
ATOM   8751  C CG  . ASP C 1 74  ? 2.138   -18.854 53.667  1.00 46.35  ? 74  ASP C CG  1 
ATOM   8752  O OD1 . ASP C 1 74  ? 1.600   -18.875 54.793  1.00 52.65  ? 74  ASP C OD1 1 
ATOM   8753  O OD2 . ASP C 1 74  ? 2.554   -17.807 53.128  1.00 49.57  ? 74  ASP C OD2 1 
ATOM   8754  N N   . VAL C 1 75  ? 0.267   -21.737 55.284  1.00 46.22  ? 75  VAL C N   1 
ATOM   8755  C CA  . VAL C 1 75  ? -1.118  -22.086 55.597  1.00 50.47  ? 75  VAL C CA  1 
ATOM   8756  C C   . VAL C 1 75  ? -2.089  -20.953 55.316  1.00 39.83  ? 75  VAL C C   1 
ATOM   8757  O O   . VAL C 1 75  ? -3.306  -21.167 55.375  1.00 41.49  ? 75  VAL C O   1 
ATOM   8758  C CB  . VAL C 1 75  ? -1.265  -22.529 57.064  1.00 50.33  ? 75  VAL C CB  1 
ATOM   8759  C CG1 . VAL C 1 75  ? -0.656  -23.907 57.255  1.00 46.96  ? 75  VAL C CG1 1 
ATOM   8760  C CG2 . VAL C 1 75  ? -0.616  -21.519 57.994  1.00 42.69  ? 75  VAL C CG2 1 
ATOM   8761  N N   . PHE C 1 76  ? -1.595  -19.751 55.019  1.00 38.51  ? 76  PHE C N   1 
ATOM   8762  C CA  . PHE C 1 76  ? -2.481  -18.700 54.534  1.00 48.76  ? 76  PHE C CA  1 
ATOM   8763  C C   . PHE C 1 76  ? -2.574  -18.693 53.015  1.00 49.74  ? 76  PHE C C   1 
ATOM   8764  O O   . PHE C 1 76  ? -3.655  -18.461 52.462  1.00 53.57  ? 76  PHE C O   1 
ATOM   8765  C CB  . PHE C 1 76  ? -2.024  -17.324 55.023  1.00 51.59  ? 76  PHE C CB  1 
ATOM   8766  C CG  . PHE C 1 76  ? -2.992  -16.225 54.692  1.00 38.35  ? 76  PHE C CG  1 
ATOM   8767  C CD1 . PHE C 1 76  ? -4.132  -16.040 55.455  1.00 39.58  ? 76  PHE C CD1 1 
ATOM   8768  C CD2 . PHE C 1 76  ? -2.780  -15.397 53.602  1.00 45.07  ? 76  PHE C CD2 1 
ATOM   8769  C CE1 . PHE C 1 76  ? -5.033  -15.042 55.149  1.00 42.99  ? 76  PHE C CE1 1 
ATOM   8770  C CE2 . PHE C 1 76  ? -3.679  -14.395 53.290  1.00 42.39  ? 76  PHE C CE2 1 
ATOM   8771  C CZ  . PHE C 1 76  ? -4.807  -14.220 54.066  1.00 44.05  ? 76  PHE C CZ  1 
ATOM   8772  N N   . LEU C 1 77  ? -1.453  -18.932 52.328  1.00 50.26  ? 77  LEU C N   1 
ATOM   8773  C CA  . LEU C 1 77  ? -1.489  -19.084 50.877  1.00 44.39  ? 77  LEU C CA  1 
ATOM   8774  C C   . LEU C 1 77  ? -2.378  -20.249 50.468  1.00 55.28  ? 77  LEU C C   1 
ATOM   8775  O O   . LEU C 1 77  ? -3.033  -20.196 49.420  1.00 49.80  ? 77  LEU C O   1 
ATOM   8776  C CB  . LEU C 1 77  ? -0.072  -19.282 50.338  1.00 38.22  ? 77  LEU C CB  1 
ATOM   8777  C CG  . LEU C 1 77  ? 0.550   -18.116 49.574  1.00 45.24  ? 77  LEU C CG  1 
ATOM   8778  C CD1 . LEU C 1 77  ? 1.903   -18.516 49.011  1.00 43.69  ? 77  LEU C CD1 1 
ATOM   8779  C CD2 . LEU C 1 77  ? -0.380  -17.658 48.463  1.00 55.42  ? 77  LEU C CD2 1 
ATOM   8780  N N   . GLU C 1 78  ? -2.408  -21.305 51.283  1.00 59.43  ? 78  GLU C N   1 
ATOM   8781  C CA  . GLU C 1 78  ? -3.279  -22.444 51.019  1.00 56.09  ? 78  GLU C CA  1 
ATOM   8782  C C   . GLU C 1 78  ? -4.748  -22.041 51.042  1.00 61.82  ? 78  GLU C C   1 
ATOM   8783  O O   . GLU C 1 78  ? -5.561  -22.607 50.302  1.00 63.92  ? 78  GLU C O   1 
ATOM   8784  C CB  . GLU C 1 78  ? -2.994  -23.541 52.046  1.00 46.97  ? 78  GLU C CB  1 
ATOM   8785  C CG  . GLU C 1 78  ? -3.267  -24.959 51.572  1.00 59.77  ? 78  GLU C CG  1 
ATOM   8786  C CD  . GLU C 1 78  ? -2.700  -25.243 50.199  1.00 74.21  ? 78  GLU C CD  1 
ATOM   8787  O OE1 . GLU C 1 78  ? -1.462  -25.177 50.036  1.00 73.57  ? 78  GLU C OE1 1 
ATOM   8788  O OE2 . GLU C 1 78  ? -3.488  -25.558 49.287  1.00 68.53  ? 78  GLU C OE2 1 
ATOM   8789  N N   . ALA C 1 79  ? -5.104  -21.062 51.873  1.00 58.49  ? 79  ALA C N   1 
ATOM   8790  C CA  . ALA C 1 79  ? -6.464  -20.545 51.943  1.00 58.82  ? 79  ALA C CA  1 
ATOM   8791  C C   . ALA C 1 79  ? -6.766  -19.537 50.843  1.00 57.38  ? 79  ALA C C   1 
ATOM   8792  O O   . ALA C 1 79  ? -7.821  -18.894 50.881  1.00 56.62  ? 79  ALA C O   1 
ATOM   8793  C CB  . ALA C 1 79  ? -6.717  -19.914 53.315  1.00 57.45  ? 79  ALA C CB  1 
ATOM   8794  N N   . ILE C 1 80  ? -5.861  -19.376 49.883  1.00 57.09  ? 80  ILE C N   1 
ATOM   8795  C CA  . ILE C 1 80  ? -6.089  -18.561 48.699  1.00 61.23  ? 80  ILE C CA  1 
ATOM   8796  C C   . ILE C 1 80  ? -6.225  -19.428 47.453  1.00 68.05  ? 80  ILE C C   1 
ATOM   8797  O O   . ILE C 1 80  ? -7.169  -19.273 46.678  1.00 76.48  ? 80  ILE C O   1 
ATOM   8798  C CB  . ILE C 1 80  ? -4.967  -17.514 48.520  1.00 52.64  ? 80  ILE C CB  1 
ATOM   8799  C CG1 . ILE C 1 80  ? -4.796  -16.679 49.792  1.00 50.07  ? 80  ILE C CG1 1 
ATOM   8800  C CG2 . ILE C 1 80  ? -5.262  -16.632 47.318  1.00 45.06  ? 80  ILE C CG2 1 
ATOM   8801  C CD1 . ILE C 1 80  ? -5.591  -15.392 49.796  1.00 48.82  ? 80  ILE C CD1 1 
ATOM   8802  N N   . ARG C 1 81  ? -5.286  -20.355 47.247  1.00 66.93  ? 81  ARG C N   1 
ATOM   8803  C CA  . ARG C 1 81  ? -5.373  -21.263 46.108  1.00 64.54  ? 81  ARG C CA  1 
ATOM   8804  C C   . ARG C 1 81  ? -6.541  -22.232 46.236  1.00 68.88  ? 81  ARG C C   1 
ATOM   8805  O O   . ARG C 1 81  ? -6.912  -22.876 45.250  1.00 81.85  ? 81  ARG C O   1 
ATOM   8806  C CB  . ARG C 1 81  ? -4.050  -22.017 45.952  1.00 50.39  ? 81  ARG C CB  1 
ATOM   8807  C CG  . ARG C 1 81  ? -3.775  -23.028 47.049  1.00 67.76  ? 81  ARG C CG  1 
ATOM   8808  C CD  . ARG C 1 81  ? -3.393  -24.381 46.480  1.00 70.64  ? 81  ARG C CD  1 
ATOM   8809  N NE  . ARG C 1 81  ? -4.523  -25.300 46.433  1.00 66.43  ? 81  ARG C NE  1 
ATOM   8810  C CZ  . ARG C 1 81  ? -4.443  -26.552 46.007  1.00 73.03  ? 81  ARG C CZ  1 
ATOM   8811  N NH1 . ARG C 1 81  ? -3.294  -27.070 45.603  1.00 77.95  ? 81  ARG C NH1 1 
ATOM   8812  N NH2 . ARG C 1 81  ? -5.539  -27.304 45.990  1.00 81.08  ? 81  ARG C NH2 1 
ATOM   8813  N N   . LYS C 1 82  ? -7.136  -22.333 47.419  1.00 66.22  ? 82  LYS C N   1 
ATOM   8814  C CA  . LYS C 1 82  ? -8.217  -23.275 47.661  1.00 65.57  ? 82  LYS C CA  1 
ATOM   8815  C C   . LYS C 1 82  ? -9.501  -22.838 46.960  1.00 65.29  ? 82  LYS C C   1 
ATOM   8816  O O   . LYS C 1 82  ? -9.749  -21.648 46.748  1.00 55.76  ? 82  LYS C O   1 
ATOM   8817  C CB  . LYS C 1 82  ? -8.457  -23.404 49.165  1.00 68.57  ? 82  LYS C CB  1 
ATOM   8818  C CG  . LYS C 1 82  ? -9.219  -24.634 49.593  1.00 75.61  ? 82  LYS C CG  1 
ATOM   8819  C CD  . LYS C 1 82  ? -9.005  -24.887 51.076  1.00 71.68  ? 82  LYS C CD  1 
ATOM   8820  C CE  . LYS C 1 82  ? -9.931  -25.968 51.590  1.00 61.70  ? 82  LYS C CE  1 
ATOM   8821  N NZ  . LYS C 1 82  ? -9.298  -26.943 52.515  1.00 61.97  ? 82  LYS C NZ  1 
ATOM   8822  N N   . ASP C 1 83  ? -10.314 -23.825 46.591  1.00 73.16  ? 83  ASP C N   1 
ATOM   8823  C CA  . ASP C 1 83  ? -11.638 -23.546 46.052  1.00 65.70  ? 83  ASP C CA  1 
ATOM   8824  C C   . ASP C 1 83  ? -12.493 -22.878 47.128  1.00 67.38  ? 83  ASP C C   1 
ATOM   8825  O O   . ASP C 1 83  ? -12.471 -23.302 48.291  1.00 70.16  ? 83  ASP C O   1 
ATOM   8826  C CB  . ASP C 1 83  ? -12.285 -24.846 45.563  1.00 75.33  ? 83  ASP C CB  1 
ATOM   8827  C CG  . ASP C 1 83  ? -13.703 -24.655 45.033  1.00 83.94  ? 83  ASP C CG  1 
ATOM   8828  O OD1 . ASP C 1 83  ? -14.579 -24.162 45.772  1.00 86.50  ? 83  ASP C OD1 1 
ATOM   8829  O OD2 . ASP C 1 83  ? -13.944 -25.015 43.861  1.00 75.97  ? 83  ASP C OD2 1 
ATOM   8830  N N   . PRO C 1 84  ? -13.256 -21.837 46.781  1.00 68.65  ? 84  PRO C N   1 
ATOM   8831  C CA  . PRO C 1 84  ? -14.016 -21.103 47.809  1.00 74.93  ? 84  PRO C CA  1 
ATOM   8832  C C   . PRO C 1 84  ? -15.072 -21.930 48.531  1.00 76.99  ? 84  PRO C C   1 
ATOM   8833  O O   . PRO C 1 84  ? -15.502 -21.527 49.619  1.00 79.10  ? 84  PRO C O   1 
ATOM   8834  C CB  . PRO C 1 84  ? -14.653 -19.952 47.019  1.00 76.78  ? 84  PRO C CB  1 
ATOM   8835  C CG  . PRO C 1 84  ? -13.774 -19.781 45.832  1.00 75.86  ? 84  PRO C CG  1 
ATOM   8836  C CD  . PRO C 1 84  ? -13.297 -21.158 45.476  1.00 74.73  ? 84  PRO C CD  1 
ATOM   8837  N N   . ASP C 1 85  ? -15.515 -23.056 47.970  1.00 71.20  ? 85  ASP C N   1 
ATOM   8838  C CA  . ASP C 1 85  ? -16.414 -23.940 48.702  1.00 76.10  ? 85  ASP C CA  1 
ATOM   8839  C C   . ASP C 1 85  ? -15.672 -24.885 49.632  1.00 80.70  ? 85  ASP C C   1 
ATOM   8840  O O   . ASP C 1 85  ? -16.244 -25.345 50.628  1.00 79.91  ? 85  ASP C O   1 
ATOM   8841  C CB  . ASP C 1 85  ? -17.268 -24.767 47.738  1.00 73.95  ? 85  ASP C CB  1 
ATOM   8842  C CG  . ASP C 1 85  ? -17.899 -23.929 46.652  1.00 85.64  ? 85  ASP C CG  1 
ATOM   8843  O OD1 . ASP C 1 85  ? -17.265 -23.756 45.592  1.00 81.79  ? 85  ASP C OD1 1 
ATOM   8844  O OD2 . ASP C 1 85  ? -19.031 -23.445 46.859  1.00 93.44  ? 85  ASP C OD2 1 
ATOM   8845  N N   . ASP C 1 86  ? -14.410 -25.184 49.326  1.00 78.63  ? 86  ASP C N   1 
ATOM   8846  C CA  . ASP C 1 86  ? -13.650 -26.146 50.113  1.00 78.96  ? 86  ASP C CA  1 
ATOM   8847  C C   . ASP C 1 86  ? -13.194 -25.578 51.452  1.00 73.86  ? 86  ASP C C   1 
ATOM   8848  O O   . ASP C 1 86  ? -12.944 -26.354 52.380  1.00 79.31  ? 86  ASP C O   1 
ATOM   8849  C CB  . ASP C 1 86  ? -12.441 -26.627 49.306  1.00 74.08  ? 86  ASP C CB  1 
ATOM   8850  C CG  . ASP C 1 86  ? -12.327 -28.140 49.263  1.00 82.33  ? 86  ASP C CG  1 
ATOM   8851  O OD1 . ASP C 1 86  ? -13.206 -28.825 49.827  1.00 73.35  ? 86  ASP C OD1 1 
ATOM   8852  O OD2 . ASP C 1 86  ? -11.350 -28.641 48.666  1.00 84.71  ? 86  ASP C OD2 1 
ATOM   8853  N N   . LEU C 1 87  ? -13.098 -24.254 51.580  1.00 63.64  ? 87  LEU C N   1 
ATOM   8854  C CA  . LEU C 1 87  ? -12.448 -23.642 52.731  1.00 63.62  ? 87  LEU C CA  1 
ATOM   8855  C C   . LEU C 1 87  ? -13.173 -23.979 54.033  1.00 66.55  ? 87  LEU C C   1 
ATOM   8856  O O   . LEU C 1 87  ? -14.304 -24.470 54.051  1.00 66.13  ? 87  LEU C O   1 
ATOM   8857  C CB  . LEU C 1 87  ? -12.375 -22.123 52.578  1.00 67.47  ? 87  LEU C CB  1 
ATOM   8858  C CG  . LEU C 1 87  ? -11.781 -21.498 51.317  1.00 66.75  ? 87  LEU C CG  1 
ATOM   8859  C CD1 . LEU C 1 87  ? -12.591 -20.275 50.928  1.00 62.06  ? 87  LEU C CD1 1 
ATOM   8860  C CD2 . LEU C 1 87  ? -10.323 -21.129 51.535  1.00 56.18  ? 87  LEU C CD2 1 
ATOM   8861  N N   . GLU C 1 88  ? -12.492 -23.693 55.137  1.00 74.62  ? 88  GLU C N   1 
ATOM   8862  C CA  . GLU C 1 88  ? -13.015 -23.889 56.480  1.00 74.51  ? 88  GLU C CA  1 
ATOM   8863  C C   . GLU C 1 88  ? -13.451 -22.557 57.079  1.00 72.89  ? 88  GLU C C   1 
ATOM   8864  O O   . GLU C 1 88  ? -13.065 -21.482 56.614  1.00 69.71  ? 88  GLU C O   1 
ATOM   8865  C CB  . GLU C 1 88  ? -11.963 -24.547 57.378  1.00 62.83  ? 88  GLU C CB  1 
ATOM   8866  C CG  . GLU C 1 88  ? -12.488 -25.706 58.204  1.00 59.92  ? 88  GLU C CG  1 
ATOM   8867  C CD  . GLU C 1 88  ? -12.458 -27.017 57.448  1.00 73.85  ? 88  GLU C CD  1 
ATOM   8868  O OE1 . GLU C 1 88  ? -11.349 -27.516 57.164  1.00 74.21  ? 88  GLU C OE1 1 
ATOM   8869  O OE2 . GLU C 1 88  ? -13.545 -27.550 57.137  1.00 82.09  ? 88  GLU C OE2 1 
ATOM   8870  N N   . LYS C 1 89  ? -14.270 -22.647 58.130  1.00 65.24  ? 89  LYS C N   1 
ATOM   8871  C CA  . LYS C 1 89  ? -14.723 -21.442 58.819  1.00 68.24  ? 89  LYS C CA  1 
ATOM   8872  C C   . LYS C 1 89  ? -13.546 -20.667 59.398  1.00 64.97  ? 89  LYS C C   1 
ATOM   8873  O O   . LYS C 1 89  ? -13.513 -19.432 59.335  1.00 66.19  ? 89  LYS C O   1 
ATOM   8874  C CB  . LYS C 1 89  ? -15.723 -21.814 59.915  1.00 70.21  ? 89  LYS C CB  1 
ATOM   8875  C CG  . LYS C 1 89  ? -15.925 -20.747 60.981  1.00 61.60  ? 89  LYS C CG  1 
ATOM   8876  C CD  . LYS C 1 89  ? -16.937 -21.196 62.027  1.00 70.05  ? 89  LYS C CD  1 
ATOM   8877  C CE  . LYS C 1 89  ? -16.339 -22.215 62.985  1.00 76.05  ? 89  LYS C CE  1 
ATOM   8878  N NZ  . LYS C 1 89  ? -15.815 -21.577 64.226  1.00 72.53  ? 89  LYS C NZ  1 
ATOM   8879  N N   . GLU C 1 90  ? -12.566 -21.378 59.960  1.00 66.91  ? 90  GLU C N   1 
ATOM   8880  C CA  . GLU C 1 90  ? -11.386 -20.717 60.511  1.00 67.11  ? 90  GLU C CA  1 
ATOM   8881  C C   . GLU C 1 90  ? -10.564 -20.043 59.419  1.00 63.80  ? 90  GLU C C   1 
ATOM   8882  O O   . GLU C 1 90  ? -10.016 -18.955 59.632  1.00 69.37  ? 90  GLU C O   1 
ATOM   8883  C CB  . GLU C 1 90  ? -10.536 -21.725 61.284  1.00 66.10  ? 90  GLU C CB  1 
ATOM   8884  C CG  . GLU C 1 90  ? -11.264 -22.393 62.442  1.00 69.85  ? 90  GLU C CG  1 
ATOM   8885  C CD  . GLU C 1 90  ? -12.016 -23.644 62.025  1.00 76.06  ? 90  GLU C CD  1 
ATOM   8886  O OE1 . GLU C 1 90  ? -12.266 -23.817 60.814  1.00 74.35  ? 90  GLU C OE1 1 
ATOM   8887  O OE2 . GLU C 1 90  ? -12.362 -24.453 62.911  1.00 77.13  ? 90  GLU C OE2 1 
ATOM   8888  N N   . GLU C 1 91  ? -10.455 -20.677 58.249  1.00 60.63  ? 91  GLU C N   1 
ATOM   8889  C CA  . GLU C 1 91  ? -9.771  -20.037 57.130  1.00 55.26  ? 91  GLU C CA  1 
ATOM   8890  C C   . GLU C 1 91  ? -10.566 -18.852 56.599  1.00 54.08  ? 91  GLU C C   1 
ATOM   8891  O O   . GLU C 1 91  ? -9.975  -17.867 56.139  1.00 52.78  ? 91  GLU C O   1 
ATOM   8892  C CB  . GLU C 1 91  ? -9.518  -21.051 56.016  1.00 50.41  ? 91  GLU C CB  1 
ATOM   8893  C CG  . GLU C 1 91  ? -8.774  -22.291 56.474  1.00 58.51  ? 91  GLU C CG  1 
ATOM   8894  C CD  . GLU C 1 91  ? -8.618  -23.317 55.371  1.00 69.13  ? 91  GLU C CD  1 
ATOM   8895  O OE1 . GLU C 1 91  ? -8.017  -22.984 54.327  1.00 74.54  ? 91  GLU C OE1 1 
ATOM   8896  O OE2 . GLU C 1 91  ? -9.096  -24.457 55.548  1.00 63.31  ? 91  GLU C OE2 1 
ATOM   8897  N N   . VAL C 1 92  ? -11.898 -18.932 56.646  1.00 61.00  ? 92  VAL C N   1 
ATOM   8898  C CA  . VAL C 1 92  ? -12.724 -17.789 56.270  1.00 59.95  ? 92  VAL C CA  1 
ATOM   8899  C C   . VAL C 1 92  ? -12.443 -16.612 57.193  1.00 57.78  ? 92  VAL C C   1 
ATOM   8900  O O   . VAL C 1 92  ? -12.286 -15.472 56.739  1.00 52.19  ? 92  VAL C O   1 
ATOM   8901  C CB  . VAL C 1 92  ? -14.214 -18.183 56.279  1.00 58.49  ? 92  VAL C CB  1 
ATOM   8902  C CG1 . VAL C 1 92  ? -15.100 -16.949 56.381  1.00 58.15  ? 92  VAL C CG1 1 
ATOM   8903  C CG2 . VAL C 1 92  ? -14.557 -18.987 55.034  1.00 58.48  ? 92  VAL C CG2 1 
ATOM   8904  N N   . GLU C 1 93  ? -12.355 -16.871 58.502  1.00 59.43  ? 93  GLU C N   1 
ATOM   8905  C CA  . GLU C 1 93  ? -12.010 -15.813 59.447  1.00 58.54  ? 93  GLU C CA  1 
ATOM   8906  C C   . GLU C 1 93  ? -10.599 -15.295 59.199  1.00 63.00  ? 93  GLU C C   1 
ATOM   8907  O O   . GLU C 1 93  ? -10.330 -14.098 59.361  1.00 62.16  ? 93  GLU C O   1 
ATOM   8908  C CB  . GLU C 1 93  ? -12.161 -16.319 60.884  1.00 54.66  ? 93  GLU C CB  1 
ATOM   8909  C CG  . GLU C 1 93  ? -11.738 -15.317 61.949  1.00 65.05  ? 93  GLU C CG  1 
ATOM   8910  C CD  . GLU C 1 93  ? -10.669 -15.858 62.879  1.00 73.49  ? 93  GLU C CD  1 
ATOM   8911  O OE1 . GLU C 1 93  ? -10.459 -15.254 63.953  1.00 72.55  ? 93  GLU C OE1 1 
ATOM   8912  O OE2 . GLU C 1 93  ? -10.039 -16.883 62.538  1.00 64.19  ? 93  GLU C OE2 1 
ATOM   8913  N N   . LYS C 1 94  ? -9.685  -16.182 58.799  1.00 60.12  ? 94  LYS C N   1 
ATOM   8914  C CA  . LYS C 1 94  ? -8.326  -15.756 58.479  1.00 54.57  ? 94  LYS C CA  1 
ATOM   8915  C C   . LYS C 1 94  ? -8.317  -14.781 57.309  1.00 53.60  ? 94  LYS C C   1 
ATOM   8916  O O   . LYS C 1 94  ? -7.547  -13.813 57.301  1.00 56.58  ? 94  LYS C O   1 
ATOM   8917  C CB  . LYS C 1 94  ? -7.453  -16.972 58.168  1.00 54.76  ? 94  LYS C CB  1 
ATOM   8918  C CG  . LYS C 1 94  ? -6.683  -17.518 59.361  1.00 56.49  ? 94  LYS C CG  1 
ATOM   8919  C CD  . LYS C 1 94  ? -5.404  -18.213 58.918  1.00 55.73  ? 94  LYS C CD  1 
ATOM   8920  C CE  . LYS C 1 94  ? -5.519  -19.727 59.035  1.00 55.94  ? 94  LYS C CE  1 
ATOM   8921  N NZ  . LYS C 1 94  ? -5.374  -20.192 60.444  1.00 50.99  ? 94  LYS C NZ  1 
ATOM   8922  N N   . LEU C 1 95  ? -9.169  -15.019 56.310  1.00 59.16  ? 95  LEU C N   1 
ATOM   8923  C CA  . LEU C 1 95  ? -9.162  -14.176 55.119  1.00 60.19  ? 95  LEU C CA  1 
ATOM   8924  C C   . LEU C 1 95  ? -9.758  -12.799 55.395  1.00 53.79  ? 95  LEU C C   1 
ATOM   8925  O O   . LEU C 1 95  ? -9.259  -11.792 54.878  1.00 54.34  ? 95  LEU C O   1 
ATOM   8926  C CB  . LEU C 1 95  ? -9.907  -14.873 53.981  1.00 69.39  ? 95  LEU C CB  1 
ATOM   8927  C CG  . LEU C 1 95  ? -9.067  -15.880 53.190  1.00 65.23  ? 95  LEU C CG  1 
ATOM   8928  C CD1 . LEU C 1 95  ? -9.913  -17.053 52.717  1.00 63.15  ? 95  LEU C CD1 1 
ATOM   8929  C CD2 . LEU C 1 95  ? -8.387  -15.195 52.017  1.00 48.78  ? 95  LEU C CD2 1 
ATOM   8930  N N   . ILE C 1 96  ? -10.828 -12.726 56.192  1.00 48.56  ? 96  ILE C N   1 
ATOM   8931  C CA  . ILE C 1 96  ? -11.427 -11.422 56.470  1.00 55.04  ? 96  ILE C CA  1 
ATOM   8932  C C   . ILE C 1 96  ? -10.522 -10.599 57.379  1.00 60.30  ? 96  ILE C C   1 
ATOM   8933  O O   . ILE C 1 96  ? -10.321 -9.400  57.153  1.00 58.01  ? 96  ILE C O   1 
ATOM   8934  C CB  . ILE C 1 96  ? -12.842 -11.566 57.064  1.00 51.78  ? 96  ILE C CB  1 
ATOM   8935  C CG1 . ILE C 1 96  ? -12.930 -12.764 58.003  1.00 52.16  ? 96  ILE C CG1 1 
ATOM   8936  C CG2 . ILE C 1 96  ? -13.879 -11.674 55.953  1.00 57.63  ? 96  ILE C CG2 1 
ATOM   8937  C CD1 . ILE C 1 96  ? -14.289 -12.935 58.655  1.00 54.76  ? 96  ILE C CD1 1 
ATOM   8938  N N   . GLU C 1 97  ? -9.957  -11.224 58.417  1.00 59.12  ? 97  GLU C N   1 
ATOM   8939  C CA  . GLU C 1 97  ? -9.117  -10.477 59.348  1.00 64.17  ? 97  GLU C CA  1 
ATOM   8940  C C   . GLU C 1 97  ? -7.834  -9.989  58.686  1.00 55.33  ? 97  GLU C C   1 
ATOM   8941  O O   . GLU C 1 97  ? -7.325  -8.920  59.043  1.00 54.94  ? 97  GLU C O   1 
ATOM   8942  C CB  . GLU C 1 97  ? -8.794  -11.325 60.578  1.00 61.80  ? 97  GLU C CB  1 
ATOM   8943  C CG  . GLU C 1 97  ? -9.849  -11.234 61.675  1.00 63.56  ? 97  GLU C CG  1 
ATOM   8944  C CD  . GLU C 1 97  ? -9.511  -10.194 62.729  1.00 71.26  ? 97  GLU C CD  1 
ATOM   8945  O OE1 . GLU C 1 97  ? -9.719  -8.990  62.466  1.00 69.00  ? 97  GLU C OE1 1 
ATOM   8946  O OE2 . GLU C 1 97  ? -9.046  -10.579 63.823  1.00 69.74  ? 97  GLU C OE2 1 
ATOM   8947  N N   . PHE C 1 98  ? -7.291  -10.750 57.731  1.00 45.99  ? 98  PHE C N   1 
ATOM   8948  C CA  . PHE C 1 98  ? -6.147  -10.253 56.972  1.00 49.02  ? 98  PHE C CA  1 
ATOM   8949  C C   . PHE C 1 98  ? -6.546  -9.089  56.074  1.00 53.93  ? 98  PHE C C   1 
ATOM   8950  O O   . PHE C 1 98  ? -5.792  -8.119  55.932  1.00 49.00  ? 98  PHE C O   1 
ATOM   8951  C CB  . PHE C 1 98  ? -5.523  -11.367 56.137  1.00 49.79  ? 98  PHE C CB  1 
ATOM   8952  C CG  . PHE C 1 98  ? -4.285  -10.938 55.406  1.00 44.85  ? 98  PHE C CG  1 
ATOM   8953  C CD1 . PHE C 1 98  ? -3.159  -10.540 56.106  1.00 44.52  ? 98  PHE C CD1 1 
ATOM   8954  C CD2 . PHE C 1 98  ? -4.255  -10.904 54.023  1.00 38.33  ? 98  PHE C CD2 1 
ATOM   8955  C CE1 . PHE C 1 98  ? -2.022  -10.134 55.441  1.00 41.03  ? 98  PHE C CE1 1 
ATOM   8956  C CE2 . PHE C 1 98  ? -3.121  -10.499 53.354  1.00 36.92  ? 98  PHE C CE2 1 
ATOM   8957  C CZ  . PHE C 1 98  ? -2.004  -10.112 54.065  1.00 35.25  ? 98  PHE C CZ  1 
ATOM   8958  N N   . THR C 1 99  ? -7.722  -9.175  55.448  1.00 58.13  ? 99  THR C N   1 
ATOM   8959  C CA  . THR C 1 99  ? -8.213  -8.069  54.637  1.00 52.02  ? 99  THR C CA  1 
ATOM   8960  C C   . THR C 1 99  ? -8.705  -6.908  55.492  1.00 51.68  ? 99  THR C C   1 
ATOM   8961  O O   . THR C 1 99  ? -8.746  -5.772  55.007  1.00 53.64  ? 99  THR C O   1 
ATOM   8962  C CB  . THR C 1 99  ? -9.329  -8.555  53.710  1.00 45.73  ? 99  THR C CB  1 
ATOM   8963  O OG1 . THR C 1 99  ? -9.051  -9.894  53.284  1.00 47.04  ? 99  THR C OG1 1 
ATOM   8964  C CG2 . THR C 1 99  ? -9.456  -7.650  52.493  1.00 46.24  ? 99  THR C CG2 1 
ATOM   8965  N N   . LYS C 1 100 ? -9.077  -7.164  56.750  1.00 46.28  ? 100 LYS C N   1 
ATOM   8966  C CA  . LYS C 1 100 ? -9.471  -6.077  57.641  1.00 54.53  ? 100 LYS C CA  1 
ATOM   8967  C C   . LYS C 1 100 ? -8.259  -5.289  58.126  1.00 50.19  ? 100 LYS C C   1 
ATOM   8968  O O   . LYS C 1 100 ? -8.303  -4.055  58.203  1.00 43.48  ? 100 LYS C O   1 
ATOM   8969  C CB  . LYS C 1 100 ? -10.266 -6.631  58.825  1.00 59.76  ? 100 LYS C CB  1 
ATOM   8970  C CG  . LYS C 1 100 ? -11.727 -6.926  58.507  1.00 52.89  ? 100 LYS C CG  1 
ATOM   8971  C CD  . LYS C 1 100 ? -12.454 -7.524  59.702  1.00 50.49  ? 100 LYS C CD  1 
ATOM   8972  C CE  . LYS C 1 100 ? -12.631 -6.506  60.818  1.00 56.31  ? 100 LYS C CE  1 
ATOM   8973  N NZ  . LYS C 1 100 ? -13.378 -7.078  61.975  1.00 58.74  ? 100 LYS C NZ  1 
ATOM   8974  N N   . LEU C 1 101 ? -7.166  -5.987  58.451  1.00 54.27  ? 101 LEU C N   1 
ATOM   8975  C CA  . LEU C 1 101 ? -5.963  -5.319  58.943  1.00 58.49  ? 101 LEU C CA  1 
ATOM   8976  C C   . LEU C 1 101 ? -5.251  -4.540  57.843  1.00 50.52  ? 101 LEU C C   1 
ATOM   8977  O O   . LEU C 1 101 ? -4.533  -3.582  58.145  1.00 50.91  ? 101 LEU C O   1 
ATOM   8978  C CB  . LEU C 1 101 ? -5.025  -6.353  59.576  1.00 60.64  ? 101 LEU C CB  1 
ATOM   8979  C CG  . LEU C 1 101 ? -3.718  -5.961  60.281  1.00 65.00  ? 101 LEU C CG  1 
ATOM   8980  C CD1 . LEU C 1 101 ? -2.527  -5.924  59.324  1.00 58.03  ? 101 LEU C CD1 1 
ATOM   8981  C CD2 . LEU C 1 101 ? -3.848  -4.643  61.036  1.00 58.57  ? 101 LEU C CD2 1 
ATOM   8982  N N   . ASN C 1 102 ? -5.442  -4.917  56.580  1.00 52.82  ? 102 ASN C N   1 
ATOM   8983  C CA  . ASN C 1 102 ? -4.852  -4.220  55.446  1.00 49.49  ? 102 ASN C CA  1 
ATOM   8984  C C   . ASN C 1 102 ? -5.840  -3.296  54.747  1.00 46.57  ? 102 ASN C C   1 
ATOM   8985  O O   . ASN C 1 102 ? -5.541  -2.802  53.657  1.00 51.10  ? 102 ASN C O   1 
ATOM   8986  C CB  . ASN C 1 102 ? -4.297  -5.226  54.436  1.00 42.72  ? 102 ASN C CB  1 
ATOM   8987  C CG  . ASN C 1 102 ? -3.256  -6.141  55.036  1.00 40.89  ? 102 ASN C CG  1 
ATOM   8988  O OD1 . ASN C 1 102 ? -2.859  -5.980  56.189  1.00 48.72  ? 102 ASN C OD1 1 
ATOM   8989  N ND2 . ASN C 1 102 ? -2.808  -7.112  54.255  1.00 40.99  ? 102 ASN C ND2 1 
ATOM   8990  N N   . TYR C 1 103 ? -6.999  -3.046  55.357  1.00 44.82  ? 103 TYR C N   1 
ATOM   8991  C CA  . TYR C 1 103 ? -8.103  -2.395  54.657  1.00 50.09  ? 103 TYR C CA  1 
ATOM   8992  C C   . TYR C 1 103 ? -7.722  -1.004  54.159  1.00 54.18  ? 103 TYR C C   1 
ATOM   8993  O O   . TYR C 1 103 ? -7.908  -0.681  52.979  1.00 52.71  ? 103 TYR C O   1 
ATOM   8994  C CB  . TYR C 1 103 ? -9.315  -2.324  55.588  1.00 52.43  ? 103 TYR C CB  1 
ATOM   8995  C CG  . TYR C 1 103 ? -10.597 -1.846  54.944  1.00 61.86  ? 103 TYR C CG  1 
ATOM   8996  C CD1 . TYR C 1 103 ? -10.882 -0.489  54.837  1.00 53.37  ? 103 TYR C CD1 1 
ATOM   8997  C CD2 . TYR C 1 103 ? -11.533 -2.753  54.463  1.00 69.41  ? 103 TYR C CD2 1 
ATOM   8998  C CE1 . TYR C 1 103 ? -12.057 -0.049  54.257  1.00 53.45  ? 103 TYR C CE1 1 
ATOM   8999  C CE2 . TYR C 1 103 ? -12.710 -2.322  53.883  1.00 74.42  ? 103 TYR C CE2 1 
ATOM   9000  C CZ  . TYR C 1 103 ? -12.966 -0.971  53.782  1.00 62.72  ? 103 TYR C CZ  1 
ATOM   9001  O OH  . TYR C 1 103 ? -14.138 -0.543  53.207  1.00 60.95  ? 103 TYR C OH  1 
ATOM   9002  N N   . GLU C 1 104 ? -7.174  -0.170  55.040  1.00 55.43  ? 104 GLU C N   1 
ATOM   9003  C CA  . GLU C 1 104 ? -7.039  1.254   54.759  1.00 46.18  ? 104 GLU C CA  1 
ATOM   9004  C C   . GLU C 1 104 ? -5.823  1.603   53.906  1.00 52.79  ? 104 GLU C C   1 
ATOM   9005  O O   . GLU C 1 104 ? -5.703  2.758   53.483  1.00 47.49  ? 104 GLU C O   1 
ATOM   9006  C CB  . GLU C 1 104 ? -6.987  2.033   56.076  1.00 50.77  ? 104 GLU C CB  1 
ATOM   9007  C CG  . GLU C 1 104 ? -8.007  1.559   57.107  1.00 55.18  ? 104 GLU C CG  1 
ATOM   9008  C CD  . GLU C 1 104 ? -7.891  2.284   58.437  1.00 74.34  ? 104 GLU C CD  1 
ATOM   9009  O OE1 . GLU C 1 104 ? -7.304  3.385   58.471  1.00 75.37  ? 104 GLU C OE1 1 
ATOM   9010  O OE2 . GLU C 1 104 ? -8.385  1.747   59.452  1.00 72.00  ? 104 GLU C OE2 1 
ATOM   9011  N N   . LYS C 1 105 ? -4.932  0.652   53.640  1.00 58.11  ? 105 LYS C N   1 
ATOM   9012  C CA  . LYS C 1 105 ? -3.710  0.966   52.908  1.00 46.94  ? 105 LYS C CA  1 
ATOM   9013  C C   . LYS C 1 105 ? -4.019  1.247   51.438  1.00 52.21  ? 105 LYS C C   1 
ATOM   9014  O O   . LYS C 1 105 ? -4.891  0.599   50.851  1.00 53.74  ? 105 LYS C O   1 
ATOM   9015  C CB  . LYS C 1 105 ? -2.707  -0.177  53.026  1.00 36.83  ? 105 LYS C CB  1 
ATOM   9016  C CG  . LYS C 1 105 ? -2.350  -0.529  54.460  1.00 42.38  ? 105 LYS C CG  1 
ATOM   9017  C CD  . LYS C 1 105 ? -1.461  -1.758  54.526  1.00 45.35  ? 105 LYS C CD  1 
ATOM   9018  C CE  . LYS C 1 105 ? -1.164  -2.152  55.965  1.00 39.68  ? 105 LYS C CE  1 
ATOM   9019  N NZ  . LYS C 1 105 ? 0.063   -2.991  56.068  1.00 42.27  ? 105 LYS C NZ  1 
ATOM   9020  N N   . PRO C 1 106 ? -3.320  2.207   50.820  1.00 50.24  ? 106 PRO C N   1 
ATOM   9021  C CA  . PRO C 1 106 ? -3.634  2.566   49.423  1.00 48.54  ? 106 PRO C CA  1 
ATOM   9022  C C   . PRO C 1 106 ? -3.543  1.407   48.444  1.00 46.84  ? 106 PRO C C   1 
ATOM   9023  O O   . PRO C 1 106 ? -4.326  1.356   47.491  1.00 49.98  ? 106 PRO C O   1 
ATOM   9024  C CB  . PRO C 1 106 ? -2.596  3.651   49.100  1.00 52.04  ? 106 PRO C CB  1 
ATOM   9025  C CG  . PRO C 1 106 ? -2.212  4.238   50.412  1.00 49.15  ? 106 PRO C CG  1 
ATOM   9026  C CD  . PRO C 1 106 ? -2.476  3.216   51.487  1.00 50.60  ? 106 PRO C CD  1 
ATOM   9027  N N   . ILE C 1 107 ? -2.606  0.477   48.636  1.00 52.17  ? 107 ILE C N   1 
ATOM   9028  C CA  . ILE C 1 107 ? -2.502  -0.661  47.727  1.00 48.19  ? 107 ILE C CA  1 
ATOM   9029  C C   . ILE C 1 107 ? -3.661  -1.633  47.875  1.00 49.66  ? 107 ILE C C   1 
ATOM   9030  O O   . ILE C 1 107 ? -3.817  -2.528  47.037  1.00 49.77  ? 107 ILE C O   1 
ATOM   9031  C CB  . ILE C 1 107 ? -1.166  -1.410  47.919  1.00 51.33  ? 107 ILE C CB  1 
ATOM   9032  C CG1 . ILE C 1 107 ? -1.223  -2.312  49.153  1.00 43.86  ? 107 ILE C CG1 1 
ATOM   9033  C CG2 . ILE C 1 107 ? -0.008  -0.427  48.009  1.00 44.22  ? 107 ILE C CG2 1 
ATOM   9034  C CD1 . ILE C 1 107 ? -0.030  -3.233  49.285  1.00 36.06  ? 107 ILE C CD1 1 
ATOM   9035  N N   . TYR C 1 108 ? -4.476  -1.480  48.919  1.00 54.84  ? 108 TYR C N   1 
ATOM   9036  C CA  . TYR C 1 108 ? -5.672  -2.285  49.134  1.00 59.42  ? 108 TYR C CA  1 
ATOM   9037  C C   . TYR C 1 108 ? -6.946  -1.503  48.832  1.00 61.33  ? 108 TYR C C   1 
ATOM   9038  O O   . TYR C 1 108 ? -7.977  -1.714  49.474  1.00 66.06  ? 108 TYR C O   1 
ATOM   9039  C CB  . TYR C 1 108 ? -5.722  -2.804  50.567  1.00 45.65  ? 108 TYR C CB  1 
ATOM   9040  C CG  . TYR C 1 108 ? -5.283  -4.235  50.744  1.00 49.24  ? 108 TYR C CG  1 
ATOM   9041  C CD1 . TYR C 1 108 ? -3.944  -4.553  50.921  1.00 56.84  ? 108 TYR C CD1 1 
ATOM   9042  C CD2 . TYR C 1 108 ? -6.210  -5.268  50.743  1.00 46.11  ? 108 TYR C CD2 1 
ATOM   9043  C CE1 . TYR C 1 108 ? -3.540  -5.861  51.091  1.00 54.00  ? 108 TYR C CE1 1 
ATOM   9044  C CE2 . TYR C 1 108 ? -5.815  -6.581  50.911  1.00 47.25  ? 108 TYR C CE2 1 
ATOM   9045  C CZ  . TYR C 1 108 ? -4.478  -6.872  51.084  1.00 50.14  ? 108 TYR C CZ  1 
ATOM   9046  O OH  . TYR C 1 108 ? -4.078  -8.177  51.251  1.00 45.29  ? 108 TYR C OH  1 
ATOM   9047  N N   . ARG C 1 109 ? -6.890  -0.596  47.866  1.00 46.97  ? 109 ARG C N   1 
ATOM   9048  C CA  . ARG C 1 109 ? -7.989  0.321   47.585  1.00 46.92  ? 109 ARG C CA  1 
ATOM   9049  C C   . ARG C 1 109 ? -8.695  -0.131  46.312  1.00 55.20  ? 109 ARG C C   1 
ATOM   9050  O O   . ARG C 1 109 ? -8.396  0.341   45.215  1.00 49.13  ? 109 ARG C O   1 
ATOM   9051  C CB  . ARG C 1 109 ? -7.477  1.738   47.463  1.00 52.76  ? 109 ARG C CB  1 
ATOM   9052  C CG  . ARG C 1 109 ? -8.552  2.792   47.613  1.00 67.11  ? 109 ARG C CG  1 
ATOM   9053  C CD  . ARG C 1 109 ? -7.939  4.176   47.765  1.00 69.76  ? 109 ARG C CD  1 
ATOM   9054  N NE  . ARG C 1 109 ? -6.861  4.527   46.839  1.00 65.98  ? 109 ARG C NE  1 
ATOM   9055  C CZ  . ARG C 1 109 ? -6.836  4.303   45.528  1.00 75.13  ? 109 ARG C CZ  1 
ATOM   9056  N NH1 . ARG C 1 109 ? -7.875  3.791   44.884  1.00 76.37  ? 109 ARG C NH1 1 
ATOM   9057  N NH2 . ARG C 1 109 ? -5.748  4.635   44.838  1.00 67.66  ? 109 ARG C NH2 1 
ATOM   9058  N N   . PHE C 1 110 ? -9.657  -1.035  46.475  1.00 65.59  ? 110 PHE C N   1 
ATOM   9059  C CA  . PHE C 1 110 ? -10.431 -1.580  45.371  1.00 63.43  ? 110 PHE C CA  1 
ATOM   9060  C C   . PHE C 1 110 ? -11.914 -1.413  45.665  1.00 62.11  ? 110 PHE C C   1 
ATOM   9061  O O   . PHE C 1 110 ? -12.330 -1.337  46.825  1.00 54.60  ? 110 PHE C O   1 
ATOM   9062  C CB  . PHE C 1 110 ? -10.107 -3.062  45.137  1.00 51.47  ? 110 PHE C CB  1 
ATOM   9063  C CG  . PHE C 1 110 ? -8.785  -3.296  44.462  1.00 49.70  ? 110 PHE C CG  1 
ATOM   9064  C CD1 . PHE C 1 110 ? -8.519  -2.753  43.216  1.00 50.32  ? 110 PHE C CD1 1 
ATOM   9065  C CD2 . PHE C 1 110 ? -7.810  -4.067  45.072  1.00 53.24  ? 110 PHE C CD2 1 
ATOM   9066  C CE1 . PHE C 1 110 ? -7.302  -2.972  42.593  1.00 48.86  ? 110 PHE C CE1 1 
ATOM   9067  C CE2 . PHE C 1 110 ? -6.592  -4.289  44.456  1.00 48.23  ? 110 PHE C CE2 1 
ATOM   9068  C CZ  . PHE C 1 110 ? -6.339  -3.741  43.215  1.00 46.76  ? 110 PHE C CZ  1 
ATOM   9069  N N   . GLU C 1 111 ? -12.711 -1.348  44.596  1.00 62.70  ? 111 GLU C N   1 
ATOM   9070  C CA  . GLU C 1 111 ? -14.144 -1.122  44.754  1.00 64.05  ? 111 GLU C CA  1 
ATOM   9071  C C   . GLU C 1 111 ? -14.819 -2.278  45.486  1.00 73.33  ? 111 GLU C C   1 
ATOM   9072  O O   . GLU C 1 111 ? -15.640 -2.057  46.384  1.00 75.38  ? 111 GLU C O   1 
ATOM   9073  C CB  . GLU C 1 111 ? -14.794 -0.903  43.388  1.00 75.97  ? 111 GLU C CB  1 
ATOM   9074  C CG  . GLU C 1 111 ? -14.113 -1.641  42.248  1.00 80.38  ? 111 GLU C CG  1 
ATOM   9075  C CD  . GLU C 1 111 ? -14.541 -1.138  40.883  1.00 75.76  ? 111 GLU C CD  1 
ATOM   9076  O OE1 . GLU C 1 111 ? -14.267 0.039   40.568  1.00 83.76  ? 111 GLU C OE1 1 
ATOM   9077  O OE2 . GLU C 1 111 ? -15.152 -1.921  40.127  1.00 73.39  ? 111 GLU C OE2 1 
ATOM   9078  N N   . ARG C 1 112 ? -14.482 -3.517  45.120  1.00 77.44  ? 112 ARG C N   1 
ATOM   9079  C CA  . ARG C 1 112 ? -15.170 -4.675  45.682  1.00 70.26  ? 112 ARG C CA  1 
ATOM   9080  C C   . ARG C 1 112 ? -14.748 -4.970  47.117  1.00 81.43  ? 112 ARG C C   1 
ATOM   9081  O O   . ARG C 1 112 ? -15.531 -5.550  47.878  1.00 80.59  ? 112 ARG C O   1 
ATOM   9082  C CB  . ARG C 1 112 ? -14.929 -5.907  44.811  1.00 61.33  ? 112 ARG C CB  1 
ATOM   9083  C CG  . ARG C 1 112 ? -15.963 -6.129  43.730  1.00 77.24  ? 112 ARG C CG  1 
ATOM   9084  C CD  . ARG C 1 112 ? -17.357 -6.278  44.309  1.00 77.28  ? 112 ARG C CD  1 
ATOM   9085  N NE  . ARG C 1 112 ? -17.602 -7.616  44.833  1.00 70.50  ? 112 ARG C NE  1 
ATOM   9086  C CZ  . ARG C 1 112 ? -18.018 -8.643  44.104  1.00 73.02  ? 112 ARG C CZ  1 
ATOM   9087  N NH1 . ARG C 1 112 ? -18.243 -8.524  42.805  1.00 76.49  ? 112 ARG C NH1 1 
ATOM   9088  N NH2 . ARG C 1 112 ? -18.210 -9.820  44.692  1.00 70.38  ? 112 ARG C NH2 1 
ATOM   9089  N N   . ILE C 1 113 ? -13.525 -4.600  47.500  1.00 85.21  ? 113 ILE C N   1 
ATOM   9090  C CA  . ILE C 1 113 ? -13.081 -4.822  48.874  1.00 78.66  ? 113 ILE C CA  1 
ATOM   9091  C C   . ILE C 1 113 ? -13.897 -3.977  49.845  1.00 73.29  ? 113 ILE C C   1 
ATOM   9092  O O   . ILE C 1 113 ? -14.197 -4.407  50.966  1.00 69.00  ? 113 ILE C O   1 
ATOM   9093  C CB  . ILE C 1 113 ? -11.573 -4.537  49.008  1.00 68.56  ? 113 ILE C CB  1 
ATOM   9094  C CG1 . ILE C 1 113 ? -10.788 -5.298  47.937  1.00 62.41  ? 113 ILE C CG1 1 
ATOM   9095  C CG2 . ILE C 1 113 ? -11.080 -4.900  50.401  1.00 58.40  ? 113 ILE C CG2 1 
ATOM   9096  C CD1 . ILE C 1 113 ? -9.291  -5.314  48.174  1.00 60.53  ? 113 ILE C CD1 1 
ATOM   9097  N N   . ARG C 1 114 ? -14.268 -2.763  49.432  1.00 65.02  ? 114 ARG C N   1 
ATOM   9098  C CA  . ARG C 1 114 ? -15.013 -1.867  50.310  1.00 64.34  ? 114 ARG C CA  1 
ATOM   9099  C C   . ARG C 1 114 ? -16.394 -2.417  50.649  1.00 72.62  ? 114 ARG C C   1 
ATOM   9100  O O   . ARG C 1 114 ? -16.906 -2.170  51.747  1.00 73.73  ? 114 ARG C O   1 
ATOM   9101  C CB  . ARG C 1 114 ? -15.134 -0.489  49.659  1.00 71.40  ? 114 ARG C CB  1 
ATOM   9102  C CG  . ARG C 1 114 ? -14.321 0.600   50.338  1.00 67.74  ? 114 ARG C CG  1 
ATOM   9103  C CD  . ARG C 1 114 ? -12.831 0.429   50.088  1.00 62.79  ? 114 ARG C CD  1 
ATOM   9104  N NE  . ARG C 1 114 ? -12.083 1.633   50.433  1.00 69.04  ? 114 ARG C NE  1 
ATOM   9105  C CZ  . ARG C 1 114 ? -11.684 2.546   49.558  1.00 74.28  ? 114 ARG C CZ  1 
ATOM   9106  N NH1 . ARG C 1 114 ? -11.936 2.422   48.265  1.00 69.28  ? 114 ARG C NH1 1 
ATOM   9107  N NH2 . ARG C 1 114 ? -11.016 3.611   49.991  1.00 75.11  ? 114 ARG C NH2 1 
ATOM   9108  N N   . GLU C 1 115 ? -17.009 -3.162  49.732  1.00 67.03  ? 115 GLU C N   1 
ATOM   9109  C CA  . GLU C 1 115 ? -18.370 -3.650  49.918  1.00 64.91  ? 115 GLU C CA  1 
ATOM   9110  C C   . GLU C 1 115 ? -18.441 -5.070  50.461  1.00 72.21  ? 115 GLU C C   1 
ATOM   9111  O O   . GLU C 1 115 ? -19.358 -5.379  51.228  1.00 81.25  ? 115 GLU C O   1 
ATOM   9112  C CB  . GLU C 1 115 ? -19.143 -3.582  48.599  1.00 79.02  ? 115 GLU C CB  1 
ATOM   9113  C CG  . GLU C 1 115 ? -18.345 -4.026  47.385  1.00 72.10  ? 115 GLU C CG  1 
ATOM   9114  C CD  . GLU C 1 115 ? -18.745 -3.283  46.127  1.00 87.35  ? 115 GLU C CD  1 
ATOM   9115  O OE1 . GLU C 1 115 ? -18.559 -2.049  46.082  1.00 88.48  ? 115 GLU C OE1 1 
ATOM   9116  O OE2 . GLU C 1 115 ? -19.253 -3.929  45.188  1.00 84.17  ? 115 GLU C OE2 1 
ATOM   9117  N N   . LEU C 1 116 ? -17.504 -5.942  50.079  1.00 73.63  ? 116 LEU C N   1 
ATOM   9118  C CA  . LEU C 1 116 ? -17.512 -7.311  50.588  1.00 78.58  ? 116 LEU C CA  1 
ATOM   9119  C C   . LEU C 1 116 ? -17.351 -7.349  52.100  1.00 73.46  ? 116 LEU C C   1 
ATOM   9120  O O   . LEU C 1 116 ? -17.844 -8.275  52.754  1.00 68.15  ? 116 LEU C O   1 
ATOM   9121  C CB  . LEU C 1 116 ? -16.403 -8.124  49.922  1.00 76.00  ? 116 LEU C CB  1 
ATOM   9122  C CG  . LEU C 1 116 ? -16.830 -9.224  48.949  1.00 70.15  ? 116 LEU C CG  1 
ATOM   9123  C CD1 . LEU C 1 116 ? -17.770 -8.666  47.901  1.00 64.77  ? 116 LEU C CD1 1 
ATOM   9124  C CD2 . LEU C 1 116 ? -15.605 -9.841  48.298  1.00 60.09  ? 116 LEU C CD2 1 
ATOM   9125  N N   . MET C 1 117 ? -16.670 -6.356  52.672  1.00 70.76  ? 117 MET C N   1 
ATOM   9126  C CA  . MET C 1 117 ? -16.438 -6.302  54.109  1.00 67.01  ? 117 MET C CA  1 
ATOM   9127  C C   . MET C 1 117 ? -17.661 -5.863  54.899  1.00 66.96  ? 117 MET C C   1 
ATOM   9128  O O   . MET C 1 117 ? -17.629 -5.919  56.134  1.00 69.52  ? 117 MET C O   1 
ATOM   9129  C CB  . MET C 1 117 ? -15.266 -5.370  54.415  1.00 71.67  ? 117 MET C CB  1 
ATOM   9130  C CG  . MET C 1 117 ? -13.946 -6.074  54.291  1.00 67.79  ? 117 MET C CG  1 
ATOM   9131  S SD  . MET C 1 117 ? -13.895 -7.382  55.524  1.00 85.00  ? 117 MET C SD  1 
ATOM   9132  C CE  . MET C 1 117 ? -12.502 -8.324  54.947  1.00 51.00  ? 117 MET C CE  1 
ATOM   9133  N N   . ASN C 1 118 ? -18.726 -5.430  54.229  1.00 69.85  ? 118 ASN C N   1 
ATOM   9134  C CA  . ASN C 1 118 ? -19.940 -5.010  54.916  1.00 77.52  ? 118 ASN C CA  1 
ATOM   9135  C C   . ASN C 1 118 ? -20.995 -6.105  54.993  1.00 69.35  ? 118 ASN C C   1 
ATOM   9136  O O   . ASN C 1 118 ? -21.784 -6.120  55.943  1.00 70.62  ? 118 ASN C O   1 
ATOM   9137  C CB  . ASN C 1 118 ? -20.530 -3.775  54.228  1.00 76.45  ? 118 ASN C CB  1 
ATOM   9138  C CG  . ASN C 1 118 ? -19.506 -2.669  54.045  1.00 83.99  ? 118 ASN C CG  1 
ATOM   9139  O OD1 . ASN C 1 118 ? -18.594 -2.511  54.857  1.00 76.83  ? 118 ASN C OD1 1 
ATOM   9140  N ND2 . ASN C 1 118 ? -19.649 -1.900  52.972  1.00 67.86  ? 118 ASN C ND2 1 
ATOM   9141  N N   . LYS C 1 119 ? -21.029 -7.016  54.024  1.00 74.74  ? 119 LYS C N   1 
ATOM   9142  C CA  . LYS C 1 119 ? -21.918 -8.166  54.113  1.00 71.41  ? 119 LYS C CA  1 
ATOM   9143  C C   . LYS C 1 119 ? -21.399 -9.144  55.159  1.00 75.78  ? 119 LYS C C   1 
ATOM   9144  O O   . LYS C 1 119 ? -20.195 -9.400  55.251  1.00 87.24  ? 119 LYS C O   1 
ATOM   9145  C CB  . LYS C 1 119 ? -22.035 -8.857  52.754  1.00 72.21  ? 119 LYS C CB  1 
ATOM   9146  C CG  . LYS C 1 119 ? -22.685 -8.004  51.676  1.00 74.18  ? 119 LYS C CG  1 
ATOM   9147  C CD  . LYS C 1 119 ? -21.671 -7.580  50.625  1.00 73.36  ? 119 LYS C CD  1 
ATOM   9148  C CE  . LYS C 1 119 ? -22.338 -7.302  49.287  1.00 74.47  ? 119 LYS C CE  1 
ATOM   9149  N NZ  . LYS C 1 119 ? -21.378 -7.420  48.153  1.00 72.82  ? 119 LYS C NZ  1 
ATOM   9150  N N   . GLU C 1 120 ? -22.318 -9.689  55.958  1.00 90.04  ? 120 GLU C N   1 
ATOM   9151  C CA  . GLU C 1 120 ? -21.921 -10.574 57.048  1.00 98.76  ? 120 GLU C CA  1 
ATOM   9152  C C   . GLU C 1 120 ? -21.589 -11.984 56.568  1.00 100.46 ? 120 GLU C C   1 
ATOM   9153  O O   . GLU C 1 120 ? -20.761 -12.662 57.190  1.00 100.75 ? 120 GLU C O   1 
ATOM   9154  C CB  . GLU C 1 120 ? -23.020 -10.618 58.112  1.00 88.83  ? 120 GLU C CB  1 
ATOM   9155  C CG  . GLU C 1 120 ? -23.259 -9.285  58.813  1.00 94.28  ? 120 GLU C CG  1 
ATOM   9156  C CD  . GLU C 1 120 ? -22.043 -8.795  59.582  1.00 93.43  ? 120 GLU C CD  1 
ATOM   9157  O OE1 . GLU C 1 120 ? -21.184 -8.119  58.977  1.00 88.80  ? 120 GLU C OE1 1 
ATOM   9158  O OE2 . GLU C 1 120 ? -21.944 -9.086  60.792  1.00 80.61  ? 120 GLU C OE2 1 
ATOM   9159  N N   . LYS C 1 121 ? -22.212 -12.440 55.481  1.00 98.90  ? 121 LYS C N   1 
ATOM   9160  C CA  . LYS C 1 121 ? -21.991 -13.774 54.942  1.00 90.79  ? 121 LYS C CA  1 
ATOM   9161  C C   . LYS C 1 121 ? -21.529 -13.645 53.494  1.00 88.42  ? 121 LYS C C   1 
ATOM   9162  O O   . LYS C 1 121 ? -21.957 -12.742 52.769  1.00 88.89  ? 121 LYS C O   1 
ATOM   9163  C CB  . LYS C 1 121 ? -23.283 -14.633 55.096  1.00 83.88  ? 121 LYS C CB  1 
ATOM   9164  C CG  . LYS C 1 121 ? -23.297 -16.093 54.560  1.00 83.14  ? 121 LYS C CG  1 
ATOM   9165  C CD  . LYS C 1 121 ? -23.131 -16.262 53.048  1.00 82.72  ? 121 LYS C CD  1 
ATOM   9166  C CE  . LYS C 1 121 ? -23.147 -17.717 52.643  1.00 83.77  ? 121 LYS C CE  1 
ATOM   9167  N NZ  . LYS C 1 121 ? -23.413 -17.842 51.193  1.00 79.25  ? 121 LYS C NZ  1 
ATOM   9168  N N   . LEU C 1 122 ? -20.627 -14.540 53.085  1.00 97.85  ? 122 LEU C N   1 
ATOM   9169  C CA  . LEU C 1 122 ? -20.072 -14.551 51.737  1.00 101.22 ? 122 LEU C CA  1 
ATOM   9170  C C   . LEU C 1 122 ? -20.369 -15.887 51.069  1.00 94.26  ? 122 LEU C C   1 
ATOM   9171  O O   . LEU C 1 122 ? -20.143 -16.945 51.665  1.00 90.37  ? 122 LEU C O   1 
ATOM   9172  C CB  . LEU C 1 122 ? -18.563 -14.300 51.765  1.00 87.71  ? 122 LEU C CB  1 
ATOM   9173  C CG  . LEU C 1 122 ? -18.151 -12.831 51.758  1.00 82.77  ? 122 LEU C CG  1 
ATOM   9174  C CD1 . LEU C 1 122 ? -18.143 -12.283 53.173  1.00 78.33  ? 122 LEU C CD1 1 
ATOM   9175  C CD2 . LEU C 1 122 ? -16.793 -12.668 51.106  1.00 80.96  ? 122 LEU C CD2 1 
ATOM   9176  N N   . ASN C 1 123 ? -20.879 -15.835 49.839  1.00 92.16  ? 123 ASN C N   1 
ATOM   9177  C CA  . ASN C 1 123 ? -21.098 -17.031 49.039  1.00 79.38  ? 123 ASN C CA  1 
ATOM   9178  C C   . ASN C 1 123 ? -19.866 -17.305 48.175  1.00 79.63  ? 123 ASN C C   1 
ATOM   9179  O O   . ASN C 1 123 ? -18.821 -16.667 48.325  1.00 79.27  ? 123 ASN C O   1 
ATOM   9180  C CB  . ASN C 1 123 ? -22.363 -16.891 48.195  1.00 79.69  ? 123 ASN C CB  1 
ATOM   9181  C CG  . ASN C 1 123 ? -22.608 -15.467 47.730  1.00 78.31  ? 123 ASN C CG  1 
ATOM   9182  O OD1 . ASN C 1 123 ? -21.694 -14.784 47.264  1.00 75.99  ? 123 ASN C OD1 1 
ATOM   9183  N ND2 . ASN C 1 123 ? -23.850 -15.017 47.845  1.00 81.46  ? 123 ASN C ND2 1 
ATOM   9184  N N   . ARG C 1 124 ? -19.979 -18.267 47.255  1.00 79.77  ? 124 ARG C N   1 
ATOM   9185  C CA  . ARG C 1 124 ? -18.825 -18.643 46.444  1.00 74.88  ? 124 ARG C CA  1 
ATOM   9186  C C   . ARG C 1 124 ? -18.383 -17.507 45.530  1.00 78.39  ? 124 ARG C C   1 
ATOM   9187  O O   . ARG C 1 124 ? -17.183 -17.232 45.412  1.00 75.78  ? 124 ARG C O   1 
ATOM   9188  C CB  . ARG C 1 124 ? -19.132 -19.894 45.622  1.00 75.18  ? 124 ARG C CB  1 
ATOM   9189  C CG  . ARG C 1 124 ? -17.878 -20.620 45.178  1.00 72.13  ? 124 ARG C CG  1 
ATOM   9190  C CD  . ARG C 1 124 ? -18.038 -21.272 43.818  1.00 75.90  ? 124 ARG C CD  1 
ATOM   9191  N NE  . ARG C 1 124 ? -16.739 -21.615 43.252  1.00 72.40  ? 124 ARG C NE  1 
ATOM   9192  C CZ  . ARG C 1 124 ? -16.153 -20.956 42.262  1.00 73.53  ? 124 ARG C CZ  1 
ATOM   9193  N NH1 . ARG C 1 124 ? -16.745 -19.933 41.666  1.00 72.58  ? 124 ARG C NH1 1 
ATOM   9194  N NH2 . ARG C 1 124 ? -14.942 -21.331 41.860  1.00 75.23  ? 124 ARG C NH2 1 
ATOM   9195  N N   . GLU C 1 125 ? -19.332 -16.835 44.876  1.00 81.32  ? 125 GLU C N   1 
ATOM   9196  C CA  . GLU C 1 125 ? -18.963 -15.770 43.951  1.00 79.50  ? 125 GLU C CA  1 
ATOM   9197  C C   . GLU C 1 125 ? -18.403 -14.556 44.682  1.00 72.09  ? 125 GLU C C   1 
ATOM   9198  O O   . GLU C 1 125 ? -17.610 -13.801 44.107  1.00 68.69  ? 125 GLU C O   1 
ATOM   9199  C CB  . GLU C 1 125 ? -20.165 -15.378 43.091  1.00 86.63  ? 125 GLU C CB  1 
ATOM   9200  C CG  . GLU C 1 125 ? -21.446 -15.109 43.861  1.00 93.56  ? 125 GLU C CG  1 
ATOM   9201  C CD  . GLU C 1 125 ? -21.891 -13.663 43.762  1.00 94.81  ? 125 GLU C CD  1 
ATOM   9202  O OE1 . GLU C 1 125 ? -21.266 -12.898 42.996  1.00 98.16  ? 125 GLU C OE1 1 
ATOM   9203  O OE2 . GLU C 1 125 ? -22.875 -13.295 44.438  1.00 81.89  ? 125 GLU C OE2 1 
ATOM   9204  N N   . GLU C 1 126 ? -18.804 -14.346 45.938  1.00 75.09  ? 126 GLU C N   1 
ATOM   9205  C CA  . GLU C 1 126 ? -18.217 -13.271 46.730  1.00 67.70  ? 126 GLU C CA  1 
ATOM   9206  C C   . GLU C 1 126 ? -16.817 -13.630 47.216  1.00 64.42  ? 126 GLU C C   1 
ATOM   9207  O O   . GLU C 1 126 ? -15.913 -12.789 47.179  1.00 71.57  ? 126 GLU C O   1 
ATOM   9208  C CB  . GLU C 1 126 ? -19.124 -12.930 47.915  1.00 71.10  ? 126 GLU C CB  1 
ATOM   9209  C CG  . GLU C 1 126 ? -19.918 -11.646 47.727  1.00 87.76  ? 126 GLU C CG  1 
ATOM   9210  C CD  . GLU C 1 126 ? -21.323 -11.727 48.298  1.00 86.08  ? 126 GLU C CD  1 
ATOM   9211  O OE1 . GLU C 1 126 ? -21.588 -12.638 49.111  1.00 73.71  ? 126 GLU C OE1 1 
ATOM   9212  O OE2 . GLU C 1 126 ? -22.163 -10.877 47.932  1.00 75.39  ? 126 GLU C OE2 1 
ATOM   9213  N N   . LEU C 1 127 ? -16.618 -14.873 47.667  1.00 64.18  ? 127 LEU C N   1 
ATOM   9214  C CA  . LEU C 1 127 ? -15.328 -15.263 48.233  1.00 66.00  ? 127 LEU C CA  1 
ATOM   9215  C C   . LEU C 1 127 ? -14.206 -15.191 47.207  1.00 64.45  ? 127 LEU C C   1 
ATOM   9216  O O   . LEU C 1 127 ? -13.054 -14.923 47.567  1.00 65.61  ? 127 LEU C O   1 
ATOM   9217  C CB  . LEU C 1 127 ? -15.408 -16.675 48.814  1.00 65.97  ? 127 LEU C CB  1 
ATOM   9218  C CG  . LEU C 1 127 ? -16.185 -16.858 50.118  1.00 69.64  ? 127 LEU C CG  1 
ATOM   9219  C CD1 . LEU C 1 127 ? -16.413 -18.336 50.397  1.00 78.20  ? 127 LEU C CD1 1 
ATOM   9220  C CD2 . LEU C 1 127 ? -15.456 -16.195 51.275  1.00 60.24  ? 127 LEU C CD2 1 
ATOM   9221  N N   . LEU C 1 128 ? -14.515 -15.437 45.933  1.00 69.23  ? 128 LEU C N   1 
ATOM   9222  C CA  . LEU C 1 128 ? -13.473 -15.444 44.913  1.00 63.89  ? 128 LEU C CA  1 
ATOM   9223  C C   . LEU C 1 128 ? -12.838 -14.067 44.764  1.00 58.84  ? 128 LEU C C   1 
ATOM   9224  O O   . LEU C 1 128 ? -11.626 -13.954 44.547  1.00 56.32  ? 128 LEU C O   1 
ATOM   9225  C CB  . LEU C 1 128 ? -14.060 -15.934 43.587  1.00 62.72  ? 128 LEU C CB  1 
ATOM   9226  C CG  . LEU C 1 128 ? -13.577 -17.329 43.181  1.00 62.90  ? 128 LEU C CG  1 
ATOM   9227  C CD1 . LEU C 1 128 ? -13.766 -17.573 41.707  1.00 64.88  ? 128 LEU C CD1 1 
ATOM   9228  C CD2 . LEU C 1 128 ? -12.122 -17.509 43.557  1.00 59.88  ? 128 LEU C CD2 1 
ATOM   9229  N N   . ASP C 1 129 ? -13.640 -13.008 44.883  1.00 60.19  ? 129 ASP C N   1 
ATOM   9230  C CA  . ASP C 1 129 ? -13.085 -11.660 44.870  1.00 57.98  ? 129 ASP C CA  1 
ATOM   9231  C C   . ASP C 1 129 ? -12.287 -11.382 46.138  1.00 55.39  ? 129 ASP C C   1 
ATOM   9232  O O   . ASP C 1 129 ? -11.222 -10.760 46.082  1.00 53.31  ? 129 ASP C O   1 
ATOM   9233  C CB  . ASP C 1 129 ? -14.204 -10.637 44.692  1.00 65.80  ? 129 ASP C CB  1 
ATOM   9234  C CG  . ASP C 1 129 ? -15.108 -10.965 43.521  1.00 74.80  ? 129 ASP C CG  1 
ATOM   9235  O OD1 . ASP C 1 129 ? -15.270 -12.164 43.211  1.00 78.85  ? 129 ASP C OD1 1 
ATOM   9236  O OD2 . ASP C 1 129 ? -15.644 -10.024 42.900  1.00 77.46  ? 129 ASP C OD2 1 
ATOM   9237  N N   . LEU C 1 130 ? -12.781 -11.846 47.289  1.00 59.24  ? 130 LEU C N   1 
ATOM   9238  C CA  . LEU C 1 130 ? -12.025 -11.696 48.529  1.00 53.38  ? 130 LEU C CA  1 
ATOM   9239  C C   . LEU C 1 130 ? -10.688 -12.420 48.445  1.00 51.23  ? 130 LEU C C   1 
ATOM   9240  O O   . LEU C 1 130 ? -9.672  -11.930 48.950  1.00 49.39  ? 130 LEU C O   1 
ATOM   9241  C CB  . LEU C 1 130 ? -12.843 -12.220 49.710  1.00 54.38  ? 130 LEU C CB  1 
ATOM   9242  C CG  . LEU C 1 130 ? -12.513 -11.676 51.102  1.00 52.91  ? 130 LEU C CG  1 
ATOM   9243  C CD1 . LEU C 1 130 ? -12.898 -10.209 51.225  1.00 53.24  ? 130 LEU C CD1 1 
ATOM   9244  C CD2 . LEU C 1 130 ? -13.199 -12.507 52.178  1.00 56.70  ? 130 LEU C CD2 1 
ATOM   9245  N N   . GLN C 1 131 ? -10.674 -13.596 47.813  1.00 52.01  ? 131 GLN C N   1 
ATOM   9246  C CA  . GLN C 1 131 ? -9.428  -14.333 47.636  1.00 53.70  ? 131 GLN C CA  1 
ATOM   9247  C C   . GLN C 1 131 ? -8.511  -13.644 46.632  1.00 49.16  ? 131 GLN C C   1 
ATOM   9248  O O   . GLN C 1 131 ? -7.303  -13.521 46.866  1.00 47.01  ? 131 GLN C O   1 
ATOM   9249  C CB  . GLN C 1 131 ? -9.734  -15.763 47.189  1.00 56.34  ? 131 GLN C CB  1 
ATOM   9250  C CG  . GLN C 1 131 ? -9.865  -16.759 48.328  1.00 51.70  ? 131 GLN C CG  1 
ATOM   9251  C CD  . GLN C 1 131 ? -10.235 -18.148 47.846  1.00 55.99  ? 131 GLN C CD  1 
ATOM   9252  O OE1 . GLN C 1 131 ? -10.635 -18.335 46.697  1.00 62.44  ? 131 GLN C OE1 1 
ATOM   9253  N NE2 . GLN C 1 131 ? -10.103 -19.134 48.726  1.00 66.60  ? 131 GLN C NE2 1 
ATOM   9254  N N   . THR C 1 132 ? -9.068  -13.181 45.509  1.00 54.09  ? 132 THR C N   1 
ATOM   9255  C CA  . THR C 1 132 ? -8.244  -12.648 44.427  1.00 52.92  ? 132 THR C CA  1 
ATOM   9256  C C   . THR C 1 132 ? -7.814  -11.207 44.679  1.00 50.85  ? 132 THR C C   1 
ATOM   9257  O O   . THR C 1 132 ? -6.664  -10.848 44.403  1.00 52.70  ? 132 THR C O   1 
ATOM   9258  C CB  . THR C 1 132 ? -8.990  -12.743 43.096  1.00 56.45  ? 132 THR C CB  1 
ATOM   9259  O OG1 . THR C 1 132 ? -9.727  -13.972 43.044  1.00 54.29  ? 132 THR C OG1 1 
ATOM   9260  C CG2 . THR C 1 132 ? -8.012  -12.678 41.930  1.00 51.97  ? 132 THR C CG2 1 
ATOM   9261  N N   . LEU C 1 133 ? -8.720  -10.363 45.181  1.00 49.56  ? 133 LEU C N   1 
ATOM   9262  C CA  . LEU C 1 133 ? -8.368  -8.962  45.391  1.00 48.53  ? 133 LEU C CA  1 
ATOM   9263  C C   . LEU C 1 133 ? -7.260  -8.813  46.423  1.00 49.82  ? 133 LEU C C   1 
ATOM   9264  O O   . LEU C 1 133 ? -6.471  -7.864  46.355  1.00 49.99  ? 133 LEU C O   1 
ATOM   9265  C CB  . LEU C 1 133 ? -9.600  -8.165  45.806  1.00 50.16  ? 133 LEU C CB  1 
ATOM   9266  C CG  . LEU C 1 133 ? -10.544 -7.854  44.649  1.00 52.66  ? 133 LEU C CG  1 
ATOM   9267  C CD1 . LEU C 1 133 ? -11.885 -7.427  45.185  1.00 58.65  ? 133 LEU C CD1 1 
ATOM   9268  C CD2 . LEU C 1 133 ? -9.954  -6.783  43.745  1.00 52.26  ? 133 LEU C CD2 1 
ATOM   9269  N N   . ASN C 1 134 ? -7.191  -9.730  47.390  1.00 46.77  ? 134 ASN C N   1 
ATOM   9270  C CA  . ASN C 1 134 ? -6.035  -9.774  48.277  1.00 47.33  ? 134 ASN C CA  1 
ATOM   9271  C C   . ASN C 1 134 ? -4.767  -10.088 47.494  1.00 47.84  ? 134 ASN C C   1 
ATOM   9272  O O   . ASN C 1 134 ? -3.711  -9.494  47.742  1.00 49.04  ? 134 ASN C O   1 
ATOM   9273  C CB  . ASN C 1 134 ? -6.259  -10.808 49.380  1.00 45.69  ? 134 ASN C CB  1 
ATOM   9274  C CG  . ASN C 1 134 ? -7.215  -10.322 50.449  1.00 43.83  ? 134 ASN C CG  1 
ATOM   9275  O OD1 . ASN C 1 134 ? -7.883  -9.302  50.282  1.00 48.95  ? 134 ASN C OD1 1 
ATOM   9276  N ND2 . ASN C 1 134 ? -7.291  -11.055 51.555  1.00 43.62  ? 134 ASN C ND2 1 
ATOM   9277  N N   . LEU C 1 135 ? -4.855  -11.020 46.542  1.00 45.29  ? 135 LEU C N   1 
ATOM   9278  C CA  . LEU C 1 135 ? -3.698  -11.371 45.724  1.00 43.33  ? 135 LEU C CA  1 
ATOM   9279  C C   . LEU C 1 135 ? -3.234  -10.187 44.882  1.00 41.55  ? 135 LEU C C   1 
ATOM   9280  O O   . LEU C 1 135 ? -2.042  -9.863  44.850  1.00 39.96  ? 135 LEU C O   1 
ATOM   9281  C CB  . LEU C 1 135 ? -4.035  -12.559 44.821  1.00 50.74  ? 135 LEU C CB  1 
ATOM   9282  C CG  . LEU C 1 135 ? -3.524  -13.950 45.191  1.00 42.94  ? 135 LEU C CG  1 
ATOM   9283  C CD1 . LEU C 1 135 ? -4.230  -14.988 44.341  1.00 45.05  ? 135 LEU C CD1 1 
ATOM   9284  C CD2 . LEU C 1 135 ? -2.024  -14.045 45.004  1.00 46.44  ? 135 LEU C CD2 1 
ATOM   9285  N N   . LEU C 1 136 ? -4.168  -9.529  44.190  1.00 43.23  ? 136 LEU C N   1 
ATOM   9286  C CA  . LEU C 1 136 ? -3.808  -8.424  43.309  1.00 43.26  ? 136 LEU C CA  1 
ATOM   9287  C C   . LEU C 1 136 ? -3.344  -7.193  44.076  1.00 46.04  ? 136 LEU C C   1 
ATOM   9288  O O   . LEU C 1 136 ? -2.713  -6.311  43.482  1.00 41.40  ? 136 LEU C O   1 
ATOM   9289  C CB  . LEU C 1 136 ? -4.991  -8.047  42.412  1.00 49.72  ? 136 LEU C CB  1 
ATOM   9290  C CG  . LEU C 1 136 ? -5.786  -9.161  41.728  1.00 52.77  ? 136 LEU C CG  1 
ATOM   9291  C CD1 . LEU C 1 136 ? -7.212  -8.700  41.457  1.00 50.81  ? 136 LEU C CD1 1 
ATOM   9292  C CD2 . LEU C 1 136 ? -5.111  -9.602  40.438  1.00 48.07  ? 136 LEU C CD2 1 
ATOM   9293  N N   . ALA C 1 137 ? -3.643  -7.111  45.375  1.00 45.96  ? 137 ALA C N   1 
ATOM   9294  C CA  . ALA C 1 137 ? -3.296  -5.921  46.146  1.00 41.63  ? 137 ALA C CA  1 
ATOM   9295  C C   . ALA C 1 137 ? -1.787  -5.730  46.230  1.00 39.81  ? 137 ALA C C   1 
ATOM   9296  O O   . ALA C 1 137 ? -1.294  -4.596  46.199  1.00 46.78  ? 137 ALA C O   1 
ATOM   9297  C CB  . ALA C 1 137 ? -3.905  -6.008  47.544  1.00 48.74  ? 137 ALA C CB  1 
ATOM   9298  N N   . TRP C 1 138 ? -1.035  -6.826  46.334  1.00 43.81  ? 138 TRP C N   1 
ATOM   9299  C CA  . TRP C 1 138 ? 0.415   -6.783  46.480  1.00 44.80  ? 138 TRP C CA  1 
ATOM   9300  C C   . TRP C 1 138 ? 1.137   -6.958  45.148  1.00 49.59  ? 138 TRP C C   1 
ATOM   9301  O O   . TRP C 1 138 ? 2.232   -7.530  45.108  1.00 49.08  ? 138 TRP C O   1 
ATOM   9302  C CB  . TRP C 1 138 ? 0.878   -7.846  47.477  1.00 42.33  ? 138 TRP C CB  1 
ATOM   9303  C CG  . TRP C 1 138 ? 0.166   -7.788  48.795  1.00 49.80  ? 138 TRP C CG  1 
ATOM   9304  C CD1 . TRP C 1 138 ? -1.094  -8.236  49.067  1.00 53.60  ? 138 TRP C CD1 1 
ATOM   9305  C CD2 . TRP C 1 138 ? 0.671   -7.247  50.021  1.00 47.90  ? 138 TRP C CD2 1 
ATOM   9306  N NE1 . TRP C 1 138 ? -1.403  -8.010  50.385  1.00 56.52  ? 138 TRP C NE1 1 
ATOM   9307  C CE2 . TRP C 1 138 ? -0.336  -7.402  50.993  1.00 54.76  ? 138 TRP C CE2 1 
ATOM   9308  C CE3 . TRP C 1 138 ? 1.878   -6.650  50.392  1.00 46.87  ? 138 TRP C CE3 1 
ATOM   9309  C CZ2 . TRP C 1 138 ? -0.174  -6.978  52.310  1.00 50.21  ? 138 TRP C CZ2 1 
ATOM   9310  C CZ3 . TRP C 1 138 ? 2.036   -6.227  51.698  1.00 52.26  ? 138 TRP C CZ3 1 
ATOM   9311  C CH2 . TRP C 1 138 ? 1.017   -6.393  52.642  1.00 47.94  ? 138 TRP C CH2 1 
ATOM   9312  N N   . CYS C 1 139 ? 0.545   -6.481  44.056  1.00 39.11  ? 139 CYS C N   1 
ATOM   9313  C CA  . CYS C 1 139 ? 1.144   -6.642  42.738  1.00 40.72  ? 139 CYS C CA  1 
ATOM   9314  C C   . CYS C 1 139 ? 2.236   -5.599  42.530  1.00 42.56  ? 139 CYS C C   1 
ATOM   9315  O O   . CYS C 1 139 ? 2.018   -4.406  42.759  1.00 47.76  ? 139 CYS C O   1 
ATOM   9316  C CB  . CYS C 1 139 ? 0.075   -6.528  41.653  1.00 47.65  ? 139 CYS C CB  1 
ATOM   9317  S SG  . CYS C 1 139 ? 0.541   -7.245  40.063  1.00 59.01  ? 139 CYS C SG  1 
ATOM   9318  N N   . GLY C 1 140 ? 3.407   -6.054  42.092  1.00 45.22  ? 140 GLY C N   1 
ATOM   9319  C CA  . GLY C 1 140 ? 4.564   -5.196  41.951  1.00 41.81  ? 140 GLY C CA  1 
ATOM   9320  C C   . GLY C 1 140 ? 4.556   -4.398  40.660  1.00 51.91  ? 140 GLY C C   1 
ATOM   9321  O O   . GLY C 1 140 ? 3.617   -4.434  39.864  1.00 56.95  ? 140 GLY C O   1 
ATOM   9322  N N   . ARG C 1 141 ? 5.654   -3.665  40.455  1.00 47.27  ? 141 ARG C N   1 
ATOM   9323  C CA  . ARG C 1 141 ? 5.747   -2.762  39.311  1.00 47.53  ? 141 ARG C CA  1 
ATOM   9324  C C   . ARG C 1 141 ? 5.686   -3.516  37.988  1.00 40.94  ? 141 ARG C C   1 
ATOM   9325  O O   . ARG C 1 141 ? 5.023   -3.072  37.044  1.00 40.54  ? 141 ARG C O   1 
ATOM   9326  C CB  . ARG C 1 141 ? 7.035   -1.941  39.399  1.00 40.86  ? 141 ARG C CB  1 
ATOM   9327  C CG  . ARG C 1 141 ? 6.994   -0.640  38.616  1.00 40.97  ? 141 ARG C CG  1 
ATOM   9328  C CD  . ARG C 1 141 ? 8.352   0.038   38.591  1.00 35.50  ? 141 ARG C CD  1 
ATOM   9329  N NE  . ARG C 1 141 ? 9.246   -0.587  37.625  1.00 35.86  ? 141 ARG C NE  1 
ATOM   9330  C CZ  . ARG C 1 141 ? 9.923   0.073   36.695  1.00 43.57  ? 141 ARG C CZ  1 
ATOM   9331  N NH1 . ARG C 1 141 ? 9.843   1.389   36.585  1.00 51.92  ? 141 ARG C NH1 1 
ATOM   9332  N NH2 . ARG C 1 141 ? 10.700  -0.603  35.855  1.00 47.44  ? 141 ARG C NH2 1 
ATOM   9333  N N   . THR C 1 142 ? 6.374   -4.656  37.899  1.00 48.62  ? 142 THR C N   1 
ATOM   9334  C CA  . THR C 1 142 ? 6.457   -5.379  36.633  1.00 52.17  ? 142 THR C CA  1 
ATOM   9335  C C   . THR C 1 142 ? 5.149   -6.088  36.297  1.00 52.05  ? 142 THR C C   1 
ATOM   9336  O O   . THR C 1 142 ? 4.686   -6.031  35.152  1.00 58.44  ? 142 THR C O   1 
ATOM   9337  C CB  . THR C 1 142 ? 7.620   -6.374  36.676  1.00 56.77  ? 142 THR C CB  1 
ATOM   9338  O OG1 . THR C 1 142 ? 8.820   -5.724  36.240  1.00 59.08  ? 142 THR C OG1 1 
ATOM   9339  C CG2 . THR C 1 142 ? 7.352   -7.572  35.774  1.00 56.32  ? 142 THR C CG2 1 
ATOM   9340  N N   . LEU C 1 143 ? 4.534   -6.750  37.277  1.00 49.97  ? 143 LEU C N   1 
ATOM   9341  C CA  . LEU C 1 143 ? 3.302   -7.483  37.017  1.00 58.17  ? 143 LEU C CA  1 
ATOM   9342  C C   . LEU C 1 143 ? 2.084   -6.574  36.916  1.00 57.74  ? 143 LEU C C   1 
ATOM   9343  O O   . LEU C 1 143 ? 1.058   -6.999  36.373  1.00 53.89  ? 143 LEU C O   1 
ATOM   9344  C CB  . LEU C 1 143 ? 3.086   -8.540  38.100  1.00 58.39  ? 143 LEU C CB  1 
ATOM   9345  C CG  . LEU C 1 143 ? 4.088   -9.693  38.054  1.00 58.76  ? 143 LEU C CG  1 
ATOM   9346  C CD1 . LEU C 1 143 ? 3.889   -10.615 39.234  1.00 53.57  ? 143 LEU C CD1 1 
ATOM   9347  C CD2 . LEU C 1 143 ? 3.964   -10.462 36.746  1.00 51.08  ? 143 LEU C CD2 1 
ATOM   9348  N N   . ARG C 1 144 ? 2.167   -5.343  37.427  1.00 59.33  ? 144 ARG C N   1 
ATOM   9349  C CA  . ARG C 1 144 ? 1.111   -4.371  37.164  1.00 55.01  ? 144 ARG C CA  1 
ATOM   9350  C C   . ARG C 1 144 ? 1.025   -4.055  35.677  1.00 54.92  ? 144 ARG C C   1 
ATOM   9351  O O   . ARG C 1 144 ? -0.072  -3.941  35.120  1.00 63.16  ? 144 ARG C O   1 
ATOM   9352  C CB  . ARG C 1 144 ? 1.350   -3.094  37.970  1.00 56.82  ? 144 ARG C CB  1 
ATOM   9353  C CG  . ARG C 1 144 ? 0.717   -3.085  39.351  1.00 59.65  ? 144 ARG C CG  1 
ATOM   9354  C CD  . ARG C 1 144 ? 1.499   -2.176  40.283  1.00 62.97  ? 144 ARG C CD  1 
ATOM   9355  N NE  . ARG C 1 144 ? 0.967   -2.161  41.641  1.00 60.73  ? 144 ARG C NE  1 
ATOM   9356  C CZ  . ARG C 1 144 ? 0.185   -1.208  42.130  1.00 52.78  ? 144 ARG C CZ  1 
ATOM   9357  N NH1 . ARG C 1 144 ? -0.188  -0.173  41.393  1.00 40.79  ? 144 ARG C NH1 1 
ATOM   9358  N NH2 . ARG C 1 144 ? -0.231  -1.295  43.392  1.00 54.72  ? 144 ARG C NH2 1 
ATOM   9359  N N   . LYS C 1 145 ? 2.178   -3.911  35.019  1.00 51.58  ? 145 LYS C N   1 
ATOM   9360  C CA  . LYS C 1 145 ? 2.206   -3.703  33.577  1.00 48.07  ? 145 LYS C CA  1 
ATOM   9361  C C   . LYS C 1 145 ? 1.798   -4.954  32.807  1.00 59.70  ? 145 LYS C C   1 
ATOM   9362  O O   . LYS C 1 145 ? 1.502   -4.861  31.611  1.00 67.59  ? 145 LYS C O   1 
ATOM   9363  C CB  . LYS C 1 145 ? 3.603   -3.260  33.140  1.00 45.69  ? 145 LYS C CB  1 
ATOM   9364  C CG  . LYS C 1 145 ? 3.947   -1.822  33.498  1.00 44.94  ? 145 LYS C CG  1 
ATOM   9365  C CD  . LYS C 1 145 ? 5.371   -1.711  34.026  1.00 55.98  ? 145 LYS C CD  1 
ATOM   9366  C CE  . LYS C 1 145 ? 6.387   -1.662  32.892  1.00 67.22  ? 145 LYS C CE  1 
ATOM   9367  N NZ  . LYS C 1 145 ? 7.785   -1.581  33.405  1.00 62.20  ? 145 LYS C NZ  1 
ATOM   9368  N N   . ASP C 1 146 ? 1.773   -6.113  33.464  1.00 64.15  ? 146 ASP C N   1 
ATOM   9369  C CA  . ASP C 1 146 ? 1.457   -7.387  32.829  1.00 63.35  ? 146 ASP C CA  1 
ATOM   9370  C C   . ASP C 1 146 ? 0.000   -7.794  33.016  1.00 50.15  ? 146 ASP C C   1 
ATOM   9371  O O   . ASP C 1 146 ? -0.659  -8.202  32.055  1.00 52.44  ? 146 ASP C O   1 
ATOM   9372  C CB  . ASP C 1 146 ? 2.379   -8.483  33.378  1.00 73.74  ? 146 ASP C CB  1 
ATOM   9373  C CG  . ASP C 1 146 ? 3.509   -8.827  32.426  1.00 79.63  ? 146 ASP C CG  1 
ATOM   9374  O OD1 . ASP C 1 146 ? 4.028   -7.909  31.758  1.00 81.69  ? 146 ASP C OD1 1 
ATOM   9375  O OD2 . ASP C 1 146 ? 3.877   -10.019 32.347  1.00 86.18  ? 146 ASP C OD2 1 
ATOM   9376  N N   . LEU C 1 147 ? -0.519  -7.689  34.237  1.00 54.16  ? 147 LEU C N   1 
ATOM   9377  C CA  . LEU C 1 147 ? -1.897  -8.060  34.555  1.00 58.91  ? 147 LEU C CA  1 
ATOM   9378  C C   . LEU C 1 147 ? -2.808  -6.841  34.610  1.00 60.75  ? 147 LEU C C   1 
ATOM   9379  O O   . LEU C 1 147 ? -3.708  -6.766  35.451  1.00 59.62  ? 147 LEU C O   1 
ATOM   9380  C CB  . LEU C 1 147 ? -1.949  -8.829  35.874  1.00 60.96  ? 147 LEU C CB  1 
ATOM   9381  C CG  . LEU C 1 147 ? -0.809  -9.806  36.165  1.00 62.63  ? 147 LEU C CG  1 
ATOM   9382  C CD1 . LEU C 1 147 ? -0.671  -10.031 37.663  1.00 58.14  ? 147 LEU C CD1 1 
ATOM   9383  C CD2 . LEU C 1 147 ? -1.030  -11.125 35.438  1.00 49.70  ? 147 LEU C CD2 1 
ATOM   9384  N N   . LYS C 1 148 ? -2.580  -5.869  33.724  1.00 62.86  ? 148 LYS C N   1 
ATOM   9385  C CA  . LYS C 1 148 ? -3.310  -4.606  33.787  1.00 61.30  ? 148 LYS C CA  1 
ATOM   9386  C C   . LYS C 1 148 ? -4.811  -4.813  33.603  1.00 56.63  ? 148 LYS C C   1 
ATOM   9387  O O   . LYS C 1 148 ? -5.620  -4.273  34.366  1.00 62.69  ? 148 LYS C O   1 
ATOM   9388  C CB  . LYS C 1 148 ? -2.767  -3.637  32.734  1.00 62.64  ? 148 LYS C CB  1 
ATOM   9389  C CG  . LYS C 1 148 ? -3.260  -2.202  32.876  1.00 60.53  ? 148 LYS C CG  1 
ATOM   9390  C CD  . LYS C 1 148 ? -3.387  -1.786  34.336  1.00 67.73  ? 148 LYS C CD  1 
ATOM   9391  C CE  . LYS C 1 148 ? -2.039  -1.465  34.957  1.00 57.52  ? 148 LYS C CE  1 
ATOM   9392  N NZ  . LYS C 1 148 ? -2.197  -0.905  36.327  1.00 64.86  ? 148 LYS C NZ  1 
ATOM   9393  N N   . ASP C 1 149 ? -5.203  -5.598  32.596  1.00 60.34  ? 149 ASP C N   1 
ATOM   9394  C CA  . ASP C 1 149 ? -6.627  -5.807  32.342  1.00 66.48  ? 149 ASP C CA  1 
ATOM   9395  C C   . ASP C 1 149 ? -7.305  -6.522  33.503  1.00 59.44  ? 149 ASP C C   1 
ATOM   9396  O O   . ASP C 1 149 ? -8.477  -6.258  33.795  1.00 60.93  ? 149 ASP C O   1 
ATOM   9397  C CB  . ASP C 1 149 ? -6.824  -6.586  31.042  1.00 63.52  ? 149 ASP C CB  1 
ATOM   9398  C CG  . ASP C 1 149 ? -7.172  -5.686  29.871  1.00 82.90  ? 149 ASP C CG  1 
ATOM   9399  O OD1 . ASP C 1 149 ? -8.265  -5.081  29.886  1.00 92.95  ? 149 ASP C OD1 1 
ATOM   9400  O OD2 . ASP C 1 149 ? -6.351  -5.580  28.935  1.00 86.33  ? 149 ASP C OD2 1 
ATOM   9401  N N   . LEU C 1 150 ? -6.592  -7.434  34.167  1.00 57.50  ? 150 LEU C N   1 
ATOM   9402  C CA  . LEU C 1 150 ? -7.140  -8.084  35.352  1.00 56.87  ? 150 LEU C CA  1 
ATOM   9403  C C   . LEU C 1 150 ? -7.293  -7.095  36.503  1.00 58.12  ? 150 LEU C C   1 
ATOM   9404  O O   . LEU C 1 150 ? -8.267  -7.162  37.261  1.00 56.13  ? 150 LEU C O   1 
ATOM   9405  C CB  . LEU C 1 150 ? -6.252  -9.259  35.764  1.00 57.20  ? 150 LEU C CB  1 
ATOM   9406  C CG  . LEU C 1 150 ? -6.223  -10.475 34.833  1.00 56.73  ? 150 LEU C CG  1 
ATOM   9407  C CD1 . LEU C 1 150 ? -5.188  -10.303 33.727  1.00 56.66  ? 150 LEU C CD1 1 
ATOM   9408  C CD2 . LEU C 1 150 ? -5.955  -11.749 35.620  1.00 55.68  ? 150 LEU C CD2 1 
ATOM   9409  N N   . LEU C 1 151 ? -6.331  -6.178  36.657  1.00 58.43  ? 151 LEU C N   1 
ATOM   9410  C CA  . LEU C 1 151 ? -6.432  -5.162  37.702  1.00 52.47  ? 151 LEU C CA  1 
ATOM   9411  C C   . LEU C 1 151 ? -7.572  -4.188  37.425  1.00 60.55  ? 151 LEU C C   1 
ATOM   9412  O O   . LEU C 1 151 ? -8.322  -3.827  38.340  1.00 56.34  ? 151 LEU C O   1 
ATOM   9413  C CB  . LEU C 1 151 ? -5.110  -4.406  37.838  1.00 50.30  ? 151 LEU C CB  1 
ATOM   9414  C CG  . LEU C 1 151 ? -3.973  -5.077  38.614  1.00 56.57  ? 151 LEU C CG  1 
ATOM   9415  C CD1 . LEU C 1 151 ? -2.649  -4.890  37.888  1.00 49.59  ? 151 LEU C CD1 1 
ATOM   9416  C CD2 . LEU C 1 151 ? -3.891  -4.528  40.029  1.00 50.78  ? 151 LEU C CD2 1 
ATOM   9417  N N   . ASN C 1 152 ? -7.715  -3.748  36.169  1.00 57.76  ? 152 ASN C N   1 
ATOM   9418  C CA  . ASN C 1 152 ? -8.801  -2.839  35.812  1.00 66.10  ? 152 ASN C CA  1 
ATOM   9419  C C   . ASN C 1 152 ? -10.169 -3.486  35.948  1.00 72.62  ? 152 ASN C C   1 
ATOM   9420  O O   . ASN C 1 152 ? -11.167 -2.770  36.079  1.00 62.54  ? 152 ASN C O   1 
ATOM   9421  C CB  . ASN C 1 152 ? -8.627  -2.333  34.381  1.00 61.42  ? 152 ASN C CB  1 
ATOM   9422  C CG  . ASN C 1 152 ? -7.479  -1.356  34.240  1.00 65.67  ? 152 ASN C CG  1 
ATOM   9423  O OD1 . ASN C 1 152 ? -6.424  -1.696  33.710  1.00 62.06  ? 152 ASN C OD1 1 
ATOM   9424  N ND2 . ASN C 1 152 ? -7.679  -0.134  34.718  1.00 69.31  ? 152 ASN C ND2 1 
ATOM   9425  N N   . LYS C 1 153 ? -10.232 -4.819  35.910  1.00 78.19  ? 153 LYS C N   1 
ATOM   9426  C CA  . LYS C 1 153 ? -11.501 -5.529  36.013  1.00 63.23  ? 153 LYS C CA  1 
ATOM   9427  C C   . LYS C 1 153 ? -12.240 -5.151  37.290  1.00 73.51  ? 153 LYS C C   1 
ATOM   9428  O O   . LYS C 1 153 ? -13.340 -4.587  37.249  1.00 71.00  ? 153 LYS C O   1 
ATOM   9429  C CB  . LYS C 1 153 ? -11.244 -7.037  35.961  1.00 65.90  ? 153 LYS C CB  1 
ATOM   9430  C CG  . LYS C 1 153 ? -12.344 -7.864  35.324  1.00 75.26  ? 153 LYS C CG  1 
ATOM   9431  C CD  . LYS C 1 153 ? -11.980 -9.340  35.374  1.00 73.66  ? 153 LYS C CD  1 
ATOM   9432  C CE  . LYS C 1 153 ? -13.082 -10.215 34.808  1.00 85.65  ? 153 LYS C CE  1 
ATOM   9433  N NZ  . LYS C 1 153 ? -12.897 -11.641 35.196  1.00 93.25  ? 153 LYS C NZ  1 
ATOM   9434  N N   . GLY C 1 154 ? -11.649 -5.467  38.440  1.00 67.96  ? 154 GLY C N   1 
ATOM   9435  C CA  . GLY C 1 154 ? -12.206 -5.070  39.718  1.00 71.05  ? 154 GLY C CA  1 
ATOM   9436  C C   . GLY C 1 154 ? -13.379 -5.920  40.158  1.00 78.87  ? 154 GLY C C   1 
ATOM   9437  O O   . GLY C 1 154 ? -13.594 -6.122  41.357  1.00 75.14  ? 154 GLY C O   1 
ATOM   9438  N N   . ARG C 1 155 ? -14.137 -6.432  39.196  1.00 83.54  ? 155 ARG C N   1 
ATOM   9439  C CA  . ARG C 1 155 ? -15.343 -7.194  39.460  1.00 84.76  ? 155 ARG C CA  1 
ATOM   9440  C C   . ARG C 1 155 ? -15.055 -8.688  39.331  1.00 80.95  ? 155 ARG C C   1 
ATOM   9441  O O   . ARG C 1 155 ? -13.904 -9.106  39.180  1.00 71.28  ? 155 ARG C O   1 
ATOM   9442  C CB  . ARG C 1 155 ? -16.468 -6.726  38.534  1.00 88.09  ? 155 ARG C CB  1 
ATOM   9443  C CG  . ARG C 1 155 ? -17.124 -5.437  39.008  1.00 81.99  ? 155 ARG C CG  1 
ATOM   9444  C CD  . ARG C 1 155 ? -17.120 -5.396  40.529  1.00 87.30  ? 155 ARG C CD  1 
ATOM   9445  N NE  . ARG C 1 155 ? -17.338 -4.066  41.086  1.00 96.20  ? 155 ARG C NE  1 
ATOM   9446  C CZ  . ARG C 1 155 ? -18.346 -3.743  41.885  1.00 96.95  ? 155 ARG C CZ  1 
ATOM   9447  N NH1 . ARG C 1 155 ? -19.270 -4.628  42.226  1.00 92.18  ? 155 ARG C NH1 1 
ATOM   9448  N NH2 . ARG C 1 155 ? -18.425 -2.502  42.360  1.00 86.75  ? 155 ARG C NH2 1 
ATOM   9449  N N   . ASN C 1 156 ? -16.117 -9.493  39.379  1.00 84.10  ? 156 ASN C N   1 
ATOM   9450  C CA  . ASN C 1 156 ? -16.063 -10.935 39.599  1.00 90.58  ? 156 ASN C CA  1 
ATOM   9451  C C   . ASN C 1 156 ? -14.929 -11.612 38.842  1.00 82.85  ? 156 ASN C C   1 
ATOM   9452  O O   . ASN C 1 156 ? -14.844 -11.529 37.613  1.00 73.59  ? 156 ASN C O   1 
ATOM   9453  C CB  . ASN C 1 156 ? -17.400 -11.560 39.196  1.00 78.20  ? 156 ASN C CB  1 
ATOM   9454  C CG  . ASN C 1 156 ? -17.963 -12.467 40.270  1.00 79.85  ? 156 ASN C CG  1 
ATOM   9455  O OD1 . ASN C 1 156 ? -17.219 -13.083 41.033  1.00 79.34  ? 156 ASN C OD1 1 
ATOM   9456  N ND2 . ASN C 1 156 ? -19.286 -12.555 40.333  1.00 75.77  ? 156 ASN C ND2 1 
ATOM   9457  N N   . TYR C 1 157 ? -14.061 -12.290 39.587  1.00 77.91  ? 157 TYR C N   1 
ATOM   9458  C CA  . TYR C 1 157 ? -12.976 -13.083 39.035  1.00 76.67  ? 157 TYR C CA  1 
ATOM   9459  C C   . TYR C 1 157 ? -13.335 -14.561 39.120  1.00 71.14  ? 157 TYR C C   1 
ATOM   9460  O O   . TYR C 1 157 ? -14.028 -14.993 40.045  1.00 65.81  ? 157 TYR C O   1 
ATOM   9461  C CB  . TYR C 1 157 ? -11.665 -12.821 39.786  1.00 60.62  ? 157 TYR C CB  1 
ATOM   9462  C CG  . TYR C 1 157 ? -11.137 -11.412 39.639  1.00 66.38  ? 157 TYR C CG  1 
ATOM   9463  C CD1 . TYR C 1 157 ? -11.534 -10.403 40.509  1.00 65.47  ? 157 TYR C CD1 1 
ATOM   9464  C CD2 . TYR C 1 157 ? -10.243 -11.088 38.626  1.00 77.42  ? 157 TYR C CD2 1 
ATOM   9465  C CE1 . TYR C 1 157 ? -11.055 -9.112  40.372  1.00 67.63  ? 157 TYR C CE1 1 
ATOM   9466  C CE2 . TYR C 1 157 ? -9.759  -9.802  38.482  1.00 70.46  ? 157 TYR C CE2 1 
ATOM   9467  C CZ  . TYR C 1 157 ? -10.168 -8.818  39.358  1.00 67.83  ? 157 TYR C CZ  1 
ATOM   9468  O OH  . TYR C 1 157 ? -9.687  -7.537  39.214  1.00 65.43  ? 157 TYR C OH  1 
ATOM   9469  N N   . THR C 1 158 ? -12.878 -15.328 38.137  1.00 71.53  ? 158 THR C N   1 
ATOM   9470  C CA  . THR C 1 158 ? -13.079 -16.768 38.136  1.00 67.13  ? 158 THR C CA  1 
ATOM   9471  C C   . THR C 1 158 ? -11.900 -17.467 38.808  1.00 64.49  ? 158 THR C C   1 
ATOM   9472  O O   . THR C 1 158 ? -10.827 -16.888 38.997  1.00 64.18  ? 158 THR C O   1 
ATOM   9473  C CB  . THR C 1 158 ? -13.260 -17.298 36.711  1.00 69.63  ? 158 THR C CB  1 
ATOM   9474  O OG1 . THR C 1 158 ? -12.421 -16.563 35.812  1.00 68.78  ? 158 THR C OG1 1 
ATOM   9475  C CG2 . THR C 1 158 ? -14.712 -17.160 36.270  1.00 73.03  ? 158 THR C CG2 1 
ATOM   9476  N N   . GLN C 1 159 ? -12.118 -18.732 39.176  1.00 65.27  ? 159 GLN C N   1 
ATOM   9477  C CA  . GLN C 1 159 ? -11.059 -19.504 39.819  1.00 63.10  ? 159 GLN C CA  1 
ATOM   9478  C C   . GLN C 1 159 ? -9.859  -19.677 38.897  1.00 68.00  ? 159 GLN C C   1 
ATOM   9479  O O   . GLN C 1 159 ? -8.721  -19.796 39.368  1.00 65.21  ? 159 GLN C O   1 
ATOM   9480  C CB  . GLN C 1 159 ? -11.604 -20.867 40.260  1.00 64.58  ? 159 GLN C CB  1 
ATOM   9481  C CG  . GLN C 1 159 ? -10.547 -21.869 40.728  1.00 62.94  ? 159 GLN C CG  1 
ATOM   9482  C CD  . GLN C 1 159 ? -9.907  -21.486 42.054  1.00 75.15  ? 159 GLN C CD  1 
ATOM   9483  O OE1 . GLN C 1 159 ? -10.232 -20.464 42.654  1.00 78.82  ? 159 GLN C OE1 1 
ATOM   9484  N NE2 . GLN C 1 159 ? -8.975  -22.320 42.516  1.00 65.79  ? 159 GLN C NE2 1 
ATOM   9485  N N   . GLU C 1 160 ? -10.092 -19.682 37.583  1.00 66.65  ? 160 GLU C N   1 
ATOM   9486  C CA  . GLU C 1 160 ? -8.993  -19.815 36.635  1.00 69.47  ? 160 GLU C CA  1 
ATOM   9487  C C   . GLU C 1 160 ? -8.155  -18.542 36.575  1.00 69.05  ? 160 GLU C C   1 
ATOM   9488  O O   . GLU C 1 160 ? -6.923  -18.608 36.495  1.00 59.61  ? 160 GLU C O   1 
ATOM   9489  C CB  . GLU C 1 160 ? -9.544  -20.175 35.254  1.00 67.68  ? 160 GLU C CB  1 
ATOM   9490  C CG  . GLU C 1 160 ? -10.162 -21.566 35.190  1.00 81.81  ? 160 GLU C CG  1 
ATOM   9491  C CD  . GLU C 1 160 ? -11.593 -21.602 35.698  1.00 85.17  ? 160 GLU C CD  1 
ATOM   9492  O OE1 . GLU C 1 160 ? -12.469 -20.974 35.066  1.00 87.73  ? 160 GLU C OE1 1 
ATOM   9493  O OE2 . GLU C 1 160 ? -11.840 -22.251 36.737  1.00 80.62  ? 160 GLU C OE2 1 
ATOM   9494  N N   . GLU C 1 161 ? -8.804  -17.373 36.616  1.00 76.17  ? 161 GLU C N   1 
ATOM   9495  C CA  . GLU C 1 161 ? -8.061  -16.115 36.576  1.00 78.02  ? 161 GLU C CA  1 
ATOM   9496  C C   . GLU C 1 161 ? -7.234  -15.909 37.841  1.00 62.92  ? 161 GLU C C   1 
ATOM   9497  O O   . GLU C 1 161 ? -6.077  -15.477 37.767  1.00 62.99  ? 161 GLU C O   1 
ATOM   9498  C CB  . GLU C 1 161 ? -9.015  -14.938 36.367  1.00 71.42  ? 161 GLU C CB  1 
ATOM   9499  C CG  . GLU C 1 161 ? -9.363  -14.673 34.911  1.00 73.12  ? 161 GLU C CG  1 
ATOM   9500  C CD  . GLU C 1 161 ? -10.622 -13.842 34.757  1.00 85.60  ? 161 GLU C CD  1 
ATOM   9501  O OE1 . GLU C 1 161 ? -11.606 -14.115 35.475  1.00 86.32  ? 161 GLU C OE1 1 
ATOM   9502  O OE2 . GLU C 1 161 ? -10.626 -12.916 33.918  1.00 85.52  ? 161 GLU C OE2 1 
ATOM   9503  N N   . LYS C 1 162 ? -7.810  -16.204 39.011  1.00 65.19  ? 162 LYS C N   1 
ATOM   9504  C CA  . LYS C 1 162 ? -7.063  -16.050 40.256  1.00 74.02  ? 162 LYS C CA  1 
ATOM   9505  C C   . LYS C 1 162 ? -5.860  -16.981 40.292  1.00 62.27  ? 162 LYS C C   1 
ATOM   9506  O O   . LYS C 1 162 ? -4.779  -16.598 40.754  1.00 59.71  ? 162 LYS C O   1 
ATOM   9507  C CB  . LYS C 1 162 ? -7.969  -16.314 41.460  1.00 71.76  ? 162 LYS C CB  1 
ATOM   9508  C CG  . LYS C 1 162 ? -7.277  -16.078 42.797  1.00 74.19  ? 162 LYS C CG  1 
ATOM   9509  C CD  . LYS C 1 162 ? -7.299  -17.310 43.689  1.00 76.33  ? 162 LYS C CD  1 
ATOM   9510  C CE  . LYS C 1 162 ? -8.686  -17.909 43.762  1.00 69.85  ? 162 LYS C CE  1 
ATOM   9511  N NZ  . LYS C 1 162 ? -8.781  -19.023 44.744  1.00 75.34  ? 162 LYS C NZ  1 
ATOM   9512  N N   . GLU C 1 163 ? -6.037  -18.214 39.818  1.00 53.92  ? 163 GLU C N   1 
ATOM   9513  C CA  . GLU C 1 163 ? -4.931  -19.159 39.756  1.00 53.00  ? 163 GLU C CA  1 
ATOM   9514  C C   . GLU C 1 163 ? -3.891  -18.735 38.725  1.00 56.21  ? 163 GLU C C   1 
ATOM   9515  O O   . GLU C 1 163 ? -2.708  -19.064 38.866  1.00 50.91  ? 163 GLU C O   1 
ATOM   9516  C CB  . GLU C 1 163 ? -5.476  -20.552 39.445  1.00 65.10  ? 163 GLU C CB  1 
ATOM   9517  C CG  . GLU C 1 163 ? -4.474  -21.677 39.551  1.00 57.99  ? 163 GLU C CG  1 
ATOM   9518  C CD  . GLU C 1 163 ? -5.084  -23.012 39.179  1.00 65.56  ? 163 GLU C CD  1 
ATOM   9519  O OE1 . GLU C 1 163 ? -5.917  -23.522 39.957  1.00 57.69  ? 163 GLU C OE1 1 
ATOM   9520  O OE2 . GLU C 1 163 ? -4.736  -23.545 38.104  1.00 86.57  ? 163 GLU C OE2 1 
ATOM   9521  N N   . TYR C 1 164 ? -4.314  -18.005 37.690  1.00 61.67  ? 164 TYR C N   1 
ATOM   9522  C CA  . TYR C 1 164 ? -3.369  -17.462 36.718  1.00 55.84  ? 164 TYR C CA  1 
ATOM   9523  C C   . TYR C 1 164 ? -2.412  -16.476 37.378  1.00 52.16  ? 164 TYR C C   1 
ATOM   9524  O O   . TYR C 1 164 ? -1.213  -16.463 37.075  1.00 50.36  ? 164 TYR C O   1 
ATOM   9525  C CB  . TYR C 1 164 ? -4.135  -16.800 35.572  1.00 57.16  ? 164 TYR C CB  1 
ATOM   9526  C CG  . TYR C 1 164 ? -3.281  -16.065 34.561  1.00 61.95  ? 164 TYR C CG  1 
ATOM   9527  C CD1 . TYR C 1 164 ? -2.649  -16.747 33.528  1.00 57.60  ? 164 TYR C CD1 1 
ATOM   9528  C CD2 . TYR C 1 164 ? -3.126  -14.686 34.627  1.00 66.81  ? 164 TYR C CD2 1 
ATOM   9529  C CE1 . TYR C 1 164 ? -1.875  -16.077 32.597  1.00 58.88  ? 164 TYR C CE1 1 
ATOM   9530  C CE2 . TYR C 1 164 ? -2.355  -14.008 33.701  1.00 73.84  ? 164 TYR C CE2 1 
ATOM   9531  C CZ  . TYR C 1 164 ? -1.732  -14.708 32.688  1.00 73.77  ? 164 TYR C CZ  1 
ATOM   9532  O OH  . TYR C 1 164 ? -0.963  -14.038 31.764  1.00 69.37  ? 164 TYR C OH  1 
ATOM   9533  N N   . VAL C 1 165 ? -2.928  -15.641 38.284  1.00 50.87  ? 165 VAL C N   1 
ATOM   9534  C CA  . VAL C 1 165 ? -2.075  -14.715 39.025  1.00 49.50  ? 165 VAL C CA  1 
ATOM   9535  C C   . VAL C 1 165 ? -1.085  -15.481 39.892  1.00 45.52  ? 165 VAL C C   1 
ATOM   9536  O O   . VAL C 1 165 ? 0.083   -15.091 40.021  1.00 43.81  ? 165 VAL C O   1 
ATOM   9537  C CB  . VAL C 1 165 ? -2.938  -13.755 39.866  1.00 47.06  ? 165 VAL C CB  1 
ATOM   9538  C CG1 . VAL C 1 165 ? -2.060  -12.833 40.701  1.00 44.66  ? 165 VAL C CG1 1 
ATOM   9539  C CG2 . VAL C 1 165 ? -3.867  -12.951 38.969  1.00 48.98  ? 165 VAL C CG2 1 
ATOM   9540  N N   . LEU C 1 166 ? -1.535  -16.582 40.500  1.00 46.02  ? 166 LEU C N   1 
ATOM   9541  C CA  . LEU C 1 166 ? -0.673  -17.354 41.389  1.00 44.51  ? 166 LEU C CA  1 
ATOM   9542  C C   . LEU C 1 166 ? 0.539   -17.899 40.647  1.00 53.48  ? 166 LEU C C   1 
ATOM   9543  O O   . LEU C 1 166 ? 1.660   -17.872 41.167  1.00 51.75  ? 166 LEU C O   1 
ATOM   9544  C CB  . LEU C 1 166 ? -1.469  -18.492 42.022  1.00 45.55  ? 166 LEU C CB  1 
ATOM   9545  C CG  . LEU C 1 166 ? -2.144  -18.165 43.354  1.00 53.09  ? 166 LEU C CG  1 
ATOM   9546  C CD1 . LEU C 1 166 ? -2.922  -19.361 43.868  1.00 52.99  ? 166 LEU C CD1 1 
ATOM   9547  C CD2 . LEU C 1 166 ? -1.114  -17.710 44.376  1.00 42.47  ? 166 LEU C CD2 1 
ATOM   9548  N N   . ASN C 1 167 ? 0.330   -18.403 39.433  1.00 56.93  ? 167 ASN C N   1 
ATOM   9549  C CA  . ASN C 1 167 ? 1.440   -18.925 38.645  1.00 56.95  ? 167 ASN C CA  1 
ATOM   9550  C C   . ASN C 1 167 ? 2.426   -17.816 38.288  1.00 55.93  ? 167 ASN C C   1 
ATOM   9551  O O   . ASN C 1 167 ? 3.643   -17.985 38.426  1.00 52.45  ? 167 ASN C O   1 
ATOM   9552  C CB  . ASN C 1 167 ? 0.894   -19.613 37.393  1.00 49.44  ? 167 ASN C CB  1 
ATOM   9553  C CG  . ASN C 1 167 ? 1.974   -20.245 36.546  1.00 57.05  ? 167 ASN C CG  1 
ATOM   9554  O OD1 . ASN C 1 167 ? 2.905   -19.583 36.110  1.00 50.43  ? 167 ASN C OD1 1 
ATOM   9555  N ND2 . ASN C 1 167 ? 1.846   -21.541 36.300  1.00 80.74  ? 167 ASN C ND2 1 
ATOM   9556  N N   . LYS C 1 168 ? 1.916   -16.669 37.828  1.00 53.31  ? 168 LYS C N   1 
ATOM   9557  C CA  . LYS C 1 168 ? 2.792   -15.558 37.464  1.00 45.33  ? 168 LYS C CA  1 
ATOM   9558  C C   . LYS C 1 168 ? 3.565   -15.047 38.673  1.00 52.67  ? 168 LYS C C   1 
ATOM   9559  O O   . LYS C 1 168 ? 4.739   -14.675 38.558  1.00 54.07  ? 168 LYS C O   1 
ATOM   9560  C CB  . LYS C 1 168 ? 1.974   -14.427 36.840  1.00 45.67  ? 168 LYS C CB  1 
ATOM   9561  C CG  . LYS C 1 168 ? 1.343   -14.776 35.507  1.00 47.70  ? 168 LYS C CG  1 
ATOM   9562  C CD  . LYS C 1 168 ? 2.400   -15.045 34.452  1.00 56.81  ? 168 LYS C CD  1 
ATOM   9563  C CE  . LYS C 1 168 ? 1.845   -15.893 33.319  1.00 61.87  ? 168 LYS C CE  1 
ATOM   9564  N NZ  . LYS C 1 168 ? 2.420   -17.267 33.325  1.00 59.47  ? 168 LYS C NZ  1 
ATOM   9565  N N   . TYR C 1 169 ? 2.916   -15.010 39.840  1.00 52.91  ? 169 TYR C N   1 
ATOM   9566  C CA  . TYR C 1 169 ? 3.584   -14.544 41.051  1.00 41.89  ? 169 TYR C CA  1 
ATOM   9567  C C   . TYR C 1 169 ? 4.797   -15.405 41.378  1.00 46.62  ? 169 TYR C C   1 
ATOM   9568  O O   . TYR C 1 169 ? 5.855   -14.886 41.754  1.00 50.85  ? 169 TYR C O   1 
ATOM   9569  C CB  . TYR C 1 169 ? 2.604   -14.544 42.224  1.00 43.94  ? 169 TYR C CB  1 
ATOM   9570  C CG  . TYR C 1 169 ? 1.812   -13.265 42.367  1.00 46.55  ? 169 TYR C CG  1 
ATOM   9571  C CD1 . TYR C 1 169 ? 1.882   -12.274 41.400  1.00 44.09  ? 169 TYR C CD1 1 
ATOM   9572  C CD2 . TYR C 1 169 ? 1.002   -13.045 43.472  1.00 45.56  ? 169 TYR C CD2 1 
ATOM   9573  C CE1 . TYR C 1 169 ? 1.166   -11.101 41.525  1.00 49.14  ? 169 TYR C CE1 1 
ATOM   9574  C CE2 . TYR C 1 169 ? 0.280   -11.871 43.607  1.00 38.93  ? 169 TYR C CE2 1 
ATOM   9575  C CZ  . TYR C 1 169 ? 0.366   -10.904 42.629  1.00 40.03  ? 169 TYR C CZ  1 
ATOM   9576  O OH  . TYR C 1 169 ? -0.348  -9.734  42.754  1.00 44.26  ? 169 TYR C OH  1 
ATOM   9577  N N   . PHE C 1 170 ? 4.665   -16.727 41.245  1.00 45.86  ? 170 PHE C N   1 
ATOM   9578  C CA  . PHE C 1 170 ? 5.767   -17.615 41.589  1.00 57.28  ? 170 PHE C CA  1 
ATOM   9579  C C   . PHE C 1 170 ? 6.874   -17.606 40.543  1.00 54.73  ? 170 PHE C C   1 
ATOM   9580  O O   . PHE C 1 170 ? 8.010   -17.972 40.862  1.00 49.22  ? 170 PHE C O   1 
ATOM   9581  C CB  . PHE C 1 170 ? 5.245   -19.034 41.805  1.00 53.20  ? 170 PHE C CB  1 
ATOM   9582  C CG  . PHE C 1 170 ? 4.667   -19.255 43.172  1.00 51.60  ? 170 PHE C CG  1 
ATOM   9583  C CD1 . PHE C 1 170 ? 3.342   -18.951 43.437  1.00 51.48  ? 170 PHE C CD1 1 
ATOM   9584  C CD2 . PHE C 1 170 ? 5.453   -19.753 44.197  1.00 47.70  ? 170 PHE C CD2 1 
ATOM   9585  C CE1 . PHE C 1 170 ? 2.808   -19.149 44.695  1.00 52.56  ? 170 PHE C CE1 1 
ATOM   9586  C CE2 . PHE C 1 170 ? 4.926   -19.953 45.459  1.00 49.27  ? 170 PHE C CE2 1 
ATOM   9587  C CZ  . PHE C 1 170 ? 3.600   -19.651 45.708  1.00 55.11  ? 170 PHE C CZ  1 
ATOM   9588  N N   . GLU C 1 171 ? 6.574   -17.202 39.305  1.00 51.53  ? 171 GLU C N   1 
ATOM   9589  C CA  . GLU C 1 171 ? 7.643   -16.970 38.341  1.00 45.99  ? 171 GLU C CA  1 
ATOM   9590  C C   . GLU C 1 171 ? 8.510   -15.789 38.748  1.00 43.48  ? 171 GLU C C   1 
ATOM   9591  O O   . GLU C 1 171 ? 9.715   -15.775 38.466  1.00 48.37  ? 171 GLU C O   1 
ATOM   9592  C CB  . GLU C 1 171 ? 7.066   -16.732 36.948  1.00 45.38  ? 171 GLU C CB  1 
ATOM   9593  C CG  . GLU C 1 171 ? 6.848   -17.991 36.131  1.00 45.94  ? 171 GLU C CG  1 
ATOM   9594  C CD  . GLU C 1 171 ? 5.651   -17.888 35.216  1.00 65.33  ? 171 GLU C CD  1 
ATOM   9595  O OE1 . GLU C 1 171 ? 5.288   -16.753 34.842  1.00 68.14  ? 171 GLU C OE1 1 
ATOM   9596  O OE2 . GLU C 1 171 ? 5.106   -18.938 34.824  1.00 68.13  ? 171 GLU C OE2 1 
ATOM   9597  N N   . ILE C 1 172 ? 7.911   -14.787 39.392  1.00 46.40  ? 172 ILE C N   1 
ATOM   9598  C CA  . ILE C 1 172 ? 8.670   -13.642 39.881  1.00 46.91  ? 172 ILE C CA  1 
ATOM   9599  C C   . ILE C 1 172 ? 9.587   -14.061 41.025  1.00 49.22  ? 172 ILE C C   1 
ATOM   9600  O O   . ILE C 1 172 ? 10.730  -13.597 41.127  1.00 49.67  ? 172 ILE C O   1 
ATOM   9601  C CB  . ILE C 1 172 ? 7.702   -12.517 40.294  1.00 37.17  ? 172 ILE C CB  1 
ATOM   9602  C CG1 . ILE C 1 172 ? 7.283   -11.707 39.066  1.00 37.15  ? 172 ILE C CG1 1 
ATOM   9603  C CG2 . ILE C 1 172 ? 8.317   -11.620 41.354  1.00 36.72  ? 172 ILE C CG2 1 
ATOM   9604  C CD1 . ILE C 1 172 ? 8.440   -11.108 38.305  1.00 47.90  ? 172 ILE C CD1 1 
ATOM   9605  N N   . ILE C 1 173 ? 9.108   -14.953 41.895  1.00 44.20  ? 173 ILE C N   1 
ATOM   9606  C CA  . ILE C 1 173 ? 9.928   -15.428 43.005  1.00 37.22  ? 173 ILE C CA  1 
ATOM   9607  C C   . ILE C 1 173 ? 11.083  -16.282 42.494  1.00 37.88  ? 173 ILE C C   1 
ATOM   9608  O O   . ILE C 1 173 ? 12.201  -16.216 43.019  1.00 36.46  ? 173 ILE C O   1 
ATOM   9609  C CB  . ILE C 1 173 ? 9.055   -16.190 44.018  1.00 41.92  ? 173 ILE C CB  1 
ATOM   9610  C CG1 . ILE C 1 173 ? 7.848   -15.337 44.415  1.00 42.88  ? 173 ILE C CG1 1 
ATOM   9611  C CG2 . ILE C 1 173 ? 9.868   -16.576 45.244  1.00 38.61  ? 173 ILE C CG2 1 
ATOM   9612  C CD1 . ILE C 1 173 ? 6.997   -15.946 45.504  1.00 32.90  ? 173 ILE C CD1 1 
ATOM   9613  N N   . LYS C 1 174 ? 10.835  -17.099 41.466  1.00 39.59  ? 174 LYS C N   1 
ATOM   9614  C CA  . LYS C 1 174 ? 11.905  -17.891 40.869  1.00 35.36  ? 174 LYS C CA  1 
ATOM   9615  C C   . LYS C 1 174 ? 12.984  -17.022 40.237  1.00 39.53  ? 174 LYS C C   1 
ATOM   9616  O O   . LYS C 1 174 ? 14.124  -17.476 40.093  1.00 53.05  ? 174 LYS C O   1 
ATOM   9617  C CB  . LYS C 1 174 ? 11.334  -18.847 39.816  1.00 37.35  ? 174 LYS C CB  1 
ATOM   9618  C CG  . LYS C 1 174 ? 10.429  -19.939 40.368  1.00 42.02  ? 174 LYS C CG  1 
ATOM   9619  C CD  . LYS C 1 174 ? 9.551   -20.528 39.268  1.00 49.58  ? 174 LYS C CD  1 
ATOM   9620  C CE  . LYS C 1 174 ? 9.191   -21.983 39.544  1.00 47.44  ? 174 LYS C CE  1 
ATOM   9621  N NZ  . LYS C 1 174 ? 8.028   -22.108 40.467  1.00 41.00  ? 174 LYS C NZ  1 
ATOM   9622  N N   . LYS C 1 175 ? 12.655  -15.786 39.864  1.00 42.74  ? 175 LYS C N   1 
ATOM   9623  C CA  . LYS C 1 175 ? 13.580  -14.886 39.189  1.00 39.25  ? 175 LYS C CA  1 
ATOM   9624  C C   . LYS C 1 175 ? 14.149  -13.815 40.113  1.00 42.90  ? 175 LYS C C   1 
ATOM   9625  O O   . LYS C 1 175 ? 14.743  -12.846 39.627  1.00 41.19  ? 175 LYS C O   1 
ATOM   9626  C CB  . LYS C 1 175 ? 12.884  -14.220 37.999  1.00 47.15  ? 175 LYS C CB  1 
ATOM   9627  C CG  . LYS C 1 175 ? 13.314  -14.746 36.640  1.00 49.85  ? 175 LYS C CG  1 
ATOM   9628  C CD  . LYS C 1 175 ? 12.269  -14.437 35.578  1.00 53.77  ? 175 LYS C CD  1 
ATOM   9629  C CE  . LYS C 1 175 ? 12.412  -13.015 35.061  1.00 53.75  ? 175 LYS C CE  1 
ATOM   9630  N NZ  . LYS C 1 175 ? 13.453  -12.911 33.999  1.00 47.60  ? 175 LYS C NZ  1 
ATOM   9631  N N   . THR C 1 176 ? 13.983  -13.960 41.428  1.00 49.84  ? 176 THR C N   1 
ATOM   9632  C CA  . THR C 1 176 ? 14.355  -12.894 42.353  1.00 37.59  ? 176 THR C CA  1 
ATOM   9633  C C   . THR C 1 176 ? 15.832  -12.937 42.736  1.00 36.76  ? 176 THR C C   1 
ATOM   9634  O O   . THR C 1 176 ? 16.501  -11.902 42.728  1.00 40.08  ? 176 THR C O   1 
ATOM   9635  C CB  . THR C 1 176 ? 13.473  -12.950 43.604  1.00 42.39  ? 176 THR C CB  1 
ATOM   9636  O OG1 . THR C 1 176 ? 12.229  -12.289 43.335  1.00 34.02  ? 176 THR C OG1 1 
ATOM   9637  C CG2 . THR C 1 176 ? 14.156  -12.264 44.782  1.00 37.18  ? 176 THR C CG2 1 
ATOM   9638  N N   . LEU C 1 177 ? 16.366  -14.108 43.089  1.00 40.14  ? 177 LEU C N   1 
ATOM   9639  C CA  . LEU C 1 177 ? 17.799  -14.170 43.359  1.00 33.76  ? 177 LEU C CA  1 
ATOM   9640  C C   . LEU C 1 177 ? 18.604  -13.866 42.102  1.00 38.52  ? 177 LEU C C   1 
ATOM   9641  O O   . LEU C 1 177 ? 19.598  -13.135 42.157  1.00 37.21  ? 177 LEU C O   1 
ATOM   9642  C CB  . LEU C 1 177 ? 18.194  -15.531 43.929  1.00 43.19  ? 177 LEU C CB  1 
ATOM   9643  C CG  . LEU C 1 177 ? 17.867  -15.803 45.400  1.00 31.01  ? 177 LEU C CG  1 
ATOM   9644  C CD1 . LEU C 1 177 ? 18.125  -14.568 46.261  1.00 27.61  ? 177 LEU C CD1 1 
ATOM   9645  C CD2 . LEU C 1 177 ? 16.446  -16.305 45.565  1.00 41.98  ? 177 LEU C CD2 1 
ATOM   9646  N N   . SER C 1 178 ? 18.166  -14.393 40.953  1.00 44.35  ? 178 SER C N   1 
ATOM   9647  C CA  . SER C 1 178 ? 18.924  -14.236 39.715  1.00 47.96  ? 178 SER C CA  1 
ATOM   9648  C C   . SER C 1 178 ? 19.088  -12.773 39.320  1.00 47.75  ? 178 SER C C   1 
ATOM   9649  O O   . SER C 1 178 ? 20.084  -12.416 38.680  1.00 50.03  ? 178 SER C O   1 
ATOM   9650  C CB  . SER C 1 178 ? 18.246  -15.015 38.586  1.00 40.52  ? 178 SER C CB  1 
ATOM   9651  O OG  . SER C 1 178 ? 17.663  -16.212 39.068  1.00 62.28  ? 178 SER C OG  1 
ATOM   9652  N N   . ILE C 1 179 ? 18.132  -11.915 39.678  1.00 41.65  ? 179 ILE C N   1 
ATOM   9653  C CA  . ILE C 1 179 ? 18.277  -10.508 39.321  1.00 32.06  ? 179 ILE C CA  1 
ATOM   9654  C C   . ILE C 1 179 ? 19.248  -9.809  40.272  1.00 36.09  ? 179 ILE C C   1 
ATOM   9655  O O   . ILE C 1 179 ? 19.945  -8.871  39.869  1.00 43.31  ? 179 ILE C O   1 
ATOM   9656  C CB  . ILE C 1 179 ? 16.905  -9.808  39.273  1.00 31.84  ? 179 ILE C CB  1 
ATOM   9657  C CG1 . ILE C 1 179 ? 17.061  -8.334  38.912  1.00 50.29  ? 179 ILE C CG1 1 
ATOM   9658  C CG2 . ILE C 1 179 ? 16.185  -9.908  40.593  1.00 32.96  ? 179 ILE C CG2 1 
ATOM   9659  C CD1 . ILE C 1 179 ? 15.794  -7.552  39.078  1.00 50.82  ? 179 ILE C CD1 1 
ATOM   9660  N N   . TYR C 1 180 ? 19.335  -10.258 41.526  1.00 29.66  ? 180 TYR C N   1 
ATOM   9661  C CA  . TYR C 1 180 ? 20.354  -9.717  42.421  1.00 35.29  ? 180 TYR C CA  1 
ATOM   9662  C C   . TYR C 1 180 ? 21.755  -10.092 41.950  1.00 35.54  ? 180 TYR C C   1 
ATOM   9663  O O   . TYR C 1 180 ? 22.680  -9.275  42.032  1.00 35.64  ? 180 TYR C O   1 
ATOM   9664  C CB  . TYR C 1 180 ? 20.117  -10.189 43.857  1.00 35.53  ? 180 TYR C CB  1 
ATOM   9665  C CG  . TYR C 1 180 ? 18.955  -9.493  44.534  1.00 27.80  ? 180 TYR C CG  1 
ATOM   9666  C CD1 . TYR C 1 180 ? 19.073  -8.188  44.991  1.00 29.24  ? 180 TYR C CD1 1 
ATOM   9667  C CD2 . TYR C 1 180 ? 17.743  -10.141 44.717  1.00 31.43  ? 180 TYR C CD2 1 
ATOM   9668  C CE1 . TYR C 1 180 ? 18.013  -7.548  45.606  1.00 30.08  ? 180 TYR C CE1 1 
ATOM   9669  C CE2 . TYR C 1 180 ? 16.676  -9.512  45.328  1.00 26.57  ? 180 TYR C CE2 1 
ATOM   9670  C CZ  . TYR C 1 180 ? 16.817  -8.217  45.772  1.00 27.40  ? 180 TYR C CZ  1 
ATOM   9671  O OH  . TYR C 1 180 ? 15.758  -7.586  46.383  1.00 25.66  ? 180 TYR C OH  1 
ATOM   9672  N N   . ARG C 1 181 ? 21.937  -11.321 41.457  1.00 36.68  ? 181 ARG C N   1 
ATOM   9673  C CA  . ARG C 1 181 ? 23.204  -11.665 40.818  1.00 37.98  ? 181 ARG C CA  1 
ATOM   9674  C C   . ARG C 1 181 ? 23.432  -10.818 39.574  1.00 42.24  ? 181 ARG C C   1 
ATOM   9675  O O   . ARG C 1 181 ? 24.552  -10.360 39.323  1.00 46.03  ? 181 ARG C O   1 
ATOM   9676  C CB  . ARG C 1 181 ? 23.248  -13.154 40.461  1.00 42.53  ? 181 ARG C CB  1 
ATOM   9677  C CG  . ARG C 1 181 ? 22.307  -14.039 41.253  1.00 40.98  ? 181 ARG C CG  1 
ATOM   9678  C CD  . ARG C 1 181 ? 22.447  -15.503 40.861  1.00 47.10  ? 181 ARG C CD  1 
ATOM   9679  N NE  . ARG C 1 181 ? 21.385  -16.322 41.435  1.00 56.79  ? 181 ARG C NE  1 
ATOM   9680  C CZ  . ARG C 1 181 ? 21.563  -17.527 41.959  1.00 70.93  ? 181 ARG C CZ  1 
ATOM   9681  N NH1 . ARG C 1 181 ? 22.760  -18.091 42.006  1.00 71.30  ? 181 ARG C NH1 1 
ATOM   9682  N NH2 . ARG C 1 181 ? 20.514  -18.185 42.446  1.00 68.88  ? 181 ARG C NH2 1 
ATOM   9683  N N   . GLU C 1 182 ? 22.379  -10.595 38.783  1.00 36.05  ? 182 GLU C N   1 
ATOM   9684  C CA  . GLU C 1 182 ? 22.542  -9.860  37.533  1.00 33.94  ? 182 GLU C CA  1 
ATOM   9685  C C   . GLU C 1 182 ? 22.970  -8.419  37.782  1.00 35.71  ? 182 GLU C C   1 
ATOM   9686  O O   . GLU C 1 182 ? 23.857  -7.906  37.090  1.00 46.79  ? 182 GLU C O   1 
ATOM   9687  C CB  . GLU C 1 182 ? 21.249  -9.902  36.717  1.00 36.80  ? 182 GLU C CB  1 
ATOM   9688  C CG  . GLU C 1 182 ? 21.464  -9.656  35.229  1.00 43.44  ? 182 GLU C CG  1 
ATOM   9689  C CD  . GLU C 1 182 ? 20.167  -9.596  34.446  1.00 47.72  ? 182 GLU C CD  1 
ATOM   9690  O OE1 . GLU C 1 182 ? 19.319  -10.497 34.619  1.00 39.08  ? 182 GLU C OE1 1 
ATOM   9691  O OE2 . GLU C 1 182 ? 19.997  -8.646  33.651  1.00 46.15  ? 182 GLU C OE2 1 
ATOM   9692  N N   . ILE C 1 183 ? 22.362  -7.749  38.764  1.00 32.52  ? 183 ILE C N   1 
ATOM   9693  C CA  . ILE C 1 183 ? 22.694  -6.345  38.993  1.00 38.85  ? 183 ILE C CA  1 
ATOM   9694  C C   . ILE C 1 183 ? 24.127  -6.202  39.494  1.00 39.96  ? 183 ILE C C   1 
ATOM   9695  O O   . ILE C 1 183 ? 24.821  -5.239  39.147  1.00 38.45  ? 183 ILE C O   1 
ATOM   9696  C CB  . ILE C 1 183 ? 21.677  -5.684  39.947  1.00 35.70  ? 183 ILE C CB  1 
ATOM   9697  C CG1 . ILE C 1 183 ? 21.739  -6.285  41.354  1.00 29.22  ? 183 ILE C CG1 1 
ATOM   9698  C CG2 . ILE C 1 183 ? 20.269  -5.756  39.371  1.00 30.87  ? 183 ILE C CG2 1 
ATOM   9699  C CD1 . ILE C 1 183 ? 22.350  -5.356  42.385  1.00 29.55  ? 183 ILE C CD1 1 
ATOM   9700  N N   . LYS C 1 184 ? 24.601  -7.150  40.310  1.00 32.92  ? 184 LYS C N   1 
ATOM   9701  C CA  . LYS C 1 184 ? 25.988  -7.084  40.761  1.00 33.70  ? 184 LYS C CA  1 
ATOM   9702  C C   . LYS C 1 184 ? 26.957  -7.489  39.657  1.00 44.21  ? 184 LYS C C   1 
ATOM   9703  O O   . LYS C 1 184 ? 28.027  -6.885  39.519  1.00 48.45  ? 184 LYS C O   1 
ATOM   9704  C CB  . LYS C 1 184 ? 26.205  -7.957  41.996  1.00 42.05  ? 184 LYS C CB  1 
ATOM   9705  C CG  . LYS C 1 184 ? 27.579  -7.741  42.623  1.00 43.18  ? 184 LYS C CG  1 
ATOM   9706  C CD  . LYS C 1 184 ? 27.798  -8.566  43.878  1.00 32.07  ? 184 LYS C CD  1 
ATOM   9707  C CE  . LYS C 1 184 ? 27.764  -10.057 43.594  1.00 34.84  ? 184 LYS C CE  1 
ATOM   9708  N NZ  . LYS C 1 184 ? 28.515  -10.807 44.638  1.00 40.13  ? 184 LYS C NZ  1 
ATOM   9709  N N   . GLU C 1 185 ? 26.610  -8.514  38.875  1.00 40.95  ? 185 GLU C N   1 
ATOM   9710  C CA  . GLU C 1 185 ? 27.464  -8.908  37.758  1.00 35.16  ? 185 GLU C CA  1 
ATOM   9711  C C   . GLU C 1 185 ? 27.545  -7.803  36.713  1.00 36.10  ? 185 GLU C C   1 
ATOM   9712  O O   . GLU C 1 185 ? 28.627  -7.509  36.191  1.00 37.21  ? 185 GLU C O   1 
ATOM   9713  C CB  . GLU C 1 185 ? 26.953  -10.205 37.128  1.00 35.99  ? 185 GLU C CB  1 
ATOM   9714  C CG  . GLU C 1 185 ? 27.767  -11.441 37.489  1.00 36.43  ? 185 GLU C CG  1 
ATOM   9715  C CD  . GLU C 1 185 ? 27.896  -11.650 38.987  1.00 55.20  ? 185 GLU C CD  1 
ATOM   9716  O OE1 . GLU C 1 185 ? 26.859  -11.833 39.657  1.00 57.79  ? 185 GLU C OE1 1 
ATOM   9717  O OE2 . GLU C 1 185 ? 29.037  -11.634 39.495  1.00 66.41  ? 185 GLU C OE2 1 
ATOM   9718  N N   . GLU C 1 186 ? 26.414  -7.170  36.405  1.00 45.32  ? 186 GLU C N   1 
ATOM   9719  C CA  . GLU C 1 186 ? 26.363  -6.098  35.419  1.00 39.89  ? 186 GLU C CA  1 
ATOM   9720  C C   . GLU C 1 186 ? 26.839  -4.761  35.973  1.00 36.17  ? 186 GLU C C   1 
ATOM   9721  O O   . GLU C 1 186 ? 26.869  -3.776  35.229  1.00 46.59  ? 186 GLU C O   1 
ATOM   9722  C CB  . GLU C 1 186 ? 24.940  -5.955  34.871  1.00 37.08  ? 186 GLU C CB  1 
ATOM   9723  C CG  . GLU C 1 186 ? 24.476  -7.140  34.031  1.00 49.07  ? 186 GLU C CG  1 
ATOM   9724  C CD  . GLU C 1 186 ? 23.469  -6.746  32.966  1.00 53.57  ? 186 GLU C CD  1 
ATOM   9725  O OE1 . GLU C 1 186 ? 22.745  -5.750  33.172  1.00 62.10  ? 186 GLU C OE1 1 
ATOM   9726  O OE2 . GLU C 1 186 ? 23.398  -7.435  31.925  1.00 48.70  ? 186 GLU C OE2 1 
ATOM   9727  N N   . GLY C 1 187 ? 27.193  -4.698  37.255  1.00 36.83  ? 187 GLY C N   1 
ATOM   9728  C CA  . GLY C 1 187 ? 27.775  -3.505  37.834  1.00 38.75  ? 187 GLY C CA  1 
ATOM   9729  C C   . GLY C 1 187 ? 26.804  -2.402  38.181  1.00 37.49  ? 187 GLY C C   1 
ATOM   9730  O O   . GLY C 1 187 ? 27.239  -1.266  38.405  1.00 33.75  ? 187 GLY C O   1 
ATOM   9731  N N   . LYS C 1 188 ? 25.505  -2.690  38.232  1.00 35.57  ? 188 LYS C N   1 
ATOM   9732  C CA  . LYS C 1 188 ? 24.516  -1.667  38.539  1.00 32.50  ? 188 LYS C CA  1 
ATOM   9733  C C   . LYS C 1 188 ? 24.320  -1.451  40.035  1.00 31.29  ? 188 LYS C C   1 
ATOM   9734  O O   . LYS C 1 188 ? 23.693  -0.460  40.421  1.00 37.74  ? 188 LYS C O   1 
ATOM   9735  C CB  . LYS C 1 188 ? 23.172  -2.018  37.889  1.00 34.57  ? 188 LYS C CB  1 
ATOM   9736  C CG  . LYS C 1 188 ? 23.143  -1.863  36.369  1.00 34.44  ? 188 LYS C CG  1 
ATOM   9737  C CD  . LYS C 1 188 ? 24.162  -0.841  35.875  1.00 51.19  ? 188 LYS C CD  1 
ATOM   9738  C CE  . LYS C 1 188 ? 23.492  0.445   35.414  1.00 68.43  ? 188 LYS C CE  1 
ATOM   9739  N NZ  . LYS C 1 188 ? 24.483  1.510   35.089  1.00 58.04  ? 188 LYS C NZ  1 
ATOM   9740  N N   . GLY C 1 189 ? 24.839  -2.334  40.879  1.00 31.56  ? 189 GLY C N   1 
ATOM   9741  C CA  . GLY C 1 189 ? 24.705  -2.151  42.314  1.00 29.11  ? 189 GLY C CA  1 
ATOM   9742  C C   . GLY C 1 189 ? 25.429  -3.243  43.071  1.00 34.22  ? 189 GLY C C   1 
ATOM   9743  O O   . GLY C 1 189 ? 25.845  -4.260  42.504  1.00 38.13  ? 189 GLY C O   1 
ATOM   9744  N N   . SER C 1 190 ? 25.569  -3.015  44.375  1.00 35.43  ? 190 SER C N   1 
ATOM   9745  C CA  . SER C 1 190 ? 26.241  -3.939  45.277  1.00 27.51  ? 190 SER C CA  1 
ATOM   9746  C C   . SER C 1 190 ? 25.229  -4.569  46.224  1.00 26.51  ? 190 SER C C   1 
ATOM   9747  O O   . SER C 1 190 ? 24.354  -3.882  46.760  1.00 25.90  ? 190 SER C O   1 
ATOM   9748  C CB  . SER C 1 190 ? 27.331  -3.230  46.086  1.00 27.56  ? 190 SER C CB  1 
ATOM   9749  O OG  . SER C 1 190 ? 28.468  -2.958  45.289  1.00 33.97  ? 190 SER C OG  1 
ATOM   9750  N N   . VAL C 1 191 ? 25.353  -5.878  46.427  1.00 26.49  ? 191 VAL C N   1 
ATOM   9751  C CA  . VAL C 1 191 ? 24.497  -6.618  47.348  1.00 25.73  ? 191 VAL C CA  1 
ATOM   9752  C C   . VAL C 1 191 ? 25.333  -7.030  48.551  1.00 25.49  ? 191 VAL C C   1 
ATOM   9753  O O   . VAL C 1 191 ? 26.338  -7.738  48.411  1.00 26.08  ? 191 VAL C O   1 
ATOM   9754  C CB  . VAL C 1 191 ? 23.848  -7.838  46.677  1.00 26.04  ? 191 VAL C CB  1 
ATOM   9755  C CG1 . VAL C 1 191 ? 22.546  -7.438  45.999  1.00 29.18  ? 191 VAL C CG1 1 
ATOM   9756  C CG2 . VAL C 1 191 ? 24.793  -8.463  45.676  1.00 30.11  ? 191 VAL C CG2 1 
ATOM   9757  N N   . SER C 1 192 ? 24.919  -6.585  49.730  1.00 24.78  ? 192 SER C N   1 
ATOM   9758  C CA  . SER C 1 192 ? 25.547  -6.954  50.988  1.00 26.40  ? 192 SER C CA  1 
ATOM   9759  C C   . SER C 1 192 ? 24.649  -7.931  51.736  1.00 24.14  ? 192 SER C C   1 
ATOM   9760  O O   . SER C 1 192 ? 23.478  -8.123  51.399  1.00 23.87  ? 192 SER C O   1 
ATOM   9761  C CB  . SER C 1 192 ? 25.816  -5.716  51.850  1.00 24.40  ? 192 SER C CB  1 
ATOM   9762  O OG  . SER C 1 192 ? 24.672  -5.370  52.609  1.00 23.75  ? 192 SER C OG  1 
ATOM   9763  N N   . THR C 1 193 ? 25.214  -8.554  52.765  1.00 24.19  ? 193 THR C N   1 
ATOM   9764  C CA  . THR C 1 193 ? 24.469  -9.467  53.614  1.00 24.12  ? 193 THR C CA  1 
ATOM   9765  C C   . THR C 1 193 ? 24.666  -9.078  55.071  1.00 29.81  ? 193 THR C C   1 
ATOM   9766  O O   . THR C 1 193 ? 25.605  -8.362  55.426  1.00 27.17  ? 193 THR C O   1 
ATOM   9767  C CB  . THR C 1 193 ? 24.887  -10.931 53.398  1.00 27.91  ? 193 THR C CB  1 
ATOM   9768  O OG1 . THR C 1 193 ? 23.926  -11.798 54.013  1.00 24.23  ? 193 THR C OG1 1 
ATOM   9769  C CG2 . THR C 1 193 ? 26.256  -11.192 54.004  1.00 34.41  ? 193 THR C CG2 1 
ATOM   9770  N N   . SER C 1 194 ? 23.753  -9.545  55.904  1.00 27.15  ? 194 SER C N   1 
ATOM   9771  C CA  . SER C 1 194 ? 23.779  -9.351  57.340  1.00 37.03  ? 194 SER C CA  1 
ATOM   9772  C C   . SER C 1 194 ? 24.079  -10.670 58.035  1.00 32.58  ? 194 SER C C   1 
ATOM   9773  O O   . SER C 1 194 ? 24.069  -11.732 57.405  1.00 23.97  ? 194 SER C O   1 
ATOM   9774  C CB  . SER C 1 194 ? 22.431  -8.799  57.820  1.00 28.07  ? 194 SER C CB  1 
ATOM   9775  O OG  . SER C 1 194 ? 22.415  -7.383  57.788  1.00 26.56  ? 194 SER C OG  1 
ATOM   9776  N N   . PRO C 1 195 ? 24.383  -10.639 59.334  1.00 27.69  ? 195 PRO C N   1 
ATOM   9777  C CA  . PRO C 1 195 ? 24.394  -11.882 60.110  1.00 24.74  ? 195 PRO C CA  1 
ATOM   9778  C C   . PRO C 1 195 ? 23.108  -12.668 59.887  1.00 26.92  ? 195 PRO C C   1 
ATOM   9779  O O   . PRO C 1 195 ? 22.030  -12.096 59.706  1.00 21.35  ? 195 PRO C O   1 
ATOM   9780  C CB  . PRO C 1 195 ? 24.530  -11.390 61.553  1.00 22.31  ? 195 PRO C CB  1 
ATOM   9781  C CG  . PRO C 1 195 ? 25.376  -10.164 61.412  1.00 21.90  ? 195 PRO C CG  1 
ATOM   9782  C CD  . PRO C 1 195 ? 24.960  -9.518  60.100  1.00 23.73  ? 195 PRO C CD  1 
ATOM   9783  N N   . TYR C 1 196 ? 23.243  -13.997 59.915  1.00 30.04  ? 196 TYR C N   1 
ATOM   9784  C CA  . TYR C 1 196 ? 22.279  -14.882 59.262  1.00 21.95  ? 196 TYR C CA  1 
ATOM   9785  C C   . TYR C 1 196 ? 20.844  -14.612 59.700  1.00 19.97  ? 196 TYR C C   1 
ATOM   9786  O O   . TYR C 1 196 ? 19.953  -14.425 58.864  1.00 18.39  ? 196 TYR C O   1 
ATOM   9787  C CB  . TYR C 1 196 ? 22.651  -16.340 59.534  1.00 20.25  ? 196 TYR C CB  1 
ATOM   9788  C CG  . TYR C 1 196 ? 22.166  -17.292 58.470  1.00 20.36  ? 196 TYR C CG  1 
ATOM   9789  C CD1 . TYR C 1 196 ? 20.822  -17.631 58.375  1.00 23.97  ? 196 TYR C CD1 1 
ATOM   9790  C CD2 . TYR C 1 196 ? 23.050  -17.851 57.558  1.00 21.31  ? 196 TYR C CD2 1 
ATOM   9791  C CE1 . TYR C 1 196 ? 20.372  -18.501 57.402  1.00 25.88  ? 196 TYR C CE1 1 
ATOM   9792  C CE2 . TYR C 1 196 ? 22.610  -18.722 56.583  1.00 25.59  ? 196 TYR C CE2 1 
ATOM   9793  C CZ  . TYR C 1 196 ? 21.271  -19.045 56.508  1.00 34.57  ? 196 TYR C CZ  1 
ATOM   9794  O OH  . TYR C 1 196 ? 20.831  -19.913 55.536  1.00 44.78  ? 196 TYR C OH  1 
ATOM   9795  N N   . TYR C 1 197 ? 20.597  -14.591 61.007  1.00 19.38  ? 197 TYR C N   1 
ATOM   9796  C CA  . TYR C 1 197 ? 19.243  -14.461 61.528  1.00 19.04  ? 197 TYR C CA  1 
ATOM   9797  C C   . TYR C 1 197 ? 18.990  -13.087 62.139  1.00 24.45  ? 197 TYR C C   1 
ATOM   9798  O O   . TYR C 1 197 ? 18.179  -12.949 63.058  1.00 25.28  ? 197 TYR C O   1 
ATOM   9799  C CB  . TYR C 1 197 ? 18.954  -15.572 62.533  1.00 18.15  ? 197 TYR C CB  1 
ATOM   9800  C CG  . TYR C 1 197 ? 18.881  -16.931 61.875  1.00 20.79  ? 197 TYR C CG  1 
ATOM   9801  C CD1 . TYR C 1 197 ? 17.787  -17.286 61.096  1.00 19.70  ? 197 TYR C CD1 1 
ATOM   9802  C CD2 . TYR C 1 197 ? 19.913  -17.849 62.010  1.00 24.67  ? 197 TYR C CD2 1 
ATOM   9803  C CE1 . TYR C 1 197 ? 17.718  -18.519 60.482  1.00 20.79  ? 197 TYR C CE1 1 
ATOM   9804  C CE2 . TYR C 1 197 ? 19.851  -19.085 61.400  1.00 20.78  ? 197 TYR C CE2 1 
ATOM   9805  C CZ  . TYR C 1 197 ? 18.753  -19.413 60.637  1.00 21.33  ? 197 TYR C CZ  1 
ATOM   9806  O OH  . TYR C 1 197 ? 18.687  -20.644 60.029  1.00 22.64  ? 197 TYR C OH  1 
ATOM   9807  N N   . HIS C 1 198 ? 19.671  -12.066 61.621  1.00 23.07  ? 198 HIS C N   1 
ATOM   9808  C CA  . HIS C 1 198 ? 19.432  -10.672 61.986  1.00 26.49  ? 198 HIS C CA  1 
ATOM   9809  C C   . HIS C 1 198 ? 19.427  -10.423 63.486  1.00 26.83  ? 198 HIS C C   1 
ATOM   9810  O O   . HIS C 1 198 ? 18.446  -9.848  64.024  1.00 34.28  ? 198 HIS C O   1 
ATOM   9811  C CB  . HIS C 1 198 ? 18.128  -10.209 61.353  1.00 27.23  ? 198 HIS C CB  1 
ATOM   9812  C CG  . HIS C 1 198 ? 18.029  -8.728  61.166  1.00 27.43  ? 198 HIS C CG  1 
ATOM   9813  N ND1 . HIS C 1 198 ? 17.213  -7.934  61.944  1.00 26.80  ? 198 HIS C ND1 1 
ATOM   9814  C CD2 . HIS C 1 198 ? 18.625  -7.899  60.277  1.00 22.48  ? 198 HIS C CD2 1 
ATOM   9815  C CE1 . HIS C 1 198 ? 17.318  -6.678  61.550  1.00 29.45  ? 198 HIS C CE1 1 
ATOM   9816  N NE2 . HIS C 1 198 ? 18.170  -6.629  60.541  1.00 31.47  ? 198 HIS C NE2 1 
ATOM   9817  N N   . PRO C 1 199 ? 20.462  -10.807 64.219  1.00 27.74  ? 199 PRO C N   1 
ATOM   9818  C CA  . PRO C 1 199 ? 20.490  -10.579 65.662  1.00 25.68  ? 199 PRO C CA  1 
ATOM   9819  C C   . PRO C 1 199 ? 21.219  -9.286  66.015  1.00 29.11  ? 199 PRO C C   1 
ATOM   9820  O O   . PRO C 1 199 ? 21.823  -8.627  65.168  1.00 32.55  ? 199 PRO C O   1 
ATOM   9821  C CB  . PRO C 1 199 ? 21.256  -11.801 66.178  1.00 27.62  ? 199 PRO C CB  1 
ATOM   9822  C CG  . PRO C 1 199 ? 22.244  -12.094 65.066  1.00 25.45  ? 199 PRO C CG  1 
ATOM   9823  C CD  . PRO C 1 199 ? 21.693  -11.494 63.778  1.00 26.09  ? 199 PRO C CD  1 
ATOM   9824  N N   . LEU C 1 200 ? 21.152  -8.936  67.298  1.00 32.32  ? 200 LEU C N   1 
ATOM   9825  C CA  . LEU C 1 200 ? 21.931  -7.818  67.827  1.00 26.31  ? 200 LEU C CA  1 
ATOM   9826  C C   . LEU C 1 200 ? 23.278  -8.368  68.276  1.00 28.10  ? 200 LEU C C   1 
ATOM   9827  O O   . LEU C 1 200 ? 23.451  -8.808  69.415  1.00 28.42  ? 200 LEU C O   1 
ATOM   9828  C CB  . LEU C 1 200 ? 21.197  -7.115  68.960  1.00 23.43  ? 200 LEU C CB  1 
ATOM   9829  C CG  . LEU C 1 200 ? 19.919  -6.369  68.582  1.00 21.02  ? 200 LEU C CG  1 
ATOM   9830  C CD1 . LEU C 1 200 ? 19.205  -5.890  69.833  1.00 25.95  ? 200 LEU C CD1 1 
ATOM   9831  C CD2 . LEU C 1 200 ? 20.242  -5.204  67.661  1.00 22.90  ? 200 LEU C CD2 1 
ATOM   9832  N N   . ILE C 1 201 ? 24.238  -8.353  67.356  1.00 27.49  ? 201 ILE C N   1 
ATOM   9833  C CA  . ILE C 1 201 ? 25.597  -8.833  67.601  1.00 20.42  ? 201 ILE C CA  1 
ATOM   9834  C C   . ILE C 1 201 ? 26.209  -8.151  68.823  1.00 30.31  ? 201 ILE C C   1 
ATOM   9835  O O   . ILE C 1 201 ? 26.859  -8.837  69.626  1.00 29.44  ? 201 ILE C O   1 
ATOM   9836  C CB  . ILE C 1 201 ? 26.478  -8.646  66.354  1.00 20.39  ? 201 ILE C CB  1 
ATOM   9837  C CG1 . ILE C 1 201 ? 25.921  -9.455  65.183  1.00 24.65  ? 201 ILE C CG1 1 
ATOM   9838  C CG2 . ILE C 1 201 ? 27.905  -9.070  66.642  1.00 20.90  ? 201 ILE C CG2 1 
ATOM   9839  C CD1 . ILE C 1 201 ? 25.917  -10.950 65.422  1.00 34.35  ? 201 ILE C CD1 1 
ATOM   9840  N N   . PRO C 1 202 ? 26.052  -6.828  69.019  1.00 25.85  ? 202 PRO C N   1 
ATOM   9841  C CA  . PRO C 1 202 ? 26.604  -6.218  70.242  1.00 19.76  ? 202 PRO C CA  1 
ATOM   9842  C C   . PRO C 1 202 ? 26.129  -6.869  71.531  1.00 21.82  ? 202 PRO C C   1 
ATOM   9843  O O   . PRO C 1 202 ? 26.918  -7.004  72.473  1.00 24.19  ? 202 PRO C O   1 
ATOM   9844  C CB  . PRO C 1 202 ? 26.136  -4.760  70.139  1.00 17.76  ? 202 PRO C CB  1 
ATOM   9845  C CG  . PRO C 1 202 ? 26.053  -4.507  68.687  1.00 17.36  ? 202 PRO C CG  1 
ATOM   9846  C CD  . PRO C 1 202 ? 25.565  -5.793  68.082  1.00 16.82  ? 202 PRO C CD  1 
ATOM   9847  N N   . ILE C 1 203 ? 24.862  -7.278  71.603  1.00 22.12  ? 203 ILE C N   1 
ATOM   9848  C CA  . ILE C 1 203 ? 24.367  -7.950  72.801  1.00 19.91  ? 203 ILE C CA  1 
ATOM   9849  C C   . ILE C 1 203 ? 25.020  -9.319  72.954  1.00 19.73  ? 203 ILE C C   1 
ATOM   9850  O O   . ILE C 1 203 ? 25.462  -9.695  74.046  1.00 19.81  ? 203 ILE C O   1 
ATOM   9851  C CB  . ILE C 1 203 ? 22.833  -8.064  72.763  1.00 26.80  ? 203 ILE C CB  1 
ATOM   9852  C CG1 . ILE C 1 203 ? 22.202  -6.684  72.576  1.00 24.19  ? 203 ILE C CG1 1 
ATOM   9853  C CG2 . ILE C 1 203 ? 22.318  -8.725  74.031  1.00 25.40  ? 203 ILE C CG2 1 
ATOM   9854  C CD1 . ILE C 1 203 ? 22.521  -5.730  73.683  1.00 18.57  ? 203 ILE C CD1 1 
ATOM   9855  N N   . LEU C 1 204 ? 25.085  -10.086 71.861  1.00 23.36  ? 204 LEU C N   1 
ATOM   9856  C CA  . LEU C 1 204 ? 25.644  -11.433 71.925  1.00 20.96  ? 204 LEU C CA  1 
ATOM   9857  C C   . LEU C 1 204 ? 27.131  -11.407 72.253  1.00 20.33  ? 204 LEU C C   1 
ATOM   9858  O O   . LEU C 1 204 ? 27.615  -12.241 73.026  1.00 21.04  ? 204 LEU C O   1 
ATOM   9859  C CB  . LEU C 1 204 ? 25.398  -12.163 70.606  1.00 21.77  ? 204 LEU C CB  1 
ATOM   9860  C CG  . LEU C 1 204 ? 23.960  -12.169 70.086  1.00 20.76  ? 204 LEU C CG  1 
ATOM   9861  C CD1 . LEU C 1 204 ? 23.898  -12.849 68.730  1.00 25.49  ? 204 LEU C CD1 1 
ATOM   9862  C CD2 . LEU C 1 204 ? 23.036  -12.855 71.079  1.00 21.89  ? 204 LEU C CD2 1 
ATOM   9863  N N   . LEU C 1 205 ? 27.873  -10.464 71.670  1.00 22.07  ? 205 LEU C N   1 
ATOM   9864  C CA  . LEU C 1 205 ? 29.303  -10.375 71.946  1.00 20.27  ? 205 LEU C CA  1 
ATOM   9865  C C   . LEU C 1 205 ? 29.559  -9.990  73.397  1.00 23.02  ? 205 LEU C C   1 
ATOM   9866  O O   . LEU C 1 205 ? 30.337  -10.649 74.098  1.00 28.00  ? 205 LEU C O   1 
ATOM   9867  C CB  . LEU C 1 205 ? 29.957  -9.371  70.996  1.00 23.13  ? 205 LEU C CB  1 
ATOM   9868  C CG  . LEU C 1 205 ? 30.182  -9.860  69.564  1.00 26.01  ? 205 LEU C CG  1 
ATOM   9869  C CD1 . LEU C 1 205 ? 30.810  -8.768  68.722  1.00 27.94  ? 205 LEU C CD1 1 
ATOM   9870  C CD2 . LEU C 1 205 ? 31.050  -11.108 69.551  1.00 35.26  ? 205 LEU C CD2 1 
ATOM   9871  N N   . ASN C 1 206 ? 28.907  -8.930  73.867  1.00 25.34  ? 206 ASN C N   1 
ATOM   9872  C CA  . ASN C 1 206 ? 29.043  -8.479  75.247  1.00 21.30  ? 206 ASN C CA  1 
ATOM   9873  C C   . ASN C 1 206 ? 27.773  -7.750  75.666  1.00 22.14  ? 206 ASN C C   1 
ATOM   9874  O O   . ASN C 1 206 ? 27.552  -6.602  75.259  1.00 23.57  ? 206 ASN C O   1 
ATOM   9875  C CB  . ASN C 1 206 ? 30.262  -7.570  75.410  1.00 30.32  ? 206 ASN C CB  1 
ATOM   9876  C CG  . ASN C 1 206 ? 30.429  -7.059  76.834  1.00 36.96  ? 206 ASN C CG  1 
ATOM   9877  O OD1 . ASN C 1 206 ? 29.847  -7.600  77.776  1.00 36.17  ? 206 ASN C OD1 1 
ATOM   9878  N ND2 . ASN C 1 206 ? 31.223  -6.006  76.992  1.00 44.56  ? 206 ASN C ND2 1 
ATOM   9879  N N   . PRO C 1 207 ? 26.926  -8.374  76.489  1.00 21.98  ? 207 PRO C N   1 
ATOM   9880  C CA  . PRO C 1 207 ? 25.675  -7.715  76.902  1.00 22.10  ? 207 PRO C CA  1 
ATOM   9881  C C   . PRO C 1 207 ? 25.890  -6.441  77.704  1.00 23.75  ? 207 PRO C C   1 
ATOM   9882  O O   . PRO C 1 207 ? 24.917  -5.712  77.942  1.00 21.64  ? 207 PRO C O   1 
ATOM   9883  C CB  . PRO C 1 207 ? 24.970  -8.788  77.745  1.00 21.41  ? 207 PRO C CB  1 
ATOM   9884  C CG  . PRO C 1 207 ? 25.662  -10.083 77.398  1.00 23.26  ? 207 PRO C CG  1 
ATOM   9885  C CD  . PRO C 1 207 ? 27.072  -9.711  77.084  1.00 21.69  ? 207 PRO C CD  1 
ATOM   9886  N N   . ASN C 1 208 ? 27.124  -6.148  78.119  1.00 27.51  ? 208 ASN C N   1 
ATOM   9887  C CA  . ASN C 1 208 ? 27.425  -4.923  78.850  1.00 23.61  ? 208 ASN C CA  1 
ATOM   9888  C C   . ASN C 1 208 ? 27.312  -3.678  77.981  1.00 26.55  ? 208 ASN C C   1 
ATOM   9889  O O   . ASN C 1 208 ? 27.427  -2.565  78.509  1.00 38.47  ? 208 ASN C O   1 
ATOM   9890  C CB  . ASN C 1 208 ? 28.832  -4.996  79.452  1.00 24.62  ? 208 ASN C CB  1 
ATOM   9891  C CG  . ASN C 1 208 ? 28.914  -5.947  80.629  1.00 25.61  ? 208 ASN C CG  1 
ATOM   9892  O OD1 . ASN C 1 208 ? 27.998  -6.022  81.448  1.00 25.92  ? 208 ASN C OD1 1 
ATOM   9893  N ND2 . ASN C 1 208 ? 30.021  -6.674  80.726  1.00 38.71  ? 208 ASN C ND2 1 
ATOM   9894  N N   . CYS C 1 209 ? 27.103  -3.836  76.672  1.00 21.84  ? 209 CYS C N   1 
ATOM   9895  C CA  . CYS C 1 209 ? 27.037  -2.689  75.778  1.00 21.59  ? 209 CYS C CA  1 
ATOM   9896  C C   . CYS C 1 209 ? 25.752  -1.886  75.943  1.00 21.69  ? 209 CYS C C   1 
ATOM   9897  O O   . CYS C 1 209 ? 25.704  -0.730  75.508  1.00 28.33  ? 209 CYS C O   1 
ATOM   9898  C CB  . CYS C 1 209 ? 27.188  -3.145  74.327  1.00 20.55  ? 209 CYS C CB  1 
ATOM   9899  S SG  . CYS C 1 209 ? 25.913  -4.277  73.749  1.00 28.63  ? 209 CYS C SG  1 
ATOM   9900  N N   . VAL C 1 210 ? 24.717  -2.461  76.562  1.00 21.56  ? 210 VAL C N   1 
ATOM   9901  C CA  . VAL C 1 210 ? 23.502  -1.699  76.835  1.00 21.93  ? 210 VAL C CA  1 
ATOM   9902  C C   . VAL C 1 210 ? 23.804  -0.528  77.758  1.00 24.45  ? 210 VAL C C   1 
ATOM   9903  O O   . VAL C 1 210 ? 23.104  0.491   77.734  1.00 23.91  ? 210 VAL C O   1 
ATOM   9904  C CB  . VAL C 1 210 ? 22.407  -2.607  77.439  1.00 21.87  ? 210 VAL C CB  1 
ATOM   9905  C CG1 . VAL C 1 210 ? 22.116  -3.775  76.525  1.00 20.71  ? 210 VAL C CG1 1 
ATOM   9906  C CG2 . VAL C 1 210 ? 22.806  -3.097  78.824  1.00 22.80  ? 210 VAL C CG2 1 
ATOM   9907  N N   . TYR C 1 211 ? 24.861  -0.641  78.564  1.00 27.96  ? 211 TYR C N   1 
ATOM   9908  C CA  . TYR C 1 211 ? 25.146  0.318   79.620  1.00 25.98  ? 211 TYR C CA  1 
ATOM   9909  C C   . TYR C 1 211 ? 25.912  1.542   79.140  1.00 30.82  ? 211 TYR C C   1 
ATOM   9910  O O   . TYR C 1 211 ? 26.067  2.493   79.917  1.00 40.76  ? 211 TYR C O   1 
ATOM   9911  C CB  . TYR C 1 211 ? 25.922  -0.371  80.740  1.00 26.48  ? 211 TYR C CB  1 
ATOM   9912  C CG  . TYR C 1 211 ? 25.132  -1.462  81.421  1.00 26.34  ? 211 TYR C CG  1 
ATOM   9913  C CD1 . TYR C 1 211 ? 23.897  -1.195  81.993  1.00 26.84  ? 211 TYR C CD1 1 
ATOM   9914  C CD2 . TYR C 1 211 ? 25.614  -2.762  81.479  1.00 25.92  ? 211 TYR C CD2 1 
ATOM   9915  C CE1 . TYR C 1 211 ? 23.169  -2.189  82.615  1.00 26.89  ? 211 TYR C CE1 1 
ATOM   9916  C CE2 . TYR C 1 211 ? 24.893  -3.764  82.098  1.00 25.98  ? 211 TYR C CE2 1 
ATOM   9917  C CZ  . TYR C 1 211 ? 23.672  -3.471  82.664  1.00 26.45  ? 211 TYR C CZ  1 
ATOM   9918  O OH  . TYR C 1 211 ? 22.948  -4.462  83.283  1.00 26.69  ? 211 TYR C OH  1 
ATOM   9919  N N   . GLU C 1 212 ? 26.398  1.547   77.897  1.00 32.39  ? 212 GLU C N   1 
ATOM   9920  C CA  . GLU C 1 212 ? 26.970  2.771   77.345  1.00 40.00  ? 212 GLU C CA  1 
ATOM   9921  C C   . GLU C 1 212 ? 25.938  3.888   77.320  1.00 38.32  ? 212 GLU C C   1 
ATOM   9922  O O   . GLU C 1 212 ? 26.239  5.032   77.680  1.00 32.94  ? 212 GLU C O   1 
ATOM   9923  C CB  . GLU C 1 212 ? 27.502  2.531   75.931  1.00 35.32  ? 212 GLU C CB  1 
ATOM   9924  C CG  . GLU C 1 212 ? 28.995  2.269   75.836  1.00 38.60  ? 212 GLU C CG  1 
ATOM   9925  C CD  . GLU C 1 212 ? 29.315  0.799   75.687  1.00 55.83  ? 212 GLU C CD  1 
ATOM   9926  O OE1 . GLU C 1 212 ? 28.445  -0.026  76.020  1.00 60.43  ? 212 GLU C OE1 1 
ATOM   9927  O OE2 . GLU C 1 212 ? 30.425  0.470   75.220  1.00 63.85  ? 212 GLU C OE2 1 
ATOM   9928  N N   . THR C 1 213 ? 24.711  3.567   76.915  1.00 32.05  ? 213 THR C N   1 
ATOM   9929  C CA  . THR C 1 213 ? 23.661  4.551   76.696  1.00 29.14  ? 213 THR C CA  1 
ATOM   9930  C C   . THR C 1 213 ? 22.676  4.658   77.853  1.00 31.71  ? 213 THR C C   1 
ATOM   9931  O O   . THR C 1 213 ? 22.192  5.756   78.140  1.00 43.80  ? 213 THR C O   1 
ATOM   9932  C CB  . THR C 1 213 ? 22.900  4.219   75.409  1.00 36.93  ? 213 THR C CB  1 
ATOM   9933  O OG1 . THR C 1 213 ? 23.058  2.826   75.110  1.00 30.36  ? 213 THR C OG1 1 
ATOM   9934  C CG2 . THR C 1 213 ? 23.445  5.042   74.252  1.00 31.04  ? 213 THR C CG2 1 
ATOM   9935  N N   . THR C 1 214 ? 22.353  3.549   78.518  1.00 38.26  ? 214 THR C N   1 
ATOM   9936  C CA  . THR C 1 214 ? 21.371  3.527   79.606  1.00 30.44  ? 214 THR C CA  1 
ATOM   9937  C C   . THR C 1 214 ? 21.958  2.782   80.800  1.00 32.41  ? 214 THR C C   1 
ATOM   9938  O O   . THR C 1 214 ? 21.644  1.607   81.030  1.00 39.76  ? 214 THR C O   1 
ATOM   9939  C CB  . THR C 1 214 ? 20.058  2.887   79.150  1.00 27.23  ? 214 THR C CB  1 
ATOM   9940  O OG1 . THR C 1 214 ? 20.324  1.608   78.562  1.00 31.29  ? 214 THR C OG1 1 
ATOM   9941  C CG2 . THR C 1 214 ? 19.362  3.768   78.121  1.00 27.35  ? 214 THR C CG2 1 
ATOM   9942  N N   . PRO C 1 215 ? 22.803  3.444   81.596  1.00 29.81  ? 215 PRO C N   1 
ATOM   9943  C CA  . PRO C 1 215 ? 23.562  2.733   82.638  1.00 30.31  ? 215 PRO C CA  1 
ATOM   9944  C C   . PRO C 1 215 ? 22.730  2.183   83.791  1.00 31.09  ? 215 PRO C C   1 
ATOM   9945  O O   . PRO C 1 215 ? 23.307  1.568   84.694  1.00 31.68  ? 215 PRO C O   1 
ATOM   9946  C CB  . PRO C 1 215 ? 24.544  3.804   83.145  1.00 31.95  ? 215 PRO C CB  1 
ATOM   9947  C CG  . PRO C 1 215 ? 24.602  4.828   82.056  1.00 31.78  ? 215 PRO C CG  1 
ATOM   9948  C CD  . PRO C 1 215 ? 23.231  4.846   81.461  1.00 33.33  ? 215 PRO C CD  1 
ATOM   9949  N N   . ASN C 1 216 ? 21.410  2.371   83.815  1.00 35.51  ? 216 ASN C N   1 
ATOM   9950  C CA  . ASN C 1 216 ? 20.601  1.900   84.936  1.00 39.04  ? 216 ASN C CA  1 
ATOM   9951  C C   . ASN C 1 216 ? 19.537  0.885   84.538  1.00 45.80  ? 216 ASN C C   1 
ATOM   9952  O O   . ASN C 1 216 ? 18.693  0.537   85.374  1.00 52.08  ? 216 ASN C O   1 
ATOM   9953  C CB  . ASN C 1 216 ? 19.940  3.079   85.658  1.00 47.91  ? 216 ASN C CB  1 
ATOM   9954  C CG  . ASN C 1 216 ? 19.686  2.791   87.130  1.00 55.79  ? 216 ASN C CG  1 
ATOM   9955  O OD1 . ASN C 1 216 ? 20.396  2.001   87.751  1.00 50.38  ? 216 ASN C OD1 1 
ATOM   9956  N ND2 . ASN C 1 216 ? 18.665  3.428   87.690  1.00 63.23  ? 216 ASN C ND2 1 
ATOM   9957  N N   . VAL C 1 217 ? 19.549  0.391   83.299  1.00 35.54  ? 217 VAL C N   1 
ATOM   9958  C CA  . VAL C 1 217 ? 18.549  -0.589  82.893  1.00 28.50  ? 217 VAL C CA  1 
ATOM   9959  C C   . VAL C 1 217 ? 18.824  -1.917  83.586  1.00 38.24  ? 217 VAL C C   1 
ATOM   9960  O O   . VAL C 1 217 ? 19.976  -2.268  83.879  1.00 35.47  ? 217 VAL C O   1 
ATOM   9961  C CB  . VAL C 1 217 ? 18.523  -0.765  81.364  1.00 26.80  ? 217 VAL C CB  1 
ATOM   9962  C CG1 . VAL C 1 217 ? 17.834  0.415   80.707  1.00 38.12  ? 217 VAL C CG1 1 
ATOM   9963  C CG2 . VAL C 1 217 ? 19.928  -0.966  80.822  1.00 25.84  ? 217 VAL C CG2 1 
ATOM   9964  N N   . LYS C 1 218 ? 17.755  -2.661  83.857  1.00 38.74  ? 218 LYS C N   1 
ATOM   9965  C CA  . LYS C 1 218 ? 17.847  -3.998  84.425  1.00 29.14  ? 218 LYS C CA  1 
ATOM   9966  C C   . LYS C 1 218 ? 17.713  -5.007  83.294  1.00 26.99  ? 218 LYS C C   1 
ATOM   9967  O O   . LYS C 1 218 ? 16.718  -4.996  82.560  1.00 26.52  ? 218 LYS C O   1 
ATOM   9968  C CB  . LYS C 1 218 ? 16.768  -4.224  85.483  1.00 33.39  ? 218 LYS C CB  1 
ATOM   9969  C CG  . LYS C 1 218 ? 16.450  -2.998  86.332  1.00 42.69  ? 218 LYS C CG  1 
ATOM   9970  C CD  . LYS C 1 218 ? 16.022  -3.380  87.744  1.00 43.01  ? 218 LYS C CD  1 
ATOM   9971  C CE  . LYS C 1 218 ? 14.656  -2.798  88.088  1.00 42.41  ? 218 LYS C CE  1 
ATOM   9972  N NZ  . LYS C 1 218 ? 14.115  -3.345  89.367  1.00 41.93  ? 218 LYS C NZ  1 
ATOM   9973  N N   . ILE C 1 219 ? 18.724  -5.858  83.140  1.00 27.26  ? 219 ILE C N   1 
ATOM   9974  C CA  . ILE C 1 219 ? 18.733  -6.875  82.088  1.00 31.24  ? 219 ILE C CA  1 
ATOM   9975  C C   . ILE C 1 219 ? 19.039  -8.224  82.728  1.00 30.89  ? 219 ILE C C   1 
ATOM   9976  O O   . ILE C 1 219 ? 19.646  -8.287  83.805  1.00 32.74  ? 219 ILE C O   1 
ATOM   9977  C CB  . ILE C 1 219 ? 19.747  -6.539  80.970  1.00 23.80  ? 219 ILE C CB  1 
ATOM   9978  C CG1 . ILE C 1 219 ? 21.185  -6.751  81.447  1.00 24.14  ? 219 ILE C CG1 1 
ATOM   9979  C CG2 . ILE C 1 219 ? 19.541  -5.116  80.463  1.00 23.68  ? 219 ILE C CG2 1 
ATOM   9980  C CD1 . ILE C 1 219 ? 22.184  -6.864  80.314  1.00 23.07  ? 219 ILE C CD1 1 
ATOM   9981  N N   . PRO C 1 220 ? 18.621  -9.320  82.097  1.00 27.47  ? 220 PRO C N   1 
ATOM   9982  C CA  . PRO C 1 220 ? 18.784  -10.643 82.710  1.00 25.60  ? 220 PRO C CA  1 
ATOM   9983  C C   . PRO C 1 220 ? 20.241  -10.989 82.980  1.00 25.81  ? 220 PRO C C   1 
ATOM   9984  O O   . PRO C 1 220 ? 21.179  -10.316 82.547  1.00 30.51  ? 220 PRO C O   1 
ATOM   9985  C CB  . PRO C 1 220 ? 18.171  -11.588 81.670  1.00 24.79  ? 220 PRO C CB  1 
ATOM   9986  C CG  . PRO C 1 220 ? 17.184  -10.747 80.943  1.00 24.58  ? 220 PRO C CG  1 
ATOM   9987  C CD  . PRO C 1 220 ? 17.803  -9.382  80.875  1.00 23.84  ? 220 PRO C CD  1 
ATOM   9988  N N   . ASP C 1 221 ? 20.416  -12.074 83.733  1.00 30.39  ? 221 ASP C N   1 
ATOM   9989  C CA  . ASP C 1 221 ? 21.734  -12.571 84.123  1.00 34.61  ? 221 ASP C CA  1 
ATOM   9990  C C   . ASP C 1 221 ? 22.252  -13.465 83.003  1.00 34.09  ? 221 ASP C C   1 
ATOM   9991  O O   . ASP C 1 221 ? 21.953  -14.659 82.942  1.00 36.10  ? 221 ASP C O   1 
ATOM   9992  C CB  . ASP C 1 221 ? 21.652  -13.315 85.450  1.00 35.52  ? 221 ASP C CB  1 
ATOM   9993  C CG  . ASP C 1 221 ? 23.015  -13.716 85.980  1.00 52.80  ? 221 ASP C CG  1 
ATOM   9994  O OD1 . ASP C 1 221 ? 23.900  -12.842 86.056  1.00 48.76  ? 221 ASP C OD1 1 
ATOM   9995  O OD2 . ASP C 1 221 ? 23.195  -14.903 86.328  1.00 64.46  ? 221 ASP C OD2 1 
ATOM   9996  N N   . PHE C 1 222 ? 23.045  -12.879 82.105  1.00 29.59  ? 222 PHE C N   1 
ATOM   9997  C CA  . PHE C 1 222 ? 23.624  -13.631 80.998  1.00 37.20  ? 222 PHE C CA  1 
ATOM   9998  C C   . PHE C 1 222 ? 24.748  -14.529 81.499  1.00 37.41  ? 222 PHE C C   1 
ATOM   9999  O O   . PHE C 1 222 ? 25.927  -14.254 81.253  1.00 33.89  ? 222 PHE C O   1 
ATOM   10000 C CB  . PHE C 1 222 ? 24.155  -12.688 79.913  1.00 35.44  ? 222 PHE C CB  1 
ATOM   10001 C CG  . PHE C 1 222 ? 23.081  -11.982 79.126  1.00 25.68  ? 222 PHE C CG  1 
ATOM   10002 C CD1 . PHE C 1 222 ? 22.335  -10.962 79.697  1.00 22.68  ? 222 PHE C CD1 1 
ATOM   10003 C CD2 . PHE C 1 222 ? 22.835  -12.327 77.805  1.00 31.13  ? 222 PHE C CD2 1 
ATOM   10004 C CE1 . PHE C 1 222 ? 21.356  -10.305 78.968  1.00 23.34  ? 222 PHE C CE1 1 
ATOM   10005 C CE2 . PHE C 1 222 ? 21.858  -11.674 77.072  1.00 27.75  ? 222 PHE C CE2 1 
ATOM   10006 C CZ  . PHE C 1 222 ? 21.117  -10.662 77.654  1.00 20.86  ? 222 PHE C CZ  1 
ATOM   10007 N N   . ALA C 1 223 ? 24.393  -15.605 82.200  1.00 29.06  ? 223 ALA C N   1 
ATOM   10008 C CA  . ALA C 1 223 ? 25.370  -16.542 82.739  1.00 31.03  ? 223 ALA C CA  1 
ATOM   10009 C C   . ALA C 1 223 ? 25.863  -17.548 81.706  1.00 36.24  ? 223 ALA C C   1 
ATOM   10010 O O   . ALA C 1 223 ? 26.494  -18.543 82.081  1.00 44.15  ? 223 ALA C O   1 
ATOM   10011 C CB  . ALA C 1 223 ? 24.781  -17.278 83.945  1.00 43.32  ? 223 ALA C CB  1 
ATOM   10012 N N   . VAL C 1 224 ? 25.577  -17.318 80.426  1.00 40.06  ? 224 VAL C N   1 
ATOM   10013 C CA  . VAL C 1 224 ? 26.037  -18.160 79.330  1.00 33.54  ? 224 VAL C CA  1 
ATOM   10014 C C   . VAL C 1 224 ? 26.576  -17.241 78.242  1.00 26.95  ? 224 VAL C C   1 
ATOM   10015 O O   . VAL C 1 224 ? 26.193  -16.071 78.149  1.00 30.90  ? 224 VAL C O   1 
ATOM   10016 C CB  . VAL C 1 224 ? 24.904  -19.072 78.801  1.00 32.50  ? 224 VAL C CB  1 
ATOM   10017 C CG1 . VAL C 1 224 ? 23.879  -18.260 78.027  1.00 28.09  ? 224 VAL C CG1 1 
ATOM   10018 C CG2 . VAL C 1 224 ? 25.463  -20.210 77.950  1.00 30.68  ? 224 VAL C CG2 1 
ATOM   10019 N N   . SER C 1 225 ? 27.481  -17.769 77.422  1.00 30.48  ? 225 SER C N   1 
ATOM   10020 C CA  . SER C 1 225 ? 28.229  -16.962 76.464  1.00 36.58  ? 225 SER C CA  1 
ATOM   10021 C C   . SER C 1 225 ? 27.627  -17.100 75.070  1.00 34.02  ? 225 SER C C   1 
ATOM   10022 O O   . SER C 1 225 ? 27.509  -18.214 74.546  1.00 29.44  ? 225 SER C O   1 
ATOM   10023 C CB  . SER C 1 225 ? 29.703  -17.368 76.453  1.00 37.16  ? 225 SER C CB  1 
ATOM   10024 O OG  . SER C 1 225 ? 30.455  -16.540 75.581  1.00 41.12  ? 225 SER C OG  1 
ATOM   10025 N N   . PHE C 1 226 ? 27.256  -15.966 74.472  1.00 38.20  ? 226 PHE C N   1 
ATOM   10026 C CA  . PHE C 1 226 ? 26.835  -15.898 73.079  1.00 28.78  ? 226 PHE C CA  1 
ATOM   10027 C C   . PHE C 1 226 ? 27.952  -15.429 72.154  1.00 28.62  ? 226 PHE C C   1 
ATOM   10028 O O   . PHE C 1 226 ? 27.686  -15.135 70.984  1.00 33.40  ? 226 PHE C O   1 
ATOM   10029 C CB  . PHE C 1 226 ? 25.636  -14.959 72.918  1.00 26.67  ? 226 PHE C CB  1 
ATOM   10030 C CG  . PHE C 1 226 ? 24.377  -15.435 73.584  1.00 27.35  ? 226 PHE C CG  1 
ATOM   10031 C CD1 . PHE C 1 226 ? 23.585  -16.404 72.990  1.00 28.74  ? 226 PHE C CD1 1 
ATOM   10032 C CD2 . PHE C 1 226 ? 23.963  -14.884 74.785  1.00 32.48  ? 226 PHE C CD2 1 
ATOM   10033 C CE1 . PHE C 1 226 ? 22.414  -16.830 73.596  1.00 25.16  ? 226 PHE C CE1 1 
ATOM   10034 C CE2 . PHE C 1 226 ? 22.795  -15.306 75.395  1.00 29.73  ? 226 PHE C CE2 1 
ATOM   10035 C CZ  . PHE C 1 226 ? 22.020  -16.282 74.799  1.00 21.25  ? 226 PHE C CZ  1 
ATOM   10036 N N   . ARG C 1 227 ? 29.188  -15.331 72.653  1.00 36.52  ? 227 ARG C N   1 
ATOM   10037 C CA  . ARG C 1 227 ? 30.272  -14.784 71.841  1.00 34.29  ? 227 ARG C CA  1 
ATOM   10038 C C   . ARG C 1 227 ? 30.537  -15.647 70.613  1.00 34.16  ? 227 ARG C C   1 
ATOM   10039 O O   . ARG C 1 227 ? 30.763  -15.124 69.515  1.00 34.00  ? 227 ARG C O   1 
ATOM   10040 C CB  . ARG C 1 227 ? 31.543  -14.638 72.683  1.00 31.94  ? 227 ARG C CB  1 
ATOM   10041 C CG  . ARG C 1 227 ? 32.631  -13.805 72.012  1.00 39.67  ? 227 ARG C CG  1 
ATOM   10042 C CD  . ARG C 1 227 ? 33.105  -12.651 72.889  1.00 46.71  ? 227 ARG C CD  1 
ATOM   10043 N NE  . ARG C 1 227 ? 33.638  -11.554 72.088  1.00 60.89  ? 227 ARG C NE  1 
ATOM   10044 C CZ  . ARG C 1 227 ? 34.286  -10.505 72.578  1.00 58.59  ? 227 ARG C CZ  1 
ATOM   10045 N NH1 . ARG C 1 227 ? 34.521  -10.381 73.874  1.00 53.40  ? 227 ARG C NH1 1 
ATOM   10046 N NH2 . ARG C 1 227 ? 34.710  -9.557  71.745  1.00 52.95  ? 227 ARG C NH2 1 
ATOM   10047 N N   . GLU C 1 228 ? 30.508  -16.972 70.776  1.00 36.52  ? 228 GLU C N   1 
ATOM   10048 C CA  . GLU C 1 228 ? 30.735  -17.863 69.642  1.00 37.39  ? 228 GLU C CA  1 
ATOM   10049 C C   . GLU C 1 228 ? 29.546  -17.880 68.690  1.00 36.32  ? 228 GLU C C   1 
ATOM   10050 O O   . GLU C 1 228 ? 29.709  -18.174 67.500  1.00 40.77  ? 228 GLU C O   1 
ATOM   10051 C CB  . GLU C 1 228 ? 31.037  -19.280 70.130  1.00 38.36  ? 228 GLU C CB  1 
ATOM   10052 C CG  . GLU C 1 228 ? 30.357  -19.661 71.443  1.00 47.14  ? 228 GLU C CG  1 
ATOM   10053 C CD  . GLU C 1 228 ? 31.152  -19.239 72.666  1.00 60.33  ? 228 GLU C CD  1 
ATOM   10054 O OE1 . GLU C 1 228 ? 31.412  -18.026 72.818  1.00 48.21  ? 228 GLU C OE1 1 
ATOM   10055 O OE2 . GLU C 1 228 ? 31.520  -20.120 73.472  1.00 64.49  ? 228 GLU C OE2 1 
ATOM   10056 N N   . ASP C 1 229 ? 28.347  -17.576 69.189  1.00 36.42  ? 229 ASP C N   1 
ATOM   10057 C CA  . ASP C 1 229 ? 27.177  -17.549 68.319  1.00 33.17  ? 229 ASP C CA  1 
ATOM   10058 C C   . ASP C 1 229 ? 27.147  -16.300 67.450  1.00 23.42  ? 229 ASP C C   1 
ATOM   10059 O O   . ASP C 1 229 ? 26.700  -16.356 66.298  1.00 23.42  ? 229 ASP C O   1 
ATOM   10060 C CB  . ASP C 1 229 ? 25.901  -17.646 69.144  1.00 40.62  ? 229 ASP C CB  1 
ATOM   10061 C CG  . ASP C 1 229 ? 25.551  -19.068 69.472  1.00 39.20  ? 229 ASP C CG  1 
ATOM   10062 O OD1 . ASP C 1 229 ? 26.473  -19.911 69.463  1.00 35.19  ? 229 ASP C OD1 1 
ATOM   10063 O OD2 . ASP C 1 229 ? 24.363  -19.348 69.733  1.00 28.48  ? 229 ASP C OD2 1 
ATOM   10064 N N   . ALA C 1 230 ? 27.603  -15.160 67.979  1.00 19.78  ? 230 ALA C N   1 
ATOM   10065 C CA  . ALA C 1 230 ? 27.770  -13.987 67.130  1.00 29.01  ? 230 ALA C CA  1 
ATOM   10066 C C   . ALA C 1 230 ? 28.754  -14.269 66.006  1.00 38.79  ? 230 ALA C C   1 
ATOM   10067 O O   . ALA C 1 230 ? 28.646  -13.683 64.922  1.00 39.49  ? 230 ALA C O   1 
ATOM   10068 C CB  . ALA C 1 230 ? 28.231  -12.791 67.962  1.00 26.03  ? 230 ALA C CB  1 
ATOM   10069 N N   . SER C 1 231 ? 29.719  -15.159 66.248  1.00 35.09  ? 231 SER C N   1 
ATOM   10070 C CA  . SER C 1 231 ? 30.635  -15.573 65.193  1.00 26.06  ? 231 SER C CA  1 
ATOM   10071 C C   . SER C 1 231 ? 29.938  -16.471 64.179  1.00 30.27  ? 231 SER C C   1 
ATOM   10072 O O   . SER C 1 231 ? 30.186  -16.363 62.972  1.00 29.51  ? 231 SER C O   1 
ATOM   10073 C CB  . SER C 1 231 ? 31.840  -16.286 65.803  1.00 28.79  ? 231 SER C CB  1 
ATOM   10074 O OG  . SER C 1 231 ? 33.004  -16.077 65.026  1.00 48.51  ? 231 SER C OG  1 
ATOM   10075 N N   . LYS C 1 232 ? 29.070  -17.370 64.651  1.00 29.79  ? 232 LYS C N   1 
ATOM   10076 C CA  . LYS C 1 232 ? 28.354  -18.256 63.737  1.00 28.36  ? 232 LYS C CA  1 
ATOM   10077 C C   . LYS C 1 232 ? 27.434  -17.472 62.813  1.00 29.76  ? 232 LYS C C   1 
ATOM   10078 O O   . LYS C 1 232 ? 27.315  -17.795 61.626  1.00 33.35  ? 232 LYS C O   1 
ATOM   10079 C CB  . LYS C 1 232 ? 27.551  -19.293 64.517  1.00 30.09  ? 232 LYS C CB  1 
ATOM   10080 C CG  . LYS C 1 232 ? 27.613  -20.685 63.919  1.00 35.16  ? 232 LYS C CG  1 
ATOM   10081 C CD  . LYS C 1 232 ? 27.273  -21.740 64.953  1.00 51.84  ? 232 LYS C CD  1 
ATOM   10082 C CE  . LYS C 1 232 ? 28.304  -21.768 66.079  1.00 45.19  ? 232 LYS C CE  1 
ATOM   10083 N NZ  . LYS C 1 232 ? 27.803  -22.483 67.283  1.00 47.28  ? 232 LYS C NZ  1 
ATOM   10084 N N   . HIS C 1 233 ? 26.762  -16.444 63.342  1.00 26.23  ? 233 HIS C N   1 
ATOM   10085 C CA  . HIS C 1 233 ? 25.862  -15.638 62.525  1.00 19.11  ? 233 HIS C CA  1 
ATOM   10086 C C   . HIS C 1 233 ? 26.608  -14.979 61.372  1.00 21.66  ? 233 HIS C C   1 
ATOM   10087 O O   . HIS C 1 233 ? 26.154  -15.014 60.223  1.00 25.85  ? 233 HIS C O   1 
ATOM   10088 C CB  . HIS C 1 233 ? 25.180  -14.581 63.395  1.00 20.83  ? 233 HIS C CB  1 
ATOM   10089 C CG  . HIS C 1 233 ? 23.961  -15.076 64.112  1.00 25.08  ? 233 HIS C CG  1 
ATOM   10090 N ND1 . HIS C 1 233 ? 23.883  -15.157 65.486  1.00 31.54  ? 233 HIS C ND1 1 
ATOM   10091 C CD2 . HIS C 1 233 ? 22.769  -15.514 63.642  1.00 24.20  ? 233 HIS C CD2 1 
ATOM   10092 C CE1 . HIS C 1 233 ? 22.694  -15.621 65.831  1.00 26.11  ? 233 HIS C CE1 1 
ATOM   10093 N NE2 . HIS C 1 233 ? 22.000  -15.847 64.730  1.00 23.78  ? 233 HIS C NE2 1 
ATOM   10094 N N   . VAL C 1 234 ? 27.760  -14.373 61.662  1.00 24.17  ? 234 VAL C N   1 
ATOM   10095 C CA  . VAL C 1 234 ? 28.518  -13.692 60.617  1.00 25.14  ? 234 VAL C CA  1 
ATOM   10096 C C   . VAL C 1 234 ? 29.108  -14.699 59.635  1.00 25.84  ? 234 VAL C C   1 
ATOM   10097 O O   . VAL C 1 234 ? 29.080  -14.487 58.417  1.00 23.39  ? 234 VAL C O   1 
ATOM   10098 C CB  . VAL C 1 234 ? 29.605  -12.802 61.246  1.00 19.94  ? 234 VAL C CB  1 
ATOM   10099 C CG1 . VAL C 1 234 ? 30.566  -12.302 60.180  1.00 25.31  ? 234 VAL C CG1 1 
ATOM   10100 C CG2 . VAL C 1 234 ? 28.972  -11.634 61.987  1.00 21.78  ? 234 VAL C CG2 1 
ATOM   10101 N N   . GLU C 1 235 ? 29.643  -15.811 60.144  1.00 30.36  ? 235 GLU C N   1 
ATOM   10102 C CA  . GLU C 1 235 ? 30.318  -16.772 59.276  1.00 23.65  ? 235 GLU C CA  1 
ATOM   10103 C C   . GLU C 1 235 ? 29.333  -17.484 58.357  1.00 24.83  ? 235 GLU C C   1 
ATOM   10104 O O   . GLU C 1 235 ? 29.564  -17.589 57.146  1.00 35.11  ? 235 GLU C O   1 
ATOM   10105 C CB  . GLU C 1 235 ? 31.097  -17.783 60.117  1.00 35.79  ? 235 GLU C CB  1 
ATOM   10106 C CG  . GLU C 1 235 ? 32.504  -17.338 60.467  1.00 46.79  ? 235 GLU C CG  1 
ATOM   10107 C CD  . GLU C 1 235 ? 33.552  -17.949 59.558  1.00 67.23  ? 235 GLU C CD  1 
ATOM   10108 O OE1 . GLU C 1 235 ? 33.649  -19.194 59.510  1.00 68.99  ? 235 GLU C OE1 1 
ATOM   10109 O OE2 . GLU C 1 235 ? 34.278  -17.184 58.889  1.00 70.97  ? 235 GLU C OE2 1 
ATOM   10110 N N   . LEU C 1 236 ? 28.229  -17.986 58.915  1.00 26.62  ? 236 LEU C N   1 
ATOM   10111 C CA  . LEU C 1 236 ? 27.249  -18.704 58.106  1.00 24.76  ? 236 LEU C CA  1 
ATOM   10112 C C   . LEU C 1 236 ? 26.611  -17.807 57.055  1.00 29.63  ? 236 LEU C C   1 
ATOM   10113 O O   . LEU C 1 236 ? 26.157  -18.305 56.020  1.00 36.78  ? 236 LEU C O   1 
ATOM   10114 C CB  . LEU C 1 236 ? 26.173  -19.316 59.007  1.00 23.18  ? 236 LEU C CB  1 
ATOM   10115 C CG  . LEU C 1 236 ? 26.381  -20.745 59.513  1.00 25.75  ? 236 LEU C CG  1 
ATOM   10116 C CD1 . LEU C 1 236 ? 27.838  -21.017 59.857  1.00 26.04  ? 236 LEU C CD1 1 
ATOM   10117 C CD2 . LEU C 1 236 ? 25.493  -21.018 60.718  1.00 37.00  ? 236 LEU C CD2 1 
ATOM   10118 N N   . ALA C 1 237 ? 26.573  -16.497 57.299  1.00 27.16  ? 237 ALA C N   1 
ATOM   10119 C CA  . ALA C 1 237 ? 26.075  -15.563 56.295  1.00 23.01  ? 237 ALA C CA  1 
ATOM   10120 C C   . ALA C 1 237 ? 27.011  -15.486 55.096  1.00 28.17  ? 237 ALA C C   1 
ATOM   10121 O O   . ALA C 1 237 ? 26.557  -15.360 53.952  1.00 31.84  ? 237 ALA C O   1 
ATOM   10122 C CB  . ALA C 1 237 ? 25.890  -14.181 56.916  1.00 25.28  ? 237 ALA C CB  1 
ATOM   10123 N N   . LYS C 1 238 ? 28.322  -15.545 55.336  1.00 29.13  ? 238 LYS C N   1 
ATOM   10124 C CA  . LYS C 1 238 ? 29.271  -15.548 54.229  1.00 29.23  ? 238 LYS C CA  1 
ATOM   10125 C C   . LYS C 1 238 ? 29.158  -16.820 53.398  1.00 35.45  ? 238 LYS C C   1 
ATOM   10126 O O   . LYS C 1 238 ? 29.359  -16.782 52.179  1.00 39.11  ? 238 LYS C O   1 
ATOM   10127 C CB  . LYS C 1 238 ? 30.696  -15.370 54.758  1.00 35.64  ? 238 LYS C CB  1 
ATOM   10128 C CG  . LYS C 1 238 ? 30.927  -14.029 55.441  1.00 34.47  ? 238 LYS C CG  1 
ATOM   10129 C CD  . LYS C 1 238 ? 32.271  -13.972 56.149  1.00 33.71  ? 238 LYS C CD  1 
ATOM   10130 C CE  . LYS C 1 238 ? 33.422  -14.008 55.159  1.00 36.52  ? 238 LYS C CE  1 
ATOM   10131 N NZ  . LYS C 1 238 ? 34.700  -14.359 55.837  1.00 52.22  ? 238 LYS C NZ  1 
ATOM   10132 N N   . GLU C 1 239 ? 28.845  -17.950 54.036  1.00 32.26  ? 239 GLU C N   1 
ATOM   10133 C CA  . GLU C 1 239 ? 28.607  -19.181 53.290  1.00 29.91  ? 239 GLU C CA  1 
ATOM   10134 C C   . GLU C 1 239 ? 27.388  -19.045 52.384  1.00 40.53  ? 239 GLU C C   1 
ATOM   10135 O O   . GLU C 1 239 ? 27.446  -19.365 51.191  1.00 36.63  ? 239 GLU C O   1 
ATOM   10136 C CB  . GLU C 1 239 ? 28.431  -20.355 54.254  1.00 32.12  ? 239 GLU C CB  1 
ATOM   10137 C CG  . GLU C 1 239 ? 29.483  -21.442 54.110  1.00 52.04  ? 239 GLU C CG  1 
ATOM   10138 C CD  . GLU C 1 239 ? 29.114  -22.718 54.844  1.00 62.02  ? 239 GLU C CD  1 
ATOM   10139 O OE1 . GLU C 1 239 ? 28.355  -22.644 55.834  1.00 47.34  ? 239 GLU C OE1 1 
ATOM   10140 O OE2 . GLU C 1 239 ? 29.582  -23.799 54.428  1.00 61.45  ? 239 GLU C OE2 1 
ATOM   10141 N N   . LYS C 1 240 ? 26.272  -18.561 52.938  1.00 36.99  ? 240 LYS C N   1 
ATOM   10142 C CA  . LYS C 1 240 ? 25.064  -18.387 52.138  1.00 33.63  ? 240 LYS C CA  1 
ATOM   10143 C C   . LYS C 1 240 ? 25.266  -17.345 51.044  1.00 33.62  ? 240 LYS C C   1 
ATOM   10144 O O   . LYS C 1 240 ? 24.662  -17.447 49.969  1.00 39.82  ? 240 LYS C O   1 
ATOM   10145 C CB  . LYS C 1 240 ? 23.889  -18.008 53.044  1.00 32.91  ? 240 LYS C CB  1 
ATOM   10146 C CG  . LYS C 1 240 ? 22.588  -17.698 52.315  1.00 31.84  ? 240 LYS C CG  1 
ATOM   10147 C CD  . LYS C 1 240 ? 22.124  -18.865 51.455  1.00 38.14  ? 240 LYS C CD  1 
ATOM   10148 C CE  . LYS C 1 240 ? 21.683  -20.044 52.303  1.00 42.47  ? 240 LYS C CE  1 
ATOM   10149 N NZ  . LYS C 1 240 ? 20.687  -20.893 51.591  1.00 35.83  ? 240 LYS C NZ  1 
ATOM   10150 N N   . TYR C 1 241 ? 26.109  -16.341 51.296  1.00 28.32  ? 241 TYR C N   1 
ATOM   10151 C CA  . TYR C 1 241 ? 26.462  -15.389 50.248  1.00 32.00  ? 241 TYR C CA  1 
ATOM   10152 C C   . TYR C 1 241 ? 27.252  -16.066 49.133  1.00 32.82  ? 241 TYR C C   1 
ATOM   10153 O O   . TYR C 1 241 ? 27.011  -15.806 47.948  1.00 34.57  ? 241 TYR C O   1 
ATOM   10154 C CB  . TYR C 1 241 ? 27.254  -14.228 50.850  1.00 35.57  ? 241 TYR C CB  1 
ATOM   10155 C CG  . TYR C 1 241 ? 27.398  -13.026 49.942  1.00 38.43  ? 241 TYR C CG  1 
ATOM   10156 C CD1 . TYR C 1 241 ? 26.458  -12.003 49.958  1.00 34.05  ? 241 TYR C CD1 1 
ATOM   10157 C CD2 . TYR C 1 241 ? 28.485  -12.904 49.082  1.00 31.19  ? 241 TYR C CD2 1 
ATOM   10158 C CE1 . TYR C 1 241 ? 26.590  -10.898 49.135  1.00 43.32  ? 241 TYR C CE1 1 
ATOM   10159 C CE2 . TYR C 1 241 ? 28.626  -11.802 48.257  1.00 27.93  ? 241 TYR C CE2 1 
ATOM   10160 C CZ  . TYR C 1 241 ? 27.676  -10.803 48.287  1.00 39.34  ? 241 TYR C CZ  1 
ATOM   10161 O OH  . TYR C 1 241 ? 27.812  -9.705  47.466  1.00 35.68  ? 241 TYR C OH  1 
ATOM   10162 N N   . PHE C 1 242 ? 28.195  -16.942 49.492  1.00 30.16  ? 242 PHE C N   1 
ATOM   10163 C CA  . PHE C 1 242 ? 28.964  -17.662 48.481  1.00 32.76  ? 242 PHE C CA  1 
ATOM   10164 C C   . PHE C 1 242 ? 28.083  -18.603 47.670  1.00 31.09  ? 242 PHE C C   1 
ATOM   10165 O O   . PHE C 1 242 ? 28.402  -18.917 46.519  1.00 32.73  ? 242 PHE C O   1 
ATOM   10166 C CB  . PHE C 1 242 ? 30.105  -18.439 49.142  1.00 30.74  ? 242 PHE C CB  1 
ATOM   10167 C CG  . PHE C 1 242 ? 31.168  -18.897 48.180  1.00 35.67  ? 242 PHE C CG  1 
ATOM   10168 C CD1 . PHE C 1 242 ? 31.052  -20.109 47.517  1.00 34.71  ? 242 PHE C CD1 1 
ATOM   10169 C CD2 . PHE C 1 242 ? 32.286  -18.115 47.939  1.00 45.57  ? 242 PHE C CD2 1 
ATOM   10170 C CE1 . PHE C 1 242 ? 32.031  -20.530 46.631  1.00 39.22  ? 242 PHE C CE1 1 
ATOM   10171 C CE2 . PHE C 1 242 ? 33.268  -18.531 47.055  1.00 44.54  ? 242 PHE C CE2 1 
ATOM   10172 C CZ  . PHE C 1 242 ? 33.140  -19.739 46.400  1.00 37.31  ? 242 PHE C CZ  1 
ATOM   10173 N N   . GLU C 1 243 ? 26.977  -19.068 48.250  1.00 35.67  ? 243 GLU C N   1 
ATOM   10174 C CA  . GLU C 1 243 ? 26.070  -19.951 47.529  1.00 36.99  ? 243 GLU C CA  1 
ATOM   10175 C C   . GLU C 1 243 ? 25.228  -19.219 46.491  1.00 37.11  ? 243 GLU C C   1 
ATOM   10176 O O   . GLU C 1 243 ? 24.791  -19.843 45.519  1.00 41.17  ? 243 GLU C O   1 
ATOM   10177 C CB  . GLU C 1 243 ? 25.153  -20.678 48.515  1.00 35.47  ? 243 GLU C CB  1 
ATOM   10178 C CG  . GLU C 1 243 ? 24.405  -21.854 47.910  1.00 52.00  ? 243 GLU C CG  1 
ATOM   10179 C CD  . GLU C 1 243 ? 23.393  -22.453 48.863  1.00 59.93  ? 243 GLU C CD  1 
ATOM   10180 O OE1 . GLU C 1 243 ? 23.036  -21.779 49.852  1.00 51.13  ? 243 GLU C OE1 1 
ATOM   10181 O OE2 . GLU C 1 243 ? 22.952  -23.596 48.619  1.00 66.00  ? 243 GLU C OE2 1 
ATOM   10182 N N   . ILE C 1 244 ? 24.999  -17.919 46.664  1.00 30.16  ? 244 ILE C N   1 
ATOM   10183 C CA  . ILE C 1 244 ? 24.083  -17.186 45.799  1.00 30.27  ? 244 ILE C CA  1 
ATOM   10184 C C   . ILE C 1 244 ? 24.869  -16.383 44.769  1.00 33.67  ? 244 ILE C C   1 
ATOM   10185 O O   . ILE C 1 244 ? 24.444  -16.249 43.615  1.00 40.79  ? 244 ILE C O   1 
ATOM   10186 C CB  . ILE C 1 244 ? 23.155  -16.278 46.628  1.00 30.71  ? 244 ILE C CB  1 
ATOM   10187 C CG1 . ILE C 1 244 ? 22.211  -17.138 47.475  1.00 31.68  ? 244 ILE C CG1 1 
ATOM   10188 C CG2 . ILE C 1 244 ? 22.369  -15.321 45.731  1.00 43.78  ? 244 ILE C CG2 1 
ATOM   10189 C CD1 . ILE C 1 244 ? 20.906  -17.486 46.785  1.00 53.15  ? 244 ILE C CD1 1 
ATOM   10190 N N   . PHE C 1 245 ? 26.029  -15.856 45.171  1.00 30.61  ? 245 PHE C N   1 
ATOM   10191 C CA  . PHE C 1 245 ? 26.834  -15.022 44.292  1.00 31.42  ? 245 PHE C CA  1 
ATOM   10192 C C   . PHE C 1 245 ? 28.231  -15.566 44.027  1.00 32.76  ? 245 PHE C C   1 
ATOM   10193 O O   . PHE C 1 245 ? 28.930  -15.023 43.162  1.00 33.86  ? 245 PHE C O   1 
ATOM   10194 C CB  . PHE C 1 245 ? 26.946  -13.599 44.862  1.00 29.96  ? 245 PHE C CB  1 
ATOM   10195 C CG  . PHE C 1 245 ? 25.617  -12.970 45.182  1.00 31.05  ? 245 PHE C CG  1 
ATOM   10196 C CD1 . PHE C 1 245 ? 24.772  -12.551 44.169  1.00 33.95  ? 245 PHE C CD1 1 
ATOM   10197 C CD2 . PHE C 1 245 ? 25.211  -12.806 46.496  1.00 32.68  ? 245 PHE C CD2 1 
ATOM   10198 C CE1 . PHE C 1 245 ? 23.547  -11.979 44.460  1.00 28.78  ? 245 PHE C CE1 1 
ATOM   10199 C CE2 . PHE C 1 245 ? 23.987  -12.234 46.792  1.00 26.29  ? 245 PHE C CE2 1 
ATOM   10200 C CZ  . PHE C 1 245 ? 23.155  -11.820 45.774  1.00 27.14  ? 245 PHE C CZ  1 
ATOM   10201 N N   . GLY C 1 246 ? 28.658  -16.609 44.737  1.00 42.22  ? 246 GLY C N   1 
ATOM   10202 C CA  . GLY C 1 246 ? 29.915  -17.269 44.433  1.00 39.78  ? 246 GLY C CA  1 
ATOM   10203 C C   . GLY C 1 246 ? 31.159  -16.444 44.665  1.00 43.56  ? 246 GLY C C   1 
ATOM   10204 O O   . GLY C 1 246 ? 32.203  -16.742 44.080  1.00 42.27  ? 246 GLY C O   1 
ATOM   10205 N N   . GLU C 1 247 ? 31.087  -15.406 45.501  1.00 46.00  ? 247 GLU C N   1 
ATOM   10206 C CA  . GLU C 1 247 ? 32.226  -14.514 45.693  1.00 47.07  ? 247 GLU C CA  1 
ATOM   10207 C C   . GLU C 1 247 ? 32.766  -14.529 47.117  1.00 36.88  ? 247 GLU C C   1 
ATOM   10208 O O   . GLU C 1 247 ? 33.944  -14.852 47.305  1.00 39.38  ? 247 GLU C O   1 
ATOM   10209 C CB  . GLU C 1 247 ? 31.834  -13.090 45.281  1.00 48.29  ? 247 GLU C CB  1 
ATOM   10210 C CG  . GLU C 1 247 ? 32.839  -12.427 44.363  1.00 49.56  ? 247 GLU C CG  1 
ATOM   10211 C CD  . GLU C 1 247 ? 32.559  -10.954 44.171  1.00 67.44  ? 247 GLU C CD  1 
ATOM   10212 O OE1 . GLU C 1 247 ? 31.389  -10.547 44.332  1.00 52.82  ? 247 GLU C OE1 1 
ATOM   10213 O OE2 . GLU C 1 247 ? 33.507  -10.204 43.858  1.00 95.24  ? 247 GLU C OE2 1 
ATOM   10214 N N   . HIS C 1 248 ? 31.921  -14.218 48.122  1.00 35.03  ? 248 HIS C N   1 
ATOM   10215 C CA  . HIS C 1 248 ? 32.170  -13.909 49.538  1.00 35.72  ? 248 HIS C CA  1 
ATOM   10216 C C   . HIS C 1 248 ? 32.003  -12.411 49.750  1.00 37.65  ? 248 HIS C C   1 
ATOM   10217 O O   . HIS C 1 248 ? 32.592  -11.613 49.009  1.00 43.94  ? 248 HIS C O   1 
ATOM   10218 C CB  . HIS C 1 248 ? 33.556  -14.339 50.024  1.00 31.49  ? 248 HIS C CB  1 
ATOM   10219 C CG  . HIS C 1 248 ? 33.570  -15.668 50.708  1.00 40.69  ? 248 HIS C CG  1 
ATOM   10220 N ND1 . HIS C 1 248 ? 34.638  -16.536 50.628  1.00 54.88  ? 248 HIS C ND1 1 
ATOM   10221 C CD2 . HIS C 1 248 ? 32.646  -16.278 51.487  1.00 38.95  ? 248 HIS C CD2 1 
ATOM   10222 C CE1 . HIS C 1 248 ? 34.370  -17.624 51.326  1.00 52.07  ? 248 HIS C CE1 1 
ATOM   10223 N NE2 . HIS C 1 248 ? 33.168  -17.493 51.858  1.00 50.77  ? 248 HIS C NE2 1 
ATOM   10224 N N   . PRO C 1 249 ? 31.233  -11.991 50.749  1.00 33.48  ? 249 PRO C N   1 
ATOM   10225 C CA  . PRO C 1 249 ? 30.939  -10.565 50.904  1.00 33.88  ? 249 PRO C CA  1 
ATOM   10226 C C   . PRO C 1 249 ? 32.060  -9.808  51.600  1.00 33.60  ? 249 PRO C C   1 
ATOM   10227 O O   . PRO C 1 249 ? 32.842  -10.364 52.377  1.00 29.01  ? 249 PRO C O   1 
ATOM   10228 C CB  . PRO C 1 249 ? 29.671  -10.563 51.763  1.00 26.20  ? 249 PRO C CB  1 
ATOM   10229 C CG  . PRO C 1 249 ? 29.800  -11.797 52.599  1.00 30.59  ? 249 PRO C CG  1 
ATOM   10230 C CD  . PRO C 1 249 ? 30.630  -12.797 51.822  1.00 34.77  ? 249 PRO C CD  1 
ATOM   10231 N N   . VAL C 1 250 ? 32.129  -8.512  51.292  1.00 27.93  ? 250 VAL C N   1 
ATOM   10232 C CA  . VAL C 1 250 ? 33.025  -7.589  51.980  1.00 25.06  ? 250 VAL C CA  1 
ATOM   10233 C C   . VAL C 1 250 ? 32.288  -6.363  52.502  1.00 24.05  ? 250 VAL C C   1 
ATOM   10234 O O   . VAL C 1 250 ? 32.891  -5.519  53.174  1.00 27.77  ? 250 VAL C O   1 
ATOM   10235 C CB  . VAL C 1 250 ? 34.197  -7.149  51.081  1.00 28.17  ? 250 VAL C CB  1 
ATOM   10236 C CG1 . VAL C 1 250 ? 35.071  -8.344  50.726  1.00 27.97  ? 250 VAL C CG1 1 
ATOM   10237 C CG2 . VAL C 1 250 ? 33.682  -6.454  49.828  1.00 33.01  ? 250 VAL C CG2 1 
ATOM   10238 N N   . TYR C 1 251 ? 31.002  -6.216  52.192  1.00 24.90  ? 251 TYR C N   1 
ATOM   10239 C CA  . TYR C 1 251 ? 30.149  -5.174  52.761  1.00 23.05  ? 251 TYR C CA  1 
ATOM   10240 C C   . TYR C 1 251 ? 29.026  -5.847  53.533  1.00 26.52  ? 251 TYR C C   1 
ATOM   10241 O O   . TYR C 1 251 ? 28.451  -6.837  53.072  1.00 25.43  ? 251 TYR C O   1 
ATOM   10242 C CB  . TYR C 1 251 ? 29.582  -4.251  51.668  1.00 28.95  ? 251 TYR C CB  1 
ATOM   10243 C CG  . TYR C 1 251 ? 30.613  -3.862  50.638  1.00 29.86  ? 251 TYR C CG  1 
ATOM   10244 C CD1 . TYR C 1 251 ? 31.697  -3.076  50.991  1.00 36.46  ? 251 TYR C CD1 1 
ATOM   10245 C CD2 . TYR C 1 251 ? 30.510  -4.286  49.319  1.00 31.62  ? 251 TYR C CD2 1 
ATOM   10246 C CE1 . TYR C 1 251 ? 32.653  -2.722  50.070  1.00 37.71  ? 251 TYR C CE1 1 
ATOM   10247 C CE2 . TYR C 1 251 ? 31.465  -3.935  48.383  1.00 43.92  ? 251 TYR C CE2 1 
ATOM   10248 C CZ  . TYR C 1 251 ? 32.536  -3.152  48.768  1.00 42.47  ? 251 TYR C CZ  1 
ATOM   10249 O OH  . TYR C 1 251 ? 33.502  -2.792  47.860  1.00 42.03  ? 251 TYR C OH  1 
ATOM   10250 N N   . MET C 1 252 ? 28.725  -5.311  54.709  1.00 31.17  ? 252 MET C N   1 
ATOM   10251 C CA  . MET C 1 252 ? 27.675  -5.853  55.557  1.00 27.35  ? 252 MET C CA  1 
ATOM   10252 C C   . MET C 1 252 ? 26.837  -4.713  56.110  1.00 22.44  ? 252 MET C C   1 
ATOM   10253 O O   . MET C 1 252 ? 27.323  -3.592  56.278  1.00 37.79  ? 252 MET C O   1 
ATOM   10254 C CB  . MET C 1 252 ? 28.245  -6.681  56.717  1.00 30.69  ? 252 MET C CB  1 
ATOM   10255 C CG  . MET C 1 252 ? 28.699  -8.079  56.344  1.00 44.70  ? 252 MET C CG  1 
ATOM   10256 S SD  . MET C 1 252 ? 28.328  -9.309  57.608  1.00 54.78  ? 252 MET C SD  1 
ATOM   10257 C CE  . MET C 1 252 ? 28.673  -10.823 56.715  1.00 30.21  ? 252 MET C CE  1 
ATOM   10258 N N   . TRP C 1 253 ? 25.573  -5.008  56.387  1.00 22.34  ? 253 TRP C N   1 
ATOM   10259 C CA  . TRP C 1 253 ? 24.715  -4.074  57.102  1.00 20.03  ? 253 TRP C CA  1 
ATOM   10260 C C   . TRP C 1 253 ? 24.429  -4.659  58.474  1.00 20.60  ? 253 TRP C C   1 
ATOM   10261 O O   . TRP C 1 253 ? 23.681  -5.644  58.572  1.00 28.74  ? 253 TRP C O   1 
ATOM   10262 C CB  . TRP C 1 253 ? 23.410  -3.819  56.345  1.00 18.49  ? 253 TRP C CB  1 
ATOM   10263 C CG  . TRP C 1 253 ? 22.358  -3.145  57.172  1.00 18.30  ? 253 TRP C CG  1 
ATOM   10264 C CD1 . TRP C 1 253 ? 21.218  -3.708  57.667  1.00 22.38  ? 253 TRP C CD1 1 
ATOM   10265 C CD2 . TRP C 1 253 ? 22.351  -1.780  57.606  1.00 20.69  ? 253 TRP C CD2 1 
ATOM   10266 N NE1 . TRP C 1 253 ? 20.499  -2.777  58.381  1.00 18.11  ? 253 TRP C NE1 1 
ATOM   10267 C CE2 . TRP C 1 253 ? 21.174  -1.585  58.358  1.00 18.59  ? 253 TRP C CE2 1 
ATOM   10268 C CE3 . TRP C 1 253 ? 23.226  -0.702  57.431  1.00 26.02  ? 253 TRP C CE3 1 
ATOM   10269 C CZ2 . TRP C 1 253 ? 20.851  -0.360  58.934  1.00 19.12  ? 253 TRP C CZ2 1 
ATOM   10270 C CZ3 . TRP C 1 253 ? 22.905  0.514   58.009  1.00 21.91  ? 253 TRP C CZ3 1 
ATOM   10271 C CH2 . TRP C 1 253 ? 21.727  0.675   58.750  1.00 19.74  ? 253 TRP C CH2 1 
ATOM   10272 N N   . PRO C 1 254 ? 25.011  -4.128  59.544  1.00 17.38  ? 254 PRO C N   1 
ATOM   10273 C CA  . PRO C 1 254 ? 24.726  -4.654  60.879  1.00 16.85  ? 254 PRO C CA  1 
ATOM   10274 C C   . PRO C 1 254 ? 23.255  -4.493  61.210  1.00 18.85  ? 254 PRO C C   1 
ATOM   10275 O O   . PRO C 1 254 ? 22.671  -3.424  60.971  1.00 17.37  ? 254 PRO C O   1 
ATOM   10276 C CB  . PRO C 1 254 ? 25.607  -3.795  61.797  1.00 20.91  ? 254 PRO C CB  1 
ATOM   10277 C CG  . PRO C 1 254 ? 25.861  -2.548  61.022  1.00 17.73  ? 254 PRO C CG  1 
ATOM   10278 C CD  . PRO C 1 254 ? 25.911  -2.964  59.584  1.00 18.99  ? 254 PRO C CD  1 
ATOM   10279 N N   . PRO C 1 255 ? 22.619  -5.516  61.725  1.00 19.26  ? 255 PRO C N   1 
ATOM   10280 C CA  . PRO C 1 255 ? 21.204  -5.448  62.010  1.00 21.14  ? 255 PRO C CA  1 
ATOM   10281 C C   . PRO C 1 255 ? 20.790  -4.336  62.907  1.00 21.47  ? 255 PRO C C   1 
ATOM   10282 O O   . PRO C 1 255 ? 21.366  -4.161  63.928  1.00 26.43  ? 255 PRO C O   1 
ATOM   10283 C CB  . PRO C 1 255 ? 20.935  -6.775  62.646  1.00 22.81  ? 255 PRO C CB  1 
ATOM   10284 C CG  . PRO C 1 255 ? 21.925  -7.648  62.049  1.00 21.54  ? 255 PRO C CG  1 
ATOM   10285 C CD  . PRO C 1 255 ? 23.144  -6.838  62.032  1.00 19.41  ? 255 PRO C CD  1 
ATOM   10286 N N   . GLU C 1 256 ? 19.776  -3.607  62.497  1.00 24.18  ? 256 GLU C N   1 
ATOM   10287 C CA  . GLU C 1 256 ? 19.266  -2.492  63.218  1.00 18.67  ? 256 GLU C CA  1 
ATOM   10288 C C   . GLU C 1 256 ? 20.325  -1.468  63.392  1.00 17.71  ? 256 GLU C C   1 
ATOM   10289 O O   . GLU C 1 256 ? 20.272  -0.705  64.279  1.00 18.46  ? 256 GLU C O   1 
ATOM   10290 C CB  . GLU C 1 256 ? 18.715  -2.923  64.551  1.00 27.53  ? 256 GLU C CB  1 
ATOM   10291 C CG  . GLU C 1 256 ? 17.670  -4.024  64.495  1.00 32.96  ? 256 GLU C CG  1 
ATOM   10292 C CD  . GLU C 1 256 ? 16.352  -3.589  63.902  1.00 36.38  ? 256 GLU C CD  1 
ATOM   10293 O OE1 . GLU C 1 256 ? 16.208  -2.429  63.578  1.00 31.33  ? 256 GLU C OE1 1 
ATOM   10294 O OE2 . GLU C 1 256 ? 15.462  -4.409  63.783  1.00 35.74  ? 256 GLU C OE2 1 
ATOM   10295 N N   . ALA C 1 257 ? 21.290  -1.489  62.508  1.00 17.69  ? 257 ALA C N   1 
ATOM   10296 C CA  . ALA C 1 257 ? 22.439  -0.607  62.507  1.00 21.12  ? 257 ALA C CA  1 
ATOM   10297 C C   . ALA C 1 257 ? 23.276  -0.747  63.770  1.00 23.66  ? 257 ALA C C   1 
ATOM   10298 O O   . ALA C 1 257 ? 24.053  0.091   64.084  1.00 22.82  ? 257 ALA C O   1 
ATOM   10299 C CB  . ALA C 1 257 ? 22.018  0.830   62.306  1.00 19.11  ? 257 ALA C CB  1 
ATOM   10300 N N   . SER C 1 258 ? 23.095  -1.837  64.472  1.00 20.09  ? 258 SER C N   1 
ATOM   10301 C CA  . SER C 1 258 ? 23.752  -2.081  65.748  1.00 17.27  ? 258 SER C CA  1 
ATOM   10302 C C   . SER C 1 258 ? 25.264  -2.081  65.582  1.00 17.50  ? 258 SER C C   1 
ATOM   10303 O O   . SER C 1 258 ? 25.813  -2.787  64.732  1.00 17.30  ? 258 SER C O   1 
ATOM   10304 C CB  . SER C 1 258 ? 23.286  -3.411  66.340  1.00 26.19  ? 258 SER C CB  1 
ATOM   10305 O OG  . SER C 1 258 ? 22.953  -3.269  67.710  1.00 24.99  ? 258 SER C OG  1 
ATOM   10306 N N   . VAL C 1 259 ? 25.936  -1.289  66.409  1.00 22.67  ? 259 VAL C N   1 
ATOM   10307 C CA  . VAL C 1 259 ? 27.376  -1.110  66.317  1.00 24.13  ? 259 VAL C CA  1 
ATOM   10308 C C   . VAL C 1 259 ? 27.944  -1.023  67.726  1.00 25.45  ? 259 VAL C C   1 
ATOM   10309 O O   . VAL C 1 259 ? 27.265  -0.608  68.670  1.00 24.13  ? 259 VAL C O   1 
ATOM   10310 C CB  . VAL C 1 259 ? 27.739  0.142   65.484  1.00 26.84  ? 259 VAL C CB  1 
ATOM   10311 C CG1 . VAL C 1 259 ? 27.686  1.393   66.337  1.00 26.43  ? 259 VAL C CG1 1 
ATOM   10312 C CG2 . VAL C 1 259 ? 29.103  -0.015  64.849  1.00 19.84  ? 259 VAL C CG2 1 
ATOM   10313 N N   . SER C 1 260 ? 29.195  -1.447  67.861  1.00 19.54  ? 260 SER C N   1 
ATOM   10314 C CA  . SER C 1 260 ? 29.922  -1.399  69.121  1.00 20.27  ? 260 SER C CA  1 
ATOM   10315 C C   . SER C 1 260 ? 31.390  -1.648  68.805  1.00 24.95  ? 260 SER C C   1 
ATOM   10316 O O   . SER C 1 260 ? 31.741  -2.067  67.699  1.00 34.81  ? 260 SER C O   1 
ATOM   10317 C CB  . SER C 1 260 ? 29.384  -2.419  70.128  1.00 24.24  ? 260 SER C CB  1 
ATOM   10318 O OG  . SER C 1 260 ? 29.728  -3.740  69.757  1.00 26.03  ? 260 SER C OG  1 
ATOM   10319 N N   . ASN C 1 261 ? 32.246  -1.375  69.791  1.00 27.79  ? 261 ASN C N   1 
ATOM   10320 C CA  . ASN C 1 261 ? 33.681  -1.537  69.579  1.00 24.58  ? 261 ASN C CA  1 
ATOM   10321 C C   . ASN C 1 261 ? 34.036  -2.984  69.265  1.00 34.06  ? 261 ASN C C   1 
ATOM   10322 O O   . ASN C 1 261 ? 34.846  -3.252  68.370  1.00 38.44  ? 261 ASN C O   1 
ATOM   10323 C CB  . ASN C 1 261 ? 34.446  -1.043  70.804  1.00 36.54  ? 261 ASN C CB  1 
ATOM   10324 C CG  . ASN C 1 261 ? 34.222  0.428   71.070  1.00 40.51  ? 261 ASN C CG  1 
ATOM   10325 O OD1 . ASN C 1 261 ? 34.888  1.278   70.491  1.00 41.91  ? 261 ASN C OD1 1 
ATOM   10326 N ND2 . ASN C 1 261 ? 33.271  0.736   71.945  1.00 43.61  ? 261 ASN C ND2 1 
ATOM   10327 N N   . GLU C 1 262 ? 33.432  -3.934  69.983  1.00 34.30  ? 262 GLU C N   1 
ATOM   10328 C CA  . GLU C 1 262 ? 33.725  -5.342  69.742  1.00 32.83  ? 262 GLU C CA  1 
ATOM   10329 C C   . GLU C 1 262 ? 33.053  -5.863  68.478  1.00 32.39  ? 262 GLU C C   1 
ATOM   10330 O O   . GLU C 1 262 ? 33.602  -6.749  67.814  1.00 41.82  ? 262 GLU C O   1 
ATOM   10331 C CB  . GLU C 1 262 ? 33.305  -6.182  70.947  1.00 39.74  ? 262 GLU C CB  1 
ATOM   10332 C CG  . GLU C 1 262 ? 34.245  -6.063  72.137  1.00 43.77  ? 262 GLU C CG  1 
ATOM   10333 C CD  . GLU C 1 262 ? 33.695  -5.161  73.229  1.00 50.39  ? 262 GLU C CD  1 
ATOM   10334 O OE1 . GLU C 1 262 ? 32.715  -4.431  72.969  1.00 51.40  ? 262 GLU C OE1 1 
ATOM   10335 O OE2 . GLU C 1 262 ? 34.241  -5.186  74.351  1.00 44.56  ? 262 GLU C OE2 1 
ATOM   10336 N N   . ALA C 1 263 ? 31.874  -5.340  68.134  1.00 25.45  ? 263 ALA C N   1 
ATOM   10337 C CA  . ALA C 1 263 ? 31.220  -5.741  66.891  1.00 24.34  ? 263 ALA C CA  1 
ATOM   10338 C C   . ALA C 1 263 ? 32.053  -5.341  65.681  1.00 26.53  ? 263 ALA C C   1 
ATOM   10339 O O   . ALA C 1 263 ? 32.289  -6.153  64.776  1.00 26.28  ? 263 ALA C O   1 
ATOM   10340 C CB  . ALA C 1 263 ? 29.820  -5.131  66.812  1.00 18.90  ? 263 ALA C CB  1 
ATOM   10341 N N   . LEU C 1 264 ? 32.519  -4.089  65.655  1.00 21.31  ? 264 LEU C N   1 
ATOM   10342 C CA  . LEU C 1 264 ? 33.368  -3.633  64.560  1.00 20.21  ? 264 LEU C CA  1 
ATOM   10343 C C   . LEU C 1 264 ? 34.646  -4.452  64.463  1.00 23.23  ? 264 LEU C C   1 
ATOM   10344 O O   . LEU C 1 264 ? 35.202  -4.610  63.370  1.00 28.53  ? 264 LEU C O   1 
ATOM   10345 C CB  . LEU C 1 264 ? 33.696  -2.151  64.731  1.00 20.44  ? 264 LEU C CB  1 
ATOM   10346 C CG  . LEU C 1 264 ? 32.487  -1.229  64.604  1.00 19.83  ? 264 LEU C CG  1 
ATOM   10347 C CD1 . LEU C 1 264 ? 32.818  0.188   65.047  1.00 20.93  ? 264 LEU C CD1 1 
ATOM   10348 C CD2 . LEU C 1 264 ? 31.988  -1.248  63.172  1.00 19.77  ? 264 LEU C CD2 1 
ATOM   10349 N N   . GLU C 1 265 ? 35.131  -4.976  65.589  1.00 29.36  ? 265 GLU C N   1 
ATOM   10350 C CA  . GLU C 1 265 ? 36.243  -5.918  65.538  1.00 32.25  ? 265 GLU C CA  1 
ATOM   10351 C C   . GLU C 1 265 ? 35.818  -7.222  64.874  1.00 29.44  ? 265 GLU C C   1 
ATOM   10352 O O   . GLU C 1 265 ? 36.490  -7.709  63.958  1.00 33.62  ? 265 GLU C O   1 
ATOM   10353 C CB  . GLU C 1 265 ? 36.778  -6.177  66.948  1.00 23.80  ? 265 GLU C CB  1 
ATOM   10354 C CG  . GLU C 1 265 ? 37.404  -4.953  67.600  1.00 32.04  ? 265 GLU C CG  1 
ATOM   10355 C CD  . GLU C 1 265 ? 37.797  -5.191  69.047  1.00 49.13  ? 265 GLU C CD  1 
ATOM   10356 O OE1 . GLU C 1 265 ? 37.226  -6.103  69.682  1.00 54.42  ? 265 GLU C OE1 1 
ATOM   10357 O OE2 . GLU C 1 265 ? 38.673  -4.458  69.552  1.00 45.38  ? 265 GLU C OE2 1 
ATOM   10358 N N   . LEU C 1 266 ? 34.681  -7.781  65.301  1.00 28.77  ? 266 LEU C N   1 
ATOM   10359 C CA  . LEU C 1 266 ? 34.234  -9.072  64.782  1.00 25.82  ? 266 LEU C CA  1 
ATOM   10360 C C   . LEU C 1 266 ? 34.016  -9.025  63.276  1.00 28.99  ? 266 LEU C C   1 
ATOM   10361 O O   . LEU C 1 266 ? 34.396  -9.958  62.557  1.00 29.61  ? 266 LEU C O   1 
ATOM   10362 C CB  . LEU C 1 266 ? 32.950  -9.505  65.491  1.00 25.13  ? 266 LEU C CB  1 
ATOM   10363 C CG  . LEU C 1 266 ? 32.386  -10.877 65.110  1.00 23.56  ? 266 LEU C CG  1 
ATOM   10364 C CD1 . LEU C 1 266 ? 32.849  -11.953 66.083  1.00 34.61  ? 266 LEU C CD1 1 
ATOM   10365 C CD2 . LEU C 1 266 ? 30.867  -10.828 65.044  1.00 23.91  ? 266 LEU C CD2 1 
ATOM   10366 N N   . TYR C 1 267 ? 33.397  -7.954  62.780  1.00 28.34  ? 267 TYR C N   1 
ATOM   10367 C CA  . TYR C 1 267 ? 33.210  -7.817  61.341  1.00 25.93  ? 267 TYR C CA  1 
ATOM   10368 C C   . TYR C 1 267 ? 34.550  -7.724  60.622  1.00 27.79  ? 267 TYR C C   1 
ATOM   10369 O O   . TYR C 1 267 ? 34.733  -8.320  59.554  1.00 29.59  ? 267 TYR C O   1 
ATOM   10370 C CB  . TYR C 1 267 ? 32.339  -6.596  61.043  1.00 25.86  ? 267 TYR C CB  1 
ATOM   10371 C CG  . TYR C 1 267 ? 30.904  -6.766  61.489  1.00 21.00  ? 267 TYR C CG  1 
ATOM   10372 C CD1 . TYR C 1 267 ? 30.140  -7.833  61.037  1.00 24.59  ? 267 TYR C CD1 1 
ATOM   10373 C CD2 . TYR C 1 267 ? 30.318  -5.868  62.374  1.00 19.32  ? 267 TYR C CD2 1 
ATOM   10374 C CE1 . TYR C 1 267 ? 28.830  -8.000  61.446  1.00 26.87  ? 267 TYR C CE1 1 
ATOM   10375 C CE2 . TYR C 1 267 ? 29.006  -6.028  62.788  1.00 18.88  ? 267 TYR C CE2 1 
ATOM   10376 C CZ  . TYR C 1 267 ? 28.269  -7.095  62.321  1.00 24.56  ? 267 TYR C CZ  1 
ATOM   10377 O OH  . TYR C 1 267 ? 26.965  -7.259  62.728  1.00 36.98  ? 267 TYR C OH  1 
ATOM   10378 N N   . TYR C 1 268 ? 35.504  -6.990  61.200  1.00 31.57  ? 268 TYR C N   1 
ATOM   10379 C CA  . TYR C 1 268 ? 36.829  -6.893  60.595  1.00 30.12  ? 268 TYR C CA  1 
ATOM   10380 C C   . TYR C 1 268 ? 37.549  -8.237  60.611  1.00 30.59  ? 268 TYR C C   1 
ATOM   10381 O O   . TYR C 1 268 ? 38.275  -8.568  59.666  1.00 33.25  ? 268 TYR C O   1 
ATOM   10382 C CB  . TYR C 1 268 ? 37.661  -5.829  61.311  1.00 31.32  ? 268 TYR C CB  1 
ATOM   10383 C CG  . TYR C 1 268 ? 39.149  -6.054  61.188  1.00 28.72  ? 268 TYR C CG  1 
ATOM   10384 C CD1 . TYR C 1 268 ? 39.823  -5.729  60.019  1.00 27.22  ? 268 TYR C CD1 1 
ATOM   10385 C CD2 . TYR C 1 268 ? 39.879  -6.596  62.238  1.00 33.02  ? 268 TYR C CD2 1 
ATOM   10386 C CE1 . TYR C 1 268 ? 41.183  -5.936  59.899  1.00 28.97  ? 268 TYR C CE1 1 
ATOM   10387 C CE2 . TYR C 1 268 ? 41.239  -6.807  62.126  1.00 30.71  ? 268 TYR C CE2 1 
ATOM   10388 C CZ  . TYR C 1 268 ? 41.886  -6.475  60.954  1.00 33.29  ? 268 TYR C CZ  1 
ATOM   10389 O OH  . TYR C 1 268 ? 43.242  -6.681  60.836  1.00 37.67  ? 268 TYR C OH  1 
ATOM   10390 N N   . GLU C 1 269 ? 37.368  -9.022  61.678  1.00 34.15  ? 269 GLU C N   1 
ATOM   10391 C CA  . GLU C 1 269 ? 38.005  -10.336 61.752  1.00 33.43  ? 269 GLU C CA  1 
ATOM   10392 C C   . GLU C 1 269 ? 37.539  -11.275 60.649  1.00 34.35  ? 269 GLU C C   1 
ATOM   10393 O O   . GLU C 1 269 ? 38.258  -12.220 60.309  1.00 33.24  ? 269 GLU C O   1 
ATOM   10394 C CB  . GLU C 1 269 ? 37.731  -10.991 63.107  1.00 38.46  ? 269 GLU C CB  1 
ATOM   10395 C CG  . GLU C 1 269 ? 38.170  -10.193 64.318  1.00 51.01  ? 269 GLU C CG  1 
ATOM   10396 C CD  . GLU C 1 269 ? 37.821  -10.885 65.621  1.00 60.57  ? 269 GLU C CD  1 
ATOM   10397 O OE1 . GLU C 1 269 ? 37.517  -12.097 65.591  1.00 65.10  ? 269 GLU C OE1 1 
ATOM   10398 O OE2 . GLU C 1 269 ? 37.829  -10.211 66.672  1.00 55.66  ? 269 GLU C OE2 1 
ATOM   10399 N N   . LYS C 1 270 ? 36.356  -11.041 60.085  1.00 29.78  ? 270 LYS C N   1 
ATOM   10400 C CA  . LYS C 1 270 ? 35.756  -11.945 59.116  1.00 31.58  ? 270 LYS C CA  1 
ATOM   10401 C C   . LYS C 1 270 ? 35.914  -11.468 57.678  1.00 36.09  ? 270 LYS C C   1 
ATOM   10402 O O   . LYS C 1 270 ? 35.306  -12.050 56.774  1.00 29.77  ? 270 LYS C O   1 
ATOM   10403 C CB  . LYS C 1 270 ? 34.275  -12.148 59.446  1.00 37.40  ? 270 LYS C CB  1 
ATOM   10404 C CG  . LYS C 1 270 ? 34.041  -12.681 60.851  1.00 33.16  ? 270 LYS C CG  1 
ATOM   10405 C CD  . LYS C 1 270 ? 34.153  -14.194 60.885  1.00 27.07  ? 270 LYS C CD  1 
ATOM   10406 C CE  . LYS C 1 270 ? 34.405  -14.700 62.296  1.00 27.39  ? 270 LYS C CE  1 
ATOM   10407 N NZ  . LYS C 1 270 ? 35.560  -15.639 62.353  1.00 34.48  ? 270 LYS C NZ  1 
ATOM   10408 N N   . GLY C 1 271 ? 36.709  -10.428 57.446  1.00 39.25  ? 271 GLY C N   1 
ATOM   10409 C CA  . GLY C 1 271 ? 36.982  -9.958  56.103  1.00 34.80  ? 271 GLY C CA  1 
ATOM   10410 C C   . GLY C 1 271 ? 36.112  -8.826  55.604  1.00 28.84  ? 271 GLY C C   1 
ATOM   10411 O O   . GLY C 1 271 ? 36.178  -8.502  54.411  1.00 28.22  ? 271 GLY C O   1 
ATOM   10412 N N   . ILE C 1 272 ? 35.302  -8.219  56.465  1.00 25.73  ? 272 ILE C N   1 
ATOM   10413 C CA  . ILE C 1 272 ? 34.441  -7.115  56.054  1.00 25.78  ? 272 ILE C CA  1 
ATOM   10414 C C   . ILE C 1 272 ? 35.265  -5.836  55.994  1.00 26.36  ? 272 ILE C C   1 
ATOM   10415 O O   . ILE C 1 272 ? 35.960  -5.484  56.955  1.00 34.96  ? 272 ILE C O   1 
ATOM   10416 C CB  . ILE C 1 272 ? 33.250  -6.967  57.013  1.00 23.42  ? 272 ILE C CB  1 
ATOM   10417 C CG1 . ILE C 1 272 ? 32.562  -8.318  57.203  1.00 23.47  ? 272 ILE C CG1 1 
ATOM   10418 C CG2 . ILE C 1 272 ? 32.269  -5.928  56.496  1.00 22.91  ? 272 ILE C CG2 1 
ATOM   10419 C CD1 . ILE C 1 272 ? 32.096  -8.949  55.911  1.00 24.47  ? 272 ILE C CD1 1 
ATOM   10420 N N   . ASN C 1 273 ? 35.190  -5.137  54.860  1.00 32.23  ? 273 ASN C N   1 
ATOM   10421 C CA  . ASN C 1 273 ? 35.943  -3.905  54.664  1.00 38.20  ? 273 ASN C CA  1 
ATOM   10422 C C   . ASN C 1 273 ? 35.131  -2.647  54.937  1.00 32.38  ? 273 ASN C C   1 
ATOM   10423 O O   . ASN C 1 273 ? 35.727  -1.589  55.174  1.00 29.66  ? 273 ASN C O   1 
ATOM   10424 C CB  . ASN C 1 273 ? 36.493  -3.834  53.233  1.00 28.24  ? 273 ASN C CB  1 
ATOM   10425 C CG  . ASN C 1 273 ? 37.292  -5.065  52.854  1.00 33.34  ? 273 ASN C CG  1 
ATOM   10426 O OD1 . ASN C 1 273 ? 37.890  -5.718  53.708  1.00 37.66  ? 273 ASN C OD1 1 
ATOM   10427 N ND2 . ASN C 1 273 ? 37.310  -5.385  51.565  1.00 41.08  ? 273 ASN C ND2 1 
ATOM   10428 N N   . MET C 1 274 ? 33.802  -2.730  54.914  1.00 24.65  ? 274 MET C N   1 
ATOM   10429 C CA  . MET C 1 274 ? 32.973  -1.545  55.077  1.00 24.11  ? 274 MET C CA  1 
ATOM   10430 C C   . MET C 1 274 ? 31.614  -1.947  55.630  1.00 25.73  ? 274 MET C C   1 
ATOM   10431 O O   . MET C 1 274 ? 31.138  -3.060  55.392  1.00 27.47  ? 274 MET C O   1 
ATOM   10432 C CB  . MET C 1 274 ? 32.809  -0.793  53.751  1.00 34.42  ? 274 MET C CB  1 
ATOM   10433 C CG  . MET C 1 274 ? 32.221  0.601   53.886  1.00 31.21  ? 274 MET C CG  1 
ATOM   10434 S SD  . MET C 1 274 ? 30.427  0.600   53.714  1.00 40.63  ? 274 MET C SD  1 
ATOM   10435 C CE  . MET C 1 274 ? 30.249  0.075   52.011  1.00 26.23  ? 274 MET C CE  1 
ATOM   10436 N N   . LEU C 1 275 ? 30.997  -1.022  56.365  1.00 24.54  ? 275 LEU C N   1 
ATOM   10437 C CA  . LEU C 1 275 ? 29.655  -1.209  56.905  1.00 24.34  ? 275 LEU C CA  1 
ATOM   10438 C C   . LEU C 1 275 ? 29.099  0.155   57.296  1.00 25.82  ? 275 LEU C C   1 
ATOM   10439 O O   . LEU C 1 275 ? 29.817  1.158   57.307  1.00 26.54  ? 275 LEU C O   1 
ATOM   10440 C CB  . LEU C 1 275 ? 29.656  -2.187  58.087  1.00 20.56  ? 275 LEU C CB  1 
ATOM   10441 C CG  . LEU C 1 275 ? 30.006  -1.699  59.491  1.00 21.28  ? 275 LEU C CG  1 
ATOM   10442 C CD1 . LEU C 1 275 ? 29.817  -2.831  60.488  1.00 25.81  ? 275 LEU C CD1 1 
ATOM   10443 C CD2 . LEU C 1 275 ? 31.427  -1.171  59.553  1.00 28.78  ? 275 LEU C CD2 1 
ATOM   10444 N N   . ALA C 1 276 ? 27.804  0.183   57.615  1.00 22.11  ? 276 ALA C N   1 
ATOM   10445 C CA  . ALA C 1 276 ? 27.094  1.434   57.846  1.00 23.44  ? 276 ALA C CA  1 
ATOM   10446 C C   . ALA C 1 276 ? 26.279  1.368   59.131  1.00 20.92  ? 276 ALA C C   1 
ATOM   10447 O O   . ALA C 1 276 ? 25.899  0.293   59.600  1.00 26.90  ? 276 ALA C O   1 
ATOM   10448 C CB  . ALA C 1 276 ? 26.171  1.785   56.673  1.00 27.33  ? 276 ALA C CB  1 
ATOM   10449 N N   . THR C 1 277 ? 26.008  2.546   59.690  1.00 20.58  ? 277 THR C N   1 
ATOM   10450 C CA  . THR C 1 277 ? 25.239  2.681   60.922  1.00 25.86  ? 277 THR C CA  1 
ATOM   10451 C C   . THR C 1 277 ? 24.614  4.075   60.952  1.00 22.57  ? 277 THR C C   1 
ATOM   10452 O O   . THR C 1 277 ? 24.755  4.858   60.008  1.00 21.98  ? 277 THR C O   1 
ATOM   10453 C CB  . THR C 1 277 ? 26.117  2.406   62.149  1.00 24.28  ? 277 THR C CB  1 
ATOM   10454 O OG1 . THR C 1 277 ? 25.457  2.866   63.335  1.00 27.66  ? 277 THR C OG1 1 
ATOM   10455 C CG2 . THR C 1 277 ? 27.463  3.088   62.005  1.00 20.13  ? 277 THR C CG2 1 
ATOM   10456 N N   . ASP C 1 278 ? 23.920  4.383   62.045  1.00 21.09  ? 278 ASP C N   1 
ATOM   10457 C CA  . ASP C 1 278 ? 23.027  5.532   62.085  1.00 23.47  ? 278 ASP C CA  1 
ATOM   10458 C C   . ASP C 1 278 ? 23.737  6.816   62.506  1.00 37.93  ? 278 ASP C C   1 
ATOM   10459 O O   . ASP C 1 278 ? 24.796  6.804   63.137  1.00 36.64  ? 278 ASP C O   1 
ATOM   10460 C CB  . ASP C 1 278 ? 21.855  5.273   63.032  1.00 29.31  ? 278 ASP C CB  1 
ATOM   10461 C CG  . ASP C 1 278 ? 20.781  6.347   62.940  1.00 35.97  ? 278 ASP C CG  1 
ATOM   10462 O OD1 . ASP C 1 278 ? 20.399  6.717   61.807  1.00 28.54  ? 278 ASP C OD1 1 
ATOM   10463 O OD2 . ASP C 1 278 ? 20.328  6.832   63.999  1.00 28.58  ? 278 ASP C OD2 1 
ATOM   10464 N N   . GLU C 1 279 ? 23.101  7.939   62.157  1.00 37.13  ? 279 GLU C N   1 
ATOM   10465 C CA  . GLU C 1 279 ? 23.611  9.261   62.507  1.00 28.06  ? 279 GLU C CA  1 
ATOM   10466 C C   . GLU C 1 279 ? 23.601  9.491   64.016  1.00 36.87  ? 279 GLU C C   1 
ATOM   10467 O O   . GLU C 1 279 ? 24.495  10.156  64.553  1.00 46.77  ? 279 GLU C O   1 
ATOM   10468 C CB  . GLU C 1 279 ? 22.778  10.326  61.791  1.00 34.81  ? 279 GLU C CB  1 
ATOM   10469 C CG  . GLU C 1 279 ? 23.076  11.763  62.182  1.00 50.99  ? 279 GLU C CG  1 
ATOM   10470 C CD  . GLU C 1 279 ? 22.902  12.724  61.022  1.00 43.04  ? 279 GLU C CD  1 
ATOM   10471 O OE1 . GLU C 1 279 ? 22.240  12.349  60.030  1.00 38.18  ? 279 GLU C OE1 1 
ATOM   10472 O OE2 . GLU C 1 279 ? 23.416  13.860  61.109  1.00 34.24  ? 279 GLU C OE2 1 
ATOM   10473 N N   . VAL C 1 280 ? 22.592  8.965   64.718  1.00 39.53  ? 280 VAL C N   1 
ATOM   10474 C CA  . VAL C 1 280 ? 22.497  9.204   66.156  1.00 30.43  ? 280 VAL C CA  1 
ATOM   10475 C C   . VAL C 1 280 ? 23.580  8.460   66.930  1.00 24.52  ? 280 VAL C C   1 
ATOM   10476 O O   . VAL C 1 280 ? 23.928  8.867   68.044  1.00 26.18  ? 280 VAL C O   1 
ATOM   10477 C CB  . VAL C 1 280 ? 21.096  8.839   66.688  1.00 25.70  ? 280 VAL C CB  1 
ATOM   10478 C CG1 . VAL C 1 280 ? 21.021  7.370   67.077  1.00 25.34  ? 280 VAL C CG1 1 
ATOM   10479 C CG2 . VAL C 1 280 ? 20.738  9.724   67.873  1.00 27.14  ? 280 VAL C CG2 1 
ATOM   10480 N N   . ILE C 1 281 ? 24.118  7.372   66.378  1.00 28.69  ? 281 ILE C N   1 
ATOM   10481 C CA  . ILE C 1 281 ? 25.275  6.732   66.996  1.00 24.83  ? 281 ILE C CA  1 
ATOM   10482 C C   . ILE C 1 281 ? 26.514  7.601   66.821  1.00 23.40  ? 281 ILE C C   1 
ATOM   10483 O O   . ILE C 1 281 ? 27.317  7.758   67.749  1.00 24.57  ? 281 ILE C O   1 
ATOM   10484 C CB  . ILE C 1 281 ? 25.474  5.320   66.418  1.00 30.34  ? 281 ILE C CB  1 
ATOM   10485 C CG1 . ILE C 1 281 ? 24.505  4.342   67.087  1.00 26.55  ? 281 ILE C CG1 1 
ATOM   10486 C CG2 . ILE C 1 281 ? 26.916  4.864   66.594  1.00 26.49  ? 281 ILE C CG2 1 
ATOM   10487 C CD1 . ILE C 1 281 ? 24.458  2.986   66.434  1.00 23.13  ? 281 ILE C CD1 1 
ATOM   10488 N N   . LEU C 1 282 ? 26.680  8.187   65.631  1.00 27.95  ? 282 LEU C N   1 
ATOM   10489 C CA  . LEU C 1 282 ? 27.775  9.124   65.398  1.00 28.76  ? 282 LEU C CA  1 
ATOM   10490 C C   . LEU C 1 282 ? 27.728  10.298  66.365  1.00 35.33  ? 282 LEU C C   1 
ATOM   10491 O O   . LEU C 1 282 ? 28.777  10.821  66.759  1.00 37.47  ? 282 LEU C O   1 
ATOM   10492 C CB  . LEU C 1 282 ? 27.727  9.627   63.954  1.00 25.51  ? 282 LEU C CB  1 
ATOM   10493 C CG  . LEU C 1 282 ? 28.861  10.536  63.476  1.00 31.28  ? 282 LEU C CG  1 
ATOM   10494 C CD1 . LEU C 1 282 ? 30.119  9.729   63.199  1.00 26.26  ? 282 LEU C CD1 1 
ATOM   10495 C CD2 . LEU C 1 282 ? 28.439  11.316  62.240  1.00 34.28  ? 282 LEU C CD2 1 
ATOM   10496 N N   . LYS C 1 283 ? 26.525  10.726  66.754  1.00 35.58  ? 283 LYS C N   1 
ATOM   10497 C CA  . LYS C 1 283 ? 26.397  11.850  67.675  1.00 28.52  ? 283 LYS C CA  1 
ATOM   10498 C C   . LYS C 1 283 ? 26.994  11.522  69.038  1.00 28.51  ? 283 LYS C C   1 
ATOM   10499 O O   . LYS C 1 283 ? 27.629  12.376  69.666  1.00 29.99  ? 283 LYS C O   1 
ATOM   10500 C CB  . LYS C 1 283 ? 24.928  12.249  67.809  1.00 32.04  ? 283 LYS C CB  1 
ATOM   10501 C CG  . LYS C 1 283 ? 24.568  13.534  67.081  1.00 48.06  ? 283 LYS C CG  1 
ATOM   10502 C CD  . LYS C 1 283 ? 23.271  14.128  67.605  1.00 42.60  ? 283 LYS C CD  1 
ATOM   10503 C CE  . LYS C 1 283 ? 22.216  14.198  66.511  1.00 51.07  ? 283 LYS C CE  1 
ATOM   10504 N NZ  . LYS C 1 283 ? 20.864  14.485  67.062  1.00 47.22  ? 283 LYS C NZ  1 
ATOM   10505 N N   . ASN C 1 284 ? 26.809  10.290  69.509  1.00 27.09  ? 284 ASN C N   1 
ATOM   10506 C CA  . ASN C 1 284 ? 27.321  9.881   70.811  1.00 27.23  ? 284 ASN C CA  1 
ATOM   10507 C C   . ASN C 1 284 ? 28.780  9.443   70.773  1.00 34.91  ? 284 ASN C C   1 
ATOM   10508 O O   . ASN C 1 284 ? 29.304  9.025   71.811  1.00 36.11  ? 284 ASN C O   1 
ATOM   10509 C CB  . ASN C 1 284 ? 26.473  8.741   71.389  1.00 26.18  ? 284 ASN C CB  1 
ATOM   10510 C CG  . ASN C 1 284 ? 24.984  8.961   71.204  1.00 26.36  ? 284 ASN C CG  1 
ATOM   10511 O OD1 . ASN C 1 284 ? 24.507  10.095  71.215  1.00 32.06  ? 284 ASN C OD1 1 
ATOM   10512 N ND2 . ASN C 1 284 ? 24.239  7.872   71.042  1.00 25.21  ? 284 ASN C ND2 1 
ATOM   10513 N N   . SER C 1 285 ? 29.447  9.523   69.622  1.00 32.99  ? 285 SER C N   1 
ATOM   10514 C CA  . SER C 1 285 ? 30.790  8.977   69.475  1.00 28.02  ? 285 SER C CA  1 
ATOM   10515 C C   . SER C 1 285 ? 31.850  9.993   69.073  1.00 34.99  ? 285 SER C C   1 
ATOM   10516 O O   . SER C 1 285 ? 33.016  9.808   69.430  1.00 45.89  ? 285 SER C O   1 
ATOM   10517 C CB  . SER C 1 285 ? 30.785  7.834   68.448  1.00 35.06  ? 285 SER C CB  1 
ATOM   10518 O OG  . SER C 1 285 ? 29.667  6.983   68.646  1.00 37.18  ? 285 SER C OG  1 
ATOM   10519 N N   . VAL C 1 286 ? 31.493  11.047  68.338  1.00 42.12  ? 286 VAL C N   1 
ATOM   10520 C CA  . VAL C 1 286 ? 32.431  12.101  67.976  1.00 36.03  ? 286 VAL C CA  1 
ATOM   10521 C C   . VAL C 1 286 ? 31.804  13.448  68.308  1.00 38.52  ? 286 VAL C C   1 
ATOM   10522 O O   . VAL C 1 286 ? 30.583  13.587  68.406  1.00 53.03  ? 286 VAL C O   1 
ATOM   10523 C CB  . VAL C 1 286 ? 32.838  12.053  66.487  1.00 39.86  ? 286 VAL C CB  1 
ATOM   10524 C CG1 . VAL C 1 286 ? 33.787  10.891  66.230  1.00 49.98  ? 286 VAL C CG1 1 
ATOM   10525 C CG2 . VAL C 1 286 ? 31.609  11.960  65.602  1.00 39.95  ? 286 VAL C CG2 1 
ATOM   10526 N N   . GLU C 1 287 ? 32.665  14.453  68.485  1.00 34.41  ? 287 GLU C N   1 
ATOM   10527 C CA  . GLU C 1 287 ? 32.176  15.780  68.845  1.00 50.97  ? 287 GLU C CA  1 
ATOM   10528 C C   . GLU C 1 287 ? 31.687  16.554  67.626  1.00 53.75  ? 287 GLU C C   1 
ATOM   10529 O O   . GLU C 1 287 ? 30.618  17.173  67.670  1.00 52.16  ? 287 GLU C O   1 
ATOM   10530 C CB  . GLU C 1 287 ? 33.265  16.570  69.572  1.00 44.32  ? 287 GLU C CB  1 
ATOM   10531 C CG  . GLU C 1 287 ? 32.784  17.910  70.107  1.00 48.61  ? 287 GLU C CG  1 
ATOM   10532 C CD  . GLU C 1 287 ? 33.886  18.947  70.183  1.00 70.60  ? 287 GLU C CD  1 
ATOM   10533 O OE1 . GLU C 1 287 ? 34.783  18.933  69.314  1.00 82.18  ? 287 GLU C OE1 1 
ATOM   10534 O OE2 . GLU C 1 287 ? 33.851  19.783  71.111  1.00 83.57  ? 287 GLU C OE2 1 
ATOM   10535 N N   . ARG C 1 288 ? 32.449  16.532  66.532  1.00 53.33  ? 288 ARG C N   1 
ATOM   10536 C CA  . ARG C 1 288 ? 32.084  17.247  65.309  1.00 52.73  ? 288 ARG C CA  1 
ATOM   10537 C C   . ARG C 1 288 ? 31.393  16.260  64.371  1.00 45.60  ? 288 ARG C C   1 
ATOM   10538 O O   . ARG C 1 288 ? 31.967  15.766  63.402  1.00 41.72  ? 288 ARG C O   1 
ATOM   10539 C CB  . ARG C 1 288 ? 33.316  17.881  64.674  1.00 54.50  ? 288 ARG C CB  1 
ATOM   10540 C CG  . ARG C 1 288 ? 33.959  18.958  65.532  1.00 60.40  ? 288 ARG C CG  1 
ATOM   10541 C CD  . ARG C 1 288 ? 33.454  20.338  65.148  1.00 69.02  ? 288 ARG C CD  1 
ATOM   10542 N NE  . ARG C 1 288 ? 34.195  20.906  64.027  1.00 81.16  ? 288 ARG C NE  1 
ATOM   10543 C CZ  . ARG C 1 288 ? 35.476  21.249  64.060  1.00 82.98  ? 288 ARG C CZ  1 
ATOM   10544 N NH1 . ARG C 1 288 ? 36.199  21.129  65.164  1.00 74.02  ? 288 ARG C NH1 1 
ATOM   10545 N NH2 . ARG C 1 288 ? 36.045  21.732  62.960  1.00 85.05  ? 288 ARG C NH2 1 
ATOM   10546 N N   . ALA C 1 289 ? 30.122  15.986  64.671  1.00 59.50  ? 289 ALA C N   1 
ATOM   10547 C CA  . ALA C 1 289 ? 29.371  14.915  64.016  1.00 61.30  ? 289 ALA C CA  1 
ATOM   10548 C C   . ALA C 1 289 ? 28.977  15.336  62.603  1.00 61.28  ? 289 ALA C C   1 
ATOM   10549 O O   . ALA C 1 289 ? 27.869  15.814  62.341  1.00 73.45  ? 289 ALA C O   1 
ATOM   10550 C CB  . ALA C 1 289 ? 28.148  14.536  64.843  1.00 49.27  ? 289 ALA C CB  1 
ATOM   10551 N N   . SER C 1 290 ? 29.912  15.139  61.671  1.00 49.01  ? 290 SER C N   1 
ATOM   10552 C CA  . SER C 1 290 ? 29.623  15.267  60.250  1.00 58.91  ? 290 SER C CA  1 
ATOM   10553 C C   . SER C 1 290 ? 29.432  13.878  59.664  1.00 43.63  ? 290 SER C C   1 
ATOM   10554 O O   . SER C 1 290 ? 30.365  13.062  59.721  1.00 40.57  ? 290 SER C O   1 
ATOM   10555 C CB  . SER C 1 290 ? 30.751  15.996  59.528  1.00 64.91  ? 290 SER C CB  1 
ATOM   10556 O OG  . SER C 1 290 ? 30.730  17.385  59.808  1.00 59.26  ? 290 SER C OG  1 
ATOM   10557 N N   . PRO C 1 291 ? 28.256  13.544  59.136  1.00 32.60  ? 291 PRO C N   1 
ATOM   10558 C CA  . PRO C 1 291 ? 28.022  12.196  58.598  1.00 34.60  ? 291 PRO C CA  1 
ATOM   10559 C C   . PRO C 1 291 ? 28.301  12.023  57.111  1.00 42.14  ? 291 PRO C C   1 
ATOM   10560 O O   . PRO C 1 291 ? 27.897  10.998  56.553  1.00 47.54  ? 291 PRO C O   1 
ATOM   10561 C CB  . PRO C 1 291 ? 26.528  11.987  58.885  1.00 29.97  ? 291 PRO C CB  1 
ATOM   10562 C CG  . PRO C 1 291 ? 25.937  13.360  58.854  1.00 32.14  ? 291 PRO C CG  1 
ATOM   10563 C CD  . PRO C 1 291 ? 27.029  14.359  59.150  1.00 37.45  ? 291 PRO C CD  1 
ATOM   10564 N N   . TYR C 1 292 ? 28.968  12.971  56.451  1.00 40.68  ? 292 TYR C N   1 
ATOM   10565 C CA  . TYR C 1 292 ? 29.134  12.938  55.002  1.00 38.60  ? 292 TYR C CA  1 
ATOM   10566 C C   . TYR C 1 292 ? 30.542  12.547  54.570  1.00 36.64  ? 292 TYR C C   1 
ATOM   10567 O O   . TYR C 1 292 ? 30.942  12.835  53.437  1.00 36.41  ? 292 TYR C O   1 
ATOM   10568 C CB  . TYR C 1 292 ? 28.751  14.288  54.400  1.00 40.29  ? 292 TYR C CB  1 
ATOM   10569 C CG  . TYR C 1 292 ? 27.371  14.724  54.809  1.00 36.98  ? 292 TYR C CG  1 
ATOM   10570 C CD1 . TYR C 1 292 ? 26.271  13.922  54.547  1.00 35.90  ? 292 TYR C CD1 1 
ATOM   10571 C CD2 . TYR C 1 292 ? 27.165  15.927  55.468  1.00 38.45  ? 292 TYR C CD2 1 
ATOM   10572 C CE1 . TYR C 1 292 ? 25.004  14.305  54.922  1.00 36.27  ? 292 TYR C CE1 1 
ATOM   10573 C CE2 . TYR C 1 292 ? 25.899  16.321  55.848  1.00 38.83  ? 292 TYR C CE2 1 
ATOM   10574 C CZ  . TYR C 1 292 ? 24.822  15.506  55.572  1.00 37.73  ? 292 TYR C CZ  1 
ATOM   10575 O OH  . TYR C 1 292 ? 23.556  15.893  55.947  1.00 43.64  ? 292 TYR C OH  1 
ATOM   10576 N N   . LEU C 1 293 ? 31.300  11.888  55.439  1.00 33.58  ? 293 LEU C N   1 
ATOM   10577 C CA  . LEU C 1 293 ? 32.648  11.463  55.106  1.00 35.82  ? 293 LEU C CA  1 
ATOM   10578 C C   . LEU C 1 293 ? 32.854  10.017  55.530  1.00 31.41  ? 293 LEU C C   1 
ATOM   10579 O O   . LEU C 1 293 ? 32.213  9.525   56.463  1.00 29.78  ? 293 LEU C O   1 
ATOM   10580 C CB  . LEU C 1 293 ? 33.714  12.370  55.757  1.00 38.77  ? 293 LEU C CB  1 
ATOM   10581 C CG  . LEU C 1 293 ? 33.776  12.602  57.268  1.00 48.73  ? 293 LEU C CG  1 
ATOM   10582 C CD1 . LEU C 1 293 ? 35.108  13.230  57.628  1.00 53.85  ? 293 LEU C CD1 1 
ATOM   10583 C CD2 . LEU C 1 293 ? 32.659  13.508  57.729  1.00 43.03  ? 293 LEU C CD2 1 
ATOM   10584 N N   . ARG C 1 294 ? 33.753  9.338   54.822  1.00 31.72  ? 294 ARG C N   1 
ATOM   10585 C CA  . ARG C 1 294 ? 34.073  7.952   55.136  1.00 30.18  ? 294 ARG C CA  1 
ATOM   10586 C C   . ARG C 1 294 ? 34.924  7.889   56.397  1.00 34.13  ? 294 ARG C C   1 
ATOM   10587 O O   . ARG C 1 294 ? 35.968  8.538   56.486  1.00 39.57  ? 294 ARG C O   1 
ATOM   10588 C CB  . ARG C 1 294 ? 34.808  7.309   53.961  1.00 31.08  ? 294 ARG C CB  1 
ATOM   10589 C CG  . ARG C 1 294 ? 35.302  5.896   54.210  1.00 29.97  ? 294 ARG C CG  1 
ATOM   10590 C CD  . ARG C 1 294 ? 35.737  5.247   52.905  1.00 38.29  ? 294 ARG C CD  1 
ATOM   10591 N NE  . ARG C 1 294 ? 36.589  6.132   52.118  1.00 48.96  ? 294 ARG C NE  1 
ATOM   10592 C CZ  . ARG C 1 294 ? 37.665  5.741   51.449  1.00 58.44  ? 294 ARG C CZ  1 
ATOM   10593 N NH1 . ARG C 1 294 ? 38.051  4.476   51.438  1.00 65.36  ? 294 ARG C NH1 1 
ATOM   10594 N NH2 . ARG C 1 294 ? 38.371  6.643   50.771  1.00 48.44  ? 294 ARG C NH2 1 
ATOM   10595 N N   . TYR C 1 295 ? 34.481  7.112   57.376  1.00 28.30  ? 295 TYR C N   1 
ATOM   10596 C CA  . TYR C 1 295 ? 35.175  7.019   58.651  1.00 27.66  ? 295 TYR C CA  1 
ATOM   10597 C C   . TYR C 1 295 ? 35.992  5.737   58.706  1.00 33.89  ? 295 TYR C C   1 
ATOM   10598 O O   . TYR C 1 295 ? 35.462  4.645   58.481  1.00 37.19  ? 295 TYR C O   1 
ATOM   10599 C CB  . TYR C 1 295 ? 34.186  7.075   59.816  1.00 26.46  ? 295 TYR C CB  1 
ATOM   10600 C CG  . TYR C 1 295 ? 33.668  8.466   60.090  1.00 29.26  ? 295 TYR C CG  1 
ATOM   10601 C CD1 . TYR C 1 295 ? 34.426  9.383   60.807  1.00 29.98  ? 295 TYR C CD1 1 
ATOM   10602 C CD2 . TYR C 1 295 ? 32.425  8.869   59.620  1.00 28.25  ? 295 TYR C CD2 1 
ATOM   10603 C CE1 . TYR C 1 295 ? 33.955  10.659  61.055  1.00 32.58  ? 295 TYR C CE1 1 
ATOM   10604 C CE2 . TYR C 1 295 ? 31.947  10.142  59.863  1.00 30.39  ? 295 TYR C CE2 1 
ATOM   10605 C CZ  . TYR C 1 295 ? 32.715  11.033  60.580  1.00 30.58  ? 295 TYR C CZ  1 
ATOM   10606 O OH  . TYR C 1 295 ? 32.240  12.301  60.823  1.00 31.31  ? 295 TYR C OH  1 
ATOM   10607 N N   . TYR C 1 296 ? 37.283  5.879   58.991  1.00 33.64  ? 296 TYR C N   1 
ATOM   10608 C CA  . TYR C 1 296 ? 38.158  4.741   59.234  1.00 28.14  ? 296 TYR C CA  1 
ATOM   10609 C C   . TYR C 1 296 ? 38.120  4.415   60.720  1.00 34.81  ? 296 TYR C C   1 
ATOM   10610 O O   . TYR C 1 296 ? 38.513  5.243   61.548  1.00 36.33  ? 296 TYR C O   1 
ATOM   10611 C CB  . TYR C 1 296 ? 39.588  5.048   58.794  1.00 34.17  ? 296 TYR C CB  1 
ATOM   10612 C CG  . TYR C 1 296 ? 39.892  4.684   57.361  1.00 55.29  ? 296 TYR C CG  1 
ATOM   10613 C CD1 . TYR C 1 296 ? 40.217  3.381   57.008  1.00 49.00  ? 296 TYR C CD1 1 
ATOM   10614 C CD2 . TYR C 1 296 ? 39.858  5.648   56.359  1.00 52.35  ? 296 TYR C CD2 1 
ATOM   10615 C CE1 . TYR C 1 296 ? 40.497  3.046   55.697  1.00 68.91  ? 296 TYR C CE1 1 
ATOM   10616 C CE2 . TYR C 1 296 ? 40.135  5.323   55.046  1.00 50.52  ? 296 TYR C CE2 1 
ATOM   10617 C CZ  . TYR C 1 296 ? 40.454  4.021   54.720  1.00 79.02  ? 296 TYR C CZ  1 
ATOM   10618 O OH  . TYR C 1 296 ? 40.732  3.694   53.411  1.00 82.75  ? 296 TYR C OH  1 
ATOM   10619 N N   . PHE C 1 297 ? 37.640  3.223   61.060  1.00 37.96  ? 297 PHE C N   1 
ATOM   10620 C CA  . PHE C 1 297 ? 37.617  2.782   62.449  1.00 26.96  ? 297 PHE C CA  1 
ATOM   10621 C C   . PHE C 1 297 ? 38.940  2.095   62.761  1.00 29.41  ? 297 PHE C C   1 
ATOM   10622 O O   . PHE C 1 297 ? 39.189  0.976   62.300  1.00 29.44  ? 297 PHE C O   1 
ATOM   10623 C CB  . PHE C 1 297 ? 36.444  1.846   62.723  1.00 23.74  ? 297 PHE C CB  1 
ATOM   10624 C CG  . PHE C 1 297 ? 36.431  1.313   64.123  1.00 23.35  ? 297 PHE C CG  1 
ATOM   10625 C CD1 . PHE C 1 297 ? 36.230  2.164   65.194  1.00 24.76  ? 297 PHE C CD1 1 
ATOM   10626 C CD2 . PHE C 1 297 ? 36.655  -0.028  64.374  1.00 23.10  ? 297 PHE C CD2 1 
ATOM   10627 C CE1 . PHE C 1 297 ? 36.231  1.684   66.487  1.00 23.46  ? 297 PHE C CE1 1 
ATOM   10628 C CE2 . PHE C 1 297 ? 36.659  -0.514  65.667  1.00 23.01  ? 297 PHE C CE2 1 
ATOM   10629 C CZ  . PHE C 1 297 ? 36.445  0.344   66.723  1.00 23.19  ? 297 PHE C CZ  1 
ATOM   10630 N N   . ARG C 1 298 ? 39.789  2.774   63.536  1.00 33.13  ? 298 ARG C N   1 
ATOM   10631 C CA  . ARG C 1 298 ? 41.071  2.233   63.992  1.00 28.73  ? 298 ARG C CA  1 
ATOM   10632 C C   . ARG C 1 298 ? 41.951  1.788   62.828  1.00 29.79  ? 298 ARG C C   1 
ATOM   10633 O O   . ARG C 1 298 ? 42.766  0.874   62.973  1.00 31.88  ? 298 ARG C O   1 
ATOM   10634 C CB  . ARG C 1 298 ? 40.863  1.077   64.975  1.00 27.97  ? 298 ARG C CB  1 
ATOM   10635 C CG  . ARG C 1 298 ? 40.214  1.494   66.283  1.00 27.45  ? 298 ARG C CG  1 
ATOM   10636 C CD  . ARG C 1 298 ? 40.222  0.367   67.303  1.00 28.15  ? 298 ARG C CD  1 
ATOM   10637 N NE  . ARG C 1 298 ? 39.359  0.677   68.437  1.00 26.66  ? 298 ARG C NE  1 
ATOM   10638 C CZ  . ARG C 1 298 ? 38.670  -0.223  69.124  1.00 34.18  ? 298 ARG C CZ  1 
ATOM   10639 N NH1 . ARG C 1 298 ? 38.744  -1.514  68.842  1.00 40.67  ? 298 ARG C NH1 1 
ATOM   10640 N NH2 . ARG C 1 298 ? 37.882  0.182   70.116  1.00 35.90  ? 298 ARG C NH2 1 
ATOM   10641 N N   . GLU C 1 299 ? 41.795  2.435   61.672  1.00 30.11  ? 299 GLU C N   1 
ATOM   10642 C CA  . GLU C 1 299 ? 42.498  2.048   60.446  1.00 33.77  ? 299 GLU C CA  1 
ATOM   10643 C C   . GLU C 1 299 ? 42.303  0.565   60.141  1.00 36.02  ? 299 GLU C C   1 
ATOM   10644 O O   . GLU C 1 299 ? 43.205  -0.114  59.645  1.00 43.19  ? 299 GLU C O   1 
ATOM   10645 C CB  . GLU C 1 299 ? 43.988  2.391   60.526  1.00 43.89  ? 299 GLU C CB  1 
ATOM   10646 C CG  . GLU C 1 299 ? 44.301  3.868   60.689  1.00 52.55  ? 299 GLU C CG  1 
ATOM   10647 C CD  . GLU C 1 299 ? 45.687  4.105   61.263  1.00 64.90  ? 299 GLU C CD  1 
ATOM   10648 O OE1 . GLU C 1 299 ? 46.646  3.459   60.789  1.00 54.59  ? 299 GLU C OE1 1 
ATOM   10649 O OE2 . GLU C 1 299 ? 45.821  4.938   62.185  1.00 62.32  ? 299 GLU C OE2 1 
ATOM   10650 N N   . LEU C 1 300 ? 41.115  0.053   60.449  1.00 29.60  ? 300 LEU C N   1 
ATOM   10651 C CA  . LEU C 1 300 ? 40.824  -1.364  60.273  1.00 28.09  ? 300 LEU C CA  1 
ATOM   10652 C C   . LEU C 1 300 ? 39.642  -1.638  59.360  1.00 31.31  ? 300 LEU C C   1 
ATOM   10653 O O   . LEU C 1 300 ? 39.727  -2.520  58.501  1.00 36.09  ? 300 LEU C O   1 
ATOM   10654 C CB  . LEU C 1 300 ? 40.569  -2.023  61.637  1.00 27.27  ? 300 LEU C CB  1 
ATOM   10655 C CG  . LEU C 1 300 ? 41.802  -2.245  62.518  1.00 28.63  ? 300 LEU C CG  1 
ATOM   10656 C CD1 . LEU C 1 300 ? 41.429  -2.963  63.808  1.00 27.96  ? 300 LEU C CD1 1 
ATOM   10657 C CD2 . LEU C 1 300 ? 42.868  -3.015  61.756  1.00 32.05  ? 300 LEU C CD2 1 
ATOM   10658 N N   . ILE C 1 301 ? 38.540  -0.912  59.516  1.00 28.04  ? 301 ILE C N   1 
ATOM   10659 C CA  . ILE C 1 301 ? 37.323  -1.194  58.762  1.00 24.96  ? 301 ILE C CA  1 
ATOM   10660 C C   . ILE C 1 301 ? 36.592  0.119   58.514  1.00 29.66  ? 301 ILE C C   1 
ATOM   10661 O O   . ILE C 1 301 ? 36.405  0.922   59.434  1.00 33.87  ? 301 ILE C O   1 
ATOM   10662 C CB  . ILE C 1 301 ? 36.436  -2.220  59.501  1.00 23.68  ? 301 ILE C CB  1 
ATOM   10663 C CG1 . ILE C 1 301 ? 35.144  -2.490  58.728  1.00 24.10  ? 301 ILE C CG1 1 
ATOM   10664 C CG2 . ILE C 1 301 ? 36.150  -1.768  60.931  1.00 22.93  ? 301 ILE C CG2 1 
ATOM   10665 C CD1 . ILE C 1 301 ? 34.216  -3.459  59.425  1.00 23.36  ? 301 ILE C CD1 1 
ATOM   10666 N N   . SER C 1 302 ? 36.202  0.352   57.263  1.00 34.45  ? 302 SER C N   1 
ATOM   10667 C CA  . SER C 1 302 ? 35.530  1.596   56.914  1.00 27.58  ? 302 SER C CA  1 
ATOM   10668 C C   . SER C 1 302 ? 34.093  1.581   57.416  1.00 25.26  ? 302 SER C C   1 
ATOM   10669 O O   . SER C 1 302 ? 33.380  0.585   57.266  1.00 32.15  ? 302 SER C O   1 
ATOM   10670 C CB  . SER C 1 302 ? 35.563  1.812   55.402  1.00 32.29  ? 302 SER C CB  1 
ATOM   10671 O OG  . SER C 1 302 ? 36.889  1.731   54.905  1.00 46.89  ? 302 SER C OG  1 
ATOM   10672 N N   . VAL C 1 303 ? 33.670  2.686   58.022  1.00 29.35  ? 303 VAL C N   1 
ATOM   10673 C CA  . VAL C 1 303 ? 32.313  2.836   58.532  1.00 25.92  ? 303 VAL C CA  1 
ATOM   10674 C C   . VAL C 1 303 ? 31.697  4.068   57.890  1.00 23.67  ? 303 VAL C C   1 
ATOM   10675 O O   . VAL C 1 303 ? 32.299  5.148   57.902  1.00 34.13  ? 303 VAL C O   1 
ATOM   10676 C CB  . VAL C 1 303 ? 32.284  2.955   60.068  1.00 22.35  ? 303 VAL C CB  1 
ATOM   10677 C CG1 . VAL C 1 303 ? 30.850  2.928   60.571  1.00 22.06  ? 303 VAL C CG1 1 
ATOM   10678 C CG2 . VAL C 1 303 ? 33.105  1.848   60.708  1.00 21.84  ? 303 VAL C CG2 1 
ATOM   10679 N N   . PHE C 1 304 ? 30.506  3.905   57.326  1.00 23.43  ? 304 PHE C N   1 
ATOM   10680 C CA  . PHE C 1 304 ? 29.727  5.013   56.804  1.00 24.78  ? 304 PHE C CA  1 
ATOM   10681 C C   . PHE C 1 304 ? 28.540  5.259   57.724  1.00 24.90  ? 304 PHE C C   1 
ATOM   10682 O O   . PHE C 1 304 ? 28.020  4.332   58.350  1.00 24.67  ? 304 PHE C O   1 
ATOM   10683 C CB  . PHE C 1 304 ? 29.243  4.733   55.377  1.00 28.20  ? 304 PHE C CB  1 
ATOM   10684 C CG  . PHE C 1 304 ? 30.264  5.044   54.315  1.00 28.42  ? 304 PHE C CG  1 
ATOM   10685 C CD1 . PHE C 1 304 ? 30.588  6.354   54.008  1.00 27.93  ? 304 PHE C CD1 1 
ATOM   10686 C CD2 . PHE C 1 304 ? 30.889  4.025   53.618  1.00 28.94  ? 304 PHE C CD2 1 
ATOM   10687 C CE1 . PHE C 1 304 ? 31.521  6.638   53.031  1.00 29.50  ? 304 PHE C CE1 1 
ATOM   10688 C CE2 . PHE C 1 304 ? 31.823  4.303   52.640  1.00 28.21  ? 304 PHE C CE2 1 
ATOM   10689 C CZ  . PHE C 1 304 ? 32.140  5.611   52.347  1.00 33.91  ? 304 PHE C CZ  1 
ATOM   10690 N N   . PHE C 1 305 ? 28.128  6.518   57.822  1.00 25.14  ? 305 PHE C N   1 
ATOM   10691 C CA  . PHE C 1 305 ? 27.040  6.907   58.707  1.00 26.11  ? 305 PHE C CA  1 
ATOM   10692 C C   . PHE C 1 305 ? 25.898  7.472   57.877  1.00 32.26  ? 305 PHE C C   1 
ATOM   10693 O O   . PHE C 1 305 ? 26.097  8.399   57.084  1.00 39.01  ? 305 PHE C O   1 
ATOM   10694 C CB  . PHE C 1 305 ? 27.523  7.915   59.751  1.00 24.73  ? 305 PHE C CB  1 
ATOM   10695 C CG  . PHE C 1 305 ? 28.327  7.288   60.858  1.00 23.78  ? 305 PHE C CG  1 
ATOM   10696 C CD1 . PHE C 1 305 ? 27.703  6.797   61.992  1.00 26.96  ? 305 PHE C CD1 1 
ATOM   10697 C CD2 . PHE C 1 305 ? 29.703  7.171   60.753  1.00 24.88  ? 305 PHE C CD2 1 
ATOM   10698 C CE1 . PHE C 1 305 ? 28.438  6.217   63.012  1.00 25.72  ? 305 PHE C CE1 1 
ATOM   10699 C CE2 . PHE C 1 305 ? 30.445  6.586   61.766  1.00 29.64  ? 305 PHE C CE2 1 
ATOM   10700 C CZ  . PHE C 1 305 ? 29.811  6.108   62.897  1.00 29.43  ? 305 PHE C CZ  1 
ATOM   10701 N N   . ARG C 1 306 ? 24.706  6.910   58.065  1.00 24.68  ? 306 ARG C N   1 
ATOM   10702 C CA  . ARG C 1 306 ? 23.563  7.238   57.229  1.00 30.82  ? 306 ARG C CA  1 
ATOM   10703 C C   . ARG C 1 306 ? 22.890  8.523   57.698  1.00 26.91  ? 306 ARG C C   1 
ATOM   10704 O O   . ARG C 1 306 ? 22.835  8.816   58.896  1.00 27.65  ? 306 ARG C O   1 
ATOM   10705 C CB  . ARG C 1 306 ? 22.558  6.084   57.230  1.00 32.52  ? 306 ARG C CB  1 
ATOM   10706 C CG  . ARG C 1 306 ? 21.779  5.930   58.527  1.00 32.24  ? 306 ARG C CG  1 
ATOM   10707 C CD  . ARG C 1 306 ? 20.299  5.708   58.266  1.00 26.40  ? 306 ARG C CD  1 
ATOM   10708 N NE  . ARG C 1 306 ? 19.509  5.823   59.486  1.00 24.82  ? 306 ARG C NE  1 
ATOM   10709 C CZ  . ARG C 1 306 ? 18.231  5.483   59.586  1.00 31.02  ? 306 ARG C CZ  1 
ATOM   10710 N NH1 . ARG C 1 306 ? 17.565  4.989   58.554  1.00 40.81  ? 306 ARG C NH1 1 
ATOM   10711 N NH2 . ARG C 1 306 ? 17.606  5.640   60.750  1.00 34.41  ? 306 ARG C NH2 1 
ATOM   10712 N N   . ASP C 1 307 ? 22.385  9.294   56.739  1.00 35.28  ? 307 ASP C N   1 
ATOM   10713 C CA  . ASP C 1 307 ? 21.663  10.527  57.038  1.00 44.52  ? 307 ASP C CA  1 
ATOM   10714 C C   . ASP C 1 307 ? 20.255  10.164  57.493  1.00 42.42  ? 307 ASP C C   1 
ATOM   10715 O O   . ASP C 1 307 ? 19.437  9.701   56.692  1.00 41.04  ? 307 ASP C O   1 
ATOM   10716 C CB  . ASP C 1 307 ? 21.635  11.436  55.813  1.00 37.76  ? 307 ASP C CB  1 
ATOM   10717 C CG  . ASP C 1 307 ? 21.266  12.864  56.158  1.00 42.29  ? 307 ASP C CG  1 
ATOM   10718 O OD1 . ASP C 1 307 ? 20.136  13.091  56.638  1.00 45.82  ? 307 ASP C OD1 1 
ATOM   10719 O OD2 . ASP C 1 307 ? 22.112  13.760  55.954  1.00 35.27  ? 307 ASP C OD2 1 
ATOM   10720 N N   . LYS C 1 308 ? 19.973  10.368  58.783  1.00 37.77  ? 308 LYS C N   1 
ATOM   10721 C CA  . LYS C 1 308 ? 18.697  9.921   59.336  1.00 36.00  ? 308 LYS C CA  1 
ATOM   10722 C C   . LYS C 1 308 ? 17.522  10.705  58.763  1.00 39.22  ? 308 LYS C C   1 
ATOM   10723 O O   . LYS C 1 308 ? 16.483  10.119  58.442  1.00 44.37  ? 308 LYS C O   1 
ATOM   10724 C CB  . LYS C 1 308 ? 18.711  10.029  60.860  1.00 41.21  ? 308 LYS C CB  1 
ATOM   10725 C CG  . LYS C 1 308 ? 17.459  9.462   61.514  1.00 40.68  ? 308 LYS C CG  1 
ATOM   10726 C CD  . LYS C 1 308 ? 17.365  9.836   62.983  1.00 32.74  ? 308 LYS C CD  1 
ATOM   10727 C CE  . LYS C 1 308 ? 16.672  8.741   63.783  1.00 48.92  ? 308 LYS C CE  1 
ATOM   10728 N NZ  . LYS C 1 308 ? 17.552  7.558   64.009  1.00 40.32  ? 308 LYS C NZ  1 
ATOM   10729 N N   . THR C 1 309 ? 17.663  12.027  58.632  1.00 44.39  ? 309 THR C N   1 
ATOM   10730 C CA  . THR C 1 309 ? 16.530  12.843  58.201  1.00 40.95  ? 309 THR C CA  1 
ATOM   10731 C C   . THR C 1 309 ? 16.062  12.448  56.806  1.00 38.46  ? 309 THR C C   1 
ATOM   10732 O O   . THR C 1 309 ? 14.857  12.328  56.563  1.00 38.95  ? 309 THR C O   1 
ATOM   10733 C CB  . THR C 1 309 ? 16.890  14.329  58.250  1.00 37.61  ? 309 THR C CB  1 
ATOM   10734 O OG1 . THR C 1 309 ? 18.071  14.570  57.476  1.00 40.67  ? 309 THR C OG1 1 
ATOM   10735 C CG2 . THR C 1 309 ? 17.126  14.773  59.689  1.00 34.93  ? 309 THR C CG2 1 
ATOM   10736 N N   . LEU C 1 310 ? 16.997  12.226  55.879  1.00 40.89  ? 310 LEU C N   1 
ATOM   10737 C CA  . LEU C 1 310 ? 16.611  11.792  54.539  1.00 34.70  ? 310 LEU C CA  1 
ATOM   10738 C C   . LEU C 1 310 ? 16.027  10.384  54.554  1.00 34.39  ? 310 LEU C C   1 
ATOM   10739 O O   . LEU C 1 310 ? 15.017  10.118  53.892  1.00 36.59  ? 310 LEU C O   1 
ATOM   10740 C CB  . LEU C 1 310 ? 17.810  11.859  53.592  1.00 30.69  ? 310 LEU C CB  1 
ATOM   10741 C CG  . LEU C 1 310 ? 18.574  13.179  53.495  1.00 36.73  ? 310 LEU C CG  1 
ATOM   10742 C CD1 . LEU C 1 310 ? 19.443  13.183  52.251  1.00 32.76  ? 310 LEU C CD1 1 
ATOM   10743 C CD2 . LEU C 1 310 ? 17.618  14.362  53.485  1.00 36.42  ? 310 LEU C CD2 1 
ATOM   10744 N N   . SER C 1 311 ? 16.646  9.470   55.306  1.00 29.35  ? 311 SER C N   1 
ATOM   10745 C CA  . SER C 1 311 ? 16.184  8.086   55.314  1.00 28.60  ? 311 SER C CA  1 
ATOM   10746 C C   . SER C 1 311 ? 14.822  7.946   55.982  1.00 31.87  ? 311 SER C C   1 
ATOM   10747 O O   . SER C 1 311 ? 14.036  7.074   55.601  1.00 34.88  ? 311 SER C O   1 
ATOM   10748 C CB  . SER C 1 311 ? 17.210  7.192   56.009  1.00 28.88  ? 311 SER C CB  1 
ATOM   10749 O OG  . SER C 1 311 ? 18.471  7.267   55.366  1.00 32.86  ? 311 SER C OG  1 
ATOM   10750 N N   . ASP C 1 312 ? 14.523  8.782   56.977  1.00 37.76  ? 312 ASP C N   1 
ATOM   10751 C CA  . ASP C 1 312 ? 13.223  8.713   57.631  1.00 36.33  ? 312 ASP C CA  1 
ATOM   10752 C C   . ASP C 1 312 ? 12.143  9.480   56.880  1.00 36.14  ? 312 ASP C C   1 
ATOM   10753 O O   . ASP C 1 312 ? 10.955  9.254   57.134  1.00 39.97  ? 312 ASP C O   1 
ATOM   10754 C CB  . ASP C 1 312 ? 13.325  9.231   59.067  1.00 37.30  ? 312 ASP C CB  1 
ATOM   10755 C CG  . ASP C 1 312 ? 14.005  8.241   59.994  1.00 44.98  ? 312 ASP C CG  1 
ATOM   10756 O OD1 . ASP C 1 312 ? 14.263  7.099   59.558  1.00 44.17  ? 312 ASP C OD1 1 
ATOM   10757 O OD2 . ASP C 1 312 ? 14.282  8.603   61.155  1.00 62.60  ? 312 ASP C OD2 1 
ATOM   10758 N N   . LEU C 1 313 ? 12.519  10.382  55.968  1.00 37.69  ? 313 LEU C N   1 
ATOM   10759 C CA  . LEU C 1 313 ? 11.518  11.046  55.139  1.00 37.53  ? 313 LEU C CA  1 
ATOM   10760 C C   . LEU C 1 313 ? 10.873  10.062  54.172  1.00 34.98  ? 313 LEU C C   1 
ATOM   10761 O O   . LEU C 1 313 ? 9.644   10.013  54.047  1.00 35.00  ? 313 LEU C O   1 
ATOM   10762 C CB  . LEU C 1 313 ? 12.142  12.216  54.379  1.00 32.93  ? 313 LEU C CB  1 
ATOM   10763 C CG  . LEU C 1 313 ? 12.367  13.514  55.155  1.00 34.08  ? 313 LEU C CG  1 
ATOM   10764 C CD1 . LEU C 1 313 ? 13.444  14.335  54.480  1.00 34.32  ? 313 LEU C CD1 1 
ATOM   10765 C CD2 . LEU C 1 313 ? 11.083  14.317  55.285  1.00 35.56  ? 313 LEU C CD2 1 
ATOM   10766 N N   . ILE C 1 314 ? 11.692  9.273   53.476  1.00 30.80  ? 314 ILE C N   1 
ATOM   10767 C CA  . ILE C 1 314 ? 11.163  8.253   52.575  1.00 30.40  ? 314 ILE C CA  1 
ATOM   10768 C C   . ILE C 1 314 ? 10.390  7.201   53.359  1.00 33.10  ? 314 ILE C C   1 
ATOM   10769 O O   . ILE C 1 314 ? 9.342   6.716   52.916  1.00 36.17  ? 314 ILE C O   1 
ATOM   10770 C CB  . ILE C 1 314 ? 12.309  7.629   51.755  1.00 29.51  ? 314 ILE C CB  1 
ATOM   10771 C CG1 . ILE C 1 314 ? 12.904  8.663   50.797  1.00 31.23  ? 314 ILE C CG1 1 
ATOM   10772 C CG2 . ILE C 1 314 ? 11.831  6.400   50.996  1.00 29.13  ? 314 ILE C CG2 1 
ATOM   10773 C CD1 . ILE C 1 314 ? 14.018  8.121   49.926  1.00 29.36  ? 314 ILE C CD1 1 
ATOM   10774 N N   . GLY C 1 315 ? 10.887  6.842   54.544  1.00 32.63  ? 315 GLY C N   1 
ATOM   10775 C CA  . GLY C 1 315 ? 10.282  5.756   55.293  1.00 29.57  ? 315 GLY C CA  1 
ATOM   10776 C C   . GLY C 1 315 ? 8.995   6.108   56.008  1.00 31.58  ? 315 GLY C C   1 
ATOM   10777 O O   . GLY C 1 315 ? 8.154   5.231   56.226  1.00 38.40  ? 315 GLY C O   1 
ATOM   10778 N N   . PHE C 1 316 ? 8.817   7.372   56.397  1.00 34.94  ? 316 PHE C N   1 
ATOM   10779 C CA  . PHE C 1 316 ? 7.701   7.679   57.285  1.00 38.49  ? 316 PHE C CA  1 
ATOM   10780 C C   . PHE C 1 316 ? 6.831   8.862   56.869  1.00 40.34  ? 316 PHE C C   1 
ATOM   10781 O O   . PHE C 1 316 ? 5.634   8.870   57.170  1.00 49.82  ? 316 PHE C O   1 
ATOM   10782 C CB  . PHE C 1 316 ? 8.231   7.896   58.706  1.00 32.79  ? 316 PHE C CB  1 
ATOM   10783 C CG  . PHE C 1 316 ? 8.903   6.685   59.290  1.00 33.98  ? 316 PHE C CG  1 
ATOM   10784 C CD1 . PHE C 1 316 ? 8.171   5.542   59.555  1.00 42.87  ? 316 PHE C CD1 1 
ATOM   10785 C CD2 . PHE C 1 316 ? 10.259  6.689   59.576  1.00 44.92  ? 316 PHE C CD2 1 
ATOM   10786 C CE1 . PHE C 1 316 ? 8.773   4.421   60.089  1.00 39.87  ? 316 PHE C CE1 1 
ATOM   10787 C CE2 . PHE C 1 316 ? 10.870  5.564   60.115  1.00 42.96  ? 316 PHE C CE2 1 
ATOM   10788 C CZ  . PHE C 1 316 ? 10.124  4.431   60.371  1.00 36.86  ? 316 PHE C CZ  1 
ATOM   10789 N N   . SER C 1 317 ? 7.392   9.862   56.193  1.00 37.36  ? 317 SER C N   1 
ATOM   10790 C CA  . SER C 1 317 ? 6.634   11.078  55.896  1.00 44.04  ? 317 SER C CA  1 
ATOM   10791 C C   . SER C 1 317 ? 6.209   11.213  54.442  1.00 46.55  ? 317 SER C C   1 
ATOM   10792 O O   . SER C 1 317 ? 5.094   11.666  54.176  1.00 52.65  ? 317 SER C O   1 
ATOM   10793 C CB  . SER C 1 317 ? 7.436   12.322  56.293  1.00 45.58  ? 317 SER C CB  1 
ATOM   10794 O OG  . SER C 1 317 ? 8.800   12.175  55.962  1.00 41.94  ? 317 SER C OG  1 
ATOM   10795 N N   . TYR C 1 318 ? 7.058   10.828  53.488  1.00 41.43  ? 318 TYR C N   1 
ATOM   10796 C CA  . TYR C 1 318 ? 6.749   11.040  52.078  1.00 35.42  ? 318 TYR C CA  1 
ATOM   10797 C C   . TYR C 1 318 ? 5.549   10.231  51.595  1.00 39.25  ? 318 TYR C C   1 
ATOM   10798 O O   . TYR C 1 318 ? 5.114   10.431  50.455  1.00 41.17  ? 318 TYR C O   1 
ATOM   10799 C CB  . TYR C 1 318 ? 7.963   10.704  51.207  1.00 34.34  ? 318 TYR C CB  1 
ATOM   10800 C CG  . TYR C 1 318 ? 9.030   11.777  51.142  1.00 37.84  ? 318 TYR C CG  1 
ATOM   10801 C CD1 . TYR C 1 318 ? 8.716   13.120  51.326  1.00 42.06  ? 318 TYR C CD1 1 
ATOM   10802 C CD2 . TYR C 1 318 ? 10.353  11.444  50.876  1.00 36.62  ? 318 TYR C CD2 1 
ATOM   10803 C CE1 . TYR C 1 318 ? 9.695   14.099  51.259  1.00 36.28  ? 318 TYR C CE1 1 
ATOM   10804 C CE2 . TYR C 1 318 ? 11.336  12.412  50.806  1.00 33.73  ? 318 TYR C CE2 1 
ATOM   10805 C CZ  . TYR C 1 318 ? 11.003  13.737  50.997  1.00 35.14  ? 318 TYR C CZ  1 
ATOM   10806 O OH  . TYR C 1 318 ? 11.984  14.700  50.927  1.00 35.58  ? 318 TYR C OH  1 
ATOM   10807 N N   . HIS C 1 319 ? 5.014   9.322   52.417  1.00 43.06  ? 319 HIS C N   1 
ATOM   10808 C CA  . HIS C 1 319 ? 3.861   8.529   51.997  1.00 44.34  ? 319 HIS C CA  1 
ATOM   10809 C C   . HIS C 1 319 ? 2.607   9.384   51.853  1.00 48.77  ? 319 HIS C C   1 
ATOM   10810 O O   . HIS C 1 319 ? 1.772   9.117   50.980  1.00 44.01  ? 319 HIS C O   1 
ATOM   10811 C CB  . HIS C 1 319 ? 3.619   7.386   52.986  1.00 41.58  ? 319 HIS C CB  1 
ATOM   10812 C CG  . HIS C 1 319 ? 2.594   7.694   54.034  1.00 45.22  ? 319 HIS C CG  1 
ATOM   10813 N ND1 . HIS C 1 319 ? 2.903   8.346   55.208  1.00 39.86  ? 319 HIS C ND1 1 
ATOM   10814 C CD2 . HIS C 1 319 ? 1.265   7.439   54.084  1.00 38.17  ? 319 HIS C CD2 1 
ATOM   10815 C CE1 . HIS C 1 319 ? 1.809   8.481   55.936  1.00 37.84  ? 319 HIS C CE1 1 
ATOM   10816 N NE2 . HIS C 1 319 ? 0.801   7.940   55.277  1.00 38.43  ? 319 HIS C NE2 1 
ATOM   10817 N N   . ALA C 1 320 ? 2.452   10.409  52.696  1.00 42.92  ? 320 ALA C N   1 
ATOM   10818 C CA  . ALA C 1 320 ? 1.333   11.339  52.609  1.00 41.32  ? 320 ALA C CA  1 
ATOM   10819 C C   . ALA C 1 320 ? 1.647   12.537  51.725  1.00 47.81  ? 320 ALA C C   1 
ATOM   10820 O O   . ALA C 1 320 ? 1.077   13.619  51.918  1.00 43.36  ? 320 ALA C O   1 
ATOM   10821 C CB  . ALA C 1 320 ? 0.922   11.800  54.009  1.00 42.23  ? 320 ALA C CB  1 
ATOM   10822 N N   . TRP C 1 321 ? 2.544   12.366  50.759  1.00 48.59  ? 321 TRP C N   1 
ATOM   10823 C CA  . TRP C 1 321 ? 3.045   13.446  49.929  1.00 56.71  ? 321 TRP C CA  1 
ATOM   10824 C C   . TRP C 1 321 ? 2.695   13.197  48.469  1.00 57.39  ? 321 TRP C C   1 
ATOM   10825 O O   . TRP C 1 321 ? 2.551   12.050  48.034  1.00 53.09  ? 321 TRP C O   1 
ATOM   10826 C CB  . TRP C 1 321 ? 4.567   13.570  50.054  1.00 43.06  ? 321 TRP C CB  1 
ATOM   10827 C CG  . TRP C 1 321 ? 5.065   14.475  51.137  1.00 42.88  ? 321 TRP C CG  1 
ATOM   10828 C CD1 . TRP C 1 321 ? 4.763   14.418  52.467  1.00 50.27  ? 321 TRP C CD1 1 
ATOM   10829 C CD2 . TRP C 1 321 ? 5.990   15.554  50.983  1.00 40.77  ? 321 TRP C CD2 1 
ATOM   10830 N NE1 . TRP C 1 321 ? 5.436   15.408  53.146  1.00 40.79  ? 321 TRP C NE1 1 
ATOM   10831 C CE2 . TRP C 1 321 ? 6.196   16.118  52.255  1.00 44.86  ? 321 TRP C CE2 1 
ATOM   10832 C CE3 . TRP C 1 321 ? 6.654   16.107  49.888  1.00 50.05  ? 321 TRP C CE3 1 
ATOM   10833 C CZ2 . TRP C 1 321 ? 7.043   17.206  52.460  1.00 50.32  ? 321 TRP C CZ2 1 
ATOM   10834 C CZ3 . TRP C 1 321 ? 7.495   17.181  50.093  1.00 52.03  ? 321 TRP C CZ3 1 
ATOM   10835 C CH2 . TRP C 1 321 ? 7.683   17.720  51.367  1.00 51.96  ? 321 TRP C CH2 1 
ATOM   10836 N N   . ASN C 1 322 ? 2.556   14.285  47.716  1.00 47.63  ? 322 ASN C N   1 
ATOM   10837 C CA  . ASN C 1 322 ? 2.563   14.193  46.265  1.00 53.58  ? 322 ASN C CA  1 
ATOM   10838 C C   . ASN C 1 322 ? 3.955   13.782  45.792  1.00 55.73  ? 322 ASN C C   1 
ATOM   10839 O O   . ASN C 1 322 ? 4.969   14.132  46.402  1.00 54.63  ? 322 ASN C O   1 
ATOM   10840 C CB  . ASN C 1 322 ? 2.146   15.532  45.648  1.00 46.72  ? 322 ASN C CB  1 
ATOM   10841 C CG  . ASN C 1 322 ? 2.428   15.618  44.153  1.00 66.49  ? 322 ASN C CG  1 
ATOM   10842 O OD1 . ASN C 1 322 ? 2.469   14.608  43.450  1.00 75.08  ? 322 ASN C OD1 1 
ATOM   10843 N ND2 . ASN C 1 322 ? 2.622   16.838  43.662  1.00 71.40  ? 322 ASN C ND2 1 
ATOM   10844 N N   . ALA C 1 323 ? 3.995   13.014  44.701  1.00 58.52  ? 323 ALA C N   1 
ATOM   10845 C CA  . ALA C 1 323 ? 5.270   12.504  44.201  1.00 50.26  ? 323 ALA C CA  1 
ATOM   10846 C C   . ALA C 1 323 ? 6.193   13.639  43.773  1.00 53.26  ? 323 ALA C C   1 
ATOM   10847 O O   . ALA C 1 323 ? 7.358   13.694  44.183  1.00 44.50  ? 323 ALA C O   1 
ATOM   10848 C CB  . ALA C 1 323 ? 5.030   11.538  43.040  1.00 57.95  ? 323 ALA C CB  1 
ATOM   10849 N N   . GLU C 1 324 ? 5.685   14.559  42.948  1.00 64.02  ? 324 GLU C N   1 
ATOM   10850 C CA  . GLU C 1 324 ? 6.505   15.674  42.485  1.00 63.74  ? 324 GLU C CA  1 
ATOM   10851 C C   . GLU C 1 324 ? 6.898   16.597  43.630  1.00 55.95  ? 324 GLU C C   1 
ATOM   10852 O O   . GLU C 1 324 ? 7.964   17.221  43.584  1.00 56.93  ? 324 GLU C O   1 
ATOM   10853 C CB  . GLU C 1 324 ? 5.767   16.455  41.400  1.00 65.39  ? 324 GLU C CB  1 
ATOM   10854 C CG  . GLU C 1 324 ? 5.549   15.668  40.118  1.00 68.42  ? 324 GLU C CG  1 
ATOM   10855 C CD  . GLU C 1 324 ? 6.497   16.080  39.010  1.00 75.97  ? 324 GLU C CD  1 
ATOM   10856 O OE1 . GLU C 1 324 ? 7.339   16.972  39.250  1.00 80.96  ? 324 GLU C OE1 1 
ATOM   10857 O OE2 . GLU C 1 324 ? 6.398   15.515  37.901  1.00 71.75  ? 324 GLU C OE2 1 
ATOM   10858 N N   . ASP C 1 325 ? 6.051   16.709  44.654  1.00 52.22  ? 325 ASP C N   1 
ATOM   10859 C CA  . ASP C 1 325 ? 6.430   17.471  45.838  1.00 44.67  ? 325 ASP C CA  1 
ATOM   10860 C C   . ASP C 1 325 ? 7.508   16.745  46.636  1.00 49.18  ? 325 ASP C C   1 
ATOM   10861 O O   . ASP C 1 325 ? 8.416   17.380  47.186  1.00 42.20  ? 325 ASP C O   1 
ATOM   10862 C CB  . ASP C 1 325 ? 5.197   17.734  46.701  1.00 52.03  ? 325 ASP C CB  1 
ATOM   10863 C CG  . ASP C 1 325 ? 4.126   18.517  45.962  1.00 71.04  ? 325 ASP C CG  1 
ATOM   10864 O OD1 . ASP C 1 325 ? 4.436   19.097  44.899  1.00 64.03  ? 325 ASP C OD1 1 
ATOM   10865 O OD2 . ASP C 1 325 ? 2.973   18.551  46.442  1.00 76.43  ? 325 ASP C OD2 1 
ATOM   10866 N N   . ALA C 1 326 ? 7.427   15.413  46.701  1.00 46.99  ? 326 ALA C N   1 
ATOM   10867 C CA  . ALA C 1 326 ? 8.383   14.643  47.492  1.00 40.96  ? 326 ALA C CA  1 
ATOM   10868 C C   . ALA C 1 326 ? 9.767   14.652  46.861  1.00 44.74  ? 326 ALA C C   1 
ATOM   10869 O O   . ALA C 1 326 ? 10.774  14.815  47.562  1.00 44.13  ? 326 ALA C O   1 
ATOM   10870 C CB  . ALA C 1 326 ? 7.885   13.210  47.670  1.00 38.24  ? 326 ALA C CB  1 
ATOM   10871 N N   . VAL C 1 327 ? 9.839   14.473  45.543  1.00 39.22  ? 327 VAL C N   1 
ATOM   10872 C CA  . VAL C 1 327 ? 11.134  14.437  44.877  1.00 38.07  ? 327 VAL C CA  1 
ATOM   10873 C C   . VAL C 1 327 ? 11.831  15.788  44.989  1.00 39.06  ? 327 VAL C C   1 
ATOM   10874 O O   . VAL C 1 327 ? 13.019  15.861  45.323  1.00 39.78  ? 327 VAL C O   1 
ATOM   10875 C CB  . VAL C 1 327 ? 10.964  13.995  43.412  1.00 53.23  ? 327 VAL C CB  1 
ATOM   10876 C CG1 . VAL C 1 327 ? 12.215  14.307  42.606  1.00 41.62  ? 327 VAL C CG1 1 
ATOM   10877 C CG2 . VAL C 1 327 ? 10.623  12.515  43.351  1.00 38.45  ? 327 VAL C CG2 1 
ATOM   10878 N N   . ARG C 1 328 ? 11.102  16.878  44.742  1.00 40.94  ? 328 ARG C N   1 
ATOM   10879 C CA  . ARG C 1 328 ? 11.716  18.198  44.818  1.00 42.14  ? 328 ARG C CA  1 
ATOM   10880 C C   . ARG C 1 328 ? 12.087  18.591  46.242  1.00 44.82  ? 328 ARG C C   1 
ATOM   10881 O O   . ARG C 1 328 ? 12.962  19.445  46.425  1.00 47.27  ? 328 ARG C O   1 
ATOM   10882 C CB  . ARG C 1 328 ? 10.796  19.254  44.204  1.00 44.53  ? 328 ARG C CB  1 
ATOM   10883 C CG  . ARG C 1 328 ? 11.202  19.664  42.793  1.00 49.78  ? 328 ARG C CG  1 
ATOM   10884 C CD  . ARG C 1 328 ? 10.028  20.219  42.011  1.00 48.01  ? 328 ARG C CD  1 
ATOM   10885 N NE  . ARG C 1 328 ? 9.057   20.850  42.895  1.00 58.45  ? 328 ARG C NE  1 
ATOM   10886 C CZ  . ARG C 1 328 ? 7.751   20.628  42.855  1.00 66.32  ? 328 ARG C CZ  1 
ATOM   10887 N NH1 . ARG C 1 328 ? 7.216   19.813  41.960  1.00 65.92  ? 328 ARG C NH1 1 
ATOM   10888 N NH2 . ARG C 1 328 ? 6.962   21.235  43.738  1.00 57.29  ? 328 ARG C NH2 1 
ATOM   10889 N N   . ASP C 1 329 ? 11.442  18.002  47.253  1.00 41.69  ? 329 ASP C N   1 
ATOM   10890 C CA  . ASP C 1 329 ? 11.906  18.192  48.624  1.00 46.75  ? 329 ASP C CA  1 
ATOM   10891 C C   . ASP C 1 329 ? 13.169  17.382  48.889  1.00 41.65  ? 329 ASP C C   1 
ATOM   10892 O O   . ASP C 1 329 ? 14.103  17.866  49.540  1.00 43.44  ? 329 ASP C O   1 
ATOM   10893 C CB  . ASP C 1 329 ? 10.807  17.805  49.612  1.00 42.69  ? 329 ASP C CB  1 
ATOM   10894 C CG  . ASP C 1 329 ? 11.262  17.896  51.057  1.00 41.27  ? 329 ASP C CG  1 
ATOM   10895 O OD1 . ASP C 1 329 ? 11.537  19.022  51.524  1.00 46.62  ? 329 ASP C OD1 1 
ATOM   10896 O OD2 . ASP C 1 329 ? 11.342  16.844  51.726  1.00 39.29  ? 329 ASP C OD2 1 
ATOM   10897 N N   . PHE C 1 330 ? 13.208  16.142  48.394  1.00 42.30  ? 330 PHE C N   1 
ATOM   10898 C CA  . PHE C 1 330 ? 14.392  15.302  48.552  1.00 35.62  ? 330 PHE C CA  1 
ATOM   10899 C C   . PHE C 1 330 ? 15.589  15.888  47.811  1.00 36.02  ? 330 PHE C C   1 
ATOM   10900 O O   . PHE C 1 330 ? 16.702  15.933  48.348  1.00 38.67  ? 330 PHE C O   1 
ATOM   10901 C CB  . PHE C 1 330 ? 14.082  13.890  48.052  1.00 36.50  ? 330 PHE C CB  1 
ATOM   10902 C CG  . PHE C 1 330 ? 15.146  12.880  48.363  1.00 32.98  ? 330 PHE C CG  1 
ATOM   10903 C CD1 . PHE C 1 330 ? 15.130  12.183  49.559  1.00 32.04  ? 330 PHE C CD1 1 
ATOM   10904 C CD2 . PHE C 1 330 ? 16.151  12.609  47.449  1.00 35.83  ? 330 PHE C CD2 1 
ATOM   10905 C CE1 . PHE C 1 330 ? 16.104  11.245  49.844  1.00 33.59  ? 330 PHE C CE1 1 
ATOM   10906 C CE2 . PHE C 1 330 ? 17.129  11.672  47.727  1.00 31.53  ? 330 PHE C CE2 1 
ATOM   10907 C CZ  . PHE C 1 330 ? 17.105  10.989  48.926  1.00 35.47  ? 330 PHE C CZ  1 
ATOM   10908 N N   . ILE C 1 331 ? 15.376  16.345  46.574  1.00 38.21  ? 331 ILE C N   1 
ATOM   10909 C CA  . ILE C 1 331 ? 16.464  16.940  45.802  1.00 37.74  ? 331 ILE C CA  1 
ATOM   10910 C C   . ILE C 1 331 ? 16.921  18.248  46.436  1.00 45.80  ? 331 ILE C C   1 
ATOM   10911 O O   . ILE C 1 331 ? 18.118  18.561  46.453  1.00 47.15  ? 331 ILE C O   1 
ATOM   10912 C CB  . ILE C 1 331 ? 16.033  17.138  44.337  1.00 39.53  ? 331 ILE C CB  1 
ATOM   10913 C CG1 . ILE C 1 331 ? 15.633  15.800  43.715  1.00 37.94  ? 331 ILE C CG1 1 
ATOM   10914 C CG2 . ILE C 1 331 ? 17.144  17.791  43.529  1.00 39.81  ? 331 ILE C CG2 1 
ATOM   10915 C CD1 . ILE C 1 331 ? 16.723  14.769  43.761  1.00 36.41  ? 331 ILE C CD1 1 
ATOM   10916 N N   . GLY C 1 332 ? 15.980  19.032  46.964  1.00 44.54  ? 332 GLY C N   1 
ATOM   10917 C CA  . GLY C 1 332 ? 16.345  20.296  47.584  1.00 44.28  ? 332 GLY C CA  1 
ATOM   10918 C C   . GLY C 1 332 ? 17.193  20.117  48.829  1.00 44.35  ? 332 GLY C C   1 
ATOM   10919 O O   . GLY C 1 332 ? 18.131  20.883  49.067  1.00 44.17  ? 332 GLY C O   1 
ATOM   10920 N N   . ARG C 1 333 ? 16.869  19.113  49.648  1.00 40.42  ? 333 ARG C N   1 
ATOM   10921 C CA  . ARG C 1 333 ? 17.685  18.837  50.826  1.00 42.97  ? 333 ARG C CA  1 
ATOM   10922 C C   . ARG C 1 333 ? 19.086  18.394  50.426  1.00 44.86  ? 333 ARG C C   1 
ATOM   10923 O O   . ARG C 1 333 ? 20.072  18.779  51.065  1.00 49.02  ? 333 ARG C O   1 
ATOM   10924 C CB  . ARG C 1 333 ? 17.015  17.780  51.699  1.00 36.82  ? 333 ARG C CB  1 
ATOM   10925 C CG  . ARG C 1 333 ? 15.840  18.295  52.510  1.00 37.76  ? 333 ARG C CG  1 
ATOM   10926 C CD  . ARG C 1 333 ? 15.060  17.135  53.093  1.00 36.64  ? 333 ARG C CD  1 
ATOM   10927 N NE  . ARG C 1 333 ? 13.779  17.539  53.659  1.00 37.65  ? 333 ARG C NE  1 
ATOM   10928 C CZ  . ARG C 1 333 ? 13.613  17.962  54.904  1.00 38.30  ? 333 ARG C CZ  1 
ATOM   10929 N NH1 . ARG C 1 333 ? 14.638  18.098  55.730  1.00 38.13  ? 333 ARG C NH1 1 
ATOM   10930 N NH2 . ARG C 1 333 ? 12.388  18.255  55.332  1.00 39.31  ? 333 ARG C NH2 1 
ATOM   10931 N N   . LEU C 1 334 ? 19.192  17.577  49.374  1.00 41.37  ? 334 LEU C N   1 
ATOM   10932 C CA  . LEU C 1 334 ? 20.502  17.252  48.819  1.00 47.94  ? 334 LEU C CA  1 
ATOM   10933 C C   . LEU C 1 334 ? 21.220  18.511  48.354  1.00 51.08  ? 334 LEU C C   1 
ATOM   10934 O O   . LEU C 1 334 ? 22.428  18.666  48.572  1.00 53.75  ? 334 LEU C O   1 
ATOM   10935 C CB  . LEU C 1 334 ? 20.358  16.271  47.654  1.00 45.27  ? 334 LEU C CB  1 
ATOM   10936 C CG  . LEU C 1 334 ? 20.080  14.796  47.935  1.00 40.15  ? 334 LEU C CG  1 
ATOM   10937 C CD1 . LEU C 1 334 ? 20.279  13.991  46.662  1.00 34.58  ? 334 LEU C CD1 1 
ATOM   10938 C CD2 . LEU C 1 334 ? 20.974  14.275  49.047  1.00 40.71  ? 334 LEU C CD2 1 
ATOM   10939 N N   . LYS C 1 335 ? 20.487  19.421  47.709  1.00 48.03  ? 335 LYS C N   1 
ATOM   10940 C CA  . LYS C 1 335 ? 21.075  20.676  47.254  1.00 48.47  ? 335 LYS C CA  1 
ATOM   10941 C C   . LYS C 1 335 ? 21.588  21.500  48.427  1.00 49.78  ? 335 LYS C C   1 
ATOM   10942 O O   . LYS C 1 335 ? 22.670  22.096  48.351  1.00 53.88  ? 335 LYS C O   1 
ATOM   10943 C CB  . LYS C 1 335 ? 20.043  21.462  46.446  1.00 51.27  ? 335 LYS C CB  1 
ATOM   10944 C CG  . LYS C 1 335 ? 20.621  22.545  45.558  1.00 44.16  ? 335 LYS C CG  1 
ATOM   10945 C CD  . LYS C 1 335 ? 19.632  22.922  44.467  1.00 52.94  ? 335 LYS C CD  1 
ATOM   10946 C CE  . LYS C 1 335 ? 18.314  23.400  45.055  1.00 51.72  ? 335 LYS C CE  1 
ATOM   10947 N NZ  . LYS C 1 335 ? 17.166  23.132  44.145  1.00 50.00  ? 335 LYS C NZ  1 
ATOM   10948 N N   . LYS C 1 336 ? 20.826  21.544  49.523  1.00 48.42  ? 336 LYS C N   1 
ATOM   10949 C CA  . LYS C 1 336 ? 21.272  22.263  50.712  1.00 49.37  ? 336 LYS C CA  1 
ATOM   10950 C C   . LYS C 1 336 ? 22.518  21.628  51.318  1.00 53.65  ? 336 LYS C C   1 
ATOM   10951 O O   . LYS C 1 336 ? 23.377  22.336  51.856  1.00 60.48  ? 336 LYS C O   1 
ATOM   10952 C CB  . LYS C 1 336 ? 20.148  22.314  51.749  1.00 52.90  ? 336 LYS C CB  1 
ATOM   10953 C CG  . LYS C 1 336 ? 18.971  23.194  51.360  1.00 50.29  ? 336 LYS C CG  1 
ATOM   10954 C CD  . LYS C 1 336 ? 17.824  23.027  52.342  1.00 72.57  ? 336 LYS C CD  1 
ATOM   10955 C CE  . LYS C 1 336 ? 18.198  23.560  53.717  1.00 69.07  ? 336 LYS C CE  1 
ATOM   10956 N NZ  . LYS C 1 336 ? 17.176  23.216  54.745  1.00 63.06  ? 336 LYS C NZ  1 
ATOM   10957 N N   . ILE C 1 337 ? 22.628  20.299  51.254  1.00 52.04  ? 337 ILE C N   1 
ATOM   10958 C CA  . ILE C 1 337 ? 23.808  19.619  51.778  1.00 45.43  ? 337 ILE C CA  1 
ATOM   10959 C C   . ILE C 1 337 ? 25.027  19.912  50.910  1.00 40.71  ? 337 ILE C C   1 
ATOM   10960 O O   . ILE C 1 337 ? 26.141  20.087  51.418  1.00 46.39  ? 337 ILE C O   1 
ATOM   10961 C CB  . ILE C 1 337 ? 23.538  18.107  51.897  1.00 51.46  ? 337 ILE C CB  1 
ATOM   10962 C CG1 . ILE C 1 337 ? 22.592  17.824  53.068  1.00 49.87  ? 337 ILE C CG1 1 
ATOM   10963 C CG2 . ILE C 1 337 ? 24.838  17.333  52.060  1.00 43.91  ? 337 ILE C CG2 1 
ATOM   10964 C CD1 . ILE C 1 337 ? 21.666  16.643  52.845  1.00 35.69  ? 337 ILE C CD1 1 
ATOM   10965 N N   . HIS C 1 338 ? 24.832  19.984  49.591  1.00 45.11  ? 338 HIS C N   1 
ATOM   10966 C CA  . HIS C 1 338 ? 25.945  20.226  48.677  1.00 43.79  ? 338 HIS C CA  1 
ATOM   10967 C C   . HIS C 1 338 ? 26.615  21.565  48.958  1.00 43.87  ? 338 HIS C C   1 
ATOM   10968 O O   . HIS C 1 338 ? 27.846  21.675  48.912  1.00 41.98  ? 338 HIS C O   1 
ATOM   10969 C CB  . HIS C 1 338 ? 25.446  20.167  47.233  1.00 40.04  ? 338 HIS C CB  1 
ATOM   10970 C CG  . HIS C 1 338 ? 26.535  20.023  46.216  1.00 51.97  ? 338 HIS C CG  1 
ATOM   10971 N ND1 . HIS C 1 338 ? 27.086  21.100  45.556  1.00 54.52  ? 338 HIS C ND1 1 
ATOM   10972 C CD2 . HIS C 1 338 ? 27.169  18.926  45.737  1.00 47.62  ? 338 HIS C CD2 1 
ATOM   10973 C CE1 . HIS C 1 338 ? 28.014  20.675  44.717  1.00 48.37  ? 338 HIS C CE1 1 
ATOM   10974 N NE2 . HIS C 1 338 ? 28.085  19.359  44.809  1.00 43.20  ? 338 HIS C NE2 1 
ATOM   10975 N N   . GLU C 1 339 ? 25.824  22.592  49.257  1.00 54.84  ? 339 GLU C N   1 
ATOM   10976 C CA  . GLU C 1 339 ? 26.329  23.942  49.467  1.00 59.72  ? 339 GLU C CA  1 
ATOM   10977 C C   . GLU C 1 339 ? 26.647  24.250  50.926  1.00 61.63  ? 339 GLU C C   1 
ATOM   10978 O O   . GLU C 1 339 ? 27.099  25.361  51.222  1.00 57.07  ? 339 GLU C O   1 
ATOM   10979 C CB  . GLU C 1 339 ? 25.319  24.963  48.933  1.00 53.10  ? 339 GLU C CB  1 
ATOM   10980 C CG  . GLU C 1 339 ? 24.034  25.044  49.739  1.00 62.04  ? 339 GLU C CG  1 
ATOM   10981 C CD  . GLU C 1 339 ? 23.219  26.277  49.410  1.00 76.30  ? 339 GLU C CD  1 
ATOM   10982 O OE1 . GLU C 1 339 ? 22.565  26.291  48.345  1.00 68.07  ? 339 GLU C OE1 1 
ATOM   10983 O OE2 . GLU C 1 339 ? 23.235  27.233  50.214  1.00 85.93  ? 339 GLU C OE2 1 
ATOM   10984 N N   . SER C 1 340 ? 26.416  23.309  51.842  1.00 56.54  ? 340 SER C N   1 
ATOM   10985 C CA  . SER C 1 340 ? 26.759  23.509  53.243  1.00 57.10  ? 340 SER C CA  1 
ATOM   10986 C C   . SER C 1 340 ? 28.134  22.964  53.602  1.00 59.33  ? 340 SER C C   1 
ATOM   10987 O O   . SER C 1 340 ? 28.644  23.276  54.683  1.00 63.58  ? 340 SER C O   1 
ATOM   10988 C CB  . SER C 1 340 ? 25.706  22.858  54.146  1.00 54.95  ? 340 SER C CB  1 
ATOM   10989 O OG  . SER C 1 340 ? 25.735  21.447  54.024  1.00 50.79  ? 340 SER C OG  1 
ATOM   10990 N N   . VAL C 1 341 ? 28.739  22.163  52.730  1.00 57.41  ? 341 VAL C N   1 
ATOM   10991 C CA  . VAL C 1 341 ? 30.043  21.564  52.977  1.00 57.00  ? 341 VAL C CA  1 
ATOM   10992 C C   . VAL C 1 341 ? 30.981  21.953  51.843  1.00 62.76  ? 341 VAL C C   1 
ATOM   10993 O O   . VAL C 1 341 ? 30.557  22.144  50.698  1.00 69.08  ? 341 VAL C O   1 
ATOM   10994 C CB  . VAL C 1 341 ? 29.946  20.027  53.123  1.00 52.84  ? 341 VAL C CB  1 
ATOM   10995 C CG1 . VAL C 1 341 ? 28.794  19.652  54.050  1.00 56.86  ? 341 VAL C CG1 1 
ATOM   10996 C CG2 . VAL C 1 341 ? 29.775  19.356  51.766  1.00 54.71  ? 341 VAL C CG2 1 
ATOM   10997 N N   . ASP C 1 342 ? 32.264  22.100  52.174  1.00 60.90  ? 342 ASP C N   1 
ATOM   10998 C CA  . ASP C 1 342 ? 33.282  22.461  51.195  1.00 65.76  ? 342 ASP C CA  1 
ATOM   10999 C C   . ASP C 1 342 ? 34.187  21.282  50.847  1.00 57.50  ? 342 ASP C C   1 
ATOM   11000 O O   . ASP C 1 342 ? 35.345  21.467  50.467  1.00 52.90  ? 342 ASP C O   1 
ATOM   11001 C CB  . ASP C 1 342 ? 34.107  23.650  51.684  1.00 72.37  ? 342 ASP C CB  1 
ATOM   11002 C CG  . ASP C 1 342 ? 34.665  23.446  53.076  1.00 87.51  ? 342 ASP C CG  1 
ATOM   11003 O OD1 . ASP C 1 342 ? 33.869  23.443  54.038  1.00 81.53  ? 342 ASP C OD1 1 
ATOM   11004 O OD2 . ASP C 1 342 ? 35.899  23.299  53.208  1.00 96.34  ? 342 ASP C OD2 1 
ATOM   11005 N N   . PHE C 1 343 ? 33.671  20.066  50.986  1.00 59.63  ? 343 PHE C N   1 
ATOM   11006 C CA  . PHE C 1 343 ? 34.304  18.858  50.469  1.00 51.36  ? 343 PHE C CA  1 
ATOM   11007 C C   . PHE C 1 343 ? 33.290  18.136  49.587  1.00 54.36  ? 343 PHE C C   1 
ATOM   11008 O O   . PHE C 1 343 ? 32.172  18.618  49.377  1.00 51.54  ? 343 PHE C O   1 
ATOM   11009 C CB  . PHE C 1 343 ? 34.811  17.942  51.593  1.00 48.22  ? 343 PHE C CB  1 
ATOM   11010 C CG  . PHE C 1 343 ? 33.787  17.633  52.654  1.00 51.33  ? 343 PHE C CG  1 
ATOM   11011 C CD1 . PHE C 1 343 ? 33.457  18.575  53.618  1.00 57.95  ? 343 PHE C CD1 1 
ATOM   11012 C CD2 . PHE C 1 343 ? 33.158  16.399  52.687  1.00 54.20  ? 343 PHE C CD2 1 
ATOM   11013 C CE1 . PHE C 1 343 ? 32.516  18.290  54.589  1.00 59.31  ? 343 PHE C CE1 1 
ATOM   11014 C CE2 . PHE C 1 343 ? 32.214  16.106  53.656  1.00 50.38  ? 343 PHE C CE2 1 
ATOM   11015 C CZ  . PHE C 1 343 ? 31.894  17.057  54.609  1.00 57.43  ? 343 PHE C CZ  1 
ATOM   11016 N N   . GLN C 1 344 ? 33.678  16.982  49.052  1.00 44.99  ? 344 GLN C N   1 
ATOM   11017 C CA  . GLN C 1 344 ? 32.734  16.211  48.257  1.00 43.34  ? 344 GLN C CA  1 
ATOM   11018 C C   . GLN C 1 344 ? 31.931  15.297  49.174  1.00 45.70  ? 344 GLN C C   1 
ATOM   11019 O O   . GLN C 1 344 ? 32.436  14.257  49.616  1.00 52.70  ? 344 GLN C O   1 
ATOM   11020 C CB  . GLN C 1 344 ? 33.451  15.411  47.167  1.00 37.76  ? 344 GLN C CB  1 
ATOM   11021 C CG  . GLN C 1 344 ? 33.194  15.943  45.760  1.00 40.26  ? 344 GLN C CG  1 
ATOM   11022 C CD  . GLN C 1 344 ? 33.901  15.144  44.682  1.00 40.40  ? 344 GLN C CD  1 
ATOM   11023 O OE1 . GLN C 1 344 ? 34.652  14.215  44.973  1.00 52.79  ? 344 GLN C OE1 1 
ATOM   11024 N NE2 . GLN C 1 344 ? 33.661  15.505  43.425  1.00 39.50  ? 344 GLN C NE2 1 
ATOM   11025 N N   . PRO C 1 345 ? 30.682  15.647  49.478  1.00 40.22  ? 345 PRO C N   1 
ATOM   11026 C CA  . PRO C 1 345 ? 29.934  14.896  50.489  1.00 42.62  ? 345 PRO C CA  1 
ATOM   11027 C C   . PRO C 1 345 ? 29.499  13.532  49.980  1.00 39.00  ? 345 PRO C C   1 
ATOM   11028 O O   . PRO C 1 345 ? 29.283  13.324  48.783  1.00 44.54  ? 345 PRO C O   1 
ATOM   11029 C CB  . PRO C 1 345 ? 28.725  15.794  50.766  1.00 41.24  ? 345 PRO C CB  1 
ATOM   11030 C CG  . PRO C 1 345 ? 28.488  16.482  49.463  1.00 40.98  ? 345 PRO C CG  1 
ATOM   11031 C CD  . PRO C 1 345 ? 29.845  16.666  48.818  1.00 43.71  ? 345 PRO C CD  1 
ATOM   11032 N N   . VAL C 1 346 ? 29.376  12.593  50.915  1.00 42.67  ? 346 VAL C N   1 
ATOM   11033 C CA  . VAL C 1 346 ? 28.829  11.268  50.647  1.00 36.45  ? 346 VAL C CA  1 
ATOM   11034 C C   . VAL C 1 346 ? 27.610  11.089  51.538  1.00 41.34  ? 346 VAL C C   1 
ATOM   11035 O O   . VAL C 1 346 ? 27.722  11.143  52.769  1.00 38.02  ? 346 VAL C O   1 
ATOM   11036 C CB  . VAL C 1 346 ? 29.859  10.155  50.894  1.00 31.25  ? 346 VAL C CB  1 
ATOM   11037 C CG1 . VAL C 1 346 ? 29.427  8.875   50.197  1.00 30.37  ? 346 VAL C CG1 1 
ATOM   11038 C CG2 . VAL C 1 346 ? 31.236  10.587  50.414  1.00 38.54  ? 346 VAL C CG2 1 
ATOM   11039 N N   . VAL C 1 347 ? 26.452  10.874  50.923  1.00 41.36  ? 347 VAL C N   1 
ATOM   11040 C CA  . VAL C 1 347 ? 25.191  10.725  51.639  1.00 35.08  ? 347 VAL C CA  1 
ATOM   11041 C C   . VAL C 1 347 ? 24.746  9.276   51.515  1.00 36.84  ? 347 VAL C C   1 
ATOM   11042 O O   . VAL C 1 347 ? 24.562  8.766   50.402  1.00 39.47  ? 347 VAL C O   1 
ATOM   11043 C CB  . VAL C 1 347 ? 24.115  11.682  51.104  1.00 30.47  ? 347 VAL C CB  1 
ATOM   11044 C CG1 . VAL C 1 347 ? 22.773  11.384  51.753  1.00 32.33  ? 347 VAL C CG1 1 
ATOM   11045 C CG2 . VAL C 1 347 ? 24.522  13.128  51.349  1.00 34.07  ? 347 VAL C CG2 1 
ATOM   11046 N N   . PHE C 1 348 ? 24.577  8.612   52.654  1.00 38.69  ? 348 PHE C N   1 
ATOM   11047 C CA  . PHE C 1 348 ? 24.059  7.252   52.703  1.00 28.08  ? 348 PHE C CA  1 
ATOM   11048 C C   . PHE C 1 348 ? 22.576  7.307   53.048  1.00 28.98  ? 348 PHE C C   1 
ATOM   11049 O O   . PHE C 1 348 ? 22.199  7.811   54.112  1.00 28.28  ? 348 PHE C O   1 
ATOM   11050 C CB  . PHE C 1 348 ? 24.820  6.410   53.726  1.00 40.91  ? 348 PHE C CB  1 
ATOM   11051 C CG  . PHE C 1 348 ? 25.886  5.538   53.124  1.00 36.37  ? 348 PHE C CG  1 
ATOM   11052 C CD1 . PHE C 1 348 ? 27.012  6.100   52.544  1.00 28.88  ? 348 PHE C CD1 1 
ATOM   11053 C CD2 . PHE C 1 348 ? 25.762  4.156   53.142  1.00 29.58  ? 348 PHE C CD2 1 
ATOM   11054 C CE1 . PHE C 1 348 ? 27.994  5.303   51.988  1.00 28.19  ? 348 PHE C CE1 1 
ATOM   11055 C CE2 . PHE C 1 348 ? 26.741  3.352   52.589  1.00 32.22  ? 348 PHE C CE2 1 
ATOM   11056 C CZ  . PHE C 1 348 ? 27.861  3.927   52.011  1.00 34.22  ? 348 PHE C CZ  1 
ATOM   11057 N N   . VAL C 1 349 ? 21.741  6.802   52.147  1.00 33.91  ? 349 VAL C N   1 
ATOM   11058 C CA  . VAL C 1 349 ? 20.306  6.684   52.370  1.00 31.49  ? 349 VAL C CA  1 
ATOM   11059 C C   . VAL C 1 349 ? 20.027  5.204   52.595  1.00 29.36  ? 349 VAL C C   1 
ATOM   11060 O O   . VAL C 1 349 ? 19.903  4.431   51.639  1.00 31.83  ? 349 VAL C O   1 
ATOM   11061 C CB  . VAL C 1 349 ? 19.492  7.244   51.199  1.00 31.10  ? 349 VAL C CB  1 
ATOM   11062 C CG1 . VAL C 1 349 ? 18.014  7.296   51.557  1.00 33.27  ? 349 VAL C CG1 1 
ATOM   11063 C CG2 . VAL C 1 349 ? 19.996  8.624   50.820  1.00 33.79  ? 349 VAL C CG2 1 
ATOM   11064 N N   . VAL C 1 350 ? 19.977  4.830   53.867  1.00 31.59  ? 350 VAL C N   1 
ATOM   11065 C CA  . VAL C 1 350 ? 19.765  3.461   54.305  1.00 33.60  ? 350 VAL C CA  1 
ATOM   11066 C C   . VAL C 1 350 ? 18.451  3.243   55.015  1.00 33.80  ? 350 VAL C C   1 
ATOM   11067 O O   . VAL C 1 350 ? 18.111  3.939   55.919  1.00 29.26  ? 350 VAL C O   1 
ATOM   11068 C CB  . VAL C 1 350 ? 20.928  2.944   55.146  1.00 26.32  ? 350 VAL C CB  1 
ATOM   11069 C CG1 . VAL C 1 350 ? 20.671  1.530   55.529  1.00 36.66  ? 350 VAL C CG1 1 
ATOM   11070 C CG2 . VAL C 1 350 ? 22.176  2.969   54.345  1.00 26.24  ? 350 VAL C CG2 1 
ATOM   11071 N N   . LEU C 1 351 ? 17.732  2.235   54.568  1.00 32.22  ? 351 LEU C N   1 
ATOM   11072 C CA  . LEU C 1 351 ? 16.420  1.955   55.062  1.00 28.20  ? 351 LEU C CA  1 
ATOM   11073 C C   . LEU C 1 351 ? 15.845  0.598   54.649  1.00 33.24  ? 351 LEU C C   1 
ATOM   11074 O O   . LEU C 1 351 ? 16.283  0.017   53.703  1.00 34.29  ? 351 LEU C O   1 
ATOM   11075 C CB  . LEU C 1 351 ? 15.578  3.042   54.436  1.00 31.07  ? 351 LEU C CB  1 
ATOM   11076 C CG  . LEU C 1 351 ? 14.119  3.147   54.673  1.00 34.67  ? 351 LEU C CG  1 
ATOM   11077 C CD1 . LEU C 1 351 ? 13.898  3.733   56.039  1.00 32.76  ? 351 LEU C CD1 1 
ATOM   11078 C CD2 . LEU C 1 351 ? 13.596  4.040   53.592  1.00 32.72  ? 351 LEU C CD2 1 
ATOM   11079 N N   . ASP C 1 352 ? 14.846  0.112   55.380  1.00 33.34  ? 352 ASP C N   1 
ATOM   11080 C CA  . ASP C 1 352 ? 14.155  -1.133  55.095  1.00 26.26  ? 352 ASP C CA  1 
ATOM   11081 C C   . ASP C 1 352 ? 13.432  -0.852  53.841  1.00 30.73  ? 352 ASP C C   1 
ATOM   11082 O O   . ASP C 1 352 ? 12.530  -0.043  53.816  1.00 37.90  ? 352 ASP C O   1 
ATOM   11083 C CB  . ASP C 1 352 ? 13.104  -1.413  56.139  1.00 37.85  ? 352 ASP C CB  1 
ATOM   11084 C CG  . ASP C 1 352 ? 13.678  -1.864  57.450  1.00 57.52  ? 352 ASP C CG  1 
ATOM   11085 O OD1 . ASP C 1 352 ? 14.891  -1.726  57.625  1.00 56.67  ? 352 ASP C OD1 1 
ATOM   11086 O OD2 . ASP C 1 352 ? 12.911  -2.366  58.303  1.00 60.36  ? 352 ASP C OD2 1 
ATOM   11087 N N   . GLY C 1 353 ? 13.795  -1.522  52.780  1.00 27.88  ? 353 GLY C N   1 
ATOM   11088 C CA  . GLY C 1 353 ? 13.225  -1.174  51.495  1.00 32.50  ? 353 GLY C CA  1 
ATOM   11089 C C   . GLY C 1 353 ? 12.006  -1.953  51.044  1.00 35.60  ? 353 GLY C C   1 
ATOM   11090 O O   . GLY C 1 353 ? 11.809  -2.129  49.838  1.00 36.71  ? 353 GLY C O   1 
ATOM   11091 N N   . GLU C 1 354 ? 11.179  -2.428  51.978  1.00 34.35  ? 354 GLU C N   1 
ATOM   11092 C CA  . GLU C 1 354 ? 9.952   -3.113  51.577  1.00 32.32  ? 354 GLU C CA  1 
ATOM   11093 C C   . GLU C 1 354 ? 8.712   -2.751  52.384  1.00 35.07  ? 354 GLU C C   1 
ATOM   11094 O O   . GLU C 1 354 ? 7.604   -3.010  51.902  1.00 33.80  ? 354 GLU C O   1 
ATOM   11095 C CB  . GLU C 1 354 ? 10.145  -4.633  51.644  1.00 27.77  ? 354 GLU C CB  1 
ATOM   11096 C CG  . GLU C 1 354 ? 10.184  -5.186  53.057  1.00 34.58  ? 354 GLU C CG  1 
ATOM   11097 C CD  . GLU C 1 354 ? 11.580  -5.576  53.489  1.00 36.80  ? 354 GLU C CD  1 
ATOM   11098 O OE1 . GLU C 1 354 ? 12.365  -4.672  53.844  1.00 49.19  ? 354 GLU C OE1 1 
ATOM   11099 O OE2 . GLU C 1 354 ? 11.894  -6.784  53.476  1.00 36.09  ? 354 GLU C OE2 1 
ATOM   11100 N N   . ASN C 1 355 ? 8.829   -2.151  53.568  1.00 37.32  ? 355 ASN C N   1 
ATOM   11101 C CA  . ASN C 1 355 ? 7.673   -2.006  54.446  1.00 37.19  ? 355 ASN C CA  1 
ATOM   11102 C C   . ASN C 1 355 ? 6.956   -0.670  54.308  1.00 40.65  ? 355 ASN C C   1 
ATOM   11103 O O   . ASN C 1 355 ? 5.884   -0.502  54.900  1.00 52.39  ? 355 ASN C O   1 
ATOM   11104 C CB  . ASN C 1 355 ? 8.088   -2.199  55.909  1.00 36.37  ? 355 ASN C CB  1 
ATOM   11105 C CG  . ASN C 1 355 ? 6.947   -2.699  56.775  1.00 48.14  ? 355 ASN C CG  1 
ATOM   11106 O OD1 . ASN C 1 355 ? 5.937   -3.188  56.270  1.00 48.03  ? 355 ASN C OD1 1 
ATOM   11107 N ND2 . ASN C 1 355 ? 7.100   -2.570  58.088  1.00 41.35  ? 355 ASN C ND2 1 
ATOM   11108 N N   . CYS C 1 356 ? 7.502   0.276   53.547  1.00 37.57  ? 356 CYS C N   1 
ATOM   11109 C CA  . CYS C 1 356 ? 6.896   1.595   53.441  1.00 36.81  ? 356 CYS C CA  1 
ATOM   11110 C C   . CYS C 1 356 ? 6.132   1.810   52.141  1.00 36.02  ? 356 CYS C C   1 
ATOM   11111 O O   . CYS C 1 356 ? 5.339   2.754   52.057  1.00 39.07  ? 356 CYS C O   1 
ATOM   11112 C CB  . CYS C 1 356 ? 7.968   2.684   53.580  1.00 36.58  ? 356 CYS C CB  1 
ATOM   11113 S SG  . CYS C 1 356 ? 9.272   2.633   52.324  1.00 37.56  ? 356 CYS C SG  1 
ATOM   11114 N N   . TRP C 1 357 ? 6.340   0.960   51.135  1.00 30.34  ? 357 TRP C N   1 
ATOM   11115 C CA  . TRP C 1 357 ? 5.691   1.157   49.845  1.00 31.13  ? 357 TRP C CA  1 
ATOM   11116 C C   . TRP C 1 357 ? 4.212   0.793   49.858  1.00 43.43  ? 357 TRP C C   1 
ATOM   11117 O O   . TRP C 1 357 ? 3.499   1.149   48.914  1.00 47.56  ? 357 TRP C O   1 
ATOM   11118 C CB  . TRP C 1 357 ? 6.423   0.353   48.771  1.00 30.82  ? 357 TRP C CB  1 
ATOM   11119 C CG  . TRP C 1 357 ? 7.909   0.568   48.777  1.00 32.66  ? 357 TRP C CG  1 
ATOM   11120 C CD1 . TRP C 1 357 ? 8.874   -0.396  48.800  1.00 42.02  ? 357 TRP C CD1 1 
ATOM   11121 C CD2 . TRP C 1 357 ? 8.600   1.826   48.759  1.00 33.15  ? 357 TRP C CD2 1 
ATOM   11122 N NE1 . TRP C 1 357 ? 10.122  0.181   48.799  1.00 36.38  ? 357 TRP C NE1 1 
ATOM   11123 C CE2 . TRP C 1 357 ? 9.981   1.544   48.773  1.00 28.67  ? 357 TRP C CE2 1 
ATOM   11124 C CE3 . TRP C 1 357 ? 8.186   3.163   48.731  1.00 30.96  ? 357 TRP C CE3 1 
ATOM   11125 C CZ2 . TRP C 1 357 ? 10.948  2.547   48.762  1.00 30.25  ? 357 TRP C CZ2 1 
ATOM   11126 C CZ3 . TRP C 1 357 ? 9.148   4.157   48.720  1.00 33.56  ? 357 TRP C CZ3 1 
ATOM   11127 C CH2 . TRP C 1 357 ? 10.512  3.843   48.735  1.00 42.66  ? 357 TRP C CH2 1 
ATOM   11128 N N   . GLU C 1 358 ? 3.733   0.108   50.895  1.00 48.74  ? 358 GLU C N   1 
ATOM   11129 C CA  . GLU C 1 358 ? 2.319   -0.226  51.001  1.00 43.87  ? 358 GLU C CA  1 
ATOM   11130 C C   . GLU C 1 358 ? 1.472   0.940   51.494  1.00 36.79  ? 358 GLU C C   1 
ATOM   11131 O O   . GLU C 1 358 ? 0.244   0.818   51.537  1.00 37.51  ? 358 GLU C O   1 
ATOM   11132 C CB  . GLU C 1 358 ? 2.130   -1.431  51.926  1.00 45.94  ? 358 GLU C CB  1 
ATOM   11133 C CG  . GLU C 1 358 ? 2.963   -1.383  53.196  1.00 45.85  ? 358 GLU C CG  1 
ATOM   11134 C CD  . GLU C 1 358 ? 3.311   -2.764  53.711  1.00 54.15  ? 358 GLU C CD  1 
ATOM   11135 O OE1 . GLU C 1 358 ? 2.426   -3.417  54.304  1.00 54.22  ? 358 GLU C OE1 1 
ATOM   11136 O OE2 . GLU C 1 358 ? 4.466   -3.198  53.518  1.00 53.80  ? 358 GLU C OE2 1 
ATOM   11137 N N   . TYR C 1 359 ? 2.094   2.060   51.869  1.00 38.33  ? 359 TYR C N   1 
ATOM   11138 C CA  . TYR C 1 359 ? 1.368   3.245   52.299  1.00 40.70  ? 359 TYR C CA  1 
ATOM   11139 C C   . TYR C 1 359 ? 1.429   4.385   51.295  1.00 37.44  ? 359 TYR C C   1 
ATOM   11140 O O   . TYR C 1 359 ? 0.644   5.331   51.411  1.00 37.18  ? 359 TYR C O   1 
ATOM   11141 C CB  . TYR C 1 359 ? 1.901   3.727   53.656  1.00 35.84  ? 359 TYR C CB  1 
ATOM   11142 C CG  . TYR C 1 359 ? 1.682   2.720   54.764  1.00 34.68  ? 359 TYR C CG  1 
ATOM   11143 C CD1 . TYR C 1 359 ? 2.632   1.745   55.041  1.00 40.93  ? 359 TYR C CD1 1 
ATOM   11144 C CD2 . TYR C 1 359 ? 0.519   2.736   55.526  1.00 38.16  ? 359 TYR C CD2 1 
ATOM   11145 C CE1 . TYR C 1 359 ? 2.433   0.818   56.048  1.00 45.64  ? 359 TYR C CE1 1 
ATOM   11146 C CE2 . TYR C 1 359 ? 0.312   1.813   56.536  1.00 37.10  ? 359 TYR C CE2 1 
ATOM   11147 C CZ  . TYR C 1 359 ? 1.271   0.857   56.793  1.00 42.48  ? 359 TYR C CZ  1 
ATOM   11148 O OH  . TYR C 1 359 ? 1.070   -0.064  57.797  1.00 34.96  ? 359 TYR C OH  1 
ATOM   11149 N N   . TYR C 1 360 ? 2.338   4.324   50.326  1.00 38.87  ? 360 TYR C N   1 
ATOM   11150 C CA  . TYR C 1 360 ? 2.345   5.264   49.219  1.00 37.49  ? 360 TYR C CA  1 
ATOM   11151 C C   . TYR C 1 360 ? 1.212   4.943   48.250  1.00 38.37  ? 360 TYR C C   1 
ATOM   11152 O O   . TYR C 1 360 ? 0.706   3.818   48.193  1.00 43.03  ? 360 TYR C O   1 
ATOM   11153 C CB  . TYR C 1 360 ? 3.668   5.204   48.458  1.00 40.94  ? 360 TYR C CB  1 
ATOM   11154 C CG  . TYR C 1 360 ? 4.855   5.864   49.119  1.00 38.78  ? 360 TYR C CG  1 
ATOM   11155 C CD1 . TYR C 1 360 ? 5.278   5.479   50.382  1.00 33.04  ? 360 TYR C CD1 1 
ATOM   11156 C CD2 . TYR C 1 360 ? 5.581   6.845   48.455  1.00 34.34  ? 360 TYR C CD2 1 
ATOM   11157 C CE1 . TYR C 1 360 ? 6.374   6.071   50.978  1.00 32.36  ? 360 TYR C CE1 1 
ATOM   11158 C CE2 . TYR C 1 360 ? 6.677   7.442   49.041  1.00 33.42  ? 360 TYR C CE2 1 
ATOM   11159 C CZ  . TYR C 1 360 ? 7.069   7.050   50.303  1.00 32.54  ? 360 TYR C CZ  1 
ATOM   11160 O OH  . TYR C 1 360 ? 8.162   7.636   50.894  1.00 32.00  ? 360 TYR C OH  1 
ATOM   11161 N N   . GLU C 1 361 ? 0.821   5.947   47.471  1.00 38.57  ? 361 GLU C N   1 
ATOM   11162 C CA  . GLU C 1 361 ? -0.122  5.712   46.388  1.00 46.58  ? 361 GLU C CA  1 
ATOM   11163 C C   . GLU C 1 361 ? 0.547   4.893   45.289  1.00 46.57  ? 361 GLU C C   1 
ATOM   11164 O O   . GLU C 1 361 ? 1.647   5.226   44.838  1.00 46.12  ? 361 GLU C O   1 
ATOM   11165 C CB  . GLU C 1 361 ? -0.636  7.037   45.827  1.00 60.40  ? 361 GLU C CB  1 
ATOM   11166 C CG  . GLU C 1 361 ? -2.140  7.074   45.597  1.00 64.33  ? 361 GLU C CG  1 
ATOM   11167 C CD  . GLU C 1 361 ? -2.931  7.063   46.892  1.00 61.52  ? 361 GLU C CD  1 
ATOM   11168 O OE1 . GLU C 1 361 ? -2.818  8.036   47.666  1.00 66.60  ? 361 GLU C OE1 1 
ATOM   11169 O OE2 . GLU C 1 361 ? -3.668  6.083   47.134  1.00 57.28  ? 361 GLU C OE2 1 
ATOM   11170 N N   . GLU C 1 362 ? -0.120  3.814   44.870  1.00 42.14  ? 362 GLU C N   1 
ATOM   11171 C CA  . GLU C 1 362 ? 0.354   2.949   43.788  1.00 39.61  ? 362 GLU C CA  1 
ATOM   11172 C C   . GLU C 1 362 ? 1.727   2.351   44.097  1.00 37.67  ? 362 GLU C C   1 
ATOM   11173 O O   . GLU C 1 362 ? 2.648   2.406   43.278  1.00 39.57  ? 362 GLU C O   1 
ATOM   11174 C CB  . GLU C 1 362 ? 0.382   3.702   42.455  1.00 47.24  ? 362 GLU C CB  1 
ATOM   11175 C CG  . GLU C 1 362 ? -0.954  3.774   41.736  1.00 58.36  ? 362 GLU C CG  1 
ATOM   11176 C CD  . GLU C 1 362 ? -1.671  5.087   41.980  1.00 75.17  ? 362 GLU C CD  1 
ATOM   11177 O OE1 . GLU C 1 362 ? -0.997  6.140   41.991  1.00 74.08  ? 362 GLU C OE1 1 
ATOM   11178 O OE2 . GLU C 1 362 ? -2.909  5.069   42.151  1.00 71.90  ? 362 GLU C OE2 1 
ATOM   11179 N N   . ASN C 1 363 ? 1.864   1.784   45.298  1.00 43.82  ? 363 ASN C N   1 
ATOM   11180 C CA  . ASN C 1 363 ? 3.059   1.043   45.708  1.00 40.36  ? 363 ASN C CA  1 
ATOM   11181 C C   . ASN C 1 363 ? 4.309   1.925   45.731  1.00 36.86  ? 363 ASN C C   1 
ATOM   11182 O O   . ASN C 1 363 ? 5.436   1.422   45.757  1.00 35.62  ? 363 ASN C O   1 
ATOM   11183 C CB  . ASN C 1 363 ? 3.274   -0.182  44.801  1.00 48.44  ? 363 ASN C CB  1 
ATOM   11184 C CG  . ASN C 1 363 ? 4.344   -1.132  45.319  1.00 45.21  ? 363 ASN C CG  1 
ATOM   11185 O OD1 . ASN C 1 363 ? 4.678   -1.127  46.502  1.00 35.44  ? 363 ASN C OD1 1 
ATOM   11186 N ND2 . ASN C 1 363 ? 4.893   -1.948  44.423  1.00 49.75  ? 363 ASN C ND2 1 
ATOM   11187 N N   . GLY C 1 364 ? 4.142   3.245   45.720  1.00 34.72  ? 364 GLY C N   1 
ATOM   11188 C CA  . GLY C 1 364 ? 5.297   4.107   45.590  1.00 38.57  ? 364 GLY C CA  1 
ATOM   11189 C C   . GLY C 1 364 ? 5.948   4.075   44.230  1.00 42.40  ? 364 GLY C C   1 
ATOM   11190 O O   . GLY C 1 364 ? 7.004   4.686   44.049  1.00 39.88  ? 364 GLY C O   1 
ATOM   11191 N N   . ILE C 1 365 ? 5.348   3.367   43.270  1.00 43.19  ? 365 ILE C N   1 
ATOM   11192 C CA  . ILE C 1 365 ? 5.895   3.346   41.911  1.00 42.61  ? 365 ILE C CA  1 
ATOM   11193 C C   . ILE C 1 365 ? 5.998   4.745   41.328  1.00 46.56  ? 365 ILE C C   1 
ATOM   11194 O O   . ILE C 1 365 ? 7.038   5.068   40.730  1.00 43.36  ? 365 ILE C O   1 
ATOM   11195 C CB  . ILE C 1 365 ? 5.089   2.380   41.035  1.00 40.81  ? 365 ILE C CB  1 
ATOM   11196 C CG1 . ILE C 1 365 ? 5.239   0.954   41.562  1.00 35.73  ? 365 ILE C CG1 1 
ATOM   11197 C CG2 . ILE C 1 365 ? 5.531   2.479   39.583  1.00 41.61  ? 365 ILE C CG2 1 
ATOM   11198 C CD1 . ILE C 1 365 ? 4.188   0.011   41.061  1.00 36.82  ? 365 ILE C CD1 1 
ATOM   11199 N N   . PRO C 1 366 ? 4.990   5.624   41.437  1.00 40.59  ? 366 PRO C N   1 
ATOM   11200 C CA  . PRO C 1 366 ? 5.198   7.002   40.964  1.00 42.46  ? 366 PRO C CA  1 
ATOM   11201 C C   . PRO C 1 366 ? 6.319   7.734   41.685  1.00 41.23  ? 366 PRO C C   1 
ATOM   11202 O O   . PRO C 1 366 ? 7.041   8.512   41.051  1.00 38.46  ? 366 PRO C O   1 
ATOM   11203 C CB  . PRO C 1 366 ? 3.830   7.660   41.205  1.00 40.62  ? 366 PRO C CB  1 
ATOM   11204 C CG  . PRO C 1 366 ? 3.193   6.823   42.260  1.00 40.35  ? 366 PRO C CG  1 
ATOM   11205 C CD  . PRO C 1 366 ? 3.607   5.431   41.909  1.00 38.84  ? 366 PRO C CD  1 
ATOM   11206 N N   . PHE C 1 367 ? 6.497   7.505   42.989  1.00 36.69  ? 367 PHE C N   1 
ATOM   11207 C CA  . PHE C 1 367 ? 7.517   8.249   43.724  1.00 35.88  ? 367 PHE C CA  1 
ATOM   11208 C C   . PHE C 1 367 ? 8.921   7.822   43.313  1.00 34.83  ? 367 PHE C C   1 
ATOM   11209 O O   . PHE C 1 367 ? 9.794   8.666   43.076  1.00 36.75  ? 367 PHE C O   1 
ATOM   11210 C CB  . PHE C 1 367 ? 7.332   8.071   45.231  1.00 34.98  ? 367 PHE C CB  1 
ATOM   11211 C CG  . PHE C 1 367 ? 8.549   8.447   46.030  1.00 33.92  ? 367 PHE C CG  1 
ATOM   11212 C CD1 . PHE C 1 367 ? 8.899   9.777   46.191  1.00 34.58  ? 367 PHE C CD1 1 
ATOM   11213 C CD2 . PHE C 1 367 ? 9.350   7.474   46.608  1.00 32.45  ? 367 PHE C CD2 1 
ATOM   11214 C CE1 . PHE C 1 367 ? 10.019  10.132  46.917  1.00 33.77  ? 367 PHE C CE1 1 
ATOM   11215 C CE2 . PHE C 1 367 ? 10.473  7.824   47.337  1.00 31.67  ? 367 PHE C CE2 1 
ATOM   11216 C CZ  . PHE C 1 367 ? 10.807  9.155   47.491  1.00 32.32  ? 367 PHE C CZ  1 
ATOM   11217 N N   . LEU C 1 368 ? 9.163   6.512   43.234  1.00 34.64  ? 368 LEU C N   1 
ATOM   11218 C CA  . LEU C 1 368 ? 10.505  6.033   42.919  1.00 35.56  ? 368 LEU C CA  1 
ATOM   11219 C C   . LEU C 1 368 ? 10.876  6.325   41.472  1.00 41.57  ? 368 LEU C C   1 
ATOM   11220 O O   . LEU C 1 368 ? 12.011  6.723   41.187  1.00 41.85  ? 368 LEU C O   1 
ATOM   11221 C CB  . LEU C 1 368 ? 10.613  4.539   43.219  1.00 31.98  ? 368 LEU C CB  1 
ATOM   11222 C CG  . LEU C 1 368 ? 10.908  4.231   44.688  1.00 30.79  ? 368 LEU C CG  1 
ATOM   11223 C CD1 . LEU C 1 368 ? 10.713  2.754   44.986  1.00 30.18  ? 368 LEU C CD1 1 
ATOM   11224 C CD2 . LEU C 1 368 ? 12.316  4.680   45.050  1.00 30.06  ? 368 LEU C CD2 1 
ATOM   11225 N N   . GLU C 1 369 ? 9.935   6.136   40.545  1.00 44.01  ? 369 GLU C N   1 
ATOM   11226 C CA  . GLU C 1 369 ? 10.203  6.469   39.150  1.00 36.49  ? 369 GLU C CA  1 
ATOM   11227 C C   . GLU C 1 369 ? 10.450  7.962   38.980  1.00 37.43  ? 369 GLU C C   1 
ATOM   11228 O O   . GLU C 1 369 ? 11.316  8.371   38.197  1.00 37.94  ? 369 GLU C O   1 
ATOM   11229 C CB  . GLU C 1 369 ? 9.045   6.006   38.266  1.00 40.79  ? 369 GLU C CB  1 
ATOM   11230 C CG  . GLU C 1 369 ? 8.972   4.499   38.086  1.00 42.78  ? 369 GLU C CG  1 
ATOM   11231 C CD  . GLU C 1 369 ? 8.088   4.094   36.926  1.00 56.02  ? 369 GLU C CD  1 
ATOM   11232 O OE1 . GLU C 1 369 ? 6.975   4.644   36.808  1.00 59.52  ? 369 GLU C OE1 1 
ATOM   11233 O OE2 . GLU C 1 369 ? 8.506   3.224   36.132  1.00 60.08  ? 369 GLU C OE2 1 
ATOM   11234 N N   . LYS C 1 370 ? 9.695   8.792   39.704  1.00 40.55  ? 370 LYS C N   1 
ATOM   11235 C CA  . LYS C 1 370 ? 9.940   10.231  39.674  1.00 42.80  ? 370 LYS C CA  1 
ATOM   11236 C C   . LYS C 1 370 ? 11.311  10.570  40.247  1.00 41.86  ? 370 LYS C C   1 
ATOM   11237 O O   . LYS C 1 370 ? 12.036  11.403  39.690  1.00 48.15  ? 370 LYS C O   1 
ATOM   11238 C CB  . LYS C 1 370 ? 8.846   10.969  40.446  1.00 39.54  ? 370 LYS C CB  1 
ATOM   11239 C CG  . LYS C 1 370 ? 8.638   12.407  40.011  1.00 41.41  ? 370 LYS C CG  1 
ATOM   11240 C CD  . LYS C 1 370 ? 7.530   12.502  38.981  1.00 56.08  ? 370 LYS C CD  1 
ATOM   11241 C CE  . LYS C 1 370 ? 6.210   12.011  39.551  1.00 56.19  ? 370 LYS C CE  1 
ATOM   11242 N NZ  . LYS C 1 370 ? 5.365   11.360  38.513  1.00 57.30  ? 370 LYS C NZ  1 
ATOM   11243 N N   . LEU C 1 371 ? 11.683  9.935   41.359  1.00 36.03  ? 371 LEU C N   1 
ATOM   11244 C CA  . LEU C 1 371 ? 12.967  10.228  41.987  1.00 35.08  ? 371 LEU C CA  1 
ATOM   11245 C C   . LEU C 1 371 ? 14.127  9.729   41.135  1.00 36.64  ? 371 LEU C C   1 
ATOM   11246 O O   . LEU C 1 371 ? 15.086  10.468  40.881  1.00 41.62  ? 371 LEU C O   1 
ATOM   11247 C CB  . LEU C 1 371 ? 13.019  9.610   43.386  1.00 33.60  ? 371 LEU C CB  1 
ATOM   11248 C CG  . LEU C 1 371 ? 14.395  9.523   44.049  1.00 32.51  ? 371 LEU C CG  1 
ATOM   11249 C CD1 . LEU C 1 371 ? 14.845  10.896  44.510  1.00 38.50  ? 371 LEU C CD1 1 
ATOM   11250 C CD2 . LEU C 1 371 ? 14.370  8.549   45.215  1.00 31.20  ? 371 LEU C CD2 1 
ATOM   11251 N N   . TYR C 1 372 ? 14.054  8.476   40.680  1.00 34.31  ? 372 TYR C N   1 
ATOM   11252 C CA  . TYR C 1 372 ? 15.176  7.881   39.960  1.00 34.61  ? 372 TYR C CA  1 
ATOM   11253 C C   . TYR C 1 372 ? 15.437  8.596   38.640  1.00 41.99  ? 372 TYR C C   1 
ATOM   11254 O O   . TYR C 1 372 ? 16.595  8.815   38.265  1.00 50.96  ? 372 TYR C O   1 
ATOM   11255 C CB  . TYR C 1 372 ? 14.922  6.392   39.728  1.00 33.51  ? 372 TYR C CB  1 
ATOM   11256 C CG  . TYR C 1 372 ? 15.055  5.553   40.979  1.00 32.00  ? 372 TYR C CG  1 
ATOM   11257 C CD1 . TYR C 1 372 ? 15.717  6.041   42.099  1.00 31.18  ? 372 TYR C CD1 1 
ATOM   11258 C CD2 . TYR C 1 372 ? 14.535  4.265   41.034  1.00 31.64  ? 372 TYR C CD2 1 
ATOM   11259 C CE1 . TYR C 1 372 ? 15.850  5.275   43.241  1.00 30.01  ? 372 TYR C CE1 1 
ATOM   11260 C CE2 . TYR C 1 372 ? 14.662  3.491   42.172  1.00 36.30  ? 372 TYR C CE2 1 
ATOM   11261 C CZ  . TYR C 1 372 ? 15.319  4.002   43.273  1.00 32.44  ? 372 TYR C CZ  1 
ATOM   11262 O OH  . TYR C 1 372 ? 15.449  3.234   44.408  1.00 28.66  ? 372 TYR C OH  1 
ATOM   11263 N N   . SER C 1 373 ? 14.377  8.962   37.917  1.00 37.03  ? 373 SER C N   1 
ATOM   11264 C CA  . SER C 1 373 ? 14.568  9.721   36.687  1.00 38.79  ? 373 SER C CA  1 
ATOM   11265 C C   . SER C 1 373 ? 15.119  11.112  36.971  1.00 45.26  ? 373 SER C C   1 
ATOM   11266 O O   . SER C 1 373 ? 15.813  11.687  36.126  1.00 59.65  ? 373 SER C O   1 
ATOM   11267 C CB  . SER C 1 373 ? 13.255  9.812   35.907  1.00 40.37  ? 373 SER C CB  1 
ATOM   11268 O OG  . SER C 1 373 ? 12.192  10.265  36.727  1.00 50.84  ? 373 SER C OG  1 
ATOM   11269 N N   . THR C 1 374 ? 14.826  11.666  38.151  1.00 38.73  ? 374 THR C N   1 
ATOM   11270 C CA  . THR C 1 374 ? 15.369  12.972  38.511  1.00 39.33  ? 374 THR C CA  1 
ATOM   11271 C C   . THR C 1 374 ? 16.857  12.883  38.827  1.00 41.60  ? 374 THR C C   1 
ATOM   11272 O O   . THR C 1 374 ? 17.642  13.730  38.384  1.00 43.12  ? 374 THR C O   1 
ATOM   11273 C CB  . THR C 1 374 ? 14.601  13.552  39.697  1.00 39.12  ? 374 THR C CB  1 
ATOM   11274 O OG1 . THR C 1 374 ? 13.197  13.348  39.500  1.00 50.66  ? 374 THR C OG1 1 
ATOM   11275 C CG2 . THR C 1 374 ? 14.869  15.044  39.821  1.00 42.20  ? 374 THR C CG2 1 
ATOM   11276 N N   . LEU C 1 375 ? 17.263  11.868  39.598  1.00 46.43  ? 375 LEU C N   1 
ATOM   11277 C CA  . LEU C 1 375 ? 18.687  11.633  39.829  1.00 47.08  ? 375 LEU C CA  1 
ATOM   11278 C C   . LEU C 1 375 ? 19.425  11.382  38.523  1.00 46.79  ? 375 LEU C C   1 
ATOM   11279 O O   . LEU C 1 375 ? 20.612  11.707  38.403  1.00 39.92  ? 375 LEU C O   1 
ATOM   11280 C CB  . LEU C 1 375 ? 18.883  10.439  40.764  1.00 45.19  ? 375 LEU C CB  1 
ATOM   11281 C CG  . LEU C 1 375 ? 19.045  10.644  42.269  1.00 42.22  ? 375 LEU C CG  1 
ATOM   11282 C CD1 . LEU C 1 375 ? 17.991  11.588  42.809  1.00 33.72  ? 375 LEU C CD1 1 
ATOM   11283 C CD2 . LEU C 1 375 ? 18.967  9.300   42.968  1.00 31.71  ? 375 LEU C CD2 1 
ATOM   11284 N N   . GLU C 1 376 ? 18.736  10.793  37.544  1.00 46.57  ? 376 GLU C N   1 
ATOM   11285 C CA  . GLU C 1 376 ? 19.347  10.499  36.253  1.00 50.40  ? 376 GLU C CA  1 
ATOM   11286 C C   . GLU C 1 376 ? 19.770  11.775  35.537  1.00 57.86  ? 376 GLU C C   1 
ATOM   11287 O O   . GLU C 1 376 ? 20.850  11.833  34.938  1.00 64.38  ? 376 GLU C O   1 
ATOM   11288 C CB  . GLU C 1 376 ? 18.358  9.705   35.402  1.00 53.59  ? 376 GLU C CB  1 
ATOM   11289 C CG  . GLU C 1 376 ? 18.930  8.488   34.716  1.00 63.50  ? 376 GLU C CG  1 
ATOM   11290 C CD  . GLU C 1 376 ? 17.891  7.784   33.870  1.00 61.28  ? 376 GLU C CD  1 
ATOM   11291 O OE1 . GLU C 1 376 ? 16.725  8.232   33.872  1.00 61.76  ? 376 GLU C OE1 1 
ATOM   11292 O OE2 . GLU C 1 376 ? 18.236  6.783   33.209  1.00 66.00  ? 376 GLU C OE2 1 
ATOM   11293 N N   . LYS C 1 377 ? 18.932  12.806  35.590  1.00 48.46  ? 377 LYS C N   1 
ATOM   11294 C CA  . LYS C 1 377 ? 19.175  14.052  34.878  1.00 43.03  ? 377 LYS C CA  1 
ATOM   11295 C C   . LYS C 1 377 ? 19.910  15.089  35.719  1.00 50.82  ? 377 LYS C C   1 
ATOM   11296 O O   . LYS C 1 377 ? 20.132  16.206  35.242  1.00 51.40  ? 377 LYS C O   1 
ATOM   11297 C CB  . LYS C 1 377 ? 17.844  14.626  34.379  1.00 45.57  ? 377 LYS C CB  1 
ATOM   11298 C CG  . LYS C 1 377 ? 17.034  13.655  33.522  1.00 49.63  ? 377 LYS C CG  1 
ATOM   11299 C CD  . LYS C 1 377 ? 15.535  13.860  33.705  1.00 56.49  ? 377 LYS C CD  1 
ATOM   11300 C CE  . LYS C 1 377 ? 14.723  12.876  32.869  1.00 49.08  ? 377 LYS C CE  1 
ATOM   11301 N NZ  . LYS C 1 377 ? 14.786  11.481  33.394  1.00 44.83  ? 377 LYS C NZ  1 
ATOM   11302 N N   . GLU C 1 378 ? 20.292  14.749  36.947  1.00 58.96  ? 378 GLU C N   1 
ATOM   11303 C CA  . GLU C 1 378 ? 21.019  15.663  37.824  1.00 56.75  ? 378 GLU C CA  1 
ATOM   11304 C C   . GLU C 1 378 ? 22.514  15.410  37.666  1.00 57.39  ? 378 GLU C C   1 
ATOM   11305 O O   . GLU C 1 378 ? 23.018  14.351  38.055  1.00 50.33  ? 378 GLU C O   1 
ATOM   11306 C CB  . GLU C 1 378 ? 20.571  15.487  39.273  1.00 49.47  ? 378 GLU C CB  1 
ATOM   11307 C CG  . GLU C 1 378 ? 20.441  16.791  40.030  1.00 42.97  ? 378 GLU C CG  1 
ATOM   11308 C CD  . GLU C 1 378 ? 19.158  17.532  39.713  1.00 62.51  ? 378 GLU C CD  1 
ATOM   11309 O OE1 . GLU C 1 378 ? 18.092  16.884  39.662  1.00 63.72  ? 378 GLU C OE1 1 
ATOM   11310 O OE2 . GLU C 1 378 ? 19.215  18.764  39.509  1.00 66.32  ? 378 GLU C OE2 1 
ATOM   11311 N N   . GLU C 1 379 ? 23.222  16.386  37.093  1.00 60.53  ? 379 GLU C N   1 
ATOM   11312 C CA  . GLU C 1 379 ? 24.629  16.192  36.764  1.00 58.94  ? 379 GLU C CA  1 
ATOM   11313 C C   . GLU C 1 379 ? 25.519  16.230  38.000  1.00 59.58  ? 379 GLU C C   1 
ATOM   11314 O O   . GLU C 1 379 ? 26.529  15.519  38.052  1.00 60.74  ? 379 GLU C O   1 
ATOM   11315 C CB  . GLU C 1 379 ? 25.080  17.245  35.751  1.00 58.31  ? 379 GLU C CB  1 
ATOM   11316 C CG  . GLU C 1 379 ? 24.575  18.648  36.049  1.00 81.62  ? 379 GLU C CG  1 
ATOM   11317 C CD  . GLU C 1 379 ? 23.228  18.930  35.410  1.00 94.75  ? 379 GLU C CD  1 
ATOM   11318 O OE1 . GLU C 1 379 ? 23.200  19.390  34.248  1.00 97.06  ? 379 GLU C OE1 1 
ATOM   11319 O OE2 . GLU C 1 379 ? 22.196  18.691  36.072  1.00 89.17  ? 379 GLU C OE2 1 
ATOM   11320 N N   . TRP C 1 380 ? 25.173  17.044  38.999  1.00 52.53  ? 380 TRP C N   1 
ATOM   11321 C CA  . TRP C 1 380 ? 26.008  17.156  40.189  1.00 46.71  ? 380 TRP C CA  1 
ATOM   11322 C C   . TRP C 1 380 ? 25.835  15.990  41.152  1.00 41.98  ? 380 TRP C C   1 
ATOM   11323 O O   . TRP C 1 380 ? 26.651  15.841  42.068  1.00 42.42  ? 380 TRP C O   1 
ATOM   11324 C CB  . TRP C 1 380 ? 25.721  18.468  40.927  1.00 47.58  ? 380 TRP C CB  1 
ATOM   11325 C CG  . TRP C 1 380 ? 24.268  18.740  41.162  1.00 41.53  ? 380 TRP C CG  1 
ATOM   11326 C CD1 . TRP C 1 380 ? 23.355  19.166  40.243  1.00 46.18  ? 380 TRP C CD1 1 
ATOM   11327 C CD2 . TRP C 1 380 ? 23.559  18.609  42.401  1.00 41.24  ? 380 TRP C CD2 1 
ATOM   11328 N NE1 . TRP C 1 380 ? 22.123  19.312  40.832  1.00 51.18  ? 380 TRP C NE1 1 
ATOM   11329 C CE2 . TRP C 1 380 ? 22.220  18.973  42.156  1.00 46.87  ? 380 TRP C CE2 1 
ATOM   11330 C CE3 . TRP C 1 380 ? 23.927  18.221  43.693  1.00 39.28  ? 380 TRP C CE3 1 
ATOM   11331 C CZ2 . TRP C 1 380 ? 21.247  18.958  43.154  1.00 40.55  ? 380 TRP C CZ2 1 
ATOM   11332 C CZ3 . TRP C 1 380 ? 22.960  18.207  44.683  1.00 45.86  ? 380 TRP C CZ3 1 
ATOM   11333 C CH2 . TRP C 1 380 ? 21.636  18.573  44.407  1.00 39.28  ? 380 TRP C CH2 1 
ATOM   11334 N N   . ILE C 1 381 ? 24.806  15.167  40.976  1.00 45.65  ? 381 ILE C N   1 
ATOM   11335 C CA  . ILE C 1 381 ? 24.590  13.989  41.806  1.00 42.14  ? 381 ILE C CA  1 
ATOM   11336 C C   . ILE C 1 381 ? 25.103  12.776  41.047  1.00 41.91  ? 381 ILE C C   1 
ATOM   11337 O O   . ILE C 1 381 ? 24.698  12.530  39.904  1.00 47.93  ? 381 ILE C O   1 
ATOM   11338 C CB  . ILE C 1 381 ? 23.109  13.820  42.179  1.00 36.38  ? 381 ILE C CB  1 
ATOM   11339 C CG1 . ILE C 1 381 ? 22.505  15.156  42.614  1.00 40.57  ? 381 ILE C CG1 1 
ATOM   11340 C CG2 . ILE C 1 381 ? 22.955  12.779  43.280  1.00 33.89  ? 381 ILE C CG2 1 
ATOM   11341 C CD1 . ILE C 1 381 ? 21.097  15.039  43.154  1.00 36.13  ? 381 ILE C CD1 1 
ATOM   11342 N N   . GLU C 1 382 ? 26.003  12.023  41.673  1.00 34.63  ? 382 GLU C N   1 
ATOM   11343 C CA  . GLU C 1 382 ? 26.484  10.755  41.135  1.00 35.83  ? 382 GLU C CA  1 
ATOM   11344 C C   . GLU C 1 382 ? 26.144  9.662   42.138  1.00 37.31  ? 382 GLU C C   1 
ATOM   11345 O O   . GLU C 1 382 ? 26.765  9.578   43.203  1.00 43.42  ? 382 GLU C O   1 
ATOM   11346 C CB  . GLU C 1 382 ? 27.989  10.796  40.862  1.00 44.75  ? 382 GLU C CB  1 
ATOM   11347 C CG  . GLU C 1 382 ? 28.530  9.528   40.210  1.00 56.08  ? 382 GLU C CG  1 
ATOM   11348 C CD  . GLU C 1 382 ? 30.030  9.571   39.980  1.00 61.46  ? 382 GLU C CD  1 
ATOM   11349 O OE1 . GLU C 1 382 ? 30.601  10.682  39.959  1.00 45.13  ? 382 GLU C OE1 1 
ATOM   11350 O OE2 . GLU C 1 382 ? 30.640  8.491   39.821  1.00 69.27  ? 382 GLU C OE2 1 
ATOM   11351 N N   . THR C 1 383 ? 25.157  8.834   41.807  1.00 33.85  ? 383 THR C N   1 
ATOM   11352 C CA  . THR C 1 383 ? 24.861  7.680   42.641  1.00 33.98  ? 383 THR C CA  1 
ATOM   11353 C C   . THR C 1 383 ? 25.999  6.674   42.548  1.00 31.56  ? 383 THR C C   1 
ATOM   11354 O O   . THR C 1 383 ? 26.591  6.477   41.484  1.00 39.62  ? 383 THR C O   1 
ATOM   11355 C CB  . THR C 1 383 ? 23.543  7.025   42.224  1.00 31.86  ? 383 THR C CB  1 
ATOM   11356 O OG1 . THR C 1 383 ? 23.539  6.807   40.809  1.00 35.70  ? 383 THR C OG1 1 
ATOM   11357 C CG2 . THR C 1 383 ? 22.364  7.907   42.604  1.00 30.87  ? 383 THR C CG2 1 
ATOM   11358 N N   . LEU C 1 384 ? 26.313  6.041   43.672  1.00 29.95  ? 384 LEU C N   1 
ATOM   11359 C CA  . LEU C 1 384 ? 27.427  5.113   43.745  1.00 34.26  ? 384 LEU C CA  1 
ATOM   11360 C C   . LEU C 1 384 ? 26.963  3.760   44.260  1.00 34.56  ? 384 LEU C C   1 
ATOM   11361 O O   . LEU C 1 384 ? 25.946  3.641   44.949  1.00 30.95  ? 384 LEU C O   1 
ATOM   11362 C CB  . LEU C 1 384 ? 28.544  5.641   44.658  1.00 32.22  ? 384 LEU C CB  1 
ATOM   11363 C CG  . LEU C 1 384 ? 29.232  6.945   44.259  1.00 36.44  ? 384 LEU C CG  1 
ATOM   11364 C CD1 . LEU C 1 384 ? 30.122  7.435   45.389  1.00 31.17  ? 384 LEU C CD1 1 
ATOM   11365 C CD2 . LEU C 1 384 ? 30.033  6.760   42.981  1.00 40.20  ? 384 LEU C CD2 1 
ATOM   11366 N N   . THR C 1 385 ? 27.726  2.736   43.896  1.00 35.43  ? 385 THR C N   1 
ATOM   11367 C CA  . THR C 1 385 ? 27.603  1.447   44.547  1.00 32.23  ? 385 THR C CA  1 
ATOM   11368 C C   . THR C 1 385 ? 28.437  1.440   45.824  1.00 32.42  ? 385 THR C C   1 
ATOM   11369 O O   . THR C 1 385 ? 29.190  2.374   46.111  1.00 36.49  ? 385 THR C O   1 
ATOM   11370 C CB  . THR C 1 385 ? 28.047  0.318   43.618  1.00 29.36  ? 385 THR C CB  1 
ATOM   11371 O OG1 . THR C 1 385 ? 29.476  0.319   43.517  1.00 34.26  ? 385 THR C OG1 1 
ATOM   11372 C CG2 . THR C 1 385 ? 27.449  0.496   42.236  1.00 29.90  ? 385 THR C CG2 1 
ATOM   11373 N N   . LEU C 1 386 ? 28.291  0.371   46.606  1.00 35.07  ? 386 LEU C N   1 
ATOM   11374 C CA  . LEU C 1 386 ? 29.093  0.254   47.818  1.00 35.28  ? 386 LEU C CA  1 
ATOM   11375 C C   . LEU C 1 386 ? 30.570  0.084   47.485  1.00 40.42  ? 386 LEU C C   1 
ATOM   11376 O O   . LEU C 1 386 ? 31.435  0.593   48.209  1.00 42.43  ? 386 LEU C O   1 
ATOM   11377 C CB  . LEU C 1 386 ? 28.580  -0.900  48.685  1.00 37.65  ? 386 LEU C CB  1 
ATOM   11378 C CG  . LEU C 1 386 ? 27.117  -0.788  49.147  1.00 31.32  ? 386 LEU C CG  1 
ATOM   11379 C CD1 . LEU C 1 386 ? 26.692  -2.010  49.950  1.00 30.49  ? 386 LEU C CD1 1 
ATOM   11380 C CD2 . LEU C 1 386 ? 26.875  0.491   49.944  1.00 31.77  ? 386 LEU C CD2 1 
ATOM   11381 N N   . GLU C 1 387 ? 30.882  -0.613  46.391  1.00 39.54  ? 387 GLU C N   1 
ATOM   11382 C CA  . GLU C 1 387 ? 32.271  -0.699  45.950  1.00 36.00  ? 387 GLU C CA  1 
ATOM   11383 C C   . GLU C 1 387 ? 32.803  0.668   45.543  1.00 35.76  ? 387 GLU C C   1 
ATOM   11384 O O   . GLU C 1 387 ? 33.879  1.086   45.985  1.00 36.03  ? 387 GLU C O   1 
ATOM   11385 C CB  . GLU C 1 387 ? 32.396  -1.686  44.788  1.00 33.72  ? 387 GLU C CB  1 
ATOM   11386 C CG  . GLU C 1 387 ? 33.725  -2.427  44.765  1.00 44.67  ? 387 GLU C CG  1 
ATOM   11387 C CD  . GLU C 1 387 ? 34.764  -1.737  43.896  1.00 75.23  ? 387 GLU C CD  1 
ATOM   11388 O OE1 . GLU C 1 387 ? 34.508  -0.658  43.339  1.00 78.78  ? 387 GLU C OE1 1 
ATOM   11389 O OE2 . GLU C 1 387 ? 35.868  -2.336  43.770  1.00 79.81  ? 387 GLU C OE2 1 
ATOM   11390 N N   . GLU C 1 388 ? 32.065  1.371   44.682  1.00 38.74  ? 388 GLU C N   1 
ATOM   11391 C CA  . GLU C 1 388 ? 32.503  2.684   44.226  1.00 31.62  ? 388 GLU C CA  1 
ATOM   11392 C C   . GLU C 1 388 ? 32.699  3.637   45.398  1.00 37.90  ? 388 GLU C C   1 
ATOM   11393 O O   . GLU C 1 388 ? 33.627  4.453   45.393  1.00 45.86  ? 388 GLU C O   1 
ATOM   11394 C CB  . GLU C 1 388 ? 31.493  3.252   43.229  1.00 32.01  ? 388 GLU C CB  1 
ATOM   11395 C CG  . GLU C 1 388 ? 31.480  2.537   41.884  1.00 32.21  ? 388 GLU C CG  1 
ATOM   11396 C CD  . GLU C 1 388 ? 30.263  2.885   41.044  1.00 42.04  ? 388 GLU C CD  1 
ATOM   11397 O OE1 . GLU C 1 388 ? 29.709  3.989   41.221  1.00 48.55  ? 388 GLU C OE1 1 
ATOM   11398 O OE2 . GLU C 1 388 ? 29.862  2.055   40.200  1.00 39.31  ? 388 GLU C OE2 1 
ATOM   11399 N N   . ALA C 1 389 ? 31.834  3.550   46.414  1.00 37.13  ? 389 ALA C N   1 
ATOM   11400 C CA  . ALA C 1 389 ? 32.000  4.369   47.608  1.00 31.89  ? 389 ALA C CA  1 
ATOM   11401 C C   . ALA C 1 389 ? 33.239  3.987   48.409  1.00 42.42  ? 389 ALA C C   1 
ATOM   11402 O O   . ALA C 1 389 ? 33.685  4.775   49.248  1.00 53.40  ? 389 ALA C O   1 
ATOM   11403 C CB  . ALA C 1 389 ? 30.760  4.268   48.494  1.00 29.53  ? 389 ALA C CB  1 
ATOM   11404 N N   . MET C 1 390 ? 33.802  2.802   48.177  1.00 46.08  ? 390 MET C N   1 
ATOM   11405 C CA  . MET C 1 390 ? 35.003  2.382   48.888  1.00 42.88  ? 390 MET C CA  1 
ATOM   11406 C C   . MET C 1 390 ? 36.285  2.783   48.173  1.00 48.79  ? 390 MET C C   1 
ATOM   11407 O O   . MET C 1 390 ? 37.301  3.027   48.835  1.00 54.57  ? 390 MET C O   1 
ATOM   11408 C CB  . MET C 1 390 ? 34.993  0.864   49.100  1.00 45.35  ? 390 MET C CB  1 
ATOM   11409 C CG  . MET C 1 390 ? 34.501  0.435   50.471  1.00 46.92  ? 390 MET C CG  1 
ATOM   11410 S SD  . MET C 1 390 ? 35.379  1.290   51.794  1.00 62.50  ? 390 MET C SD  1 
ATOM   11411 C CE  . MET C 1 390 ? 36.881  0.320   51.891  1.00 52.83  ? 390 MET C CE  1 
ATOM   11412 N N   . ARG C 1 391 ? 36.265  2.855   46.844  1.00 44.52  ? 391 ARG C N   1 
ATOM   11413 C CA  . ARG C 1 391 ? 37.428  3.262   46.069  1.00 47.04  ? 391 ARG C CA  1 
ATOM   11414 C C   . ARG C 1 391 ? 37.435  4.756   45.764  1.00 48.03  ? 391 ARG C C   1 
ATOM   11415 O O   . ARG C 1 391 ? 38.313  5.225   45.031  1.00 55.74  ? 391 ARG C O   1 
ATOM   11416 C CB  . ARG C 1 391 ? 37.502  2.455   44.769  1.00 48.32  ? 391 ARG C CB  1 
ATOM   11417 C CG  . ARG C 1 391 ? 38.913  2.291   44.218  1.00 62.41  ? 391 ARG C CG  1 
ATOM   11418 C CD  . ARG C 1 391 ? 39.749  1.382   45.105  1.00 72.14  ? 391 ARG C CD  1 
ATOM   11419 N NE  . ARG C 1 391 ? 41.121  1.861   45.233  1.00 73.28  ? 391 ARG C NE  1 
ATOM   11420 C CZ  . ARG C 1 391 ? 41.707  2.169   46.383  1.00 63.04  ? 391 ARG C CZ  1 
ATOM   11421 N NH1 . ARG C 1 391 ? 41.065  2.063   47.536  1.00 49.92  ? 391 ARG C NH1 1 
ATOM   11422 N NH2 . ARG C 1 391 ? 42.967  2.596   46.375  1.00 49.55  ? 391 ARG C NH2 1 
ATOM   11423 N N   . LYS C 1 392 ? 36.483  5.510   46.308  1.00 43.08  ? 392 LYS C N   1 
ATOM   11424 C CA  . LYS C 1 392 ? 36.449  6.957   46.116  1.00 48.38  ? 392 LYS C CA  1 
ATOM   11425 C C   . LYS C 1 392 ? 37.657  7.585   46.801  1.00 55.10  ? 392 LYS C C   1 
ATOM   11426 O O   . LYS C 1 392 ? 37.718  7.648   48.033  1.00 66.53  ? 392 LYS C O   1 
ATOM   11427 C CB  . LYS C 1 392 ? 35.150  7.534   46.671  1.00 48.78  ? 392 LYS C CB  1 
ATOM   11428 C CG  . LYS C 1 392 ? 34.019  7.611   45.663  1.00 39.70  ? 392 LYS C CG  1 
ATOM   11429 C CD  . LYS C 1 392 ? 34.322  8.623   44.573  1.00 47.11  ? 392 LYS C CD  1 
ATOM   11430 C CE  . LYS C 1 392 ? 33.314  8.524   43.441  1.00 46.06  ? 392 LYS C CE  1 
ATOM   11431 N NZ  . LYS C 1 392 ? 33.508  7.293   42.628  1.00 58.20  ? 392 LYS C NZ  1 
ATOM   11432 N N   . GLU C 1 393 ? 38.624  8.044   46.006  1.00 47.88  ? 393 GLU C N   1 
ATOM   11433 C CA  . GLU C 1 393 ? 39.799  8.710   46.551  1.00 42.76  ? 393 GLU C CA  1 
ATOM   11434 C C   . GLU C 1 393 ? 39.576  10.195  46.799  1.00 38.95  ? 393 GLU C C   1 
ATOM   11435 O O   . GLU C 1 393 ? 40.397  10.822  47.476  1.00 53.31  ? 393 GLU C O   1 
ATOM   11436 C CB  . GLU C 1 393 ? 40.995  8.528   45.611  1.00 60.83  ? 393 GLU C CB  1 
ATOM   11437 C CG  . GLU C 1 393 ? 41.646  7.155   45.682  1.00 78.42  ? 393 GLU C CG  1 
ATOM   11438 C CD  . GLU C 1 393 ? 42.553  6.875   44.500  1.00 83.53  ? 393 GLU C CD  1 
ATOM   11439 O OE1 . GLU C 1 393 ? 42.937  5.701   44.307  1.00 63.73  ? 393 GLU C OE1 1 
ATOM   11440 O OE2 . GLU C 1 393 ? 42.884  7.829   43.765  1.00 81.21  ? 393 GLU C OE2 1 
ATOM   11441 N N   . ASP C 1 394 ? 38.487  10.766  46.282  1.00 43.97  ? 394 ASP C N   1 
ATOM   11442 C CA  . ASP C 1 394 ? 38.232  12.200  46.355  1.00 44.46  ? 394 ASP C CA  1 
ATOM   11443 C C   . ASP C 1 394 ? 37.213  12.559  47.431  1.00 42.90  ? 394 ASP C C   1 
ATOM   11444 O O   . ASP C 1 394 ? 36.464  13.529  47.276  1.00 42.30  ? 394 ASP C O   1 
ATOM   11445 C CB  . ASP C 1 394 ? 37.769  12.719  44.993  1.00 45.88  ? 394 ASP C CB  1 
ATOM   11446 C CG  . ASP C 1 394 ? 38.568  13.918  44.523  1.00 58.92  ? 394 ASP C CG  1 
ATOM   11447 O OD1 . ASP C 1 394 ? 39.278  14.523  45.356  1.00 49.07  ? 394 ASP C OD1 1 
ATOM   11448 O OD2 . ASP C 1 394 ? 38.487  14.254  43.323  1.00 53.52  ? 394 ASP C OD2 1 
ATOM   11449 N N   . VAL C 1 395 ? 37.171  11.799  48.523  1.00 45.09  ? 395 VAL C N   1 
ATOM   11450 C CA  . VAL C 1 395 ? 36.201  12.026  49.586  1.00 45.30  ? 395 VAL C CA  1 
ATOM   11451 C C   . VAL C 1 395 ? 36.940  12.226  50.901  1.00 38.15  ? 395 VAL C C   1 
ATOM   11452 O O   . VAL C 1 395 ? 38.051  11.723  51.099  1.00 37.89  ? 395 VAL C O   1 
ATOM   11453 C CB  . VAL C 1 395 ? 35.190  10.863  49.698  1.00 46.09  ? 395 VAL C CB  1 
ATOM   11454 C CG1 . VAL C 1 395 ? 34.354  10.764  48.430  1.00 34.53  ? 395 VAL C CG1 1 
ATOM   11455 C CG2 . VAL C 1 395 ? 35.912  9.552   49.976  1.00 43.76  ? 395 VAL C CG2 1 
ATOM   11456 N N   . LYS C 1 396 ? 36.311  12.977  51.802  1.00 37.70  ? 396 LYS C N   1 
ATOM   11457 C CA  . LYS C 1 396 ? 36.895  13.241  53.109  1.00 39.09  ? 396 LYS C CA  1 
ATOM   11458 C C   . LYS C 1 396 ? 36.881  11.976  53.960  1.00 37.32  ? 396 LYS C C   1 
ATOM   11459 O O   . LYS C 1 396 ? 35.940  11.179  53.899  1.00 36.03  ? 396 LYS C O   1 
ATOM   11460 C CB  . LYS C 1 396 ? 36.128  14.365  53.808  1.00 44.83  ? 396 LYS C CB  1 
ATOM   11461 C CG  . LYS C 1 396 ? 37.001  15.444  54.434  1.00 40.12  ? 396 LYS C CG  1 
ATOM   11462 C CD  . LYS C 1 396 ? 36.342  16.018  55.679  1.00 44.62  ? 396 LYS C CD  1 
ATOM   11463 C CE  . LYS C 1 396 ? 36.927  17.370  56.057  1.00 51.70  ? 396 LYS C CE  1 
ATOM   11464 N NZ  . LYS C 1 396 ? 36.332  17.888  57.323  1.00 42.75  ? 396 LYS C NZ  1 
ATOM   11465 N N   . THR C 1 397 ? 37.939  11.784  54.748  1.00 36.89  ? 397 THR C N   1 
ATOM   11466 C CA  . THR C 1 397 ? 38.045  10.619  55.616  1.00 34.91  ? 397 THR C CA  1 
ATOM   11467 C C   . THR C 1 397 ? 38.553  11.039  56.986  1.00 34.05  ? 397 THR C C   1 
ATOM   11468 O O   . THR C 1 397 ? 39.542  11.771  57.087  1.00 35.48  ? 397 THR C O   1 
ATOM   11469 C CB  . THR C 1 397 ? 38.974  9.553   55.022  1.00 35.74  ? 397 THR C CB  1 
ATOM   11470 O OG1 . THR C 1 397 ? 40.061  10.190  54.337  1.00 52.61  ? 397 THR C OG1 1 
ATOM   11471 C CG2 . THR C 1 397 ? 38.215  8.667   54.046  1.00 36.10  ? 397 THR C CG2 1 
ATOM   11472 N N   . GLU C 1 398 ? 37.882  10.566  58.032  1.00 34.77  ? 398 GLU C N   1 
ATOM   11473 C CA  . GLU C 1 398 ? 38.275  10.821  59.410  1.00 35.53  ? 398 GLU C CA  1 
ATOM   11474 C C   . GLU C 1 398 ? 38.455  9.500   60.142  1.00 34.92  ? 398 GLU C C   1 
ATOM   11475 O O   . GLU C 1 398 ? 37.720  8.538   59.897  1.00 28.50  ? 398 GLU C O   1 
ATOM   11476 C CB  . GLU C 1 398 ? 37.235  11.681  60.137  1.00 43.65  ? 398 GLU C CB  1 
ATOM   11477 C CG  . GLU C 1 398 ? 37.816  12.585  61.213  1.00 44.14  ? 398 GLU C CG  1 
ATOM   11478 C CD  . GLU C 1 398 ? 36.790  13.544  61.783  1.00 58.15  ? 398 GLU C CD  1 
ATOM   11479 O OE1 . GLU C 1 398 ? 36.607  13.558  63.020  1.00 53.58  ? 398 GLU C OE1 1 
ATOM   11480 O OE2 . GLU C 1 398 ? 36.165  14.284  60.993  1.00 52.88  ? 398 GLU C OE2 1 
ATOM   11481 N N   . VAL C 1 399 ? 39.432  9.458   61.035  1.00 39.90  ? 399 VAL C N   1 
ATOM   11482 C CA  . VAL C 1 399 ? 39.707  8.273   61.836  1.00 28.73  ? 399 VAL C CA  1 
ATOM   11483 C C   . VAL C 1 399 ? 38.967  8.393   63.159  1.00 28.99  ? 399 VAL C C   1 
ATOM   11484 O O   . VAL C 1 399 ? 38.895  9.475   63.753  1.00 28.59  ? 399 VAL C O   1 
ATOM   11485 C CB  . VAL C 1 399 ? 41.222  8.098   62.056  1.00 34.72  ? 399 VAL C CB  1 
ATOM   11486 C CG1 . VAL C 1 399 ? 41.510  6.799   62.798  1.00 29.07  ? 399 VAL C CG1 1 
ATOM   11487 C CG2 . VAL C 1 399 ? 41.960  8.130   60.725  1.00 36.53  ? 399 VAL C CG2 1 
ATOM   11488 N N   . ILE C 1 400 ? 38.399  7.281   63.618  1.00 29.26  ? 400 ILE C N   1 
ATOM   11489 C CA  . ILE C 1 400 ? 37.735  7.210   64.912  1.00 34.24  ? 400 ILE C CA  1 
ATOM   11490 C C   . ILE C 1 400 ? 38.270  5.997   65.660  1.00 31.51  ? 400 ILE C C   1 
ATOM   11491 O O   . ILE C 1 400 ? 38.535  4.951   65.058  1.00 31.00  ? 400 ILE C O   1 
ATOM   11492 C CB  . ILE C 1 400 ? 36.199  7.136   64.772  1.00 31.20  ? 400 ILE C CB  1 
ATOM   11493 C CG1 . ILE C 1 400 ? 35.793  5.946   63.902  1.00 34.26  ? 400 ILE C CG1 1 
ATOM   11494 C CG2 . ILE C 1 400 ? 35.652  8.433   64.196  1.00 27.57  ? 400 ILE C CG2 1 
ATOM   11495 C CD1 . ILE C 1 400 ? 34.397  5.447   64.181  1.00 33.39  ? 400 ILE C CD1 1 
ATOM   11496 N N   . GLU C 1 401 ? 38.443  6.145   66.974  1.00 28.04  ? 401 GLU C N   1 
ATOM   11497 C CA  . GLU C 1 401 ? 38.999  5.077   67.793  1.00 31.69  ? 401 GLU C CA  1 
ATOM   11498 C C   . GLU C 1 401 ? 37.948  4.291   68.562  1.00 27.77  ? 401 GLU C C   1 
ATOM   11499 O O   . GLU C 1 401 ? 38.248  3.189   69.034  1.00 33.11  ? 401 GLU C O   1 
ATOM   11500 C CB  . GLU C 1 401 ? 40.023  5.644   68.782  1.00 29.93  ? 401 GLU C CB  1 
ATOM   11501 C CG  . GLU C 1 401 ? 41.204  6.319   68.110  1.00 36.10  ? 401 GLU C CG  1 
ATOM   11502 C CD  . GLU C 1 401 ? 41.900  5.408   67.119  1.00 45.75  ? 401 GLU C CD  1 
ATOM   11503 O OE1 . GLU C 1 401 ? 42.184  4.245   67.476  1.00 48.40  ? 401 GLU C OE1 1 
ATOM   11504 O OE2 . GLU C 1 401 ? 42.154  5.851   65.978  1.00 59.24  ? 401 GLU C OE2 1 
ATOM   11505 N N   . SER C 1 402 ? 36.736  4.820   68.700  1.00 20.99  ? 402 SER C N   1 
ATOM   11506 C CA  . SER C 1 402 ? 35.703  4.118   69.445  1.00 24.26  ? 402 SER C CA  1 
ATOM   11507 C C   . SER C 1 402 ? 34.337  4.665   69.064  1.00 30.31  ? 402 SER C C   1 
ATOM   11508 O O   . SER C 1 402 ? 34.207  5.822   68.654  1.00 29.75  ? 402 SER C O   1 
ATOM   11509 C CB  . SER C 1 402 ? 35.921  4.244   70.956  1.00 27.33  ? 402 SER C CB  1 
ATOM   11510 O OG  . SER C 1 402 ? 35.675  5.568   71.400  1.00 23.96  ? 402 SER C OG  1 
ATOM   11511 N N   . VAL C 1 403 ? 33.321  3.814   69.212  1.00 31.94  ? 403 VAL C N   1 
ATOM   11512 C CA  . VAL C 1 403 ? 31.927  4.193   69.042  1.00 28.10  ? 403 VAL C CA  1 
ATOM   11513 C C   . VAL C 1 403 ? 31.167  3.767   70.290  1.00 29.92  ? 403 VAL C C   1 
ATOM   11514 O O   . VAL C 1 403 ? 31.587  2.871   71.026  1.00 27.57  ? 403 VAL C O   1 
ATOM   11515 C CB  . VAL C 1 403 ? 31.289  3.566   67.782  1.00 21.52  ? 403 VAL C CB  1 
ATOM   11516 C CG1 . VAL C 1 403 ? 32.031  4.005   66.532  1.00 24.19  ? 403 VAL C CG1 1 
ATOM   11517 C CG2 . VAL C 1 403 ? 31.280  2.048   67.892  1.00 30.57  ? 403 VAL C CG2 1 
ATOM   11518 N N   . LYS C 1 404 ? 30.038  4.429   70.528  1.00 29.18  ? 404 LYS C N   1 
ATOM   11519 C CA  . LYS C 1 404 ? 29.173  4.089   71.647  1.00 23.21  ? 404 LYS C CA  1 
ATOM   11520 C C   . LYS C 1 404 ? 28.090  3.133   71.163  1.00 23.27  ? 404 LYS C C   1 
ATOM   11521 O O   . LYS C 1 404 ? 27.468  3.365   70.121  1.00 26.66  ? 404 LYS C O   1 
ATOM   11522 C CB  . LYS C 1 404 ? 28.555  5.344   72.262  1.00 28.01  ? 404 LYS C CB  1 
ATOM   11523 C CG  . LYS C 1 404 ? 28.580  5.348   73.783  1.00 24.98  ? 404 LYS C CG  1 
ATOM   11524 C CD  . LYS C 1 404 ? 28.264  6.721   74.354  1.00 41.24  ? 404 LYS C CD  1 
ATOM   11525 C CE  . LYS C 1 404 ? 28.407  6.731   75.869  1.00 51.62  ? 404 LYS C CE  1 
ATOM   11526 N NZ  . LYS C 1 404 ? 27.081  6.765   76.548  1.00 54.51  ? 404 LYS C NZ  1 
ATOM   11527 N N   . ALA C 1 405 ? 27.874  2.060   71.921  1.00 25.54  ? 405 ALA C N   1 
ATOM   11528 C CA  . ALA C 1 405 ? 27.032  0.966   71.455  1.00 20.75  ? 405 ALA C CA  1 
ATOM   11529 C C   . ALA C 1 405 ? 25.562  1.363   71.460  1.00 22.49  ? 405 ALA C C   1 
ATOM   11530 O O   . ALA C 1 405 ? 25.057  1.911   72.446  1.00 33.13  ? 405 ALA C O   1 
ATOM   11531 C CB  . ALA C 1 405 ? 27.246  -0.268  72.327  1.00 20.91  ? 405 ALA C CB  1 
ATOM   11532 N N   . GLY C 1 406 ? 24.877  1.065   70.363  1.00 27.59  ? 406 GLY C N   1 
ATOM   11533 C CA  . GLY C 1 406 ? 23.468  1.375   70.249  1.00 30.17  ? 406 GLY C CA  1 
ATOM   11534 C C   . GLY C 1 406 ? 22.927  0.882   68.926  1.00 23.97  ? 406 GLY C C   1 
ATOM   11535 O O   . GLY C 1 406 ? 23.604  0.170   68.181  1.00 26.60  ? 406 GLY C O   1 
ATOM   11536 N N   . THR C 1 407 ? 21.685  1.266   68.644  1.00 20.63  ? 407 THR C N   1 
ATOM   11537 C CA  . THR C 1 407 ? 21.019  0.941   67.392  1.00 30.23  ? 407 THR C CA  1 
ATOM   11538 C C   . THR C 1 407 ? 20.454  2.220   66.791  1.00 29.58  ? 407 THR C C   1 
ATOM   11539 O O   . THR C 1 407 ? 20.427  3.272   67.433  1.00 26.30  ? 407 THR C O   1 
ATOM   11540 C CB  . THR C 1 407 ? 19.891  -0.077  67.597  1.00 27.27  ? 407 THR C CB  1 
ATOM   11541 O OG1 . THR C 1 407 ? 18.920  0.470   68.495  1.00 28.86  ? 407 THR C OG1 1 
ATOM   11542 C CG2 . THR C 1 407 ? 20.434  -1.375  68.171  1.00 23.42  ? 407 THR C CG2 1 
ATOM   11543 N N   . TRP C 1 408 ? 19.984  2.126   65.546  1.00 24.35  ? 408 TRP C N   1 
ATOM   11544 C CA  . TRP C 1 408 ? 19.347  3.290   64.943  1.00 34.13  ? 408 TRP C CA  1 
ATOM   11545 C C   . TRP C 1 408 ? 17.985  3.587   65.554  1.00 36.05  ? 408 TRP C C   1 
ATOM   11546 O O   . TRP C 1 408 ? 17.395  4.627   65.235  1.00 37.47  ? 408 TRP C O   1 
ATOM   11547 C CB  . TRP C 1 408 ? 19.233  3.130   63.422  1.00 30.05  ? 408 TRP C CB  1 
ATOM   11548 C CG  . TRP C 1 408 ? 18.433  1.971   62.919  1.00 29.12  ? 408 TRP C CG  1 
ATOM   11549 C CD1 . TRP C 1 408 ? 17.815  1.008   63.656  1.00 34.55  ? 408 TRP C CD1 1 
ATOM   11550 C CD2 . TRP C 1 408 ? 18.171  1.659   61.548  1.00 26.65  ? 408 TRP C CD2 1 
ATOM   11551 N NE1 . TRP C 1 408 ? 17.179  0.114   62.827  1.00 31.07  ? 408 TRP C NE1 1 
ATOM   11552 C CE2 . TRP C 1 408 ? 17.384  0.492   61.527  1.00 30.97  ? 408 TRP C CE2 1 
ATOM   11553 C CE3 . TRP C 1 408 ? 18.527  2.255   60.334  1.00 24.38  ? 408 TRP C CE3 1 
ATOM   11554 C CZ2 . TRP C 1 408 ? 16.946  -0.090  60.339  1.00 28.55  ? 408 TRP C CZ2 1 
ATOM   11555 C CZ3 . TRP C 1 408 ? 18.091  1.678   59.158  1.00 29.08  ? 408 TRP C CZ3 1 
ATOM   11556 C CH2 . TRP C 1 408 ? 17.311  0.517   59.169  1.00 30.94  ? 408 TRP C CH2 1 
ATOM   11557 N N   . PHE C 1 409 ? 17.478  2.707   66.416  1.00 35.00  ? 409 PHE C N   1 
ATOM   11558 C CA  . PHE C 1 409 ? 16.280  2.980   67.208  1.00 34.77  ? 409 PHE C CA  1 
ATOM   11559 C C   . PHE C 1 409 ? 16.699  3.751   68.453  1.00 31.91  ? 409 PHE C C   1 
ATOM   11560 O O   . PHE C 1 409 ? 17.022  3.172   69.491  1.00 34.40  ? 409 PHE C O   1 
ATOM   11561 C CB  . PHE C 1 409 ? 15.563  1.688   67.577  1.00 36.96  ? 409 PHE C CB  1 
ATOM   11562 C CG  . PHE C 1 409 ? 14.723  1.124   66.472  1.00 38.39  ? 409 PHE C CG  1 
ATOM   11563 C CD1 . PHE C 1 409 ? 15.287  0.323   65.497  1.00 38.04  ? 409 PHE C CD1 1 
ATOM   11564 C CD2 . PHE C 1 409 ? 13.368  1.395   66.408  1.00 41.42  ? 409 PHE C CD2 1 
ATOM   11565 C CE1 . PHE C 1 409 ? 14.518  -0.196  64.476  1.00 36.25  ? 409 PHE C CE1 1 
ATOM   11566 C CE2 . PHE C 1 409 ? 12.593  0.878   65.390  1.00 44.47  ? 409 PHE C CE2 1 
ATOM   11567 C CZ  . PHE C 1 409 ? 13.169  0.080   64.422  1.00 40.97  ? 409 PHE C CZ  1 
ATOM   11568 N N   . ASP C 1 410 ? 16.715  5.077   68.336  1.00 41.29  ? 410 ASP C N   1 
ATOM   11569 C CA  . ASP C 1 410 ? 16.947  6.009   69.436  1.00 45.01  ? 410 ASP C CA  1 
ATOM   11570 C C   . ASP C 1 410 ? 18.327  5.863   70.075  1.00 37.76  ? 410 ASP C C   1 
ATOM   11571 O O   . ASP C 1 410 ? 18.562  6.419   71.154  1.00 40.29  ? 410 ASP C O   1 
ATOM   11572 C CB  . ASP C 1 410 ? 15.857  5.883   70.511  1.00 53.35  ? 410 ASP C CB  1 
ATOM   11573 C CG  . ASP C 1 410 ? 15.474  7.221   71.110  1.00 75.04  ? 410 ASP C CG  1 
ATOM   11574 O OD1 . ASP C 1 410 ? 15.003  8.097   70.356  1.00 95.01  ? 410 ASP C OD1 1 
ATOM   11575 O OD2 . ASP C 1 410 ? 15.641  7.396   72.337  1.00 75.97  ? 410 ASP C OD2 1 
ATOM   11576 N N   . GLY C 1 411 ? 19.247  5.134   69.443  1.00 32.44  ? 411 GLY C N   1 
ATOM   11577 C CA  . GLY C 1 411 ? 20.625  5.097   69.895  1.00 25.38  ? 411 GLY C CA  1 
ATOM   11578 C C   . GLY C 1 411 ? 20.935  4.128   71.015  1.00 26.36  ? 411 GLY C C   1 
ATOM   11579 O O   . GLY C 1 411 ? 22.061  4.143   71.525  1.00 25.38  ? 411 GLY C O   1 
ATOM   11580 N N   . ASN C 1 412 ? 19.990  3.279   71.407  1.00 24.24  ? 412 ASN C N   1 
ATOM   11581 C CA  . ASN C 1 412 ? 20.187  2.360   72.520  1.00 22.08  ? 412 ASN C CA  1 
ATOM   11582 C C   . ASN C 1 412 ? 19.559  1.019   72.157  1.00 23.92  ? 412 ASN C C   1 
ATOM   11583 O O   . ASN C 1 412 ? 19.247  0.749   70.993  1.00 32.61  ? 412 ASN C O   1 
ATOM   11584 C CB  . ASN C 1 412 ? 19.608  2.947   73.813  1.00 19.60  ? 412 ASN C CB  1 
ATOM   11585 C CG  . ASN C 1 412 ? 18.152  3.330   73.673  1.00 21.36  ? 412 ASN C CG  1 
ATOM   11586 O OD1 . ASN C 1 412 ? 17.278  2.471   73.600  1.00 24.50  ? 412 ASN C OD1 1 
ATOM   11587 N ND2 . ASN C 1 412 ? 17.884  4.630   73.628  1.00 30.07  ? 412 ASN C ND2 1 
ATOM   11588 N N   . PHE C 1 413 ? 19.388  0.159   73.163  1.00 18.28  ? 413 PHE C N   1 
ATOM   11589 C CA  . PHE C 1 413 ? 18.850  -1.182  72.964  1.00 18.15  ? 413 PHE C CA  1 
ATOM   11590 C C   . PHE C 1 413 ? 17.513  -1.384  73.671  1.00 19.32  ? 413 PHE C C   1 
ATOM   11591 O O   . PHE C 1 413 ? 17.099  -2.526  73.892  1.00 19.42  ? 413 PHE C O   1 
ATOM   11592 C CB  . PHE C 1 413 ? 19.859  -2.232  73.434  1.00 17.29  ? 413 PHE C CB  1 
ATOM   11593 C CG  . PHE C 1 413 ? 21.180  -2.160  72.724  1.00 16.37  ? 413 PHE C CG  1 
ATOM   11594 C CD1 . PHE C 1 413 ? 22.194  -1.344  73.196  1.00 16.21  ? 413 PHE C CD1 1 
ATOM   11595 C CD2 . PHE C 1 413 ? 21.401  -2.898  71.576  1.00 22.97  ? 413 PHE C CD2 1 
ATOM   11596 C CE1 . PHE C 1 413 ? 23.408  -1.276  72.541  1.00 16.04  ? 413 PHE C CE1 1 
ATOM   11597 C CE2 . PHE C 1 413 ? 22.612  -2.832  70.915  1.00 19.07  ? 413 PHE C CE2 1 
ATOM   11598 C CZ  . PHE C 1 413 ? 23.616  -2.021  71.398  1.00 18.79  ? 413 PHE C CZ  1 
ATOM   11599 N N   . LEU C 1 414 ? 16.821  -0.297  74.019  1.00 20.41  ? 414 LEU C N   1 
ATOM   11600 C CA  . LEU C 1 414 ? 15.593  -0.400  74.798  1.00 23.10  ? 414 LEU C CA  1 
ATOM   11601 C C   . LEU C 1 414 ? 14.421  -0.960  74.002  1.00 22.59  ? 414 LEU C C   1 
ATOM   11602 O O   . LEU C 1 414 ? 13.397  -1.301  74.603  1.00 25.44  ? 414 LEU C O   1 
ATOM   11603 C CB  . LEU C 1 414 ? 15.226  0.967   75.373  1.00 23.03  ? 414 LEU C CB  1 
ATOM   11604 C CG  . LEU C 1 414 ? 16.139  1.404   76.518  1.00 22.89  ? 414 LEU C CG  1 
ATOM   11605 C CD1 . LEU C 1 414 ? 16.069  2.906   76.733  1.00 23.89  ? 414 LEU C CD1 1 
ATOM   11606 C CD2 . LEU C 1 414 ? 15.768  0.657   77.785  1.00 23.69  ? 414 LEU C CD2 1 
ATOM   11607 N N   . LYS C 1 415 ? 14.537  -1.058  72.678  1.00 22.90  ? 415 LYS C N   1 
ATOM   11608 C CA  . LYS C 1 415 ? 13.493  -1.691  71.883  1.00 25.04  ? 415 LYS C CA  1 
ATOM   11609 C C   . LYS C 1 415 ? 13.549  -3.212  71.950  1.00 22.56  ? 415 LYS C C   1 
ATOM   11610 O O   . LYS C 1 415 ? 12.551  -3.870  71.638  1.00 33.08  ? 415 LYS C O   1 
ATOM   11611 C CB  . LYS C 1 415 ? 13.591  -1.229  70.427  1.00 26.73  ? 415 LYS C CB  1 
ATOM   11612 C CG  . LYS C 1 415 ? 12.313  -1.384  69.618  1.00 29.72  ? 415 LYS C CG  1 
ATOM   11613 C CD  . LYS C 1 415 ? 11.132  -0.675  70.259  1.00 45.96  ? 415 LYS C CD  1 
ATOM   11614 C CE  . LYS C 1 415 ? 9.813   -1.229  69.739  1.00 53.31  ? 415 LYS C CE  1 
ATOM   11615 N NZ  . LYS C 1 415 ? 9.409   -2.477  70.442  1.00 50.28  ? 415 LYS C NZ  1 
ATOM   11616 N N   . TRP C 1 416 ? 14.685  -3.784  72.355  1.00 21.15  ? 416 TRP C N   1 
ATOM   11617 C CA  . TRP C 1 416 ? 14.845  -5.227  72.431  1.00 20.79  ? 416 TRP C CA  1 
ATOM   11618 C C   . TRP C 1 416 ? 15.124  -5.749  73.831  1.00 20.76  ? 416 TRP C C   1 
ATOM   11619 O O   . TRP C 1 416 ? 15.030  -6.963  74.045  1.00 24.48  ? 416 TRP C O   1 
ATOM   11620 C CB  . TRP C 1 416 ? 15.978  -5.689  71.501  1.00 19.51  ? 416 TRP C CB  1 
ATOM   11621 C CG  . TRP C 1 416 ? 15.821  -5.217  70.097  1.00 19.68  ? 416 TRP C CG  1 
ATOM   11622 C CD1 . TRP C 1 416 ? 15.284  -5.912  69.054  1.00 26.36  ? 416 TRP C CD1 1 
ATOM   11623 C CD2 . TRP C 1 416 ? 16.192  -3.937  69.579  1.00 20.84  ? 416 TRP C CD2 1 
ATOM   11624 N NE1 . TRP C 1 416 ? 15.302  -5.144  67.913  1.00 26.59  ? 416 TRP C NE1 1 
ATOM   11625 C CE2 . TRP C 1 416 ? 15.855  -3.926  68.211  1.00 21.22  ? 416 TRP C CE2 1 
ATOM   11626 C CE3 . TRP C 1 416 ? 16.779  -2.799  70.138  1.00 23.94  ? 416 TRP C CE3 1 
ATOM   11627 C CZ2 . TRP C 1 416 ? 16.086  -2.823  67.397  1.00 26.30  ? 416 TRP C CZ2 1 
ATOM   11628 C CZ3 . TRP C 1 416 ? 17.005  -1.707  69.330  1.00 19.26  ? 416 TRP C CZ3 1 
ATOM   11629 C CH2 . TRP C 1 416 ? 16.661  -1.725  67.974  1.00 25.19  ? 416 TRP C CH2 1 
ATOM   11630 N N   . ILE C 1 417 ? 15.461  -4.883  74.786  1.00 20.82  ? 417 ILE C N   1 
ATOM   11631 C CA  . ILE C 1 417 ? 15.859  -5.323  76.119  1.00 20.95  ? 417 ILE C CA  1 
ATOM   11632 C C   . ILE C 1 417 ? 15.657  -4.164  77.083  1.00 22.29  ? 417 ILE C C   1 
ATOM   11633 O O   . ILE C 1 417 ? 15.542  -3.008  76.674  1.00 23.41  ? 417 ILE C O   1 
ATOM   11634 C CB  . ILE C 1 417 ? 17.327  -5.825  76.120  1.00 20.71  ? 417 ILE C CB  1 
ATOM   11635 C CG1 . ILE C 1 417 ? 17.543  -6.855  77.230  1.00 19.96  ? 417 ILE C CG1 1 
ATOM   11636 C CG2 . ILE C 1 417 ? 18.297  -4.657  76.248  1.00 21.71  ? 417 ILE C CG2 1 
ATOM   11637 C CD1 . ILE C 1 417 ? 18.917  -7.481  77.220  1.00 20.51  ? 417 ILE C CD1 1 
ATOM   11638 N N   . GLY C 1 418 ? 15.600  -4.476  78.378  1.00 22.66  ? 418 GLY C N   1 
ATOM   11639 C CA  . GLY C 1 418 ? 15.482  -3.478  79.419  1.00 23.75  ? 418 GLY C CA  1 
ATOM   11640 C C   . GLY C 1 418 ? 14.105  -3.342  80.036  1.00 29.16  ? 418 GLY C C   1 
ATOM   11641 O O   . GLY C 1 418 ? 13.986  -2.740  81.110  1.00 41.53  ? 418 GLY C O   1 
ATOM   11642 N N   . ASN C 1 419 ? 13.071  -3.879  79.399  1.00 40.53  ? 419 ASN C N   1 
ATOM   11643 C CA  . ASN C 1 419 ? 11.716  -3.848  79.929  1.00 40.78  ? 419 ASN C CA  1 
ATOM   11644 C C   . ASN C 1 419 ? 11.374  -5.201  80.541  1.00 37.17  ? 419 ASN C C   1 
ATOM   11645 O O   . ASN C 1 419 ? 12.016  -6.213  80.255  1.00 37.00  ? 419 ASN C O   1 
ATOM   11646 C CB  . ASN C 1 419 ? 10.708  -3.498  78.830  1.00 44.99  ? 419 ASN C CB  1 
ATOM   11647 C CG  . ASN C 1 419 ? 10.939  -2.116  78.241  1.00 72.97  ? 419 ASN C CG  1 
ATOM   11648 O OD1 . ASN C 1 419 ? 10.152  -1.196  78.460  1.00 77.49  ? 419 ASN C OD1 1 
ATOM   11649 N ND2 . ASN C 1 419 ? 12.020  -1.968  77.481  1.00 64.64  ? 419 ASN C ND2 1 
ATOM   11650 N N   . LYS C 1 420 ? 10.350  -5.208  81.399  1.00 39.80  ? 420 LYS C N   1 
ATOM   11651 C CA  . LYS C 1 420 ? 9.959   -6.453  82.056  1.00 39.72  ? 420 LYS C CA  1 
ATOM   11652 C C   . LYS C 1 420 ? 9.596   -7.523  81.034  1.00 36.06  ? 420 LYS C C   1 
ATOM   11653 O O   . LYS C 1 420 ? 10.129  -8.639  81.070  1.00 31.18  ? 420 LYS C O   1 
ATOM   11654 C CB  . LYS C 1 420 ? 8.786   -6.216  83.008  1.00 37.40  ? 420 LYS C CB  1 
ATOM   11655 C CG  . LYS C 1 420 ? 8.497   -7.421  83.898  1.00 36.64  ? 420 LYS C CG  1 
ATOM   11656 C CD  . LYS C 1 420 ? 7.006   -7.640  84.138  1.00 39.38  ? 420 LYS C CD  1 
ATOM   11657 C CE  . LYS C 1 420 ? 6.286   -6.351  84.500  1.00 41.23  ? 420 LYS C CE  1 
ATOM   11658 N NZ  . LYS C 1 420 ? 4.908   -6.311  83.933  1.00 43.10  ? 420 LYS C NZ  1 
ATOM   11659 N N   . GLU C 1 421 ? 8.698   -7.193  80.101  1.00 36.35  ? 421 GLU C N   1 
ATOM   11660 C CA  . GLU C 1 421 ? 8.267   -8.174  79.111  1.00 45.32  ? 421 GLU C CA  1 
ATOM   11661 C C   . GLU C 1 421 ? 9.379   -8.485  78.118  1.00 44.28  ? 421 GLU C C   1 
ATOM   11662 O O   . GLU C 1 421 ? 9.509   -9.627  77.659  1.00 42.29  ? 421 GLU C O   1 
ATOM   11663 C CB  . GLU C 1 421 ? 7.014   -7.675  78.387  1.00 41.86  ? 421 GLU C CB  1 
ATOM   11664 C CG  . GLU C 1 421 ? 5.998   -8.768  78.053  1.00 75.53  ? 421 GLU C CG  1 
ATOM   11665 C CD  . GLU C 1 421 ? 5.915   -9.864  79.105  1.00 78.77  ? 421 GLU C CD  1 
ATOM   11666 O OE1 . GLU C 1 421 ? 5.773   -9.537  80.305  1.00 66.85  ? 421 GLU C OE1 1 
ATOM   11667 O OE2 . GLU C 1 421 ? 6.004   -11.053 78.732  1.00 64.95  ? 421 GLU C OE2 1 
ATOM   11668 N N   . LYS C 1 422 ? 10.188  -7.483  77.766  1.00 40.78  ? 422 LYS C N   1 
ATOM   11669 C CA  . LYS C 1 422 ? 11.290  -7.723  76.843  1.00 38.72  ? 422 LYS C CA  1 
ATOM   11670 C C   . LYS C 1 422 ? 12.399  -8.539  77.494  1.00 33.85  ? 422 LYS C C   1 
ATOM   11671 O O   . LYS C 1 422 ? 13.114  -9.272  76.801  1.00 28.94  ? 422 LYS C O   1 
ATOM   11672 C CB  . LYS C 1 422 ? 11.832  -6.394  76.315  1.00 38.03  ? 422 LYS C CB  1 
ATOM   11673 C CG  . LYS C 1 422 ? 10.744  -5.472  75.787  1.00 40.02  ? 422 LYS C CG  1 
ATOM   11674 C CD  . LYS C 1 422 ? 11.254  -4.530  74.708  1.00 29.66  ? 422 LYS C CD  1 
ATOM   11675 C CE  . LYS C 1 422 ? 10.090  -3.847  74.005  1.00 39.57  ? 422 LYS C CE  1 
ATOM   11676 N NZ  . LYS C 1 422 ? 10.149  -2.364  74.112  1.00 54.61  ? 422 LYS C NZ  1 
ATOM   11677 N N   . ASN C 1 423 ? 12.550  -8.442  78.816  1.00 39.85  ? 423 ASN C N   1 
ATOM   11678 C CA  . ASN C 1 423 ? 13.577  -9.209  79.510  1.00 36.31  ? 423 ASN C CA  1 
ATOM   11679 C C   . ASN C 1 423 ? 13.189  -10.665 79.723  1.00 30.38  ? 423 ASN C C   1 
ATOM   11680 O O   . ASN C 1 423 ? 14.068  -11.492 79.990  1.00 25.61  ? 423 ASN C O   1 
ATOM   11681 C CB  . ASN C 1 423 ? 13.897  -8.568  80.864  1.00 32.95  ? 423 ASN C CB  1 
ATOM   11682 C CG  . ASN C 1 423 ? 14.819  -7.371  80.738  1.00 30.73  ? 423 ASN C CG  1 
ATOM   11683 O OD1 . ASN C 1 423 ? 15.558  -7.240  79.762  1.00 27.44  ? 423 ASN C OD1 1 
ATOM   11684 N ND2 . ASN C 1 423 ? 14.772  -6.482  81.724  1.00 33.40  ? 423 ASN C ND2 1 
ATOM   11685 N N   . GLU C 1 424 ? 11.904  -11.004 79.625  1.00 32.44  ? 424 GLU C N   1 
ATOM   11686 C CA  . GLU C 1 424 ? 11.517  -12.398 79.809  1.00 28.72  ? 424 GLU C CA  1 
ATOM   11687 C C   . GLU C 1 424 ? 11.967  -13.265 78.640  1.00 27.54  ? 424 GLU C C   1 
ATOM   11688 O O   . GLU C 1 424 ? 12.395  -14.408 78.840  1.00 27.53  ? 424 GLU C O   1 
ATOM   11689 C CB  . GLU C 1 424 ? 10.005  -12.499 80.021  1.00 30.98  ? 424 GLU C CB  1 
ATOM   11690 C CG  . GLU C 1 424 ? 9.480   -13.876 80.494  1.00 39.04  ? 424 GLU C CG  1 
ATOM   11691 C CD  . GLU C 1 424 ? 10.383  -14.616 81.497  1.00 64.37  ? 424 GLU C CD  1 
ATOM   11692 O OE1 . GLU C 1 424 ? 10.243  -15.869 81.568  1.00 61.88  ? 424 GLU C OE1 1 
ATOM   11693 O OE2 . GLU C 1 424 ? 11.145  -14.003 82.253  1.00 68.29  ? 424 GLU C OE2 1 
ATOM   11694 N N   . TYR C 1 425 ? 11.878  -12.745 77.416  1.00 26.74  ? 425 TYR C N   1 
ATOM   11695 C CA  . TYR C 1 425 ? 12.318  -13.521 76.262  1.00 25.84  ? 425 TYR C CA  1 
ATOM   11696 C C   . TYR C 1 425 ? 13.821  -13.777 76.306  1.00 24.35  ? 425 TYR C C   1 
ATOM   11697 O O   . TYR C 1 425 ? 14.275  -14.884 75.994  1.00 26.20  ? 425 TYR C O   1 
ATOM   11698 C CB  . TYR C 1 425 ? 11.920  -12.814 74.967  1.00 30.65  ? 425 TYR C CB  1 
ATOM   11699 C CG  . TYR C 1 425 ? 10.536  -13.190 74.488  1.00 27.38  ? 425 TYR C CG  1 
ATOM   11700 C CD1 . TYR C 1 425 ? 9.501   -13.386 75.393  1.00 30.06  ? 425 TYR C CD1 1 
ATOM   11701 C CD2 . TYR C 1 425 ? 10.266  -13.357 73.137  1.00 33.19  ? 425 TYR C CD2 1 
ATOM   11702 C CE1 . TYR C 1 425 ? 8.235   -13.732 74.966  1.00 33.93  ? 425 TYR C CE1 1 
ATOM   11703 C CE2 . TYR C 1 425 ? 9.001   -13.704 72.700  1.00 32.14  ? 425 TYR C CE2 1 
ATOM   11704 C CZ  . TYR C 1 425 ? 7.990   -13.890 73.620  1.00 32.73  ? 425 TYR C CZ  1 
ATOM   11705 O OH  . TYR C 1 425 ? 6.731   -14.235 73.189  1.00 42.86  ? 425 TYR C OH  1 
ATOM   11706 N N   . TRP C 1 426 ? 14.606  -12.772 76.700  1.00 29.16  ? 426 TRP C N   1 
ATOM   11707 C CA  . TRP C 1 426 ? 16.037  -12.994 76.891  1.00 25.76  ? 426 TRP C CA  1 
ATOM   11708 C C   . TRP C 1 426 ? 16.283  -14.035 77.976  1.00 26.75  ? 426 TRP C C   1 
ATOM   11709 O O   . TRP C 1 426 ? 17.192  -14.866 77.856  1.00 28.89  ? 426 TRP C O   1 
ATOM   11710 C CB  . TRP C 1 426 ? 16.737  -11.679 77.239  1.00 21.20  ? 426 TRP C CB  1 
ATOM   11711 C CG  . TRP C 1 426 ? 16.794  -10.702 76.100  1.00 20.35  ? 426 TRP C CG  1 
ATOM   11712 C CD1 . TRP C 1 426 ? 15.964  -9.641  75.890  1.00 24.69  ? 426 TRP C CD1 1 
ATOM   11713 C CD2 . TRP C 1 426 ? 17.731  -10.699 75.016  1.00 23.89  ? 426 TRP C CD2 1 
ATOM   11714 N NE1 . TRP C 1 426 ? 16.326  -8.975  74.743  1.00 28.22  ? 426 TRP C NE1 1 
ATOM   11715 C CE2 . TRP C 1 426 ? 17.408  -9.605  74.187  1.00 27.05  ? 426 TRP C CE2 1 
ATOM   11716 C CE3 . TRP C 1 426 ? 18.813  -11.514 74.665  1.00 20.70  ? 426 TRP C CE3 1 
ATOM   11717 C CZ2 . TRP C 1 426 ? 18.126  -9.306  73.030  1.00 26.51  ? 426 TRP C CZ2 1 
ATOM   11718 C CZ3 . TRP C 1 426 ? 19.525  -11.215 73.515  1.00 17.59  ? 426 TRP C CZ3 1 
ATOM   11719 C CH2 . TRP C 1 426 ? 19.179  -10.120 72.713  1.00 27.44  ? 426 TRP C CH2 1 
ATOM   11720 N N   . LYS C 1 427 ? 15.477  -14.008 79.041  1.00 28.70  ? 427 LYS C N   1 
ATOM   11721 C CA  . LYS C 1 427 ? 15.570  -15.034 80.076  1.00 25.29  ? 427 LYS C CA  1 
ATOM   11722 C C   . LYS C 1 427 ? 15.269  -16.416 79.508  1.00 28.47  ? 427 LYS C C   1 
ATOM   11723 O O   . LYS C 1 427 ? 15.964  -17.391 79.820  1.00 33.53  ? 427 LYS C O   1 
ATOM   11724 C CB  . LYS C 1 427 ? 14.615  -14.707 81.224  1.00 29.44  ? 427 LYS C CB  1 
ATOM   11725 C CG  . LYS C 1 427 ? 15.273  -14.034 82.418  1.00 34.20  ? 427 LYS C CG  1 
ATOM   11726 C CD  . LYS C 1 427 ? 14.361  -14.051 83.640  1.00 43.79  ? 427 LYS C CD  1 
ATOM   11727 C CE  . LYS C 1 427 ? 13.525  -12.779 83.749  1.00 35.68  ? 427 LYS C CE  1 
ATOM   11728 N NZ  . LYS C 1 427 ? 14.330  -11.574 84.088  1.00 42.22  ? 427 LYS C NZ  1 
ATOM   11729 N N   . ILE C 1 428 ? 14.232  -16.519 78.671  1.00 26.28  ? 428 ILE C N   1 
ATOM   11730 C CA  . ILE C 1 428 ? 13.896  -17.791 78.035  1.00 26.93  ? 428 ILE C CA  1 
ATOM   11731 C C   . ILE C 1 428 ? 15.039  -18.262 77.146  1.00 25.56  ? 428 ILE C C   1 
ATOM   11732 O O   . ILE C 1 428 ? 15.390  -19.449 77.130  1.00 27.49  ? 428 ILE C O   1 
ATOM   11733 C CB  . ILE C 1 428 ? 12.584  -17.654 77.238  1.00 27.87  ? 428 ILE C CB  1 
ATOM   11734 C CG1 . ILE C 1 428 ? 11.424  -17.311 78.171  1.00 29.63  ? 428 ILE C CG1 1 
ATOM   11735 C CG2 . ILE C 1 428 ? 12.293  -18.925 76.455  1.00 31.83  ? 428 ILE C CG2 1 
ATOM   11736 C CD1 . ILE C 1 428 ? 10.090  -17.288 77.480  1.00 31.01  ? 428 ILE C CD1 1 
ATOM   11737 N N   . LEU C 1 429 ? 15.635  -17.337 76.391  1.00 28.87  ? 429 LEU C N   1 
ATOM   11738 C CA  . LEU C 1 429 ? 16.732  -17.689 75.497  1.00 22.98  ? 429 LEU C CA  1 
ATOM   11739 C C   . LEU C 1 429 ? 17.957  -18.160 76.271  1.00 24.64  ? 429 LEU C C   1 
ATOM   11740 O O   . LEU C 1 429 ? 18.640  -19.101 75.848  1.00 23.33  ? 429 LEU C O   1 
ATOM   11741 C CB  . LEU C 1 429 ? 17.078  -16.490 74.617  1.00 21.72  ? 429 LEU C CB  1 
ATOM   11742 C CG  . LEU C 1 429 ? 18.092  -16.753 73.512  1.00 20.83  ? 429 LEU C CG  1 
ATOM   11743 C CD1 . LEU C 1 429 ? 17.421  -17.486 72.379  1.00 21.59  ? 429 LEU C CD1 1 
ATOM   11744 C CD2 . LEU C 1 429 ? 18.690  -15.447 73.029  1.00 19.64  ? 429 LEU C CD2 1 
ATOM   11745 N N   . ILE C 1 430 ? 18.253  -17.516 77.401  1.00 26.53  ? 430 ILE C N   1 
ATOM   11746 C CA  . ILE C 1 430 ? 19.451  -17.852 78.164  1.00 22.49  ? 430 ILE C CA  1 
ATOM   11747 C C   . ILE C 1 430 ? 19.367  -19.274 78.707  1.00 25.34  ? 430 ILE C C   1 
ATOM   11748 O O   . ILE C 1 430 ? 20.334  -20.042 78.622  1.00 29.57  ? 430 ILE C O   1 
ATOM   11749 C CB  . ILE C 1 430 ? 19.669  -16.816 79.283  1.00 22.50  ? 430 ILE C CB  1 
ATOM   11750 C CG1 . ILE C 1 430 ? 20.240  -15.522 78.694  1.00 22.84  ? 430 ILE C CG1 1 
ATOM   11751 C CG2 . ILE C 1 430 ? 20.587  -17.365 80.361  1.00 23.15  ? 430 ILE C CG2 1 
ATOM   11752 C CD1 . ILE C 1 430 ? 19.907  -14.281 79.494  1.00 24.22  ? 430 ILE C CD1 1 
ATOM   11753 N N   . GLU C 1 431 ? 18.212  -19.652 79.262  1.00 35.38  ? 431 GLU C N   1 
ATOM   11754 C CA  . GLU C 1 431 ? 18.035  -21.021 79.740  1.00 26.92  ? 431 GLU C CA  1 
ATOM   11755 C C   . GLU C 1 431 ? 18.131  -22.022 78.597  1.00 26.62  ? 431 GLU C C   1 
ATOM   11756 O O   . GLU C 1 431 ? 18.772  -23.071 78.733  1.00 27.21  ? 431 GLU C O   1 
ATOM   11757 C CB  . GLU C 1 431 ? 16.690  -21.156 80.455  1.00 29.28  ? 431 GLU C CB  1 
ATOM   11758 C CG  . GLU C 1 431 ? 16.766  -21.839 81.814  1.00 46.12  ? 431 GLU C CG  1 
ATOM   11759 C CD  . GLU C 1 431 ? 17.708  -21.135 82.775  1.00 58.78  ? 431 GLU C CD  1 
ATOM   11760 O OE1 . GLU C 1 431 ? 17.858  -19.898 82.681  1.00 62.38  ? 431 GLU C OE1 1 
ATOM   11761 O OE2 . GLU C 1 431 ? 18.301  -21.826 83.628  1.00 52.70  ? 431 GLU C OE2 1 
ATOM   11762 N N   . ALA C 1 432 ? 17.502  -21.712 77.460  1.00 26.14  ? 432 ALA C N   1 
ATOM   11763 C CA  . ALA C 1 432 ? 17.572  -22.596 76.301  1.00 26.30  ? 432 ALA C CA  1 
ATOM   11764 C C   . ALA C 1 432 ? 18.993  -22.689 75.763  1.00 26.34  ? 432 ALA C C   1 
ATOM   11765 O O   . ALA C 1 432 ? 19.413  -23.748 75.283  1.00 35.70  ? 432 ALA C O   1 
ATOM   11766 C CB  . ALA C 1 432 ? 16.616  -22.112 75.213  1.00 26.55  ? 432 ALA C CB  1 
ATOM   11767 N N   . LYS C 1 433 ? 19.742  -21.585 75.827  1.00 23.89  ? 433 LYS C N   1 
ATOM   11768 C CA  . LYS C 1 433 ? 21.127  -21.590 75.366  1.00 23.08  ? 433 LYS C CA  1 
ATOM   11769 C C   . LYS C 1 433 ? 21.964  -22.615 76.121  1.00 26.72  ? 433 LYS C C   1 
ATOM   11770 O O   . LYS C 1 433 ? 22.751  -23.352 75.515  1.00 29.10  ? 433 LYS C O   1 
ATOM   11771 C CB  . LYS C 1 433 ? 21.733  -20.195 75.525  1.00 24.17  ? 433 LYS C CB  1 
ATOM   11772 C CG  . LYS C 1 433 ? 23.063  -19.983 74.820  1.00 20.96  ? 433 LYS C CG  1 
ATOM   11773 C CD  . LYS C 1 433 ? 23.264  -20.938 73.659  1.00 24.56  ? 433 LYS C CD  1 
ATOM   11774 C CE  . LYS C 1 433 ? 24.557  -20.644 72.959  1.00 32.53  ? 433 LYS C CE  1 
ATOM   11775 N NZ  . LYS C 1 433 ? 24.288  -19.580 71.981  1.00 36.58  ? 433 LYS C NZ  1 
ATOM   11776 N N   . LYS C 1 434 ? 21.799  -22.684 77.444  1.00 33.72  ? 434 LYS C N   1 
ATOM   11777 C CA  . LYS C 1 434 ? 22.689  -23.499 78.266  1.00 25.62  ? 434 LYS C CA  1 
ATOM   11778 C C   . LYS C 1 434 ? 22.694  -24.958 77.829  1.00 28.18  ? 434 LYS C C   1 
ATOM   11779 O O   . LYS C 1 434 ? 23.697  -25.657 78.018  1.00 32.98  ? 434 LYS C O   1 
ATOM   11780 C CB  . LYS C 1 434 ? 22.293  -23.383 79.737  1.00 26.58  ? 434 LYS C CB  1 
ATOM   11781 C CG  . LYS C 1 434 ? 22.863  -22.157 80.426  1.00 29.88  ? 434 LYS C CG  1 
ATOM   11782 C CD  . LYS C 1 434 ? 22.526  -22.154 81.903  1.00 30.96  ? 434 LYS C CD  1 
ATOM   11783 C CE  . LYS C 1 434 ? 21.061  -21.827 82.123  1.00 39.48  ? 434 LYS C CE  1 
ATOM   11784 N NZ  . LYS C 1 434 ? 20.785  -21.445 83.535  1.00 48.37  ? 434 LYS C NZ  1 
ATOM   11785 N N   . LYS C 1 435 ? 21.596  -25.435 77.241  1.00 27.36  ? 435 LYS C N   1 
ATOM   11786 C CA  . LYS C 1 435 ? 21.525  -26.798 76.732  1.00 31.77  ? 435 LYS C CA  1 
ATOM   11787 C C   . LYS C 1 435 ? 21.104  -26.815 75.266  1.00 28.28  ? 435 LYS C C   1 
ATOM   11788 O O   . LYS C 1 435 ? 20.428  -27.745 74.818  1.00 35.99  ? 435 LYS C O   1 
ATOM   11789 C CB  . LYS C 1 435 ? 20.577  -27.646 77.579  1.00 40.67  ? 435 LYS C CB  1 
ATOM   11790 C CG  . LYS C 1 435 ? 20.858  -27.584 79.078  1.00 43.97  ? 435 LYS C CG  1 
ATOM   11791 C CD  . LYS C 1 435 ? 21.998  -28.510 79.482  1.00 50.62  ? 435 LYS C CD  1 
ATOM   11792 C CE  . LYS C 1 435 ? 21.968  -28.813 80.974  1.00 44.54  ? 435 LYS C CE  1 
ATOM   11793 N NZ  . LYS C 1 435 ? 23.276  -28.541 81.634  1.00 43.49  ? 435 LYS C NZ  1 
ATOM   11794 N N   . ALA C 1 436 ? 21.494  -25.793 74.505  1.00 27.24  ? 436 ALA C N   1 
ATOM   11795 C CA  . ALA C 1 436 ? 21.153  -25.724 73.089  1.00 23.14  ? 436 ALA C CA  1 
ATOM   11796 C C   . ALA C 1 436 ? 21.990  -26.730 72.310  1.00 27.48  ? 436 ALA C C   1 
ATOM   11797 O O   . ALA C 1 436 ? 23.224  -26.670 72.333  1.00 33.02  ? 436 ALA C O   1 
ATOM   11798 C CB  . ALA C 1 436 ? 21.379  -24.311 72.558  1.00 28.17  ? 436 ALA C CB  1 
ATOM   11799 N N   . LYS C 1 437 ? 21.321  -27.646 71.611  1.00 32.49  ? 437 LYS C N   1 
ATOM   11800 C CA  . LYS C 1 437 ? 21.982  -28.789 70.997  1.00 31.47  ? 437 LYS C CA  1 
ATOM   11801 C C   . LYS C 1 437 ? 22.031  -28.737 69.476  1.00 29.50  ? 437 LYS C C   1 
ATOM   11802 O O   . LYS C 1 437 ? 22.565  -29.666 68.861  1.00 35.35  ? 437 LYS C O   1 
ATOM   11803 C CB  . LYS C 1 437 ? 21.299  -30.086 71.445  1.00 26.29  ? 437 LYS C CB  1 
ATOM   11804 C CG  . LYS C 1 437 ? 22.112  -30.885 72.440  1.00 22.04  ? 437 LYS C CG  1 
ATOM   11805 C CD  . LYS C 1 437 ? 21.877  -30.398 73.854  1.00 26.35  ? 437 LYS C CD  1 
ATOM   11806 C CE  . LYS C 1 437 ? 22.356  -31.416 74.864  1.00 48.67  ? 437 LYS C CE  1 
ATOM   11807 N NZ  . LYS C 1 437 ? 22.524  -30.835 76.227  1.00 40.33  ? 437 LYS C NZ  1 
ATOM   11808 N N   . ASN C 1 438 ? 21.502  -27.689 68.850  1.00 31.58  ? 438 ASN C N   1 
ATOM   11809 C CA  . ASN C 1 438 ? 21.576  -27.562 67.401  1.00 23.02  ? 438 ASN C CA  1 
ATOM   11810 C C   . ASN C 1 438 ? 21.563  -26.078 67.049  1.00 24.41  ? 438 ASN C C   1 
ATOM   11811 O O   . ASN C 1 438 ? 21.593  -25.211 67.929  1.00 34.55  ? 438 ASN C O   1 
ATOM   11812 C CB  . ASN C 1 438 ? 20.442  -28.344 66.724  1.00 27.37  ? 438 ASN C CB  1 
ATOM   11813 C CG  . ASN C 1 438 ? 19.068  -27.830 67.104  1.00 28.59  ? 438 ASN C CG  1 
ATOM   11814 O OD1 . ASN C 1 438 ? 18.669  -26.744 66.693  1.00 27.96  ? 438 ASN C OD1 1 
ATOM   11815 N ND2 . ASN C 1 438 ? 18.337  -28.612 67.889  1.00 31.21  ? 438 ASN C ND2 1 
ATOM   11816 N N   . ASP C 1 439 ? 21.509  -25.785 65.751  1.00 25.51  ? 439 ASP C N   1 
ATOM   11817 C CA  . ASP C 1 439 ? 21.677  -24.421 65.264  1.00 33.90  ? 439 ASP C CA  1 
ATOM   11818 C C   . ASP C 1 439 ? 20.404  -23.586 65.334  1.00 26.73  ? 439 ASP C C   1 
ATOM   11819 O O   . ASP C 1 439 ? 20.457  -22.392 65.021  1.00 23.81  ? 439 ASP C O   1 
ATOM   11820 C CB  . ASP C 1 439 ? 22.204  -24.443 63.825  1.00 32.68  ? 439 ASP C CB  1 
ATOM   11821 C CG  . ASP C 1 439 ? 23.699  -24.699 63.756  1.00 53.61  ? 439 ASP C CG  1 
ATOM   11822 O OD1 . ASP C 1 439 ? 24.415  -24.281 64.692  1.00 54.30  ? 439 ASP C OD1 1 
ATOM   11823 O OD2 . ASP C 1 439 ? 24.160  -25.308 62.766  1.00 50.97  ? 439 ASP C OD2 1 
ATOM   11824 N N   . TYR C 1 440 ? 19.267  -24.167 65.732  1.00 22.49  ? 440 TYR C N   1 
ATOM   11825 C CA  . TYR C 1 440 ? 18.046  -23.377 65.854  1.00 22.69  ? 440 TYR C CA  1 
ATOM   11826 C C   . TYR C 1 440 ? 18.167  -22.285 66.906  1.00 25.96  ? 440 TYR C C   1 
ATOM   11827 O O   . TYR C 1 440 ? 17.401  -21.316 66.866  1.00 29.85  ? 440 TYR C O   1 
ATOM   11828 C CB  . TYR C 1 440 ? 16.852  -24.272 66.190  1.00 31.19  ? 440 TYR C CB  1 
ATOM   11829 C CG  . TYR C 1 440 ? 16.171  -24.869 64.982  1.00 34.65  ? 440 TYR C CG  1 
ATOM   11830 C CD1 . TYR C 1 440 ? 15.192  -24.163 64.295  1.00 39.80  ? 440 TYR C CD1 1 
ATOM   11831 C CD2 . TYR C 1 440 ? 16.501  -26.141 64.531  1.00 31.97  ? 440 TYR C CD2 1 
ATOM   11832 C CE1 . TYR C 1 440 ? 14.564  -24.704 63.189  1.00 41.14  ? 440 TYR C CE1 1 
ATOM   11833 C CE2 . TYR C 1 440 ? 15.878  -26.692 63.427  1.00 36.17  ? 440 TYR C CE2 1 
ATOM   11834 C CZ  . TYR C 1 440 ? 14.911  -25.969 62.759  1.00 48.26  ? 440 TYR C CZ  1 
ATOM   11835 O OH  . TYR C 1 440 ? 14.286  -26.514 61.660  1.00 47.21  ? 440 TYR C OH  1 
ATOM   11836 N N   . ILE C 1 441 ? 19.105  -22.417 67.848  1.00 24.80  ? 441 ILE C N   1 
ATOM   11837 C CA  . ILE C 1 441 ? 19.325  -21.357 68.827  1.00 26.62  ? 441 ILE C CA  1 
ATOM   11838 C C   . ILE C 1 441 ? 19.735  -20.066 68.131  1.00 22.72  ? 441 ILE C C   1 
ATOM   11839 O O   . ILE C 1 441 ? 19.468  -18.967 68.633  1.00 21.20  ? 441 ILE C O   1 
ATOM   11840 C CB  . ILE C 1 441 ? 20.366  -21.806 69.876  1.00 28.17  ? 441 ILE C CB  1 
ATOM   11841 C CG1 . ILE C 1 441 ? 20.414  -20.822 71.048  1.00 18.76  ? 441 ILE C CG1 1 
ATOM   11842 C CG2 . ILE C 1 441 ? 21.746  -21.969 69.241  1.00 31.78  ? 441 ILE C CG2 1 
ATOM   11843 C CD1 . ILE C 1 441 ? 19.326  -21.040 72.077  1.00 18.05  ? 441 ILE C CD1 1 
ATOM   11844 N N   . LEU C 1 442 ? 20.380  -20.172 66.966  1.00 23.47  ? 442 LEU C N   1 
ATOM   11845 C CA  . LEU C 1 442 ? 20.698  -18.983 66.183  1.00 22.00  ? 442 LEU C CA  1 
ATOM   11846 C C   . LEU C 1 442 ? 19.430  -18.273 65.724  1.00 22.45  ? 442 LEU C C   1 
ATOM   11847 O O   . LEU C 1 442 ? 19.352  -17.040 65.759  1.00 25.11  ? 442 LEU C O   1 
ATOM   11848 C CB  . LEU C 1 442 ? 21.564  -19.370 64.985  1.00 26.65  ? 442 LEU C CB  1 
ATOM   11849 C CG  . LEU C 1 442 ? 22.961  -19.915 65.289  1.00 26.48  ? 442 LEU C CG  1 
ATOM   11850 C CD1 . LEU C 1 442 ? 23.844  -19.843 64.052  1.00 24.91  ? 442 LEU C CD1 1 
ATOM   11851 C CD2 . LEU C 1 442 ? 23.599  -19.162 66.447  1.00 24.01  ? 442 LEU C CD2 1 
ATOM   11852 N N   . VAL C 1 443 ? 18.426  -19.038 65.290  1.00 22.44  ? 443 VAL C N   1 
ATOM   11853 C CA  . VAL C 1 443 ? 17.166  -18.441 64.858  1.00 23.13  ? 443 VAL C CA  1 
ATOM   11854 C C   . VAL C 1 443 ? 16.458  -17.770 66.025  1.00 22.51  ? 443 VAL C C   1 
ATOM   11855 O O   . VAL C 1 443 ? 15.803  -16.735 65.853  1.00 23.34  ? 443 VAL C O   1 
ATOM   11856 C CB  . VAL C 1 443 ? 16.264  -19.503 64.204  1.00 23.41  ? 443 VAL C CB  1 
ATOM   11857 C CG1 . VAL C 1 443 ? 15.204  -18.837 63.337  1.00 28.54  ? 443 VAL C CG1 1 
ATOM   11858 C CG2 . VAL C 1 443 ? 17.093  -20.486 63.396  1.00 30.13  ? 443 VAL C CG2 1 
ATOM   11859 N N   . ALA C 1 444 ? 16.569  -18.341 67.223  1.00 21.31  ? 444 ALA C N   1 
ATOM   11860 C CA  . ALA C 1 444 ? 15.892  -17.789 68.387  1.00 20.95  ? 444 ALA C CA  1 
ATOM   11861 C C   . ALA C 1 444 ? 16.497  -16.471 68.855  1.00 21.25  ? 444 ALA C C   1 
ATOM   11862 O O   . ALA C 1 444 ? 15.905  -15.811 69.716  1.00 21.33  ? 444 ALA C O   1 
ATOM   11863 C CB  . ALA C 1 444 ? 15.908  -18.812 69.525  1.00 21.08  ? 444 ALA C CB  1 
ATOM   11864 N N   . GLU C 1 445 ? 17.647  -16.072 68.312  1.00 21.87  ? 445 GLU C N   1 
ATOM   11865 C CA  . GLU C 1 445 ? 18.303  -14.826 68.684  1.00 22.08  ? 445 GLU C CA  1 
ATOM   11866 C C   . GLU C 1 445 ? 17.996  -13.686 67.723  1.00 23.44  ? 445 GLU C C   1 
ATOM   11867 O O   . GLU C 1 445 ? 18.583  -12.607 67.854  1.00 27.63  ? 445 GLU C O   1 
ATOM   11868 C CB  . GLU C 1 445 ? 19.815  -15.033 68.773  1.00 21.93  ? 445 GLU C CB  1 
ATOM   11869 C CG  . GLU C 1 445 ? 20.238  -16.047 69.816  1.00 22.00  ? 445 GLU C CG  1 
ATOM   11870 C CD  . GLU C 1 445 ? 21.612  -16.613 69.541  1.00 30.78  ? 445 GLU C CD  1 
ATOM   11871 O OE1 . GLU C 1 445 ? 21.906  -17.729 70.016  1.00 37.10  ? 445 GLU C OE1 1 
ATOM   11872 O OE2 . GLU C 1 445 ? 22.401  -15.938 68.846  1.00 29.48  ? 445 GLU C OE2 1 
ATOM   11873 N N   . GLY C 1 446 ? 17.111  -13.904 66.755  1.00 24.11  ? 446 GLY C N   1 
ATOM   11874 C CA  . GLY C 1 446 ? 16.728  -12.820 65.868  1.00 25.68  ? 446 GLY C CA  1 
ATOM   11875 C C   . GLY C 1 446 ? 16.135  -11.659 66.645  1.00 26.11  ? 446 GLY C C   1 
ATOM   11876 O O   . GLY C 1 446 ? 15.388  -11.847 67.608  1.00 25.50  ? 446 GLY C O   1 
ATOM   11877 N N   . SER C 1 447 ? 16.492  -10.440 66.230  1.00 27.38  ? 447 SER C N   1 
ATOM   11878 C CA  . SER C 1 447 ? 15.970  -9.255  66.904  1.00 28.09  ? 447 SER C CA  1 
ATOM   11879 C C   . SER C 1 447 ? 14.454  -9.162  66.779  1.00 29.02  ? 447 SER C C   1 
ATOM   11880 O O   . SER C 1 447 ? 13.801  -8.531  67.619  1.00 29.27  ? 447 SER C O   1 
ATOM   11881 C CB  . SER C 1 447 ? 16.629  -7.996  66.335  1.00 29.55  ? 447 SER C CB  1 
ATOM   11882 O OG  . SER C 1 447 ? 16.133  -7.698  65.043  1.00 31.17  ? 447 SER C OG  1 
ATOM   11883 N N   . ASP C 1 448 ? 13.879  -9.788  65.748  1.00 31.25  ? 448 ASP C N   1 
ATOM   11884 C CA  . ASP C 1 448 ? 12.448  -9.671  65.486  1.00 30.63  ? 448 ASP C CA  1 
ATOM   11885 C C   . ASP C 1 448 ? 11.589  -10.268 66.596  1.00 29.72  ? 448 ASP C C   1 
ATOM   11886 O O   . ASP C 1 448 ? 10.421  -9.888  66.730  1.00 36.99  ? 448 ASP C O   1 
ATOM   11887 C CB  . ASP C 1 448 ? 12.107  -10.340 64.152  1.00 31.48  ? 448 ASP C CB  1 
ATOM   11888 C CG  . ASP C 1 448 ? 13.097  -9.992  63.055  1.00 32.37  ? 448 ASP C CG  1 
ATOM   11889 O OD1 . ASP C 1 448 ? 14.214  -10.552 63.055  1.00 31.25  ? 448 ASP C OD1 1 
ATOM   11890 O OD2 . ASP C 1 448 ? 12.753  -9.159  62.188  1.00 34.43  ? 448 ASP C OD2 1 
ATOM   11891 N N   . TRP C 1 449 ? 12.126  -11.199 67.387  1.00 27.89  ? 449 TRP C N   1 
ATOM   11892 C CA  . TRP C 1 449 ? 11.330  -11.810 68.445  1.00 27.22  ? 449 TRP C CA  1 
ATOM   11893 C C   . TRP C 1 449 ? 11.248  -10.932 69.686  1.00 28.94  ? 449 TRP C C   1 
ATOM   11894 O O   . TRP C 1 449 ? 10.271  -11.022 70.438  1.00 31.34  ? 449 TRP C O   1 
ATOM   11895 C CB  . TRP C 1 449 ? 11.898  -13.185 68.806  1.00 25.47  ? 449 TRP C CB  1 
ATOM   11896 C CG  . TRP C 1 449 ? 12.264  -14.000 67.608  1.00 25.33  ? 449 TRP C CG  1 
ATOM   11897 C CD1 . TRP C 1 449 ? 13.517  -14.380 67.228  1.00 24.62  ? 449 TRP C CD1 1 
ATOM   11898 C CD2 . TRP C 1 449 ? 11.369  -14.524 66.620  1.00 26.22  ? 449 TRP C CD2 1 
ATOM   11899 N NE1 . TRP C 1 449 ? 13.458  -15.114 66.069  1.00 25.02  ? 449 TRP C NE1 1 
ATOM   11900 C CE2 . TRP C 1 449 ? 12.150  -15.216 65.675  1.00 25.98  ? 449 TRP C CE2 1 
ATOM   11901 C CE3 . TRP C 1 449 ? 9.983   -14.477 66.445  1.00 27.42  ? 449 TRP C CE3 1 
ATOM   11902 C CZ2 . TRP C 1 449 ? 11.592  -15.855 64.571  1.00 26.88  ? 449 TRP C CZ2 1 
ATOM   11903 C CZ3 . TRP C 1 449 ? 9.430   -15.114 65.350  1.00 28.29  ? 449 TRP C CZ3 1 
ATOM   11904 C CH2 . TRP C 1 449 ? 10.233  -15.793 64.427  1.00 28.15  ? 449 TRP C CH2 1 
ATOM   11905 N N   . PHE C 1 450 ? 12.252  -10.086 69.918  1.00 31.12  ? 450 PHE C N   1 
ATOM   11906 C CA  . PHE C 1 450 ? 12.247  -9.181  71.059  1.00 30.94  ? 450 PHE C CA  1 
ATOM   11907 C C   . PHE C 1 450 ? 11.708  -7.799  70.722  1.00 35.67  ? 450 PHE C C   1 
ATOM   11908 O O   . PHE C 1 450 ? 11.372  -7.041  71.639  1.00 30.57  ? 450 PHE C O   1 
ATOM   11909 C CB  . PHE C 1 450 ? 13.662  -9.043  71.636  1.00 26.88  ? 450 PHE C CB  1 
ATOM   11910 C CG  . PHE C 1 450 ? 14.408  -10.343 71.730  1.00 25.23  ? 450 PHE C CG  1 
ATOM   11911 C CD1 . PHE C 1 450 ? 14.262  -11.161 72.837  1.00 24.34  ? 450 PHE C CD1 1 
ATOM   11912 C CD2 . PHE C 1 450 ? 15.251  -10.749 70.708  1.00 29.00  ? 450 PHE C CD2 1 
ATOM   11913 C CE1 . PHE C 1 450 ? 14.945  -12.360 72.923  1.00 24.44  ? 450 PHE C CE1 1 
ATOM   11914 C CE2 . PHE C 1 450 ? 15.935  -11.947 70.789  1.00 26.34  ? 450 PHE C CE2 1 
ATOM   11915 C CZ  . PHE C 1 450 ? 15.782  -12.753 71.897  1.00 22.64  ? 450 PHE C CZ  1 
ATOM   11916 N N   . TRP C 1 451 ? 11.622  -7.458  69.435  1.00 34.69  ? 451 TRP C N   1 
ATOM   11917 C CA  . TRP C 1 451 ? 11.069  -6.167  69.039  1.00 35.16  ? 451 TRP C CA  1 
ATOM   11918 C C   . TRP C 1 451 ? 9.591   -6.069  69.393  1.00 38.19  ? 451 TRP C C   1 
ATOM   11919 O O   . TRP C 1 451 ? 9.146   -5.078  69.982  1.00 45.15  ? 451 TRP C O   1 
ATOM   11920 C CB  . TRP C 1 451 ? 11.272  -5.954  67.538  1.00 33.93  ? 451 TRP C CB  1 
ATOM   11921 C CG  . TRP C 1 451 ? 11.372  -4.518  67.130  1.00 40.59  ? 451 TRP C CG  1 
ATOM   11922 C CD1 . TRP C 1 451 ? 12.508  -3.769  67.043  1.00 46.36  ? 451 TRP C CD1 1 
ATOM   11923 C CD2 . TRP C 1 451 ? 10.293  -3.655  66.747  1.00 38.28  ? 451 TRP C CD2 1 
ATOM   11924 N NE1 . TRP C 1 451 ? 12.206  -2.495  66.626  1.00 40.36  ? 451 TRP C NE1 1 
ATOM   11925 C CE2 . TRP C 1 451 ? 10.853  -2.398  66.441  1.00 39.71  ? 451 TRP C CE2 1 
ATOM   11926 C CE3 . TRP C 1 451 ? 8.909   -3.822  66.632  1.00 39.55  ? 451 TRP C CE3 1 
ATOM   11927 C CZ2 . TRP C 1 451 ? 10.079  -1.317  66.030  1.00 42.34  ? 451 TRP C CZ2 1 
ATOM   11928 C CZ3 . TRP C 1 451 ? 8.143   -2.746  66.223  1.00 42.22  ? 451 TRP C CZ3 1 
ATOM   11929 C CH2 . TRP C 1 451 ? 8.730   -1.510  65.927  1.00 48.60  ? 451 TRP C CH2 1 
ATOM   11930 N N   . TRP C 1 452 ? 8.821   -7.105  69.064  1.00 36.33  ? 452 TRP C N   1 
ATOM   11931 C CA  . TRP C 1 452 ? 7.368   -7.071  69.130  1.00 43.83  ? 452 TRP C CA  1 
ATOM   11932 C C   . TRP C 1 452 ? 6.822   -7.405  70.512  1.00 48.05  ? 452 TRP C C   1 
ATOM   11933 O O   . TRP C 1 452 ? 5.670   -7.844  70.616  1.00 47.50  ? 452 TRP C O   1 
ATOM   11934 C CB  . TRP C 1 452 ? 6.773   -8.034  68.100  1.00 47.28  ? 452 TRP C CB  1 
ATOM   11935 C CG  . TRP C 1 452 ? 6.803   -7.540  66.682  1.00 51.15  ? 452 TRP C CG  1 
ATOM   11936 C CD1 . TRP C 1 452 ? 7.419   -8.136  65.620  1.00 38.47  ? 452 TRP C CD1 1 
ATOM   11937 C CD2 . TRP C 1 452 ? 6.189   -6.350  66.173  1.00 54.55  ? 452 TRP C CD2 1 
ATOM   11938 N NE1 . TRP C 1 452 ? 7.224   -7.391  64.482  1.00 48.97  ? 452 TRP C NE1 1 
ATOM   11939 C CE2 . TRP C 1 452 ? 6.473   -6.289  64.795  1.00 59.49  ? 452 TRP C CE2 1 
ATOM   11940 C CE3 . TRP C 1 452 ? 5.431   -5.328  66.750  1.00 59.19  ? 452 TRP C CE3 1 
ATOM   11941 C CZ2 . TRP C 1 452 ? 6.022   -5.249  63.985  1.00 70.57  ? 452 TRP C CZ2 1 
ATOM   11942 C CZ3 . TRP C 1 452 ? 4.986   -4.298  65.944  1.00 64.07  ? 452 TRP C CZ3 1 
ATOM   11943 C CH2 . TRP C 1 452 ? 5.280   -4.265  64.577  1.00 73.45  ? 452 TRP C CH2 1 
ATOM   11944 N N   . GLN C 1 453 ? 7.610   -7.223  71.568  1.00 54.72  ? 453 GLN C N   1 
ATOM   11945 C CA  . GLN C 1 453 ? 7.171   -7.562  72.921  1.00 57.42  ? 453 GLN C CA  1 
ATOM   11946 C C   . GLN C 1 453 ? 6.600   -6.322  73.610  1.00 53.56  ? 453 GLN C C   1 
ATOM   11947 O O   . GLN C 1 453 ? 7.134   -5.805  74.591  1.00 48.32  ? 453 GLN C O   1 
ATOM   11948 C CB  . GLN C 1 453 ? 8.324   -8.171  73.713  1.00 43.11  ? 453 GLN C CB  1 
ATOM   11949 C CG  . GLN C 1 453 ? 8.372   -9.691  73.665  1.00 34.81  ? 453 GLN C CG  1 
ATOM   11950 C CD  . GLN C 1 453 ? 6.992   -10.316 73.576  1.00 46.81  ? 453 GLN C CD  1 
ATOM   11951 O OE1 . GLN C 1 453 ? 6.311   -10.486 74.587  1.00 62.45  ? 453 GLN C OE1 1 
ATOM   11952 N NE2 . GLN C 1 453 ? 6.578   -10.671 72.364  1.00 43.10  ? 453 GLN C NE2 1 
ATOM   11953 N N   . GLY C 1 454 ? 5.483   -5.855  73.069  1.00 54.23  ? 454 GLY C N   1 
ATOM   11954 C CA  . GLY C 1 454 ? 4.742   -4.769  73.668  1.00 58.96  ? 454 GLY C CA  1 
ATOM   11955 C C   . GLY C 1 454 ? 5.055   -3.412  73.069  1.00 73.54  ? 454 GLY C C   1 
ATOM   11956 O O   . GLY C 1 454 ? 5.511   -3.278  71.930  1.00 69.19  ? 454 GLY C O   1 
ATOM   11957 N N   . GLU C 1 455 ? 4.750   -2.381  73.863  1.00 82.98  ? 455 GLU C N   1 
ATOM   11958 C CA  . GLU C 1 455 ? 4.949   -0.964  73.557  1.00 88.79  ? 455 GLU C CA  1 
ATOM   11959 C C   . GLU C 1 455 ? 3.944   -0.483  72.514  1.00 77.45  ? 455 GLU C C   1 
ATOM   11960 O O   . GLU C 1 455 ? 3.744   0.725   72.343  1.00 82.10  ? 455 GLU C O   1 
ATOM   11961 C CB  . GLU C 1 455 ? 6.385   -0.710  73.079  1.00 83.68  ? 455 GLU C CB  1 
ATOM   11962 C CG  . GLU C 1 455 ? 6.764   0.758   72.946  1.00 84.30  ? 455 GLU C CG  1 
ATOM   11963 C CD  . GLU C 1 455 ? 6.815   1.467   74.279  1.00 91.99  ? 455 GLU C CD  1 
ATOM   11964 O OE1 . GLU C 1 455 ? 7.563   1.000   75.162  1.00 88.60  ? 455 GLU C OE1 1 
ATOM   11965 O OE2 . GLU C 1 455 ? 6.112   2.487   74.444  1.00 74.79  ? 455 GLU C OE2 1 
ATOM   11966 N N   . GLU C 1 456 ? 3.262   -1.427  71.863  1.00 76.42  ? 456 GLU C N   1 
ATOM   11967 C CA  . GLU C 1 456 ? 2.180   -1.151  70.928  1.00 84.61  ? 456 GLU C CA  1 
ATOM   11968 C C   . GLU C 1 456 ? 1.536   -2.480  70.547  1.00 79.36  ? 456 GLU C C   1 
ATOM   11969 O O   . GLU C 1 456 ? 2.242   -3.477  70.354  1.00 73.23  ? 456 GLU C O   1 
ATOM   11970 C CB  . GLU C 1 456 ? 2.679   -0.383  69.702  1.00 87.08  ? 456 GLU C CB  1 
ATOM   11971 C CG  . GLU C 1 456 ? 3.432   -1.201  68.667  1.00 74.27  ? 456 GLU C CG  1 
ATOM   11972 C CD  . GLU C 1 456 ? 2.699   -1.266  67.346  1.00 69.70  ? 456 GLU C CD  1 
ATOM   11973 O OE1 . GLU C 1 456 ? 3.144   -2.015  66.455  1.00 66.63  ? 456 GLU C OE1 1 
ATOM   11974 O OE2 . GLU C 1 456 ? 1.675   -0.567  67.199  1.00 65.02  ? 456 GLU C OE2 1 
ATOM   11975 N N   . LYS C 1 457 ? 0.207   -2.528  70.464  1.00 65.86  ? 457 LYS C N   1 
ATOM   11976 C CA  . LYS C 1 457 ? -0.451  -3.785  70.126  1.00 74.45  ? 457 LYS C CA  1 
ATOM   11977 C C   . LYS C 1 457 ? -0.373  -4.003  68.618  1.00 78.34  ? 457 LYS C C   1 
ATOM   11978 O O   . LYS C 1 457 ? -0.802  -3.147  67.838  1.00 76.09  ? 457 LYS C O   1 
ATOM   11979 C CB  . LYS C 1 457 ? -1.894  -3.811  70.621  1.00 80.19  ? 457 LYS C CB  1 
ATOM   11980 C CG  . LYS C 1 457 ? -2.569  -5.172  70.447  1.00 72.52  ? 457 LYS C CG  1 
ATOM   11981 C CD  . LYS C 1 457 ? -1.695  -6.316  70.969  1.00 60.39  ? 457 LYS C CD  1 
ATOM   11982 C CE  . LYS C 1 457 ? -1.475  -6.237  72.476  1.00 54.05  ? 457 LYS C CE  1 
ATOM   11983 N NZ  . LYS C 1 457 ? -2.737  -5.972  73.217  1.00 76.71  ? 457 LYS C NZ  1 
ATOM   11984 N N   . ALA C 1 458 ? 0.177   -5.142  68.223  1.00 80.14  ? 458 ALA C N   1 
ATOM   11985 C CA  . ALA C 1 458 ? 0.591   -5.462  66.871  1.00 70.86  ? 458 ALA C CA  1 
ATOM   11986 C C   . ALA C 1 458 ? -0.234  -6.622  66.331  1.00 78.25  ? 458 ALA C C   1 
ATOM   11987 O O   . ALA C 1 458 ? -0.844  -7.375  67.097  1.00 76.47  ? 458 ALA C O   1 
ATOM   11988 C CB  . ALA C 1 458 ? 2.081   -5.835  66.882  1.00 65.48  ? 458 ALA C CB  1 
ATOM   11989 N N   . PRO C 1 459 ? -0.280  -6.796  65.013  1.00 82.71  ? 459 PRO C N   1 
ATOM   11990 C CA  . PRO C 1 459 ? -1.051  -7.922  64.464  1.00 73.04  ? 459 PRO C CA  1 
ATOM   11991 C C   . PRO C 1 459 ? -0.340  -9.249  64.638  1.00 66.95  ? 459 PRO C C   1 
ATOM   11992 O O   . PRO C 1 459 ? 0.868   -9.371  64.424  1.00 58.17  ? 459 PRO C O   1 
ATOM   11993 C CB  . PRO C 1 459 ? -1.201  -7.558  62.970  1.00 65.15  ? 459 PRO C CB  1 
ATOM   11994 C CG  . PRO C 1 459 ? 0.050   -6.802  62.649  1.00 75.74  ? 459 PRO C CG  1 
ATOM   11995 C CD  . PRO C 1 459 ? 0.606   -6.217  63.949  1.00 66.21  ? 459 PRO C CD  1 
ATOM   11996 N N   . PHE C 1 460 ? -1.109  -10.242 65.073  1.00 67.82  ? 460 PHE C N   1 
ATOM   11997 C CA  . PHE C 1 460 ? -0.623  -11.628 65.228  1.00 66.05  ? 460 PHE C CA  1 
ATOM   11998 C C   . PHE C 1 460 ? 0.565   -11.672 66.195  1.00 60.66  ? 460 PHE C C   1 
ATOM   11999 O O   . PHE C 1 460 ? 1.660   -12.120 65.857  1.00 56.94  ? 460 PHE C O   1 
ATOM   12000 C CB  . PHE C 1 460 ? -0.240  -12.211 63.858  1.00 67.67  ? 460 PHE C CB  1 
ATOM   12001 C CG  . PHE C 1 460 ? -1.108  -11.731 62.727  1.00 72.41  ? 460 PHE C CG  1 
ATOM   12002 C CD1 . PHE C 1 460 ? -2.438  -12.105 62.644  1.00 63.73  ? 460 PHE C CD1 1 
ATOM   12003 C CD2 . PHE C 1 460 ? -0.590  -10.891 61.750  1.00 73.05  ? 460 PHE C CD2 1 
ATOM   12004 C CE1 . PHE C 1 460 ? -3.235  -11.664 61.604  1.00 64.39  ? 460 PHE C CE1 1 
ATOM   12005 C CE2 . PHE C 1 460 ? -1.384  -10.444 60.708  1.00 79.18  ? 460 PHE C CE2 1 
ATOM   12006 C CZ  . PHE C 1 460 ? -2.708  -10.832 60.636  1.00 70.19  ? 460 PHE C CZ  1 
ATOM   12007 N N   . VAL C 1 461 ? 0.321   -11.192 67.419  1.00 61.19  ? 461 VAL C N   1 
ATOM   12008 C CA  . VAL C 1 461 ? 1.340   -11.315 68.456  1.00 52.16  ? 461 VAL C CA  1 
ATOM   12009 C C   . VAL C 1 461 ? 1.495   -12.768 68.874  1.00 40.27  ? 461 VAL C C   1 
ATOM   12010 O O   . VAL C 1 461 ? 2.595   -13.204 69.234  1.00 47.39  ? 461 VAL C O   1 
ATOM   12011 C CB  . VAL C 1 461 ? 1.019   -10.415 69.662  1.00 46.93  ? 461 VAL C CB  1 
ATOM   12012 C CG1 . VAL C 1 461 ? 1.498   -8.990  69.410  1.00 66.66  ? 461 VAL C CG1 1 
ATOM   12013 C CG2 . VAL C 1 461 ? -0.468  -10.443 69.976  1.00 65.23  ? 461 VAL C CG2 1 
ATOM   12014 N N   . GLU C 1 462 ? 0.406   -13.540 68.837  1.00 38.65  ? 462 GLU C N   1 
ATOM   12015 C CA  . GLU C 1 462 ? 0.488   -14.953 69.195  1.00 46.56  ? 462 GLU C CA  1 
ATOM   12016 C C   . GLU C 1 462 ? 1.401   -15.707 68.237  1.00 40.94  ? 462 GLU C C   1 
ATOM   12017 O O   . GLU C 1 462 ? 2.146   -16.603 68.654  1.00 42.78  ? 462 GLU C O   1 
ATOM   12018 C CB  . GLU C 1 462 ? -0.912  -15.576 69.222  1.00 53.51  ? 462 GLU C CB  1 
ATOM   12019 C CG  . GLU C 1 462 ? -0.938  -17.109 69.256  1.00 67.78  ? 462 GLU C CG  1 
ATOM   12020 C CD  . GLU C 1 462 ? -1.022  -17.748 67.879  1.00 76.74  ? 462 GLU C CD  1 
ATOM   12021 O OE1 . GLU C 1 462 ? -0.808  -17.043 66.871  1.00 80.13  ? 462 GLU C OE1 1 
ATOM   12022 O OE2 . GLU C 1 462 ? -1.285  -18.968 67.810  1.00 69.96  ? 462 GLU C OE2 1 
ATOM   12023 N N   . VAL C 1 463 ? 1.359   -15.360 66.948  1.00 46.81  ? 463 VAL C N   1 
ATOM   12024 C CA  . VAL C 1 463 ? 2.176   -16.069 65.968  1.00 40.93  ? 463 VAL C CA  1 
ATOM   12025 C C   . VAL C 1 463 ? 3.657   -15.865 66.259  1.00 33.29  ? 463 VAL C C   1 
ATOM   12026 O O   . VAL C 1 463 ? 4.447   -16.817 66.222  1.00 36.99  ? 463 VAL C O   1 
ATOM   12027 C CB  . VAL C 1 463 ? 1.820   -15.619 64.540  1.00 37.84  ? 463 VAL C CB  1 
ATOM   12028 C CG1 . VAL C 1 463 ? 2.814   -16.204 63.559  1.00 43.00  ? 463 VAL C CG1 1 
ATOM   12029 C CG2 . VAL C 1 463 ? 0.403   -16.030 64.176  1.00 39.82  ? 463 VAL C CG2 1 
ATOM   12030 N N   . PHE C 1 464 ? 4.059   -14.625 66.546  1.00 33.57  ? 464 PHE C N   1 
ATOM   12031 C CA  . PHE C 1 464 ? 5.456   -14.361 66.869  1.00 33.80  ? 464 PHE C CA  1 
ATOM   12032 C C   . PHE C 1 464 ? 5.875   -15.105 68.129  1.00 30.44  ? 464 PHE C C   1 
ATOM   12033 O O   . PHE C 1 464 ? 6.987   -15.641 68.203  1.00 31.46  ? 464 PHE C O   1 
ATOM   12034 C CB  . PHE C 1 464 ? 5.685   -12.858 67.028  1.00 32.71  ? 464 PHE C CB  1 
ATOM   12035 C CG  . PHE C 1 464 ? 6.120   -12.176 65.763  1.00 34.64  ? 464 PHE C CG  1 
ATOM   12036 C CD1 . PHE C 1 464 ? 7.407   -12.343 65.277  1.00 33.48  ? 464 PHE C CD1 1 
ATOM   12037 C CD2 . PHE C 1 464 ? 5.240   -11.374 65.055  1.00 47.83  ? 464 PHE C CD2 1 
ATOM   12038 C CE1 . PHE C 1 464 ? 7.808   -11.720 64.111  1.00 41.94  ? 464 PHE C CE1 1 
ATOM   12039 C CE2 . PHE C 1 464 ? 5.635   -10.748 63.886  1.00 50.75  ? 464 PHE C CE2 1 
ATOM   12040 C CZ  . PHE C 1 464 ? 6.921   -10.922 63.414  1.00 53.57  ? 464 PHE C CZ  1 
ATOM   12041 N N   . ASP C 1 465 ? 4.995   -15.151 69.132  1.00 32.34  ? 465 ASP C N   1 
ATOM   12042 C CA  . ASP C 1 465 ? 5.305   -15.882 70.355  1.00 36.80  ? 465 ASP C CA  1 
ATOM   12043 C C   . ASP C 1 465 ? 5.364   -17.384 70.097  1.00 33.51  ? 465 ASP C C   1 
ATOM   12044 O O   . ASP C 1 465 ? 6.303   -18.059 70.529  1.00 33.59  ? 465 ASP C O   1 
ATOM   12045 C CB  . ASP C 1 465 ? 4.275   -15.555 71.436  1.00 40.60  ? 465 ASP C CB  1 
ATOM   12046 C CG  . ASP C 1 465 ? 4.514   -16.326 72.718  1.00 41.97  ? 465 ASP C CG  1 
ATOM   12047 O OD1 . ASP C 1 465 ? 5.692   -16.519 73.085  1.00 39.91  ? 465 ASP C OD1 1 
ATOM   12048 O OD2 . ASP C 1 465 ? 3.526   -16.731 73.366  1.00 45.18  ? 465 ASP C OD2 1 
ATOM   12049 N N   . LYS C 1 466 ? 4.377   -17.921 69.375  1.00 28.94  ? 466 LYS C N   1 
ATOM   12050 C CA  . LYS C 1 466 ? 4.365   -19.352 69.082  1.00 28.18  ? 466 LYS C CA  1 
ATOM   12051 C C   . LYS C 1 466 ? 5.619   -19.766 68.323  1.00 26.85  ? 466 LYS C C   1 
ATOM   12052 O O   . LYS C 1 466 ? 6.240   -20.791 68.632  1.00 29.63  ? 466 LYS C O   1 
ATOM   12053 C CB  . LYS C 1 466 ? 3.115   -19.714 68.281  1.00 29.99  ? 466 LYS C CB  1 
ATOM   12054 C CG  . LYS C 1 466 ? 3.125   -21.130 67.729  1.00 29.50  ? 466 LYS C CG  1 
ATOM   12055 C CD  . LYS C 1 466 ? 1.852   -21.428 66.956  1.00 31.58  ? 466 LYS C CD  1 
ATOM   12056 C CE  . LYS C 1 466 ? 1.480   -22.898 67.043  1.00 32.32  ? 466 LYS C CE  1 
ATOM   12057 N NZ  . LYS C 1 466 ? 0.008   -23.087 66.930  1.00 33.52  ? 466 LYS C NZ  1 
ATOM   12058 N N   . LEU C 1 467 ? 6.003   -18.974 67.321  1.00 30.26  ? 467 LEU C N   1 
ATOM   12059 C CA  . LEU C 1 467 ? 7.206   -19.270 66.552  1.00 26.61  ? 467 LEU C CA  1 
ATOM   12060 C C   . LEU C 1 467 ? 8.442   -19.266 67.442  1.00 25.15  ? 467 LEU C C   1 
ATOM   12061 O O   . LEU C 1 467 ? 9.255   -20.196 67.397  1.00 31.90  ? 467 LEU C O   1 
ATOM   12062 C CB  . LEU C 1 467 ? 7.351   -18.257 65.416  1.00 27.97  ? 467 LEU C CB  1 
ATOM   12063 C CG  . LEU C 1 467 ? 6.830   -18.680 64.044  1.00 29.50  ? 467 LEU C CG  1 
ATOM   12064 C CD1 . LEU C 1 467 ? 6.703   -17.471 63.136  1.00 31.34  ? 467 LEU C CD1 1 
ATOM   12065 C CD2 . LEU C 1 467 ? 7.746   -19.724 63.421  1.00 28.64  ? 467 LEU C CD2 1 
ATOM   12066 N N   . PHE C 1 468 ? 8.592   -18.229 68.269  1.00 28.39  ? 468 PHE C N   1 
ATOM   12067 C CA  . PHE C 1 468 ? 9.786   -18.113 69.102  1.00 23.44  ? 468 PHE C CA  1 
ATOM   12068 C C   . PHE C 1 468 ? 9.881   -19.251 70.109  1.00 24.28  ? 468 PHE C C   1 
ATOM   12069 O O   . PHE C 1 468 ? 10.971  -19.782 70.351  1.00 27.61  ? 468 PHE C O   1 
ATOM   12070 C CB  . PHE C 1 468 ? 9.803   -16.766 69.822  1.00 23.91  ? 468 PHE C CB  1 
ATOM   12071 C CG  . PHE C 1 468 ? 10.834  -16.683 70.910  1.00 22.78  ? 468 PHE C CG  1 
ATOM   12072 C CD1 . PHE C 1 468 ? 12.174  -16.523 70.600  1.00 22.12  ? 468 PHE C CD1 1 
ATOM   12073 C CD2 . PHE C 1 468 ? 10.468  -16.783 72.240  1.00 28.33  ? 468 PHE C CD2 1 
ATOM   12074 C CE1 . PHE C 1 468 ? 13.126  -16.453 71.598  1.00 21.32  ? 468 PHE C CE1 1 
ATOM   12075 C CE2 . PHE C 1 468 ? 11.416  -16.714 73.242  1.00 21.87  ? 468 PHE C CE2 1 
ATOM   12076 C CZ  . PHE C 1 468 ? 12.746  -16.549 72.920  1.00 21.20  ? 468 PHE C CZ  1 
ATOM   12077 N N   . ARG C 1 469 ? 8.755   -19.630 70.720  1.00 26.62  ? 469 ARG C N   1 
ATOM   12078 C CA  . ARG C 1 469 ? 8.779   -20.726 71.684  1.00 21.97  ? 469 ARG C CA  1 
ATOM   12079 C C   . ARG C 1 469 ? 9.094   -22.054 71.010  1.00 29.58  ? 469 ARG C C   1 
ATOM   12080 O O   . ARG C 1 469 ? 9.768   -22.903 71.606  1.00 37.04  ? 469 ARG C O   1 
ATOM   12081 C CB  . ARG C 1 469 ? 7.446   -20.801 72.430  1.00 22.98  ? 469 ARG C CB  1 
ATOM   12082 C CG  . ARG C 1 469 ? 7.044   -19.485 73.069  1.00 31.77  ? 469 ARG C CG  1 
ATOM   12083 C CD  . ARG C 1 469 ? 7.143   -19.485 74.580  1.00 37.29  ? 469 ARG C CD  1 
ATOM   12084 N NE  . ARG C 1 469 ? 6.525   -18.286 75.135  1.00 39.06  ? 469 ARG C NE  1 
ATOM   12085 C CZ  . ARG C 1 469 ? 6.595   -17.925 76.408  1.00 36.00  ? 469 ARG C CZ  1 
ATOM   12086 N NH1 . ARG C 1 469 ? 7.220   -18.672 77.303  1.00 41.82  ? 469 ARG C NH1 1 
ATOM   12087 N NH2 . ARG C 1 469 ? 6.023   -16.788 76.794  1.00 35.52  ? 469 ARG C NH2 1 
ATOM   12088 N N   . SER C 1 470 ? 8.617   -22.254 69.779  1.00 25.06  ? 470 SER C N   1 
ATOM   12089 C CA  . SER C 1 470 ? 8.977   -23.455 69.032  1.00 21.73  ? 470 SER C CA  1 
ATOM   12090 C C   . SER C 1 470 ? 10.462  -23.467 68.687  1.00 21.28  ? 470 SER C C   1 
ATOM   12091 O O   . SER C 1 470 ? 11.118  -24.510 68.786  1.00 23.97  ? 470 SER C O   1 
ATOM   12092 C CB  . SER C 1 470 ? 8.129   -23.560 67.765  1.00 23.31  ? 470 SER C CB  1 
ATOM   12093 O OG  . SER C 1 470 ? 7.949   -24.911 67.380  1.00 37.93  ? 470 SER C OG  1 
ATOM   12094 N N   . PHE C 1 471 ? 11.010  -22.319 68.277  1.00 24.91  ? 471 PHE C N   1 
ATOM   12095 C CA  . PHE C 1 471 ? 12.441  -22.239 67.995  1.00 23.23  ? 471 PHE C CA  1 
ATOM   12096 C C   . PHE C 1 471 ? 13.263  -22.522 69.246  1.00 29.78  ? 471 PHE C C   1 
ATOM   12097 O O   . PHE C 1 471 ? 14.289  -23.209 69.182  1.00 33.05  ? 471 PHE C O   1 
ATOM   12098 C CB  . PHE C 1 471 ? 12.795  -20.863 67.430  1.00 25.01  ? 471 PHE C CB  1 
ATOM   12099 C CG  . PHE C 1 471 ? 12.276  -20.622 66.041  1.00 24.65  ? 471 PHE C CG  1 
ATOM   12100 C CD1 . PHE C 1 471 ? 12.410  -21.588 65.058  1.00 33.19  ? 471 PHE C CD1 1 
ATOM   12101 C CD2 . PHE C 1 471 ? 11.662  -19.425 65.717  1.00 23.73  ? 471 PHE C CD2 1 
ATOM   12102 C CE1 . PHE C 1 471 ? 11.932  -21.369 63.779  1.00 30.09  ? 471 PHE C CE1 1 
ATOM   12103 C CE2 . PHE C 1 471 ? 11.181  -19.200 64.441  1.00 25.27  ? 471 PHE C CE2 1 
ATOM   12104 C CZ  . PHE C 1 471 ? 11.317  -20.172 63.470  1.00 29.86  ? 471 PHE C CZ  1 
ATOM   12105 N N   . VAL C 1 472 ? 12.834  -21.987 70.390  1.00 27.96  ? 472 VAL C N   1 
ATOM   12106 C CA  . VAL C 1 472 ? 13.498  -22.283 71.657  1.00 25.58  ? 472 VAL C CA  1 
ATOM   12107 C C   . VAL C 1 472 ? 13.400  -23.772 71.968  1.00 26.52  ? 472 VAL C C   1 
ATOM   12108 O O   . VAL C 1 472 ? 14.386  -24.417 72.346  1.00 30.41  ? 472 VAL C O   1 
ATOM   12109 C CB  . VAL C 1 472 ? 12.894  -21.425 72.785  1.00 29.47  ? 472 VAL C CB  1 
ATOM   12110 C CG1 . VAL C 1 472 ? 13.021  -22.124 74.131  1.00 27.06  ? 472 VAL C CG1 1 
ATOM   12111 C CG2 . VAL C 1 472 ? 13.551  -20.056 72.819  1.00 32.67  ? 472 VAL C CG2 1 
ATOM   12112 N N   . ARG C 1 473 ? 12.203  -24.339 71.806  1.00 24.36  ? 473 ARG C N   1 
ATOM   12113 C CA  . ARG C 1 473 ? 11.993  -25.757 72.082  1.00 25.03  ? 473 ARG C CA  1 
ATOM   12114 C C   . ARG C 1 473 ? 12.794  -26.638 71.129  1.00 27.57  ? 473 ARG C C   1 
ATOM   12115 O O   . ARG C 1 473 ? 13.401  -27.630 71.549  1.00 30.45  ? 473 ARG C O   1 
ATOM   12116 C CB  . ARG C 1 473 ? 10.502  -26.074 71.988  1.00 31.06  ? 473 ARG C CB  1 
ATOM   12117 C CG  . ARG C 1 473 ? 10.105  -27.486 72.367  1.00 34.61  ? 473 ARG C CG  1 
ATOM   12118 C CD  . ARG C 1 473 ? 8.627   -27.680 72.082  1.00 39.58  ? 473 ARG C CD  1 
ATOM   12119 N NE  . ARG C 1 473 ? 7.897   -26.430 72.269  1.00 63.60  ? 473 ARG C NE  1 
ATOM   12120 C CZ  . ARG C 1 473 ? 6.905   -26.013 71.495  1.00 70.32  ? 473 ARG C CZ  1 
ATOM   12121 N NH1 . ARG C 1 473 ? 6.479   -26.733 70.468  1.00 57.15  ? 473 ARG C NH1 1 
ATOM   12122 N NH2 . ARG C 1 473 ? 6.329   -24.840 71.753  1.00 50.05  ? 473 ARG C NH2 1 
ATOM   12123 N N   . ARG C 1 474 ? 12.808  -26.290 69.841  1.00 23.59  ? 474 ARG C N   1 
ATOM   12124 C CA  . ARG C 1 474 ? 13.486  -27.121 68.850  1.00 24.73  ? 474 ARG C CA  1 
ATOM   12125 C C   . ARG C 1 474 ? 15.001  -27.084 69.010  1.00 30.23  ? 474 ARG C C   1 
ATOM   12126 O O   . ARG C 1 474 ? 15.676  -28.085 68.741  1.00 30.83  ? 474 ARG C O   1 
ATOM   12127 C CB  . ARG C 1 474 ? 13.084  -26.680 67.442  1.00 33.62  ? 474 ARG C CB  1 
ATOM   12128 C CG  . ARG C 1 474 ? 13.723  -27.476 66.319  1.00 35.30  ? 474 ARG C CG  1 
ATOM   12129 C CD  . ARG C 1 474 ? 13.311  -28.940 66.352  1.00 28.36  ? 474 ARG C CD  1 
ATOM   12130 N NE  . ARG C 1 474 ? 13.473  -29.576 65.049  1.00 35.59  ? 474 ARG C NE  1 
ATOM   12131 C CZ  . ARG C 1 474 ? 14.641  -29.859 64.486  1.00 37.95  ? 474 ARG C CZ  1 
ATOM   12132 N NH1 . ARG C 1 474 ? 15.787  -29.596 65.095  1.00 28.52  ? 474 ARG C NH1 1 
ATOM   12133 N NH2 . ARG C 1 474 ? 14.660  -30.420 63.279  1.00 37.36  ? 474 ARG C NH2 1 
ATOM   12134 N N   . ALA C 1 475 ? 15.554  -25.948 69.443  1.00 34.58  ? 475 ALA C N   1 
ATOM   12135 C CA  . ALA C 1 475 ? 16.999  -25.835 69.608  1.00 28.08  ? 475 ALA C CA  1 
ATOM   12136 C C   . ALA C 1 475 ? 17.532  -26.732 70.716  1.00 26.88  ? 475 ALA C C   1 
ATOM   12137 O O   . ALA C 1 475 ? 18.741  -26.985 70.765  1.00 22.39  ? 475 ALA C O   1 
ATOM   12138 C CB  . ALA C 1 475 ? 17.387  -24.383 69.891  1.00 23.30  ? 475 ALA C CB  1 
ATOM   12139 N N   . GLN C 1 476 ? 16.664  -27.212 71.603  1.00 30.14  ? 476 GLN C N   1 
ATOM   12140 C CA  . GLN C 1 476 ? 17.057  -28.099 72.689  1.00 26.31  ? 476 GLN C CA  1 
ATOM   12141 C C   . GLN C 1 476 ? 16.998  -29.572 72.301  1.00 21.31  ? 476 GLN C C   1 
ATOM   12142 O O   . GLN C 1 476 ? 17.357  -30.427 73.118  1.00 17.41  ? 476 GLN C O   1 
ATOM   12143 C CB  . GLN C 1 476 ? 16.168  -27.853 73.911  1.00 20.89  ? 476 GLN C CB  1 
ATOM   12144 C CG  . GLN C 1 476 ? 16.534  -26.612 74.708  1.00 17.00  ? 476 GLN C CG  1 
ATOM   12145 C CD  . GLN C 1 476 ? 16.683  -26.901 76.188  1.00 42.73  ? 476 GLN C CD  1 
ATOM   12146 O OE1 . GLN C 1 476 ? 17.106  -27.989 76.580  1.00 58.86  ? 476 GLN C OE1 1 
ATOM   12147 N NE2 . GLN C 1 476 ? 16.337  -25.926 77.021  1.00 46.47  ? 476 GLN C NE2 1 
ATOM   12148 N N   . GLU C 1 477 ? 16.553  -29.886 71.088  1.00 26.68  ? 477 GLU C N   1 
ATOM   12149 C CA  . GLU C 1 477 ? 16.458  -31.267 70.640  1.00 26.73  ? 477 GLU C CA  1 
ATOM   12150 C C   . GLU C 1 477 ? 17.817  -31.781 70.181  1.00 30.90  ? 477 GLU C C   1 
ATOM   12151 O O   . GLU C 1 477 ? 18.672  -31.021 69.718  1.00 36.18  ? 477 GLU C O   1 
ATOM   12152 C CB  . GLU C 1 477 ? 15.444  -31.394 69.502  1.00 25.90  ? 477 GLU C CB  1 
ATOM   12153 C CG  . GLU C 1 477 ? 14.080  -30.793 69.811  1.00 38.20  ? 477 GLU C CG  1 
ATOM   12154 C CD  . GLU C 1 477 ? 13.134  -31.786 70.460  1.00 49.11  ? 477 GLU C CD  1 
ATOM   12155 O OE1 . GLU C 1 477 ? 12.991  -32.903 69.920  1.00 61.17  ? 477 GLU C OE1 1 
ATOM   12156 O OE2 . GLU C 1 477 ? 12.530  -31.450 71.503  1.00 41.88  ? 477 GLU C OE2 1 
ATOM   12157 N N   . LEU C 1 478 ? 18.003  -33.090 70.305  1.00 29.26  ? 478 LEU C N   1 
ATOM   12158 C CA  . LEU C 1 478 ? 19.257  -33.718 69.926  1.00 21.79  ? 478 LEU C CA  1 
ATOM   12159 C C   . LEU C 1 478 ? 19.368  -33.832 68.407  1.00 24.30  ? 478 LEU C C   1 
ATOM   12160 O O   . LEU C 1 478 ? 18.374  -33.804 67.676  1.00 24.57  ? 478 LEU C O   1 
ATOM   12161 C CB  . LEU C 1 478 ? 19.387  -35.095 70.578  1.00 27.89  ? 478 LEU C CB  1 
ATOM   12162 C CG  . LEU C 1 478 ? 19.932  -35.122 72.009  1.00 30.89  ? 478 LEU C CG  1 
ATOM   12163 C CD1 . LEU C 1 478 ? 18.966  -34.480 72.998  1.00 35.36  ? 478 LEU C CD1 1 
ATOM   12164 C CD2 . LEU C 1 478 ? 20.249  -36.542 72.427  1.00 30.72  ? 478 LEU C CD2 1 
ATOM   12165 N N   . GLU C 1 479 ? 20.607  -33.979 67.940  1.00 26.03  ? 479 GLU C N   1 
ATOM   12166 C CA  . GLU C 1 479 ? 20.925  -33.898 66.520  1.00 31.96  ? 479 GLU C CA  1 
ATOM   12167 C C   . GLU C 1 479 ? 20.546  -35.146 65.733  1.00 36.08  ? 479 GLU C C   1 
ATOM   12168 O O   . GLU C 1 479 ? 20.640  -35.129 64.500  1.00 38.48  ? 479 GLU C O   1 
ATOM   12169 C CB  . GLU C 1 479 ? 22.421  -33.615 66.350  1.00 36.41  ? 479 GLU C CB  1 
ATOM   12170 C CG  . GLU C 1 479 ? 22.798  -32.922 65.051  1.00 45.66  ? 479 GLU C CG  1 
ATOM   12171 C CD  . GLU C 1 479 ? 23.755  -33.745 64.208  1.00 45.48  ? 479 GLU C CD  1 
ATOM   12172 O OE1 . GLU C 1 479 ? 24.318  -34.732 64.733  1.00 55.38  ? 479 GLU C OE1 1 
ATOM   12173 O OE2 . GLU C 1 479 ? 23.958  -33.397 63.026  1.00 37.85  ? 479 GLU C OE2 1 
ATOM   12174 N N   . HIS C 1 480 ? 20.120  -36.219 66.395  1.00 37.75  ? 480 HIS C N   1 
ATOM   12175 C CA  . HIS C 1 480 ? 19.842  -37.472 65.708  1.00 26.43  ? 480 HIS C CA  1 
ATOM   12176 C C   . HIS C 1 480 ? 18.609  -38.135 66.301  1.00 23.59  ? 480 HIS C C   1 
ATOM   12177 O O   . HIS C 1 480 ? 18.310  -37.983 67.489  1.00 29.24  ? 480 HIS C O   1 
ATOM   12178 C CB  . HIS C 1 480 ? 21.037  -38.428 65.795  1.00 25.29  ? 480 HIS C CB  1 
ATOM   12179 C CG  . HIS C 1 480 ? 22.145  -38.091 64.849  1.00 30.60  ? 480 HIS C CG  1 
ATOM   12180 N ND1 . HIS C 1 480 ? 21.934  -37.863 63.506  1.00 42.81  ? 480 HIS C ND1 1 
ATOM   12181 C CD2 . HIS C 1 480 ? 23.472  -37.917 65.056  1.00 32.75  ? 480 HIS C CD2 1 
ATOM   12182 C CE1 . HIS C 1 480 ? 23.085  -37.576 62.925  1.00 37.92  ? 480 HIS C CE1 1 
ATOM   12183 N NE2 . HIS C 1 480 ? 24.035  -37.606 63.842  1.00 37.23  ? 480 HIS C NE2 1 
ATOM   12184 N N   . HIS C 1 481 ? 17.895  -38.872 65.454  1.00 24.47  ? 481 HIS C N   1 
ATOM   12185 C CA  . HIS C 1 481 ? 16.810  -39.719 65.926  1.00 28.12  ? 481 HIS C CA  1 
ATOM   12186 C C   . HIS C 1 481 ? 17.379  -40.772 66.865  1.00 32.44  ? 481 HIS C C   1 
ATOM   12187 O O   . HIS C 1 481 ? 18.266  -41.542 66.482  1.00 35.74  ? 481 HIS C O   1 
ATOM   12188 C CB  . HIS C 1 481 ? 16.100  -40.379 64.742  1.00 25.64  ? 481 HIS C CB  1 
ATOM   12189 C CG  . HIS C 1 481 ? 15.409  -39.413 63.830  1.00 34.33  ? 481 HIS C CG  1 
ATOM   12190 N ND1 . HIS C 1 481 ? 16.046  -38.799 62.773  1.00 40.98  ? 481 HIS C ND1 1 
ATOM   12191 C CD2 . HIS C 1 481 ? 14.134  -38.956 63.817  1.00 38.83  ? 481 HIS C CD2 1 
ATOM   12192 C CE1 . HIS C 1 481 ? 15.194  -38.005 62.148  1.00 49.03  ? 481 HIS C CE1 1 
ATOM   12193 N NE2 . HIS C 1 481 ? 14.027  -38.081 62.763  1.00 44.48  ? 481 HIS C NE2 1 
ATOM   12194 N N   . HIS C 1 482 ? 16.881  -40.799 68.099  1.00 26.44  ? 482 HIS C N   1 
ATOM   12195 C CA  . HIS C 1 482 ? 17.472  -41.631 69.134  1.00 30.03  ? 482 HIS C CA  1 
ATOM   12196 C C   . HIS C 1 482 ? 16.392  -42.188 70.048  1.00 23.78  ? 482 HIS C C   1 
ATOM   12197 O O   . HIS C 1 482 ? 15.345  -41.570 70.255  1.00 29.95  ? 482 HIS C O   1 
ATOM   12198 C CB  . HIS C 1 482 ? 18.489  -40.840 69.970  1.00 27.16  ? 482 HIS C CB  1 
ATOM   12199 C CG  . HIS C 1 482 ? 17.873  -39.754 70.797  1.00 25.06  ? 482 HIS C CG  1 
ATOM   12200 N ND1 . HIS C 1 482 ? 17.567  -38.508 70.290  1.00 25.57  ? 482 HIS C ND1 1 
ATOM   12201 C CD2 . HIS C 1 482 ? 17.483  -39.737 72.093  1.00 21.71  ? 482 HIS C CD2 1 
ATOM   12202 C CE1 . HIS C 1 482 ? 17.030  -37.767 71.243  1.00 32.46  ? 482 HIS C CE1 1 
ATOM   12203 N NE2 . HIS C 1 482 ? 16.967  -38.490 72.347  1.00 31.76  ? 482 HIS C NE2 1 
ATOM   12204 N N   . HIS C 1 483 ? 16.670  -43.365 70.596  1.00 24.65  ? 483 HIS C N   1 
ATOM   12205 C CA  . HIS C 1 483 ? 15.928  -43.950 71.702  1.00 24.74  ? 483 HIS C CA  1 
ATOM   12206 C C   . HIS C 1 483 ? 16.894  -44.190 72.853  1.00 25.04  ? 483 HIS C C   1 
ATOM   12207 O O   . HIS C 1 483 ? 18.104  -43.992 72.729  1.00 25.26  ? 483 HIS C O   1 
ATOM   12208 C CB  . HIS C 1 483 ? 15.247  -45.258 71.291  1.00 30.45  ? 483 HIS C CB  1 
ATOM   12209 C CG  . HIS C 1 483 ? 16.207  -46.346 70.928  1.00 27.23  ? 483 HIS C CG  1 
ATOM   12210 N ND1 . HIS C 1 483 ? 16.450  -47.435 71.738  1.00 28.39  ? 483 HIS C ND1 1 
ATOM   12211 C CD2 . HIS C 1 483 ? 17.002  -46.503 69.842  1.00 30.45  ? 483 HIS C CD2 1 
ATOM   12212 C CE1 . HIS C 1 483 ? 17.339  -48.224 71.162  1.00 38.56  ? 483 HIS C CE1 1 
ATOM   12213 N NE2 . HIS C 1 483 ? 17.692  -47.680 70.011  1.00 32.18  ? 483 HIS C NE2 1 
ATOM   12214 N N   . HIS C 1 484 ? 16.353  -44.617 73.986  1.00 25.29  ? 484 HIS C N   1 
ATOM   12215 C CA  . HIS C 1 484 ? 17.197  -44.948 75.122  1.00 25.96  ? 484 HIS C CA  1 
ATOM   12216 C C   . HIS C 1 484 ? 17.859  -46.305 74.910  1.00 27.52  ? 484 HIS C C   1 
ATOM   12217 O O   . HIS C 1 484 ? 17.682  -47.226 75.703  1.00 28.59  ? 484 HIS C O   1 
ATOM   12218 C CB  . HIS C 1 484 ? 16.387  -44.941 76.415  1.00 26.03  ? 484 HIS C CB  1 
ATOM   12219 C CG  . HIS C 1 484 ? 16.934  -44.020 77.457  1.00 25.65  ? 484 HIS C CG  1 
ATOM   12220 N ND1 . HIS C 1 484 ? 17.023  -42.657 77.271  1.00 24.40  ? 484 HIS C ND1 1 
ATOM   12221 C CD2 . HIS C 1 484 ? 17.435  -44.266 78.690  1.00 26.58  ? 484 HIS C CD2 1 
ATOM   12222 C CE1 . HIS C 1 484 ? 17.548  -42.103 78.349  1.00 24.52  ? 484 HIS C CE1 1 
ATOM   12223 N NE2 . HIS C 1 484 ? 17.807  -43.057 79.225  1.00 25.88  ? 484 HIS C NE2 1 
ATOM   12224 N N   . MET D 1 1   ? -27.953 14.651  58.202  1.00 100.46 ? 1   MET D N   1 
ATOM   12225 C CA  . MET D 1 1   ? -26.587 14.582  58.707  1.00 91.95  ? 1   MET D CA  1 
ATOM   12226 C C   . MET D 1 1   ? -26.410 15.514  59.903  1.00 83.95  ? 1   MET D C   1 
ATOM   12227 O O   . MET D 1 1   ? -26.894 16.645  59.901  1.00 86.87  ? 1   MET D O   1 
ATOM   12228 C CB  . MET D 1 1   ? -25.592 14.931  57.601  1.00 99.77  ? 1   MET D CB  1 
ATOM   12229 C CG  . MET D 1 1   ? -24.152 15.040  58.061  1.00 99.08  ? 1   MET D CG  1 
ATOM   12230 S SD  . MET D 1 1   ? -23.084 15.493  56.691  1.00 115.97 ? 1   MET D SD  1 
ATOM   12231 C CE  . MET D 1 1   ? -23.429 17.247  56.640  1.00 89.02  ? 1   MET D CE  1 
ATOM   12232 N N   . LYS D 1 2   ? -25.711 15.024  60.924  1.00 87.63  ? 2   LYS D N   1 
ATOM   12233 C CA  . LYS D 1 2   ? -25.527 15.763  62.167  1.00 82.28  ? 2   LYS D CA  1 
ATOM   12234 C C   . LYS D 1 2   ? -24.422 16.799  61.990  1.00 86.86  ? 2   LYS D C   1 
ATOM   12235 O O   . LYS D 1 2   ? -23.291 16.449  61.633  1.00 85.76  ? 2   LYS D O   1 
ATOM   12236 C CB  . LYS D 1 2   ? -25.190 14.789  63.296  1.00 83.27  ? 2   LYS D CB  1 
ATOM   12237 C CG  . LYS D 1 2   ? -25.543 15.270  64.693  1.00 75.16  ? 2   LYS D CG  1 
ATOM   12238 C CD  . LYS D 1 2   ? -26.754 16.178  64.674  1.00 88.21  ? 2   LYS D CD  1 
ATOM   12239 C CE  . LYS D 1 2   ? -28.047 15.399  64.857  1.00 86.39  ? 2   LYS D CE  1 
ATOM   12240 N NZ  . LYS D 1 2   ? -29.244 16.280  64.765  1.00 99.09  ? 2   LYS D NZ  1 
ATOM   12241 N N   . LYS D 1 3   ? -24.739 18.069  62.239  1.00 88.29  ? 3   LYS D N   1 
ATOM   12242 C CA  . LYS D 1 3   ? -23.790 19.162  62.055  1.00 83.18  ? 3   LYS D CA  1 
ATOM   12243 C C   . LYS D 1 3   ? -23.386 19.733  63.408  1.00 71.86  ? 3   LYS D C   1 
ATOM   12244 O O   . LYS D 1 3   ? -24.238 19.947  64.276  1.00 80.26  ? 3   LYS D O   1 
ATOM   12245 C CB  . LYS D 1 3   ? -24.368 20.279  61.173  1.00 85.26  ? 3   LYS D CB  1 
ATOM   12246 C CG  . LYS D 1 3   ? -25.417 19.833  60.151  1.00 99.46  ? 3   LYS D CG  1 
ATOM   12247 C CD  . LYS D 1 3   ? -26.786 20.390  60.495  1.00 94.37  ? 3   LYS D CD  1 
ATOM   12248 C CE  . LYS D 1 3   ? -27.846 20.083  59.451  1.00 99.12  ? 3   LYS D CE  1 
ATOM   12249 N NZ  . LYS D 1 3   ? -29.204 20.288  60.026  1.00 89.27  ? 3   LYS D NZ  1 
ATOM   12250 N N   . LEU D 1 4   ? -22.087 19.963  63.583  1.00 77.34  ? 4   LEU D N   1 
ATOM   12251 C CA  . LEU D 1 4   ? -21.558 20.652  64.757  1.00 74.53  ? 4   LEU D CA  1 
ATOM   12252 C C   . LEU D 1 4   ? -21.528 22.142  64.445  1.00 74.86  ? 4   LEU D C   1 
ATOM   12253 O O   . LEU D 1 4   ? -20.634 22.627  63.746  1.00 76.37  ? 4   LEU D O   1 
ATOM   12254 C CB  . LEU D 1 4   ? -20.171 20.136  65.119  1.00 76.98  ? 4   LEU D CB  1 
ATOM   12255 C CG  . LEU D 1 4   ? -19.552 20.823  66.339  1.00 73.22  ? 4   LEU D CG  1 
ATOM   12256 C CD1 . LEU D 1 4   ? -19.108 19.802  67.377  1.00 67.46  ? 4   LEU D CD1 1 
ATOM   12257 C CD2 . LEU D 1 4   ? -18.397 21.724  65.930  1.00 69.32  ? 4   LEU D CD2 1 
ATOM   12258 N N   . PHE D 1 5   ? -22.510 22.871  64.963  1.00 68.87  ? 5   PHE D N   1 
ATOM   12259 C CA  . PHE D 1 5   ? -22.578 24.307  64.740  1.00 68.27  ? 5   PHE D CA  1 
ATOM   12260 C C   . PHE D 1 5   ? -21.480 25.003  65.535  1.00 66.76  ? 5   PHE D C   1 
ATOM   12261 O O   . PHE D 1 5   ? -21.400 24.858  66.760  1.00 74.51  ? 5   PHE D O   1 
ATOM   12262 C CB  . PHE D 1 5   ? -23.958 24.828  65.129  1.00 74.58  ? 5   PHE D CB  1 
ATOM   12263 C CG  . PHE D 1 5   ? -25.076 24.247  64.307  1.00 79.91  ? 5   PHE D CG  1 
ATOM   12264 C CD1 . PHE D 1 5   ? -24.897 23.981  62.960  1.00 73.46  ? 5   PHE D CD1 1 
ATOM   12265 C CD2 . PHE D 1 5   ? -26.304 23.964  64.884  1.00 82.45  ? 5   PHE D CD2 1 
ATOM   12266 C CE1 . PHE D 1 5   ? -25.922 23.446  62.202  1.00 78.21  ? 5   PHE D CE1 1 
ATOM   12267 C CE2 . PHE D 1 5   ? -27.332 23.429  64.131  1.00 75.15  ? 5   PHE D CE2 1 
ATOM   12268 C CZ  . PHE D 1 5   ? -27.141 23.169  62.789  1.00 86.61  ? 5   PHE D CZ  1 
ATOM   12269 N N   . LEU D 1 6   ? -20.631 25.750  64.836  1.00 64.60  ? 6   LEU D N   1 
ATOM   12270 C CA  . LEU D 1 6   ? -19.459 26.385  65.419  1.00 63.74  ? 6   LEU D CA  1 
ATOM   12271 C C   . LEU D 1 6   ? -19.596 27.898  65.337  1.00 60.58  ? 6   LEU D C   1 
ATOM   12272 O O   . LEU D 1 6   ? -20.033 28.436  64.316  1.00 61.22  ? 6   LEU D O   1 
ATOM   12273 C CB  . LEU D 1 6   ? -18.185 25.927  64.699  1.00 72.42  ? 6   LEU D CB  1 
ATOM   12274 C CG  . LEU D 1 6   ? -16.862 26.070  65.450  1.00 64.38  ? 6   LEU D CG  1 
ATOM   12275 C CD1 . LEU D 1 6   ? -16.995 25.553  66.859  1.00 68.86  ? 6   LEU D CD1 1 
ATOM   12276 C CD2 . LEU D 1 6   ? -15.751 25.336  64.718  1.00 75.00  ? 6   LEU D CD2 1 
ATOM   12277 N N   . VAL D 1 7   ? -19.244 28.586  66.423  1.00 66.19  ? 7   VAL D N   1 
ATOM   12278 C CA  . VAL D 1 7   ? -19.305 30.042  66.479  1.00 68.08  ? 7   VAL D CA  1 
ATOM   12279 C C   . VAL D 1 7   ? -17.978 30.570  67.010  1.00 62.66  ? 7   VAL D C   1 
ATOM   12280 O O   . VAL D 1 7   ? -17.509 30.134  68.067  1.00 65.16  ? 7   VAL D O   1 
ATOM   12281 C CB  . VAL D 1 7   ? -20.470 30.542  67.356  1.00 62.02  ? 7   VAL D CB  1 
ATOM   12282 C CG1 . VAL D 1 7   ? -20.684 32.031  67.137  1.00 58.33  ? 7   VAL D CG1 1 
ATOM   12283 C CG2 . VAL D 1 7   ? -21.749 29.773  67.054  1.00 55.68  ? 7   VAL D CG2 1 
ATOM   12284 N N   . PHE D 1 8   ? -17.385 31.511  66.281  1.00 56.81  ? 8   PHE D N   1 
ATOM   12285 C CA  . PHE D 1 8   ? -16.159 32.185  66.685  1.00 56.61  ? 8   PHE D CA  1 
ATOM   12286 C C   . PHE D 1 8   ? -16.471 33.629  67.049  1.00 55.87  ? 8   PHE D C   1 
ATOM   12287 O O   . PHE D 1 8   ? -17.209 34.311  66.333  1.00 54.37  ? 8   PHE D O   1 
ATOM   12288 C CB  . PHE D 1 8   ? -15.109 32.151  65.571  1.00 59.63  ? 8   PHE D CB  1 
ATOM   12289 C CG  . PHE D 1 8   ? -14.402 30.835  65.440  1.00 62.20  ? 8   PHE D CG  1 
ATOM   12290 C CD1 . PHE D 1 8   ? -15.029 29.755  64.843  1.00 72.29  ? 8   PHE D CD1 1 
ATOM   12291 C CD2 . PHE D 1 8   ? -13.110 30.676  65.916  1.00 61.16  ? 8   PHE D CD2 1 
ATOM   12292 C CE1 . PHE D 1 8   ? -14.381 28.542  64.721  1.00 81.36  ? 8   PHE D CE1 1 
ATOM   12293 C CE2 . PHE D 1 8   ? -12.457 29.463  65.799  1.00 66.46  ? 8   PHE D CE2 1 
ATOM   12294 C CZ  . PHE D 1 8   ? -13.094 28.394  65.200  1.00 75.52  ? 8   PHE D CZ  1 
ATOM   12295 N N   . TRP D 1 9   ? -15.903 34.094  68.161  1.00 56.26  ? 9   TRP D N   1 
ATOM   12296 C CA  . TRP D 1 9   ? -16.149 35.450  68.654  1.00 57.41  ? 9   TRP D CA  1 
ATOM   12297 C C   . TRP D 1 9   ? -14.841 36.001  69.214  1.00 50.74  ? 9   TRP D C   1 
ATOM   12298 O O   . TRP D 1 9   ? -14.452 35.666  70.336  1.00 55.42  ? 9   TRP D O   1 
ATOM   12299 C CB  . TRP D 1 9   ? -17.249 35.454  69.709  1.00 60.00  ? 9   TRP D CB  1 
ATOM   12300 C CG  . TRP D 1 9   ? -17.981 36.756  69.834  1.00 52.02  ? 9   TRP D CG  1 
ATOM   12301 C CD1 . TRP D 1 9   ? -17.612 37.961  69.312  1.00 47.60  ? 9   TRP D CD1 1 
ATOM   12302 C CD2 . TRP D 1 9   ? -19.209 36.980  70.535  1.00 46.37  ? 9   TRP D CD2 1 
ATOM   12303 N NE1 . TRP D 1 9   ? -18.538 38.922  69.643  1.00 46.05  ? 9   TRP D NE1 1 
ATOM   12304 C CE2 . TRP D 1 9   ? -19.528 38.344  70.394  1.00 45.12  ? 9   TRP D CE2 1 
ATOM   12305 C CE3 . TRP D 1 9   ? -20.070 36.159  71.267  1.00 46.03  ? 9   TRP D CE3 1 
ATOM   12306 C CZ2 . TRP D 1 9   ? -20.671 38.904  70.958  1.00 43.57  ? 9   TRP D CZ2 1 
ATOM   12307 C CZ3 . TRP D 1 9   ? -21.203 36.717  71.825  1.00 44.90  ? 9   TRP D CZ3 1 
ATOM   12308 C CH2 . TRP D 1 9   ? -21.494 38.076  71.668  1.00 43.03  ? 9   TRP D CH2 1 
ATOM   12309 N N   . TRP D 1 10  ? -14.165 36.841  68.436  1.00 51.43  ? 10  TRP D N   1 
ATOM   12310 C CA  . TRP D 1 10  ? -12.961 37.516  68.901  1.00 54.55  ? 10  TRP D CA  1 
ATOM   12311 C C   . TRP D 1 10  ? -13.347 38.872  69.486  1.00 55.11  ? 10  TRP D C   1 
ATOM   12312 O O   . TRP D 1 10  ? -14.100 39.627  68.868  1.00 53.47  ? 10  TRP D O   1 
ATOM   12313 C CB  . TRP D 1 10  ? -11.959 37.690  67.757  1.00 53.06  ? 10  TRP D CB  1 
ATOM   12314 C CG  . TRP D 1 10  ? -11.625 36.415  67.028  1.00 61.82  ? 10  TRP D CG  1 
ATOM   12315 C CD1 . TRP D 1 10  ? -12.062 36.040  65.789  1.00 61.19  ? 10  TRP D CD1 1 
ATOM   12316 C CD2 . TRP D 1 10  ? -10.778 35.353  67.490  1.00 56.00  ? 10  TRP D CD2 1 
ATOM   12317 N NE1 . TRP D 1 10  ? -11.542 34.814  65.454  1.00 63.86  ? 10  TRP D NE1 1 
ATOM   12318 C CE2 . TRP D 1 10  ? -10.751 34.370  66.481  1.00 58.06  ? 10  TRP D CE2 1 
ATOM   12319 C CE3 . TRP D 1 10  ? -10.045 35.136  68.660  1.00 55.31  ? 10  TRP D CE3 1 
ATOM   12320 C CZ2 . TRP D 1 10  ? -10.018 33.192  66.606  1.00 59.42  ? 10  TRP D CZ2 1 
ATOM   12321 C CZ3 . TRP D 1 10  ? -9.314  33.967  68.780  1.00 56.69  ? 10  TRP D CZ3 1 
ATOM   12322 C CH2 . TRP D 1 10  ? -9.309  33.009  67.760  1.00 58.71  ? 10  TRP D CH2 1 
ATOM   12323 N N   . HIS D 1 11  ? -12.838 39.172  70.676  1.00 53.49  ? 11  HIS D N   1 
ATOM   12324 C CA  . HIS D 1 11  ? -13.148 40.400  71.398  1.00 46.12  ? 11  HIS D CA  1 
ATOM   12325 C C   . HIS D 1 11  ? -11.958 41.345  71.316  1.00 46.43  ? 11  HIS D C   1 
ATOM   12326 O O   . HIS D 1 11  ? -10.842 40.968  71.673  1.00 49.75  ? 11  HIS D O   1 
ATOM   12327 C CB  . HIS D 1 11  ? -13.495 40.082  72.853  1.00 48.79  ? 11  HIS D CB  1 
ATOM   12328 C CG  . HIS D 1 11  ? -13.631 41.288  73.723  1.00 44.62  ? 11  HIS D CG  1 
ATOM   12329 N ND1 . HIS D 1 11  ? -14.713 42.135  73.649  1.00 48.38  ? 11  HIS D ND1 1 
ATOM   12330 C CD2 . HIS D 1 11  ? -12.824 41.790  74.688  1.00 43.53  ? 11  HIS D CD2 1 
ATOM   12331 C CE1 . HIS D 1 11  ? -14.566 43.113  74.524  1.00 46.43  ? 11  HIS D CE1 1 
ATOM   12332 N NE2 . HIS D 1 11  ? -13.427 42.927  75.168  1.00 48.72  ? 11  HIS D NE2 1 
ATOM   12333 N N   . MET D 1 12  ? -12.189 42.571  70.856  1.00 46.04  ? 12  MET D N   1 
ATOM   12334 C CA  . MET D 1 12  ? -11.107 43.525  70.638  1.00 55.74  ? 12  MET D CA  1 
ATOM   12335 C C   . MET D 1 12  ? -11.429 44.760  71.473  1.00 50.50  ? 12  MET D C   1 
ATOM   12336 O O   . MET D 1 12  ? -12.533 45.304  71.365  1.00 43.73  ? 12  MET D O   1 
ATOM   12337 C CB  . MET D 1 12  ? -11.050 43.855  69.142  1.00 56.64  ? 12  MET D CB  1 
ATOM   12338 C CG  . MET D 1 12  ? -10.990 42.594  68.296  1.00 49.88  ? 12  MET D CG  1 
ATOM   12339 S SD  . MET D 1 12  ? -9.566  41.535  68.079  1.00 80.27  ? 12  MET D SD  1 
ATOM   12340 C CE  . MET D 1 12  ? -8.285  42.725  67.769  1.00 69.70  ? 12  MET D CE  1 
ATOM   12341 N N   . HIS D 1 13  ? -10.495 45.179  72.324  1.00 53.79  ? 13  HIS D N   1 
ATOM   12342 C CA  . HIS D 1 13  ? -10.765 46.257  73.265  1.00 46.28  ? 13  HIS D CA  1 
ATOM   12343 C C   . HIS D 1 13  ? -9.455  46.848  73.770  1.00 48.10  ? 13  HIS D C   1 
ATOM   12344 O O   . HIS D 1 13  ? -8.501  46.112  74.031  1.00 59.45  ? 13  HIS D O   1 
ATOM   12345 C CB  . HIS D 1 13  ? -11.599 45.755  74.452  1.00 40.86  ? 13  HIS D CB  1 
ATOM   12346 C CG  . HIS D 1 13  ? -11.468 46.599  75.681  1.00 39.32  ? 13  HIS D CG  1 
ATOM   12347 N ND1 . HIS D 1 13  ? -11.847 47.923  75.720  1.00 38.38  ? 13  HIS D ND1 1 
ATOM   12348 C CD2 . HIS D 1 13  ? -10.989 46.309  76.914  1.00 38.65  ? 13  HIS D CD2 1 
ATOM   12349 C CE1 . HIS D 1 13  ? -11.615 48.411  76.926  1.00 37.19  ? 13  HIS D CE1 1 
ATOM   12350 N NE2 . HIS D 1 13  ? -11.095 47.451  77.669  1.00 37.32  ? 13  HIS D NE2 1 
ATOM   12351 N N   . GLN D 1 14  ? -9.419  48.180  73.903  1.00 42.02  ? 14  GLN D N   1 
ATOM   12352 C CA  . GLN D 1 14  ? -8.333  48.884  74.575  1.00 41.97  ? 14  GLN D CA  1 
ATOM   12353 C C   . GLN D 1 14  ? -8.928  49.921  75.516  1.00 47.01  ? 14  GLN D C   1 
ATOM   12354 O O   . GLN D 1 14  ? -9.866  50.642  75.131  1.00 51.83  ? 14  GLN D O   1 
ATOM   12355 C CB  . GLN D 1 14  ? -7.386  49.586  73.596  1.00 44.69  ? 14  GLN D CB  1 
ATOM   12356 C CG  . GLN D 1 14  ? -6.615  48.667  72.714  1.00 61.48  ? 14  GLN D CG  1 
ATOM   12357 C CD  . GLN D 1 14  ? -5.347  48.143  73.343  1.00 62.65  ? 14  GLN D CD  1 
ATOM   12358 O OE1 . GLN D 1 14  ? -4.435  48.905  73.645  1.00 62.41  ? 14  GLN D OE1 1 
ATOM   12359 N NE2 . GLN D 1 14  ? -5.277  46.831  73.535  1.00 58.81  ? 14  GLN D NE2 1 
ATOM   12360 N N   . PRO D 1 15  ? -8.414  50.045  76.735  1.00 39.35  ? 15  PRO D N   1 
ATOM   12361 C CA  . PRO D 1 15  ? -8.804  51.168  77.592  1.00 37.81  ? 15  PRO D CA  1 
ATOM   12362 C C   . PRO D 1 15  ? -8.311  52.484  77.008  1.00 41.91  ? 15  PRO D C   1 
ATOM   12363 O O   . PRO D 1 15  ? -7.506  52.528  76.075  1.00 45.54  ? 15  PRO D O   1 
ATOM   12364 C CB  . PRO D 1 15  ? -8.128  50.847  78.927  1.00 37.34  ? 15  PRO D CB  1 
ATOM   12365 C CG  . PRO D 1 15  ? -6.953  50.016  78.546  1.00 39.05  ? 15  PRO D CG  1 
ATOM   12366 C CD  . PRO D 1 15  ? -7.417  49.180  77.385  1.00 40.63  ? 15  PRO D CD  1 
ATOM   12367 N N   . LEU D 1 16  ? -8.814  53.576  77.577  1.00 46.99  ? 16  LEU D N   1 
ATOM   12368 C CA  . LEU D 1 16  ? -8.543  54.911  77.049  1.00 40.50  ? 16  LEU D CA  1 
ATOM   12369 C C   . LEU D 1 16  ? -7.166  55.372  77.514  1.00 38.86  ? 16  LEU D C   1 
ATOM   12370 O O   . LEU D 1 16  ? -7.000  55.837  78.643  1.00 37.23  ? 16  LEU D O   1 
ATOM   12371 C CB  . LEU D 1 16  ? -9.627  55.888  77.486  1.00 35.90  ? 16  LEU D CB  1 
ATOM   12372 C CG  . LEU D 1 16  ? -9.836  57.075  76.548  1.00 36.38  ? 16  LEU D CG  1 
ATOM   12373 C CD1 . LEU D 1 16  ? -10.141 56.595  75.136  1.00 38.02  ? 16  LEU D CD1 1 
ATOM   12374 C CD2 . LEU D 1 16  ? -10.943 57.982  77.060  1.00 34.83  ? 16  LEU D CD2 1 
ATOM   12375 N N   . TYR D 1 17  ? -6.171  55.251  76.633  1.00 40.03  ? 17  TYR D N   1 
ATOM   12376 C CA  . TYR D 1 17  ? -4.839  55.765  76.925  1.00 41.68  ? 17  TYR D CA  1 
ATOM   12377 C C   . TYR D 1 17  ? -4.720  57.262  76.680  1.00 43.92  ? 17  TYR D C   1 
ATOM   12378 O O   . TYR D 1 17  ? -3.696  57.852  77.040  1.00 46.98  ? 17  TYR D O   1 
ATOM   12379 C CB  . TYR D 1 17  ? -3.784  55.039  76.085  1.00 43.42  ? 17  TYR D CB  1 
ATOM   12380 C CG  . TYR D 1 17  ? -3.760  53.540  76.261  1.00 43.17  ? 17  TYR D CG  1 
ATOM   12381 C CD1 . TYR D 1 17  ? -3.527  52.967  77.504  1.00 42.78  ? 17  TYR D CD1 1 
ATOM   12382 C CD2 . TYR D 1 17  ? -3.951  52.696  75.178  1.00 44.23  ? 17  TYR D CD2 1 
ATOM   12383 C CE1 . TYR D 1 17  ? -3.501  51.594  77.663  1.00 42.73  ? 17  TYR D CE1 1 
ATOM   12384 C CE2 . TYR D 1 17  ? -3.925  51.327  75.327  1.00 44.53  ? 17  TYR D CE2 1 
ATOM   12385 C CZ  . TYR D 1 17  ? -3.700  50.779  76.569  1.00 43.78  ? 17  TYR D CZ  1 
ATOM   12386 O OH  . TYR D 1 17  ? -3.674  49.410  76.716  1.00 44.16  ? 17  TYR D OH  1 
ATOM   12387 N N   . ARG D 1 18  ? -5.731  57.886  76.082  1.00 40.47  ? 18  ARG D N   1 
ATOM   12388 C CA  . ARG D 1 18  ? -5.670  59.304  75.746  1.00 40.68  ? 18  ARG D CA  1 
ATOM   12389 C C   . ARG D 1 18  ? -5.884  60.127  77.011  1.00 39.20  ? 18  ARG D C   1 
ATOM   12390 O O   . ARG D 1 18  ? -6.981  60.137  77.578  1.00 39.59  ? 18  ARG D O   1 
ATOM   12391 C CB  . ARG D 1 18  ? -6.713  59.645  74.687  1.00 42.87  ? 18  ARG D CB  1 
ATOM   12392 C CG  . ARG D 1 18  ? -6.816  61.126  74.379  1.00 51.97  ? 18  ARG D CG  1 
ATOM   12393 C CD  . ARG D 1 18  ? -8.124  61.462  73.670  1.00 53.34  ? 18  ARG D CD  1 
ATOM   12394 N NE  . ARG D 1 18  ? -8.490  62.870  73.795  1.00 52.74  ? 18  ARG D NE  1 
ATOM   12395 C CZ  . ARG D 1 18  ? -7.753  63.894  73.386  1.00 52.56  ? 18  ARG D CZ  1 
ATOM   12396 N NH1 . ARG D 1 18  ? -6.628  63.716  72.711  1.00 61.78  ? 18  ARG D NH1 1 
ATOM   12397 N NH2 . ARG D 1 18  ? -8.163  65.133  73.649  1.00 50.61  ? 18  ARG D NH2 1 
ATOM   12398 N N   . GLU D 1 19  ? -4.836  60.813  77.449  1.00 39.81  ? 19  GLU D N   1 
ATOM   12399 C CA  . GLU D 1 19  ? -4.937  61.667  78.622  1.00 38.62  ? 19  GLU D CA  1 
ATOM   12400 C C   . GLU D 1 19  ? -5.902  62.818  78.347  1.00 41.12  ? 19  GLU D C   1 
ATOM   12401 O O   . GLU D 1 19  ? -5.929  63.352  77.233  1.00 56.24  ? 19  GLU D O   1 
ATOM   12402 C CB  . GLU D 1 19  ? -3.556  62.209  78.995  1.00 47.53  ? 19  GLU D CB  1 
ATOM   12403 C CG  . GLU D 1 19  ? -3.334  62.433  80.481  1.00 40.18  ? 19  GLU D CG  1 
ATOM   12404 C CD  . GLU D 1 19  ? -3.745  63.823  80.919  1.00 46.88  ? 19  GLU D CD  1 
ATOM   12405 O OE1 . GLU D 1 19  ? -3.674  64.751  80.086  1.00 52.54  ? 19  GLU D OE1 1 
ATOM   12406 O OE2 . GLU D 1 19  ? -4.134  63.991  82.094  1.00 48.52  ? 19  GLU D OE2 1 
ATOM   12407 N N   . PRO D 1 20  ? -6.725  63.211  79.320  1.00 38.97  ? 20  PRO D N   1 
ATOM   12408 C CA  . PRO D 1 20  ? -7.673  64.310  79.077  1.00 36.71  ? 20  PRO D CA  1 
ATOM   12409 C C   . PRO D 1 20  ? -7.042  65.699  79.074  1.00 36.22  ? 20  PRO D C   1 
ATOM   12410 O O   . PRO D 1 20  ? -7.343  66.512  78.194  1.00 36.79  ? 20  PRO D O   1 
ATOM   12411 C CB  . PRO D 1 20  ? -8.680  64.165  80.225  1.00 33.58  ? 20  PRO D CB  1 
ATOM   12412 C CG  . PRO D 1 20  ? -7.947  63.445  81.297  1.00 33.36  ? 20  PRO D CG  1 
ATOM   12413 C CD  . PRO D 1 20  ? -6.910  62.584  80.641  1.00 34.89  ? 20  PRO D CD  1 
ATOM   12414 N N   . TYR D 1 21  ? -6.164  65.986  80.040  1.00 36.28  ? 21  TYR D N   1 
ATOM   12415 C CA  . TYR D 1 21  ? -5.677  67.351  80.213  1.00 36.78  ? 21  TYR D CA  1 
ATOM   12416 C C   . TYR D 1 21  ? -4.669  67.757  79.147  1.00 40.07  ? 21  TYR D C   1 
ATOM   12417 O O   . TYR D 1 21  ? -4.527  68.954  78.874  1.00 51.96  ? 21  TYR D O   1 
ATOM   12418 C CB  . TYR D 1 21  ? -5.051  67.527  81.598  1.00 36.32  ? 21  TYR D CB  1 
ATOM   12419 C CG  . TYR D 1 21  ? -6.064  67.672  82.708  1.00 34.42  ? 21  TYR D CG  1 
ATOM   12420 C CD1 . TYR D 1 21  ? -6.712  68.879  82.930  1.00 33.77  ? 21  TYR D CD1 1 
ATOM   12421 C CD2 . TYR D 1 21  ? -6.370  66.602  83.537  1.00 39.38  ? 21  TYR D CD2 1 
ATOM   12422 C CE1 . TYR D 1 21  ? -7.639  69.015  83.945  1.00 32.11  ? 21  TYR D CE1 1 
ATOM   12423 C CE2 . TYR D 1 21  ? -7.294  66.726  84.555  1.00 35.77  ? 21  TYR D CE2 1 
ATOM   12424 C CZ  . TYR D 1 21  ? -7.925  67.933  84.755  1.00 41.53  ? 21  TYR D CZ  1 
ATOM   12425 O OH  . TYR D 1 21  ? -8.845  68.054  85.771  1.00 47.26  ? 21  TYR D OH  1 
ATOM   12426 N N   . THR D 1 22  ? -3.967  66.799  78.544  1.00 43.86  ? 22  THR D N   1 
ATOM   12427 C CA  . THR D 1 22  ? -3.000  67.096  77.498  1.00 44.95  ? 22  THR D CA  1 
ATOM   12428 C C   . THR D 1 22  ? -3.323  66.445  76.162  1.00 50.28  ? 22  THR D C   1 
ATOM   12429 O O   . THR D 1 22  ? -2.763  66.866  75.144  1.00 56.36  ? 22  THR D O   1 
ATOM   12430 C CB  . THR D 1 22  ? -1.589  66.662  77.929  1.00 43.14  ? 22  THR D CB  1 
ATOM   12431 O OG1 . THR D 1 22  ? -1.608  65.283  78.317  1.00 53.02  ? 22  THR D OG1 1 
ATOM   12432 C CG2 . THR D 1 22  ? -1.109  67.506  79.101  1.00 42.79  ? 22  THR D CG2 1 
ATOM   12433 N N   . GLY D 1 23  ? -4.195  65.440  76.134  1.00 45.93  ? 23  GLY D N   1 
ATOM   12434 C CA  . GLY D 1 23  ? -4.553  64.779  74.902  1.00 42.57  ? 23  GLY D CA  1 
ATOM   12435 C C   . GLY D 1 23  ? -3.564  63.743  74.426  1.00 44.71  ? 23  GLY D C   1 
ATOM   12436 O O   . GLY D 1 23  ? -3.822  63.085  73.409  1.00 49.20  ? 23  GLY D O   1 
ATOM   12437 N N   . GLU D 1 24  ? -2.453  63.560  75.131  1.00 44.53  ? 24  GLU D N   1 
ATOM   12438 C CA  . GLU D 1 24  ? -1.388  62.689  74.658  1.00 51.15  ? 24  GLU D CA  1 
ATOM   12439 C C   . GLU D 1 24  ? -1.709  61.232  74.963  1.00 55.25  ? 24  GLU D C   1 
ATOM   12440 O O   . GLU D 1 24  ? -2.065  60.885  76.094  1.00 54.62  ? 24  GLU D O   1 
ATOM   12441 C CB  . GLU D 1 24  ? -0.057  63.090  75.293  1.00 47.14  ? 24  GLU D CB  1 
ATOM   12442 C CG  . GLU D 1 24  ? 0.322   64.543  75.040  1.00 50.53  ? 24  GLU D CG  1 
ATOM   12443 C CD  . GLU D 1 24  ? 1.406   65.045  75.975  1.00 57.13  ? 24  GLU D CD  1 
ATOM   12444 O OE1 . GLU D 1 24  ? 1.787   64.303  76.905  1.00 52.13  ? 24  GLU D OE1 1 
ATOM   12445 O OE2 . GLU D 1 24  ? 1.878   66.184  75.776  1.00 61.47  ? 24  GLU D OE2 1 
ATOM   12446 N N   . TYR D 1 25  ? -1.589  60.382  73.946  1.00 51.83  ? 25  TYR D N   1 
ATOM   12447 C CA  . TYR D 1 25  ? -1.741  58.939  74.114  1.00 49.80  ? 25  TYR D CA  1 
ATOM   12448 C C   . TYR D 1 25  ? -0.457  58.414  74.740  1.00 51.16  ? 25  TYR D C   1 
ATOM   12449 O O   . TYR D 1 25  ? 0.564   58.267  74.064  1.00 50.30  ? 25  TYR D O   1 
ATOM   12450 C CB  . TYR D 1 25  ? -2.028  58.266  72.777  1.00 52.48  ? 25  TYR D CB  1 
ATOM   12451 C CG  . TYR D 1 25  ? -3.489  58.252  72.390  1.00 46.43  ? 25  TYR D CG  1 
ATOM   12452 C CD1 . TYR D 1 25  ? -4.065  59.336  71.742  1.00 46.42  ? 25  TYR D CD1 1 
ATOM   12453 C CD2 . TYR D 1 25  ? -4.290  57.152  72.670  1.00 54.57  ? 25  TYR D CD2 1 
ATOM   12454 C CE1 . TYR D 1 25  ? -5.400  59.326  71.385  1.00 45.48  ? 25  TYR D CE1 1 
ATOM   12455 C CE2 . TYR D 1 25  ? -5.626  57.133  72.317  1.00 52.38  ? 25  TYR D CE2 1 
ATOM   12456 C CZ  . TYR D 1 25  ? -6.176  58.222  71.674  1.00 47.99  ? 25  TYR D CZ  1 
ATOM   12457 O OH  . TYR D 1 25  ? -7.506  58.207  71.323  1.00 43.68  ? 25  TYR D OH  1 
ATOM   12458 N N   . LEU D 1 26  ? -0.501  58.135  76.042  1.00 46.10  ? 26  LEU D N   1 
ATOM   12459 C CA  . LEU D 1 26  ? 0.707   57.762  76.765  1.00 46.91  ? 26  LEU D CA  1 
ATOM   12460 C C   . LEU D 1 26  ? 1.148   56.328  76.504  1.00 53.08  ? 26  LEU D C   1 
ATOM   12461 O O   . LEU D 1 26  ? 2.304   55.994  76.784  1.00 65.74  ? 26  LEU D O   1 
ATOM   12462 C CB  . LEU D 1 26  ? 0.509   57.968  78.266  1.00 49.76  ? 26  LEU D CB  1 
ATOM   12463 C CG  . LEU D 1 26  ? 0.701   59.396  78.772  1.00 44.98  ? 26  LEU D CG  1 
ATOM   12464 C CD1 . LEU D 1 26  ? -0.624  60.135  78.842  1.00 43.27  ? 26  LEU D CD1 1 
ATOM   12465 C CD2 . LEU D 1 26  ? 1.384   59.384  80.123  1.00 44.72  ? 26  LEU D CD2 1 
ATOM   12466 N N   . LEU D 1 27  ? 0.267   55.476  75.982  1.00 51.43  ? 27  LEU D N   1 
ATOM   12467 C CA  . LEU D 1 27  ? 0.613   54.091  75.693  1.00 57.22  ? 27  LEU D CA  1 
ATOM   12468 C C   . LEU D 1 27  ? 0.274   53.782  74.240  1.00 58.76  ? 27  LEU D C   1 
ATOM   12469 O O   . LEU D 1 27  ? -0.846  54.075  73.787  1.00 64.14  ? 27  LEU D O   1 
ATOM   12470 C CB  . LEU D 1 27  ? -0.118  53.127  76.636  1.00 54.38  ? 27  LEU D CB  1 
ATOM   12471 C CG  . LEU D 1 27  ? 0.345   53.135  78.096  1.00 50.22  ? 27  LEU D CG  1 
ATOM   12472 C CD1 . LEU D 1 27  ? -0.223  51.943  78.852  1.00 48.15  ? 27  LEU D CD1 1 
ATOM   12473 C CD2 . LEU D 1 27  ? 1.865   53.152  78.187  1.00 47.99  ? 27  LEU D CD2 1 
ATOM   12474 N N   . PRO D 1 28  ? 1.201   53.203  73.479  1.00 51.51  ? 28  PRO D N   1 
ATOM   12475 C CA  . PRO D 1 28  ? 0.966   52.951  72.050  1.00 52.76  ? 28  PRO D CA  1 
ATOM   12476 C C   . PRO D 1 28  ? 0.292   51.626  71.716  1.00 52.69  ? 28  PRO D C   1 
ATOM   12477 O O   . PRO D 1 28  ? 0.300   51.243  70.543  1.00 54.08  ? 28  PRO D O   1 
ATOM   12478 C CB  . PRO D 1 28  ? 2.392   52.973  71.484  1.00 55.07  ? 28  PRO D CB  1 
ATOM   12479 C CG  . PRO D 1 28  ? 3.222   52.434  72.597  1.00 55.09  ? 28  PRO D CG  1 
ATOM   12480 C CD  . PRO D 1 28  ? 2.601   52.952  73.865  1.00 52.91  ? 28  PRO D CD  1 
ATOM   12481 N N   . TRP D 1 29  ? -0.282  50.914  72.690  1.00 51.24  ? 29  TRP D N   1 
ATOM   12482 C CA  . TRP D 1 29  ? -0.944  49.652  72.374  1.00 51.25  ? 29  TRP D CA  1 
ATOM   12483 C C   . TRP D 1 29  ? -2.192  49.845  71.521  1.00 53.44  ? 29  TRP D C   1 
ATOM   12484 O O   . TRP D 1 29  ? -2.607  48.905  70.836  1.00 60.04  ? 29  TRP D O   1 
ATOM   12485 C CB  . TRP D 1 29  ? -1.317  48.893  73.648  1.00 49.83  ? 29  TRP D CB  1 
ATOM   12486 C CG  . TRP D 1 29  ? -0.290  48.939  74.727  1.00 49.91  ? 29  TRP D CG  1 
ATOM   12487 C CD1 . TRP D 1 29  ? -0.391  49.582  75.925  1.00 49.04  ? 29  TRP D CD1 1 
ATOM   12488 C CD2 . TRP D 1 29  ? 0.995   48.305  74.718  1.00 52.25  ? 29  TRP D CD2 1 
ATOM   12489 N NE1 . TRP D 1 29  ? 0.752   49.391  76.662  1.00 50.61  ? 29  TRP D NE1 1 
ATOM   12490 C CE2 . TRP D 1 29  ? 1.620   48.612  75.943  1.00 51.16  ? 29  TRP D CE2 1 
ATOM   12491 C CE3 . TRP D 1 29  ? 1.679   47.511  73.792  1.00 59.71  ? 29  TRP D CE3 1 
ATOM   12492 C CZ2 . TRP D 1 29  ? 2.895   48.153  76.267  1.00 52.63  ? 29  TRP D CZ2 1 
ATOM   12493 C CZ3 . TRP D 1 29  ? 2.946   47.056  74.116  1.00 58.91  ? 29  TRP D CZ3 1 
ATOM   12494 C CH2 . TRP D 1 29  ? 3.540   47.378  75.343  1.00 55.08  ? 29  TRP D CH2 1 
ATOM   12495 N N   . THR D 1 30  ? -2.807  51.029  71.558  1.00 54.00  ? 30  THR D N   1 
ATOM   12496 C CA  . THR D 1 30  ? -3.918  51.303  70.653  1.00 53.91  ? 30  THR D CA  1 
ATOM   12497 C C   . THR D 1 30  ? -3.459  51.278  69.202  1.00 57.46  ? 30  THR D C   1 
ATOM   12498 O O   . THR D 1 30  ? -4.155  50.748  68.329  1.00 53.52  ? 30  THR D O   1 
ATOM   12499 C CB  . THR D 1 30  ? -4.552  52.653  70.987  1.00 61.42  ? 30  THR D CB  1 
ATOM   12500 O OG1 . THR D 1 30  ? -3.533  53.587  71.369  1.00 53.86  ? 30  THR D OG1 1 
ATOM   12501 C CG2 . THR D 1 30  ? -5.546  52.499  72.118  1.00 52.63  ? 30  THR D CG2 1 
ATOM   12502 N N   . PHE D 1 31  ? -2.287  51.851  68.928  1.00 62.03  ? 31  PHE D N   1 
ATOM   12503 C CA  . PHE D 1 31  ? -1.784  51.917  67.561  1.00 54.99  ? 31  PHE D CA  1 
ATOM   12504 C C   . PHE D 1 31  ? -1.308  50.554  67.073  1.00 56.51  ? 31  PHE D C   1 
ATOM   12505 O O   . PHE D 1 31  ? -1.636  50.134  65.957  1.00 57.66  ? 31  PHE D O   1 
ATOM   12506 C CB  . PHE D 1 31  ? -0.650  52.943  67.480  1.00 56.03  ? 31  PHE D CB  1 
ATOM   12507 C CG  . PHE D 1 31  ? -0.073  53.105  66.103  1.00 58.31  ? 31  PHE D CG  1 
ATOM   12508 C CD1 . PHE D 1 31  ? -0.638  53.994  65.203  1.00 64.75  ? 31  PHE D CD1 1 
ATOM   12509 C CD2 . PHE D 1 31  ? 1.035   52.372  65.710  1.00 60.25  ? 31  PHE D CD2 1 
ATOM   12510 C CE1 . PHE D 1 31  ? -0.110  54.147  63.935  1.00 69.22  ? 31  PHE D CE1 1 
ATOM   12511 C CE2 . PHE D 1 31  ? 1.566   52.517  64.443  1.00 62.43  ? 31  PHE D CE2 1 
ATOM   12512 C CZ  . PHE D 1 31  ? 0.994   53.407  63.555  1.00 71.55  ? 31  PHE D CZ  1 
ATOM   12513 N N   . PHE D 1 32  ? -0.538  49.844  67.901  1.00 56.60  ? 32  PHE D N   1 
ATOM   12514 C CA  . PHE D 1 32  ? 0.228   48.707  67.397  1.00 58.46  ? 32  PHE D CA  1 
ATOM   12515 C C   . PHE D 1 32  ? -0.649  47.496  67.110  1.00 58.32  ? 32  PHE D C   1 
ATOM   12516 O O   . PHE D 1 32  ? -0.349  46.724  66.192  1.00 67.60  ? 32  PHE D O   1 
ATOM   12517 C CB  . PHE D 1 32  ? 1.338   48.349  68.384  1.00 58.72  ? 32  PHE D CB  1 
ATOM   12518 C CG  . PHE D 1 32  ? 2.567   49.199  68.234  1.00 60.04  ? 32  PHE D CG  1 
ATOM   12519 C CD1 . PHE D 1 32  ? 3.036   49.537  66.974  1.00 61.97  ? 32  PHE D CD1 1 
ATOM   12520 C CD2 . PHE D 1 32  ? 3.245   49.671  69.344  1.00 59.45  ? 32  PHE D CD2 1 
ATOM   12521 C CE1 . PHE D 1 32  ? 4.162   50.324  66.823  1.00 63.28  ? 32  PHE D CE1 1 
ATOM   12522 C CE2 . PHE D 1 32  ? 4.374   50.459  69.199  1.00 60.77  ? 32  PHE D CE2 1 
ATOM   12523 C CZ  . PHE D 1 32  ? 4.833   50.785  67.937  1.00 62.69  ? 32  PHE D CZ  1 
ATOM   12524 N N   . HIS D 1 33  ? -1.721  47.302  67.874  1.00 64.40  ? 33  HIS D N   1 
ATOM   12525 C CA  . HIS D 1 33  ? -2.649  46.223  67.565  1.00 66.15  ? 33  HIS D CA  1 
ATOM   12526 C C   . HIS D 1 33  ? -3.581  46.581  66.414  1.00 56.50  ? 33  HIS D C   1 
ATOM   12527 O O   . HIS D 1 33  ? -4.169  45.679  65.807  1.00 57.10  ? 33  HIS D O   1 
ATOM   12528 C CB  . HIS D 1 33  ? -3.455  45.844  68.813  1.00 66.54  ? 33  HIS D CB  1 
ATOM   12529 C CG  . HIS D 1 33  ? -2.610  45.362  69.953  1.00 63.28  ? 33  HIS D CG  1 
ATOM   12530 N ND1 . HIS D 1 33  ? -2.810  44.144  70.566  1.00 66.05  ? 33  HIS D ND1 1 
ATOM   12531 C CD2 . HIS D 1 33  ? -1.565  45.938  70.594  1.00 64.66  ? 33  HIS D CD2 1 
ATOM   12532 C CE1 . HIS D 1 33  ? -1.921  43.988  71.532  1.00 67.36  ? 33  HIS D CE1 1 
ATOM   12533 N NE2 . HIS D 1 33  ? -1.154  45.062  71.570  1.00 67.54  ? 33  HIS D NE2 1 
ATOM   12534 N N   . ALA D 1 34  ? -3.724  47.874  66.102  1.00 56.20  ? 34  ALA D N   1 
ATOM   12535 C CA  . ALA D 1 34  ? -4.529  48.279  64.953  1.00 56.71  ? 34  ALA D CA  1 
ATOM   12536 C C   . ALA D 1 34  ? -3.847  47.915  63.651  1.00 67.78  ? 34  ALA D C   1 
ATOM   12537 O O   . ALA D 1 34  ? -4.490  47.430  62.713  1.00 69.40  ? 34  ALA D O   1 
ATOM   12538 C CB  . ALA D 1 34  ? -4.820  49.778  65.010  1.00 55.79  ? 34  ALA D CB  1 
ATOM   12539 N N   . VAL D 1 35  ? -2.540  48.118  63.593  1.00 70.20  ? 35  VAL D N   1 
ATOM   12540 C CA  . VAL D 1 35  ? -1.771  47.918  62.378  1.00 70.52  ? 35  VAL D CA  1 
ATOM   12541 C C   . VAL D 1 35  ? -1.325  46.465  62.306  1.00 68.60  ? 35  VAL D C   1 
ATOM   12542 O O   . VAL D 1 35  ? -0.535  46.089  61.433  1.00 74.27  ? 35  VAL D O   1 
ATOM   12543 C CB  . VAL D 1 35  ? -0.578  48.886  62.342  1.00 72.72  ? 35  VAL D CB  1 
ATOM   12544 C CG1 . VAL D 1 35  ? -1.070  50.311  62.544  1.00 75.49  ? 35  VAL D CG1 1 
ATOM   12545 C CG2 . VAL D 1 35  ? 0.424   48.520  63.424  1.00 67.78  ? 35  VAL D CG2 1 
ATOM   12546 N N   . LYS D 1 36  ? -1.816  45.645  63.225  1.00 62.80  ? 36  LYS D N   1 
ATOM   12547 C CA  . LYS D 1 36  ? -1.493  44.225  63.176  1.00 67.75  ? 36  LYS D CA  1 
ATOM   12548 C C   . LYS D 1 36  ? -2.716  43.322  63.266  1.00 69.20  ? 36  LYS D C   1 
ATOM   12549 O O   . LYS D 1 36  ? -2.764  42.297  62.578  1.00 73.89  ? 36  LYS D O   1 
ATOM   12550 C CB  . LYS D 1 36  ? -0.506  43.888  64.302  1.00 63.64  ? 36  LYS D CB  1 
ATOM   12551 C CG  . LYS D 1 36  ? 0.058   42.490  64.215  1.00 65.12  ? 36  LYS D CG  1 
ATOM   12552 C CD  . LYS D 1 36  ? 1.207   42.296  65.184  1.00 65.28  ? 36  LYS D CD  1 
ATOM   12553 C CE  . LYS D 1 36  ? 0.724   41.563  66.421  1.00 67.36  ? 36  LYS D CE  1 
ATOM   12554 N NZ  . LYS D 1 36  ? 1.132   42.126  67.716  1.00 72.87  ? 36  LYS D NZ  1 
ATOM   12555 N N   . ASP D 1 37  ? -3.707  43.672  64.092  1.00 68.00  ? 37  ASP D N   1 
ATOM   12556 C CA  . ASP D 1 37  ? -4.828  42.759  64.309  1.00 65.76  ? 37  ASP D CA  1 
ATOM   12557 C C   . ASP D 1 37  ? -6.205  43.396  64.150  1.00 68.90  ? 37  ASP D C   1 
ATOM   12558 O O   . ASP D 1 37  ? -7.115  42.735  63.656  1.00 61.04  ? 37  ASP D O   1 
ATOM   12559 C CB  . ASP D 1 37  ? -4.696  42.118  65.704  1.00 63.65  ? 37  ASP D CB  1 
ATOM   12560 C CG  . ASP D 1 37  ? -3.470  41.224  65.818  1.00 76.60  ? 37  ASP D CG  1 
ATOM   12561 O OD1 . ASP D 1 37  ? -3.289  40.334  64.960  1.00 83.13  ? 37  ASP D OD1 1 
ATOM   12562 O OD2 . ASP D 1 37  ? -2.686  41.417  66.772  1.00 66.59  ? 37  ASP D OD2 1 
ATOM   12563 N N   . TYR D 1 38  ? -6.378  44.661  64.547  1.00 70.35  ? 38  TYR D N   1 
ATOM   12564 C CA  . TYR D 1 38  ? -7.702  45.290  64.535  1.00 65.07  ? 38  TYR D CA  1 
ATOM   12565 C C   . TYR D 1 38  ? -8.349  45.230  63.154  1.00 59.93  ? 38  TYR D C   1 
ATOM   12566 O O   . TYR D 1 38  ? -9.572  45.089  63.047  1.00 56.85  ? 38  TYR D O   1 
ATOM   12567 C CB  . TYR D 1 38  ? -7.585  46.740  65.037  1.00 73.63  ? 38  TYR D CB  1 
ATOM   12568 C CG  . TYR D 1 38  ? -7.508  46.842  66.544  1.00 68.70  ? 38  TYR D CG  1 
ATOM   12569 C CD1 . TYR D 1 38  ? -8.300  46.040  67.342  1.00 65.22  ? 38  TYR D CD1 1 
ATOM   12570 C CD2 . TYR D 1 38  ? -6.624  47.686  67.173  1.00 64.68  ? 38  TYR D CD2 1 
ATOM   12571 C CE1 . TYR D 1 38  ? -8.230  46.100  68.693  1.00 59.12  ? 38  TYR D CE1 1 
ATOM   12572 C CE2 . TYR D 1 38  ? -6.532  47.736  68.546  1.00 66.81  ? 38  TYR D CE2 1 
ATOM   12573 C CZ  . TYR D 1 38  ? -7.324  46.948  69.288  1.00 65.97  ? 38  TYR D CZ  1 
ATOM   12574 O OH  . TYR D 1 38  ? -7.307  46.937  70.644  1.00 74.34  ? 38  TYR D OH  1 
ATOM   12575 N N   . TYR D 1 39  ? -7.551  45.288  62.092  1.00 63.45  ? 39  TYR D N   1 
ATOM   12576 C CA  . TYR D 1 39  ? -8.060  45.182  60.728  1.00 71.04  ? 39  TYR D CA  1 
ATOM   12577 C C   . TYR D 1 39  ? -7.979  43.771  60.158  1.00 76.16  ? 39  TYR D C   1 
ATOM   12578 O O   . TYR D 1 39  ? -8.869  43.360  59.406  1.00 78.43  ? 39  TYR D O   1 
ATOM   12579 C CB  . TYR D 1 39  ? -7.297  46.136  59.799  1.00 75.94  ? 39  TYR D CB  1 
ATOM   12580 C CG  . TYR D 1 39  ? -7.539  45.876  58.326  1.00 77.08  ? 39  TYR D CG  1 
ATOM   12581 C CD1 . TYR D 1 39  ? -8.612  46.460  57.669  1.00 75.25  ? 39  TYR D CD1 1 
ATOM   12582 C CD2 . TYR D 1 39  ? -6.695  45.047  57.593  1.00 80.36  ? 39  TYR D CD2 1 
ATOM   12583 C CE1 . TYR D 1 39  ? -8.841  46.227  56.327  1.00 71.60  ? 39  TYR D CE1 1 
ATOM   12584 C CE2 . TYR D 1 39  ? -6.922  44.803  56.251  1.00 82.14  ? 39  TYR D CE2 1 
ATOM   12585 C CZ  . TYR D 1 39  ? -7.995  45.398  55.623  1.00 81.36  ? 39  TYR D CZ  1 
ATOM   12586 O OH  . TYR D 1 39  ? -8.222  45.164  54.287  1.00 86.24  ? 39  TYR D OH  1 
ATOM   12587 N N   . ASP D 1 40  ? -6.926  43.023  60.489  1.00 67.58  ? 40  ASP D N   1 
ATOM   12588 C CA  . ASP D 1 40  ? -6.620  41.810  59.739  1.00 65.16  ? 40  ASP D CA  1 
ATOM   12589 C C   . ASP D 1 40  ? -7.545  40.656  60.096  1.00 74.54  ? 40  ASP D C   1 
ATOM   12590 O O   . ASP D 1 40  ? -7.886  39.846  59.229  1.00 73.01  ? 40  ASP D O   1 
ATOM   12591 C CB  . ASP D 1 40  ? -5.165  41.416  59.962  1.00 68.42  ? 40  ASP D CB  1 
ATOM   12592 C CG  . ASP D 1 40  ? -4.269  41.896  58.850  1.00 91.45  ? 40  ASP D CG  1 
ATOM   12593 O OD1 . ASP D 1 40  ? -4.596  41.647  57.671  1.00 90.30  ? 40  ASP D OD1 1 
ATOM   12594 O OD2 . ASP D 1 40  ? -3.261  42.558  59.149  1.00 99.69  ? 40  ASP D OD2 1 
ATOM   12595 N N   . MET D 1 41  ? -7.955  40.558  61.357  1.00 78.85  ? 41  MET D N   1 
ATOM   12596 C CA  . MET D 1 41  ? -8.815  39.449  61.763  1.00 61.97  ? 41  MET D CA  1 
ATOM   12597 C C   . MET D 1 41  ? -10.116 39.383  60.979  1.00 64.60  ? 41  MET D C   1 
ATOM   12598 O O   . MET D 1 41  ? -10.479 38.286  60.520  1.00 68.65  ? 41  MET D O   1 
ATOM   12599 C CB  . MET D 1 41  ? -9.085  39.539  63.260  1.00 59.65  ? 41  MET D CB  1 
ATOM   12600 C CG  . MET D 1 41  ? -7.926  39.118  64.052  1.00 68.74  ? 41  MET D CG  1 
ATOM   12601 S SD  . MET D 1 41  ? -7.970  37.336  64.049  1.00 82.66  ? 41  MET D SD  1 
ATOM   12602 C CE  . MET D 1 41  ? -7.336  37.089  65.670  1.00 59.62  ? 41  MET D CE  1 
ATOM   12603 N N   . PRO D 1 42  ? -10.868 40.473  60.798  1.00 62.45  ? 42  PRO D N   1 
ATOM   12604 C CA  . PRO D 1 42  ? -12.008 40.417  59.875  1.00 61.77  ? 42  PRO D CA  1 
ATOM   12605 C C   . PRO D 1 42  ? -11.603 40.373  58.412  1.00 68.28  ? 42  PRO D C   1 
ATOM   12606 O O   . PRO D 1 42  ? -12.450 40.056  57.569  1.00 79.01  ? 42  PRO D O   1 
ATOM   12607 C CB  . PRO D 1 42  ? -12.785 41.695  60.203  1.00 70.47  ? 42  PRO D CB  1 
ATOM   12608 C CG  . PRO D 1 42  ? -11.756 42.615  60.732  1.00 67.29  ? 42  PRO D CG  1 
ATOM   12609 C CD  . PRO D 1 42  ? -10.809 41.767  61.504  1.00 63.30  ? 42  PRO D CD  1 
ATOM   12610 N N   . ALA D 1 43  ? -10.348 40.687  58.079  1.00 70.69  ? 43  ALA D N   1 
ATOM   12611 C CA  . ALA D 1 43  ? -9.892  40.547  56.701  1.00 67.96  ? 43  ALA D CA  1 
ATOM   12612 C C   . ALA D 1 43  ? -9.696  39.088  56.308  1.00 69.65  ? 43  ALA D C   1 
ATOM   12613 O O   . ALA D 1 43  ? -9.748  38.767  55.116  1.00 71.73  ? 43  ALA D O   1 
ATOM   12614 C CB  . ALA D 1 43  ? -8.596  41.329  56.488  1.00 71.74  ? 43  ALA D CB  1 
ATOM   12615 N N   . TYR D 1 44  ? -9.465  38.203  57.285  1.00 69.27  ? 44  TYR D N   1 
ATOM   12616 C CA  . TYR D 1 44  ? -9.481  36.769  57.017  1.00 70.91  ? 44  TYR D CA  1 
ATOM   12617 C C   . TYR D 1 44  ? -10.796 36.340  56.386  1.00 73.30  ? 44  TYR D C   1 
ATOM   12618 O O   . TYR D 1 44  ? -10.822 35.419  55.561  1.00 78.09  ? 44  TYR D O   1 
ATOM   12619 C CB  . TYR D 1 44  ? -9.277  35.977  58.310  1.00 73.09  ? 44  TYR D CB  1 
ATOM   12620 C CG  . TYR D 1 44  ? -7.858  35.865  58.815  1.00 73.81  ? 44  TYR D CG  1 
ATOM   12621 C CD1 . TYR D 1 44  ? -7.057  36.986  58.981  1.00 80.26  ? 44  TYR D CD1 1 
ATOM   12622 C CD2 . TYR D 1 44  ? -7.329  34.629  59.150  1.00 70.39  ? 44  TYR D CD2 1 
ATOM   12623 C CE1 . TYR D 1 44  ? -5.764  36.874  59.459  1.00 79.17  ? 44  TYR D CE1 1 
ATOM   12624 C CE2 . TYR D 1 44  ? -6.046  34.509  59.620  1.00 70.90  ? 44  TYR D CE2 1 
ATOM   12625 C CZ  . TYR D 1 44  ? -5.267  35.629  59.777  1.00 70.43  ? 44  TYR D CZ  1 
ATOM   12626 O OH  . TYR D 1 44  ? -3.988  35.491  60.254  1.00 71.00  ? 44  TYR D OH  1 
ATOM   12627 N N   . LEU D 1 45  ? -11.894 37.001  56.765  1.00 74.40  ? 45  LEU D N   1 
ATOM   12628 C CA  . LEU D 1 45  ? -13.227 36.626  56.307  1.00 78.48  ? 45  LEU D CA  1 
ATOM   12629 C C   . LEU D 1 45  ? -13.359 36.680  54.792  1.00 78.96  ? 45  LEU D C   1 
ATOM   12630 O O   . LEU D 1 45  ? -14.255 36.037  54.235  1.00 79.77  ? 45  LEU D O   1 
ATOM   12631 C CB  . LEU D 1 45  ? -14.264 37.547  56.951  1.00 79.06  ? 45  LEU D CB  1 
ATOM   12632 C CG  . LEU D 1 45  ? -15.162 36.991  58.054  1.00 69.42  ? 45  LEU D CG  1 
ATOM   12633 C CD1 . LEU D 1 45  ? -15.908 38.122  58.744  1.00 68.31  ? 45  LEU D CD1 1 
ATOM   12634 C CD2 . LEU D 1 45  ? -16.136 35.984  57.480  1.00 66.15  ? 45  LEU D CD2 1 
ATOM   12635 N N   . LYS D 1 46  ? -12.496 37.438  54.115  1.00 72.53  ? 46  LYS D N   1 
ATOM   12636 C CA  . LYS D 1 46  ? -12.563 37.522  52.662  1.00 75.01  ? 46  LYS D CA  1 
ATOM   12637 C C   . LYS D 1 46  ? -11.832 36.363  51.995  1.00 77.24  ? 46  LYS D C   1 
ATOM   12638 O O   . LYS D 1 46  ? -12.295 35.841  50.975  1.00 79.12  ? 46  LYS D O   1 
ATOM   12639 C CB  . LYS D 1 46  ? -11.985 38.855  52.192  1.00 75.94  ? 46  LYS D CB  1 
ATOM   12640 C CG  . LYS D 1 46  ? -12.346 40.031  53.080  1.00 72.55  ? 46  LYS D CG  1 
ATOM   12641 C CD  . LYS D 1 46  ? -11.551 41.263  52.692  1.00 72.94  ? 46  LYS D CD  1 
ATOM   12642 C CE  . LYS D 1 46  ? -12.390 42.206  51.848  1.00 73.51  ? 46  LYS D CE  1 
ATOM   12643 N NZ  . LYS D 1 46  ? -12.026 43.629  52.069  1.00 72.37  ? 46  LYS D NZ  1 
ATOM   12644 N N   . ASP D 1 47  ? -10.690 35.951  52.551  1.00 80.01  ? 47  ASP D N   1 
ATOM   12645 C CA  . ASP D 1 47  ? -9.916  34.881  51.930  1.00 87.91  ? 47  ASP D CA  1 
ATOM   12646 C C   . ASP D 1 47  ? -10.559 33.517  52.146  1.00 89.79  ? 47  ASP D C   1 
ATOM   12647 O O   . ASP D 1 47  ? -10.394 32.617  51.313  1.00 87.00  ? 47  ASP D O   1 
ATOM   12648 C CB  . ASP D 1 47  ? -8.484  34.887  52.464  1.00 81.45  ? 47  ASP D CB  1 
ATOM   12649 C CG  . ASP D 1 47  ? -7.794  36.222  52.262  1.00 85.09  ? 47  ASP D CG  1 
ATOM   12650 O OD1 . ASP D 1 47  ? -8.479  37.201  51.895  1.00 83.61  ? 47  ASP D OD1 1 
ATOM   12651 O OD2 . ASP D 1 47  ? -6.563  36.289  52.455  1.00 93.01  ? 47  ASP D OD2 1 
ATOM   12652 N N   . PHE D 1 48  ? -11.283 33.342  53.249  1.00 77.84  ? 48  PHE D N   1 
ATOM   12653 C CA  . PHE D 1 48  ? -11.992 32.104  53.541  1.00 77.97  ? 48  PHE D CA  1 
ATOM   12654 C C   . PHE D 1 48  ? -13.441 32.440  53.854  1.00 76.31  ? 48  PHE D C   1 
ATOM   12655 O O   . PHE D 1 48  ? -13.710 33.294  54.704  1.00 77.37  ? 48  PHE D O   1 
ATOM   12656 C CB  . PHE D 1 48  ? -11.351 31.354  54.717  1.00 78.39  ? 48  PHE D CB  1 
ATOM   12657 C CG  . PHE D 1 48  ? -9.850  31.453  54.762  1.00 81.01  ? 48  PHE D CG  1 
ATOM   12658 C CD1 . PHE D 1 48  ? -9.228  32.528  55.381  1.00 76.44  ? 48  PHE D CD1 1 
ATOM   12659 C CD2 . PHE D 1 48  ? -9.060  30.469  54.190  1.00 82.17  ? 48  PHE D CD2 1 
ATOM   12660 C CE1 . PHE D 1 48  ? -7.849  32.620  55.425  1.00 80.00  ? 48  PHE D CE1 1 
ATOM   12661 C CE2 . PHE D 1 48  ? -7.679  30.555  54.232  1.00 81.15  ? 48  PHE D CE2 1 
ATOM   12662 C CZ  . PHE D 1 48  ? -7.073  31.632  54.850  1.00 79.67  ? 48  PHE D CZ  1 
ATOM   12663 N N   . GLU D 1 49  ? -14.368 31.775  53.172  1.00 86.94  ? 49  GLU D N   1 
ATOM   12664 C CA  . GLU D 1 49  ? -15.793 32.059  53.350  1.00 92.44  ? 49  GLU D CA  1 
ATOM   12665 C C   . GLU D 1 49  ? -16.394 31.249  54.499  1.00 90.58  ? 49  GLU D C   1 
ATOM   12666 O O   . GLU D 1 49  ? -17.414 30.579  54.345  1.00 93.98  ? 49  GLU D O   1 
ATOM   12667 C CB  . GLU D 1 49  ? -16.545 31.800  52.048  1.00 82.96  ? 49  GLU D CB  1 
ATOM   12668 C CG  . GLU D 1 49  ? -15.767 32.112  50.775  1.00 80.67  ? 49  GLU D CG  1 
ATOM   12669 C CD  . GLU D 1 49  ? -15.235 33.533  50.732  1.00 98.62  ? 49  GLU D CD  1 
ATOM   12670 O OE1 . GLU D 1 49  ? -15.964 34.459  51.146  1.00 102.61 ? 49  GLU D OE1 1 
ATOM   12671 O OE2 . GLU D 1 49  ? -14.093 33.725  50.264  1.00 98.60  ? 49  GLU D OE2 1 
ATOM   12672 N N   . ILE D 1 50  ? -15.764 31.317  55.668  1.00 90.68  ? 50  ILE D N   1 
ATOM   12673 C CA  . ILE D 1 50  ? -16.297 30.732  56.893  1.00 79.78  ? 50  ILE D CA  1 
ATOM   12674 C C   . ILE D 1 50  ? -16.626 31.864  57.854  1.00 72.43  ? 50  ILE D C   1 
ATOM   12675 O O   . ILE D 1 50  ? -15.908 32.870  57.914  1.00 69.83  ? 50  ILE D O   1 
ATOM   12676 C CB  . ILE D 1 50  ? -15.320 29.723  57.529  1.00 77.56  ? 50  ILE D CB  1 
ATOM   12677 C CG1 . ILE D 1 50  ? -13.930 30.338  57.711  1.00 71.76  ? 50  ILE D CG1 1 
ATOM   12678 C CG2 . ILE D 1 50  ? -15.247 28.454  56.695  1.00 78.31  ? 50  ILE D CG2 1 
ATOM   12679 C CD1 . ILE D 1 50  ? -13.640 30.791  59.124  1.00 69.37  ? 50  ILE D CD1 1 
ATOM   12680 N N   . LYS D 1 51  ? -17.713 31.699  58.605  1.00 80.20  ? 51  LYS D N   1 
ATOM   12681 C CA  . LYS D 1 51  ? -18.262 32.805  59.377  1.00 80.72  ? 51  LYS D CA  1 
ATOM   12682 C C   . LYS D 1 51  ? -17.401 33.130  60.590  1.00 74.34  ? 51  LYS D C   1 
ATOM   12683 O O   . LYS D 1 51  ? -16.860 32.238  61.247  1.00 70.27  ? 51  LYS D O   1 
ATOM   12684 C CB  . LYS D 1 51  ? -19.691 32.484  59.804  1.00 69.55  ? 51  LYS D CB  1 
ATOM   12685 C CG  . LYS D 1 51  ? -20.546 32.144  58.613  1.00 73.92  ? 51  LYS D CG  1 
ATOM   12686 C CD  . LYS D 1 51  ? -20.842 33.390  57.785  1.00 78.93  ? 51  LYS D CD  1 
ATOM   12687 C CE  . LYS D 1 51  ? -22.204 33.254  57.167  1.00 71.34  ? 51  LYS D CE  1 
ATOM   12688 N NZ  . LYS D 1 51  ? -23.071 32.751  58.229  1.00 82.76  ? 51  LYS D NZ  1 
ATOM   12689 N N   . LEU D 1 52  ? -17.257 34.428  60.861  1.00 62.95  ? 52  LEU D N   1 
ATOM   12690 C CA  . LEU D 1 52  ? -16.578 34.933  62.044  1.00 62.88  ? 52  LEU D CA  1 
ATOM   12691 C C   . LEU D 1 52  ? -17.421 36.035  62.667  1.00 57.80  ? 52  LEU D C   1 
ATOM   12692 O O   . LEU D 1 52  ? -18.121 36.768  61.966  1.00 59.53  ? 52  LEU D O   1 
ATOM   12693 C CB  . LEU D 1 52  ? -15.183 35.480  61.716  1.00 60.72  ? 52  LEU D CB  1 
ATOM   12694 C CG  . LEU D 1 52  ? -14.154 34.514  61.130  1.00 62.91  ? 52  LEU D CG  1 
ATOM   12695 C CD1 . LEU D 1 52  ? -12.867 35.258  60.826  1.00 63.52  ? 52  LEU D CD1 1 
ATOM   12696 C CD2 . LEU D 1 52  ? -13.900 33.356  62.082  1.00 62.68  ? 52  LEU D CD2 1 
ATOM   12697 N N   . ASN D 1 53  ? -17.346 36.156  63.991  1.00 55.91  ? 53  ASN D N   1 
ATOM   12698 C CA  . ASN D 1 53  ? -18.069 37.193  64.713  1.00 53.79  ? 53  ASN D CA  1 
ATOM   12699 C C   . ASN D 1 53  ? -17.097 37.991  65.569  1.00 56.20  ? 53  ASN D C   1 
ATOM   12700 O O   . ASN D 1 53  ? -16.107 37.457  66.074  1.00 63.56  ? 53  ASN D O   1 
ATOM   12701 C CB  . ASN D 1 53  ? -19.182 36.606  65.585  1.00 52.58  ? 53  ASN D CB  1 
ATOM   12702 C CG  . ASN D 1 53  ? -20.227 35.875  64.772  1.00 53.81  ? 53  ASN D CG  1 
ATOM   12703 O OD1 . ASN D 1 53  ? -20.718 36.389  63.768  1.00 54.59  ? 53  ASN D OD1 1 
ATOM   12704 N ND2 . ASN D 1 53  ? -20.572 34.669  65.201  1.00 54.08  ? 53  ASN D ND2 1 
ATOM   12705 N N   . PHE D 1 54  ? -17.389 39.281  65.726  1.00 51.27  ? 54  PHE D N   1 
ATOM   12706 C CA  . PHE D 1 54  ? -16.463 40.204  66.363  1.00 50.29  ? 54  PHE D CA  1 
ATOM   12707 C C   . PHE D 1 54  ? -17.199 41.106  67.341  1.00 53.44  ? 54  PHE D C   1 
ATOM   12708 O O   . PHE D 1 54  ? -18.395 41.371  67.194  1.00 53.55  ? 54  PHE D O   1 
ATOM   12709 C CB  . PHE D 1 54  ? -15.730 41.058  65.321  1.00 51.50  ? 54  PHE D CB  1 
ATOM   12710 C CG  . PHE D 1 54  ? -14.923 40.254  64.348  1.00 53.77  ? 54  PHE D CG  1 
ATOM   12711 C CD1 . PHE D 1 54  ? -13.600 39.946  64.616  1.00 57.47  ? 54  PHE D CD1 1 
ATOM   12712 C CD2 . PHE D 1 54  ? -15.490 39.794  63.171  1.00 55.36  ? 54  PHE D CD2 1 
ATOM   12713 C CE1 . PHE D 1 54  ? -12.854 39.202  63.726  1.00 56.58  ? 54  PHE D CE1 1 
ATOM   12714 C CE2 . PHE D 1 54  ? -14.749 39.048  62.277  1.00 57.53  ? 54  PHE D CE2 1 
ATOM   12715 C CZ  . PHE D 1 54  ? -13.430 38.751  62.556  1.00 60.41  ? 54  PHE D CZ  1 
ATOM   12716 N N   . ASN D 1 55  ? -16.462 41.574  68.345  1.00 55.22  ? 55  ASN D N   1 
ATOM   12717 C CA  . ASN D 1 55  ? -16.958 42.541  69.312  1.00 47.90  ? 55  ASN D CA  1 
ATOM   12718 C C   . ASN D 1 55  ? -15.944 43.667  69.434  1.00 47.50  ? 55  ASN D C   1 
ATOM   12719 O O   . ASN D 1 55  ? -14.758 43.415  69.669  1.00 45.21  ? 55  ASN D O   1 
ATOM   12720 C CB  . ASN D 1 55  ? -17.193 41.896  70.679  1.00 43.54  ? 55  ASN D CB  1 
ATOM   12721 C CG  . ASN D 1 55  ? -17.833 42.849  71.664  1.00 47.23  ? 55  ASN D CG  1 
ATOM   12722 O OD1 . ASN D 1 55  ? -19.055 42.902  71.782  1.00 52.97  ? 55  ASN D OD1 1 
ATOM   12723 N ND2 . ASN D 1 55  ? -17.010 43.610  72.378  1.00 45.01  ? 55  ASN D ND2 1 
ATOM   12724 N N   . LEU D 1 56  ? -16.409 44.903  69.272  1.00 45.80  ? 56  LEU D N   1 
ATOM   12725 C CA  . LEU D 1 56  ? -15.565 46.087  69.374  1.00 49.32  ? 56  LEU D CA  1 
ATOM   12726 C C   . LEU D 1 56  ? -16.137 47.000  70.449  1.00 53.35  ? 56  LEU D C   1 
ATOM   12727 O O   . LEU D 1 56  ? -17.286 47.443  70.341  1.00 51.49  ? 56  LEU D O   1 
ATOM   12728 C CB  . LEU D 1 56  ? -15.478 46.826  68.034  1.00 49.39  ? 56  LEU D CB  1 
ATOM   12729 C CG  . LEU D 1 56  ? -14.511 46.390  66.922  1.00 66.92  ? 56  LEU D CG  1 
ATOM   12730 C CD1 . LEU D 1 56  ? -13.118 46.964  67.156  1.00 62.77  ? 56  LEU D CD1 1 
ATOM   12731 C CD2 . LEU D 1 56  ? -14.449 44.878  66.721  1.00 57.77  ? 56  LEU D CD2 1 
ATOM   12732 N N   . THR D 1 57  ? -15.343 47.280  71.479  1.00 48.75  ? 57  THR D N   1 
ATOM   12733 C CA  . THR D 1 57  ? -15.795 48.182  72.527  1.00 40.97  ? 57  THR D CA  1 
ATOM   12734 C C   . THR D 1 57  ? -15.846 49.613  71.995  1.00 43.29  ? 57  THR D C   1 
ATOM   12735 O O   . THR D 1 57  ? -14.956 50.031  71.247  1.00 43.53  ? 57  THR D O   1 
ATOM   12736 C CB  . THR D 1 57  ? -14.876 48.110  73.748  1.00 38.20  ? 57  THR D CB  1 
ATOM   12737 O OG1 . THR D 1 57  ? -13.511 48.244  73.335  1.00 44.04  ? 57  THR D OG1 1 
ATOM   12738 C CG2 . THR D 1 57  ? -15.062 46.787  74.477  1.00 37.92  ? 57  THR D CG2 1 
ATOM   12739 N N   . PRO D 1 58  ? -16.873 50.385  72.360  1.00 37.57  ? 58  PRO D N   1 
ATOM   12740 C CA  . PRO D 1 58  ? -16.985 51.754  71.829  1.00 37.61  ? 58  PRO D CA  1 
ATOM   12741 C C   . PRO D 1 58  ? -15.796 52.634  72.167  1.00 37.65  ? 58  PRO D C   1 
ATOM   12742 O O   . PRO D 1 58  ? -15.459 53.529  71.382  1.00 41.05  ? 58  PRO D O   1 
ATOM   12743 C CB  . PRO D 1 58  ? -18.276 52.278  72.475  1.00 40.48  ? 58  PRO D CB  1 
ATOM   12744 C CG  . PRO D 1 58  ? -19.037 51.053  72.869  1.00 36.23  ? 58  PRO D CG  1 
ATOM   12745 C CD  . PRO D 1 58  ? -18.007 50.030  73.229  1.00 36.11  ? 58  PRO D CD  1 
ATOM   12746 N N   . VAL D 1 59  ? -15.147 52.408  73.313  1.00 36.87  ? 59  VAL D N   1 
ATOM   12747 C CA  . VAL D 1 59  ? -13.958 53.184  73.654  1.00 39.05  ? 59  VAL D CA  1 
ATOM   12748 C C   . VAL D 1 59  ? -12.844 52.915  72.653  1.00 41.46  ? 59  VAL D C   1 
ATOM   12749 O O   . VAL D 1 59  ? -12.072 53.819  72.309  1.00 39.68  ? 59  VAL D O   1 
ATOM   12750 C CB  . VAL D 1 59  ? -13.517 52.881  75.102  1.00 36.50  ? 59  VAL D CB  1 
ATOM   12751 C CG1 . VAL D 1 59  ? -13.274 51.389  75.299  1.00 42.00  ? 59  VAL D CG1 1 
ATOM   12752 C CG2 . VAL D 1 59  ? -12.278 53.686  75.468  1.00 43.12  ? 59  VAL D CG2 1 
ATOM   12753 N N   . LEU D 1 60  ? -12.750 51.680  72.157  1.00 43.19  ? 60  LEU D N   1 
ATOM   12754 C CA  . LEU D 1 60  ? -11.755 51.365  71.140  1.00 44.61  ? 60  LEU D CA  1 
ATOM   12755 C C   . LEU D 1 60  ? -12.065 52.048  69.814  1.00 45.03  ? 60  LEU D C   1 
ATOM   12756 O O   . LEU D 1 60  ? -11.141 52.428  69.087  1.00 44.48  ? 60  LEU D O   1 
ATOM   12757 C CB  . LEU D 1 60  ? -11.668 49.855  70.947  1.00 42.78  ? 60  LEU D CB  1 
ATOM   12758 C CG  . LEU D 1 60  ? -10.644 49.370  69.926  1.00 44.91  ? 60  LEU D CG  1 
ATOM   12759 C CD1 . LEU D 1 60  ? -9.241  49.842  70.288  1.00 45.43  ? 60  LEU D CD1 1 
ATOM   12760 C CD2 . LEU D 1 60  ? -10.718 47.868  69.839  1.00 48.16  ? 60  LEU D CD2 1 
ATOM   12761 N N   . ILE D 1 61  ? -13.349 52.212  69.484  1.00 44.24  ? 61  ILE D N   1 
ATOM   12762 C CA  . ILE D 1 61  ? -13.716 52.851  68.221  1.00 43.57  ? 61  ILE D CA  1 
ATOM   12763 C C   . ILE D 1 61  ? -13.191 54.279  68.178  1.00 45.15  ? 61  ILE D C   1 
ATOM   12764 O O   . ILE D 1 61  ? -12.572 54.701  67.194  1.00 47.41  ? 61  ILE D O   1 
ATOM   12765 C CB  . ILE D 1 61  ? -15.242 52.810  68.018  1.00 43.21  ? 61  ILE D CB  1 
ATOM   12766 C CG1 . ILE D 1 61  ? -15.791 51.418  68.330  1.00 42.58  ? 61  ILE D CG1 1 
ATOM   12767 C CG2 . ILE D 1 61  ? -15.601 53.213  66.594  1.00 44.34  ? 61  ILE D CG2 1 
ATOM   12768 C CD1 . ILE D 1 61  ? -15.317 50.351  67.379  1.00 44.43  ? 61  ILE D CD1 1 
ATOM   12769 N N   . ASP D 1 62  ? -13.408 55.037  69.259  1.00 41.95  ? 62  ASP D N   1 
ATOM   12770 C CA  . ASP D 1 62  ? -13.001 56.441  69.282  1.00 48.52  ? 62  ASP D CA  1 
ATOM   12771 C C   . ASP D 1 62  ? -11.506 56.604  69.050  1.00 48.67  ? 62  ASP D C   1 
ATOM   12772 O O   . ASP D 1 62  ? -11.074 57.607  68.470  1.00 46.59  ? 62  ASP D O   1 
ATOM   12773 C CB  . ASP D 1 62  ? -13.389 57.086  70.614  1.00 50.21  ? 62  ASP D CB  1 
ATOM   12774 C CG  . ASP D 1 62  ? -14.873 57.018  70.880  1.00 53.12  ? 62  ASP D CG  1 
ATOM   12775 O OD1 . ASP D 1 62  ? -15.641 57.004  69.900  1.00 64.45  ? 62  ASP D OD1 1 
ATOM   12776 O OD2 . ASP D 1 62  ? -15.274 56.991  72.063  1.00 40.89  ? 62  ASP D OD2 1 
ATOM   12777 N N   . GLN D 1 63  ? -10.704 55.640  69.500  1.00 44.02  ? 63  GLN D N   1 
ATOM   12778 C CA  . GLN D 1 63  ? -9.258  55.768  69.366  1.00 44.81  ? 63  GLN D CA  1 
ATOM   12779 C C   . GLN D 1 63  ? -8.792  55.454  67.948  1.00 52.22  ? 63  GLN D C   1 
ATOM   12780 O O   . GLN D 1 63  ? -7.946  56.172  67.403  1.00 55.03  ? 63  GLN D O   1 
ATOM   12781 C CB  . GLN D 1 63  ? -8.571  54.880  70.402  1.00 44.37  ? 63  GLN D CB  1 
ATOM   12782 C CG  . GLN D 1 63  ? -8.933  55.295  71.825  1.00 42.37  ? 63  GLN D CG  1 
ATOM   12783 C CD  . GLN D 1 63  ? -8.502  54.298  72.879  1.00 47.76  ? 63  GLN D CD  1 
ATOM   12784 O OE1 . GLN D 1 63  ? -7.476  54.476  73.536  1.00 46.47  ? 63  GLN D OE1 1 
ATOM   12785 N NE2 . GLN D 1 63  ? -9.293  53.248  73.059  1.00 46.13  ? 63  GLN D NE2 1 
ATOM   12786 N N   . ILE D 1 64  ? -9.338  54.405  67.326  1.00 50.40  ? 64  ILE D N   1 
ATOM   12787 C CA  . ILE D 1 64  ? -8.997  54.118  65.934  1.00 49.63  ? 64  ILE D CA  1 
ATOM   12788 C C   . ILE D 1 64  ? -9.433  55.267  65.035  1.00 50.19  ? 64  ILE D C   1 
ATOM   12789 O O   . ILE D 1 64  ? -8.722  55.642  64.094  1.00 51.95  ? 64  ILE D O   1 
ATOM   12790 C CB  . ILE D 1 64  ? -9.612  52.780  65.480  1.00 50.07  ? 64  ILE D CB  1 
ATOM   12791 C CG1 . ILE D 1 64  ? -9.329  51.675  66.498  1.00 49.31  ? 64  ILE D CG1 1 
ATOM   12792 C CG2 . ILE D 1 64  ? -9.070  52.378  64.117  1.00 52.76  ? 64  ILE D CG2 1 
ATOM   12793 C CD1 . ILE D 1 64  ? -10.363 50.570  66.488  1.00 48.87  ? 64  ILE D CD1 1 
ATOM   12794 N N   . GLN D 1 65  ? -10.609 55.838  65.304  1.00 49.93  ? 65  GLN D N   1 
ATOM   12795 C CA  . GLN D 1 65  ? -11.069 56.995  64.541  1.00 51.09  ? 65  GLN D CA  1 
ATOM   12796 C C   . GLN D 1 65  ? -10.114 58.171  64.702  1.00 49.62  ? 65  GLN D C   1 
ATOM   12797 O O   . GLN D 1 65  ? -9.762  58.838  63.722  1.00 58.68  ? 65  GLN D O   1 
ATOM   12798 C CB  . GLN D 1 65  ? -12.478 57.388  64.984  1.00 55.05  ? 65  GLN D CB  1 
ATOM   12799 C CG  . GLN D 1 65  ? -13.529 56.310  64.781  1.00 54.63  ? 65  GLN D CG  1 
ATOM   12800 C CD  . GLN D 1 65  ? -14.932 56.875  64.719  1.00 63.19  ? 65  GLN D CD  1 
ATOM   12801 O OE1 . GLN D 1 65  ? -15.223 57.914  65.313  1.00 79.06  ? 65  GLN D OE1 1 
ATOM   12802 N NE2 . GLN D 1 65  ? -15.818 56.184  64.011  1.00 67.18  ? 65  GLN D NE2 1 
ATOM   12803 N N   . GLU D 1 66  ? -9.684  58.442  65.937  1.00 54.77  ? 66  GLU D N   1 
ATOM   12804 C CA  . GLU D 1 66  ? -8.767  59.552  66.173  1.00 53.34  ? 66  GLU D CA  1 
ATOM   12805 C C   . GLU D 1 66  ? -7.421  59.310  65.503  1.00 53.91  ? 66  GLU D C   1 
ATOM   12806 O O   . GLU D 1 66  ? -6.795  60.249  64.998  1.00 55.70  ? 66  GLU D O   1 
ATOM   12807 C CB  . GLU D 1 66  ? -8.590  59.782  67.673  1.00 46.88  ? 66  GLU D CB  1 
ATOM   12808 C CG  . GLU D 1 66  ? -8.022  61.150  68.016  1.00 55.52  ? 66  GLU D CG  1 
ATOM   12809 C CD  . GLU D 1 66  ? -7.827  61.348  69.505  1.00 64.10  ? 66  GLU D CD  1 
ATOM   12810 O OE1 . GLU D 1 66  ? -8.394  60.559  70.290  1.00 64.37  ? 66  GLU D OE1 1 
ATOM   12811 O OE2 . GLU D 1 66  ? -7.108  62.294  69.891  1.00 65.26  ? 66  GLU D OE2 1 
ATOM   12812 N N   . TYR D 1 67  ? -6.954  58.058  65.500  1.00 53.73  ? 67  TYR D N   1 
ATOM   12813 C CA  . TYR D 1 67  ? -5.706  57.737  64.815  1.00 61.69  ? 67  TYR D CA  1 
ATOM   12814 C C   . TYR D 1 67  ? -5.839  57.921  63.308  1.00 61.81  ? 67  TYR D C   1 
ATOM   12815 O O   . TYR D 1 67  ? -4.904  58.390  62.649  1.00 61.04  ? 67  TYR D O   1 
ATOM   12816 C CB  . TYR D 1 67  ? -5.279  56.307  65.149  1.00 53.48  ? 67  TYR D CB  1 
ATOM   12817 C CG  . TYR D 1 67  ? -4.443  56.198  66.403  1.00 52.70  ? 67  TYR D CG  1 
ATOM   12818 C CD1 . TYR D 1 67  ? -3.146  56.689  66.443  1.00 53.87  ? 67  TYR D CD1 1 
ATOM   12819 C CD2 . TYR D 1 67  ? -4.953  55.605  67.550  1.00 52.73  ? 67  TYR D CD2 1 
ATOM   12820 C CE1 . TYR D 1 67  ? -2.380  56.592  67.591  1.00 53.28  ? 67  TYR D CE1 1 
ATOM   12821 C CE2 . TYR D 1 67  ? -4.196  55.504  68.702  1.00 53.47  ? 67  TYR D CE2 1 
ATOM   12822 C CZ  . TYR D 1 67  ? -2.909  55.999  68.717  1.00 51.48  ? 67  TYR D CZ  1 
ATOM   12823 O OH  . TYR D 1 67  ? -2.151  55.900  69.860  1.00 54.28  ? 67  TYR D OH  1 
ATOM   12824 N N   . ALA D 1 68  ? -6.996  57.561  62.745  1.00 56.69  ? 68  ALA D N   1 
ATOM   12825 C CA  . ALA D 1 68  ? -7.188  57.670  61.303  1.00 56.81  ? 68  ALA D CA  1 
ATOM   12826 C C   . ALA D 1 68  ? -7.365  59.116  60.860  1.00 60.59  ? 68  ALA D C   1 
ATOM   12827 O O   . ALA D 1 68  ? -7.001  59.464  59.730  1.00 69.06  ? 68  ALA D O   1 
ATOM   12828 C CB  . ALA D 1 68  ? -8.394  56.837  60.867  1.00 56.53  ? 68  ALA D CB  1 
ATOM   12829 N N   . GLN D 1 69  ? -7.913  59.966  61.723  1.00 56.96  ? 69  GLN D N   1 
ATOM   12830 C CA  . GLN D 1 69  ? -8.175  61.357  61.378  1.00 55.60  ? 69  GLN D CA  1 
ATOM   12831 C C   . GLN D 1 69  ? -6.931  62.233  61.455  1.00 64.46  ? 69  GLN D C   1 
ATOM   12832 O O   . GLN D 1 69  ? -7.008  63.418  61.113  1.00 76.18  ? 69  GLN D O   1 
ATOM   12833 C CB  . GLN D 1 69  ? -9.261  61.926  62.295  1.00 53.39  ? 69  GLN D CB  1 
ATOM   12834 C CG  . GLN D 1 69  ? -10.623 62.068  61.636  1.00 59.53  ? 69  GLN D CG  1 
ATOM   12835 C CD  . GLN D 1 69  ? -11.705 62.479  62.617  1.00 68.18  ? 69  GLN D CD  1 
ATOM   12836 O OE1 . GLN D 1 69  ? -11.813 63.647  62.989  1.00 63.32  ? 69  GLN D OE1 1 
ATOM   12837 N NE2 . GLN D 1 69  ? -12.510 61.514  63.047  1.00 65.92  ? 69  GLN D NE2 1 
ATOM   12838 N N   . GLY D 1 70  ? -5.800  61.688  61.900  1.00 67.77  ? 70  GLY D N   1 
ATOM   12839 C CA  . GLY D 1 70  ? -4.603  62.472  62.107  1.00 67.48  ? 70  GLY D CA  1 
ATOM   12840 C C   . GLY D 1 70  ? -4.601  63.290  63.378  1.00 66.19  ? 70  GLY D C   1 
ATOM   12841 O O   . GLY D 1 70  ? -3.624  64.006  63.633  1.00 63.27  ? 70  GLY D O   1 
ATOM   12842 N N   . LYS D 1 71  ? -5.662  63.202  64.184  1.00 55.14  ? 71  LYS D N   1 
ATOM   12843 C CA  . LYS D 1 71  ? -5.785  64.023  65.382  1.00 55.71  ? 71  LYS D CA  1 
ATOM   12844 C C   . LYS D 1 71  ? -4.930  63.514  66.535  1.00 57.19  ? 71  LYS D C   1 
ATOM   12845 O O   . LYS D 1 71  ? -4.491  64.314  67.369  1.00 66.97  ? 71  LYS D O   1 
ATOM   12846 C CB  . LYS D 1 71  ? -7.247  64.090  65.825  1.00 58.25  ? 71  LYS D CB  1 
ATOM   12847 C CG  . LYS D 1 71  ? -8.010  65.291  65.302  1.00 58.70  ? 71  LYS D CG  1 
ATOM   12848 C CD  . LYS D 1 71  ? -9.426  64.908  64.905  1.00 51.44  ? 71  LYS D CD  1 
ATOM   12849 C CE  . LYS D 1 71  ? -10.119 66.050  64.185  1.00 61.33  ? 71  LYS D CE  1 
ATOM   12850 N NZ  . LYS D 1 71  ? -9.245  66.664  63.149  1.00 56.93  ? 71  LYS D NZ  1 
ATOM   12851 N N   . ALA D 1 72  ? -4.688  62.206  66.600  1.00 57.26  ? 72  ALA D N   1 
ATOM   12852 C CA  . ALA D 1 72  ? -4.066  61.611  67.776  1.00 54.58  ? 72  ALA D CA  1 
ATOM   12853 C C   . ALA D 1 72  ? -2.652  62.144  67.983  1.00 52.10  ? 72  ALA D C   1 
ATOM   12854 O O   . ALA D 1 72  ? -1.920  62.424  67.029  1.00 54.05  ? 72  ALA D O   1 
ATOM   12855 C CB  . ALA D 1 72  ? -4.036  60.088  67.650  1.00 51.13  ? 72  ALA D CB  1 
ATOM   12856 N N   . LYS D 1 73  ? -2.276  62.288  69.252  1.00 51.00  ? 73  LYS D N   1 
ATOM   12857 C CA  . LYS D 1 73  ? -0.934  62.710  69.649  1.00 52.80  ? 73  LYS D CA  1 
ATOM   12858 C C   . LYS D 1 73  ? -0.360  61.615  70.539  1.00 51.67  ? 73  LYS D C   1 
ATOM   12859 O O   . LYS D 1 73  ? -0.431  61.688  71.767  1.00 50.25  ? 73  LYS D O   1 
ATOM   12860 C CB  . LYS D 1 73  ? -0.964  64.073  70.366  1.00 53.96  ? 73  LYS D CB  1 
ATOM   12861 C CG  . LYS D 1 73  ? -2.157  64.947  70.007  1.00 64.92  ? 73  LYS D CG  1 
ATOM   12862 C CD  . LYS D 1 73  ? -1.968  66.383  70.482  1.00 65.73  ? 73  LYS D CD  1 
ATOM   12863 C CE  . LYS D 1 73  ? -1.237  66.445  71.815  1.00 54.58  ? 73  LYS D CE  1 
ATOM   12864 N NZ  . LYS D 1 73  ? -1.196  67.830  72.358  1.00 49.23  ? 73  LYS D NZ  1 
ATOM   12865 N N   . ASP D 1 74  ? 0.222   60.599  69.908  1.00 59.70  ? 74  ASP D N   1 
ATOM   12866 C CA  . ASP D 1 74  ? 0.832   59.483  70.617  1.00 53.06  ? 74  ASP D CA  1 
ATOM   12867 C C   . ASP D 1 74  ? 2.290   59.828  70.893  1.00 60.62  ? 74  ASP D C   1 
ATOM   12868 O O   . ASP D 1 74  ? 3.047   60.135  69.965  1.00 70.33  ? 74  ASP D O   1 
ATOM   12869 C CB  . ASP D 1 74  ? 0.712   58.199  69.796  1.00 53.95  ? 74  ASP D CB  1 
ATOM   12870 C CG  . ASP D 1 74  ? 1.076   56.951  70.586  1.00 58.07  ? 74  ASP D CG  1 
ATOM   12871 O OD1 . ASP D 1 74  ? 2.084   56.968  71.324  1.00 65.96  ? 74  ASP D OD1 1 
ATOM   12872 O OD2 . ASP D 1 74  ? 0.350   55.942  70.463  1.00 58.25  ? 74  ASP D OD2 1 
ATOM   12873 N N   . VAL D 1 75  ? 2.680   59.785  72.168  1.00 57.43  ? 75  VAL D N   1 
ATOM   12874 C CA  . VAL D 1 75  ? 4.024   60.215  72.536  1.00 60.35  ? 75  VAL D CA  1 
ATOM   12875 C C   . VAL D 1 75  ? 5.072   59.240  72.005  1.00 59.03  ? 75  VAL D C   1 
ATOM   12876 O O   . VAL D 1 75  ? 6.144   59.654  71.546  1.00 64.86  ? 75  VAL D O   1 
ATOM   12877 C CB  . VAL D 1 75  ? 4.123   60.419  74.063  1.00 59.77  ? 75  VAL D CB  1 
ATOM   12878 C CG1 . VAL D 1 75  ? 4.277   59.095  74.809  1.00 53.59  ? 75  VAL D CG1 1 
ATOM   12879 C CG2 . VAL D 1 75  ? 5.266   61.367  74.399  1.00 54.73  ? 75  VAL D CG2 1 
ATOM   12880 N N   . PHE D 1 76  ? 4.781   57.937  72.040  1.00 58.38  ? 76  PHE D N   1 
ATOM   12881 C CA  . PHE D 1 76  ? 5.742   56.956  71.549  1.00 58.55  ? 76  PHE D CA  1 
ATOM   12882 C C   . PHE D 1 76  ? 5.749   56.885  70.027  1.00 60.20  ? 76  PHE D C   1 
ATOM   12883 O O   . PHE D 1 76  ? 6.811   56.721  69.418  1.00 62.34  ? 76  PHE D O   1 
ATOM   12884 C CB  . PHE D 1 76  ? 5.448   55.580  72.145  1.00 57.75  ? 76  PHE D CB  1 
ATOM   12885 C CG  . PHE D 1 76  ? 6.485   54.546  71.813  1.00 67.14  ? 76  PHE D CG  1 
ATOM   12886 C CD1 . PHE D 1 76  ? 7.732   54.577  72.414  1.00 75.42  ? 76  PHE D CD1 1 
ATOM   12887 C CD2 . PHE D 1 76  ? 6.214   53.545  70.895  1.00 73.64  ? 76  PHE D CD2 1 
ATOM   12888 C CE1 . PHE D 1 76  ? 8.691   53.627  72.107  1.00 69.52  ? 76  PHE D CE1 1 
ATOM   12889 C CE2 . PHE D 1 76  ? 7.166   52.592  70.584  1.00 64.58  ? 76  PHE D CE2 1 
ATOM   12890 C CZ  . PHE D 1 76  ? 8.406   52.633  71.191  1.00 68.60  ? 76  PHE D CZ  1 
ATOM   12891 N N   . LEU D 1 77  ? 4.575   56.994  69.399  1.00 59.32  ? 77  LEU D N   1 
ATOM   12892 C CA  . LEU D 1 77  ? 4.522   57.008  67.941  1.00 60.92  ? 77  LEU D CA  1 
ATOM   12893 C C   . LEU D 1 77  ? 5.326   58.167  67.374  1.00 62.62  ? 77  LEU D C   1 
ATOM   12894 O O   . LEU D 1 77  ? 5.920   58.045  66.297  1.00 73.38  ? 77  LEU D O   1 
ATOM   12895 C CB  . LEU D 1 77  ? 3.071   57.080  67.466  1.00 69.75  ? 77  LEU D CB  1 
ATOM   12896 C CG  . LEU D 1 77  ? 2.807   56.794  65.986  1.00 68.36  ? 77  LEU D CG  1 
ATOM   12897 C CD1 . LEU D 1 77  ? 3.229   55.378  65.637  1.00 62.30  ? 77  LEU D CD1 1 
ATOM   12898 C CD2 . LEU D 1 77  ? 1.341   57.020  65.647  1.00 67.57  ? 77  LEU D CD2 1 
ATOM   12899 N N   . GLU D 1 78  ? 5.354   59.298  68.081  1.00 65.18  ? 78  GLU D N   1 
ATOM   12900 C CA  . GLU D 1 78  ? 6.236   60.390  67.688  1.00 67.49  ? 78  GLU D CA  1 
ATOM   12901 C C   . GLU D 1 78  ? 7.697   60.021  67.909  1.00 67.82  ? 78  GLU D C   1 
ATOM   12902 O O   . GLU D 1 78  ? 8.556   60.351  67.085  1.00 70.94  ? 78  GLU D O   1 
ATOM   12903 C CB  . GLU D 1 78  ? 5.877   61.662  68.451  1.00 61.85  ? 78  GLU D CB  1 
ATOM   12904 C CG  . GLU D 1 78  ? 5.937   62.915  67.597  1.00 69.04  ? 78  GLU D CG  1 
ATOM   12905 C CD  . GLU D 1 78  ? 5.117   62.791  66.327  1.00 71.87  ? 78  GLU D CD  1 
ATOM   12906 O OE1 . GLU D 1 78  ? 3.974   62.289  66.400  1.00 75.95  ? 78  GLU D OE1 1 
ATOM   12907 O OE2 . GLU D 1 78  ? 5.620   63.184  65.252  1.00 66.93  ? 78  GLU D OE2 1 
ATOM   12908 N N   . ALA D 1 79  ? 7.994   59.308  68.999  1.00 67.32  ? 79  ALA D N   1 
ATOM   12909 C CA  . ALA D 1 79  ? 9.370   58.940  69.318  1.00 70.07  ? 79  ALA D CA  1 
ATOM   12910 C C   . ALA D 1 79  ? 10.009  58.080  68.237  1.00 73.20  ? 79  ALA D C   1 
ATOM   12911 O O   . ALA D 1 79  ? 11.233  57.908  68.246  1.00 76.39  ? 79  ALA D O   1 
ATOM   12912 C CB  . ALA D 1 79  ? 9.425   58.215  70.662  1.00 67.82  ? 79  ALA D CB  1 
ATOM   12913 N N   . ILE D 1 80  ? 9.216   57.533  67.322  1.00 80.79  ? 80  ILE D N   1 
ATOM   12914 C CA  . ILE D 1 80  ? 9.746   56.866  66.138  1.00 70.27  ? 80  ILE D CA  1 
ATOM   12915 C C   . ILE D 1 80  ? 9.821   57.817  64.955  1.00 71.72  ? 80  ILE D C   1 
ATOM   12916 O O   . ILE D 1 80  ? 10.845  57.894  64.270  1.00 86.02  ? 80  ILE D O   1 
ATOM   12917 C CB  . ILE D 1 80  ? 8.889   55.636  65.783  1.00 69.62  ? 80  ILE D CB  1 
ATOM   12918 C CG1 . ILE D 1 80  ? 8.753   54.699  66.982  1.00 70.94  ? 80  ILE D CG1 1 
ATOM   12919 C CG2 . ILE D 1 80  ? 9.496   54.939  64.586  1.00 72.08  ? 80  ILE D CG2 1 
ATOM   12920 C CD1 . ILE D 1 80  ? 10.061  54.330  67.594  1.00 73.80  ? 80  ILE D CD1 1 
ATOM   12921 N N   . ARG D 1 81  ? 8.729   58.540  64.696  1.00 70.41  ? 81  ARG D N   1 
ATOM   12922 C CA  . ARG D 1 81  ? 8.631   59.375  63.505  1.00 72.79  ? 81  ARG D CA  1 
ATOM   12923 C C   . ARG D 1 81  ? 9.708   60.453  63.462  1.00 73.31  ? 81  ARG D C   1 
ATOM   12924 O O   . ARG D 1 81  ? 10.061  60.920  62.373  1.00 85.92  ? 81  ARG D O   1 
ATOM   12925 C CB  . ARG D 1 81  ? 7.229   59.994  63.438  1.00 70.04  ? 81  ARG D CB  1 
ATOM   12926 C CG  . ARG D 1 81  ? 7.014   61.005  62.324  1.00 74.37  ? 81  ARG D CG  1 
ATOM   12927 C CD  . ARG D 1 81  ? 5.590   61.541  62.323  1.00 73.38  ? 81  ARG D CD  1 
ATOM   12928 N NE  . ARG D 1 81  ? 4.887   61.267  63.571  1.00 81.12  ? 81  ARG D NE  1 
ATOM   12929 C CZ  . ARG D 1 81  ? 3.664   60.758  63.645  1.00 90.09  ? 81  ARG D CZ  1 
ATOM   12930 N NH1 . ARG D 1 81  ? 2.975   60.452  62.558  1.00 92.58  ? 81  ARG D NH1 1 
ATOM   12931 N NH2 . ARG D 1 81  ? 3.116   60.556  64.842  1.00 81.56  ? 81  ARG D NH2 1 
ATOM   12932 N N   . LYS D 1 82  ? 10.256  60.837  64.610  1.00 72.66  ? 82  LYS D N   1 
ATOM   12933 C CA  . LYS D 1 82  ? 11.271  61.876  64.638  1.00 74.16  ? 82  LYS D CA  1 
ATOM   12934 C C   . LYS D 1 82  ? 12.636  61.327  64.232  1.00 81.20  ? 82  LYS D C   1 
ATOM   12935 O O   . LYS D 1 82  ? 12.890  60.120  64.260  1.00 77.12  ? 82  LYS D O   1 
ATOM   12936 C CB  . LYS D 1 82  ? 11.361  62.512  66.028  1.00 72.63  ? 82  LYS D CB  1 
ATOM   12937 C CG  . LYS D 1 82  ? 10.030  62.964  66.615  1.00 72.31  ? 82  LYS D CG  1 
ATOM   12938 C CD  . LYS D 1 82  ? 9.864   64.477  66.597  1.00 84.59  ? 82  LYS D CD  1 
ATOM   12939 C CE  . LYS D 1 82  ? 9.809   65.030  65.181  1.00 88.97  ? 82  LYS D CE  1 
ATOM   12940 N NZ  . LYS D 1 82  ? 9.960   66.510  65.155  1.00 72.02  ? 82  LYS D NZ  1 
ATOM   12941 N N   . ASP D 1 83  ? 13.516  62.248  63.841  1.00 90.13  ? 83  ASP D N   1 
ATOM   12942 C CA  . ASP D 1 83  ? 14.908  61.956  63.532  1.00 81.77  ? 83  ASP D CA  1 
ATOM   12943 C C   . ASP D 1 83  ? 15.698  61.753  64.826  1.00 87.49  ? 83  ASP D C   1 
ATOM   12944 O O   . ASP D 1 83  ? 15.434  62.428  65.824  1.00 88.12  ? 83  ASP D O   1 
ATOM   12945 C CB  . ASP D 1 83  ? 15.520  63.096  62.717  1.00 89.52  ? 83  ASP D CB  1 
ATOM   12946 C CG  . ASP D 1 83  ? 16.859  62.732  62.110  1.00 100.92 ? 83  ASP D CG  1 
ATOM   12947 O OD1 . ASP D 1 83  ? 17.885  62.860  62.811  1.00 102.00 ? 83  ASP D OD1 1 
ATOM   12948 O OD2 . ASP D 1 83  ? 16.885  62.323  60.930  1.00 99.00  ? 83  ASP D OD2 1 
ATOM   12949 N N   . PRO D 1 84  ? 16.654  60.822  64.842  1.00 88.53  ? 84  PRO D N   1 
ATOM   12950 C CA  . PRO D 1 84  ? 17.418  60.569  66.075  1.00 91.21  ? 84  PRO D CA  1 
ATOM   12951 C C   . PRO D 1 84  ? 18.218  61.758  66.573  1.00 89.85  ? 84  PRO D C   1 
ATOM   12952 O O   . PRO D 1 84  ? 18.493  61.832  67.776  1.00 102.79 ? 84  PRO D O   1 
ATOM   12953 C CB  . PRO D 1 84  ? 18.337  59.410  65.678  1.00 87.15  ? 84  PRO D CB  1 
ATOM   12954 C CG  . PRO D 1 84  ? 17.584  58.710  64.635  1.00 90.25  ? 84  PRO D CG  1 
ATOM   12955 C CD  . PRO D 1 84  ? 16.916  59.788  63.829  1.00 88.41  ? 84  PRO D CD  1 
ATOM   12956 N N   . ASP D 1 85  ? 18.621  62.678  65.696  1.00 85.04  ? 85  ASP D N   1 
ATOM   12957 C CA  . ASP D 1 85  ? 19.305  63.872  66.177  1.00 85.81  ? 85  ASP D CA  1 
ATOM   12958 C C   . ASP D 1 85  ? 18.338  64.824  66.869  1.00 89.38  ? 85  ASP D C   1 
ATOM   12959 O O   . ASP D 1 85  ? 18.749  65.603  67.737  1.00 92.08  ? 85  ASP D O   1 
ATOM   12960 C CB  . ASP D 1 85  ? 20.024  64.572  65.024  1.00 99.29  ? 85  ASP D CB  1 
ATOM   12961 C CG  . ASP D 1 85  ? 21.052  63.679  64.352  1.00 98.13  ? 85  ASP D CG  1 
ATOM   12962 O OD1 . ASP D 1 85  ? 22.127  63.455  64.949  1.00 92.42  ? 85  ASP D OD1 1 
ATOM   12963 O OD2 . ASP D 1 85  ? 20.789  63.204  63.227  1.00 94.09  ? 85  ASP D OD2 1 
ATOM   12964 N N   . ASP D 1 86  ? 17.056  64.775  66.501  1.00 96.14  ? 86  ASP D N   1 
ATOM   12965 C CA  . ASP D 1 86  ? 16.050  65.609  67.152  1.00 81.74  ? 86  ASP D CA  1 
ATOM   12966 C C   . ASP D 1 86  ? 15.644  65.068  68.518  1.00 93.42  ? 86  ASP D C   1 
ATOM   12967 O O   . ASP D 1 86  ? 15.185  65.837  69.370  1.00 103.06 ? 86  ASP D O   1 
ATOM   12968 C CB  . ASP D 1 86  ? 14.821  65.742  66.251  1.00 78.20  ? 86  ASP D CB  1 
ATOM   12969 C CG  . ASP D 1 86  ? 15.153  66.337  64.896  1.00 91.25  ? 86  ASP D CG  1 
ATOM   12970 O OD1 . ASP D 1 86  ? 16.289  66.136  64.416  1.00 97.19  ? 86  ASP D OD1 1 
ATOM   12971 O OD2 . ASP D 1 86  ? 14.276  67.004  64.308  1.00 100.41 ? 86  ASP D OD2 1 
ATOM   12972 N N   . LEU D 1 87  ? 15.793  63.764  68.744  1.00 90.97  ? 87  LEU D N   1 
ATOM   12973 C CA  . LEU D 1 87  ? 15.434  63.174  70.025  1.00 81.01  ? 87  LEU D CA  1 
ATOM   12974 C C   . LEU D 1 87  ? 16.435  63.580  71.107  1.00 79.97  ? 87  LEU D C   1 
ATOM   12975 O O   . LEU D 1 87  ? 17.592  63.910  70.833  1.00 77.67  ? 87  LEU D O   1 
ATOM   12976 C CB  . LEU D 1 87  ? 15.365  61.648  69.911  1.00 84.66  ? 87  LEU D CB  1 
ATOM   12977 C CG  . LEU D 1 87  ? 14.235  61.039  69.073  1.00 85.93  ? 87  LEU D CG  1 
ATOM   12978 C CD1 . LEU D 1 87  ? 14.052  59.562  69.402  1.00 73.02  ? 87  LEU D CD1 1 
ATOM   12979 C CD2 . LEU D 1 87  ? 12.930  61.795  69.275  1.00 81.38  ? 87  LEU D CD2 1 
ATOM   12980 N N   . GLU D 1 88  ? 15.971  63.546  72.356  1.00 83.82  ? 88  GLU D N   1 
ATOM   12981 C CA  . GLU D 1 88  ? 16.749  63.971  73.511  1.00 86.67  ? 88  GLU D CA  1 
ATOM   12982 C C   . GLU D 1 88  ? 16.766  62.853  74.549  1.00 82.48  ? 88  GLU D C   1 
ATOM   12983 O O   . GLU D 1 88  ? 15.881  61.997  74.576  1.00 70.95  ? 88  GLU D O   1 
ATOM   12984 C CB  . GLU D 1 88  ? 16.178  65.279  74.102  1.00 87.14  ? 88  GLU D CB  1 
ATOM   12985 C CG  . GLU D 1 88  ? 16.636  65.636  75.512  1.00 92.94  ? 88  GLU D CG  1 
ATOM   12986 C CD  . GLU D 1 88  ? 17.710  66.704  75.533  1.00 92.83  ? 88  GLU D CD  1 
ATOM   12987 O OE1 . GLU D 1 88  ? 18.476  66.802  74.551  1.00 81.60  ? 88  GLU D OE1 1 
ATOM   12988 O OE2 . GLU D 1 88  ? 17.792  67.443  76.537  1.00 83.59  ? 88  GLU D OE2 1 
ATOM   12989 N N   . LYS D 1 89  ? 17.795  62.868  75.403  1.00 86.07  ? 89  LYS D N   1 
ATOM   12990 C CA  . LYS D 1 89  ? 18.012  61.848  76.428  1.00 78.01  ? 89  LYS D CA  1 
ATOM   12991 C C   . LYS D 1 89  ? 16.730  61.430  77.141  1.00 74.36  ? 89  LYS D C   1 
ATOM   12992 O O   . LYS D 1 89  ? 16.570  60.260  77.503  1.00 80.82  ? 89  LYS D O   1 
ATOM   12993 C CB  . LYS D 1 89  ? 19.037  62.340  77.453  1.00 84.14  ? 89  LYS D CB  1 
ATOM   12994 C CG  . LYS D 1 89  ? 20.473  62.307  76.951  1.00 86.15  ? 89  LYS D CG  1 
ATOM   12995 C CD  . LYS D 1 89  ? 21.420  62.979  77.931  1.00 81.21  ? 89  LYS D CD  1 
ATOM   12996 C CE  . LYS D 1 89  ? 21.413  62.268  79.272  1.00 77.24  ? 89  LYS D CE  1 
ATOM   12997 N NZ  . LYS D 1 89  ? 22.333  62.914  80.246  1.00 78.37  ? 89  LYS D NZ  1 
ATOM   12998 N N   . GLU D 1 90  ? 15.808  62.375  77.332  1.00 72.84  ? 90  GLU D N   1 
ATOM   12999 C CA  . GLU D 1 90  ? 14.565  62.084  78.035  1.00 75.46  ? 90  GLU D CA  1 
ATOM   13000 C C   . GLU D 1 90  ? 13.610  61.208  77.231  1.00 79.67  ? 90  GLU D C   1 
ATOM   13001 O O   . GLU D 1 90  ? 12.709  60.602  77.821  1.00 72.50  ? 90  GLU D O   1 
ATOM   13002 C CB  . GLU D 1 90  ? 13.870  63.389  78.418  1.00 79.93  ? 90  GLU D CB  1 
ATOM   13003 C CG  . GLU D 1 90  ? 13.987  63.721  79.887  1.00 74.25  ? 90  GLU D CG  1 
ATOM   13004 C CD  . GLU D 1 90  ? 12.958  62.988  80.718  1.00 74.44  ? 90  GLU D CD  1 
ATOM   13005 O OE1 . GLU D 1 90  ? 11.765  63.033  80.357  1.00 62.32  ? 90  GLU D OE1 1 
ATOM   13006 O OE2 . GLU D 1 90  ? 13.344  62.362  81.729  1.00 78.07  ? 90  GLU D OE2 1 
ATOM   13007 N N   . GLU D 1 91  ? 13.765  61.136  75.909  1.00 85.49  ? 91  GLU D N   1 
ATOM   13008 C CA  . GLU D 1 91  ? 12.926  60.270  75.091  1.00 75.99  ? 91  GLU D CA  1 
ATOM   13009 C C   . GLU D 1 91  ? 13.674  59.068  74.526  1.00 70.70  ? 91  GLU D C   1 
ATOM   13010 O O   . GLU D 1 91  ? 13.073  58.273  73.796  1.00 73.72  ? 91  GLU D O   1 
ATOM   13011 C CB  . GLU D 1 91  ? 12.280  61.070  73.947  1.00 77.81  ? 91  GLU D CB  1 
ATOM   13012 C CG  . GLU D 1 91  ? 13.193  62.082  73.268  1.00 88.22  ? 91  GLU D CG  1 
ATOM   13013 C CD  . GLU D 1 91  ? 12.453  63.283  72.704  1.00 92.25  ? 91  GLU D CD  1 
ATOM   13014 O OE1 . GLU D 1 91  ? 12.919  64.423  72.927  1.00 97.77  ? 91  GLU D OE1 1 
ATOM   13015 O OE2 . GLU D 1 91  ? 11.420  63.094  72.033  1.00 102.00 ? 91  GLU D OE2 1 
ATOM   13016 N N   . VAL D 1 92  ? 14.962  58.908  74.840  1.00 69.19  ? 92  VAL D N   1 
ATOM   13017 C CA  . VAL D 1 92  ? 15.715  57.763  74.328  1.00 71.02  ? 92  VAL D CA  1 
ATOM   13018 C C   . VAL D 1 92  ? 15.311  56.478  75.041  1.00 69.83  ? 92  VAL D C   1 
ATOM   13019 O O   . VAL D 1 92  ? 15.086  55.444  74.402  1.00 70.18  ? 92  VAL D O   1 
ATOM   13020 C CB  . VAL D 1 92  ? 17.229  58.012  74.439  1.00 74.87  ? 92  VAL D CB  1 
ATOM   13021 C CG1 . VAL D 1 92  ? 17.983  57.061  73.530  1.00 75.78  ? 92  VAL D CG1 1 
ATOM   13022 C CG2 . VAL D 1 92  ? 17.552  59.426  74.039  1.00 74.37  ? 92  VAL D CG2 1 
ATOM   13023 N N   . GLU D 1 93  ? 15.219  56.517  76.373  1.00 72.65  ? 93  GLU D N   1 
ATOM   13024 C CA  . GLU D 1 93  ? 14.938  55.295  77.120  1.00 70.87  ? 93  GLU D CA  1 
ATOM   13025 C C   . GLU D 1 93  ? 13.541  54.757  76.851  1.00 71.31  ? 93  GLU D C   1 
ATOM   13026 O O   . GLU D 1 93  ? 13.284  53.578  77.117  1.00 69.13  ? 93  GLU D O   1 
ATOM   13027 C CB  . GLU D 1 93  ? 15.126  55.522  78.620  1.00 70.03  ? 93  GLU D CB  1 
ATOM   13028 C CG  . GLU D 1 93  ? 14.143  56.492  79.250  1.00 78.83  ? 93  GLU D CG  1 
ATOM   13029 C CD  . GLU D 1 93  ? 14.719  57.884  79.387  1.00 83.83  ? 93  GLU D CD  1 
ATOM   13030 O OE1 . GLU D 1 93  ? 15.960  58.009  79.448  1.00 84.12  ? 93  GLU D OE1 1 
ATOM   13031 O OE2 . GLU D 1 93  ? 13.929  58.848  79.459  1.00 76.86  ? 93  GLU D OE2 1 
ATOM   13032 N N   . LYS D 1 94  ? 12.637  55.591  76.334  1.00 75.27  ? 94  LYS D N   1 
ATOM   13033 C CA  . LYS D 1 94  ? 11.343  55.084  75.892  1.00 65.98  ? 94  LYS D CA  1 
ATOM   13034 C C   . LYS D 1 94  ? 11.520  54.052  74.789  1.00 73.82  ? 94  LYS D C   1 
ATOM   13035 O O   . LYS D 1 94  ? 10.735  53.102  74.686  1.00 71.30  ? 94  LYS D O   1 
ATOM   13036 C CB  . LYS D 1 94  ? 10.454  56.231  75.400  1.00 61.71  ? 94  LYS D CB  1 
ATOM   13037 C CG  . LYS D 1 94  ? 9.716   57.036  76.479  1.00 59.52  ? 94  LYS D CG  1 
ATOM   13038 C CD  . LYS D 1 94  ? 10.555  57.302  77.722  1.00 61.18  ? 94  LYS D CD  1 
ATOM   13039 C CE  . LYS D 1 94  ? 9.845   58.232  78.688  1.00 57.74  ? 94  LYS D CE  1 
ATOM   13040 N NZ  . LYS D 1 94  ? 9.357   59.465  78.011  1.00 57.45  ? 94  LYS D NZ  1 
ATOM   13041 N N   . LEU D 1 95  ? 12.548  54.226  73.959  1.00 77.16  ? 95  LEU D N   1 
ATOM   13042 C CA  . LEU D 1 95  ? 12.819  53.276  72.889  1.00 68.37  ? 95  LEU D CA  1 
ATOM   13043 C C   . LEU D 1 95  ? 13.435  51.989  73.422  1.00 77.27  ? 95  LEU D C   1 
ATOM   13044 O O   . LEU D 1 95  ? 13.037  50.889  73.022  1.00 79.22  ? 95  LEU D O   1 
ATOM   13045 C CB  . LEU D 1 95  ? 13.738  53.919  71.854  1.00 70.65  ? 95  LEU D CB  1 
ATOM   13046 C CG  . LEU D 1 95  ? 13.023  54.328  70.575  1.00 72.54  ? 95  LEU D CG  1 
ATOM   13047 C CD1 . LEU D 1 95  ? 14.013  54.376  69.441  1.00 73.49  ? 95  LEU D CD1 1 
ATOM   13048 C CD2 . LEU D 1 95  ? 11.918  53.330  70.294  1.00 77.41  ? 95  LEU D CD2 1 
ATOM   13049 N N   . ILE D 1 96  ? 14.416  52.105  74.319  1.00 76.03  ? 96  ILE D N   1 
ATOM   13050 C CA  . ILE D 1 96  ? 15.107  50.916  74.806  1.00 76.47  ? 96  ILE D CA  1 
ATOM   13051 C C   . ILE D 1 96  ? 14.183  50.079  75.683  1.00 86.44  ? 96  ILE D C   1 
ATOM   13052 O O   . ILE D 1 96  ? 14.203  48.845  75.623  1.00 88.14  ? 96  ILE D O   1 
ATOM   13053 C CB  . ILE D 1 96  ? 16.412  51.309  75.530  1.00 72.36  ? 96  ILE D CB  1 
ATOM   13054 C CG1 . ILE D 1 96  ? 16.145  51.919  76.909  1.00 72.03  ? 96  ILE D CG1 1 
ATOM   13055 C CG2 . ILE D 1 96  ? 17.223  52.273  74.676  1.00 74.26  ? 96  ILE D CG2 1 
ATOM   13056 C CD1 . ILE D 1 96  ? 16.359  50.962  78.067  1.00 74.14  ? 96  ILE D CD1 1 
ATOM   13057 N N   . GLU D 1 97  ? 13.347  50.730  76.499  1.00 81.31  ? 97  GLU D N   1 
ATOM   13058 C CA  . GLU D 1 97  ? 12.452  49.991  77.382  1.00 81.92  ? 97  GLU D CA  1 
ATOM   13059 C C   . GLU D 1 97  ? 11.303  49.339  76.627  1.00 72.26  ? 97  GLU D C   1 
ATOM   13060 O O   . GLU D 1 97  ? 10.677  48.413  77.156  1.00 66.19  ? 97  GLU D O   1 
ATOM   13061 C CB  . GLU D 1 97  ? 11.907  50.910  78.476  1.00 84.29  ? 97  GLU D CB  1 
ATOM   13062 C CG  . GLU D 1 97  ? 11.597  50.189  79.783  1.00 100.87 ? 97  GLU D CG  1 
ATOM   13063 C CD  . GLU D 1 97  ? 12.721  50.312  80.795  1.00 111.84 ? 97  GLU D CD  1 
ATOM   13064 O OE1 . GLU D 1 97  ? 13.688  51.057  80.527  1.00 114.07 ? 97  GLU D OE1 1 
ATOM   13065 O OE2 . GLU D 1 97  ? 12.634  49.662  81.861  1.00 104.40 ? 97  GLU D OE2 1 
ATOM   13066 N N   . PHE D 1 98  ? 11.009  49.798  75.409  1.00 68.72  ? 98  PHE D N   1 
ATOM   13067 C CA  . PHE D 1 98  ? 9.978   49.145  74.613  1.00 69.87  ? 98  PHE D CA  1 
ATOM   13068 C C   . PHE D 1 98  ? 10.524  47.922  73.888  1.00 68.21  ? 98  PHE D C   1 
ATOM   13069 O O   . PHE D 1 98  ? 9.833   46.904  73.782  1.00 64.93  ? 98  PHE D O   1 
ATOM   13070 C CB  . PHE D 1 98  ? 9.369   50.127  73.614  1.00 63.19  ? 98  PHE D CB  1 
ATOM   13071 C CG  . PHE D 1 98  ? 7.965   49.777  73.213  1.00 64.78  ? 98  PHE D CG  1 
ATOM   13072 C CD1 . PHE D 1 98  ? 6.930   49.862  74.130  1.00 65.01  ? 98  PHE D CD1 1 
ATOM   13073 C CD2 . PHE D 1 98  ? 7.682   49.340  71.928  1.00 70.92  ? 98  PHE D CD2 1 
ATOM   13074 C CE1 . PHE D 1 98  ? 5.638   49.533  73.771  1.00 74.22  ? 98  PHE D CE1 1 
ATOM   13075 C CE2 . PHE D 1 98  ? 6.391   49.007  71.562  1.00 75.89  ? 98  PHE D CE2 1 
ATOM   13076 C CZ  . PHE D 1 98  ? 5.367   49.104  72.486  1.00 88.28  ? 98  PHE D CZ  1 
ATOM   13077 N N   . THR D 1 99  ? 11.755  47.998  73.380  1.00 72.15  ? 99  THR D N   1 
ATOM   13078 C CA  . THR D 1 99  ? 12.357  46.826  72.755  1.00 69.78  ? 99  THR D CA  1 
ATOM   13079 C C   . THR D 1 99  ? 12.804  45.811  73.797  1.00 71.43  ? 99  THR D C   1 
ATOM   13080 O O   . THR D 1 99  ? 12.745  44.600  73.553  1.00 80.53  ? 99  THR D O   1 
ATOM   13081 C CB  . THR D 1 99  ? 13.531  47.236  71.870  1.00 74.52  ? 99  THR D CB  1 
ATOM   13082 O OG1 . THR D 1 99  ? 14.242  48.318  72.487  1.00 75.19  ? 99  THR D OG1 1 
ATOM   13083 C CG2 . THR D 1 99  ? 13.034  47.660  70.501  1.00 72.74  ? 99  THR D CG2 1 
ATOM   13084 N N   . LYS D 1 100 ? 13.259  46.285  74.961  1.00 69.41  ? 100 LYS D N   1 
ATOM   13085 C CA  . LYS D 1 100 ? 13.555  45.377  76.063  1.00 70.78  ? 100 LYS D CA  1 
ATOM   13086 C C   . LYS D 1 100 ? 12.309  44.615  76.496  1.00 73.78  ? 100 LYS D C   1 
ATOM   13087 O O   . LYS D 1 100 ? 12.405  43.464  76.937  1.00 74.23  ? 100 LYS D O   1 
ATOM   13088 C CB  . LYS D 1 100 ? 14.174  46.168  77.227  1.00 69.03  ? 100 LYS D CB  1 
ATOM   13089 C CG  . LYS D 1 100 ? 14.134  45.518  78.623  1.00 68.17  ? 100 LYS D CG  1 
ATOM   13090 C CD  . LYS D 1 100 ? 12.804  45.742  79.354  1.00 89.78  ? 100 LYS D CD  1 
ATOM   13091 C CE  . LYS D 1 100 ? 12.945  45.675  80.856  1.00 81.33  ? 100 LYS D CE  1 
ATOM   13092 N NZ  . LYS D 1 100 ? 11.599  45.750  81.483  1.00 61.90  ? 100 LYS D NZ  1 
ATOM   13093 N N   . LEU D 1 101 ? 11.133  45.234  76.372  1.00 78.71  ? 101 LEU D N   1 
ATOM   13094 C CA  . LEU D 1 101 ? 9.912   44.634  76.905  1.00 66.86  ? 101 LEU D CA  1 
ATOM   13095 C C   . LEU D 1 101 ? 9.431   43.480  76.028  1.00 68.96  ? 101 LEU D C   1 
ATOM   13096 O O   . LEU D 1 101 ? 9.234   42.360  76.513  1.00 80.11  ? 101 LEU D O   1 
ATOM   13097 C CB  . LEU D 1 101 ? 8.827   45.710  77.049  1.00 65.10  ? 101 LEU D CB  1 
ATOM   13098 C CG  . LEU D 1 101 ? 7.441   45.277  77.549  1.00 64.25  ? 101 LEU D CG  1 
ATOM   13099 C CD1 . LEU D 1 101 ? 6.833   46.407  78.350  1.00 56.84  ? 101 LEU D CD1 1 
ATOM   13100 C CD2 . LEU D 1 101 ? 6.495   44.876  76.433  1.00 65.24  ? 101 LEU D CD2 1 
ATOM   13101 N N   . ASN D 1 102 ? 9.258   43.728  74.733  1.00 70.64  ? 102 ASN D N   1 
ATOM   13102 C CA  . ASN D 1 102 ? 8.769   42.718  73.806  1.00 70.20  ? 102 ASN D CA  1 
ATOM   13103 C C   . ASN D 1 102 ? 9.879   41.841  73.260  1.00 71.04  ? 102 ASN D C   1 
ATOM   13104 O O   . ASN D 1 102 ? 9.736   41.296  72.162  1.00 71.72  ? 102 ASN D O   1 
ATOM   13105 C CB  . ASN D 1 102 ? 8.009   43.375  72.651  1.00 67.87  ? 102 ASN D CB  1 
ATOM   13106 C CG  . ASN D 1 102 ? 7.092   44.492  73.106  1.00 71.30  ? 102 ASN D CG  1 
ATOM   13107 O OD1 . ASN D 1 102 ? 7.544   45.568  73.491  1.00 68.82  ? 102 ASN D OD1 1 
ATOM   13108 N ND2 . ASN D 1 102 ? 5.789   44.240  73.060  1.00 62.67  ? 102 ASN D ND2 1 
ATOM   13109 N N   . TYR D 1 103 ? 10.968  41.708  74.019  1.00 72.49  ? 103 TYR D N   1 
ATOM   13110 C CA  . TYR D 1 103 ? 12.182  41.046  73.554  1.00 73.82  ? 103 TYR D CA  1 
ATOM   13111 C C   . TYR D 1 103 ? 11.905  39.632  73.056  1.00 76.74  ? 103 TYR D C   1 
ATOM   13112 O O   . TYR D 1 103 ? 12.076  39.330  71.870  1.00 78.20  ? 103 TYR D O   1 
ATOM   13113 C CB  . TYR D 1 103 ? 13.196  41.027  74.701  1.00 80.73  ? 103 TYR D CB  1 
ATOM   13114 C CG  . TYR D 1 103 ? 14.628  41.290  74.302  1.00 80.95  ? 103 TYR D CG  1 
ATOM   13115 C CD1 . TYR D 1 103 ? 15.065  41.050  73.008  1.00 82.72  ? 103 TYR D CD1 1 
ATOM   13116 C CD2 . TYR D 1 103 ? 15.551  41.745  75.230  1.00 75.19  ? 103 TYR D CD2 1 
ATOM   13117 C CE1 . TYR D 1 103 ? 16.378  41.269  72.653  1.00 80.39  ? 103 TYR D CE1 1 
ATOM   13118 C CE2 . TYR D 1 103 ? 16.866  41.977  74.877  1.00 77.60  ? 103 TYR D CE2 1 
ATOM   13119 C CZ  . TYR D 1 103 ? 17.273  41.742  73.586  1.00 87.14  ? 103 TYR D CZ  1 
ATOM   13120 O OH  . TYR D 1 103 ? 18.576  41.968  73.216  1.00 90.00  ? 103 TYR D OH  1 
ATOM   13121 N N   . GLU D 1 104 ? 11.459  38.754  73.953  1.00 78.30  ? 104 GLU D N   1 
ATOM   13122 C CA  . GLU D 1 104 ? 11.365  37.323  73.658  1.00 80.33  ? 104 GLU D CA  1 
ATOM   13123 C C   . GLU D 1 104 ? 10.023  36.987  73.003  1.00 83.35  ? 104 GLU D C   1 
ATOM   13124 O O   . GLU D 1 104 ? 9.197   36.250  73.539  1.00 75.62  ? 104 GLU D O   1 
ATOM   13125 C CB  . GLU D 1 104 ? 11.579  36.518  74.934  1.00 72.46  ? 104 GLU D CB  1 
ATOM   13126 C CG  . GLU D 1 104 ? 12.554  37.157  75.909  1.00 75.23  ? 104 GLU D CG  1 
ATOM   13127 C CD  . GLU D 1 104 ? 12.126  37.003  77.355  1.00 73.79  ? 104 GLU D CD  1 
ATOM   13128 O OE1 . GLU D 1 104 ? 12.295  35.896  77.909  1.00 71.57  ? 104 GLU D OE1 1 
ATOM   13129 O OE2 . GLU D 1 104 ? 11.621  37.986  77.938  1.00 69.00  ? 104 GLU D OE2 1 
ATOM   13130 N N   . LYS D 1 105 ? 9.825   37.536  71.806  1.00 81.43  ? 105 LYS D N   1 
ATOM   13131 C CA  . LYS D 1 105 ? 8.598   37.296  71.066  1.00 79.23  ? 105 LYS D CA  1 
ATOM   13132 C C   . LYS D 1 105 ? 8.914   36.953  69.617  1.00 74.13  ? 105 LYS D C   1 
ATOM   13133 O O   . LYS D 1 105 ? 9.849   37.515  69.032  1.00 74.95  ? 105 LYS D O   1 
ATOM   13134 C CB  . LYS D 1 105 ? 7.676   38.522  71.130  1.00 78.58  ? 105 LYS D CB  1 
ATOM   13135 C CG  . LYS D 1 105 ? 7.077   38.747  72.510  1.00 66.66  ? 105 LYS D CG  1 
ATOM   13136 C CD  . LYS D 1 105 ? 6.279   40.035  72.593  1.00 64.67  ? 105 LYS D CD  1 
ATOM   13137 C CE  . LYS D 1 105 ? 5.590   40.146  73.944  1.00 65.81  ? 105 LYS D CE  1 
ATOM   13138 N NZ  . LYS D 1 105 ? 4.798   41.399  74.076  1.00 64.03  ? 105 LYS D NZ  1 
ATOM   13139 N N   . PRO D 1 106 ? 8.150   36.039  69.009  1.00 77.47  ? 106 PRO D N   1 
ATOM   13140 C CA  . PRO D 1 106 ? 8.415   35.660  67.613  1.00 88.48  ? 106 PRO D CA  1 
ATOM   13141 C C   . PRO D 1 106 ? 8.093   36.750  66.604  1.00 84.68  ? 106 PRO D C   1 
ATOM   13142 O O   . PRO D 1 106 ? 8.265   36.522  65.401  1.00 83.60  ? 106 PRO D O   1 
ATOM   13143 C CB  . PRO D 1 106 ? 7.519   34.426  67.405  1.00 83.57  ? 106 PRO D CB  1 
ATOM   13144 C CG  . PRO D 1 106 ? 7.096   33.995  68.783  1.00 76.95  ? 106 PRO D CG  1 
ATOM   13145 C CD  . PRO D 1 106 ? 7.074   35.235  69.609  1.00 72.12  ? 106 PRO D CD  1 
ATOM   13146 N N   . ILE D 1 107 ? 7.619   37.911  67.047  1.00 74.19  ? 107 ILE D N   1 
ATOM   13147 C CA  . ILE D 1 107 ? 7.561   39.083  66.181  1.00 80.42  ? 107 ILE D CA  1 
ATOM   13148 C C   . ILE D 1 107 ? 8.803   39.949  66.357  1.00 80.87  ? 107 ILE D C   1 
ATOM   13149 O O   . ILE D 1 107 ? 9.295   40.543  65.394  1.00 84.53  ? 107 ILE D O   1 
ATOM   13150 C CB  . ILE D 1 107 ? 6.264   39.879  66.436  1.00 73.80  ? 107 ILE D CB  1 
ATOM   13151 C CG1 . ILE D 1 107 ? 6.268   40.509  67.831  1.00 69.97  ? 107 ILE D CG1 1 
ATOM   13152 C CG2 . ILE D 1 107 ? 5.048   38.981  66.257  1.00 83.46  ? 107 ILE D CG2 1 
ATOM   13153 C CD1 . ILE D 1 107 ? 4.947   41.130  68.227  1.00 66.86  ? 107 ILE D CD1 1 
ATOM   13154 N N   . TYR D 1 108 ? 9.329   40.024  67.577  1.00 75.62  ? 108 TYR D N   1 
ATOM   13155 C CA  . TYR D 1 108 ? 10.618  40.662  67.839  1.00 75.35  ? 108 TYR D CA  1 
ATOM   13156 C C   . TYR D 1 108 ? 11.748  39.644  67.768  1.00 85.47  ? 108 TYR D C   1 
ATOM   13157 O O   . TYR D 1 108 ? 12.580  39.534  68.668  1.00 92.91  ? 108 TYR D O   1 
ATOM   13158 C CB  . TYR D 1 108 ? 10.598  41.354  69.195  1.00 77.54  ? 108 TYR D CB  1 
ATOM   13159 C CG  . TYR D 1 108 ? 9.986   42.733  69.189  1.00 75.52  ? 108 TYR D CG  1 
ATOM   13160 C CD1 . TYR D 1 108 ? 8.712   42.949  68.684  1.00 75.17  ? 108 TYR D CD1 1 
ATOM   13161 C CD2 . TYR D 1 108 ? 10.685  43.821  69.691  1.00 71.70  ? 108 TYR D CD2 1 
ATOM   13162 C CE1 . TYR D 1 108 ? 8.151   44.209  68.679  1.00 70.42  ? 108 TYR D CE1 1 
ATOM   13163 C CE2 . TYR D 1 108 ? 10.133  45.085  69.690  1.00 76.06  ? 108 TYR D CE2 1 
ATOM   13164 C CZ  . TYR D 1 108 ? 8.865   45.274  69.181  1.00 80.86  ? 108 TYR D CZ  1 
ATOM   13165 O OH  . TYR D 1 108 ? 8.308   46.533  69.176  1.00 82.37  ? 108 TYR D OH  1 
ATOM   13166 N N   . ARG D 1 109 ? 11.776  38.882  66.676  1.00 88.07  ? 109 ARG D N   1 
ATOM   13167 C CA  . ARG D 1 109 ? 12.766  37.833  66.474  1.00 87.35  ? 109 ARG D CA  1 
ATOM   13168 C C   . ARG D 1 109 ? 13.778  38.199  65.395  1.00 91.09  ? 109 ARG D C   1 
ATOM   13169 O O   . ARG D 1 109 ? 14.486  37.323  64.888  1.00 90.82  ? 109 ARG D O   1 
ATOM   13170 C CB  . ARG D 1 109 ? 12.072  36.515  66.129  1.00 82.14  ? 109 ARG D CB  1 
ATOM   13171 C CG  . ARG D 1 109 ? 11.415  36.504  64.760  1.00 90.48  ? 109 ARG D CG  1 
ATOM   13172 C CD  . ARG D 1 109 ? 11.309  35.093  64.202  1.00 86.81  ? 109 ARG D CD  1 
ATOM   13173 N NE  . ARG D 1 109 ? 12.522  34.666  63.512  1.00 94.81  ? 109 ARG D NE  1 
ATOM   13174 C CZ  . ARG D 1 109 ? 12.988  35.201  62.390  1.00 88.99  ? 109 ARG D CZ  1 
ATOM   13175 N NH1 . ARG D 1 109 ? 12.358  36.192  61.780  1.00 88.11  ? 109 ARG D NH1 1 
ATOM   13176 N NH2 . ARG D 1 109 ? 14.113  34.724  61.864  1.00 91.73  ? 109 ARG D NH2 1 
ATOM   13177 N N   . PHE D 1 110 ? 13.859  39.475  65.030  1.00 87.43  ? 110 PHE D N   1 
ATOM   13178 C CA  . PHE D 1 110 ? 14.808  39.888  64.009  1.00 92.30  ? 110 PHE D CA  1 
ATOM   13179 C C   . PHE D 1 110 ? 16.225  39.831  64.570  1.00 97.51  ? 110 PHE D C   1 
ATOM   13180 O O   . PHE D 1 110 ? 16.454  40.044  65.764  1.00 90.16  ? 110 PHE D O   1 
ATOM   13181 C CB  . PHE D 1 110 ? 14.523  41.308  63.508  1.00 87.77  ? 110 PHE D CB  1 
ATOM   13182 C CG  . PHE D 1 110 ? 13.214  41.474  62.767  1.00 94.65  ? 110 PHE D CG  1 
ATOM   13183 C CD1 . PHE D 1 110 ? 12.085  40.739  63.105  1.00 97.58  ? 110 PHE D CD1 1 
ATOM   13184 C CD2 . PHE D 1 110 ? 13.128  42.361  61.705  1.00 101.27 ? 110 PHE D CD2 1 
ATOM   13185 C CE1 . PHE D 1 110 ? 10.894  40.906  62.419  1.00 93.50  ? 110 PHE D CE1 1 
ATOM   13186 C CE2 . PHE D 1 110 ? 11.938  42.537  61.019  1.00 102.66 ? 110 PHE D CE2 1 
ATOM   13187 C CZ  . PHE D 1 110 ? 10.823  41.803  61.374  1.00 100.22 ? 110 PHE D CZ  1 
ATOM   13188 N N   . GLU D 1 111 ? 17.184  39.543  63.689  1.00 104.95 ? 111 GLU D N   1 
ATOM   13189 C CA  . GLU D 1 111 ? 18.578  39.456  64.107  1.00 103.37 ? 111 GLU D CA  1 
ATOM   13190 C C   . GLU D 1 111 ? 19.139  40.799  64.560  1.00 101.44 ? 111 GLU D C   1 
ATOM   13191 O O   . GLU D 1 111 ? 20.135  40.826  65.289  1.00 101.80 ? 111 GLU D O   1 
ATOM   13192 C CB  . GLU D 1 111 ? 19.424  38.892  62.967  1.00 96.22  ? 111 GLU D CB  1 
ATOM   13193 C CG  . GLU D 1 111 ? 19.858  39.927  61.949  1.00 97.62  ? 111 GLU D CG  1 
ATOM   13194 C CD  . GLU D 1 111 ? 21.007  39.444  61.093  1.00 101.01 ? 111 GLU D CD  1 
ATOM   13195 O OE1 . GLU D 1 111 ? 20.922  38.315  60.568  1.00 102.22 ? 111 GLU D OE1 1 
ATOM   13196 O OE2 . GLU D 1 111 ? 22.002  40.184  60.960  1.00 102.55 ? 111 GLU D OE2 1 
ATOM   13197 N N   . ARG D 1 112 ? 18.524  41.909  64.156  1.00 99.46  ? 112 ARG D N   1 
ATOM   13198 C CA  . ARG D 1 112 ? 18.992  43.238  64.518  1.00 94.22  ? 112 ARG D CA  1 
ATOM   13199 C C   . ARG D 1 112 ? 18.438  43.702  65.860  1.00 93.91  ? 112 ARG D C   1 
ATOM   13200 O O   . ARG D 1 112 ? 18.362  44.910  66.111  1.00 91.21  ? 112 ARG D O   1 
ATOM   13201 C CB  . ARG D 1 112 ? 18.639  44.239  63.413  1.00 91.42  ? 112 ARG D CB  1 
ATOM   13202 C CG  . ARG D 1 112 ? 19.643  45.373  63.267  1.00 92.85  ? 112 ARG D CG  1 
ATOM   13203 C CD  . ARG D 1 112 ? 19.692  45.954  61.862  1.00 94.44  ? 112 ARG D CD  1 
ATOM   13204 N NE  . ARG D 1 112 ? 20.623  47.075  61.794  1.00 95.74  ? 112 ARG D NE  1 
ATOM   13205 C CZ  . ARG D 1 112 ? 21.692  47.131  61.010  1.00 100.10 ? 112 ARG D CZ  1 
ATOM   13206 N NH1 . ARG D 1 112 ? 22.002  46.142  60.193  1.00 107.51 ? 112 ARG D NH1 1 
ATOM   13207 N NH2 . ARG D 1 112 ? 22.466  48.212  61.042  1.00 102.20 ? 112 ARG D NH2 1 
ATOM   13208 N N   . ILE D 1 113 ? 18.039  42.770  66.720  1.00 92.94  ? 113 ILE D N   1 
ATOM   13209 C CA  . ILE D 1 113 ? 17.491  43.084  68.035  1.00 99.76  ? 113 ILE D CA  1 
ATOM   13210 C C   . ILE D 1 113 ? 18.480  42.727  69.148  1.00 101.00 ? 113 ILE D C   1 
ATOM   13211 O O   . ILE D 1 113 ? 18.940  43.602  69.886  1.00 90.33  ? 113 ILE D O   1 
ATOM   13212 C CB  . ILE D 1 113 ? 16.126  42.389  68.246  1.00 111.89 ? 113 ILE D CB  1 
ATOM   13213 C CG1 . ILE D 1 113 ? 15.005  43.125  67.516  1.00 101.29 ? 113 ILE D CG1 1 
ATOM   13214 C CG2 . ILE D 1 113 ? 15.759  42.372  69.696  1.00 105.36 ? 113 ILE D CG2 1 
ATOM   13215 C CD1 . ILE D 1 113 ? 14.458  44.328  68.280  1.00 85.30  ? 113 ILE D CD1 1 
ATOM   13216 N N   . ARG D 1 114 ? 18.842  41.445  69.265  1.00 101.78 ? 114 ARG D N   1 
ATOM   13217 C CA  . ARG D 1 114 ? 19.616  40.993  70.419  1.00 96.47  ? 114 ARG D CA  1 
ATOM   13218 C C   . ARG D 1 114 ? 21.022  41.581  70.427  1.00 93.40  ? 114 ARG D C   1 
ATOM   13219 O O   . ARG D 1 114 ? 21.565  41.892  71.494  1.00 96.64  ? 114 ARG D O   1 
ATOM   13220 C CB  . ARG D 1 114 ? 19.675  39.465  70.452  1.00 100.62 ? 114 ARG D CB  1 
ATOM   13221 C CG  . ARG D 1 114 ? 18.441  38.815  71.062  1.00 87.52  ? 114 ARG D CG  1 
ATOM   13222 C CD  . ARG D 1 114 ? 18.617  38.588  72.555  1.00 84.73  ? 114 ARG D CD  1 
ATOM   13223 N NE  . ARG D 1 114 ? 17.619  37.670  73.092  1.00 83.51  ? 114 ARG D NE  1 
ATOM   13224 C CZ  . ARG D 1 114 ? 17.842  36.387  73.340  1.00 84.16  ? 114 ARG D CZ  1 
ATOM   13225 N NH1 . ARG D 1 114 ? 19.021  35.833  73.109  1.00 88.59  ? 114 ARG D NH1 1 
ATOM   13226 N NH2 . ARG D 1 114 ? 16.858  35.643  73.837  1.00 82.57  ? 114 ARG D NH2 1 
ATOM   13227 N N   . GLU D 1 115 ? 21.630  41.732  69.251  1.00 96.14  ? 115 GLU D N   1 
ATOM   13228 C CA  . GLU D 1 115 ? 22.998  42.237  69.189  1.00 101.32 ? 115 GLU D CA  1 
ATOM   13229 C C   . GLU D 1 115 ? 23.055  43.732  69.483  1.00 96.67  ? 115 GLU D C   1 
ATOM   13230 O O   . GLU D 1 115 ? 24.012  44.215  70.100  1.00 93.93  ? 115 GLU D O   1 
ATOM   13231 C CB  . GLU D 1 115 ? 23.602  41.930  67.818  1.00 96.59  ? 115 GLU D CB  1 
ATOM   13232 C CG  . GLU D 1 115 ? 24.022  40.475  67.626  1.00 99.57  ? 115 GLU D CG  1 
ATOM   13233 C CD  . GLU D 1 115 ? 22.846  39.510  67.588  1.00 96.77  ? 115 GLU D CD  1 
ATOM   13234 O OE1 . GLU D 1 115 ? 21.700  39.965  67.395  1.00 101.37 ? 115 GLU D OE1 1 
ATOM   13235 O OE2 . GLU D 1 115 ? 23.070  38.293  67.757  1.00 97.76  ? 115 GLU D OE2 1 
ATOM   13236 N N   . LEU D 1 116 ? 22.035  44.476  69.054  1.00 97.51  ? 116 LEU D N   1 
ATOM   13237 C CA  . LEU D 1 116 ? 22.052  45.930  69.184  1.00 90.35  ? 116 LEU D CA  1 
ATOM   13238 C C   . LEU D 1 116 ? 21.797  46.384  70.615  1.00 88.26  ? 116 LEU D C   1 
ATOM   13239 O O   . LEU D 1 116 ? 22.423  47.341  71.084  1.00 88.60  ? 116 LEU D O   1 
ATOM   13240 C CB  . LEU D 1 116 ? 21.021  46.560  68.247  1.00 89.16  ? 116 LEU D CB  1 
ATOM   13241 C CG  . LEU D 1 116 ? 21.399  46.739  66.775  1.00 94.16  ? 116 LEU D CG  1 
ATOM   13242 C CD1 . LEU D 1 116 ? 21.692  45.406  66.091  1.00 93.22  ? 116 LEU D CD1 1 
ATOM   13243 C CD2 . LEU D 1 116 ? 20.308  47.505  66.039  1.00 89.92  ? 116 LEU D CD2 1 
ATOM   13244 N N   . MET D 1 117 ? 20.880  45.720  71.319  1.00 86.14  ? 117 MET D N   1 
ATOM   13245 C CA  . MET D 1 117 ? 20.470  46.166  72.645  1.00 87.02  ? 117 MET D CA  1 
ATOM   13246 C C   . MET D 1 117 ? 21.514  45.903  73.721  1.00 87.89  ? 117 MET D C   1 
ATOM   13247 O O   . MET D 1 117 ? 21.393  46.453  74.821  1.00 83.63  ? 117 MET D O   1 
ATOM   13248 C CB  . MET D 1 117 ? 19.154  45.495  73.038  1.00 81.49  ? 117 MET D CB  1 
ATOM   13249 C CG  . MET D 1 117 ? 17.967  46.438  73.050  1.00 82.41  ? 117 MET D CG  1 
ATOM   13250 S SD  . MET D 1 117 ? 18.311  47.932  73.997  1.00 87.10  ? 117 MET D SD  1 
ATOM   13251 C CE  . MET D 1 117 ? 17.523  47.534  75.554  1.00 84.02  ? 117 MET D CE  1 
ATOM   13252 N N   . ASN D 1 118 ? 22.527  45.090  73.439  1.00 100.62 ? 118 ASN D N   1 
ATOM   13253 C CA  . ASN D 1 118 ? 23.537  44.738  74.426  1.00 101.23 ? 118 ASN D CA  1 
ATOM   13254 C C   . ASN D 1 118 ? 24.757  45.648  74.380  1.00 99.47  ? 118 ASN D C   1 
ATOM   13255 O O   . ASN D 1 118 ? 25.794  45.299  74.954  1.00 96.37  ? 118 ASN D O   1 
ATOM   13256 C CB  . ASN D 1 118 ? 23.974  43.283  74.237  1.00 100.09 ? 118 ASN D CB  1 
ATOM   13257 C CG  . ASN D 1 118 ? 22.959  42.296  74.775  1.00 107.43 ? 118 ASN D CG  1 
ATOM   13258 O OD1 . ASN D 1 118 ? 23.132  41.739  75.858  1.00 111.68 ? 118 ASN D OD1 1 
ATOM   13259 N ND2 . ASN D 1 118 ? 21.889  42.077  74.019  1.00 94.49  ? 118 ASN D ND2 1 
ATOM   13260 N N   . LYS D 1 119 ? 24.664  46.796  73.719  1.00 94.40  ? 119 LYS D N   1 
ATOM   13261 C CA  . LYS D 1 119 ? 25.813  47.671  73.550  1.00 95.03  ? 119 LYS D CA  1 
ATOM   13262 C C   . LYS D 1 119 ? 25.749  48.867  74.492  1.00 104.75 ? 119 LYS D C   1 
ATOM   13263 O O   . LYS D 1 119 ? 24.679  49.290  74.936  1.00 100.56 ? 119 LYS D O   1 
ATOM   13264 C CB  . LYS D 1 119 ? 25.927  48.153  72.099  1.00 94.23  ? 119 LYS D CB  1 
ATOM   13265 C CG  . LYS D 1 119 ? 25.921  47.040  71.055  1.00 95.60  ? 119 LYS D CG  1 
ATOM   13266 C CD  . LYS D 1 119 ? 27.132  46.097  71.145  1.00 109.58 ? 119 LYS D CD  1 
ATOM   13267 C CE  . LYS D 1 119 ? 28.425  46.783  71.591  1.00 100.36 ? 119 LYS D CE  1 
ATOM   13268 N NZ  . LYS D 1 119 ? 28.904  47.803  70.622  1.00 101.90 ? 119 LYS D NZ  1 
ATOM   13269 N N   . GLU D 1 120 ? 26.931  49.410  74.790  1.00 101.55 ? 120 GLU D N   1 
ATOM   13270 C CA  . GLU D 1 120 ? 27.034  50.509  75.745  1.00 92.64  ? 120 GLU D CA  1 
ATOM   13271 C C   . GLU D 1 120 ? 26.422  51.789  75.189  1.00 94.95  ? 120 GLU D C   1 
ATOM   13272 O O   . GLU D 1 120 ? 25.634  52.458  75.868  1.00 89.16  ? 120 GLU D O   1 
ATOM   13273 C CB  . GLU D 1 120 ? 28.499  50.722  76.124  1.00 95.38  ? 120 GLU D CB  1 
ATOM   13274 C CG  . GLU D 1 120 ? 28.921  52.171  76.268  1.00 95.81  ? 120 GLU D CG  1 
ATOM   13275 C CD  . GLU D 1 120 ? 30.372  52.301  76.663  1.00 98.64  ? 120 GLU D CD  1 
ATOM   13276 O OE1 . GLU D 1 120 ? 31.211  51.599  76.060  1.00 104.66 ? 120 GLU D OE1 1 
ATOM   13277 O OE2 . GLU D 1 120 ? 30.676  53.100  77.572  1.00 98.47  ? 120 GLU D OE2 1 
ATOM   13278 N N   . LYS D 1 121 ? 26.765  52.145  73.955  1.00 111.07 ? 121 LYS D N   1 
ATOM   13279 C CA  . LYS D 1 121 ? 26.290  53.371  73.333  1.00 109.41 ? 121 LYS D CA  1 
ATOM   13280 C C   . LYS D 1 121 ? 25.451  53.040  72.107  1.00 105.80 ? 121 LYS D C   1 
ATOM   13281 O O   . LYS D 1 121 ? 25.364  51.889  71.670  1.00 106.23 ? 121 LYS D O   1 
ATOM   13282 C CB  . LYS D 1 121 ? 27.457  54.290  72.944  1.00 101.52 ? 121 LYS D CB  1 
ATOM   13283 C CG  . LYS D 1 121 ? 28.297  53.772  71.789  1.00 101.61 ? 121 LYS D CG  1 
ATOM   13284 C CD  . LYS D 1 121 ? 28.257  54.716  70.597  1.00 100.81 ? 121 LYS D CD  1 
ATOM   13285 C CE  . LYS D 1 121 ? 29.039  54.142  69.425  1.00 111.59 ? 121 LYS D CE  1 
ATOM   13286 N NZ  . LYS D 1 121 ? 28.939  54.990  68.207  1.00 104.52 ? 121 LYS D NZ  1 
ATOM   13287 N N   . LEU D 1 122 ? 24.832  54.078  71.552  1.00 96.48  ? 122 LEU D N   1 
ATOM   13288 C CA  . LEU D 1 122 ? 23.968  53.925  70.385  1.00 100.54 ? 122 LEU D CA  1 
ATOM   13289 C C   . LEU D 1 122 ? 24.093  55.191  69.549  1.00 94.54  ? 122 LEU D C   1 
ATOM   13290 O O   . LEU D 1 122 ? 23.540  56.231  69.920  1.00 89.72  ? 122 LEU D O   1 
ATOM   13291 C CB  . LEU D 1 122 ? 22.523  53.680  70.809  1.00 90.96  ? 122 LEU D CB  1 
ATOM   13292 C CG  . LEU D 1 122 ? 22.146  52.346  71.456  1.00 86.92  ? 122 LEU D CG  1 
ATOM   13293 C CD1 . LEU D 1 122 ? 21.480  52.576  72.805  1.00 85.70  ? 122 LEU D CD1 1 
ATOM   13294 C CD2 . LEU D 1 122 ? 21.237  51.542  70.540  1.00 92.85  ? 122 LEU D CD2 1 
ATOM   13295 N N   . ASN D 1 123 ? 24.815  55.109  68.432  1.00 93.90  ? 123 ASN D N   1 
ATOM   13296 C CA  . ASN D 1 123 ? 25.026  56.276  67.588  1.00 107.88 ? 123 ASN D CA  1 
ATOM   13297 C C   . ASN D 1 123 ? 23.779  56.557  66.754  1.00 106.83 ? 123 ASN D C   1 
ATOM   13298 O O   . ASN D 1 123 ? 22.799  55.809  66.784  1.00 93.21  ? 123 ASN D O   1 
ATOM   13299 C CB  . ASN D 1 123 ? 26.255  56.084  66.700  1.00 98.53  ? 123 ASN D CB  1 
ATOM   13300 C CG  . ASN D 1 123 ? 26.221  54.782  65.918  1.00 104.49 ? 123 ASN D CG  1 
ATOM   13301 O OD1 . ASN D 1 123 ? 25.153  54.272  65.571  1.00 97.83  ? 123 ASN D OD1 1 
ATOM   13302 N ND2 . ASN D 1 123 ? 27.397  54.237  65.632  1.00 105.00 ? 123 ASN D ND2 1 
ATOM   13303 N N   . ARG D 1 124 ? 23.827  57.647  65.983  1.00 108.38 ? 124 ARG D N   1 
ATOM   13304 C CA  . ARG D 1 124 ? 22.651  58.094  65.242  1.00 92.94  ? 124 ARG D CA  1 
ATOM   13305 C C   . ARG D 1 124 ? 22.135  57.002  64.314  1.00 94.88  ? 124 ARG D C   1 
ATOM   13306 O O   . ARG D 1 124 ? 20.943  56.678  64.322  1.00 93.78  ? 124 ARG D O   1 
ATOM   13307 C CB  . ARG D 1 124 ? 22.983  59.368  64.455  1.00 94.46  ? 124 ARG D CB  1 
ATOM   13308 C CG  . ARG D 1 124 ? 21.842  59.953  63.599  1.00 98.05  ? 124 ARG D CG  1 
ATOM   13309 C CD  . ARG D 1 124 ? 21.814  59.438  62.159  1.00 99.99  ? 124 ARG D CD  1 
ATOM   13310 N NE  . ARG D 1 124 ? 21.056  60.339  61.294  1.00 103.54 ? 124 ARG D NE  1 
ATOM   13311 C CZ  . ARG D 1 124 ? 20.124  59.970  60.426  1.00 96.91  ? 124 ARG D CZ  1 
ATOM   13312 N NH1 . ARG D 1 124 ? 19.836  58.697  60.223  1.00 94.01  ? 124 ARG D NH1 1 
ATOM   13313 N NH2 . ARG D 1 124 ? 19.486  60.905  59.722  1.00 102.66 ? 124 ARG D NH2 1 
ATOM   13314 N N   . GLU D 1 125 ? 23.033  56.390  63.538  1.00 95.82  ? 125 GLU D N   1 
ATOM   13315 C CA  . GLU D 1 125 ? 22.606  55.569  62.409  1.00 96.50  ? 125 GLU D CA  1 
ATOM   13316 C C   . GLU D 1 125 ? 21.881  54.301  62.847  1.00 94.78  ? 125 GLU D C   1 
ATOM   13317 O O   . GLU D 1 125 ? 20.967  53.851  62.149  1.00 94.04  ? 125 GLU D O   1 
ATOM   13318 C CB  . GLU D 1 125 ? 23.805  55.233  61.529  1.00 99.93  ? 125 GLU D CB  1 
ATOM   13319 C CG  . GLU D 1 125 ? 23.938  56.145  60.316  1.00 101.64 ? 125 GLU D CG  1 
ATOM   13320 C CD  . GLU D 1 125 ? 24.271  57.579  60.692  1.00 104.37 ? 125 GLU D CD  1 
ATOM   13321 O OE1 . GLU D 1 125 ? 24.812  57.802  61.797  1.00 109.67 ? 125 GLU D OE1 1 
ATOM   13322 O OE2 . GLU D 1 125 ? 23.971  58.489  59.890  1.00 108.16 ? 125 GLU D OE2 1 
ATOM   13323 N N   . GLU D 1 126 ? 22.267  53.701  63.974  1.00 94.22  ? 126 GLU D N   1 
ATOM   13324 C CA  . GLU D 1 126 ? 21.540  52.541  64.470  1.00 98.58  ? 126 GLU D CA  1 
ATOM   13325 C C   . GLU D 1 126 ? 20.345  52.906  65.341  1.00 97.50  ? 126 GLU D C   1 
ATOM   13326 O O   . GLU D 1 126 ? 19.570  52.012  65.698  1.00 87.61  ? 126 GLU D O   1 
ATOM   13327 C CB  . GLU D 1 126 ? 22.462  51.598  65.254  1.00 93.61  ? 126 GLU D CB  1 
ATOM   13328 C CG  . GLU D 1 126 ? 23.620  51.033  64.444  1.00 103.84 ? 126 GLU D CG  1 
ATOM   13329 C CD  . GLU D 1 126 ? 24.345  49.914  65.168  1.00 105.59 ? 126 GLU D CD  1 
ATOM   13330 O OE1 . GLU D 1 126 ? 24.125  49.753  66.387  1.00 99.45  ? 126 GLU D OE1 1 
ATOM   13331 O OE2 . GLU D 1 126 ? 25.126  49.190  64.515  1.00 100.17 ? 126 GLU D OE2 1 
ATOM   13332 N N   . LEU D 1 127 ? 20.177  54.184  65.696  1.00 100.56 ? 127 LEU D N   1 
ATOM   13333 C CA  . LEU D 1 127 ? 18.974  54.596  66.415  1.00 85.21  ? 127 LEU D CA  1 
ATOM   13334 C C   . LEU D 1 127 ? 17.726  54.373  65.571  1.00 86.40  ? 127 LEU D C   1 
ATOM   13335 O O   . LEU D 1 127 ? 16.658  54.047  66.103  1.00 89.61  ? 127 LEU D O   1 
ATOM   13336 C CB  . LEU D 1 127 ? 19.078  56.062  66.839  1.00 84.70  ? 127 LEU D CB  1 
ATOM   13337 C CG  . LEU D 1 127 ? 19.307  56.333  68.331  1.00 83.43  ? 127 LEU D CG  1 
ATOM   13338 C CD1 . LEU D 1 127 ? 20.480  55.540  68.841  1.00 85.12  ? 127 LEU D CD1 1 
ATOM   13339 C CD2 . LEU D 1 127 ? 19.513  57.815  68.612  1.00 83.36  ? 127 LEU D CD2 1 
ATOM   13340 N N   . LEU D 1 128 ? 17.839  54.565  64.251  1.00 90.61  ? 128 LEU D N   1 
ATOM   13341 C CA  . LEU D 1 128 ? 16.702  54.364  63.361  1.00 89.33  ? 128 LEU D CA  1 
ATOM   13342 C C   . LEU D 1 128 ? 16.434  52.889  63.101  1.00 86.93  ? 128 LEU D C   1 
ATOM   13343 O O   . LEU D 1 128 ? 15.281  52.512  62.871  1.00 87.46  ? 128 LEU D O   1 
ATOM   13344 C CB  . LEU D 1 128 ? 16.907  55.096  62.037  1.00 86.87  ? 128 LEU D CB  1 
ATOM   13345 C CG  . LEU D 1 128 ? 17.526  56.491  62.109  1.00 87.65  ? 128 LEU D CG  1 
ATOM   13346 C CD1 . LEU D 1 128 ? 19.042  56.404  61.992  1.00 90.44  ? 128 LEU D CD1 1 
ATOM   13347 C CD2 . LEU D 1 128 ? 16.934  57.492  61.106  1.00 91.19  ? 128 LEU D CD2 1 
ATOM   13348 N N   . ASP D 1 129 ? 17.468  52.043  63.128  1.00 87.03  ? 129 ASP D N   1 
ATOM   13349 C CA  . ASP D 1 129 ? 17.231  50.607  63.023  1.00 87.13  ? 129 ASP D CA  1 
ATOM   13350 C C   . ASP D 1 129 ? 16.320  50.132  64.147  1.00 84.35  ? 129 ASP D C   1 
ATOM   13351 O O   . ASP D 1 129 ? 15.378  49.365  63.915  1.00 83.87  ? 129 ASP D O   1 
ATOM   13352 C CB  . ASP D 1 129 ? 18.557  49.849  63.040  1.00 95.66  ? 129 ASP D CB  1 
ATOM   13353 C CG  . ASP D 1 129 ? 19.455  50.224  61.878  1.00 102.54 ? 129 ASP D CG  1 
ATOM   13354 O OD1 . ASP D 1 129 ? 19.940  51.372  61.849  1.00 99.91  ? 129 ASP D OD1 1 
ATOM   13355 O OD2 . ASP D 1 129 ? 19.662  49.377  60.983  1.00 110.22 ? 129 ASP D OD2 1 
ATOM   13356 N N   . LEU D 1 130 ? 16.574  50.601  65.370  1.00 83.17  ? 130 LEU D N   1 
ATOM   13357 C CA  . LEU D 1 130 ? 15.699  50.283  66.492  1.00 80.51  ? 130 LEU D CA  1 
ATOM   13358 C C   . LEU D 1 130 ? 14.289  50.814  66.251  1.00 78.33  ? 130 LEU D C   1 
ATOM   13359 O O   . LEU D 1 130 ? 13.302  50.124  66.528  1.00 78.49  ? 130 LEU D O   1 
ATOM   13360 C CB  . LEU D 1 130 ? 16.300  50.858  67.778  1.00 79.90  ? 130 LEU D CB  1 
ATOM   13361 C CG  . LEU D 1 130 ? 15.876  50.387  69.174  1.00 77.81  ? 130 LEU D CG  1 
ATOM   13362 C CD1 . LEU D 1 130 ? 16.820  50.967  70.212  1.00 78.16  ? 130 LEU D CD1 1 
ATOM   13363 C CD2 . LEU D 1 130 ? 14.448  50.770  69.521  1.00 83.48  ? 130 LEU D CD2 1 
ATOM   13364 N N   . GLN D 1 131 ? 14.174  52.037  65.725  1.00 78.44  ? 131 GLN D N   1 
ATOM   13365 C CA  . GLN D 1 131 ? 12.858  52.608  65.455  1.00 76.54  ? 131 GLN D CA  1 
ATOM   13366 C C   . GLN D 1 131 ? 12.111  51.808  64.393  1.00 76.87  ? 131 GLN D C   1 
ATOM   13367 O O   . GLN D 1 131 ? 10.979  51.366  64.616  1.00 75.01  ? 131 GLN D O   1 
ATOM   13368 C CB  . GLN D 1 131 ? 13.001  54.065  65.018  1.00 81.56  ? 131 GLN D CB  1 
ATOM   13369 C CG  . GLN D 1 131 ? 13.479  55.005  66.104  1.00 81.81  ? 131 GLN D CG  1 
ATOM   13370 C CD  . GLN D 1 131 ? 14.065  56.289  65.557  1.00 91.05  ? 131 GLN D CD  1 
ATOM   13371 O OE1 . GLN D 1 131 ? 13.448  56.966  64.735  1.00 90.99  ? 131 GLN D OE1 1 
ATOM   13372 N NE2 . GLN D 1 131 ? 15.266  56.631  66.008  1.00 84.94  ? 131 GLN D NE2 1 
ATOM   13373 N N   . THR D 1 132 ? 12.743  51.594  63.235  1.00 83.92  ? 132 THR D N   1 
ATOM   13374 C CA  . THR D 1 132 ? 12.050  50.996  62.093  1.00 84.87  ? 132 THR D CA  1 
ATOM   13375 C C   . THR D 1 132 ? 11.603  49.572  62.394  1.00 90.34  ? 132 THR D C   1 
ATOM   13376 O O   . THR D 1 132 ? 10.500  49.159  62.010  1.00 95.99  ? 132 THR D O   1 
ATOM   13377 C CB  . THR D 1 132 ? 12.963  50.998  60.868  1.00 85.84  ? 132 THR D CB  1 
ATOM   13378 O OG1 . THR D 1 132 ? 14.163  50.270  61.167  1.00 100.61 ? 132 THR D OG1 1 
ATOM   13379 C CG2 . THR D 1 132 ? 13.324  52.414  60.467  1.00 83.66  ? 132 THR D CG2 1 
ATOM   13380 N N   . LEU D 1 133 ? 12.459  48.815  63.084  1.00 88.58  ? 133 LEU D N   1 
ATOM   13381 C CA  . LEU D 1 133 ? 12.223  47.399  63.341  1.00 86.92  ? 133 LEU D CA  1 
ATOM   13382 C C   . LEU D 1 133 ? 11.067  47.181  64.319  1.00 76.91  ? 133 LEU D C   1 
ATOM   13383 O O   . LEU D 1 133 ? 10.323  46.201  64.194  1.00 76.38  ? 133 LEU D O   1 
ATOM   13384 C CB  . LEU D 1 133 ? 13.536  46.763  63.810  1.00 85.45  ? 133 LEU D CB  1 
ATOM   13385 C CG  . LEU D 1 133 ? 13.663  45.670  64.863  1.00 89.58  ? 133 LEU D CG  1 
ATOM   13386 C CD1 . LEU D 1 133 ? 12.890  44.450  64.455  1.00 87.76  ? 133 LEU D CD1 1 
ATOM   13387 C CD2 . LEU D 1 133 ? 15.152  45.295  64.998  1.00 84.14  ? 133 LEU D CD2 1 
ATOM   13388 N N   . ASN D 1 134 ? 10.899  48.079  65.296  1.00 75.13  ? 134 ASN D N   1 
ATOM   13389 C CA  . ASN D 1 134 ? 9.705   48.056  66.135  1.00 72.39  ? 134 ASN D CA  1 
ATOM   13390 C C   . ASN D 1 134 ? 8.447   48.052  65.276  1.00 75.75  ? 134 ASN D C   1 
ATOM   13391 O O   . ASN D 1 134 ? 7.556   47.218  65.455  1.00 78.20  ? 134 ASN D O   1 
ATOM   13392 C CB  . ASN D 1 134 ? 9.709   49.270  67.066  1.00 70.87  ? 134 ASN D CB  1 
ATOM   13393 C CG  . ASN D 1 134 ? 10.440  49.016  68.368  1.00 70.56  ? 134 ASN D CG  1 
ATOM   13394 O OD1 . ASN D 1 134 ? 10.166  48.048  69.074  1.00 69.73  ? 134 ASN D OD1 1 
ATOM   13395 N ND2 . ASN D 1 134 ? 11.367  49.905  68.703  1.00 71.28  ? 134 ASN D ND2 1 
ATOM   13396 N N   . LEU D 1 135 ? 8.370   48.980  64.321  1.00 72.67  ? 135 LEU D N   1 
ATOM   13397 C CA  . LEU D 1 135 ? 7.185   49.097  63.476  1.00 71.77  ? 135 LEU D CA  1 
ATOM   13398 C C   . LEU D 1 135 ? 7.003   47.863  62.602  1.00 80.59  ? 135 LEU D C   1 
ATOM   13399 O O   . LEU D 1 135 ? 5.883   47.359  62.452  1.00 72.63  ? 135 LEU D O   1 
ATOM   13400 C CB  . LEU D 1 135 ? 7.281   50.357  62.613  1.00 72.61  ? 135 LEU D CB  1 
ATOM   13401 C CG  . LEU D 1 135 ? 7.101   51.750  63.232  1.00 75.98  ? 135 LEU D CG  1 
ATOM   13402 C CD1 . LEU D 1 135 ? 5.635   52.012  63.517  1.00 88.35  ? 135 LEU D CD1 1 
ATOM   13403 C CD2 . LEU D 1 135 ? 7.914   51.951  64.499  1.00 79.24  ? 135 LEU D CD2 1 
ATOM   13404 N N   . LEU D 1 136 ? 8.095   47.359  62.020  1.00 84.46  ? 136 LEU D N   1 
ATOM   13405 C CA  . LEU D 1 136 ? 8.002   46.217  61.115  1.00 78.55  ? 136 LEU D CA  1 
ATOM   13406 C C   . LEU D 1 136 ? 7.534   44.960  61.834  1.00 76.06  ? 136 LEU D C   1 
ATOM   13407 O O   . LEU D 1 136 ? 6.867   44.115  61.228  1.00 76.38  ? 136 LEU D O   1 
ATOM   13408 C CB  . LEU D 1 136 ? 9.353   45.974  60.447  1.00 88.51  ? 136 LEU D CB  1 
ATOM   13409 C CG  . LEU D 1 136 ? 9.759   46.996  59.387  1.00 85.65  ? 136 LEU D CG  1 
ATOM   13410 C CD1 . LEU D 1 136 ? 11.263  47.162  59.392  1.00 92.62  ? 136 LEU D CD1 1 
ATOM   13411 C CD2 . LEU D 1 136 ? 9.264   46.575  58.013  1.00 92.21  ? 136 LEU D CD2 1 
ATOM   13412 N N   . ALA D 1 137 ? 7.879   44.813  63.115  1.00 77.17  ? 137 ALA D N   1 
ATOM   13413 C CA  . ALA D 1 137 ? 7.464   43.630  63.861  1.00 73.99  ? 137 ALA D CA  1 
ATOM   13414 C C   . ALA D 1 137 ? 5.947   43.556  63.984  1.00 71.87  ? 137 ALA D C   1 
ATOM   13415 O O   . ALA D 1 137 ? 5.359   42.472  63.883  1.00 71.82  ? 137 ALA D O   1 
ATOM   13416 C CB  . ALA D 1 137 ? 8.120   43.627  65.240  1.00 73.18  ? 137 ALA D CB  1 
ATOM   13417 N N   . TRP D 1 138 ? 5.296   44.696  64.199  1.00 71.18  ? 138 TRP D N   1 
ATOM   13418 C CA  . TRP D 1 138 ? 3.838   44.753  64.322  1.00 76.09  ? 138 TRP D CA  1 
ATOM   13419 C C   . TRP D 1 138 ? 3.173   44.900  62.954  1.00 72.43  ? 138 TRP D C   1 
ATOM   13420 O O   . TRP D 1 138 ? 2.351   45.787  62.727  1.00 80.59  ? 138 TRP D O   1 
ATOM   13421 C CB  . TRP D 1 138 ? 3.443   45.895  65.255  1.00 66.01  ? 138 TRP D CB  1 
ATOM   13422 C CG  . TRP D 1 138 ? 4.113   45.828  66.604  1.00 65.23  ? 138 TRP D CG  1 
ATOM   13423 C CD1 . TRP D 1 138 ? 5.377   46.234  66.905  1.00 66.30  ? 138 TRP D CD1 1 
ATOM   13424 C CD2 . TRP D 1 138 ? 3.548   45.346  67.829  1.00 64.06  ? 138 TRP D CD2 1 
ATOM   13425 N NE1 . TRP D 1 138 ? 5.643   46.027  68.234  1.00 65.20  ? 138 TRP D NE1 1 
ATOM   13426 C CE2 . TRP D 1 138 ? 4.535   45.482  68.826  1.00 66.48  ? 138 TRP D CE2 1 
ATOM   13427 C CE3 . TRP D 1 138 ? 2.307   44.815  68.182  1.00 68.03  ? 138 TRP D CE3 1 
ATOM   13428 C CZ2 . TRP D 1 138 ? 4.320   45.102  70.150  1.00 69.39  ? 138 TRP D CZ2 1 
ATOM   13429 C CZ3 . TRP D 1 138 ? 2.096   44.433  69.500  1.00 64.16  ? 138 TRP D CZ3 1 
ATOM   13430 C CH2 . TRP D 1 138 ? 3.096   44.579  70.465  1.00 62.07  ? 138 TRP D CH2 1 
ATOM   13431 N N   . CYS D 1 139 ? 3.529   44.011  62.032  1.00 71.16  ? 139 CYS D N   1 
ATOM   13432 C CA  . CYS D 1 139 ? 3.010   44.030  60.672  1.00 72.37  ? 139 CYS D CA  1 
ATOM   13433 C C   . CYS D 1 139 ? 1.847   43.057  60.541  1.00 73.13  ? 139 CYS D C   1 
ATOM   13434 O O   . CYS D 1 139 ? 1.838   41.995  61.169  1.00 78.28  ? 139 CYS D O   1 
ATOM   13435 C CB  . CYS D 1 139 ? 4.105   43.674  59.662  1.00 84.81  ? 139 CYS D CB  1 
ATOM   13436 S SG  . CYS D 1 139 ? 3.565   43.646  57.935  1.00 87.80  ? 139 CYS D SG  1 
ATOM   13437 N N   . GLY D 1 140 ? 0.866   43.427  59.720  1.00 71.57  ? 140 GLY D N   1 
ATOM   13438 C CA  . GLY D 1 140 ? -0.314  42.617  59.524  1.00 71.01  ? 140 GLY D CA  1 
ATOM   13439 C C   . GLY D 1 140 ? -0.258  41.774  58.260  1.00 77.62  ? 140 GLY D C   1 
ATOM   13440 O O   . GLY D 1 140 ? 0.562   42.002  57.374  1.00 84.56  ? 140 GLY D O   1 
ATOM   13441 N N   . ARG D 1 141 ? -1.157  40.786  58.190  1.00 73.12  ? 141 ARG D N   1 
ATOM   13442 C CA  . ARG D 1 141 ? -1.185  39.889  57.036  1.00 77.48  ? 141 ARG D CA  1 
ATOM   13443 C C   . ARG D 1 141 ? -1.444  40.651  55.746  1.00 80.77  ? 141 ARG D C   1 
ATOM   13444 O O   . ARG D 1 141 ? -0.852  40.343  54.705  1.00 94.39  ? 141 ARG D O   1 
ATOM   13445 C CB  . ARG D 1 141 ? -2.249  38.806  57.220  1.00 81.90  ? 141 ARG D CB  1 
ATOM   13446 C CG  . ARG D 1 141 ? -2.190  37.718  56.150  1.00 85.69  ? 141 ARG D CG  1 
ATOM   13447 C CD  . ARG D 1 141 ? -3.209  36.611  56.390  1.00 76.59  ? 141 ARG D CD  1 
ATOM   13448 N NE  . ARG D 1 141 ? -4.579  37.055  56.165  1.00 75.37  ? 141 ARG D NE  1 
ATOM   13449 C CZ  . ARG D 1 141 ? -5.345  36.634  55.167  1.00 76.57  ? 141 ARG D CZ  1 
ATOM   13450 N NH1 . ARG D 1 141 ? -4.901  35.762  54.276  1.00 83.20  ? 141 ARG D NH1 1 
ATOM   13451 N NH2 . ARG D 1 141 ? -6.585  37.103  55.058  1.00 75.38  ? 141 ARG D NH2 1 
ATOM   13452 N N   . THR D 1 142 ? -2.336  41.643  55.792  1.00 79.60  ? 142 THR D N   1 
ATOM   13453 C CA  . THR D 1 142 ? -2.705  42.370  54.583  1.00 76.57  ? 142 THR D CA  1 
ATOM   13454 C C   . THR D 1 142 ? -1.530  43.150  54.003  1.00 81.66  ? 142 THR D C   1 
ATOM   13455 O O   . THR D 1 142 ? -1.479  43.372  52.788  1.00 97.97  ? 142 THR D O   1 
ATOM   13456 C CB  . THR D 1 142 ? -3.885  43.300  54.877  1.00 84.75  ? 142 THR D CB  1 
ATOM   13457 O OG1 . THR D 1 142 ? -4.442  43.776  53.646  1.00 105.62 ? 142 THR D OG1 1 
ATOM   13458 C CG2 . THR D 1 142 ? -3.453  44.484  55.739  1.00 79.15  ? 142 THR D CG2 1 
ATOM   13459 N N   . LEU D 1 143 ? -0.578  43.562  54.841  1.00 77.29  ? 143 LEU D N   1 
ATOM   13460 C CA  . LEU D 1 143 ? 0.589   44.315  54.402  1.00 78.83  ? 143 LEU D CA  1 
ATOM   13461 C C   . LEU D 1 143 ? 1.868   43.489  54.496  1.00 80.59  ? 143 LEU D C   1 
ATOM   13462 O O   . LEU D 1 143 ? 2.949   44.034  54.729  1.00 83.28  ? 143 LEU D O   1 
ATOM   13463 C CB  . LEU D 1 143 ? 0.729   45.603  55.212  1.00 78.30  ? 143 LEU D CB  1 
ATOM   13464 C CG  . LEU D 1 143 ? 0.336   46.919  54.535  1.00 93.44  ? 143 LEU D CG  1 
ATOM   13465 C CD1 . LEU D 1 143 ? -0.997  46.791  53.815  1.00 92.12  ? 143 LEU D CD1 1 
ATOM   13466 C CD2 . LEU D 1 143 ? 0.286   48.041  55.560  1.00 79.44  ? 143 LEU D CD2 1 
ATOM   13467 N N   . ARG D 1 144 ? 1.761   42.171  54.319  1.00 81.35  ? 144 ARG D N   1 
ATOM   13468 C CA  . ARG D 1 144 ? 2.941   41.322  54.437  1.00 82.96  ? 144 ARG D CA  1 
ATOM   13469 C C   . ARG D 1 144 ? 3.764   41.333  53.154  1.00 92.32  ? 144 ARG D C   1 
ATOM   13470 O O   . ARG D 1 144 ? 4.981   41.541  53.193  1.00 97.44  ? 144 ARG D O   1 
ATOM   13471 C CB  . ARG D 1 144 ? 2.533   39.897  54.812  1.00 85.04  ? 144 ARG D CB  1 
ATOM   13472 C CG  . ARG D 1 144 ? 3.422   39.280  55.882  1.00 83.54  ? 144 ARG D CG  1 
ATOM   13473 C CD  . ARG D 1 144 ? 2.651   38.375  56.829  1.00 80.76  ? 144 ARG D CD  1 
ATOM   13474 N NE  . ARG D 1 144 ? 1.885   39.114  57.827  1.00 93.07  ? 144 ARG D NE  1 
ATOM   13475 C CZ  . ARG D 1 144 ? 2.311   39.371  59.057  1.00 88.62  ? 144 ARG D CZ  1 
ATOM   13476 N NH1 . ARG D 1 144 ? 3.526   39.029  59.452  1.00 101.18 ? 144 ARG D NH1 1 
ATOM   13477 N NH2 . ARG D 1 144 ? 1.500   39.987  59.911  1.00 73.96  ? 144 ARG D NH2 1 
ATOM   13478 N N   . LYS D 1 145 ? 3.123   41.109  52.006  1.00 90.93  ? 145 LYS D N   1 
ATOM   13479 C CA  . LYS D 1 145 ? 3.817   41.247  50.733  1.00 90.05  ? 145 LYS D CA  1 
ATOM   13480 C C   . LYS D 1 145 ? 3.778   42.670  50.192  1.00 94.58  ? 145 LYS D C   1 
ATOM   13481 O O   . LYS D 1 145 ? 4.460   42.959  49.203  1.00 104.50 ? 145 LYS D O   1 
ATOM   13482 C CB  . LYS D 1 145 ? 3.242   40.276  49.692  1.00 94.26  ? 145 LYS D CB  1 
ATOM   13483 C CG  . LYS D 1 145 ? 1.795   40.518  49.302  1.00 95.43  ? 145 LYS D CG  1 
ATOM   13484 C CD  . LYS D 1 145 ? 1.517   40.007  47.893  1.00 93.16  ? 145 LYS D CD  1 
ATOM   13485 C CE  . LYS D 1 145 ? 1.938   38.552  47.723  1.00 94.81  ? 145 LYS D CE  1 
ATOM   13486 N NZ  . LYS D 1 145 ? 1.440   37.676  48.821  1.00 92.91  ? 145 LYS D NZ  1 
ATOM   13487 N N   . ASP D 1 146 ? 2.997   43.559  50.812  1.00 97.78  ? 146 ASP D N   1 
ATOM   13488 C CA  . ASP D 1 146 ? 3.062   44.976  50.474  1.00 99.54  ? 146 ASP D CA  1 
ATOM   13489 C C   . ASP D 1 146 ? 4.309   45.625  51.063  1.00 96.48  ? 146 ASP D C   1 
ATOM   13490 O O   . ASP D 1 146 ? 4.930   46.481  50.422  1.00 89.34  ? 146 ASP D O   1 
ATOM   13491 C CB  . ASP D 1 146 ? 1.801   45.691  50.962  1.00 89.23  ? 146 ASP D CB  1 
ATOM   13492 C CG  . ASP D 1 146 ? 1.329   46.762  49.999  1.00 102.28 ? 146 ASP D CG  1 
ATOM   13493 O OD1 . ASP D 1 146 ? 2.099   47.124  49.084  1.00 91.73  ? 146 ASP D OD1 1 
ATOM   13494 O OD2 . ASP D 1 146 ? 0.186   47.241  50.158  1.00 103.66 ? 146 ASP D OD2 1 
ATOM   13495 N N   . LEU D 1 147 ? 4.689   45.227  52.278  1.00 97.24  ? 147 LEU D N   1 
ATOM   13496 C CA  . LEU D 1 147 ? 5.942   45.640  52.893  1.00 93.87  ? 147 LEU D CA  1 
ATOM   13497 C C   . LEU D 1 147 ? 7.021   44.571  52.779  1.00 98.42  ? 147 LEU D C   1 
ATOM   13498 O O   . LEU D 1 147 ? 8.045   44.665  53.465  1.00 107.70 ? 147 LEU D O   1 
ATOM   13499 C CB  . LEU D 1 147 ? 5.731   45.999  54.364  1.00 84.08  ? 147 LEU D CB  1 
ATOM   13500 C CG  . LEU D 1 147 ? 4.674   47.042  54.716  1.00 81.79  ? 147 LEU D CG  1 
ATOM   13501 C CD1 . LEU D 1 147 ? 4.076   46.739  56.080  1.00 79.08  ? 147 LEU D CD1 1 
ATOM   13502 C CD2 . LEU D 1 147 ? 5.277   48.432  54.688  1.00 101.14 ? 147 LEU D CD2 1 
ATOM   13503 N N   . LYS D 1 148 ? 6.794   43.557  51.937  1.00 90.43  ? 148 LYS D N   1 
ATOM   13504 C CA  . LYS D 1 148 ? 7.735   42.470  51.679  1.00 92.60  ? 148 LYS D CA  1 
ATOM   13505 C C   . LYS D 1 148 ? 9.177   42.959  51.620  1.00 94.35  ? 148 LYS D C   1 
ATOM   13506 O O   . LYS D 1 148 ? 10.033  42.505  52.386  1.00 94.51  ? 148 LYS D O   1 
ATOM   13507 C CB  . LYS D 1 148 ? 7.323   41.801  50.357  1.00 97.50  ? 148 LYS D CB  1 
ATOM   13508 C CG  . LYS D 1 148 ? 8.182   40.666  49.767  1.00 97.36  ? 148 LYS D CG  1 
ATOM   13509 C CD  . LYS D 1 148 ? 9.003   39.861  50.756  1.00 97.24  ? 148 LYS D CD  1 
ATOM   13510 C CE  . LYS D 1 148 ? 9.860   38.818  50.039  1.00 100.22 ? 148 LYS D CE  1 
ATOM   13511 N NZ  . LYS D 1 148 ? 11.134  39.406  49.534  1.00 102.46 ? 148 LYS D NZ  1 
ATOM   13512 N N   . ASP D 1 149 ? 9.435   43.941  50.754  1.00 95.65  ? 149 ASP D N   1 
ATOM   13513 C CA  . ASP D 1 149 ? 10.804  44.331  50.428  1.00 98.87  ? 149 ASP D CA  1 
ATOM   13514 C C   . ASP D 1 149 ? 11.619  44.677  51.669  1.00 96.85  ? 149 ASP D C   1 
ATOM   13515 O O   . ASP D 1 149 ? 12.819  44.388  51.733  1.00 98.62  ? 149 ASP D O   1 
ATOM   13516 C CB  . ASP D 1 149 ? 10.786  45.515  49.459  1.00 98.98  ? 149 ASP D CB  1 
ATOM   13517 C CG  . ASP D 1 149 ? 12.155  46.112  49.249  1.00 101.04 ? 149 ASP D CG  1 
ATOM   13518 O OD1 . ASP D 1 149 ? 12.993  45.461  48.590  1.00 103.65 ? 149 ASP D OD1 1 
ATOM   13519 O OD2 . ASP D 1 149 ? 12.396  47.229  49.751  1.00 110.62 ? 149 ASP D OD2 1 
ATOM   13520 N N   . LEU D 1 150 ? 10.983  45.275  52.672  1.00 94.06  ? 150 LEU D N   1 
ATOM   13521 C CA  . LEU D 1 150 ? 11.705  45.703  53.862  1.00 99.88  ? 150 LEU D CA  1 
ATOM   13522 C C   . LEU D 1 150 ? 11.797  44.628  54.934  1.00 96.01  ? 150 LEU D C   1 
ATOM   13523 O O   . LEU D 1 150 ? 12.735  44.649  55.741  1.00 94.49  ? 150 LEU D O   1 
ATOM   13524 C CB  . LEU D 1 150 ? 11.051  46.953  54.449  1.00 95.79  ? 150 LEU D CB  1 
ATOM   13525 C CG  . LEU D 1 150 ? 11.273  48.185  53.578  1.00 91.90  ? 150 LEU D CG  1 
ATOM   13526 C CD1 . LEU D 1 150 ? 9.958   48.850  53.196  1.00 90.42  ? 150 LEU D CD1 1 
ATOM   13527 C CD2 . LEU D 1 150 ? 12.187  49.136  54.301  1.00 91.79  ? 150 LEU D CD2 1 
ATOM   13528 N N   . LEU D 1 151 ? 10.854  43.686  54.963  1.00 92.55  ? 151 LEU D N   1 
ATOM   13529 C CA  . LEU D 1 151 ? 10.881  42.656  55.996  1.00 90.03  ? 151 LEU D CA  1 
ATOM   13530 C C   . LEU D 1 151 ? 12.058  41.702  55.814  1.00 98.31  ? 151 LEU D C   1 
ATOM   13531 O O   . LEU D 1 151 ? 12.622  41.220  56.803  1.00 100.46 ? 151 LEU D O   1 
ATOM   13532 C CB  . LEU D 1 151 ? 9.557   41.891  56.004  1.00 88.56  ? 151 LEU D CB  1 
ATOM   13533 C CG  . LEU D 1 151 ? 8.554   42.305  57.081  1.00 91.32  ? 151 LEU D CG  1 
ATOM   13534 C CD1 . LEU D 1 151 ? 7.613   41.157  57.420  1.00 94.64  ? 151 LEU D CD1 1 
ATOM   13535 C CD2 . LEU D 1 151 ? 9.261   42.805  58.334  1.00 89.75  ? 151 LEU D CD2 1 
ATOM   13536 N N   . ASN D 1 152 ? 12.439  41.414  54.570  1.00 98.12  ? 152 ASN D N   1 
ATOM   13537 C CA  . ASN D 1 152 ? 13.578  40.544  54.289  1.00 97.69  ? 152 ASN D CA  1 
ATOM   13538 C C   . ASN D 1 152 ? 14.896  41.290  54.218  1.00 99.39  ? 152 ASN D C   1 
ATOM   13539 O O   . ASN D 1 152 ? 15.953  40.657  54.303  1.00 101.27 ? 152 ASN D O   1 
ATOM   13540 C CB  . ASN D 1 152 ? 13.345  39.803  52.975  1.00 99.80  ? 152 ASN D CB  1 
ATOM   13541 C CG  . ASN D 1 152 ? 11.924  39.338  52.841  1.00 98.21  ? 152 ASN D CG  1 
ATOM   13542 O OD1 . ASN D 1 152 ? 10.995  40.140  52.900  1.00 103.38 ? 152 ASN D OD1 1 
ATOM   13543 N ND2 . ASN D 1 152 ? 11.735  38.045  52.639  1.00 99.07  ? 152 ASN D ND2 1 
ATOM   13544 N N   . LYS D 1 153 ? 14.859  42.610  54.042  1.00 98.91  ? 153 LYS D N   1 
ATOM   13545 C CA  . LYS D 1 153 ? 16.086  43.394  54.127  1.00 104.54 ? 153 LYS D CA  1 
ATOM   13546 C C   . LYS D 1 153 ? 16.759  43.189  55.478  1.00 102.85 ? 153 LYS D C   1 
ATOM   13547 O O   . LYS D 1 153 ? 17.964  42.916  55.555  1.00 101.47 ? 153 LYS D O   1 
ATOM   13548 C CB  . LYS D 1 153 ? 15.783  44.875  53.894  1.00 99.52  ? 153 LYS D CB  1 
ATOM   13549 C CG  . LYS D 1 153 ? 15.764  45.280  52.429  1.00 101.60 ? 153 LYS D CG  1 
ATOM   13550 C CD  . LYS D 1 153 ? 15.711  46.791  52.268  1.00 101.17 ? 153 LYS D CD  1 
ATOM   13551 C CE  . LYS D 1 153 ? 16.718  47.479  53.174  1.00 101.10 ? 153 LYS D CE  1 
ATOM   13552 N NZ  . LYS D 1 153 ? 16.639  48.960  53.067  1.00 100.64 ? 153 LYS D NZ  1 
ATOM   13553 N N   . GLY D 1 154 ? 15.989  43.301  56.557  1.00 107.47 ? 154 GLY D N   1 
ATOM   13554 C CA  . GLY D 1 154 ? 16.492  42.993  57.882  1.00 97.38  ? 154 GLY D CA  1 
ATOM   13555 C C   . GLY D 1 154 ? 17.463  44.019  58.425  1.00 97.23  ? 154 GLY D C   1 
ATOM   13556 O O   . GLY D 1 154 ? 17.258  44.569  59.511  1.00 93.94  ? 154 GLY D O   1 
ATOM   13557 N N   . ARG D 1 155 ? 18.525  44.289  57.671  1.00 115.44 ? 155 ARG D N   1 
ATOM   13558 C CA  . ARG D 1 155 ? 19.635  45.124  58.119  1.00 116.04 ? 155 ARG D CA  1 
ATOM   13559 C C   . ARG D 1 155 ? 19.552  46.520  57.495  1.00 114.07 ? 155 ARG D C   1 
ATOM   13560 O O   . ARG D 1 155 ? 18.978  46.706  56.415  1.00 112.03 ? 155 ARG D O   1 
ATOM   13561 C CB  . ARG D 1 155 ? 20.968  44.475  57.735  1.00 102.80 ? 155 ARG D CB  1 
ATOM   13562 C CG  . ARG D 1 155 ? 21.188  43.069  58.283  1.00 103.09 ? 155 ARG D CG  1 
ATOM   13563 C CD  . ARG D 1 155 ? 21.726  43.049  59.700  1.00 102.16 ? 155 ARG D CD  1 
ATOM   13564 N NE  . ARG D 1 155 ? 23.109  43.508  59.769  1.00 114.81 ? 155 ARG D NE  1 
ATOM   13565 C CZ  . ARG D 1 155 ? 23.783  43.688  60.897  1.00 108.40 ? 155 ARG D CZ  1 
ATOM   13566 N NH1 . ARG D 1 155 ? 23.237  43.437  62.076  1.00 101.72 ? 155 ARG D NH1 1 
ATOM   13567 N NH2 . ARG D 1 155 ? 25.035  44.133  60.840  1.00 113.08 ? 155 ARG D NH2 1 
ATOM   13568 N N   . ASN D 1 156 ? 20.143  47.498  58.190  1.00 104.42 ? 156 ASN D N   1 
ATOM   13569 C CA  . ASN D 1 156 ? 20.591  48.763  57.612  1.00 100.81 ? 156 ASN D CA  1 
ATOM   13570 C C   . ASN D 1 156 ? 19.447  49.599  57.014  1.00 99.97  ? 156 ASN D C   1 
ATOM   13571 O O   . ASN D 1 156 ? 19.302  49.732  55.794  1.00 103.30 ? 156 ASN D O   1 
ATOM   13572 C CB  . ASN D 1 156 ? 21.683  48.515  56.563  1.00 104.19 ? 156 ASN D CB  1 
ATOM   13573 C CG  . ASN D 1 156 ? 22.915  47.841  57.142  1.00 105.84 ? 156 ASN D CG  1 
ATOM   13574 O OD1 . ASN D 1 156 ? 22.961  47.515  58.327  1.00 106.46 ? 156 ASN D OD1 1 
ATOM   13575 N ND2 . ASN D 1 156 ? 23.920  47.626  56.300  1.00 108.98 ? 156 ASN D ND2 1 
ATOM   13576 N N   . TYR D 1 157 ? 18.607  50.135  57.898  1.00 106.78 ? 157 TYR D N   1 
ATOM   13577 C CA  . TYR D 1 157 ? 17.540  51.055  57.494  1.00 104.57 ? 157 TYR D CA  1 
ATOM   13578 C C   . TYR D 1 157 ? 18.003  52.504  57.612  1.00 95.19  ? 157 TYR D C   1 
ATOM   13579 O O   . TYR D 1 157 ? 18.712  52.855  58.559  1.00 94.99  ? 157 TYR D O   1 
ATOM   13580 C CB  . TYR D 1 157 ? 16.299  50.851  58.366  1.00 91.68  ? 157 TYR D CB  1 
ATOM   13581 C CG  . TYR D 1 157 ? 15.614  49.537  58.121  1.00 94.95  ? 157 TYR D CG  1 
ATOM   13582 C CD1 . TYR D 1 157 ? 16.224  48.337  58.460  1.00 102.35 ? 157 TYR D CD1 1 
ATOM   13583 C CD2 . TYR D 1 157 ? 14.360  49.494  57.534  1.00 92.08  ? 157 TYR D CD2 1 
ATOM   13584 C CE1 . TYR D 1 157 ? 15.600  47.131  58.229  1.00 99.65  ? 157 TYR D CE1 1 
ATOM   13585 C CE2 . TYR D 1 157 ? 13.731  48.296  57.300  1.00 89.90  ? 157 TYR D CE2 1 
ATOM   13586 C CZ  . TYR D 1 157 ? 14.352  47.117  57.649  1.00 91.43  ? 157 TYR D CZ  1 
ATOM   13587 O OH  . TYR D 1 157 ? 13.731  45.912  57.420  1.00 90.64  ? 157 TYR D OH  1 
ATOM   13588 N N   . THR D 1 158 ? 17.618  53.352  56.645  1.00 95.75  ? 158 THR D N   1 
ATOM   13589 C CA  . THR D 1 158 ? 18.042  54.743  56.795  1.00 96.02  ? 158 THR D CA  1 
ATOM   13590 C C   . THR D 1 158 ? 16.992  55.673  57.402  1.00 93.25  ? 158 THR D C   1 
ATOM   13591 O O   . THR D 1 158 ? 16.953  55.819  58.627  1.00 91.43  ? 158 THR D O   1 
ATOM   13592 C CB  . THR D 1 158 ? 18.452  55.310  55.429  1.00 108.20 ? 158 THR D CB  1 
ATOM   13593 O OG1 . THR D 1 158 ? 17.356  55.172  54.514  1.00 113.58 ? 158 THR D OG1 1 
ATOM   13594 C CG2 . THR D 1 158 ? 19.657  54.563  54.881  1.00 120.96 ? 158 THR D CG2 1 
ATOM   13595 N N   . GLN D 1 159 ? 16.098  56.265  56.597  1.00 92.88  ? 159 GLN D N   1 
ATOM   13596 C CA  . GLN D 1 159 ? 14.913  56.914  57.162  1.00 90.08  ? 159 GLN D CA  1 
ATOM   13597 C C   . GLN D 1 159 ? 13.663  56.662  56.334  1.00 89.35  ? 159 GLN D C   1 
ATOM   13598 O O   . GLN D 1 159 ? 12.695  56.065  56.816  1.00 87.22  ? 159 GLN D O   1 
ATOM   13599 C CB  . GLN D 1 159 ? 15.139  58.427  57.300  1.00 90.13  ? 159 GLN D CB  1 
ATOM   13600 C CG  . GLN D 1 159 ? 14.428  59.140  58.485  1.00 87.27  ? 159 GLN D CG  1 
ATOM   13601 C CD  . GLN D 1 159 ? 12.904  59.329  58.364  1.00 100.82 ? 159 GLN D CD  1 
ATOM   13602 O OE1 . GLN D 1 159 ? 12.201  58.586  57.689  1.00 102.05 ? 159 GLN D OE1 1 
ATOM   13603 N NE2 . GLN D 1 159 ? 12.403  60.355  59.039  1.00 95.50  ? 159 GLN D NE2 1 
ATOM   13604 N N   . GLU D 1 160 ? 13.713  57.069  55.060  1.00 94.57  ? 160 GLU D N   1 
ATOM   13605 C CA  . GLU D 1 160 ? 12.491  57.310  54.295  1.00 94.49  ? 160 GLU D CA  1 
ATOM   13606 C C   . GLU D 1 160 ? 11.695  56.037  54.087  1.00 96.60  ? 160 GLU D C   1 
ATOM   13607 O O   . GLU D 1 160 ? 10.500  56.100  53.778  1.00 92.77  ? 160 GLU D O   1 
ATOM   13608 C CB  . GLU D 1 160 ? 12.829  57.951  52.946  1.00 93.04  ? 160 GLU D CB  1 
ATOM   13609 C CG  . GLU D 1 160 ? 11.671  58.701  52.300  1.00 94.12  ? 160 GLU D CG  1 
ATOM   13610 C CD  . GLU D 1 160 ? 11.867  58.903  50.809  1.00 99.34  ? 160 GLU D CD  1 
ATOM   13611 O OE1 . GLU D 1 160 ? 12.611  58.110  50.195  1.00 100.47 ? 160 GLU D OE1 1 
ATOM   13612 O OE2 . GLU D 1 160 ? 11.277  59.853  50.252  1.00 99.75  ? 160 GLU D OE2 1 
ATOM   13613 N N   . GLU D 1 161 ? 12.339  54.888  54.264  1.00 92.19  ? 161 GLU D N   1 
ATOM   13614 C CA  . GLU D 1 161 ? 11.629  53.620  54.242  1.00 86.84  ? 161 GLU D CA  1 
ATOM   13615 C C   . GLU D 1 161 ? 10.643  53.521  55.400  1.00 83.31  ? 161 GLU D C   1 
ATOM   13616 O O   . GLU D 1 161 ? 9.535   53.000  55.233  1.00 85.66  ? 161 GLU D O   1 
ATOM   13617 C CB  . GLU D 1 161 ? 12.639  52.480  54.278  1.00 99.07  ? 161 GLU D CB  1 
ATOM   13618 C CG  . GLU D 1 161 ? 13.950  52.807  53.579  1.00 110.23 ? 161 GLU D CG  1 
ATOM   13619 C CD  . GLU D 1 161 ? 14.637  51.578  53.020  1.00 117.18 ? 161 GLU D CD  1 
ATOM   13620 O OE1 . GLU D 1 161 ? 14.236  51.116  51.931  1.00 106.55 ? 161 GLU D OE1 1 
ATOM   13621 O OE2 . GLU D 1 161 ? 15.579  51.075  53.667  1.00 112.12 ? 161 GLU D OE2 1 
ATOM   13622 N N   . LYS D 1 162 ? 11.027  54.011  56.583  1.00 84.58  ? 162 LYS D N   1 
ATOM   13623 C CA  . LYS D 1 162 ? 10.109  53.968  57.718  1.00 77.86  ? 162 LYS D CA  1 
ATOM   13624 C C   . LYS D 1 162 ? 8.897   54.861  57.482  1.00 77.83  ? 162 LYS D C   1 
ATOM   13625 O O   . LYS D 1 162 ? 7.762   54.450  57.739  1.00 79.42  ? 162 LYS D O   1 
ATOM   13626 C CB  . LYS D 1 162 ? 10.835  54.335  59.018  1.00 77.09  ? 162 LYS D CB  1 
ATOM   13627 C CG  . LYS D 1 162 ? 10.801  55.798  59.445  1.00 75.49  ? 162 LYS D CG  1 
ATOM   13628 C CD  . LYS D 1 162 ? 11.264  55.961  60.887  1.00 82.98  ? 162 LYS D CD  1 
ATOM   13629 C CE  . LYS D 1 162 ? 12.398  56.969  60.996  1.00 88.00  ? 162 LYS D CE  1 
ATOM   13630 N NZ  . LYS D 1 162 ? 13.077  56.905  62.320  1.00 72.18  ? 162 LYS D NZ  1 
ATOM   13631 N N   . GLU D 1 163 ? 9.107   56.074  56.961  1.00 79.71  ? 163 GLU D N   1 
ATOM   13632 C CA  . GLU D 1 163 ? 7.970   56.946  56.685  1.00 79.96  ? 163 GLU D CA  1 
ATOM   13633 C C   . GLU D 1 163 ? 6.999   56.286  55.720  1.00 81.17  ? 163 GLU D C   1 
ATOM   13634 O O   . GLU D 1 163 ? 5.788   56.528  55.790  1.00 80.37  ? 163 GLU D O   1 
ATOM   13635 C CB  . GLU D 1 163 ? 8.451   58.287  56.135  1.00 82.31  ? 163 GLU D CB  1 
ATOM   13636 C CG  . GLU D 1 163 ? 8.493   59.396  57.172  1.00 80.68  ? 163 GLU D CG  1 
ATOM   13637 C CD  . GLU D 1 163 ? 9.447   60.505  56.789  1.00 94.88  ? 163 GLU D CD  1 
ATOM   13638 O OE1 . GLU D 1 163 ? 9.355   60.997  55.645  1.00 97.35  ? 163 GLU D OE1 1 
ATOM   13639 O OE2 . GLU D 1 163 ? 10.288  60.884  57.631  1.00 92.15  ? 163 GLU D OE2 1 
ATOM   13640 N N   . TYR D 1 164 ? 7.511   55.438  54.827  1.00 83.18  ? 164 TYR D N   1 
ATOM   13641 C CA  . TYR D 1 164 ? 6.639   54.662  53.955  1.00 84.34  ? 164 TYR D CA  1 
ATOM   13642 C C   . TYR D 1 164 ? 5.776   53.690  54.752  1.00 91.29  ? 164 TYR D C   1 
ATOM   13643 O O   . TYR D 1 164 ? 4.582   53.539  54.469  1.00 94.05  ? 164 TYR D O   1 
ATOM   13644 C CB  . TYR D 1 164 ? 7.477   53.917  52.915  1.00 87.09  ? 164 TYR D CB  1 
ATOM   13645 C CG  . TYR D 1 164 ? 6.656   53.200  51.873  1.00 88.86  ? 164 TYR D CG  1 
ATOM   13646 C CD1 . TYR D 1 164 ? 5.722   53.884  51.106  1.00 90.51  ? 164 TYR D CD1 1 
ATOM   13647 C CD2 . TYR D 1 164 ? 6.812   51.838  51.655  1.00 94.83  ? 164 TYR D CD2 1 
ATOM   13648 C CE1 . TYR D 1 164 ? 4.968   53.232  50.151  1.00 92.28  ? 164 TYR D CE1 1 
ATOM   13649 C CE2 . TYR D 1 164 ? 6.063   51.176  50.704  1.00 99.14  ? 164 TYR D CE2 1 
ATOM   13650 C CZ  . TYR D 1 164 ? 5.142   51.878  49.954  1.00 94.56  ? 164 TYR D CZ  1 
ATOM   13651 O OH  . TYR D 1 164 ? 4.392   51.223  49.004  1.00 100.16 ? 164 TYR D OH  1 
ATOM   13652 N N   . VAL D 1 165 ? 6.358   53.021  55.753  1.00 90.19  ? 165 VAL D N   1 
ATOM   13653 C CA  . VAL D 1 165 ? 5.569   52.060  56.521  1.00 88.81  ? 165 VAL D CA  1 
ATOM   13654 C C   . VAL D 1 165 ? 4.582   52.785  57.430  1.00 78.93  ? 165 VAL D C   1 
ATOM   13655 O O   . VAL D 1 165 ? 3.492   52.269  57.704  1.00 80.00  ? 165 VAL D O   1 
ATOM   13656 C CB  . VAL D 1 165 ? 6.473   51.085  57.312  1.00 91.18  ? 165 VAL D CB  1 
ATOM   13657 C CG1 . VAL D 1 165 ? 7.608   50.564  56.431  1.00 97.79  ? 165 VAL D CG1 1 
ATOM   13658 C CG2 . VAL D 1 165 ? 6.987   51.686  58.614  1.00 82.31  ? 165 VAL D CG2 1 
ATOM   13659 N N   . LEU D 1 166 ? 4.933   53.982  57.910  1.00 73.89  ? 166 LEU D N   1 
ATOM   13660 C CA  . LEU D 1 166 ? 3.973   54.777  58.671  1.00 81.51  ? 166 LEU D CA  1 
ATOM   13661 C C   . LEU D 1 166 ? 2.758   55.124  57.819  1.00 87.53  ? 166 LEU D C   1 
ATOM   13662 O O   . LEU D 1 166 ? 1.612   55.001  58.270  1.00 83.86  ? 166 LEU D O   1 
ATOM   13663 C CB  . LEU D 1 166 ? 4.629   56.052  59.208  1.00 89.20  ? 166 LEU D CB  1 
ATOM   13664 C CG  . LEU D 1 166 ? 5.371   56.001  60.551  1.00 92.46  ? 166 LEU D CG  1 
ATOM   13665 C CD1 . LEU D 1 166 ? 6.731   55.335  60.439  1.00 83.20  ? 166 LEU D CD1 1 
ATOM   13666 C CD2 . LEU D 1 166 ? 5.508   57.399  61.141  1.00 86.97  ? 166 LEU D CD2 1 
ATOM   13667 N N   . ASN D 1 167 ? 2.991   55.547  56.573  1.00 86.67  ? 167 ASN D N   1 
ATOM   13668 C CA  . ASN D 1 167 ? 1.884   55.868  55.679  1.00 93.62  ? 167 ASN D CA  1 
ATOM   13669 C C   . ASN D 1 167 ? 1.056   54.629  55.363  1.00 83.79  ? 167 ASN D C   1 
ATOM   13670 O O   . ASN D 1 167 ? -0.173  54.707  55.247  1.00 81.23  ? 167 ASN D O   1 
ATOM   13671 C CB  . ASN D 1 167 ? 2.418   56.507  54.399  1.00 88.00  ? 167 ASN D CB  1 
ATOM   13672 C CG  . ASN D 1 167 ? 1.351   57.276  53.644  1.00 92.43  ? 167 ASN D CG  1 
ATOM   13673 O OD1 . ASN D 1 167 ? 1.089   58.442  53.934  1.00 90.33  ? 167 ASN D OD1 1 
ATOM   13674 N ND2 . ASN D 1 167 ? 0.738   56.627  52.660  1.00 91.22  ? 167 ASN D ND2 1 
ATOM   13675 N N   . LYS D 1 168 ? 1.713   53.479  55.202  1.00 78.17  ? 168 LYS D N   1 
ATOM   13676 C CA  . LYS D 1 168 ? 0.984   52.235  54.978  1.00 77.92  ? 168 LYS D CA  1 
ATOM   13677 C C   . LYS D 1 168 ? 0.117   51.881  56.181  1.00 83.45  ? 168 LYS D C   1 
ATOM   13678 O O   . LYS D 1 168 ? -1.028  51.442  56.023  1.00 83.73  ? 168 LYS D O   1 
ATOM   13679 C CB  . LYS D 1 168 ? 1.963   51.103  54.670  1.00 85.07  ? 168 LYS D CB  1 
ATOM   13680 C CG  . LYS D 1 168 ? 2.311   50.951  53.195  1.00 91.26  ? 168 LYS D CG  1 
ATOM   13681 C CD  . LYS D 1 168 ? 1.126   50.441  52.390  1.00 83.76  ? 168 LYS D CD  1 
ATOM   13682 C CE  . LYS D 1 168 ? 1.135   51.006  50.978  1.00 87.50  ? 168 LYS D CE  1 
ATOM   13683 N NZ  . LYS D 1 168 ? -0.217  51.452  50.543  1.00 88.22  ? 168 LYS D NZ  1 
ATOM   13684 N N   . TYR D 1 169 ? 0.650   52.060  57.393  1.00 81.89  ? 169 TYR D N   1 
ATOM   13685 C CA  . TYR D 1 169 ? -0.121  51.761  58.596  1.00 69.72  ? 169 TYR D CA  1 
ATOM   13686 C C   . TYR D 1 169 ? -1.296  52.718  58.757  1.00 68.54  ? 169 TYR D C   1 
ATOM   13687 O O   . TYR D 1 169 ? -2.383  52.310  59.180  1.00 69.22  ? 169 TYR D O   1 
ATOM   13688 C CB  . TYR D 1 169 ? 0.778   51.813  59.831  1.00 66.79  ? 169 TYR D CB  1 
ATOM   13689 C CG  . TYR D 1 169 ? 1.751   50.658  59.945  1.00 75.56  ? 169 TYR D CG  1 
ATOM   13690 C CD1 . TYR D 1 169 ? 1.661   49.559  59.100  1.00 73.93  ? 169 TYR D CD1 1 
ATOM   13691 C CD2 . TYR D 1 169 ? 2.749   50.662  60.910  1.00 73.64  ? 169 TYR D CD2 1 
ATOM   13692 C CE1 . TYR D 1 169 ? 2.546   48.502  59.207  1.00 73.77  ? 169 TYR D CE1 1 
ATOM   13693 C CE2 . TYR D 1 169 ? 3.638   49.610  61.025  1.00 66.96  ? 169 TYR D CE2 1 
ATOM   13694 C CZ  . TYR D 1 169 ? 3.531   48.533  60.171  1.00 68.86  ? 169 TYR D CZ  1 
ATOM   13695 O OH  . TYR D 1 169 ? 4.413   47.483  60.282  1.00 71.09  ? 169 TYR D OH  1 
ATOM   13696 N N   . PHE D 1 170 ? -1.097  53.999  58.438  1.00 73.23  ? 170 PHE D N   1 
ATOM   13697 C CA  . PHE D 1 170 ? -2.190  54.956  58.568  1.00 72.64  ? 170 PHE D CA  1 
ATOM   13698 C C   . PHE D 1 170 ? -3.280  54.704  57.535  1.00 71.38  ? 170 PHE D C   1 
ATOM   13699 O O   . PHE D 1 170 ? -4.457  54.975  57.801  1.00 70.58  ? 170 PHE D O   1 
ATOM   13700 C CB  . PHE D 1 170 ? -1.655  56.384  58.462  1.00 84.95  ? 170 PHE D CB  1 
ATOM   13701 C CG  . PHE D 1 170 ? -1.112  56.922  59.758  1.00 87.57  ? 170 PHE D CG  1 
ATOM   13702 C CD1 . PHE D 1 170 ? -1.956  57.168  60.829  1.00 86.21  ? 170 PHE D CD1 1 
ATOM   13703 C CD2 . PHE D 1 170 ? 0.242   57.176  59.909  1.00 92.83  ? 170 PHE D CD2 1 
ATOM   13704 C CE1 . PHE D 1 170 ? -1.461  57.660  62.025  1.00 87.26  ? 170 PHE D CE1 1 
ATOM   13705 C CE2 . PHE D 1 170 ? 0.744   57.667  61.101  1.00 93.44  ? 170 PHE D CE2 1 
ATOM   13706 C CZ  . PHE D 1 170 ? -0.109  57.910  62.161  1.00 85.56  ? 170 PHE D CZ  1 
ATOM   13707 N N   . GLU D 1 171 ? -2.917  54.190  56.357  1.00 73.97  ? 171 GLU D N   1 
ATOM   13708 C CA  . GLU D 1 171 ? -3.935  53.824  55.378  1.00 76.18  ? 171 GLU D CA  1 
ATOM   13709 C C   . GLU D 1 171 ? -4.707  52.588  55.821  1.00 74.12  ? 171 GLU D C   1 
ATOM   13710 O O   . GLU D 1 171 ? -5.916  52.487  55.580  1.00 74.39  ? 171 GLU D O   1 
ATOM   13711 C CB  . GLU D 1 171 ? -3.294  53.593  54.007  1.00 79.29  ? 171 GLU D CB  1 
ATOM   13712 C CG  . GLU D 1 171 ? -4.291  53.617  52.855  1.00 84.32  ? 171 GLU D CG  1 
ATOM   13713 C CD  . GLU D 1 171 ? -3.734  53.018  51.577  1.00 95.20  ? 171 GLU D CD  1 
ATOM   13714 O OE1 . GLU D 1 171 ? -2.591  52.514  51.600  1.00 90.55  ? 171 GLU D OE1 1 
ATOM   13715 O OE2 . GLU D 1 171 ? -4.442  53.053  50.548  1.00 87.51  ? 171 GLU D OE2 1 
ATOM   13716 N N   . ILE D 1 172 ? -4.031  51.638  56.472  1.00 72.45  ? 172 ILE D N   1 
ATOM   13717 C CA  . ILE D 1 172 ? -4.718  50.440  56.944  1.00 70.85  ? 172 ILE D CA  1 
ATOM   13718 C C   . ILE D 1 172 ? -5.509  50.709  58.218  1.00 74.30  ? 172 ILE D C   1 
ATOM   13719 O O   . ILE D 1 172 ? -6.407  49.927  58.558  1.00 71.55  ? 172 ILE D O   1 
ATOM   13720 C CB  . ILE D 1 172 ? -3.726  49.281  57.147  1.00 79.96  ? 172 ILE D CB  1 
ATOM   13721 C CG1 . ILE D 1 172 ? -4.436  47.937  56.976  1.00 81.35  ? 172 ILE D CG1 1 
ATOM   13722 C CG2 . ILE D 1 172 ? -3.075  49.351  58.518  1.00 70.82  ? 172 ILE D CG2 1 
ATOM   13723 C CD1 . ILE D 1 172 ? -5.276  47.851  55.718  1.00 73.05  ? 172 ILE D CD1 1 
ATOM   13724 N N   . ILE D 1 173 ? -5.198  51.790  58.936  1.00 76.39  ? 173 ILE D N   1 
ATOM   13725 C CA  . ILE D 1 173 ? -6.037  52.206  60.055  1.00 64.16  ? 173 ILE D CA  1 
ATOM   13726 C C   . ILE D 1 173 ? -7.374  52.733  59.545  1.00 65.99  ? 173 ILE D C   1 
ATOM   13727 O O   . ILE D 1 173 ? -8.425  52.503  60.157  1.00 63.63  ? 173 ILE D O   1 
ATOM   13728 C CB  . ILE D 1 173 ? -5.299  53.249  60.915  1.00 62.87  ? 173 ILE D CB  1 
ATOM   13729 C CG1 . ILE D 1 173 ? -4.266  52.569  61.814  1.00 61.27  ? 173 ILE D CG1 1 
ATOM   13730 C CG2 . ILE D 1 173 ? -6.274  54.050  61.764  1.00 64.00  ? 173 ILE D CG2 1 
ATOM   13731 C CD1 . ILE D 1 173 ? -3.268  53.528  62.424  1.00 60.45  ? 173 ILE D CD1 1 
ATOM   13732 N N   . LYS D 1 174 ? -7.356  53.443  58.414  1.00 67.95  ? 174 LYS D N   1 
ATOM   13733 C CA  . LYS D 1 174 ? -8.581  54.026  57.874  1.00 69.25  ? 174 LYS D CA  1 
ATOM   13734 C C   . LYS D 1 174 ? -9.543  52.950  57.381  1.00 69.86  ? 174 LYS D C   1 
ATOM   13735 O O   . LYS D 1 174 ? -10.753 53.032  57.628  1.00 69.26  ? 174 LYS D O   1 
ATOM   13736 C CB  . LYS D 1 174 ? -8.240  54.999  56.748  1.00 72.31  ? 174 LYS D CB  1 
ATOM   13737 C CG  . LYS D 1 174 ? -7.551  56.265  57.226  1.00 71.92  ? 174 LYS D CG  1 
ATOM   13738 C CD  . LYS D 1 174 ? -6.904  57.015  56.074  1.00 75.12  ? 174 LYS D CD  1 
ATOM   13739 C CE  . LYS D 1 174 ? -5.839  57.975  56.578  1.00 74.68  ? 174 LYS D CE  1 
ATOM   13740 N NZ  . LYS D 1 174 ? -6.361  59.363  56.704  1.00 75.16  ? 174 LYS D NZ  1 
ATOM   13741 N N   . LYS D 1 175 ? -9.030  51.933  56.688  1.00 71.15  ? 175 LYS D N   1 
ATOM   13742 C CA  . LYS D 1 175 ? -9.878  50.847  56.211  1.00 71.87  ? 175 LYS D CA  1 
ATOM   13743 C C   . LYS D 1 175 ? -10.285 49.890  57.324  1.00 69.01  ? 175 LYS D C   1 
ATOM   13744 O O   . LYS D 1 175 ? -11.070 48.971  57.069  1.00 69.37  ? 175 LYS D O   1 
ATOM   13745 C CB  . LYS D 1 175 ? -9.169  50.075  55.095  1.00 74.38  ? 175 LYS D CB  1 
ATOM   13746 C CG  . LYS D 1 175 ? -9.087  50.818  53.766  1.00 77.84  ? 175 LYS D CG  1 
ATOM   13747 C CD  . LYS D 1 175 ? -10.314 50.556  52.904  1.00 79.86  ? 175 LYS D CD  1 
ATOM   13748 C CE  . LYS D 1 175 ? -10.532 51.669  51.890  1.00 82.80  ? 175 LYS D CE  1 
ATOM   13749 N NZ  . LYS D 1 175 ? -9.475  51.690  50.840  1.00 85.58  ? 175 LYS D NZ  1 
ATOM   13750 N N   . THR D 1 176 ? -9.766  50.081  58.541  1.00 72.72  ? 176 THR D N   1 
ATOM   13751 C CA  . THR D 1 176 ? -10.079 49.173  59.641  1.00 66.15  ? 176 THR D CA  1 
ATOM   13752 C C   . THR D 1 176 ? -11.564 49.200  59.991  1.00 62.86  ? 176 THR D C   1 
ATOM   13753 O O   . THR D 1 176 ? -12.162 48.153  60.256  1.00 63.65  ? 176 THR D O   1 
ATOM   13754 C CB  . THR D 1 176 ? -9.228  49.521  60.865  1.00 61.20  ? 176 THR D CB  1 
ATOM   13755 O OG1 . THR D 1 176 ? -7.839  49.357  60.546  1.00 72.65  ? 176 THR D OG1 1 
ATOM   13756 C CG2 . THR D 1 176 ? -9.575  48.617  62.035  1.00 59.18  ? 176 THR D CG2 1 
ATOM   13757 N N   . LEU D 1 177 ? -12.179 50.380  60.006  1.00 63.09  ? 177 LEU D N   1 
ATOM   13758 C CA  . LEU D 1 177 ? -13.595 50.446  60.351  1.00 65.83  ? 177 LEU D CA  1 
ATOM   13759 C C   . LEU D 1 177 ? -14.481 50.009  59.191  1.00 67.73  ? 177 LEU D C   1 
ATOM   13760 O O   . LEU D 1 177 ? -15.536 49.402  59.409  1.00 64.39  ? 177 LEU D O   1 
ATOM   13761 C CB  . LEU D 1 177 ? -13.962 51.858  60.805  1.00 72.41  ? 177 LEU D CB  1 
ATOM   13762 C CG  . LEU D 1 177 ? -14.986 51.969  61.935  1.00 59.58  ? 177 LEU D CG  1 
ATOM   13763 C CD1 . LEU D 1 177 ? -14.301 51.733  63.256  1.00 56.74  ? 177 LEU D CD1 1 
ATOM   13764 C CD2 . LEU D 1 177 ? -15.633 53.334  61.918  1.00 62.53  ? 177 LEU D CD2 1 
ATOM   13765 N N   . SER D 1 178 ? -14.077 50.312  57.955  1.00 71.80  ? 178 SER D N   1 
ATOM   13766 C CA  . SER D 1 178 ? -14.852 49.855  56.808  1.00 74.26  ? 178 SER D CA  1 
ATOM   13767 C C   . SER D 1 178 ? -14.880 48.335  56.734  1.00 75.62  ? 178 SER D C   1 
ATOM   13768 O O   . SER D 1 178 ? -15.883 47.750  56.310  1.00 77.35  ? 178 SER D O   1 
ATOM   13769 C CB  . SER D 1 178 ? -14.286 50.439  55.512  1.00 73.82  ? 178 SER D CB  1 
ATOM   13770 O OG  . SER D 1 178 ? -13.092 49.776  55.131  1.00 74.18  ? 178 SER D OG  1 
ATOM   13771 N N   . ILE D 1 179 ? -13.799 47.679  57.166  1.00 72.29  ? 179 ILE D N   1 
ATOM   13772 C CA  . ILE D 1 179 ? -13.712 46.226  57.103  1.00 69.58  ? 179 ILE D CA  1 
ATOM   13773 C C   . ILE D 1 179 ? -14.653 45.529  58.072  1.00 75.59  ? 179 ILE D C   1 
ATOM   13774 O O   . ILE D 1 179 ? -14.752 44.295  58.045  1.00 76.06  ? 179 ILE D O   1 
ATOM   13775 C CB  . ILE D 1 179 ? -12.257 45.772  57.337  1.00 68.35  ? 179 ILE D CB  1 
ATOM   13776 C CG1 . ILE D 1 179 ? -11.937 44.556  56.467  1.00 70.34  ? 179 ILE D CG1 1 
ATOM   13777 C CG2 . ILE D 1 179 ? -12.003 45.465  58.800  1.00 65.03  ? 179 ILE D CG2 1 
ATOM   13778 C CD1 . ILE D 1 179 ? -11.789 44.891  55.008  1.00 77.78  ? 179 ILE D CD1 1 
ATOM   13779 N N   . TYR D 1 180 ? -15.382 46.280  58.899  1.00 76.47  ? 180 TYR D N   1 
ATOM   13780 C CA  . TYR D 1 180 ? -16.438 45.704  59.723  1.00 65.38  ? 180 TYR D CA  1 
ATOM   13781 C C   . TYR D 1 180 ? -17.837 45.988  59.197  1.00 70.10  ? 180 TYR D C   1 
ATOM   13782 O O   . TYR D 1 180 ? -18.736 45.167  59.402  1.00 64.47  ? 180 TYR D O   1 
ATOM   13783 C CB  . TYR D 1 180 ? -16.334 46.214  61.162  1.00 73.09  ? 180 TYR D CB  1 
ATOM   13784 C CG  . TYR D 1 180 ? -15.173 45.629  61.923  1.00 62.53  ? 180 TYR D CG  1 
ATOM   13785 C CD1 . TYR D 1 180 ? -15.165 44.292  62.292  1.00 63.25  ? 180 TYR D CD1 1 
ATOM   13786 C CD2 . TYR D 1 180 ? -14.078 46.411  62.259  1.00 57.74  ? 180 TYR D CD2 1 
ATOM   13787 C CE1 . TYR D 1 180 ? -14.104 43.752  62.986  1.00 56.24  ? 180 TYR D CE1 1 
ATOM   13788 C CE2 . TYR D 1 180 ? -13.010 45.880  62.951  1.00 56.27  ? 180 TYR D CE2 1 
ATOM   13789 C CZ  . TYR D 1 180 ? -13.027 44.550  63.311  1.00 55.53  ? 180 TYR D CZ  1 
ATOM   13790 O OH  . TYR D 1 180 ? -11.963 44.015  64.001  1.00 54.20  ? 180 TYR D OH  1 
ATOM   13791 N N   . ARG D 1 181 ? -18.047 47.123  58.523  1.00 70.66  ? 181 ARG D N   1 
ATOM   13792 C CA  . ARG D 1 181 ? -19.377 47.436  58.018  1.00 67.95  ? 181 ARG D CA  1 
ATOM   13793 C C   . ARG D 1 181 ? -19.774 46.520  56.874  1.00 77.70  ? 181 ARG D C   1 
ATOM   13794 O O   . ARG D 1 181 ? -20.927 46.082  56.803  1.00 88.89  ? 181 ARG D O   1 
ATOM   13795 C CB  . ARG D 1 181 ? -19.458 48.879  57.545  1.00 69.31  ? 181 ARG D CB  1 
ATOM   13796 C CG  . ARG D 1 181 ? -18.793 49.877  58.429  1.00 67.32  ? 181 ARG D CG  1 
ATOM   13797 C CD  . ARG D 1 181 ? -18.927 51.220  57.780  1.00 75.89  ? 181 ARG D CD  1 
ATOM   13798 N NE  . ARG D 1 181 ? -18.685 52.292  58.729  1.00 67.33  ? 181 ARG D NE  1 
ATOM   13799 C CZ  . ARG D 1 181 ? -17.731 53.200  58.598  1.00 67.75  ? 181 ARG D CZ  1 
ATOM   13800 N NH1 . ARG D 1 181 ? -16.883 53.171  57.582  1.00 69.91  ? 181 ARG D NH1 1 
ATOM   13801 N NH2 . ARG D 1 181 ? -17.625 54.161  59.510  1.00 66.07  ? 181 ARG D NH2 1 
ATOM   13802 N N   . GLU D 1 182 ? -18.855 46.251  55.945  1.00 87.65  ? 182 GLU D N   1 
ATOM   13803 C CA  . GLU D 1 182 ? -19.184 45.325  54.861  1.00 85.02  ? 182 GLU D CA  1 
ATOM   13804 C C   . GLU D 1 182 ? -19.620 43.971  55.402  1.00 87.46  ? 182 GLU D C   1 
ATOM   13805 O O   . GLU D 1 182 ? -20.785 43.605  55.264  1.00 88.15  ? 182 GLU D O   1 
ATOM   13806 C CB  . GLU D 1 182 ? -17.983 45.166  53.910  1.00 87.09  ? 182 GLU D CB  1 
ATOM   13807 C CG  . GLU D 1 182 ? -17.406 46.509  53.429  1.00 100.33 ? 182 GLU D CG  1 
ATOM   13808 C CD  . GLU D 1 182 ? -15.888 46.595  53.477  1.00 101.95 ? 182 GLU D CD  1 
ATOM   13809 O OE1 . GLU D 1 182 ? -15.231 45.570  53.732  1.00 97.15  ? 182 GLU D OE1 1 
ATOM   13810 O OE2 . GLU D 1 182 ? -15.355 47.704  53.251  1.00 104.74 ? 182 GLU D OE2 1 
ATOM   13811 N N   . ILE D 1 183 ? -18.756 43.311  56.189  1.00 84.36  ? 183 ILE D N   1 
ATOM   13812 C CA  . ILE D 1 183 ? -19.026 41.929  56.605  1.00 80.57  ? 183 ILE D CA  1 
ATOM   13813 C C   . ILE D 1 183 ? -20.404 41.807  57.250  1.00 73.00  ? 183 ILE D C   1 
ATOM   13814 O O   . ILE D 1 183 ? -21.011 40.731  57.226  1.00 70.37  ? 183 ILE D O   1 
ATOM   13815 C CB  . ILE D 1 183 ? -17.917 41.405  57.561  1.00 68.66  ? 183 ILE D CB  1 
ATOM   13816 C CG1 . ILE D 1 183 ? -18.044 42.000  58.967  1.00 74.31  ? 183 ILE D CG1 1 
ATOM   13817 C CG2 . ILE D 1 183 ? -16.542 41.685  56.993  1.00 69.69  ? 183 ILE D CG2 1 
ATOM   13818 C CD1 . ILE D 1 183 ? -18.618 41.030  59.997  1.00 73.91  ? 183 ILE D CD1 1 
ATOM   13819 N N   . LYS D 1 184 ? -20.928 42.898  57.822  1.00 69.24  ? 184 LYS D N   1 
ATOM   13820 C CA  . LYS D 1 184 ? -22.304 42.886  58.306  1.00 72.54  ? 184 LYS D CA  1 
ATOM   13821 C C   . LYS D 1 184 ? -23.298 42.924  57.149  1.00 80.30  ? 184 LYS D C   1 
ATOM   13822 O O   . LYS D 1 184 ? -24.357 42.288  57.214  1.00 81.75  ? 184 LYS D O   1 
ATOM   13823 C CB  . LYS D 1 184 ? -22.526 44.064  59.257  1.00 65.93  ? 184 LYS D CB  1 
ATOM   13824 C CG  . LYS D 1 184 ? -23.894 44.089  59.920  1.00 64.99  ? 184 LYS D CG  1 
ATOM   13825 C CD  . LYS D 1 184 ? -23.912 45.057  61.093  1.00 62.43  ? 184 LYS D CD  1 
ATOM   13826 C CE  . LYS D 1 184 ? -25.334 45.416  61.469  1.00 62.26  ? 184 LYS D CE  1 
ATOM   13827 N NZ  . LYS D 1 184 ? -26.220 44.231  61.331  1.00 63.70  ? 184 LYS D NZ  1 
ATOM   13828 N N   . GLU D 1 185 ? -22.981 43.670  56.084  1.00 83.96  ? 185 GLU D N   1 
ATOM   13829 C CA  . GLU D 1 185 ? -23.869 43.731  54.924  1.00 76.72  ? 185 GLU D CA  1 
ATOM   13830 C C   . GLU D 1 185 ? -23.822 42.442  54.105  1.00 78.81  ? 185 GLU D C   1 
ATOM   13831 O O   . GLU D 1 185 ? -24.869 41.893  53.744  1.00 80.25  ? 185 GLU D O   1 
ATOM   13832 C CB  . GLU D 1 185 ? -23.509 44.935  54.051  1.00 78.76  ? 185 GLU D CB  1 
ATOM   13833 C CG  . GLU D 1 185 ? -24.068 46.258  54.549  1.00 81.45  ? 185 GLU D CG  1 
ATOM   13834 C CD  . GLU D 1 185 ? -25.281 46.090  55.441  1.00 92.59  ? 185 GLU D CD  1 
ATOM   13835 O OE1 . GLU D 1 185 ? -26.373 45.802  54.907  1.00 97.89  ? 185 GLU D OE1 1 
ATOM   13836 O OE2 . GLU D 1 185 ? -25.145 46.246  56.673  1.00 86.33  ? 185 GLU D OE2 1 
ATOM   13837 N N   . GLU D 1 186 ? -22.622 41.931  53.803  1.00 80.52  ? 186 GLU D N   1 
ATOM   13838 C CA  . GLU D 1 186 ? -22.540 40.657  53.086  1.00 89.19  ? 186 GLU D CA  1 
ATOM   13839 C C   . GLU D 1 186 ? -23.067 39.476  53.892  1.00 90.12  ? 186 GLU D C   1 
ATOM   13840 O O   . GLU D 1 186 ? -23.269 38.403  53.314  1.00 92.49  ? 186 GLU D O   1 
ATOM   13841 C CB  . GLU D 1 186 ? -21.104 40.347  52.661  1.00 93.56  ? 186 GLU D CB  1 
ATOM   13842 C CG  . GLU D 1 186 ? -20.084 41.084  53.464  1.00 87.26  ? 186 GLU D CG  1 
ATOM   13843 C CD  . GLU D 1 186 ? -19.422 42.134  52.636  1.00 97.18  ? 186 GLU D CD  1 
ATOM   13844 O OE1 . GLU D 1 186 ? -20.054 43.105  52.194  1.00 104.15 ? 186 GLU D OE1 1 
ATOM   13845 O OE2 . GLU D 1 186 ? -18.206 42.026  52.493  1.00 106.77 ? 186 GLU D OE2 1 
ATOM   13846 N N   . GLY D 1 187 ? -23.287 39.631  55.194  1.00 76.28  ? 187 GLY D N   1 
ATOM   13847 C CA  . GLY D 1 187 ? -23.785 38.534  55.990  1.00 74.81  ? 187 GLY D CA  1 
ATOM   13848 C C   . GLY D 1 187 ? -22.753 37.508  56.396  1.00 74.07  ? 187 GLY D C   1 
ATOM   13849 O O   . GLY D 1 187 ? -23.126 36.477  56.970  1.00 78.43  ? 187 GLY D O   1 
ATOM   13850 N N   . LYS D 1 188 ? -21.468 37.750  56.129  1.00 73.81  ? 188 LYS D N   1 
ATOM   13851 C CA  . LYS D 1 188 ? -20.421 36.807  56.505  1.00 72.88  ? 188 LYS D CA  1 
ATOM   13852 C C   . LYS D 1 188 ? -20.062 36.871  57.982  1.00 79.24  ? 188 LYS D C   1 
ATOM   13853 O O   . LYS D 1 188 ? -19.229 36.076  58.432  1.00 73.70  ? 188 LYS D O   1 
ATOM   13854 C CB  . LYS D 1 188 ? -19.157 37.037  55.670  1.00 74.44  ? 188 LYS D CB  1 
ATOM   13855 C CG  . LYS D 1 188 ? -19.396 37.219  54.178  1.00 85.94  ? 188 LYS D CG  1 
ATOM   13856 C CD  . LYS D 1 188 ? -18.336 38.102  53.526  1.00 96.83  ? 188 LYS D CD  1 
ATOM   13857 C CE  . LYS D 1 188 ? -17.060 37.370  53.189  1.00 85.00  ? 188 LYS D CE  1 
ATOM   13858 N NZ  . LYS D 1 188 ? -15.944 38.351  53.080  1.00 79.74  ? 188 LYS D NZ  1 
ATOM   13859 N N   . GLY D 1 189 ? -20.647 37.792  58.741  1.00 74.78  ? 189 GLY D N   1 
ATOM   13860 C CA  . GLY D 1 189 ? -20.323 37.883  60.153  1.00 68.21  ? 189 GLY D CA  1 
ATOM   13861 C C   . GLY D 1 189 ? -21.249 38.834  60.875  1.00 70.76  ? 189 GLY D C   1 
ATOM   13862 O O   . GLY D 1 189 ? -21.992 39.605  60.262  1.00 74.25  ? 189 GLY D O   1 
ATOM   13863 N N   . SER D 1 190 ? -21.192 38.759  62.201  1.00 59.89  ? 190 SER D N   1 
ATOM   13864 C CA  . SER D 1 190 ? -21.925 39.655  63.079  1.00 58.09  ? 190 SER D CA  1 
ATOM   13865 C C   . SER D 1 190 ? -20.936 40.432  63.930  1.00 57.00  ? 190 SER D C   1 
ATOM   13866 O O   . SER D 1 190 ? -19.989 39.859  64.476  1.00 62.35  ? 190 SER D O   1 
ATOM   13867 C CB  . SER D 1 190 ? -22.889 38.895  63.989  1.00 56.77  ? 190 SER D CB  1 
ATOM   13868 O OG  . SER D 1 190 ? -23.687 39.791  64.746  1.00 70.20  ? 190 SER D OG  1 
ATOM   13869 N N   . VAL D 1 191 ? -21.158 41.737  64.040  1.00 55.54  ? 191 VAL D N   1 
ATOM   13870 C CA  . VAL D 1 191 ? -20.329 42.611  64.859  1.00 53.60  ? 191 VAL D CA  1 
ATOM   13871 C C   . VAL D 1 191 ? -21.161 43.076  66.043  1.00 54.18  ? 191 VAL D C   1 
ATOM   13872 O O   . VAL D 1 191 ? -22.267 43.598  65.868  1.00 57.40  ? 191 VAL D O   1 
ATOM   13873 C CB  . VAL D 1 191 ? -19.796 43.808  64.054  1.00 54.95  ? 191 VAL D CB  1 
ATOM   13874 C CG1 . VAL D 1 191 ? -18.550 44.373  64.720  1.00 53.35  ? 191 VAL D CG1 1 
ATOM   13875 C CG2 . VAL D 1 191 ? -19.497 43.390  62.627  1.00 57.78  ? 191 VAL D CG2 1 
ATOM   13876 N N   . SER D 1 192 ? -20.635 42.874  67.241  1.00 49.18  ? 192 SER D N   1 
ATOM   13877 C CA  . SER D 1 192 ? -21.286 43.285  68.471  1.00 49.94  ? 192 SER D CA  1 
ATOM   13878 C C   . SER D 1 192 ? -20.476 44.399  69.121  1.00 51.10  ? 192 SER D C   1 
ATOM   13879 O O   . SER D 1 192 ? -19.446 44.839  68.604  1.00 47.62  ? 192 SER D O   1 
ATOM   13880 C CB  . SER D 1 192 ? -21.445 42.094  69.415  1.00 45.65  ? 192 SER D CB  1 
ATOM   13881 O OG  . SER D 1 192 ? -20.182 41.637  69.852  1.00 44.66  ? 192 SER D OG  1 
ATOM   13882 N N   . THR D 1 193 ? -20.955 44.859  70.272  1.00 43.87  ? 193 THR D N   1 
ATOM   13883 C CA  . THR D 1 193 ? -20.246 45.853  71.062  1.00 50.29  ? 193 THR D CA  1 
ATOM   13884 C C   . THR D 1 193 ? -20.438 45.526  72.536  1.00 48.87  ? 193 THR D C   1 
ATOM   13885 O O   . THR D 1 193 ? -21.026 44.502  72.893  1.00 45.89  ? 193 THR D O   1 
ATOM   13886 C CB  . THR D 1 193 ? -20.712 47.272  70.712  1.00 46.87  ? 193 THR D CB  1 
ATOM   13887 O OG1 . THR D 1 193 ? -19.767 48.226  71.215  1.00 42.25  ? 193 THR D OG1 1 
ATOM   13888 C CG2 . THR D 1 193 ? -22.090 47.552  71.290  1.00 42.64  ? 193 THR D CG2 1 
ATOM   13889 N N   . SER D 1 194 ? -19.913 46.392  73.397  1.00 53.09  ? 194 SER D N   1 
ATOM   13890 C CA  . SER D 1 194 ? -19.996 46.222  74.843  1.00 41.55  ? 194 SER D CA  1 
ATOM   13891 C C   . SER D 1 194 ? -20.390 47.558  75.459  1.00 41.81  ? 194 SER D C   1 
ATOM   13892 O O   . SER D 1 194 ? -20.435 48.564  74.743  1.00 48.03  ? 194 SER D O   1 
ATOM   13893 C CB  . SER D 1 194 ? -18.659 45.724  75.401  1.00 35.56  ? 194 SER D CB  1 
ATOM   13894 O OG  . SER D 1 194 ? -18.541 44.316  75.271  1.00 36.58  ? 194 SER D OG  1 
ATOM   13895 N N   . PRO D 1 195 ? -20.704 47.623  76.759  1.00 43.09  ? 195 PRO D N   1 
ATOM   13896 C CA  . PRO D 1 195 ? -20.904 48.933  77.387  1.00 33.57  ? 195 PRO D CA  1 
ATOM   13897 C C   . PRO D 1 195 ? -19.671 49.801  77.196  1.00 33.72  ? 195 PRO D C   1 
ATOM   13898 O O   . PRO D 1 195 ? -18.540 49.311  77.191  1.00 36.56  ? 195 PRO D O   1 
ATOM   13899 C CB  . PRO D 1 195 ? -21.138 48.587  78.859  1.00 37.44  ? 195 PRO D CB  1 
ATOM   13900 C CG  . PRO D 1 195 ? -21.751 47.236  78.819  1.00 31.76  ? 195 PRO D CG  1 
ATOM   13901 C CD  . PRO D 1 195 ? -21.102 46.520  77.657  1.00 35.97  ? 195 PRO D CD  1 
ATOM   13902 N N   . TYR D 1 196 ? -19.911 51.106  77.035  1.00 34.27  ? 196 TYR D N   1 
ATOM   13903 C CA  . TYR D 1 196 ? -18.975 52.003  76.359  1.00 35.25  ? 196 TYR D CA  1 
ATOM   13904 C C   . TYR D 1 196 ? -17.514 51.805  76.755  1.00 34.46  ? 196 TYR D C   1 
ATOM   13905 O O   . TYR D 1 196 ? -16.657 51.568  75.896  1.00 35.47  ? 196 TYR D O   1 
ATOM   13906 C CB  . TYR D 1 196 ? -19.386 53.462  76.590  1.00 35.49  ? 196 TYR D CB  1 
ATOM   13907 C CG  . TYR D 1 196 ? -18.929 54.367  75.467  1.00 39.42  ? 196 TYR D CG  1 
ATOM   13908 C CD1 . TYR D 1 196 ? -17.603 54.774  75.376  1.00 37.40  ? 196 TYR D CD1 1 
ATOM   13909 C CD2 . TYR D 1 196 ? -19.813 54.792  74.483  1.00 46.50  ? 196 TYR D CD2 1 
ATOM   13910 C CE1 . TYR D 1 196 ? -17.174 55.589  74.350  1.00 39.18  ? 196 TYR D CE1 1 
ATOM   13911 C CE2 . TYR D 1 196 ? -19.391 55.608  73.449  1.00 45.90  ? 196 TYR D CE2 1 
ATOM   13912 C CZ  . TYR D 1 196 ? -18.070 56.002  73.388  1.00 40.94  ? 196 TYR D CZ  1 
ATOM   13913 O OH  . TYR D 1 196 ? -17.641 56.815  72.363  1.00 42.87  ? 196 TYR D OH  1 
ATOM   13914 N N   . TYR D 1 197 ? -17.204 51.905  78.048  1.00 32.78  ? 197 TYR D N   1 
ATOM   13915 C CA  . TYR D 1 197 ? -15.820 51.885  78.508  1.00 32.11  ? 197 TYR D CA  1 
ATOM   13916 C C   . TYR D 1 197 ? -15.453 50.572  79.194  1.00 30.94  ? 197 TYR D C   1 
ATOM   13917 O O   . TYR D 1 197 ? -14.561 50.540  80.046  1.00 33.33  ? 197 TYR D O   1 
ATOM   13918 C CB  . TYR D 1 197 ? -15.551 53.073  79.429  1.00 31.35  ? 197 TYR D CB  1 
ATOM   13919 C CG  . TYR D 1 197 ? -15.682 54.408  78.729  1.00 32.68  ? 197 TYR D CG  1 
ATOM   13920 C CD1 . TYR D 1 197 ? -14.676 54.876  77.893  1.00 33.88  ? 197 TYR D CD1 1 
ATOM   13921 C CD2 . TYR D 1 197 ? -16.813 55.195  78.897  1.00 32.87  ? 197 TYR D CD2 1 
ATOM   13922 C CE1 . TYR D 1 197 ? -14.793 56.090  77.245  1.00 35.25  ? 197 TYR D CE1 1 
ATOM   13923 C CE2 . TYR D 1 197 ? -16.937 56.413  78.255  1.00 34.23  ? 197 TYR D CE2 1 
ATOM   13924 C CZ  . TYR D 1 197 ? -15.925 56.854  77.431  1.00 35.43  ? 197 TYR D CZ  1 
ATOM   13925 O OH  . TYR D 1 197 ? -16.044 58.064  76.789  1.00 44.83  ? 197 TYR D OH  1 
ATOM   13926 N N   . HIS D 1 198 ? -16.128 49.482  78.821  1.00 31.20  ? 198 HIS D N   1 
ATOM   13927 C CA  . HIS D 1 198 ? -15.838 48.136  79.309  1.00 32.69  ? 198 HIS D CA  1 
ATOM   13928 C C   . HIS D 1 198 ? -15.908 48.041  80.832  1.00 32.77  ? 198 HIS D C   1 
ATOM   13929 O O   . HIS D 1 198 ? -14.926 47.632  81.465  1.00 34.83  ? 198 HIS D O   1 
ATOM   13930 C CB  . HIS D 1 198 ? -14.453 47.703  78.821  1.00 30.94  ? 198 HIS D CB  1 
ATOM   13931 C CG  . HIS D 1 198 ? -14.268 46.221  78.747  1.00 30.96  ? 198 HIS D CG  1 
ATOM   13932 N ND1 . HIS D 1 198 ? -13.403 45.540  79.576  1.00 30.02  ? 198 HIS D ND1 1 
ATOM   13933 C CD2 . HIS D 1 198 ? -14.813 45.292  77.927  1.00 34.55  ? 198 HIS D CD2 1 
ATOM   13934 C CE1 . HIS D 1 198 ? -13.435 44.253  79.281  1.00 31.96  ? 198 HIS D CE1 1 
ATOM   13935 N NE2 . HIS D 1 198 ? -14.282 44.076  78.282  1.00 31.62  ? 198 HIS D NE2 1 
ATOM   13936 N N   . PRO D 1 199 ? -17.030 48.391  81.459  1.00 29.60  ? 199 PRO D N   1 
ATOM   13937 C CA  . PRO D 1 199 ? -17.112 48.336  82.919  1.00 27.71  ? 199 PRO D CA  1 
ATOM   13938 C C   . PRO D 1 199 ? -17.673 47.013  83.426  1.00 31.46  ? 199 PRO D C   1 
ATOM   13939 O O   . PRO D 1 199 ? -18.303 46.244  82.697  1.00 37.79  ? 199 PRO D O   1 
ATOM   13940 C CB  . PRO D 1 199 ? -18.064 49.495  83.249  1.00 26.48  ? 199 PRO D CB  1 
ATOM   13941 C CG  . PRO D 1 199 ? -18.938 49.630  82.024  1.00 27.86  ? 199 PRO D CG  1 
ATOM   13942 C CD  . PRO D 1 199 ? -18.286 48.890  80.876  1.00 28.90  ? 199 PRO D CD  1 
ATOM   13943 N N   . LEU D 1 200 ? -17.423 46.760  84.710  1.00 31.25  ? 200 LEU D N   1 
ATOM   13944 C CA  . LEU D 1 200 ? -17.968 45.592  85.402  1.00 31.96  ? 200 LEU D CA  1 
ATOM   13945 C C   . LEU D 1 200 ? -19.411 45.903  85.781  1.00 32.45  ? 200 LEU D C   1 
ATOM   13946 O O   . LEU D 1 200 ? -19.701 46.409  86.867  1.00 33.64  ? 200 LEU D O   1 
ATOM   13947 C CB  . LEU D 1 200 ? -17.125 45.240  86.620  1.00 23.72  ? 200 LEU D CB  1 
ATOM   13948 C CG  . LEU D 1 200 ? -15.821 44.480  86.370  1.00 24.59  ? 200 LEU D CG  1 
ATOM   13949 C CD1 . LEU D 1 200 ? -15.414 43.710  87.616  1.00 22.52  ? 200 LEU D CD1 1 
ATOM   13950 C CD2 . LEU D 1 200 ? -15.959 43.544  85.177  1.00 24.47  ? 200 LEU D CD2 1 
ATOM   13951 N N   . ILE D 1 201 ? -20.327 45.585  84.861  1.00 24.97  ? 201 ILE D N   1 
ATOM   13952 C CA  . ILE D 1 201 ? -21.721 46.010  85.017  1.00 25.09  ? 201 ILE D CA  1 
ATOM   13953 C C   . ILE D 1 201 ? -22.374 45.469  86.287  1.00 28.65  ? 201 ILE D C   1 
ATOM   13954 O O   . ILE D 1 201 ? -23.014 46.255  87.004  1.00 32.92  ? 201 ILE D O   1 
ATOM   13955 C CB  . ILE D 1 201 ? -22.521 45.660  83.748  1.00 26.47  ? 201 ILE D CB  1 
ATOM   13956 C CG1 . ILE D 1 201 ? -21.941 46.400  82.543  1.00 27.55  ? 201 ILE D CG1 1 
ATOM   13957 C CG2 . ILE D 1 201 ? -23.985 46.007  83.928  1.00 26.70  ? 201 ILE D CG2 1 
ATOM   13958 C CD1 . ILE D 1 201 ? -22.069 47.904  82.639  1.00 33.03  ? 201 ILE D CD1 1 
ATOM   13959 N N   . PRO D 1 202 ? -22.270 44.176  86.625  1.00 23.90  ? 202 PRO D N   1 
ATOM   13960 C CA  . PRO D 1 202 ? -22.957 43.699  87.840  1.00 23.15  ? 202 PRO D CA  1 
ATOM   13961 C C   . PRO D 1 202 ? -22.533 44.423  89.103  1.00 22.14  ? 202 PRO D C   1 
ATOM   13962 O O   . PRO D 1 202 ? -23.355 44.594  90.012  1.00 24.19  ? 202 PRO D O   1 
ATOM   13963 C CB  . PRO D 1 202 ? -22.587 42.211  87.890  1.00 25.16  ? 202 PRO D CB  1 
ATOM   13964 C CG  . PRO D 1 202 ? -22.287 41.854  86.480  1.00 32.78  ? 202 PRO D CG  1 
ATOM   13965 C CD  . PRO D 1 202 ? -21.615 43.064  85.912  1.00 24.72  ? 202 PRO D CD  1 
ATOM   13966 N N   . ILE D 1 203 ? -21.273 44.849  89.192  1.00 21.73  ? 203 ILE D N   1 
ATOM   13967 C CA  . ILE D 1 203 ? -20.835 45.653  90.328  1.00 20.88  ? 203 ILE D CA  1 
ATOM   13968 C C   . ILE D 1 203 ? -21.519 47.014  90.315  1.00 21.01  ? 203 ILE D C   1 
ATOM   13969 O O   . ILE D 1 203 ? -21.983 47.503  91.352  1.00 20.49  ? 203 ILE D O   1 
ATOM   13970 C CB  . ILE D 1 203 ? -19.301 45.793  90.320  1.00 20.69  ? 203 ILE D CB  1 
ATOM   13971 C CG1 . ILE D 1 203 ? -18.636 44.432  90.548  1.00 20.57  ? 203 ILE D CG1 1 
ATOM   13972 C CG2 . ILE D 1 203 ? -18.856 46.813  91.361  1.00 20.26  ? 203 ILE D CG2 1 
ATOM   13973 C CD1 . ILE D 1 203 ? -17.228 44.511  91.117  1.00 22.24  ? 203 ILE D CD1 1 
ATOM   13974 N N   . LEU D 1 204 ? -21.599 47.645  89.141  1.00 24.73  ? 204 LEU D N   1 
ATOM   13975 C CA  . LEU D 1 204 ? -22.153 48.992  89.049  1.00 22.14  ? 204 LEU D CA  1 
ATOM   13976 C C   . LEU D 1 204 ? -23.640 49.021  89.380  1.00 22.26  ? 204 LEU D C   1 
ATOM   13977 O O   . LEU D 1 204 ? -24.148 50.047  89.843  1.00 24.40  ? 204 LEU D O   1 
ATOM   13978 C CB  . LEU D 1 204 ? -21.909 49.563  87.651  1.00 23.20  ? 204 LEU D CB  1 
ATOM   13979 C CG  . LEU D 1 204 ? -20.689 50.467  87.457  1.00 23.28  ? 204 LEU D CG  1 
ATOM   13980 C CD1 . LEU D 1 204 ? -19.471 49.931  88.196  1.00 22.44  ? 204 LEU D CD1 1 
ATOM   13981 C CD2 . LEU D 1 204 ? -20.382 50.631  85.976  1.00 24.48  ? 204 LEU D CD2 1 
ATOM   13982 N N   . LEU D 1 205 ? -24.352 47.919  89.147  1.00 23.22  ? 205 LEU D N   1 
ATOM   13983 C CA  . LEU D 1 205 ? -25.769 47.863  89.491  1.00 22.71  ? 205 LEU D CA  1 
ATOM   13984 C C   . LEU D 1 205 ? -25.969 47.480  90.951  1.00 26.27  ? 205 LEU D C   1 
ATOM   13985 O O   . LEU D 1 205 ? -26.673 48.172  91.694  1.00 28.85  ? 205 LEU D O   1 
ATOM   13986 C CB  . LEU D 1 205 ? -26.491 46.871  88.581  1.00 23.56  ? 205 LEU D CB  1 
ATOM   13987 C CG  . LEU D 1 205 ? -26.488 47.186  87.087  1.00 24.74  ? 205 LEU D CG  1 
ATOM   13988 C CD1 . LEU D 1 205 ? -26.707 45.916  86.296  1.00 25.46  ? 205 LEU D CD1 1 
ATOM   13989 C CD2 . LEU D 1 205 ? -27.562 48.209  86.764  1.00 25.52  ? 205 LEU D CD2 1 
ATOM   13990 N N   . ASN D 1 206 ? -25.352 46.379  91.376  1.00 25.42  ? 206 ASN D N   1 
ATOM   13991 C CA  . ASN D 1 206 ? -25.512 45.855  92.730  1.00 20.59  ? 206 ASN D CA  1 
ATOM   13992 C C   . ASN D 1 206 ? -24.159 45.321  93.179  1.00 21.82  ? 206 ASN D C   1 
ATOM   13993 O O   . ASN D 1 206 ? -23.773 44.201  92.807  1.00 25.64  ? 206 ASN D O   1 
ATOM   13994 C CB  . ASN D 1 206 ? -26.584 44.769  92.774  1.00 26.69  ? 206 ASN D CB  1 
ATOM   13995 C CG  . ASN D 1 206 ? -26.811 44.222  94.169  1.00 37.78  ? 206 ASN D CG  1 
ATOM   13996 O OD1 . ASN D 1 206 ? -26.355 44.791  95.160  1.00 27.44  ? 206 ASN D OD1 1 
ATOM   13997 N ND2 . ASN D 1 206 ? -27.526 43.106  94.251  1.00 44.58  ? 206 ASN D ND2 1 
ATOM   13998 N N   . PRO D 1 207 ? -23.412 46.089  93.976  1.00 20.53  ? 207 PRO D N   1 
ATOM   13999 C CA  . PRO D 1 207 ? -22.070 45.642  94.381  1.00 18.98  ? 207 PRO D CA  1 
ATOM   14000 C C   . PRO D 1 207 ? -22.072 44.341  95.161  1.00 18.77  ? 207 PRO D C   1 
ATOM   14001 O O   . PRO D 1 207 ? -21.025 43.690  95.249  1.00 20.30  ? 207 PRO D O   1 
ATOM   14002 C CB  . PRO D 1 207 ? -21.558 46.808  95.239  1.00 18.54  ? 207 PRO D CB  1 
ATOM   14003 C CG  . PRO D 1 207 ? -22.350 47.988  94.768  1.00 18.91  ? 207 PRO D CG  1 
ATOM   14004 C CD  . PRO D 1 207 ? -23.714 47.435  94.487  1.00 20.49  ? 207 PRO D CD  1 
ATOM   14005 N N   . ASN D 1 208 ? -23.211 43.936  95.719  1.00 18.83  ? 208 ASN D N   1 
ATOM   14006 C CA  . ASN D 1 208 ? -23.297 42.705  96.495  1.00 23.32  ? 208 ASN D CA  1 
ATOM   14007 C C   . ASN D 1 208 ? -23.150 41.447  95.646  1.00 20.83  ? 208 ASN D C   1 
ATOM   14008 O O   . ASN D 1 208 ? -23.164 40.346  96.208  1.00 20.48  ? 208 ASN D O   1 
ATOM   14009 C CB  . ASN D 1 208 ? -24.625 42.660  97.253  1.00 27.22  ? 208 ASN D CB  1 
ATOM   14010 C CG  . ASN D 1 208 ? -24.751 43.774  98.273  1.00 23.19  ? 208 ASN D CG  1 
ATOM   14011 O OD1 . ASN D 1 208 ? -24.054 43.784  99.287  1.00 25.73  ? 208 ASN D OD1 1 
ATOM   14012 N ND2 . ASN D 1 208 ? -25.642 44.722  98.007  1.00 24.02  ? 208 ASN D ND2 1 
ATOM   14013 N N   . CYS D 1 209 ? -23.013 41.570  94.323  1.00 20.61  ? 209 CYS D N   1 
ATOM   14014 C CA  . CYS D 1 209 ? -22.840 40.390  93.486  1.00 28.88  ? 209 CYS D CA  1 
ATOM   14015 C C   . CYS D 1 209 ? -21.529 39.670  93.767  1.00 28.48  ? 209 CYS D C   1 
ATOM   14016 O O   . CYS D 1 209 ? -21.413 38.478  93.461  1.00 32.57  ? 209 CYS D O   1 
ATOM   14017 C CB  . CYS D 1 209 ? -22.914 40.771  92.006  1.00 31.83  ? 209 CYS D CB  1 
ATOM   14018 S SG  . CYS D 1 209 ? -21.737 42.040  91.486  1.00 56.72  ? 209 CYS D SG  1 
ATOM   14019 N N   . VAL D 1 210 ? -20.542 40.362  94.343  1.00 22.61  ? 210 VAL D N   1 
ATOM   14020 C CA  . VAL D 1 210 ? -19.284 39.721  94.704  1.00 22.66  ? 210 VAL D CA  1 
ATOM   14021 C C   . VAL D 1 210 ? -19.496 38.644  95.757  1.00 22.90  ? 210 VAL D C   1 
ATOM   14022 O O   . VAL D 1 210 ? -18.696 37.709  95.859  1.00 21.50  ? 210 VAL D O   1 
ATOM   14023 C CB  . VAL D 1 210 ? -18.259 40.771  95.190  1.00 19.03  ? 210 VAL D CB  1 
ATOM   14024 C CG1 . VAL D 1 210 ? -18.094 41.875  94.156  1.00 19.14  ? 210 VAL D CG1 1 
ATOM   14025 C CG2 . VAL D 1 210 ? -18.673 41.353  96.535  1.00 19.58  ? 210 VAL D CG2 1 
ATOM   14026 N N   . TYR D 1 211 ? -20.569 38.746  96.542  1.00 26.37  ? 211 TYR D N   1 
ATOM   14027 C CA  . TYR D 1 211 ? -20.806 37.826  97.646  1.00 24.83  ? 211 TYR D CA  1 
ATOM   14028 C C   . TYR D 1 211 ? -21.498 36.540  97.215  1.00 24.35  ? 211 TYR D C   1 
ATOM   14029 O O   . TYR D 1 211 ? -21.653 35.635  98.042  1.00 23.95  ? 211 TYR D O   1 
ATOM   14030 C CB  . TYR D 1 211 ? -21.627 38.529  98.729  1.00 19.12  ? 211 TYR D CB  1 
ATOM   14031 C CG  . TYR D 1 211 ? -20.894 39.691  99.355  1.00 18.54  ? 211 TYR D CG  1 
ATOM   14032 C CD1 . TYR D 1 211 ? -19.725 39.487  100.077 1.00 18.43  ? 211 TYR D CD1 1 
ATOM   14033 C CD2 . TYR D 1 211 ? -21.358 40.992  99.215  1.00 18.23  ? 211 TYR D CD2 1 
ATOM   14034 C CE1 . TYR D 1 211 ? -19.045 40.544  100.649 1.00 19.06  ? 211 TYR D CE1 1 
ATOM   14035 C CE2 . TYR D 1 211 ? -20.684 42.057  99.784  1.00 21.13  ? 211 TYR D CE2 1 
ATOM   14036 C CZ  . TYR D 1 211 ? -19.527 41.826  100.500 1.00 21.85  ? 211 TYR D CZ  1 
ATOM   14037 O OH  . TYR D 1 211 ? -18.848 42.880  101.071 1.00 23.68  ? 211 TYR D OH  1 
ATOM   14038 N N   . GLU D 1 212 ? -21.911 36.433  95.952  1.00 30.54  ? 212 GLU D N   1 
ATOM   14039 C CA  . GLU D 1 212 ? -22.554 35.210  95.485  1.00 25.99  ? 212 GLU D CA  1 
ATOM   14040 C C   . GLU D 1 212 ? -21.549 34.089  95.244  1.00 26.15  ? 212 GLU D C   1 
ATOM   14041 O O   . GLU D 1 212 ? -21.894 32.913  95.401  1.00 34.27  ? 212 GLU D O   1 
ATOM   14042 C CB  . GLU D 1 212 ? -23.358 35.491  94.214  1.00 32.55  ? 212 GLU D CB  1 
ATOM   14043 C CG  . GLU D 1 212 ? -24.810 35.865  94.488  1.00 48.16  ? 212 GLU D CG  1 
ATOM   14044 C CD  . GLU D 1 212 ? -25.720 35.613  93.302  1.00 61.93  ? 212 GLU D CD  1 
ATOM   14045 O OE1 . GLU D 1 212 ? -25.688 36.417  92.346  1.00 59.40  ? 212 GLU D OE1 1 
ATOM   14046 O OE2 . GLU D 1 212 ? -26.472 34.614  93.331  1.00 48.60  ? 212 GLU D OE2 1 
ATOM   14047 N N   . THR D 1 213 ? -20.319 34.423  94.860  1.00 25.61  ? 213 THR D N   1 
ATOM   14048 C CA  . THR D 1 213 ? -19.251 33.439  94.714  1.00 22.43  ? 213 THR D CA  1 
ATOM   14049 C C   . THR D 1 213 ? -18.203 33.521  95.813  1.00 27.37  ? 213 THR D C   1 
ATOM   14050 O O   . THR D 1 213 ? -17.677 32.486  96.230  1.00 36.57  ? 213 THR D O   1 
ATOM   14051 C CB  . THR D 1 213 ? -18.563 33.591  93.352  1.00 22.84  ? 213 THR D CB  1 
ATOM   14052 O OG1 . THR D 1 213 ? -19.543 33.881  92.347  1.00 23.81  ? 213 THR D OG1 1 
ATOM   14053 C CG2 . THR D 1 213 ? -17.828 32.310  92.981  1.00 28.89  ? 213 THR D CG2 1 
ATOM   14054 N N   . THR D 1 214 ? -17.885 34.721  96.294  1.00 26.33  ? 214 THR D N   1 
ATOM   14055 C CA  . THR D 1 214 ? -16.943 34.911  97.400  1.00 25.14  ? 214 THR D CA  1 
ATOM   14056 C C   . THR D 1 214 ? -17.652 35.630  98.540  1.00 28.45  ? 214 THR D C   1 
ATOM   14057 O O   . THR D 1 214 ? -17.739 36.870  98.538  1.00 33.68  ? 214 THR D O   1 
ATOM   14058 C CB  . THR D 1 214 ? -15.714 35.697  96.947  1.00 20.57  ? 214 THR D CB  1 
ATOM   14059 O OG1 . THR D 1 214 ? -16.129 36.898  96.285  1.00 32.03  ? 214 THR D OG1 1 
ATOM   14060 C CG2 . THR D 1 214 ? -14.874 34.864  95.990  1.00 26.54  ? 214 THR D CG2 1 
ATOM   14061 N N   . PRO D 1 215 ? -18.175 34.902  99.533  1.00 26.25  ? 215 PRO D N   1 
ATOM   14062 C CA  . PRO D 1 215 ? -19.039 35.542  100.540 1.00 26.52  ? 215 PRO D CA  1 
ATOM   14063 C C   . PRO D 1 215 ? -18.322 36.375  101.594 1.00 30.41  ? 215 PRO D C   1 
ATOM   14064 O O   . PRO D 1 215 ? -18.967 37.244  102.193 1.00 32.93  ? 215 PRO D O   1 
ATOM   14065 C CB  . PRO D 1 215 ? -19.755 34.349  101.190 1.00 27.07  ? 215 PRO D CB  1 
ATOM   14066 C CG  . PRO D 1 215 ? -18.841 33.187  100.951 1.00 21.40  ? 215 PRO D CG  1 
ATOM   14067 C CD  . PRO D 1 215 ? -18.224 33.433  99.609  1.00 25.70  ? 215 PRO D CD  1 
ATOM   14068 N N   . ASN D 1 216 ? -17.034 36.152  101.854 1.00 30.08  ? 216 ASN D N   1 
ATOM   14069 C CA  . ASN D 1 216 ? -16.394 36.814  102.988 1.00 38.31  ? 216 ASN D CA  1 
ATOM   14070 C C   . ASN D 1 216 ? -15.219 37.692  102.569 1.00 37.44  ? 216 ASN D C   1 
ATOM   14071 O O   . ASN D 1 216 ? -14.152 37.651  103.190 1.00 40.52  ? 216 ASN D O   1 
ATOM   14072 C CB  . ASN D 1 216 ? -15.936 35.780  104.017 1.00 46.83  ? 216 ASN D CB  1 
ATOM   14073 C CG  . ASN D 1 216 ? -17.002 35.484  105.055 1.00 52.72  ? 216 ASN D CG  1 
ATOM   14074 O OD1 . ASN D 1 216 ? -17.279 36.305  105.930 1.00 36.12  ? 216 ASN D OD1 1 
ATOM   14075 N ND2 . ASN D 1 216 ? -17.608 34.305  104.963 1.00 41.93  ? 216 ASN D ND2 1 
ATOM   14076 N N   . VAL D 1 217 ? -15.414 38.505  101.535 1.00 27.10  ? 217 VAL D N   1 
ATOM   14077 C CA  . VAL D 1 217 ? -14.363 39.341  100.968 1.00 26.64  ? 217 VAL D CA  1 
ATOM   14078 C C   . VAL D 1 217 ? -14.631 40.796  101.336 1.00 36.72  ? 217 VAL D C   1 
ATOM   14079 O O   . VAL D 1 217 ? -15.784 41.244  101.351 1.00 36.09  ? 217 VAL D O   1 
ATOM   14080 C CB  . VAL D 1 217 ? -14.280 39.148  99.440  1.00 23.84  ? 217 VAL D CB  1 
ATOM   14081 C CG1 . VAL D 1 217 ? -15.649 39.316  98.803  1.00 27.18  ? 217 VAL D CG1 1 
ATOM   14082 C CG2 . VAL D 1 217 ? -13.275 40.096  98.830  1.00 25.44  ? 217 VAL D CG2 1 
ATOM   14083 N N   . LYS D 1 218 ? -13.560 41.528  101.641 1.00 34.83  ? 218 LYS D N   1 
ATOM   14084 C CA  . LYS D 1 218 ? -13.654 42.923  102.063 1.00 34.81  ? 218 LYS D CA  1 
ATOM   14085 C C   . LYS D 1 218 ? -13.715 43.841  100.847 1.00 31.65  ? 218 LYS D C   1 
ATOM   14086 O O   . LYS D 1 218 ? -12.774 43.883  100.044 1.00 23.93  ? 218 LYS D O   1 
ATOM   14087 C CB  . LYS D 1 218 ? -12.453 43.283  102.937 1.00 37.95  ? 218 LYS D CB  1 
ATOM   14088 C CG  . LYS D 1 218 ? -12.701 44.344  104.008 1.00 26.20  ? 218 LYS D CG  1 
ATOM   14089 C CD  . LYS D 1 218 ? -14.100 44.269  104.591 1.00 34.93  ? 218 LYS D CD  1 
ATOM   14090 C CE  . LYS D 1 218 ? -14.172 45.002  105.925 1.00 50.79  ? 218 LYS D CE  1 
ATOM   14091 N NZ  . LYS D 1 218 ? -15.566 45.139  106.431 1.00 49.57  ? 218 LYS D NZ  1 
ATOM   14092 N N   . ILE D 1 219 ? -14.819 44.572  100.713 1.00 32.95  ? 219 ILE D N   1 
ATOM   14093 C CA  . ILE D 1 219 ? -14.957 45.592  99.673  1.00 31.80  ? 219 ILE D CA  1 
ATOM   14094 C C   . ILE D 1 219 ? -15.455 46.874  100.328 1.00 26.39  ? 219 ILE D C   1 
ATOM   14095 O O   . ILE D 1 219 ? -16.080 46.835  101.397 1.00 30.97  ? 219 ILE D O   1 
ATOM   14096 C CB  . ILE D 1 219 ? -15.907 45.134  98.542  1.00 31.97  ? 219 ILE D CB  1 
ATOM   14097 C CG1 . ILE D 1 219 ? -17.316 44.876  99.074  1.00 32.79  ? 219 ILE D CG1 1 
ATOM   14098 C CG2 . ILE D 1 219 ? -15.353 43.896  97.845  1.00 33.45  ? 219 ILE D CG2 1 
ATOM   14099 C CD1 . ILE D 1 219 ? -18.385 44.916  98.001  1.00 23.96  ? 219 ILE D CD1 1 
ATOM   14100 N N   . PRO D 1 220 ? -15.184 48.028  99.723  1.00 23.99  ? 220 PRO D N   1 
ATOM   14101 C CA  . PRO D 1 220 ? -15.519 49.303  100.371 1.00 25.48  ? 220 PRO D CA  1 
ATOM   14102 C C   . PRO D 1 220 ? -17.021 49.531  100.459 1.00 29.80  ? 220 PRO D C   1 
ATOM   14103 O O   . PRO D 1 220 ? -17.841 48.773  99.935  1.00 32.47  ? 220 PRO D O   1 
ATOM   14104 C CB  . PRO D 1 220 ? -14.851 50.350  99.472  1.00 29.44  ? 220 PRO D CB  1 
ATOM   14105 C CG  . PRO D 1 220 ? -13.898 49.585  98.597  1.00 25.75  ? 220 PRO D CG  1 
ATOM   14106 C CD  . PRO D 1 220 ? -14.483 48.227  98.447  1.00 17.56  ? 220 PRO D CD  1 
ATOM   14107 N N   . ASP D 1 221 ? -17.371 50.617  101.146 1.00 25.07  ? 221 ASP D N   1 
ATOM   14108 C CA  . ASP D 1 221 ? -18.762 50.989  101.381 1.00 27.12  ? 221 ASP D CA  1 
ATOM   14109 C C   . ASP D 1 221 ? -19.253 51.841  100.216 1.00 31.95  ? 221 ASP D C   1 
ATOM   14110 O O   . ASP D 1 221 ? -18.854 53.001  100.075 1.00 29.13  ? 221 ASP D O   1 
ATOM   14111 C CB  . ASP D 1 221 ? -18.901 51.737  102.703 1.00 34.90  ? 221 ASP D CB  1 
ATOM   14112 C CG  . ASP D 1 221 ? -20.347 52.013  103.068 1.00 49.54  ? 221 ASP D CG  1 
ATOM   14113 O OD1 . ASP D 1 221 ? -21.143 51.053  103.122 1.00 48.06  ? 221 ASP D OD1 1 
ATOM   14114 O OD2 . ASP D 1 221 ? -20.686 53.193  103.301 1.00 49.14  ? 221 ASP D OD2 1 
ATOM   14115 N N   . PHE D 1 222 ? -20.129 51.269  99.388  1.00 29.14  ? 222 PHE D N   1 
ATOM   14116 C CA  . PHE D 1 222 ? -20.680 51.966  98.226  1.00 19.74  ? 222 PHE D CA  1 
ATOM   14117 C C   . PHE D 1 222 ? -21.822 52.868  98.690  1.00 26.62  ? 222 PHE D C   1 
ATOM   14118 O O   . PHE D 1 222 ? -23.005 52.526  98.619  1.00 25.04  ? 222 PHE D O   1 
ATOM   14119 C CB  . PHE D 1 222 ? -21.144 50.970  97.171  1.00 24.65  ? 222 PHE D CB  1 
ATOM   14120 C CG  . PHE D 1 222 ? -20.028 50.394  96.345  1.00 23.24  ? 222 PHE D CG  1 
ATOM   14121 C CD1 . PHE D 1 222 ? -19.074 49.567  96.918  1.00 25.11  ? 222 PHE D CD1 1 
ATOM   14122 C CD2 . PHE D 1 222 ? -19.934 50.680  94.993  1.00 18.81  ? 222 PHE D CD2 1 
ATOM   14123 C CE1 . PHE D 1 222 ? -18.047 49.036  96.158  1.00 19.33  ? 222 PHE D CE1 1 
ATOM   14124 C CE2 . PHE D 1 222 ? -18.910 50.151  94.229  1.00 18.93  ? 222 PHE D CE2 1 
ATOM   14125 C CZ  . PHE D 1 222 ? -17.965 49.329  94.812  1.00 18.53  ? 222 PHE D CZ  1 
ATOM   14126 N N   . ALA D 1 223 ? -21.451 54.056  99.167  1.00 34.34  ? 223 ALA D N   1 
ATOM   14127 C CA  . ALA D 1 223 ? -22.415 55.052  99.611  1.00 30.57  ? 223 ALA D CA  1 
ATOM   14128 C C   . ALA D 1 223 ? -22.883 55.953  98.477  1.00 32.09  ? 223 ALA D C   1 
ATOM   14129 O O   . ALA D 1 223 ? -23.321 57.083  98.731  1.00 31.55  ? 223 ALA D O   1 
ATOM   14130 C CB  . ALA D 1 223 ? -21.825 55.893  100.746 1.00 41.52  ? 223 ALA D CB  1 
ATOM   14131 N N   . VAL D 1 224 ? -22.786 55.482  97.234  1.00 28.33  ? 224 VAL D N   1 
ATOM   14132 C CA  . VAL D 1 224 ? -23.296 56.200  96.072  1.00 21.93  ? 224 VAL D CA  1 
ATOM   14133 C C   . VAL D 1 224 ? -23.795 55.168  95.070  1.00 20.77  ? 224 VAL D C   1 
ATOM   14134 O O   . VAL D 1 224 ? -23.315 54.031  95.032  1.00 26.27  ? 224 VAL D O   1 
ATOM   14135 C CB  . VAL D 1 224 ? -22.224 57.131  95.457  1.00 23.47  ? 224 VAL D CB  1 
ATOM   14136 C CG1 . VAL D 1 224 ? -21.264 56.350  94.580  1.00 26.90  ? 224 VAL D CG1 1 
ATOM   14137 C CG2 . VAL D 1 224 ? -22.881 58.257  94.668  1.00 27.82  ? 224 VAL D CG2 1 
ATOM   14138 N N   . SER D 1 225 ? -24.781 55.560  94.270  1.00 21.54  ? 225 SER D N   1 
ATOM   14139 C CA  . SER D 1 225 ? -25.409 54.653  93.320  1.00 21.83  ? 225 SER D CA  1 
ATOM   14140 C C   . SER D 1 225 ? -24.774 54.801  91.944  1.00 23.99  ? 225 SER D C   1 
ATOM   14141 O O   . SER D 1 225 ? -24.595 55.921  91.451  1.00 24.71  ? 225 SER D O   1 
ATOM   14142 C CB  . SER D 1 225 ? -26.912 54.916  93.235  1.00 32.32  ? 225 SER D CB  1 
ATOM   14143 O OG  . SER D 1 225 ? -27.612 53.758  92.806  1.00 44.98  ? 225 SER D OG  1 
ATOM   14144 N N   . PHE D 1 226 ? -24.433 53.668  91.331  1.00 23.66  ? 226 PHE D N   1 
ATOM   14145 C CA  . PHE D 1 226 ? -23.948 53.625  89.957  1.00 23.03  ? 226 PHE D CA  1 
ATOM   14146 C C   . PHE D 1 226 ? -24.987 53.068  88.992  1.00 24.78  ? 226 PHE D C   1 
ATOM   14147 O O   . PHE D 1 226 ? -24.674 52.866  87.814  1.00 34.68  ? 226 PHE D O   1 
ATOM   14148 C CB  . PHE D 1 226 ? -22.670 52.788  89.862  1.00 23.94  ? 226 PHE D CB  1 
ATOM   14149 C CG  . PHE D 1 226 ? -21.445 53.471  90.397  1.00 22.11  ? 226 PHE D CG  1 
ATOM   14150 C CD1 . PHE D 1 226 ? -21.148 53.434  91.749  1.00 21.22  ? 226 PHE D CD1 1 
ATOM   14151 C CD2 . PHE D 1 226 ? -20.582 54.139  89.544  1.00 22.75  ? 226 PHE D CD2 1 
ATOM   14152 C CE1 . PHE D 1 226 ? -20.016 54.054  92.240  1.00 20.99  ? 226 PHE D CE1 1 
ATOM   14153 C CE2 . PHE D 1 226 ? -19.450 54.764  90.031  1.00 22.50  ? 226 PHE D CE2 1 
ATOM   14154 C CZ  . PHE D 1 226 ? -19.167 54.722  91.381  1.00 21.78  ? 226 PHE D CZ  1 
ATOM   14155 N N   . ARG D 1 227 ? -26.212 52.810  89.462  1.00 23.84  ? 227 ARG D N   1 
ATOM   14156 C CA  . ARG D 1 227 ? -27.214 52.181  88.606  1.00 24.67  ? 227 ARG D CA  1 
ATOM   14157 C C   . ARG D 1 227 ? -27.538 53.042  87.391  1.00 31.20  ? 227 ARG D C   1 
ATOM   14158 O O   . ARG D 1 227 ? -27.853 52.508  86.322  1.00 27.31  ? 227 ARG D O   1 
ATOM   14159 C CB  . ARG D 1 227 ? -28.486 51.883  89.405  1.00 33.78  ? 227 ARG D CB  1 
ATOM   14160 C CG  . ARG D 1 227 ? -28.495 50.510  90.075  1.00 36.04  ? 227 ARG D CG  1 
ATOM   14161 C CD  . ARG D 1 227 ? -29.913 49.978  90.269  1.00 40.95  ? 227 ARG D CD  1 
ATOM   14162 N NE  . ARG D 1 227 ? -29.927 48.697  90.969  1.00 57.60  ? 227 ARG D NE  1 
ATOM   14163 C CZ  . ARG D 1 227 ? -30.558 47.611  90.541  1.00 61.49  ? 227 ARG D CZ  1 
ATOM   14164 N NH1 . ARG D 1 227 ? -31.246 47.610  89.410  1.00 52.16  ? 227 ARG D NH1 1 
ATOM   14165 N NH2 . ARG D 1 227 ? -30.497 46.496  91.266  1.00 50.74  ? 227 ARG D NH2 1 
ATOM   14166 N N   . GLU D 1 228 ? -27.465 54.368  87.531  1.00 38.87  ? 228 GLU D N   1 
ATOM   14167 C CA  . GLU D 1 228 ? -27.675 55.240  86.380  1.00 36.29  ? 228 GLU D CA  1 
ATOM   14168 C C   . GLU D 1 228 ? -26.491 55.190  85.423  1.00 31.10  ? 228 GLU D C   1 
ATOM   14169 O O   . GLU D 1 228 ? -26.675 55.196  84.201  1.00 29.39  ? 228 GLU D O   1 
ATOM   14170 C CB  . GLU D 1 228 ? -27.928 56.674  86.842  1.00 33.22  ? 228 GLU D CB  1 
ATOM   14171 C CG  . GLU D 1 228 ? -29.396 57.044  86.921  1.00 39.93  ? 228 GLU D CG  1 
ATOM   14172 C CD  . GLU D 1 228 ? -30.000 56.733  88.275  1.00 60.42  ? 228 GLU D CD  1 
ATOM   14173 O OE1 . GLU D 1 228 ? -29.292 56.147  89.122  1.00 54.28  ? 228 GLU D OE1 1 
ATOM   14174 O OE2 . GLU D 1 228 ? -31.182 57.075  88.492  1.00 52.76  ? 228 GLU D OE2 1 
ATOM   14175 N N   . ASP D 1 229 ? -25.270 55.144  85.957  1.00 29.23  ? 229 ASP D N   1 
ATOM   14176 C CA  . ASP D 1 229 ? -24.094 55.105  85.096  1.00 27.56  ? 229 ASP D CA  1 
ATOM   14177 C C   . ASP D 1 229 ? -24.003 53.795  84.327  1.00 28.83  ? 229 ASP D C   1 
ATOM   14178 O O   . ASP D 1 229 ? -23.407 53.754  83.244  1.00 34.22  ? 229 ASP D O   1 
ATOM   14179 C CB  . ASP D 1 229 ? -22.829 55.328  85.924  1.00 31.24  ? 229 ASP D CB  1 
ATOM   14180 C CG  . ASP D 1 229 ? -22.503 56.797  86.099  1.00 34.52  ? 229 ASP D CG  1 
ATOM   14181 O OD1 . ASP D 1 229 ? -23.356 57.641  85.756  1.00 43.51  ? 229 ASP D OD1 1 
ATOM   14182 O OD2 . ASP D 1 229 ? -21.389 57.112  86.564  1.00 30.17  ? 229 ASP D OD2 1 
ATOM   14183 N N   . ALA D 1 230 ? -24.578 52.718  84.866  1.00 27.06  ? 230 ALA D N   1 
ATOM   14184 C CA  . ALA D 1 230 ? -24.557 51.439  84.164  1.00 27.36  ? 230 ALA D CA  1 
ATOM   14185 C C   . ALA D 1 230 ? -25.318 51.519  82.847  1.00 28.98  ? 230 ALA D C   1 
ATOM   14186 O O   . ALA D 1 230 ? -24.849 51.018  81.819  1.00 39.44  ? 230 ALA D O   1 
ATOM   14187 C CB  . ALA D 1 230 ? -25.138 50.341  85.054  1.00 26.45  ? 230 ALA D CB  1 
ATOM   14188 N N   . SER D 1 231 ? -26.498 52.147  82.856  1.00 31.53  ? 231 SER D N   1 
ATOM   14189 C CA  . SER D 1 231 ? -27.261 52.290  81.620  1.00 36.92  ? 231 SER D CA  1 
ATOM   14190 C C   . SER D 1 231 ? -26.647 53.337  80.702  1.00 33.91  ? 231 SER D C   1 
ATOM   14191 O O   . SER D 1 231 ? -26.739 53.211  79.475  1.00 44.84  ? 231 SER D O   1 
ATOM   14192 C CB  . SER D 1 231 ? -28.717 52.637  81.930  1.00 31.95  ? 231 SER D CB  1 
ATOM   14193 O OG  . SER D 1 231 ? -28.908 54.039  81.987  1.00 35.01  ? 231 SER D OG  1 
ATOM   14194 N N   . LYS D 1 232 ? -26.017 54.372  81.268  1.00 31.92  ? 232 LYS D N   1 
ATOM   14195 C CA  . LYS D 1 232 ? -25.264 55.313  80.448  1.00 32.98  ? 232 LYS D CA  1 
ATOM   14196 C C   . LYS D 1 232 ? -24.103 54.633  79.739  1.00 35.67  ? 232 LYS D C   1 
ATOM   14197 O O   . LYS D 1 232 ? -23.564 55.191  78.778  1.00 34.38  ? 232 LYS D O   1 
ATOM   14198 C CB  . LYS D 1 232 ? -24.739 56.476  81.297  1.00 32.35  ? 232 LYS D CB  1 
ATOM   14199 C CG  . LYS D 1 232 ? -25.819 57.315  81.964  1.00 33.65  ? 232 LYS D CG  1 
ATOM   14200 C CD  . LYS D 1 232 ? -25.338 58.735  82.249  1.00 34.58  ? 232 LYS D CD  1 
ATOM   14201 C CE  . LYS D 1 232 ? -25.452 59.622  81.016  1.00 51.12  ? 232 LYS D CE  1 
ATOM   14202 N NZ  . LYS D 1 232 ? -24.473 60.746  81.036  1.00 49.58  ? 232 LYS D NZ  1 
ATOM   14203 N N   . HIS D 1 233 ? -23.699 53.449  80.201  1.00 33.29  ? 233 HIS D N   1 
ATOM   14204 C CA  . HIS D 1 233 ? -22.676 52.682  79.503  1.00 32.25  ? 233 HIS D CA  1 
ATOM   14205 C C   . HIS D 1 233 ? -23.267 51.891  78.344  1.00 34.28  ? 233 HIS D C   1 
ATOM   14206 O O   . HIS D 1 233 ? -22.675 51.834  77.261  1.00 39.18  ? 233 HIS D O   1 
ATOM   14207 C CB  . HIS D 1 233 ? -21.970 51.743  80.481  1.00 30.62  ? 233 HIS D CB  1 
ATOM   14208 C CG  . HIS D 1 233 ? -20.825 52.376  81.206  1.00 29.72  ? 233 HIS D CG  1 
ATOM   14209 N ND1 . HIS D 1 233 ? -19.644 52.712  80.582  1.00 30.30  ? 233 HIS D ND1 1 
ATOM   14210 C CD2 . HIS D 1 233 ? -20.681 52.735  82.504  1.00 28.39  ? 233 HIS D CD2 1 
ATOM   14211 C CE1 . HIS D 1 233 ? -18.821 53.250  81.464  1.00 29.36  ? 233 HIS D CE1 1 
ATOM   14212 N NE2 . HIS D 1 233 ? -19.426 53.277  82.638  1.00 30.96  ? 233 HIS D NE2 1 
ATOM   14213 N N   . VAL D 1 234 ? -24.430 51.274  78.554  1.00 33.58  ? 234 VAL D N   1 
ATOM   14214 C CA  . VAL D 1 234 ? -25.056 50.478  77.503  1.00 34.97  ? 234 VAL D CA  1 
ATOM   14215 C C   . VAL D 1 234 ? -25.689 51.375  76.446  1.00 37.87  ? 234 VAL D C   1 
ATOM   14216 O O   . VAL D 1 234 ? -25.512 51.157  75.241  1.00 38.46  ? 234 VAL D O   1 
ATOM   14217 C CB  . VAL D 1 234 ? -26.088 49.509  78.109  1.00 34.38  ? 234 VAL D CB  1 
ATOM   14218 C CG1 . VAL D 1 234 ? -26.747 48.689  77.012  1.00 35.98  ? 234 VAL D CG1 1 
ATOM   14219 C CG2 . VAL D 1 234 ? -25.429 48.607  79.139  1.00 32.67  ? 234 VAL D CG2 1 
ATOM   14220 N N   . GLU D 1 235 ? -26.441 52.391  76.879  1.00 49.33  ? 235 GLU D N   1 
ATOM   14221 C CA  . GLU D 1 235 ? -27.158 53.238  75.929  1.00 49.98  ? 235 GLU D CA  1 
ATOM   14222 C C   . GLU D 1 235 ? -26.201 54.048  75.062  1.00 44.77  ? 235 GLU D C   1 
ATOM   14223 O O   . GLU D 1 235 ? -26.410 54.169  73.850  1.00 51.67  ? 235 GLU D O   1 
ATOM   14224 C CB  . GLU D 1 235 ? -28.126 54.161  76.667  1.00 42.49  ? 235 GLU D CB  1 
ATOM   14225 C CG  . GLU D 1 235 ? -29.509 53.561  76.875  1.00 46.78  ? 235 GLU D CG  1 
ATOM   14226 C CD  . GLU D 1 235 ? -30.445 53.805  75.702  1.00 51.57  ? 235 GLU D CD  1 
ATOM   14227 O OE1 . GLU D 1 235 ? -29.980 53.784  74.542  1.00 58.74  ? 235 GLU D OE1 1 
ATOM   14228 O OE2 . GLU D 1 235 ? -31.651 54.021  75.940  1.00 46.06  ? 235 GLU D OE2 1 
ATOM   14229 N N   . LEU D 1 236 ? -25.149 54.614  75.661  1.00 43.07  ? 236 LEU D N   1 
ATOM   14230 C CA  . LEU D 1 236 ? -24.144 55.318  74.869  1.00 40.67  ? 236 LEU D CA  1 
ATOM   14231 C C   . LEU D 1 236 ? -23.479 54.378  73.873  1.00 50.00  ? 236 LEU D C   1 
ATOM   14232 O O   . LEU D 1 236 ? -23.159 54.778  72.747  1.00 64.91  ? 236 LEU D O   1 
ATOM   14233 C CB  . LEU D 1 236 ? -23.097 55.952  75.783  1.00 48.37  ? 236 LEU D CB  1 
ATOM   14234 C CG  . LEU D 1 236 ? -23.185 57.455  76.053  1.00 55.04  ? 236 LEU D CG  1 
ATOM   14235 C CD1 . LEU D 1 236 ? -24.256 57.763  77.085  1.00 61.04  ? 236 LEU D CD1 1 
ATOM   14236 C CD2 . LEU D 1 236 ? -21.832 57.982  76.512  1.00 60.97  ? 236 LEU D CD2 1 
ATOM   14237 N N   . ALA D 1 237 ? -23.261 53.125  74.275  1.00 39.66  ? 237 ALA D N   1 
ATOM   14238 C CA  . ALA D 1 237 ? -22.678 52.142  73.370  1.00 40.51  ? 237 ALA D CA  1 
ATOM   14239 C C   . ALA D 1 237 ? -23.576 51.898  72.165  1.00 43.19  ? 237 ALA D C   1 
ATOM   14240 O O   . ALA D 1 237 ? -23.088 51.740  71.039  1.00 44.24  ? 237 ALA D O   1 
ATOM   14241 C CB  . ALA D 1 237 ? -22.424 50.836  74.118  1.00 38.93  ? 237 ALA D CB  1 
ATOM   14242 N N   . LYS D 1 238 ? -24.892 51.854  72.384  1.00 47.02  ? 238 LYS D N   1 
ATOM   14243 C CA  . LYS D 1 238 ? -25.817 51.598  71.286  1.00 49.20  ? 238 LYS D CA  1 
ATOM   14244 C C   . LYS D 1 238 ? -25.757 52.704  70.240  1.00 56.56  ? 238 LYS D C   1 
ATOM   14245 O O   . LYS D 1 238 ? -25.892 52.439  69.040  1.00 60.37  ? 238 LYS D O   1 
ATOM   14246 C CB  . LYS D 1 238 ? -27.239 51.443  71.826  1.00 44.66  ? 238 LYS D CB  1 
ATOM   14247 C CG  . LYS D 1 238 ? -27.538 50.064  72.395  1.00 55.51  ? 238 LYS D CG  1 
ATOM   14248 C CD  . LYS D 1 238 ? -28.980 49.950  72.865  1.00 52.34  ? 238 LYS D CD  1 
ATOM   14249 C CE  . LYS D 1 238 ? -29.958 50.180  71.724  1.00 64.25  ? 238 LYS D CE  1 
ATOM   14250 N NZ  . LYS D 1 238 ? -31.319 49.673  72.051  1.00 65.14  ? 238 LYS D NZ  1 
ATOM   14251 N N   . GLU D 1 239 ? -25.564 53.949  70.674  1.00 48.70  ? 239 GLU D N   1 
ATOM   14252 C CA  . GLU D 1 239 ? -25.531 55.058  69.729  1.00 48.69  ? 239 GLU D CA  1 
ATOM   14253 C C   . GLU D 1 239 ? -24.192 55.162  69.009  1.00 49.44  ? 239 GLU D C   1 
ATOM   14254 O O   . GLU D 1 239 ? -24.148 55.610  67.858  1.00 52.07  ? 239 GLU D O   1 
ATOM   14255 C CB  . GLU D 1 239 ? -25.867 56.371  70.446  1.00 48.86  ? 239 GLU D CB  1 
ATOM   14256 C CG  . GLU D 1 239 ? -26.920 56.281  71.579  1.00 62.60  ? 239 GLU D CG  1 
ATOM   14257 C CD  . GLU D 1 239 ? -28.245 55.583  71.225  1.00 63.74  ? 239 GLU D CD  1 
ATOM   14258 O OE1 . GLU D 1 239 ? -28.360 54.939  70.158  1.00 67.64  ? 239 GLU D OE1 1 
ATOM   14259 O OE2 . GLU D 1 239 ? -29.187 55.668  72.036  1.00 57.98  ? 239 GLU D OE2 1 
ATOM   14260 N N   . LYS D 1 240 ? -23.095 54.772  69.660  1.00 47.71  ? 240 LYS D N   1 
ATOM   14261 C CA  . LYS D 1 240 ? -21.832 54.656  68.941  1.00 48.50  ? 240 LYS D CA  1 
ATOM   14262 C C   . LYS D 1 240 ? -21.900 53.530  67.917  1.00 49.89  ? 240 LYS D C   1 
ATOM   14263 O O   . LYS D 1 240 ? -21.341 53.642  66.820  1.00 55.44  ? 240 LYS D O   1 
ATOM   14264 C CB  . LYS D 1 240 ? -20.675 54.437  69.919  1.00 46.37  ? 240 LYS D CB  1 
ATOM   14265 C CG  . LYS D 1 240 ? -19.291 54.505  69.277  1.00 47.17  ? 240 LYS D CG  1 
ATOM   14266 C CD  . LYS D 1 240 ? -19.253 55.503  68.121  1.00 58.50  ? 240 LYS D CD  1 
ATOM   14267 C CE  . LYS D 1 240 ? -17.898 56.157  67.971  1.00 49.98  ? 240 LYS D CE  1 
ATOM   14268 N NZ  . LYS D 1 240 ? -17.678 57.168  69.039  1.00 58.42  ? 240 LYS D NZ  1 
ATOM   14269 N N   . TYR D 1 241 ? -22.585 52.436  68.256  1.00 50.52  ? 241 TYR D N   1 
ATOM   14270 C CA  . TYR D 1 241 ? -22.841 51.394  67.268  1.00 53.35  ? 241 TYR D CA  1 
ATOM   14271 C C   . TYR D 1 241 ? -23.663 51.938  66.106  1.00 58.83  ? 241 TYR D C   1 
ATOM   14272 O O   . TYR D 1 241 ? -23.451 51.554  64.950  1.00 55.37  ? 241 TYR D O   1 
ATOM   14273 C CB  . TYR D 1 241 ? -23.555 50.214  67.927  1.00 49.39  ? 241 TYR D CB  1 
ATOM   14274 C CG  . TYR D 1 241 ? -23.457 48.923  67.153  1.00 50.50  ? 241 TYR D CG  1 
ATOM   14275 C CD1 . TYR D 1 241 ? -22.385 48.059  67.336  1.00 52.75  ? 241 TYR D CD1 1 
ATOM   14276 C CD2 . TYR D 1 241 ? -24.435 48.570  66.232  1.00 60.05  ? 241 TYR D CD2 1 
ATOM   14277 C CE1 . TYR D 1 241 ? -22.295 46.875  66.627  1.00 59.59  ? 241 TYR D CE1 1 
ATOM   14278 C CE2 . TYR D 1 241 ? -24.354 47.391  65.521  1.00 53.71  ? 241 TYR D CE2 1 
ATOM   14279 C CZ  . TYR D 1 241 ? -23.284 46.547  65.722  1.00 55.33  ? 241 TYR D CZ  1 
ATOM   14280 O OH  . TYR D 1 241 ? -23.201 45.375  65.008  1.00 61.29  ? 241 TYR D OH  1 
ATOM   14281 N N   . PHE D 1 242 ? -24.610 52.833  66.401  1.00 61.89  ? 242 PHE D N   1 
ATOM   14282 C CA  . PHE D 1 242 ? -25.397 53.472  65.351  1.00 56.07  ? 242 PHE D CA  1 
ATOM   14283 C C   . PHE D 1 242 ? -24.515 54.290  64.417  1.00 65.42  ? 242 PHE D C   1 
ATOM   14284 O O   . PHE D 1 242 ? -24.665 54.223  63.191  1.00 73.05  ? 242 PHE D O   1 
ATOM   14285 C CB  . PHE D 1 242 ? -26.471 54.360  65.979  1.00 63.55  ? 242 PHE D CB  1 
ATOM   14286 C CG  . PHE D 1 242 ? -27.642 54.635  65.080  1.00 70.74  ? 242 PHE D CG  1 
ATOM   14287 C CD1 . PHE D 1 242 ? -27.636 55.723  64.221  1.00 63.13  ? 242 PHE D CD1 1 
ATOM   14288 C CD2 . PHE D 1 242 ? -28.753 53.813  65.102  1.00 66.51  ? 242 PHE D CD2 1 
ATOM   14289 C CE1 . PHE D 1 242 ? -28.716 55.980  63.398  1.00 62.93  ? 242 PHE D CE1 1 
ATOM   14290 C CE2 . PHE D 1 242 ? -29.836 54.063  64.285  1.00 67.93  ? 242 PHE D CE2 1 
ATOM   14291 C CZ  . PHE D 1 242 ? -29.818 55.148  63.431  1.00 67.82  ? 242 PHE D CZ  1 
ATOM   14292 N N   . GLU D 1 243 ? -23.572 55.051  64.978  1.00 68.10  ? 243 GLU D N   1 
ATOM   14293 C CA  . GLU D 1 243 ? -22.717 55.926  64.184  1.00 67.26  ? 243 GLU D CA  1 
ATOM   14294 C C   . GLU D 1 243 ? -21.817 55.159  63.227  1.00 60.10  ? 243 GLU D C   1 
ATOM   14295 O O   . GLU D 1 243 ? -21.189 55.781  62.362  1.00 61.58  ? 243 GLU D O   1 
ATOM   14296 C CB  . GLU D 1 243 ? -21.862 56.801  65.107  1.00 66.38  ? 243 GLU D CB  1 
ATOM   14297 C CG  . GLU D 1 243 ? -22.632 57.896  65.829  1.00 75.79  ? 243 GLU D CG  1 
ATOM   14298 C CD  . GLU D 1 243 ? -21.737 59.026  66.301  1.00 88.13  ? 243 GLU D CD  1 
ATOM   14299 O OE1 . GLU D 1 243 ? -20.823 58.763  67.110  1.00 81.11  ? 243 GLU D OE1 1 
ATOM   14300 O OE2 . GLU D 1 243 ? -21.944 60.177  65.859  1.00 85.75  ? 243 GLU D OE2 1 
ATOM   14301 N N   . ILE D 1 244 ? -21.726 53.838  63.365  1.00 59.18  ? 244 ILE D N   1 
ATOM   14302 C CA  . ILE D 1 244 ? -20.856 53.023  62.535  1.00 66.06  ? 244 ILE D CA  1 
ATOM   14303 C C   . ILE D 1 244 ? -21.650 52.153  61.568  1.00 61.87  ? 244 ILE D C   1 
ATOM   14304 O O   . ILE D 1 244 ? -21.285 52.033  60.397  1.00 68.67  ? 244 ILE D O   1 
ATOM   14305 C CB  . ILE D 1 244 ? -19.921 52.160  63.411  1.00 67.21  ? 244 ILE D CB  1 
ATOM   14306 C CG1 . ILE D 1 244 ? -19.197 53.026  64.447  1.00 55.54  ? 244 ILE D CG1 1 
ATOM   14307 C CG2 . ILE D 1 244 ? -18.914 51.415  62.547  1.00 63.26  ? 244 ILE D CG2 1 
ATOM   14308 C CD1 . ILE D 1 244 ? -18.540 54.267  63.871  1.00 62.46  ? 244 ILE D CD1 1 
ATOM   14309 N N   . PHE D 1 245 ? -22.741 51.542  62.034  1.00 64.12  ? 245 PHE D N   1 
ATOM   14310 C CA  . PHE D 1 245 ? -23.493 50.581  61.234  1.00 66.75  ? 245 PHE D CA  1 
ATOM   14311 C C   . PHE D 1 245 ? -24.927 51.021  60.963  1.00 64.75  ? 245 PHE D C   1 
ATOM   14312 O O   . PHE D 1 245 ? -25.728 50.210  60.481  1.00 66.15  ? 245 PHE D O   1 
ATOM   14313 C CB  . PHE D 1 245 ? -23.486 49.212  61.919  1.00 60.98  ? 245 PHE D CB  1 
ATOM   14314 C CG  . PHE D 1 245 ? -22.108 48.681  62.198  1.00 66.44  ? 245 PHE D CG  1 
ATOM   14315 C CD1 . PHE D 1 245 ? -21.145 48.656  61.204  1.00 66.40  ? 245 PHE D CD1 1 
ATOM   14316 C CD2 . PHE D 1 245 ? -21.770 48.226  63.459  1.00 61.64  ? 245 PHE D CD2 1 
ATOM   14317 C CE1 . PHE D 1 245 ? -19.876 48.173  61.463  1.00 64.65  ? 245 PHE D CE1 1 
ATOM   14318 C CE2 . PHE D 1 245 ? -20.504 47.742  63.725  1.00 55.97  ? 245 PHE D CE2 1 
ATOM   14319 C CZ  . PHE D 1 245 ? -19.555 47.716  62.726  1.00 57.75  ? 245 PHE D CZ  1 
ATOM   14320 N N   . GLY D 1 246 ? -25.272 52.274  61.257  1.00 64.05  ? 246 GLY D N   1 
ATOM   14321 C CA  . GLY D 1 246 ? -26.592 52.794  60.935  1.00 70.13  ? 246 GLY D CA  1 
ATOM   14322 C C   . GLY D 1 246 ? -27.738 52.023  61.551  1.00 72.69  ? 246 GLY D C   1 
ATOM   14323 O O   . GLY D 1 246 ? -28.838 52.005  60.989  1.00 75.31  ? 246 GLY D O   1 
ATOM   14324 N N   . GLU D 1 247 ? -27.511 51.383  62.695  1.00 67.70  ? 247 GLU D N   1 
ATOM   14325 C CA  . GLU D 1 247 ? -28.523 50.541  63.315  1.00 71.91  ? 247 GLU D CA  1 
ATOM   14326 C C   . GLU D 1 247 ? -28.114 50.272  64.755  1.00 68.94  ? 247 GLU D C   1 
ATOM   14327 O O   . GLU D 1 247 ? -26.943 50.402  65.120  1.00 60.82  ? 247 GLU D O   1 
ATOM   14328 C CB  . GLU D 1 247 ? -28.703 49.229  62.536  1.00 71.62  ? 247 GLU D CB  1 
ATOM   14329 C CG  . GLU D 1 247 ? -29.921 48.409  62.926  1.00 74.19  ? 247 GLU D CG  1 
ATOM   14330 C CD  . GLU D 1 247 ? -29.686 46.918  62.784  1.00 75.63  ? 247 GLU D CD  1 
ATOM   14331 O OE1 . GLU D 1 247 ? -28.963 46.517  61.847  1.00 63.43  ? 247 GLU D OE1 1 
ATOM   14332 O OE2 . GLU D 1 247 ? -30.216 46.149  63.613  1.00 71.30  ? 247 GLU D OE2 1 
ATOM   14333 N N   . HIS D 1 248 ? -29.099 49.903  65.571  1.00 68.94  ? 248 HIS D N   1 
ATOM   14334 C CA  . HIS D 1 248 ? -28.889 49.532  66.964  1.00 62.34  ? 248 HIS D CA  1 
ATOM   14335 C C   . HIS D 1 248 ? -28.526 48.054  67.070  1.00 63.07  ? 248 HIS D C   1 
ATOM   14336 O O   . HIS D 1 248 ? -29.154 47.215  66.423  1.00 59.11  ? 248 HIS D O   1 
ATOM   14337 C CB  . HIS D 1 248 ? -30.139 49.806  67.792  1.00 58.04  ? 248 HIS D CB  1 
ATOM   14338 C CG  . HIS D 1 248 ? -30.318 51.243  68.166  1.00 66.57  ? 248 HIS D CG  1 
ATOM   14339 N ND1 . HIS D 1 248 ? -29.489 52.240  67.702  1.00 66.76  ? 248 HIS D ND1 1 
ATOM   14340 C CD2 . HIS D 1 248 ? -31.228 51.851  68.963  1.00 68.11  ? 248 HIS D CD2 1 
ATOM   14341 C CE1 . HIS D 1 248 ? -29.883 53.402  68.191  1.00 68.05  ? 248 HIS D CE1 1 
ATOM   14342 N NE2 . HIS D 1 248 ? -30.934 53.193  68.962  1.00 77.33  ? 248 HIS D NE2 1 
ATOM   14343 N N   . PRO D 1 249 ? -27.522 47.714  67.874  1.00 63.39  ? 249 PRO D N   1 
ATOM   14344 C CA  . PRO D 1 249 ? -27.135 46.307  68.013  1.00 56.13  ? 249 PRO D CA  1 
ATOM   14345 C C   . PRO D 1 249 ? -28.143 45.531  68.846  1.00 64.09  ? 249 PRO D C   1 
ATOM   14346 O O   . PRO D 1 249 ? -28.902 46.088  69.644  1.00 53.35  ? 249 PRO D O   1 
ATOM   14347 C CB  . PRO D 1 249 ? -25.775 46.380  68.712  1.00 50.85  ? 249 PRO D CB  1 
ATOM   14348 C CG  . PRO D 1 249 ? -25.850 47.634  69.521  1.00 55.00  ? 249 PRO D CG  1 
ATOM   14349 C CD  . PRO D 1 249 ? -26.751 48.593  68.772  1.00 54.82  ? 249 PRO D CD  1 
ATOM   14350 N N   . VAL D 1 250 ? -28.135 44.213  68.650  1.00 62.08  ? 250 VAL D N   1 
ATOM   14351 C CA  . VAL D 1 250 ? -29.047 43.318  69.353  1.00 60.75  ? 250 VAL D CA  1 
ATOM   14352 C C   . VAL D 1 250 ? -28.240 42.224  70.036  1.00 60.68  ? 250 VAL D C   1 
ATOM   14353 O O   . VAL D 1 250 ? -28.778 41.430  70.818  1.00 57.19  ? 250 VAL D O   1 
ATOM   14354 C CB  . VAL D 1 250 ? -30.092 42.723  68.393  1.00 61.18  ? 250 VAL D CB  1 
ATOM   14355 C CG1 . VAL D 1 250 ? -31.257 43.683  68.225  1.00 60.03  ? 250 VAL D CG1 1 
ATOM   14356 C CG2 . VAL D 1 250 ? -29.456 42.414  67.048  1.00 53.27  ? 250 VAL D CG2 1 
ATOM   14357 N N   . TYR D 1 251 ? -26.943 42.175  69.740  1.00 61.83  ? 251 TYR D N   1 
ATOM   14358 C CA  . TYR D 1 251 ? -26.020 41.228  70.349  1.00 53.28  ? 251 TYR D CA  1 
ATOM   14359 C C   . TYR D 1 251 ? -24.901 42.009  71.025  1.00 48.83  ? 251 TYR D C   1 
ATOM   14360 O O   . TYR D 1 251 ? -24.302 42.897  70.409  1.00 51.17  ? 251 TYR D O   1 
ATOM   14361 C CB  . TYR D 1 251 ? -25.457 40.259  69.304  1.00 49.58  ? 251 TYR D CB  1 
ATOM   14362 C CG  . TYR D 1 251 ? -26.487 39.761  68.306  1.00 70.74  ? 251 TYR D CG  1 
ATOM   14363 C CD1 . TYR D 1 251 ? -27.481 38.869  68.691  1.00 66.84  ? 251 TYR D CD1 1 
ATOM   14364 C CD2 . TYR D 1 251 ? -26.460 40.176  66.978  1.00 75.79  ? 251 TYR D CD2 1 
ATOM   14365 C CE1 . TYR D 1 251 ? -28.419 38.407  67.787  1.00 71.45  ? 251 TYR D CE1 1 
ATOM   14366 C CE2 . TYR D 1 251 ? -27.396 39.718  66.065  1.00 74.97  ? 251 TYR D CE2 1 
ATOM   14367 C CZ  . TYR D 1 251 ? -28.373 38.834  66.477  1.00 70.34  ? 251 TYR D CZ  1 
ATOM   14368 O OH  . TYR D 1 251 ? -29.310 38.375  65.579  1.00 77.14  ? 251 TYR D OH  1 
ATOM   14369 N N   . MET D 1 252 ? -24.630 41.686  72.290  1.00 43.93  ? 252 MET D N   1 
ATOM   14370 C CA  . MET D 1 252 ? -23.660 42.409  73.102  1.00 41.37  ? 252 MET D CA  1 
ATOM   14371 C C   . MET D 1 252 ? -22.784 41.417  73.852  1.00 39.20  ? 252 MET D C   1 
ATOM   14372 O O   . MET D 1 252 ? -23.259 40.362  74.279  1.00 40.03  ? 252 MET D O   1 
ATOM   14373 C CB  . MET D 1 252 ? -24.370 43.349  74.094  1.00 45.54  ? 252 MET D CB  1 
ATOM   14374 C CG  . MET D 1 252 ? -23.627 44.641  74.404  1.00 51.95  ? 252 MET D CG  1 
ATOM   14375 S SD  . MET D 1 252 ? -24.700 45.996  74.925  1.00 55.80  ? 252 MET D SD  1 
ATOM   14376 C CE  . MET D 1 252 ? -24.919 46.880  73.381  1.00 43.18  ? 252 MET D CE  1 
ATOM   14377 N N   . TRP D 1 253 ? -21.501 41.751  74.009  1.00 38.43  ? 253 TRP D N   1 
ATOM   14378 C CA  . TRP D 1 253 ? -20.597 40.924  74.799  1.00 39.58  ? 253 TRP D CA  1 
ATOM   14379 C C   . TRP D 1 253 ? -20.368 41.572  76.153  1.00 40.00  ? 253 TRP D C   1 
ATOM   14380 O O   . TRP D 1 253 ? -19.891 42.716  76.208  1.00 39.79  ? 253 TRP D O   1 
ATOM   14381 C CB  . TRP D 1 253 ? -19.267 40.719  74.084  1.00 38.04  ? 253 TRP D CB  1 
ATOM   14382 C CG  . TRP D 1 253 ? -18.223 40.087  74.964  1.00 37.88  ? 253 TRP D CG  1 
ATOM   14383 C CD1 . TRP D 1 253 ? -17.102 40.684  75.466  1.00 38.46  ? 253 TRP D CD1 1 
ATOM   14384 C CD2 . TRP D 1 253 ? -18.212 38.740  75.456  1.00 36.47  ? 253 TRP D CD2 1 
ATOM   14385 N NE1 . TRP D 1 253 ? -16.393 39.792  76.234  1.00 34.95  ? 253 TRP D NE1 1 
ATOM   14386 C CE2 . TRP D 1 253 ? -17.054 38.592  76.244  1.00 35.34  ? 253 TRP D CE2 1 
ATOM   14387 C CE3 . TRP D 1 253 ? -19.069 37.645  75.304  1.00 37.16  ? 253 TRP D CE3 1 
ATOM   14388 C CZ2 . TRP D 1 253 ? -16.731 37.394  76.879  1.00 34.91  ? 253 TRP D CZ2 1 
ATOM   14389 C CZ3 . TRP D 1 253 ? -18.745 36.456  75.935  1.00 37.29  ? 253 TRP D CZ3 1 
ATOM   14390 C CH2 . TRP D 1 253 ? -17.587 36.341  76.712  1.00 35.61  ? 253 TRP D CH2 1 
ATOM   14391 N N   . PRO D 1 254 ? -20.689 40.902  77.255  1.00 33.93  ? 254 PRO D N   1 
ATOM   14392 C CA  . PRO D 1 254 ? -20.472 41.492  78.576  1.00 33.67  ? 254 PRO D CA  1 
ATOM   14393 C C   . PRO D 1 254 ? -18.996 41.498  78.928  1.00 34.49  ? 254 PRO D C   1 
ATOM   14394 O O   . PRO D 1 254 ? -18.309 40.478  78.765  1.00 39.85  ? 254 PRO D O   1 
ATOM   14395 C CB  . PRO D 1 254 ? -21.265 40.567  79.506  1.00 31.35  ? 254 PRO D CB  1 
ATOM   14396 C CG  . PRO D 1 254 ? -21.248 39.256  78.814  1.00 32.52  ? 254 PRO D CG  1 
ATOM   14397 C CD  . PRO D 1 254 ? -21.267 39.550  77.338  1.00 34.28  ? 254 PRO D CD  1 
ATOM   14398 N N   . PRO D 1 255 ? -18.476 42.627  79.405  1.00 30.61  ? 255 PRO D N   1 
ATOM   14399 C CA  . PRO D 1 255 ? -17.044 42.714  79.718  1.00 30.10  ? 255 PRO D CA  1 
ATOM   14400 C C   . PRO D 1 255 ? -16.610 41.632  80.697  1.00 29.24  ? 255 PRO D C   1 
ATOM   14401 O O   . PRO D 1 255 ? -17.228 41.431  81.741  1.00 34.81  ? 255 PRO D O   1 
ATOM   14402 C CB  . PRO D 1 255 ? -16.906 44.114  80.326  1.00 29.62  ? 255 PRO D CB  1 
ATOM   14403 C CG  . PRO D 1 255 ? -18.032 44.889  79.723  1.00 31.99  ? 255 PRO D CG  1 
ATOM   14404 C CD  . PRO D 1 255 ? -19.167 43.912  79.607  1.00 31.72  ? 255 PRO D CD  1 
ATOM   14405 N N   . GLU D 1 256 ? -15.524 40.938  80.348  1.00 32.30  ? 256 GLU D N   1 
ATOM   14406 C CA  . GLU D 1 256 ? -14.985 39.830  81.144  1.00 31.37  ? 256 GLU D CA  1 
ATOM   14407 C C   . GLU D 1 256 ? -16.035 38.756  81.412  1.00 29.13  ? 256 GLU D C   1 
ATOM   14408 O O   . GLU D 1 256 ? -15.958 38.037  82.411  1.00 28.36  ? 256 GLU D O   1 
ATOM   14409 C CB  . GLU D 1 256 ? -14.385 40.327  82.465  1.00 27.62  ? 256 GLU D CB  1 
ATOM   14410 C CG  . GLU D 1 256 ? -13.794 41.727  82.411  1.00 27.39  ? 256 GLU D CG  1 
ATOM   14411 C CD  . GLU D 1 256 ? -12.358 41.737  81.935  1.00 29.61  ? 256 GLU D CD  1 
ATOM   14412 O OE1 . GLU D 1 256 ? -11.887 40.696  81.431  1.00 31.30  ? 256 GLU D OE1 1 
ATOM   14413 O OE2 . GLU D 1 256 ? -11.700 42.791  82.062  1.00 37.45  ? 256 GLU D OE2 1 
ATOM   14414 N N   . ALA D 1 257 ? -17.019 38.639  80.519  1.00 30.16  ? 257 ALA D N   1 
ATOM   14415 C CA  . ALA D 1 257 ? -18.169 37.751  80.689  1.00 30.37  ? 257 ALA D CA  1 
ATOM   14416 C C   . ALA D 1 257 ? -18.937 38.049  81.970  1.00 34.07  ? 257 ALA D C   1 
ATOM   14417 O O   . ALA D 1 257 ? -19.632 37.175  82.498  1.00 31.92  ? 257 ALA D O   1 
ATOM   14418 C CB  . ALA D 1 257 ? -17.751 36.275  80.650  1.00 30.97  ? 257 ALA D CB  1 
ATOM   14419 N N   . SER D 1 258 ? -18.824 39.276  82.481  1.00 31.59  ? 258 SER D N   1 
ATOM   14420 C CA  . SER D 1 258 ? -19.499 39.644  83.719  1.00 31.25  ? 258 SER D CA  1 
ATOM   14421 C C   . SER D 1 258 ? -21.004 39.560  83.532  1.00 30.81  ? 258 SER D C   1 
ATOM   14422 O O   . SER D 1 258 ? -21.571 40.220  82.655  1.00 28.06  ? 258 SER D O   1 
ATOM   14423 C CB  . SER D 1 258 ? -19.097 41.054  84.147  1.00 30.94  ? 258 SER D CB  1 
ATOM   14424 O OG  . SER D 1 258 ? -19.439 42.004  83.149  1.00 39.25  ? 258 SER D OG  1 
ATOM   14425 N N   . VAL D 1 259 ? -21.653 38.744  84.356  1.00 31.22  ? 259 VAL D N   1 
ATOM   14426 C CA  . VAL D 1 259 ? -23.094 38.562  84.270  1.00 32.78  ? 259 VAL D CA  1 
ATOM   14427 C C   . VAL D 1 259 ? -23.662 38.452  85.676  1.00 33.26  ? 259 VAL D C   1 
ATOM   14428 O O   . VAL D 1 259 ? -22.984 38.024  86.615  1.00 29.92  ? 259 VAL D O   1 
ATOM   14429 C CB  . VAL D 1 259 ? -23.472 37.322  83.423  1.00 29.35  ? 259 VAL D CB  1 
ATOM   14430 C CG1 . VAL D 1 259 ? -23.409 36.052  84.258  1.00 28.41  ? 259 VAL D CG1 1 
ATOM   14431 C CG2 . VAL D 1 259 ? -24.844 37.499  82.809  1.00 30.93  ? 259 VAL D CG2 1 
ATOM   14432 N N   . SER D 1 260 ? -24.913 38.876  85.814  1.00 26.99  ? 260 SER D N   1 
ATOM   14433 C CA  . SER D 1 260 ? -25.685 38.710  87.035  1.00 26.03  ? 260 SER D CA  1 
ATOM   14434 C C   . SER D 1 260 ? -27.147 38.782  86.637  1.00 26.49  ? 260 SER D C   1 
ATOM   14435 O O   . SER D 1 260 ? -27.480 39.209  85.528  1.00 35.33  ? 260 SER D O   1 
ATOM   14436 C CB  . SER D 1 260 ? -25.349 39.777  88.082  1.00 28.85  ? 260 SER D CB  1 
ATOM   14437 O OG  . SER D 1 260 ? -25.577 41.082  87.578  1.00 25.31  ? 260 SER D OG  1 
ATOM   14438 N N   . ASN D 1 261 ? -28.021 38.352  87.549  1.00 29.13  ? 261 ASN D N   1 
ATOM   14439 C CA  . ASN D 1 261 ? -29.449 38.447  87.270  1.00 28.14  ? 261 ASN D CA  1 
ATOM   14440 C C   . ASN D 1 261 ? -29.853 39.892  87.013  1.00 32.52  ? 261 ASN D C   1 
ATOM   14441 O O   . ASN D 1 261 ? -30.597 40.177  86.070  1.00 35.44  ? 261 ASN D O   1 
ATOM   14442 C CB  . ASN D 1 261 ? -30.263 37.857  88.420  1.00 26.78  ? 261 ASN D CB  1 
ATOM   14443 C CG  . ASN D 1 261 ? -30.080 36.361  88.552  1.00 27.99  ? 261 ASN D CG  1 
ATOM   14444 O OD1 . ASN D 1 261 ? -29.569 35.704  87.644  1.00 37.34  ? 261 ASN D OD1 1 
ATOM   14445 N ND2 . ASN D 1 261 ? -30.510 35.809  89.680  1.00 33.58  ? 261 ASN D ND2 1 
ATOM   14446 N N   . GLU D 1 262 ? -29.346 40.820  87.826  1.00 32.68  ? 262 GLU D N   1 
ATOM   14447 C CA  . GLU D 1 262 ? -29.665 42.230  87.636  1.00 27.54  ? 262 GLU D CA  1 
ATOM   14448 C C   . GLU D 1 262 ? -29.130 42.749  86.307  1.00 27.68  ? 262 GLU D C   1 
ATOM   14449 O O   . GLU D 1 262 ? -29.807 43.524  85.621  1.00 31.86  ? 262 GLU D O   1 
ATOM   14450 C CB  . GLU D 1 262 ? -29.111 43.047  88.803  1.00 32.38  ? 262 GLU D CB  1 
ATOM   14451 C CG  . GLU D 1 262 ? -29.583 42.569  90.172  1.00 46.95  ? 262 GLU D CG  1 
ATOM   14452 C CD  . GLU D 1 262 ? -28.572 41.673  90.866  1.00 53.55  ? 262 GLU D CD  1 
ATOM   14453 O OE1 . GLU D 1 262 ? -27.379 42.041  90.907  1.00 51.47  ? 262 GLU D OE1 1 
ATOM   14454 O OE2 . GLU D 1 262 ? -28.973 40.603  91.373  1.00 50.89  ? 262 GLU D OE2 1 
ATOM   14455 N N   . ALA D 1 263 ? -27.919 42.337  85.926  1.00 27.94  ? 263 ALA D N   1 
ATOM   14456 C CA  . ALA D 1 263 ? -27.344 42.801  84.666  1.00 27.39  ? 263 ALA D CA  1 
ATOM   14457 C C   . ALA D 1 263 ? -28.107 42.252  83.467  1.00 28.97  ? 263 ALA D C   1 
ATOM   14458 O O   . ALA D 1 263 ? -28.339 42.976  82.493  1.00 32.89  ? 263 ALA D O   1 
ATOM   14459 C CB  . ALA D 1 263 ? -25.868 42.417  84.585  1.00 26.95  ? 263 ALA D CB  1 
ATOM   14460 N N   . LEU D 1 264 ? -28.508 40.979  83.521  1.00 31.93  ? 264 LEU D N   1 
ATOM   14461 C CA  . LEU D 1 264 ? -29.227 40.375  82.403  1.00 30.96  ? 264 LEU D CA  1 
ATOM   14462 C C   . LEU D 1 264 ? -30.501 41.145  82.083  1.00 31.79  ? 264 LEU D C   1 
ATOM   14463 O O   . LEU D 1 264 ? -30.818 41.376  80.910  1.00 33.23  ? 264 LEU D O   1 
ATOM   14464 C CB  . LEU D 1 264 ? -29.554 38.915  82.718  1.00 31.78  ? 264 LEU D CB  1 
ATOM   14465 C CG  . LEU D 1 264 ? -28.408 37.913  82.563  1.00 33.18  ? 264 LEU D CG  1 
ATOM   14466 C CD1 . LEU D 1 264 ? -28.792 36.553  83.124  1.00 31.26  ? 264 LEU D CD1 1 
ATOM   14467 C CD2 . LEU D 1 264 ? -28.000 37.797  81.103  1.00 32.57  ? 264 LEU D CD2 1 
ATOM   14468 N N   . GLU D 1 265 ? -31.242 41.549  83.114  1.00 31.02  ? 265 GLU D N   1 
ATOM   14469 C CA  . GLU D 1 265 ? -32.450 42.337  82.897  1.00 31.82  ? 265 GLU D CA  1 
ATOM   14470 C C   . GLU D 1 265 ? -32.123 43.703  82.306  1.00 32.11  ? 265 GLU D C   1 
ATOM   14471 O O   . GLU D 1 265 ? -32.863 44.205  81.452  1.00 40.37  ? 265 GLU D O   1 
ATOM   14472 C CB  . GLU D 1 265 ? -33.221 42.474  84.208  1.00 34.95  ? 265 GLU D CB  1 
ATOM   14473 C CG  . GLU D 1 265 ? -33.210 41.196  85.028  1.00 37.72  ? 265 GLU D CG  1 
ATOM   14474 C CD  . GLU D 1 265 ? -34.192 41.207  86.179  1.00 39.93  ? 265 GLU D CD  1 
ATOM   14475 O OE1 . GLU D 1 265 ? -33.906 41.866  87.200  1.00 35.29  ? 265 GLU D OE1 1 
ATOM   14476 O OE2 . GLU D 1 265 ? -35.243 40.541  86.067  1.00 59.70  ? 265 GLU D OE2 1 
ATOM   14477 N N   . LEU D 1 266 ? -31.019 44.318  82.741  1.00 30.96  ? 266 LEU D N   1 
ATOM   14478 C CA  . LEU D 1 266 ? -30.629 45.615  82.193  1.00 31.30  ? 266 LEU D CA  1 
ATOM   14479 C C   . LEU D 1 266 ? -30.417 45.534  80.686  1.00 32.89  ? 266 LEU D C   1 
ATOM   14480 O O   . LEU D 1 266 ? -30.887 46.396  79.935  1.00 36.72  ? 266 LEU D O   1 
ATOM   14481 C CB  . LEU D 1 266 ? -29.363 46.126  82.881  1.00 30.68  ? 266 LEU D CB  1 
ATOM   14482 C CG  . LEU D 1 266 ? -28.771 47.391  82.250  1.00 30.36  ? 266 LEU D CG  1 
ATOM   14483 C CD1 . LEU D 1 266 ? -29.515 48.634  82.723  1.00 30.35  ? 266 LEU D CD1 1 
ATOM   14484 C CD2 . LEU D 1 266 ? -27.279 47.507  82.528  1.00 29.39  ? 266 LEU D CD2 1 
ATOM   14485 N N   . TYR D 1 267 ? -29.708 44.499  80.225  1.00 33.08  ? 267 TYR D N   1 
ATOM   14486 C CA  . TYR D 1 267 ? -29.539 44.299  78.789  1.00 34.77  ? 267 TYR D CA  1 
ATOM   14487 C C   . TYR D 1 267 ? -30.887 44.105  78.106  1.00 39.22  ? 267 TYR D C   1 
ATOM   14488 O O   . TYR D 1 267 ? -31.134 44.662  77.029  1.00 37.95  ? 267 TYR D O   1 
ATOM   14489 C CB  . TYR D 1 267 ? -28.629 43.100  78.524  1.00 34.73  ? 267 TYR D CB  1 
ATOM   14490 C CG  . TYR D 1 267 ? -27.167 43.342  78.828  1.00 33.65  ? 267 TYR D CG  1 
ATOM   14491 C CD1 . TYR D 1 267 ? -26.321 43.896  77.878  1.00 39.71  ? 267 TYR D CD1 1 
ATOM   14492 C CD2 . TYR D 1 267 ? -26.631 43.004  80.062  1.00 31.96  ? 267 TYR D CD2 1 
ATOM   14493 C CE1 . TYR D 1 267 ? -24.984 44.114  78.154  1.00 33.56  ? 267 TYR D CE1 1 
ATOM   14494 C CE2 . TYR D 1 267 ? -25.298 43.218  80.347  1.00 31.09  ? 267 TYR D CE2 1 
ATOM   14495 C CZ  . TYR D 1 267 ? -24.479 43.772  79.390  1.00 31.88  ? 267 TYR D CZ  1 
ATOM   14496 O OH  . TYR D 1 267 ? -23.151 43.985  79.673  1.00 31.11  ? 267 TYR D OH  1 
ATOM   14497 N N   . TYR D 1 268 ? -31.771 43.317  78.722  1.00 38.70  ? 268 TYR D N   1 
ATOM   14498 C CA  . TYR D 1 268 ? -33.109 43.127  78.172  1.00 37.74  ? 268 TYR D CA  1 
ATOM   14499 C C   . TYR D 1 268 ? -33.862 44.449  78.095  1.00 43.75  ? 268 TYR D C   1 
ATOM   14500 O O   . TYR D 1 268 ? -34.612 44.691  77.142  1.00 50.85  ? 268 TYR D O   1 
ATOM   14501 C CB  . TYR D 1 268 ? -33.880 42.111  79.016  1.00 39.11  ? 268 TYR D CB  1 
ATOM   14502 C CG  . TYR D 1 268 ? -35.341 41.984  78.648  1.00 43.79  ? 268 TYR D CG  1 
ATOM   14503 C CD1 . TYR D 1 268 ? -35.739 41.214  77.562  1.00 46.73  ? 268 TYR D CD1 1 
ATOM   14504 C CD2 . TYR D 1 268 ? -36.324 42.629  79.389  1.00 41.53  ? 268 TYR D CD2 1 
ATOM   14505 C CE1 . TYR D 1 268 ? -37.074 41.094  77.222  1.00 45.55  ? 268 TYR D CE1 1 
ATOM   14506 C CE2 . TYR D 1 268 ? -37.660 42.515  79.056  1.00 39.99  ? 268 TYR D CE2 1 
ATOM   14507 C CZ  . TYR D 1 268 ? -38.029 41.747  77.973  1.00 41.82  ? 268 TYR D CZ  1 
ATOM   14508 O OH  . TYR D 1 268 ? -39.359 41.631  77.639  1.00 50.97  ? 268 TYR D OH  1 
ATOM   14509 N N   . GLU D 1 269 ? -33.679 45.316  79.094  1.00 37.68  ? 269 GLU D N   1 
ATOM   14510 C CA  . GLU D 1 269 ? -34.297 46.637  79.047  1.00 37.35  ? 269 GLU D CA  1 
ATOM   14511 C C   . GLU D 1 269 ? -33.736 47.470  77.901  1.00 38.54  ? 269 GLU D C   1 
ATOM   14512 O O   . GLU D 1 269 ? -34.473 48.232  77.263  1.00 49.46  ? 269 GLU D O   1 
ATOM   14513 C CB  . GLU D 1 269 ? -34.102 47.359  80.381  1.00 42.46  ? 269 GLU D CB  1 
ATOM   14514 C CG  . GLU D 1 269 ? -34.794 46.693  81.559  1.00 39.78  ? 269 GLU D CG  1 
ATOM   14515 C CD  . GLU D 1 269 ? -34.159 47.051  82.889  1.00 47.81  ? 269 GLU D CD  1 
ATOM   14516 O OE1 . GLU D 1 269 ? -33.527 48.125  82.978  1.00 44.17  ? 269 GLU D OE1 1 
ATOM   14517 O OE2 . GLU D 1 269 ? -34.288 46.256  83.844  1.00 50.31  ? 269 GLU D OE2 1 
ATOM   14518 N N   . LYS D 1 270 ? -32.440 47.339  77.621  1.00 38.05  ? 270 LYS D N   1 
ATOM   14519 C CA  . LYS D 1 270 ? -31.791 48.091  76.558  1.00 40.52  ? 270 LYS D CA  1 
ATOM   14520 C C   . LYS D 1 270 ? -31.847 47.380  75.207  1.00 47.26  ? 270 LYS D C   1 
ATOM   14521 O O   . LYS D 1 270 ? -31.011 47.652  74.338  1.00 44.97  ? 270 LYS D O   1 
ATOM   14522 C CB  . LYS D 1 270 ? -30.338 48.391  76.933  1.00 37.85  ? 270 LYS D CB  1 
ATOM   14523 C CG  . LYS D 1 270 ? -30.177 49.184  78.222  1.00 36.15  ? 270 LYS D CG  1 
ATOM   14524 C CD  . LYS D 1 270 ? -30.987 50.469  78.192  1.00 36.92  ? 270 LYS D CD  1 
ATOM   14525 C CE  . LYS D 1 270 ? -31.255 50.982  79.599  1.00 35.40  ? 270 LYS D CE  1 
ATOM   14526 N NZ  . LYS D 1 270 ? -32.428 51.899  79.652  1.00 52.88  ? 270 LYS D NZ  1 
ATOM   14527 N N   . GLY D 1 271 ? -32.809 46.482  75.014  1.00 47.29  ? 271 GLY D N   1 
ATOM   14528 C CA  . GLY D 1 271 ? -33.027 45.862  73.718  1.00 43.99  ? 271 GLY D CA  1 
ATOM   14529 C C   . GLY D 1 271 ? -31.927 44.948  73.217  1.00 44.74  ? 271 GLY D C   1 
ATOM   14530 O O   . GLY D 1 271 ? -31.553 45.026  72.040  1.00 53.12  ? 271 GLY D O   1 
ATOM   14531 N N   . ILE D 1 272 ? -31.401 44.082  74.078  1.00 46.07  ? 272 ILE D N   1 
ATOM   14532 C CA  . ILE D 1 272 ? -30.447 43.051  73.682  1.00 45.89  ? 272 ILE D CA  1 
ATOM   14533 C C   . ILE D 1 272 ? -31.177 41.717  73.628  1.00 53.44  ? 272 ILE D C   1 
ATOM   14534 O O   . ILE D 1 272 ? -32.003 41.412  74.498  1.00 60.12  ? 272 ILE D O   1 
ATOM   14535 C CB  . ILE D 1 272 ? -29.245 42.993  74.645  1.00 46.26  ? 272 ILE D CB  1 
ATOM   14536 C CG1 . ILE D 1 272 ? -28.505 44.330  74.639  1.00 41.46  ? 272 ILE D CG1 1 
ATOM   14537 C CG2 . ILE D 1 272 ? -28.302 41.856  74.270  1.00 45.03  ? 272 ILE D CG2 1 
ATOM   14538 C CD1 . ILE D 1 272 ? -27.681 44.555  73.395  1.00 41.38  ? 272 ILE D CD1 1 
ATOM   14539 N N   . ASN D 1 273 ? -30.899 40.931  72.590  1.00 45.35  ? 273 ASN D N   1 
ATOM   14540 C CA  . ASN D 1 273 ? -31.536 39.632  72.416  1.00 54.53  ? 273 ASN D CA  1 
ATOM   14541 C C   . ASN D 1 273 ? -30.652 38.470  72.849  1.00 52.82  ? 273 ASN D C   1 
ATOM   14542 O O   . ASN D 1 273 ? -31.158 37.496  73.416  1.00 54.82  ? 273 ASN D O   1 
ATOM   14543 C CB  . ASN D 1 273 ? -31.950 39.439  70.953  1.00 56.02  ? 273 ASN D CB  1 
ATOM   14544 C CG  . ASN D 1 273 ? -33.217 40.193  70.604  1.00 62.28  ? 273 ASN D CG  1 
ATOM   14545 O OD1 . ASN D 1 273 ? -33.168 41.266  70.002  1.00 62.72  ? 273 ASN D OD1 1 
ATOM   14546 N ND2 . ASN D 1 273 ? -34.361 39.638  70.987  1.00 78.08  ? 273 ASN D ND2 1 
ATOM   14547 N N   . MET D 1 274 ? -29.346 38.550  72.597  1.00 46.46  ? 274 MET D N   1 
ATOM   14548 C CA  . MET D 1 274 ? -28.429 37.471  72.933  1.00 47.98  ? 274 MET D CA  1 
ATOM   14549 C C   . MET D 1 274 ? -27.158 38.057  73.530  1.00 47.99  ? 274 MET D C   1 
ATOM   14550 O O   . MET D 1 274 ? -26.756 39.174  73.196  1.00 61.23  ? 274 MET D O   1 
ATOM   14551 C CB  . MET D 1 274 ? -28.095 36.616  71.694  1.00 56.86  ? 274 MET D CB  1 
ATOM   14552 C CG  . MET D 1 274 ? -27.156 35.435  71.958  1.00 58.04  ? 274 MET D CG  1 
ATOM   14553 S SD  . MET D 1 274 ? -25.381 35.750  71.807  1.00 64.85  ? 274 MET D SD  1 
ATOM   14554 C CE  . MET D 1 274 ? -25.326 36.820  70.379  1.00 50.67  ? 274 MET D CE  1 
ATOM   14555 N N   . LEU D 1 275 ? -26.546 37.303  74.441  1.00 43.60  ? 275 LEU D N   1 
ATOM   14556 C CA  . LEU D 1 275 ? -25.171 37.550  74.847  1.00 42.62  ? 275 LEU D CA  1 
ATOM   14557 C C   . LEU D 1 275 ? -24.553 36.224  75.261  1.00 42.72  ? 275 LEU D C   1 
ATOM   14558 O O   . LEU D 1 275 ? -25.245 35.217  75.429  1.00 44.87  ? 275 LEU D O   1 
ATOM   14559 C CB  . LEU D 1 275 ? -25.057 38.580  75.979  1.00 40.73  ? 275 LEU D CB  1 
ATOM   14560 C CG  . LEU D 1 275 ? -25.853 38.445  77.270  1.00 39.46  ? 275 LEU D CG  1 
ATOM   14561 C CD1 . LEU D 1 275 ? -25.001 38.890  78.442  1.00 45.79  ? 275 LEU D CD1 1 
ATOM   14562 C CD2 . LEU D 1 275 ? -27.087 39.301  77.187  1.00 40.45  ? 275 LEU D CD2 1 
ATOM   14563 N N   . ALA D 1 276 ? -23.235 36.236  75.420  1.00 42.31  ? 276 ALA D N   1 
ATOM   14564 C CA  . ALA D 1 276 ? -22.482 35.050  75.786  1.00 48.58  ? 276 ALA D CA  1 
ATOM   14565 C C   . ALA D 1 276 ? -21.735 35.287  77.091  1.00 45.05  ? 276 ALA D C   1 
ATOM   14566 O O   . ALA D 1 276 ? -21.522 36.425  77.512  1.00 43.83  ? 276 ALA D O   1 
ATOM   14567 C CB  . ALA D 1 276 ? -21.499 34.652  74.678  1.00 49.19  ? 276 ALA D CB  1 
ATOM   14568 N N   . THR D 1 277 ? -21.347 34.194  77.738  1.00 42.36  ? 277 THR D N   1 
ATOM   14569 C CA  . THR D 1 277 ? -20.591 34.263  78.982  1.00 39.74  ? 277 THR D CA  1 
ATOM   14570 C C   . THR D 1 277 ? -19.909 32.916  79.205  1.00 45.71  ? 277 THR D C   1 
ATOM   14571 O O   . THR D 1 277 ? -20.085 31.973  78.429  1.00 54.07  ? 277 THR D O   1 
ATOM   14572 C CB  . THR D 1 277 ? -21.490 34.654  80.158  1.00 39.03  ? 277 THR D CB  1 
ATOM   14573 O OG1 . THR D 1 277 ? -20.699 34.781  81.346  1.00 43.80  ? 277 THR D OG1 1 
ATOM   14574 C CG2 . THR D 1 277 ? -22.574 33.617  80.371  1.00 38.94  ? 277 THR D CG2 1 
ATOM   14575 N N   . ASP D 1 278 ? -19.122 32.837  80.273  1.00 39.76  ? 278 ASP D N   1 
ATOM   14576 C CA  . ASP D 1 278 ? -18.267 31.681  80.507  1.00 42.57  ? 278 ASP D CA  1 
ATOM   14577 C C   . ASP D 1 278 ? -19.050 30.524  81.117  1.00 47.24  ? 278 ASP D C   1 
ATOM   14578 O O   . ASP D 1 278 ? -19.985 30.720  81.899  1.00 48.50  ? 278 ASP D O   1 
ATOM   14579 C CB  . ASP D 1 278 ? -17.102 32.059  81.421  1.00 42.53  ? 278 ASP D CB  1 
ATOM   14580 C CG  . ASP D 1 278 ? -15.955 31.075  81.339  1.00 40.98  ? 278 ASP D CG  1 
ATOM   14581 O OD1 . ASP D 1 278 ? -15.907 30.301  80.359  1.00 42.38  ? 278 ASP D OD1 1 
ATOM   14582 O OD2 . ASP D 1 278 ? -15.097 31.080  82.247  1.00 40.60  ? 278 ASP D OD2 1 
ATOM   14583 N N   . GLU D 1 279 ? -18.641 29.303  80.759  1.00 46.39  ? 279 GLU D N   1 
ATOM   14584 C CA  . GLU D 1 279 ? -19.294 28.101  81.264  1.00 43.30  ? 279 GLU D CA  1 
ATOM   14585 C C   . GLU D 1 279 ? -18.993 27.832  82.733  1.00 47.18  ? 279 GLU D C   1 
ATOM   14586 O O   . GLU D 1 279 ? -19.667 26.992  83.340  1.00 43.02  ? 279 GLU D O   1 
ATOM   14587 C CB  . GLU D 1 279 ? -18.890 26.888  80.423  1.00 45.30  ? 279 GLU D CB  1 
ATOM   14588 C CG  . GLU D 1 279 ? -17.390 26.685  80.297  1.00 45.78  ? 279 GLU D CG  1 
ATOM   14589 C CD  . GLU D 1 279 ? -17.005 25.219  80.251  1.00 55.42  ? 279 GLU D CD  1 
ATOM   14590 O OE1 . GLU D 1 279 ? -17.913 24.362  80.283  1.00 66.53  ? 279 GLU D OE1 1 
ATOM   14591 O OE2 . GLU D 1 279 ? -15.794 24.923  80.178  1.00 64.72  ? 279 GLU D OE2 1 
ATOM   14592 N N   . VAL D 1 280 ? -17.999 28.508  83.315  1.00 43.74  ? 280 VAL D N   1 
ATOM   14593 C CA  . VAL D 1 280 ? -17.808 28.411  84.758  1.00 41.56  ? 280 VAL D CA  1 
ATOM   14594 C C   . VAL D 1 280 ? -18.987 29.044  85.486  1.00 42.20  ? 280 VAL D C   1 
ATOM   14595 O O   . VAL D 1 280 ? -19.337 28.631  86.598  1.00 46.01  ? 280 VAL D O   1 
ATOM   14596 C CB  . VAL D 1 280 ? -16.462 29.040  85.175  1.00 40.34  ? 280 VAL D CB  1 
ATOM   14597 C CG1 . VAL D 1 280 ? -16.516 30.560  85.092  1.00 38.90  ? 280 VAL D CG1 1 
ATOM   14598 C CG2 . VAL D 1 280 ? -16.075 28.590  86.579  1.00 45.50  ? 280 VAL D CG2 1 
ATOM   14599 N N   . ILE D 1 281 ? -19.620 30.048  84.876  1.00 38.81  ? 281 ILE D N   1 
ATOM   14600 C CA  . ILE D 1 281 ? -20.857 30.596  85.419  1.00 37.79  ? 281 ILE D CA  1 
ATOM   14601 C C   . ILE D 1 281 ? -21.995 29.595  85.253  1.00 38.80  ? 281 ILE D C   1 
ATOM   14602 O O   . ILE D 1 281 ? -22.832 29.429  86.149  1.00 41.23  ? 281 ILE D O   1 
ATOM   14603 C CB  . ILE D 1 281 ? -21.167 31.947  84.750  1.00 36.95  ? 281 ILE D CB  1 
ATOM   14604 C CG1 . ILE D 1 281 ? -20.115 32.977  85.168  1.00 35.94  ? 281 ILE D CG1 1 
ATOM   14605 C CG2 . ILE D 1 281 ? -22.569 32.421  85.107  1.00 36.20  ? 281 ILE D CG2 1 
ATOM   14606 C CD1 . ILE D 1 281 ? -20.325 34.350  84.591  1.00 35.22  ? 281 ILE D CD1 1 
ATOM   14607 N N   . LEU D 1 282 ? -22.037 28.908  84.108  1.00 41.76  ? 282 LEU D N   1 
ATOM   14608 C CA  . LEU D 1 282 ? -22.997 27.825  83.919  1.00 41.59  ? 282 LEU D CA  1 
ATOM   14609 C C   . LEU D 1 282 ? -22.803 26.734  84.963  1.00 42.15  ? 282 LEU D C   1 
ATOM   14610 O O   . LEU D 1 282 ? -23.777 26.165  85.470  1.00 42.57  ? 282 LEU D O   1 
ATOM   14611 C CB  . LEU D 1 282 ? -22.853 27.249  82.511  1.00 43.53  ? 282 LEU D CB  1 
ATOM   14612 C CG  . LEU D 1 282 ? -23.813 26.169  82.019  1.00 45.02  ? 282 LEU D CG  1 
ATOM   14613 C CD1 . LEU D 1 282 ? -25.249 26.656  82.054  1.00 44.63  ? 282 LEU D CD1 1 
ATOM   14614 C CD2 . LEU D 1 282 ? -23.421 25.767  80.613  1.00 50.97  ? 282 LEU D CD2 1 
ATOM   14615 N N   . LYS D 1 283 ? -21.546 26.432  85.298  1.00 46.16  ? 283 LYS D N   1 
ATOM   14616 C CA  . LYS D 1 283 ? -21.261 25.411  86.299  1.00 50.79  ? 283 LYS D CA  1 
ATOM   14617 C C   . LYS D 1 283 ? -21.791 25.813  87.671  1.00 45.83  ? 283 LYS D C   1 
ATOM   14618 O O   . LYS D 1 283 ? -22.277 24.966  88.430  1.00 42.48  ? 283 LYS D O   1 
ATOM   14619 C CB  . LYS D 1 283 ? -19.756 25.152  86.357  1.00 51.58  ? 283 LYS D CB  1 
ATOM   14620 C CG  . LYS D 1 283 ? -19.375 23.781  86.885  1.00 55.88  ? 283 LYS D CG  1 
ATOM   14621 C CD  . LYS D 1 283 ? -18.080 23.840  87.678  1.00 65.75  ? 283 LYS D CD  1 
ATOM   14622 C CE  . LYS D 1 283 ? -17.034 24.691  86.972  1.00 63.18  ? 283 LYS D CE  1 
ATOM   14623 N NZ  . LYS D 1 283 ? -16.071 25.299  87.931  1.00 57.93  ? 283 LYS D NZ  1 
ATOM   14624 N N   . ASN D 1 284 ? -21.706 27.099  88.008  1.00 48.46  ? 284 ASN D N   1 
ATOM   14625 C CA  . ASN D 1 284 ? -22.142 27.582  89.313  1.00 42.55  ? 284 ASN D CA  1 
ATOM   14626 C C   . ASN D 1 284 ? -23.639 27.847  89.392  1.00 38.40  ? 284 ASN D C   1 
ATOM   14627 O O   . ASN D 1 284 ? -24.124 28.222  90.465  1.00 44.50  ? 284 ASN D O   1 
ATOM   14628 C CB  . ASN D 1 284 ? -21.388 28.863  89.689  1.00 39.83  ? 284 ASN D CB  1 
ATOM   14629 C CG  . ASN D 1 284 ? -19.883 28.685  89.669  1.00 46.04  ? 284 ASN D CG  1 
ATOM   14630 O OD1 . ASN D 1 284 ? -19.379 27.564  89.602  1.00 53.53  ? 284 ASN D OD1 1 
ATOM   14631 N ND2 . ASN D 1 284 ? -19.156 29.795  89.741  1.00 36.75  ? 284 ASN D ND2 1 
ATOM   14632 N N   . SER D 1 285 ? -24.382 27.671  88.304  1.00 40.50  ? 285 SER D N   1 
ATOM   14633 C CA  . SER D 1 285 ? -25.799 28.022  88.288  1.00 38.82  ? 285 SER D CA  1 
ATOM   14634 C C   . SER D 1 285 ? -26.719 26.861  87.947  1.00 43.97  ? 285 SER D C   1 
ATOM   14635 O O   . SER D 1 285 ? -27.799 26.751  88.533  1.00 45.43  ? 285 SER D O   1 
ATOM   14636 C CB  . SER D 1 285 ? -26.040 29.172  87.300  1.00 38.11  ? 285 SER D CB  1 
ATOM   14637 O OG  . SER D 1 285 ? -25.031 30.161  87.421  1.00 37.84  ? 285 SER D OG  1 
ATOM   14638 N N   . VAL D 1 286 ? -26.334 25.995  87.012  1.00 49.12  ? 286 VAL D N   1 
ATOM   14639 C CA  . VAL D 1 286 ? -27.136 24.842  86.621  1.00 59.69  ? 286 VAL D CA  1 
ATOM   14640 C C   . VAL D 1 286 ? -26.321 23.579  86.869  1.00 60.61  ? 286 VAL D C   1 
ATOM   14641 O O   . VAL D 1 286 ? -25.098 23.574  86.693  1.00 45.73  ? 286 VAL D O   1 
ATOM   14642 C CB  . VAL D 1 286 ? -27.593 24.929  85.149  1.00 54.65  ? 286 VAL D CB  1 
ATOM   14643 C CG1 . VAL D 1 286 ? -28.864 24.122  84.943  1.00 59.06  ? 286 VAL D CG1 1 
ATOM   14644 C CG2 . VAL D 1 286 ? -27.820 26.380  84.747  1.00 50.58  ? 286 VAL D CG2 1 
ATOM   14645 N N   . GLU D 1 287 ? -27.008 22.507  87.275  1.00 61.33  ? 287 GLU D N   1 
ATOM   14646 C CA  . GLU D 1 287 ? -26.359 21.325  87.837  1.00 60.04  ? 287 GLU D CA  1 
ATOM   14647 C C   . GLU D 1 287 ? -25.408 20.627  86.872  1.00 76.67  ? 287 GLU D C   1 
ATOM   14648 O O   . GLU D 1 287 ? -24.190 20.637  87.078  1.00 88.43  ? 287 GLU D O   1 
ATOM   14649 C CB  . GLU D 1 287 ? -27.420 20.326  88.300  1.00 62.68  ? 287 GLU D CB  1 
ATOM   14650 C CG  . GLU D 1 287 ? -28.341 20.846  89.388  1.00 77.86  ? 287 GLU D CG  1 
ATOM   14651 C CD  . GLU D 1 287 ? -29.024 19.726  90.147  1.00 84.32  ? 287 GLU D CD  1 
ATOM   14652 O OE1 . GLU D 1 287 ? -29.485 18.763  89.499  1.00 81.12  ? 287 GLU D OE1 1 
ATOM   14653 O OE2 . GLU D 1 287 ? -29.097 19.807  91.392  1.00 83.06  ? 287 GLU D OE2 1 
ATOM   14654 N N   . ARG D 1 288 ? -25.951 20.017  85.815  1.00 73.30  ? 288 ARG D N   1 
ATOM   14655 C CA  . ARG D 1 288 ? -25.159 19.319  84.798  1.00 68.68  ? 288 ARG D CA  1 
ATOM   14656 C C   . ARG D 1 288 ? -25.649 19.824  83.448  1.00 61.74  ? 288 ARG D C   1 
ATOM   14657 O O   . ARG D 1 288 ? -26.492 19.200  82.800  1.00 75.88  ? 288 ARG D O   1 
ATOM   14658 C CB  . ARG D 1 288 ? -25.288 17.798  84.917  1.00 66.60  ? 288 ARG D CB  1 
ATOM   14659 C CG  . ARG D 1 288 ? -25.122 17.246  86.322  1.00 55.71  ? 288 ARG D CG  1 
ATOM   14660 C CD  . ARG D 1 288 ? -26.085 16.090  86.573  1.00 65.19  ? 288 ARG D CD  1 
ATOM   14661 N NE  . ARG D 1 288 ? -27.481 16.515  86.553  1.00 81.19  ? 288 ARG D NE  1 
ATOM   14662 C CZ  . ARG D 1 288 ? -28.302 16.363  85.522  1.00 68.89  ? 288 ARG D CZ  1 
ATOM   14663 N NH1 . ARG D 1 288 ? -27.899 15.796  84.396  1.00 64.18  ? 288 ARG D NH1 1 
ATOM   14664 N NH2 . ARG D 1 288 ? -29.556 16.794  85.621  1.00 58.28  ? 288 ARG D NH2 1 
ATOM   14665 N N   . ALA D 1 289 ? -25.103 20.954  83.018  1.00 51.67  ? 289 ALA D N   1 
ATOM   14666 C CA  . ALA D 1 289 ? -25.539 21.623  81.804  1.00 54.71  ? 289 ALA D CA  1 
ATOM   14667 C C   . ALA D 1 289 ? -24.378 21.695  80.827  1.00 52.95  ? 289 ALA D C   1 
ATOM   14668 O O   . ALA D 1 289 ? -23.290 22.162  81.183  1.00 50.92  ? 289 ALA D O   1 
ATOM   14669 C CB  . ALA D 1 289 ? -26.067 23.026  82.112  1.00 66.17  ? 289 ALA D CB  1 
ATOM   14670 N N   . SER D 1 290 ? -24.611 21.231  79.605  1.00 53.87  ? 290 SER D N   1 
ATOM   14671 C CA  . SER D 1 290 ? -23.615 21.393  78.564  1.00 58.92  ? 290 SER D CA  1 
ATOM   14672 C C   . SER D 1 290 ? -23.432 22.878  78.262  1.00 57.05  ? 290 SER D C   1 
ATOM   14673 O O   . SER D 1 290 ? -24.340 23.682  78.484  1.00 62.55  ? 290 SER D O   1 
ATOM   14674 C CB  . SER D 1 290 ? -24.030 20.650  77.297  1.00 61.21  ? 290 SER D CB  1 
ATOM   14675 O OG  . SER D 1 290 ? -23.459 19.357  77.246  1.00 60.37  ? 290 SER D OG  1 
ATOM   14676 N N   . PRO D 1 291 ? -22.248 23.280  77.803  1.00 52.11  ? 291 PRO D N   1 
ATOM   14677 C CA  . PRO D 1 291 ? -22.095 24.660  77.327  1.00 50.75  ? 291 PRO D CA  1 
ATOM   14678 C C   . PRO D 1 291 ? -22.727 24.888  75.968  1.00 60.63  ? 291 PRO D C   1 
ATOM   14679 O O   . PRO D 1 291 ? -22.999 26.042  75.614  1.00 60.90  ? 291 PRO D O   1 
ATOM   14680 C CB  . PRO D 1 291 ? -20.569 24.853  77.277  1.00 50.39  ? 291 PRO D CB  1 
ATOM   14681 C CG  . PRO D 1 291 ? -19.977 23.633  77.951  1.00 62.30  ? 291 PRO D CG  1 
ATOM   14682 C CD  . PRO D 1 291 ? -20.977 22.544  77.774  1.00 61.04  ? 291 PRO D CD  1 
ATOM   14683 N N   . TYR D 1 292 ? -22.978 23.827  75.209  1.00 56.43  ? 292 TYR D N   1 
ATOM   14684 C CA  . TYR D 1 292 ? -23.425 23.934  73.821  1.00 55.63  ? 292 TYR D CA  1 
ATOM   14685 C C   . TYR D 1 292 ? -24.943 23.786  73.710  1.00 56.43  ? 292 TYR D C   1 
ATOM   14686 O O   . TYR D 1 292 ? -25.457 22.878  73.056  1.00 58.60  ? 292 TYR D O   1 
ATOM   14687 C CB  . TYR D 1 292 ? -22.710 22.892  72.964  1.00 62.01  ? 292 TYR D CB  1 
ATOM   14688 C CG  . TYR D 1 292 ? -21.343 22.506  73.484  1.00 61.54  ? 292 TYR D CG  1 
ATOM   14689 C CD1 . TYR D 1 292 ? -20.245 23.329  73.283  1.00 63.56  ? 292 TYR D CD1 1 
ATOM   14690 C CD2 . TYR D 1 292 ? -21.152 21.312  74.171  1.00 58.26  ? 292 TYR D CD2 1 
ATOM   14691 C CE1 . TYR D 1 292 ? -18.993 22.978  73.751  1.00 65.69  ? 292 TYR D CE1 1 
ATOM   14692 C CE2 . TYR D 1 292 ? -19.905 20.952  74.644  1.00 58.08  ? 292 TYR D CE2 1 
ATOM   14693 C CZ  . TYR D 1 292 ? -18.830 21.788  74.431  1.00 64.58  ? 292 TYR D CZ  1 
ATOM   14694 O OH  . TYR D 1 292 ? -17.586 21.431  74.901  1.00 71.06  ? 292 TYR D OH  1 
ATOM   14695 N N   . LEU D 1 293 ? -25.671 24.691  74.360  1.00 54.77  ? 293 LEU D N   1 
ATOM   14696 C CA  . LEU D 1 293 ? -27.101 24.834  74.125  1.00 55.43  ? 293 LEU D CA  1 
ATOM   14697 C C   . LEU D 1 293 ? -27.453 26.313  74.064  1.00 58.49  ? 293 LEU D C   1 
ATOM   14698 O O   . LEU D 1 293 ? -26.607 27.192  74.261  1.00 59.62  ? 293 LEU D O   1 
ATOM   14699 C CB  . LEU D 1 293 ? -27.964 24.139  75.188  1.00 55.47  ? 293 LEU D CB  1 
ATOM   14700 C CG  . LEU D 1 293 ? -27.647 22.745  75.725  1.00 66.97  ? 293 LEU D CG  1 
ATOM   14701 C CD1 . LEU D 1 293 ? -26.707 22.848  76.883  1.00 55.66  ? 293 LEU D CD1 1 
ATOM   14702 C CD2 . LEU D 1 293 ? -28.927 22.043  76.154  1.00 74.32  ? 293 LEU D CD2 1 
ATOM   14703 N N   . ARG D 1 294 ? -28.726 26.576  73.785  1.00 60.43  ? 294 ARG D N   1 
ATOM   14704 C CA  . ARG D 1 294 ? -29.282 27.921  73.739  1.00 53.87  ? 294 ARG D CA  1 
ATOM   14705 C C   . ARG D 1 294 ? -30.188 28.091  74.951  1.00 52.05  ? 294 ARG D C   1 
ATOM   14706 O O   . ARG D 1 294 ? -31.274 27.505  75.007  1.00 53.63  ? 294 ARG D O   1 
ATOM   14707 C CB  . ARG D 1 294 ? -30.051 28.143  72.439  1.00 55.17  ? 294 ARG D CB  1 
ATOM   14708 C CG  . ARG D 1 294 ? -30.744 29.489  72.348  1.00 54.28  ? 294 ARG D CG  1 
ATOM   14709 C CD  . ARG D 1 294 ? -31.018 29.864  70.903  1.00 56.55  ? 294 ARG D CD  1 
ATOM   14710 N NE  . ARG D 1 294 ? -32.196 29.184  70.379  1.00 68.28  ? 294 ARG D NE  1 
ATOM   14711 C CZ  . ARG D 1 294 ? -32.365 28.850  69.107  1.00 72.07  ? 294 ARG D CZ  1 
ATOM   14712 N NH1 . ARG D 1 294 ? -31.437 29.099  68.198  1.00 65.86  ? 294 ARG D NH1 1 
ATOM   14713 N NH2 . ARG D 1 294 ? -33.494 28.252  68.738  1.00 71.91  ? 294 ARG D NH2 1 
ATOM   14714 N N   . TYR D 1 295 ? -29.745 28.885  75.917  1.00 49.78  ? 295 TYR D N   1 
ATOM   14715 C CA  . TYR D 1 295 ? -30.520 29.133  77.121  1.00 48.49  ? 295 TYR D CA  1 
ATOM   14716 C C   . TYR D 1 295 ? -31.341 30.405  76.969  1.00 48.37  ? 295 TYR D C   1 
ATOM   14717 O O   . TYR D 1 295 ? -30.933 31.354  76.297  1.00 51.62  ? 295 TYR D O   1 
ATOM   14718 C CB  . TYR D 1 295 ? -29.618 29.256  78.350  1.00 46.57  ? 295 TYR D CB  1 
ATOM   14719 C CG  . TYR D 1 295 ? -28.789 28.031  78.639  1.00 47.25  ? 295 TYR D CG  1 
ATOM   14720 C CD1 . TYR D 1 295 ? -27.571 27.831  78.007  1.00 47.68  ? 295 TYR D CD1 1 
ATOM   14721 C CD2 . TYR D 1 295 ? -29.221 27.077  79.549  1.00 47.60  ? 295 TYR D CD2 1 
ATOM   14722 C CE1 . TYR D 1 295 ? -26.808 26.716  78.269  1.00 48.43  ? 295 TYR D CE1 1 
ATOM   14723 C CE2 . TYR D 1 295 ? -28.465 25.958  79.817  1.00 48.41  ? 295 TYR D CE2 1 
ATOM   14724 C CZ  . TYR D 1 295 ? -27.258 25.783  79.174  1.00 48.81  ? 295 TYR D CZ  1 
ATOM   14725 O OH  . TYR D 1 295 ? -26.498 24.671  79.438  1.00 55.21  ? 295 TYR D OH  1 
ATOM   14726 N N   . TYR D 1 296 ? -32.509 30.412  77.603  1.00 47.66  ? 296 TYR D N   1 
ATOM   14727 C CA  . TYR D 1 296 ? -33.355 31.594  77.683  1.00 52.14  ? 296 TYR D CA  1 
ATOM   14728 C C   . TYR D 1 296 ? -33.463 31.997  79.145  1.00 50.88  ? 296 TYR D C   1 
ATOM   14729 O O   . TYR D 1 296 ? -33.948 31.217  79.972  1.00 44.99  ? 296 TYR D O   1 
ATOM   14730 C CB  . TYR D 1 296 ? -34.742 31.328  77.092  1.00 51.58  ? 296 TYR D CB  1 
ATOM   14731 C CG  . TYR D 1 296 ? -34.727 30.910  75.640  1.00 61.62  ? 296 TYR D CG  1 
ATOM   14732 C CD1 . TYR D 1 296 ? -33.714 31.324  74.785  1.00 63.87  ? 296 TYR D CD1 1 
ATOM   14733 C CD2 . TYR D 1 296 ? -35.728 30.097  75.122  1.00 67.69  ? 296 TYR D CD2 1 
ATOM   14734 C CE1 . TYR D 1 296 ? -33.698 30.941  73.457  1.00 56.65  ? 296 TYR D CE1 1 
ATOM   14735 C CE2 . TYR D 1 296 ? -35.720 29.709  73.794  1.00 63.10  ? 296 TYR D CE2 1 
ATOM   14736 C CZ  . TYR D 1 296 ? -34.702 30.134  72.966  1.00 55.76  ? 296 TYR D CZ  1 
ATOM   14737 O OH  . TYR D 1 296 ? -34.687 29.753  71.643  1.00 57.73  ? 296 TYR D OH  1 
ATOM   14738 N N   . PHE D 1 297 ? -33.003 33.202  79.463  1.00 46.44  ? 297 PHE D N   1 
ATOM   14739 C CA  . PHE D 1 297 ? -33.106 33.726  80.821  1.00 41.30  ? 297 PHE D CA  1 
ATOM   14740 C C   . PHE D 1 297 ? -34.537 34.197  81.030  1.00 46.06  ? 297 PHE D C   1 
ATOM   14741 O O   . PHE D 1 297 ? -34.924 35.272  80.567  1.00 50.99  ? 297 PHE D O   1 
ATOM   14742 C CB  . PHE D 1 297 ? -32.106 34.854  81.041  1.00 39.66  ? 297 PHE D CB  1 
ATOM   14743 C CG  . PHE D 1 297 ? -32.088 35.385  82.445  1.00 41.97  ? 297 PHE D CG  1 
ATOM   14744 C CD1 . PHE D 1 297 ? -31.689 34.581  83.499  1.00 37.29  ? 297 PHE D CD1 1 
ATOM   14745 C CD2 . PHE D 1 297 ? -32.468 36.689  82.711  1.00 38.36  ? 297 PHE D CD2 1 
ATOM   14746 C CE1 . PHE D 1 297 ? -31.669 35.069  84.789  1.00 35.74  ? 297 PHE D CE1 1 
ATOM   14747 C CE2 . PHE D 1 297 ? -32.451 37.181  83.999  1.00 35.21  ? 297 PHE D CE2 1 
ATOM   14748 C CZ  . PHE D 1 297 ? -32.047 36.369  85.038  1.00 34.68  ? 297 PHE D CZ  1 
ATOM   14749 N N   . ARG D 1 298 ? -35.332 33.373  81.717  1.00 50.17  ? 298 ARG D N   1 
ATOM   14750 C CA  . ARG D 1 298 ? -36.726 33.686  82.038  1.00 50.35  ? 298 ARG D CA  1 
ATOM   14751 C C   . ARG D 1 298 ? -37.557 33.934  80.782  1.00 50.28  ? 298 ARG D C   1 
ATOM   14752 O O   . ARG D 1 298 ? -38.526 34.697  80.810  1.00 60.93  ? 298 ARG D O   1 
ATOM   14753 C CB  . ARG D 1 298 ? -36.821 34.885  82.988  1.00 48.25  ? 298 ARG D CB  1 
ATOM   14754 C CG  . ARG D 1 298 ? -35.806 34.861  84.122  1.00 38.44  ? 298 ARG D CG  1 
ATOM   14755 C CD  . ARG D 1 298 ? -36.046 35.991  85.108  1.00 36.73  ? 298 ARG D CD  1 
ATOM   14756 N NE  . ARG D 1 298 ? -35.227 35.845  86.305  1.00 35.33  ? 298 ARG D NE  1 
ATOM   14757 C CZ  . ARG D 1 298 ? -34.579 36.840  86.896  1.00 33.78  ? 298 ARG D CZ  1 
ATOM   14758 N NH1 . ARG D 1 298 ? -34.636 38.076  86.429  1.00 33.35  ? 298 ARG D NH1 1 
ATOM   14759 N NH2 . ARG D 1 298 ? -33.845 36.585  87.975  1.00 32.79  ? 298 ARG D NH2 1 
ATOM   14760 N N   . GLU D 1 299 ? -37.186 33.286  79.675  1.00 51.47  ? 299 GLU D N   1 
ATOM   14761 C CA  . GLU D 1 299 ? -37.835 33.490  78.377  1.00 63.08  ? 299 GLU D CA  1 
ATOM   14762 C C   . GLU D 1 299 ? -37.799 34.961  77.966  1.00 51.65  ? 299 GLU D C   1 
ATOM   14763 O O   . GLU D 1 299 ? -38.744 35.482  77.370  1.00 51.29  ? 299 GLU D O   1 
ATOM   14764 C CB  . GLU D 1 299 ? -39.273 32.963  78.380  1.00 73.45  ? 299 GLU D CB  1 
ATOM   14765 C CG  . GLU D 1 299 ? -39.415 31.515  78.819  1.00 81.62  ? 299 GLU D CG  1 
ATOM   14766 C CD  . GLU D 1 299 ? -40.866 31.080  78.942  1.00 90.40  ? 299 GLU D CD  1 
ATOM   14767 O OE1 . GLU D 1 299 ? -41.733 31.947  79.181  1.00 92.51  ? 299 GLU D OE1 1 
ATOM   14768 O OE2 . GLU D 1 299 ? -41.141 29.870  78.797  1.00 74.29  ? 299 GLU D OE2 1 
ATOM   14769 N N   . LEU D 1 300 ? -36.697 35.635  78.283  1.00 44.90  ? 300 LEU D N   1 
ATOM   14770 C CA  . LEU D 1 300 ? -36.535 37.055  77.987  1.00 44.16  ? 300 LEU D CA  1 
ATOM   14771 C C   . LEU D 1 300 ? -35.298 37.365  77.158  1.00 47.06  ? 300 LEU D C   1 
ATOM   14772 O O   . LEU D 1 300 ? -35.341 38.263  76.315  1.00 53.47  ? 300 LEU D O   1 
ATOM   14773 C CB  . LEU D 1 300 ? -36.487 37.866  79.293  1.00 47.98  ? 300 LEU D CB  1 
ATOM   14774 C CG  . LEU D 1 300 ? -37.698 37.773  80.225  1.00 44.20  ? 300 LEU D CG  1 
ATOM   14775 C CD1 . LEU D 1 300 ? -37.378 38.368  81.588  1.00 39.52  ? 300 LEU D CD1 1 
ATOM   14776 C CD2 . LEU D 1 300 ? -38.911 38.455  79.611  1.00 47.63  ? 300 LEU D CD2 1 
ATOM   14777 N N   . ILE D 1 301 ? -34.194 36.651  77.374  1.00 45.71  ? 301 ILE D N   1 
ATOM   14778 C CA  . ILE D 1 301 ? -32.948 36.931  76.669  1.00 43.69  ? 301 ILE D CA  1 
ATOM   14779 C C   . ILE D 1 301 ? -32.177 35.626  76.518  1.00 45.97  ? 301 ILE D C   1 
ATOM   14780 O O   . ILE D 1 301 ? -32.226 34.750  77.386  1.00 50.01  ? 301 ILE D O   1 
ATOM   14781 C CB  . ILE D 1 301 ? -32.127 38.015  77.411  1.00 41.68  ? 301 ILE D CB  1 
ATOM   14782 C CG1 . ILE D 1 301 ? -30.811 38.306  76.693  1.00 41.80  ? 301 ILE D CG1 1 
ATOM   14783 C CG2 . ILE D 1 301 ? -31.877 37.615  78.857  1.00 40.07  ? 301 ILE D CG2 1 
ATOM   14784 C CD1 . ILE D 1 301 ? -30.479 39.777  76.658  1.00 41.01  ? 301 ILE D CD1 1 
ATOM   14785 N N   . SER D 1 302 ? -31.465 35.494  75.399  1.00 49.24  ? 302 SER D N   1 
ATOM   14786 C CA  . SER D 1 302 ? -30.737 34.273  75.082  1.00 49.59  ? 302 SER D CA  1 
ATOM   14787 C C   . SER D 1 302 ? -29.297 34.361  75.573  1.00 45.05  ? 302 SER D C   1 
ATOM   14788 O O   . SER D 1 302 ? -28.631 35.387  75.411  1.00 47.72  ? 302 SER D O   1 
ATOM   14789 C CB  . SER D 1 302 ? -30.748 34.007  73.578  1.00 51.63  ? 302 SER D CB  1 
ATOM   14790 O OG  . SER D 1 302 ? -32.004 33.515  73.155  1.00 52.82  ? 302 SER D OG  1 
ATOM   14791 N N   . VAL D 1 303 ? -28.818 33.271  76.168  1.00 44.97  ? 303 VAL D N   1 
ATOM   14792 C CA  . VAL D 1 303 ? -27.456 33.192  76.681  1.00 43.94  ? 303 VAL D CA  1 
ATOM   14793 C C   . VAL D 1 303 ? -26.776 31.971  76.083  1.00 45.42  ? 303 VAL D C   1 
ATOM   14794 O O   . VAL D 1 303 ? -27.336 30.869  76.098  1.00 46.58  ? 303 VAL D O   1 
ATOM   14795 C CB  . VAL D 1 303 ? -27.419 33.127  78.218  1.00 42.27  ? 303 VAL D CB  1 
ATOM   14796 C CG1 . VAL D 1 303 ? -25.977 33.173  78.706  1.00 45.28  ? 303 VAL D CG1 1 
ATOM   14797 C CG2 . VAL D 1 303 ? -28.221 34.268  78.816  1.00 40.97  ? 303 VAL D CG2 1 
ATOM   14798 N N   . PHE D 1 304 ? -25.576 32.172  75.554  1.00 46.05  ? 304 PHE D N   1 
ATOM   14799 C CA  . PHE D 1 304 ? -24.713 31.102  75.082  1.00 46.75  ? 304 PHE D CA  1 
ATOM   14800 C C   . PHE D 1 304 ? -23.487 31.056  75.983  1.00 47.51  ? 304 PHE D C   1 
ATOM   14801 O O   . PHE D 1 304 ? -22.989 32.100  76.417  1.00 47.76  ? 304 PHE D O   1 
ATOM   14802 C CB  . PHE D 1 304 ? -24.304 31.345  73.626  1.00 53.84  ? 304 PHE D CB  1 
ATOM   14803 C CG  . PHE D 1 304 ? -25.467 31.408  72.670  1.00 67.93  ? 304 PHE D CG  1 
ATOM   14804 C CD1 . PHE D 1 304 ? -26.612 30.659  72.891  1.00 69.59  ? 304 PHE D CD1 1 
ATOM   14805 C CD2 . PHE D 1 304 ? -25.405 32.203  71.536  1.00 66.33  ? 304 PHE D CD2 1 
ATOM   14806 C CE1 . PHE D 1 304 ? -27.674 30.713  72.004  1.00 76.16  ? 304 PHE D CE1 1 
ATOM   14807 C CE2 . PHE D 1 304 ? -26.456 32.253  70.643  1.00 66.87  ? 304 PHE D CE2 1 
ATOM   14808 C CZ  . PHE D 1 304 ? -27.597 31.511  70.877  1.00 75.43  ? 304 PHE D CZ  1 
ATOM   14809 N N   . PHE D 1 305 ? -23.009 29.857  76.285  1.00 51.56  ? 305 PHE D N   1 
ATOM   14810 C CA  . PHE D 1 305 ? -21.904 29.689  77.222  1.00 47.71  ? 305 PHE D CA  1 
ATOM   14811 C C   . PHE D 1 305 ? -20.674 29.226  76.453  1.00 51.61  ? 305 PHE D C   1 
ATOM   14812 O O   . PHE D 1 305 ? -20.644 28.105  75.933  1.00 62.21  ? 305 PHE D O   1 
ATOM   14813 C CB  . PHE D 1 305 ? -22.278 28.713  78.335  1.00 47.37  ? 305 PHE D CB  1 
ATOM   14814 C CG  . PHE D 1 305 ? -23.191 29.310  79.369  1.00 43.71  ? 305 PHE D CG  1 
ATOM   14815 C CD1 . PHE D 1 305 ? -24.565 29.242  79.220  1.00 44.13  ? 305 PHE D CD1 1 
ATOM   14816 C CD2 . PHE D 1 305 ? -22.676 29.959  80.477  1.00 43.66  ? 305 PHE D CD2 1 
ATOM   14817 C CE1 . PHE D 1 305 ? -25.408 29.797  80.164  1.00 42.84  ? 305 PHE D CE1 1 
ATOM   14818 C CE2 . PHE D 1 305 ? -23.515 30.511  81.427  1.00 40.75  ? 305 PHE D CE2 1 
ATOM   14819 C CZ  . PHE D 1 305 ? -24.881 30.433  81.268  1.00 41.13  ? 305 PHE D CZ  1 
ATOM   14820 N N   . ARG D 1 306 ? -19.665 30.093  76.383  1.00 49.08  ? 306 ARG D N   1 
ATOM   14821 C CA  . ARG D 1 306 ? -18.452 29.767  75.647  1.00 59.73  ? 306 ARG D CA  1 
ATOM   14822 C C   . ARG D 1 306 ? -17.748 28.577  76.284  1.00 51.32  ? 306 ARG D C   1 
ATOM   14823 O O   . ARG D 1 306 ? -17.619 28.489  77.510  1.00 48.64  ? 306 ARG D O   1 
ATOM   14824 C CB  . ARG D 1 306 ? -17.516 30.983  75.583  1.00 55.67  ? 306 ARG D CB  1 
ATOM   14825 C CG  . ARG D 1 306 ? -16.830 31.361  76.896  1.00 50.21  ? 306 ARG D CG  1 
ATOM   14826 C CD  . ARG D 1 306 ? -15.348 31.664  76.683  1.00 45.44  ? 306 ARG D CD  1 
ATOM   14827 N NE  . ARG D 1 306 ? -14.573 31.537  77.912  1.00 43.64  ? 306 ARG D NE  1 
ATOM   14828 C CZ  . ARG D 1 306 ? -13.289 31.851  78.027  1.00 43.69  ? 306 ARG D CZ  1 
ATOM   14829 N NH1 . ARG D 1 306 ? -12.599 32.327  77.004  1.00 44.44  ? 306 ARG D NH1 1 
ATOM   14830 N NH2 . ARG D 1 306 ? -12.682 31.684  79.199  1.00 43.11  ? 306 ARG D NH2 1 
ATOM   14831 N N   . ASP D 1 307 ? -17.320 27.641  75.442  1.00 54.26  ? 307 ASP D N   1 
ATOM   14832 C CA  . ASP D 1 307 ? -16.570 26.497  75.936  1.00 55.59  ? 307 ASP D CA  1 
ATOM   14833 C C   . ASP D 1 307 ? -15.187 26.989  76.342  1.00 49.08  ? 307 ASP D C   1 
ATOM   14834 O O   . ASP D 1 307 ? -14.360 27.327  75.489  1.00 51.15  ? 307 ASP D O   1 
ATOM   14835 C CB  . ASP D 1 307 ? -16.494 25.392  74.886  1.00 53.06  ? 307 ASP D CB  1 
ATOM   14836 C CG  . ASP D 1 307 ? -16.136 24.049  75.492  1.00 55.11  ? 307 ASP D CG  1 
ATOM   14837 O OD1 . ASP D 1 307 ? -15.961 23.983  76.730  1.00 63.55  ? 307 ASP D OD1 1 
ATOM   14838 O OD2 . ASP D 1 307 ? -16.058 23.057  74.742  1.00 57.68  ? 307 ASP D OD2 1 
ATOM   14839 N N   . LYS D 1 308 ? -14.940 27.023  77.653  1.00 47.95  ? 308 LYS D N   1 
ATOM   14840 C CA  . LYS D 1 308 ? -13.728 27.644  78.177  1.00 47.18  ? 308 LYS D CA  1 
ATOM   14841 C C   . LYS D 1 308 ? -12.477 26.909  77.709  1.00 48.68  ? 308 LYS D C   1 
ATOM   14842 O O   . LYS D 1 308 ? -11.475 27.538  77.357  1.00 48.67  ? 308 LYS D O   1 
ATOM   14843 C CB  . LYS D 1 308 ? -13.789 27.676  79.703  1.00 45.97  ? 308 LYS D CB  1 
ATOM   14844 C CG  . LYS D 1 308 ? -12.479 27.397  80.412  1.00 46.21  ? 308 LYS D CG  1 
ATOM   14845 C CD  . LYS D 1 308 ? -12.742 27.208  81.892  1.00 46.68  ? 308 LYS D CD  1 
ATOM   14846 C CE  . LYS D 1 308 ? -11.559 27.592  82.758  1.00 72.69  ? 308 LYS D CE  1 
ATOM   14847 N NZ  . LYS D 1 308 ? -11.620 26.910  84.083  1.00 72.10  ? 308 LYS D NZ  1 
ATOM   14848 N N   . THR D 1 309 ? -12.510 25.574  77.683  1.00 52.60  ? 309 THR D N   1 
ATOM   14849 C CA  . THR D 1 309 ? -11.300 24.848  77.307  1.00 53.38  ? 309 THR D CA  1 
ATOM   14850 C C   . THR D 1 309 ? -10.892 25.206  75.876  1.00 52.53  ? 309 THR D C   1 
ATOM   14851 O O   . THR D 1 309 ? -9.765  25.676  75.629  1.00 52.65  ? 309 THR D O   1 
ATOM   14852 C CB  . THR D 1 309 ? -11.504 23.332  77.472  1.00 53.27  ? 309 THR D CB  1 
ATOM   14853 O OG1 . THR D 1 309 ? -10.603 22.623  76.608  1.00 62.37  ? 309 THR D OG1 1 
ATOM   14854 C CG2 . THR D 1 309 ? -12.960 22.936  77.155  1.00 53.58  ? 309 THR D CG2 1 
ATOM   14855 N N   . LEU D 1 310 ? -11.829 25.104  74.928  1.00 53.17  ? 310 LEU D N   1 
ATOM   14856 C CA  . LEU D 1 310 ? -11.474 25.353  73.527  1.00 55.97  ? 310 LEU D CA  1 
ATOM   14857 C C   . LEU D 1 310 ? -11.008 26.783  73.282  1.00 56.54  ? 310 LEU D C   1 
ATOM   14858 O O   . LEU D 1 310 ? -10.127 27.015  72.445  1.00 54.83  ? 310 LEU D O   1 
ATOM   14859 C CB  . LEU D 1 310 ? -12.667 25.009  72.605  1.00 55.27  ? 310 LEU D CB  1 
ATOM   14860 C CG  . LEU D 1 310 ? -12.869 23.527  72.280  1.00 57.28  ? 310 LEU D CG  1 
ATOM   14861 C CD1 . LEU D 1 310 ? -13.247 22.680  73.481  1.00 62.94  ? 310 LEU D CD1 1 
ATOM   14862 C CD2 . LEU D 1 310 ? -13.886 23.341  71.141  1.00 64.04  ? 310 LEU D CD2 1 
ATOM   14863 N N   . SER D 1 311 ? -11.590 27.742  73.987  1.00 60.92  ? 311 SER D N   1 
ATOM   14864 C CA  . SER D 1 311 ? -11.123 29.117  73.879  1.00 50.35  ? 311 SER D CA  1 
ATOM   14865 C C   . SER D 1 311 ? -9.769  29.290  74.553  1.00 50.08  ? 311 SER D C   1 
ATOM   14866 O O   . SER D 1 311 ? -8.892  29.996  74.036  1.00 50.34  ? 311 SER D O   1 
ATOM   14867 C CB  . SER D 1 311 ? -12.146 30.072  74.496  1.00 48.61  ? 311 SER D CB  1 
ATOM   14868 O OG  . SER D 1 311 ? -13.438 29.784  73.994  1.00 48.99  ? 311 SER D OG  1 
ATOM   14869 N N   . ASP D 1 312 ? -9.573  28.633  75.697  1.00 52.32  ? 312 ASP D N   1 
ATOM   14870 C CA  . ASP D 1 312 ? -8.315  28.768  76.420  1.00 56.19  ? 312 ASP D CA  1 
ATOM   14871 C C   . ASP D 1 312 ? -7.135  28.190  75.645  1.00 61.88  ? 312 ASP D C   1 
ATOM   14872 O O   . ASP D 1 312 ? -6.018  28.700  75.768  1.00 61.70  ? 312 ASP D O   1 
ATOM   14873 C CB  . ASP D 1 312 ? -8.413  28.107  77.796  1.00 52.09  ? 312 ASP D CB  1 
ATOM   14874 C CG  . ASP D 1 312 ? -8.918  29.059  78.868  1.00 60.99  ? 312 ASP D CG  1 
ATOM   14875 O OD1 . ASP D 1 312 ? -8.927  30.286  78.626  1.00 81.04  ? 312 ASP D OD1 1 
ATOM   14876 O OD2 . ASP D 1 312 ? -9.316  28.576  79.950  1.00 53.40  ? 312 ASP D OD2 1 
ATOM   14877 N N   . LEU D 1 313 ? -7.331  27.118  74.874  1.00 56.17  ? 313 LEU D N   1 
ATOM   14878 C CA  . LEU D 1 313 ? -6.188  26.551  74.165  1.00 54.65  ? 313 LEU D CA  1 
ATOM   14879 C C   . LEU D 1 313 ? -5.614  27.553  73.172  1.00 57.92  ? 313 LEU D C   1 
ATOM   14880 O O   . LEU D 1 313 ? -4.395  27.753  73.105  1.00 64.29  ? 313 LEU D O   1 
ATOM   14881 C CB  . LEU D 1 313 ? -6.555  25.260  73.434  1.00 56.40  ? 313 LEU D CB  1 
ATOM   14882 C CG  . LEU D 1 313 ? -7.197  23.997  73.995  1.00 57.65  ? 313 LEU D CG  1 
ATOM   14883 C CD1 . LEU D 1 313 ? -8.475  23.592  73.160  1.00 67.75  ? 313 LEU D CD1 1 
ATOM   14884 C CD2 . LEU D 1 313 ? -6.099  22.910  74.114  1.00 58.70  ? 313 LEU D CD2 1 
ATOM   14885 N N   . ILE D 1 314 ? -6.482  28.193  72.388  1.00 54.54  ? 314 ILE D N   1 
ATOM   14886 C CA  . ILE D 1 314 ? -6.006  29.146  71.391  1.00 54.94  ? 314 ILE D CA  1 
ATOM   14887 C C   . ILE D 1 314 ? -5.296  30.308  72.070  1.00 53.78  ? 314 ILE D C   1 
ATOM   14888 O O   . ILE D 1 314 ? -4.203  30.713  71.662  1.00 62.27  ? 314 ILE D O   1 
ATOM   14889 C CB  . ILE D 1 314 ? -7.168  29.638  70.509  1.00 54.86  ? 314 ILE D CB  1 
ATOM   14890 C CG1 . ILE D 1 314 ? -8.034  28.463  70.050  1.00 55.93  ? 314 ILE D CG1 1 
ATOM   14891 C CG2 . ILE D 1 314 ? -6.627  30.407  69.303  1.00 56.45  ? 314 ILE D CG2 1 
ATOM   14892 C CD1 . ILE D 1 314 ? -9.103  28.843  69.049  1.00 56.31  ? 314 ILE D CD1 1 
ATOM   14893 N N   . GLY D 1 315 ? -5.894  30.846  73.136  1.00 52.05  ? 315 GLY D N   1 
ATOM   14894 C CA  . GLY D 1 315 ? -5.358  32.046  73.753  1.00 56.69  ? 315 GLY D CA  1 
ATOM   14895 C C   . GLY D 1 315 ? -4.129  31.840  74.610  1.00 56.66  ? 315 GLY D C   1 
ATOM   14896 O O   . GLY D 1 315 ? -3.391  32.802  74.846  1.00 57.62  ? 315 GLY D O   1 
ATOM   14897 N N   . PHE D 1 316 ? -3.887  30.617  75.086  1.00 51.86  ? 316 PHE D N   1 
ATOM   14898 C CA  . PHE D 1 316 ? -2.778  30.398  76.008  1.00 57.07  ? 316 PHE D CA  1 
ATOM   14899 C C   . PHE D 1 316 ? -1.945  29.151  75.742  1.00 68.79  ? 316 PHE D C   1 
ATOM   14900 O O   . PHE D 1 316 ? -0.877  29.025  76.349  1.00 72.41  ? 316 PHE D O   1 
ATOM   14901 C CB  . PHE D 1 316 ? -3.298  30.337  77.454  1.00 60.78  ? 316 PHE D CB  1 
ATOM   14902 C CG  . PHE D 1 316 ? -3.475  31.686  78.095  1.00 64.28  ? 316 PHE D CG  1 
ATOM   14903 C CD1 . PHE D 1 316 ? -2.483  32.649  78.006  1.00 64.64  ? 316 PHE D CD1 1 
ATOM   14904 C CD2 . PHE D 1 316 ? -4.636  31.990  78.789  1.00 57.67  ? 316 PHE D CD2 1 
ATOM   14905 C CE1 . PHE D 1 316 ? -2.644  33.892  78.595  1.00 48.26  ? 316 PHE D CE1 1 
ATOM   14906 C CE2 . PHE D 1 316 ? -4.803  33.230  79.380  1.00 53.95  ? 316 PHE D CE2 1 
ATOM   14907 C CZ  . PHE D 1 316 ? -3.806  34.182  79.283  1.00 46.88  ? 316 PHE D CZ  1 
ATOM   14908 N N   . SER D 1 317 ? -2.369  28.236  74.874  1.00 67.39  ? 317 SER D N   1 
ATOM   14909 C CA  . SER D 1 317 ? -1.706  26.941  74.750  1.00 62.91  ? 317 SER D CA  1 
ATOM   14910 C C   . SER D 1 317 ? -1.108  26.678  73.377  1.00 68.02  ? 317 SER D C   1 
ATOM   14911 O O   . SER D 1 317 ? -0.034  26.079  73.286  1.00 68.64  ? 317 SER D O   1 
ATOM   14912 C CB  . SER D 1 317 ? -2.692  25.813  75.093  1.00 58.50  ? 317 SER D CB  1 
ATOM   14913 O OG  . SER D 1 317 ? -3.443  26.130  76.252  1.00 68.67  ? 317 SER D OG  1 
ATOM   14914 N N   . TYR D 1 318 ? -1.772  27.100  72.303  1.00 71.66  ? 318 TYR D N   1 
ATOM   14915 C CA  . TYR D 1 318 ? -1.328  26.785  70.950  1.00 68.17  ? 318 TYR D CA  1 
ATOM   14916 C C   . TYR D 1 318 ? -0.161  27.644  70.475  1.00 67.95  ? 318 TYR D C   1 
ATOM   14917 O O   . TYR D 1 318 ? 0.185   27.578  69.290  1.00 72.90  ? 318 TYR D O   1 
ATOM   14918 C CB  . TYR D 1 318 ? -2.491  26.921  69.962  1.00 66.50  ? 318 TYR D CB  1 
ATOM   14919 C CG  . TYR D 1 318 ? -3.544  25.842  70.082  1.00 60.53  ? 318 TYR D CG  1 
ATOM   14920 C CD1 . TYR D 1 318 ? -3.268  24.637  70.714  1.00 61.31  ? 318 TYR D CD1 1 
ATOM   14921 C CD2 . TYR D 1 318 ? -4.815  26.029  69.553  1.00 60.16  ? 318 TYR D CD2 1 
ATOM   14922 C CE1 . TYR D 1 318 ? -4.231  23.650  70.821  1.00 61.71  ? 318 TYR D CE1 1 
ATOM   14923 C CE2 . TYR D 1 318 ? -5.783  25.050  69.655  1.00 60.56  ? 318 TYR D CE2 1 
ATOM   14924 C CZ  . TYR D 1 318 ? -5.487  23.863  70.289  1.00 61.33  ? 318 TYR D CZ  1 
ATOM   14925 O OH  . TYR D 1 318 ? -6.453  22.888  70.390  1.00 61.95  ? 318 TYR D OH  1 
ATOM   14926 N N   . HIS D 1 319 ? 0.449   28.449  71.346  1.00 69.58  ? 319 HIS D N   1 
ATOM   14927 C CA  . HIS D 1 319 ? 1.617   29.214  70.924  1.00 70.39  ? 319 HIS D CA  1 
ATOM   14928 C C   . HIS D 1 319 ? 2.862   28.340  70.830  1.00 71.55  ? 319 HIS D C   1 
ATOM   14929 O O   . HIS D 1 319 ? 3.704   28.561  69.954  1.00 74.01  ? 319 HIS D O   1 
ATOM   14930 C CB  . HIS D 1 319 ? 1.864   30.396  71.867  1.00 63.48  ? 319 HIS D CB  1 
ATOM   14931 C CG  . HIS D 1 319 ? 2.240   30.001  73.261  1.00 61.18  ? 319 HIS D CG  1 
ATOM   14932 N ND1 . HIS D 1 319 ? 1.485   29.137  74.026  1.00 69.63  ? 319 HIS D ND1 1 
ATOM   14933 C CD2 . HIS D 1 319 ? 3.294   30.362  74.032  1.00 59.00  ? 319 HIS D CD2 1 
ATOM   14934 C CE1 . HIS D 1 319 ? 2.059   28.981  75.206  1.00 83.98  ? 319 HIS D CE1 1 
ATOM   14935 N NE2 . HIS D 1 319 ? 3.158   29.713  75.235  1.00 75.30  ? 319 HIS D NE2 1 
ATOM   14936 N N   . ALA D 1 320 ? 2.989   27.345  71.707  1.00 66.61  ? 320 ALA D N   1 
ATOM   14937 C CA  . ALA D 1 320 ? 4.095   26.399  71.672  1.00 69.85  ? 320 ALA D CA  1 
ATOM   14938 C C   . ALA D 1 320 ? 3.742   25.125  70.917  1.00 70.70  ? 320 ALA D C   1 
ATOM   14939 O O   . ALA D 1 320 ? 4.506   24.154  70.964  1.00 67.67  ? 320 ALA D O   1 
ATOM   14940 C CB  . ALA D 1 320 ? 4.545   26.058  73.094  1.00 64.33  ? 320 ALA D CB  1 
ATOM   14941 N N   . TRP D 1 321 ? 2.607   25.107  70.226  1.00 79.55  ? 321 TRP D N   1 
ATOM   14942 C CA  . TRP D 1 321 ? 2.127   23.938  69.503  1.00 77.88  ? 321 TRP D CA  1 
ATOM   14943 C C   . TRP D 1 321 ? 2.305   24.162  68.009  1.00 77.33  ? 321 TRP D C   1 
ATOM   14944 O O   . TRP D 1 321 ? 1.909   25.209  67.484  1.00 80.00  ? 321 TRP D O   1 
ATOM   14945 C CB  . TRP D 1 321 ? 0.655   23.673  69.822  1.00 74.39  ? 321 TRP D CB  1 
ATOM   14946 C CG  . TRP D 1 321 ? 0.442   22.735  70.964  1.00 76.54  ? 321 TRP D CG  1 
ATOM   14947 C CD1 . TRP D 1 321 ? 1.037   22.787  72.192  1.00 71.31  ? 321 TRP D CD1 1 
ATOM   14948 C CD2 . TRP D 1 321 ? -0.438  21.607  70.991  1.00 82.76  ? 321 TRP D CD2 1 
ATOM   14949 N NE1 . TRP D 1 321 ? 0.585   21.756  72.979  1.00 79.95  ? 321 TRP D NE1 1 
ATOM   14950 C CE2 . TRP D 1 321 ? -0.322  21.017  72.266  1.00 87.36  ? 321 TRP D CE2 1 
ATOM   14951 C CE3 . TRP D 1 321 ? -1.311  21.037  70.061  1.00 75.98  ? 321 TRP D CE3 1 
ATOM   14952 C CZ2 . TRP D 1 321 ? -1.047  19.885  72.632  1.00 88.69  ? 321 TRP D CZ2 1 
ATOM   14953 C CZ3 . TRP D 1 321 ? -2.029  19.913  70.426  1.00 72.79  ? 321 TRP D CZ3 1 
ATOM   14954 C CH2 . TRP D 1 321 ? -1.893  19.350  71.700  1.00 82.50  ? 321 TRP D CH2 1 
ATOM   14955 N N   . ASN D 1 322 ? 2.894   23.181  67.327  1.00 71.05  ? 322 ASN D N   1 
ATOM   14956 C CA  . ASN D 1 322 ? 3.074   23.294  65.887  1.00 71.84  ? 322 ASN D CA  1 
ATOM   14957 C C   . ASN D 1 322 ? 1.719   23.353  65.191  1.00 76.72  ? 322 ASN D C   1 
ATOM   14958 O O   . ASN D 1 322 ? 0.723   22.807  65.674  1.00 78.28  ? 322 ASN D O   1 
ATOM   14959 C CB  . ASN D 1 322 ? 3.899   22.125  65.351  1.00 74.29  ? 322 ASN D CB  1 
ATOM   14960 C CG  . ASN D 1 322 ? 5.310   22.536  64.979  1.00 75.43  ? 322 ASN D CG  1 
ATOM   14961 O OD1 . ASN D 1 322 ? 5.965   23.278  65.711  1.00 74.52  ? 322 ASN D OD1 1 
ATOM   14962 N ND2 . ASN D 1 322 ? 5.779   22.069  63.826  1.00 77.52  ? 322 ASN D ND2 1 
ATOM   14963 N N   . ALA D 1 323 ? 1.693   24.037  64.045  1.00 81.76  ? 323 ALA D N   1 
ATOM   14964 C CA  . ALA D 1 323 ? 0.428   24.414  63.422  1.00 81.36  ? 323 ALA D CA  1 
ATOM   14965 C C   . ALA D 1 323 ? -0.424  23.192  63.098  1.00 82.18  ? 323 ALA D C   1 
ATOM   14966 O O   . ALA D 1 323 ? -1.566  23.079  63.556  1.00 80.76  ? 323 ALA D O   1 
ATOM   14967 C CB  . ALA D 1 323 ? 0.696   25.236  62.160  1.00 82.88  ? 323 ALA D CB  1 
ATOM   14968 N N   . GLU D 1 324 ? 0.130   22.242  62.341  1.00 84.58  ? 324 GLU D N   1 
ATOM   14969 C CA  . GLU D 1 324 ? -0.660  21.096  61.908  1.00 85.71  ? 324 GLU D CA  1 
ATOM   14970 C C   . GLU D 1 324 ? -1.010  20.147  63.047  1.00 85.92  ? 324 GLU D C   1 
ATOM   14971 O O   . GLU D 1 324 ? -1.900  19.307  62.875  1.00 87.11  ? 324 GLU D O   1 
ATOM   14972 C CB  . GLU D 1 324 ? 0.074   20.336  60.802  1.00 89.14  ? 324 GLU D CB  1 
ATOM   14973 C CG  . GLU D 1 324 ? 0.724   21.232  59.764  1.00 90.13  ? 324 GLU D CG  1 
ATOM   14974 C CD  . GLU D 1 324 ? 2.235   21.142  59.781  1.00 92.58  ? 324 GLU D CD  1 
ATOM   14975 O OE1 . GLU D 1 324 ? 2.850   21.639  60.748  1.00 89.91  ? 324 GLU D OE1 1 
ATOM   14976 O OE2 . GLU D 1 324 ? 2.806   20.571  58.829  1.00 94.09  ? 324 GLU D OE2 1 
ATOM   14977 N N   . ASP D 1 325 ? -0.336  20.252  64.193  1.00 90.69  ? 325 ASP D N   1 
ATOM   14978 C CA  . ASP D 1 325 ? -0.735  19.472  65.360  1.00 93.05  ? 325 ASP D CA  1 
ATOM   14979 C C   . ASP D 1 325 ? -1.900  20.125  66.092  1.00 82.96  ? 325 ASP D C   1 
ATOM   14980 O O   . ASP D 1 325 ? -2.802  19.430  66.574  1.00 79.02  ? 325 ASP D O   1 
ATOM   14981 C CB  . ASP D 1 325 ? 0.452   19.297  66.309  1.00 88.42  ? 325 ASP D CB  1 
ATOM   14982 C CG  . ASP D 1 325 ? 1.611   18.566  65.666  1.00 86.87  ? 325 ASP D CG  1 
ATOM   14983 O OD1 . ASP D 1 325 ? 1.384   17.489  65.077  1.00 86.18  ? 325 ASP D OD1 1 
ATOM   14984 O OD2 . ASP D 1 325 ? 2.752   19.068  65.757  1.00 85.63  ? 325 ASP D OD2 1 
ATOM   14985 N N   . ALA D 1 326 ? -1.892  21.456  66.187  1.00 78.28  ? 326 ALA D N   1 
ATOM   14986 C CA  . ALA D 1 326 ? -2.944  22.158  66.916  1.00 75.86  ? 326 ALA D CA  1 
ATOM   14987 C C   . ALA D 1 326 ? -4.286  22.040  66.204  1.00 76.12  ? 326 ALA D C   1 
ATOM   14988 O O   . ALA D 1 326 ? -5.314  21.784  66.842  1.00 75.32  ? 326 ALA D O   1 
ATOM   14989 C CB  . ALA D 1 326 ? -2.561  23.626  67.103  1.00 74.60  ? 326 ALA D CB  1 
ATOM   14990 N N   . VAL D 1 327 ? -4.299  22.232  64.882  1.00 77.81  ? 327 VAL D N   1 
ATOM   14991 C CA  . VAL D 1 327 ? -5.551  22.146  64.135  1.00 78.29  ? 327 VAL D CA  1 
ATOM   14992 C C   . VAL D 1 327 ? -6.153  20.754  64.261  1.00 83.07  ? 327 VAL D C   1 
ATOM   14993 O O   . VAL D 1 327 ? -7.366  20.603  64.443  1.00 78.44  ? 327 VAL D O   1 
ATOM   14994 C CB  . VAL D 1 327 ? -5.335  22.537  62.661  1.00 82.24  ? 327 VAL D CB  1 
ATOM   14995 C CG1 . VAL D 1 327 ? -6.660  22.906  62.021  1.00 80.31  ? 327 VAL D CG1 1 
ATOM   14996 C CG2 . VAL D 1 327 ? -4.375  23.703  62.552  1.00 79.99  ? 327 VAL D CG2 1 
ATOM   14997 N N   . ARG D 1 328 ? -5.319  19.716  64.167  1.00 93.14  ? 328 ARG D N   1 
ATOM   14998 C CA  . ARG D 1 328 ? -5.815  18.353  64.334  1.00 95.90  ? 328 ARG D CA  1 
ATOM   14999 C C   . ARG D 1 328 ? -6.369  18.131  65.736  1.00 88.67  ? 328 ARG D C   1 
ATOM   15000 O O   . ARG D 1 328 ? -7.425  17.509  65.903  1.00 79.58  ? 328 ARG D O   1 
ATOM   15001 C CB  . ARG D 1 328 ? -4.703  17.349  64.038  1.00 83.75  ? 328 ARG D CB  1 
ATOM   15002 C CG  . ARG D 1 328 ? -4.442  17.110  62.562  1.00 86.42  ? 328 ARG D CG  1 
ATOM   15003 C CD  . ARG D 1 328 ? -3.786  15.756  62.348  1.00 88.82  ? 328 ARG D CD  1 
ATOM   15004 N NE  . ARG D 1 328 ? -2.629  15.572  63.215  1.00 108.52 ? 328 ARG D NE  1 
ATOM   15005 C CZ  . ARG D 1 328 ? -2.591  14.747  64.253  1.00 110.36 ? 328 ARG D CZ  1 
ATOM   15006 N NH1 . ARG D 1 328 ? -3.635  14.005  64.584  1.00 112.21 ? 328 ARG D NH1 1 
ATOM   15007 N NH2 . ARG D 1 328 ? -1.481  14.669  64.980  1.00 113.66 ? 328 ARG D NH2 1 
ATOM   15008 N N   . ASP D 1 329 ? -5.665  18.625  66.759  1.00 81.53  ? 329 ASP D N   1 
ATOM   15009 C CA  . ASP D 1 329 ? -6.163  18.503  68.126  1.00 78.41  ? 329 ASP D CA  1 
ATOM   15010 C C   . ASP D 1 329 ? -7.476  19.254  68.296  1.00 75.20  ? 329 ASP D C   1 
ATOM   15011 O O   . ASP D 1 329 ? -8.409  18.754  68.933  1.00 76.65  ? 329 ASP D O   1 
ATOM   15012 C CB  . ASP D 1 329 ? -5.112  19.017  69.113  1.00 74.79  ? 329 ASP D CB  1 
ATOM   15013 C CG  . ASP D 1 329 ? -5.607  19.031  70.553  1.00 72.77  ? 329 ASP D CG  1 
ATOM   15014 O OD1 . ASP D 1 329 ? -6.416  19.916  70.908  1.00 71.05  ? 329 ASP D OD1 1 
ATOM   15015 O OD2 . ASP D 1 329 ? -5.177  18.159  71.338  1.00 74.50  ? 329 ASP D OD2 1 
ATOM   15016 N N   . PHE D 1 330 ? -7.565  20.458  67.727  1.00 73.93  ? 330 PHE D N   1 
ATOM   15017 C CA  . PHE D 1 330 ? -8.762  21.281  67.871  1.00 72.47  ? 330 PHE D CA  1 
ATOM   15018 C C   . PHE D 1 330 ? -9.980  20.588  67.272  1.00 81.57  ? 330 PHE D C   1 
ATOM   15019 O O   . PHE D 1 330 ? -11.015 20.446  67.934  1.00 73.85  ? 330 PHE D O   1 
ATOM   15020 C CB  . PHE D 1 330 ? -8.515  22.647  67.222  1.00 72.16  ? 330 PHE D CB  1 
ATOM   15021 C CG  . PHE D 1 330 ? -9.678  23.601  67.305  1.00 70.80  ? 330 PHE D CG  1 
ATOM   15022 C CD1 . PHE D 1 330 ? -10.738 23.521  66.413  1.00 71.75  ? 330 PHE D CD1 1 
ATOM   15023 C CD2 . PHE D 1 330 ? -9.701  24.588  68.273  1.00 68.71  ? 330 PHE D CD2 1 
ATOM   15024 C CE1 . PHE D 1 330 ? -11.796 24.408  66.493  1.00 70.61  ? 330 PHE D CE1 1 
ATOM   15025 C CE2 . PHE D 1 330 ? -10.759 25.472  68.358  1.00 70.61  ? 330 PHE D CE2 1 
ATOM   15026 C CZ  . PHE D 1 330 ? -11.808 25.379  67.467  1.00 79.79  ? 330 PHE D CZ  1 
ATOM   15027 N N   . ILE D 1 331 ? -9.874  20.142  66.018  1.00 84.57  ? 331 ILE D N   1 
ATOM   15028 C CA  . ILE D 1 331 ? -10.990 19.440  65.392  1.00 77.00  ? 331 ILE D CA  1 
ATOM   15029 C C   . ILE D 1 331 ? -11.242 18.110  66.088  1.00 77.38  ? 331 ILE D C   1 
ATOM   15030 O O   . ILE D 1 331 ? -12.382 17.632  66.139  1.00 78.68  ? 331 ILE D O   1 
ATOM   15031 C CB  . ILE D 1 331 ? -10.738 19.256  63.884  1.00 79.96  ? 331 ILE D CB  1 
ATOM   15032 C CG1 . ILE D 1 331 ? -10.197 20.550  63.270  1.00 79.23  ? 331 ILE D CG1 1 
ATOM   15033 C CG2 . ILE D 1 331 ? -12.016 18.830  63.182  1.00 82.91  ? 331 ILE D CG2 1 
ATOM   15034 C CD1 . ILE D 1 331 ? -11.251 21.607  63.022  1.00 78.29  ? 331 ILE D CD1 1 
ATOM   15035 N N   . GLY D 1 332 ? -10.192 17.489  66.630  1.00 77.61  ? 332 GLY D N   1 
ATOM   15036 C CA  . GLY D 1 332 ? -10.385 16.310  67.456  1.00 85.06  ? 332 GLY D CA  1 
ATOM   15037 C C   . GLY D 1 332 ? -11.174 16.598  68.718  1.00 82.26  ? 332 GLY D C   1 
ATOM   15038 O O   . GLY D 1 332 ? -11.885 15.725  69.224  1.00 75.85  ? 332 GLY D O   1 
ATOM   15039 N N   . ARG D 1 333 ? -11.045 17.813  69.256  1.00 85.73  ? 333 ARG D N   1 
ATOM   15040 C CA  . ARG D 1 333 ? -11.852 18.197  70.408  1.00 75.97  ? 333 ARG D CA  1 
ATOM   15041 C C   . ARG D 1 333 ? -13.305 18.429  70.007  1.00 72.79  ? 333 ARG D C   1 
ATOM   15042 O O   . ARG D 1 333 ? -14.225 18.049  70.741  1.00 70.90  ? 333 ARG D O   1 
ATOM   15043 C CB  . ARG D 1 333 ? -11.263 19.444  71.072  1.00 69.56  ? 333 ARG D CB  1 
ATOM   15044 C CG  . ARG D 1 333 ? -9.865  19.235  71.642  1.00 69.53  ? 333 ARG D CG  1 
ATOM   15045 C CD  . ARG D 1 333 ? -9.788  19.589  73.118  1.00 67.58  ? 333 ARG D CD  1 
ATOM   15046 N NE  . ARG D 1 333 ? -8.417  19.832  73.551  1.00 67.37  ? 333 ARG D NE  1 
ATOM   15047 C CZ  . ARG D 1 333 ? -8.018  19.807  74.816  1.00 66.28  ? 333 ARG D CZ  1 
ATOM   15048 N NH1 . ARG D 1 333 ? -8.873  19.605  75.805  1.00 65.21  ? 333 ARG D NH1 1 
ATOM   15049 N NH2 . ARG D 1 333 ? -6.727  19.970  75.093  1.00 66.42  ? 333 ARG D NH2 1 
ATOM   15050 N N   . LEU D 1 334 ? -13.532 19.047  68.842  1.00 76.88  ? 334 LEU D N   1 
ATOM   15051 C CA  . LEU D 1 334 ? -14.901 19.246  68.373  1.00 75.01  ? 334 LEU D CA  1 
ATOM   15052 C C   . LEU D 1 334 ? -15.553 17.931  67.982  1.00 77.21  ? 334 LEU D C   1 
ATOM   15053 O O   . LEU D 1 334 ? -16.745 17.727  68.239  1.00 77.24  ? 334 LEU D O   1 
ATOM   15054 C CB  . LEU D 1 334 ? -14.945 20.196  67.180  1.00 73.03  ? 334 LEU D CB  1 
ATOM   15055 C CG  . LEU D 1 334 ? -14.355 21.594  67.252  1.00 71.61  ? 334 LEU D CG  1 
ATOM   15056 C CD1 . LEU D 1 334 ? -14.004 22.009  65.838  1.00 80.78  ? 334 LEU D CD1 1 
ATOM   15057 C CD2 . LEU D 1 334 ? -15.342 22.556  67.879  1.00 69.78  ? 334 LEU D CD2 1 
ATOM   15058 N N   . LYS D 1 335 ? -14.799 17.035  67.335  1.00 76.31  ? 335 LYS D N   1 
ATOM   15059 C CA  . LYS D 1 335 ? -15.391 15.774  66.907  1.00 78.37  ? 335 LYS D CA  1 
ATOM   15060 C C   . LYS D 1 335 ? -15.885 14.969  68.098  1.00 80.65  ? 335 LYS D C   1 
ATOM   15061 O O   . LYS D 1 335 ? -16.898 14.272  67.991  1.00 85.29  ? 335 LYS D O   1 
ATOM   15062 C CB  . LYS D 1 335 ? -14.397 14.958  66.075  1.00 80.62  ? 335 LYS D CB  1 
ATOM   15063 C CG  . LYS D 1 335 ? -13.269 14.318  66.862  1.00 80.48  ? 335 LYS D CG  1 
ATOM   15064 C CD  . LYS D 1 335 ? -12.797 13.025  66.224  1.00 83.29  ? 335 LYS D CD  1 
ATOM   15065 C CE  . LYS D 1 335 ? -13.241 11.817  67.033  1.00 83.63  ? 335 LYS D CE  1 
ATOM   15066 N NZ  . LYS D 1 335 ? -13.141 10.553  66.251  1.00 86.55  ? 335 LYS D NZ  1 
ATOM   15067 N N   . LYS D 1 336 ? -15.202 15.073  69.242  1.00 83.52  ? 336 LYS D N   1 
ATOM   15068 C CA  . LYS D 1 336 ? -15.688 14.441  70.465  1.00 78.38  ? 336 LYS D CA  1 
ATOM   15069 C C   . LYS D 1 336 ? -17.010 15.051  70.916  1.00 79.45  ? 336 LYS D C   1 
ATOM   15070 O O   . LYS D 1 336 ? -17.905 14.336  71.379  1.00 78.70  ? 336 LYS D O   1 
ATOM   15071 C CB  . LYS D 1 336 ? -14.638 14.562  71.570  1.00 77.49  ? 336 LYS D CB  1 
ATOM   15072 C CG  . LYS D 1 336 ? -13.624 13.428  71.595  1.00 75.65  ? 336 LYS D CG  1 
ATOM   15073 C CD  . LYS D 1 336 ? -12.621 13.584  72.735  1.00 74.32  ? 336 LYS D CD  1 
ATOM   15074 C CE  . LYS D 1 336 ? -13.212 14.326  73.927  1.00 71.99  ? 336 LYS D CE  1 
ATOM   15075 N NZ  . LYS D 1 336 ? -14.141 13.467  74.714  1.00 72.20  ? 336 LYS D NZ  1 
ATOM   15076 N N   . ILE D 1 337 ? -17.146 16.374  70.796  1.00 83.21  ? 337 ILE D N   1 
ATOM   15077 C CA  . ILE D 1 337 ? -18.393 17.040  71.165  1.00 82.66  ? 337 ILE D CA  1 
ATOM   15078 C C   . ILE D 1 337 ? -19.535 16.570  70.272  1.00 83.77  ? 337 ILE D C   1 
ATOM   15079 O O   . ILE D 1 337 ? -20.659 16.341  70.737  1.00 73.10  ? 337 ILE D O   1 
ATOM   15080 C CB  . ILE D 1 337 ? -18.212 18.568  71.099  1.00 76.30  ? 337 ILE D CB  1 
ATOM   15081 C CG1 . ILE D 1 337 ? -17.071 19.005  72.019  1.00 68.83  ? 337 ILE D CG1 1 
ATOM   15082 C CG2 . ILE D 1 337 ? -19.509 19.280  71.449  1.00 83.21  ? 337 ILE D CG2 1 
ATOM   15083 C CD1 . ILE D 1 337 ? -16.450 20.329  71.638  1.00 67.26  ? 337 ILE D CD1 1 
ATOM   15084 N N   . HIS D 1 338 ? -19.262 16.419  68.975  1.00 87.75  ? 338 HIS D N   1 
ATOM   15085 C CA  . HIS D 1 338 ? -20.295 16.036  68.018  1.00 82.26  ? 338 HIS D CA  1 
ATOM   15086 C C   . HIS D 1 338 ? -20.830 14.632  68.283  1.00 88.34  ? 338 HIS D C   1 
ATOM   15087 O O   . HIS D 1 338 ? -21.973 14.326  67.922  1.00 92.12  ? 338 HIS D O   1 
ATOM   15088 C CB  . HIS D 1 338 ? -19.726 16.147  66.602  1.00 85.51  ? 338 HIS D CB  1 
ATOM   15089 C CG  . HIS D 1 338 ? -20.646 15.656  65.530  1.00 86.28  ? 338 HIS D CG  1 
ATOM   15090 N ND1 . HIS D 1 338 ? -20.691 14.336  65.135  1.00 91.06  ? 338 HIS D ND1 1 
ATOM   15091 C CD2 . HIS D 1 338 ? -21.539 16.312  64.751  1.00 82.14  ? 338 HIS D CD2 1 
ATOM   15092 C CE1 . HIS D 1 338 ? -21.582 14.198  64.169  1.00 89.15  ? 338 HIS D CE1 1 
ATOM   15093 N NE2 . HIS D 1 338 ? -22.108 15.383  63.916  1.00 86.11  ? 338 HIS D NE2 1 
ATOM   15094 N N   . GLU D 1 339 ? -20.032 13.772  68.918  1.00 86.24  ? 339 GLU D N   1 
ATOM   15095 C CA  . GLU D 1 339 ? -20.402 12.382  69.159  1.00 85.51  ? 339 GLU D CA  1 
ATOM   15096 C C   . GLU D 1 339 ? -20.804 12.093  70.599  1.00 86.61  ? 339 GLU D C   1 
ATOM   15097 O O   . GLU D 1 339 ? -21.245 10.975  70.885  1.00 82.58  ? 339 GLU D O   1 
ATOM   15098 C CB  . GLU D 1 339 ? -19.238 11.459  68.777  1.00 81.83  ? 339 GLU D CB  1 
ATOM   15099 C CG  . GLU D 1 339 ? -17.938 11.919  69.395  1.00 83.65  ? 339 GLU D CG  1 
ATOM   15100 C CD  . GLU D 1 339 ? -16.967 10.806  69.695  1.00 89.89  ? 339 GLU D CD  1 
ATOM   15101 O OE1 . GLU D 1 339 ? -16.631 10.049  68.763  1.00 83.72  ? 339 GLU D OE1 1 
ATOM   15102 O OE2 . GLU D 1 339 ? -16.519 10.711  70.857  1.00 90.79  ? 339 GLU D OE2 1 
ATOM   15103 N N   . SER D 1 340 ? -20.659 13.051  71.509  1.00 84.58  ? 340 SER D N   1 
ATOM   15104 C CA  . SER D 1 340 ? -20.994 12.826  72.908  1.00 86.26  ? 340 SER D CA  1 
ATOM   15105 C C   . SER D 1 340 ? -22.432 13.190  73.246  1.00 82.51  ? 340 SER D C   1 
ATOM   15106 O O   . SER D 1 340 ? -22.871 12.931  74.373  1.00 74.02  ? 340 SER D O   1 
ATOM   15107 C CB  . SER D 1 340 ? -20.054 13.626  73.817  1.00 89.53  ? 340 SER D CB  1 
ATOM   15108 O OG  . SER D 1 340 ? -18.749 13.697  73.272  1.00 103.99 ? 340 SER D OG  1 
ATOM   15109 N N   . VAL D 1 341 ? -23.172 13.788  72.311  1.00 86.09  ? 341 VAL D N   1 
ATOM   15110 C CA  . VAL D 1 341 ? -24.500 14.316  72.578  1.00 80.73  ? 341 VAL D CA  1 
ATOM   15111 C C   . VAL D 1 341 ? -25.456 13.844  71.489  1.00 76.82  ? 341 VAL D C   1 
ATOM   15112 O O   . VAL D 1 341 ? -25.053 13.507  70.374  1.00 78.45  ? 341 VAL D O   1 
ATOM   15113 C CB  . VAL D 1 341 ? -24.493 15.859  72.678  1.00 72.48  ? 341 VAL D CB  1 
ATOM   15114 C CG1 . VAL D 1 341 ? -23.302 16.348  73.498  1.00 70.60  ? 341 VAL D CG1 1 
ATOM   15115 C CG2 . VAL D 1 341 ? -24.487 16.492  71.300  1.00 78.96  ? 341 VAL D CG2 1 
ATOM   15116 N N   . ASP D 1 342 ? -26.745 13.821  71.831  1.00 87.59  ? 342 ASP D N   1 
ATOM   15117 C CA  . ASP D 1 342 ? -27.798 13.335  70.939  1.00 89.37  ? 342 ASP D CA  1 
ATOM   15118 C C   . ASP D 1 342 ? -28.550 14.474  70.264  1.00 89.84  ? 342 ASP D C   1 
ATOM   15119 O O   . ASP D 1 342 ? -29.761 14.385  70.038  1.00 85.39  ? 342 ASP D O   1 
ATOM   15120 C CB  . ASP D 1 342 ? -28.767 12.434  71.703  1.00 84.30  ? 342 ASP D CB  1 
ATOM   15121 C CG  . ASP D 1 342 ? -29.495 13.164  72.820  1.00 83.48  ? 342 ASP D CG  1 
ATOM   15122 O OD1 . ASP D 1 342 ? -28.836 13.580  73.795  1.00 79.27  ? 342 ASP D OD1 1 
ATOM   15123 O OD2 . ASP D 1 342 ? -30.730 13.322  72.717  1.00 80.24  ? 342 ASP D OD2 1 
ATOM   15124 N N   . PHE D 1 343 ? -27.851 15.557  69.934  1.00 89.66  ? 343 PHE D N   1 
ATOM   15125 C CA  . PHE D 1 343 ? -28.471 16.749  69.370  1.00 83.38  ? 343 PHE D CA  1 
ATOM   15126 C C   . PHE D 1 343 ? -27.397 17.558  68.655  1.00 81.34  ? 343 PHE D C   1 
ATOM   15127 O O   . PHE D 1 343 ? -26.215 17.206  68.668  1.00 79.45  ? 343 PHE D O   1 
ATOM   15128 C CB  . PHE D 1 343 ? -29.175 17.586  70.446  1.00 75.08  ? 343 PHE D CB  1 
ATOM   15129 C CG  . PHE D 1 343 ? -28.351 17.820  71.693  1.00 76.19  ? 343 PHE D CG  1 
ATOM   15130 C CD1 . PHE D 1 343 ? -28.139 16.813  72.626  1.00 72.92  ? 343 PHE D CD1 1 
ATOM   15131 C CD2 . PHE D 1 343 ? -27.849 19.079  71.966  1.00 75.16  ? 343 PHE D CD2 1 
ATOM   15132 C CE1 . PHE D 1 343 ? -27.406 17.054  73.777  1.00 71.02  ? 343 PHE D CE1 1 
ATOM   15133 C CE2 . PHE D 1 343 ? -27.105 19.320  73.105  1.00 69.17  ? 343 PHE D CE2 1 
ATOM   15134 C CZ  . PHE D 1 343 ? -26.885 18.308  74.011  1.00 74.03  ? 343 PHE D CZ  1 
ATOM   15135 N N   . GLN D 1 344 ? -27.819 18.659  68.040  1.00 76.17  ? 344 GLN D N   1 
ATOM   15136 C CA  . GLN D 1 344 ? -26.902 19.521  67.314  1.00 76.68  ? 344 GLN D CA  1 
ATOM   15137 C C   . GLN D 1 344 ? -26.264 20.510  68.278  1.00 84.65  ? 344 GLN D C   1 
ATOM   15138 O O   . GLN D 1 344 ? -26.983 21.316  68.887  1.00 81.74  ? 344 GLN D O   1 
ATOM   15139 C CB  . GLN D 1 344 ? -27.637 20.260  66.215  1.00 81.83  ? 344 GLN D CB  1 
ATOM   15140 C CG  . GLN D 1 344 ? -28.096 19.319  65.137  1.00 82.49  ? 344 GLN D CG  1 
ATOM   15141 C CD  . GLN D 1 344 ? -28.690 20.005  63.944  1.00 85.50  ? 344 GLN D CD  1 
ATOM   15142 O OE1 . GLN D 1 344 ? -28.469 19.599  62.811  1.00 84.34  ? 344 GLN D OE1 1 
ATOM   15143 N NE2 . GLN D 1 344 ? -29.451 21.063  64.183  1.00 83.24  ? 344 GLN D NE2 1 
ATOM   15144 N N   . PRO D 1 345 ? -24.949 20.496  68.446  1.00 86.04  ? 345 PRO D N   1 
ATOM   15145 C CA  . PRO D 1 345 ? -24.316 21.368  69.435  1.00 73.24  ? 345 PRO D CA  1 
ATOM   15146 C C   . PRO D 1 345 ? -24.119 22.776  68.891  1.00 77.13  ? 345 PRO D C   1 
ATOM   15147 O O   . PRO D 1 345 ? -24.302 23.051  67.705  1.00 86.30  ? 345 PRO D O   1 
ATOM   15148 C CB  . PRO D 1 345 ? -22.973 20.678  69.680  1.00 70.02  ? 345 PRO D CB  1 
ATOM   15149 C CG  . PRO D 1 345 ? -22.640 20.103  68.337  1.00 78.87  ? 345 PRO D CG  1 
ATOM   15150 C CD  . PRO D 1 345 ? -23.958 19.680  67.719  1.00 85.40  ? 345 PRO D CD  1 
ATOM   15151 N N   . VAL D 1 346 ? -23.745 23.676  69.796  1.00 76.45  ? 346 VAL D N   1 
ATOM   15152 C CA  . VAL D 1 346 ? -23.285 25.002  69.408  1.00 66.43  ? 346 VAL D CA  1 
ATOM   15153 C C   . VAL D 1 346 ? -22.057 25.349  70.247  1.00 64.83  ? 346 VAL D C   1 
ATOM   15154 O O   . VAL D 1 346 ? -22.153 25.674  71.437  1.00 63.18  ? 346 VAL D O   1 
ATOM   15155 C CB  . VAL D 1 346 ? -24.417 26.047  69.513  1.00 65.79  ? 346 VAL D CB  1 
ATOM   15156 C CG1 . VAL D 1 346 ? -24.947 26.212  70.942  1.00 64.10  ? 346 VAL D CG1 1 
ATOM   15157 C CG2 . VAL D 1 346 ? -23.963 27.382  68.935  1.00 65.38  ? 346 VAL D CG2 1 
ATOM   15158 N N   . VAL D 1 347 ? -20.880 25.238  69.640  1.00 65.44  ? 347 VAL D N   1 
ATOM   15159 C CA  . VAL D 1 347 ? -19.626 25.464  70.349  1.00 64.23  ? 347 VAL D CA  1 
ATOM   15160 C C   . VAL D 1 347 ? -19.239 26.927  70.183  1.00 68.13  ? 347 VAL D C   1 
ATOM   15161 O O   . VAL D 1 347 ? -18.992 27.390  69.063  1.00 68.89  ? 347 VAL D O   1 
ATOM   15162 C CB  . VAL D 1 347 ? -18.517 24.534  69.836  1.00 67.36  ? 347 VAL D CB  1 
ATOM   15163 C CG1 . VAL D 1 347 ? -17.183 24.901  70.473  1.00 72.11  ? 347 VAL D CG1 1 
ATOM   15164 C CG2 . VAL D 1 347 ? -18.866 23.080  70.107  1.00 68.08  ? 347 VAL D CG2 1 
ATOM   15165 N N   . PHE D 1 348 ? -19.180 27.649  71.297  1.00 68.99  ? 348 PHE D N   1 
ATOM   15166 C CA  . PHE D 1 348 ? -18.814 29.056  71.299  1.00 60.53  ? 348 PHE D CA  1 
ATOM   15167 C C   . PHE D 1 348 ? -17.357 29.212  71.699  1.00 59.96  ? 348 PHE D C   1 
ATOM   15168 O O   . PHE D 1 348 ? -16.920 28.653  72.709  1.00 59.20  ? 348 PHE D O   1 
ATOM   15169 C CB  . PHE D 1 348 ? -19.723 29.841  72.238  1.00 59.06  ? 348 PHE D CB  1 
ATOM   15170 C CG  . PHE D 1 348 ? -20.636 30.763  71.516  1.00 59.44  ? 348 PHE D CG  1 
ATOM   15171 C CD1 . PHE D 1 348 ? -21.851 30.303  71.054  1.00 60.84  ? 348 PHE D CD1 1 
ATOM   15172 C CD2 . PHE D 1 348 ? -20.291 32.085  71.303  1.00 58.97  ? 348 PHE D CD2 1 
ATOM   15173 C CE1 . PHE D 1 348 ? -22.697 31.122  70.363  1.00 60.95  ? 348 PHE D CE1 1 
ATOM   15174 C CE2 . PHE D 1 348 ? -21.147 32.928  70.629  1.00 59.46  ? 348 PHE D CE2 1 
ATOM   15175 C CZ  . PHE D 1 348 ? -22.357 32.445  70.163  1.00 62.20  ? 348 PHE D CZ  1 
ATOM   15176 N N   . VAL D 1 349 ? -16.612 29.969  70.903  1.00 60.45  ? 349 VAL D N   1 
ATOM   15177 C CA  . VAL D 1 349 ? -15.195 30.205  71.133  1.00 60.17  ? 349 VAL D CA  1 
ATOM   15178 C C   . VAL D 1 349 ? -15.022 31.714  71.230  1.00 61.88  ? 349 VAL D C   1 
ATOM   15179 O O   . VAL D 1 349 ? -14.925 32.405  70.208  1.00 60.39  ? 349 VAL D O   1 
ATOM   15180 C CB  . VAL D 1 349 ? -14.320 29.606  70.028  1.00 61.93  ? 349 VAL D CB  1 
ATOM   15181 C CG1 . VAL D 1 349 ? -12.849 29.822  70.345  1.00 61.70  ? 349 VAL D CG1 1 
ATOM   15182 C CG2 . VAL D 1 349 ? -14.625 28.124  69.857  1.00 63.00  ? 349 VAL D CG2 1 
ATOM   15183 N N   . VAL D 1 350 ? -14.993 32.230  72.457  1.00 58.77  ? 350 VAL D N   1 
ATOM   15184 C CA  . VAL D 1 350 ? -14.886 33.660  72.721  1.00 56.83  ? 350 VAL D CA  1 
ATOM   15185 C C   . VAL D 1 350 ? -13.633 33.906  73.549  1.00 56.09  ? 350 VAL D C   1 
ATOM   15186 O O   . VAL D 1 350 ? -13.433 33.261  74.585  1.00 64.54  ? 350 VAL D O   1 
ATOM   15187 C CB  . VAL D 1 350 ? -16.130 34.201  73.450  1.00 55.71  ? 350 VAL D CB  1 
ATOM   15188 C CG1 . VAL D 1 350 ? -16.132 35.722  73.438  1.00 55.22  ? 350 VAL D CG1 1 
ATOM   15189 C CG2 . VAL D 1 350 ? -17.402 33.650  72.823  1.00 59.15  ? 350 VAL D CG2 1 
ATOM   15190 N N   . LEU D 1 351 ? -12.800 34.839  73.099  1.00 56.42  ? 351 LEU D N   1 
ATOM   15191 C CA  . LEU D 1 351 ? -11.577 35.208  73.805  1.00 55.92  ? 351 LEU D CA  1 
ATOM   15192 C C   . LEU D 1 351 ? -11.054 36.505  73.198  1.00 56.35  ? 351 LEU D C   1 
ATOM   15193 O O   . LEU D 1 351 ? -11.597 37.017  72.214  1.00 57.10  ? 351 LEU D O   1 
ATOM   15194 C CB  . LEU D 1 351 ? -10.526 34.097  73.738  1.00 56.69  ? 351 LEU D CB  1 
ATOM   15195 C CG  . LEU D 1 351 ? -9.926  33.812  72.362  1.00 58.44  ? 351 LEU D CG  1 
ATOM   15196 C CD1 . LEU D 1 351 ? -8.449  33.481  72.481  1.00 59.03  ? 351 LEU D CD1 1 
ATOM   15197 C CD2 . LEU D 1 351 ? -10.678 32.675  71.691  1.00 59.36  ? 351 LEU D CD2 1 
ATOM   15198 N N   . ASP D 1 352 ? -9.989  37.029  73.773  1.00 56.00  ? 352 ASP D N   1 
ATOM   15199 C CA  . ASP D 1 352 ? -9.383  38.228  73.263  1.00 56.94  ? 352 ASP D CA  1 
ATOM   15200 C C   . ASP D 1 352 ? -8.508  37.899  72.106  1.00 58.22  ? 352 ASP D C   1 
ATOM   15201 O O   . ASP D 1 352 ? -7.389  37.497  72.262  1.00 58.71  ? 352 ASP D O   1 
ATOM   15202 C CB  . ASP D 1 352 ? -8.530  38.907  74.307  1.00 63.47  ? 352 ASP D CB  1 
ATOM   15203 C CG  . ASP D 1 352 ? -9.258  39.130  75.565  1.00 73.98  ? 352 ASP D CG  1 
ATOM   15204 O OD1 . ASP D 1 352 ? -10.149 38.335  75.852  1.00 70.52  ? 352 ASP D OD1 1 
ATOM   15205 O OD2 . ASP D 1 352 ? -8.942  40.091  76.268  1.00 80.67  ? 352 ASP D OD2 1 
ATOM   15206 N N   . GLY D 1 353 ? -9.045  38.109  70.932  1.00 59.25  ? 353 GLY D N   1 
ATOM   15207 C CA  . GLY D 1 353 ? -8.318  37.824  69.712  1.00 61.05  ? 353 GLY D CA  1 
ATOM   15208 C C   . GLY D 1 353 ? -7.406  38.936  69.231  1.00 61.90  ? 353 GLY D C   1 
ATOM   15209 O O   . GLY D 1 353 ? -7.422  39.276  68.041  1.00 65.76  ? 353 GLY D O   1 
ATOM   15210 N N   . GLU D 1 354 ? -6.621  39.523  70.142  1.00 61.16  ? 354 GLU D N   1 
ATOM   15211 C CA  . GLU D 1 354 ? -5.621  40.515  69.760  1.00 62.11  ? 354 GLU D CA  1 
ATOM   15212 C C   . GLU D 1 354 ? -4.278  40.358  70.453  1.00 62.13  ? 354 GLU D C   1 
ATOM   15213 O O   . GLU D 1 354 ? -3.260  40.752  69.873  1.00 63.48  ? 354 GLU D O   1 
ATOM   15214 C CB  . GLU D 1 354 ? -6.156  41.922  70.042  1.00 71.09  ? 354 GLU D CB  1 
ATOM   15215 C CG  . GLU D 1 354 ? -6.804  42.087  71.407  1.00 75.32  ? 354 GLU D CG  1 
ATOM   15216 C CD  . GLU D 1 354 ? -6.002  43.005  72.317  1.00 77.04  ? 354 GLU D CD  1 
ATOM   15217 O OE1 . GLU D 1 354 ? -4.877  43.399  71.932  1.00 85.77  ? 354 GLU D OE1 1 
ATOM   15218 O OE2 . GLU D 1 354 ? -6.516  43.374  73.394  1.00 75.46  ? 354 GLU D OE2 1 
ATOM   15219 N N   . ASN D 1 355 ? -4.216  39.772  71.645  1.00 60.86  ? 355 ASN D N   1 
ATOM   15220 C CA  . ASN D 1 355 ? -3.040  39.897  72.490  1.00 60.74  ? 355 ASN D CA  1 
ATOM   15221 C C   . ASN D 1 355 ? -2.285  38.593  72.660  1.00 64.62  ? 355 ASN D C   1 
ATOM   15222 O O   . ASN D 1 355 ? -1.276  38.558  73.373  1.00 73.24  ? 355 ASN D O   1 
ATOM   15223 C CB  . ASN D 1 355 ? -3.462  40.461  73.845  1.00 59.04  ? 355 ASN D CB  1 
ATOM   15224 C CG  . ASN D 1 355 ? -4.786  39.897  74.315  1.00 71.24  ? 355 ASN D CG  1 
ATOM   15225 O OD1 . ASN D 1 355 ? -5.845  40.487  74.094  1.00 75.55  ? 355 ASN D OD1 1 
ATOM   15226 N ND2 . ASN D 1 355 ? -4.732  38.740  74.965  1.00 75.15  ? 355 ASN D ND2 1 
ATOM   15227 N N   . CYS D 1 356 ? -2.743  37.529  72.012  1.00 61.72  ? 356 CYS D N   1 
ATOM   15228 C CA  . CYS D 1 356 ? -2.081  36.242  72.083  1.00 62.36  ? 356 CYS D CA  1 
ATOM   15229 C C   . CYS D 1 356 ? -1.207  35.946  70.873  1.00 70.63  ? 356 CYS D C   1 
ATOM   15230 O O   . CYS D 1 356 ? -0.282  35.139  70.989  1.00 83.47  ? 356 CYS D O   1 
ATOM   15231 C CB  . CYS D 1 356 ? -3.124  35.132  72.241  1.00 61.73  ? 356 CYS D CB  1 
ATOM   15232 S SG  . CYS D 1 356 ? -4.359  35.059  70.926  1.00 71.90  ? 356 CYS D SG  1 
ATOM   15233 N N   . TRP D 1 357 ? -1.466  36.577  69.725  1.00 67.31  ? 357 TRP D N   1 
ATOM   15234 C CA  . TRP D 1 357 ? -0.740  36.261  68.496  1.00 67.55  ? 357 TRP D CA  1 
ATOM   15235 C C   . TRP D 1 357 ? 0.698   36.756  68.499  1.00 68.62  ? 357 TRP D C   1 
ATOM   15236 O O   . TRP D 1 357 ? 1.463   36.378  67.608  1.00 70.49  ? 357 TRP D O   1 
ATOM   15237 C CB  . TRP D 1 357 ? -1.484  36.847  67.302  1.00 68.37  ? 357 TRP D CB  1 
ATOM   15238 C CG  . TRP D 1 357 ? -2.928  36.628  67.437  1.00 67.20  ? 357 TRP D CG  1 
ATOM   15239 C CD1 . TRP D 1 357 ? -3.864  37.563  67.738  1.00 66.00  ? 357 TRP D CD1 1 
ATOM   15240 C CD2 . TRP D 1 357 ? -3.623  35.386  67.301  1.00 67.21  ? 357 TRP D CD2 1 
ATOM   15241 N NE1 . TRP D 1 357 ? -5.107  36.983  67.806  1.00 65.25  ? 357 TRP D NE1 1 
ATOM   15242 C CE2 . TRP D 1 357 ? -4.985  35.646  67.533  1.00 65.99  ? 357 TRP D CE2 1 
ATOM   15243 C CE3 . TRP D 1 357 ? -3.228  34.079  67.003  1.00 68.26  ? 357 TRP D CE3 1 
ATOM   15244 C CZ2 . TRP D 1 357 ? -5.955  34.648  67.474  1.00 66.65  ? 357 TRP D CZ2 1 
ATOM   15245 C CZ3 . TRP D 1 357 ? -4.198  33.090  66.943  1.00 70.66  ? 357 TRP D CZ3 1 
ATOM   15246 C CH2 . TRP D 1 357 ? -5.541  33.383  67.175  1.00 69.67  ? 357 TRP D CH2 1 
ATOM   15247 N N   . GLU D 1 358 ? 1.084   37.591  69.458  1.00 67.81  ? 358 GLU D N   1 
ATOM   15248 C CA  . GLU D 1 358 ? 2.480   37.982  69.566  1.00 68.73  ? 358 GLU D CA  1 
ATOM   15249 C C   . GLU D 1 358 ? 3.330   36.909  70.230  1.00 68.93  ? 358 GLU D C   1 
ATOM   15250 O O   . GLU D 1 358 ? 4.553   37.066  70.304  1.00 71.53  ? 358 GLU D O   1 
ATOM   15251 C CB  . GLU D 1 358 ? 2.611   39.304  70.329  1.00 73.45  ? 358 GLU D CB  1 
ATOM   15252 C CG  . GLU D 1 358 ? 1.895   39.340  71.663  1.00 69.82  ? 358 GLU D CG  1 
ATOM   15253 C CD  . GLU D 1 358 ? 0.844   40.430  71.719  1.00 67.21  ? 358 GLU D CD  1 
ATOM   15254 O OE1 . GLU D 1 358 ? -0.168  40.319  70.996  1.00 71.25  ? 358 GLU D OE1 1 
ATOM   15255 O OE2 . GLU D 1 358 ? 1.032   41.401  72.482  1.00 66.95  ? 358 GLU D OE2 1 
ATOM   15256 N N   . TYR D 1 359 ? 2.713   35.831  70.712  1.00 68.00  ? 359 TYR D N   1 
ATOM   15257 C CA  . TYR D 1 359 ? 3.429   34.679  71.239  1.00 68.38  ? 359 TYR D CA  1 
ATOM   15258 C C   . TYR D 1 359 ? 3.381   33.486  70.295  1.00 73.95  ? 359 TYR D C   1 
ATOM   15259 O O   . TYR D 1 359 ? 4.003   32.457  70.582  1.00 70.42  ? 359 TYR D O   1 
ATOM   15260 C CB  . TYR D 1 359 ? 2.867   34.296  72.613  1.00 66.47  ? 359 TYR D CB  1 
ATOM   15261 C CG  . TYR D 1 359 ? 2.953   35.415  73.631  1.00 65.21  ? 359 TYR D CG  1 
ATOM   15262 C CD1 . TYR D 1 359 ? 1.973   36.398  73.699  1.00 64.01  ? 359 TYR D CD1 1 
ATOM   15263 C CD2 . TYR D 1 359 ? 4.019   35.495  74.517  1.00 65.38  ? 359 TYR D CD2 1 
ATOM   15264 C CE1 . TYR D 1 359 ? 2.051   37.425  74.622  1.00 66.20  ? 359 TYR D CE1 1 
ATOM   15265 C CE2 . TYR D 1 359 ? 4.105   36.517  75.444  1.00 64.39  ? 359 TYR D CE2 1 
ATOM   15266 C CZ  . TYR D 1 359 ? 3.119   37.479  75.492  1.00 64.35  ? 359 TYR D CZ  1 
ATOM   15267 O OH  . TYR D 1 359 ? 3.200   38.499  76.413  1.00 67.72  ? 359 TYR D OH  1 
ATOM   15268 N N   . TYR D 1 360 ? 2.660   33.597  69.181  1.00 81.02  ? 360 TYR D N   1 
ATOM   15269 C CA  . TYR D 1 360 ? 2.661   32.601  68.121  1.00 72.04  ? 360 TYR D CA  1 
ATOM   15270 C C   . TYR D 1 360 ? 3.818   32.860  67.159  1.00 74.28  ? 360 TYR D C   1 
ATOM   15271 O O   . TYR D 1 360 ? 4.422   33.934  67.147  1.00 80.45  ? 360 TYR D O   1 
ATOM   15272 C CB  . TYR D 1 360 ? 1.344   32.625  67.343  1.00 72.21  ? 360 TYR D CB  1 
ATOM   15273 C CG  . TYR D 1 360 ? 0.150   32.000  68.032  1.00 71.91  ? 360 TYR D CG  1 
ATOM   15274 C CD1 . TYR D 1 360 ? 0.007   32.040  69.413  1.00 71.39  ? 360 TYR D CD1 1 
ATOM   15275 C CD2 . TYR D 1 360 ? -0.838  31.368  67.291  1.00 70.68  ? 360 TYR D CD2 1 
ATOM   15276 C CE1 . TYR D 1 360 ? -1.089  31.468  70.032  1.00 67.01  ? 360 TYR D CE1 1 
ATOM   15277 C CE2 . TYR D 1 360 ? -1.931  30.794  67.899  1.00 69.33  ? 360 TYR D CE2 1 
ATOM   15278 C CZ  . TYR D 1 360 ? -2.053  30.847  69.268  1.00 67.50  ? 360 TYR D CZ  1 
ATOM   15279 O OH  . TYR D 1 360 ? -3.146  30.272  69.867  1.00 66.31  ? 360 TYR D OH  1 
ATOM   15280 N N   . GLU D 1 361 ? 4.109   31.866  66.325  1.00 80.51  ? 361 GLU D N   1 
ATOM   15281 C CA  . GLU D 1 361 ? 5.142   32.012  65.307  1.00 87.46  ? 361 GLU D CA  1 
ATOM   15282 C C   . GLU D 1 361 ? 4.594   32.824  64.138  1.00 88.20  ? 361 GLU D C   1 
ATOM   15283 O O   . GLU D 1 361 ? 3.585   32.447  63.530  1.00 83.68  ? 361 GLU D O   1 
ATOM   15284 C CB  . GLU D 1 361 ? 5.634   30.644  64.838  1.00 97.25  ? 361 GLU D CB  1 
ATOM   15285 C CG  . GLU D 1 361 ? 6.365   29.840  65.907  1.00 102.46 ? 361 GLU D CG  1 
ATOM   15286 C CD  . GLU D 1 361 ? 7.790   30.318  66.145  1.00 118.74 ? 361 GLU D CD  1 
ATOM   15287 O OE1 . GLU D 1 361 ? 8.214   31.300  65.500  1.00 121.75 ? 361 GLU D OE1 1 
ATOM   15288 O OE2 . GLU D 1 361 ? 8.487   29.706  66.983  1.00 127.66 ? 361 GLU D OE2 1 
ATOM   15289 N N   . GLU D 1 362 ? 5.261   33.940  63.835  1.00 90.98  ? 362 GLU D N   1 
ATOM   15290 C CA  . GLU D 1 362 ? 4.882   34.846  62.745  1.00 89.04  ? 362 GLU D CA  1 
ATOM   15291 C C   . GLU D 1 362 ? 3.417   35.285  62.856  1.00 79.21  ? 362 GLU D C   1 
ATOM   15292 O O   . GLU D 1 362 ? 2.715   35.490  61.864  1.00 80.02  ? 362 GLU D O   1 
ATOM   15293 C CB  . GLU D 1 362 ? 5.237   34.231  61.377  1.00 83.62  ? 362 GLU D CB  1 
ATOM   15294 C CG  . GLU D 1 362 ? 4.177   33.462  60.601  1.00 84.04  ? 362 GLU D CG  1 
ATOM   15295 C CD  . GLU D 1 362 ? 4.496   33.363  59.119  1.00 92.52  ? 362 GLU D CD  1 
ATOM   15296 O OE1 . GLU D 1 362 ? 5.495   32.706  58.757  1.00 99.43  ? 362 GLU D OE1 1 
ATOM   15297 O OE2 . GLU D 1 362 ? 3.757   33.968  58.317  1.00 100.47 ? 362 GLU D OE2 1 
ATOM   15298 N N   . ASN D 1 363 ? 2.973   35.496  64.095  1.00 76.89  ? 363 ASN D N   1 
ATOM   15299 C CA  . ASN D 1 363 ? 1.665   36.088  64.387  1.00 75.13  ? 363 ASN D CA  1 
ATOM   15300 C C   . ASN D 1 363 ? 0.521   35.143  64.022  1.00 78.47  ? 363 ASN D C   1 
ATOM   15301 O O   . ASN D 1 363 ? -0.528  35.564  63.534  1.00 86.24  ? 363 ASN D O   1 
ATOM   15302 C CB  . ASN D 1 363 ? 1.514   37.453  63.706  1.00 81.96  ? 363 ASN D CB  1 
ATOM   15303 C CG  . ASN D 1 363 ? 0.291   38.216  64.169  1.00 86.87  ? 363 ASN D CG  1 
ATOM   15304 O OD1 . ASN D 1 363 ? -0.770  38.165  63.547  1.00 86.09  ? 363 ASN D OD1 1 
ATOM   15305 N ND2 . ASN D 1 363 ? 0.412   38.857  65.308  1.00 77.05  ? 363 ASN D ND2 1 
ATOM   15306 N N   . GLY D 1 364 ? 0.725   33.851  64.260  1.00 77.97  ? 364 GLY D N   1 
ATOM   15307 C CA  . GLY D 1 364 ? -0.372  32.913  64.157  1.00 78.07  ? 364 GLY D CA  1 
ATOM   15308 C C   . GLY D 1 364 ? -0.972  32.784  62.772  1.00 78.10  ? 364 GLY D C   1 
ATOM   15309 O O   . GLY D 1 364 ? -2.057  32.222  62.607  1.00 76.06  ? 364 GLY D O   1 
ATOM   15310 N N   . ILE D 1 365 ? -0.280  33.313  61.763  1.00 84.26  ? 365 ILE D N   1 
ATOM   15311 C CA  . ILE D 1 365 ? -0.750  33.169  60.383  1.00 82.91  ? 365 ILE D CA  1 
ATOM   15312 C C   . ILE D 1 365 ? -0.831  31.703  59.965  1.00 82.35  ? 365 ILE D C   1 
ATOM   15313 O O   . ILE D 1 365 ? -1.872  31.293  59.426  1.00 81.73  ? 365 ILE D O   1 
ATOM   15314 C CB  . ILE D 1 365 ? 0.118   34.001  59.432  1.00 84.13  ? 365 ILE D CB  1 
ATOM   15315 C CG1 . ILE D 1 365 ? 0.050   35.485  59.793  1.00 81.04  ? 365 ILE D CG1 1 
ATOM   15316 C CG2 . ILE D 1 365 ? -0.313  33.777  57.985  1.00 85.49  ? 365 ILE D CG2 1 
ATOM   15317 C CD1 . ILE D 1 365 ? -1.170  36.187  59.278  1.00 80.78  ? 365 ILE D CD1 1 
ATOM   15318 N N   . PRO D 1 366 ? 0.198   30.872  60.168  1.00 82.25  ? 366 PRO D N   1 
ATOM   15319 C CA  . PRO D 1 366 ? 0.034   29.455  59.799  1.00 83.46  ? 366 PRO D CA  1 
ATOM   15320 C C   . PRO D 1 366 ? -1.078  28.715  60.545  1.00 81.80  ? 366 PRO D C   1 
ATOM   15321 O O   . PRO D 1 366 ? -1.765  27.903  59.915  1.00 82.84  ? 366 PRO D O   1 
ATOM   15322 C CB  . PRO D 1 366 ? 1.432   28.869  60.056  1.00 84.50  ? 366 PRO D CB  1 
ATOM   15323 C CG  . PRO D 1 366 ? 2.120   29.848  60.930  1.00 83.14  ? 366 PRO D CG  1 
ATOM   15324 C CD  . PRO D 1 366 ? 1.599   31.173  60.510  1.00 82.71  ? 366 PRO D CD  1 
ATOM   15325 N N   . PHE D 1 367 ? -1.289  28.953  61.847  1.00 80.47  ? 367 PHE D N   1 
ATOM   15326 C CA  . PHE D 1 367 ? -2.395  28.299  62.549  1.00 81.31  ? 367 PHE D CA  1 
ATOM   15327 C C   . PHE D 1 367 ? -3.749  28.775  62.031  1.00 84.51  ? 367 PHE D C   1 
ATOM   15328 O O   . PHE D 1 367 ? -4.635  27.963  61.742  1.00 91.27  ? 367 PHE D O   1 
ATOM   15329 C CB  . PHE D 1 367 ? -2.288  28.560  64.049  1.00 75.58  ? 367 PHE D CB  1 
ATOM   15330 C CG  . PHE D 1 367 ? -3.499  28.142  64.831  1.00 80.25  ? 367 PHE D CG  1 
ATOM   15331 C CD1 . PHE D 1 367 ? -3.737  26.807  65.094  1.00 82.11  ? 367 PHE D CD1 1 
ATOM   15332 C CD2 . PHE D 1 367 ? -4.387  29.086  65.325  1.00 87.93  ? 367 PHE D CD2 1 
ATOM   15333 C CE1 . PHE D 1 367 ? -4.831  26.418  65.826  1.00 77.53  ? 367 PHE D CE1 1 
ATOM   15334 C CE2 . PHE D 1 367 ? -5.488  28.703  66.056  1.00 78.73  ? 367 PHE D CE2 1 
ATOM   15335 C CZ  . PHE D 1 367 ? -5.710  27.366  66.307  1.00 71.04  ? 367 PHE D CZ  1 
ATOM   15336 N N   . LEU D 1 368 ? -3.944  30.094  61.952  1.00 81.90  ? 368 LEU D N   1 
ATOM   15337 C CA  . LEU D 1 368 ? -5.248  30.628  61.571  1.00 76.82  ? 368 LEU D CA  1 
ATOM   15338 C C   . LEU D 1 368 ? -5.590  30.305  60.121  1.00 78.82  ? 368 LEU D C   1 
ATOM   15339 O O   . LEU D 1 368 ? -6.772  30.184  59.776  1.00 78.79  ? 368 LEU D O   1 
ATOM   15340 C CB  . LEU D 1 368 ? -5.283  32.137  61.805  1.00 78.89  ? 368 LEU D CB  1 
ATOM   15341 C CG  . LEU D 1 368 ? -5.743  32.629  63.178  1.00 78.65  ? 368 LEU D CG  1 
ATOM   15342 C CD1 . LEU D 1 368 ? -5.068  33.947  63.526  1.00 72.20  ? 368 LEU D CD1 1 
ATOM   15343 C CD2 . LEU D 1 368 ? -7.256  32.768  63.213  1.00 78.75  ? 368 LEU D CD2 1 
ATOM   15344 N N   . GLU D 1 369 ? -4.582  30.167  59.259  1.00 83.91  ? 369 GLU D N   1 
ATOM   15345 C CA  . GLU D 1 369 ? -4.851  29.776  57.880  1.00 84.79  ? 369 GLU D CA  1 
ATOM   15346 C C   . GLU D 1 369 ? -5.219  28.301  57.779  1.00 84.13  ? 369 GLU D C   1 
ATOM   15347 O O   . GLU D 1 369 ? -6.186  27.947  57.095  1.00 85.08  ? 369 GLU D O   1 
ATOM   15348 C CB  . GLU D 1 369 ? -3.642  30.089  56.997  1.00 95.09  ? 369 GLU D CB  1 
ATOM   15349 C CG  . GLU D 1 369 ? -3.565  31.544  56.562  1.00 85.53  ? 369 GLU D CG  1 
ATOM   15350 C CD  . GLU D 1 369 ? -2.959  31.715  55.184  1.00 100.05 ? 369 GLU D CD  1 
ATOM   15351 O OE1 . GLU D 1 369 ? -3.714  31.665  54.190  1.00 124.34 ? 369 GLU D OE1 1 
ATOM   15352 O OE2 . GLU D 1 369 ? -1.727  31.904  55.095  1.00 111.06 ? 369 GLU D OE2 1 
ATOM   15353 N N   . LYS D 1 370 ? -4.464  27.428  58.454  1.00 83.92  ? 370 LYS D N   1 
ATOM   15354 C CA  . LYS D 1 370 ? -4.796  26.006  58.450  1.00 85.35  ? 370 LYS D CA  1 
ATOM   15355 C C   . LYS D 1 370 ? -6.102  25.738  59.182  1.00 91.16  ? 370 LYS D C   1 
ATOM   15356 O O   . LYS D 1 370 ? -6.891  24.883  58.762  1.00 88.66  ? 370 LYS D O   1 
ATOM   15357 C CB  . LYS D 1 370 ? -3.664  25.186  59.069  1.00 84.92  ? 370 LYS D CB  1 
ATOM   15358 C CG  . LYS D 1 370 ? -3.437  23.843  58.385  1.00 90.65  ? 370 LYS D CG  1 
ATOM   15359 C CD  . LYS D 1 370 ? -3.559  23.954  56.871  1.00 89.85  ? 370 LYS D CD  1 
ATOM   15360 C CE  . LYS D 1 370 ? -3.239  22.631  56.195  1.00 92.42  ? 370 LYS D CE  1 
ATOM   15361 N NZ  . LYS D 1 370 ? -2.764  22.818  54.796  1.00 95.20  ? 370 LYS D NZ  1 
ATOM   15362 N N   . LEU D 1 371 ? -6.347  26.448  60.284  1.00 89.54  ? 371 LEU D N   1 
ATOM   15363 C CA  . LEU D 1 371 ? -7.625  26.300  60.970  1.00 87.64  ? 371 LEU D CA  1 
ATOM   15364 C C   . LEU D 1 371 ? -8.772  26.653  60.032  1.00 89.17  ? 371 LEU D C   1 
ATOM   15365 O O   . LEU D 1 371 ? -9.571  25.787  59.654  1.00 93.68  ? 371 LEU D O   1 
ATOM   15366 C CB  . LEU D 1 371 ? -7.651  27.167  62.237  1.00 79.23  ? 371 LEU D CB  1 
ATOM   15367 C CG  . LEU D 1 371 ? -8.985  27.380  62.952  1.00 74.42  ? 371 LEU D CG  1 
ATOM   15368 C CD1 . LEU D 1 371 ? -9.496  26.069  63.507  1.00 74.31  ? 371 LEU D CD1 1 
ATOM   15369 C CD2 . LEU D 1 371 ? -8.837  28.398  64.072  1.00 72.13  ? 371 LEU D CD2 1 
ATOM   15370 N N   . TYR D 1 372 ? -8.804  27.907  59.569  1.00 88.40  ? 372 TYR D N   1 
ATOM   15371 C CA  . TYR D 1 372 ? -9.926  28.394  58.770  1.00 87.11  ? 372 TYR D CA  1 
ATOM   15372 C C   . TYR D 1 372 ? -10.146 27.559  57.517  1.00 89.95  ? 372 TYR D C   1 
ATOM   15373 O O   . TYR D 1 372 ? -11.288 27.414  57.066  1.00 93.33  ? 372 TYR D O   1 
ATOM   15374 C CB  . TYR D 1 372 ? -9.702  29.861  58.385  1.00 87.49  ? 372 TYR D CB  1 
ATOM   15375 C CG  . TYR D 1 372 ? -9.941  30.846  59.509  1.00 78.53  ? 372 TYR D CG  1 
ATOM   15376 C CD1 . TYR D 1 372 ? -10.109 30.417  60.818  1.00 75.57  ? 372 TYR D CD1 1 
ATOM   15377 C CD2 . TYR D 1 372 ? -10.005 32.209  59.254  1.00 77.34  ? 372 TYR D CD2 1 
ATOM   15378 C CE1 . TYR D 1 372 ? -10.327 31.318  61.843  1.00 73.39  ? 372 TYR D CE1 1 
ATOM   15379 C CE2 . TYR D 1 372 ? -10.223 33.115  60.272  1.00 75.16  ? 372 TYR D CE2 1 
ATOM   15380 C CZ  . TYR D 1 372 ? -10.385 32.665  61.566  1.00 73.18  ? 372 TYR D CZ  1 
ATOM   15381 O OH  . TYR D 1 372 ? -10.604 33.565  62.584  1.00 71.14  ? 372 TYR D OH  1 
ATOM   15382 N N   . SER D 1 373 ? -9.080  27.002  56.941  1.00 84.75  ? 373 SER D N   1 
ATOM   15383 C CA  . SER D 1 373 ? -9.248  26.179  55.748  1.00 91.99  ? 373 SER D CA  1 
ATOM   15384 C C   . SER D 1 373 ? -9.888  24.839  56.085  1.00 89.14  ? 373 SER D C   1 
ATOM   15385 O O   . SER D 1 373 ? -10.661 24.296  55.285  1.00 89.59  ? 373 SER D O   1 
ATOM   15386 C CB  . SER D 1 373 ? -7.899  25.965  55.055  1.00 104.02 ? 373 SER D CB  1 
ATOM   15387 O OG  . SER D 1 373 ? -7.047  25.137  55.829  1.00 100.50 ? 373 SER D OG  1 
ATOM   15388 N N   . THR D 1 374 ? -9.568  24.285  57.257  1.00 86.08  ? 374 THR D N   1 
ATOM   15389 C CA  . THR D 1 374 ? -10.144 23.004  57.646  1.00 86.29  ? 374 THR D CA  1 
ATOM   15390 C C   . THR D 1 374 ? -11.648 23.095  57.860  1.00 97.97  ? 374 THR D C   1 
ATOM   15391 O O   . THR D 1 374 ? -12.354 22.106  57.643  1.00 102.26 ? 374 THR D O   1 
ATOM   15392 C CB  . THR D 1 374 ? -9.459  22.480  58.909  1.00 90.18  ? 374 THR D CB  1 
ATOM   15393 O OG1 . THR D 1 374 ? -8.081  22.872  58.905  1.00 90.57  ? 374 THR D OG1 1 
ATOM   15394 C CG2 . THR D 1 374 ? -9.550  20.963  58.973  1.00 86.04  ? 374 THR D CG2 1 
ATOM   15395 N N   . LEU D 1 375 ? -12.160 24.252  58.291  1.00 96.01  ? 375 LEU D N   1 
ATOM   15396 C CA  . LEU D 1 375 ? -13.605 24.389  58.446  1.00 82.89  ? 375 LEU D CA  1 
ATOM   15397 C C   . LEU D 1 375 ? -14.332 24.349  57.111  1.00 88.09  ? 375 LEU D C   1 
ATOM   15398 O O   . LEU D 1 375 ? -15.539 24.084  57.088  1.00 85.39  ? 375 LEU D O   1 
ATOM   15399 C CB  . LEU D 1 375 ? -13.973 25.686  59.177  1.00 80.52  ? 375 LEU D CB  1 
ATOM   15400 C CG  . LEU D 1 375 ? -13.584 25.898  60.647  1.00 77.93  ? 375 LEU D CG  1 
ATOM   15401 C CD1 . LEU D 1 375 ? -13.673 24.587  61.423  1.00 83.33  ? 375 LEU D CD1 1 
ATOM   15402 C CD2 . LEU D 1 375 ? -12.233 26.590  60.847  1.00 77.35  ? 375 LEU D CD2 1 
ATOM   15403 N N   . GLU D 1 376 ? -13.637 24.623  56.002  1.00 95.78  ? 376 GLU D N   1 
ATOM   15404 C CA  . GLU D 1 376 ? -14.282 24.572  54.691  1.00 91.33  ? 376 GLU D CA  1 
ATOM   15405 C C   . GLU D 1 376 ? -14.436 23.140  54.188  1.00 91.82  ? 376 GLU D C   1 
ATOM   15406 O O   . GLU D 1 376 ? -15.435 22.810  53.539  1.00 100.90 ? 376 GLU D O   1 
ATOM   15407 C CB  . GLU D 1 376 ? -13.492 25.410  53.685  1.00 98.66  ? 376 GLU D CB  1 
ATOM   15408 C CG  . GLU D 1 376 ? -13.245 26.844  54.128  1.00 100.76 ? 376 GLU D CG  1 
ATOM   15409 C CD  . GLU D 1 376 ? -12.681 27.707  53.018  1.00 90.80  ? 376 GLU D CD  1 
ATOM   15410 O OE1 . GLU D 1 376 ? -11.769 27.238  52.304  1.00 92.78  ? 376 GLU D OE1 1 
ATOM   15411 O OE2 . GLU D 1 376 ? -13.152 28.851  52.854  1.00 90.30  ? 376 GLU D OE2 1 
ATOM   15412 N N   . LYS D 1 377 ? -13.460 22.277  54.476  1.00 92.17  ? 377 LYS D N   1 
ATOM   15413 C CA  . LYS D 1 377 ? -13.537 20.899  54.003  1.00 106.43 ? 377 LYS D CA  1 
ATOM   15414 C C   . LYS D 1 377 ? -14.511 20.065  54.825  1.00 107.49 ? 377 LYS D C   1 
ATOM   15415 O O   . LYS D 1 377 ? -15.166 19.172  54.279  1.00 118.02 ? 377 LYS D O   1 
ATOM   15416 C CB  . LYS D 1 377 ? -12.147 20.255  54.008  1.00 112.73 ? 377 LYS D CB  1 
ATOM   15417 C CG  . LYS D 1 377 ? -11.487 20.168  55.377  1.00 103.27 ? 377 LYS D CG  1 
ATOM   15418 C CD  . LYS D 1 377 ? -10.000 19.866  55.265  1.00 93.78  ? 377 LYS D CD  1 
ATOM   15419 C CE  . LYS D 1 377 ? -9.290  20.893  54.398  1.00 94.64  ? 377 LYS D CE  1 
ATOM   15420 N NZ  . LYS D 1 377 ? -7.822  20.913  54.649  1.00 94.66  ? 377 LYS D NZ  1 
ATOM   15421 N N   . GLU D 1 378 ? -14.629 20.340  56.122  1.00 90.85  ? 378 GLU D N   1 
ATOM   15422 C CA  . GLU D 1 378 ? -15.526 19.586  56.992  1.00 89.89  ? 378 GLU D CA  1 
ATOM   15423 C C   . GLU D 1 378 ? -16.947 20.101  56.800  1.00 93.03  ? 378 GLU D C   1 
ATOM   15424 O O   . GLU D 1 378 ? -17.257 21.242  57.156  1.00 87.87  ? 378 GLU D O   1 
ATOM   15425 C CB  . GLU D 1 378 ? -15.092 19.705  58.450  1.00 91.00  ? 378 GLU D CB  1 
ATOM   15426 C CG  . GLU D 1 378 ? -13.617 19.429  58.677  1.00 91.64  ? 378 GLU D CG  1 
ATOM   15427 C CD  . GLU D 1 378 ? -13.368 18.112  59.381  1.00 93.42  ? 378 GLU D CD  1 
ATOM   15428 O OE1 . GLU D 1 378 ? -14.221 17.206  59.273  1.00 104.63 ? 378 GLU D OE1 1 
ATOM   15429 O OE2 . GLU D 1 378 ? -12.316 17.981  60.040  1.00 94.34  ? 378 GLU D OE2 1 
ATOM   15430 N N   . GLU D 1 379 ? -17.812 19.258  56.234  1.00 100.67 ? 379 GLU D N   1 
ATOM   15431 C CA  . GLU D 1 379 ? -19.193 19.648  55.989  1.00 103.11 ? 379 GLU D CA  1 
ATOM   15432 C C   . GLU D 1 379 ? -20.059 19.568  57.240  1.00 106.76 ? 379 GLU D C   1 
ATOM   15433 O O   . GLU D 1 379 ? -21.116 20.206  57.283  1.00 107.67 ? 379 GLU D O   1 
ATOM   15434 C CB  . GLU D 1 379 ? -19.789 18.784  54.874  1.00 107.81 ? 379 GLU D CB  1 
ATOM   15435 C CG  . GLU D 1 379 ? -20.216 17.394  55.308  1.00 111.71 ? 379 GLU D CG  1 
ATOM   15436 C CD  . GLU D 1 379 ? -19.048 16.465  55.577  1.00 109.30 ? 379 GLU D CD  1 
ATOM   15437 O OE1 . GLU D 1 379 ? -18.007 16.595  54.899  1.00 106.85 ? 379 GLU D OE1 1 
ATOM   15438 O OE2 . GLU D 1 379 ? -19.170 15.609  56.477  1.00 99.54  ? 379 GLU D OE2 1 
ATOM   15439 N N   . TRP D 1 380 ? -19.640 18.806  58.254  1.00 98.38  ? 380 TRP D N   1 
ATOM   15440 C CA  . TRP D 1 380 ? -20.384 18.788  59.509  1.00 86.81  ? 380 TRP D CA  1 
ATOM   15441 C C   . TRP D 1 380 ? -20.158 20.063  60.308  1.00 86.74  ? 380 TRP D C   1 
ATOM   15442 O O   . TRP D 1 380 ? -21.062 20.518  61.017  1.00 82.29  ? 380 TRP D O   1 
ATOM   15443 C CB  . TRP D 1 380 ? -20.004 17.563  60.346  1.00 90.78  ? 380 TRP D CB  1 
ATOM   15444 C CG  . TRP D 1 380 ? -18.524 17.359  60.537  1.00 91.33  ? 380 TRP D CG  1 
ATOM   15445 C CD1 . TRP D 1 380 ? -17.619 16.978  59.589  1.00 90.21  ? 380 TRP D CD1 1 
ATOM   15446 C CD2 . TRP D 1 380 ? -17.785 17.511  61.758  1.00 83.98  ? 380 TRP D CD2 1 
ATOM   15447 N NE1 . TRP D 1 380 ? -16.364 16.891  60.141  1.00 98.96  ? 380 TRP D NE1 1 
ATOM   15448 C CE2 . TRP D 1 380 ? -16.438 17.212  61.470  1.00 84.76  ? 380 TRP D CE2 1 
ATOM   15449 C CE3 . TRP D 1 380 ? -18.131 17.873  63.063  1.00 81.51  ? 380 TRP D CE3 1 
ATOM   15450 C CZ2 . TRP D 1 380 ? -15.438 17.264  62.439  1.00 83.17  ? 380 TRP D CZ2 1 
ATOM   15451 C CZ3 . TRP D 1 380 ? -17.136 17.925  64.024  1.00 79.93  ? 380 TRP D CZ3 1 
ATOM   15452 C CH2 . TRP D 1 380 ? -15.806 17.622  63.707  1.00 80.77  ? 380 TRP D CH2 1 
ATOM   15453 N N   . ILE D 1 381 ? -18.969 20.655  60.205  1.00 92.34  ? 381 ILE D N   1 
ATOM   15454 C CA  . ILE D 1 381 ? -18.658 21.889  60.922  1.00 93.08  ? 381 ILE D CA  1 
ATOM   15455 C C   . ILE D 1 381 ? -19.253 23.045  60.123  1.00 89.22  ? 381 ILE D C   1 
ATOM   15456 O O   . ILE D 1 381 ? -18.655 23.520  59.156  1.00 97.57  ? 381 ILE D O   1 
ATOM   15457 C CB  . ILE D 1 381 ? -17.155 22.069  61.137  1.00 80.32  ? 381 ILE D CB  1 
ATOM   15458 C CG1 . ILE D 1 381 ? -16.571 20.872  61.890  1.00 80.09  ? 381 ILE D CG1 1 
ATOM   15459 C CG2 . ILE D 1 381 ? -16.898 23.349  61.903  1.00 77.72  ? 381 ILE D CG2 1 
ATOM   15460 C CD1 . ILE D 1 381 ? -15.069 20.941  62.075  1.00 82.10  ? 381 ILE D CD1 1 
ATOM   15461 N N   . GLU D 1 382 ? -20.437 23.498  60.521  1.00 82.60  ? 382 GLU D N   1 
ATOM   15462 C CA  . GLU D 1 382 ? -21.056 24.683  59.941  1.00 80.34  ? 382 GLU D CA  1 
ATOM   15463 C C   . GLU D 1 382 ? -20.796 25.844  60.894  1.00 77.58  ? 382 GLU D C   1 
ATOM   15464 O O   . GLU D 1 382 ? -21.342 25.881  62.003  1.00 75.84  ? 382 GLU D O   1 
ATOM   15465 C CB  . GLU D 1 382 ? -22.551 24.466  59.704  1.00 91.43  ? 382 GLU D CB  1 
ATOM   15466 C CG  . GLU D 1 382 ? -23.397 25.733  59.772  1.00 93.26  ? 382 GLU D CG  1 
ATOM   15467 C CD  . GLU D 1 382 ? -24.651 25.649  58.926  1.00 109.21 ? 382 GLU D CD  1 
ATOM   15468 O OE1 . GLU D 1 382 ? -25.338 24.608  58.985  1.00 105.34 ? 382 GLU D OE1 1 
ATOM   15469 O OE2 . GLU D 1 382 ? -24.955 26.627  58.211  1.00 110.75 ? 382 GLU D OE2 1 
ATOM   15470 N N   . THR D 1 383 ? -19.928 26.765  60.484  1.00 79.69  ? 383 THR D N   1 
ATOM   15471 C CA  . THR D 1 383 ? -19.668 27.954  61.280  1.00 75.23  ? 383 THR D CA  1 
ATOM   15472 C C   . THR D 1 383 ? -20.788 28.961  61.064  1.00 75.06  ? 383 THR D C   1 
ATOM   15473 O O   . THR D 1 383 ? -21.272 29.143  59.943  1.00 92.45  ? 383 THR D O   1 
ATOM   15474 C CB  . THR D 1 383 ? -18.312 28.574  60.925  1.00 75.30  ? 383 THR D CB  1 
ATOM   15475 O OG1 . THR D 1 383 ? -18.352 29.107  59.595  1.00 81.82  ? 383 THR D OG1 1 
ATOM   15476 C CG2 . THR D 1 383 ? -17.188 27.540  61.029  1.00 75.81  ? 383 THR D CG2 1 
ATOM   15477 N N   . LEU D 1 384 ? -21.204 29.612  62.143  1.00 73.18  ? 384 LEU D N   1 
ATOM   15478 C CA  . LEU D 1 384 ? -22.350 30.505  62.102  1.00 73.18  ? 384 LEU D CA  1 
ATOM   15479 C C   . LEU D 1 384 ? -21.956 31.908  62.532  1.00 71.21  ? 384 LEU D C   1 
ATOM   15480 O O   . LEU D 1 384 ? -20.829 32.176  62.957  1.00 70.23  ? 384 LEU D O   1 
ATOM   15481 C CB  . LEU D 1 384 ? -23.484 30.009  63.005  1.00 71.88  ? 384 LEU D CB  1 
ATOM   15482 C CG  . LEU D 1 384 ? -24.063 28.620  62.767  1.00 73.30  ? 384 LEU D CG  1 
ATOM   15483 C CD1 . LEU D 1 384 ? -24.538 28.070  64.090  1.00 71.79  ? 384 LEU D CD1 1 
ATOM   15484 C CD2 . LEU D 1 384 ? -25.204 28.681  61.770  1.00 75.21  ? 384 LEU D CD2 1 
ATOM   15485 N N   . THR D 1 385 ? -22.927 32.798  62.406  1.00 71.19  ? 385 THR D N   1 
ATOM   15486 C CA  . THR D 1 385 ? -22.881 34.148  62.928  1.00 69.77  ? 385 THR D CA  1 
ATOM   15487 C C   . THR D 1 385 ? -23.916 34.294  64.034  1.00 68.28  ? 385 THR D C   1 
ATOM   15488 O O   . THR D 1 385 ? -24.812 33.459  64.192  1.00 68.66  ? 385 THR D O   1 
ATOM   15489 C CB  . THR D 1 385 ? -23.134 35.153  61.809  1.00 75.41  ? 385 THR D CB  1 
ATOM   15490 O OG1 . THR D 1 385 ? -24.455 34.945  61.293  1.00 76.43  ? 385 THR D OG1 1 
ATOM   15491 C CG2 . THR D 1 385 ? -22.119 34.950  60.703  1.00 72.86  ? 385 THR D CG2 1 
ATOM   15492 N N   . LEU D 1 386 ? -23.780 35.370  64.813  1.00 66.69  ? 386 LEU D N   1 
ATOM   15493 C CA  . LEU D 1 386 ? -24.618 35.524  65.999  1.00 65.17  ? 386 LEU D CA  1 
ATOM   15494 C C   . LEU D 1 386 ? -26.096 35.625  65.645  1.00 75.83  ? 386 LEU D C   1 
ATOM   15495 O O   . LEU D 1 386 ? -26.951 35.288  66.471  1.00 79.04  ? 386 LEU D O   1 
ATOM   15496 C CB  . LEU D 1 386 ? -24.168 36.744  66.801  1.00 66.88  ? 386 LEU D CB  1 
ATOM   15497 C CG  . LEU D 1 386 ? -22.678 36.722  67.152  1.00 62.73  ? 386 LEU D CG  1 
ATOM   15498 C CD1 . LEU D 1 386 ? -22.228 38.042  67.761  1.00 61.52  ? 386 LEU D CD1 1 
ATOM   15499 C CD2 . LEU D 1 386 ? -22.359 35.558  68.082  1.00 61.80  ? 386 LEU D CD2 1 
ATOM   15500 N N   . GLU D 1 387 ? -26.424 36.094  64.438  1.00 87.40  ? 387 GLU D N   1 
ATOM   15501 C CA  . GLU D 1 387 ? -27.814 36.022  63.999  1.00 85.68  ? 387 GLU D CA  1 
ATOM   15502 C C   . GLU D 1 387 ? -28.202 34.605  63.602  1.00 86.80  ? 387 GLU D C   1 
ATOM   15503 O O   . GLU D 1 387 ? -29.294 34.141  63.945  1.00 82.48  ? 387 GLU D O   1 
ATOM   15504 C CB  . GLU D 1 387 ? -28.093 36.993  62.843  1.00 77.03  ? 387 GLU D CB  1 
ATOM   15505 C CG  . GLU D 1 387 ? -27.188 36.923  61.604  1.00 92.44  ? 387 GLU D CG  1 
ATOM   15506 C CD  . GLU D 1 387 ? -25.780 37.427  61.849  1.00 84.33  ? 387 GLU D CD  1 
ATOM   15507 O OE1 . GLU D 1 387 ? -25.471 37.779  62.999  1.00 72.48  ? 387 GLU D OE1 1 
ATOM   15508 O OE2 . GLU D 1 387 ? -24.995 37.504  60.875  1.00 81.79  ? 387 GLU D OE2 1 
ATOM   15509 N N   . GLU D 1 388 ? -27.326 33.897  62.891  1.00 71.81  ? 388 GLU D N   1 
ATOM   15510 C CA  . GLU D 1 388 ? -27.685 32.549  62.466  1.00 72.84  ? 388 GLU D CA  1 
ATOM   15511 C C   . GLU D 1 388 ? -27.760 31.589  63.643  1.00 74.70  ? 388 GLU D C   1 
ATOM   15512 O O   . GLU D 1 388 ? -28.578 30.660  63.640  1.00 73.50  ? 388 GLU D O   1 
ATOM   15513 C CB  . GLU D 1 388 ? -26.699 32.039  61.429  1.00 77.67  ? 388 GLU D CB  1 
ATOM   15514 C CG  . GLU D 1 388 ? -27.025 32.497  60.044  1.00 80.16  ? 388 GLU D CG  1 
ATOM   15515 C CD  . GLU D 1 388 ? -25.807 32.505  59.179  1.00 77.54  ? 388 GLU D CD  1 
ATOM   15516 O OE1 . GLU D 1 388 ? -24.821 31.842  59.571  1.00 80.08  ? 388 GLU D OE1 1 
ATOM   15517 O OE2 . GLU D 1 388 ? -25.825 33.168  58.131  1.00 79.07  ? 388 GLU D OE2 1 
ATOM   15518 N N   . ALA D 1 389 ? -26.911 31.782  64.652  1.00 72.81  ? 389 ALA D N   1 
ATOM   15519 C CA  . ALA D 1 389 ? -27.011 30.963  65.852  1.00 68.56  ? 389 ALA D CA  1 
ATOM   15520 C C   . ALA D 1 389 ? -28.278 31.259  66.642  1.00 72.21  ? 389 ALA D C   1 
ATOM   15521 O O   . ALA D 1 389 ? -28.743 30.394  67.393  1.00 67.30  ? 389 ALA D O   1 
ATOM   15522 C CB  . ALA D 1 389 ? -25.781 31.168  66.737  1.00 66.47  ? 389 ALA D CB  1 
ATOM   15523 N N   . MET D 1 390 ? -28.844 32.456  66.489  1.00 79.36  ? 390 MET D N   1 
ATOM   15524 C CA  . MET D 1 390 ? -30.052 32.842  67.209  1.00 74.37  ? 390 MET D CA  1 
ATOM   15525 C C   . MET D 1 390 ? -31.328 32.407  66.502  1.00 75.27  ? 390 MET D C   1 
ATOM   15526 O O   . MET D 1 390 ? -32.346 32.177  67.164  1.00 68.68  ? 390 MET D O   1 
ATOM   15527 C CB  . MET D 1 390 ? -30.080 34.359  67.413  1.00 72.43  ? 390 MET D CB  1 
ATOM   15528 C CG  . MET D 1 390 ? -29.767 34.801  68.829  1.00 63.76  ? 390 MET D CG  1 
ATOM   15529 S SD  . MET D 1 390 ? -30.779 33.945  70.046  1.00 77.09  ? 390 MET D SD  1 
ATOM   15530 C CE  . MET D 1 390 ? -32.263 34.947  70.016  1.00 63.67  ? 390 MET D CE  1 
ATOM   15531 N N   . ARG D 1 391 ? -31.299 32.293  65.175  1.00 78.12  ? 391 ARG D N   1 
ATOM   15532 C CA  . ARG D 1 391 ? -32.480 31.924  64.409  1.00 84.10  ? 391 ARG D CA  1 
ATOM   15533 C C   . ARG D 1 391 ? -32.570 30.432  64.116  1.00 82.92  ? 391 ARG D C   1 
ATOM   15534 O O   . ARG D 1 391 ? -33.653 29.956  63.755  1.00 87.78  ? 391 ARG D O   1 
ATOM   15535 C CB  . ARG D 1 391 ? -32.529 32.698  63.079  1.00 77.79  ? 391 ARG D CB  1 
ATOM   15536 C CG  . ARG D 1 391 ? -33.048 34.145  63.151  1.00 79.97  ? 391 ARG D CG  1 
ATOM   15537 C CD  . ARG D 1 391 ? -32.184 35.032  64.037  1.00 89.55  ? 391 ARG D CD  1 
ATOM   15538 N NE  . ARG D 1 391 ? -32.644 36.414  64.100  1.00 96.49  ? 391 ARG D NE  1 
ATOM   15539 C CZ  . ARG D 1 391 ? -33.701 36.830  64.784  1.00 82.06  ? 391 ARG D CZ  1 
ATOM   15540 N NH1 . ARG D 1 391 ? -34.449 35.991  65.484  1.00 76.60  ? 391 ARG D NH1 1 
ATOM   15541 N NH2 . ARG D 1 391 ? -34.011 38.123  64.771  1.00 70.89  ? 391 ARG D NH2 1 
ATOM   15542 N N   . LYS D 1 392 ? -31.471 29.689  64.256  1.00 74.88  ? 392 LYS D N   1 
ATOM   15543 C CA  . LYS D 1 392 ? -31.451 28.272  63.899  1.00 79.80  ? 392 LYS D CA  1 
ATOM   15544 C C   . LYS D 1 392 ? -32.373 27.470  64.807  1.00 79.17  ? 392 LYS D C   1 
ATOM   15545 O O   . LYS D 1 392 ? -32.090 27.295  65.994  1.00 85.32  ? 392 LYS D O   1 
ATOM   15546 C CB  . LYS D 1 392 ? -30.023 27.725  63.961  1.00 76.43  ? 392 LYS D CB  1 
ATOM   15547 C CG  . LYS D 1 392 ? -29.813 26.417  63.212  1.00 76.70  ? 392 LYS D CG  1 
ATOM   15548 C CD  . LYS D 1 392 ? -30.578 26.387  61.894  1.00 79.26  ? 392 LYS D CD  1 
ATOM   15549 C CE  . LYS D 1 392 ? -29.826 27.097  60.778  1.00 80.10  ? 392 LYS D CE  1 
ATOM   15550 N NZ  . LYS D 1 392 ? -28.439 26.576  60.630  1.00 80.98  ? 392 LYS D NZ  1 
ATOM   15551 N N   . GLU D 1 393 ? -33.484 26.993  64.253  1.00 80.69  ? 393 GLU D N   1 
ATOM   15552 C CA  . GLU D 1 393 ? -34.512 26.357  65.068  1.00 80.39  ? 393 GLU D CA  1 
ATOM   15553 C C   . GLU D 1 393 ? -34.043 25.009  65.612  1.00 77.06  ? 393 GLU D C   1 
ATOM   15554 O O   . GLU D 1 393 ? -34.425 24.608  66.720  1.00 76.13  ? 393 GLU D O   1 
ATOM   15555 C CB  . GLU D 1 393 ? -35.778 26.192  64.227  1.00 79.50  ? 393 GLU D CB  1 
ATOM   15556 C CG  . GLU D 1 393 ? -36.088 27.389  63.336  1.00 80.18  ? 393 GLU D CG  1 
ATOM   15557 C CD  . GLU D 1 393 ? -37.577 27.637  63.137  1.00 84.86  ? 393 GLU D CD  1 
ATOM   15558 O OE1 . GLU D 1 393 ? -38.352 27.313  64.056  1.00 81.15  ? 393 GLU D OE1 1 
ATOM   15559 O OE2 . GLU D 1 393 ? -37.978 28.141  62.067  1.00 83.30  ? 393 GLU D OE2 1 
ATOM   15560 N N   . ASP D 1 394 ? -33.211 24.298  64.848  1.00 78.20  ? 394 ASP D N   1 
ATOM   15561 C CA  . ASP D 1 394 ? -32.795 22.939  65.194  1.00 78.65  ? 394 ASP D CA  1 
ATOM   15562 C C   . ASP D 1 394 ? -31.599 22.999  66.145  1.00 82.49  ? 394 ASP D C   1 
ATOM   15563 O O   . ASP D 1 394 ? -30.440 22.838  65.754  1.00 81.83  ? 394 ASP D O   1 
ATOM   15564 C CB  . ASP D 1 394 ? -32.467 22.147  63.935  1.00 94.80  ? 394 ASP D CB  1 
ATOM   15565 C CG  . ASP D 1 394 ? -33.568 22.208  62.898  1.00 102.31 ? 394 ASP D CG  1 
ATOM   15566 O OD1 . ASP D 1 394 ? -34.039 23.320  62.591  1.00 90.44  ? 394 ASP D OD1 1 
ATOM   15567 O OD2 . ASP D 1 394 ? -33.957 21.136  62.385  1.00 113.30 ? 394 ASP D OD2 1 
ATOM   15568 N N   . VAL D 1 395 ? -31.897 23.231  67.424  1.00 85.51  ? 395 VAL D N   1 
ATOM   15569 C CA  . VAL D 1 395 ? -30.895 23.174  68.487  1.00 72.60  ? 395 VAL D CA  1 
ATOM   15570 C C   . VAL D 1 395 ? -31.641 23.085  69.810  1.00 71.47  ? 395 VAL D C   1 
ATOM   15571 O O   . VAL D 1 395 ? -32.723 23.659  69.966  1.00 75.50  ? 395 VAL D O   1 
ATOM   15572 C CB  . VAL D 1 395 ? -29.940 24.396  68.433  1.00 70.99  ? 395 VAL D CB  1 
ATOM   15573 C CG1 . VAL D 1 395 ? -30.704 25.695  68.644  1.00 70.05  ? 395 VAL D CG1 1 
ATOM   15574 C CG2 . VAL D 1 395 ? -28.805 24.251  69.442  1.00 69.20  ? 395 VAL D CG2 1 
ATOM   15575 N N   . LYS D 1 396 ? -31.073 22.345  70.762  1.00 71.80  ? 396 LYS D N   1 
ATOM   15576 C CA  . LYS D 1 396 ? -31.749 22.139  72.036  1.00 70.65  ? 396 LYS D CA  1 
ATOM   15577 C C   . LYS D 1 396 ? -31.667 23.393  72.893  1.00 67.59  ? 396 LYS D C   1 
ATOM   15578 O O   . LYS D 1 396 ? -30.618 24.036  72.988  1.00 66.88  ? 396 LYS D O   1 
ATOM   15579 C CB  . LYS D 1 396 ? -31.166 20.950  72.803  1.00 72.36  ? 396 LYS D CB  1 
ATOM   15580 C CG  . LYS D 1 396 ? -32.251 20.137  73.499  1.00 70.59  ? 396 LYS D CG  1 
ATOM   15581 C CD  . LYS D 1 396 ? -31.761 19.344  74.694  1.00 69.88  ? 396 LYS D CD  1 
ATOM   15582 C CE  . LYS D 1 396 ? -30.380 18.739  74.471  1.00 78.39  ? 396 LYS D CE  1 
ATOM   15583 N NZ  . LYS D 1 396 ? -29.861 18.144  75.736  1.00 69.04  ? 396 LYS D NZ  1 
ATOM   15584 N N   . THR D 1 397 ? -32.791 23.734  73.516  1.00 66.85  ? 397 THR D N   1 
ATOM   15585 C CA  . THR D 1 397 ? -32.932 24.942  74.312  1.00 60.63  ? 397 THR D CA  1 
ATOM   15586 C C   . THR D 1 397 ? -33.544 24.605  75.663  1.00 57.27  ? 397 THR D C   1 
ATOM   15587 O O   . THR D 1 397 ? -34.479 23.803  75.749  1.00 57.52  ? 397 THR D O   1 
ATOM   15588 C CB  . THR D 1 397 ? -33.807 25.980  73.593  1.00 68.70  ? 397 THR D CB  1 
ATOM   15589 O OG1 . THR D 1 397 ? -35.144 25.477  73.471  1.00 75.45  ? 397 THR D OG1 1 
ATOM   15590 C CG2 . THR D 1 397 ? -33.256 26.286  72.206  1.00 71.90  ? 397 THR D CG2 1 
ATOM   15591 N N   . GLU D 1 398 ? -33.012 25.227  76.715  1.00 57.55  ? 398 GLU D N   1 
ATOM   15592 C CA  . GLU D 1 398 ? -33.529 25.074  78.067  1.00 55.37  ? 398 GLU D CA  1 
ATOM   15593 C C   . GLU D 1 398 ? -33.634 26.444  78.724  1.00 52.65  ? 398 GLU D C   1 
ATOM   15594 O O   . GLU D 1 398 ? -32.821 27.335  78.465  1.00 50.71  ? 398 GLU D O   1 
ATOM   15595 C CB  . GLU D 1 398 ? -32.640 24.151  78.911  1.00 50.38  ? 398 GLU D CB  1 
ATOM   15596 C CG  . GLU D 1 398 ? -33.369 23.466  80.054  1.00 62.91  ? 398 GLU D CG  1 
ATOM   15597 C CD  . GLU D 1 398 ? -32.428 22.999  81.146  1.00 82.71  ? 398 GLU D CD  1 
ATOM   15598 O OE1 . GLU D 1 398 ? -31.227 22.816  80.858  1.00 101.85 ? 398 GLU D OE1 1 
ATOM   15599 O OE2 . GLU D 1 398 ? -32.890 22.814  82.291  1.00 76.77  ? 398 GLU D OE2 1 
ATOM   15600 N N   . VAL D 1 399 ? -34.640 26.602  79.579  1.00 48.52  ? 399 VAL D N   1 
ATOM   15601 C CA  . VAL D 1 399 ? -34.929 27.874  80.232  1.00 47.02  ? 399 VAL D CA  1 
ATOM   15602 C C   . VAL D 1 399 ? -34.351 27.858  81.638  1.00 47.34  ? 399 VAL D C   1 
ATOM   15603 O O   . VAL D 1 399 ? -34.474 26.864  82.365  1.00 44.53  ? 399 VAL D O   1 
ATOM   15604 C CB  . VAL D 1 399 ? -36.445 28.153  80.262  1.00 45.65  ? 399 VAL D CB  1 
ATOM   15605 C CG1 . VAL D 1 399 ? -36.710 29.631  80.504  1.00 48.88  ? 399 VAL D CG1 1 
ATOM   15606 C CG2 . VAL D 1 399 ? -37.092 27.698  78.963  1.00 48.81  ? 399 VAL D CG2 1 
ATOM   15607 N N   . ILE D 1 400 ? -33.706 28.962  82.019  1.00 47.60  ? 400 ILE D N   1 
ATOM   15608 C CA  . ILE D 1 400 ? -33.156 29.148  83.354  1.00 43.70  ? 400 ILE D CA  1 
ATOM   15609 C C   . ILE D 1 400 ? -33.687 30.464  83.904  1.00 39.66  ? 400 ILE D C   1 
ATOM   15610 O O   . ILE D 1 400 ? -34.192 31.314  83.168  1.00 42.44  ? 400 ILE D O   1 
ATOM   15611 C CB  . ILE D 1 400 ? -31.612 29.139  83.365  1.00 43.54  ? 400 ILE D CB  1 
ATOM   15612 C CG1 . ILE D 1 400 ? -31.067 30.470  82.842  1.00 34.35  ? 400 ILE D CG1 1 
ATOM   15613 C CG2 . ILE D 1 400 ? -31.073 27.975  82.541  1.00 53.37  ? 400 ILE D CG2 1 
ATOM   15614 C CD1 . ILE D 1 400 ? -29.558 30.545  82.830  1.00 36.02  ? 400 ILE D CD1 1 
ATOM   15615 N N   . GLU D 1 401 ? -33.568 30.628  85.223  1.00 34.18  ? 401 GLU D N   1 
ATOM   15616 C CA  . GLU D 1 401 ? -34.123 31.791  85.901  1.00 33.06  ? 401 GLU D CA  1 
ATOM   15617 C C   . GLU D 1 401 ? -33.123 32.586  86.718  1.00 30.55  ? 401 GLU D C   1 
ATOM   15618 O O   . GLU D 1 401 ? -33.458 33.692  87.157  1.00 29.31  ? 401 GLU D O   1 
ATOM   15619 C CB  . GLU D 1 401 ? -35.271 31.372  86.828  1.00 33.99  ? 401 GLU D CB  1 
ATOM   15620 C CG  . GLU D 1 401 ? -36.600 31.571  86.180  1.00 42.81  ? 401 GLU D CG  1 
ATOM   15621 C CD  . GLU D 1 401 ? -37.506 30.395  86.378  1.00 60.58  ? 401 GLU D CD  1 
ATOM   15622 O OE1 . GLU D 1 401 ? -37.170 29.502  87.186  1.00 60.01  ? 401 GLU D OE1 1 
ATOM   15623 O OE2 . GLU D 1 401 ? -38.525 30.338  85.673  1.00 67.04  ? 401 GLU D OE2 1 
ATOM   15624 N N   . SER D 1 402 ? -31.927 32.061  86.955  1.00 29.76  ? 402 SER D N   1 
ATOM   15625 C CA  . SER D 1 402 ? -30.939 32.793  87.726  1.00 27.70  ? 402 SER D CA  1 
ATOM   15626 C C   . SER D 1 402 ? -29.560 32.275  87.359  1.00 27.51  ? 402 SER D C   1 
ATOM   15627 O O   . SER D 1 402 ? -29.403 31.148  86.884  1.00 33.15  ? 402 SER D O   1 
ATOM   15628 C CB  . SER D 1 402 ? -31.188 32.662  89.232  1.00 27.34  ? 402 SER D CB  1 
ATOM   15629 O OG  . SER D 1 402 ? -31.227 31.304  89.633  1.00 33.08  ? 402 SER D OG  1 
ATOM   15630 N N   . VAL D 1 403 ? -28.562 33.123  87.582  1.00 25.84  ? 403 VAL D N   1 
ATOM   15631 C CA  . VAL D 1 403 ? -27.167 32.758  87.395  1.00 25.67  ? 403 VAL D CA  1 
ATOM   15632 C C   . VAL D 1 403 ? -26.376 33.298  88.574  1.00 31.81  ? 403 VAL D C   1 
ATOM   15633 O O   . VAL D 1 403 ? -26.666 34.376  89.102  1.00 28.27  ? 403 VAL D O   1 
ATOM   15634 C CB  . VAL D 1 403 ? -26.591 33.292  86.064  1.00 25.74  ? 403 VAL D CB  1 
ATOM   15635 C CG1 . VAL D 1 403 ? -27.087 32.455  84.895  1.00 27.77  ? 403 VAL D CG1 1 
ATOM   15636 C CG2 . VAL D 1 403 ? -26.952 34.759  85.877  1.00 27.77  ? 403 VAL D CG2 1 
ATOM   15637 N N   . LYS D 1 404 ? -25.380 32.531  89.001  1.00 29.80  ? 404 LYS D N   1 
ATOM   15638 C CA  . LYS D 1 404 ? -24.468 33.011  90.026  1.00 27.72  ? 404 LYS D CA  1 
ATOM   15639 C C   . LYS D 1 404 ? -23.559 34.062  89.406  1.00 24.00  ? 404 LYS D C   1 
ATOM   15640 O O   . LYS D 1 404 ? -22.859 33.783  88.426  1.00 29.23  ? 404 LYS D O   1 
ATOM   15641 C CB  . LYS D 1 404 ? -23.660 31.855  90.605  1.00 33.05  ? 404 LYS D CB  1 
ATOM   15642 C CG  . LYS D 1 404 ? -22.911 32.196  91.882  1.00 34.24  ? 404 LYS D CG  1 
ATOM   15643 C CD  . LYS D 1 404 ? -22.705 30.962  92.754  1.00 40.67  ? 404 LYS D CD  1 
ATOM   15644 C CE  . LYS D 1 404 ? -24.009 30.218  93.024  1.00 42.03  ? 404 LYS D CE  1 
ATOM   15645 N NZ  . LYS D 1 404 ? -25.122 31.127  93.419  1.00 42.11  ? 404 LYS D NZ  1 
ATOM   15646 N N   . ALA D 1 405 ? -23.587 35.273  89.958  1.00 23.90  ? 405 ALA D N   1 
ATOM   15647 C CA  . ALA D 1 405 ? -22.831 36.376  89.383  1.00 21.35  ? 405 ALA D CA  1 
ATOM   15648 C C   . ALA D 1 405 ? -21.344 36.050  89.348  1.00 24.50  ? 405 ALA D C   1 
ATOM   15649 O O   . ALA D 1 405 ? -20.804 35.433  90.271  1.00 26.50  ? 405 ALA D O   1 
ATOM   15650 C CB  . ALA D 1 405 ? -23.070 37.654  90.186  1.00 20.18  ? 405 ALA D CB  1 
ATOM   15651 N N   . GLY D 1 406 ? -20.687 36.457  88.270  1.00 20.67  ? 406 GLY D N   1 
ATOM   15652 C CA  . GLY D 1 406 ? -19.267 36.193  88.143  1.00 24.25  ? 406 GLY D CA  1 
ATOM   15653 C C   . GLY D 1 406 ? -18.733 36.697  86.821  1.00 28.69  ? 406 GLY D C   1 
ATOM   15654 O O   . GLY D 1 406 ? -19.443 37.333  86.033  1.00 36.01  ? 406 GLY D O   1 
ATOM   15655 N N   . THR D 1 407 ? -17.452 36.405  86.599  1.00 22.67  ? 407 THR D N   1 
ATOM   15656 C CA  . THR D 1 407 ? -16.749 36.758  85.373  1.00 23.69  ? 407 THR D CA  1 
ATOM   15657 C C   . THR D 1 407 ? -16.128 35.495  84.794  1.00 29.92  ? 407 THR D C   1 
ATOM   15658 O O   . THR D 1 407 ? -16.424 34.394  85.267  1.00 33.61  ? 407 THR D O   1 
ATOM   15659 C CB  . THR D 1 407 ? -15.676 37.814  85.648  1.00 23.22  ? 407 THR D CB  1 
ATOM   15660 O OG1 . THR D 1 407 ? -14.682 37.267  86.525  1.00 28.03  ? 407 THR D OG1 1 
ATOM   15661 C CG2 . THR D 1 407 ? -16.291 39.047  86.297  1.00 21.49  ? 407 THR D CG2 1 
ATOM   15662 N N   . TRP D 1 408 ? -15.280 35.621  83.776  1.00 27.68  ? 408 TRP D N   1 
ATOM   15663 C CA  . TRP D 1 408 ? -14.579 34.446  83.275  1.00 29.18  ? 408 TRP D CA  1 
ATOM   15664 C C   . TRP D 1 408 ? -13.235 34.228  83.957  1.00 33.15  ? 408 TRP D C   1 
ATOM   15665 O O   . TRP D 1 408 ? -12.538 33.262  83.630  1.00 41.70  ? 408 TRP D O   1 
ATOM   15666 C CB  . TRP D 1 408 ? -14.408 34.515  81.748  1.00 36.76  ? 408 TRP D CB  1 
ATOM   15667 C CG  . TRP D 1 408 ? -13.630 35.680  81.206  1.00 31.19  ? 408 TRP D CG  1 
ATOM   15668 C CD1 . TRP D 1 408 ? -12.914 36.599  81.911  1.00 30.10  ? 408 TRP D CD1 1 
ATOM   15669 C CD2 . TRP D 1 408 ? -13.484 36.032  79.824  1.00 32.89  ? 408 TRP D CD2 1 
ATOM   15670 N NE1 . TRP D 1 408 ? -12.336 37.507  81.055  1.00 33.67  ? 408 TRP D NE1 1 
ATOM   15671 C CE2 . TRP D 1 408 ? -12.671 37.180  79.768  1.00 37.29  ? 408 TRP D CE2 1 
ATOM   15672 C CE3 . TRP D 1 408 ? -13.967 35.488  78.629  1.00 36.70  ? 408 TRP D CE3 1 
ATOM   15673 C CZ2 . TRP D 1 408 ? -12.329 37.795  78.563  1.00 38.96  ? 408 TRP D CZ2 1 
ATOM   15674 C CZ3 . TRP D 1 408 ? -13.626 36.099  77.434  1.00 41.93  ? 408 TRP D CZ3 1 
ATOM   15675 C CH2 . TRP D 1 408 ? -12.816 37.241  77.411  1.00 41.93  ? 408 TRP D CH2 1 
ATOM   15676 N N   . PHE D 1 409 ? -12.860 35.092  84.899  1.00 31.31  ? 409 PHE D N   1 
ATOM   15677 C CA  . PHE D 1 409 ? -11.697 34.866  85.756  1.00 36.29  ? 409 PHE D CA  1 
ATOM   15678 C C   . PHE D 1 409 ? -12.183 34.191  87.032  1.00 44.85  ? 409 PHE D C   1 
ATOM   15679 O O   . PHE D 1 409 ? -12.743 34.844  87.919  1.00 47.51  ? 409 PHE D O   1 
ATOM   15680 C CB  . PHE D 1 409 ? -10.976 36.174  86.064  1.00 41.15  ? 409 PHE D CB  1 
ATOM   15681 C CG  . PHE D 1 409 ? -10.102 36.669  84.948  1.00 41.06  ? 409 PHE D CG  1 
ATOM   15682 C CD1 . PHE D 1 409 ? -10.612 37.508  83.971  1.00 38.14  ? 409 PHE D CD1 1 
ATOM   15683 C CD2 . PHE D 1 409 ? -8.769  36.294  84.874  1.00 37.74  ? 409 PHE D CD2 1 
ATOM   15684 C CE1 . PHE D 1 409 ? -9.810  37.967  82.942  1.00 46.28  ? 409 PHE D CE1 1 
ATOM   15685 C CE2 . PHE D 1 409 ? -7.962  36.748  83.846  1.00 52.67  ? 409 PHE D CE2 1 
ATOM   15686 C CZ  . PHE D 1 409 ? -8.483  37.586  82.879  1.00 56.47  ? 409 PHE D CZ  1 
ATOM   15687 N N   . ASP D 1 410 ? -11.995 32.869  87.110  1.00 44.19  ? 410 ASP D N   1 
ATOM   15688 C CA  . ASP D 1 410 ? -12.357 32.058  88.272  1.00 42.00  ? 410 ASP D CA  1 
ATOM   15689 C C   . ASP D 1 410 ? -13.861 32.044  88.527  1.00 38.26  ? 410 ASP D C   1 
ATOM   15690 O O   . ASP D 1 410 ? -14.323 31.407  89.479  1.00 46.73  ? 410 ASP D O   1 
ATOM   15691 C CB  . ASP D 1 410 ? -11.634 32.550  89.531  1.00 44.08  ? 410 ASP D CB  1 
ATOM   15692 C CG  . ASP D 1 410 ? -10.145 32.724  89.322  1.00 58.21  ? 410 ASP D CG  1 
ATOM   15693 O OD1 . ASP D 1 410 ? -9.433  31.701  89.243  1.00 69.81  ? 410 ASP D OD1 1 
ATOM   15694 O OD2 . ASP D 1 410 ? -9.688  33.883  89.241  1.00 67.55  ? 410 ASP D OD2 1 
ATOM   15695 N N   . GLY D 1 411 ? -14.634 32.727  87.687  1.00 31.87  ? 411 GLY D N   1 
ATOM   15696 C CA  . GLY D 1 411 ? -16.051 32.868  87.935  1.00 26.50  ? 411 GLY D CA  1 
ATOM   15697 C C   . GLY D 1 411 ? -16.416 33.876  88.999  1.00 26.79  ? 411 GLY D C   1 
ATOM   15698 O O   . GLY D 1 411 ? -17.568 33.888  89.445  1.00 33.14  ? 411 GLY D O   1 
ATOM   15699 N N   . ASN D 1 412 ? -15.473 34.716  89.428  1.00 31.02  ? 412 ASN D N   1 
ATOM   15700 C CA  . ASN D 1 412 ? -15.719 35.696  90.477  1.00 22.08  ? 412 ASN D CA  1 
ATOM   15701 C C   . ASN D 1 412 ? -15.057 37.017  90.101  1.00 28.27  ? 412 ASN D C   1 
ATOM   15702 O O   . ASN D 1 412 ? -14.441 37.152  89.038  1.00 28.80  ? 412 ASN D O   1 
ATOM   15703 C CB  . ASN D 1 412 ? -15.225 35.188  91.839  1.00 22.48  ? 412 ASN D CB  1 
ATOM   15704 C CG  . ASN D 1 412 ? -13.731 34.910  91.861  1.00 23.78  ? 412 ASN D CG  1 
ATOM   15705 O OD1 . ASN D 1 412 ? -12.914 35.791  91.593  1.00 23.63  ? 412 ASN D OD1 1 
ATOM   15706 N ND2 . ASN D 1 412 ? -13.369 33.678  92.194  1.00 30.91  ? 412 ASN D ND2 1 
ATOM   15707 N N   . PHE D 1 413 ? -15.181 37.997  90.998  1.00 20.91  ? 413 PHE D N   1 
ATOM   15708 C CA  . PHE D 1 413 ? -14.700 39.354  90.771  1.00 19.71  ? 413 PHE D CA  1 
ATOM   15709 C C   . PHE D 1 413 ? -13.412 39.660  91.529  1.00 22.64  ? 413 PHE D C   1 
ATOM   15710 O O   . PHE D 1 413 ? -13.068 40.835  91.701  1.00 26.21  ? 413 PHE D O   1 
ATOM   15711 C CB  . PHE D 1 413 ? -15.777 40.370  91.159  1.00 18.33  ? 413 PHE D CB  1 
ATOM   15712 C CG  . PHE D 1 413 ? -17.089 40.171  90.452  1.00 18.03  ? 413 PHE D CG  1 
ATOM   15713 C CD1 . PHE D 1 413 ? -18.032 39.283  90.943  1.00 22.98  ? 413 PHE D CD1 1 
ATOM   15714 C CD2 . PHE D 1 413 ? -17.382 40.882  89.303  1.00 20.91  ? 413 PHE D CD2 1 
ATOM   15715 C CE1 . PHE D 1 413 ? -19.239 39.103  90.296  1.00 18.00  ? 413 PHE D CE1 1 
ATOM   15716 C CE2 . PHE D 1 413 ? -18.588 40.706  88.653  1.00 22.15  ? 413 PHE D CE2 1 
ATOM   15717 C CZ  . PHE D 1 413 ? -19.517 39.814  89.152  1.00 17.99  ? 413 PHE D CZ  1 
ATOM   15718 N N   . LEU D 1 414 ? -12.691 38.633  91.987  1.00 21.58  ? 414 LEU D N   1 
ATOM   15719 C CA  . LEU D 1 414 ? -11.517 38.868  92.822  1.00 22.07  ? 414 LEU D CA  1 
ATOM   15720 C C   . LEU D 1 414 ? -10.340 39.443  92.048  1.00 22.98  ? 414 LEU D C   1 
ATOM   15721 O O   . LEU D 1 414 ? -9.346  39.834  92.669  1.00 23.68  ? 414 LEU D O   1 
ATOM   15722 C CB  . LEU D 1 414 ? -11.098 37.575  93.523  1.00 23.38  ? 414 LEU D CB  1 
ATOM   15723 C CG  . LEU D 1 414 ? -11.917 37.244  94.773  1.00 22.89  ? 414 LEU D CG  1 
ATOM   15724 C CD1 . LEU D 1 414 ? -11.387 35.995  95.456  1.00 24.57  ? 414 LEU D CD1 1 
ATOM   15725 C CD2 . LEU D 1 414 ? -11.926 38.423  95.735  1.00 22.04  ? 414 LEU D CD2 1 
ATOM   15726 N N   . LYS D 1 415 ? -10.419 39.499  90.720  1.00 23.26  ? 415 LYS D N   1 
ATOM   15727 C CA  . LYS D 1 415 ? -9.377  40.135  89.926  1.00 24.86  ? 415 LYS D CA  1 
ATOM   15728 C C   . LYS D 1 415 ? -9.547  41.646  89.833  1.00 26.38  ? 415 LYS D C   1 
ATOM   15729 O O   . LYS D 1 415 ? -8.641  42.326  89.339  1.00 34.49  ? 415 LYS D O   1 
ATOM   15730 C CB  . LYS D 1 415 ? -9.349  39.525  88.521  1.00 29.86  ? 415 LYS D CB  1 
ATOM   15731 C CG  . LYS D 1 415 ? -7.974  39.502  87.876  1.00 34.58  ? 415 LYS D CG  1 
ATOM   15732 C CD  . LYS D 1 415 ? -6.998  38.646  88.657  1.00 42.07  ? 415 LYS D CD  1 
ATOM   15733 C CE  . LYS D 1 415 ? -5.582  38.846  88.148  1.00 58.23  ? 415 LYS D CE  1 
ATOM   15734 N NZ  . LYS D 1 415 ? -5.217  40.290  88.123  1.00 55.58  ? 415 LYS D NZ  1 
ATOM   15735 N N   . TRP D 1 416 ? -10.676 42.186  90.299  1.00 21.71  ? 416 TRP D N   1 
ATOM   15736 C CA  . TRP D 1 416 ? -10.953 43.612  90.211  1.00 20.94  ? 416 TRP D CA  1 
ATOM   15737 C C   . TRP D 1 416 ? -11.244 44.271  91.548  1.00 20.10  ? 416 TRP D C   1 
ATOM   15738 O O   . TRP D 1 416 ? -11.181 45.502  91.633  1.00 24.45  ? 416 TRP D O   1 
ATOM   15739 C CB  . TRP D 1 416 ? -12.149 43.871  89.284  1.00 20.21  ? 416 TRP D CB  1 
ATOM   15740 C CG  . TRP D 1 416 ? -11.955 43.349  87.904  1.00 21.36  ? 416 TRP D CG  1 
ATOM   15741 C CD1 . TRP D 1 416 ? -11.474 44.034  86.829  1.00 25.45  ? 416 TRP D CD1 1 
ATOM   15742 C CD2 . TRP D 1 416 ? -12.225 42.020  87.447  1.00 21.92  ? 416 TRP D CD2 1 
ATOM   15743 N NE1 . TRP D 1 416 ? -11.432 43.216  85.727  1.00 31.60  ? 416 TRP D NE1 1 
ATOM   15744 C CE2 . TRP D 1 416 ? -11.888 41.973  86.080  1.00 30.01  ? 416 TRP D CE2 1 
ATOM   15745 C CE3 . TRP D 1 416 ? -12.719 40.865  88.060  1.00 22.38  ? 416 TRP D CE3 1 
ATOM   15746 C CZ2 . TRP D 1 416 ? -12.030 40.817  85.316  1.00 31.40  ? 416 TRP D CZ2 1 
ATOM   15747 C CZ3 . TRP D 1 416 ? -12.860 39.720  87.301  1.00 27.69  ? 416 TRP D CZ3 1 
ATOM   15748 C CH2 . TRP D 1 416 ? -12.517 39.703  85.943  1.00 31.27  ? 416 TRP D CH2 1 
ATOM   15749 N N   . ILE D 1 417 ? -11.562 43.498  92.585  1.00 21.56  ? 417 ILE D N   1 
ATOM   15750 C CA  . ILE D 1 417 ? -12.030 44.059  93.843  1.00 20.74  ? 417 ILE D CA  1 
ATOM   15751 C C   . ILE D 1 417 ? -11.792 43.026  94.931  1.00 19.46  ? 417 ILE D C   1 
ATOM   15752 O O   . ILE D 1 417 ? -11.739 41.822  94.663  1.00 20.01  ? 417 ILE D O   1 
ATOM   15753 C CB  . ILE D 1 417 ? -13.525 44.459  93.741  1.00 27.04  ? 417 ILE D CB  1 
ATOM   15754 C CG1 . ILE D 1 417 ? -13.907 45.458  94.834  1.00 22.38  ? 417 ILE D CG1 1 
ATOM   15755 C CG2 . ILE D 1 417 ? -14.426 43.227  93.786  1.00 22.82  ? 417 ILE D CG2 1 
ATOM   15756 C CD1 . ILE D 1 417 ? -15.203 46.189  94.550  1.00 16.22  ? 417 ILE D CD1 1 
ATOM   15757 N N   . GLY D 1 418 ? -11.623 43.498  96.156  1.00 23.87  ? 418 GLY D N   1 
ATOM   15758 C CA  . GLY D 1 418 ? -11.584 42.633  97.311  1.00 24.27  ? 418 GLY D CA  1 
ATOM   15759 C C   . GLY D 1 418 ? -10.263 42.484  98.050  1.00 27.85  ? 418 GLY D C   1 
ATOM   15760 O O   . GLY D 1 418 ? -10.135 41.557  98.860  1.00 35.29  ? 418 GLY D O   1 
ATOM   15761 N N   . ASN D 1 419 ? -9.286  43.351  97.800  1.00 25.97  ? 419 ASN D N   1 
ATOM   15762 C CA  . ASN D 1 419 ? -8.050  43.363  98.568  1.00 28.70  ? 419 ASN D CA  1 
ATOM   15763 C C   . ASN D 1 419 ? -7.634  44.806  98.801  1.00 37.62  ? 419 ASN D C   1 
ATOM   15764 O O   . ASN D 1 419 ? -8.137  45.729  98.157  1.00 37.58  ? 419 ASN D O   1 
ATOM   15765 C CB  . ASN D 1 419 ? -6.935  42.581  97.865  1.00 31.39  ? 419 ASN D CB  1 
ATOM   15766 C CG  . ASN D 1 419 ? -6.597  43.147  96.507  1.00 36.94  ? 419 ASN D CG  1 
ATOM   15767 O OD1 . ASN D 1 419 ? -7.361  42.991  95.555  1.00 38.99  ? 419 ASN D OD1 1 
ATOM   15768 N ND2 . ASN D 1 419 ? -5.453  43.813  96.405  1.00 40.56  ? 419 ASN D ND2 1 
ATOM   15769 N N   . LYS D 1 420 ? -6.693  44.990  99.732  1.00 33.93  ? 420 LYS D N   1 
ATOM   15770 C CA  . LYS D 1 420 ? -6.337  46.332  100.184 1.00 35.54  ? 420 LYS D CA  1 
ATOM   15771 C C   . LYS D 1 420 ? -5.919  47.238  99.031  1.00 37.10  ? 420 LYS D C   1 
ATOM   15772 O O   . LYS D 1 420 ? -6.148  48.453  99.087  1.00 41.37  ? 420 LYS D O   1 
ATOM   15773 C CB  . LYS D 1 420 ? -5.222  46.254  101.229 1.00 47.90  ? 420 LYS D CB  1 
ATOM   15774 C CG  . LYS D 1 420 ? -4.915  47.582  101.910 1.00 46.63  ? 420 LYS D CG  1 
ATOM   15775 C CD  . LYS D 1 420 ? -4.642  47.405  103.396 1.00 65.03  ? 420 LYS D CD  1 
ATOM   15776 C CE  . LYS D 1 420 ? -5.895  46.990  104.149 1.00 57.48  ? 420 LYS D CE  1 
ATOM   15777 N NZ  . LYS D 1 420 ? -5.589  46.580  105.549 1.00 45.40  ? 420 LYS D NZ  1 
ATOM   15778 N N   . GLU D 1 421 ? -5.326  46.678  97.976  1.00 34.51  ? 421 GLU D N   1 
ATOM   15779 C CA  . GLU D 1 421 ? -4.904  47.498  96.845  1.00 40.76  ? 421 GLU D CA  1 
ATOM   15780 C C   . GLU D 1 421 ? -6.029  47.719  95.837  1.00 41.75  ? 421 GLU D C   1 
ATOM   15781 O O   . GLU D 1 421 ? -6.271  48.856  95.418  1.00 45.84  ? 421 GLU D O   1 
ATOM   15782 C CB  . GLU D 1 421 ? -3.690  46.868  96.156  1.00 55.87  ? 421 GLU D CB  1 
ATOM   15783 C CG  . GLU D 1 421 ? -2.788  47.882  95.466  1.00 64.47  ? 421 GLU D CG  1 
ATOM   15784 C CD  . GLU D 1 421 ? -2.802  49.234  96.157  1.00 58.77  ? 421 GLU D CD  1 
ATOM   15785 O OE1 . GLU D 1 421 ? -3.472  50.159  95.648  1.00 60.79  ? 421 GLU D OE1 1 
ATOM   15786 O OE2 . GLU D 1 421 ? -2.146  49.371  97.211  1.00 69.79  ? 421 GLU D OE2 1 
ATOM   15787 N N   . LYS D 1 422 ? -6.726  46.653  95.436  1.00 41.09  ? 422 LYS D N   1 
ATOM   15788 C CA  . LYS D 1 422 ? -7.822  46.823  94.485  1.00 38.30  ? 422 LYS D CA  1 
ATOM   15789 C C   . LYS D 1 422 ? -9.007  47.548  95.115  1.00 34.82  ? 422 LYS D C   1 
ATOM   15790 O O   . LYS D 1 422 ? -9.767  48.216  94.406  1.00 35.81  ? 422 LYS D O   1 
ATOM   15791 C CB  . LYS D 1 422 ? -8.254  45.468  93.922  1.00 34.72  ? 422 LYS D CB  1 
ATOM   15792 C CG  . LYS D 1 422 ? -7.232  44.837  92.981  1.00 39.41  ? 422 LYS D CG  1 
ATOM   15793 C CD  . LYS D 1 422 ? -7.742  43.531  92.384  1.00 38.29  ? 422 LYS D CD  1 
ATOM   15794 C CE  . LYS D 1 422 ? -6.598  42.704  91.810  1.00 35.52  ? 422 LYS D CE  1 
ATOM   15795 N NZ  . LYS D 1 422 ? -6.335  43.016  90.376  1.00 31.28  ? 422 LYS D NZ  1 
ATOM   15796 N N   . ASN D 1 423 ? -9.185  47.430  96.433  1.00 31.87  ? 423 ASN D N   1 
ATOM   15797 C CA  . ASN D 1 423 ? -10.211 48.215  97.111  1.00 27.72  ? 423 ASN D CA  1 
ATOM   15798 C C   . ASN D 1 423 ? -9.868  49.698  97.150  1.00 28.33  ? 423 ASN D C   1 
ATOM   15799 O O   . ASN D 1 423 ? -10.769 50.524  97.330  1.00 26.00  ? 423 ASN D O   1 
ATOM   15800 C CB  . ASN D 1 423 ? -10.423 47.706  98.540  1.00 21.93  ? 423 ASN D CB  1 
ATOM   15801 C CG  . ASN D 1 423 ? -11.185 46.393  98.589  1.00 28.48  ? 423 ASN D CG  1 
ATOM   15802 O OD1 . ASN D 1 423 ? -11.699 45.922  97.577  1.00 34.57  ? 423 ASN D OD1 1 
ATOM   15803 N ND2 . ASN D 1 423 ? -11.254 45.793  99.774  1.00 22.95  ? 423 ASN D ND2 1 
ATOM   15804 N N   . GLU D 1 424 ? -8.590  50.054  96.995  1.00 22.41  ? 424 GLU D N   1 
ATOM   15805 C CA  . GLU D 1 424 ? -8.202  51.456  97.093  1.00 20.52  ? 424 GLU D CA  1 
ATOM   15806 C C   . GLU D 1 424 ? -8.598  52.239  95.848  1.00 29.63  ? 424 GLU D C   1 
ATOM   15807 O O   . GLU D 1 424 ? -8.992  53.407  95.949  1.00 32.55  ? 424 GLU D O   1 
ATOM   15808 C CB  . GLU D 1 424 ? -6.699  51.576  97.345  1.00 27.91  ? 424 GLU D CB  1 
ATOM   15809 C CG  . GLU D 1 424 ? -6.279  52.967  97.780  1.00 38.50  ? 424 GLU D CG  1 
ATOM   15810 C CD  . GLU D 1 424 ? -7.247  53.573  98.776  1.00 47.74  ? 424 GLU D CD  1 
ATOM   15811 O OE1 . GLU D 1 424 ? -7.370  53.030  99.896  1.00 43.16  ? 424 GLU D OE1 1 
ATOM   15812 O OE2 . GLU D 1 424 ? -7.890  54.588  98.434  1.00 39.20  ? 424 GLU D OE2 1 
ATOM   15813 N N   . TYR D 1 425 ? -8.489  51.623  94.669  1.00 25.63  ? 425 TYR D N   1 
ATOM   15814 C CA  . TYR D 1 425 ? -8.956  52.281  93.452  1.00 23.39  ? 425 TYR D CA  1 
ATOM   15815 C C   . TYR D 1 425 ? -10.461 52.498  93.492  1.00 26.00  ? 425 TYR D C   1 
ATOM   15816 O O   . TYR D 1 425 ? -10.957 53.553  93.079  1.00 32.07  ? 425 TYR D O   1 
ATOM   15817 C CB  . TYR D 1 425 ? -8.569  51.460  92.224  1.00 32.20  ? 425 TYR D CB  1 
ATOM   15818 C CG  . TYR D 1 425 ? -7.373  52.000  91.478  1.00 40.14  ? 425 TYR D CG  1 
ATOM   15819 C CD1 . TYR D 1 425 ? -6.320  52.596  92.158  1.00 37.58  ? 425 TYR D CD1 1 
ATOM   15820 C CD2 . TYR D 1 425 ? -7.297  51.916  90.092  1.00 40.45  ? 425 TYR D CD2 1 
ATOM   15821 C CE1 . TYR D 1 425 ? -5.226  53.091  91.483  1.00 38.74  ? 425 TYR D CE1 1 
ATOM   15822 C CE2 . TYR D 1 425 ? -6.205  52.409  89.408  1.00 37.90  ? 425 TYR D CE2 1 
ATOM   15823 C CZ  . TYR D 1 425 ? -5.174  52.995  90.110  1.00 43.09  ? 425 TYR D CZ  1 
ATOM   15824 O OH  . TYR D 1 425 ? -4.084  53.487  89.437  1.00 50.88  ? 425 TYR D OH  1 
ATOM   15825 N N   . TRP D 1 426 ? -11.205 51.503  93.981  1.00 19.95  ? 426 TRP D N   1 
ATOM   15826 C CA  . TRP D 1 426 ? -12.653 51.640  94.084  1.00 17.80  ? 426 TRP D CA  1 
ATOM   15827 C C   . TRP D 1 426 ? -13.030 52.763  95.039  1.00 19.33  ? 426 TRP D C   1 
ATOM   15828 O O   . TRP D 1 426 ? -13.945 53.545  94.758  1.00 26.37  ? 426 TRP D O   1 
ATOM   15829 C CB  . TRP D 1 426 ? -13.271 50.316  94.532  1.00 18.33  ? 426 TRP D CB  1 
ATOM   15830 C CG  . TRP D 1 426 ? -13.378 49.336  93.419  1.00 18.47  ? 426 TRP D CG  1 
ATOM   15831 C CD1 . TRP D 1 426 ? -12.603 48.231  93.216  1.00 18.89  ? 426 TRP D CD1 1 
ATOM   15832 C CD2 . TRP D 1 426 ? -14.305 49.383  92.332  1.00 18.49  ? 426 TRP D CD2 1 
ATOM   15833 N NE1 . TRP D 1 426 ? -12.998 47.581  92.072  1.00 23.28  ? 426 TRP D NE1 1 
ATOM   15834 C CE2 . TRP D 1 426 ? -14.041 48.269  91.510  1.00 20.86  ? 426 TRP D CE2 1 
ATOM   15835 C CE3 . TRP D 1 426 ? -15.336 50.256  91.976  1.00 18.34  ? 426 TRP D CE3 1 
ATOM   15836 C CZ2 . TRP D 1 426 ? -14.773 48.008  90.354  1.00 21.37  ? 426 TRP D CZ2 1 
ATOM   15837 C CZ3 . TRP D 1 426 ? -16.060 49.995  90.830  1.00 18.75  ? 426 TRP D CZ3 1 
ATOM   15838 C CH2 . TRP D 1 426 ? -15.776 48.881  90.031  1.00 20.59  ? 426 TRP D CH2 1 
ATOM   15839 N N   . LYS D 1 427 ? -12.325 52.867  96.167  1.00 23.24  ? 427 LYS D N   1 
ATOM   15840 C CA  . LYS D 1 427 ? -12.594 53.946  97.112  1.00 29.27  ? 427 LYS D CA  1 
ATOM   15841 C C   . LYS D 1 427 ? -12.381 55.309  96.463  1.00 18.38  ? 427 LYS D C   1 
ATOM   15842 O O   . LYS D 1 427 ? -13.151 56.247  96.702  1.00 18.51  ? 427 LYS D O   1 
ATOM   15843 C CB  . LYS D 1 427 ? -11.706 53.786  98.345  1.00 27.09  ? 427 LYS D CB  1 
ATOM   15844 C CG  . LYS D 1 427 ? -12.340 54.252  99.645  1.00 31.65  ? 427 LYS D CG  1 
ATOM   15845 C CD  . LYS D 1 427 ? -11.444 53.935  100.832 1.00 36.99  ? 427 LYS D CD  1 
ATOM   15846 C CE  . LYS D 1 427 ? -11.035 52.470  100.835 1.00 42.32  ? 427 LYS D CE  1 
ATOM   15847 N NZ  . LYS D 1 427 ? -9.714  52.264  101.492 1.00 33.09  ? 427 LYS D NZ  1 
ATOM   15848 N N   . ILE D 1 428 ? -11.342 55.434  95.633  1.00 18.10  ? 428 ILE D N   1 
ATOM   15849 C CA  . ILE D 1 428 ? -11.121 56.675  94.896  1.00 17.90  ? 428 ILE D CA  1 
ATOM   15850 C C   . ILE D 1 428 ? -12.281 56.944  93.947  1.00 17.34  ? 428 ILE D C   1 
ATOM   15851 O O   . ILE D 1 428 ? -12.751 58.081  93.822  1.00 27.23  ? 428 ILE D O   1 
ATOM   15852 C CB  . ILE D 1 428 ? -9.777  56.621  94.147  1.00 18.04  ? 428 ILE D CB  1 
ATOM   15853 C CG1 . ILE D 1 428 ? -8.611  56.611  95.138  1.00 18.93  ? 428 ILE D CG1 1 
ATOM   15854 C CG2 . ILE D 1 428 ? -9.651  57.789  93.181  1.00 19.42  ? 428 ILE D CG2 1 
ATOM   15855 C CD1 . ILE D 1 428 ? -7.265  56.366  94.491  1.00 19.40  ? 428 ILE D CD1 1 
ATOM   15856 N N   . LEU D 1 429 ? -12.759 55.903  93.260  1.00 17.06  ? 429 LEU D N   1 
ATOM   15857 C CA  . LEU D 1 429 ? -13.872 56.076  92.332  1.00 16.86  ? 429 LEU D CA  1 
ATOM   15858 C C   . LEU D 1 429 ? -15.139 56.519  93.053  1.00 17.09  ? 429 LEU D C   1 
ATOM   15859 O O   . LEU D 1 429 ? -15.857 57.403  92.572  1.00 23.04  ? 429 LEU D O   1 
ATOM   15860 C CB  . LEU D 1 429 ? -14.125 54.779  91.566  1.00 16.91  ? 429 LEU D CB  1 
ATOM   15861 C CG  . LEU D 1 429 ? -15.327 54.793  90.618  1.00 17.08  ? 429 LEU D CG  1 
ATOM   15862 C CD1 . LEU D 1 429 ? -15.116 55.816  89.519  1.00 19.71  ? 429 LEU D CD1 1 
ATOM   15863 C CD2 . LEU D 1 429 ? -15.579 53.417  90.028  1.00 17.49  ? 429 LEU D CD2 1 
ATOM   15864 N N   . ILE D 1 430 ? -15.433 55.913  94.206  1.00 20.63  ? 430 ILE D N   1 
ATOM   15865 C CA  . ILE D 1 430 ? -16.681 56.206  94.911  1.00 22.22  ? 430 ILE D CA  1 
ATOM   15866 C C   . ILE D 1 430 ? -16.721 57.664  95.360  1.00 31.48  ? 430 ILE D C   1 
ATOM   15867 O O   . ILE D 1 430 ? -17.725 58.362  95.169  1.00 36.45  ? 430 ILE D O   1 
ATOM   15868 C CB  . ILE D 1 430 ? -16.867 55.240  96.094  1.00 20.49  ? 430 ILE D CB  1 
ATOM   15869 C CG1 . ILE D 1 430 ? -16.871 53.791  95.599  1.00 18.65  ? 430 ILE D CG1 1 
ATOM   15870 C CG2 . ILE D 1 430 ? -18.146 55.554  96.845  1.00 22.06  ? 430 ILE D CG2 1 
ATOM   15871 C CD1 . ILE D 1 430 ? -17.002 52.763  96.700  1.00 19.46  ? 430 ILE D CD1 1 
ATOM   15872 N N   . GLU D 1 431 ? -15.631 58.151  95.958  1.00 29.88  ? 431 GLU D N   1 
ATOM   15873 C CA  . GLU D 1 431 ? -15.596 59.558  96.346  1.00 23.47  ? 431 GLU D CA  1 
ATOM   15874 C C   . GLU D 1 431 ? -15.581 60.473  95.129  1.00 25.32  ? 431 GLU D C   1 
ATOM   15875 O O   . GLU D 1 431 ? -16.085 61.601  95.196  1.00 42.37  ? 431 GLU D O   1 
ATOM   15876 C CB  . GLU D 1 431 ? -14.388 59.840  97.239  1.00 25.33  ? 431 GLU D CB  1 
ATOM   15877 C CG  . GLU D 1 431 ? -14.514 61.131  98.034  1.00 48.00  ? 431 GLU D CG  1 
ATOM   15878 C CD  . GLU D 1 431 ? -15.010 60.905  99.449  1.00 66.34  ? 431 GLU D CD  1 
ATOM   15879 O OE1 . GLU D 1 431 ? -16.185 60.518  99.620  1.00 71.76  ? 431 GLU D OE1 1 
ATOM   15880 O OE2 . GLU D 1 431 ? -14.223 61.125  100.393 1.00 63.93  ? 431 GLU D OE2 1 
ATOM   15881 N N   . ALA D 1 432 ? -15.001 60.015  94.018  1.00 17.75  ? 432 ALA D N   1 
ATOM   15882 C CA  . ALA D 1 432 ? -15.072 60.781  92.778  1.00 18.18  ? 432 ALA D CA  1 
ATOM   15883 C C   . ALA D 1 432 ? -16.503 60.854  92.259  1.00 24.98  ? 432 ALA D C   1 
ATOM   15884 O O   . ALA D 1 432 ? -16.947 61.911  91.795  1.00 30.90  ? 432 ALA D O   1 
ATOM   15885 C CB  . ALA D 1 432 ? -14.149 60.167  91.727  1.00 17.16  ? 432 ALA D CB  1 
ATOM   15886 N N   . LYS D 1 433 ? -17.238 59.741  92.331  1.00 20.72  ? 433 LYS D N   1 
ATOM   15887 C CA  . LYS D 1 433 ? -18.618 59.727  91.854  1.00 21.51  ? 433 LYS D CA  1 
ATOM   15888 C C   . LYS D 1 433 ? -19.505 60.649  92.681  1.00 21.16  ? 433 LYS D C   1 
ATOM   15889 O O   . LYS D 1 433 ? -20.468 61.219  92.154  1.00 24.08  ? 433 LYS D O   1 
ATOM   15890 C CB  . LYS D 1 433 ? -19.157 58.294  91.873  1.00 19.41  ? 433 LYS D CB  1 
ATOM   15891 C CG  . LYS D 1 433 ? -20.603 58.139  91.415  1.00 21.98  ? 433 LYS D CG  1 
ATOM   15892 C CD  . LYS D 1 433 ? -20.834 58.781  90.057  1.00 31.34  ? 433 LYS D CD  1 
ATOM   15893 C CE  . LYS D 1 433 ? -22.065 58.209  89.368  1.00 32.53  ? 433 LYS D CE  1 
ATOM   15894 N NZ  . LYS D 1 433 ? -23.108 57.744  90.324  1.00 39.91  ? 433 LYS D NZ  1 
ATOM   15895 N N   . LYS D 1 434 ? -19.197 60.814  93.970  1.00 25.86  ? 434 LYS D N   1 
ATOM   15896 C CA  . LYS D 1 434 ? -19.999 61.687  94.822  1.00 27.11  ? 434 LYS D CA  1 
ATOM   15897 C C   . LYS D 1 434 ? -19.921 63.138  94.361  1.00 31.02  ? 434 LYS D C   1 
ATOM   15898 O O   . LYS D 1 434 ? -20.930 63.854  94.366  1.00 30.06  ? 434 LYS D O   1 
ATOM   15899 C CB  . LYS D 1 434 ? -19.541 61.569  96.273  1.00 20.68  ? 434 LYS D CB  1 
ATOM   15900 C CG  . LYS D 1 434 ? -19.950 60.283  96.962  1.00 33.14  ? 434 LYS D CG  1 
ATOM   15901 C CD  . LYS D 1 434 ? -20.408 60.562  98.383  1.00 29.79  ? 434 LYS D CD  1 
ATOM   15902 C CE  . LYS D 1 434 ? -20.245 59.338  99.266  1.00 30.00  ? 434 LYS D CE  1 
ATOM   15903 N NZ  . LYS D 1 434 ? -18.843 59.209  99.747  1.00 43.87  ? 434 LYS D NZ  1 
ATOM   15904 N N   . LYS D 1 435 ? -18.731 63.591  93.969  1.00 26.26  ? 435 LYS D N   1 
ATOM   15905 C CA  . LYS D 1 435 ? -18.509 64.962  93.532  1.00 22.87  ? 435 LYS D CA  1 
ATOM   15906 C C   . LYS D 1 435 ? -18.379 65.072  92.016  1.00 29.65  ? 435 LYS D C   1 
ATOM   15907 O O   . LYS D 1 435 ? -17.880 66.085  91.515  1.00 37.96  ? 435 LYS D O   1 
ATOM   15908 C CB  . LYS D 1 435 ? -17.264 65.533  94.213  1.00 34.23  ? 435 LYS D CB  1 
ATOM   15909 C CG  . LYS D 1 435 ? -17.516 66.115  95.596  1.00 40.13  ? 435 LYS D CG  1 
ATOM   15910 C CD  . LYS D 1 435 ? -16.244 66.709  96.189  1.00 44.55  ? 435 LYS D CD  1 
ATOM   15911 C CE  . LYS D 1 435 ? -15.200 65.640  96.482  1.00 46.48  ? 435 LYS D CE  1 
ATOM   15912 N NZ  . LYS D 1 435 ? -15.116 65.328  97.938  1.00 40.68  ? 435 LYS D NZ  1 
ATOM   15913 N N   . ALA D 1 436 ? -18.815 64.051  91.281  1.00 25.38  ? 436 ALA D N   1 
ATOM   15914 C CA  . ALA D 1 436 ? -18.632 64.025  89.836  1.00 24.27  ? 436 ALA D CA  1 
ATOM   15915 C C   . ALA D 1 436 ? -19.490 65.083  89.153  1.00 24.30  ? 436 ALA D C   1 
ATOM   15916 O O   . ALA D 1 436 ? -20.578 65.433  89.617  1.00 27.73  ? 436 ALA D O   1 
ATOM   15917 C CB  . ALA D 1 436 ? -18.972 62.642  89.284  1.00 26.89  ? 436 ALA D CB  1 
ATOM   15918 N N   . LYS D 1 437 ? -18.986 65.592  88.028  1.00 24.35  ? 437 LYS D N   1 
ATOM   15919 C CA  . LYS D 1 437 ? -19.676 66.636  87.282  1.00 20.58  ? 437 LYS D CA  1 
ATOM   15920 C C   . LYS D 1 437 ? -19.782 66.372  85.787  1.00 20.99  ? 437 LYS D C   1 
ATOM   15921 O O   . LYS D 1 437 ? -20.574 67.050  85.123  1.00 31.76  ? 437 LYS D O   1 
ATOM   15922 C CB  . LYS D 1 437 ? -18.983 67.990  87.493  1.00 20.96  ? 437 LYS D CB  1 
ATOM   15923 C CG  . LYS D 1 437 ? -19.450 68.740  88.731  1.00 24.05  ? 437 LYS D CG  1 
ATOM   15924 C CD  . LYS D 1 437 ? -18.272 69.112  89.613  1.00 39.53  ? 437 LYS D CD  1 
ATOM   15925 C CE  . LYS D 1 437 ? -18.656 69.124  91.083  1.00 39.97  ? 437 LYS D CE  1 
ATOM   15926 N NZ  . LYS D 1 437 ? -17.454 69.089  91.963  1.00 25.27  ? 437 LYS D NZ  1 
ATOM   15927 N N   . ASN D 1 438 ? -19.024 65.427  85.235  1.00 20.94  ? 438 ASN D N   1 
ATOM   15928 C CA  . ASN D 1 438 ? -19.117 65.112  83.818  1.00 21.46  ? 438 ASN D CA  1 
ATOM   15929 C C   . ASN D 1 438 ? -18.887 63.619  83.625  1.00 21.53  ? 438 ASN D C   1 
ATOM   15930 O O   . ASN D 1 438 ? -18.447 62.911  84.536  1.00 23.44  ? 438 ASN D O   1 
ATOM   15931 C CB  . ASN D 1 438 ? -18.124 65.935  82.987  1.00 21.84  ? 438 ASN D CB  1 
ATOM   15932 C CG  . ASN D 1 438 ? -16.701 65.812  83.485  1.00 21.18  ? 438 ASN D CG  1 
ATOM   15933 O OD1 . ASN D 1 438 ? -15.951 64.952  83.033  1.00 21.13  ? 438 ASN D OD1 1 
ATOM   15934 N ND2 . ASN D 1 438 ? -16.319 66.679  84.414  1.00 27.82  ? 438 ASN D ND2 1 
ATOM   15935 N N   . ASP D 1 439 ? -19.180 63.151  82.414  1.00 21.92  ? 439 ASP D N   1 
ATOM   15936 C CA  . ASP D 1 439 ? -19.171 61.729  82.082  1.00 22.04  ? 439 ASP D CA  1 
ATOM   15937 C C   . ASP D 1 439 ? -17.774 61.120  82.055  1.00 24.27  ? 439 ASP D C   1 
ATOM   15938 O O   . ASP D 1 439 ? -17.662 59.934  81.711  1.00 23.66  ? 439 ASP D O   1 
ATOM   15939 C CB  . ASP D 1 439 ? -19.873 61.518  80.739  1.00 38.00  ? 439 ASP D CB  1 
ATOM   15940 C CG  . ASP D 1 439 ? -21.336 61.157  80.900  1.00 59.54  ? 439 ASP D CG  1 
ATOM   15941 O OD1 . ASP D 1 439 ? -21.994 61.746  81.783  1.00 59.83  ? 439 ASP D OD1 1 
ATOM   15942 O OD2 . ASP D 1 439 ? -21.828 60.282  80.157  1.00 64.39  ? 439 ASP D OD2 1 
ATOM   15943 N N   . TYR D 1 440 ? -16.718 61.857  82.411  1.00 25.06  ? 440 TYR D N   1 
ATOM   15944 C CA  . TYR D 1 440 ? -15.404 61.244  82.578  1.00 21.27  ? 440 TYR D CA  1 
ATOM   15945 C C   . TYR D 1 440 ? -15.387 60.230  83.710  1.00 19.66  ? 440 TYR D C   1 
ATOM   15946 O O   . TYR D 1 440 ? -14.442 59.440  83.798  1.00 25.76  ? 440 TYR D O   1 
ATOM   15947 C CB  . TYR D 1 440 ? -14.342 62.314  82.838  1.00 25.56  ? 440 TYR D CB  1 
ATOM   15948 C CG  . TYR D 1 440 ? -13.606 62.772  81.600  1.00 26.10  ? 440 TYR D CG  1 
ATOM   15949 C CD1 . TYR D 1 440 ? -12.456 62.127  81.174  1.00 26.31  ? 440 TYR D CD1 1 
ATOM   15950 C CD2 . TYR D 1 440 ? -14.061 63.857  80.861  1.00 30.93  ? 440 TYR D CD2 1 
ATOM   15951 C CE1 . TYR D 1 440 ? -11.781 62.545  80.045  1.00 31.70  ? 440 TYR D CE1 1 
ATOM   15952 C CE2 . TYR D 1 440 ? -13.392 64.283  79.731  1.00 32.44  ? 440 TYR D CE2 1 
ATOM   15953 C CZ  . TYR D 1 440 ? -12.253 63.624  79.327  1.00 32.96  ? 440 TYR D CZ  1 
ATOM   15954 O OH  . TYR D 1 440 ? -11.586 64.047  78.200  1.00 29.34  ? 440 TYR D OH  1 
ATOM   15955 N N   . ILE D 1 441 ? -16.401 60.249  84.579  1.00 19.19  ? 441 ILE D N   1 
ATOM   15956 C CA  . ILE D 1 441 ? -16.544 59.210  85.592  1.00 25.13  ? 441 ILE D CA  1 
ATOM   15957 C C   . ILE D 1 441 ? -16.728 57.847  84.935  1.00 21.51  ? 441 ILE D C   1 
ATOM   15958 O O   . ILE D 1 441 ? -16.268 56.828  85.463  1.00 24.48  ? 441 ILE D O   1 
ATOM   15959 C CB  . ILE D 1 441 ? -17.706 59.558  86.548  1.00 20.22  ? 441 ILE D CB  1 
ATOM   15960 C CG1 . ILE D 1 441 ? -17.582 58.789  87.865  1.00 17.88  ? 441 ILE D CG1 1 
ATOM   15961 C CG2 . ILE D 1 441 ? -19.066 59.341  85.882  1.00 23.23  ? 441 ILE D CG2 1 
ATOM   15962 C CD1 . ILE D 1 441 ? -16.484 59.310  88.768  1.00 17.37  ? 441 ILE D CD1 1 
ATOM   15963 N N   . LEU D 1 442 ? -17.389 57.804  83.773  1.00 21.78  ? 442 LEU D N   1 
ATOM   15964 C CA  . LEU D 1 442 ? -17.581 56.536  83.074  1.00 21.74  ? 442 LEU D CA  1 
ATOM   15965 C C   . LEU D 1 442 ? -16.256 55.956  82.599  1.00 24.29  ? 442 LEU D C   1 
ATOM   15966 O O   . LEU D 1 442 ? -16.065 54.734  82.612  1.00 26.68  ? 442 LEU D O   1 
ATOM   15967 C CB  . LEU D 1 442 ? -18.537 56.716  81.897  1.00 22.39  ? 442 LEU D CB  1 
ATOM   15968 C CG  . LEU D 1 442 ? -19.883 57.386  82.163  1.00 27.79  ? 442 LEU D CG  1 
ATOM   15969 C CD1 . LEU D 1 442 ? -20.654 57.486  80.863  1.00 34.30  ? 442 LEU D CD1 1 
ATOM   15970 C CD2 . LEU D 1 442 ? -20.669 56.601  83.194  1.00 28.35  ? 442 LEU D CD2 1 
ATOM   15971 N N   . VAL D 1 443 ? -15.335 56.812  82.152  1.00 28.55  ? 443 VAL D N   1 
ATOM   15972 C CA  . VAL D 1 443 ? -14.011 56.332  81.774  1.00 21.58  ? 443 VAL D CA  1 
ATOM   15973 C C   . VAL D 1 443 ? -13.283 55.775  82.990  1.00 20.52  ? 443 VAL D C   1 
ATOM   15974 O O   . VAL D 1 443 ? -12.578 54.762  82.901  1.00 23.77  ? 443 VAL D O   1 
ATOM   15975 C CB  . VAL D 1 443 ? -13.206 57.456  81.097  1.00 22.67  ? 443 VAL D CB  1 
ATOM   15976 C CG1 . VAL D 1 443 ? -11.936 56.895  80.479  1.00 25.75  ? 443 VAL D CG1 1 
ATOM   15977 C CG2 . VAL D 1 443 ? -14.054 58.160  80.049  1.00 24.30  ? 443 VAL D CG2 1 
ATOM   15978 N N   . ALA D 1 444 ? -13.446 56.421  84.147  1.00 20.35  ? 444 ALA D N   1 
ATOM   15979 C CA  . ALA D 1 444 ? -12.817 55.957  85.377  1.00 19.33  ? 444 ALA D CA  1 
ATOM   15980 C C   . ALA D 1 444 ? -13.441 54.676  85.913  1.00 21.81  ? 444 ALA D C   1 
ATOM   15981 O O   . ALA D 1 444 ? -12.884 54.081  86.842  1.00 28.67  ? 444 ALA D O   1 
ATOM   15982 C CB  . ALA D 1 444 ? -12.882 57.048  86.447  1.00 18.02  ? 444 ALA D CB  1 
ATOM   15983 N N   . GLU D 1 445 ? -14.572 54.240  85.362  1.00 19.56  ? 445 GLU D N   1 
ATOM   15984 C CA  . GLU D 1 445 ? -15.202 52.987  85.758  1.00 20.84  ? 445 GLU D CA  1 
ATOM   15985 C C   . GLU D 1 445 ? -14.771 51.807  84.898  1.00 24.57  ? 445 GLU D C   1 
ATOM   15986 O O   . GLU D 1 445 ? -15.267 50.696  85.111  1.00 25.41  ? 445 GLU D O   1 
ATOM   15987 C CB  . GLU D 1 445 ? -16.728 53.115  85.709  1.00 20.55  ? 445 GLU D CB  1 
ATOM   15988 C CG  . GLU D 1 445 ? -17.301 54.107  86.699  1.00 23.70  ? 445 GLU D CG  1 
ATOM   15989 C CD  . GLU D 1 445 ? -18.602 54.713  86.218  1.00 31.01  ? 445 GLU D CD  1 
ATOM   15990 O OE1 . GLU D 1 445 ? -19.077 54.323  85.129  1.00 32.43  ? 445 GLU D OE1 1 
ATOM   15991 O OE2 . GLU D 1 445 ? -19.144 55.590  86.921  1.00 28.55  ? 445 GLU D OE2 1 
ATOM   15992 N N   . GLY D 1 446 ? -13.879 52.022  83.934  1.00 27.58  ? 446 GLY D N   1 
ATOM   15993 C CA  . GLY D 1 446 ? -13.433 50.920  83.099  1.00 29.05  ? 446 GLY D CA  1 
ATOM   15994 C C   . GLY D 1 446 ? -12.785 49.827  83.930  1.00 29.67  ? 446 GLY D C   1 
ATOM   15995 O O   . GLY D 1 446 ? -12.062 50.095  84.892  1.00 29.42  ? 446 GLY D O   1 
ATOM   15996 N N   . SER D 1 447 ? -13.059 48.576  83.554  1.00 30.70  ? 447 SER D N   1 
ATOM   15997 C CA  . SER D 1 447 ? -12.557 47.438  84.317  1.00 31.58  ? 447 SER D CA  1 
ATOM   15998 C C   . SER D 1 447 ? -11.039 47.342  84.287  1.00 32.71  ? 447 SER D C   1 
ATOM   15999 O O   . SER D 1 447 ? -10.452 46.719  85.177  1.00 33.64  ? 447 SER D O   1 
ATOM   16000 C CB  . SER D 1 447 ? -13.161 46.140  83.781  1.00 32.71  ? 447 SER D CB  1 
ATOM   16001 O OG  . SER D 1 447 ? -12.517 45.740  82.583  1.00 34.08  ? 447 SER D OG  1 
ATOM   16002 N N   . ASP D 1 448 ? -10.393 47.948  83.288  1.00 33.17  ? 448 ASP D N   1 
ATOM   16003 C CA  . ASP D 1 448 ? -8.954  47.775  83.112  1.00 34.66  ? 448 ASP D CA  1 
ATOM   16004 C C   . ASP D 1 448 ? -8.162  48.401  84.254  1.00 34.37  ? 448 ASP D C   1 
ATOM   16005 O O   . ASP D 1 448 ? -7.128  47.861  84.665  1.00 35.79  ? 448 ASP D O   1 
ATOM   16006 C CB  . ASP D 1 448 ? -8.523  48.366  81.770  1.00 35.39  ? 448 ASP D CB  1 
ATOM   16007 C CG  . ASP D 1 448 ? -9.312  47.801  80.604  1.00 35.93  ? 448 ASP D CG  1 
ATOM   16008 O OD1 . ASP D 1 448 ? -10.445 48.273  80.369  1.00 34.83  ? 448 ASP D OD1 1 
ATOM   16009 O OD2 . ASP D 1 448 ? -8.801  46.886  79.924  1.00 37.73  ? 448 ASP D OD2 1 
ATOM   16010 N N   . TRP D 1 449 ? -8.624  49.541  84.777  1.00 32.76  ? 449 TRP D N   1 
ATOM   16011 C CA  . TRP D 1 449 ? -7.869  50.240  85.816  1.00 32.61  ? 449 TRP D CA  1 
ATOM   16012 C C   . TRP D 1 449 ? -7.740  49.394  87.078  1.00 33.09  ? 449 TRP D C   1 
ATOM   16013 O O   . TRP D 1 449 ? -6.705  49.428  87.755  1.00 34.15  ? 449 TRP D O   1 
ATOM   16014 C CB  . TRP D 1 449 ? -8.529  51.582  86.134  1.00 30.82  ? 449 TRP D CB  1 
ATOM   16015 C CG  . TRP D 1 449 ? -8.981  52.338  84.919  1.00 30.39  ? 449 TRP D CG  1 
ATOM   16016 C CD1 . TRP D 1 449 ? -10.261 52.691  84.602  1.00 29.18  ? 449 TRP D CD1 1 
ATOM   16017 C CD2 . TRP D 1 449 ? -8.154  52.838  83.861  1.00 31.51  ? 449 TRP D CD2 1 
ATOM   16018 N NE1 . TRP D 1 449 ? -10.282 53.377  83.412  1.00 29.51  ? 449 TRP D NE1 1 
ATOM   16019 C CE2 . TRP D 1 449 ? -9.001  53.481  82.937  1.00 30.93  ? 449 TRP D CE2 1 
ATOM   16020 C CE3 . TRP D 1 449 ? -6.780  52.805  83.605  1.00 33.20  ? 449 TRP D CE3 1 
ATOM   16021 C CZ2 . TRP D 1 449 ? -8.519  54.085  81.776  1.00 35.89  ? 449 TRP D CZ2 1 
ATOM   16022 C CZ3 . TRP D 1 449 ? -6.303  53.404  82.451  1.00 34.22  ? 449 TRP D CZ3 1 
ATOM   16023 C CH2 . TRP D 1 449 ? -7.170  54.035  81.552  1.00 35.98  ? 449 TRP D CH2 1 
ATOM   16024 N N   . PHE D 1 450 ? -8.781  48.638  87.417  1.00 32.58  ? 450 PHE D N   1 
ATOM   16025 C CA  . PHE D 1 450 ? -8.744  47.795  88.604  1.00 33.29  ? 450 PHE D CA  1 
ATOM   16026 C C   . PHE D 1 450 ? -8.048  46.462  88.361  1.00 35.41  ? 450 PHE D C   1 
ATOM   16027 O O   . PHE D 1 450 ? -7.580  45.838  89.320  1.00 36.99  ? 450 PHE D O   1 
ATOM   16028 C CB  . PHE D 1 450 ? -10.169 47.563  89.111  1.00 32.14  ? 450 PHE D CB  1 
ATOM   16029 C CG  . PHE D 1 450 ? -11.012 48.808  89.118  1.00 30.18  ? 450 PHE D CG  1 
ATOM   16030 C CD1 . PHE D 1 450 ? -10.935 49.704  90.171  1.00 29.39  ? 450 PHE D CD1 1 
ATOM   16031 C CD2 . PHE D 1 450 ? -11.865 49.093  88.062  1.00 29.38  ? 450 PHE D CD2 1 
ATOM   16032 C CE1 . PHE D 1 450 ? -11.702 50.854  90.179  1.00 27.75  ? 450 PHE D CE1 1 
ATOM   16033 C CE2 . PHE D 1 450 ? -12.635 50.244  88.063  1.00 27.84  ? 450 PHE D CE2 1 
ATOM   16034 C CZ  . PHE D 1 450 ? -12.553 51.125  89.124  1.00 26.99  ? 450 PHE D CZ  1 
ATOM   16035 N N   . TRP D 1 451 ? -7.972  46.010  87.107  1.00 41.65  ? 451 TRP D N   1 
ATOM   16036 C CA  . TRP D 1 451 ? -7.270  44.766  86.804  1.00 42.18  ? 451 TRP D CA  1 
ATOM   16037 C C   . TRP D 1 451 ? -5.767  44.909  87.011  1.00 43.01  ? 451 TRP D C   1 
ATOM   16038 O O   . TRP D 1 451 ? -5.117  43.998  87.536  1.00 41.78  ? 451 TRP D O   1 
ATOM   16039 C CB  . TRP D 1 451 ? -7.570  44.338  85.368  1.00 42.62  ? 451 TRP D CB  1 
ATOM   16040 C CG  . TRP D 1 451 ? -7.399  42.872  85.117  1.00 53.00  ? 451 TRP D CG  1 
ATOM   16041 C CD1 . TRP D 1 451 ? -8.369  41.915  85.161  1.00 52.92  ? 451 TRP D CD1 1 
ATOM   16042 C CD2 . TRP D 1 451 ? -6.181  42.194  84.783  1.00 56.91  ? 451 TRP D CD2 1 
ATOM   16043 N NE1 . TRP D 1 451 ? -7.834  40.683  84.871  1.00 52.25  ? 451 TRP D NE1 1 
ATOM   16044 C CE2 . TRP D 1 451 ? -6.491  40.827  84.637  1.00 58.21  ? 451 TRP D CE2 1 
ATOM   16045 C CE3 . TRP D 1 451 ? -4.860  42.610  84.592  1.00 59.86  ? 451 TRP D CE3 1 
ATOM   16046 C CZ2 . TRP D 1 451 ? -5.528  39.873  84.310  1.00 60.69  ? 451 TRP D CZ2 1 
ATOM   16047 C CZ3 . TRP D 1 451 ? -3.905  41.662  84.267  1.00 73.18  ? 451 TRP D CZ3 1 
ATOM   16048 C CH2 . TRP D 1 451 ? -4.244  40.310  84.130  1.00 62.59  ? 451 TRP D CH2 1 
ATOM   16049 N N   . TRP D 1 452 ? -5.200  46.041  86.607  1.00 45.86  ? 452 TRP D N   1 
ATOM   16050 C CA  . TRP D 1 452 ? -3.752  46.250  86.637  1.00 41.29  ? 452 TRP D CA  1 
ATOM   16051 C C   . TRP D 1 452 ? -3.288  46.825  87.971  1.00 48.98  ? 452 TRP D C   1 
ATOM   16052 O O   . TRP D 1 452 ? -2.599  47.843  88.027  1.00 48.03  ? 452 TRP D O   1 
ATOM   16053 C CB  . TRP D 1 452 ? -3.345  47.153  85.480  1.00 41.22  ? 452 TRP D CB  1 
ATOM   16054 C CG  . TRP D 1 452 ? -3.320  46.454  84.159  1.00 47.13  ? 452 TRP D CG  1 
ATOM   16055 C CD1 . TRP D 1 452 ? -4.057  46.762  83.054  1.00 41.34  ? 452 TRP D CD1 1 
ATOM   16056 C CD2 . TRP D 1 452 ? -2.513  45.325  83.801  1.00 47.61  ? 452 TRP D CD2 1 
ATOM   16057 N NE1 . TRP D 1 452 ? -3.760  45.896  82.030  1.00 57.18  ? 452 TRP D NE1 1 
ATOM   16058 C CE2 . TRP D 1 452 ? -2.815  45.004  82.463  1.00 51.99  ? 452 TRP D CE2 1 
ATOM   16059 C CE3 . TRP D 1 452 ? -1.566  44.555  84.481  1.00 52.03  ? 452 TRP D CE3 1 
ATOM   16060 C CZ2 . TRP D 1 452 ? -2.202  43.947  81.792  1.00 59.74  ? 452 TRP D CZ2 1 
ATOM   16061 C CZ3 . TRP D 1 452 ? -0.963  43.506  83.814  1.00 59.75  ? 452 TRP D CZ3 1 
ATOM   16062 C CH2 . TRP D 1 452 ? -1.280  43.212  82.484  1.00 64.81  ? 452 TRP D CH2 1 
ATOM   16063 N N   . GLN D 1 453 ? -3.661  46.161  89.063  1.00 58.60  ? 453 GLN D N   1 
ATOM   16064 C CA  . GLN D 1 453 ? -3.324  46.614  90.403  1.00 46.61  ? 453 GLN D CA  1 
ATOM   16065 C C   . GLN D 1 453 ? -3.009  45.400  91.264  1.00 43.90  ? 453 GLN D C   1 
ATOM   16066 O O   . GLN D 1 453 ? -3.263  44.255  90.882  1.00 57.45  ? 453 GLN D O   1 
ATOM   16067 C CB  . GLN D 1 453 ? -4.461  47.438  91.021  1.00 49.81  ? 453 GLN D CB  1 
ATOM   16068 C CG  . GLN D 1 453 ? -4.550  48.867  90.502  1.00 51.00  ? 453 GLN D CG  1 
ATOM   16069 C CD  . GLN D 1 453 ? -3.404  49.738  90.984  1.00 58.28  ? 453 GLN D CD  1 
ATOM   16070 O OE1 . GLN D 1 453 ? -3.363  50.135  92.148  1.00 58.44  ? 453 GLN D OE1 1 
ATOM   16071 N NE2 . GLN D 1 453 ? -2.472  50.047  90.088  1.00 57.51  ? 453 GLN D NE2 1 
ATOM   16072 N N   . GLY D 1 454 ? -2.448  45.659  92.437  1.00 51.02  ? 454 GLY D N   1 
ATOM   16073 C CA  . GLY D 1 454 ? -2.058  44.596  93.338  1.00 53.66  ? 454 GLY D CA  1 
ATOM   16074 C C   . GLY D 1 454 ? -0.602  44.210  93.173  1.00 78.51  ? 454 GLY D C   1 
ATOM   16075 O O   . GLY D 1 454 ? 0.216   44.939  92.604  1.00 86.38  ? 454 GLY D O   1 
ATOM   16076 N N   . GLU D 1 455 ? -0.281  43.019  93.680  1.00 99.17  ? 455 GLU D N   1 
ATOM   16077 C CA  . GLU D 1 455 ? 1.093   42.526  93.678  1.00 101.94 ? 455 GLU D CA  1 
ATOM   16078 C C   . GLU D 1 455 ? 1.578   42.106  92.293  1.00 108.52 ? 455 GLU D C   1 
ATOM   16079 O O   . GLU D 1 455 ? 2.759   41.770  92.149  1.00 109.48 ? 455 GLU D O   1 
ATOM   16080 C CB  . GLU D 1 455 ? 1.222   41.359  94.664  1.00 91.55  ? 455 GLU D CB  1 
ATOM   16081 C CG  . GLU D 1 455 ? 2.638   41.107  95.179  1.00 103.55 ? 455 GLU D CG  1 
ATOM   16082 C CD  . GLU D 1 455 ? 3.275   42.340  95.795  1.00 92.88  ? 455 GLU D CD  1 
ATOM   16083 O OE1 . GLU D 1 455 ? 2.952   42.662  96.957  1.00 101.39 ? 455 GLU D OE1 1 
ATOM   16084 O OE2 . GLU D 1 455 ? 4.107   42.983  95.119  1.00 79.67  ? 455 GLU D OE2 1 
ATOM   16085 N N   . GLU D 1 456 ? 0.717   42.116  91.276  1.00 103.94 ? 456 GLU D N   1 
ATOM   16086 C CA  . GLU D 1 456 ? 1.133   41.776  89.914  1.00 111.89 ? 456 GLU D CA  1 
ATOM   16087 C C   . GLU D 1 456 ? 1.936   42.945  89.352  1.00 111.56 ? 456 GLU D C   1 
ATOM   16088 O O   . GLU D 1 456 ? 1.388   43.905  88.806  1.00 102.40 ? 456 GLU D O   1 
ATOM   16089 C CB  . GLU D 1 456 ? -0.075  41.453  89.043  1.00 104.30 ? 456 GLU D CB  1 
ATOM   16090 C CG  . GLU D 1 456 ? -1.314  42.268  89.368  1.00 86.62  ? 456 GLU D CG  1 
ATOM   16091 C CD  . GLU D 1 456 ? -2.548  41.757  88.656  1.00 86.09  ? 456 GLU D CD  1 
ATOM   16092 O OE1 . GLU D 1 456 ? -2.471  41.508  87.434  1.00 61.63  ? 456 GLU D OE1 1 
ATOM   16093 O OE2 . GLU D 1 456 ? -3.597  41.606  89.319  1.00 89.81  ? 456 GLU D OE2 1 
ATOM   16094 N N   . LYS D 1 457 ? 3.261   42.858  89.486  1.00 105.90 ? 457 LYS D N   1 
ATOM   16095 C CA  . LYS D 1 457 ? 4.166   43.921  89.048  1.00 101.01 ? 457 LYS D CA  1 
ATOM   16096 C C   . LYS D 1 457 ? 4.514   43.688  87.580  1.00 99.67  ? 457 LYS D C   1 
ATOM   16097 O O   . LYS D 1 457 ? 5.562   43.150  87.218  1.00 90.78  ? 457 LYS D O   1 
ATOM   16098 C CB  . LYS D 1 457 ? 5.390   43.981  89.950  1.00 100.13 ? 457 LYS D CB  1 
ATOM   16099 C CG  . LYS D 1 457 ? 5.020   44.140  91.426  1.00 85.08  ? 457 LYS D CG  1 
ATOM   16100 C CD  . LYS D 1 457 ? 6.125   43.692  92.371  1.00 88.05  ? 457 LYS D CD  1 
ATOM   16101 C CE  . LYS D 1 457 ? 6.703   42.345  91.977  1.00 96.74  ? 457 LYS D CE  1 
ATOM   16102 N NZ  . LYS D 1 457 ? 7.987   42.082  92.686  1.00 72.72  ? 457 LYS D NZ  1 
ATOM   16103 N N   . ALA D 1 458 ? 3.591   44.124  86.723  1.00 104.53 ? 458 ALA D N   1 
ATOM   16104 C CA  . ALA D 1 458 ? 3.526   43.901  85.281  1.00 91.06  ? 458 ALA D CA  1 
ATOM   16105 C C   . ALA D 1 458 ? 3.804   45.227  84.561  1.00 79.72  ? 458 ALA D C   1 
ATOM   16106 O O   . ALA D 1 458 ? 4.058   46.224  85.248  1.00 73.78  ? 458 ALA D O   1 
ATOM   16107 C CB  . ALA D 1 458 ? 2.161   43.285  84.966  1.00 83.48  ? 458 ALA D CB  1 
ATOM   16108 N N   . PRO D 1 459 ? 3.830   45.302  83.222  1.00 76.15  ? 459 PRO D N   1 
ATOM   16109 C CA  . PRO D 1 459 ? 4.424   46.487  82.590  1.00 65.00  ? 459 PRO D CA  1 
ATOM   16110 C C   . PRO D 1 459 ? 3.624   47.765  82.805  1.00 63.02  ? 459 PRO D C   1 
ATOM   16111 O O   . PRO D 1 459 ? 2.395   47.756  82.909  1.00 67.83  ? 459 PRO D O   1 
ATOM   16112 C CB  . PRO D 1 459 ? 4.475   46.119  81.100  1.00 70.97  ? 459 PRO D CB  1 
ATOM   16113 C CG  . PRO D 1 459 ? 3.891   44.748  80.978  1.00 73.63  ? 459 PRO D CG  1 
ATOM   16114 C CD  . PRO D 1 459 ? 3.119   44.497  82.213  1.00 76.02  ? 459 PRO D CD  1 
ATOM   16115 N N   . PHE D 1 460 ? 4.362   48.877  82.876  1.00 69.26  ? 460 PHE D N   1 
ATOM   16116 C CA  . PHE D 1 460 ? 3.828   50.246  82.851  1.00 65.37  ? 460 PHE D CA  1 
ATOM   16117 C C   . PHE D 1 460 ? 2.650   50.432  83.810  1.00 53.72  ? 460 PHE D C   1 
ATOM   16118 O O   . PHE D 1 460 ? 1.527   50.726  83.409  1.00 47.63  ? 460 PHE D O   1 
ATOM   16119 C CB  . PHE D 1 460 ? 3.449   50.642  81.424  1.00 60.48  ? 460 PHE D CB  1 
ATOM   16120 C CG  . PHE D 1 460 ? 4.601   50.639  80.460  1.00 63.89  ? 460 PHE D CG  1 
ATOM   16121 C CD1 . PHE D 1 460 ? 5.661   51.516  80.631  1.00 64.38  ? 460 PHE D CD1 1 
ATOM   16122 C CD2 . PHE D 1 460 ? 4.630   49.761  79.391  1.00 58.67  ? 460 PHE D CD2 1 
ATOM   16123 C CE1 . PHE D 1 460 ? 6.728   51.516  79.752  1.00 60.84  ? 460 PHE D CE1 1 
ATOM   16124 C CE2 . PHE D 1 460 ? 5.694   49.758  78.507  1.00 60.23  ? 460 PHE D CE2 1 
ATOM   16125 C CZ  . PHE D 1 460 ? 6.745   50.637  78.689  1.00 62.12  ? 460 PHE D CZ  1 
ATOM   16126 N N   . VAL D 1 461 ? 2.939   50.267  85.103  1.00 52.53  ? 461 VAL D N   1 
ATOM   16127 C CA  . VAL D 1 461 ? 1.928   50.518  86.125  1.00 47.70  ? 461 VAL D CA  1 
ATOM   16128 C C   . VAL D 1 461 ? 1.869   51.981  86.551  1.00 46.76  ? 461 VAL D C   1 
ATOM   16129 O O   . VAL D 1 461 ? 0.858   52.409  87.126  1.00 51.75  ? 461 VAL D O   1 
ATOM   16130 C CB  . VAL D 1 461 ? 2.146   49.630  87.363  1.00 48.68  ? 461 VAL D CB  1 
ATOM   16131 C CG1 . VAL D 1 461 ? 2.482   48.216  86.947  1.00 53.70  ? 461 VAL D CG1 1 
ATOM   16132 C CG2 . VAL D 1 461 ? 3.242   50.202  88.251  1.00 52.89  ? 461 VAL D CG2 1 
ATOM   16133 N N   . GLU D 1 462 ? 2.923   52.759  86.297  1.00 48.28  ? 462 GLU D N   1 
ATOM   16134 C CA  . GLU D 1 462 ? 2.859   54.188  86.581  1.00 47.28  ? 462 GLU D CA  1 
ATOM   16135 C C   . GLU D 1 462 ? 1.944   54.896  85.592  1.00 48.23  ? 462 GLU D C   1 
ATOM   16136 O O   . GLU D 1 462 ? 1.176   55.788  85.972  1.00 55.25  ? 462 GLU D O   1 
ATOM   16137 C CB  . GLU D 1 462 ? 4.262   54.795  86.551  1.00 50.12  ? 462 GLU D CB  1 
ATOM   16138 C CG  . GLU D 1 462 ? 4.442   56.029  87.434  1.00 52.02  ? 462 GLU D CG  1 
ATOM   16139 C CD  . GLU D 1 462 ? 3.845   57.288  86.826  1.00 69.36  ? 462 GLU D CD  1 
ATOM   16140 O OE1 . GLU D 1 462 ? 4.507   57.910  85.968  1.00 61.93  ? 462 GLU D OE1 1 
ATOM   16141 O OE2 . GLU D 1 462 ? 2.720   57.667  87.218  1.00 55.50  ? 462 GLU D OE2 1 
ATOM   16142 N N   . VAL D 1 463 ? 2.005   54.505  84.318  1.00 46.15  ? 463 VAL D N   1 
ATOM   16143 C CA  . VAL D 1 463 ? 1.147   55.116  83.309  1.00 44.71  ? 463 VAL D CA  1 
ATOM   16144 C C   . VAL D 1 463 ? -0.316  54.794  83.584  1.00 41.92  ? 463 VAL D C   1 
ATOM   16145 O O   . VAL D 1 463 ? -1.189  55.661  83.465  1.00 40.12  ? 463 VAL D O   1 
ATOM   16146 C CB  . VAL D 1 463 ? 1.573   54.662  81.902  1.00 57.98  ? 463 VAL D CB  1 
ATOM   16147 C CG1 . VAL D 1 463 ? 0.971   55.575  80.852  1.00 57.86  ? 463 VAL D CG1 1 
ATOM   16148 C CG2 . VAL D 1 463 ? 3.090   54.636  81.789  1.00 68.04  ? 463 VAL D CG2 1 
ATOM   16149 N N   . PHE D 1 464 ? -0.608  53.543  83.952  1.00 41.76  ? 464 PHE D N   1 
ATOM   16150 C CA  . PHE D 1 464 ? -1.985  53.169  84.261  1.00 39.63  ? 464 PHE D CA  1 
ATOM   16151 C C   . PHE D 1 464 ? -2.515  53.935  85.467  1.00 40.40  ? 464 PHE D C   1 
ATOM   16152 O O   . PHE D 1 464 ? -3.702  54.276  85.510  1.00 42.53  ? 464 PHE D O   1 
ATOM   16153 C CB  . PHE D 1 464 ? -2.084  51.661  84.501  1.00 40.03  ? 464 PHE D CB  1 
ATOM   16154 C CG  . PHE D 1 464 ? -2.706  50.903  83.359  1.00 40.04  ? 464 PHE D CG  1 
ATOM   16155 C CD1 . PHE D 1 464 ? -4.081  50.768  83.269  1.00 41.68  ? 464 PHE D CD1 1 
ATOM   16156 C CD2 . PHE D 1 464 ? -1.916  50.323  82.379  1.00 46.12  ? 464 PHE D CD2 1 
ATOM   16157 C CE1 . PHE D 1 464 ? -4.657  50.072  82.221  1.00 47.72  ? 464 PHE D CE1 1 
ATOM   16158 C CE2 . PHE D 1 464 ? -2.488  49.624  81.328  1.00 45.06  ? 464 PHE D CE2 1 
ATOM   16159 C CZ  . PHE D 1 464 ? -3.859  49.501  81.249  1.00 40.49  ? 464 PHE D CZ  1 
ATOM   16160 N N   . ASP D 1 465 ? -1.659  54.211  86.454  1.00 38.55  ? 465 ASP D N   1 
ATOM   16161 C CA  . ASP D 1 465 ? -2.102  54.983  87.611  1.00 41.21  ? 465 ASP D CA  1 
ATOM   16162 C C   . ASP D 1 465 ? -2.295  56.453  87.263  1.00 41.50  ? 465 ASP D C   1 
ATOM   16163 O O   . ASP D 1 465 ? -3.291  57.065  87.668  1.00 41.30  ? 465 ASP D O   1 
ATOM   16164 C CB  . ASP D 1 465 ? -1.112  54.836  88.764  1.00 45.57  ? 465 ASP D CB  1 
ATOM   16165 C CG  . ASP D 1 465 ? -1.571  55.563  90.014  1.00 38.10  ? 465 ASP D CG  1 
ATOM   16166 O OD1 . ASP D 1 465 ? -2.573  55.130  90.619  1.00 38.34  ? 465 ASP D OD1 1 
ATOM   16167 O OD2 . ASP D 1 465 ? -0.937  56.570  90.388  1.00 48.75  ? 465 ASP D OD2 1 
ATOM   16168 N N   . LYS D 1 466 ? -1.351  57.039  86.522  1.00 40.77  ? 466 LYS D N   1 
ATOM   16169 C CA  . LYS D 1 466 ? -1.472  58.447  86.158  1.00 37.35  ? 466 LYS D CA  1 
ATOM   16170 C C   . LYS D 1 466 ? -2.718  58.687  85.318  1.00 39.69  ? 466 LYS D C   1 
ATOM   16171 O O   . LYS D 1 466 ? -3.421  59.688  85.506  1.00 46.50  ? 466 LYS D O   1 
ATOM   16172 C CB  . LYS D 1 466 ? -0.221  58.909  85.408  1.00 39.86  ? 466 LYS D CB  1 
ATOM   16173 C CG  . LYS D 1 466 ? -0.126  60.422  85.255  1.00 41.93  ? 466 LYS D CG  1 
ATOM   16174 C CD  . LYS D 1 466 ? 1.269   60.873  84.840  1.00 59.23  ? 466 LYS D CD  1 
ATOM   16175 C CE  . LYS D 1 466 ? 1.437   60.841  83.331  1.00 62.98  ? 466 LYS D CE  1 
ATOM   16176 N NZ  . LYS D 1 466 ? 2.832   60.503  82.929  1.00 47.33  ? 466 LYS D NZ  1 
ATOM   16177 N N   . LEU D 1 467 ? -3.008  57.777  84.385  1.00 36.31  ? 467 LEU D N   1 
ATOM   16178 C CA  . LEU D 1 467 ? -4.197  57.922  83.554  1.00 34.65  ? 467 LEU D CA  1 
ATOM   16179 C C   . LEU D 1 467 ? -5.470  57.823  84.385  1.00 32.35  ? 467 LEU D C   1 
ATOM   16180 O O   . LEU D 1 467 ? -6.422  58.580  84.163  1.00 36.27  ? 467 LEU D O   1 
ATOM   16181 C CB  . LEU D 1 467 ? -4.191  56.870  82.445  1.00 35.73  ? 467 LEU D CB  1 
ATOM   16182 C CG  . LEU D 1 467 ? -3.431  57.280  81.183  1.00 37.80  ? 467 LEU D CG  1 
ATOM   16183 C CD1 . LEU D 1 467 ? -2.773  56.079  80.521  1.00 39.65  ? 467 LEU D CD1 1 
ATOM   16184 C CD2 . LEU D 1 467 ? -4.363  57.991  80.216  1.00 40.92  ? 467 LEU D CD2 1 
ATOM   16185 N N   . PHE D 1 468 ? -5.506  56.900  85.349  1.00 32.01  ? 468 PHE D N   1 
ATOM   16186 C CA  . PHE D 1 468 ? -6.701  56.749  86.173  1.00 32.18  ? 468 PHE D CA  1 
ATOM   16187 C C   . PHE D 1 468 ? -6.947  57.985  87.029  1.00 29.53  ? 468 PHE D C   1 
ATOM   16188 O O   . PHE D 1 468 ? -8.092  58.430  87.170  1.00 34.09  ? 468 PHE D O   1 
ATOM   16189 C CB  . PHE D 1 468 ? -6.587  55.504  87.053  1.00 33.46  ? 468 PHE D CB  1 
ATOM   16190 C CG  . PHE D 1 468 ? -7.727  55.341  88.020  1.00 28.82  ? 468 PHE D CG  1 
ATOM   16191 C CD1 . PHE D 1 468 ? -8.920  54.771  87.607  1.00 28.95  ? 468 PHE D CD1 1 
ATOM   16192 C CD2 . PHE D 1 468 ? -7.608  55.753  89.339  1.00 31.31  ? 468 PHE D CD2 1 
ATOM   16193 C CE1 . PHE D 1 468 ? -9.974  54.616  88.488  1.00 32.49  ? 468 PHE D CE1 1 
ATOM   16194 C CE2 . PHE D 1 468 ? -8.660  55.602  90.226  1.00 32.22  ? 468 PHE D CE2 1 
ATOM   16195 C CZ  . PHE D 1 468 ? -9.844  55.032  89.799  1.00 34.02  ? 468 PHE D CZ  1 
ATOM   16196 N N   . ARG D 1 469 ? -5.888  58.549  87.614  1.00 32.10  ? 469 ARG D N   1 
ATOM   16197 C CA  . ARG D 1 469 ? -6.048  59.754  88.423  1.00 31.11  ? 469 ARG D CA  1 
ATOM   16198 C C   . ARG D 1 469 ? -6.528  60.926  87.576  1.00 30.96  ? 469 ARG D C   1 
ATOM   16199 O O   . ARG D 1 469 ? -7.327  61.749  88.037  1.00 30.94  ? 469 ARG D O   1 
ATOM   16200 C CB  . ARG D 1 469 ? -4.731  60.098  89.117  1.00 38.58  ? 469 ARG D CB  1 
ATOM   16201 C CG  . ARG D 1 469 ? -4.277  59.078  90.151  1.00 31.91  ? 469 ARG D CG  1 
ATOM   16202 C CD  . ARG D 1 469 ? -5.259  58.977  91.307  1.00 33.53  ? 469 ARG D CD  1 
ATOM   16203 N NE  . ARG D 1 469 ? -4.634  59.313  92.582  1.00 43.58  ? 469 ARG D NE  1 
ATOM   16204 C CZ  . ARG D 1 469 ? -3.847  58.498  93.272  1.00 45.96  ? 469 ARG D CZ  1 
ATOM   16205 N NH1 . ARG D 1 469 ? -3.567  57.278  92.840  1.00 33.21  ? 469 ARG D NH1 1 
ATOM   16206 N NH2 . ARG D 1 469 ? -3.327  58.919  94.423  1.00 44.53  ? 469 ARG D NH2 1 
ATOM   16207 N N   . SER D 1 470 ? -6.041  61.021  86.336  1.00 31.21  ? 470 SER D N   1 
ATOM   16208 C CA  . SER D 1 470 ? -6.423  62.129  85.467  1.00 29.80  ? 470 SER D CA  1 
ATOM   16209 C C   . SER D 1 470 ? -7.910  62.094  85.133  1.00 28.56  ? 470 SER D C   1 
ATOM   16210 O O   . SER D 1 470 ? -8.580  63.133  85.163  1.00 38.11  ? 470 SER D O   1 
ATOM   16211 C CB  . SER D 1 470 ? -5.585  62.104  84.190  1.00 32.19  ? 470 SER D CB  1 
ATOM   16212 O OG  . SER D 1 470 ? -4.321  62.704  84.404  1.00 35.21  ? 470 SER D OG  1 
ATOM   16213 N N   . PHE D 1 471 ? -8.444  60.912  84.811  1.00 28.00  ? 471 PHE D N   1 
ATOM   16214 C CA  . PHE D 1 471 ? -9.872  60.810  84.519  1.00 26.83  ? 471 PHE D CA  1 
ATOM   16215 C C   . PHE D 1 471 ? -10.711 61.119  85.753  1.00 25.89  ? 471 PHE D C   1 
ATOM   16216 O O   . PHE D 1 471 ? -11.790 61.715  85.644  1.00 31.32  ? 471 PHE D O   1 
ATOM   16217 C CB  . PHE D 1 471 ? -10.214 59.422  83.976  1.00 27.13  ? 471 PHE D CB  1 
ATOM   16218 C CG  . PHE D 1 471 ? -9.547  59.096  82.668  1.00 28.95  ? 471 PHE D CG  1 
ATOM   16219 C CD1 . PHE D 1 471 ? -9.589  59.991  81.611  1.00 29.73  ? 471 PHE D CD1 1 
ATOM   16220 C CD2 . PHE D 1 471 ? -8.898  57.886  82.489  1.00 29.96  ? 471 PHE D CD2 1 
ATOM   16221 C CE1 . PHE D 1 471 ? -8.983  59.694  80.407  1.00 31.56  ? 471 PHE D CE1 1 
ATOM   16222 C CE2 . PHE D 1 471 ? -8.289  57.583  81.285  1.00 31.59  ? 471 PHE D CE2 1 
ATOM   16223 C CZ  . PHE D 1 471 ? -8.332  58.489  80.244  1.00 32.46  ? 471 PHE D CZ  1 
ATOM   16224 N N   . VAL D 1 472 ? -10.237 60.716  86.933  1.00 28.29  ? 472 VAL D N   1 
ATOM   16225 C CA  . VAL D 1 472 ? -10.971 60.989  88.164  1.00 24.51  ? 472 VAL D CA  1 
ATOM   16226 C C   . VAL D 1 472 ? -10.928 62.478  88.499  1.00 27.91  ? 472 VAL D C   1 
ATOM   16227 O O   . VAL D 1 472 ? -11.935 63.059  88.923  1.00 35.04  ? 472 VAL D O   1 
ATOM   16228 C CB  . VAL D 1 472 ? -10.420 60.119  89.311  1.00 23.79  ? 472 VAL D CB  1 
ATOM   16229 C CG1 . VAL D 1 472 ? -10.678 60.769  90.660  1.00 22.99  ? 472 VAL D CG1 1 
ATOM   16230 C CG2 . VAL D 1 472 ? -11.039 58.729  89.257  1.00 23.69  ? 472 VAL D CG2 1 
ATOM   16231 N N   . ARG D 1 473 ? -9.770  63.120  88.319  1.00 30.20  ? 473 ARG D N   1 
ATOM   16232 C CA  . ARG D 1 473 ? -9.691  64.562  88.542  1.00 33.14  ? 473 ARG D CA  1 
ATOM   16233 C C   . ARG D 1 473 ? -10.522 65.329  87.519  1.00 29.95  ? 473 ARG D C   1 
ATOM   16234 O O   . ARG D 1 473 ? -11.223 66.285  87.872  1.00 29.38  ? 473 ARG D O   1 
ATOM   16235 C CB  . ARG D 1 473 ? -8.239  65.035  88.504  1.00 31.96  ? 473 ARG D CB  1 
ATOM   16236 C CG  . ARG D 1 473 ? -8.039  66.407  89.133  1.00 31.87  ? 473 ARG D CG  1 
ATOM   16237 C CD  . ARG D 1 473 ? -6.927  67.187  88.453  1.00 39.23  ? 473 ARG D CD  1 
ATOM   16238 N NE  . ARG D 1 473 ? -5.921  66.310  87.867  1.00 46.17  ? 473 ARG D NE  1 
ATOM   16239 C CZ  . ARG D 1 473 ? -4.856  66.731  87.199  1.00 53.24  ? 473 ARG D CZ  1 
ATOM   16240 N NH1 . ARG D 1 473 ? -4.625  68.020  87.004  1.00 49.96  ? 473 ARG D NH1 1 
ATOM   16241 N NH2 . ARG D 1 473 ? -3.999  65.836  86.715  1.00 44.24  ? 473 ARG D NH2 1 
ATOM   16242 N N   . ARG D 1 474 ? -10.455 64.925  86.248  1.00 31.18  ? 474 ARG D N   1 
ATOM   16243 C CA  . ARG D 1 474 ? -11.233 65.592  85.207  1.00 33.58  ? 474 ARG D CA  1 
ATOM   16244 C C   . ARG D 1 474 ? -12.732 65.457  85.450  1.00 33.29  ? 474 ARG D C   1 
ATOM   16245 O O   . ARG D 1 474 ? -13.504 66.356  85.096  1.00 27.28  ? 474 ARG D O   1 
ATOM   16246 C CB  . ARG D 1 474 ? -10.856 65.022  83.838  1.00 29.23  ? 474 ARG D CB  1 
ATOM   16247 C CG  . ARG D 1 474 ? -11.607 65.617  82.652  1.00 29.37  ? 474 ARG D CG  1 
ATOM   16248 C CD  . ARG D 1 474 ? -11.641 67.138  82.685  1.00 33.75  ? 474 ARG D CD  1 
ATOM   16249 N NE  . ARG D 1 474 ? -11.316 67.709  81.384  1.00 44.45  ? 474 ARG D NE  1 
ATOM   16250 C CZ  . ARG D 1 474 ? -12.201 68.270  80.571  1.00 53.40  ? 474 ARG D CZ  1 
ATOM   16251 N NH1 . ARG D 1 474 ? -13.482 68.347  80.893  1.00 44.84  ? 474 ARG D NH1 1 
ATOM   16252 N NH2 . ARG D 1 474 ? -11.789 68.766  79.406  1.00 41.47  ? 474 ARG D NH2 1 
ATOM   16253 N N   . ALA D 1 475 ? -13.161 64.356  86.068  1.00 27.69  ? 475 ALA D N   1 
ATOM   16254 C CA  . ALA D 1 475 ? -14.582 64.104  86.271  1.00 22.16  ? 475 ALA D CA  1 
ATOM   16255 C C   . ALA D 1 475 ? -15.212 65.012  87.318  1.00 23.34  ? 475 ALA D C   1 
ATOM   16256 O O   . ALA D 1 475 ? -16.441 65.003  87.455  1.00 26.64  ? 475 ALA D O   1 
ATOM   16257 C CB  . ALA D 1 475 ? -14.804 62.642  86.662  1.00 21.77  ? 475 ALA D CB  1 
ATOM   16258 N N   . GLN D 1 476 ? -14.418 65.784  88.060  1.00 21.62  ? 476 GLN D N   1 
ATOM   16259 C CA  . GLN D 1 476 ? -14.936 66.627  89.130  1.00 25.21  ? 476 GLN D CA  1 
ATOM   16260 C C   . GLN D 1 476 ? -14.766 68.116  88.843  1.00 29.42  ? 476 GLN D C   1 
ATOM   16261 O O   . GLN D 1 476 ? -14.771 68.927  89.775  1.00 21.95  ? 476 GLN D O   1 
ATOM   16262 C CB  . GLN D 1 476 ? -14.269 66.263  90.457  1.00 19.89  ? 476 GLN D CB  1 
ATOM   16263 C CG  . GLN D 1 476 ? -14.656 64.892  90.986  1.00 24.26  ? 476 GLN D CG  1 
ATOM   16264 C CD  . GLN D 1 476 ? -13.712 64.388  92.060  1.00 30.64  ? 476 GLN D CD  1 
ATOM   16265 O OE1 . GLN D 1 476 ? -14.095 64.242  93.221  1.00 33.81  ? 476 GLN D OE1 1 
ATOM   16266 N NE2 . GLN D 1 476 ? -12.468 64.124  91.678  1.00 29.63  ? 476 GLN D NE2 1 
ATOM   16267 N N   . GLU D 1 477 ? -14.624 68.493  87.576  1.00 32.01  ? 477 GLU D N   1 
ATOM   16268 C CA  . GLU D 1 477 ? -14.377 69.875  87.199  1.00 27.60  ? 477 GLU D CA  1 
ATOM   16269 C C   . GLU D 1 477 ? -15.650 70.556  86.710  1.00 39.68  ? 477 GLU D C   1 
ATOM   16270 O O   . GLU D 1 477 ? -16.561 69.919  86.173  1.00 38.20  ? 477 GLU D O   1 
ATOM   16271 C CB  . GLU D 1 477 ? -13.299 69.967  86.117  1.00 24.36  ? 477 GLU D CB  1 
ATOM   16272 C CG  . GLU D 1 477 ? -11.907 69.568  86.584  1.00 33.34  ? 477 GLU D CG  1 
ATOM   16273 C CD  . GLU D 1 477 ? -10.809 70.291  85.825  1.00 40.35  ? 477 GLU D CD  1 
ATOM   16274 O OE1 . GLU D 1 477 ? -10.892 70.358  84.580  1.00 52.49  ? 477 GLU D OE1 1 
ATOM   16275 O OE2 . GLU D 1 477 ? -9.861  70.786  86.471  1.00 33.72  ? 477 GLU D OE2 1 
ATOM   16276 N N   . LEU D 1 478 ? -15.696 71.868  86.921  1.00 38.40  ? 478 LEU D N   1 
ATOM   16277 C CA  . LEU D 1 478 ? -16.747 72.759  86.442  1.00 23.86  ? 478 LEU D CA  1 
ATOM   16278 C C   . LEU D 1 478 ? -16.400 73.234  85.030  1.00 32.31  ? 478 LEU D C   1 
ATOM   16279 O O   . LEU D 1 478 ? -15.607 72.593  84.335  1.00 36.17  ? 478 LEU D O   1 
ATOM   16280 C CB  . LEU D 1 478 ? -16.931 73.921  87.422  1.00 23.52  ? 478 LEU D CB  1 
ATOM   16281 C CG  . LEU D 1 478 ? -16.798 73.635  88.918  1.00 22.05  ? 478 LEU D CG  1 
ATOM   16282 C CD1 . LEU D 1 478 ? -16.999 74.901  89.730  1.00 22.28  ? 478 LEU D CD1 1 
ATOM   16283 C CD2 . LEU D 1 478 ? -17.786 72.576  89.366  1.00 28.45  ? 478 LEU D CD2 1 
ATOM   16284 N N   . GLU D 1 479 ? -17.019 74.326  84.567  1.00 32.16  ? 479 GLU D N   1 
ATOM   16285 C CA  . GLU D 1 479 ? -16.606 74.983  83.321  1.00 29.11  ? 479 GLU D CA  1 
ATOM   16286 C C   . GLU D 1 479 ? -16.279 76.470  83.562  1.00 30.12  ? 479 GLU D C   1 
ATOM   16287 O O   . GLU D 1 479 ? -17.169 77.325  83.568  1.00 30.64  ? 479 GLU D O   1 
ATOM   16288 C CB  . GLU D 1 479 ? -17.659 74.785  82.236  1.00 30.25  ? 479 GLU D CB  1 
ATOM   16289 C CG  . GLU D 1 479 ? -19.111 75.050  82.618  1.00 38.30  ? 479 GLU D CG  1 
ATOM   16290 C CD  . GLU D 1 479 ? -19.602 76.426  82.185  1.00 36.22  ? 479 GLU D CD  1 
ATOM   16291 O OE1 . GLU D 1 479 ? -19.621 76.705  80.969  1.00 33.80  ? 479 GLU D OE1 1 
ATOM   16292 O OE2 . GLU D 1 479 ? -19.985 77.228  83.066  1.00 31.03  ? 479 GLU D OE2 1 
ATOM   16293 N N   . HIS D 1 480 ? -14.980 76.762  83.731  1.00 35.10  ? 480 HIS D N   1 
ATOM   16294 C CA  . HIS D 1 480 ? -14.364 78.062  83.471  1.00 34.91  ? 480 HIS D CA  1 
ATOM   16295 C C   . HIS D 1 480 ? -14.921 79.197  84.341  1.00 32.17  ? 480 HIS D C   1 
ATOM   16296 O O   . HIS D 1 480 ? -15.701 80.043  83.898  1.00 36.35  ? 480 HIS D O   1 
ATOM   16297 C CB  . HIS D 1 480 ? -14.468 78.398  81.984  1.00 39.79  ? 480 HIS D CB  1 
ATOM   16298 C CG  . HIS D 1 480 ? -13.155 78.317  81.258  1.00 56.70  ? 480 HIS D CG  1 
ATOM   16299 N ND1 . HIS D 1 480 ? -12.083 79.118  81.584  1.00 51.61  ? 480 HIS D ND1 1 
ATOM   16300 C CD2 . HIS D 1 480 ? -12.737 77.546  80.228  1.00 62.54  ? 480 HIS D CD2 1 
ATOM   16301 C CE1 . HIS D 1 480 ? -11.061 78.849  80.793  1.00 52.88  ? 480 HIS D CE1 1 
ATOM   16302 N NE2 . HIS D 1 480 ? -11.433 77.898  79.959  1.00 58.24  ? 480 HIS D NE2 1 
ATOM   16303 N N   . HIS D 1 481 ? -14.518 79.166  85.609  1.00 30.69  ? 481 HIS D N   1 
ATOM   16304 C CA  . HIS D 1 481 ? -14.989 80.089  86.642  1.00 30.12  ? 481 HIS D CA  1 
ATOM   16305 C C   . HIS D 1 481 ? -13.808 80.744  87.357  1.00 30.62  ? 481 HIS D C   1 
ATOM   16306 O O   . HIS D 1 481 ? -12.643 80.433  87.099  1.00 40.07  ? 481 HIS D O   1 
ATOM   16307 C CB  . HIS D 1 481 ? -15.829 79.328  87.663  1.00 27.85  ? 481 HIS D CB  1 
ATOM   16308 C CG  . HIS D 1 481 ? -15.136 78.103  88.162  1.00 26.55  ? 481 HIS D CG  1 
ATOM   16309 N ND1 . HIS D 1 481 ? -14.274 78.124  89.238  1.00 26.01  ? 481 HIS D ND1 1 
ATOM   16310 C CD2 . HIS D 1 481 ? -15.107 76.839  87.680  1.00 27.29  ? 481 HIS D CD2 1 
ATOM   16311 C CE1 . HIS D 1 481 ? -13.782 76.912  89.426  1.00 31.93  ? 481 HIS D CE1 1 
ATOM   16312 N NE2 . HIS D 1 481 ? -14.270 76.114  88.493  1.00 27.12  ? 481 HIS D NE2 1 
ATOM   16313 N N   . HIS D 1 482 ? -14.132 81.656  88.275  1.00 30.38  ? 482 HIS D N   1 
ATOM   16314 C CA  . HIS D 1 482 ? -13.204 82.168  89.277  1.00 30.51  ? 482 HIS D CA  1 
ATOM   16315 C C   . HIS D 1 482 ? -14.013 82.757  90.425  1.00 29.51  ? 482 HIS D C   1 
ATOM   16316 O O   . HIS D 1 482 ? -15.206 83.029  90.288  1.00 29.24  ? 482 HIS D O   1 
ATOM   16317 C CB  . HIS D 1 482 ? -12.245 83.225  88.712  1.00 32.97  ? 482 HIS D CB  1 
ATOM   16318 C CG  . HIS D 1 482 ? -12.813 84.610  88.674  1.00 34.24  ? 482 HIS D CG  1 
ATOM   16319 N ND1 . HIS D 1 482 ? -13.511 85.103  87.592  1.00 36.40  ? 482 HIS D ND1 1 
ATOM   16320 C CD2 . HIS D 1 482 ? -12.775 85.611  89.585  1.00 34.55  ? 482 HIS D CD2 1 
ATOM   16321 C CE1 . HIS D 1 482 ? -13.876 86.349  87.839  1.00 36.76  ? 482 HIS D CE1 1 
ATOM   16322 N NE2 . HIS D 1 482 ? -13.444 86.680  89.042  1.00 36.07  ? 482 HIS D NE2 1 
ATOM   16323 N N   . HIS D 1 483 ? -13.349 82.959  91.560  1.00 29.31  ? 483 HIS D N   1 
ATOM   16324 C CA  . HIS D 1 483 ? -14.001 83.526  92.736  1.00 28.46  ? 483 HIS D CA  1 
ATOM   16325 C C   . HIS D 1 483 ? -14.211 85.031  92.601  1.00 31.07  ? 483 HIS D C   1 
ATOM   16326 O O   . HIS D 1 483 ? -14.534 85.710  93.576  1.00 29.93  ? 483 HIS D O   1 
ATOM   16327 C CB  . HIS D 1 483 ? -13.188 83.228  93.996  1.00 30.78  ? 483 HIS D CB  1 
ATOM   16328 C CG  . HIS D 1 483 ? -13.840 82.247  94.918  1.00 28.33  ? 483 HIS D CG  1 
ATOM   16329 N ND1 . HIS D 1 483 ? -14.668 82.632  95.950  1.00 29.62  ? 483 HIS D ND1 1 
ATOM   16330 C CD2 . HIS D 1 483 ? -13.789 80.894  94.961  1.00 29.59  ? 483 HIS D CD2 1 
ATOM   16331 C CE1 . HIS D 1 483 ? -15.099 81.560  96.590  1.00 30.30  ? 483 HIS D CE1 1 
ATOM   16332 N NE2 . HIS D 1 483 ? -14.581 80.491  96.010  1.00 27.72  ? 483 HIS D NE2 1 
HETATM 16333 O O   . HOH E 2 .   ? 8.762   -8.255  24.797  1.00 39.14  ? 501 HOH A O   1 
HETATM 16334 O O   . HOH E 2 .   ? 14.930  12.290  9.647   1.00 8.46   ? 502 HOH A O   1 
HETATM 16335 O O   . HOH E 2 .   ? -10.705 14.644  24.124  1.00 21.70  ? 503 HOH A O   1 
HETATM 16336 O O   . HOH E 2 .   ? -1.859  -7.975  18.246  1.00 17.03  ? 504 HOH A O   1 
HETATM 16337 O O   . HOH E 2 .   ? 36.902  16.718  21.724  1.00 22.91  ? 505 HOH A O   1 
HETATM 16338 O O   . HOH E 2 .   ? 23.792  -14.402 -21.655 1.00 25.67  ? 506 HOH A O   1 
HETATM 16339 O O   . HOH E 2 .   ? -1.911  -12.098 13.726  1.00 17.95  ? 507 HOH A O   1 
HETATM 16340 O O   . HOH E 2 .   ? 24.207  -0.540  18.532  1.00 19.30  ? 508 HOH A O   1 
HETATM 16341 O O   . HOH E 2 .   ? 0.495   9.727   -25.677 1.00 25.11  ? 509 HOH A O   1 
HETATM 16342 O O   . HOH E 2 .   ? -7.436  3.931   6.015   1.00 17.24  ? 510 HOH A O   1 
HETATM 16343 O O   . HOH E 2 .   ? 24.169  -22.682 -14.293 1.00 14.47  ? 511 HOH A O   1 
HETATM 16344 O O   . HOH E 2 .   ? -18.062 18.805  -5.484  1.00 24.63  ? 512 HOH A O   1 
HETATM 16345 O O   . HOH E 2 .   ? 9.553   2.235   17.867  1.00 9.93   ? 513 HOH A O   1 
HETATM 16346 O O   . HOH E 2 .   ? 29.648  1.942   30.219  1.00 23.61  ? 514 HOH A O   1 
HETATM 16347 O O   . HOH E 2 .   ? 6.708   -19.702 15.861  1.00 31.23  ? 515 HOH A O   1 
HETATM 16348 O O   . HOH E 2 .   ? 9.551   -21.144 15.601  1.00 16.81  ? 516 HOH A O   1 
HETATM 16349 O O   . HOH E 2 .   ? 32.129  -0.624  -2.041  1.00 27.05  ? 517 HOH A O   1 
HETATM 16350 O O   . HOH E 2 .   ? 12.895  -20.352 -9.807  1.00 28.56  ? 518 HOH A O   1 
HETATM 16351 O O   . HOH E 2 .   ? 42.767  12.310  -2.640  1.00 30.27  ? 519 HOH A O   1 
HETATM 16352 O O   . HOH E 2 .   ? 13.271  25.365  22.586  1.00 35.10  ? 520 HOH A O   1 
HETATM 16353 O O   . HOH E 2 .   ? -2.220  10.795  -8.779  1.00 10.33  ? 521 HOH A O   1 
HETATM 16354 O O   . HOH E 2 .   ? 10.923  -3.873  -9.569  1.00 40.23  ? 522 HOH A O   1 
HETATM 16355 O O   . HOH E 2 .   ? -1.752  3.264   23.780  1.00 14.53  ? 523 HOH A O   1 
HETATM 16356 O O   . HOH E 2 .   ? -11.435 -0.273  22.202  1.00 28.31  ? 524 HOH A O   1 
HETATM 16357 O O   . HOH E 2 .   ? -2.478  -8.265  21.502  1.00 26.33  ? 525 HOH A O   1 
HETATM 16358 O O   . HOH E 2 .   ? -2.557  10.507  31.924  1.00 24.86  ? 526 HOH A O   1 
HETATM 16359 O O   . HOH E 2 .   ? 3.789   24.355  19.286  1.00 13.06  ? 527 HOH A O   1 
HETATM 16360 O O   . HOH E 2 .   ? 7.422   8.443   -8.679  1.00 17.14  ? 528 HOH A O   1 
HETATM 16361 O O   . HOH E 2 .   ? 14.685  11.643  5.958   1.00 13.95  ? 529 HOH A O   1 
HETATM 16362 O O   . HOH E 2 .   ? 0.727   -15.232 11.534  1.00 23.08  ? 530 HOH A O   1 
HETATM 16363 O O   . HOH E 2 .   ? 1.453   -10.032 17.953  1.00 23.48  ? 531 HOH A O   1 
HETATM 16364 O O   . HOH E 2 .   ? -4.881  6.399   8.558   1.00 16.13  ? 532 HOH A O   1 
HETATM 16365 O O   . HOH E 2 .   ? 32.565  -16.690 -1.781  1.00 12.33  ? 533 HOH A O   1 
HETATM 16366 O O   . HOH E 2 .   ? 0.897   -6.593  -20.016 1.00 25.20  ? 534 HOH A O   1 
HETATM 16367 O O   . HOH E 2 .   ? -1.147  -16.866 5.285   1.00 15.32  ? 535 HOH A O   1 
HETATM 16368 O O   . HOH E 2 .   ? -12.561 3.844   11.910  1.00 16.06  ? 536 HOH A O   1 
HETATM 16369 O O   . HOH E 2 .   ? 28.259  16.015  2.929   1.00 35.06  ? 537 HOH A O   1 
HETATM 16370 O O   . HOH E 2 .   ? 44.966  -2.412  21.999  1.00 23.93  ? 538 HOH A O   1 
HETATM 16371 O O   . HOH E 2 .   ? 1.706   -11.183 9.978   1.00 21.75  ? 539 HOH A O   1 
HETATM 16372 O O   . HOH E 2 .   ? -3.471  -8.645  -15.166 1.00 29.36  ? 540 HOH A O   1 
HETATM 16373 O O   . HOH E 2 .   ? 10.839  2.206   1.267   1.00 17.09  ? 541 HOH A O   1 
HETATM 16374 O O   . HOH E 2 .   ? 19.310  -12.047 14.574  1.00 19.35  ? 542 HOH A O   1 
HETATM 16375 O O   . HOH E 2 .   ? -9.712  -10.515 -12.785 1.00 29.22  ? 543 HOH A O   1 
HETATM 16376 O O   . HOH E 2 .   ? 16.582  5.097   17.799  1.00 8.17   ? 544 HOH A O   1 
HETATM 16377 O O   . HOH E 2 .   ? -9.443  -14.098 -7.623  1.00 26.33  ? 545 HOH A O   1 
HETATM 16378 O O   . HOH E 2 .   ? -21.010 7.744   15.372  1.00 28.79  ? 546 HOH A O   1 
HETATM 16379 O O   . HOH E 2 .   ? 15.281  14.046  18.562  1.00 13.79  ? 547 HOH A O   1 
HETATM 16380 O O   . HOH E 2 .   ? 48.689  -4.942  3.883   1.00 34.94  ? 548 HOH A O   1 
HETATM 16381 O O   . HOH E 2 .   ? -6.983  21.611  10.458  1.00 25.11  ? 549 HOH A O   1 
HETATM 16382 O O   . HOH E 2 .   ? 4.404   -9.230  -17.187 1.00 23.98  ? 550 HOH A O   1 
HETATM 16383 O O   . HOH E 2 .   ? -0.625  21.120  16.054  1.00 21.93  ? 551 HOH A O   1 
HETATM 16384 O O   . HOH E 2 .   ? -20.697 -11.498 -2.132  1.00 29.46  ? 552 HOH A O   1 
HETATM 16385 O O   . HOH E 2 .   ? 0.725   -10.491 15.948  1.00 21.01  ? 553 HOH A O   1 
HETATM 16386 O O   . HOH E 2 .   ? 17.902  3.975   18.381  1.00 12.79  ? 554 HOH A O   1 
HETATM 16387 O O   . HOH E 2 .   ? 26.101  -22.292 -13.545 1.00 22.81  ? 555 HOH A O   1 
HETATM 16388 O O   . HOH E 2 .   ? 27.070  -21.776 -15.530 1.00 20.79  ? 556 HOH A O   1 
HETATM 16389 O O   . HOH E 2 .   ? 27.223  -21.218 -12.005 1.00 24.19  ? 557 HOH A O   1 
HETATM 16390 O O   . HOH E 2 .   ? 5.075   -20.394 16.904  1.00 24.71  ? 558 HOH A O   1 
HETATM 16391 O O   . HOH E 2 .   ? -12.584 -10.036 4.204   1.00 16.56  ? 559 HOH A O   1 
HETATM 16392 O O   . HOH E 2 .   ? -10.144 -10.958 5.622   1.00 19.36  ? 560 HOH A O   1 
HETATM 16393 O O   . HOH E 2 .   ? 15.631  14.069  5.330   1.00 26.33  ? 561 HOH A O   1 
HETATM 16394 O O   . HOH E 2 .   ? 28.656  -20.998 -17.072 1.00 28.10  ? 562 HOH A O   1 
HETATM 16395 O O   . HOH E 2 .   ? 27.579  -24.112 -13.035 1.00 28.21  ? 563 HOH A O   1 
HETATM 16396 O O   . HOH E 2 .   ? 30.955  -21.284 -10.533 1.00 30.39  ? 564 HOH A O   1 
HETATM 16397 O O   . HOH E 2 .   ? 32.188  -22.647 -11.771 1.00 43.18  ? 565 HOH A O   1 
HETATM 16398 O O   . HOH F 2 .   ? -19.369 35.919  43.237  1.00 30.23  ? 501 HOH B O   1 
HETATM 16399 O O   . HOH F 2 .   ? 0.986   55.336  21.655  1.00 19.67  ? 502 HOH B O   1 
HETATM 16400 O O   . HOH F 2 .   ? -7.610  56.506  33.521  1.00 30.55  ? 503 HOH B O   1 
HETATM 16401 O O   . HOH F 2 .   ? -41.182 24.038  24.923  1.00 32.16  ? 504 HOH B O   1 
HETATM 16402 O O   . HOH F 2 .   ? 8.874   51.721  8.736   1.00 45.30  ? 505 HOH B O   1 
HETATM 16403 O O   . HOH F 2 .   ? -23.323 34.597  17.973  1.00 20.00  ? 506 HOH B O   1 
HETATM 16404 O O   . HOH F 2 .   ? -0.677  31.981  5.425   1.00 16.19  ? 507 HOH B O   1 
HETATM 16405 O O   . HOH F 2 .   ? -0.767  38.603  35.008  1.00 12.61  ? 508 HOH B O   1 
HETATM 16406 O O   . HOH F 2 .   ? 4.348   37.479  -0.343  1.00 19.29  ? 509 HOH B O   1 
HETATM 16407 O O   . HOH F 2 .   ? 15.885  48.585  12.644  1.00 26.84  ? 510 HOH B O   1 
HETATM 16408 O O   . HOH F 2 .   ? 0.335   42.307  43.182  1.00 25.43  ? 511 HOH B O   1 
HETATM 16409 O O   . HOH F 2 .   ? -47.390 20.259  28.121  1.00 36.42  ? 512 HOH B O   1 
HETATM 16410 O O   . HOH F 2 .   ? 3.500   31.513  10.676  1.00 18.08  ? 513 HOH B O   1 
HETATM 16411 O O   . HOH F 2 .   ? -25.114 60.228  1.122   1.00 26.33  ? 514 HOH B O   1 
HETATM 16412 O O   . HOH F 2 .   ? -43.951 26.821  39.315  1.00 32.67  ? 515 HOH B O   1 
HETATM 16413 O O   . HOH F 2 .   ? -15.239 39.894  39.543  1.00 15.97  ? 516 HOH B O   1 
HETATM 16414 O O   . HOH F 2 .   ? -12.196 23.330  36.115  1.00 16.13  ? 517 HOH B O   1 
HETATM 16415 O O   . HOH F 2 .   ? 5.744   33.070  26.988  1.00 16.68  ? 518 HOH B O   1 
HETATM 16416 O O   . HOH F 2 .   ? -23.763 26.077  10.565  1.00 36.67  ? 519 HOH B O   1 
HETATM 16417 O O   . HOH F 2 .   ? 11.540  24.768  13.917  1.00 31.24  ? 520 HOH B O   1 
HETATM 16418 O O   . HOH F 2 .   ? -25.248 28.524  38.365  1.00 20.58  ? 521 HOH B O   1 
HETATM 16419 O O   . HOH F 2 .   ? -8.187  38.314  18.575  1.00 12.06  ? 522 HOH B O   1 
HETATM 16420 O O   . HOH F 2 .   ? -44.365 46.415  30.160  1.00 30.43  ? 523 HOH B O   1 
HETATM 16421 O O   . HOH F 2 .   ? -27.894 37.669  1.750   1.00 22.39  ? 524 HOH B O   1 
HETATM 16422 O O   . HOH F 2 .   ? -8.826  31.528  20.683  1.00 21.80  ? 525 HOH B O   1 
HETATM 16423 O O   . HOH F 2 .   ? -1.557  53.857  34.230  1.00 22.19  ? 526 HOH B O   1 
HETATM 16424 O O   . HOH F 2 .   ? -17.555 54.596  32.501  1.00 19.62  ? 527 HOH B O   1 
HETATM 16425 O O   . HOH F 2 .   ? -18.313 25.636  44.615  1.00 27.82  ? 528 HOH B O   1 
HETATM 16426 O O   . HOH F 2 .   ? -18.775 52.433  16.199  1.00 31.67  ? 529 HOH B O   1 
HETATM 16427 O O   . HOH F 2 .   ? 14.336  49.433  34.036  1.00 23.53  ? 530 HOH B O   1 
HETATM 16428 O O   . HOH F 2 .   ? 14.127  36.056  12.148  1.00 19.82  ? 531 HOH B O   1 
HETATM 16429 O O   . HOH F 2 .   ? -10.806 49.765  44.611  1.00 36.00  ? 532 HOH B O   1 
HETATM 16430 O O   . HOH F 2 .   ? -0.105  60.036  25.135  1.00 21.23  ? 533 HOH B O   1 
HETATM 16431 O O   . HOH F 2 .   ? -7.167  39.896  49.260  1.00 26.33  ? 534 HOH B O   1 
HETATM 16432 O O   . HOH F 2 .   ? 7.121   51.570  27.170  1.00 19.78  ? 535 HOH B O   1 
HETATM 16433 O O   . HOH F 2 .   ? 15.155  48.015  10.877  1.00 25.64  ? 536 HOH B O   1 
HETATM 16434 O O   . HOH F 2 .   ? -10.099 31.731  18.839  1.00 41.63  ? 537 HOH B O   1 
HETATM 16435 O O   . HOH F 2 .   ? -17.201 55.261  11.288  1.00 21.71  ? 538 HOH B O   1 
HETATM 16436 O O   . HOH F 2 .   ? -7.214  30.229  19.825  1.00 35.72  ? 539 HOH B O   1 
HETATM 16437 O O   . HOH F 2 .   ? -28.722 38.030  0.096   1.00 28.91  ? 540 HOH B O   1 
HETATM 16438 O O   . HOH F 2 .   ? -19.670 55.242  11.713  1.00 26.03  ? 541 HOH B O   1 
HETATM 16439 O O   . HOH G 2 .   ? 22.325  1.272   88.138  1.00 26.74  ? 501 HOH C O   1 
HETATM 16440 O O   . HOH G 2 .   ? 5.088   8.172   59.153  1.00 26.33  ? 502 HOH C O   1 
HETATM 16441 O O   . HOH G 2 .   ? 31.727  6.635   39.396  1.00 35.11  ? 503 HOH C O   1 
HETATM 16442 O O   . HOH G 2 .   ? 4.999   5.557   36.479  1.00 32.89  ? 504 HOH C O   1 
HETATM 16443 O O   . HOH G 2 .   ? 23.832  7.977   38.951  1.00 29.60  ? 505 HOH C O   1 
HETATM 16444 O O   . HOH G 2 .   ? 17.984  -20.457 57.570  1.00 34.25  ? 506 HOH C O   1 
HETATM 16445 O O   . HOH G 2 .   ? 33.694  -0.300  73.957  1.00 27.44  ? 507 HOH C O   1 
HETATM 16446 O O   . HOH G 2 .   ? 34.869  -9.872  76.116  1.00 35.24  ? 508 HOH C O   1 
HETATM 16447 O O   . HOH G 2 .   ? 12.549  -3.702  35.775  1.00 31.59  ? 509 HOH C O   1 
HETATM 16448 O O   . HOH G 2 .   ? 6.246   13.944  36.025  1.00 40.24  ? 510 HOH C O   1 
HETATM 16449 O O   . HOH G 2 .   ? 7.654   -25.223 54.329  1.00 35.47  ? 511 HOH C O   1 
HETATM 16450 O O   . HOH G 2 .   ? 26.998  -20.918 81.501  1.00 29.61  ? 512 HOH C O   1 
HETATM 16451 O O   . HOH G 2 .   ? -20.961 -4.926  57.981  1.00 59.97  ? 513 HOH C O   1 
HETATM 16452 O O   . HOH G 2 .   ? 2.438   16.726  48.728  1.00 41.66  ? 514 HOH C O   1 
HETATM 16453 O O   . HOH G 2 .   ? -0.717  -18.596 61.469  1.00 15.91  ? 515 HOH C O   1 
HETATM 16454 O O   . HOH G 2 .   ? 17.870  -17.215 82.761  1.00 15.31  ? 516 HOH C O   1 
HETATM 16455 O O   . HOH G 2 .   ? 41.215  4.217   49.237  1.00 43.25  ? 517 HOH C O   1 
HETATM 16456 O O   . HOH G 2 .   ? 17.485  -48.120 78.310  1.00 36.28  ? 518 HOH C O   1 
HETATM 16457 O O   . HOH G 2 .   ? 15.114  21.018  50.743  1.00 32.98  ? 519 HOH C O   1 
HETATM 16458 O O   . HOH G 2 .   ? 25.606  -10.598 86.101  1.00 16.08  ? 520 HOH C O   1 
HETATM 16459 O O   . HOH G 2 .   ? -5.912  5.969   49.162  1.00 35.95  ? 521 HOH C O   1 
HETATM 16460 O O   . HOH G 2 .   ? 3.318   -8.247  81.152  1.00 31.83  ? 522 HOH C O   1 
HETATM 16461 O O   . HOH G 2 .   ? 6.310   -24.121 41.731  1.00 25.36  ? 523 HOH C O   1 
HETATM 16462 O O   . HOH G 2 .   ? 37.386  -14.933 66.349  1.00 26.33  ? 524 HOH C O   1 
HETATM 16463 O O   . HOH G 2 .   ? 36.609  8.266   67.919  1.00 30.18  ? 525 HOH C O   1 
HETATM 16464 O O   . HOH G 2 .   ? 15.852  -34.766 71.599  1.00 13.79  ? 526 HOH C O   1 
HETATM 16465 O O   . HOH G 2 .   ? 15.081  4.561   62.028  1.00 17.50  ? 527 HOH C O   1 
HETATM 16466 O O   . HOH G 2 .   ? 19.284  4.293   82.685  1.00 24.90  ? 528 HOH C O   1 
HETATM 16467 O O   . HOH G 2 .   ? 33.523  18.204  58.741  1.00 26.72  ? 529 HOH C O   1 
HETATM 16468 O O   . HOH G 2 .   ? 14.352  -8.671  85.229  1.00 16.29  ? 530 HOH C O   1 
HETATM 16469 O O   . HOH G 2 .   ? 28.322  -20.724 79.209  1.00 29.79  ? 531 HOH C O   1 
HETATM 16470 O O   . HOH G 2 .   ? 25.537  7.353   37.170  1.00 30.60  ? 532 HOH C O   1 
HETATM 16471 O O   . HOH H 2 .   ? -5.275  60.954  93.671  1.00 39.25  ? 501 HOH D O   1 
HETATM 16472 O O   . HOH H 2 .   ? -5.409  62.740  71.229  1.00 49.44  ? 502 HOH D O   1 
HETATM 16473 O O   . HOH H 2 .   ? -17.303 47.337  103.165 1.00 33.14  ? 503 HOH D O   1 
HETATM 16474 O O   . HOH H 2 .   ? -16.644 86.241  94.122  1.00 23.03  ? 504 HOH D O   1 
HETATM 16475 O O   . HOH H 2 .   ? -24.099 36.329  52.971  1.00 38.96  ? 505 HOH D O   1 
HETATM 16476 O O   . HOH H 2 .   ? -2.209  66.550  85.529  1.00 20.80  ? 506 HOH D O   1 
HETATM 16477 O O   . HOH H 2 .   ? -8.738  61.557  77.349  1.00 28.93  ? 507 HOH D O   1 
HETATM 16478 O O   . HOH H 2 .   ? 33.352  51.926  76.847  1.00 34.59  ? 508 HOH D O   1 
HETATM 16479 O O   . HOH H 2 .   ? -10.854 52.741  60.358  1.00 48.19  ? 509 HOH D O   1 
HETATM 16480 O O   . HOH H 2 .   ? -4.516  45.756  107.641 1.00 31.50  ? 510 HOH D O   1 
HETATM 16481 O O   . HOH H 2 .   ? -33.331 35.681  73.106  1.00 41.66  ? 511 HOH D O   1 
HETATM 16482 O O   . HOH H 2 .   ? -14.010 86.362  96.089  1.00 23.53  ? 512 HOH D O   1 
HETATM 16483 O O   . HOH H 2 .   ? -25.785 36.483  57.147  1.00 44.45  ? 513 HOH D O   1 
HETATM 16484 O O   . HOH H 2 .   ? -25.270 51.485  99.622  1.00 24.96  ? 514 HOH D O   1 
HETATM 16485 O O   . HOH H 2 .   ? -5.100  37.769  50.655  1.00 28.94  ? 515 HOH D O   1 
HETATM 16486 O O   . HOH H 2 .   ? -23.774 51.860  103.166 1.00 13.86  ? 516 HOH D O   1 
HETATM 16487 O O   . HOH H 2 .   ? -20.393 47.753  100.301 1.00 15.31  ? 517 HOH D O   1 
HETATM 16488 O O   . HOH H 2 .   ? -6.031  19.363  77.865  1.00 30.77  ? 518 HOH D O   1 
HETATM 16489 O O   . HOH H 2 .   ? 15.630  33.075  74.780  1.00 28.34  ? 519 HOH D O   1 
HETATM 16490 O O   . HOH H 2 .   ? -10.899 29.784  91.051  1.00 19.34  ? 520 HOH D O   1 
HETATM 16491 O O   . HOH H 2 .   ? 15.174  68.854  69.275  1.00 33.05  ? 521 HOH D O   1 
HETATM 16492 O O   . HOH H 2 .   ? -21.350 22.729  83.427  1.00 38.38  ? 522 HOH D O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . MET A 1   ? 0.6381 0.6568 0.5535 0.0384  0.0732  -0.1142 1   MET A N   
2     C CA  . MET A 1   ? 0.6364 0.6369 0.5541 0.0435  0.0624  -0.1139 1   MET A CA  
3     C C   . MET A 1   ? 0.5488 0.5406 0.4763 0.0471  0.0543  -0.1052 1   MET A C   
4     O O   . MET A 1   ? 0.7213 0.7080 0.6313 0.0410  0.0532  -0.0902 1   MET A O   
5     C CB  . MET A 1   ? 0.5940 0.5830 0.4808 0.0377  0.0597  -0.1082 1   MET A CB  
6     C CG  . MET A 1   ? 0.5468 0.5184 0.4356 0.0410  0.0485  -0.1070 1   MET A CG  
7     S SD  . MET A 1   ? 0.8422 0.8039 0.7031 0.0341  0.0464  -0.1058 1   MET A SD  
8     C CE  . MET A 1   ? 0.6028 0.5661 0.4387 0.0218  0.0478  -0.0890 1   MET A CE  
9     N N   . LYS A 2   ? 0.3733 0.3600 0.3298 0.0557  0.0465  -0.1092 2   LYS A N   
10    C CA  . LYS A 2   ? 0.3150 0.2882 0.2806 0.0565  0.0351  -0.0933 2   LYS A CA  
11    C C   . LYS A 2   ? 0.3589 0.3142 0.3053 0.0547  0.0259  -0.0848 2   LYS A C   
12    O O   . LYS A 2   ? 0.4178 0.3672 0.3599 0.0574  0.0232  -0.0940 2   LYS A O   
13    C CB  . LYS A 2   ? 0.3772 0.3493 0.3787 0.0649  0.0277  -0.0982 2   LYS A CB  
14    C CG  . LYS A 2   ? 0.2960 0.2556 0.3068 0.0644  0.0154  -0.0816 2   LYS A CG  
15    C CD  . LYS A 2   ? 0.3289 0.2912 0.3760 0.0709  0.0090  -0.0843 2   LYS A CD  
16    C CE  . LYS A 2   ? 0.3009 0.2467 0.3569 0.0715  -0.0064 -0.0725 2   LYS A CE  
17    N NZ  . LYS A 2   ? 0.2952 0.2426 0.3821 0.0749  -0.0140 -0.0733 2   LYS A NZ  
18    N N   . LYS A 3   ? 0.3395 0.2868 0.2753 0.0500  0.0213  -0.0680 3   LYS A N   
19    C CA  . LYS A 3   ? 0.3461 0.2789 0.2627 0.0474  0.0139  -0.0593 3   LYS A CA  
20    C C   . LYS A 3   ? 0.2977 0.2196 0.2264 0.0483  0.0026  -0.0476 3   LYS A C   
21    O O   . LYS A 3   ? 0.2342 0.1597 0.1792 0.0483  0.0013  -0.0420 3   LYS A O   
22    C CB  . LYS A 3   ? 0.3867 0.3200 0.2755 0.0399  0.0191  -0.0501 3   LYS A CB  
23    C CG  . LYS A 3   ? 0.3825 0.3187 0.2485 0.0370  0.0245  -0.0574 3   LYS A CG  
24    C CD  . LYS A 3   ? 0.4203 0.3634 0.2674 0.0283  0.0313  -0.0487 3   LYS A CD  
25    C CE  . LYS A 3   ? 0.6124 0.5685 0.4497 0.0216  0.0352  -0.0539 3   LYS A CE  
26    N NZ  . LYS A 3   ? 0.6434 0.5919 0.4746 0.0206  0.0270  -0.0514 3   LYS A NZ  
27    N N   . LEU A 4   ? 0.2766 0.1862 0.1967 0.0483  -0.0057 -0.0441 4   LEU A N   
28    C CA  . LEU A 4   ? 0.2526 0.1528 0.1756 0.0464  -0.0152 -0.0313 4   LEU A CA  
29    C C   . LEU A 4   ? 0.3201 0.2164 0.2187 0.0410  -0.0140 -0.0219 4   LEU A C   
30    O O   . LEU A 4   ? 0.3282 0.2214 0.2092 0.0403  -0.0130 -0.0249 4   LEU A O   
31    C CB  . LEU A 4   ? 0.2666 0.1567 0.1994 0.0496  -0.0260 -0.0337 4   LEU A CB  
32    C CG  . LEU A 4   ? 0.1976 0.0836 0.1336 0.0448  -0.0352 -0.0203 4   LEU A CG  
33    C CD1 . LEU A 4   ? 0.3503 0.2414 0.3106 0.0434  -0.0423 -0.0201 4   LEU A CD1 
34    C CD2 . LEU A 4   ? 0.1855 0.0669 0.1012 0.0415  -0.0374 -0.0162 4   LEU A CD2 
35    N N   . PHE A 5   ? 0.2966 0.1930 0.1950 0.0372  -0.0144 -0.0108 5   PHE A N   
36    C CA  . PHE A 5   ? 0.2582 0.1501 0.1372 0.0327  -0.0141 -0.0019 5   PHE A CA  
37    C C   . PHE A 5   ? 0.2196 0.1083 0.1059 0.0304  -0.0223 0.0027  5   PHE A C   
38    O O   . PHE A 5   ? 0.2576 0.1563 0.1641 0.0264  -0.0245 0.0053  5   PHE A O   
39    C CB  . PHE A 5   ? 0.2972 0.1941 0.1745 0.0284  -0.0084 0.0051  5   PHE A CB  
40    C CG  . PHE A 5   ? 0.3251 0.2322 0.2019 0.0279  0.0013  -0.0007 5   PHE A CG  
41    C CD1 . PHE A 5   ? 0.3848 0.2941 0.2435 0.0262  0.0073  -0.0045 5   PHE A CD1 
42    C CD2 . PHE A 5   ? 0.3482 0.2641 0.2429 0.0283  0.0042  -0.0020 5   PHE A CD2 
43    C CE1 . PHE A 5   ? 0.4031 0.3240 0.2607 0.0244  0.0169  -0.0100 5   PHE A CE1 
44    C CE2 . PHE A 5   ? 0.3847 0.3122 0.2802 0.0275  0.0136  -0.0078 5   PHE A CE2 
45    C CZ  . PHE A 5   ? 0.4264 0.3567 0.3029 0.0253  0.0204  -0.0121 5   PHE A CZ  
46    N N   . LEU A 6   ? 0.2435 0.1319 0.1253 0.0286  -0.0231 0.0006  6   LEU A N   
47    C CA  . LEU A 6   ? 0.2054 0.1018 0.1016 0.0236  -0.0266 0.0006  6   LEU A CA  
48    C C   . LEU A 6   ? 0.1421 0.0505 0.0472 0.0178  -0.0218 0.0035  6   LEU A C   
49    O O   . LEU A 6   ? 0.2438 0.1512 0.1424 0.0179  -0.0187 0.0043  6   LEU A O   
50    C CB  . LEU A 6   ? 0.1693 0.0555 0.0566 0.0272  -0.0320 -0.0041 6   LEU A CB  
51    C CG  . LEU A 6   ? 0.2029 0.0959 0.1031 0.0226  -0.0364 -0.0043 6   LEU A CG  
52    C CD1 . LEU A 6   ? 0.1476 0.0493 0.0645 0.0199  -0.0393 -0.0017 6   LEU A CD1 
53    C CD2 . LEU A 6   ? 0.2813 0.1627 0.1716 0.0265  -0.0425 -0.0091 6   LEU A CD2 
54    N N   . VAL A 7   ? 0.1319 0.0462 0.0468 0.0140  -0.0230 0.0045  7   VAL A N   
55    C CA  . VAL A 7   ? 0.1670 0.0823 0.0821 0.0113  -0.0216 0.0048  7   VAL A CA  
56    C C   . VAL A 7   ? 0.2349 0.1499 0.1535 0.0092  -0.0257 0.0033  7   VAL A C   
57    O O   . VAL A 7   ? 0.2228 0.1412 0.1483 0.0067  -0.0285 0.0039  7   VAL A O   
58    C CB  . VAL A 7   ? 0.1231 0.0439 0.0433 0.0088  -0.0191 0.0072  7   VAL A CB  
59    C CG1 . VAL A 7   ? 0.1222 0.0430 0.0418 0.0071  -0.0182 0.0070  7   VAL A CG1 
60    C CG2 . VAL A 7   ? 0.1693 0.0909 0.0869 0.0102  -0.0153 0.0092  7   VAL A CG2 
61    N N   . PHE A 8   ? 0.2830 0.1944 0.1975 0.0098  -0.0262 0.0022  8   PHE A N   
62    C CA  . PHE A 8   ? 0.1715 0.0830 0.0892 0.0077  -0.0294 0.0014  8   PHE A CA  
63    C C   . PHE A 8   ? 0.1407 0.0558 0.0612 0.0059  -0.0277 0.0025  8   PHE A C   
64    O O   . PHE A 8   ? 0.1873 0.1012 0.1040 0.0072  -0.0253 0.0032  8   PHE A O   
65    C CB  . PHE A 8   ? 0.1840 0.0899 0.0962 0.0098  -0.0314 0.0001  8   PHE A CB  
66    C CG  . PHE A 8   ? 0.2668 0.1689 0.1778 0.0110  -0.0348 -0.0017 8   PHE A CG  
67    C CD1 . PHE A 8   ? 0.2816 0.1843 0.1982 0.0083  -0.0391 -0.0022 8   PHE A CD1 
68    C CD2 . PHE A 8   ? 0.2167 0.1144 0.1208 0.0147  -0.0340 -0.0025 8   PHE A CD2 
69    C CE1 . PHE A 8   ? 0.2276 0.1261 0.1435 0.0094  -0.0432 -0.0040 8   PHE A CE1 
70    C CE2 . PHE A 8   ? 0.2574 0.1510 0.1602 0.0166  -0.0378 -0.0046 8   PHE A CE2 
71    C CZ  . PHE A 8   ? 0.2741 0.1683 0.1834 0.0140  -0.0426 -0.0056 8   PHE A CZ  
72    N N   . TRP A 9   ? 0.2894 0.2085 0.2162 0.0027  -0.0295 0.0031  9   TRP A N   
73    C CA  . TRP A 9   ? 0.1526 0.0752 0.0820 0.0012  -0.0281 0.0040  9   TRP A CA  
74    C C   . TRP A 9   ? 0.1557 0.0803 0.0892 -0.0010 -0.0308 0.0044  9   TRP A C   
75    O O   . TRP A 9   ? 0.2344 0.1629 0.1735 -0.0049 -0.0323 0.0057  9   TRP A O   
76    C CB  . TRP A 9   ? 0.1788 0.1060 0.1121 -0.0011 -0.0263 0.0054  9   TRP A CB  
77    C CG  . TRP A 9   ? 0.1786 0.1077 0.1122 -0.0015 -0.0242 0.0059  9   TRP A CG  
78    C CD1 . TRP A 9   ? 0.2055 0.1329 0.1369 0.0001  -0.0241 0.0055  9   TRP A CD1 
79    C CD2 . TRP A 9   ? 0.1814 0.1141 0.1174 -0.0036 -0.0224 0.0071  9   TRP A CD2 
80    N NE1 . TRP A 9   ? 0.1940 0.1230 0.1261 -0.0006 -0.0223 0.0062  9   TRP A NE1 
81    C CE2 . TRP A 9   ? 0.1856 0.1178 0.1203 -0.0031 -0.0211 0.0070  9   TRP A CE2 
82    C CE3 . TRP A 9   ? 0.2102 0.1464 0.1495 -0.0059 -0.0221 0.0084  9   TRP A CE3 
83    C CZ2 . TRP A 9   ? 0.1782 0.1125 0.1140 -0.0050 -0.0193 0.0077  9   TRP A CZ2 
84    C CZ3 . TRP A 9   ? 0.1917 0.1309 0.1326 -0.0080 -0.0205 0.0094  9   TRP A CZ3 
85    C CH2 . TRP A 9   ? 0.1846 0.1225 0.1234 -0.0076 -0.0190 0.0088  9   TRP A CH2 
86    N N   . TRP A 10  ? 0.1908 0.1132 0.1219 0.0010  -0.0317 0.0039  10  TRP A N   
87    C CA  . TRP A 10  ? 0.1533 0.0782 0.0881 -0.0005 -0.0339 0.0048  10  TRP A CA  
88    C C   . TRP A 10  ? 0.1937 0.1236 0.1315 -0.0011 -0.0323 0.0061  10  TRP A C   
89    O O   . TRP A 10  ? 0.2338 0.1624 0.1688 0.0014  -0.0306 0.0057  10  TRP A O   
90    C CB  . TRP A 10  ? 0.1741 0.0954 0.1054 0.0023  -0.0360 0.0042  10  TRP A CB  
91    C CG  . TRP A 10  ? 0.1714 0.0868 0.0978 0.0037  -0.0375 0.0028  10  TRP A CG  
92    C CD1 . TRP A 10  ? 0.2003 0.1110 0.1199 0.0068  -0.0367 0.0021  10  TRP A CD1 
93    C CD2 . TRP A 10  ? 0.2142 0.1274 0.1419 0.0020  -0.0403 0.0022  10  TRP A CD2 
94    N NE1 . TRP A 10  ? 0.1975 0.1036 0.1136 0.0076  -0.0384 0.0009  10  TRP A NE1 
95    C CE2 . TRP A 10  ? 0.3253 0.2323 0.2463 0.0050  -0.0408 0.0006  10  TRP A CE2 
96    C CE3 . TRP A 10  ? 0.1958 0.1112 0.1294 -0.0020 -0.0427 0.0033  10  TRP A CE3 
97    C CZ2 . TRP A 10  ? 0.2965 0.1992 0.2167 0.0048  -0.0439 -0.0006 10  TRP A CZ2 
98    C CZ3 . TRP A 10  ? 0.1876 0.0983 0.1207 -0.0028 -0.0462 0.0024  10  TRP A CZ3 
99    C CH2 . TRP A 10  ? 0.2347 0.1389 0.1611 0.0009  -0.0469 0.0001  10  TRP A CH2 
100   N N   . HIS A 11  ? 0.1666 0.1019 0.1097 -0.0047 -0.0332 0.0079  11  HIS A N   
101   C CA  . HIS A 11  ? 0.1588 0.0997 0.1043 -0.0056 -0.0316 0.0092  11  HIS A CA  
102   C C   . HIS A 11  ? 0.1659 0.1108 0.1130 -0.0043 -0.0334 0.0102  11  HIS A C   
103   O O   . HIS A 11  ? 0.3718 0.3197 0.3216 -0.0071 -0.0354 0.0117  11  HIS A O   
104   C CB  . HIS A 11  ? 0.1635 0.1095 0.1129 -0.0113 -0.0311 0.0111  11  HIS A CB  
105   C CG  . HIS A 11  ? 0.1312 0.0849 0.0824 -0.0135 -0.0299 0.0129  11  HIS A CG  
106   N ND1 . HIS A 11  ? 0.1878 0.1427 0.1369 -0.0112 -0.0276 0.0121  11  HIS A ND1 
107   C CD2 . HIS A 11  ? 0.1724 0.1338 0.1263 -0.0181 -0.0308 0.0152  11  HIS A CD2 
108   C CE1 . HIS A 11  ? 0.1571 0.1212 0.1071 -0.0138 -0.0270 0.0130  11  HIS A CE1 
109   N NE2 . HIS A 11  ? 0.1146 0.0835 0.0674 -0.0182 -0.0287 0.0148  11  HIS A NE2 
110   N N   . MET A 12  ? 0.1785 0.1239 0.1244 -0.0001 -0.0331 0.0096  12  MET A N   
111   C CA  . MET A 12  ? 0.1869 0.1379 0.1350 0.0021  -0.0353 0.0102  12  MET A CA  
112   C C   . MET A 12  ? 0.1722 0.1331 0.1225 0.0018  -0.0343 0.0105  12  MET A C   
113   O O   . MET A 12  ? 0.2042 0.1627 0.1529 0.0034  -0.0327 0.0097  12  MET A O   
114   C CB  . MET A 12  ? 0.1862 0.1314 0.1320 0.0073  -0.0372 0.0091  12  MET A CB  
115   C CG  . MET A 12  ? 0.1473 0.0836 0.0879 0.0077  -0.0374 0.0080  12  MET A CG  
116   S SD  . MET A 12  ? 0.2797 0.2151 0.2205 0.0054  -0.0398 0.0080  12  MET A SD  
117   C CE  . MET A 12  ? 0.1955 0.1228 0.1295 0.0088  -0.0417 0.0070  12  MET A CE  
118   N N   . HIS A 13  ? 0.1619 0.1353 0.1153 -0.0006 -0.0356 0.0106  13  HIS A N   
119   C CA  . HIS A 13  ? 0.1923 0.1770 0.1452 -0.0026 -0.0364 0.0077  13  HIS A CA  
120   C C   . HIS A 13  ? 0.2166 0.2154 0.1733 -0.0047 -0.0399 0.0050  13  HIS A C   
121   O O   . HIS A 13  ? 0.3020 0.3036 0.2613 -0.0059 -0.0391 0.0070  13  HIS A O   
122   C CB  . HIS A 13  ? 0.2049 0.1928 0.1567 -0.0084 -0.0324 0.0080  13  HIS A CB  
123   C CG  . HIS A 13  ? 0.2673 0.2679 0.2185 -0.0147 -0.0330 0.0034  13  HIS A CG  
124   N ND1 . HIS A 13  ? 0.2708 0.2752 0.2191 -0.0160 -0.0343 -0.0037 13  HIS A ND1 
125   C CD2 . HIS A 13  ? 0.2688 0.2792 0.2230 -0.0222 -0.0315 0.0039  13  HIS A CD2 
126   C CE1 . HIS A 13  ? 0.2495 0.2694 0.2014 -0.0243 -0.0312 -0.0086 13  HIS A CE1 
127   N NE2 . HIS A 13  ? 0.2264 0.2496 0.1810 -0.0284 -0.0298 -0.0024 13  HIS A NE2 
128   N N   . GLN A 14  ? 0.2536 0.2610 0.2116 -0.0054 -0.0443 -0.0014 14  GLN A N   
129   C CA  . GLN A 14  ? 0.2318 0.2579 0.1969 -0.0093 -0.0470 -0.0074 14  GLN A CA  
130   C C   . GLN A 14  ? 0.2656 0.3052 0.2341 -0.0160 -0.0444 -0.0170 14  GLN A C   
131   O O   . GLN A 14  ? 0.2675 0.3005 0.2414 -0.0085 -0.0413 -0.0229 14  GLN A O   
132   C CB  . GLN A 14  ? 0.1987 0.2270 0.1712 -0.0040 -0.0533 -0.0079 14  GLN A CB  
133   C CG  . GLN A 14  ? 0.2511 0.2702 0.2214 -0.0005 -0.0520 0.0001  14  GLN A CG  
134   C CD  . GLN A 14  ? 0.2185 0.2443 0.1886 -0.0048 -0.0490 0.0011  14  GLN A CD  
135   O OE1 . GLN A 14  ? 0.2498 0.2812 0.2207 -0.0109 -0.0482 -0.0015 14  GLN A OE1 
136   N NE2 . GLN A 14  ? 0.2267 0.2454 0.1960 -0.0027 -0.0483 0.0054  14  GLN A NE2 
137   N N   . PRO A 15  ? 0.1864 0.2405 0.1585 -0.0254 -0.0382 -0.0185 15  PRO A N   
138   C CA  . PRO A 15  ? 0.1772 0.2508 0.1561 -0.0313 -0.0305 -0.0302 15  PRO A CA  
139   C C   . PRO A 15  ? 0.2361 0.3256 0.2325 -0.0249 -0.0305 -0.0438 15  PRO A C   
140   O O   . PRO A 15  ? 0.2611 0.3521 0.2645 -0.0194 -0.0361 -0.0421 15  PRO A O   
141   C CB  . PRO A 15  ? 0.2309 0.3157 0.2082 -0.0424 -0.0246 -0.0254 15  PRO A CB  
142   C CG  . PRO A 15  ? 0.1848 0.2576 0.1579 -0.0413 -0.0295 -0.0136 15  PRO A CG  
143   C CD  . PRO A 15  ? 0.1868 0.2425 0.1588 -0.0302 -0.0376 -0.0114 15  PRO A CD  
144   N N   . LEU A 16  ? 0.2055 0.3027 0.2115 -0.0238 -0.0226 -0.0563 16  LEU A N   
145   C CA  . LEU A 16  ? 0.1445 0.2523 0.1719 -0.0149 -0.0204 -0.0692 16  LEU A CA  
146   C C   . LEU A 16  ? 0.1424 0.2782 0.1794 -0.0219 -0.0196 -0.0742 16  LEU A C   
147   O O   . LEU A 16  ? 0.1212 0.2800 0.1571 -0.0350 -0.0129 -0.0804 16  LEU A O   
148   C CB  . LEU A 16  ? 0.1179 0.2299 0.1540 -0.0139 -0.0115 -0.0832 16  LEU A CB  
149   C CG  . LEU A 16  ? 0.1230 0.2428 0.1843 -0.0027 -0.0095 -0.0978 16  LEU A CG  
150   C CD1 . LEU A 16  ? 0.1264 0.2211 0.1931 0.0132  -0.0185 -0.0909 16  LEU A CD1 
151   C CD2 . LEU A 16  ? 0.1290 0.2555 0.1992 -0.0038 0.0001  -0.1136 16  LEU A CD2 
152   N N   . TYR A 17  ? 0.2066 0.3416 0.2525 -0.0141 -0.0266 -0.0713 17  TYR A N   
153   C CA  . TYR A 17  ? 0.1966 0.3582 0.2536 -0.0197 -0.0267 -0.0758 17  TYR A CA  
154   C C   . TYR A 17  ? 0.1107 0.2907 0.1939 -0.0123 -0.0217 -0.0927 17  TYR A C   
155   O O   . TYR A 17  ? 0.1093 0.3145 0.2049 -0.0164 -0.0207 -0.0985 17  TYR A O   
156   C CB  . TYR A 17  ? 0.2007 0.3531 0.2539 -0.0162 -0.0375 -0.0637 17  TYR A CB  
157   C CG  . TYR A 17  ? 0.1606 0.2922 0.1897 -0.0229 -0.0411 -0.0465 17  TYR A CG  
158   C CD1 . TYR A 17  ? 0.1758 0.3094 0.1933 -0.0353 -0.0352 -0.0397 17  TYR A CD1 
159   C CD2 . TYR A 17  ? 0.2283 0.3351 0.2479 -0.0149 -0.0495 -0.0368 17  TYR A CD2 
160   C CE1 . TYR A 17  ? 0.1975 0.3089 0.1991 -0.0379 -0.0381 -0.0256 17  TYR A CE1 
161   C CE2 . TYR A 17  ? 0.2399 0.3247 0.2413 -0.0193 -0.0513 -0.0228 17  TYR A CE2 
162   C CZ  . TYR A 17  ? 0.2222 0.3096 0.2174 -0.0293 -0.0456 -0.0187 17  TYR A CZ  
163   O OH  . TYR A 17  ? 0.2426 0.3110 0.2269 -0.0295 -0.0460 -0.0091 17  TYR A OH  
164   N N   . ARG A 18  ? 0.1156 0.2841 0.2087 -0.0016 -0.0187 -0.1010 18  ARG A N   
165   C CA  . ARG A 18  ? 0.1202 0.3025 0.2413 0.0080  -0.0153 -0.1174 18  ARG A CA  
166   C C   . ARG A 18  ? 0.1217 0.3330 0.2503 -0.0026 -0.0026 -0.1344 18  ARG A C   
167   O O   . ARG A 18  ? 0.1249 0.3311 0.2464 -0.0062 0.0041  -0.1397 18  ARG A O   
168   C CB  . ARG A 18  ? 0.1270 0.2823 0.2556 0.0235  -0.0187 -0.1183 18  ARG A CB  
169   C CG  . ARG A 18  ? 0.1331 0.2964 0.2933 0.0367  -0.0194 -0.1320 18  ARG A CG  
170   C CD  . ARG A 18  ? 0.1420 0.2777 0.3087 0.0498  -0.0225 -0.1328 18  ARG A CD  
171   N NE  . ARG A 18  ? 0.1505 0.2958 0.3479 0.0594  -0.0199 -0.1499 18  ARG A NE  
172   C CZ  . ARG A 18  ? 0.2783 0.4362 0.4814 0.0529  -0.0096 -0.1647 18  ARG A CZ  
173   N NH1 . ARG A 18  ? 0.3597 0.5289 0.5477 0.0403  0.0001  -0.1691 18  ARG A NH1 
174   N NH2 . ARG A 18  ? 0.4171 0.5762 0.6406 0.0584  -0.0098 -0.1744 18  ARG A NH2 
175   N N   . GLU A 19  ? 0.1520 0.3948 0.2945 -0.0082 0.0009  -0.1432 19  GLU A N   
176   C CA  . GLU A 19  ? 0.1275 0.3941 0.2717 -0.0187 0.0133  -0.1587 19  GLU A CA  
177   C C   . GLU A 19  ? 0.1983 0.4612 0.3630 -0.0077 0.0179  -0.1761 19  GLU A C   
178   O O   . GLU A 19  ? 0.2091 0.4659 0.3952 0.0067  0.0129  -0.1803 19  GLU A O   
179   C CB  . GLU A 19  ? 0.1340 0.4204 0.2784 -0.0255 0.0150  -0.1602 19  GLU A CB  
180   C CG  . GLU A 19  ? 0.2118 0.5158 0.3394 -0.0423 0.0250  -0.1665 19  GLU A CG  
181   C CD  . GLU A 19  ? 0.3061 0.6253 0.4512 -0.0409 0.0319  -0.1886 19  GLU A CD  
182   O OE1 . GLU A 19  ? 0.3030 0.6255 0.4732 -0.0288 0.0295  -0.1968 19  GLU A OE1 
183   O OE2 . GLU A 19  ? 0.3658 0.6922 0.4999 -0.0522 0.0384  -0.1970 19  GLU A OE2 
184   N N   . PRO A 20  ? 0.2512 0.5130 0.4080 -0.0148 0.0253  -0.1842 20  PRO A N   
185   C CA  . PRO A 20  ? 0.2517 0.5008 0.4256 -0.0045 0.0265  -0.1958 20  PRO A CA  
186   C C   . PRO A 20  ? 0.2879 0.5505 0.4855 0.0003  0.0277  -0.2104 20  PRO A C   
187   O O   . PRO A 20  ? 0.3374 0.5853 0.5544 0.0141  0.0239  -0.2150 20  PRO A O   
188   C CB  . PRO A 20  ? 0.1591 0.4092 0.3178 -0.0177 0.0336  -0.1987 20  PRO A CB  
189   C CG  . PRO A 20  ? 0.2757 0.5448 0.4124 -0.0363 0.0365  -0.1931 20  PRO A CG  
190   C CD  . PRO A 20  ? 0.2711 0.5412 0.4024 -0.0336 0.0309  -0.1806 20  PRO A CD  
191   N N   . TYR A 21  ? 0.2296 0.5188 0.4254 -0.0110 0.0324  -0.2172 21  TYR A N   
192   C CA  . TYR A 21  ? 0.2777 0.5820 0.4963 -0.0074 0.0348  -0.2332 21  TYR A CA  
193   C C   . TYR A 21  ? 0.3127 0.6131 0.5504 0.0072  0.0272  -0.2298 21  TYR A C   
194   O O   . TYR A 21  ? 0.3589 0.6483 0.6190 0.0207  0.0234  -0.2357 21  TYR A O   
195   C CB  . TYR A 21  ? 0.2674 0.6006 0.4755 -0.0249 0.0423  -0.2415 21  TYR A CB  
196   C CG  . TYR A 21  ? 0.3030 0.6413 0.4984 -0.0387 0.0488  -0.2479 21  TYR A CG  
197   C CD1 . TYR A 21  ? 0.3857 0.7232 0.5985 -0.0353 0.0524  -0.2623 21  TYR A CD1 
198   C CD2 . TYR A 21  ? 0.3674 0.7097 0.5334 -0.0551 0.0503  -0.2381 21  TYR A CD2 
199   C CE1 . TYR A 21  ? 0.5456 0.8886 0.7482 -0.0482 0.0579  -0.2672 21  TYR A CE1 
200   C CE2 . TYR A 21  ? 0.4269 0.7738 0.5825 -0.0682 0.0546  -0.2424 21  TYR A CE2 
201   C CZ  . TYR A 21  ? 0.5402 0.8884 0.7149 -0.0648 0.0588  -0.2570 21  TYR A CZ  
202   O OH  . TYR A 21  ? 0.5806 0.9347 0.7464 -0.0782 0.0632  -0.2605 21  TYR A OH  
203   N N   . THR A 22  ? 0.2120 0.5203 0.4409 0.0040  0.0239  -0.2188 22  THR A N   
204   C CA  . THR A 22  ? 0.1738 0.4790 0.4197 0.0164  0.0156  -0.2136 22  THR A CA  
205   C C   . THR A 22  ? 0.2431 0.5190 0.4906 0.0303  0.0047  -0.1996 22  THR A C   
206   O O   . THR A 22  ? 0.2439 0.5114 0.5072 0.0424  -0.0038 -0.1957 22  THR A O   
207   C CB  . THR A 22  ? 0.3198 0.6434 0.5553 0.0069  0.0152  -0.2054 22  THR A CB  
208   O OG1 . THR A 22  ? 0.3576 0.6678 0.5745 0.0049  0.0087  -0.1862 22  THR A OG1 
209   C CG2 . THR A 22  ? 0.3862 0.7341 0.6074 -0.0110 0.0257  -0.2140 22  THR A CG2 
210   N N   . GLY A 23  ? 0.1930 0.4526 0.4235 0.0284  0.0044  -0.1914 23  GLY A N   
211   C CA  . GLY A 23  ? 0.3067 0.5377 0.5355 0.0407  -0.0062 -0.1776 23  GLY A CA  
212   C C   . GLY A 23  ? 0.2850 0.5146 0.5052 0.0409  -0.0154 -0.1611 23  GLY A C   
213   O O   . GLY A 23  ? 0.3177 0.5228 0.5354 0.0510  -0.0259 -0.1488 23  GLY A O   
214   N N   . GLU A 24  ? 0.2913 0.5434 0.5036 0.0285  -0.0126 -0.1591 24  GLU A N   
215   C CA  . GLU A 24  ? 0.1846 0.4344 0.3881 0.0269  -0.0221 -0.1432 24  GLU A CA  
216   C C   . GLU A 24  ? 0.1511 0.3914 0.3276 0.0167  -0.0248 -0.1289 24  GLU A C   
217   O O   . GLU A 24  ? 0.1618 0.4099 0.3236 0.0038  -0.0164 -0.1310 24  GLU A O   
218   C CB  . GLU A 24  ? 0.1692 0.4436 0.3758 0.0181  -0.0184 -0.1463 24  GLU A CB  
219   C CG  . GLU A 24  ? 0.4002 0.6841 0.6338 0.0279  -0.0179 -0.1589 24  GLU A CG  
220   C CD  . GLU A 24  ? 0.7219 1.0325 0.9585 0.0185  -0.0133 -0.1629 24  GLU A CD  
221   O OE1 . GLU A 24  ? 0.6704 0.9915 0.9293 0.0253  -0.0129 -0.1732 24  GLU A OE1 
222   O OE2 . GLU A 24  ? 0.7637 1.0832 0.9799 0.0040  -0.0106 -0.1550 24  GLU A OE2 
223   N N   . TYR A 25  ? 0.1382 0.3581 0.3050 0.0218  -0.0368 -0.1133 25  TYR A N   
224   C CA  . TYR A 25  ? 0.1118 0.3155 0.2482 0.0121  -0.0402 -0.0972 25  TYR A CA  
225   C C   . TYR A 25  ? 0.1132 0.3313 0.2394 -0.0014 -0.0391 -0.0907 25  TYR A C   
226   O O   . TYR A 25  ? 0.1138 0.3324 0.2450 0.0016  -0.0453 -0.0853 25  TYR A O   
227   C CB  . TYR A 25  ? 0.1197 0.2905 0.2451 0.0225  -0.0516 -0.0827 25  TYR A CB  
228   C CG  . TYR A 25  ? 0.1533 0.2980 0.2740 0.0314  -0.0508 -0.0820 25  TYR A CG  
229   C CD1 . TYR A 25  ? 0.1519 0.2954 0.2948 0.0432  -0.0493 -0.0931 25  TYR A CD1 
230   C CD2 . TYR A 25  ? 0.1845 0.3059 0.2799 0.0278  -0.0519 -0.0705 25  TYR A CD2 
231   C CE1 . TYR A 25  ? 0.1312 0.2501 0.2697 0.0504  -0.0492 -0.0918 25  TYR A CE1 
232   C CE2 . TYR A 25  ? 0.2093 0.3080 0.3002 0.0349  -0.0511 -0.0695 25  TYR A CE2 
233   C CZ  . TYR A 25  ? 0.1299 0.2269 0.2417 0.0458  -0.0499 -0.0798 25  TYR A CZ  
234   O OH  . TYR A 25  ? 0.1361 0.2097 0.2434 0.0519  -0.0498 -0.0782 25  TYR A OH  
235   N N   . LEU A 26  ? 0.1492 0.3744 0.2588 -0.0161 -0.0309 -0.0891 26  LEU A N   
236   C CA  . LEU A 26  ? 0.1240 0.3584 0.2227 -0.0286 -0.0286 -0.0818 26  LEU A CA  
237   C C   . LEU A 26  ? 0.1890 0.3999 0.2681 -0.0319 -0.0374 -0.0627 26  LEU A C   
238   O O   . LEU A 26  ? 0.1499 0.3647 0.2239 -0.0395 -0.0382 -0.0561 26  LEU A O   
239   C CB  . LEU A 26  ? 0.1211 0.3687 0.2083 -0.0420 -0.0170 -0.0861 26  LEU A CB  
240   C CG  . LEU A 26  ? 0.1244 0.3928 0.2276 -0.0402 -0.0069 -0.1065 26  LEU A CG  
241   C CD1 . LEU A 26  ? 0.1321 0.4124 0.2184 -0.0550 0.0037  -0.1091 26  LEU A CD1 
242   C CD2 . LEU A 26  ? 0.1283 0.4157 0.2564 -0.0330 -0.0063 -0.1189 26  LEU A CD2 
243   N N   . LEU A 27  ? 0.1516 0.3375 0.2202 -0.0262 -0.0438 -0.0546 27  LEU A N   
244   C CA  . LEU A 27  ? 0.1133 0.2740 0.1644 -0.0280 -0.0514 -0.0385 27  LEU A CA  
245   C C   . LEU A 27  ? 0.1706 0.3115 0.2217 -0.0156 -0.0604 -0.0345 27  LEU A C   
246   O O   . LEU A 27  ? 0.2833 0.4192 0.3364 -0.0081 -0.0600 -0.0394 27  LEU A O   
247   C CB  . LEU A 27  ? 0.1799 0.3264 0.2117 -0.0362 -0.0474 -0.0306 27  LEU A CB  
248   C CG  . LEU A 27  ? 0.1274 0.2860 0.1533 -0.0487 -0.0407 -0.0282 27  LEU A CG  
249   C CD1 . LEU A 27  ? 0.1616 0.3087 0.1722 -0.0547 -0.0361 -0.0217 27  LEU A CD1 
250   C CD2 . LEU A 27  ? 0.2401 0.3936 0.2643 -0.0508 -0.0460 -0.0207 27  LEU A CD2 
251   N N   . PRO A 28  ? 0.1974 0.3256 0.2453 -0.0134 -0.0685 -0.0256 28  PRO A N   
252   C CA  . PRO A 28  ? 0.1532 0.2643 0.1990 -0.0027 -0.0750 -0.0205 28  PRO A CA  
253   C C   . PRO A 28  ? 0.2268 0.3138 0.2513 -0.0044 -0.0747 -0.0095 28  PRO A C   
254   O O   . PRO A 28  ? 0.3495 0.4240 0.3676 0.0031  -0.0752 -0.0048 28  PRO A O   
255   C CB  . PRO A 28  ? 0.1965 0.3104 0.2468 -0.0034 -0.0804 -0.0152 28  PRO A CB  
256   C CG  . PRO A 28  ? 0.2408 0.3508 0.2841 -0.0140 -0.0808 -0.0127 28  PRO A CG  
257   C CD  . PRO A 28  ? 0.1886 0.3187 0.2355 -0.0200 -0.0708 -0.0211 28  PRO A CD  
258   N N   . TRP A 29  ? 0.2011 0.2784 0.2159 -0.0108 -0.0721 -0.0091 29  TRP A N   
259   C CA  . TRP A 29  ? 0.2175 0.2862 0.2169 -0.0038 -0.0636 -0.0092 29  TRP A CA  
260   C C   . TRP A 29  ? 0.1904 0.2451 0.1855 -0.0004 -0.0648 -0.0022 29  TRP A C   
261   O O   . TRP A 29  ? 0.1686 0.2061 0.1551 0.0036  -0.0623 0.0029  29  TRP A O   
262   C CB  . TRP A 29  ? 0.2567 0.3159 0.2502 -0.0110 -0.0624 -0.0087 29  TRP A CB  
263   C CG  . TRP A 29  ? 0.2586 0.3251 0.2531 -0.0204 -0.0602 -0.0059 29  TRP A CG  
264   C CD1 . TRP A 29  ? 0.2837 0.3654 0.2805 -0.0313 -0.0549 -0.0062 29  TRP A CD1 
265   C CD2 . TRP A 29  ? 0.2800 0.3426 0.2726 -0.0202 -0.0615 -0.0024 29  TRP A CD2 
266   N NE1 . TRP A 29  ? 0.3272 0.4127 0.3229 -0.0376 -0.0543 -0.0021 29  TRP A NE1 
267   C CE2 . TRP A 29  ? 0.3354 0.4082 0.3293 -0.0311 -0.0589 0.0003  29  TRP A CE2 
268   C CE3 . TRP A 29  ? 0.3204 0.3749 0.3094 -0.0138 -0.0630 -0.0002 29  TRP A CE3 
269   C CZ2 . TRP A 29  ? 0.4271 0.4991 0.4194 -0.0355 -0.0603 0.0052  29  TRP A CZ2 
270   C CZ3 . TRP A 29  ? 0.3459 0.3988 0.3336 -0.0195 -0.0647 0.0049  29  TRP A CZ3 
271   C CH2 . TRP A 29  ? 0.4437 0.5049 0.4333 -0.0297 -0.0640 0.0073  29  TRP A CH2 
272   N N   . THR A 30  ? 0.2320 0.2867 0.2360 0.0047  -0.0681 -0.0090 30  THR A N   
273   C CA  . THR A 30  ? 0.2224 0.2574 0.2238 0.0154  -0.0693 -0.0087 30  THR A CA  
274   C C   . THR A 30  ? 0.2542 0.2779 0.2562 0.0220  -0.0722 -0.0038 30  THR A C   
275   O O   . THR A 30  ? 0.2512 0.2568 0.2428 0.0238  -0.0695 0.0017  30  THR A O   
276   C CB  . THR A 30  ? 0.2163 0.2598 0.2327 0.0229  -0.0716 -0.0210 30  THR A CB  
277   O OG1 . THR A 30  ? 0.2651 0.3239 0.2816 0.0131  -0.0635 -0.0272 30  THR A OG1 
278   C CG2 . THR A 30  ? 0.2119 0.2323 0.2225 0.0317  -0.0726 -0.0182 30  THR A CG2 
279   N N   . PHE A 31  ? 0.2493 0.2858 0.2640 0.0240  -0.0767 -0.0067 31  PHE A N   
280   C CA  . PHE A 31  ? 0.1836 0.2114 0.1989 0.0291  -0.0797 -0.0024 31  PHE A CA  
281   C C   . PHE A 31  ? 0.2377 0.2577 0.2383 0.0233  -0.0758 0.0052  31  PHE A C   
282   O O   . PHE A 31  ? 0.2736 0.2791 0.2665 0.0255  -0.0743 0.0089  31  PHE A O   
283   C CB  . PHE A 31  ? 0.1438 0.1897 0.1776 0.0318  -0.0849 -0.0073 31  PHE A CB  
284   C CG  . PHE A 31  ? 0.1434 0.1831 0.1766 0.0349  -0.0884 -0.0021 31  PHE A CG  
285   C CD1 . PHE A 31  ? 0.2194 0.2452 0.2542 0.0424  -0.0908 -0.0005 31  PHE A CD1 
286   C CD2 . PHE A 31  ? 0.1944 0.2427 0.2250 0.0291  -0.0891 0.0015  31  PHE A CD2 
287   C CE1 . PHE A 31  ? 0.2009 0.2229 0.2344 0.0438  -0.0941 0.0044  31  PHE A CE1 
288   C CE2 . PHE A 31  ? 0.2036 0.2476 0.2334 0.0317  -0.0925 0.0055  31  PHE A CE2 
289   C CZ  . PHE A 31  ? 0.1596 0.1909 0.1908 0.0388  -0.0951 0.0070  31  PHE A CZ  
290   N N   . PHE A 32  ? 0.2389 0.2707 0.2373 0.0158  -0.0736 0.0060  32  PHE A N   
291   C CA  . PHE A 32  ? 0.1267 0.1535 0.1164 0.0129  -0.0707 0.0099  32  PHE A CA  
292   C C   . PHE A 32  ? 0.1770 0.1840 0.1555 0.0123  -0.0669 0.0118  32  PHE A C   
293   O O   . PHE A 32  ? 0.2591 0.2528 0.2314 0.0126  -0.0683 0.0133  32  PHE A O   
294   C CB  . PHE A 32  ? 0.1556 0.1978 0.1466 0.0068  -0.0700 0.0082  32  PHE A CB  
295   C CG  . PHE A 32  ? 0.1760 0.2334 0.1763 0.0066  -0.0754 0.0068  32  PHE A CG  
296   C CD1 . PHE A 32  ? 0.1867 0.2378 0.1866 0.0099  -0.0787 0.0095  32  PHE A CD1 
297   C CD2 . PHE A 32  ? 0.2084 0.2883 0.2188 0.0021  -0.0770 0.0020  32  PHE A CD2 
298   C CE1 . PHE A 32  ? 0.1462 0.2117 0.1554 0.0098  -0.0839 0.0084  32  PHE A CE1 
299   C CE2 . PHE A 32  ? 0.2402 0.3353 0.2613 0.0009  -0.0813 0.0009  32  PHE A CE2 
300   C CZ  . PHE A 32  ? 0.1996 0.2878 0.2203 0.0054  -0.0853 0.0043  32  PHE A CZ  
301   N N   . HIS A 33  ? 0.1414 0.1471 0.1177 0.0109  -0.0627 0.0110  33  HIS A N   
302   C CA  . HIS A 33  ? 0.1847 0.1725 0.1525 0.0104  -0.0596 0.0121  33  HIS A CA  
303   C C   . HIS A 33  ? 0.2537 0.2301 0.2191 0.0155  -0.0600 0.0121  33  HIS A C   
304   O O   . HIS A 33  ? 0.3018 0.2650 0.2599 0.0149  -0.0587 0.0123  33  HIS A O   
305   C CB  . HIS A 33  ? 0.1831 0.1738 0.1497 0.0068  -0.0553 0.0117  33  HIS A CB  
306   C CG  . HIS A 33  ? 0.1907 0.1843 0.1565 0.0008  -0.0548 0.0126  33  HIS A CG  
307   N ND1 . HIS A 33  ? 0.3236 0.3040 0.2853 -0.0021 -0.0553 0.0145  33  HIS A ND1 
308   C CD2 . HIS A 33  ? 0.2409 0.2481 0.2098 -0.0035 -0.0546 0.0113  33  HIS A CD2 
309   C CE1 . HIS A 33  ? 0.3241 0.3081 0.2870 -0.0080 -0.0557 0.0160  33  HIS A CE1 
310   N NE2 . HIS A 33  ? 0.3113 0.3108 0.2779 -0.0093 -0.0550 0.0145  33  HIS A NE2 
311   N N   . ALA A 34  ? 0.1962 0.1783 0.1683 0.0202  -0.0623 0.0115  34  ALA A N   
312   C CA  . ALA A 34  ? 0.1774 0.1483 0.1476 0.0248  -0.0634 0.0120  34  ALA A CA  
313   C C   . ALA A 34  ? 0.2041 0.1686 0.1707 0.0257  -0.0673 0.0138  34  ALA A C   
314   O O   . ALA A 34  ? 0.2507 0.2040 0.2103 0.0264  -0.0674 0.0147  34  ALA A O   
315   C CB  . ALA A 34  ? 0.1755 0.1498 0.1554 0.0307  -0.0673 0.0098  34  ALA A CB  
316   N N   . VAL A 35  ? 0.1497 0.1224 0.1206 0.0253  -0.0709 0.0143  35  VAL A N   
317   C CA  . VAL A 35  ? 0.1604 0.1277 0.1273 0.0257  -0.0751 0.0161  35  VAL A CA  
318   C C   . VAL A 35  ? 0.2200 0.1790 0.1770 0.0212  -0.0736 0.0159  35  VAL A C   
319   O O   . VAL A 35  ? 0.2608 0.2124 0.2114 0.0212  -0.0762 0.0171  35  VAL A O   
320   C CB  . VAL A 35  ? 0.2018 0.1817 0.1779 0.0271  -0.0800 0.0167  35  VAL A CB  
321   C CG1 . VAL A 35  ? 0.2534 0.2416 0.2421 0.0327  -0.0824 0.0162  35  VAL A CG1 
322   C CG2 . VAL A 35  ? 0.2160 0.2070 0.1945 0.0226  -0.0786 0.0154  35  VAL A CG2 
323   N N   . LYS A 36  ? 0.2735 0.2335 0.2294 0.0174  -0.0698 0.0146  36  LYS A N   
324   C CA  . LYS A 36  ? 0.3288 0.2812 0.2782 0.0135  -0.0691 0.0141  36  LYS A CA  
325   C C   . LYS A 36  ? 0.3481 0.2904 0.2911 0.0125  -0.0650 0.0128  36  LYS A C   
326   O O   . LYS A 36  ? 0.3157 0.2496 0.2520 0.0115  -0.0654 0.0120  36  LYS A O   
327   C CB  . LYS A 36  ? 0.3362 0.2961 0.2897 0.0094  -0.0690 0.0143  36  LYS A CB  
328   C CG  . LYS A 36  ? 0.3383 0.2897 0.2868 0.0055  -0.0697 0.0141  36  LYS A CG  
329   C CD  . LYS A 36  ? 0.3745 0.3326 0.3275 0.0008  -0.0702 0.0151  36  LYS A CD  
330   C CE  . LYS A 36  ? 0.3585 0.3212 0.3143 -0.0014 -0.0661 0.0155  36  LYS A CE  
331   N NZ  . LYS A 36  ? 0.3061 0.2573 0.2580 -0.0038 -0.0638 0.0151  36  LYS A NZ  
332   N N   . ASP A 37  ? 0.3100 0.2540 0.2550 0.0127  -0.0612 0.0122  37  ASP A N   
333   C CA  . ASP A 37  ? 0.2549 0.1914 0.1951 0.0113  -0.0573 0.0108  37  ASP A CA  
334   C C   . ASP A 37  ? 0.3031 0.2367 0.2412 0.0139  -0.0550 0.0105  37  ASP A C   
335   O O   . ASP A 37  ? 0.3331 0.2595 0.2650 0.0139  -0.0535 0.0097  37  ASP A O   
336   C CB  . ASP A 37  ? 0.2951 0.2352 0.2388 0.0074  -0.0547 0.0107  37  ASP A CB  
337   C CG  . ASP A 37  ? 0.4244 0.3630 0.3681 0.0038  -0.0569 0.0111  37  ASP A CG  
338   O OD1 . ASP A 37  ? 0.4939 0.4239 0.4324 0.0037  -0.0580 0.0099  37  ASP A OD1 
339   O OD2 . ASP A 37  ? 0.3283 0.2747 0.2770 0.0010  -0.0577 0.0127  37  ASP A OD2 
340   N N   . TYR A 38  ? 0.3388 0.2783 0.2823 0.0162  -0.0551 0.0111  38  TYR A N   
341   C CA  . TYR A 38  ? 0.2324 0.1688 0.1747 0.0180  -0.0528 0.0109  38  TYR A CA  
342   C C   . TYR A 38  ? 0.2952 0.2239 0.2315 0.0200  -0.0545 0.0121  38  TYR A C   
343   O O   . TYR A 38  ? 0.3523 0.2760 0.2841 0.0198  -0.0520 0.0120  38  TYR A O   
344   C CB  . TYR A 38  ? 0.1829 0.1268 0.1330 0.0209  -0.0535 0.0111  38  TYR A CB  
345   C CG  . TYR A 38  ? 0.1758 0.1286 0.1302 0.0182  -0.0511 0.0105  38  TYR A CG  
346   C CD1 . TYR A 38  ? 0.2302 0.1812 0.1812 0.0136  -0.0480 0.0102  38  TYR A CD1 
347   C CD2 . TYR A 38  ? 0.2630 0.2276 0.2256 0.0201  -0.0526 0.0101  38  TYR A CD2 
348   C CE1 . TYR A 38  ? 0.2436 0.2036 0.1979 0.0102  -0.0463 0.0106  38  TYR A CE1 
349   C CE2 . TYR A 38  ? 0.2543 0.2289 0.2189 0.0165  -0.0517 0.0091  38  TYR A CE2 
350   C CZ  . TYR A 38  ? 0.2224 0.1959 0.1828 0.0112  -0.0475 0.0102  38  TYR A CZ  
351   O OH  . TYR A 38  ? 0.3519 0.3376 0.3141 0.0066  -0.0459 0.0098  38  TYR A OH  
352   N N   . TYR A 39  ? 0.2612 0.1896 0.1973 0.0216  -0.0591 0.0138  39  TYR A N   
353   C CA  . TYR A 39  ? 0.2309 0.1526 0.1606 0.0227  -0.0612 0.0161  39  TYR A CA  
354   C C   . TYR A 39  ? 0.2543 0.1709 0.1752 0.0201  -0.0604 0.0154  39  TYR A C   
355   O O   . TYR A 39  ? 0.2494 0.1606 0.1633 0.0197  -0.0591 0.0164  39  TYR A O   
356   C CB  . TYR A 39  ? 0.3119 0.2357 0.2454 0.0256  -0.0672 0.0191  39  TYR A CB  
357   C CG  . TYR A 39  ? 0.2971 0.2144 0.2234 0.0260  -0.0702 0.0228  39  TYR A CG  
358   C CD1 . TYR A 39  ? 0.3492 0.2625 0.2754 0.0277  -0.0708 0.0256  39  TYR A CD1 
359   C CD2 . TYR A 39  ? 0.2183 0.1334 0.1376 0.0243  -0.0727 0.0239  39  TYR A CD2 
360   C CE1 . TYR A 39  ? 0.3816 0.2894 0.3008 0.0274  -0.0739 0.0301  39  TYR A CE1 
361   C CE2 . TYR A 39  ? 0.2204 0.1306 0.1322 0.0241  -0.0757 0.0280  39  TYR A CE2 
362   C CZ  . TYR A 39  ? 0.3758 0.2826 0.2875 0.0254  -0.0763 0.0314  39  TYR A CZ  
363   O OH  . TYR A 39  ? 0.5331 0.4353 0.4368 0.0245  -0.0796 0.0366  39  TYR A OH  
364   N N   . ASP A 40  ? 0.2644 0.1827 0.1858 0.0185  -0.0614 0.0140  40  ASP A N   
365   C CA  . ASP A 40  ? 0.3019 0.2150 0.2156 0.0169  -0.0618 0.0135  40  ASP A CA  
366   C C   . ASP A 40  ? 0.2789 0.1883 0.1895 0.0153  -0.0571 0.0109  40  ASP A C   
367   O O   . ASP A 40  ? 0.2645 0.1690 0.1676 0.0151  -0.0566 0.0107  40  ASP A O   
368   C CB  . ASP A 40  ? 0.3414 0.2570 0.2573 0.0158  -0.0651 0.0130  40  ASP A CB  
369   C CG  . ASP A 40  ? 0.5015 0.4230 0.4229 0.0176  -0.0696 0.0154  40  ASP A CG  
370   O OD1 . ASP A 40  ? 0.4643 0.3920 0.3938 0.0187  -0.0691 0.0154  40  ASP A OD1 
371   O OD2 . ASP A 40  ? 0.4553 0.3757 0.3730 0.0179  -0.0740 0.0174  40  ASP A OD2 
372   N N   . MET A 41  ? 0.3008 0.2132 0.2169 0.0143  -0.0539 0.0092  41  MET A N   
373   C CA  . MET A 41  ? 0.2546 0.1641 0.1687 0.0129  -0.0500 0.0072  41  MET A CA  
374   C C   . MET A 41  ? 0.2964 0.2023 0.2044 0.0140  -0.0476 0.0079  41  MET A C   
375   O O   . MET A 41  ? 0.4179 0.3198 0.3204 0.0138  -0.0463 0.0071  41  MET A O   
376   C CB  . MET A 41  ? 0.2171 0.1315 0.1384 0.0110  -0.0477 0.0063  41  MET A CB  
377   C CG  . MET A 41  ? 0.3068 0.2192 0.2279 0.0089  -0.0454 0.0046  41  MET A CG  
378   S SD  . MET A 41  ? 0.3602 0.2704 0.2828 0.0065  -0.0485 0.0039  41  MET A SD  
379   C CE  . MET A 41  ? 0.2410 0.1560 0.1674 0.0065  -0.0523 0.0058  41  MET A CE  
380   N N   . PRO A 42  ? 0.2167 0.1238 0.1256 0.0151  -0.0471 0.0096  42  PRO A N   
381   C CA  . PRO A 42  ? 0.2170 0.1202 0.1195 0.0156  -0.0455 0.0114  42  PRO A CA  
382   C C   . PRO A 42  ? 0.3240 0.2239 0.2191 0.0160  -0.0487 0.0142  42  PRO A C   
383   O O   . PRO A 42  ? 0.3345 0.2315 0.2228 0.0155  -0.0472 0.0160  42  PRO A O   
384   C CB  . PRO A 42  ? 0.2193 0.1242 0.1256 0.0165  -0.0453 0.0130  42  PRO A CB  
385   C CG  . PRO A 42  ? 0.2333 0.1424 0.1464 0.0177  -0.0483 0.0130  42  PRO A CG  
386   C CD  . PRO A 42  ? 0.2611 0.1728 0.1768 0.0161  -0.0480 0.0104  42  PRO A CD  
387   N N   . ALA A 43  ? 0.2958 0.1966 0.1917 0.0166  -0.0531 0.0152  43  ALA A N   
388   C CA  . ALA A 43  ? 0.2713 0.1699 0.1598 0.0165  -0.0568 0.0187  43  ALA A CA  
389   C C   . ALA A 43  ? 0.3071 0.2033 0.1876 0.0153  -0.0558 0.0175  43  ALA A C   
390   O O   . ALA A 43  ? 0.4076 0.3026 0.2795 0.0145  -0.0580 0.0206  43  ALA A O   
391   C CB  . ALA A 43  ? 0.2906 0.1919 0.1830 0.0175  -0.0622 0.0202  43  ALA A CB  
392   N N   . TYR A 44  ? 0.2721 0.1678 0.1549 0.0151  -0.0530 0.0134  44  TYR A N   
393   C CA  . TYR A 44  ? 0.2436 0.1368 0.1192 0.0147  -0.0519 0.0120  44  TYR A CA  
394   C C   . TYR A 44  ? 0.2944 0.1870 0.1625 0.0141  -0.0489 0.0141  44  TYR A C   
395   O O   . TYR A 44  ? 0.2823 0.1748 0.1413 0.0134  -0.0489 0.0146  44  TYR A O   
396   C CB  . TYR A 44  ? 0.2663 0.1585 0.1470 0.0149  -0.0499 0.0079  44  TYR A CB  
397   C CG  . TYR A 44  ? 0.3349 0.2274 0.2209 0.0144  -0.0532 0.0062  44  TYR A CG  
398   C CD1 . TYR A 44  ? 0.3345 0.2306 0.2295 0.0136  -0.0535 0.0059  44  TYR A CD1 
399   C CD2 . TYR A 44  ? 0.2592 0.1492 0.1408 0.0144  -0.0561 0.0052  44  TYR A CD2 
400   C CE1 . TYR A 44  ? 0.2432 0.1406 0.1431 0.0125  -0.0565 0.0052  44  TYR A CE1 
401   C CE2 . TYR A 44  ? 0.2137 0.1038 0.1002 0.0135  -0.0595 0.0041  44  TYR A CE2 
402   C CZ  . TYR A 44  ? 0.1883 0.0822 0.0841 0.0123  -0.0596 0.0044  44  TYR A CZ  
403   O OH  . TYR A 44  ? 0.2419 0.1367 0.1425 0.0107  -0.0629 0.0042  44  TYR A OH  
404   N N   . LEU A 45  ? 0.2945 0.1876 0.1658 0.0141  -0.0463 0.0153  45  LEU A N   
405   C CA  . LEU A 45  ? 0.3761 0.2691 0.2411 0.0131  -0.0432 0.0177  45  LEU A CA  
406   C C   . LEU A 45  ? 0.3304 0.2238 0.1855 0.0114  -0.0459 0.0227  45  LEU A C   
407   O O   . LEU A 45  ? 0.4126 0.3074 0.2597 0.0095  -0.0435 0.0248  45  LEU A O   
408   C CB  . LEU A 45  ? 0.3079 0.2013 0.1789 0.0132  -0.0406 0.0182  45  LEU A CB  
409   C CG  . LEU A 45  ? 0.2994 0.1939 0.1778 0.0137  -0.0370 0.0139  45  LEU A CG  
410   C CD1 . LEU A 45  ? 0.3196 0.2154 0.2026 0.0133  -0.0347 0.0145  45  LEU A CD1 
411   C CD2 . LEU A 45  ? 0.2511 0.1453 0.1254 0.0138  -0.0341 0.0123  45  LEU A CD2 
412   N N   . LYS A 46  ? 0.2803 0.1735 0.1354 0.0115  -0.0511 0.0251  46  LYS A N   
413   C CA  . LYS A 46  ? 0.3825 0.2766 0.2276 0.0095  -0.0546 0.0304  46  LYS A CA  
414   C C   . LYS A 46  ? 0.3073 0.2039 0.1427 0.0079  -0.0551 0.0289  46  LYS A C   
415   O O   . LYS A 46  ? 0.3507 0.2501 0.1746 0.0052  -0.0559 0.0323  46  LYS A O   
416   C CB  . LYS A 46  ? 0.3663 0.2598 0.2155 0.0104  -0.0607 0.0339  46  LYS A CB  
417   C CG  . LYS A 46  ? 0.3316 0.2239 0.1922 0.0127  -0.0605 0.0335  46  LYS A CG  
418   C CD  . LYS A 46  ? 0.5489 0.4401 0.4108 0.0133  -0.0662 0.0396  46  LYS A CD  
419   C CE  . LYS A 46  ? 0.5791 0.4723 0.4490 0.0156  -0.0707 0.0386  46  LYS A CE  
420   N NZ  . LYS A 46  ? 0.3967 0.2890 0.2662 0.0162  -0.0778 0.0451  46  LYS A NZ  
421   N N   . ASP A 47  ? 0.3799 0.2762 0.2192 0.0094  -0.0548 0.0237  47  ASP A N   
422   C CA  . ASP A 47  ? 0.3197 0.2185 0.1503 0.0082  -0.0560 0.0213  47  ASP A CA  
423   C C   . ASP A 47  ? 0.3355 0.2360 0.1624 0.0082  -0.0509 0.0168  47  ASP A C   
424   O O   . ASP A 47  ? 0.3932 0.2982 0.2101 0.0065  -0.0510 0.0143  47  ASP A O   
425   C CB  . ASP A 47  ? 0.2993 0.1963 0.1358 0.0096  -0.0598 0.0185  47  ASP A CB  
426   C CG  . ASP A 47  ? 0.4117 0.3092 0.2505 0.0094  -0.0654 0.0226  47  ASP A CG  
427   O OD1 . ASP A 47  ? 0.5336 0.4337 0.3630 0.0073  -0.0692 0.0256  47  ASP A OD1 
428   O OD2 . ASP A 47  ? 0.5002 0.3965 0.3499 0.0112  -0.0662 0.0227  47  ASP A OD2 
429   N N   . PHE A 48  ? 0.3947 0.2931 0.2291 0.0099  -0.0467 0.0152  48  PHE A N   
430   C CA  . PHE A 48  ? 0.3212 0.2217 0.1539 0.0105  -0.0424 0.0110  48  PHE A CA  
431   C C   . PHE A 48  ? 0.3712 0.2737 0.2034 0.0096  -0.0376 0.0131  48  PHE A C   
432   O O   . PHE A 48  ? 0.4133 0.3128 0.2522 0.0100  -0.0373 0.0161  48  PHE A O   
433   C CB  . PHE A 48  ? 0.3207 0.2166 0.1638 0.0136  -0.0427 0.0069  48  PHE A CB  
434   C CG  . PHE A 48  ? 0.2842 0.1781 0.1282 0.0141  -0.0475 0.0048  48  PHE A CG  
435   C CD1 . PHE A 48  ? 0.2684 0.1599 0.1190 0.0142  -0.0511 0.0067  48  PHE A CD1 
436   C CD2 . PHE A 48  ? 0.2806 0.1763 0.1186 0.0141  -0.0485 0.0003  48  PHE A CD2 
437   C CE1 . PHE A 48  ? 0.2581 0.1483 0.1096 0.0142  -0.0556 0.0052  48  PHE A CE1 
438   C CE2 . PHE A 48  ? 0.2423 0.1359 0.0811 0.0142  -0.0533 -0.0016 48  PHE A CE2 
439   C CZ  . PHE A 48  ? 0.2381 0.1288 0.0837 0.0142  -0.0568 0.0014  48  PHE A CZ  
440   N N   . GLU A 49  ? 0.3771 0.2859 0.2012 0.0080  -0.0338 0.0108  49  GLU A N   
441   C CA  . GLU A 49  ? 0.3768 0.2894 0.1991 0.0064  -0.0290 0.0129  49  GLU A CA  
442   C C   . GLU A 49  ? 0.3573 0.2683 0.1889 0.0090  -0.0255 0.0099  49  GLU A C   
443   O O   . GLU A 49  ? 0.4392 0.3567 0.2677 0.0084  -0.0212 0.0066  49  GLU A O   
444   C CB  . GLU A 49  ? 0.3648 0.2881 0.1731 0.0027  -0.0260 0.0114  49  GLU A CB  
445   C CG  . GLU A 49  ? 0.5506 0.4762 0.3484 -0.0002 -0.0298 0.0155  49  GLU A CG  
446   C CD  . GLU A 49  ? 0.7383 0.6561 0.5409 -0.0001 -0.0337 0.0233  49  GLU A CD  
447   O OE1 . GLU A 49  ? 0.6655 0.5816 0.4715 -0.0006 -0.0315 0.0270  49  GLU A OE1 
448   O OE2 . GLU A 49  ? 0.7677 0.6818 0.5710 0.0004  -0.0391 0.0251  49  GLU A OE2 
449   N N   . ILE A 50  ? 0.2900 0.1938 0.1332 0.0117  -0.0275 0.0104  50  ILE A N   
450   C CA  . ILE A 50  ? 0.2066 0.1088 0.0593 0.0139  -0.0252 0.0085  50  ILE A CA  
451   C C   . ILE A 50  ? 0.2584 0.1580 0.1188 0.0134  -0.0248 0.0112  50  ILE A C   
452   O O   . ILE A 50  ? 0.3112 0.2095 0.1703 0.0122  -0.0269 0.0140  50  ILE A O   
453   C CB  . ILE A 50  ? 0.1993 0.0976 0.0584 0.0168  -0.0280 0.0046  50  ILE A CB  
454   C CG1 . ILE A 50  ? 0.2524 0.1463 0.1177 0.0169  -0.0320 0.0052  50  ILE A CG1 
455   C CG2 . ILE A 50  ? 0.3309 0.2320 0.1821 0.0171  -0.0291 0.0006  50  ILE A CG2 
456   C CD1 . ILE A 50  ? 0.3115 0.2023 0.1848 0.0184  -0.0345 0.0021  50  ILE A CD1 
457   N N   . LYS A 51  ? 0.3200 0.2198 0.1881 0.0143  -0.0225 0.0099  51  LYS A N   
458   C CA  . LYS A 51  ? 0.2249 0.1245 0.1001 0.0134  -0.0218 0.0108  51  LYS A CA  
459   C C   . LYS A 51  ? 0.2239 0.1227 0.1082 0.0142  -0.0237 0.0077  51  LYS A C   
460   O O   . LYS A 51  ? 0.1935 0.0921 0.0805 0.0153  -0.0242 0.0053  51  LYS A O   
461   C CB  . LYS A 51  ? 0.2549 0.1576 0.1313 0.0124  -0.0175 0.0121  51  LYS A CB  
462   C CG  . LYS A 51  ? 0.3296 0.2354 0.1965 0.0103  -0.0150 0.0153  51  LYS A CG  
463   C CD  . LYS A 51  ? 0.2810 0.1852 0.1428 0.0083  -0.0171 0.0192  51  LYS A CD  
464   C CE  . LYS A 51  ? 0.3263 0.2343 0.1812 0.0051  -0.0142 0.0233  51  LYS A CE  
465   N NZ  . LYS A 51  ? 0.3838 0.2990 0.2315 0.0040  -0.0106 0.0220  51  LYS A NZ  
466   N N   . LEU A 52  ? 0.2417 0.1410 0.1301 0.0133  -0.0251 0.0080  52  LEU A N   
467   C CA  . LEU A 52  ? 0.1975 0.0986 0.0936 0.0128  -0.0268 0.0056  52  LEU A CA  
468   C C   . LEU A 52  ? 0.1819 0.0859 0.0823 0.0116  -0.0259 0.0064  52  LEU A C   
469   O O   . LEU A 52  ? 0.2126 0.1151 0.1098 0.0117  -0.0261 0.0087  52  LEU A O   
470   C CB  . LEU A 52  ? 0.2816 0.1809 0.1773 0.0133  -0.0308 0.0049  52  LEU A CB  
471   C CG  . LEU A 52  ? 0.2694 0.1654 0.1609 0.0145  -0.0327 0.0037  52  LEU A CG  
472   C CD1 . LEU A 52  ? 0.2350 0.1299 0.1269 0.0144  -0.0368 0.0036  52  LEU A CD1 
473   C CD2 . LEU A 52  ? 0.2761 0.1722 0.1714 0.0146  -0.0325 0.0014  52  LEU A CD2 
474   N N   . ASN A 53  ? 0.2513 0.1592 0.1584 0.0101  -0.0254 0.0051  53  ASN A N   
475   C CA  . ASN A 53  ? 0.1386 0.0496 0.0496 0.0089  -0.0242 0.0058  53  ASN A CA  
476   C C   . ASN A 53  ? 0.2128 0.1271 0.1293 0.0078  -0.0263 0.0049  53  ASN A C   
477   O O   . ASN A 53  ? 0.2351 0.1507 0.1547 0.0068  -0.0280 0.0040  53  ASN A O   
478   C CB  . ASN A 53  ? 0.1436 0.0575 0.0571 0.0074  -0.0214 0.0059  53  ASN A CB  
479   C CG  . ASN A 53  ? 0.1903 0.1020 0.0989 0.0084  -0.0190 0.0072  53  ASN A CG  
480   O OD1 . ASN A 53  ? 0.2568 0.1672 0.1623 0.0082  -0.0174 0.0091  53  ASN A OD1 
481   N ND2 . ASN A 53  ? 0.1835 0.0947 0.0912 0.0092  -0.0191 0.0064  53  ASN A ND2 
482   N N   . PHE A 54  ? 0.1756 0.0911 0.0935 0.0081  -0.0263 0.0058  54  PHE A N   
483   C CA  . PHE A 54  ? 0.1598 0.0786 0.0825 0.0077  -0.0282 0.0056  54  PHE A CA  
484   C C   . PHE A 54  ? 0.2455 0.1676 0.1715 0.0066  -0.0266 0.0061  54  PHE A C   
485   O O   . PHE A 54  ? 0.1791 0.0990 0.1027 0.0073  -0.0251 0.0068  54  PHE A O   
486   C CB  . PHE A 54  ? 0.1678 0.0844 0.0886 0.0102  -0.0312 0.0065  54  PHE A CB  
487   C CG  . PHE A 54  ? 0.2055 0.1185 0.1221 0.0110  -0.0329 0.0064  54  PHE A CG  
488   C CD1 . PHE A 54  ? 0.1965 0.1105 0.1152 0.0102  -0.0348 0.0053  54  PHE A CD1 
489   C CD2 . PHE A 54  ? 0.2221 0.1304 0.1321 0.0123  -0.0329 0.0078  54  PHE A CD2 
490   C CE1 . PHE A 54  ? 0.1803 0.0904 0.0945 0.0111  -0.0367 0.0051  54  PHE A CE1 
491   C CE2 . PHE A 54  ? 0.1788 0.0839 0.0840 0.0129  -0.0345 0.0080  54  PHE A CE2 
492   C CZ  . PHE A 54  ? 0.2033 0.1090 0.1105 0.0125  -0.0364 0.0063  54  PHE A CZ  
493   N N   . ASN A 55  ? 0.1610 0.0879 0.0922 0.0046  -0.0271 0.0061  55  ASN A N   
494   C CA  . ASN A 55  ? 0.1881 0.1185 0.1222 0.0036  -0.0259 0.0067  55  ASN A CA  
495   C C   . ASN A 55  ? 0.2193 0.1522 0.1559 0.0057  -0.0280 0.0072  55  ASN A C   
496   O O   . ASN A 55  ? 0.2848 0.2202 0.2236 0.0055  -0.0300 0.0075  55  ASN A O   
497   C CB  . ASN A 55  ? 0.1913 0.1268 0.1295 -0.0011 -0.0249 0.0074  55  ASN A CB  
498   C CG  . ASN A 55  ? 0.1953 0.1342 0.1348 -0.0030 -0.0232 0.0082  55  ASN A CG  
499   O OD1 . ASN A 55  ? 0.2344 0.1714 0.1720 -0.0034 -0.0213 0.0079  55  ASN A OD1 
500   N ND2 . ASN A 55  ? 0.1866 0.1316 0.1288 -0.0044 -0.0239 0.0093  55  ASN A ND2 
501   N N   . LEU A 56  ? 0.1870 0.1191 0.1234 0.0079  -0.0278 0.0075  56  LEU A N   
502   C CA  . LEU A 56  ? 0.1303 0.0656 0.0705 0.0112  -0.0304 0.0079  56  LEU A CA  
503   C C   . LEU A 56  ? 0.2233 0.1556 0.1598 0.0109  -0.0317 0.0068  56  LEU A C   
504   O O   . LEU A 56  ? 0.3548 0.2791 0.2868 0.0117  -0.0308 0.0063  56  LEU A O   
505   C CB  . LEU A 56  ? 0.1488 0.0783 0.0887 0.0159  -0.0329 0.0084  56  LEU A CB  
506   C CG  . LEU A 56  ? 0.1282 0.0543 0.0647 0.0165  -0.0349 0.0088  56  LEU A CG  
507   C CD1 . LEU A 56  ? 0.1388 0.0593 0.0748 0.0200  -0.0375 0.0107  56  LEU A CD1 
508   C CD2 . LEU A 56  ? 0.1259 0.0568 0.0657 0.0166  -0.0374 0.0086  56  LEU A CD2 
509   N N   . THR A 57  ? 0.1718 0.1102 0.1077 0.0091  -0.0346 0.0061  57  THR A N   
510   C CA  . THR A 57  ? 0.1981 0.1378 0.1266 0.0071  -0.0376 0.0016  57  THR A CA  
511   C C   . THR A 57  ? 0.2430 0.1814 0.1840 0.0147  -0.0374 -0.0061 57  THR A C   
512   O O   . THR A 57  ? 0.2672 0.2043 0.2142 0.0216  -0.0426 -0.0057 57  THR A O   
513   C CB  . THR A 57  ? 0.2189 0.1792 0.1520 -0.0014 -0.0362 -0.0010 57  THR A CB  
514   O OG1 . THR A 57  ? 0.2033 0.1695 0.1427 0.0021  -0.0406 -0.0011 57  THR A OG1 
515   C CG2 . THR A 57  ? 0.1719 0.1394 0.1100 -0.0076 -0.0298 0.0052  57  THR A CG2 
516   N N   . PRO A 58  ? 0.2016 0.1400 0.1481 0.0137  -0.0319 -0.0131 58  PRO A N   
517   C CA  . PRO A 58  ? 0.2065 0.1430 0.1683 0.0215  -0.0320 -0.0214 58  PRO A CA  
518   C C   . PRO A 58  ? 0.2376 0.1927 0.2142 0.0226  -0.0323 -0.0301 58  PRO A C   
519   O O   . PRO A 58  ? 0.2120 0.1643 0.2019 0.0317  -0.0361 -0.0336 58  PRO A O   
520   C CB  . PRO A 58  ? 0.1920 0.1272 0.1559 0.0177  -0.0252 -0.0286 58  PRO A CB  
521   C CG  . PRO A 58  ? 0.2063 0.1366 0.1536 0.0100  -0.0232 -0.0204 58  PRO A CG  
522   C CD  . PRO A 58  ? 0.2087 0.1488 0.1490 0.0054  -0.0260 -0.0142 58  PRO A CD  
523   N N   . VAL A 59  ? 0.2484 0.2233 0.2238 0.0132  -0.0288 -0.0332 59  VAL A N   
524   C CA  . VAL A 59  ? 0.1318 0.1272 0.1211 0.0128  -0.0284 -0.0415 59  VAL A CA  
525   C C   . VAL A 59  ? 0.1683 0.1604 0.1592 0.0193  -0.0368 -0.0348 59  VAL A C   
526   O O   . VAL A 59  ? 0.2160 0.2166 0.2227 0.0253  -0.0390 -0.0409 59  VAL A O   
527   C CB  . VAL A 59  ? 0.1453 0.1626 0.1303 -0.0009 -0.0233 -0.0445 59  VAL A CB  
528   C CG1 . VAL A 59  ? 0.2157 0.2269 0.1828 -0.0080 -0.0266 -0.0315 59  VAL A CG1 
529   C CG2 . VAL A 59  ? 0.1192 0.1593 0.1169 -0.0027 -0.0233 -0.0514 59  VAL A CG2 
530   N N   . LEU A 60  ? 0.2147 0.1949 0.1900 0.0183  -0.0418 -0.0226 60  LEU A N   
531   C CA  . LEU A 60  ? 0.2111 0.1864 0.1861 0.0243  -0.0500 -0.0163 60  LEU A CA  
532   C C   . LEU A 60  ? 0.1768 0.1363 0.1579 0.0359  -0.0548 -0.0151 60  LEU A C   
533   O O   . LEU A 60  ? 0.2834 0.2452 0.2736 0.0420  -0.0609 -0.0150 60  LEU A O   
534   C CB  . LEU A 60  ? 0.2059 0.1719 0.1631 0.0204  -0.0536 -0.0052 60  LEU A CB  
535   C CG  . LEU A 60  ? 0.2007 0.1631 0.1604 0.0227  -0.0544 0.0002  60  LEU A CG  
536   C CD1 . LEU A 60  ? 0.2106 0.1894 0.1795 0.0223  -0.0590 -0.0030 60  LEU A CD1 
537   C CD2 . LEU A 60  ? 0.1891 0.1492 0.1439 0.0161  -0.0466 0.0061  60  LEU A CD2 
538   N N   . ILE A 61  ? 0.2037 0.1471 0.1801 0.0385  -0.0528 -0.0134 61  ILE A N   
539   C CA  . ILE A 61  ? 0.2308 0.1598 0.2126 0.0468  -0.0569 -0.0110 61  ILE A CA  
540   C C   . ILE A 61  ? 0.2555 0.1918 0.2609 0.0547  -0.0588 -0.0215 61  ILE A C   
541   O O   . ILE A 61  ? 0.2715 0.2070 0.2841 0.0575  -0.0619 -0.0186 61  ILE A O   
542   C CB  . ILE A 61  ? 0.2095 0.1268 0.1831 0.0432  -0.0514 -0.0075 61  ILE A CB  
543   C CG1 . ILE A 61  ? 0.2617 0.1786 0.2185 0.0347  -0.0472 0.0004  61  ILE A CG1 
544   C CG2 . ILE A 61  ? 0.2099 0.1223 0.1909 0.0456  -0.0516 -0.0046 61  ILE A CG2 
545   C CD1 . ILE A 61  ? 0.2542 0.1647 0.2051 0.0311  -0.0419 0.0025  61  ILE A CD1 
546   N N   . ASP A 62  ? 0.2398 0.1923 0.2559 0.0505  -0.0509 -0.0336 62  ASP A N   
547   C CA  . ASP A 62  ? 0.1880 0.1525 0.2290 0.0565  -0.0503 -0.0462 62  ASP A CA  
548   C C   . ASP A 62  ? 0.2237 0.2025 0.2747 0.0593  -0.0558 -0.0463 62  ASP A C   
549   O O   . ASP A 62  ? 0.2220 0.2004 0.2916 0.0688  -0.0614 -0.0497 62  ASP A O   
550   C CB  . ASP A 62  ? 0.2121 0.1948 0.2602 0.0493  -0.0395 -0.0602 62  ASP A CB  
551   C CG  . ASP A 62  ? 0.3313 0.3004 0.3748 0.0479  -0.0346 -0.0627 62  ASP A CG  
552   O OD1 . ASP A 62  ? 0.3349 0.2808 0.3745 0.0541  -0.0397 -0.0550 62  ASP A OD1 
553   O OD2 . ASP A 62  ? 0.3602 0.3423 0.4032 0.0397  -0.0258 -0.0719 62  ASP A OD2 
554   N N   . GLN A 63  ? 0.2281 0.2191 0.2679 0.0511  -0.0551 -0.0423 63  GLN A N   
555   C CA  . GLN A 63  ? 0.1514 0.1574 0.2002 0.0522  -0.0600 -0.0426 63  GLN A CA  
556   C C   . GLN A 63  ? 0.1947 0.1845 0.2389 0.0598  -0.0712 -0.0313 63  GLN A C   
557   O O   . GLN A 63  ? 0.2415 0.2383 0.3006 0.0655  -0.0770 -0.0329 63  GLN A O   
558   C CB  . GLN A 63  ? 0.1308 0.1529 0.1684 0.0400  -0.0568 -0.0409 63  GLN A CB  
559   C CG  . GLN A 63  ? 0.1261 0.1723 0.1723 0.0314  -0.0470 -0.0532 63  GLN A CG  
560   C CD  . GLN A 63  ? 0.2448 0.3027 0.2763 0.0177  -0.0447 -0.0485 63  GLN A CD  
561   O OE1 . GLN A 63  ? 0.3199 0.4013 0.3585 0.0106  -0.0425 -0.0537 63  GLN A OE1 
562   N NE2 . GLN A 63  ? 0.2860 0.3280 0.2976 0.0135  -0.0455 -0.0384 63  GLN A NE2 
563   N N   . ILE A 64  ? 0.2788 0.2485 0.3013 0.0573  -0.0724 -0.0198 64  ILE A N   
564   C CA  . ILE A 64  ? 0.2075 0.1661 0.2203 0.0548  -0.0728 -0.0099 64  ILE A CA  
565   C C   . ILE A 64  ? 0.2005 0.1539 0.2268 0.0609  -0.0749 -0.0112 64  ILE A C   
566   O O   . ILE A 64  ? 0.2148 0.1694 0.2457 0.0625  -0.0787 -0.0078 64  ILE A O   
567   C CB  . ILE A 64  ? 0.1556 0.1020 0.1473 0.0474  -0.0672 -0.0014 64  ILE A CB  
568   C CG1 . ILE A 64  ? 0.1457 0.0977 0.1264 0.0401  -0.0644 0.0012  64  ILE A CG1 
569   C CG2 . ILE A 64  ? 0.1634 0.1028 0.1512 0.0466  -0.0669 0.0053  64  ILE A CG2 
570   C CD1 . ILE A 64  ? 0.2565 0.2017 0.2239 0.0337  -0.0572 0.0051  64  ILE A CD1 
571   N N   . GLN A 65  ? 0.1729 0.1206 0.2061 0.0640  -0.0724 -0.0159 65  GLN A N   
572   C CA  . GLN A 65  ? 0.2091 0.1514 0.2556 0.0689  -0.0742 -0.0166 65  GLN A CA  
573   C C   . GLN A 65  ? 0.2392 0.1955 0.3102 0.0754  -0.0777 -0.0260 65  GLN A C   
574   O O   . GLN A 65  ? 0.2873 0.2409 0.3668 0.0788  -0.0822 -0.0230 65  GLN A O   
575   C CB  . GLN A 65  ? 0.3255 0.2591 0.3738 0.0694  -0.0696 -0.0202 65  GLN A CB  
576   C CG  . GLN A 65  ? 0.2327 0.1530 0.2599 0.0633  -0.0664 -0.0097 65  GLN A CG  
577   C CD  . GLN A 65  ? 0.2971 0.2080 0.3271 0.0638  -0.0627 -0.0116 65  GLN A CD  
578   O OE1 . GLN A 65  ? 0.3364 0.2496 0.3720 0.0642  -0.0586 -0.0205 65  GLN A OE1 
579   N NE2 . GLN A 65  ? 0.4131 0.3140 0.4394 0.0633  -0.0639 -0.0036 65  GLN A NE2 
580   N N   . GLU A 66  ? 0.2853 0.2594 0.3694 0.0769  -0.0754 -0.0381 66  GLU A N   
581   C CA  . GLU A 66  ? 0.2712 0.2640 0.3815 0.0820  -0.0764 -0.0493 66  GLU A CA  
582   C C   . GLU A 66  ? 0.2421 0.2398 0.3519 0.0820  -0.0830 -0.0423 66  GLU A C   
583   O O   . GLU A 66  ? 0.2695 0.2723 0.3967 0.0867  -0.0863 -0.0451 66  GLU A O   
584   C CB  . GLU A 66  ? 0.2537 0.2715 0.3779 0.0810  -0.0697 -0.0652 66  GLU A CB  
585   C CG  . GLU A 66  ? 0.2992 0.3307 0.4496 0.0844  -0.0638 -0.0817 66  GLU A CG  
586   C CD  . GLU A 66  ? 0.2590 0.3238 0.4234 0.0802  -0.0552 -0.0981 66  GLU A CD  
587   O OE1 . GLU A 66  ? 0.2576 0.3281 0.4018 0.0688  -0.0493 -0.0951 66  GLU A OE1 
588   O OE2 . GLU A 66  ? 0.2948 0.3775 0.4806 0.0816  -0.0521 -0.1099 66  GLU A OE2 
589   N N   . TYR A 67  ? 0.2707 0.2669 0.3606 0.0762  -0.0846 -0.0332 67  TYR A N   
590   C CA  . TYR A 67  ? 0.2171 0.2158 0.3035 0.0747  -0.0896 -0.0258 67  TYR A CA  
591   C C   . TYR A 67  ? 0.2317 0.2131 0.3106 0.0756  -0.0929 -0.0156 67  TYR A C   
592   O O   . TYR A 67  ? 0.2565 0.2415 0.3437 0.0782  -0.0979 -0.0132 67  TYR A O   
593   C CB  . TYR A 67  ? 0.2500 0.2505 0.3162 0.0667  -0.0887 -0.0193 67  TYR A CB  
594   C CG  . TYR A 67  ? 0.1827 0.2072 0.2581 0.0637  -0.0877 -0.0275 67  TYR A CG  
595   C CD1 . TYR A 67  ? 0.1872 0.2205 0.2620 0.0609  -0.0836 -0.0341 67  TYR A CD1 
596   C CD2 . TYR A 67  ? 0.2200 0.2612 0.3043 0.0619  -0.0903 -0.0284 67  TYR A CD2 
597   C CE1 . TYR A 67  ? 0.1491 0.2083 0.2297 0.0534  -0.0802 -0.0412 67  TYR A CE1 
598   C CE2 . TYR A 67  ? 0.2683 0.3345 0.3598 0.0558  -0.0879 -0.0354 67  TYR A CE2 
599   C CZ  . TYR A 67  ? 0.1393 0.2155 0.2288 0.0509  -0.0829 -0.0419 67  TYR A CZ  
600   O OH  . TYR A 67  ? 0.2112 0.3135 0.3044 0.0406  -0.0783 -0.0480 67  TYR A OH  
601   N N   . ALA A 68  ? 0.2946 0.2595 0.3584 0.0732  -0.0901 -0.0095 68  ALA A N   
602   C CA  . ALA A 68  ? 0.2387 0.1909 0.2952 0.0729  -0.0925 -0.0001 68  ALA A CA  
603   C C   . ALA A 68  ? 0.2223 0.1725 0.2988 0.0802  -0.0970 -0.0030 68  ALA A C   
604   O O   . ALA A 68  ? 0.3832 0.3262 0.4581 0.0811  -0.1015 0.0044  68  ALA A O   
605   C CB  . ALA A 68  ? 0.3479 0.2872 0.3853 0.0678  -0.0874 0.0059  68  ALA A CB  
606   N N   . GLN A 69  ? 0.2196 0.1765 0.3157 0.0851  -0.0955 -0.0144 69  GLN A N   
607   C CA  . GLN A 69  ? 0.2394 0.1962 0.3582 0.0922  -0.0991 -0.0194 69  GLN A CA  
608   C C   . GLN A 69  ? 0.2579 0.2325 0.3992 0.0969  -0.1025 -0.0274 69  GLN A C   
609   O O   . GLN A 69  ? 0.3567 0.3341 0.5204 0.1031  -0.1049 -0.0339 69  GLN A O   
610   C CB  . GLN A 69  ? 0.4034 0.3573 0.5319 0.0944  -0.0940 -0.0287 69  GLN A CB  
611   C CG  . GLN A 69  ? 0.6085 0.5467 0.7165 0.0895  -0.0900 -0.0216 69  GLN A CG  
612   C CD  . GLN A 69  ? 0.6290 0.5640 0.7475 0.0916  -0.0853 -0.0308 69  GLN A CD  
613   O OE1 . GLN A 69  ? 0.4728 0.4067 0.5815 0.0877  -0.0790 -0.0335 69  GLN A OE1 
614   N NE2 . GLN A 69  ? 0.6036 0.5371 0.7425 0.0974  -0.0883 -0.0359 69  GLN A NE2 
615   N N   . GLY A 70  ? 0.2396 0.2269 0.3762 0.0939  -0.1025 -0.0273 70  GLY A N   
616   C CA  . GLY A 70  ? 0.2200 0.2271 0.3778 0.0973  -0.1048 -0.0350 70  GLY A CA  
617   C C   . GLY A 70  ? 0.2490 0.2730 0.4314 0.1010  -0.0992 -0.0523 70  GLY A C   
618   O O   . GLY A 70  ? 0.2242 0.2586 0.4308 0.1065  -0.1008 -0.0603 70  GLY A O   
619   N N   . LYS A 71  ? 0.2979 0.3260 0.4745 0.0976  -0.0919 -0.0591 71  LYS A N   
620   C CA  . LYS A 71  ? 0.3621 0.4081 0.5595 0.0991  -0.0840 -0.0770 71  LYS A CA  
621   C C   . LYS A 71  ? 0.3569 0.4288 0.5554 0.0933  -0.0775 -0.0861 71  LYS A C   
622   O O   . LYS A 71  ? 0.3988 0.4932 0.6164 0.0928  -0.0700 -0.1022 71  LYS A O   
623   C CB  . LYS A 71  ? 0.3252 0.3564 0.5180 0.0991  -0.0792 -0.0798 71  LYS A CB  
624   C CG  . LYS A 71  ? 0.2985 0.3110 0.4979 0.1043  -0.0839 -0.0756 71  LYS A CG  
625   C CD  . LYS A 71  ? 0.3493 0.3464 0.5400 0.1027  -0.0793 -0.0758 71  LYS A CD  
626   C CE  . LYS A 71  ? 0.3442 0.3288 0.5486 0.1080  -0.0828 -0.0763 71  LYS A CE  
627   N NZ  . LYS A 71  ? 0.2988 0.2798 0.5072 0.1071  -0.0757 -0.0858 71  LYS A NZ  
628   N N   . ALA A 72  ? 0.2284 0.2991 0.4063 0.0877  -0.0797 -0.0762 72  ALA A N   
629   C CA  . ALA A 72  ? 0.2597 0.3566 0.4371 0.0801  -0.0742 -0.0829 72  ALA A CA  
630   C C   . ALA A 72  ? 0.1692 0.2914 0.3628 0.0784  -0.0743 -0.0885 72  ALA A C   
631   O O   . ALA A 72  ? 0.3071 0.4235 0.4975 0.0798  -0.0820 -0.0784 72  ALA A O   
632   C CB  . ALA A 72  ? 0.2763 0.3625 0.4259 0.0737  -0.0781 -0.0690 72  ALA A CB  
633   N N   . LYS A 73  ? 0.1576 0.3082 0.3670 0.0739  -0.0646 -0.1045 73  LYS A N   
634   C CA  . LYS A 73  ? 0.2368 0.4141 0.4596 0.0699  -0.0627 -0.1103 73  LYS A CA  
635   C C   . LYS A 73  ? 0.2603 0.4525 0.4654 0.0564  -0.0610 -0.1042 73  LYS A C   
636   O O   . LYS A 73  ? 0.2787 0.4943 0.4832 0.0454  -0.0513 -0.1129 73  LYS A O   
637   C CB  . LYS A 73  ? 0.3086 0.5070 0.5532 0.0699  -0.0522 -0.1299 73  LYS A CB  
638   C CG  . LYS A 73  ? 0.4145 0.5957 0.6751 0.0814  -0.0539 -0.1358 73  LYS A CG  
639   C CD  . LYS A 73  ? 0.4149 0.6090 0.6863 0.0785  -0.0419 -0.1545 73  LYS A CD  
640   C CE  . LYS A 73  ? 0.5228 0.6920 0.7865 0.0820  -0.0414 -0.1533 73  LYS A CE  
641   N NZ  . LYS A 73  ? 0.3597 0.5405 0.6322 0.0779  -0.0300 -0.1711 73  LYS A NZ  
642   N N   . ASP A 74  ? 0.2938 0.4693 0.4810 0.0555  -0.0705 -0.0877 74  ASP A N   
643   C CA  . ASP A 74  ? 0.2582 0.4388 0.4240 0.0422  -0.0705 -0.0786 74  ASP A CA  
644   C C   . ASP A 74  ? 0.2325 0.4347 0.4065 0.0359  -0.0699 -0.0795 74  ASP A C   
645   O O   . ASP A 74  ? 0.1783 0.3754 0.3579 0.0413  -0.0774 -0.0734 74  ASP A O   
646   C CB  . ASP A 74  ? 0.2727 0.4233 0.4145 0.0436  -0.0794 -0.0614 74  ASP A CB  
647   C CG  . ASP A 74  ? 0.2682 0.4170 0.3855 0.0299  -0.0783 -0.0519 74  ASP A CG  
648   O OD1 . ASP A 74  ? 0.3206 0.4881 0.4386 0.0195  -0.0750 -0.0526 74  ASP A OD1 
649   O OD2 . ASP A 74  ? 0.2820 0.4083 0.3786 0.0292  -0.0802 -0.0428 74  ASP A OD2 
650   N N   . VAL A 75  ? 0.3104 0.5359 0.4833 0.0235  -0.0607 -0.0860 75  VAL A N   
651   C CA  . VAL A 75  ? 0.2816 0.5294 0.4641 0.0173  -0.0585 -0.0886 75  VAL A CA  
652   C C   . VAL A 75  ? 0.2266 0.4642 0.3940 0.0115  -0.0672 -0.0723 75  VAL A C   
653   O O   . VAL A 75  ? 0.1890 0.4356 0.3677 0.0128  -0.0712 -0.0711 75  VAL A O   
654   C CB  . VAL A 75  ? 0.3262 0.5981 0.5066 0.0042  -0.0457 -0.0984 75  VAL A CB  
655   C CG1 . VAL A 75  ? 0.1550 0.4288 0.3405 0.0073  -0.0374 -0.1115 75  VAL A CG1 
656   C CG2 . VAL A 75  ? 0.2812 0.5483 0.4349 -0.0114 -0.0449 -0.0857 75  VAL A CG2 
657   N N   . PHE A 76  ? 0.2279 0.4458 0.3703 0.0050  -0.0701 -0.0600 76  PHE A N   
658   C CA  . PHE A 76  ? 0.1780 0.3822 0.3060 -0.0005 -0.0780 -0.0452 76  PHE A CA  
659   C C   . PHE A 76  ? 0.2096 0.3965 0.3386 0.0106  -0.0874 -0.0382 76  PHE A C   
660   O O   . PHE A 76  ? 0.1960 0.3830 0.3257 0.0090  -0.0933 -0.0313 76  PHE A O   
661   C CB  . PHE A 76  ? 0.2226 0.4074 0.3248 -0.0101 -0.0777 -0.0351 76  PHE A CB  
662   C CG  . PHE A 76  ? 0.2076 0.3732 0.2963 -0.0150 -0.0860 -0.0223 76  PHE A CG  
663   C CD1 . PHE A 76  ? 0.2856 0.4590 0.3746 -0.0234 -0.0858 -0.0220 76  PHE A CD1 
664   C CD2 . PHE A 76  ? 0.2842 0.4249 0.3593 -0.0112 -0.0924 -0.0115 76  PHE A CD2 
665   C CE1 . PHE A 76  ? 0.3289 0.4829 0.4080 -0.0241 -0.0931 -0.0159 76  PHE A CE1 
666   C CE2 . PHE A 76  ? 0.3230 0.4409 0.3853 -0.0139 -0.0965 -0.0040 76  PHE A CE2 
667   C CZ  . PHE A 76  ? 0.2991 0.4248 0.3658 -0.0155 -0.0982 -0.0125 76  PHE A CZ  
668   N N   . LEU A 77  ? 0.3491 0.5199 0.4768 0.0212  -0.0886 -0.0393 77  LEU A N   
669   C CA  . LEU A 77  ? 0.2433 0.3950 0.3691 0.0312  -0.0960 -0.0322 77  LEU A CA  
670   C C   . LEU A 77  ? 0.2267 0.3926 0.3766 0.0383  -0.0993 -0.0375 77  LEU A C   
671   O O   . LEU A 77  ? 0.3272 0.4849 0.4743 0.0411  -0.1057 -0.0294 77  LEU A O   
672   C CB  . LEU A 77  ? 0.2222 0.3525 0.3425 0.0402  -0.0959 -0.0326 77  LEU A CB  
673   C CG  . LEU A 77  ? 0.3082 0.4129 0.4158 0.0461  -0.1014 -0.0218 77  LEU A CG  
674   C CD1 . LEU A 77  ? 0.2046 0.2990 0.2877 0.0372  -0.1013 -0.0105 77  LEU A CD1 
675   C CD2 . LEU A 77  ? 0.3013 0.3852 0.4038 0.0532  -0.1005 -0.0220 77  LEU A CD2 
676   N N   . GLU A 78  ? 0.2018 0.3895 0.3752 0.0411  -0.0938 -0.0517 78  GLU A N   
677   C CA  . GLU A 78  ? 0.1936 0.3966 0.3919 0.0474  -0.0959 -0.0577 78  GLU A CA  
678   C C   . GLU A 78  ? 0.1542 0.3721 0.3524 0.0386  -0.0986 -0.0523 78  GLU A C   
679   O O   . GLU A 78  ? 0.1606 0.3830 0.3717 0.0436  -0.1042 -0.0505 78  GLU A O   
680   C CB  . GLU A 78  ? 0.2412 0.4649 0.4630 0.0506  -0.0869 -0.0756 78  GLU A CB  
681   C CG  . GLU A 78  ? 0.3607 0.5949 0.6103 0.0603  -0.0887 -0.0834 78  GLU A CG  
682   C CD  . GLU A 78  ? 0.7385 1.0037 1.0082 0.0566  -0.0783 -0.1002 78  GLU A CD  
683   O OE1 . GLU A 78  ? 0.7804 1.0492 1.0580 0.0591  -0.0702 -0.1131 78  GLU A OE1 
684   O OE2 . GLU A 78  ? 0.6826 0.9683 0.9592 0.0505  -0.0778 -0.1005 78  GLU A OE2 
685   N N   . ALA A 79  ? 0.1551 0.3795 0.3387 0.0251  -0.0951 -0.0488 79  ALA A N   
686   C CA  . ALA A 79  ? 0.1491 0.3836 0.3311 0.0155  -0.0984 -0.0422 79  ALA A CA  
687   C C   . ALA A 79  ? 0.1591 0.3736 0.3251 0.0157  -0.1078 -0.0273 79  ALA A C   
688   O O   . ALA A 79  ? 0.2978 0.5205 0.4707 0.0144  -0.1130 -0.0233 79  ALA A O   
689   C CB  . ALA A 79  ? 0.1449 0.3852 0.3138 0.0006  -0.0927 -0.0415 79  ALA A CB  
690   N N   . ILE A 80  ? 0.1551 0.3452 0.2989 0.0169  -0.1087 -0.0198 80  ILE A N   
691   C CA  . ILE A 80  ? 0.1576 0.3313 0.2842 0.0181  -0.1138 -0.0087 80  ILE A CA  
692   C C   . ILE A 80  ? 0.1669 0.3381 0.3069 0.0303  -0.1192 -0.0098 80  ILE A C   
693   O O   . ILE A 80  ? 0.2823 0.4547 0.4202 0.0301  -0.1243 -0.0044 80  ILE A O   
694   C CB  . ILE A 80  ? 0.1552 0.3046 0.2563 0.0180  -0.1106 -0.0036 80  ILE A CB  
695   C CG1 . ILE A 80  ? 0.1476 0.2995 0.2348 0.0054  -0.1056 -0.0011 80  ILE A CG1 
696   C CG2 . ILE A 80  ? 0.1623 0.2957 0.2469 0.0209  -0.1132 0.0034  80  ILE A CG2 
697   C CD1 . ILE A 80  ? 0.1825 0.3407 0.2585 -0.0034 -0.1037 0.0023  80  ILE A CD1 
698   N N   . ARG A 81  ? 0.1687 0.3362 0.3228 0.0406  -0.1184 -0.0170 81  ARG A N   
699   C CA  . ARG A 81  ? 0.1801 0.3416 0.3469 0.0517  -0.1241 -0.0168 81  ARG A CA  
700   C C   . ARG A 81  ? 0.1846 0.3693 0.3740 0.0525  -0.1277 -0.0199 81  ARG A C   
701   O O   . ARG A 81  ? 0.1951 0.3757 0.3875 0.0571  -0.1344 -0.0147 81  ARG A O   
702   C CB  . ARG A 81  ? 0.1818 0.3363 0.3614 0.0614  -0.1216 -0.0249 81  ARG A CB  
703   C CG  . ARG A 81  ? 0.2804 0.4218 0.4687 0.0718  -0.1278 -0.0223 81  ARG A CG  
704   C CD  . ARG A 81  ? 0.3636 0.4869 0.5513 0.0784  -0.1255 -0.0254 81  ARG A CD  
705   N NE  . ARG A 81  ? 0.5111 0.6104 0.6861 0.0821  -0.1309 -0.0152 81  ARG A NE  
706   C CZ  . ARG A 81  ? 0.5316 0.6096 0.6941 0.0839  -0.1292 -0.0124 81  ARG A CZ  
707   N NH1 . ARG A 81  ? 0.6104 0.6867 0.7717 0.0834  -0.1229 -0.0189 81  ARG A NH1 
708   N NH2 . ARG A 81  ? 0.4544 0.5141 0.6056 0.0855  -0.1338 -0.0029 81  ARG A NH2 
709   N N   . LYS A 82  ? 0.2370 0.4120 0.3901 0.0591  -0.0370 -0.1261 82  LYS A N   
710   C CA  . LYS A 82  ? 0.1929 0.3986 0.3778 0.0653  -0.0381 -0.1376 82  LYS A CA  
711   C C   . LYS A 82  ? 0.2292 0.4425 0.4264 0.0603  -0.0451 -0.1334 82  LYS A C   
712   O O   . LYS A 82  ? 0.2330 0.4387 0.4188 0.0483  -0.0424 -0.1232 82  LYS A O   
713   C CB  . LYS A 82  ? 0.1775 0.4181 0.3745 0.0599  -0.0208 -0.1440 82  LYS A CB  
714   C CG  . LYS A 82  ? 0.1852 0.4404 0.3942 0.0714  -0.0171 -0.1608 82  LYS A CG  
715   C CD  . LYS A 82  ? 0.1797 0.4771 0.4015 0.0642  0.0006  -0.1672 82  LYS A CD  
716   C CE  . LYS A 82  ? 0.2565 0.5609 0.4697 0.0681  0.0096  -0.1788 82  LYS A CE  
717   N NZ  . LYS A 82  ? 0.4178 0.7546 0.6303 0.0569  0.0255  -0.1791 82  LYS A NZ  
718   N N   . ASP A 83  ? 0.2360 0.4650 0.4592 0.0700  -0.0547 -0.1427 83  ASP A N   
719   C CA  . ASP A 83  ? 0.1983 0.4459 0.4412 0.0645  -0.0591 -0.1426 83  ASP A CA  
720   C C   . ASP A 83  ? 0.2587 0.5379 0.5170 0.0520  -0.0417 -0.1430 83  ASP A C   
721   O O   . ASP A 83  ? 0.3360 0.6377 0.6044 0.0540  -0.0297 -0.1502 83  ASP A O   
722   C CB  . ASP A 83  ? 0.2524 0.5148 0.5237 0.0783  -0.0731 -0.1531 83  ASP A CB  
723   C CG  . ASP A 83  ? 0.2427 0.5195 0.5311 0.0730  -0.0820 -0.1527 83  ASP A CG  
724   O OD1 . ASP A 83  ? 0.3162 0.6168 0.6210 0.0630  -0.0706 -0.1542 83  ASP A OD1 
725   O OD2 . ASP A 83  ? 0.2328 0.4919 0.5118 0.0767  -0.0993 -0.1486 83  ASP A OD2 
726   N N   . PRO A 84  ? 0.2101 0.4923 0.4710 0.0386  -0.0398 -0.1354 84  PRO A N   
727   C CA  . PRO A 84  ? 0.2243 0.5333 0.4991 0.0248  -0.0232 -0.1317 84  PRO A CA  
728   C C   . PRO A 84  ? 0.2254 0.5688 0.5271 0.0270  -0.0164 -0.1405 84  PRO A C   
729   O O   . PRO A 84  ? 0.2237 0.5856 0.5269 0.0176  -0.0004 -0.1360 84  PRO A O   
730   C CB  . PRO A 84  ? 0.1950 0.4959 0.4730 0.0122  -0.0273 -0.1240 84  PRO A CB  
731   C CG  . PRO A 84  ? 0.2069 0.4709 0.4583 0.0174  -0.0410 -0.1212 84  PRO A CG  
732   C CD  . PRO A 84  ? 0.2345 0.4949 0.4849 0.0344  -0.0523 -0.1297 84  PRO A CD  
733   N N   . ASP A 85  ? 0.1886 0.5346 0.5047 0.0383  -0.0281 -0.1498 85  ASP A N   
734   C CA  . ASP A 85  ? 0.2110 0.5827 0.5475 0.0413  -0.0216 -0.1578 85  ASP A CA  
735   C C   . ASP A 85  ? 0.1830 0.5637 0.5124 0.0466  -0.0096 -0.1646 85  ASP A C   
736   O O   . ASP A 85  ? 0.2381 0.6444 0.5801 0.0441  0.0015  -0.1693 85  ASP A O   
737   C CB  . ASP A 85  ? 0.2410 0.6103 0.5935 0.0542  -0.0384 -0.1664 85  ASP A CB  
738   C CG  . ASP A 85  ? 0.3828 0.7616 0.7525 0.0463  -0.0446 -0.1635 85  ASP A CG  
739   O OD1 . ASP A 85  ? 0.4501 0.8338 0.8200 0.0308  -0.0364 -0.1549 85  ASP A OD1 
740   O OD2 . ASP A 85  ? 0.4042 0.7846 0.7878 0.0553  -0.0581 -0.1693 85  ASP A OD2 
741   N N   . ASP A 86  ? 0.1803 0.5410 0.4895 0.0535  -0.0116 -0.1658 86  ASP A N   
742   C CA  . ASP A 86  ? 0.1875 0.5533 0.4881 0.0590  -0.0022 -0.1744 86  ASP A CA  
743   C C   . ASP A 86  ? 0.1825 0.5597 0.4655 0.0454  0.0154  -0.1663 86  ASP A C   
744   O O   . ASP A 86  ? 0.1918 0.5797 0.4674 0.0472  0.0248  -0.1739 86  ASP A O   
745   C CB  . ASP A 86  ? 0.1904 0.5267 0.4782 0.0728  -0.0138 -0.1794 86  ASP A CB  
746   C CG  . ASP A 86  ? 0.2738 0.5967 0.5768 0.0872  -0.0322 -0.1854 86  ASP A CG  
747   O OD1 . ASP A 86  ? 0.3904 0.7314 0.7155 0.0907  -0.0330 -0.1930 86  ASP A OD1 
748   O OD2 . ASP A 86  ? 0.3211 0.6153 0.6134 0.0949  -0.0463 -0.1814 86  ASP A OD2 
749   N N   . LEU A 87  ? 0.1710 0.5458 0.4472 0.0317  0.0191  -0.1510 87  LEU A N   
750   C CA  . LEU A 87  ? 0.1677 0.5461 0.4236 0.0196  0.0325  -0.1398 87  LEU A CA  
751   C C   . LEU A 87  ? 0.1783 0.5860 0.4387 0.0093  0.0475  -0.1359 87  LEU A C   
752   O O   . LEU A 87  ? 0.1810 0.6037 0.4614 0.0031  0.0491  -0.1323 87  LEU A O   
753   C CB  . LEU A 87  ? 0.1547 0.5177 0.4045 0.0085  0.0302  -0.1240 87  LEU A CB  
754   C CG  . LEU A 87  ? 0.1523 0.4753 0.3816 0.0155  0.0171  -0.1221 87  LEU A CG  
755   C CD1 . LEU A 87  ? 0.1657 0.4669 0.3861 0.0034  0.0145  -0.1061 87  LEU A CD1 
756   C CD2 . LEU A 87  ? 0.1584 0.4678 0.3617 0.0203  0.0207  -0.1237 87  LEU A CD2 
757   N N   . GLU A 88  ? 0.2099 0.6261 0.4514 0.0071  0.0578  -0.1365 88  GLU A N   
758   C CA  . GLU A 88  ? 0.2679 0.7114 0.5083 -0.0039 0.0719  -0.1301 88  GLU A CA  
759   C C   . GLU A 88  ? 0.2071 0.6478 0.4396 -0.0208 0.0777  -0.1059 88  GLU A C   
760   O O   . GLU A 88  ? 0.2517 0.6696 0.4743 -0.0236 0.0725  -0.0959 88  GLU A O   
761   C CB  . GLU A 88  ? 0.2133 0.6671 0.4346 -0.0005 0.0789  -0.1402 88  GLU A CB  
762   C CG  . GLU A 88  ? 0.2192 0.6686 0.4483 0.0166  0.0716  -0.1641 88  GLU A CG  
763   C CD  . GLU A 88  ? 0.3422 0.8099 0.6006 0.0228  0.0703  -0.1762 88  GLU A CD  
764   O OE1 . GLU A 88  ? 0.2862 0.7794 0.5544 0.0129  0.0800  -0.1699 88  GLU A OE1 
765   O OE2 . GLU A 88  ? 0.3048 0.7607 0.5773 0.0374  0.0592  -0.1908 88  GLU A OE2 
766   N N   . LYS A 89  ? 0.2079 0.6717 0.4466 -0.0319 0.0884  -0.0962 89  LYS A N   
767   C CA  . LYS A 89  ? 0.2621 0.7218 0.4983 -0.0478 0.0933  -0.0717 89  LYS A CA  
768   C C   . LYS A 89  ? 0.3088 0.7536 0.5153 -0.0521 0.0946  -0.0596 89  LYS A C   
769   O O   . LYS A 89  ? 0.3412 0.7698 0.5457 -0.0617 0.0935  -0.0405 89  LYS A O   
770   C CB  . LYS A 89  ? 0.4209 0.9092 0.6681 -0.0582 0.1050  -0.0637 89  LYS A CB  
771   C CG  . LYS A 89  ? 0.4100 0.9213 0.6826 -0.0517 0.1060  -0.0805 89  LYS A CG  
772   C CD  . LYS A 89  ? 0.3504 0.8530 0.6519 -0.0519 0.0970  -0.0798 89  LYS A CD  
773   C CE  . LYS A 89  ? 0.2311 0.7612 0.5607 -0.0502 0.1002  -0.0899 89  LYS A CE  
774   N NZ  . LYS A 89  ? 0.2611 0.8179 0.5952 -0.0633 0.1150  -0.0780 89  LYS A NZ  
775   N N   . GLU A 90  ? 0.3573 0.8064 0.5424 -0.0450 0.0962  -0.0711 90  GLU A N   
776   C CA  . GLU A 90  ? 0.3249 0.7600 0.4818 -0.0481 0.0959  -0.0612 90  GLU A CA  
777   C C   . GLU A 90  ? 0.2782 0.6838 0.4306 -0.0412 0.0858  -0.0640 90  GLU A C   
778   O O   . GLU A 90  ? 0.2349 0.6239 0.3717 -0.0469 0.0843  -0.0493 90  GLU A O   
779   C CB  . GLU A 90  ? 0.4822 0.9337 0.6189 -0.0441 0.1004  -0.0737 90  GLU A CB  
780   C CG  . GLU A 90  ? 0.5523 0.9971 0.6896 -0.0283 0.0943  -0.0994 90  GLU A CG  
781   C CD  . GLU A 90  ? 0.7539 1.2090 0.8703 -0.0257 0.0970  -0.1110 90  GLU A CD  
782   O OE1 . GLU A 90  ? 0.8727 1.3371 0.9695 -0.0360 0.1018  -0.0974 90  GLU A OE1 
783   O OE2 . GLU A 90  ? 0.7613 1.2141 0.8822 -0.0133 0.0930  -0.1336 90  GLU A OE2 
784   N N   . GLU A 91  ? 0.2324 0.6311 0.3985 -0.0287 0.0783  -0.0823 91  GLU A N   
785   C CA  . GLU A 91  ? 0.2523 0.6243 0.4158 -0.0224 0.0684  -0.0847 91  GLU A CA  
786   C C   . GLU A 91  ? 0.2251 0.5838 0.4006 -0.0316 0.0646  -0.0692 91  GLU A C   
787   O O   . GLU A 91  ? 0.2022 0.5321 0.3644 -0.0325 0.0585  -0.0611 91  GLU A O   
788   C CB  . GLU A 91  ? 0.1924 0.5594 0.3690 -0.0059 0.0593  -0.1068 91  GLU A CB  
789   C CG  . GLU A 91  ? 0.2915 0.6690 0.4618 0.0039  0.0619  -0.1246 91  GLU A CG  
790   C CD  . GLU A 91  ? 0.3199 0.6850 0.5040 0.0211  0.0506  -0.1439 91  GLU A CD  
791   O OE1 . GLU A 91  ? 0.3784 0.7182 0.5547 0.0291  0.0420  -0.1465 91  GLU A OE1 
792   O OE2 . GLU A 91  ? 0.3993 0.7788 0.6025 0.0270  0.0498  -0.1553 91  GLU A OE2 
793   N N   . VAL A 92  ? 0.1614 0.5316 0.3585 -0.0381 0.0663  -0.0643 92  VAL A N   
794   C CA  . VAL A 92  ? 0.1547 0.5116 0.3659 -0.0479 0.0624  -0.0509 92  VAL A CA  
795   C C   . VAL A 92  ? 0.1604 0.5095 0.3595 -0.0610 0.0685  -0.0277 92  VAL A C   
796   O O   . VAL A 92  ? 0.2553 0.5824 0.4538 -0.0658 0.0638  -0.0180 92  VAL A O   
797   C CB  . VAL A 92  ? 0.1592 0.5306 0.3988 -0.0512 0.0622  -0.0530 92  VAL A CB  
798   C CG1 . VAL A 92  ? 0.1555 0.5118 0.4112 -0.0622 0.0580  -0.0404 92  VAL A CG1 
799   C CG2 . VAL A 92  ? 0.1555 0.5310 0.4073 -0.0370 0.0534  -0.0747 92  VAL A CG2 
800   N N   . GLU A 93  ? 0.1758 0.5419 0.3656 -0.0664 0.0782  -0.0188 93  GLU A N   
801   C CA  . GLU A 93  ? 0.2980 0.6554 0.4759 -0.0772 0.0820  0.0040  93  GLU A CA  
802   C C   . GLU A 93  ? 0.2743 0.6125 0.4278 -0.0739 0.0779  0.0070  93  GLU A C   
803   O O   . GLU A 93  ? 0.3356 0.6561 0.4846 -0.0808 0.0763  0.0249  93  GLU A O   
804   C CB  . GLU A 93  ? 0.3529 0.7348 0.5224 -0.0828 0.0919  0.0107  93  GLU A CB  
805   C CG  . GLU A 93  ? 0.4768 0.8776 0.6718 -0.0894 0.0977  0.0129  93  GLU A CG  
806   C CD  . GLU A 93  ? 0.6915 1.0805 0.9010 -0.1026 0.0990  0.0350  93  GLU A CD  
807   O OE1 . GLU A 93  ? 0.6223 0.9839 0.8310 -0.1049 0.0928  0.0446  93  GLU A OE1 
808   O OE2 . GLU A 93  ? 0.8651 1.2721 1.0880 -0.1108 0.1065  0.0419  93  GLU A OE2 
809   N N   . LYS A 94  ? 0.3104 0.6507 0.4499 -0.0628 0.0757  -0.0109 94  LYS A N   
810   C CA  . LYS A 94  ? 0.1656 0.4875 0.2847 -0.0595 0.0715  -0.0098 94  LYS A CA  
811   C C   . LYS A 94  ? 0.1895 0.4776 0.3151 -0.0578 0.0619  -0.0076 94  LYS A C   
812   O O   . LYS A 94  ? 0.1901 0.4558 0.3049 -0.0609 0.0589  0.0048  94  LYS A O   
813   C CB  . LYS A 94  ? 0.1809 0.5097 0.2865 -0.0473 0.0710  -0.0315 94  LYS A CB  
814   C CG  . LYS A 94  ? 0.2242 0.5707 0.3103 -0.0483 0.0769  -0.0326 94  LYS A CG  
815   C CD  . LYS A 94  ? 0.3001 0.6560 0.3830 -0.0357 0.0765  -0.0585 94  LYS A CD  
816   C CE  . LYS A 94  ? 0.3738 0.7086 0.4431 -0.0270 0.0706  -0.0686 94  LYS A CE  
817   N NZ  . LYS A 94  ? 0.3526 0.6548 0.4317 -0.0184 0.0596  -0.0735 94  LYS A NZ  
818   N N   . LEU A 95  ? 0.2900 0.5702 0.4314 -0.0518 0.0556  -0.0201 95  LEU A N   
819   C CA  . LEU A 95  ? 0.2218 0.4670 0.3649 -0.0491 0.0452  -0.0204 95  LEU A CA  
820   C C   . LEU A 95  ? 0.2414 0.4789 0.3997 -0.0615 0.0464  -0.0034 95  LEU A C   
821   O O   . LEU A 95  ? 0.2708 0.4790 0.4256 -0.0612 0.0402  -0.0004 95  LEU A O   
822   C CB  . LEU A 95  ? 0.2175 0.4610 0.3738 -0.0406 0.0374  -0.0371 95  LEU A CB  
823   C CG  . LEU A 95  ? 0.2797 0.4981 0.4187 -0.0273 0.0272  -0.0496 95  LEU A CG  
824   C CD1 . LEU A 95  ? 0.4209 0.6503 0.5475 -0.0186 0.0301  -0.0595 95  LEU A CD1 
825   C CD2 . LEU A 95  ? 0.1817 0.3960 0.3352 -0.0215 0.0173  -0.0607 95  LEU A CD2 
826   N N   . ILE A 96  ? 0.2770 0.5408 0.4544 -0.0726 0.0544  0.0072  96  ILE A N   
827   C CA  . ILE A 96  ? 0.2360 0.4917 0.4310 -0.0852 0.0555  0.0254  96  ILE A CA  
828   C C   . ILE A 96  ? 0.2947 0.5393 0.4728 -0.0888 0.0577  0.0435  96  ILE A C   
829   O O   . ILE A 96  ? 0.3618 0.5811 0.5453 -0.0919 0.0536  0.0530  96  ILE A O   
830   C CB  . ILE A 96  ? 0.1709 0.4461 0.3882 -0.0931 0.0615  0.0308  96  ILE A CB  
831   C CG1 . ILE A 96  ? 0.1556 0.4374 0.3980 -0.0919 0.0564  0.0154  96  ILE A CG1 
832   C CG2 . ILE A 96  ? 0.2762 0.5353 0.5019 -0.1035 0.0636  0.0499  96  ILE A CG2 
833   C CD1 . ILE A 96  ? 0.1644 0.4725 0.4220 -0.0934 0.0623  0.0126  96  ILE A CD1 
834   N N   . GLU A 97  ? 0.3020 0.5618 0.4582 -0.0866 0.0630  0.0460  97  GLU A N   
835   C CA  . GLU A 97  ? 0.3155 0.5650 0.4528 -0.0885 0.0629  0.0615  97  GLU A CA  
836   C C   . GLU A 97  ? 0.3231 0.5494 0.4511 -0.0840 0.0567  0.0601  97  GLU A C   
837   O O   . GLU A 97  ? 0.3212 0.5279 0.4482 -0.0864 0.0535  0.0739  97  GLU A O   
838   C CB  . GLU A 97  ? 0.3535 0.6269 0.4679 -0.0865 0.0681  0.0597  97  GLU A CB  
839   C CG  . GLU A 97  ? 0.4812 0.7597 0.5872 -0.0937 0.0701  0.0794  97  GLU A CG  
840   C CD  . GLU A 97  ? 0.6629 0.9633 0.7426 -0.0916 0.0727  0.0760  97  GLU A CD  
841   O OE1 . GLU A 97  ? 0.4559 0.7499 0.5181 -0.0859 0.0690  0.0697  97  GLU A OE1 
842   O OE2 . GLU A 97  ? 0.8620 1.1868 0.9393 -0.0961 0.0784  0.0788  97  GLU A OE2 
843   N N   . PHE A 98  ? 0.2769 0.4968 0.3950 -0.0742 0.0530  0.0409  98  PHE A N   
844   C CA  . PHE A 98  ? 0.2471 0.4347 0.3521 -0.0671 0.0457  0.0362  98  PHE A CA  
845   C C   . PHE A 98  ? 0.2218 0.3845 0.3453 -0.0700 0.0410  0.0403  98  PHE A C   
846   O O   . PHE A 98  ? 0.2986 0.4412 0.4192 -0.0701 0.0383  0.0474  98  PHE A O   
847   C CB  . PHE A 98  ? 0.2500 0.4296 0.3407 -0.0549 0.0413  0.0147  98  PHE A CB  
848   C CG  . PHE A 98  ? 0.1442 0.2961 0.2169 -0.0486 0.0355  0.0109  98  PHE A CG  
849   C CD1 . PHE A 98  ? 0.1667 0.3194 0.2228 -0.0492 0.0370  0.0174  98  PHE A CD1 
850   C CD2 . PHE A 98  ? 0.2116 0.3391 0.2838 -0.0427 0.0287  0.0007  98  PHE A CD2 
851   C CE1 . PHE A 98  ? 0.1957 0.3247 0.2376 -0.0443 0.0322  0.0139  98  PHE A CE1 
852   C CE2 . PHE A 98  ? 0.2028 0.3072 0.2586 -0.0382 0.0246  -0.0020 98  PHE A CE2 
853   C CZ  . PHE A 98  ? 0.2269 0.3318 0.2689 -0.0390 0.0267  0.0046  98  PHE A CZ  
854   N N   . THR A 99  ? 0.1478 0.3129 0.2920 -0.0723 0.0401  0.0343  99  THR A N   
855   C CA  . THR A 99  ? 0.2291 0.3721 0.3925 -0.0753 0.0355  0.0344  99  THR A CA  
856   C C   . THR A 99  ? 0.2806 0.4214 0.4631 -0.0858 0.0383  0.0557  99  THR A C   
857   O O   . THR A 99  ? 0.2537 0.3710 0.4456 -0.0862 0.0347  0.0579  99  THR A O   
858   C CB  . THR A 99  ? 0.2418 0.3911 0.4239 -0.0760 0.0330  0.0220  99  THR A CB  
859   O OG1 . THR A 99  ? 0.2016 0.3568 0.3680 -0.0659 0.0298  0.0051  99  THR A OG1 
860   C CG2 . THR A 99  ? 0.1490 0.2740 0.3458 -0.0771 0.0268  0.0154  99  THR A CG2 
861   N N   . LYS A 100 ? 0.2595 0.4205 0.4440 -0.0923 0.0440  0.0688  100 LYS A N   
862   C CA  . LYS A 100 ? 0.1820 0.3309 0.3707 -0.0968 0.0438  0.0853  100 LYS A CA  
863   C C   . LYS A 100 ? 0.1847 0.3200 0.3575 -0.0925 0.0408  0.0940  100 LYS A C   
864   O O   . LYS A 100 ? 0.2390 0.3563 0.4212 -0.0931 0.0370  0.1037  100 LYS A O   
865   C CB  . LYS A 100 ? 0.2631 0.4348 0.4499 -0.1028 0.0497  0.0964  100 LYS A CB  
866   C CG  . LYS A 100 ? 0.2909 0.4796 0.4951 -0.1076 0.0537  0.0883  100 LYS A CG  
867   C CD  . LYS A 100 ? 0.4071 0.6032 0.6214 -0.1166 0.0574  0.1037  100 LYS A CD  
868   C CE  . LYS A 100 ? 0.5071 0.7332 0.7261 -0.1205 0.0652  0.0986  100 LYS A CE  
869   N NZ  . LYS A 100 ? 0.4637 0.7130 0.6585 -0.1150 0.0699  0.0948  100 LYS A NZ  
870   N N   . LEU A 101 ? 0.2613 0.4065 0.4117 -0.0878 0.0420  0.0900  101 LEU A N   
871   C CA  . LEU A 101 ? 0.1751 0.3099 0.3105 -0.0841 0.0388  0.0971  101 LEU A CA  
872   C C   . LEU A 101 ? 0.1676 0.2751 0.3125 -0.0803 0.0342  0.0911  101 LEU A C   
873   O O   . LEU A 101 ? 0.2175 0.3108 0.3649 -0.0785 0.0307  0.0995  101 LEU A O   
874   C CB  . LEU A 101 ? 0.1769 0.3295 0.2862 -0.0805 0.0411  0.0910  101 LEU A CB  
875   C CG  . LEU A 101 ? 0.2979 0.4468 0.3895 -0.0777 0.0379  0.0982  101 LEU A CG  
876   C CD1 . LEU A 101 ? 0.3798 0.5430 0.4661 -0.0815 0.0374  0.1144  101 LEU A CD1 
877   C CD2 . LEU A 101 ? 0.3276 0.4871 0.3967 -0.0736 0.0394  0.0853  101 LEU A CD2 
878   N N   . ASN A 102 ? 0.2407 0.3419 0.3917 -0.0783 0.0336  0.0755  102 ASN A N   
879   C CA  . ASN A 102 ? 0.2847 0.3591 0.4370 -0.0726 0.0294  0.0639  102 ASN A CA  
880   C C   . ASN A 102 ? 0.2130 0.2736 0.3954 -0.0764 0.0276  0.0606  102 ASN A C   
881   O O   . ASN A 102 ? 0.2705 0.3117 0.4546 -0.0721 0.0249  0.0472  102 ASN A O   
882   C CB  . ASN A 102 ? 0.1498 0.2189 0.2781 -0.0638 0.0273  0.0433  102 ASN A CB  
883   C CG  . ASN A 102 ? 0.1443 0.2277 0.2469 -0.0601 0.0288  0.0429  102 ASN A CG  
884   O OD1 . ASN A 102 ? 0.2477 0.3333 0.3403 -0.0604 0.0295  0.0521  102 ASN A OD1 
885   N ND2 . ASN A 102 ? 0.1607 0.2547 0.2546 -0.0564 0.0289  0.0309  102 ASN A ND2 
886   N N   . TYR A 103 ? 0.3161 0.3838 0.5117 -0.0815 0.0283  0.0679  103 TYR A N   
887   C CA  . TYR A 103 ? 0.2966 0.3524 0.5150 -0.0837 0.0257  0.0597  103 TYR A CA  
888   C C   . TYR A 103 ? 0.3071 0.3386 0.5363 -0.0797 0.0222  0.0571  103 TYR A C   
889   O O   . TYR A 103 ? 0.2931 0.3116 0.5322 -0.0778 0.0199  0.0405  103 TYR A O   
890   C CB  . TYR A 103 ? 0.1877 0.2554 0.4186 -0.0907 0.0275  0.0713  103 TYR A CB  
891   C CG  . TYR A 103 ? 0.2512 0.3128 0.5047 -0.0942 0.0251  0.0610  103 TYR A CG  
892   C CD1 . TYR A 103 ? 0.3029 0.3696 0.5587 -0.0936 0.0236  0.0427  103 TYR A CD1 
893   C CD2 . TYR A 103 ? 0.3432 0.3948 0.6174 -0.0977 0.0235  0.0694  103 TYR A CD2 
894   C CE1 . TYR A 103 ? 0.4413 0.5039 0.7169 -0.0967 0.0204  0.0320  103 TYR A CE1 
895   C CE2 . TYR A 103 ? 0.3765 0.4229 0.6720 -0.1011 0.0211  0.0591  103 TYR A CE2 
896   C CZ  . TYR A 103 ? 0.4247 0.4770 0.7197 -0.1007 0.0196  0.0400  103 TYR A CZ  
897   O OH  . TYR A 103 ? 0.5456 0.5941 0.8610 -0.1041 0.0163  0.0288  103 TYR A OH  
898   N N   . GLU A 104 ? 0.4224 0.4498 0.6507 -0.0778 0.0216  0.0720  104 GLU A N   
899   C CA  . GLU A 104 ? 0.3610 0.3693 0.6058 -0.0733 0.0185  0.0705  104 GLU A CA  
900   C C   . GLU A 104 ? 0.2641 0.2620 0.4984 -0.0671 0.0186  0.0584  104 GLU A C   
901   O O   . GLU A 104 ? 0.2523 0.2364 0.5015 -0.0626 0.0172  0.0534  104 GLU A O   
902   C CB  . GLU A 104 ? 0.3451 0.3553 0.5984 -0.0734 0.0164  0.0922  104 GLU A CB  
903   C CG  . GLU A 104 ? 0.6541 0.6824 0.8840 -0.0750 0.0178  0.1072  104 GLU A CG  
904   C CD  . GLU A 104 ? 0.6733 0.6993 0.8873 -0.0694 0.0171  0.1055  104 GLU A CD  
905   O OE1 . GLU A 104 ? 0.4613 0.5001 0.6508 -0.0699 0.0196  0.1045  104 GLU A OE1 
906   O OE2 . GLU A 104 ? 0.4767 0.4893 0.7044 -0.0644 0.0143  0.1044  104 GLU A OE2 
907   N N   . LYS A 105 ? 0.2468 0.2521 0.4582 -0.0667 0.0208  0.0534  105 LYS A N   
908   C CA  . LYS A 105 ? 0.1722 0.1676 0.3730 -0.0619 0.0215  0.0424  105 LYS A CA  
909   C C   . LYS A 105 ? 0.1759 0.1593 0.3830 -0.0607 0.0213  0.0199  105 LYS A C   
910   O O   . LYS A 105 ? 0.2433 0.2311 0.4523 -0.0637 0.0203  0.0107  105 LYS A O   
911   C CB  . LYS A 105 ? 0.1600 0.1663 0.3331 -0.0612 0.0234  0.0432  105 LYS A CB  
912   C CG  . LYS A 105 ? 0.1969 0.2194 0.3625 -0.0638 0.0239  0.0633  105 LYS A CG  
913   C CD  . LYS A 105 ? 0.2408 0.2743 0.3733 -0.0602 0.0247  0.0586  105 LYS A CD  
914   C CE  . LYS A 105 ? 0.1828 0.2351 0.3076 -0.0635 0.0255  0.0765  105 LYS A CE  
915   N NZ  . LYS A 105 ? 0.1675 0.2299 0.2618 -0.0596 0.0260  0.0686  105 LYS A NZ  
916   N N   . PRO A 106 ? 0.1698 0.1407 0.3801 -0.0562 0.0220  0.0096  106 PRO A N   
917   C CA  . PRO A 106 ? 0.1750 0.1374 0.3883 -0.0551 0.0219  -0.0134 106 PRO A CA  
918   C C   . PRO A 106 ? 0.1704 0.1368 0.3559 -0.0549 0.0212  -0.0270 106 PRO A C   
919   O O   . PRO A 106 ? 0.1768 0.1407 0.3627 -0.0554 0.0193  -0.0449 106 PRO A O   
920   C CB  . PRO A 106 ? 0.1789 0.1324 0.3968 -0.0500 0.0245  -0.0197 106 PRO A CB  
921   C CG  . PRO A 106 ? 0.1794 0.1348 0.4110 -0.0483 0.0236  0.0012  106 PRO A CG  
922   C CD  . PRO A 106 ? 0.1714 0.1382 0.3864 -0.0521 0.0226  0.0183  106 PRO A CD  
923   N N   . ILE A 107 ? 0.1630 0.1369 0.3199 -0.0522 0.0212  -0.0193 107 ILE A N   
924   C CA  . ILE A 107 ? 0.2212 0.1988 0.3485 -0.0491 0.0185  -0.0298 107 ILE A CA  
925   C C   . ILE A 107 ? 0.2800 0.2690 0.4109 -0.0511 0.0151  -0.0296 107 ILE A C   
926   O O   . ILE A 107 ? 0.2509 0.2442 0.3607 -0.0478 0.0116  -0.0367 107 ILE A O   
927   C CB  . ILE A 107 ? 0.1931 0.1722 0.2917 -0.0450 0.0194  -0.0236 107 ILE A CB  
928   C CG1 . ILE A 107 ? 0.1878 0.1786 0.2871 -0.0461 0.0200  -0.0073 107 ILE A CG1 
929   C CG2 . ILE A 107 ? 0.1973 0.1674 0.2934 -0.0435 0.0230  -0.0245 107 ILE A CG2 
930   C CD1 . ILE A 107 ? 0.1532 0.1481 0.2241 -0.0421 0.0190  -0.0063 107 ILE A CD1 
931   N N   . TYR A 108 ? 0.2183 0.2127 0.3769 -0.0567 0.0158  -0.0209 108 TYR A N   
932   C CA  . TYR A 108 ? 0.1774 0.1848 0.3451 -0.0600 0.0135  -0.0217 108 TYR A CA  
933   C C   . TYR A 108 ? 0.2205 0.2238 0.4180 -0.0655 0.0114  -0.0310 108 TYR A C   
934   O O   . TYR A 108 ? 0.2640 0.2785 0.4789 -0.0707 0.0103  -0.0288 108 TYR A O   
935   C CB  . TYR A 108 ? 0.1769 0.1992 0.3512 -0.0637 0.0168  -0.0025 108 TYR A CB  
936   C CG  . TYR A 108 ? 0.1499 0.1844 0.2965 -0.0587 0.0172  -0.0006 108 TYR A CG  
937   C CD1 . TYR A 108 ? 0.1700 0.1986 0.2930 -0.0536 0.0181  0.0014  108 TYR A CD1 
938   C CD2 . TYR A 108 ? 0.1781 0.2305 0.3251 -0.0592 0.0168  -0.0021 108 TYR A CD2 
939   C CE1 . TYR A 108 ? 0.2070 0.2452 0.3077 -0.0491 0.0180  0.0012  108 TYR A CE1 
940   C CE2 . TYR A 108 ? 0.2602 0.3236 0.3854 -0.0538 0.0172  -0.0029 108 TYR A CE2 
941   C CZ  . TYR A 108 ? 0.2429 0.2980 0.3451 -0.0488 0.0176  -0.0015 108 TYR A CZ  
942   O OH  . TYR A 108 ? 0.2179 0.2823 0.3013 -0.0435 0.0176  -0.0042 108 TYR A OH  
943   N N   . ARG A 109 ? 0.2773 0.2661 0.4830 -0.0650 0.0113  -0.0428 109 ARG A N   
944   C CA  . ARG A 109 ? 0.2700 0.2544 0.4993 -0.0677 0.0089  -0.0532 109 ARG A CA  
945   C C   . ARG A 109 ? 0.2945 0.2852 0.5143 -0.0681 0.0033  -0.0729 109 ARG A C   
946   O O   . ARG A 109 ? 0.1979 0.1835 0.4025 -0.0649 0.0014  -0.0897 109 ARG A O   
947   C CB  . ARG A 109 ? 0.1972 0.1678 0.4341 -0.0635 0.0111  -0.0590 109 ARG A CB  
948   C CG  . ARG A 109 ? 0.2534 0.2195 0.5212 -0.0647 0.0112  -0.0517 109 ARG A CG  
949   C CD  . ARG A 109 ? 0.2211 0.1773 0.5018 -0.0601 0.0124  -0.0654 109 ARG A CD  
950   N NE  . ARG A 109 ? 0.2156 0.1670 0.4843 -0.0553 0.0162  -0.0646 109 ARG A NE  
951   C CZ  . ARG A 109 ? 0.2394 0.1875 0.5178 -0.0531 0.0181  -0.0475 109 ARG A CZ  
952   N NH1 . ARG A 109 ? 0.3952 0.3436 0.6925 -0.0551 0.0163  -0.0287 109 ARG A NH1 
953   N NH2 . ARG A 109 ? 0.2216 0.1669 0.4896 -0.0490 0.0214  -0.0490 109 ARG A NH2 
954   N N   . PHE A 110 ? 0.2986 0.3034 0.5262 -0.0719 0.0003  -0.0700 110 PHE A N   
955   C CA  . PHE A 110 ? 0.2202 0.2343 0.4447 -0.0723 -0.0068 -0.0864 110 PHE A CA  
956   C C   . PHE A 110 ? 0.2638 0.2838 0.5162 -0.0773 -0.0076 -0.0833 110 PHE A C   
957   O O   . PHE A 110 ? 0.3143 0.3398 0.5818 -0.0813 -0.0035 -0.0657 110 PHE A O   
958   C CB  . PHE A 110 ? 0.2371 0.2651 0.4361 -0.0669 -0.0101 -0.0834 110 PHE A CB  
959   C CG  . PHE A 110 ? 0.2370 0.2576 0.3989 -0.0587 -0.0100 -0.0832 110 PHE A CG  
960   C CD1 . PHE A 110 ? 0.2163 0.2334 0.3558 -0.0551 -0.0159 -0.0978 110 PHE A CD1 
961   C CD2 . PHE A 110 ? 0.2501 0.2685 0.3997 -0.0556 -0.0043 -0.0678 110 PHE A CD2 
962   C CE1 . PHE A 110 ? 0.2240 0.2341 0.3307 -0.0489 -0.0155 -0.0955 110 PHE A CE1 
963   C CE2 . PHE A 110 ? 0.2488 0.2598 0.3672 -0.0492 -0.0042 -0.0676 110 PHE A CE2 
964   C CZ  . PHE A 110 ? 0.3164 0.3226 0.4140 -0.0461 -0.0096 -0.0807 110 PHE A CZ  
965   N N   . GLU A 111 ? 0.2132 0.2328 0.4708 -0.0775 -0.0127 -0.0998 111 GLU A N   
966   C CA  . GLU A 111 ? 0.2731 0.2984 0.5574 -0.0831 -0.0141 -0.0986 111 GLU A CA  
967   C C   . GLU A 111 ? 0.3160 0.3618 0.6045 -0.0863 -0.0160 -0.0920 111 GLU A C   
968   O O   . GLU A 111 ? 0.3491 0.4016 0.6588 -0.0923 -0.0132 -0.0804 111 GLU A O   
969   C CB  . GLU A 111 ? 0.3019 0.3252 0.5899 -0.0826 -0.0196 -0.1195 111 GLU A CB  
970   C CG  . GLU A 111 ? 0.4128 0.4384 0.7317 -0.0888 -0.0207 -0.1195 111 GLU A CG  
971   C CD  . GLU A 111 ? 0.5726 0.5845 0.9152 -0.0913 -0.0145 -0.1053 111 GLU A CD  
972   O OE1 . GLU A 111 ? 0.5753 0.5747 0.9123 -0.0869 -0.0104 -0.1012 111 GLU A OE1 
973   O OE2 . GLU A 111 ? 0.5398 0.5544 0.9069 -0.0977 -0.0143 -0.0976 111 GLU A OE2 
974   N N   . ARG A 112 ? 0.2707 0.3278 0.5392 -0.0821 -0.0209 -0.0994 112 ARG A N   
975   C CA  . ARG A 112 ? 0.2712 0.3509 0.5451 -0.0830 -0.0225 -0.0947 112 ARG A CA  
976   C C   . ARG A 112 ? 0.2581 0.3446 0.5390 -0.0860 -0.0131 -0.0736 112 ARG A C   
977   O O   . ARG A 112 ? 0.3357 0.4376 0.6337 -0.0911 -0.0098 -0.0639 112 ARG A O   
978   C CB  . ARG A 112 ? 0.2067 0.2950 0.4562 -0.0754 -0.0307 -0.1060 112 ARG A CB  
979   C CG  . ARG A 112 ? 0.1825 0.2946 0.4349 -0.0721 -0.0339 -0.1038 112 ARG A CG  
980   C CD  . ARG A 112 ? 0.2770 0.4038 0.5567 -0.0779 -0.0376 -0.1096 112 ARG A CD  
981   N NE  . ARG A 112 ? 0.3349 0.4859 0.6173 -0.0730 -0.0434 -0.1131 112 ARG A NE  
982   C CZ  . ARG A 112 ? 0.2605 0.4300 0.5659 -0.0769 -0.0427 -0.1115 112 ARG A CZ  
983   N NH1 . ARG A 112 ? 0.2424 0.4088 0.5693 -0.0868 -0.0371 -0.1056 112 ARG A NH1 
984   N NH2 . ARG A 112 ? 0.1849 0.3762 0.4921 -0.0703 -0.0480 -0.1155 112 ARG A NH2 
985   N N   . ILE A 113 ? 0.1764 0.2524 0.4416 -0.0830 -0.0084 -0.0654 113 ILE A N   
986   C CA  . ILE A 113 ? 0.2214 0.3045 0.4865 -0.0848 0.0003  -0.0443 113 ILE A CA  
987   C C   . ILE A 113 ? 0.2973 0.3779 0.5849 -0.0929 0.0049  -0.0295 113 ILE A C   
988   O O   . ILE A 113 ? 0.2950 0.3919 0.5883 -0.0976 0.0103  -0.0140 113 ILE A O   
989   C CB  . ILE A 113 ? 0.1694 0.2375 0.4064 -0.0779 0.0035  -0.0375 113 ILE A CB  
990   C CG1 . ILE A 113 ? 0.2256 0.2999 0.4292 -0.0676 0.0013  -0.0418 113 ILE A CG1 
991   C CG2 . ILE A 113 ? 0.2075 0.2776 0.4530 -0.0830 0.0114  -0.0154 113 ILE A CG2 
992   C CD1 . ILE A 113 ? 0.2980 0.3572 0.4745 -0.0615 0.0035  -0.0374 113 ILE A CD1 
993   N N   . ARG A 114 ? 0.3517 0.4123 0.6488 -0.0937 0.0026  -0.0343 114 ARG A N   
994   C CA  . ARG A 114 ? 0.3180 0.3741 0.6363 -0.1002 0.0050  -0.0222 114 ARG A CA  
995   C C   . ARG A 114 ? 0.3214 0.3970 0.6556 -0.1071 0.0045  -0.0217 114 ARG A C   
996   O O   . ARG A 114 ? 0.4058 0.4882 0.7520 -0.1142 0.0090  -0.0052 114 ARG A O   
997   C CB  . ARG A 114 ? 0.3736 0.4074 0.7035 -0.0982 0.0018  -0.0332 114 ARG A CB  
998   C CG  . ARG A 114 ? 0.3654 0.3874 0.7149 -0.1015 0.0045  -0.0177 114 ARG A CG  
999   C CD  . ARG A 114 ? 0.3975 0.3990 0.7464 -0.0947 0.0045  -0.0206 114 ARG A CD  
1000  N NE  . ARG A 114 ? 0.6755 0.6771 1.0006 -0.0897 0.0072  -0.0138 114 ARG A NE  
1001  C CZ  . ARG A 114 ? 0.6244 0.6154 0.9373 -0.0829 0.0069  -0.0254 114 ARG A CZ  
1002  N NH1 . ARG A 114 ? 0.5877 0.5689 0.9079 -0.0798 0.0045  -0.0450 114 ARG A NH1 
1003  N NH2 . ARG A 114 ? 0.4867 0.4788 0.7792 -0.0795 0.0095  -0.0176 114 ARG A NH2 
1004  N N   . GLU A 115 ? 0.2248 0.3109 0.5587 -0.1052 -0.0013 -0.0396 115 GLU A N   
1005  C CA  . GLU A 115 ? 0.2276 0.3335 0.5787 -0.1111 -0.0025 -0.0411 115 GLU A CA  
1006  C C   . GLU A 115 ? 0.2032 0.3368 0.5502 -0.1124 0.0029  -0.0303 115 GLU A C   
1007  O O   . GLU A 115 ? 0.2511 0.4008 0.6125 -0.1204 0.0074  -0.0198 115 GLU A O   
1008  C CB  . GLU A 115 ? 0.2176 0.3261 0.5698 -0.1077 -0.0120 -0.0644 115 GLU A CB  
1009  C CG  . GLU A 115 ? 0.3186 0.4053 0.6772 -0.1075 -0.0165 -0.0773 115 GLU A CG  
1010  C CD  . GLU A 115 ? 0.3377 0.4273 0.6863 -0.1025 -0.0261 -0.1005 115 GLU A CD  
1011  O OE1 . GLU A 115 ? 0.4399 0.5497 0.7867 -0.1011 -0.0310 -0.1058 115 GLU A OE1 
1012  O OE2 . GLU A 115 ? 0.3434 0.4170 0.6853 -0.0994 -0.0289 -0.1132 115 GLU A OE2 
1013  N N   . LEU A 116 ? 0.2464 0.3874 0.5745 -0.1047 0.0031  -0.0338 116 LEU A N   
1014  C CA  . LEU A 116 ? 0.2002 0.3698 0.5257 -0.1042 0.0089  -0.0268 116 LEU A CA  
1015  C C   . LEU A 116 ? 0.2512 0.4280 0.5764 -0.1117 0.0192  -0.0039 116 LEU A C   
1016  O O   . LEU A 116 ? 0.2324 0.4354 0.5645 -0.1170 0.0252  0.0035  116 LEU A O   
1017  C CB  . LEU A 116 ? 0.1607 0.3349 0.4665 -0.0936 0.0074  -0.0358 116 LEU A CB  
1018  C CG  . LEU A 116 ? 0.2286 0.4048 0.5247 -0.0836 -0.0035 -0.0566 116 LEU A CG  
1019  C CD1 . LEU A 116 ? 0.2355 0.4320 0.5537 -0.0861 -0.0080 -0.0650 116 LEU A CD1 
1020  C CD2 . LEU A 116 ? 0.2361 0.3847 0.5168 -0.0796 -0.0114 -0.0670 116 LEU A CD2 
1021  N N   . MET A 117 ? 0.2425 0.3977 0.5578 -0.1119 0.0213  0.0070  117 MET A N   
1022  C CA  . MET A 117 ? 0.2200 0.3808 0.5301 -0.1180 0.0297  0.0281  117 MET A CA  
1023  C C   . MET A 117 ? 0.3784 0.5419 0.7081 -0.1287 0.0320  0.0372  117 MET A C   
1024  O O   . MET A 117 ? 0.3677 0.5462 0.6955 -0.1352 0.0399  0.0518  117 MET A O   
1025  C CB  . MET A 117 ? 0.2147 0.3504 0.5110 -0.1141 0.0293  0.0369  117 MET A CB  
1026  C CG  . MET A 117 ? 0.3302 0.4639 0.6069 -0.1049 0.0283  0.0298  117 MET A CG  
1027  S SD  . MET A 117 ? 0.3283 0.4978 0.5952 -0.1019 0.0338  0.0270  117 MET A SD  
1028  C CE  . MET A 117 ? 0.2791 0.4645 0.5363 -0.1090 0.0440  0.0488  117 MET A CE  
1029  N N   . ASN A 118 ? 0.3822 0.5314 0.7308 -0.1308 0.0256  0.0278  118 ASN A N   
1030  C CA  . ASN A 118 ? 0.3356 0.4874 0.7066 -0.1413 0.0271  0.0349  118 ASN A CA  
1031  C C   . ASN A 118 ? 0.3018 0.4835 0.6851 -0.1467 0.0284  0.0279  118 ASN A C   
1032  O O   . ASN A 118 ? 0.3454 0.5340 0.7476 -0.1570 0.0309  0.0343  118 ASN A O   
1033  C CB  . ASN A 118 ? 0.3387 0.4618 0.7272 -0.1409 0.0198  0.0269  118 ASN A CB  
1034  C CG  . ASN A 118 ? 0.4135 0.5116 0.8022 -0.1395 0.0204  0.0404  118 ASN A CG  
1035  O OD1 . ASN A 118 ? 0.3045 0.3978 0.6736 -0.1337 0.0224  0.0479  118 ASN A OD1 
1036  N ND2 . ASN A 118 ? 0.4596 0.5423 0.8725 -0.1443 0.0181  0.0436  118 ASN A ND2 
1037  N N   . LYS A 119 ? 0.3274 0.5272 0.7024 -0.1396 0.0264  0.0153  119 LYS A N   
1038  C CA  . LYS A 119 ? 0.3612 0.5919 0.7494 -0.1424 0.0268  0.0085  119 LYS A CA  
1039  C C   . LYS A 119 ? 0.4287 0.6909 0.8126 -0.1489 0.0389  0.0213  119 LYS A C   
1040  O O   . LYS A 119 ? 0.4944 0.7553 0.8604 -0.1482 0.0465  0.0313  119 LYS A O   
1041  C CB  . LYS A 119 ? 0.3374 0.5746 0.7199 -0.1299 0.0193  -0.0103 119 LYS A CB  
1042  C CG  . LYS A 119 ? 0.4152 0.6572 0.8165 -0.1299 0.0105  -0.0262 119 LYS A CG  
1043  C CD  . LYS A 119 ? 0.3605 0.6047 0.7518 -0.1164 0.0017  -0.0456 119 LYS A CD  
1044  C CE  . LYS A 119 ? 0.4132 0.6263 0.7899 -0.1104 -0.0062 -0.0563 119 LYS A CE  
1045  N NZ  . LYS A 119 ? 0.5553 0.7523 0.9458 -0.1157 -0.0128 -0.0649 119 LYS A NZ  
1046  N N   . GLU A 120 ? 0.4421 0.7334 0.8430 -0.1552 0.0413  0.0190  120 GLU A N   
1047  C CA  . GLU A 120 ? 0.4003 0.7250 0.7996 -0.1626 0.0550  0.0256  120 GLU A CA  
1048  C C   . GLU A 120 ? 0.3108 0.6621 0.6971 -0.1498 0.0555  0.0205  120 GLU A C   
1049  O O   . GLU A 120 ? 0.4430 0.7843 0.8260 -0.1426 0.0713  0.0138  120 GLU A O   
1050  C CB  . GLU A 120 ? 0.5056 0.8496 0.9301 -0.1756 0.0579  0.0272  120 GLU A CB  
1051  C CG  . GLU A 120 ? 0.7624 1.0763 1.2029 -0.1845 0.0534  0.0344  120 GLU A CG  
1052  C CD  . GLU A 120 ? 0.9179 1.2206 1.3763 -0.1812 0.0397  0.0208  120 GLU A CD  
1053  O OE1 . GLU A 120 ? 0.7736 1.0721 1.2245 -0.1680 0.0311  0.0071  120 GLU A OE1 
1054  O OE2 . GLU A 120 ? 0.8780 1.1743 1.3588 -0.1913 0.0379  0.0223  120 GLU A OE2 
1055  N N   . LYS A 121 ? 0.2073 0.5666 0.6134 -0.1393 0.0454  0.0131  121 LYS A N   
1056  C CA  . LYS A 121 ? 0.2759 0.6463 0.6799 -0.1225 0.0471  0.0013  121 LYS A CA  
1057  C C   . LYS A 121 ? 0.3127 0.6651 0.7081 -0.1108 0.0341  -0.0222 121 LYS A C   
1058  O O   . LYS A 121 ? 0.3450 0.6891 0.7535 -0.1132 0.0247  -0.0314 121 LYS A O   
1059  C CB  . LYS A 121 ? 0.4705 0.8730 0.8964 -0.1228 0.0535  -0.0008 121 LYS A CB  
1060  C CG  . LYS A 121 ? 0.5423 0.9628 0.9599 -0.1184 0.0687  0.0018  121 LYS A CG  
1061  C CD  . LYS A 121 ? 0.2169 0.6242 0.6281 -0.1273 0.0810  0.0192  121 LYS A CD  
1062  C CE  . LYS A 121 ? 0.3708 0.8040 0.7785 -0.1319 0.0971  0.0237  121 LYS A CE  
1063  N NZ  . LYS A 121 ? 0.2530 0.6783 0.6269 -0.1341 0.1050  0.0338  121 LYS A NZ  
1064  N N   . LEU A 122 ? 0.3070 0.6533 0.6806 -0.0980 0.0334  -0.0318 122 LEU A N   
1065  C CA  . LEU A 122 ? 0.2748 0.6016 0.6372 -0.0870 0.0207  -0.0499 122 LEU A CA  
1066  C C   . LEU A 122 ? 0.2159 0.5601 0.5828 -0.0743 0.0146  -0.0674 122 LEU A C   
1067  O O   . LEU A 122 ? 0.1970 0.5618 0.5606 -0.0681 0.0218  -0.0693 122 LEU A O   
1068  C CB  . LEU A 122 ? 0.2746 0.5838 0.6107 -0.0812 0.0221  -0.0487 122 LEU A CB  
1069  C CG  . LEU A 122 ? 0.1969 0.4747 0.5258 -0.0869 0.0189  -0.0424 122 LEU A CG  
1070  C CD1 . LEU A 122 ? 0.2594 0.5326 0.6039 -0.1017 0.0233  -0.0256 122 LEU A CD1 
1071  C CD2 . LEU A 122 ? 0.1462 0.4144 0.4511 -0.0830 0.0240  -0.0374 122 LEU A CD2 
1072  N N   . ASN A 123 ? 0.2372 0.5724 0.6106 -0.0700 0.0007  -0.0804 123 ASN A N   
1073  C CA  . ASN A 123 ? 0.1682 0.5169 0.5462 -0.0571 -0.0081 -0.0956 123 ASN A CA  
1074  C C   . ASN A 123 ? 0.1777 0.5111 0.5328 -0.0425 -0.0172 -0.1051 123 ASN A C   
1075  O O   . ASN A 123 ? 0.2416 0.5558 0.5778 -0.0431 -0.0159 -0.1009 123 ASN A O   
1076  C CB  . ASN A 123 ? 0.2043 0.5546 0.6012 -0.0601 -0.0193 -0.1032 123 ASN A CB  
1077  C CG  . ASN A 123 ? 0.2569 0.5790 0.6444 -0.0631 -0.0302 -0.1071 123 ASN A CG  
1078  O OD1 . ASN A 123 ? 0.2267 0.5306 0.5924 -0.0548 -0.0374 -0.1121 123 ASN A OD1 
1079  N ND2 . ASN A 123 ? 0.3196 0.6386 0.7235 -0.0748 -0.0315 -0.1055 123 ASN A ND2 
1080  N N   . ARG A 124 ? 0.1907 0.5323 0.5487 -0.0292 -0.0273 -0.1172 124 ARG A N   
1081  C CA  . ARG A 124 ? 0.1612 0.4899 0.4992 -0.0142 -0.0362 -0.1240 124 ARG A CA  
1082  C C   . ARG A 124 ? 0.1599 0.4606 0.4793 -0.0147 -0.0476 -0.1243 124 ARG A C   
1083  O O   . ARG A 124 ? 0.2452 0.5264 0.5393 -0.0090 -0.0482 -0.1216 124 ARG A O   
1084  C CB  . ARG A 124 ? 0.2261 0.5658 0.5737 0.0000  -0.0470 -0.1348 124 ARG A CB  
1085  C CG  . ARG A 124 ? 0.2473 0.5727 0.5766 0.0162  -0.0562 -0.1397 124 ARG A CG  
1086  C CD  . ARG A 124 ? 0.2618 0.5845 0.5956 0.0288  -0.0745 -0.1469 124 ARG A CD  
1087  N NE  . ARG A 124 ? 0.1910 0.4920 0.5037 0.0421  -0.0859 -0.1473 124 ARG A NE  
1088  C CZ  . ARG A 124 ? 0.1932 0.4720 0.4861 0.0437  -0.1008 -0.1444 124 ARG A CZ  
1089  N NH1 . ARG A 124 ? 0.1970 0.4728 0.4881 0.0337  -0.1063 -0.1435 124 ARG A NH1 
1090  N NH2 . ARG A 124 ? 0.1988 0.4575 0.4722 0.0552  -0.1102 -0.1422 124 ARG A NH2 
1091  N N   . GLU A 125 ? 0.1833 0.4773 0.5090 -0.0215 -0.0558 -0.1266 125 GLU A N   
1092  C CA  . GLU A 125 ? 0.2870 0.5551 0.5927 -0.0230 -0.0654 -0.1282 125 GLU A CA  
1093  C C   . GLU A 125 ? 0.2641 0.5164 0.5623 -0.0343 -0.0538 -0.1192 125 GLU A C   
1094  O O   . GLU A 125 ? 0.2706 0.4947 0.5392 -0.0319 -0.0559 -0.1162 125 GLU A O   
1095  C CB  . GLU A 125 ? 0.2353 0.5017 0.5477 -0.0266 -0.0770 -0.1351 125 GLU A CB  
1096  C CG  . GLU A 125 ? 0.3193 0.6049 0.6454 -0.0178 -0.0865 -0.1415 125 GLU A CG  
1097  C CD  . GLU A 125 ? 0.5254 0.8088 0.8370 -0.0010 -0.0956 -0.1433 125 GLU A CD  
1098  O OE1 . GLU A 125 ? 0.6028 0.8651 0.8875 0.0038  -0.1024 -0.1417 125 GLU A OE1 
1099  O OE2 . GLU A 125 ? 0.4701 0.7717 0.7977 0.0073  -0.0958 -0.1459 125 GLU A OE2 
1100  N N   . GLU A 126 ? 0.3125 0.5760 0.6297 -0.0456 -0.0403 -0.1107 126 GLU A N   
1101  C CA  . GLU A 126 ? 0.2567 0.5055 0.5688 -0.0555 -0.0294 -0.0992 126 GLU A CA  
1102  C C   . GLU A 126 ? 0.1506 0.3901 0.4344 -0.0481 -0.0214 -0.0904 126 GLU A C   
1103  O O   . GLU A 126 ? 0.1672 0.3814 0.4291 -0.0492 -0.0189 -0.0833 126 GLU A O   
1104  C CB  . GLU A 126 ? 0.2309 0.4907 0.5652 -0.0687 -0.0181 -0.0875 126 GLU A CB  
1105  C CG  . GLU A 126 ? 0.3327 0.5859 0.6834 -0.0768 -0.0243 -0.0914 126 GLU A CG  
1106  C CD  . GLU A 126 ? 0.4198 0.6938 0.7958 -0.0866 -0.0169 -0.0831 126 GLU A CD  
1107  O OE1 . GLU A 126 ? 0.4607 0.7473 0.8392 -0.0914 -0.0045 -0.0690 126 GLU A OE1 
1108  O OE2 . GLU A 126 ? 0.4600 0.7392 0.8525 -0.0900 -0.0236 -0.0905 126 GLU A OE2 
1109  N N   . LEU A 127 ? 0.1529 0.4139 0.4387 -0.0407 -0.0174 -0.0921 127 LEU A N   
1110  C CA  . LEU A 127 ? 0.1465 0.3994 0.4058 -0.0330 -0.0114 -0.0872 127 LEU A CA  
1111  C C   . LEU A 127 ? 0.1493 0.3736 0.3794 -0.0215 -0.0226 -0.0919 127 LEU A C   
1112  O O   . LEU A 127 ? 0.2128 0.4186 0.4178 -0.0190 -0.0188 -0.0856 127 LEU A O   
1113  C CB  . LEU A 127 ? 0.1676 0.4515 0.4383 -0.0270 -0.0050 -0.0922 127 LEU A CB  
1114  C CG  . LEU A 127 ? 0.1485 0.4648 0.4429 -0.0392 0.0095  -0.0854 127 LEU A CG  
1115  C CD1 . LEU A 127 ? 0.1452 0.4895 0.4512 -0.0313 0.0128  -0.0943 127 LEU A CD1 
1116  C CD2 . LEU A 127 ? 0.1399 0.4506 0.4160 -0.0465 0.0220  -0.0701 127 LEU A CD2 
1117  N N   . LEU A 128 ? 0.1880 0.4102 0.4213 -0.0150 -0.0369 -0.1018 128 LEU A N   
1118  C CA  . LEU A 128 ? 0.1818 0.3772 0.3866 -0.0062 -0.0481 -0.1037 128 LEU A CA  
1119  C C   . LEU A 128 ? 0.2255 0.3951 0.4116 -0.0139 -0.0462 -0.0979 128 LEU A C   
1120  O O   . LEU A 128 ? 0.1775 0.3248 0.3361 -0.0099 -0.0460 -0.0934 128 LEU A O   
1121  C CB  . LEU A 128 ? 0.1719 0.3735 0.3848 0.0005  -0.0647 -0.1136 128 LEU A CB  
1122  C CG  . LEU A 128 ? 0.1786 0.3806 0.3855 0.0161  -0.0744 -0.1173 128 LEU A CG  
1123  C CD1 . LEU A 128 ? 0.1906 0.3963 0.4025 0.0218  -0.0932 -0.1240 128 LEU A CD1 
1124  C CD2 . LEU A 128 ? 0.1981 0.3718 0.3720 0.0216  -0.0732 -0.1104 128 LEU A CD2 
1125  N N   . ASP A 129 ? 0.2206 0.3930 0.4239 -0.0252 -0.0445 -0.0987 129 ASP A N   
1126  C CA  . ASP A 129 ? 0.1665 0.3158 0.3578 -0.0323 -0.0419 -0.0953 129 ASP A CA  
1127  C C   . ASP A 129 ? 0.1593 0.2997 0.3415 -0.0353 -0.0289 -0.0824 129 ASP A C   
1128  O O   . ASP A 129 ? 0.2028 0.3210 0.3647 -0.0353 -0.0275 -0.0790 129 ASP A O   
1129  C CB  . ASP A 129 ? 0.1780 0.3331 0.3961 -0.0436 -0.0430 -0.1005 129 ASP A CB  
1130  C CG  . ASP A 129 ? 0.3328 0.4947 0.5557 -0.0414 -0.0576 -0.1148 129 ASP A CG  
1131  O OD1 . ASP A 129 ? 0.3574 0.5289 0.5738 -0.0314 -0.0663 -0.1185 129 ASP A OD1 
1132  O OD2 . ASP A 129 ? 0.2898 0.4481 0.5244 -0.0495 -0.0611 -0.1227 129 ASP A OD2 
1133  N N   . LEU A 130 ? 0.1959 0.3555 0.3927 -0.0384 -0.0194 -0.0753 130 LEU A N   
1134  C CA  . LEU A 130 ? 0.1479 0.3025 0.3348 -0.0416 -0.0083 -0.0622 130 LEU A CA  
1135  C C   . LEU A 130 ? 0.1474 0.2919 0.3055 -0.0312 -0.0089 -0.0621 130 LEU A C   
1136  O O   . LEU A 130 ? 0.1647 0.2924 0.3055 -0.0321 -0.0049 -0.0547 130 LEU A O   
1137  C CB  . LEU A 130 ? 0.1441 0.3258 0.3525 -0.0490 0.0021  -0.0541 130 LEU A CB  
1138  C CG  . LEU A 130 ? 0.1423 0.3212 0.3428 -0.0550 0.0126  -0.0380 130 LEU A CG  
1139  C CD1 . LEU A 130 ? 0.1449 0.3009 0.3497 -0.0625 0.0122  -0.0306 130 LEU A CD1 
1140  C CD2 . LEU A 130 ? 0.1790 0.3887 0.3971 -0.0630 0.0230  -0.0288 130 LEU A CD2 
1141  N N   . GLN A 131 ? 0.1491 0.3034 0.3046 -0.0213 -0.0141 -0.0705 131 GLN A N   
1142  C CA  . GLN A 131 ? 0.1516 0.2930 0.2827 -0.0113 -0.0164 -0.0717 131 GLN A CA  
1143  C C   . GLN A 131 ? 0.1935 0.3057 0.3017 -0.0096 -0.0231 -0.0709 131 GLN A C   
1144  O O   . GLN A 131 ? 0.2005 0.2969 0.2889 -0.0086 -0.0198 -0.0655 131 GLN A O   
1145  C CB  . GLN A 131 ? 0.1555 0.3096 0.2932 0.0000  -0.0236 -0.0821 131 GLN A CB  
1146  C CG  . GLN A 131 ? 0.1515 0.3357 0.3073 0.0009  -0.0151 -0.0853 131 GLN A CG  
1147  C CD  . GLN A 131 ? 0.2250 0.4220 0.3933 0.0133  -0.0232 -0.0977 131 GLN A CD  
1148  O OE1 . GLN A 131 ? 0.1955 0.3840 0.3655 0.0189  -0.0364 -0.1022 131 GLN A OE1 
1149  N NE2 . GLN A 131 ? 0.2174 0.4363 0.3949 0.0177  -0.0158 -0.1035 131 GLN A NE2 
1150  N N   . THR A 132 ? 0.1781 0.2850 0.2887 -0.0100 -0.0324 -0.0768 132 THR A N   
1151  C CA  . THR A 132 ? 0.1722 0.2559 0.2591 -0.0080 -0.0392 -0.0776 132 THR A CA  
1152  C C   . THR A 132 ? 0.2257 0.2948 0.3062 -0.0162 -0.0318 -0.0724 132 THR A C   
1153  O O   . THR A 132 ? 0.3109 0.3619 0.3692 -0.0147 -0.0312 -0.0693 132 THR A O   
1154  C CB  . THR A 132 ? 0.1822 0.2692 0.2726 -0.0064 -0.0518 -0.0864 132 THR A CB  
1155  O OG1 . THR A 132 ? 0.2045 0.3078 0.3073 0.0017  -0.0590 -0.0909 132 THR A OG1 
1156  C CG2 . THR A 132 ? 0.2977 0.3643 0.3594 -0.0037 -0.0593 -0.0864 132 THR A CG2 
1157  N N   . LEU A 133 ? 0.2036 0.2805 0.3061 -0.0251 -0.0262 -0.0713 133 LEU A N   
1158  C CA  . LEU A 133 ? 0.1886 0.2514 0.2906 -0.0320 -0.0200 -0.0669 133 LEU A CA  
1159  C C   . LEU A 133 ? 0.2226 0.2801 0.3147 -0.0318 -0.0114 -0.0553 133 LEU A C   
1160  O O   . LEU A 133 ? 0.2744 0.3163 0.3567 -0.0335 -0.0084 -0.0522 133 LEU A O   
1161  C CB  . LEU A 133 ? 0.1629 0.2337 0.2951 -0.0414 -0.0171 -0.0675 133 LEU A CB  
1162  C CG  . LEU A 133 ? 0.1722 0.2417 0.3115 -0.0436 -0.0256 -0.0814 133 LEU A CG  
1163  C CD1 . LEU A 133 ? 0.2173 0.2984 0.3917 -0.0528 -0.0242 -0.0833 133 LEU A CD1 
1164  C CD2 . LEU A 133 ? 0.2048 0.2546 0.3284 -0.0442 -0.0259 -0.0867 133 LEU A CD2 
1165  N N   . ASN A 134 ? 0.2209 0.2933 0.3163 -0.0300 -0.0074 -0.0500 134 ASN A N   
1166  C CA  . ASN A 134 ? 0.1898 0.2594 0.2725 -0.0293 -0.0009 -0.0408 134 ASN A CA  
1167  C C   . ASN A 134 ? 0.2276 0.2794 0.2840 -0.0225 -0.0048 -0.0435 134 ASN A C   
1168  O O   . ASN A 134 ? 0.2848 0.3270 0.3300 -0.0237 -0.0006 -0.0371 134 ASN A O   
1169  C CB  . ASN A 134 ? 0.1674 0.2599 0.2566 -0.0283 0.0038  -0.0382 134 ASN A CB  
1170  C CG  . ASN A 134 ? 0.2031 0.3091 0.3069 -0.0377 0.0127  -0.0256 134 ASN A CG  
1171  O OD1 . ASN A 134 ? 0.1656 0.2643 0.2620 -0.0408 0.0166  -0.0156 134 ASN A OD1 
1172  N ND2 . ASN A 134 ? 0.2615 0.3883 0.3871 -0.0427 0.0153  -0.0247 134 ASN A ND2 
1173  N N   . LEU A 135 ? 0.1874 0.2351 0.2348 -0.0158 -0.0133 -0.0518 135 LEU A N   
1174  C CA  . LEU A 135 ? 0.1700 0.1992 0.1934 -0.0107 -0.0177 -0.0524 135 LEU A CA  
1175  C C   . LEU A 135 ? 0.2974 0.3109 0.3109 -0.0150 -0.0178 -0.0525 135 LEU A C   
1176  O O   . LEU A 135 ? 0.2736 0.2741 0.2723 -0.0157 -0.0147 -0.0483 135 LEU A O   
1177  C CB  . LEU A 135 ? 0.2009 0.2305 0.2195 -0.0023 -0.0280 -0.0587 135 LEU A CB  
1178  C CG  . LEU A 135 ? 0.1744 0.2151 0.1990 0.0048  -0.0284 -0.0611 135 LEU A CG  
1179  C CD1 . LEU A 135 ? 0.1865 0.2220 0.2070 0.0142  -0.0405 -0.0660 135 LEU A CD1 
1180  C CD2 . LEU A 135 ? 0.1720 0.2063 0.1855 0.0048  -0.0218 -0.0566 135 LEU A CD2 
1181  N N   . LEU A 136 ? 0.2487 0.2651 0.2717 -0.0182 -0.0212 -0.0588 136 LEU A N   
1182  C CA  . LEU A 136 ? 0.1876 0.1922 0.2016 -0.0219 -0.0212 -0.0628 136 LEU A CA  
1183  C C   . LEU A 136 ? 0.2008 0.2000 0.2235 -0.0276 -0.0117 -0.0584 136 LEU A C   
1184  O O   . LEU A 136 ? 0.2438 0.2323 0.2566 -0.0295 -0.0095 -0.0611 136 LEU A O   
1185  C CB  . LEU A 136 ? 0.3247 0.3364 0.3490 -0.0243 -0.0276 -0.0734 136 LEU A CB  
1186  C CG  . LEU A 136 ? 0.2727 0.2908 0.2892 -0.0184 -0.0393 -0.0778 136 LEU A CG  
1187  C CD1 . LEU A 136 ? 0.2063 0.2338 0.2344 -0.0220 -0.0459 -0.0892 136 LEU A CD1 
1188  C CD2 . LEU A 136 ? 0.2673 0.2724 0.2537 -0.0140 -0.0443 -0.0747 136 LEU A CD2 
1189  N N   . ALA A 137 ? 0.2627 0.2703 0.3043 -0.0304 -0.0062 -0.0511 137 ALA A N   
1190  C CA  . ALA A 137 ? 0.2941 0.2968 0.3468 -0.0351 0.0012  -0.0443 137 ALA A CA  
1191  C C   . ALA A 137 ? 0.2581 0.2511 0.2923 -0.0330 0.0044  -0.0387 137 ALA A C   
1192  O O   . ALA A 137 ? 0.3452 0.3304 0.3836 -0.0355 0.0087  -0.0372 137 ALA A O   
1193  C CB  . ALA A 137 ? 0.2453 0.2611 0.3198 -0.0391 0.0053  -0.0344 137 ALA A CB  
1194  N N   . TRP A 138 ? 0.1880 0.1815 0.2045 -0.0283 0.0022  -0.0365 138 TRP A N   
1195  C CA  . TRP A 138 ? 0.2337 0.2188 0.2341 -0.0270 0.0047  -0.0316 138 TRP A CA  
1196  C C   . TRP A 138 ? 0.2409 0.2131 0.2196 -0.0248 0.0010  -0.0366 138 TRP A C   
1197  O O   . TRP A 138 ? 0.2874 0.2532 0.2508 -0.0224 0.0000  -0.0336 138 TRP A O   
1198  C CB  . TRP A 138 ? 0.2455 0.2392 0.2423 -0.0243 0.0049  -0.0267 138 TRP A CB  
1199  C CG  . TRP A 138 ? 0.2193 0.2292 0.2343 -0.0278 0.0091  -0.0200 138 TRP A CG  
1200  C CD1 . TRP A 138 ? 0.2384 0.2616 0.2691 -0.0292 0.0087  -0.0212 138 TRP A CD1 
1201  C CD2 . TRP A 138 ? 0.1897 0.2056 0.2091 -0.0314 0.0139  -0.0096 138 TRP A CD2 
1202  N NE1 . TRP A 138 ? 0.1429 0.1799 0.1867 -0.0341 0.0139  -0.0110 138 TRP A NE1 
1203  C CE2 . TRP A 138 ? 0.1418 0.1747 0.1781 -0.0353 0.0165  -0.0033 138 TRP A CE2 
1204  C CE3 . TRP A 138 ? 0.2665 0.2766 0.2778 -0.0323 0.0158  -0.0043 138 TRP A CE3 
1205  C CZ2 . TRP A 138 ? 0.2503 0.2942 0.2931 -0.0399 0.0205  0.0096  138 TRP A CZ2 
1206  C CZ3 . TRP A 138 ? 0.2091 0.2304 0.2282 -0.0361 0.0190  0.0071  138 TRP A CZ3 
1207  C CH2 . TRP A 138 ? 0.2062 0.2443 0.2398 -0.0399 0.0210  0.0146  138 TRP A CH2 
1208  N N   . CYS A 139 ? 0.2420 0.2111 0.2193 -0.0262 -0.0010 -0.0441 139 CYS A N   
1209  C CA  . CYS A 139 ? 0.3031 0.2631 0.2576 -0.0253 -0.0047 -0.0475 139 CYS A CA  
1210  C C   . CYS A 139 ? 0.3592 0.3115 0.3064 -0.0290 0.0023  -0.0461 139 CYS A C   
1211  O O   . CYS A 139 ? 0.4436 0.3976 0.4044 -0.0323 0.0080  -0.0503 139 CYS A O   
1212  C CB  . CYS A 139 ? 0.3019 0.2660 0.2563 -0.0261 -0.0101 -0.0573 139 CYS A CB  
1213  S SG  . CYS A 139 ? 0.3494 0.3080 0.2741 -0.0236 -0.0196 -0.0582 139 CYS A SG  
1214  N N   . GLY A 140 ? 0.3799 0.3240 0.3085 -0.0283 0.0020  -0.0407 140 GLY A N   
1215  C CA  . GLY A 140 ? 0.3583 0.2973 0.2805 -0.0323 0.0090  -0.0392 140 GLY A CA  
1216  C C   . GLY A 140 ? 0.3229 0.2621 0.2344 -0.0358 0.0110  -0.0471 140 GLY A C   
1217  O O   . GLY A 140 ? 0.4363 0.3788 0.3420 -0.0352 0.0055  -0.0534 140 GLY A O   
1218  N N   . ARG A 141 ? 0.3126 0.2507 0.2217 -0.0397 0.0190  -0.0476 141 ARG A N   
1219  C CA  . ARG A 141 ? 0.3550 0.2970 0.2546 -0.0436 0.0234  -0.0573 141 ARG A CA  
1220  C C   . ARG A 141 ? 0.3966 0.3365 0.2664 -0.0449 0.0170  -0.0553 141 ARG A C   
1221  O O   . ARG A 141 ? 0.3615 0.3081 0.2220 -0.0467 0.0153  -0.0647 141 ARG A O   
1222  C CB  . ARG A 141 ? 0.2838 0.2272 0.1873 -0.0475 0.0340  -0.0577 141 ARG A CB  
1223  C CG  . ARG A 141 ? 0.3799 0.3306 0.2724 -0.0520 0.0405  -0.0694 141 ARG A CG  
1224  C CD  . ARG A 141 ? 0.3055 0.2608 0.2085 -0.0551 0.0522  -0.0720 141 ARG A CD  
1225  N NE  . ARG A 141 ? 0.3067 0.2604 0.1876 -0.0600 0.0554  -0.0629 141 ARG A NE  
1226  C CZ  . ARG A 141 ? 0.2822 0.2443 0.1466 -0.0660 0.0630  -0.0682 141 ARG A CZ  
1227  N NH1 . ARG A 141 ? 0.3626 0.3362 0.2284 -0.0673 0.0683  -0.0849 141 ARG A NH1 
1228  N NH2 . ARG A 141 ? 0.3417 0.3015 0.1883 -0.0715 0.0657  -0.0570 141 ARG A NH2 
1229  N N   . THR A 142 ? 0.4778 0.4087 0.3331 -0.0441 0.0126  -0.0429 142 THR A N   
1230  C CA  . THR A 142 ? 0.4714 0.3985 0.2995 -0.0455 0.0055  -0.0372 142 THR A CA  
1231  C C   . THR A 142 ? 0.4831 0.4140 0.3092 -0.0411 -0.0058 -0.0411 142 THR A C   
1232  O O   . THR A 142 ? 0.6063 0.5431 0.4143 -0.0436 -0.0099 -0.0445 142 THR A O   
1233  C CB  . THR A 142 ? 0.4910 0.4047 0.3109 -0.0449 0.0019  -0.0230 142 THR A CB  
1234  O OG1 . THR A 142 ? 0.5703 0.4823 0.3901 -0.0507 0.0121  -0.0196 142 THR A OG1 
1235  C CG2 . THR A 142 ? 0.4746 0.3821 0.2699 -0.0454 -0.0079 -0.0140 142 THR A CG2 
1236  N N   . LEU A 143 ? 0.4180 0.3484 0.2627 -0.0349 -0.0110 -0.0410 143 LEU A N   
1237  C CA  . LEU A 143 ? 0.3615 0.2970 0.2078 -0.0303 -0.0222 -0.0444 143 LEU A CA  
1238  C C   . LEU A 143 ? 0.4275 0.3755 0.2871 -0.0321 -0.0208 -0.0586 143 LEU A C   
1239  O O   . LEU A 143 ? 0.5008 0.4558 0.3588 -0.0302 -0.0302 -0.0634 143 LEU A O   
1240  C CB  . LEU A 143 ? 0.5013 0.4342 0.3636 -0.0233 -0.0275 -0.0400 143 LEU A CB  
1241  C CG  . LEU A 143 ? 0.4226 0.3431 0.2734 -0.0194 -0.0347 -0.0289 143 LEU A CG  
1242  C CD1 . LEU A 143 ? 0.3944 0.3155 0.2643 -0.0124 -0.0374 -0.0288 143 LEU A CD1 
1243  C CD2 . LEU A 143 ? 0.4746 0.3935 0.3069 -0.0179 -0.0467 -0.0248 143 LEU A CD2 
1244  N N   . ARG A 144 ? 0.4518 0.4026 0.3271 -0.0355 -0.0101 -0.0657 144 ARG A N   
1245  C CA  . ARG A 144 ? 0.3494 0.3099 0.2390 -0.0379 -0.0087 -0.0806 144 ARG A CA  
1246  C C   . ARG A 144 ? 0.4843 0.4516 0.3513 -0.0420 -0.0107 -0.0901 144 ARG A C   
1247  O O   . ARG A 144 ? 0.5726 0.5492 0.4478 -0.0438 -0.0130 -0.1045 144 ARG A O   
1248  C CB  . ARG A 144 ? 0.3850 0.3450 0.2987 -0.0401 0.0026  -0.0853 144 ARG A CB  
1249  C CG  . ARG A 144 ? 0.4393 0.3979 0.3792 -0.0373 0.0033  -0.0783 144 ARG A CG  
1250  C CD  . ARG A 144 ? 0.4467 0.4065 0.4154 -0.0397 0.0110  -0.0841 144 ARG A CD  
1251  N NE  . ARG A 144 ? 0.5468 0.5070 0.5379 -0.0382 0.0115  -0.0741 144 ARG A NE  
1252  C CZ  . ARG A 144 ? 0.6316 0.5940 0.6524 -0.0401 0.0136  -0.0762 144 ARG A CZ  
1253  N NH1 . ARG A 144 ? 0.7550 0.7177 0.7902 -0.0427 0.0152  -0.0902 144 ARG A NH1 
1254  N NH2 . ARG A 144 ? 0.3908 0.3554 0.4275 -0.0397 0.0140  -0.0642 144 ARG A NH2 
1255  N N   . LYS A 145 ? 0.4658 0.4299 0.3045 -0.0445 -0.0098 -0.0823 145 LYS A N   
1256  C CA  . LYS A 145 ? 0.5182 0.4914 0.3295 -0.0491 -0.0126 -0.0882 145 LYS A CA  
1257  C C   . LYS A 145 ? 0.4591 0.4338 0.2528 -0.0462 -0.0284 -0.0807 145 LYS A C   
1258  O O   . LYS A 145 ? 0.5056 0.4924 0.2878 -0.0474 -0.0346 -0.0883 145 LYS A O   
1259  C CB  . LYS A 145 ? 0.5624 0.5337 0.3522 -0.0544 -0.0035 -0.0811 145 LYS A CB  
1260  C CG  . LYS A 145 ? 0.5934 0.5639 0.4020 -0.0566 0.0117  -0.0873 145 LYS A CG  
1261  C CD  . LYS A 145 ? 0.5051 0.4764 0.2961 -0.0615 0.0203  -0.0789 145 LYS A CD  
1262  C CE  . LYS A 145 ? 0.5011 0.4663 0.3105 -0.0625 0.0317  -0.0772 145 LYS A CE  
1263  N NZ  . LYS A 145 ? 0.5849 0.5538 0.4279 -0.0596 0.0373  -0.0917 145 LYS A NZ  
1264  N N   . ASP A 146 ? 0.5597 0.5233 0.3561 -0.0404 -0.0356 -0.0656 146 ASP A N   
1265  C CA  . ASP A 146 ? 0.6088 0.5722 0.3923 -0.0360 -0.0515 -0.0567 146 ASP A CA  
1266  C C   . ASP A 146 ? 0.5020 0.4742 0.3074 -0.0306 -0.0610 -0.0653 146 ASP A C   
1267  O O   . ASP A 146 ? 0.4389 0.4180 0.2346 -0.0282 -0.0750 -0.0639 146 ASP A O   
1268  C CB  . ASP A 146 ? 0.6101 0.5569 0.3903 -0.0316 -0.0551 -0.0385 146 ASP A CB  
1269  C CG  . ASP A 146 ? 1.0974 1.0398 0.8490 -0.0323 -0.0664 -0.0239 146 ASP A CG  
1270  O OD1 . ASP A 146 ? 1.1084 1.0618 0.8366 -0.0382 -0.0686 -0.0265 146 ASP A OD1 
1271  O OD2 . ASP A 146 ? 1.0812 1.0093 0.8340 -0.0273 -0.0734 -0.0098 146 ASP A OD2 
1272  N N   . LEU A 147 ? 0.4820 0.4554 0.3175 -0.0291 -0.0543 -0.0729 147 LEU A N   
1273  C CA  . LEU A 147 ? 0.4120 0.3952 0.2718 -0.0253 -0.0614 -0.0804 147 LEU A CA  
1274  C C   . LEU A 147 ? 0.4419 0.4364 0.3163 -0.0308 -0.0573 -0.0983 147 LEU A C   
1275  O O   . LEU A 147 ? 0.3981 0.3980 0.3015 -0.0302 -0.0566 -0.1045 147 LEU A O   
1276  C CB  . LEU A 147 ? 0.3582 0.3365 0.2427 -0.0203 -0.0575 -0.0745 147 LEU A CB  
1277  C CG  . LEU A 147 ? 0.4137 0.3785 0.2895 -0.0157 -0.0572 -0.0601 147 LEU A CG  
1278  C CD1 . LEU A 147 ? 0.2588 0.2249 0.1597 -0.0112 -0.0537 -0.0585 147 LEU A CD1 
1279  C CD2 . LEU A 147 ? 0.3788 0.3397 0.2361 -0.0110 -0.0712 -0.0514 147 LEU A CD2 
1280  N N   . LYS A 148 ? 0.5149 0.5139 0.3705 -0.0368 -0.0543 -0.1074 148 LYS A N   
1281  C CA  . LYS A 148 ? 0.4545 0.4614 0.3267 -0.0415 -0.0492 -0.1253 148 LYS A CA  
1282  C C   . LYS A 148 ? 0.4511 0.4688 0.3408 -0.0405 -0.0599 -0.1328 148 LYS A C   
1283  O O   . LYS A 148 ? 0.5311 0.5513 0.4512 -0.0424 -0.0558 -0.1420 148 LYS A O   
1284  C CB  . LYS A 148 ? 0.5152 0.5246 0.3647 -0.0450 -0.0445 -0.1294 148 LYS A CB  
1285  C CG  . LYS A 148 ? 0.6984 0.7017 0.5505 -0.0474 -0.0288 -0.1305 148 LYS A CG  
1286  C CD  . LYS A 148 ? 0.8040 0.8097 0.6875 -0.0490 -0.0204 -0.1453 148 LYS A CD  
1287  C CE  . LYS A 148 ? 0.7725 0.7718 0.6666 -0.0499 -0.0062 -0.1449 148 LYS A CE  
1288  N NZ  . LYS A 148 ? 0.6259 0.6284 0.5494 -0.0510 0.0012  -0.1593 148 LYS A NZ  
1289  N N   . ASP A 149 ? 0.5130 0.5375 0.3856 -0.0378 -0.0741 -0.1277 149 ASP A N   
1290  C CA  . ASP A 149 ? 0.4977 0.5347 0.3878 -0.0372 -0.0847 -0.1345 149 ASP A CA  
1291  C C   . ASP A 149 ? 0.4806 0.5200 0.4038 -0.0331 -0.0861 -0.1336 149 ASP A C   
1292  O O   . ASP A 149 ? 0.4432 0.4907 0.3948 -0.0356 -0.0859 -0.1426 149 ASP A O   
1293  C CB  . ASP A 149 ? 0.5494 0.5935 0.4141 -0.0350 -0.1004 -0.1272 149 ASP A CB  
1294  C CG  . ASP A 149 ? 0.8384 0.8951 0.7027 -0.0393 -0.1068 -0.1383 149 ASP A CG  
1295  O OD1 . ASP A 149 ? 0.8154 0.8776 0.7084 -0.0419 -0.1028 -0.1513 149 ASP A OD1 
1296  O OD2 . ASP A 149 ? 1.0174 1.0782 0.8528 -0.0404 -0.1162 -0.1335 149 ASP A OD2 
1297  N N   . LEU A 150 ? 0.4671 0.4982 0.3882 -0.0270 -0.0858 -0.1201 150 LEU A N   
1298  C CA  . LEU A 150 ? 0.3043 0.3369 0.2561 -0.0233 -0.0831 -0.1156 150 LEU A CA  
1299  C C   . LEU A 150 ? 0.3228 0.3526 0.2997 -0.0291 -0.0694 -0.1210 150 LEU A C   
1300  O O   . LEU A 150 ? 0.3041 0.3428 0.3113 -0.0308 -0.0688 -0.1249 150 LEU A O   
1301  C CB  . LEU A 150 ? 0.2748 0.2965 0.2182 -0.0159 -0.0821 -0.0993 150 LEU A CB  
1302  C CG  . LEU A 150 ? 0.2871 0.3103 0.2196 -0.0076 -0.0966 -0.0911 150 LEU A CG  
1303  C CD1 . LEU A 150 ? 0.2936 0.3032 0.2229 -0.0014 -0.0924 -0.0780 150 LEU A CD1 
1304  C CD2 . LEU A 150 ? 0.2837 0.3250 0.2414 -0.0039 -0.1068 -0.0975 150 LEU A CD2 
1305  N N   . LEU A 151 ? 0.3837 0.4018 0.3501 -0.0323 -0.0586 -0.1201 151 LEU A N   
1306  C CA  . LEU A 151 ? 0.3300 0.3439 0.3216 -0.0371 -0.0467 -0.1236 151 LEU A CA  
1307  C C   . LEU A 151 ? 0.3465 0.3680 0.3575 -0.0435 -0.0480 -0.1417 151 LEU A C   
1308  O O   . LEU A 151 ? 0.4060 0.4269 0.4488 -0.0472 -0.0424 -0.1440 151 LEU A O   
1309  C CB  . LEU A 151 ? 0.3324 0.3335 0.3094 -0.0380 -0.0360 -0.1189 151 LEU A CB  
1310  C CG  . LEU A 151 ? 0.3039 0.2964 0.2701 -0.0331 -0.0329 -0.1016 151 LEU A CG  
1311  C CD1 . LEU A 151 ? 0.4314 0.4134 0.3798 -0.0346 -0.0243 -0.0981 151 LEU A CD1 
1312  C CD2 . LEU A 151 ? 0.2891 0.2831 0.2822 -0.0324 -0.0280 -0.0941 151 LEU A CD2 
1313  N N   . ASN A 152 ? 0.3473 0.3743 0.3395 -0.0441 -0.0542 -0.1494 152 ASN A N   
1314  C CA  . ASN A 152 ? 0.3732 0.4063 0.3824 -0.0483 -0.0544 -0.1620 152 ASN A CA  
1315  C C   . ASN A 152 ? 0.3800 0.4252 0.4139 -0.0489 -0.0629 -0.1645 152 ASN A C   
1316  O O   . ASN A 152 ? 0.4396 0.4879 0.5003 -0.0531 -0.0609 -0.1729 152 ASN A O   
1317  C CB  . ASN A 152 ? 0.4886 0.5258 0.4685 -0.0492 -0.0582 -0.1691 152 ASN A CB  
1318  C CG  . ASN A 152 ? 0.5936 0.6245 0.5711 -0.0517 -0.0466 -0.1764 152 ASN A CG  
1319  O OD1 . ASN A 152 ? 0.6333 0.6574 0.6372 -0.0528 -0.0372 -0.1784 152 ASN A OD1 
1320  N ND2 . ASN A 152 ? 0.7633 0.7977 0.7101 -0.0524 -0.0476 -0.1799 152 ASN A ND2 
1321  N N   . LYS A 153 ? 0.3612 0.4139 0.3886 -0.0443 -0.0725 -0.1574 153 LYS A N   
1322  C CA  . LYS A 153 ? 0.2769 0.3441 0.3297 -0.0443 -0.0803 -0.1596 153 LYS A CA  
1323  C C   . LYS A 153 ? 0.3300 0.3972 0.4212 -0.0488 -0.0717 -0.1584 153 LYS A C   
1324  O O   . LYS A 153 ? 0.2946 0.3694 0.4122 -0.0533 -0.0724 -0.1644 153 LYS A O   
1325  C CB  . LYS A 153 ? 0.3703 0.4453 0.4126 -0.0366 -0.0912 -0.1512 153 LYS A CB  
1326  C CG  . LYS A 153 ? 0.3036 0.3951 0.3496 -0.0346 -0.1049 -0.1550 153 LYS A CG  
1327  C CD  . LYS A 153 ? 0.2870 0.3835 0.3215 -0.0249 -0.1163 -0.1453 153 LYS A CD  
1328  C CE  . LYS A 153 ? 0.3585 0.4746 0.4144 -0.0221 -0.1275 -0.1481 153 LYS A CE  
1329  N NZ  . LYS A 153 ? 0.2975 0.4195 0.3604 -0.0118 -0.1343 -0.1395 153 LYS A NZ  
1330  N N   . GLY A 154 ? 0.3401 0.3987 0.4345 -0.0483 -0.0636 -0.1493 154 GLY A N   
1331  C CA  . GLY A 154 ? 0.2609 0.3179 0.3882 -0.0533 -0.0540 -0.1432 154 GLY A CA  
1332  C C   . GLY A 154 ? 0.3395 0.4129 0.4911 -0.0536 -0.0560 -0.1369 154 GLY A C   
1333  O O   . GLY A 154 ? 0.2248 0.2986 0.3958 -0.0565 -0.0470 -0.1254 154 GLY A O   
1334  N N   . ARG A 155 ? 0.3770 0.4659 0.5278 -0.0506 -0.0678 -0.1436 155 ARG A N   
1335  C CA  . ARG A 155 ? 0.2409 0.3495 0.4200 -0.0517 -0.0699 -0.1413 155 ARG A CA  
1336  C C   . ARG A 155 ? 0.2892 0.4123 0.4579 -0.0438 -0.0841 -0.1460 155 ARG A C   
1337  O O   . ARG A 155 ? 0.3416 0.4586 0.4815 -0.0392 -0.0926 -0.1500 155 ARG A O   
1338  C CB  . ARG A 155 ? 0.2987 0.4110 0.5087 -0.0609 -0.0668 -0.1462 155 ARG A CB  
1339  C CG  . ARG A 155 ? 0.4238 0.5328 0.6241 -0.0616 -0.0739 -0.1595 155 ARG A CG  
1340  C CD  . ARG A 155 ? 0.3756 0.4790 0.6022 -0.0700 -0.0680 -0.1637 155 ARG A CD  
1341  N NE  . ARG A 155 ? 0.3051 0.4142 0.5632 -0.0756 -0.0605 -0.1524 155 ARG A NE  
1342  C CZ  . ARG A 155 ? 0.3757 0.4728 0.6535 -0.0819 -0.0511 -0.1459 155 ARG A CZ  
1343  N NH1 . ARG A 155 ? 0.2885 0.3676 0.5618 -0.0824 -0.0480 -0.1516 155 ARG A NH1 
1344  N NH2 . ARG A 155 ? 0.4114 0.5159 0.7135 -0.0874 -0.0448 -0.1324 155 ARG A NH2 
1345  N N   . ASN A 156 ? 0.2918 0.4349 0.4843 -0.0423 -0.0857 -0.1436 156 ASN A N   
1346  C CA  . ASN A 156 ? 0.2661 0.4251 0.4571 -0.0340 -0.0990 -0.1469 156 ASN A CA  
1347  C C   . ASN A 156 ? 0.2244 0.3739 0.3832 -0.0221 -0.1052 -0.1404 156 ASN A C   
1348  O O   . ASN A 156 ? 0.2404 0.3880 0.3783 -0.0173 -0.1185 -0.1438 156 ASN A O   
1349  C CB  . ASN A 156 ? 0.2603 0.4219 0.4490 -0.0369 -0.1080 -0.1564 156 ASN A CB  
1350  C CG  . ASN A 156 ? 0.3736 0.5408 0.5934 -0.0476 -0.1015 -0.1611 156 ASN A CG  
1351  O OD1 . ASN A 156 ? 0.4083 0.5666 0.6251 -0.0535 -0.1015 -0.1689 156 ASN A OD1 
1352  N ND2 . ASN A 156 ? 0.3763 0.5586 0.6259 -0.0501 -0.0954 -0.1560 156 ASN A ND2 
1353  N N   . TYR A 157 ? 0.2126 0.3550 0.3664 -0.0176 -0.0946 -0.1289 157 TYR A N   
1354  C CA  . TYR A 157 ? 0.2439 0.3737 0.3702 -0.0067 -0.0981 -0.1210 157 TYR A CA  
1355  C C   . TYR A 157 ? 0.2650 0.4117 0.4060 0.0038  -0.1057 -0.1209 157 TYR A C   
1356  O O   . TYR A 157 ? 0.2760 0.4419 0.4456 0.0029  -0.0994 -0.1225 157 TYR A O   
1357  C CB  . TYR A 157 ? 0.2068 0.3199 0.3202 -0.0074 -0.0834 -0.1108 157 TYR A CB  
1358  C CG  . TYR A 157 ? 0.2408 0.3352 0.3374 -0.0150 -0.0773 -0.1105 157 TYR A CG  
1359  C CD1 . TYR A 157 ? 0.2245 0.3044 0.2906 -0.0131 -0.0837 -0.1112 157 TYR A CD1 
1360  C CD2 . TYR A 157 ? 0.2896 0.3821 0.4022 -0.0241 -0.0651 -0.1090 157 TYR A CD2 
1361  C CE1 . TYR A 157 ? 0.3032 0.3690 0.3561 -0.0197 -0.0770 -0.1130 157 TYR A CE1 
1362  C CE2 . TYR A 157 ? 0.2686 0.3447 0.3702 -0.0298 -0.0597 -0.1101 157 TYR A CE2 
1363  C CZ  . TYR A 157 ? 0.3143 0.3781 0.3866 -0.0273 -0.0651 -0.1134 157 TYR A CZ  
1364  O OH  . TYR A 157 ? 0.3044 0.3547 0.3677 -0.0327 -0.0587 -0.1166 157 TYR A OH  
1365  N N   . THR A 158 ? 0.2304 0.3705 0.3529 0.0136  -0.1191 -0.1187 158 THR A N   
1366  C CA  . THR A 158 ? 0.2332 0.3863 0.3704 0.0258  -0.1286 -0.1188 158 THR A CA  
1367  C C   . THR A 158 ? 0.2304 0.3687 0.3562 0.0344  -0.1225 -0.1107 158 THR A C   
1368  O O   . THR A 158 ? 0.2935 0.4103 0.3952 0.0314  -0.1141 -0.1038 158 THR A O   
1369  C CB  . THR A 158 ? 0.2644 0.4197 0.3921 0.0318  -0.1498 -0.1200 158 THR A CB  
1370  O OG1 . THR A 158 ? 0.3264 0.4566 0.4179 0.0357  -0.1546 -0.1100 158 THR A OG1 
1371  C CG2 . THR A 158 ? 0.2612 0.4261 0.3910 0.0214  -0.1546 -0.1286 158 THR A CG2 
1372  N N   . GLN A 159 ? 0.2300 0.3816 0.3764 0.0455  -0.1269 -0.1132 159 GLN A N   
1373  C CA  . GLN A 159 ? 0.2283 0.3686 0.3696 0.0540  -0.1210 -0.1092 159 GLN A CA  
1374  C C   . GLN A 159 ? 0.2452 0.3560 0.3552 0.0591  -0.1300 -0.0995 159 GLN A C   
1375  O O   . GLN A 159 ? 0.3006 0.3930 0.3947 0.0593  -0.1214 -0.0942 159 GLN A O   
1376  C CB  . GLN A 159 ? 0.2274 0.3895 0.4008 0.0657  -0.1248 -0.1169 159 GLN A CB  
1377  C CG  . GLN A 159 ? 0.2294 0.3807 0.4010 0.0760  -0.1207 -0.1164 159 GLN A CG  
1378  C CD  . GLN A 159 ? 0.2132 0.3705 0.3857 0.0694  -0.1001 -0.1184 159 GLN A CD  
1379  O OE1 . GLN A 159 ? 0.2005 0.3788 0.3868 0.0598  -0.0891 -0.1213 159 GLN A OE1 
1380  N NE2 . GLN A 159 ? 0.2161 0.3557 0.3746 0.0739  -0.0953 -0.1163 159 GLN A NE2 
1381  N N   . GLU A 160 ? 0.2638 0.3710 0.3642 0.0625  -0.1477 -0.0964 160 GLU A N   
1382  C CA  . GLU A 160 ? 0.3506 0.4308 0.4198 0.0655  -0.1562 -0.0845 160 GLU A CA  
1383  C C   . GLU A 160 ? 0.2940 0.3572 0.3323 0.0533  -0.1456 -0.0796 160 GLU A C   
1384  O O   . GLU A 160 ? 0.3503 0.3906 0.3661 0.0537  -0.1431 -0.0702 160 GLU A O   
1385  C CB  . GLU A 160 ? 0.5269 0.6106 0.5917 0.0711  -0.1783 -0.0805 160 GLU A CB  
1386  C CG  . GLU A 160 ? 0.6928 0.7501 0.7280 0.0749  -0.1888 -0.0651 160 GLU A CG  
1387  C CD  . GLU A 160 ? 0.9706 1.0162 1.0208 0.0888  -0.1942 -0.0604 160 GLU A CD  
1388  O OE1 . GLU A 160 ? 0.9275 0.9832 0.9997 0.1003  -0.2103 -0.0609 160 GLU A OE1 
1389  O OE2 . GLU A 160 ? 0.8226 0.8494 0.8650 0.0883  -0.1829 -0.0573 160 GLU A OE2 
1390  N N   . GLU A 161 ? 0.2728 0.3468 0.3122 0.0425  -0.1394 -0.0863 161 GLU A N   
1391  C CA  . GLU A 161 ? 0.2697 0.3293 0.2859 0.0317  -0.1278 -0.0839 161 GLU A CA  
1392  C C   . GLU A 161 ? 0.3070 0.3572 0.3251 0.0302  -0.1111 -0.0808 161 GLU A C   
1393  O O   . GLU A 161 ? 0.2833 0.3142 0.2784 0.0270  -0.1051 -0.0739 161 GLU A O   
1394  C CB  . GLU A 161 ? 0.2643 0.3376 0.2890 0.0212  -0.1246 -0.0940 161 GLU A CB  
1395  C CG  . GLU A 161 ? 0.3597 0.4423 0.3763 0.0203  -0.1408 -0.0986 161 GLU A CG  
1396  C CD  . GLU A 161 ? 0.3877 0.4843 0.4176 0.0097  -0.1378 -0.1117 161 GLU A CD  
1397  O OE1 . GLU A 161 ? 0.4002 0.4917 0.4366 0.0020  -0.1226 -0.1145 161 GLU A OE1 
1398  O OE2 . GLU A 161 ? 0.5417 0.6541 0.5774 0.0092  -0.1514 -0.1194 161 GLU A OE2 
1399  N N   . LYS A 162 ? 0.2581 0.3237 0.3031 0.0319  -0.1036 -0.0859 162 LYS A N   
1400  C CA  . LYS A 162 ? 0.2228 0.2833 0.2688 0.0306  -0.0889 -0.0831 162 LYS A CA  
1401  C C   . LYS A 162 ? 0.2320 0.2747 0.2645 0.0391  -0.0921 -0.0773 162 LYS A C   
1402  O O   . LYS A 162 ? 0.3195 0.3475 0.3374 0.0359  -0.0831 -0.0723 162 LYS A O   
1403  C CB  . LYS A 162 ? 0.2078 0.2928 0.2840 0.0308  -0.0811 -0.0894 162 LYS A CB  
1404  C CG  . LYS A 162 ? 0.1956 0.2803 0.2717 0.0282  -0.0661 -0.0866 162 LYS A CG  
1405  C CD  . LYS A 162 ? 0.1846 0.2976 0.2887 0.0279  -0.0584 -0.0924 162 LYS A CD  
1406  C CE  . LYS A 162 ? 0.1909 0.3187 0.3140 0.0395  -0.0682 -0.1006 162 LYS A CE  
1407  N NZ  . LYS A 162 ? 0.1811 0.3407 0.3328 0.0387  -0.0594 -0.1075 162 LYS A NZ  
1408  N N   . GLU A 163 ? 0.2449 0.2885 0.2847 0.0500  -0.1055 -0.0780 163 GLU A N   
1409  C CA  . GLU A 163 ? 0.2578 0.2813 0.2877 0.0580  -0.1105 -0.0721 163 GLU A CA  
1410  C C   . GLU A 163 ? 0.2723 0.2713 0.2698 0.0528  -0.1137 -0.0607 163 GLU A C   
1411  O O   . GLU A 163 ? 0.2770 0.2567 0.2619 0.0531  -0.1101 -0.0547 163 GLU A O   
1412  C CB  . GLU A 163 ? 0.2714 0.3003 0.3198 0.0713  -0.1261 -0.0745 163 GLU A CB  
1413  C CG  . GLU A 163 ? 0.3375 0.3847 0.4169 0.0795  -0.1209 -0.0861 163 GLU A CG  
1414  C CD  . GLU A 163 ? 0.5464 0.6040 0.6506 0.0930  -0.1367 -0.0905 163 GLU A CD  
1415  O OE1 . GLU A 163 ? 0.5798 0.6176 0.6782 0.1014  -0.1507 -0.0829 163 GLU A OE1 
1416  O OE2 . GLU A 163 ? 0.5565 0.6424 0.6877 0.0950  -0.1356 -0.1007 163 GLU A OE2 
1417  N N   . TYR A 164 ? 0.3073 0.3085 0.2912 0.0474  -0.1203 -0.0584 164 TYR A N   
1418  C CA  . TYR A 164 ? 0.2968 0.2794 0.2487 0.0412  -0.1219 -0.0483 164 TYR A CA  
1419  C C   . TYR A 164 ? 0.2892 0.2624 0.2298 0.0323  -0.1050 -0.0474 164 TYR A C   
1420  O O   . TYR A 164 ? 0.2931 0.2475 0.2146 0.0302  -0.1029 -0.0385 164 TYR A O   
1421  C CB  . TYR A 164 ? 0.3083 0.3008 0.2485 0.0359  -0.1301 -0.0499 164 TYR A CB  
1422  C CG  . TYR A 164 ? 0.3368 0.3151 0.2425 0.0286  -0.1304 -0.0410 164 TYR A CG  
1423  C CD1 . TYR A 164 ? 0.4243 0.3847 0.3117 0.0319  -0.1390 -0.0265 164 TYR A CD1 
1424  C CD2 . TYR A 164 ? 0.4143 0.3977 0.3074 0.0179  -0.1217 -0.0471 164 TYR A CD2 
1425  C CE1 . TYR A 164 ? 0.4638 0.4140 0.3189 0.0238  -0.1381 -0.0173 164 TYR A CE1 
1426  C CE2 . TYR A 164 ? 0.4835 0.4577 0.3455 0.0109  -0.1204 -0.0406 164 TYR A CE2 
1427  C CZ  . TYR A 164 ? 0.5539 0.5126 0.3958 0.0134  -0.1282 -0.0251 164 TYR A CZ  
1428  O OH  . TYR A 164 ? 0.6411 0.5933 0.4514 0.0051  -0.1259 -0.0175 164 TYR A OH  
1429  N N   . VAL A 165 ? 0.2913 0.2779 0.2454 0.0266  -0.0934 -0.0555 165 VAL A N   
1430  C CA  . VAL A 165 ? 0.2508 0.2303 0.1984 0.0190  -0.0784 -0.0541 165 VAL A CA  
1431  C C   . VAL A 165 ? 0.2484 0.2173 0.1967 0.0231  -0.0739 -0.0500 165 VAL A C   
1432  O O   . VAL A 165 ? 0.3609 0.3143 0.2928 0.0193  -0.0690 -0.0438 165 VAL A O   
1433  C CB  . VAL A 165 ? 0.2316 0.2279 0.1989 0.0133  -0.0687 -0.0615 165 VAL A CB  
1434  C CG1 . VAL A 165 ? 0.2188 0.2092 0.1843 0.0075  -0.0547 -0.0582 165 VAL A CG1 
1435  C CG2 . VAL A 165 ? 0.2367 0.2399 0.2027 0.0073  -0.0720 -0.0672 165 VAL A CG2 
1436  N N   . LEU A 166 ? 0.2417 0.2206 0.2102 0.0308  -0.0754 -0.0551 166 LEU A N   
1437  C CA  . LEU A 166 ? 0.2396 0.2115 0.2110 0.0347  -0.0709 -0.0552 166 LEU A CA  
1438  C C   . LEU A 166 ? 0.2964 0.2440 0.2519 0.0380  -0.0788 -0.0471 166 LEU A C   
1439  O O   . LEU A 166 ? 0.4449 0.3800 0.3937 0.0361  -0.0732 -0.0447 166 LEU A O   
1440  C CB  . LEU A 166 ? 0.2343 0.2239 0.2310 0.0433  -0.0722 -0.0646 166 LEU A CB  
1441  C CG  . LEU A 166 ? 0.2151 0.2277 0.2277 0.0393  -0.0595 -0.0711 166 LEU A CG  
1442  C CD1 . LEU A 166 ? 0.2130 0.2484 0.2515 0.0471  -0.0625 -0.0809 166 LEU A CD1 
1443  C CD2 . LEU A 166 ? 0.2099 0.2184 0.2166 0.0370  -0.0496 -0.0709 166 LEU A CD2 
1444  N N   . ASN A 167 ? 0.2825 0.2236 0.2324 0.0423  -0.0925 -0.0421 167 ASN A N   
1445  C CA  . ASN A 167 ? 0.3134 0.2305 0.2479 0.0441  -0.1008 -0.0310 167 ASN A CA  
1446  C C   . ASN A 167 ? 0.4231 0.3278 0.3318 0.0328  -0.0934 -0.0224 167 ASN A C   
1447  O O   . ASN A 167 ? 0.3712 0.2575 0.2709 0.0309  -0.0921 -0.0153 167 ASN A O   
1448  C CB  . ASN A 167 ? 0.3216 0.2371 0.2553 0.0507  -0.1183 -0.0251 167 ASN A CB  
1449  C CG  . ASN A 167 ? 0.5589 0.4505 0.4894 0.0566  -0.1294 -0.0141 167 ASN A CG  
1450  O OD1 . ASN A 167 ? 0.4902 0.3670 0.4226 0.0564  -0.1239 -0.0136 167 ASN A OD1 
1451  N ND2 . ASN A 167 ? 0.6435 0.5313 0.5703 0.0616  -0.1461 -0.0048 167 ASN A ND2 
1452  N N   . LYS A 168 ? 0.4551 0.3703 0.3538 0.0251  -0.0885 -0.0239 168 LYS A N   
1453  C CA  . LYS A 168 ? 0.2993 0.2067 0.1772 0.0147  -0.0794 -0.0186 168 LYS A CA  
1454  C C   . LYS A 168 ? 0.2987 0.2035 0.1830 0.0112  -0.0662 -0.0211 168 LYS A C   
1455  O O   . LYS A 168 ? 0.3408 0.2326 0.2122 0.0058  -0.0615 -0.0145 168 LYS A O   
1456  C CB  . LYS A 168 ? 0.2956 0.2168 0.1672 0.0083  -0.0762 -0.0241 168 LYS A CB  
1457  C CG  . LYS A 168 ? 0.3182 0.2418 0.1740 0.0083  -0.0887 -0.0203 168 LYS A CG  
1458  C CD  . LYS A 168 ? 0.5607 0.4685 0.3895 0.0038  -0.0911 -0.0067 168 LYS A CD  
1459  C CE  . LYS A 168 ? 0.6271 0.5434 0.4327 -0.0020 -0.0963 -0.0054 168 LYS A CE  
1460  N NZ  . LYS A 168 ? 0.8990 0.8043 0.6764 -0.0099 -0.0937 0.0074  168 LYS A NZ  
1461  N N   . TYR A 169 ? 0.2814 0.2005 0.1856 0.0136  -0.0605 -0.0300 169 TYR A N   
1462  C CA  . TYR A 169 ? 0.2597 0.1800 0.1693 0.0100  -0.0491 -0.0317 169 TYR A CA  
1463  C C   . TYR A 169 ? 0.2657 0.1716 0.1743 0.0133  -0.0511 -0.0293 169 TYR A C   
1464  O O   . TYR A 169 ? 0.3952 0.2939 0.2977 0.0079  -0.0443 -0.0264 169 TYR A O   
1465  C CB  . TYR A 169 ? 0.2279 0.1686 0.1579 0.0116  -0.0437 -0.0397 169 TYR A CB  
1466  C CG  . TYR A 169 ? 0.2171 0.1693 0.1513 0.0052  -0.0378 -0.0414 169 TYR A CG  
1467  C CD1 . TYR A 169 ? 0.2258 0.1740 0.1487 0.0013  -0.0405 -0.0405 169 TYR A CD1 
1468  C CD2 . TYR A 169 ? 0.2006 0.1682 0.1509 0.0026  -0.0298 -0.0440 169 TYR A CD2 
1469  C CE1 . TYR A 169 ? 0.2179 0.1755 0.1481 -0.0043 -0.0354 -0.0447 169 TYR A CE1 
1470  C CE2 . TYR A 169 ? 0.2095 0.1851 0.1679 -0.0034 -0.0252 -0.0451 169 TYR A CE2 
1471  C CZ  . TYR A 169 ? 0.2014 0.1711 0.1510 -0.0064 -0.0281 -0.0466 169 TYR A CZ  
1472  O OH  . TYR A 169 ? 0.2282 0.2046 0.1889 -0.0120 -0.0238 -0.0502 169 TYR A OH  
1473  N N   . PHE A 170 ? 0.2790 0.1809 0.1963 0.0224  -0.0610 -0.0314 170 PHE A N   
1474  C CA  . PHE A 170 ? 0.4364 0.3233 0.3569 0.0259  -0.0636 -0.0314 170 PHE A CA  
1475  C C   . PHE A 170 ? 0.4443 0.3076 0.3472 0.0211  -0.0677 -0.0188 170 PHE A C   
1476  O O   . PHE A 170 ? 0.4046 0.2551 0.3065 0.0183  -0.0651 -0.0174 170 PHE A O   
1477  C CB  . PHE A 170 ? 0.3832 0.2725 0.3227 0.0380  -0.0728 -0.0389 170 PHE A CB  
1478  C CG  . PHE A 170 ? 0.5216 0.4314 0.4792 0.0416  -0.0654 -0.0527 170 PHE A CG  
1479  C CD1 . PHE A 170 ? 0.4886 0.4229 0.4542 0.0404  -0.0598 -0.0577 170 PHE A CD1 
1480  C CD2 . PHE A 170 ? 0.5500 0.4556 0.5162 0.0449  -0.0636 -0.0610 170 PHE A CD2 
1481  C CE1 . PHE A 170 ? 0.5070 0.4627 0.4874 0.0422  -0.0521 -0.0685 170 PHE A CE1 
1482  C CE2 . PHE A 170 ? 0.5868 0.5151 0.5667 0.0472  -0.0560 -0.0743 170 PHE A CE2 
1483  C CZ  . PHE A 170 ? 0.5598 0.5138 0.5458 0.0456  -0.0500 -0.0770 170 PHE A CZ  
1484  N N   . GLU A 171 ? 0.4186 0.2777 0.3071 0.0191  -0.0741 -0.0096 171 GLU A N   
1485  C CA  . GLU A 171 ? 0.4161 0.2569 0.2847 0.0119  -0.0756 0.0041  171 GLU A CA  
1486  C C   . GLU A 171 ? 0.4971 0.3394 0.3570 0.0012  -0.0618 0.0045  171 GLU A C   
1487  O O   . GLU A 171 ? 0.5110 0.3382 0.3627 -0.0047 -0.0602 0.0127  171 GLU A O   
1488  C CB  . GLU A 171 ? 0.4868 0.3294 0.3382 0.0101  -0.0832 0.0128  171 GLU A CB  
1489  C CG  . GLU A 171 ? 0.7234 0.5455 0.5587 0.0073  -0.0922 0.0300  171 GLU A CG  
1490  C CD  . GLU A 171 ? 0.7270 0.5553 0.5405 0.0039  -0.0991 0.0389  171 GLU A CD  
1491  O OE1 . GLU A 171 ? 0.6654 0.5129 0.4744 0.0013  -0.0939 0.0300  171 GLU A OE1 
1492  O OE2 . GLU A 171 ? 0.7721 0.5864 0.5734 0.0033  -0.1100 0.0549  171 GLU A OE2 
1493  N N   . ILE A 172 ? 0.4790 0.3394 0.3430 -0.0014 -0.0523 -0.0036 172 ILE A N   
1494  C CA  . ILE A 172 ? 0.4124 0.2760 0.2723 -0.0102 -0.0400 -0.0036 172 ILE A CA  
1495  C C   . ILE A 172 ? 0.4271 0.2862 0.2974 -0.0103 -0.0364 -0.0064 172 ILE A C   
1496  O O   . ILE A 172 ? 0.4793 0.3318 0.3443 -0.0176 -0.0308 -0.0020 172 ILE A O   
1497  C CB  . ILE A 172 ? 0.3344 0.2170 0.2005 -0.0119 -0.0326 -0.0109 172 ILE A CB  
1498  C CG1 . ILE A 172 ? 0.3400 0.2260 0.1921 -0.0156 -0.0336 -0.0093 172 ILE A CG1 
1499  C CG2 . ILE A 172 ? 0.2999 0.1881 0.1719 -0.0177 -0.0213 -0.0125 172 ILE A CG2 
1500  C CD1 . ILE A 172 ? 0.4755 0.3556 0.3108 -0.0245 -0.0272 -0.0031 172 ILE A CD1 
1501  N N   . ILE A 173 ? 0.3733 0.2380 0.2589 -0.0027 -0.0393 -0.0148 173 ILE A N   
1502  C CA  . ILE A 173 ? 0.3044 0.1678 0.1989 -0.0028 -0.0364 -0.0201 173 ILE A CA  
1503  C C   . ILE A 173 ? 0.4283 0.2686 0.3199 -0.0038 -0.0424 -0.0150 173 ILE A C   
1504  O O   . ILE A 173 ? 0.4889 0.3239 0.3810 -0.0096 -0.0383 -0.0151 173 ILE A O   
1505  C CB  . ILE A 173 ? 0.3430 0.2214 0.2536 0.0053  -0.0374 -0.0320 173 ILE A CB  
1506  C CG1 . ILE A 173 ? 0.3379 0.2385 0.2527 0.0043  -0.0311 -0.0344 173 ILE A CG1 
1507  C CG2 . ILE A 173 ? 0.3297 0.2100 0.2474 0.0047  -0.0343 -0.0398 173 ILE A CG2 
1508  C CD1 . ILE A 173 ? 0.3534 0.2711 0.2832 0.0119  -0.0324 -0.0442 173 ILE A CD1 
1509  N N   . LYS A 174 ? 0.4482 0.2743 0.3383 0.0014  -0.0529 -0.0097 174 LYS A N   
1510  C CA  . LYS A 174 ? 0.4316 0.2328 0.3202 -0.0004 -0.0596 -0.0016 174 LYS A CA  
1511  C C   . LYS A 174 ? 0.4251 0.2182 0.2968 -0.0128 -0.0541 0.0113  174 LYS A C   
1512  O O   . LYS A 174 ? 0.4896 0.2648 0.3621 -0.0178 -0.0558 0.0173  174 LYS A O   
1513  C CB  . LYS A 174 ? 0.5064 0.2945 0.3974 0.0079  -0.0734 0.0046  174 LYS A CB  
1514  C CG  . LYS A 174 ? 0.5667 0.3689 0.4738 0.0202  -0.0783 -0.0074 174 LYS A CG  
1515  C CD  . LYS A 174 ? 0.5588 0.3453 0.4762 0.0302  -0.0937 -0.0031 174 LYS A CD  
1516  C CE  . LYS A 174 ? 0.7102 0.5154 0.6437 0.0419  -0.0980 -0.0145 174 LYS A CE  
1517  N NZ  . LYS A 174 ? 0.6450 0.4407 0.5825 0.0501  -0.1139 -0.0054 174 LYS A NZ  
1518  N N   . LYS A 175 ? 0.4497 0.2562 0.3081 -0.0181 -0.0471 0.0147  175 LYS A N   
1519  C CA  . LYS A 175 ? 0.4587 0.2625 0.3019 -0.0298 -0.0399 0.0247  175 LYS A CA  
1520  C C   . LYS A 175 ? 0.4616 0.2749 0.3110 -0.0364 -0.0285 0.0191  175 LYS A C   
1521  O O   . LYS A 175 ? 0.4675 0.2781 0.3092 -0.0462 -0.0223 0.0262  175 LYS A O   
1522  C CB  . LYS A 175 ? 0.4731 0.2886 0.3003 -0.0321 -0.0377 0.0282  175 LYS A CB  
1523  C CG  . LYS A 175 ? 0.5633 0.3694 0.3694 -0.0401 -0.0393 0.0433  175 LYS A CG  
1524  C CD  . LYS A 175 ? 0.6846 0.5009 0.4758 -0.0382 -0.0436 0.0447  175 LYS A CD  
1525  C CE  . LYS A 175 ? 0.9007 0.7049 0.6720 -0.0422 -0.0524 0.0623  175 LYS A CE  
1526  N NZ  . LYS A 175 ? 0.7347 0.5379 0.4892 -0.0557 -0.0429 0.0726  175 LYS A NZ  
1527  N N   . THR A 176 ? 0.4086 0.2348 0.2720 -0.0316 -0.0258 0.0072  176 THR A N   
1528  C CA  . THR A 176 ? 0.3258 0.1665 0.1944 -0.0371 -0.0157 0.0032  176 THR A CA  
1529  C C   . THR A 176 ? 0.3972 0.2293 0.2684 -0.0451 -0.0132 0.0062  176 THR A C   
1530  O O   . THR A 176 ? 0.4549 0.2925 0.3232 -0.0533 -0.0053 0.0103  176 THR A O   
1531  C CB  . THR A 176 ? 0.3133 0.1701 0.1949 -0.0308 -0.0149 -0.0075 176 THR A CB  
1532  O OG1 . THR A 176 ? 0.3921 0.2606 0.2735 -0.0264 -0.0144 -0.0094 176 THR A OG1 
1533  C CG2 . THR A 176 ? 0.3108 0.1805 0.1993 -0.0363 -0.0072 -0.0095 176 THR A CG2 
1534  N N   . LEU A 177 ? 0.3484 0.1681 0.2274 -0.0430 -0.0196 0.0028  177 LEU A N   
1535  C CA  . LEU A 177 ? 0.3054 0.1187 0.1903 -0.0513 -0.0177 0.0034  177 LEU A CA  
1536  C C   . LEU A 177 ? 0.3534 0.1510 0.2289 -0.0607 -0.0167 0.0173  177 LEU A C   
1537  O O   . LEU A 177 ? 0.3283 0.1269 0.2070 -0.0704 -0.0113 0.0201  177 LEU A O   
1538  C CB  . LEU A 177 ? 0.3130 0.1172 0.2106 -0.0467 -0.0250 -0.0067 177 LEU A CB  
1539  C CG  . LEU A 177 ? 0.2937 0.1188 0.1997 -0.0407 -0.0236 -0.0210 177 LEU A CG  
1540  C CD1 . LEU A 177 ? 0.3319 0.1503 0.2480 -0.0318 -0.0315 -0.0329 177 LEU A CD1 
1541  C CD2 . LEU A 177 ? 0.2841 0.1226 0.1954 -0.0482 -0.0184 -0.0248 177 LEU A CD2 
1542  N N   . SER A 178 ? 0.3462 0.1316 0.2103 -0.0587 -0.0220 0.0269  178 SER A N   
1543  C CA  . SER A 178 ? 0.3668 0.1399 0.2188 -0.0688 -0.0208 0.0425  178 SER A CA  
1544  C C   . SER A 178 ? 0.3579 0.1488 0.2005 -0.0775 -0.0081 0.0454  178 SER A C   
1545  O O   . SER A 178 ? 0.4053 0.1938 0.2459 -0.0888 -0.0023 0.0534  178 SER A O   
1546  C CB  . SER A 178 ? 0.3882 0.1481 0.2278 -0.0644 -0.0302 0.0533  178 SER A CB  
1547  O OG  . SER A 178 ? 0.5742 0.3100 0.4241 -0.0612 -0.0416 0.0571  178 SER A OG  
1548  N N   . ILE A 179 ? 0.3858 0.1953 0.2253 -0.0724 -0.0035 0.0382  179 ILE A N   
1549  C CA  . ILE A 179 ? 0.3435 0.1703 0.1778 -0.0792 0.0084  0.0382  179 ILE A CA  
1550  C C   . ILE A 179 ? 0.3800 0.2170 0.2302 -0.0843 0.0161  0.0330  179 ILE A C   
1551  O O   . ILE A 179 ? 0.4382 0.2872 0.2881 -0.0918 0.0262  0.0342  179 ILE A O   
1552  C CB  . ILE A 179 ? 0.3157 0.1580 0.1469 -0.0723 0.0106  0.0304  179 ILE A CB  
1553  C CG1 . ILE A 179 ? 0.3550 0.2105 0.1757 -0.0793 0.0211  0.0314  179 ILE A CG1 
1554  C CG2 . ILE A 179 ? 0.3734 0.2282 0.2228 -0.0663 0.0124  0.0192  179 ILE A CG2 
1555  C CD1 . ILE A 179 ? 0.5905 0.4527 0.3984 -0.0751 0.0193  0.0284  179 ILE A CD1 
1556  N N   . TYR A 180 ? 0.4382 0.2732 0.3031 -0.0805 0.0113  0.0262  180 TYR A N   
1557  C CA  . TYR A 180 ? 0.3983 0.2429 0.2780 -0.0864 0.0163  0.0226  180 TYR A CA  
1558  C C   . TYR A 180 ? 0.3671 0.1988 0.2477 -0.0975 0.0168  0.0305  180 TYR A C   
1559  O O   . TYR A 180 ? 0.3752 0.2195 0.2644 -0.1049 0.0243  0.0315  180 TYR A O   
1560  C CB  . TYR A 180 ? 0.3077 0.1577 0.2002 -0.0796 0.0108  0.0123  180 TYR A CB  
1561  C CG  . TYR A 180 ? 0.2599 0.1282 0.1559 -0.0723 0.0133  0.0067  180 TYR A CG  
1562  C CD1 . TYR A 180 ? 0.2487 0.1347 0.1539 -0.0750 0.0207  0.0061  180 TYR A CD1 
1563  C CD2 . TYR A 180 ? 0.2751 0.1428 0.1678 -0.0629 0.0081  0.0026  180 TYR A CD2 
1564  C CE1 . TYR A 180 ? 0.2499 0.1503 0.1611 -0.0688 0.0223  0.0027  180 TYR A CE1 
1565  C CE2 . TYR A 180 ? 0.2382 0.1221 0.1358 -0.0577 0.0105  -0.0011 180 TYR A CE2 
1566  C CZ  . TYR A 180 ? 0.2316 0.1305 0.1384 -0.0608 0.0174  -0.0003 180 TYR A CZ  
1567  O OH  . TYR A 180 ? 0.2920 0.2047 0.2064 -0.0561 0.0191  -0.0022 180 TYR A OH  
1568  N N   . ARG A 181 ? 0.3690 0.1783 0.2450 -0.0974 0.0082  0.0361  181 ARG A N   
1569  C CA  . ARG A 181 ? 0.3578 0.1603 0.2395 -0.1046 0.0079  0.0450  181 ARG A CA  
1570  C C   . ARG A 181 ? 0.3868 0.2011 0.2581 -0.1107 0.0168  0.0549  181 ARG A C   
1571  O O   . ARG A 181 ? 0.3808 0.2048 0.2610 -0.1185 0.0234  0.0582  181 ARG A O   
1572  C CB  . ARG A 181 ? 0.3798 0.1576 0.2613 -0.1007 -0.0036 0.0500  181 ARG A CB  
1573  C CG  . ARG A 181 ? 0.4322 0.1986 0.3284 -0.0953 -0.0122 0.0377  181 ARG A CG  
1574  C CD  . ARG A 181 ? 0.5186 0.2655 0.4274 -0.0966 -0.0195 0.0429  181 ARG A CD  
1575  N NE  . ARG A 181 ? 0.5461 0.2974 0.4611 -0.1078 -0.0129 0.0524  181 ARG A NE  
1576  C CZ  . ARG A 181 ? 0.6026 0.3429 0.5358 -0.1126 -0.0155 0.0528  181 ARG A CZ  
1577  N NH1 . ARG A 181 ? 0.6686 0.3927 0.6160 -0.1068 -0.0245 0.0429  181 ARG A NH1 
1578  N NH2 . ARG A 181 ? 0.5251 0.2714 0.4636 -0.1233 -0.0083 0.0619  181 ARG A NH2 
1579  N N   . GLU A 182 ? 0.3702 0.1853 0.2228 -0.1073 0.0170  0.0588  182 GLU A N   
1580  C CA  . GLU A 182 ? 0.4097 0.2363 0.2496 -0.1130 0.0244  0.0671  182 GLU A CA  
1581  C C   . GLU A 182 ? 0.4977 0.3486 0.3455 -0.1175 0.0375  0.0602  182 GLU A C   
1582  O O   . GLU A 182 ? 0.5149 0.3757 0.3640 -0.1251 0.0447  0.0659  182 GLU A O   
1583  C CB  . GLU A 182 ? 0.4659 0.2910 0.2845 -0.1080 0.0210  0.0694  182 GLU A CB  
1584  C CG  . GLU A 182 ? 0.6518 0.4909 0.4545 -0.1136 0.0279  0.0762  182 GLU A CG  
1585  C CD  . GLU A 182 ? 0.8247 0.6706 0.6092 -0.1086 0.0269  0.0721  182 GLU A CD  
1586  O OE1 . GLU A 182 ? 0.8361 0.6676 0.6120 -0.1021 0.0154  0.0756  182 GLU A OE1 
1587  O OE2 . GLU A 182 ? 0.8831 0.7493 0.6636 -0.1107 0.0372  0.0643  182 GLU A OE2 
1588  N N   . ILE A 183 ? 0.4480 0.3091 0.3032 -0.1128 0.0406  0.0485  183 ILE A N   
1589  C CA  . ILE A 183 ? 0.3881 0.2721 0.2551 -0.1155 0.0520  0.0416  183 ILE A CA  
1590  C C   . ILE A 183 ? 0.3640 0.2534 0.2521 -0.1205 0.0536  0.0412  183 ILE A C   
1591  O O   . ILE A 183 ? 0.4486 0.3561 0.3471 -0.1248 0.0628  0.0391  183 ILE A O   
1592  C CB  . ILE A 183 ? 0.3091 0.2022 0.1813 -0.1087 0.0543  0.0308  183 ILE A CB  
1593  C CG1 . ILE A 183 ? 0.2920 0.1769 0.1753 -0.1041 0.0464  0.0269  183 ILE A CG1 
1594  C CG2 . ILE A 183 ? 0.3115 0.2018 0.1639 -0.1048 0.0538  0.0299  183 ILE A CG2 
1595  C CD1 . ILE A 183 ? 0.2700 0.1721 0.1737 -0.1024 0.0506  0.0193  183 ILE A CD1 
1596  N N   . LYS A 184 ? 0.3424 0.2176 0.2383 -0.1200 0.0448  0.0417  184 LYS A N   
1597  C CA  . LYS A 184 ? 0.3253 0.2057 0.2414 -0.1257 0.0453  0.0406  184 LYS A CA  
1598  C C   . LYS A 184 ? 0.3487 0.2265 0.2654 -0.1346 0.0485  0.0511  184 LYS A C   
1599  O O   . LYS A 184 ? 0.3619 0.2541 0.2935 -0.1408 0.0549  0.0510  184 LYS A O   
1600  C CB  . LYS A 184 ? 0.3355 0.2019 0.2592 -0.1232 0.0347  0.0356  184 LYS A CB  
1601  C CG  . LYS A 184 ? 0.3202 0.1932 0.2650 -0.1292 0.0337  0.0318  184 LYS A CG  
1602  C CD  . LYS A 184 ? 0.3267 0.1821 0.2765 -0.1283 0.0227  0.0264  184 LYS A CD  
1603  C CE  . LYS A 184 ? 0.3305 0.1911 0.3012 -0.1359 0.0209  0.0224  184 LYS A CE  
1604  N NZ  . LYS A 184 ? 0.4951 0.3633 0.4737 -0.1442 0.0287  0.0316  184 LYS A NZ  
1605  N N   . GLU A 185 ? 0.3705 0.2311 0.2726 -0.1353 0.0439  0.0611  185 GLU A N   
1606  C CA  . GLU A 185 ? 0.4632 0.3196 0.3665 -0.1441 0.0464  0.0735  185 GLU A CA  
1607  C C   . GLU A 185 ? 0.4052 0.2805 0.2983 -0.1491 0.0581  0.0784  185 GLU A C   
1608  O O   . GLU A 185 ? 0.4202 0.3026 0.3210 -0.1578 0.0645  0.0852  185 GLU A O   
1609  C CB  . GLU A 185 ? 0.5259 0.3568 0.4196 -0.1426 0.0364  0.0838  185 GLU A CB  
1610  C CG  . GLU A 185 ? 0.5963 0.4079 0.5016 -0.1371 0.0249  0.0769  185 GLU A CG  
1611  C CD  . GLU A 185 ? 0.8502 0.6634 0.7800 -0.1425 0.0248  0.0704  185 GLU A CD  
1612  O OE1 . GLU A 185 ? 0.8903 0.6967 0.8296 -0.1379 0.0175  0.0590  185 GLU A OE1 
1613  O OE2 . GLU A 185 ? 0.9447 0.7666 0.8844 -0.1516 0.0316  0.0762  185 GLU A OE2 
1614  N N   . GLU A 186 ? 0.4237 0.2170 0.2400 0.0360  -0.0028 0.0664  186 GLU A N   
1615  C CA  . GLU A 186 ? 0.5525 0.3505 0.3534 0.0294  0.0000  0.0673  186 GLU A CA  
1616  C C   . GLU A 186 ? 0.5305 0.3455 0.3449 0.0194  0.0082  0.0577  186 GLU A C   
1617  O O   . GLU A 186 ? 0.6005 0.4225 0.4056 0.0142  0.0114  0.0559  186 GLU A O   
1618  C CB  . GLU A 186 ? 0.5960 0.4053 0.3895 0.0373  -0.0111 0.0687  186 GLU A CB  
1619  C CG  . GLU A 186 ? 0.6924 0.4880 0.4744 0.0493  -0.0210 0.0787  186 GLU A CG  
1620  C CD  . GLU A 186 ? 0.9166 0.7309 0.7016 0.0585  -0.0340 0.0774  186 GLU A CD  
1621  O OE1 . GLU A 186 ? 0.8378 0.6752 0.6404 0.0566  -0.0353 0.0673  186 GLU A OE1 
1622  O OE2 . GLU A 186 ? 0.8120 0.6215 0.5860 0.0662  -0.0424 0.0853  186 GLU A OE2 
1623  N N   . GLY A 187 ? 0.4724 0.2939 0.3080 0.0171  0.0114  0.0514  187 GLY A N   
1624  C CA  . GLY A 187 ? 0.4129 0.2480 0.2615 0.0083  0.0193  0.0438  187 GLY A CA  
1625  C C   . GLY A 187 ? 0.3535 0.2099 0.2134 0.0097  0.0165  0.0360  187 GLY A C   
1626  O O   . GLY A 187 ? 0.3936 0.2606 0.2625 0.0036  0.0230  0.0302  187 GLY A O   
1627  N N   . LYS A 188 ? 0.3412 0.2045 0.2017 0.0176  0.0070  0.0353  188 LYS A N   
1628  C CA  . LYS A 188 ? 0.2680 0.1493 0.1385 0.0178  0.0046  0.0275  188 LYS A CA  
1629  C C   . LYS A 188 ? 0.2929 0.1852 0.1868 0.0182  0.0043  0.0211  188 LYS A C   
1630  O O   . LYS A 188 ? 0.3360 0.2409 0.2390 0.0172  0.0038  0.0146  188 LYS A O   
1631  C CB  . LYS A 188 ? 0.3721 0.2583 0.2344 0.0244  -0.0055 0.0286  188 LYS A CB  
1632  C CG  . LYS A 188 ? 0.4235 0.3012 0.2602 0.0231  -0.0058 0.0343  188 LYS A CG  
1633  C CD  . LYS A 188 ? 0.4759 0.3566 0.3034 0.0309  -0.0179 0.0379  188 LYS A CD  
1634  C CE  . LYS A 188 ? 0.3737 0.2499 0.1747 0.0280  -0.0186 0.0415  188 LYS A CE  
1635  N NZ  . LYS A 188 ? 0.4561 0.3148 0.2402 0.0217  -0.0085 0.0474  188 LYS A NZ  
1636  N N   . GLY A 189 ? 0.2855 0.1716 0.1875 0.0191  0.0049  0.0228  189 GLY A N   
1637  C CA  . GLY A 189 ? 0.2163 0.1118 0.1374 0.0182  0.0052  0.0172  189 GLY A CA  
1638  C C   . GLY A 189 ? 0.2179 0.1036 0.1432 0.0178  0.0070  0.0192  189 GLY A C   
1639  O O   . GLY A 189 ? 0.2359 0.1064 0.1503 0.0200  0.0069  0.0248  189 GLY A O   
1640  N N   . SER A 190 ? 0.2012 0.0946 0.1412 0.0147  0.0086  0.0145  190 SER A N   
1641  C CA  . SER A 190 ? 0.2014 0.0876 0.1463 0.0134  0.0100  0.0142  190 SER A CA  
1642  C C   . SER A 190 ? 0.2092 0.1012 0.1632 0.0193  0.0049  0.0112  190 SER A C   
1643  O O   . SER A 190 ? 0.2366 0.1417 0.1973 0.0216  0.0014  0.0081  190 SER A O   
1644  C CB  . SER A 190 ? 0.1916 0.0838 0.1457 0.0052  0.0149  0.0110  190 SER A CB  
1645  O OG  . SER A 190 ? 0.2685 0.1550 0.2158 -0.0012 0.0210  0.0135  190 SER A OG  
1646  N N   . VAL A 191 ? 0.1995 0.0811 0.1532 0.0214  0.0054  0.0115  191 VAL A N   
1647  C CA  . VAL A 191 ? 0.2014 0.0884 0.1640 0.0267  0.0022  0.0078  191 VAL A CA  
1648  C C   . VAL A 191 ? 0.2118 0.0949 0.1792 0.0215  0.0060  0.0041  191 VAL A C   
1649  O O   . VAL A 191 ? 0.3719 0.2395 0.3326 0.0185  0.0097  0.0056  191 VAL A O   
1650  C CB  . VAL A 191 ? 0.2073 0.0862 0.1652 0.0368  -0.0015 0.0110  191 VAL A CB  
1651  C CG1 . VAL A 191 ? 0.1988 0.0878 0.1688 0.0423  -0.0039 0.0059  191 VAL A CG1 
1652  C CG2 . VAL A 191 ? 0.2128 0.0956 0.1634 0.0411  -0.0062 0.0153  191 VAL A CG2 
1653  N N   . SER A 192 ? 0.1750 0.0712 0.1524 0.0195  0.0052  -0.0008 192 SER A N   
1654  C CA  . SER A 192 ? 0.1733 0.0682 0.1543 0.0145  0.0078  -0.0050 192 SER A CA  
1655  C C   . SER A 192 ? 0.2146 0.1130 0.2006 0.0200  0.0068  -0.0091 192 SER A C   
1656  O O   . SER A 192 ? 0.1926 0.0990 0.1826 0.0268  0.0036  -0.0089 192 SER A O   
1657  C CB  . SER A 192 ? 0.1648 0.0720 0.1517 0.0070  0.0077  -0.0068 192 SER A CB  
1658  O OG  . SER A 192 ? 0.2084 0.1289 0.2014 0.0095  0.0046  -0.0078 192 SER A OG  
1659  N N   . THR A 193 ? 0.2396 0.1334 0.2258 0.0164  0.0098  -0.0134 193 THR A N   
1660  C CA  . THR A 193 ? 0.1754 0.0739 0.1665 0.0199  0.0106  -0.0186 193 THR A CA  
1661  C C   . THR A 193 ? 0.2226 0.1301 0.2157 0.0114  0.0117  -0.0226 193 THR A C   
1662  O O   . THR A 193 ? 0.2846 0.1938 0.2760 0.0038  0.0111  -0.0212 193 THR A O   
1663  C CB  . THR A 193 ? 0.1941 0.0758 0.1810 0.0246  0.0141  -0.0209 193 THR A CB  
1664  O OG1 . THR A 193 ? 0.3477 0.2366 0.3415 0.0304  0.0153  -0.0264 193 THR A OG1 
1665  C CG2 . THR A 193 ? 0.2034 0.0730 0.1835 0.0153  0.0181  -0.0237 193 THR A CG2 
1666  N N   . SER A 194 ? 0.2363 0.1511 0.2335 0.0129  0.0130  -0.0275 194 SER A N   
1667  C CA  . SER A 194 ? 0.1617 0.0825 0.1576 0.0051  0.0145  -0.0314 194 SER A CA  
1668  C C   . SER A 194 ? 0.2593 0.1712 0.2512 0.0049  0.0195  -0.0379 194 SER A C   
1669  O O   . SER A 194 ? 0.3323 0.2350 0.3251 0.0128  0.0218  -0.0396 194 SER A O   
1670  C CB  . SER A 194 ? 0.1986 0.1352 0.2004 0.0051  0.0131  -0.0319 194 SER A CB  
1671  O OG  . SER A 194 ? 0.2855 0.2283 0.2888 0.0023  0.0091  -0.0269 194 SER A OG  
1672  N N   . PRO A 195 ? 0.2334 0.1467 0.2200 -0.0036 0.0213  -0.0419 195 PRO A N   
1673  C CA  . PRO A 195 ? 0.2466 0.1526 0.2286 -0.0041 0.0270  -0.0499 195 PRO A CA  
1674  C C   . PRO A 195 ? 0.2373 0.1503 0.2272 0.0048  0.0302  -0.0536 195 PRO A C   
1675  O O   . PRO A 195 ? 0.2956 0.2232 0.2930 0.0071  0.0279  -0.0510 195 PRO A O   
1676  C CB  . PRO A 195 ? 0.2339 0.1462 0.2086 -0.0153 0.0268  -0.0525 195 PRO A CB  
1677  C CG  . PRO A 195 ? 0.1842 0.1002 0.1588 -0.0206 0.0208  -0.0457 195 PRO A CG  
1678  C CD  . PRO A 195 ? 0.1769 0.0970 0.1602 -0.0130 0.0178  -0.0394 195 PRO A CD  
1679  N N   . TYR A 196 ? 0.2091 0.1115 0.1978 0.0097  0.0359  -0.0601 196 TYR A N   
1680  C CA  . TYR A 196 ? 0.2119 0.1181 0.2112 0.0223  0.0381  -0.0623 196 TYR A CA  
1681  C C   . TYR A 196 ? 0.2397 0.1688 0.2490 0.0232  0.0379  -0.0632 196 TYR A C   
1682  O O   . TYR A 196 ? 0.2687 0.2081 0.2877 0.0296  0.0335  -0.0588 196 TYR A O   
1683  C CB  . TYR A 196 ? 0.2328 0.1258 0.2294 0.0265  0.0457  -0.0712 196 TYR A CB  
1684  C CG  . TYR A 196 ? 0.2410 0.1305 0.2480 0.0424  0.0465  -0.0713 196 TYR A CG  
1685  C CD1 . TYR A 196 ? 0.2337 0.1433 0.2553 0.0505  0.0472  -0.0738 196 TYR A CD1 
1686  C CD2 . TYR A 196 ? 0.2568 0.1258 0.2587 0.0487  0.0445  -0.0674 196 TYR A CD2 
1687  C CE1 . TYR A 196 ? 0.2617 0.1712 0.2941 0.0659  0.0463  -0.0732 196 TYR A CE1 
1688  C CE2 . TYR A 196 ? 0.2663 0.1340 0.2761 0.0637  0.0423  -0.0654 196 TYR A CE2 
1689  C CZ  . TYR A 196 ? 0.2589 0.1469 0.2836 0.0729  0.0431  -0.0681 196 TYR A CZ  
1690  O OH  . TYR A 196 ? 0.2698 0.1583 0.3021 0.0886  0.0401  -0.0657 196 TYR A OH  
1691  N N   . TYR A 197 ? 0.1993 0.1365 0.2054 0.0156  0.0426  -0.0690 197 TYR A N   
1692  C CA  . TYR A 197 ? 0.1903 0.1481 0.2053 0.0152  0.0444  -0.0709 197 TYR A CA  
1693  C C   . TYR A 197 ? 0.1807 0.1470 0.1907 0.0044  0.0404  -0.0655 197 TYR A C   
1694  O O   . TYR A 197 ? 0.2843 0.2631 0.2950 -0.0012 0.0438  -0.0680 197 TYR A O   
1695  C CB  . TYR A 197 ? 0.2028 0.1646 0.2180 0.0148  0.0539  -0.0812 197 TYR A CB  
1696  C CG  . TYR A 197 ? 0.2138 0.1722 0.2396 0.0287  0.0580  -0.0868 197 TYR A CG  
1697  C CD1 . TYR A 197 ? 0.2067 0.1808 0.2503 0.0393  0.0563  -0.0860 197 TYR A CD1 
1698  C CD2 . TYR A 197 ? 0.2332 0.1725 0.2515 0.0313  0.0634  -0.0930 197 TYR A CD2 
1699  C CE1 . TYR A 197 ? 0.2183 0.1901 0.2728 0.0538  0.0591  -0.0904 197 TYR A CE1 
1700  C CE2 . TYR A 197 ? 0.2463 0.1812 0.2731 0.0450  0.0657  -0.0957 197 TYR A CE2 
1701  C CZ  . TYR A 197 ? 0.2526 0.2039 0.2975 0.0568  0.0634  -0.0940 197 TYR A CZ  
1702  O OH  . TYR A 197 ? 0.3880 0.3356 0.4396 0.0711  0.0640  -0.0944 197 TYR A OH  
1703  N N   . HIS A 198 ? 0.2225 0.1818 0.2276 0.0015  0.0338  -0.0582 198 HIS A N   
1704  C CA  . HIS A 198 ? 0.2772 0.2425 0.2790 -0.0061 0.0292  -0.0521 198 HIS A CA  
1705  C C   . HIS A 198 ? 0.2830 0.2501 0.2738 -0.0168 0.0316  -0.0538 198 HIS A C   
1706  O O   . HIS A 198 ? 0.2520 0.2281 0.2426 -0.0216 0.0315  -0.0517 198 HIS A O   
1707  C CB  . HIS A 198 ? 0.2115 0.1903 0.2241 -0.0031 0.0274  -0.0499 198 HIS A CB  
1708  C CG  . HIS A 198 ? 0.1897 0.1692 0.2009 -0.0068 0.0214  -0.0426 198 HIS A CG  
1709  N ND1 . HIS A 198 ? 0.1938 0.1801 0.2031 -0.0138 0.0212  -0.0407 198 HIS A ND1 
1710  C CD2 . HIS A 198 ? 0.2081 0.1814 0.2191 -0.0044 0.0161  -0.0371 198 HIS A CD2 
1711  C CE1 . HIS A 198 ? 0.2619 0.2452 0.2705 -0.0147 0.0158  -0.0346 198 HIS A CE1 
1712  N NE2 . HIS A 198 ? 0.2874 0.2641 0.2974 -0.0091 0.0129  -0.0327 198 HIS A NE2 
1713  N N   . PRO A 199 ? 0.3134 0.2713 0.2934 -0.0215 0.0335  -0.0573 199 PRO A N   
1714  C CA  . PRO A 199 ? 0.3901 0.3501 0.3571 -0.0320 0.0349  -0.0585 199 PRO A CA  
1715  C C   . PRO A 199 ? 0.4179 0.3764 0.3782 -0.0381 0.0269  -0.0504 199 PRO A C   
1716  O O   . PRO A 199 ? 0.3322 0.2872 0.2975 -0.0349 0.0216  -0.0456 199 PRO A O   
1717  C CB  . PRO A 199 ? 0.2447 0.1952 0.2030 -0.0340 0.0402  -0.0671 199 PRO A CB  
1718  C CG  . PRO A 199 ? 0.2033 0.1423 0.1667 -0.0275 0.0380  -0.0664 199 PRO A CG  
1719  C CD  . PRO A 199 ? 0.2059 0.1500 0.1831 -0.0188 0.0341  -0.0601 199 PRO A CD  
1720  N N   . LEU A 200 ? 0.3573 0.3191 0.3062 -0.0466 0.0264  -0.0490 200 LEU A N   
1721  C CA  . LEU A 200 ? 0.3034 0.2645 0.2451 -0.0519 0.0184  -0.0415 200 LEU A CA  
1722  C C   . LEU A 200 ? 0.2983 0.2539 0.2309 -0.0569 0.0169  -0.0453 200 LEU A C   
1723  O O   . LEU A 200 ? 0.3680 0.3234 0.2863 -0.0649 0.0181  -0.0486 200 LEU A O   
1724  C CB  . LEU A 200 ? 0.2832 0.2484 0.2148 -0.0586 0.0177  -0.0372 200 LEU A CB  
1725  C CG  . LEU A 200 ? 0.2707 0.2396 0.2109 -0.0554 0.0174  -0.0319 200 LEU A CG  
1726  C CD1 . LEU A 200 ? 0.1997 0.1701 0.1278 -0.0633 0.0195  -0.0291 200 LEU A CD1 
1727  C CD2 . LEU A 200 ? 0.1906 0.1576 0.1384 -0.0508 0.0094  -0.0241 200 LEU A CD2 
1728  N N   . ILE A 201 ? 0.2233 0.1743 0.1634 -0.0532 0.0144  -0.0451 201 ILE A N   
1729  C CA  . ILE A 201 ? 0.2147 0.1595 0.1485 -0.0583 0.0135  -0.0495 201 ILE A CA  
1730  C C   . ILE A 201 ? 0.3373 0.2872 0.2592 -0.0679 0.0071  -0.0470 201 ILE A C   
1731  O O   . ILE A 201 ? 0.3710 0.3175 0.2810 -0.0755 0.0086  -0.0537 201 ILE A O   
1732  C CB  . ILE A 201 ? 0.3390 0.2791 0.2834 -0.0536 0.0113  -0.0472 201 ILE A CB  
1733  C CG1 . ILE A 201 ? 0.2580 0.1896 0.2093 -0.0451 0.0179  -0.0512 201 ILE A CG1 
1734  C CG2 . ILE A 201 ? 0.3249 0.2612 0.2636 -0.0615 0.0088  -0.0501 201 ILE A CG2 
1735  C CD1 . ILE A 201 ? 0.3230 0.2445 0.2665 -0.0467 0.0251  -0.0612 201 ILE A CD1 
1736  N N   . PRO A 202 ? 0.2546 0.2124 0.1788 -0.0678 -0.0006 -0.0378 202 PRO A N   
1737  C CA  . PRO A 202 ? 0.2414 0.2049 0.1537 -0.0760 -0.0079 -0.0347 202 PRO A CA  
1738  C C   . PRO A 202 ? 0.3292 0.2915 0.2229 -0.0836 -0.0044 -0.0389 202 PRO A C   
1739  O O   . PRO A 202 ? 0.4215 0.3850 0.3021 -0.0922 -0.0076 -0.0422 202 PRO A O   
1740  C CB  . PRO A 202 ? 0.2101 0.1799 0.1293 -0.0715 -0.0151 -0.0236 202 PRO A CB  
1741  C CG  . PRO A 202 ? 0.2391 0.2072 0.1753 -0.0627 -0.0131 -0.0223 202 PRO A CG  
1742  C CD  . PRO A 202 ? 0.2222 0.1833 0.1598 -0.0600 -0.0037 -0.0300 202 PRO A CD  
1743  N N   . ILE A 203 ? 0.2750 0.2359 0.1666 -0.0816 0.0023  -0.0395 203 ILE A N   
1744  C CA  . ILE A 203 ? 0.2879 0.2483 0.1609 -0.0896 0.0071  -0.0438 203 ILE A CA  
1745  C C   . ILE A 203 ? 0.2922 0.2467 0.1590 -0.0929 0.0151  -0.0568 203 ILE A C   
1746  O O   . ILE A 203 ? 0.3295 0.2832 0.1778 -0.1022 0.0166  -0.0620 203 ILE A O   
1747  C CB  . ILE A 203 ? 0.3252 0.2871 0.1991 -0.0875 0.0132  -0.0414 203 ILE A CB  
1748  C CG1 . ILE A 203 ? 0.2971 0.2611 0.1736 -0.0855 0.0053  -0.0288 203 ILE A CG1 
1749  C CG2 . ILE A 203 ? 0.3056 0.2673 0.1601 -0.0964 0.0203  -0.0468 203 ILE A CG2 
1750  C CD1 . ILE A 203 ? 0.3154 0.2797 0.1916 -0.0856 0.0110  -0.0260 203 ILE A CD1 
1751  N N   . LEU A 204 ? 0.2956 0.2448 0.1766 -0.0855 0.0203  -0.0622 204 LEU A N   
1752  C CA  . LEU A 204 ? 0.3557 0.2960 0.2315 -0.0873 0.0282  -0.0745 204 LEU A CA  
1753  C C   . LEU A 204 ? 0.4156 0.3520 0.2805 -0.0964 0.0231  -0.0779 204 LEU A C   
1754  O O   . LEU A 204 ? 0.4595 0.3922 0.3158 -0.1002 0.0281  -0.0847 204 LEU A O   
1755  C CB  . LEU A 204 ? 0.3069 0.2406 0.2002 -0.0762 0.0333  -0.0774 204 LEU A CB  
1756  C CG  . LEU A 204 ? 0.2525 0.1913 0.1570 -0.0674 0.0396  -0.0772 204 LEU A CG  
1757  C CD1 . LEU A 204 ? 0.2479 0.1793 0.1666 -0.0564 0.0443  -0.0814 204 LEU A CD1 
1758  C CD2 . LEU A 204 ? 0.2883 0.2312 0.1816 -0.0726 0.0479  -0.0840 204 LEU A CD2 
1759  N N   . LEU A 205 ? 0.3721 0.3132 0.2437 -0.0970 0.0130  -0.0702 205 LEU A N   
1760  C CA  . LEU A 205 ? 0.2881 0.2294 0.1546 -0.1047 0.0078  -0.0723 205 LEU A CA  
1761  C C   . LEU A 205 ? 0.3660 0.3171 0.2175 -0.1134 0.0008  -0.0688 205 LEU A C   
1762  O O   . LEU A 205 ? 0.4325 0.3833 0.2754 -0.1198 0.0010  -0.0733 205 LEU A O   
1763  C CB  . LEU A 205 ? 0.2738 0.2177 0.1545 -0.1029 0.0007  -0.0673 205 LEU A CB  
1764  C CG  . LEU A 205 ? 0.2703 0.2029 0.1645 -0.0955 0.0068  -0.0700 205 LEU A CG  
1765  C CD1 . LEU A 205 ? 0.2524 0.1924 0.1634 -0.0887 0.0010  -0.0600 205 LEU A CD1 
1766  C CD2 . LEU A 205 ? 0.5563 0.4812 0.4490 -0.0994 0.0095  -0.0757 205 LEU A CD2 
1767  N N   . ASN A 206 ? 0.4210 0.3799 0.2684 -0.1137 -0.0059 -0.0602 206 ASN A N   
1768  C CA  . ASN A 206 ? 0.3583 0.3254 0.1902 -0.1206 -0.0133 -0.0547 206 ASN A CA  
1769  C C   . ASN A 206 ? 0.4066 0.3753 0.2312 -0.1190 -0.0144 -0.0466 206 ASN A C   
1770  O O   . ASN A 206 ? 0.3709 0.3441 0.2084 -0.1118 -0.0208 -0.0359 206 ASN A O   
1771  C CB  . ASN A 206 ? 0.3596 0.3375 0.1972 -0.1229 -0.0263 -0.0485 206 ASN A CB  
1772  C CG  . ASN A 206 ? 0.4881 0.4740 0.3101 -0.1298 -0.0337 -0.0446 206 ASN A CG  
1773  O OD1 . ASN A 206 ? 0.4850 0.4671 0.2903 -0.1337 -0.0290 -0.0458 206 ASN A OD1 
1774  N ND2 . ASN A 206 ? 0.5222 0.5199 0.3503 -0.1314 -0.0450 -0.0401 206 ASN A ND2 
1775  N N   . PRO A 207 ? 0.4212 0.3865 0.2308 -0.1229 -0.0066 -0.0496 207 PRO A N   
1776  C CA  . PRO A 207 ? 0.4168 0.3825 0.2197 -0.1220 -0.0060 -0.0412 207 PRO A CA  
1777  C C   . PRO A 207 ? 0.4434 0.4142 0.2373 -0.1240 -0.0194 -0.0277 207 PRO A C   
1778  O O   . PRO A 207 ? 0.5208 0.4898 0.3138 -0.1210 -0.0199 -0.0182 207 PRO A O   
1779  C CB  . PRO A 207 ? 0.3745 0.3371 0.1627 -0.1278 0.0057  -0.0487 207 PRO A CB  
1780  C CG  . PRO A 207 ? 0.3856 0.3443 0.1827 -0.1258 0.0143  -0.0616 207 PRO A CG  
1781  C CD  . PRO A 207 ? 0.3395 0.2999 0.1426 -0.1262 0.0046  -0.0607 207 PRO A CD  
1782  N N   . ASN A 208 ? 0.4027 0.3800 0.1935 -0.1275 -0.0296 -0.0258 208 ASN A N   
1783  C CA  . ASN A 208 ? 0.4054 0.3888 0.1905 -0.1271 -0.0432 -0.0124 208 ASN A CA  
1784  C C   . ASN A 208 ? 0.4323 0.4189 0.2365 -0.1172 -0.0511 -0.0028 208 ASN A C   
1785  O O   . ASN A 208 ? 0.4870 0.4772 0.2883 -0.1145 -0.0622 0.0094  208 ASN A O   
1786  C CB  . ASN A 208 ? 0.4415 0.4338 0.2233 -0.1318 -0.0512 -0.0136 208 ASN A CB  
1787  C CG  . ASN A 208 ? 0.4323 0.4213 0.1953 -0.1406 -0.0442 -0.0207 208 ASN A CG  
1788  O OD1 . ASN A 208 ? 0.5833 0.5673 0.3302 -0.1436 -0.0407 -0.0170 208 ASN A OD1 
1789  N ND2 . ASN A 208 ? 0.4996 0.4907 0.2644 -0.1450 -0.0418 -0.0310 208 ASN A ND2 
1790  N N   . CYS A 209 ? 0.3779 0.3628 0.2047 -0.1097 -0.0447 -0.0074 209 CYS A N   
1791  C CA  . CYS A 209 ? 0.3469 0.3344 0.1956 -0.0987 -0.0494 0.0008  209 CYS A CA  
1792  C C   . CYS A 209 ? 0.4252 0.4054 0.2723 -0.0935 -0.0480 0.0103  209 CYS A C   
1793  O O   . CYS A 209 ? 0.4644 0.4454 0.3253 -0.0849 -0.0535 0.0185  209 CYS A O   
1794  C CB  . CYS A 209 ? 0.2918 0.2779 0.1611 -0.0931 -0.0420 -0.0069 209 CYS A CB  
1795  S SG  . CYS A 209 ? 0.4089 0.3842 0.2794 -0.0908 -0.0266 -0.0143 209 CYS A SG  
1796  N N   . VAL A 210 ? 0.3951 0.3677 0.2259 -0.0990 -0.0400 0.0086  210 VAL A N   
1797  C CA  . VAL A 210 ? 0.3136 0.2781 0.1401 -0.0967 -0.0385 0.0177  210 VAL A CA  
1798  C C   . VAL A 210 ? 0.3431 0.3067 0.1581 -0.0962 -0.0512 0.0313  210 VAL A C   
1799  O O   . VAL A 210 ? 0.3856 0.3411 0.2023 -0.0912 -0.0529 0.0410  210 VAL A O   
1800  C CB  . VAL A 210 ? 0.3884 0.3471 0.1990 -0.1047 -0.0264 0.0123  210 VAL A CB  
1801  C CG1 . VAL A 210 ? 0.3632 0.3246 0.1839 -0.1046 -0.0151 -0.0020 210 VAL A CG1 
1802  C CG2 . VAL A 210 ? 0.4006 0.3584 0.1822 -0.1155 -0.0294 0.0145  210 VAL A CG2 
1803  N N   . TYR A 211 ? 0.3791 0.3503 0.1822 -0.1013 -0.0605 0.0322  211 TYR A N   
1804  C CA  . TYR A 211 ? 0.3564 0.3283 0.1472 -0.1006 -0.0741 0.0455  211 TYR A CA  
1805  C C   . TYR A 211 ? 0.3720 0.3527 0.1848 -0.0895 -0.0857 0.0523  211 TYR A C   
1806  O O   . TYR A 211 ? 0.4420 0.4234 0.2485 -0.0858 -0.0978 0.0644  211 TYR A O   
1807  C CB  . TYR A 211 ? 0.3792 0.3577 0.1515 -0.1099 -0.0780 0.0423  211 TYR A CB  
1808  C CG  . TYR A 211 ? 0.3919 0.3628 0.1445 -0.1199 -0.0655 0.0353  211 TYR A CG  
1809  C CD1 . TYR A 211 ? 0.4077 0.3666 0.1460 -0.1220 -0.0607 0.0425  211 TYR A CD1 
1810  C CD2 . TYR A 211 ? 0.3943 0.3694 0.1443 -0.1270 -0.0577 0.0210  211 TYR A CD2 
1811  C CE1 . TYR A 211 ? 0.4218 0.3759 0.1445 -0.1312 -0.0486 0.0355  211 TYR A CE1 
1812  C CE2 . TYR A 211 ? 0.4062 0.3756 0.1409 -0.1350 -0.0456 0.0141  211 TYR A CE2 
1813  C CZ  . TYR A 211 ? 0.4307 0.3909 0.1522 -0.1373 -0.0411 0.0212  211 TYR A CZ  
1814  O OH  . TYR A 211 ? 0.6005 0.5570 0.3088 -0.1455 -0.0286 0.0138  211 TYR A OH  
1815  N N   . GLU A 212 ? 0.3686 0.3562 0.2067 -0.0838 -0.0823 0.0449  212 GLU A N   
1816  C CA  . GLU A 212 ? 0.3941 0.3914 0.2545 -0.0733 -0.0915 0.0503  212 GLU A CA  
1817  C C   . GLU A 212 ? 0.4349 0.4212 0.2998 -0.0631 -0.0937 0.0620  212 GLU A C   
1818  O O   . GLU A 212 ? 0.4778 0.4693 0.3488 -0.0555 -0.1052 0.0717  212 GLU A O   
1819  C CB  . GLU A 212 ? 0.3481 0.3520 0.2321 -0.0702 -0.0849 0.0401  212 GLU A CB  
1820  C CG  . GLU A 212 ? 0.4410 0.4497 0.3199 -0.0803 -0.0798 0.0275  212 GLU A CG  
1821  C CD  . GLU A 212 ? 0.5153 0.5400 0.4104 -0.0807 -0.0857 0.0233  212 GLU A CD  
1822  O OE1 . GLU A 212 ? 0.6172 0.6542 0.5216 -0.0758 -0.0972 0.0308  212 GLU A OE1 
1823  O OE2 . GLU A 212 ? 0.5412 0.5660 0.4401 -0.0859 -0.0787 0.0124  212 GLU A OE2 
1824  N N   . THR A 213 ? 0.3961 0.3674 0.2585 -0.0630 -0.0828 0.0609  213 THR A N   
1825  C CA  . THR A 213 ? 0.3948 0.3529 0.2615 -0.0546 -0.0830 0.0702  213 THR A CA  
1826  C C   . THR A 213 ? 0.4756 0.4166 0.3176 -0.0604 -0.0807 0.0779  213 THR A C   
1827  O O   . THR A 213 ? 0.4958 0.4234 0.3369 -0.0542 -0.0834 0.0879  213 THR A O   
1828  C CB  . THR A 213 ? 0.3139 0.2683 0.2001 -0.0495 -0.0726 0.0630  213 THR A CB  
1829  O OG1 . THR A 213 ? 0.3038 0.2582 0.1855 -0.0577 -0.0615 0.0522  213 THR A OG1 
1830  C CG2 . THR A 213 ? 0.2614 0.2291 0.1723 -0.0412 -0.0760 0.0595  213 THR A CG2 
1831  N N   . THR A 214 ? 0.4613 0.4012 0.2828 -0.0725 -0.0751 0.0733  214 THR A N   
1832  C CA  . THR A 214 ? 0.4898 0.4142 0.2858 -0.0802 -0.0715 0.0801  214 THR A CA  
1833  C C   . THR A 214 ? 0.5037 0.4335 0.2747 -0.0908 -0.0750 0.0798  214 THR A C   
1834  O O   . THR A 214 ? 0.5392 0.4719 0.3001 -0.1008 -0.0655 0.0696  214 THR A O   
1835  C CB  . THR A 214 ? 0.5402 0.4572 0.3383 -0.0851 -0.0560 0.0723  214 THR A CB  
1836  O OG1 . THR A 214 ? 0.4952 0.4249 0.3049 -0.0875 -0.0484 0.0577  214 THR A OG1 
1837  C CG2 . THR A 214 ? 0.4652 0.3723 0.2808 -0.0763 -0.0536 0.0755  214 THR A CG2 
1838  N N   . PRO A 215 ? 0.4177 0.3507 0.1847 -0.0866 -0.0864 0.0881  215 PRO A N   
1839  C CA  . PRO A 215 ? 0.4242 0.3675 0.1771 -0.0939 -0.0901 0.0845  215 PRO A CA  
1840  C C   . PRO A 215 ? 0.4841 0.4176 0.2115 -0.1042 -0.0829 0.0851  215 PRO A C   
1841  O O   . PRO A 215 ? 0.5214 0.4621 0.2354 -0.1103 -0.0859 0.0826  215 PRO A O   
1842  C CB  . PRO A 215 ? 0.4483 0.3994 0.2083 -0.0839 -0.1056 0.0944  215 PRO A CB  
1843  C CG  . PRO A 215 ? 0.4297 0.3779 0.2124 -0.0709 -0.1090 0.0999  215 PRO A CG  
1844  C CD  . PRO A 215 ? 0.4115 0.3416 0.1907 -0.0734 -0.0970 0.0997  215 PRO A CD  
1845  N N   . ASN A 216 ? 0.5709 0.4890 0.2914 -0.1069 -0.0731 0.0877  216 ASN A N   
1846  C CA  . ASN A 216 ? 0.5011 0.4106 0.1986 -0.1168 -0.0661 0.0887  216 ASN A CA  
1847  C C   . ASN A 216 ? 0.5291 0.4371 0.2234 -0.1267 -0.0495 0.0771  216 ASN A C   
1848  O O   . ASN A 216 ? 0.5246 0.4264 0.2018 -0.1355 -0.0418 0.0768  216 ASN A O   
1849  C CB  . ASN A 216 ? 0.5272 0.4195 0.2170 -0.1124 -0.0690 0.1027  216 ASN A CB  
1850  C CG  . ASN A 216 ? 0.6641 0.5577 0.3476 -0.1052 -0.0839 0.1141  216 ASN A CG  
1851  O OD1 . ASN A 216 ? 0.6670 0.5630 0.3664 -0.0928 -0.0939 0.1205  216 ASN A OD1 
1852  N ND2 . ASN A 216 ? 0.8293 0.7222 0.4901 -0.1125 -0.0852 0.1165  216 ASN A ND2 
1853  N N   . VAL A 217 ? 0.4847 0.3991 0.1953 -0.1254 -0.0434 0.0675  217 VAL A N   
1854  C CA  . VAL A 217 ? 0.5058 0.4202 0.2172 -0.1326 -0.0273 0.0567  217 VAL A CA  
1855  C C   . VAL A 217 ? 0.4890 0.4118 0.1889 -0.1418 -0.0203 0.0452  217 VAL A C   
1856  O O   . VAL A 217 ? 0.5532 0.4839 0.2494 -0.1423 -0.0273 0.0422  217 VAL A O   
1857  C CB  . VAL A 217 ? 0.4647 0.3834 0.1968 -0.1271 -0.0234 0.0503  217 VAL A CB  
1858  C CG1 . VAL A 217 ? 0.5628 0.4740 0.3071 -0.1169 -0.0327 0.0616  217 VAL A CG1 
1859  C CG2 . VAL A 217 ? 0.3931 0.3250 0.1317 -0.1263 -0.0255 0.0397  217 VAL A CG2 
1860  N N   . LYS A 218 ? 0.5834 0.5049 0.2789 -0.1493 -0.0060 0.0380  218 LYS A N   
1861  C CA  . LYS A 218 ? 0.5362 0.4645 0.2222 -0.1578 0.0032  0.0262  218 LYS A CA  
1862  C C   . LYS A 218 ? 0.4938 0.4308 0.1970 -0.1563 0.0146  0.0113  218 LYS A C   
1863  O O   . LYS A 218 ? 0.5328 0.4704 0.2443 -0.1576 0.0260  0.0070  218 LYS A O   
1864  C CB  . LYS A 218 ? 0.5182 0.4401 0.1881 -0.1667 0.0113  0.0284  218 LYS A CB  
1865  C CG  . LYS A 218 ? 0.5262 0.4416 0.1732 -0.1705 0.0021  0.0388  218 LYS A CG  
1866  C CD  . LYS A 218 ? 0.7209 0.6400 0.3511 -0.1811 0.0104  0.0303  218 LYS A CD  
1867  C CE  . LYS A 218 ? 0.6976 0.6071 0.3029 -0.1869 0.0057  0.0417  218 LYS A CE  
1868  N NZ  . LYS A 218 ? 0.7550 0.6656 0.3451 -0.1985 0.0185  0.0336  218 LYS A NZ  
1869  N N   . ILE A 219 ? 0.4314 0.3754 0.1409 -0.1533 0.0116  0.0034  219 ILE A N   
1870  C CA  . ILE A 219 ? 0.4166 0.3674 0.1422 -0.1505 0.0219  -0.0111 219 ILE A CA  
1871  C C   . ILE A 219 ? 0.4270 0.3817 0.1452 -0.1567 0.0312  -0.0231 219 ILE A C   
1872  O O   . ILE A 219 ? 0.4503 0.4035 0.1511 -0.1629 0.0265  -0.0205 219 ILE A O   
1873  C CB  . ILE A 219 ? 0.4558 0.4094 0.1950 -0.1426 0.0136  -0.0128 219 ILE A CB  
1874  C CG1 . ILE A 219 ? 0.4504 0.4073 0.1833 -0.1449 0.0063  -0.0164 219 ILE A CG1 
1875  C CG2 . ILE A 219 ? 0.4952 0.4446 0.2390 -0.1367 0.0024  0.0008  219 ILE A CG2 
1876  C CD1 . ILE A 219 ? 0.5143 0.4747 0.2621 -0.1383 -0.0017 -0.0187 219 ILE A CD1 
1877  N N   . PRO A 220 ? 0.4169 0.3767 0.1482 -0.1549 0.0442  -0.0364 220 PRO A N   
1878  C CA  . PRO A 220 ? 0.4347 0.3972 0.1594 -0.1603 0.0539  -0.0476 220 PRO A CA  
1879  C C   . PRO A 220 ? 0.4880 0.4498 0.2073 -0.1609 0.0484  -0.0529 220 PRO A C   
1880  O O   . PRO A 220 ? 0.6808 0.6417 0.4039 -0.1569 0.0371  -0.0486 220 PRO A O   
1881  C CB  . PRO A 220 ? 0.4188 0.3875 0.1641 -0.1547 0.0675  -0.0593 220 PRO A CB  
1882  C CG  . PRO A 220 ? 0.3910 0.3598 0.1536 -0.1453 0.0624  -0.0572 220 PRO A CG  
1883  C CD  . PRO A 220 ? 0.4328 0.3963 0.1861 -0.1469 0.0503  -0.0417 220 PRO A CD  
1884  N N   . ASP A 221 ? 0.5669 0.5294 0.2779 -0.1662 0.0565  -0.0626 221 ASP A N   
1885  C CA  . ASP A 221 ? 0.5835 0.5447 0.2888 -0.1681 0.0530  -0.0691 221 ASP A CA  
1886  C C   . ASP A 221 ? 0.4552 0.4161 0.1804 -0.1599 0.0598  -0.0810 221 ASP A C   
1887  O O   . ASP A 221 ? 0.5230 0.4854 0.2569 -0.1573 0.0727  -0.0908 221 ASP A O   
1888  C CB  . ASP A 221 ? 0.5304 0.4911 0.2158 -0.1779 0.0588  -0.0740 221 ASP A CB  
1889  C CG  . ASP A 221 ? 0.8304 0.7893 0.5097 -0.1807 0.0567  -0.0822 221 ASP A CG  
1890  O OD1 . ASP A 221 ? 0.9346 0.8937 0.6077 -0.1823 0.0435  -0.0760 221 ASP A OD1 
1891  O OD2 . ASP A 221 ? 0.8913 0.8491 0.5728 -0.1811 0.0682  -0.0951 221 ASP A OD2 
1892  N N   . PHE A 222 ? 0.4800 0.4391 0.2131 -0.1555 0.0508  -0.0800 222 PHE A N   
1893  C CA  . PHE A 222 ? 0.4723 0.4284 0.2239 -0.1471 0.0555  -0.0895 222 PHE A CA  
1894  C C   . PHE A 222 ? 0.5080 0.4596 0.2526 -0.1510 0.0591  -0.0998 222 PHE A C   
1895  O O   . PHE A 222 ? 0.5801 0.5296 0.3212 -0.1536 0.0507  -0.0993 222 PHE A O   
1896  C CB  . PHE A 222 ? 0.4389 0.3944 0.2025 -0.1411 0.0447  -0.0832 222 PHE A CB  
1897  C CG  . PHE A 222 ? 0.5122 0.4701 0.2879 -0.1346 0.0445  -0.0770 222 PHE A CG  
1898  C CD1 . PHE A 222 ? 0.5412 0.5019 0.3075 -0.1383 0.0403  -0.0662 222 PHE A CD1 
1899  C CD2 . PHE A 222 ? 0.3614 0.3175 0.1571 -0.1249 0.0485  -0.0818 222 PHE A CD2 
1900  C CE1 . PHE A 222 ? 0.5534 0.5154 0.3298 -0.1331 0.0405  -0.0608 222 PHE A CE1 
1901  C CE2 . PHE A 222 ? 0.3425 0.3013 0.1487 -0.1194 0.0484  -0.0768 222 PHE A CE2 
1902  C CZ  . PHE A 222 ? 0.4031 0.3649 0.1994 -0.1239 0.0446  -0.0667 222 PHE A CZ  
1903  N N   . ALA A 223 ? 0.4612 0.4119 0.2044 -0.1517 0.0720  -0.1097 223 ALA A N   
1904  C CA  . ALA A 223 ? 0.4844 0.4294 0.2194 -0.1556 0.0770  -0.1205 223 ALA A CA  
1905  C C   . ALA A 223 ? 0.4830 0.4199 0.2343 -0.1468 0.0806  -0.1290 223 ALA A C   
1906  O O   . ALA A 223 ? 0.7251 0.6552 0.4711 -0.1490 0.0858  -0.1388 223 ALA A O   
1907  C CB  . ALA A 223 ? 0.5411 0.4883 0.2678 -0.1597 0.0897  -0.1278 223 ALA A CB  
1908  N N   . VAL A 224 ? 0.5915 0.5280 0.3616 -0.1370 0.0780  -0.1254 224 VAL A N   
1909  C CA  . VAL A 224 ? 0.6219 0.5490 0.4070 -0.1282 0.0799  -0.1313 224 VAL A CA  
1910  C C   . VAL A 224 ? 0.5001 0.4269 0.2934 -0.1256 0.0683  -0.1227 224 VAL A C   
1911  O O   . VAL A 224 ? 0.4855 0.4200 0.2771 -0.1276 0.0605  -0.1128 224 VAL A O   
1912  C CB  . VAL A 224 ? 0.5674 0.4936 0.3704 -0.1161 0.0908  -0.1373 224 VAL A CB  
1913  C CG1 . VAL A 224 ? 0.5315 0.4444 0.3428 -0.1089 0.0951  -0.1459 224 VAL A CG1 
1914  C CG2 . VAL A 224 ? 0.5499 0.4836 0.3476 -0.1188 0.1011  -0.1421 224 VAL A CG2 
1915  N N   . SER A 225 ? 0.4964 0.4134 0.2983 -0.1213 0.0674  -0.1264 225 SER A N   
1916  C CA  . SER A 225 ? 0.4084 0.3245 0.2199 -0.1187 0.0578  -0.1195 225 SER A CA  
1917  C C   . SER A 225 ? 0.4406 0.3526 0.2715 -0.1058 0.0615  -0.1190 225 SER A C   
1918  O O   . SER A 225 ? 0.4787 0.3813 0.3172 -0.0984 0.0694  -0.1262 225 SER A O   
1919  C CB  . SER A 225 ? 0.4131 0.3211 0.2212 -0.1237 0.0542  -0.1231 225 SER A CB  
1920  O OG  . SER A 225 ? 0.4515 0.3567 0.2727 -0.1193 0.0480  -0.1182 225 SER A OG  
1921  N N   . PHE A 226 ? 0.4502 0.3690 0.2886 -0.1027 0.0554  -0.1105 226 PHE A N   
1922  C CA  . PHE A 226 ? 0.4321 0.3480 0.2885 -0.0912 0.0570  -0.1088 226 PHE A CA  
1923  C C   . PHE A 226 ? 0.3313 0.2401 0.1956 -0.0892 0.0500  -0.1051 226 PHE A C   
1924  O O   . PHE A 226 ? 0.3118 0.2197 0.1890 -0.0815 0.0482  -0.1009 226 PHE A O   
1925  C CB  . PHE A 226 ? 0.3726 0.2992 0.2326 -0.0894 0.0552  -0.1024 226 PHE A CB  
1926  C CG  . PHE A 226 ? 0.3604 0.2941 0.2176 -0.0894 0.0643  -0.1063 226 PHE A CG  
1927  C CD1 . PHE A 226 ? 0.3396 0.2726 0.2098 -0.0798 0.0740  -0.1131 226 PHE A CD1 
1928  C CD2 . PHE A 226 ? 0.3762 0.3181 0.2186 -0.0989 0.0628  -0.1023 226 PHE A CD2 
1929  C CE1 . PHE A 226 ? 0.3473 0.2896 0.2173 -0.0802 0.0827  -0.1169 226 PHE A CE1 
1930  C CE2 . PHE A 226 ? 0.4044 0.3532 0.2444 -0.1001 0.0719  -0.1056 226 PHE A CE2 
1931  C CZ  . PHE A 226 ? 0.3416 0.2917 0.1965 -0.0911 0.0822  -0.1133 226 PHE A CZ  
1932  N N   . ARG A 227 ? 0.3810 0.2853 0.2379 -0.0966 0.0464  -0.1068 227 ARG A N   
1933  C CA  . ARG A 227 ? 0.3526 0.2530 0.2165 -0.0971 0.0397  -0.1028 227 ARG A CA  
1934  C C   . ARG A 227 ? 0.3591 0.2442 0.2333 -0.0884 0.0452  -0.1060 227 ARG A C   
1935  O O   . ARG A 227 ? 0.3908 0.2728 0.2748 -0.0848 0.0414  -0.1008 227 ARG A O   
1936  C CB  . ARG A 227 ? 0.4093 0.3128 0.2624 -0.1088 0.0339  -0.1036 227 ARG A CB  
1937  C CG  . ARG A 227 ? 0.4350 0.3540 0.2785 -0.1165 0.0257  -0.0979 227 ARG A CG  
1938  C CD  . ARG A 227 ? 0.4785 0.4038 0.3173 -0.1260 0.0168  -0.0963 227 ARG A CD  
1939  N NE  . ARG A 227 ? 0.4907 0.4145 0.3433 -0.1242 0.0128  -0.0935 227 ARG A NE  
1940  C CZ  . ARG A 227 ? 0.5886 0.5251 0.4475 -0.1269 0.0025  -0.0863 227 ARG A CZ  
1941  N NH1 . ARG A 227 ? 0.6024 0.5534 0.4553 -0.1307 -0.0061 -0.0804 227 ARG A NH1 
1942  N NH2 . ARG A 227 ? 0.6933 0.6281 0.5654 -0.1255 0.0009  -0.0846 227 ARG A NH2 
1943  N N   . GLU A 228 ? 0.4003 0.2752 0.2719 -0.0849 0.0539  -0.1140 228 GLU A N   
1944  C CA  . GLU A 228 ? 0.3747 0.2337 0.2552 -0.0753 0.0584  -0.1160 228 GLU A CA  
1945  C C   . GLU A 228 ? 0.4983 0.3591 0.3924 -0.0620 0.0606  -0.1127 228 GLU A C   
1946  O O   . GLU A 228 ? 0.5658 0.4175 0.4692 -0.0541 0.0595  -0.1089 228 GLU A O   
1947  C CB  . GLU A 228 ? 0.4806 0.3277 0.3542 -0.0751 0.0664  -0.1258 228 GLU A CB  
1948  C CG  . GLU A 228 ? 0.5194 0.3480 0.4006 -0.0646 0.0708  -0.1277 228 GLU A CG  
1949  C CD  . GLU A 228 ? 0.6897 0.5094 0.5747 -0.0661 0.0653  -0.1215 228 GLU A CD  
1950  O OE1 . GLU A 228 ? 0.7864 0.6075 0.6642 -0.0781 0.0612  -0.1212 228 GLU A OE1 
1951  O OE2 . GLU A 228 ? 0.7078 0.5201 0.6030 -0.0554 0.0652  -0.1168 228 GLU A OE2 
1952  N N   . ASP A 229 ? 0.4170 0.2899 0.3120 -0.0598 0.0636  -0.1139 229 ASP A N   
1953  C CA  . ASP A 229 ? 0.3202 0.1979 0.2291 -0.0479 0.0655  -0.1112 229 ASP A CA  
1954  C C   . ASP A 229 ? 0.3383 0.2196 0.2541 -0.0470 0.0578  -0.1022 229 ASP A C   
1955  O O   . ASP A 229 ? 0.2887 0.1672 0.2167 -0.0364 0.0577  -0.0988 229 ASP A O   
1956  C CB  . ASP A 229 ? 0.3180 0.2103 0.2260 -0.0485 0.0705  -0.1144 229 ASP A CB  
1957  C CG  . ASP A 229 ? 0.4900 0.3797 0.3996 -0.0427 0.0799  -0.1232 229 ASP A CG  
1958  O OD1 . ASP A 229 ? 0.5994 0.4744 0.5106 -0.0370 0.0821  -0.1266 229 ASP A OD1 
1959  O OD2 . ASP A 229 ? 0.4431 0.3451 0.3519 -0.0441 0.0854  -0.1266 229 ASP A OD2 
1960  N N   . ALA A 230 ? 0.4403 0.3285 0.3487 -0.0578 0.0510  -0.0980 230 ALA A N   
1961  C CA  . ALA A 230 ? 0.2888 0.1801 0.2038 -0.0576 0.0436  -0.0898 230 ALA A CA  
1962  C C   . ALA A 230 ? 0.3435 0.2219 0.2643 -0.0540 0.0421  -0.0872 230 ALA A C   
1963  O O   . ALA A 230 ? 0.4557 0.3326 0.3858 -0.0477 0.0398  -0.0814 230 ALA A O   
1964  C CB  . ALA A 230 ? 0.2710 0.1729 0.1773 -0.0693 0.0357  -0.0858 230 ALA A CB  
1965  N N   . SER A 231 ? 0.3625 0.2310 0.2767 -0.0585 0.0438  -0.0912 231 SER A N   
1966  C CA  . SER A 231 ? 0.3704 0.2248 0.2884 -0.0558 0.0437  -0.0889 231 SER A CA  
1967  C C   . SER A 231 ? 0.3350 0.1788 0.2610 -0.0416 0.0482  -0.0886 231 SER A C   
1968  O O   . SER A 231 ? 0.3336 0.1698 0.2654 -0.0362 0.0463  -0.0826 231 SER A O   
1969  C CB  . SER A 231 ? 0.4101 0.2556 0.3187 -0.0644 0.0454  -0.0944 231 SER A CB  
1970  O OG  . SER A 231 ? 0.5358 0.3915 0.4398 -0.0767 0.0392  -0.0926 231 SER A OG  
1971  N N   . LYS A 232 ? 0.3101 0.1542 0.2365 -0.0351 0.0540  -0.0946 232 LYS A N   
1972  C CA  . LYS A 232 ? 0.3204 0.1576 0.2562 -0.0203 0.0572  -0.0942 232 LYS A CA  
1973  C C   . LYS A 232 ? 0.2969 0.1433 0.2437 -0.0126 0.0536  -0.0871 232 LYS A C   
1974  O O   . LYS A 232 ? 0.2914 0.1304 0.2452 -0.0020 0.0524  -0.0826 232 LYS A O   
1975  C CB  . LYS A 232 ? 0.3331 0.1734 0.2692 -0.0153 0.0641  -0.1026 232 LYS A CB  
1976  C CG  . LYS A 232 ? 0.3881 0.2125 0.3167 -0.0162 0.0687  -0.1095 232 LYS A CG  
1977  C CD  . LYS A 232 ? 0.3677 0.1977 0.2947 -0.0142 0.0761  -0.1187 232 LYS A CD  
1978  C CE  . LYS A 232 ? 0.5346 0.3564 0.4473 -0.0253 0.0794  -0.1261 232 LYS A CE  
1979  N NZ  . LYS A 232 ? 0.6249 0.4610 0.5306 -0.0328 0.0832  -0.1318 232 LYS A NZ  
1980  N N   . HIS A 233 ? 0.3555 0.2175 0.3030 -0.0180 0.0515  -0.0860 233 HIS A N   
1981  C CA  . HIS A 233 ? 0.2545 0.1255 0.2124 -0.0116 0.0484  -0.0800 233 HIS A CA  
1982  C C   . HIS A 233 ? 0.2836 0.1472 0.2434 -0.0107 0.0428  -0.0713 233 HIS A C   
1983  O O   . HIS A 233 ? 0.3209 0.1850 0.2892 -0.0006 0.0406  -0.0656 233 HIS A O   
1984  C CB  . HIS A 233 ? 0.2386 0.1303 0.1965 -0.0186 0.0447  -0.0770 233 HIS A CB  
1985  C CG  . HIS A 233 ? 0.2391 0.1426 0.1996 -0.0164 0.0502  -0.0827 233 HIS A CG  
1986  N ND1 . HIS A 233 ? 0.2290 0.1437 0.2032 -0.0064 0.0510  -0.0811 233 HIS A ND1 
1987  C CD2 . HIS A 233 ? 0.2496 0.1567 0.2006 -0.0239 0.0554  -0.0900 233 HIS A CD2 
1988  C CE1 . HIS A 233 ? 0.2327 0.1581 0.2072 -0.0079 0.0572  -0.0875 233 HIS A CE1 
1989  N NE2 . HIS A 233 ? 0.2456 0.1659 0.2052 -0.0184 0.0602  -0.0929 233 HIS A NE2 
1990  N N   . VAL A 234 ? 0.2871 0.1451 0.2390 -0.0216 0.0404  -0.0703 234 VAL A N   
1991  C CA  . VAL A 234 ? 0.3238 0.1746 0.2770 -0.0220 0.0368  -0.0630 234 VAL A CA  
1992  C C   . VAL A 234 ? 0.2815 0.1150 0.2336 -0.0152 0.0391  -0.0621 234 VAL A C   
1993  O O   . VAL A 234 ? 0.3525 0.1802 0.3082 -0.0077 0.0375  -0.0555 234 VAL A O   
1994  C CB  . VAL A 234 ? 0.2815 0.1365 0.2296 -0.0359 0.0331  -0.0622 234 VAL A CB  
1995  C CG1 . VAL A 234 ? 0.2427 0.0965 0.1950 -0.0365 0.0298  -0.0543 234 VAL A CG1 
1996  C CG2 . VAL A 234 ? 0.2365 0.1116 0.1849 -0.0414 0.0290  -0.0619 234 VAL A CG2 
1997  N N   . GLU A 235 ? 0.3164 0.1410 0.2623 -0.0178 0.0429  -0.0684 235 GLU A N   
1998  C CA  . GLU A 235 ? 0.3365 0.1423 0.2799 -0.0133 0.0450  -0.0678 235 GLU A CA  
1999  C C   . GLU A 235 ? 0.3445 0.1460 0.2951 0.0027  0.0452  -0.0650 235 GLU A C   
2000  O O   . GLU A 235 ? 0.3552 0.1442 0.3056 0.0081  0.0437  -0.0592 235 GLU A O   
2001  C CB  . GLU A 235 ? 0.4003 0.1976 0.3359 -0.0188 0.0494  -0.0764 235 GLU A CB  
2002  C CG  . GLU A 235 ? 0.4948 0.2850 0.4224 -0.0322 0.0491  -0.0770 235 GLU A CG  
2003  C CD  . GLU A 235 ? 0.8547 0.6397 0.7738 -0.0391 0.0531  -0.0865 235 GLU A CD  
2004  O OE1 . GLU A 235 ? 0.9427 0.7197 0.8614 -0.0310 0.0576  -0.0919 235 GLU A OE1 
2005  O OE2 . GLU A 235 ? 0.9381 0.7278 0.8512 -0.0524 0.0517  -0.0887 235 GLU A OE2 
2006  N N   . LEU A 236 ? 0.3025 0.1154 0.2596 0.0102  0.0468  -0.0691 236 LEU A N   
2007  C CA  . LEU A 236 ? 0.3036 0.1171 0.2701 0.0260  0.0460  -0.0668 236 LEU A CA  
2008  C C   . LEU A 236 ? 0.2853 0.1075 0.2580 0.0306  0.0408  -0.0583 236 LEU A C   
2009  O O   . LEU A 236 ? 0.3025 0.1211 0.2803 0.0420  0.0379  -0.0532 236 LEU A O   
2010  C CB  . LEU A 236 ? 0.3031 0.1287 0.2759 0.0319  0.0503  -0.0749 236 LEU A CB  
2011  C CG  . LEU A 236 ? 0.3238 0.1408 0.2894 0.0279  0.0562  -0.0840 236 LEU A CG  
2012  C CD1 . LEU A 236 ? 0.3196 0.1530 0.2892 0.0286  0.0614  -0.0920 236 LEU A CD1 
2013  C CD2 . LEU A 236 ? 0.3484 0.1468 0.3142 0.0379  0.0569  -0.0846 236 LEU A CD2 
2014  N N   . ALA A 237 ? 0.2688 0.1024 0.2411 0.0220  0.0392  -0.0566 237 ALA A N   
2015  C CA  . ALA A 237 ? 0.2588 0.0990 0.2356 0.0254  0.0346  -0.0487 237 ALA A CA  
2016  C C   . ALA A 237 ? 0.3099 0.1359 0.2809 0.0255  0.0317  -0.0407 237 ALA A C   
2017  O O   . ALA A 237 ? 0.3075 0.1339 0.2811 0.0336  0.0281  -0.0339 237 ALA A O   
2018  C CB  . ALA A 237 ? 0.2692 0.1277 0.2472 0.0150  0.0315  -0.0473 237 ALA A CB  
2019  N N   . LYS A 238 ? 0.3148 0.1293 0.2775 0.0156  0.0335  -0.0416 238 LYS A N   
2020  C CA  . LYS A 238 ? 0.2832 0.0845 0.2401 0.0137  0.0323  -0.0346 238 LYS A CA  
2021  C C   . LYS A 238 ? 0.3611 0.1485 0.3177 0.0251  0.0321  -0.0317 238 LYS A C   
2022  O O   . LYS A 238 ? 0.4491 0.2295 0.4027 0.0286  0.0297  -0.0236 238 LYS A O   
2023  C CB  . LYS A 238 ? 0.2924 0.0867 0.2420 -0.0004 0.0349  -0.0373 238 LYS A CB  
2024  C CG  . LYS A 238 ? 0.2747 0.0833 0.2255 -0.0118 0.0334  -0.0378 238 LYS A CG  
2025  C CD  . LYS A 238 ? 0.2846 0.0903 0.2301 -0.0254 0.0352  -0.0418 238 LYS A CD  
2026  C CE  . LYS A 238 ? 0.3844 0.1755 0.3245 -0.0290 0.0370  -0.0373 238 LYS A CE  
2027  N NZ  . LYS A 238 ? 0.3907 0.1740 0.3251 -0.0393 0.0399  -0.0431 238 LYS A NZ  
2028  N N   . GLU A 239 ? 0.3146 0.0978 0.2739 0.0311  0.0346  -0.0382 239 GLU A N   
2029  C CA  . GLU A 239 ? 0.3353 0.1051 0.2958 0.0427  0.0340  -0.0357 239 GLU A CA  
2030  C C   . GLU A 239 ? 0.3451 0.1266 0.3159 0.0567  0.0294  -0.0313 239 GLU A C   
2031  O O   . GLU A 239 ? 0.3900 0.1628 0.3604 0.0647  0.0263  -0.0241 239 GLU A O   
2032  C CB  . GLU A 239 ? 0.4739 0.2348 0.4344 0.0447  0.0385  -0.0448 239 GLU A CB  
2033  C CG  . GLU A 239 ? 0.6427 0.3886 0.5920 0.0315  0.0427  -0.0482 239 GLU A CG  
2034  C CD  . GLU A 239 ? 0.7225 0.4501 0.6636 0.0282  0.0421  -0.0402 239 GLU A CD  
2035  O OE1 . GLU A 239 ? 0.8171 0.5293 0.7577 0.0377  0.0418  -0.0370 239 GLU A OE1 
2036  O OE2 . GLU A 239 ? 0.5950 0.3241 0.5304 0.0162  0.0421  -0.0372 239 GLU A OE2 
2037  N N   . LYS A 240 ? 0.3097 0.1114 0.2895 0.0594  0.0288  -0.0354 240 LYS A N   
2038  C CA  . LYS A 240 ? 0.2966 0.1127 0.2872 0.0713  0.0241  -0.0313 240 LYS A CA  
2039  C C   . LYS A 240 ? 0.2900 0.1061 0.2747 0.0697  0.0191  -0.0210 240 LYS A C   
2040  O O   . LYS A 240 ? 0.3693 0.1863 0.3561 0.0792  0.0143  -0.0142 240 LYS A O   
2041  C CB  . LYS A 240 ? 0.2924 0.1305 0.2929 0.0725  0.0255  -0.0380 240 LYS A CB  
2042  C CG  . LYS A 240 ? 0.2668 0.1233 0.2800 0.0841  0.0208  -0.0346 240 LYS A CG  
2043  C CD  . LYS A 240 ? 0.4693 0.3300 0.4960 0.0965  0.0218  -0.0379 240 LYS A CD  
2044  C CE  . LYS A 240 ? 0.3536 0.2239 0.3879 0.1079  0.0150  -0.0294 240 LYS A CE  
2045  N NZ  . LYS A 240 ? 0.2982 0.1692 0.3453 0.1201  0.0164  -0.0309 240 LYS A NZ  
2046  N N   . TYR A 241 ? 0.2792 0.0951 0.2561 0.0577  0.0201  -0.0200 241 TYR A N   
2047  C CA  . TYR A 241 ? 0.2758 0.0899 0.2454 0.0548  0.0167  -0.0113 241 TYR A CA  
2048  C C   . TYR A 241 ? 0.2992 0.0938 0.2593 0.0557  0.0165  -0.0045 241 TYR A C   
2049  O O   . TYR A 241 ? 0.4054 0.1983 0.3604 0.0598  0.0125  0.0037  241 TYR A O   
2050  C CB  . TYR A 241 ? 0.2621 0.0797 0.2274 0.0413  0.0189  -0.0127 241 TYR A CB  
2051  C CG  . TYR A 241 ? 0.2575 0.0753 0.2163 0.0376  0.0165  -0.0053 241 TYR A CG  
2052  C CD1 . TYR A 241 ? 0.3202 0.1238 0.2690 0.0312  0.0185  -0.0003 241 TYR A CD1 
2053  C CD2 . TYR A 241 ? 0.2375 0.0756 0.2024 0.0385  0.0122  -0.0039 241 TYR A CD2 
2054  C CE1 . TYR A 241 ? 0.3357 0.1398 0.2781 0.0273  0.0177  0.0057  241 TYR A CE1 
2055  C CE2 . TYR A 241 ? 0.2336 0.0746 0.1934 0.0345  0.0104  0.0017  241 TYR A CE2 
2056  C CZ  . TYR A 241 ? 0.2666 0.0894 0.2145 0.0294  0.0137  0.0065  241 TYR A CZ  
2057  O OH  . TYR A 241 ? 0.3217 0.1484 0.2644 0.0251  0.0132  0.0114  241 TYR A OH  
2058  N N   . PHE A 242 ? 0.3452 0.1244 0.3013 0.0515  0.0208  -0.0078 242 PHE A N   
2059  C CA  . PHE A 242 ? 0.3426 0.1009 0.2892 0.0524  0.0214  -0.0017 242 PHE A CA  
2060  C C   . PHE A 242 ? 0.3868 0.1426 0.3375 0.0676  0.0170  0.0032  242 PHE A C   
2061  O O   . PHE A 242 ? 0.4289 0.1730 0.3707 0.0705  0.0146  0.0120  242 PHE A O   
2062  C CB  . PHE A 242 ? 0.3602 0.1025 0.3024 0.0452  0.0269  -0.0075 242 PHE A CB  
2063  C CG  . PHE A 242 ? 0.3897 0.1084 0.3209 0.0445  0.0284  -0.0015 242 PHE A CG  
2064  C CD1 . PHE A 242 ? 0.4130 0.1184 0.3454 0.0562  0.0272  0.0004  242 PHE A CD1 
2065  C CD2 . PHE A 242 ? 0.3956 0.1059 0.3159 0.0321  0.0311  0.0024  242 PHE A CD2 
2066  C CE1 . PHE A 242 ? 0.5018 0.1835 0.4229 0.0555  0.0286  0.0066  242 PHE A CE1 
2067  C CE2 . PHE A 242 ? 0.4248 0.1127 0.3339 0.0306  0.0331  0.0081  242 PHE A CE2 
2068  C CZ  . PHE A 242 ? 0.4875 0.1600 0.3961 0.0423  0.0318  0.0105  242 PHE A CZ  
2069  N N   . GLU A 243 ? 0.3506 0.1179 0.3147 0.0773  0.0160  -0.0026 243 GLU A N   
2070  C CA  . GLU A 243 ? 0.3639 0.1318 0.3350 0.0923  0.0116  0.0015  243 GLU A CA  
2071  C C   . GLU A 243 ? 0.3574 0.1357 0.3261 0.0973  0.0045  0.0108  243 GLU A C   
2072  O O   . GLU A 243 ? 0.4774 0.2465 0.4412 0.1048  0.0004  0.0191  243 GLU A O   
2073  C CB  . GLU A 243 ? 0.3559 0.1395 0.3446 0.1008  0.0127  -0.0075 243 GLU A CB  
2074  C CG  . GLU A 243 ? 0.4037 0.1895 0.4032 0.1167  0.0089  -0.0043 243 GLU A CG  
2075  C CD  . GLU A 243 ? 0.4513 0.2613 0.4708 0.1247  0.0097  -0.0121 243 GLU A CD  
2076  O OE1 . GLU A 243 ? 0.3472 0.1628 0.3712 0.1192  0.0156  -0.0226 243 GLU A OE1 
2077  O OE2 . GLU A 243 ? 0.5084 0.3329 0.5385 0.1361  0.0044  -0.0078 243 GLU A OE2 
2078  N N   . ILE A 244 ? 0.3960 0.1926 0.3669 0.0930  0.0028  0.0095  244 ILE A N   
2079  C CA  . ILE A 244 ? 0.3674 0.1754 0.3355 0.0975  -0.0044 0.0168  244 ILE A CA  
2080  C C   . ILE A 244 ? 0.3359 0.1291 0.2856 0.0897  -0.0045 0.0250  244 ILE A C   
2081  O O   . ILE A 244 ? 0.3698 0.1584 0.3111 0.0951  -0.0096 0.0335  244 ILE A O   
2082  C CB  . ILE A 244 ? 0.2976 0.1301 0.2751 0.0962  -0.0063 0.0116  244 ILE A CB  
2083  C CG1 . ILE A 244 ? 0.2882 0.1339 0.2826 0.1004  -0.0032 0.0020  244 ILE A CG1 
2084  C CG2 . ILE A 244 ? 0.3577 0.2050 0.3353 0.1032  -0.0151 0.0173  244 ILE A CG2 
2085  C CD1 . ILE A 244 ? 0.2945 0.1536 0.3027 0.1142  -0.0077 0.0024  244 ILE A CD1 
2086  N N   . PHE A 245 ? 0.3290 0.1157 0.2722 0.0766  0.0013  0.0224  245 PHE A N   
2087  C CA  . PHE A 245 ? 0.3341 0.1119 0.2620 0.0679  0.0024  0.0287  245 PHE A CA  
2088  C C   . PHE A 245 ? 0.4261 0.1805 0.3425 0.0610  0.0076  0.0318  245 PHE A C   
2089  O O   . PHE A 245 ? 0.5610 0.3075 0.4646 0.0531  0.0097  0.0371  245 PHE A O   
2090  C CB  . PHE A 245 ? 0.3522 0.1416 0.2819 0.0576  0.0050  0.0243  245 PHE A CB  
2091  C CG  . PHE A 245 ? 0.3516 0.1622 0.2907 0.0633  0.0000  0.0215  245 PHE A CG  
2092  C CD1 . PHE A 245 ? 0.3456 0.1634 0.2795 0.0688  -0.0063 0.0271  245 PHE A CD1 
2093  C CD2 . PHE A 245 ? 0.3175 0.1409 0.2694 0.0627  0.0014  0.0131  245 PHE A CD2 
2094  C CE1 . PHE A 245 ? 0.3224 0.1637 0.2670 0.0719  -0.0113 0.0234  245 PHE A CE1 
2095  C CE2 . PHE A 245 ? 0.2777 0.1249 0.2404 0.0655  -0.0030 0.0100  245 PHE A CE2 
2096  C CZ  . PHE A 245 ? 0.2483 0.1055 0.2085 0.0695  -0.0094 0.0148  245 PHE A CZ  
2097  N N   . GLY A 246 ? 0.4742 0.2173 0.3946 0.0633  0.0103  0.0282  246 GLY A N   
2098  C CA  . GLY A 246 ? 0.4740 0.1933 0.3829 0.0577  0.0147  0.0314  246 GLY A CA  
2099  C C   . GLY A 246 ? 0.4321 0.1466 0.3352 0.0414  0.0213  0.0281  246 GLY A C   
2100  O O   . GLY A 246 ? 0.4308 0.1276 0.3222 0.0346  0.0250  0.0322  246 GLY A O   
2101  N N   . GLU A 247 ? 0.4886 0.2193 0.4000 0.0347  0.0228  0.0210  247 GLU A N   
2102  C CA  . GLU A 247 ? 0.4912 0.2214 0.3998 0.0193  0.0284  0.0173  247 GLU A CA  
2103  C C   . GLU A 247 ? 0.4701 0.2178 0.3904 0.0158  0.0286  0.0084  247 GLU A C   
2104  O O   . GLU A 247 ? 0.5419 0.3039 0.4706 0.0237  0.0248  0.0067  247 GLU A O   
2105  C CB  . GLU A 247 ? 0.5145 0.2471 0.4149 0.0117  0.0296  0.0234  247 GLU A CB  
2106  C CG  . GLU A 247 ? 0.5394 0.2875 0.4422 0.0181  0.0248  0.0265  247 GLU A CG  
2107  C CD  . GLU A 247 ? 0.6539 0.4002 0.5453 0.0123  0.0265  0.0332  247 GLU A CD  
2108  O OE1 . GLU A 247 ? 0.6392 0.3946 0.5330 0.0018  0.0303  0.0306  247 GLU A OE1 
2109  O OE2 . GLU A 247 ? 0.7338 0.4702 0.6140 0.0182  0.0242  0.0410  247 GLU A OE2 
2110  N N   . HIS A 248 ? 0.3860 0.1329 0.3064 0.0035  0.0328  0.0028  248 HIS A N   
2111  C CA  . HIS A 248 ? 0.3570 0.1200 0.2864 -0.0013 0.0328  -0.0050 248 HIS A CA  
2112  C C   . HIS A 248 ? 0.3590 0.1392 0.2927 -0.0036 0.0306  -0.0030 248 HIS A C   
2113  O O   . HIS A 248 ? 0.4633 0.2428 0.3922 -0.0078 0.0315  0.0025  248 HIS A O   
2114  C CB  . HIS A 248 ? 0.4218 0.1814 0.3493 -0.0149 0.0368  -0.0108 248 HIS A CB  
2115  C CG  . HIS A 248 ? 0.5068 0.2566 0.4337 -0.0130 0.0387  -0.0175 248 HIS A CG  
2116  N ND1 . HIS A 248 ? 0.5597 0.3053 0.4837 -0.0245 0.0420  -0.0237 248 HIS A ND1 
2117  C CD2 . HIS A 248 ? 0.4606 0.2046 0.3898 -0.0011 0.0378  -0.0196 248 HIS A CD2 
2118  C CE1 . HIS A 248 ? 0.4402 0.1762 0.3632 -0.0198 0.0435  -0.0293 248 HIS A CE1 
2119  N NE2 . HIS A 248 ? 0.4363 0.1713 0.3631 -0.0054 0.0413  -0.0271 248 HIS A NE2 
2120  N N   . PRO A 249 ? 0.3114 0.1066 0.2536 -0.0011 0.0284  -0.0076 249 PRO A N   
2121  C CA  . PRO A 249 ? 0.2669 0.0772 0.2136 -0.0047 0.0269  -0.0067 249 PRO A CA  
2122  C C   . PRO A 249 ? 0.3015 0.1183 0.2505 -0.0189 0.0293  -0.0100 249 PRO A C   
2123  O O   . PRO A 249 ? 0.3128 0.1280 0.2618 -0.0254 0.0307  -0.0156 249 PRO A O   
2124  C CB  . PRO A 249 ? 0.2402 0.0662 0.1962 0.0024  0.0234  -0.0107 249 PRO A CB  
2125  C CG  . PRO A 249 ? 0.2517 0.0682 0.2068 0.0037  0.0259  -0.0171 249 PRO A CG  
2126  C CD  . PRO A 249 ? 0.3686 0.1671 0.3162 0.0031  0.0283  -0.0148 249 PRO A CD  
2127  N N   . VAL A 250 ? 0.2703 0.1008 0.2232 -0.0230 0.0284  -0.0067 250 VAL A N   
2128  C CA  . VAL A 250 ? 0.3477 0.1927 0.3076 -0.0345 0.0289  -0.0096 250 VAL A CA  
2129  C C   . VAL A 250 ? 0.2572 0.1269 0.2286 -0.0320 0.0241  -0.0101 250 VAL A C   
2130  O O   . VAL A 250 ? 0.2675 0.1515 0.2463 -0.0394 0.0227  -0.0127 250 VAL A O   
2131  C CB  . VAL A 250 ? 0.2786 0.1193 0.2351 -0.0431 0.0335  -0.0061 250 VAL A CB  
2132  C CG1 . VAL A 250 ? 0.2843 0.1039 0.2307 -0.0487 0.0379  -0.0066 250 VAL A CG1 
2133  C CG2 . VAL A 250 ? 0.2409 0.0815 0.1936 -0.0362 0.0336  0.0005  250 VAL A CG2 
2134  N N   . TYR A 251 ? 0.1980 0.0727 0.1709 -0.0220 0.0211  -0.0076 251 TYR A N   
2135  C CA  . TYR A 251 ? 0.1874 0.0816 0.1697 -0.0192 0.0169  -0.0081 251 TYR A CA  
2136  C C   . TYR A 251 ? 0.1922 0.0880 0.1757 -0.0134 0.0143  -0.0110 251 TYR A C   
2137  O O   . TYR A 251 ? 0.2704 0.1559 0.2494 -0.0066 0.0148  -0.0109 251 TYR A O   
2138  C CB  . TYR A 251 ? 0.2021 0.1016 0.1850 -0.0143 0.0164  -0.0039 251 TYR A CB  
2139  C CG  . TYR A 251 ? 0.2090 0.1046 0.1884 -0.0196 0.0207  -0.0010 251 TYR A CG  
2140  C CD1 . TYR A 251 ? 0.2019 0.1050 0.1873 -0.0289 0.0230  -0.0028 251 TYR A CD1 
2141  C CD2 . TYR A 251 ? 0.2312 0.1168 0.2011 -0.0159 0.0226  0.0034  251 TYR A CD2 
2142  C CE1 . TYR A 251 ? 0.3476 0.2491 0.3310 -0.0349 0.0281  -0.0007 251 TYR A CE1 
2143  C CE2 . TYR A 251 ? 0.2124 0.0942 0.1776 -0.0219 0.0278  0.0061  251 TYR A CE2 
2144  C CZ  . TYR A 251 ? 0.3319 0.2220 0.3045 -0.0317 0.0311  0.0037  251 TYR A CZ  
2145  O OH  . TYR A 251 ? 0.4887 0.3769 0.4578 -0.0387 0.0373  0.0058  251 TYR A OH  
2146  N N   . MET A 252 ? 0.1623 0.0712 0.1516 -0.0159 0.0116  -0.0135 252 MET A N   
2147  C CA  . MET A 252 ? 0.1589 0.0708 0.1489 -0.0124 0.0102  -0.0167 252 MET A CA  
2148  C C   . MET A 252 ? 0.1569 0.0840 0.1531 -0.0125 0.0066  -0.0157 252 MET A C   
2149  O O   . MET A 252 ? 0.1613 0.0962 0.1611 -0.0171 0.0048  -0.0143 252 MET A O   
2150  C CB  . MET A 252 ? 0.1688 0.0746 0.1544 -0.0180 0.0122  -0.0219 252 MET A CB  
2151  C CG  . MET A 252 ? 0.1830 0.0734 0.1632 -0.0131 0.0159  -0.0249 252 MET A CG  
2152  S SD  . MET A 252 ? 0.4702 0.3545 0.4446 -0.0194 0.0190  -0.0332 252 MET A SD  
2153  C CE  . MET A 252 ? 0.2508 0.1133 0.2202 -0.0111 0.0241  -0.0357 252 MET A CE  
2154  N N   . TRP A 253 ? 0.2148 0.1459 0.2127 -0.0074 0.0056  -0.0164 253 TRP A N   
2155  C CA  . TRP A 253 ? 0.2019 0.1440 0.2037 -0.0083 0.0029  -0.0156 253 TRP A CA  
2156  C C   . TRP A 253 ? 0.1789 0.1233 0.1779 -0.0122 0.0033  -0.0190 253 TRP A C   
2157  O O   . TRP A 253 ? 0.2933 0.2356 0.2911 -0.0096 0.0058  -0.0226 253 TRP A O   
2158  C CB  . TRP A 253 ? 0.1631 0.1090 0.1680 -0.0025 0.0019  -0.0147 253 TRP A CB  
2159  C CG  . TRP A 253 ? 0.1273 0.0810 0.1345 -0.0042 0.0003  -0.0148 253 TRP A CG  
2160  C CD1 . TRP A 253 ? 0.1219 0.0797 0.1298 -0.0041 0.0012  -0.0175 253 TRP A CD1 
2161  C CD2 . TRP A 253 ? 0.1387 0.0962 0.1478 -0.0065 -0.0021 -0.0119 253 TRP A CD2 
2162  N NE1 . TRP A 253 ? 0.1354 0.0976 0.1437 -0.0074 -0.0002 -0.0160 253 TRP A NE1 
2163  C CE2 . TRP A 253 ? 0.1140 0.0750 0.1228 -0.0082 -0.0026 -0.0123 253 TRP A CE2 
2164  C CE3 . TRP A 253 ? 0.1536 0.1119 0.1652 -0.0070 -0.0035 -0.0090 253 TRP A CE3 
2165  C CZ2 . TRP A 253 ? 0.1128 0.0750 0.1221 -0.0100 -0.0049 -0.0092 253 TRP A CZ2 
2166  C CZ3 . TRP A 253 ? 0.1554 0.1170 0.1696 -0.0075 -0.0059 -0.0065 253 TRP A CZ3 
2167  C CH2 . TRP A 253 ? 0.1290 0.0909 0.1412 -0.0088 -0.0068 -0.0062 253 TRP A CH2 
2168  N N   . PRO A 254 ? 0.1374 0.0866 0.1351 -0.0180 0.0009  -0.0181 254 PRO A N   
2169  C CA  . PRO A 254 ? 0.1633 0.1142 0.1553 -0.0226 0.0013  -0.0211 254 PRO A CA  
2170  C C   . PRO A 254 ? 0.1561 0.1115 0.1488 -0.0206 0.0020  -0.0211 254 PRO A C   
2171  O O   . PRO A 254 ? 0.1537 0.1128 0.1501 -0.0189 -0.0004 -0.0172 254 PRO A O   
2172  C CB  . PRO A 254 ? 0.1706 0.1270 0.1612 -0.0284 -0.0033 -0.0183 254 PRO A CB  
2173  C CG  . PRO A 254 ? 0.1507 0.1110 0.1493 -0.0247 -0.0059 -0.0134 254 PRO A CG  
2174  C CD  . PRO A 254 ? 0.1281 0.0828 0.1299 -0.0199 -0.0026 -0.0141 254 PRO A CD  
2175  N N   . PRO A 255 ? 0.1536 0.1085 0.1431 -0.0212 0.0060  -0.0260 255 PRO A N   
2176  C CA  . PRO A 255 ? 0.1615 0.1226 0.1530 -0.0204 0.0078  -0.0268 255 PRO A CA  
2177  C C   . PRO A 255 ? 0.1379 0.1024 0.1256 -0.0254 0.0048  -0.0222 255 PRO A C   
2178  O O   . PRO A 255 ? 0.2876 0.2514 0.2675 -0.0310 0.0029  -0.0208 255 PRO A O   
2179  C CB  . PRO A 255 ? 0.2135 0.1744 0.2011 -0.0218 0.0134  -0.0336 255 PRO A CB  
2180  C CG  . PRO A 255 ? 0.1539 0.1056 0.1409 -0.0188 0.0148  -0.0365 255 PRO A CG  
2181  C CD  . PRO A 255 ? 0.1948 0.1433 0.1795 -0.0223 0.0101  -0.0319 255 PRO A CD  
2182  N N   . GLU A 256 ? 0.1740 0.1413 0.1667 -0.0234 0.0039  -0.0196 256 GLU A N   
2183  C CA  . GLU A 256 ? 0.2744 0.2413 0.2637 -0.0271 0.0012  -0.0145 256 GLU A CA  
2184  C C   . GLU A 256 ? 0.1665 0.1307 0.1544 -0.0270 -0.0042 -0.0093 256 GLU A C   
2185  O O   . GLU A 256 ? 0.1670 0.1298 0.1494 -0.0302 -0.0073 -0.0046 256 GLU A O   
2186  C CB  . GLU A 256 ? 0.1807 0.1489 0.1610 -0.0340 0.0041  -0.0154 256 GLU A CB  
2187  C CG  . GLU A 256 ? 0.2092 0.1833 0.1923 -0.0343 0.0106  -0.0222 256 GLU A CG  
2188  C CD  . GLU A 256 ? 0.3314 0.3105 0.3208 -0.0348 0.0126  -0.0226 256 GLU A CD  
2189  O OE1 . GLU A 256 ? 0.2666 0.2538 0.2599 -0.0358 0.0180  -0.0282 256 GLU A OE1 
2190  O OE2 . GLU A 256 ? 0.3706 0.3462 0.3617 -0.0343 0.0090  -0.0181 256 GLU A OE2 
2191  N N   . ALA A 257 ? 0.1339 0.0977 0.1271 -0.0233 -0.0053 -0.0098 257 ALA A N   
2192  C CA  . ALA A 257 ? 0.1282 0.0929 0.1237 -0.0229 -0.0097 -0.0060 257 ALA A CA  
2193  C C   . ALA A 257 ? 0.1566 0.1235 0.1451 -0.0285 -0.0129 -0.0049 257 ALA A C   
2194  O O   . ALA A 257 ? 0.1577 0.1283 0.1490 -0.0284 -0.0178 -0.0011 257 ALA A O   
2195  C CB  . ALA A 257 ? 0.1258 0.0899 0.1260 -0.0194 -0.0125 -0.0011 257 ALA A CB  
2196  N N   . SER A 258 ? 0.1553 0.1212 0.1349 -0.0334 -0.0103 -0.0086 258 SER A N   
2197  C CA  . SER A 258 ? 0.1549 0.1229 0.1248 -0.0399 -0.0136 -0.0077 258 SER A CA  
2198  C C   . SER A 258 ? 0.1561 0.1266 0.1278 -0.0422 -0.0159 -0.0100 258 SER A C   
2199  O O   . SER A 258 ? 0.1548 0.1215 0.1286 -0.0419 -0.0115 -0.0154 258 SER A O   
2200  C CB  . SER A 258 ? 0.2161 0.1820 0.1747 -0.0451 -0.0087 -0.0123 258 SER A CB  
2201  O OG  . SER A 258 ? 0.3543 0.3177 0.3158 -0.0433 -0.0024 -0.0198 258 SER A OG  
2202  N N   . VAL A 259 ? 0.1604 0.1372 0.1315 -0.0447 -0.0228 -0.0058 259 VAL A N   
2203  C CA  . VAL A 259 ? 0.1624 0.1446 0.1366 -0.0485 -0.0258 -0.0080 259 VAL A CA  
2204  C C   . VAL A 259 ? 0.1848 0.1731 0.1486 -0.0557 -0.0322 -0.0068 259 VAL A C   
2205  O O   . VAL A 259 ? 0.2172 0.2055 0.1724 -0.0563 -0.0355 -0.0020 259 VAL A O   
2206  C CB  . VAL A 259 ? 0.1541 0.1432 0.1435 -0.0434 -0.0287 -0.0041 259 VAL A CB  
2207  C CG1 . VAL A 259 ? 0.2618 0.2449 0.2583 -0.0394 -0.0221 -0.0072 259 VAL A CG1 
2208  C CG2 . VAL A 259 ? 0.1504 0.1422 0.1439 -0.0374 -0.0333 0.0034  259 VAL A CG2 
2209  N N   . SER A 260 ? 0.1810 0.1739 0.1445 -0.0621 -0.0340 -0.0112 260 SER A N   
2210  C CA  . SER A 260 ? 0.1938 0.1960 0.1495 -0.0695 -0.0420 -0.0103 260 SER A CA  
2211  C C   . SER A 260 ? 0.2744 0.2834 0.2369 -0.0755 -0.0432 -0.0153 260 SER A C   
2212  O O   . SER A 260 ? 0.2647 0.2669 0.2333 -0.0752 -0.0364 -0.0201 260 SER A O   
2213  C CB  . SER A 260 ? 0.2827 0.2786 0.2180 -0.0767 -0.0400 -0.0141 260 SER A CB  
2214  O OG  . SER A 260 ? 0.3474 0.3350 0.2774 -0.0819 -0.0323 -0.0243 260 SER A OG  
2215  N N   . ASN A 261 ? 0.3504 0.3731 0.3117 -0.0814 -0.0525 -0.0138 261 ASN A N   
2216  C CA  . ASN A 261 ? 0.2079 0.2387 0.1749 -0.0899 -0.0539 -0.0196 261 ASN A CA  
2217  C C   . ASN A 261 ? 0.3301 0.3462 0.2847 -0.0982 -0.0456 -0.0301 261 ASN A C   
2218  O O   . ASN A 261 ? 0.4230 0.4367 0.3836 -0.1031 -0.0416 -0.0355 261 ASN A O   
2219  C CB  . ASN A 261 ? 0.2846 0.3342 0.2502 -0.0959 -0.0662 -0.0171 261 ASN A CB  
2220  C CG  . ASN A 261 ? 0.2400 0.3018 0.2156 -0.0860 -0.0750 -0.0060 261 ASN A CG  
2221  O OD1 . ASN A 261 ? 0.2089 0.2856 0.2038 -0.0820 -0.0790 -0.0031 261 ASN A OD1 
2222  N ND2 . ASN A 261 ? 0.2266 0.2815 0.1890 -0.0821 -0.0775 0.0000  261 ASN A ND2 
2223  N N   . GLU A 262 ? 0.3289 0.3343 0.2661 -0.1001 -0.0422 -0.0331 262 GLU A N   
2224  C CA  . GLU A 262 ? 0.2717 0.2617 0.1972 -0.1064 -0.0334 -0.0437 262 GLU A CA  
2225  C C   . GLU A 262 ? 0.2543 0.2291 0.1867 -0.0982 -0.0231 -0.0455 262 GLU A C   
2226  O O   . GLU A 262 ? 0.3682 0.3306 0.2987 -0.1017 -0.0165 -0.0529 262 GLU A O   
2227  C CB  . GLU A 262 ? 0.3444 0.3300 0.2494 -0.1110 -0.0326 -0.0469 262 GLU A CB  
2228  C CG  . GLU A 262 ? 0.4741 0.4715 0.3695 -0.1193 -0.0407 -0.0467 262 GLU A CG  
2229  C CD  . GLU A 262 ? 0.5995 0.6071 0.4871 -0.1183 -0.0502 -0.0376 262 GLU A CD  
2230  O OE1 . GLU A 262 ? 0.5333 0.5373 0.4027 -0.1219 -0.0487 -0.0387 262 GLU A OE1 
2231  O OE2 . GLU A 262 ? 0.6639 0.6823 0.5645 -0.1122 -0.0580 -0.0283 262 GLU A OE2 
2232  N N   . ALA A 263 ? 0.2378 0.2126 0.1775 -0.0875 -0.0220 -0.0388 263 ALA A N   
2233  C CA  . ALA A 263 ? 0.2980 0.2608 0.2444 -0.0793 -0.0138 -0.0398 263 ALA A CA  
2234  C C   . ALA A 263 ? 0.2418 0.2054 0.2016 -0.0776 -0.0136 -0.0378 263 ALA A C   
2235  O O   . ALA A 263 ? 0.3501 0.3006 0.3105 -0.0763 -0.0070 -0.0415 263 ALA A O   
2236  C CB  . ALA A 263 ? 0.2012 0.1650 0.1506 -0.0700 -0.0130 -0.0340 263 ALA A CB  
2237  N N   . LEU A 264 ? 0.1923 0.1708 0.1625 -0.0772 -0.0205 -0.0318 264 LEU A N   
2238  C CA  . LEU A 264 ? 0.2040 0.1857 0.1869 -0.0770 -0.0194 -0.0306 264 LEU A CA  
2239  C C   . LEU A 264 ? 0.3335 0.3103 0.3127 -0.0881 -0.0169 -0.0377 264 LEU A C   
2240  O O   . LEU A 264 ? 0.2824 0.2516 0.2664 -0.0888 -0.0116 -0.0387 264 LEU A O   
2241  C CB  . LEU A 264 ? 0.2378 0.2390 0.2339 -0.0746 -0.0271 -0.0240 264 LEU A CB  
2242  C CG  . LEU A 264 ? 0.2642 0.2676 0.2666 -0.0631 -0.0283 -0.0169 264 LEU A CG  
2243  C CD1 . LEU A 264 ? 0.2623 0.2820 0.2704 -0.0614 -0.0378 -0.0110 264 LEU A CD1 
2244  C CD2 . LEU A 264 ? 0.1954 0.1963 0.2088 -0.0570 -0.0232 -0.0152 264 LEU A CD2 
2245  N N   . GLU A 265 ? 0.4014 0.3815 0.3707 -0.0978 -0.0205 -0.0426 265 GLU A N   
2246  C CA  . GLU A 265 ? 0.2772 0.2491 0.2403 -0.1091 -0.0171 -0.0508 265 GLU A CA  
2247  C C   . GLU A 265 ? 0.3151 0.2623 0.2699 -0.1050 -0.0068 -0.0553 265 GLU A C   
2248  O O   . GLU A 265 ? 0.3246 0.2610 0.2810 -0.1064 -0.0014 -0.0571 265 GLU A O   
2249  C CB  . GLU A 265 ? 0.3331 0.3136 0.2863 -0.1162 -0.0225 -0.0541 265 GLU A CB  
2250  C CG  . GLU A 265 ? 0.4812 0.4862 0.4442 -0.1212 -0.0327 -0.0507 265 GLU A CG  
2251  C CD  . GLU A 265 ? 0.5867 0.5998 0.5375 -0.1270 -0.0389 -0.0528 265 GLU A CD  
2252  O OE1 . GLU A 265 ? 0.4598 0.4602 0.3943 -0.1272 -0.0350 -0.0565 265 GLU A OE1 
2253  O OE2 . GLU A 265 ? 0.5600 0.5927 0.5178 -0.1311 -0.0475 -0.0508 265 GLU A OE2 
2254  N N   . LEU A 266 ? 0.3482 0.2868 0.2945 -0.0994 -0.0041 -0.0568 266 LEU A N   
2255  C CA  . LEU A 266 ? 0.2943 0.2121 0.2343 -0.0938 0.0051  -0.0612 266 LEU A CA  
2256  C C   . LEU A 266 ? 0.2433 0.1502 0.1913 -0.0863 0.0094  -0.0574 266 LEU A C   
2257  O O   . LEU A 266 ? 0.3412 0.2320 0.2866 -0.0839 0.0154  -0.0593 266 LEU A O   
2258  C CB  . LEU A 266 ? 0.2768 0.1921 0.2087 -0.0892 0.0072  -0.0637 266 LEU A CB  
2259  C CG  . LEU A 266 ? 0.2525 0.1504 0.1825 -0.0800 0.0160  -0.0672 266 LEU A CG  
2260  C CD1 . LEU A 266 ? 0.3082 0.1958 0.2286 -0.0829 0.0213  -0.0748 266 LEU A CD1 
2261  C CD2 . LEU A 266 ? 0.2418 0.1453 0.1730 -0.0721 0.0168  -0.0653 266 LEU A CD2 
2262  N N   . TYR A 267 ? 0.2205 0.1388 0.1790 -0.0791 0.0060  -0.0495 267 TYR A N   
2263  C CA  . TYR A 267 ? 0.2571 0.1676 0.2223 -0.0712 0.0096  -0.0448 267 TYR A CA  
2264  C C   . TYR A 267 ? 0.2366 0.1412 0.2034 -0.0790 0.0118  -0.0453 267 TYR A C   
2265  O O   . TYR A 267 ? 0.2336 0.1204 0.1975 -0.0763 0.0175  -0.0449 267 TYR A O   
2266  C CB  . TYR A 267 ? 0.2351 0.1606 0.2107 -0.0632 0.0053  -0.0370 267 TYR A CB  
2267  C CG  . TYR A 267 ? 0.2674 0.1953 0.2415 -0.0553 0.0047  -0.0359 267 TYR A CG  
2268  C CD1 . TYR A 267 ? 0.2388 0.1540 0.2080 -0.0494 0.0099  -0.0392 267 TYR A CD1 
2269  C CD2 . TYR A 267 ? 0.1752 0.1181 0.1532 -0.0538 -0.0009 -0.0317 267 TYR A CD2 
2270  C CE1 . TYR A 267 ? 0.1854 0.1054 0.1548 -0.0434 0.0099  -0.0389 267 TYR A CE1 
2271  C CE2 . TYR A 267 ? 0.2086 0.1528 0.1845 -0.0484 -0.0007 -0.0308 267 TYR A CE2 
2272  C CZ  . TYR A 267 ? 0.2447 0.1788 0.2169 -0.0438 0.0050  -0.0347 267 TYR A CZ  
2273  O OH  . TYR A 267 ? 0.3661 0.3040 0.3377 -0.0396 0.0058  -0.0345 267 TYR A OH  
2274  N N   . TYR A 268 ? 0.2405 0.1604 0.2122 -0.0890 0.0073  -0.0459 268 TYR A N   
2275  C CA  . TYR A 268 ? 0.2357 0.1547 0.2111 -0.0969 0.0097  -0.0462 268 TYR A CA  
2276  C C   . TYR A 268 ? 0.2626 0.1635 0.2274 -0.0998 0.0148  -0.0509 268 TYR A C   
2277  O O   . TYR A 268 ? 0.3162 0.2052 0.2801 -0.1009 0.0198  -0.0495 268 TYR A O   
2278  C CB  . TYR A 268 ? 0.3339 0.2780 0.3191 -0.1057 0.0028  -0.0461 268 TYR A CB  
2279  C CG  . TYR A 268 ? 0.2601 0.2072 0.2489 -0.1147 0.0047  -0.0479 268 TYR A CG  
2280  C CD1 . TYR A 268 ? 0.2377 0.1813 0.2325 -0.1152 0.0100  -0.0446 268 TYR A CD1 
2281  C CD2 . TYR A 268 ? 0.2510 0.2045 0.2363 -0.1235 0.0016  -0.0529 268 TYR A CD2 
2282  C CE1 . TYR A 268 ? 0.2665 0.2131 0.2643 -0.1245 0.0124  -0.0463 268 TYR A CE1 
2283  C CE2 . TYR A 268 ? 0.2634 0.2201 0.2523 -0.1327 0.0035  -0.0550 268 TYR A CE2 
2284  C CZ  . TYR A 268 ? 0.2629 0.2162 0.2583 -0.1333 0.0091  -0.0517 268 TYR A CZ  
2285  O OH  . TYR A 268 ? 0.3921 0.3487 0.3908 -0.1433 0.0116  -0.0539 268 TYR A OH  
2286  N N   . GLU A 269 ? 0.2913 0.1893 0.2472 -0.1014 0.0142  -0.0565 269 GLU A N   
2287  C CA  . GLU A 269 ? 0.2856 0.1660 0.2315 -0.1042 0.0194  -0.0619 269 GLU A CA  
2288  C C   . GLU A 269 ? 0.2929 0.1505 0.2340 -0.0938 0.0259  -0.0609 269 GLU A C   
2289  O O   . GLU A 269 ? 0.3904 0.2309 0.3241 -0.0950 0.0307  -0.0643 269 GLU A O   
2290  C CB  . GLU A 269 ? 0.3330 0.2173 0.2703 -0.1084 0.0175  -0.0685 269 GLU A CB  
2291  C CG  . GLU A 269 ? 0.4547 0.3550 0.3927 -0.1208 0.0122  -0.0712 269 GLU A CG  
2292  C CD  . GLU A 269 ? 0.6925 0.6083 0.6262 -0.1230 0.0058  -0.0730 269 GLU A CD  
2293  O OE1 . GLU A 269 ? 0.6602 0.5669 0.5827 -0.1210 0.0089  -0.0776 269 GLU A OE1 
2294  O OE2 . GLU A 269 ? 0.5687 0.5059 0.5100 -0.1266 -0.0022 -0.0695 269 GLU A OE2 
2295  N N   . LYS A 270 ? 0.2780 0.1352 0.2231 -0.0834 0.0258  -0.0562 270 LYS A N   
2296  C CA  . LYS A 270 ? 0.2843 0.1229 0.2265 -0.0721 0.0305  -0.0541 270 LYS A CA  
2297  C C   . LYS A 270 ? 0.2814 0.1146 0.2272 -0.0687 0.0316  -0.0466 270 LYS A C   
2298  O O   . LYS A 270 ? 0.2850 0.1055 0.2291 -0.0582 0.0338  -0.0431 270 LYS A O   
2299  C CB  . LYS A 270 ? 0.2727 0.1147 0.2162 -0.0621 0.0298  -0.0548 270 LYS A CB  
2300  C CG  . LYS A 270 ? 0.2777 0.1244 0.2158 -0.0654 0.0299  -0.0622 270 LYS A CG  
2301  C CD  . LYS A 270 ? 0.4031 0.2334 0.3355 -0.0586 0.0356  -0.0671 270 LYS A CD  
2302  C CE  . LYS A 270 ? 0.4092 0.2425 0.3339 -0.0650 0.0370  -0.0755 270 LYS A CE  
2303  N NZ  . LYS A 270 ? 0.5747 0.3950 0.4923 -0.0719 0.0400  -0.0800 270 LYS A NZ  
2304  N N   . GLY A 271 ? 0.2762 0.1201 0.2272 -0.0773 0.0301  -0.0439 271 GLY A N   
2305  C CA  . GLY A 271 ? 0.2756 0.1151 0.2286 -0.0756 0.0323  -0.0372 271 GLY A CA  
2306  C C   . GLY A 271 ? 0.2556 0.1046 0.2151 -0.0688 0.0301  -0.0319 271 GLY A C   
2307  O O   . GLY A 271 ? 0.2942 0.1361 0.2524 -0.0647 0.0324  -0.0261 271 GLY A O   
2308  N N   . ILE A 272 ? 0.2389 0.1029 0.2041 -0.0680 0.0258  -0.0338 272 ILE A N   
2309  C CA  . ILE A 272 ? 0.2185 0.0977 0.1921 -0.0596 0.0224  -0.0280 272 ILE A CA  
2310  C C   . ILE A 272 ? 0.2094 0.1071 0.1931 -0.0663 0.0206  -0.0256 272 ILE A C   
2311  O O   . ILE A 272 ? 0.2066 0.1189 0.1956 -0.0743 0.0171  -0.0287 272 ILE A O   
2312  C CB  . ILE A 272 ? 0.2050 0.0960 0.1815 -0.0534 0.0178  -0.0293 272 ILE A CB  
2313  C CG1 . ILE A 272 ? 0.2141 0.0896 0.1830 -0.0464 0.0205  -0.0325 272 ILE A CG1 
2314  C CG2 . ILE A 272 ? 0.1861 0.0919 0.1711 -0.0456 0.0143  -0.0237 272 ILE A CG2 
2315  C CD1 . ILE A 272 ? 0.2195 0.0808 0.1858 -0.0367 0.0233  -0.0284 272 ILE A CD1 
2316  N N   . ASN A 273 ? 0.2063 0.1044 0.1926 -0.0630 0.0230  -0.0204 273 ASN A N   
2317  C CA  . ASN A 273 ? 0.1990 0.1151 0.1961 -0.0684 0.0230  -0.0188 273 ASN A CA  
2318  C C   . ASN A 273 ? 0.1973 0.1341 0.2056 -0.0610 0.0178  -0.0164 273 ASN A C   
2319  O O   . ASN A 273 ? 0.2276 0.1836 0.2479 -0.0647 0.0160  -0.0164 273 ASN A O   
2320  C CB  . ASN A 273 ? 0.2086 0.1148 0.2017 -0.0697 0.0295  -0.0148 273 ASN A CB  
2321  C CG  . ASN A 273 ? 0.3094 0.1897 0.2890 -0.0758 0.0351  -0.0157 273 ASN A CG  
2322  O OD1 . ASN A 273 ? 0.3438 0.2176 0.3199 -0.0823 0.0348  -0.0207 273 ASN A OD1 
2323  N ND2 . ASN A 273 ? 0.4257 0.2904 0.3962 -0.0736 0.0401  -0.0107 273 ASN A ND2 
2324  N N   . MET A 274 ? 0.2067 0.1402 0.2121 -0.0506 0.0155  -0.0146 274 MET A N   
2325  C CA  . MET A 274 ? 0.1572 0.1061 0.1715 -0.0438 0.0116  -0.0122 274 MET A CA  
2326  C C   . MET A 274 ? 0.1491 0.0950 0.1595 -0.0366 0.0081  -0.0123 274 MET A C   
2327  O O   . MET A 274 ? 0.2165 0.1486 0.2185 -0.0334 0.0099  -0.0132 274 MET A O   
2328  C CB  . MET A 274 ? 0.2924 0.2413 0.3082 -0.0396 0.0154  -0.0088 274 MET A CB  
2329  C CG  . MET A 274 ? 0.2157 0.1725 0.2362 -0.0308 0.0127  -0.0069 274 MET A CG  
2330  S SD  . MET A 274 ? 0.3816 0.3245 0.3915 -0.0221 0.0127  -0.0054 274 MET A SD  
2331  C CE  . MET A 274 ? 0.1857 0.1406 0.2033 -0.0160 0.0082  -0.0052 274 MET A CE  
2332  N N   . LEU A 275 ? 0.1388 0.0978 0.1559 -0.0341 0.0033  -0.0113 275 LEU A N   
2333  C CA  . LEU A 275 ? 0.1509 0.1088 0.1654 -0.0280 0.0008  -0.0108 275 LEU A CA  
2334  C C   . LEU A 275 ? 0.1516 0.1211 0.1743 -0.0240 -0.0027 -0.0078 275 LEU A C   
2335  O O   . LEU A 275 ? 0.1861 0.1657 0.2174 -0.0252 -0.0034 -0.0066 275 LEU A O   
2336  C CB  . LEU A 275 ? 0.1379 0.0936 0.1462 -0.0317 -0.0011 -0.0139 275 LEU A CB  
2337  C CG  . LEU A 275 ? 0.2424 0.2092 0.2531 -0.0382 -0.0058 -0.0143 275 LEU A CG  
2338  C CD1 . LEU A 275 ? 0.2095 0.1824 0.2195 -0.0354 -0.0104 -0.0120 275 LEU A CD1 
2339  C CD2 . LEU A 275 ? 0.2686 0.2291 0.2716 -0.0463 -0.0045 -0.0194 275 LEU A CD2 
2340  N N   . ALA A 276 ? 0.1321 0.1001 0.1528 -0.0191 -0.0043 -0.0069 276 ALA A N   
2341  C CA  . ALA A 276 ? 0.1707 0.1453 0.1974 -0.0150 -0.0072 -0.0041 276 ALA A CA  
2342  C C   . ALA A 276 ? 0.1800 0.1546 0.2025 -0.0155 -0.0109 -0.0031 276 ALA A C   
2343  O O   . ALA A 276 ? 0.1678 0.1381 0.1830 -0.0184 -0.0102 -0.0054 276 ALA A O   
2344  C CB  . ALA A 276 ? 0.1379 0.1084 0.1649 -0.0092 -0.0044 -0.0037 276 ALA A CB  
2345  N N   . THR A 277 ? 0.1140 0.0927 0.1407 -0.0127 -0.0143 0.0003  277 THR A N   
2346  C CA  . THR A 277 ? 0.1736 0.1503 0.1945 -0.0136 -0.0174 0.0024  277 THR A CA  
2347  C C   . THR A 277 ? 0.1929 0.1685 0.2181 -0.0083 -0.0194 0.0062  277 THR A C   
2348  O O   . THR A 277 ? 0.1894 0.1662 0.2222 -0.0037 -0.0177 0.0061  277 THR A O   
2349  C CB  . THR A 277 ? 0.1243 0.1061 0.1412 -0.0191 -0.0218 0.0034  277 THR A CB  
2350  O OG1 . THR A 277 ? 0.1545 0.1331 0.1633 -0.0203 -0.0245 0.0064  277 THR A OG1 
2351  C CG2 . THR A 277 ? 0.1245 0.1172 0.1510 -0.0182 -0.0263 0.0060  277 THR A CG2 
2352  N N   . ASP A 278 ? 0.2863 0.2580 0.3053 -0.0093 -0.0223 0.0095  278 ASP A N   
2353  C CA  . ASP A 278 ? 0.2628 0.2288 0.2833 -0.0048 -0.0237 0.0134  278 ASP A CA  
2354  C C   . ASP A 278 ? 0.2064 0.1786 0.2358 0.0001  -0.0286 0.0176  278 ASP A C   
2355  O O   . ASP A 278 ? 0.2267 0.2089 0.2588 -0.0018 -0.0327 0.0188  278 ASP A O   
2356  C CB  . ASP A 278 ? 0.2700 0.2284 0.2793 -0.0088 -0.0249 0.0162  278 ASP A CB  
2357  C CG  . ASP A 278 ? 0.3543 0.3019 0.3625 -0.0063 -0.0232 0.0177  278 ASP A CG  
2358  O OD1 . ASP A 278 ? 0.2995 0.2453 0.3125 -0.0038 -0.0193 0.0137  278 ASP A OD1 
2359  O OD2 . ASP A 278 ? 0.4774 0.4172 0.4784 -0.0076 -0.0257 0.0230  278 ASP A OD2 
2360  N N   . GLU A 279 ? 0.1983 0.1650 0.2330 0.0066  -0.0281 0.0194  279 GLU A N   
2361  C CA  . GLU A 279 ? 0.2142 0.1868 0.2591 0.0133  -0.0327 0.0236  279 GLU A CA  
2362  C C   . GLU A 279 ? 0.2336 0.2012 0.2719 0.0142  -0.0397 0.0313  279 GLU A C   
2363  O O   . GLU A 279 ? 0.2390 0.2142 0.2855 0.0199  -0.0457 0.0358  279 GLU A O   
2364  C CB  . GLU A 279 ? 0.2022 0.1704 0.2560 0.0211  -0.0286 0.0216  279 GLU A CB  
2365  C CG  . GLU A 279 ? 0.2357 0.1858 0.2820 0.0229  -0.0267 0.0226  279 GLU A CG  
2366  C CD  . GLU A 279 ? 0.3819 0.3272 0.4375 0.0319  -0.0240 0.0213  279 GLU A CD  
2367  O OE1 . GLU A 279 ? 0.3380 0.2888 0.4039 0.0395  -0.0279 0.0252  279 GLU A OE1 
2368  O OE2 . GLU A 279 ? 0.3932 0.3300 0.4463 0.0317  -0.0180 0.0160  279 GLU A OE2 
2369  N N   . VAL A 280 ? 0.2627 0.2182 0.2863 0.0089  -0.0391 0.0330  280 VAL A N   
2370  C CA  . VAL A 280 ? 0.2745 0.2254 0.2877 0.0073  -0.0457 0.0408  280 VAL A CA  
2371  C C   . VAL A 280 ? 0.2831 0.2489 0.2951 0.0030  -0.0514 0.0416  280 VAL A C   
2372  O O   . VAL A 280 ? 0.2235 0.1936 0.2343 0.0053  -0.0597 0.0484  280 VAL A O   
2373  C CB  . VAL A 280 ? 0.2570 0.1933 0.2541 0.0003  -0.0421 0.0415  280 VAL A CB  
2374  C CG1 . VAL A 280 ? 0.2415 0.1767 0.2236 -0.0056 -0.0474 0.0476  280 VAL A CG1 
2375  C CG2 . VAL A 280 ? 0.3680 0.2872 0.3643 0.0044  -0.0396 0.0437  280 VAL A CG2 
2376  N N   . ILE A 281 ? 0.2337 0.2070 0.2456 -0.0033 -0.0473 0.0345  281 ILE A N   
2377  C CA  . ILE A 281 ? 0.1652 0.1519 0.1763 -0.0086 -0.0516 0.0333  281 ILE A CA  
2378  C C   . ILE A 281 ? 0.1803 0.1822 0.2078 -0.0030 -0.0570 0.0349  281 ILE A C   
2379  O O   . ILE A 281 ? 0.1886 0.2017 0.2160 -0.0048 -0.0650 0.0381  281 ILE A O   
2380  C CB  . ILE A 281 ? 0.1916 0.1798 0.2004 -0.0152 -0.0449 0.0249  281 ILE A CB  
2381  C CG1 . ILE A 281 ? 0.1722 0.1489 0.1674 -0.0200 -0.0395 0.0228  281 ILE A CG1 
2382  C CG2 . ILE A 281 ? 0.2021 0.2019 0.2095 -0.0217 -0.0486 0.0225  281 ILE A CG2 
2383  C CD1 . ILE A 281 ? 0.2641 0.2347 0.2447 -0.0236 -0.0433 0.0286  281 ILE A CD1 
2384  N N   . LEU A 282 ? 0.2127 0.2165 0.2546 0.0036  -0.0526 0.0324  282 LEU A N   
2385  C CA  . LEU A 282 ? 0.1512 0.1714 0.2113 0.0094  -0.0562 0.0331  282 LEU A CA  
2386  C C   . LEU A 282 ? 0.1656 0.1881 0.2293 0.0173  -0.0654 0.0416  282 LEU A C   
2387  O O   . LEU A 282 ? 0.2244 0.2648 0.2983 0.0189  -0.0729 0.0439  282 LEU A O   
2388  C CB  . LEU A 282 ? 0.1526 0.1722 0.2249 0.0149  -0.0482 0.0284  282 LEU A CB  
2389  C CG  . LEU A 282 ? 0.1394 0.1758 0.2326 0.0220  -0.0492 0.0281  282 LEU A CG  
2390  C CD1 . LEU A 282 ? 0.1343 0.1907 0.2353 0.0149  -0.0513 0.0251  282 LEU A CD1 
2391  C CD2 . LEU A 282 ? 0.1334 0.1647 0.2335 0.0267  -0.0398 0.0231  282 LEU A CD2 
2392  N N   . LYS A 283 ? 0.1750 0.1794 0.2304 0.0222  -0.0652 0.0465  283 LYS A N   
2393  C CA  . LYS A 283 ? 0.2122 0.2144 0.2687 0.0307  -0.0741 0.0559  283 LYS A CA  
2394  C C   . LYS A 283 ? 0.2038 0.2120 0.2480 0.0249  -0.0840 0.0619  283 LYS A C   
2395  O O   . LYS A 283 ? 0.2143 0.2337 0.2652 0.0310  -0.0942 0.0685  283 LYS A O   
2396  C CB  . LYS A 283 ? 0.3284 0.3055 0.3754 0.0352  -0.0707 0.0597  283 LYS A CB  
2397  C CG  . LYS A 283 ? 0.2839 0.2530 0.3403 0.0402  -0.0610 0.0533  283 LYS A CG  
2398  C CD  . LYS A 283 ? 0.2959 0.2841 0.3744 0.0464  -0.0590 0.0481  283 LYS A CD  
2399  C CE  . LYS A 283 ? 0.3069 0.2852 0.3949 0.0563  -0.0528 0.0454  283 LYS A CE  
2400  N NZ  . LYS A 283 ? 0.1779 0.1520 0.2642 0.0515  -0.0422 0.0362  283 LYS A NZ  
2401  N N   . ASN A 284 ? 0.2038 0.2054 0.2296 0.0134  -0.0813 0.0595  284 ASN A N   
2402  C CA  . ASN A 284 ? 0.2167 0.2234 0.2277 0.0062  -0.0896 0.0638  284 ASN A CA  
2403  C C   . ASN A 284 ? 0.2141 0.2453 0.2356 0.0025  -0.0953 0.0600  284 ASN A C   
2404  O O   . ASN A 284 ? 0.2708 0.3119 0.2864 0.0005  -0.1060 0.0652  284 ASN A O   
2405  C CB  . ASN A 284 ? 0.2201 0.2142 0.2100 -0.0053 -0.0831 0.0601  284 ASN A CB  
2406  C CG  . ASN A 284 ? 0.3213 0.2930 0.2973 -0.0044 -0.0797 0.0655  284 ASN A CG  
2407  O OD1 . ASN A 284 ? 0.3900 0.3522 0.3708 0.0048  -0.0818 0.0718  284 ASN A OD1 
2408  N ND2 . ASN A 284 ? 0.2612 0.2241 0.2203 -0.0142 -0.0737 0.0624  284 ASN A ND2 
2409  N N   . SER A 285 ? 0.2327 0.2737 0.2686 0.0008  -0.0886 0.0512  285 SER A N   
2410  C CA  . SER A 285 ? 0.1872 0.2492 0.2312 -0.0062 -0.0917 0.0459  285 SER A CA  
2411  C C   . SER A 285 ? 0.2136 0.2978 0.2817 0.0017  -0.0981 0.0478  285 SER A C   
2412  O O   . SER A 285 ? 0.3797 0.4822 0.4512 -0.0005 -0.1086 0.0503  285 SER A O   
2413  C CB  . SER A 285 ? 0.1886 0.2476 0.2334 -0.0135 -0.0805 0.0357  285 SER A CB  
2414  O OG  . SER A 285 ? 0.2178 0.2585 0.2432 -0.0194 -0.0744 0.0334  285 SER A OG  
2415  N N   . VAL A 286 ? 0.2120 0.2963 0.2972 0.0108  -0.0918 0.0462  286 VAL A N   
2416  C CA  . VAL A 286 ? 0.1973 0.3044 0.3083 0.0186  -0.0954 0.0463  286 VAL A CA  
2417  C C   . VAL A 286 ? 0.2907 0.3922 0.4086 0.0340  -0.1003 0.0547  286 VAL A C   
2418  O O   . VAL A 286 ? 0.3718 0.4490 0.4756 0.0379  -0.0979 0.0589  286 VAL A O   
2419  C CB  . VAL A 286 ? 0.1556 0.2685 0.2813 0.0171  -0.0837 0.0374  286 VAL A CB  
2420  C CG1 . VAL A 286 ? 0.2407 0.3836 0.3928 0.0198  -0.0869 0.0353  286 VAL A CG1 
2421  C CG2 . VAL A 286 ? 0.1845 0.2899 0.2964 0.0031  -0.0766 0.0302  286 VAL A CG2 
2422  N N   . GLU A 287 ? 0.3474 0.4718 0.4882 0.0429  -0.1071 0.0570  287 GLU A N   
2423  C CA  . GLU A 287 ? 0.4434 0.5652 0.5895 0.0580  -0.1158 0.0667  287 GLU A CA  
2424  C C   . GLU A 287 ? 0.5497 0.6535 0.7023 0.0703  -0.1066 0.0661  287 GLU A C   
2425  O O   . GLU A 287 ? 0.7975 0.8742 0.9334 0.0743  -0.1055 0.0714  287 GLU A O   
2426  C CB  . GLU A 287 ? 0.4705 0.6225 0.6341 0.0629  -0.1227 0.0657  287 GLU A CB  
2427  C CG  . GLU A 287 ? 0.6202 0.7694 0.7855 0.0791  -0.1283 0.0725  287 GLU A CG  
2428  C CD  . GLU A 287 ? 0.7164 0.8938 0.9096 0.0892  -0.1281 0.0678  287 GLU A CD  
2429  O OE1 . GLU A 287 ? 0.6788 0.8703 0.8902 0.0858  -0.1193 0.0592  287 GLU A OE1 
2430  O OE2 . GLU A 287 ? 0.5889 0.7748 0.7855 0.1005  -0.1366 0.0726  287 GLU A OE2 
2431  N N   . ARG A 288 ? 0.3863 0.5042 0.5615 0.0754  -0.0987 0.0589  288 ARG A N   
2432  C CA  . ARG A 288 ? 0.3634 0.4652 0.5437 0.0859  -0.0884 0.0559  288 ARG A CA  
2433  C C   . ARG A 288 ? 0.3393 0.4459 0.5272 0.0786  -0.0760 0.0456  288 ARG A C   
2434  O O   . ARG A 288 ? 0.3451 0.4731 0.5552 0.0816  -0.0714 0.0399  288 ARG A O   
2435  C CB  . ARG A 288 ? 0.5028 0.6158 0.6981 0.1011  -0.0892 0.0566  288 ARG A CB  
2436  C CG  . ARG A 288 ? 0.4910 0.5922 0.6735 0.1101  -0.0987 0.0665  288 ARG A CG  
2437  C CD  . ARG A 288 ? 0.5321 0.6623 0.7306 0.1184  -0.1074 0.0681  288 ARG A CD  
2438  N NE  . ARG A 288 ? 0.7000 0.8186 0.8946 0.1342  -0.1116 0.0753  288 ARG A NE  
2439  C CZ  . ARG A 288 ? 0.6950 0.7994 0.8702 0.1360  -0.1210 0.0853  288 ARG A CZ  
2440  N NH1 . ARG A 288 ? 0.6641 0.7646 0.8214 0.1226  -0.1273 0.0891  288 ARG A NH1 
2441  N NH2 . ARG A 288 ? 0.6839 0.7772 0.8567 0.1515  -0.1238 0.0919  288 ARG A NH2 
2442  N N   . ALA A 289 ? 0.2872 0.3731 0.4537 0.0684  -0.0693 0.0426  289 ALA A N   
2443  C CA  . ALA A 289 ? 0.1892 0.2769 0.3547 0.0591  -0.0581 0.0335  289 ALA A CA  
2444  C C   . ALA A 289 ? 0.2085 0.2746 0.3676 0.0628  -0.0474 0.0294  289 ALA A C   
2445  O O   . ALA A 289 ? 0.2902 0.3359 0.4410 0.0694  -0.0483 0.0332  289 ALA A O   
2446  C CB  . ALA A 289 ? 0.1593 0.2428 0.3063 0.0442  -0.0590 0.0323  289 ALA A CB  
2447  N N   . SER A 290 ? 0.1523 0.2226 0.3143 0.0575  -0.0374 0.0216  290 SER A N   
2448  C CA  . SER A 290 ? 0.1400 0.1923 0.2938 0.0585  -0.0272 0.0166  290 SER A CA  
2449  C C   . SER A 290 ? 0.1549 0.1997 0.2923 0.0460  -0.0226 0.0131  290 SER A C   
2450  O O   . SER A 290 ? 0.1745 0.2332 0.3152 0.0381  -0.0217 0.0107  290 SER A O   
2451  C CB  . SER A 290 ? 0.1871 0.2508 0.3586 0.0652  -0.0187 0.0105  290 SER A CB  
2452  O OG  . SER A 290 ? 0.1857 0.2334 0.3465 0.0636  -0.0087 0.0048  290 SER A OG  
2453  N N   . PRO A 291 ? 0.1323 0.1558 0.2528 0.0439  -0.0198 0.0124  291 PRO A N   
2454  C CA  . PRO A 291 ? 0.1246 0.1420 0.2310 0.0337  -0.0161 0.0093  291 PRO A CA  
2455  C C   . PRO A 291 ? 0.1619 0.1827 0.2705 0.0316  -0.0069 0.0032  291 PRO A C   
2456  O O   . PRO A 291 ? 0.1356 0.1503 0.2326 0.0246  -0.0039 0.0012  291 PRO A O   
2457  C CB  . PRO A 291 ? 0.2434 0.2399 0.3343 0.0334  -0.0163 0.0105  291 PRO A CB  
2458  C CG  . PRO A 291 ? 0.3552 0.3435 0.4513 0.0432  -0.0175 0.0128  291 PRO A CG  
2459  C CD  . PRO A 291 ? 0.1634 0.1682 0.2788 0.0510  -0.0185 0.0132  291 PRO A CD  
2460  N N   . TYR A 292 ? 0.2515 0.2815 0.3739 0.0378  -0.0022 0.0004  292 TYR A N   
2461  C CA  . TYR A 292 ? 0.2147 0.2468 0.3373 0.0358  0.0075  -0.0054 292 TYR A CA  
2462  C C   . TYR A 292 ? 0.1551 0.2062 0.2877 0.0298  0.0102  -0.0069 292 TYR A C   
2463  O O   . TYR A 292 ? 0.1185 0.1775 0.2578 0.0301  0.0186  -0.0112 292 TYR A O   
2464  C CB  . TYR A 292 ? 0.1894 0.2187 0.3193 0.0454  0.0130  -0.0090 292 TYR A CB  
2465  C CG  . TYR A 292 ? 0.2054 0.2148 0.3261 0.0504  0.0099  -0.0074 292 TYR A CG  
2466  C CD1 . TYR A 292 ? 0.2654 0.2587 0.3676 0.0444  0.0089  -0.0072 292 TYR A CD1 
2467  C CD2 . TYR A 292 ? 0.2001 0.2066 0.3308 0.0610  0.0081  -0.0062 292 TYR A CD2 
2468  C CE1 . TYR A 292 ? 0.3227 0.2985 0.4167 0.0470  0.0067  -0.0061 292 TYR A CE1 
2469  C CE2 . TYR A 292 ? 0.1899 0.1754 0.3107 0.0643  0.0059  -0.0046 292 TYR A CE2 
2470  C CZ  . TYR A 292 ? 0.2815 0.2521 0.3838 0.0564  0.0054  -0.0048 292 TYR A CZ  
2471  O OH  . TYR A 292 ? 0.3399 0.2904 0.4326 0.0578  0.0039  -0.0036 292 TYR A OH  
2472  N N   . LEU A 293 ? 0.1574 0.2154 0.2900 0.0233  0.0040  -0.0039 293 LEU A N   
2473  C CA  . LEU A 293 ? 0.1164 0.1920 0.2584 0.0158  0.0057  -0.0054 293 LEU A CA  
2474  C C   . LEU A 293 ? 0.1083 0.1746 0.2347 0.0049  0.0051  -0.0049 293 LEU A C   
2475  O O   . LEU A 293 ? 0.1635 0.2151 0.2759 0.0042  0.0008  -0.0027 293 LEU A O   
2476  C CB  . LEU A 293 ? 0.1192 0.2158 0.2793 0.0181  -0.0022 -0.0029 293 LEU A CB  
2477  C CG  . LEU A 293 ? 0.1114 0.2289 0.2955 0.0264  -0.0001 -0.0048 293 LEU A CG  
2478  C CD1 . LEU A 293 ? 0.2171 0.3251 0.4038 0.0402  -0.0026 -0.0026 293 LEU A CD1 
2479  C CD2 . LEU A 293 ? 0.1102 0.2534 0.3117 0.0235  -0.0076 -0.0033 293 LEU A CD2 
2480  N N   . ARG A 294 ? 0.1093 0.1838 0.2384 -0.0037 0.0102  -0.0074 294 ARG A N   
2481  C CA  . ARG A 294 ? 0.1108 0.1786 0.2286 -0.0143 0.0091  -0.0072 294 ARG A CA  
2482  C C   . ARG A 294 ? 0.1102 0.1935 0.2377 -0.0186 0.0010  -0.0064 294 ARG A C   
2483  O O   . ARG A 294 ? 0.1095 0.2148 0.2559 -0.0180 -0.0001 -0.0072 294 ARG A O   
2484  C CB  . ARG A 294 ? 0.1163 0.1827 0.2305 -0.0226 0.0186  -0.0098 294 ARG A CB  
2485  C CG  . ARG A 294 ? 0.1216 0.1737 0.2206 -0.0322 0.0189  -0.0096 294 ARG A CG  
2486  C CD  . ARG A 294 ? 0.2145 0.2713 0.3156 -0.0429 0.0265  -0.0117 294 ARG A CD  
2487  N NE  . ARG A 294 ? 0.2938 0.3353 0.3814 -0.0435 0.0352  -0.0111 294 ARG A NE  
2488  C CZ  . ARG A 294 ? 0.3185 0.3668 0.4108 -0.0411 0.0426  -0.0123 294 ARG A CZ  
2489  N NH1 . ARG A 294 ? 0.2443 0.3144 0.3565 -0.0368 0.0431  -0.0146 294 ARG A NH1 
2490  N NH2 . ARG A 294 ? 0.4511 0.4837 0.5274 -0.0426 0.0497  -0.0112 294 ARG A NH2 
2491  N N   . TYR A 295 ? 0.1113 0.1849 0.2266 -0.0228 -0.0047 -0.0051 295 TYR A N   
2492  C CA  . TYR A 295 ? 0.1130 0.2000 0.2339 -0.0274 -0.0133 -0.0044 295 TYR A CA  
2493  C C   . TYR A 295 ? 0.1189 0.2016 0.2310 -0.0406 -0.0118 -0.0077 295 TYR A C   
2494  O O   . TYR A 295 ? 0.1219 0.1842 0.2176 -0.0435 -0.0077 -0.0086 295 TYR A O   
2495  C CB  . TYR A 295 ? 0.1132 0.1933 0.2262 -0.0217 -0.0219 -0.0004 295 TYR A CB  
2496  C CG  . TYR A 295 ? 0.1117 0.1996 0.2366 -0.0098 -0.0259 0.0034  295 TYR A CG  
2497  C CD1 . TYR A 295 ? 0.1138 0.2232 0.2548 -0.0070 -0.0335 0.0055  295 TYR A CD1 
2498  C CD2 . TYR A 295 ? 0.1103 0.1838 0.2305 -0.0011 -0.0222 0.0046  295 TYR A CD2 
2499  C CE1 . TYR A 295 ? 0.1154 0.2297 0.2674 0.0054  -0.0372 0.0094  295 TYR A CE1 
2500  C CE2 . TYR A 295 ? 0.1123 0.1894 0.2423 0.0099  -0.0251 0.0076  295 TYR A CE2 
2501  C CZ  . TYR A 295 ? 0.1152 0.2118 0.2611 0.0138  -0.0325 0.0103  295 TYR A CZ  
2502  O OH  . TYR A 295 ? 0.1819 0.2799 0.3377 0.0262  -0.0354 0.0137  295 TYR A OH  
2503  N N   . TYR A 296 ? 0.1219 0.2242 0.2458 -0.0484 -0.0151 -0.0097 296 TYR A N   
2504  C CA  . TYR A 296 ? 0.1304 0.2297 0.2465 -0.0622 -0.0148 -0.0136 296 TYR A CA  
2505  C C   . TYR A 296 ? 0.1338 0.2372 0.2446 -0.0643 -0.0256 -0.0129 296 TYR A C   
2506  O O   . TYR A 296 ? 0.1335 0.2594 0.2577 -0.0635 -0.0339 -0.0116 296 TYR A O   
2507  C CB  . TYR A 296 ? 0.1340 0.2532 0.2657 -0.0720 -0.0112 -0.0172 296 TYR A CB  
2508  C CG  . TYR A 296 ? 0.1372 0.2466 0.2666 -0.0757 0.0011  -0.0188 296 TYR A CG  
2509  C CD1 . TYR A 296 ? 0.1467 0.2283 0.2573 -0.0727 0.0072  -0.0174 296 TYR A CD1 
2510  C CD2 . TYR A 296 ? 0.1395 0.2685 0.2853 -0.0826 0.0067  -0.0216 296 TYR A CD2 
2511  C CE1 . TYR A 296 ? 0.1457 0.2172 0.2515 -0.0761 0.0177  -0.0178 296 TYR A CE1 
2512  C CE2 . TYR A 296 ? 0.1454 0.2644 0.2866 -0.0870 0.0186  -0.0225 296 TYR A CE2 
2513  C CZ  . TYR A 296 ? 0.1492 0.2385 0.2692 -0.0836 0.0237  -0.0202 296 TYR A CZ  
2514  O OH  . TYR A 296 ? 0.2240 0.3024 0.3370 -0.0880 0.0348  -0.0200 296 TYR A OH  
2515  N N   . PHE A 297 ? 0.1387 0.2212 0.2298 -0.0667 -0.0255 -0.0137 297 PHE A N   
2516  C CA  . PHE A 297 ? 0.1450 0.2298 0.2276 -0.0705 -0.0343 -0.0139 297 PHE A CA  
2517  C C   . PHE A 297 ? 0.1665 0.2586 0.2485 -0.0855 -0.0353 -0.0199 297 PHE A C   
2518  O O   . PHE A 297 ? 0.1643 0.2387 0.2340 -0.0936 -0.0288 -0.0246 297 PHE A O   
2519  C CB  . PHE A 297 ? 0.1471 0.2085 0.2099 -0.0676 -0.0327 -0.0136 297 PHE A CB  
2520  C CG  . PHE A 297 ? 0.1559 0.2185 0.2073 -0.0721 -0.0404 -0.0141 297 PHE A CG  
2521  C CD1 . PHE A 297 ? 0.1549 0.2266 0.2075 -0.0656 -0.0491 -0.0083 297 PHE A CD1 
2522  C CD2 . PHE A 297 ? 0.1680 0.2214 0.2061 -0.0833 -0.0387 -0.0204 297 PHE A CD2 
2523  C CE1 . PHE A 297 ? 0.1925 0.2650 0.2320 -0.0705 -0.0562 -0.0082 297 PHE A CE1 
2524  C CE2 . PHE A 297 ? 0.1782 0.2330 0.2040 -0.0883 -0.0453 -0.0217 297 PHE A CE2 
2525  C CZ  . PHE A 297 ? 0.1839 0.2489 0.2098 -0.0821 -0.0542 -0.0153 297 PHE A CZ  
2526  N N   . ARG A 298 ? 0.1683 0.2866 0.2641 -0.0892 -0.0438 -0.0198 298 ARG A N   
2527  C CA  . ARG A 298 ? 0.1692 0.2990 0.2657 -0.1048 -0.0468 -0.0259 298 ARG A CA  
2528  C C   . ARG A 298 ? 0.1743 0.2974 0.2730 -0.1156 -0.0361 -0.0315 298 ARG A C   
2529  O O   . ARG A 298 ? 0.3107 0.4261 0.4004 -0.1253 -0.0345 -0.0366 298 ARG A O   
2530  C CB  . ARG A 298 ? 0.1817 0.2982 0.2564 -0.1116 -0.0511 -0.0290 298 ARG A CB  
2531  C CG  . ARG A 298 ? 0.1806 0.3003 0.2487 -0.1026 -0.0609 -0.0230 298 ARG A CG  
2532  C CD  . ARG A 298 ? 0.2228 0.3480 0.2787 -0.1115 -0.0693 -0.0261 298 ARG A CD  
2533  N NE  . ARG A 298 ? 0.2290 0.3289 0.2606 -0.1162 -0.0642 -0.0307 298 ARG A NE  
2534  C CZ  . ARG A 298 ? 0.2960 0.3887 0.3113 -0.1137 -0.0686 -0.0283 298 ARG A CZ  
2535  N NH1 . ARG A 298 ? 0.2184 0.3242 0.2369 -0.1064 -0.0787 -0.0200 298 ARG A NH1 
2536  N NH2 . ARG A 298 ? 0.2548 0.3258 0.2500 -0.1179 -0.0620 -0.0339 298 ARG A NH2 
2537  N N   . GLU A 299 ? 0.1661 0.2854 0.2727 -0.1093 -0.0274 -0.0292 299 GLU A N   
2538  C CA  . GLU A 299 ? 0.2886 0.3990 0.3951 -0.1189 -0.0163 -0.0330 299 GLU A CA  
2539  C C   . GLU A 299 ? 0.2552 0.3323 0.3379 -0.1244 -0.0103 -0.0360 299 GLU A C   
2540  O O   . GLU A 299 ? 0.2740 0.3398 0.3511 -0.1322 -0.0039 -0.0388 299 GLU A O   
2541  C CB  . GLU A 299 ? 0.3273 0.4590 0.4483 -0.1270 -0.0173 -0.0357 299 GLU A CB  
2542  C CG  . GLU A 299 ? 0.3529 0.5193 0.4996 -0.1200 -0.0240 -0.0330 299 GLU A CG  
2543  C CD  . GLU A 299 ? 0.4096 0.5972 0.5716 -0.1275 -0.0248 -0.0358 299 GLU A CD  
2544  O OE1 . GLU A 299 ? 0.4380 0.6140 0.5893 -0.1392 -0.0215 -0.0401 299 GLU A OE1 
2545  O OE2 . GLU A 299 ? 0.4360 0.6517 0.6211 -0.1212 -0.0285 -0.0340 299 GLU A OE2 
2546  N N   . LEU A 300 ? 0.1942 0.2539 0.2622 -0.1174 -0.0123 -0.0346 300 LEU A N   
2547  C CA  . LEU A 300 ? 0.1968 0.2251 0.2442 -0.1196 -0.0061 -0.0374 300 LEU A CA  
2548  C C   . LEU A 300 ? 0.2295 0.2392 0.2707 -0.1068 -0.0002 -0.0326 300 LEU A C   
2549  O O   . LEU A 300 ? 0.2489 0.2375 0.2812 -0.1086 0.0080  -0.0331 300 LEU A O   
2550  C CB  . LEU A 300 ? 0.2032 0.2258 0.2373 -0.1203 -0.0122 -0.0403 300 LEU A CB  
2551  C CG  . LEU A 300 ? 0.2116 0.2521 0.2480 -0.1270 -0.0205 -0.0432 300 LEU A CG  
2552  C CD1 . LEU A 300 ? 0.2181 0.2503 0.2382 -0.1260 -0.0250 -0.0452 300 LEU A CD1 
2553  C CD2 . LEU A 300 ? 0.2810 0.3174 0.3161 -0.1370 -0.0159 -0.0478 300 LEU A CD2 
2554  N N   . ILE A 301 ? 0.2212 0.2378 0.2664 -0.0941 -0.0046 -0.0277 301 ILE A N   
2555  C CA  . ILE A 301 ? 0.1686 0.1694 0.2072 -0.0823 -0.0007 -0.0239 301 ILE A CA  
2556  C C   . ILE A 301 ? 0.1542 0.1702 0.2064 -0.0729 -0.0020 -0.0191 301 ILE A C   
2557  O O   . ILE A 301 ? 0.1486 0.1866 0.2148 -0.0730 -0.0073 -0.0182 301 ILE A O   
2558  C CB  . ILE A 301 ? 0.1686 0.1579 0.1949 -0.0770 -0.0038 -0.0244 301 ILE A CB  
2559  C CG1 . ILE A 301 ? 0.2299 0.1990 0.2471 -0.0685 0.0017  -0.0227 301 ILE A CG1 
2560  C CG2 . ILE A 301 ? 0.1577 0.1630 0.1903 -0.0706 -0.0118 -0.0208 301 ILE A CG2 
2561  C CD1 . ILE A 301 ? 0.3294 0.2835 0.3335 -0.0676 0.0021  -0.0261 301 ILE A CD1 
2562  N N   . SER A 302 ? 0.1500 0.1539 0.1979 -0.0643 0.0026  -0.0162 302 SER A N   
2563  C CA  . SER A 302 ? 0.1388 0.1525 0.1964 -0.0549 0.0025  -0.0126 302 SER A CA  
2564  C C   . SER A 302 ? 0.1319 0.1391 0.1838 -0.0452 -0.0015 -0.0102 302 SER A C   
2565  O O   . SER A 302 ? 0.1862 0.1768 0.2257 -0.0434 0.0002  -0.0107 302 SER A O   
2566  C CB  . SER A 302 ? 0.1417 0.1476 0.1975 -0.0538 0.0109  -0.0117 302 SER A CB  
2567  O OG  . SER A 302 ? 0.1654 0.1835 0.2310 -0.0621 0.0149  -0.0133 302 SER A OG  
2568  N N   . VAL A 303 ? 0.1243 0.1444 0.1857 -0.0390 -0.0065 -0.0077 303 VAL A N   
2569  C CA  . VAL A 303 ? 0.1198 0.1340 0.1762 -0.0313 -0.0101 -0.0052 303 VAL A CA  
2570  C C   . VAL A 303 ? 0.1139 0.1312 0.1779 -0.0225 -0.0084 -0.0030 303 VAL A C   
2571  O O   . VAL A 303 ? 0.1134 0.1441 0.1905 -0.0211 -0.0077 -0.0028 303 VAL A O   
2572  C CB  . VAL A 303 ? 0.1215 0.1436 0.1779 -0.0325 -0.0183 -0.0037 303 VAL A CB  
2573  C CG1 . VAL A 303 ? 0.1207 0.1321 0.1671 -0.0276 -0.0202 -0.0016 303 VAL A CG1 
2574  C CG2 . VAL A 303 ? 0.1295 0.1531 0.1806 -0.0430 -0.0200 -0.0072 303 VAL A CG2 
2575  N N   . PHE A 304 ? 0.1118 0.1172 0.1681 -0.0168 -0.0073 -0.0021 304 PHE A N   
2576  C CA  . PHE A 304 ? 0.1227 0.1280 0.1835 -0.0089 -0.0062 -0.0008 304 PHE A CA  
2577  C C   . PHE A 304 ? 0.1306 0.1304 0.1868 -0.0051 -0.0109 0.0016  304 PHE A C   
2578  O O   . PHE A 304 ? 0.1416 0.1346 0.1882 -0.0081 -0.0126 0.0014  304 PHE A O   
2579  C CB  . PHE A 304 ? 0.1870 0.1827 0.2416 -0.0071 0.0001  -0.0024 304 PHE A CB  
2580  C CG  . PHE A 304 ? 0.1122 0.1118 0.1698 -0.0106 0.0060  -0.0039 304 PHE A CG  
2581  C CD1 . PHE A 304 ? 0.1120 0.1213 0.1800 -0.0078 0.0095  -0.0047 304 PHE A CD1 
2582  C CD2 . PHE A 304 ? 0.1175 0.1100 0.1672 -0.0170 0.0087  -0.0046 304 PHE A CD2 
2583  C CE1 . PHE A 304 ? 0.1185 0.1321 0.1887 -0.0123 0.0161  -0.0061 304 PHE A CE1 
2584  C CE2 . PHE A 304 ? 0.1450 0.1391 0.1957 -0.0216 0.0148  -0.0054 304 PHE A CE2 
2585  C CZ  . PHE A 304 ? 0.1223 0.1278 0.1832 -0.0198 0.0187  -0.0061 304 PHE A CZ  
2586  N N   . PHE A 305 ? 0.1090 0.1110 0.1719 0.0014  -0.0124 0.0035  305 PHE A N   
2587  C CA  . PHE A 305 ? 0.1122 0.1068 0.1702 0.0044  -0.0163 0.0064  305 PHE A CA  
2588  C C   . PHE A 305 ? 0.1372 0.1220 0.1929 0.0092  -0.0123 0.0049  305 PHE A C   
2589  O O   . PHE A 305 ? 0.1854 0.1726 0.2487 0.0140  -0.0093 0.0036  305 PHE A O   
2590  C CB  . PHE A 305 ? 0.1169 0.1196 0.1830 0.0080  -0.0227 0.0108  305 PHE A CB  
2591  C CG  . PHE A 305 ? 0.1178 0.1322 0.1857 0.0024  -0.0278 0.0119  305 PHE A CG  
2592  C CD1 . PHE A 305 ? 0.1227 0.1334 0.1794 -0.0024 -0.0324 0.0140  305 PHE A CD1 
2593  C CD2 . PHE A 305 ? 0.1154 0.1450 0.1956 0.0009  -0.0275 0.0102  305 PHE A CD2 
2594  C CE1 . PHE A 305 ? 0.1258 0.1469 0.1823 -0.0085 -0.0373 0.0141  305 PHE A CE1 
2595  C CE2 . PHE A 305 ? 0.1177 0.1587 0.1993 -0.0056 -0.0326 0.0103  305 PHE A CE2 
2596  C CZ  . PHE A 305 ? 0.1233 0.1595 0.1923 -0.0103 -0.0378 0.0121  305 PHE A CZ  
2597  N N   . ARG A 306 ? 0.1134 0.0882 0.1589 0.0072  -0.0119 0.0042  306 ARG A N   
2598  C CA  . ARG A 306 ? 0.1151 0.0813 0.1573 0.0099  -0.0086 0.0018  306 ARG A CA  
2599  C C   . ARG A 306 ? 0.2130 0.1738 0.2587 0.0149  -0.0099 0.0038  306 ARG A C   
2600  O O   . ARG A 306 ? 0.2483 0.2090 0.2953 0.0159  -0.0145 0.0084  306 ARG A O   
2601  C CB  . ARG A 306 ? 0.1220 0.0819 0.1546 0.0060  -0.0083 0.0004  306 ARG A CB  
2602  C CG  . ARG A 306 ? 0.2244 0.1799 0.2524 0.0035  -0.0115 0.0033  306 ARG A CG  
2603  C CD  . ARG A 306 ? 0.1657 0.1173 0.1867 -0.0003 -0.0099 0.0006  306 ARG A CD  
2604  N NE  . ARG A 306 ? 0.2277 0.1754 0.2433 -0.0042 -0.0116 0.0033  306 ARG A NE  
2605  C CZ  . ARG A 306 ? 0.2631 0.2030 0.2751 -0.0060 -0.0108 0.0035  306 ARG A CZ  
2606  N NH1 . ARG A 306 ? 0.3915 0.3270 0.4051 -0.0043 -0.0087 0.0003  306 ARG A NH1 
2607  N NH2 . ARG A 306 ? 0.3083 0.2441 0.3138 -0.0105 -0.0118 0.0067  306 ARG A NH2 
2608  N N   . ASP A 307 ? 0.2530 0.2081 0.2990 0.0181  -0.0059 0.0004  307 ASP A N   
2609  C CA  . ASP A 307 ? 0.2709 0.2166 0.3187 0.0230  -0.0058 0.0011  307 ASP A CA  
2610  C C   . ASP A 307 ? 0.3316 0.2655 0.3694 0.0186  -0.0072 0.0020  307 ASP A C   
2611  O O   . ASP A 307 ? 0.3374 0.2663 0.3691 0.0155  -0.0045 -0.0024 307 ASP A O   
2612  C CB  . ASP A 307 ? 0.2841 0.2273 0.3345 0.0270  0.0000  -0.0043 307 ASP A CB  
2613  C CG  . ASP A 307 ? 0.4344 0.3668 0.4882 0.0334  0.0008  -0.0044 307 ASP A CG  
2614  O OD1 . ASP A 307 ? 0.3842 0.3025 0.4301 0.0313  0.0003  -0.0044 307 ASP A OD1 
2615  O OD2 . ASP A 307 ? 0.3373 0.2753 0.4022 0.0404  0.0025  -0.0047 307 ASP A OD2 
2616  N N   . LYS A 308 ? 0.3657 0.2960 0.4012 0.0179  -0.0117 0.0077  308 LYS A N   
2617  C CA  . LYS A 308 ? 0.3078 0.2295 0.3330 0.0114  -0.0124 0.0089  308 LYS A CA  
2618  C C   . LYS A 308 ? 0.3561 0.2639 0.3770 0.0105  -0.0091 0.0057  308 LYS A C   
2619  O O   . LYS A 308 ? 0.3922 0.2984 0.4073 0.0040  -0.0072 0.0022  308 LYS A O   
2620  C CB  . LYS A 308 ? 0.3429 0.2616 0.3643 0.0107  -0.0175 0.0164  308 LYS A CB  
2621  C CG  . LYS A 308 ? 0.4049 0.3143 0.4146 0.0030  -0.0170 0.0180  308 LYS A CG  
2622  C CD  . LYS A 308 ? 0.4081 0.3029 0.4120 0.0045  -0.0201 0.0254  308 LYS A CD  
2623  C CE  . LYS A 308 ? 0.5715 0.4612 0.5623 -0.0046 -0.0203 0.0289  308 LYS A CE  
2624  N NZ  . LYS A 308 ? 0.5175 0.4107 0.5059 -0.0126 -0.0149 0.0219  308 LYS A NZ  
2625  N N   . THR A 309 ? 0.3331 0.2311 0.3575 0.0168  -0.0083 0.0062  309 THR A N   
2626  C CA  . THR A 309 ? 0.3026 0.1841 0.3215 0.0152  -0.0049 0.0026  309 THR A CA  
2627  C C   . THR A 309 ? 0.3398 0.2252 0.3574 0.0121  -0.0007 -0.0060 309 THR A C   
2628  O O   . THR A 309 ? 0.3715 0.2500 0.3824 0.0055  0.0010  -0.0099 309 THR A O   
2629  C CB  . THR A 309 ? 0.2179 0.0865 0.2412 0.0241  -0.0044 0.0045  309 THR A CB  
2630  O OG1 . THR A 309 ? 0.4700 0.3436 0.5006 0.0298  -0.0001 -0.0020 309 THR A OG1 
2631  C CG2 . THR A 309 ? 0.2060 0.0787 0.2346 0.0303  -0.0101 0.0133  309 THR A CG2 
2632  N N   . LEU A 310 ? 0.2702 0.1673 0.2937 0.0163  0.0009  -0.0090 310 LEU A N   
2633  C CA  . LEU A 310 ? 0.2738 0.1745 0.2938 0.0136  0.0042  -0.0163 310 LEU A CA  
2634  C C   . LEU A 310 ? 0.2497 0.1584 0.2648 0.0065  0.0022  -0.0171 310 LEU A C   
2635  O O   . LEU A 310 ? 0.3516 0.2587 0.3615 0.0017  0.0030  -0.0222 310 LEU A O   
2636  C CB  . LEU A 310 ? 0.2572 0.1678 0.2827 0.0189  0.0067  -0.0181 310 LEU A CB  
2637  C CG  . LEU A 310 ? 0.2358 0.1400 0.2660 0.0258  0.0111  -0.0212 310 LEU A CG  
2638  C CD1 . LEU A 310 ? 0.2923 0.2084 0.3270 0.0289  0.0150  -0.0238 310 LEU A CD1 
2639  C CD2 . LEU A 310 ? 0.1899 0.0792 0.2120 0.0234  0.0143  -0.0278 310 LEU A CD2 
2640  N N   . SER A 311 ? 0.2168 0.1350 0.2342 0.0058  -0.0006 -0.0126 311 SER A N   
2641  C CA  . SER A 311 ? 0.2299 0.1559 0.2443 0.0005  -0.0019 -0.0137 311 SER A CA  
2642  C C   . SER A 311 ? 0.2501 0.1704 0.2606 -0.0061 -0.0022 -0.0141 311 SER A C   
2643  O O   . SER A 311 ? 0.2619 0.1879 0.2708 -0.0107 -0.0022 -0.0180 311 SER A O   
2644  C CB  . SER A 311 ? 0.2304 0.1652 0.2474 0.0012  -0.0038 -0.0097 311 SER A CB  
2645  O OG  . SER A 311 ? 0.2724 0.2122 0.2933 0.0056  -0.0030 -0.0094 311 SER A OG  
2646  N N   . ASP A 312 ? 0.3448 0.2545 0.3536 -0.0067 -0.0026 -0.0099 312 ASP A N   
2647  C CA  . ASP A 312 ? 0.2768 0.1788 0.2803 -0.0143 -0.0018 -0.0098 312 ASP A CA  
2648  C C   . ASP A 312 ? 0.2367 0.1310 0.2375 -0.0180 0.0006  -0.0161 312 ASP A C   
2649  O O   . ASP A 312 ? 0.2636 0.1593 0.2620 -0.0264 0.0015  -0.0192 312 ASP A O   
2650  C CB  . ASP A 312 ? 0.3343 0.2237 0.3341 -0.0136 -0.0031 -0.0025 312 ASP A CB  
2651  C CG  . ASP A 312 ? 0.4302 0.3267 0.4276 -0.0166 -0.0051 0.0026  312 ASP A CG  
2652  O OD1 . ASP A 312 ? 0.3875 0.2983 0.3886 -0.0155 -0.0059 0.0011  312 ASP A OD1 
2653  O OD2 . ASP A 312 ? 0.5722 0.4587 0.5625 -0.0203 -0.0057 0.0080  312 ASP A OD2 
2654  N N   . LEU A 313 ? 0.2809 0.1678 0.2823 -0.0127 0.0020  -0.0189 313 LEU A N   
2655  C CA  . LEU A 313 ? 0.2324 0.1107 0.2297 -0.0168 0.0045  -0.0262 313 LEU A CA  
2656  C C   . LEU A 313 ? 0.2281 0.1213 0.2251 -0.0221 0.0035  -0.0323 313 LEU A C   
2657  O O   . LEU A 313 ? 0.2502 0.1418 0.2442 -0.0305 0.0041  -0.0372 313 LEU A O   
2658  C CB  . LEU A 313 ? 0.2026 0.0723 0.2005 -0.0092 0.0071  -0.0290 313 LEU A CB  
2659  C CG  . LEU A 313 ? 0.2433 0.0941 0.2416 -0.0038 0.0086  -0.0253 313 LEU A CG  
2660  C CD1 . LEU A 313 ? 0.2532 0.1044 0.2571 0.0066  0.0110  -0.0270 313 LEU A CD1 
2661  C CD2 . LEU A 313 ? 0.2769 0.1074 0.2676 -0.0103 0.0114  -0.0291 313 LEU A CD2 
2662  N N   . ILE A 314 ? 0.1727 0.0805 0.1729 -0.0174 0.0017  -0.0319 314 ILE A N   
2663  C CA  . ILE A 314 ? 0.1798 0.1021 0.1799 -0.0205 -0.0005 -0.0364 314 ILE A CA  
2664  C C   . ILE A 314 ? 0.1911 0.1230 0.1946 -0.0267 -0.0019 -0.0357 314 ILE A C   
2665  O O   . ILE A 314 ? 0.2463 0.1850 0.2501 -0.0333 -0.0028 -0.0409 314 ILE A O   
2666  C CB  . ILE A 314 ? 0.1737 0.1059 0.1749 -0.0134 -0.0018 -0.0346 314 ILE A CB  
2667  C CG1 . ILE A 314 ? 0.1625 0.0884 0.1591 -0.0095 0.0005  -0.0377 314 ILE A CG1 
2668  C CG2 . ILE A 314 ? 0.2004 0.1478 0.2026 -0.0149 -0.0053 -0.0365 314 ILE A CG2 
2669  C CD1 . ILE A 314 ? 0.1547 0.0847 0.1531 -0.0027 0.0015  -0.0338 314 ILE A CD1 
2670  N N   . GLY A 315 ? 0.2227 0.1564 0.2289 -0.0252 -0.0019 -0.0299 315 GLY A N   
2671  C CA  . GLY A 315 ? 0.1648 0.1095 0.1745 -0.0303 -0.0021 -0.0299 315 GLY A CA  
2672  C C   . GLY A 315 ? 0.2000 0.1387 0.2076 -0.0402 0.0004  -0.0310 315 GLY A C   
2673  O O   . GLY A 315 ? 0.2935 0.2446 0.3052 -0.0462 0.0010  -0.0335 315 GLY A O   
2674  N N   . PHE A 316 ? 0.1759 0.0957 0.1776 -0.0421 0.0022  -0.0293 316 PHE A N   
2675  C CA  . PHE A 316 ? 0.1906 0.1007 0.1881 -0.0523 0.0051  -0.0291 316 PHE A CA  
2676  C C   . PHE A 316 ? 0.2091 0.1010 0.2010 -0.0568 0.0071  -0.0327 316 PHE A C   
2677  O O   . PHE A 316 ? 0.3442 0.2271 0.3319 -0.0671 0.0100  -0.0334 316 PHE A O   
2678  C CB  . PHE A 316 ? 0.2046 0.1046 0.1973 -0.0518 0.0060  -0.0204 316 PHE A CB  
2679  C CG  . PHE A 316 ? 0.2462 0.1617 0.2423 -0.0491 0.0049  -0.0176 316 PHE A CG  
2680  C CD1 . PHE A 316 ? 0.2345 0.1626 0.2326 -0.0566 0.0074  -0.0197 316 PHE A CD1 
2681  C CD2 . PHE A 316 ? 0.3029 0.2203 0.3005 -0.0396 0.0022  -0.0137 316 PHE A CD2 
2682  C CE1 . PHE A 316 ? 0.2690 0.2097 0.2697 -0.0539 0.0073  -0.0182 316 PHE A CE1 
2683  C CE2 . PHE A 316 ? 0.3709 0.3004 0.3705 -0.0380 0.0017  -0.0121 316 PHE A CE2 
2684  C CZ  . PHE A 316 ? 0.2654 0.2055 0.2660 -0.0448 0.0043  -0.0145 316 PHE A CZ  
2685  N N   . SER A 317 ? 0.2374 0.1222 0.2281 -0.0503 0.0064  -0.0355 317 SER A N   
2686  C CA  . SER A 317 ? 0.2676 0.1308 0.2517 -0.0533 0.0092  -0.0390 317 SER A CA  
2687  C C   . SER A 317 ? 0.3139 0.1812 0.2968 -0.0565 0.0090  -0.0491 317 SER A C   
2688  O O   . SER A 317 ? 0.2739 0.1350 0.2532 -0.0647 0.0103  -0.0536 317 SER A O   
2689  C CB  . SER A 317 ? 0.3104 0.1566 0.2928 -0.0423 0.0098  -0.0336 317 SER A CB  
2690  O OG  . SER A 317 ? 0.5637 0.3898 0.5410 -0.0431 0.0122  -0.0356 317 SER A OG  
2691  N N   . TYR A 318 ? 0.2440 0.1246 0.2295 -0.0491 0.0066  -0.0513 318 TYR A N   
2692  C CA  . TYR A 318 ? 0.2306 0.1121 0.2116 -0.0510 0.0064  -0.0603 318 TYR A CA  
2693  C C   . TYR A 318 ? 0.2322 0.1285 0.2141 -0.0622 0.0038  -0.0673 318 TYR A C   
2694  O O   . TYR A 318 ? 0.2428 0.1388 0.2192 -0.0663 0.0032  -0.0755 318 TYR A O   
2695  C CB  . TYR A 318 ? 0.2184 0.1105 0.2001 -0.0410 0.0046  -0.0599 318 TYR A CB  
2696  C CG  . TYR A 318 ? 0.2219 0.1003 0.2025 -0.0312 0.0081  -0.0571 318 TYR A CG  
2697  C CD1 . TYR A 318 ? 0.2548 0.1107 0.2320 -0.0310 0.0125  -0.0585 318 TYR A CD1 
2698  C CD2 . TYR A 318 ? 0.2532 0.1414 0.2370 -0.0222 0.0074  -0.0532 318 TYR A CD2 
2699  C CE1 . TYR A 318 ? 0.2439 0.0899 0.2229 -0.0208 0.0156  -0.0564 318 TYR A CE1 
2700  C CE2 . TYR A 318 ? 0.2113 0.0905 0.1966 -0.0137 0.0110  -0.0514 318 TYR A CE2 
2701  C CZ  . TYR A 318 ? 0.2284 0.0879 0.2123 -0.0124 0.0149  -0.0530 318 TYR A CZ  
2702  O OH  . TYR A 318 ? 0.2773 0.1305 0.2654 -0.0027 0.0184  -0.0515 318 TYR A OH  
2703  N N   . HIS A 319 ? 0.2229 0.1338 0.2119 -0.0672 0.0022  -0.0647 319 HIS A N   
2704  C CA  . HIS A 319 ? 0.2234 0.1531 0.2166 -0.0771 -0.0006 -0.0715 319 HIS A CA  
2705  C C   . HIS A 319 ? 0.2447 0.1638 0.2326 -0.0864 0.0014  -0.0760 319 HIS A C   
2706  O O   . HIS A 319 ? 0.2501 0.1817 0.2383 -0.0919 -0.0017 -0.0827 319 HIS A O   
2707  C CB  . HIS A 319 ? 0.2113 0.1582 0.2145 -0.0800 -0.0009 -0.0677 319 HIS A CB  
2708  C CG  . HIS A 319 ? 0.2196 0.1507 0.2205 -0.0854 0.0044  -0.0626 319 HIS A CG  
2709  N ND1 . HIS A 319 ? 0.2366 0.1610 0.2348 -0.0948 0.0072  -0.0633 319 HIS A ND1 
2710  C CD2 . HIS A 319 ? 0.2157 0.1387 0.2156 -0.0796 0.0063  -0.0538 319 HIS A CD2 
2711  C CE1 . HIS A 319 ? 0.2426 0.1535 0.2373 -0.0960 0.0111  -0.0560 319 HIS A CE1 
2712  N NE2 . HIS A 319 ? 0.2558 0.1650 0.2510 -0.0880 0.0105  -0.0508 319 HIS A NE2 
2713  N N   . ALA A 320 ? 0.2627 0.1593 0.2457 -0.0871 0.0060  -0.0715 320 ALA A N   
2714  C CA  . ALA A 320 ? 0.3566 0.2404 0.3343 -0.0947 0.0084  -0.0747 320 ALA A CA  
2715  C C   . ALA A 320 ? 0.2959 0.1645 0.2653 -0.0905 0.0091  -0.0796 320 ALA A C   
2716  O O   . ALA A 320 ? 0.3250 0.1792 0.2892 -0.0958 0.0117  -0.0826 320 ALA A O   
2717  C CB  . ALA A 320 ? 0.2935 0.1592 0.2688 -0.0971 0.0128  -0.0673 320 ALA A CB  
2718  N N   . TRP A 321 ? 0.2858 0.1571 0.2537 -0.0815 0.0076  -0.0809 321 TRP A N   
2719  C CA  . TRP A 321 ? 0.3813 0.2401 0.3412 -0.0767 0.0093  -0.0860 321 TRP A CA  
2720  C C   . TRP A 321 ? 0.4312 0.3069 0.3876 -0.0800 0.0052  -0.0941 321 TRP A C   
2721  O O   . TRP A 321 ? 0.5170 0.4147 0.4783 -0.0815 0.0003  -0.0944 321 TRP A O   
2722  C CB  . TRP A 321 ? 0.3187 0.1681 0.2785 -0.0637 0.0115  -0.0815 321 TRP A CB  
2723  C CG  . TRP A 321 ? 0.3542 0.1881 0.3173 -0.0579 0.0141  -0.0727 321 TRP A CG  
2724  C CD1 . TRP A 321 ? 0.3670 0.2004 0.3340 -0.0618 0.0137  -0.0659 321 TRP A CD1 
2725  C CD2 . TRP A 321 ? 0.3359 0.1544 0.2989 -0.0466 0.0170  -0.0695 321 TRP A CD2 
2726  N NE1 . TRP A 321 ? 0.3932 0.2107 0.3609 -0.0539 0.0155  -0.0581 321 TRP A NE1 
2727  C CE2 . TRP A 321 ? 0.3199 0.1290 0.2865 -0.0440 0.0171  -0.0602 321 TRP A CE2 
2728  C CE3 . TRP A 321 ? 0.3047 0.1179 0.2651 -0.0384 0.0197  -0.0736 321 TRP A CE3 
2729  C CZ2 . TRP A 321 ? 0.3052 0.1009 0.2741 -0.0329 0.0184  -0.0547 321 TRP A CZ2 
2730  C CZ3 . TRP A 321 ? 0.3352 0.1360 0.2992 -0.0274 0.0220  -0.0688 321 TRP A CZ3 
2731  C CH2 . TRP A 321 ? 0.3316 0.1242 0.3003 -0.0244 0.0208  -0.0593 321 TRP A CH2 
2732  N N   . ASN A 322 ? 0.3631 0.2284 0.3106 -0.0805 0.0070  -0.1007 322 ASN A N   
2733  C CA  . ASN A 322 ? 0.4005 0.2787 0.3413 -0.0809 0.0034  -0.1074 322 ASN A CA  
2734  C C   . ASN A 322 ? 0.4139 0.2973 0.3538 -0.0704 0.0032  -0.1044 322 ASN A C   
2735  O O   . ASN A 322 ? 0.4170 0.2882 0.3594 -0.0618 0.0077  -0.0993 322 ASN A O   
2736  C CB  . ASN A 322 ? 0.3686 0.2320 0.2986 -0.0829 0.0067  -0.1151 322 ASN A CB  
2737  C CG  . ASN A 322 ? 0.5562 0.4171 0.4853 -0.0950 0.0062  -0.1199 322 ASN A CG  
2738  O OD1 . ASN A 322 ? 0.6275 0.5044 0.5633 -0.1030 0.0021  -0.1193 322 ASN A OD1 
2739  N ND2 . ASN A 322 ? 0.5894 0.4305 0.5107 -0.0966 0.0109  -0.1253 322 ASN A ND2 
2740  N N   . ALA A 323 ? 0.2419 0.3081 0.3671 -0.0324 -0.0231 -0.1296 323 ALA A N   
2741  C CA  . ALA A 323 ? 0.1484 0.2188 0.2501 -0.0243 -0.0242 -0.1237 323 ALA A CA  
2742  C C   . ALA A 323 ? 0.1612 0.2259 0.2644 -0.0204 -0.0212 -0.1293 323 ALA A C   
2743  O O   . ALA A 323 ? 0.2056 0.2631 0.3015 -0.0163 -0.0211 -0.1221 323 ALA A O   
2744  C CB  . ALA A 323 ? 0.1490 0.2397 0.2313 -0.0208 -0.0267 -0.1243 323 ALA A CB  
2745  N N   . GLU A 324 ? 0.2814 0.3513 0.3955 -0.0219 -0.0187 -0.1432 324 GLU A N   
2746  C CA  . GLU A 324 ? 0.3355 0.4040 0.4545 -0.0184 -0.0150 -0.1509 324 GLU A CA  
2747  C C   . GLU A 324 ? 0.3291 0.3769 0.4673 -0.0169 -0.0138 -0.1462 324 GLU A C   
2748  O O   . GLU A 324 ? 0.3051 0.3512 0.4410 -0.0120 -0.0126 -0.1437 324 GLU A O   
2749  C CB  . GLU A 324 ? 0.3883 0.4656 0.5182 -0.0212 -0.0127 -0.1684 324 GLU A CB  
2750  C CG  . GLU A 324 ? 0.5030 0.5922 0.6261 -0.0177 -0.0092 -0.1778 324 GLU A CG  
2751  C CD  . GLU A 324 ? 0.7077 0.8163 0.8213 -0.0205 -0.0097 -0.1900 324 GLU A CD  
2752  O OE1 . GLU A 324 ? 0.7265 0.8384 0.8440 -0.0250 -0.0128 -0.1939 324 GLU A OE1 
2753  O OE2 . GLU A 324 ? 0.7637 0.8851 0.8660 -0.0187 -0.0072 -0.1959 324 GLU A OE2 
2754  N N   . ASP A 325 ? 0.3562 0.3882 0.5147 -0.0214 -0.0143 -0.1436 325 ASP A N   
2755  C CA  . ASP A 325 ? 0.2492 0.2594 0.4272 -0.0197 -0.0143 -0.1353 325 ASP A CA  
2756  C C   . ASP A 325 ? 0.2334 0.2380 0.3989 -0.0171 -0.0177 -0.1194 325 ASP A C   
2757  O O   . ASP A 325 ? 0.1843 0.1794 0.3580 -0.0120 -0.0182 -0.1144 325 ASP A O   
2758  C CB  . ASP A 325 ? 0.3463 0.3397 0.5454 -0.0265 -0.0144 -0.1313 325 ASP A CB  
2759  C CG  . ASP A 325 ? 0.4765 0.4751 0.6871 -0.0308 -0.0120 -0.1480 325 ASP A CG  
2760  O OD1 . ASP A 325 ? 0.4786 0.4864 0.6908 -0.0268 -0.0095 -0.1627 325 ASP A OD1 
2761  O OD2 . ASP A 325 ? 0.4485 0.4427 0.6670 -0.0390 -0.0125 -0.1466 325 ASP A OD2 
2762  N N   . ALA A 326 ? 0.2633 0.2746 0.4104 -0.0203 -0.0204 -0.1118 326 ALA A N   
2763  C CA  . ALA A 326 ? 0.2266 0.2331 0.3607 -0.0189 -0.0244 -0.0980 326 ALA A CA  
2764  C C   . ALA A 326 ? 0.2156 0.2295 0.3343 -0.0122 -0.0246 -0.1001 326 ALA A C   
2765  O O   . ALA A 326 ? 0.2744 0.2800 0.3921 -0.0086 -0.0261 -0.0878 326 ALA A O   
2766  C CB  . ALA A 326 ? 0.1520 0.1689 0.2690 -0.0224 -0.0264 -0.0918 326 ALA A CB  
2767  N N   . VAL A 327 ? 0.1940 0.2255 0.2975 -0.0101 -0.0218 -0.1093 327 VAL A N   
2768  C CA  . VAL A 327 ? 0.1424 0.1821 0.2312 -0.0057 -0.0205 -0.1100 327 VAL A CA  
2769  C C   . VAL A 327 ? 0.2098 0.2460 0.3208 -0.0027 -0.0170 -0.1182 327 VAL A C   
2770  O O   . VAL A 327 ? 0.1829 0.2183 0.2934 0.0003  -0.0175 -0.1156 327 VAL A O   
2771  C CB  . VAL A 327 ? 0.1687 0.2270 0.2366 -0.0053 -0.0184 -0.1140 327 VAL A CB  
2772  C CG1 . VAL A 327 ? 0.1343 0.2013 0.1900 -0.0029 -0.0154 -0.1147 327 VAL A CG1 
2773  C CG2 . VAL A 327 ? 0.1910 0.2518 0.2389 -0.0057 -0.0222 -0.1037 327 VAL A CG2 
2774  N N   . ARG A 328 ? 0.2062 0.2408 0.3389 -0.0032 -0.0138 -0.1288 328 ARG A N   
2775  C CA  . ARG A 328 ? 0.1573 0.1890 0.3142 0.0011  -0.0103 -0.1370 328 ARG A CA  
2776  C C   . ARG A 328 ? 0.1551 0.1676 0.3307 0.0048  -0.0141 -0.1250 328 ARG A C   
2777  O O   . ARG A 328 ? 0.1543 0.1689 0.3404 0.0105  -0.0130 -0.1260 328 ARG A O   
2778  C CB  . ARG A 328 ? 0.1743 0.2050 0.3510 -0.0007 -0.0072 -0.1497 328 ARG A CB  
2779  C CG  . ARG A 328 ? 0.1828 0.2346 0.3492 -0.0021 -0.0027 -0.1654 328 ARG A CG  
2780  C CD  . ARG A 328 ? 0.2882 0.3370 0.4798 -0.0022 0.0008  -0.1809 328 ARG A CD  
2781  N NE  . ARG A 328 ? 0.4820 0.5225 0.6807 -0.0076 -0.0011 -0.1831 328 ARG A NE  
2782  C CZ  . ARG A 328 ? 0.5258 0.5451 0.7488 -0.0086 -0.0022 -0.1801 328 ARG A CZ  
2783  N NH1 . ARG A 328 ? 0.4630 0.4664 0.7060 -0.0033 -0.0025 -0.1730 328 ARG A NH1 
2784  N NH2 . ARG A 328 ? 0.4599 0.4738 0.6875 -0.0152 -0.0033 -0.1827 328 ARG A NH2 
2785  N N   . ASP A 329 ? 0.1561 0.1511 0.3366 0.0016  -0.0188 -0.1120 329 ASP A N   
2786  C CA  . ASP A 329 ? 0.1569 0.1345 0.3503 0.0048  -0.0239 -0.0942 329 ASP A CA  
2787  C C   . ASP A 329 ? 0.1435 0.1318 0.3129 0.0069  -0.0268 -0.0805 329 ASP A C   
2788  O O   . ASP A 329 ? 0.1437 0.1318 0.3235 0.0123  -0.0291 -0.0725 329 ASP A O   
2789  C CB  . ASP A 329 ? 0.1630 0.1242 0.3587 -0.0011 -0.0273 -0.0789 329 ASP A CB  
2790  C CG  . ASP A 329 ? 0.2252 0.1735 0.4247 0.0018  -0.0330 -0.0544 329 ASP A CG  
2791  O OD1 . ASP A 329 ? 0.2528 0.1877 0.4802 0.0072  -0.0347 -0.0515 329 ASP A OD1 
2792  O OD2 . ASP A 329 ? 0.2164 0.1682 0.3910 -0.0007 -0.0363 -0.0383 329 ASP A OD2 
2793  N N   . PHE A 330 ? 0.1338 0.1318 0.2728 0.0028  -0.0270 -0.0782 330 PHE A N   
2794  C CA  . PHE A 330 ? 0.1247 0.1292 0.2399 0.0034  -0.0297 -0.0662 330 PHE A CA  
2795  C C   . PHE A 330 ? 0.1444 0.1615 0.2647 0.0070  -0.0268 -0.0732 330 PHE A C   
2796  O O   . PHE A 330 ? 0.1509 0.1688 0.2731 0.0088  -0.0302 -0.0621 330 PHE A O   
2797  C CB  . PHE A 330 ? 0.1187 0.1303 0.2040 -0.0001 -0.0296 -0.0663 330 PHE A CB  
2798  C CG  . PHE A 330 ? 0.1137 0.1255 0.1743 -0.0003 -0.0329 -0.0531 330 PHE A CG  
2799  C CD1 . PHE A 330 ? 0.1146 0.1162 0.1663 -0.0015 -0.0373 -0.0377 330 PHE A CD1 
2800  C CD2 . PHE A 330 ? 0.1115 0.1334 0.1568 -0.0002 -0.0311 -0.0566 330 PHE A CD2 
2801  C CE1 . PHE A 330 ? 0.1134 0.1137 0.1425 -0.0021 -0.0405 -0.0284 330 PHE A CE1 
2802  C CE2 . PHE A 330 ? 0.1104 0.1292 0.1346 -0.0016 -0.0343 -0.0453 330 PHE A CE2 
2803  C CZ  . PHE A 330 ? 0.1114 0.1189 0.1279 -0.0023 -0.0393 -0.0325 330 PHE A CZ  
2804  N N   . ILE A 331 ? 0.1255 0.1551 0.2479 0.0073  -0.0204 -0.0921 331 ILE A N   
2805  C CA  . ILE A 331 ? 0.1259 0.1711 0.2534 0.0099  -0.0152 -0.1000 331 ILE A CA  
2806  C C   . ILE A 331 ? 0.1449 0.1869 0.3081 0.0166  -0.0150 -0.1012 331 ILE A C   
2807  O O   . ILE A 331 ? 0.2046 0.2581 0.3759 0.0192  -0.0139 -0.0982 331 ILE A O   
2808  C CB  . ILE A 331 ? 0.1470 0.2082 0.2655 0.0083  -0.0077 -0.1205 331 ILE A CB  
2809  C CG1 . ILE A 331 ? 0.2111 0.2756 0.2957 0.0033  -0.0101 -0.1168 331 ILE A CG1 
2810  C CG2 . ILE A 331 ? 0.1342 0.2147 0.2549 0.0097  -0.0005 -0.1276 331 ILE A CG2 
2811  C CD1 . ILE A 331 ? 0.1850 0.2469 0.2461 0.0013  -0.0142 -0.0978 331 ILE A CD1 
2812  N N   . GLY A 332 ? 0.1400 0.1667 0.3272 0.0194  -0.0161 -0.1053 332 GLY A N   
2813  C CA  . GLY A 332 ? 0.1484 0.1683 0.3715 0.0276  -0.0174 -0.1039 332 GLY A CA  
2814  C C   . GLY A 332 ? 0.1439 0.1598 0.3681 0.0294  -0.0264 -0.0799 332 GLY A C   
2815  O O   . GLY A 332 ? 0.1465 0.1694 0.3944 0.0364  -0.0279 -0.0774 332 GLY A O   
2816  N N   . ARG A 333 ? 0.1390 0.1455 0.3380 0.0233  -0.0327 -0.0629 333 ARG A N   
2817  C CA  . ARG A 333 ? 0.1369 0.1420 0.3303 0.0235  -0.0418 -0.0416 333 ARG A CA  
2818  C C   . ARG A 333 ? 0.1415 0.1664 0.3241 0.0220  -0.0412 -0.0420 333 ARG A C   
2819  O O   . ARG A 333 ? 0.2737 0.3056 0.4700 0.0251  -0.0471 -0.0327 333 ARG A O   
2820  C CB  . ARG A 333 ? 0.1362 0.1290 0.3020 0.0169  -0.0466 -0.0268 333 ARG A CB  
2821  C CG  . ARG A 333 ? 0.1454 0.1214 0.3193 0.0151  -0.0452 -0.0270 333 ARG A CG  
2822  C CD  . ARG A 333 ? 0.1564 0.1174 0.3308 0.0141  -0.0527 -0.0049 333 ARG A CD  
2823  N NE  . ARG A 333 ? 0.1658 0.1122 0.3450 0.0096  -0.0497 -0.0044 333 ARG A NE  
2824  C CZ  . ARG A 333 ? 0.3481 0.2791 0.5319 0.0074  -0.0539 0.0139  333 ARG A CZ  
2825  N NH1 . ARG A 333 ? 0.2706 0.1991 0.4520 0.0102  -0.0624 0.0338  333 ARG A NH1 
2826  N NH2 . ARG A 333 ? 0.3761 0.2954 0.5664 0.0013  -0.0497 0.0128  333 ARG A NH2 
2827  N N   . LEU A 334 ? 0.1210 0.1554 0.2796 0.0166  -0.0349 -0.0515 334 LEU A N   
2828  C CA  . LEU A 334 ? 0.1637 0.2151 0.3114 0.0131  -0.0332 -0.0511 334 LEU A CA  
2829  C C   . LEU A 334 ? 0.2516 0.3217 0.4302 0.0185  -0.0278 -0.0613 334 LEU A C   
2830  O O   . LEU A 334 ? 0.1921 0.2766 0.3766 0.0170  -0.0297 -0.0556 334 LEU A O   
2831  C CB  . LEU A 334 ? 0.1527 0.2083 0.2693 0.0070  -0.0273 -0.0580 334 LEU A CB  
2832  C CG  . LEU A 334 ? 0.1222 0.1628 0.2091 0.0029  -0.0321 -0.0486 334 LEU A CG  
2833  C CD1 . LEU A 334 ? 0.1112 0.1571 0.1701 -0.0012 -0.0275 -0.0539 334 LEU A CD1 
2834  C CD2 . LEU A 334 ? 0.1113 0.1446 0.1890 0.0003  -0.0408 -0.0319 334 LEU A CD2 
2835  N N   . LYS A 335 ? 0.2819 0.3535 0.4819 0.0245  -0.0206 -0.0779 335 LYS A N   
2836  C CA  . LYS A 335 ? 0.2277 0.3176 0.4608 0.0317  -0.0143 -0.0899 335 LYS A CA  
2837  C C   . LYS A 335 ? 0.1372 0.2264 0.4010 0.0391  -0.0235 -0.0767 335 LYS A C   
2838  O O   . LYS A 335 ? 0.1778 0.2888 0.4613 0.0418  -0.0221 -0.0775 335 LYS A O   
2839  C CB  . LYS A 335 ? 0.1825 0.2695 0.4332 0.0375  -0.0056 -0.1120 335 LYS A CB  
2840  C CG  . LYS A 335 ? 0.1417 0.2529 0.3872 0.0359  0.0080  -0.1330 335 LYS A CG  
2841  C CD  . LYS A 335 ? 0.3211 0.4555 0.5838 0.0381  0.0126  -0.1328 335 LYS A CD  
2842  C CE  . LYS A 335 ? 0.4727 0.6289 0.7208 0.0334  0.0262  -0.1496 335 LYS A CE  
2843  N NZ  . LYS A 335 ? 0.3104 0.4934 0.5638 0.0306  0.0313  -0.1448 335 LYS A NZ  
2844  N N   . LYS A 336 ? 0.1353 0.2015 0.4034 0.0419  -0.0333 -0.0633 336 LYS A N   
2845  C CA  . LYS A 336 ? 0.2259 0.2907 0.5211 0.0495  -0.0441 -0.0481 336 LYS A CA  
2846  C C   . LYS A 336 ? 0.2843 0.3618 0.5642 0.0432  -0.0532 -0.0318 336 LYS A C   
2847  O O   . LYS A 336 ? 0.3159 0.4041 0.6139 0.0473  -0.0588 -0.0239 336 LYS A O   
2848  C CB  . LYS A 336 ? 0.2170 0.2521 0.5130 0.0514  -0.0512 -0.0355 336 LYS A CB  
2849  C CG  . LYS A 336 ? 0.2850 0.3056 0.5991 0.0554  -0.0433 -0.0499 336 LYS A CG  
2850  C CD  . LYS A 336 ? 0.5069 0.5019 0.8294 0.0568  -0.0505 -0.0343 336 LYS A CD  
2851  C CE  . LYS A 336 ? 0.4023 0.3780 0.7073 0.0495  -0.0501 -0.0319 336 LYS A CE  
2852  N NZ  . LYS A 336 ? 0.4589 0.4190 0.7539 0.0465  -0.0602 -0.0059 336 LYS A NZ  
2853  N N   . ILE A 337 ? 0.2260 0.2992 0.4658 0.0319  -0.0537 -0.0269 337 ILE A N   
2854  C CA  . ILE A 337 ? 0.1226 0.2071 0.3467 0.0242  -0.0610 -0.0155 337 ILE A CA  
2855  C C   . ILE A 337 ? 0.1248 0.2373 0.3628 0.0221  -0.0538 -0.0255 337 ILE A C   
2856  O O   . ILE A 337 ? 0.1933 0.3229 0.4439 0.0202  -0.0607 -0.0181 337 ILE A O   
2857  C CB  . ILE A 337 ? 0.1195 0.1898 0.2989 0.0137  -0.0619 -0.0103 337 ILE A CB  
2858  C CG1 . ILE A 337 ? 0.1253 0.1720 0.2928 0.0153  -0.0671 -0.0010 337 ILE A CG1 
2859  C CG2 . ILE A 337 ? 0.1195 0.1977 0.2830 0.0052  -0.0697 -0.0006 337 ILE A CG2 
2860  C CD1 . ILE A 337 ? 0.1264 0.1606 0.2570 0.0084  -0.0631 -0.0027 337 ILE A CD1 
2861  N N   . HIS A 338 ? 0.1664 0.2862 0.4018 0.0214  -0.0397 -0.0424 338 HIS A N   
2862  C CA  . HIS A 338 ? 0.1857 0.3338 0.4309 0.0177  -0.0302 -0.0519 338 HIS A CA  
2863  C C   . HIS A 338 ? 0.2575 0.4286 0.5501 0.0276  -0.0305 -0.0555 338 HIS A C   
2864  O O   . HIS A 338 ? 0.2404 0.4370 0.5429 0.0229  -0.0271 -0.0559 338 HIS A O   
2865  C CB  . HIS A 338 ? 0.1751 0.3267 0.4064 0.0160  -0.0151 -0.0693 338 HIS A CB  
2866  C CG  . HIS A 338 ? 0.1297 0.3110 0.3658 0.0107  -0.0031 -0.0784 338 HIS A CG  
2867  N ND1 . HIS A 338 ? 0.2007 0.4054 0.4694 0.0186  0.0080  -0.0948 338 HIS A ND1 
2868  C CD2 . HIS A 338 ? 0.2094 0.4008 0.4219 -0.0021 0.0007  -0.0732 338 HIS A CD2 
2869  C CE1 . HIS A 338 ? 0.2045 0.4353 0.4685 0.0101  0.0188  -0.0990 338 HIS A CE1 
2870  N NE2 . HIS A 338 ? 0.1952 0.4173 0.4254 -0.0030 0.0142  -0.0851 338 HIS A NE2 
2871  N N   . GLU A 339 ? 0.2554 0.4116 0.5679 0.0398  -0.0332 -0.0557 339 GLU A N   
2872  C CA  . GLU A 339 ? 0.1683 0.3356 0.5113 0.0493  -0.0323 -0.0567 339 GLU A CA  
2873  C C   . GLU A 339 ? 0.1998 0.3618 0.5514 0.0528  -0.0484 -0.0366 339 GLU A C   
2874  O O   . GLU A 339 ? 0.2137 0.3925 0.5896 0.0590  -0.0498 -0.0349 339 GLU A O   
2875  C CB  . GLU A 339 ? 0.2068 0.3602 0.5661 0.0598  -0.0243 -0.0712 339 GLU A CB  
2876  C CG  . GLU A 339 ? 0.3803 0.5015 0.7273 0.0605  -0.0279 -0.0700 339 GLU A CG  
2877  C CD  . GLU A 339 ? 0.7071 0.8201 1.0572 0.0632  -0.0157 -0.0917 339 GLU A CD  
2878  O OE1 . GLU A 339 ? 0.7143 0.8446 1.0536 0.0588  -0.0037 -0.1078 339 GLU A OE1 
2879  O OE2 . GLU A 339 ? 0.6809 0.7702 1.0418 0.0682  -0.0184 -0.0920 339 GLU A OE2 
2880  N N   . SER A 340 ? 0.1988 0.3397 0.5297 0.0491  -0.0602 -0.0216 340 SER A N   
2881  C CA  . SER A 340 ? 0.2208 0.3564 0.5533 0.0515  -0.0751 -0.0025 340 SER A CA  
2882  C C   . SER A 340 ? 0.2279 0.3881 0.5561 0.0437  -0.0818 0.0047  340 SER A C   
2883  O O   . SER A 340 ? 0.2281 0.3945 0.5658 0.0475  -0.0923 0.0160  340 SER A O   
2884  C CB  . SER A 340 ? 0.2237 0.3310 0.5298 0.0480  -0.0839 0.0111  340 SER A CB  
2885  O OG  . SER A 340 ? 0.1757 0.2859 0.4511 0.0361  -0.0905 0.0191  340 SER A OG  
2886  N N   . VAL A 341 ? 0.1948 0.3689 0.5087 0.0320  -0.0764 -0.0018 341 VAL A N   
2887  C CA  . VAL A 341 ? 0.1734 0.3685 0.4816 0.0213  -0.0822 0.0036  341 VAL A CA  
2888  C C   . VAL A 341 ? 0.2316 0.4586 0.5628 0.0191  -0.0698 -0.0087 341 VAL A C   
2889  O O   . VAL A 341 ? 0.3080 0.5384 0.6476 0.0226  -0.0553 -0.0226 341 VAL A O   
2890  C CB  . VAL A 341 ? 0.1413 0.3234 0.4109 0.0065  -0.0867 0.0083  341 VAL A CB  
2891  C CG1 . VAL A 341 ? 0.1394 0.2915 0.3841 0.0088  -0.0963 0.0198  341 VAL A CG1 
2892  C CG2 . VAL A 341 ? 0.1938 0.3761 0.4541 -0.0002 -0.0741 -0.0039 341 VAL A CG2 
2893  N N   . ASP A 342 ? 0.2396 0.4912 0.5791 0.0124  -0.0749 -0.0041 342 ASP A N   
2894  C CA  . ASP A 342 ? 0.2335 0.5192 0.5958 0.0086  -0.0636 -0.0128 342 ASP A CA  
2895  C C   . ASP A 342 ? 0.2533 0.5474 0.5962 -0.0109 -0.0575 -0.0150 342 ASP A C   
2896  O O   . ASP A 342 ? 0.3446 0.6659 0.7031 -0.0173 -0.0466 -0.0200 342 ASP A O   
2897  C CB  . ASP A 342 ? 0.4118 0.7237 0.7999 0.0124  -0.0724 -0.0068 342 ASP A CB  
2898  C CG  . ASP A 342 ? 0.5032 0.8053 0.8728 0.0073  -0.0911 0.0057  342 ASP A CG  
2899  O OD1 . ASP A 342 ? 0.4835 0.7554 0.8347 0.0130  -0.0994 0.0134  342 ASP A OD1 
2900  O OD2 . ASP A 342 ? 0.4397 0.7641 0.8122 -0.0030 -0.0968 0.0072  342 ASP A OD2 
2901  N N   . PHE A 343 ? 0.1955 0.4651 0.5047 -0.0207 -0.0638 -0.0103 343 PHE A N   
2902  C CA  . PHE A 343 ? 0.1725 0.4421 0.4600 -0.0397 -0.0597 -0.0111 343 PHE A CA  
2903  C C   . PHE A 343 ? 0.1172 0.3618 0.3777 -0.0399 -0.0512 -0.0167 343 PHE A C   
2904  O O   . PHE A 343 ? 0.1861 0.4164 0.4470 -0.0265 -0.0490 -0.0209 343 PHE A O   
2905  C CB  . PHE A 343 ? 0.1794 0.4351 0.4433 -0.0504 -0.0742 -0.0033 343 PHE A CB  
2906  C CG  . PHE A 343 ? 0.1368 0.3617 0.3771 -0.0425 -0.0865 0.0050  343 PHE A CG  
2907  C CD1 . PHE A 343 ? 0.1449 0.3726 0.3979 -0.0311 -0.0970 0.0113  343 PHE A CD1 
2908  C CD2 . PHE A 343 ? 0.1350 0.3289 0.3395 -0.0466 -0.0870 0.0073  343 PHE A CD2 
2909  C CE1 . PHE A 343 ? 0.1510 0.3519 0.3814 -0.0254 -0.1065 0.0201  343 PHE A CE1 
2910  C CE2 . PHE A 343 ? 0.1761 0.3447 0.3588 -0.0400 -0.0960 0.0145  343 PHE A CE2 
2911  C CZ  . PHE A 343 ? 0.1480 0.3203 0.3435 -0.0301 -0.1053 0.0212  343 PHE A CZ  
2912  N N   . GLN A 344 ? 0.1227 0.3571 0.3510 -0.0549 -0.0453 -0.0154 344 GLN A N   
2913  C CA  . GLN A 344 ? 0.1326 0.3384 0.3222 -0.0549 -0.0378 -0.0176 344 GLN A CA  
2914  C C   . GLN A 344 ? 0.1266 0.2987 0.2860 -0.0545 -0.0512 -0.0090 344 GLN A C   
2915  O O   . GLN A 344 ? 0.1882 0.3483 0.3263 -0.0666 -0.0579 -0.0024 344 GLN A O   
2916  C CB  . GLN A 344 ? 0.1536 0.3617 0.3218 -0.0698 -0.0260 -0.0180 344 GLN A CB  
2917  C CG  . GLN A 344 ? 0.1451 0.3841 0.3328 -0.0695 -0.0084 -0.0281 344 GLN A CG  
2918  C CD  . GLN A 344 ? 0.1669 0.4021 0.3241 -0.0828 0.0039  -0.0262 344 GLN A CD  
2919  O OE1 . GLN A 344 ? 0.2274 0.4509 0.3606 -0.0784 0.0117  -0.0305 344 GLN A OE1 
2920  N NE2 . GLN A 344 ? 0.1568 0.4023 0.3153 -0.0998 0.0051  -0.0189 344 GLN A NE2 
2921  N N   . PRO A 345 ? 0.1215 0.2779 0.2789 -0.0417 -0.0546 -0.0095 345 PRO A N   
2922  C CA  . PRO A 345 ? 0.1251 0.2546 0.2570 -0.0412 -0.0666 -0.0010 345 PRO A CA  
2923  C C   . PRO A 345 ? 0.1559 0.2597 0.2473 -0.0462 -0.0620 -0.0014 345 PRO A C   
2924  O O   . PRO A 345 ? 0.3654 0.4692 0.4473 -0.0472 -0.0503 -0.0074 345 PRO A O   
2925  C CB  . PRO A 345 ? 0.1200 0.2445 0.2682 -0.0263 -0.0690 -0.0012 345 PRO A CB  
2926  C CG  . PRO A 345 ? 0.1147 0.2489 0.2772 -0.0202 -0.0545 -0.0138 345 PRO A CG  
2927  C CD  . PRO A 345 ? 0.1153 0.2766 0.2921 -0.0280 -0.0464 -0.0188 345 PRO A CD  
2928  N N   . VAL A 346 ? 0.2226 0.3056 0.2897 -0.0488 -0.0718 0.0052  346 VAL A N   
2929  C CA  . VAL A 346 ? 0.1642 0.2213 0.1958 -0.0498 -0.0692 0.0051  346 VAL A CA  
2930  C C   . VAL A 346 ? 0.2184 0.2619 0.2432 -0.0404 -0.0738 0.0077  346 VAL A C   
2931  O O   . VAL A 346 ? 0.2748 0.3213 0.3092 -0.0380 -0.0835 0.0138  346 VAL A O   
2932  C CB  . VAL A 346 ? 0.1925 0.2355 0.2000 -0.0619 -0.0744 0.0085  346 VAL A CB  
2933  C CG1 . VAL A 346 ? 0.2163 0.2502 0.2160 -0.0603 -0.0838 0.0128  346 VAL A CG1 
2934  C CG2 . VAL A 346 ? 0.2192 0.2393 0.1960 -0.0621 -0.0681 0.0070  346 VAL A CG2 
2935  N N   . VAL A 347 ? 0.2152 0.2462 0.2249 -0.0352 -0.0671 0.0040  347 VAL A N   
2936  C CA  . VAL A 347 ? 0.1387 0.1589 0.1442 -0.0275 -0.0691 0.0059  347 VAL A CA  
2937  C C   . VAL A 347 ? 0.2048 0.2060 0.1781 -0.0285 -0.0679 0.0058  347 VAL A C   
2938  O O   . VAL A 347 ? 0.2073 0.2049 0.1703 -0.0273 -0.0608 0.0007  347 VAL A O   
2939  C CB  . VAL A 347 ? 0.1237 0.1505 0.1494 -0.0195 -0.0619 -0.0006 347 VAL A CB  
2940  C CG1 . VAL A 347 ? 0.1639 0.1796 0.1889 -0.0139 -0.0645 0.0033  347 VAL A CG1 
2941  C CG2 . VAL A 347 ? 0.1197 0.1659 0.1795 -0.0171 -0.0613 -0.0030 347 VAL A CG2 
2942  N N   . PHE A 348 ? 0.1926 0.1835 0.1524 -0.0283 -0.0707 0.0107  348 PHE A N   
2943  C CA  . PHE A 348 ? 0.1526 0.1291 0.0912 -0.0254 -0.0639 0.0088  348 PHE A CA  
2944  C C   . PHE A 348 ? 0.1986 0.1734 0.1374 -0.0193 -0.0617 0.0093  348 PHE A C   
2945  O O   . PHE A 348 ? 0.1568 0.1340 0.1026 -0.0185 -0.0664 0.0150  348 PHE A O   
2946  C CB  . PHE A 348 ? 0.1659 0.1354 0.0933 -0.0286 -0.0655 0.0106  348 PHE A CB  
2947  C CG  . PHE A 348 ? 0.2080 0.1682 0.1246 -0.0337 -0.0641 0.0078  348 PHE A CG  
2948  C CD1 . PHE A 348 ? 0.2270 0.1927 0.1501 -0.0414 -0.0673 0.0083  348 PHE A CD1 
2949  C CD2 . PHE A 348 ? 0.2311 0.1774 0.1323 -0.0318 -0.0605 0.0051  348 PHE A CD2 
2950  C CE1 . PHE A 348 ? 0.1906 0.1446 0.1019 -0.0486 -0.0671 0.0075  348 PHE A CE1 
2951  C CE2 . PHE A 348 ? 0.2464 0.1790 0.1364 -0.0371 -0.0612 0.0038  348 PHE A CE2 
2952  C CZ  . PHE A 348 ? 0.2029 0.1378 0.0966 -0.0463 -0.0646 0.0056  348 PHE A CZ  
2953  N N   . VAL A 349 ? 0.1972 0.1690 0.1293 -0.0154 -0.0552 0.0046  349 VAL A N   
2954  C CA  . VAL A 349 ? 0.1771 0.1482 0.1082 -0.0111 -0.0529 0.0041  349 VAL A CA  
2955  C C   . VAL A 349 ? 0.1857 0.1519 0.1039 -0.0084 -0.0468 0.0026  349 VAL A C   
2956  O O   . VAL A 349 ? 0.2366 0.2015 0.1509 -0.0062 -0.0426 -0.0011 349 VAL A O   
2957  C CB  . VAL A 349 ? 0.1752 0.1514 0.1133 -0.0086 -0.0520 -0.0021 349 VAL A CB  
2958  C CG1 . VAL A 349 ? 0.2557 0.2320 0.1956 -0.0057 -0.0510 -0.0029 349 VAL A CG1 
2959  C CG2 . VAL A 349 ? 0.1298 0.1152 0.0903 -0.0099 -0.0538 -0.0041 349 VAL A CG2 
2960  N N   . VAL A 350 ? 0.1522 0.1168 0.0643 -0.0087 -0.0473 0.0058  350 VAL A N   
2961  C CA  . VAL A 350 ? 0.1991 0.1610 0.1000 -0.0063 -0.0430 0.0031  350 VAL A CA  
2962  C C   . VAL A 350 ? 0.1838 0.1503 0.0813 -0.0043 -0.0413 0.0051  350 VAL A C   
2963  O O   . VAL A 350 ? 0.2852 0.2531 0.1832 -0.0069 -0.0447 0.0116  350 VAL A O   
2964  C CB  . VAL A 350 ? 0.1994 0.1562 0.0913 -0.0095 -0.0455 0.0033  350 VAL A CB  
2965  C CG1 . VAL A 350 ? 0.2571 0.2085 0.1364 -0.0067 -0.0420 -0.0015 350 VAL A CG1 
2966  C CG2 . VAL A 350 ? 0.2268 0.1787 0.1215 -0.0139 -0.0490 0.0031  350 VAL A CG2 
2967  N N   . LEU A 351 ? 0.1609 0.1295 0.0546 -0.0004 -0.0367 0.0008  351 LEU A N   
2968  C CA  . LEU A 351 ? 0.2256 0.1994 0.1130 0.0009  -0.0345 0.0021  351 LEU A CA  
2969  C C   . LEU A 351 ? 0.1883 0.1635 0.0709 0.0059  -0.0298 -0.0045 351 LEU A C   
2970  O O   . LEU A 351 ? 0.1889 0.1596 0.0749 0.0089  -0.0296 -0.0083 351 LEU A O   
2971  C CB  . LEU A 351 ? 0.2138 0.1887 0.1075 -0.0009 -0.0377 0.0059  351 LEU A CB  
2972  C CG  . LEU A 351 ? 0.2676 0.2453 0.1711 0.0020  -0.0384 -0.0008 351 LEU A CG  
2973  C CD1 . LEU A 351 ? 0.2864 0.2742 0.2088 -0.0002 -0.0348 -0.0003 351 LEU A CD1 
2974  C CD2 . LEU A 351 ? 0.2508 0.2262 0.1649 0.0002  -0.0418 -0.0016 351 LEU A CD2 
2975  N N   . ASP A 352 ? 0.2277 0.2082 0.1009 0.0073  -0.0261 -0.0050 352 ASP A N   
2976  C CA  . ASP A 352 ? 0.1938 0.1765 0.0633 0.0146  -0.0216 -0.0121 352 ASP A CA  
2977  C C   . ASP A 352 ? 0.2035 0.1920 0.0853 0.0196  -0.0229 -0.0153 352 ASP A C   
2978  O O   . ASP A 352 ? 0.1961 0.1937 0.0850 0.0181  -0.0244 -0.0144 352 ASP A O   
2979  C CB  . ASP A 352 ? 0.2439 0.2365 0.1025 0.0157  -0.0151 -0.0124 352 ASP A CB  
2980  C CG  . ASP A 352 ? 0.3603 0.3501 0.2045 0.0099  -0.0136 -0.0102 352 ASP A CG  
2981  O OD1 . ASP A 352 ? 0.3727 0.3543 0.2160 0.0085  -0.0174 -0.0119 352 ASP A OD1 
2982  O OD2 . ASP A 352 ? 0.3797 0.3776 0.2131 0.0071  -0.0081 -0.0066 352 ASP A OD2 
2983  N N   . GLY A 353 ? 0.1725 0.1568 0.0561 0.0263  -0.0234 -0.0192 353 GLY A N   
2984  C CA  . GLY A 353 ? 0.1628 0.1538 0.0572 0.0302  -0.0258 -0.0211 353 GLY A CA  
2985  C C   . GLY A 353 ? 0.2462 0.2542 0.1449 0.0403  -0.0245 -0.0271 353 GLY A C   
2986  O O   . GLY A 353 ? 0.4585 0.4719 0.3631 0.0462  -0.0277 -0.0291 353 GLY A O   
2987  N N   . GLU A 354 ? 0.1695 0.1901 0.0655 0.0424  -0.0192 -0.0300 354 GLU A N   
2988  C CA  . GLU A 354 ? 0.1680 0.2131 0.0765 0.0503  -0.0159 -0.0362 354 GLU A CA  
2989  C C   . GLU A 354 ? 0.2079 0.2736 0.1341 0.0412  -0.0087 -0.0347 354 GLU A C   
2990  O O   . GLU A 354 ? 0.1901 0.2791 0.1368 0.0425  -0.0074 -0.0388 354 GLU A O   
2991  C CB  . GLU A 354 ? 0.1888 0.2324 0.0871 0.0631  -0.0120 -0.0414 354 GLU A CB  
2992  C CG  . GLU A 354 ? 0.2758 0.3137 0.1606 0.0592  -0.0042 -0.0410 354 GLU A CG  
2993  C CD  . GLU A 354 ? 0.4604 0.4690 0.3297 0.0578  -0.0072 -0.0393 354 GLU A CD  
2994  O OE1 . GLU A 354 ? 0.9017 0.9040 0.7650 0.0679  -0.0053 -0.0454 354 GLU A OE1 
2995  O OE2 . GLU A 354 ? 0.4331 0.4272 0.2987 0.0468  -0.0116 -0.0329 354 GLU A OE2 
2996  N N   . ASN A 355 ? 0.2830 0.3418 0.2028 0.0314  -0.0048 -0.0280 355 ASN A N   
2997  C CA  . ASN A 355 ? 0.1857 0.2622 0.1182 0.0231  0.0039  -0.0244 355 ASN A CA  
2998  C C   . ASN A 355 ? 0.1991 0.2797 0.1535 0.0114  0.0023  -0.0202 355 ASN A C   
2999  O O   . ASN A 355 ? 0.1606 0.2579 0.1317 0.0038  0.0092  -0.0178 355 ASN A O   
3000  C CB  . ASN A 355 ? 0.1828 0.2505 0.0942 0.0186  0.0092  -0.0178 355 ASN A CB  
3001  C CG  . ASN A 355 ? 0.2603 0.3246 0.1508 0.0296  0.0126  -0.0251 355 ASN A CG  
3002  O OD1 . ASN A 355 ? 0.2649 0.3457 0.1632 0.0388  0.0181  -0.0332 355 ASN A OD1 
3003  N ND2 . ASN A 355 ? 0.4946 0.5378 0.3602 0.0289  0.0090  -0.0235 355 ASN A ND2 
3004  N N   . CYS A 356 ? 0.1589 0.2249 0.1147 0.0093  -0.0058 -0.0197 356 CYS A N   
3005  C CA  . CYS A 356 ? 0.1466 0.2126 0.1232 -0.0010 -0.0071 -0.0174 356 CYS A CA  
3006  C C   . CYS A 356 ? 0.2027 0.2852 0.2013 -0.0011 -0.0095 -0.0278 356 CYS A C   
3007  O O   . CYS A 356 ? 0.2627 0.3490 0.2826 -0.0107 -0.0085 -0.0285 356 CYS A O   
3008  C CB  . CYS A 356 ? 0.1840 0.2284 0.1542 -0.0032 -0.0136 -0.0129 356 CYS A CB  
3009  S SG  . CYS A 356 ? 0.3571 0.3919 0.3123 0.0061  -0.0214 -0.0197 356 CYS A SG  
3010  N N   . TRP A 357 ? 0.1712 0.2630 0.1650 0.0091  -0.0132 -0.0357 357 TRP A N   
3011  C CA  . TRP A 357 ? 0.1201 0.2276 0.1304 0.0091  -0.0182 -0.0455 357 TRP A CA  
3012  C C   . TRP A 357 ? 0.1619 0.2973 0.1959 0.0052  -0.0143 -0.0506 357 TRP A C   
3013  O O   . TRP A 357 ? 0.2000 0.3488 0.2530 -0.0004 -0.0178 -0.0590 357 TRP A O   
3014  C CB  . TRP A 357 ? 0.1203 0.2274 0.1153 0.0213  -0.0252 -0.0494 357 TRP A CB  
3015  C CG  . TRP A 357 ? 0.1238 0.2051 0.0956 0.0244  -0.0275 -0.0435 357 TRP A CG  
3016  C CD1 . TRP A 357 ? 0.1642 0.2328 0.1157 0.0328  -0.0273 -0.0395 357 TRP A CD1 
3017  C CD2 . TRP A 357 ? 0.1650 0.2309 0.1340 0.0185  -0.0302 -0.0421 357 TRP A CD2 
3018  N NE1 . TRP A 357 ? 0.2646 0.3112 0.2006 0.0308  -0.0303 -0.0351 357 TRP A NE1 
3019  C CE2 . TRP A 357 ? 0.1812 0.2277 0.1284 0.0226  -0.0319 -0.0363 357 TRP A CE2 
3020  C CE3 . TRP A 357 ? 0.2746 0.3417 0.2592 0.0103  -0.0311 -0.0465 357 TRP A CE3 
3021  C CZ2 . TRP A 357 ? 0.1501 0.1820 0.0921 0.0184  -0.0343 -0.0337 357 TRP A CZ2 
3022  C CZ3 . TRP A 357 ? 0.1618 0.2135 0.1410 0.0080  -0.0329 -0.0447 357 TRP A CZ3 
3023  C CH2 . TRP A 357 ? 0.1182 0.1543 0.0769 0.0119  -0.0345 -0.0378 357 TRP A CH2 
3024  N N   . GLU A 358 ? 0.2004 0.3469 0.2344 0.0074  -0.0066 -0.0469 358 GLU A N   
3025  C CA  . GLU A 358 ? 0.1243 0.3014 0.1839 0.0027  -0.0017 -0.0514 358 GLU A CA  
3026  C C   . GLU A 358 ? 0.1488 0.3265 0.2306 -0.0150 0.0018  -0.0498 358 GLU A C   
3027  O O   . GLU A 358 ? 0.3038 0.5062 0.4116 -0.0221 0.0031  -0.0562 358 GLU A O   
3028  C CB  . GLU A 358 ? 0.1335 0.3231 0.1883 0.0081  0.0083  -0.0478 358 GLU A CB  
3029  C CG  . GLU A 358 ? 0.2525 0.4214 0.2875 0.0032  0.0157  -0.0367 358 GLU A CG  
3030  C CD  . GLU A 358 ? 0.3420 0.5198 0.3634 0.0125  0.0243  -0.0367 358 GLU A CD  
3031  O OE1 . GLU A 358 ? 0.3818 0.5871 0.4193 0.0095  0.0342  -0.0379 358 GLU A OE1 
3032  O OE2 . GLU A 358 ? 0.4162 0.5744 0.4117 0.0224  0.0218  -0.0365 358 GLU A OE2 
3033  N N   . TYR A 359 ? 0.1484 0.2991 0.2221 -0.0221 0.0027  -0.0411 359 TYR A N   
3034  C CA  . TYR A 359 ? 0.1339 0.2777 0.2287 -0.0377 0.0049  -0.0383 359 TYR A CA  
3035  C C   . TYR A 359 ? 0.1291 0.2627 0.2337 -0.0401 -0.0036 -0.0485 359 TYR A C   
3036  O O   . TYR A 359 ? 0.1356 0.2591 0.2593 -0.0519 -0.0026 -0.0485 359 TYR A O   
3037  C CB  . TYR A 359 ? 0.2013 0.3217 0.2838 -0.0432 0.0099  -0.0218 359 TYR A CB  
3038  C CG  . TYR A 359 ? 0.1539 0.2841 0.2217 -0.0416 0.0192  -0.0124 359 TYR A CG  
3039  C CD1 . TYR A 359 ? 0.1637 0.3120 0.2474 -0.0527 0.0295  -0.0070 359 TYR A CD1 
3040  C CD2 . TYR A 359 ? 0.1575 0.2793 0.1955 -0.0299 0.0183  -0.0099 359 TYR A CD2 
3041  C CE1 . TYR A 359 ? 0.2569 0.4170 0.3257 -0.0512 0.0396  0.0003  359 TYR A CE1 
3042  C CE2 . TYR A 359 ? 0.1842 0.3154 0.2073 -0.0282 0.0274  -0.0042 359 TYR A CE2 
3043  C CZ  . TYR A 359 ? 0.1761 0.3275 0.2139 -0.0385 0.0385  0.0007  359 TYR A CZ  
3044  O OH  . TYR A 359 ? 0.2520 0.4156 0.2735 -0.0368 0.0492  0.0053  359 TYR A OH  
3045  N N   . TYR A 360 ? 0.1211 0.2566 0.2129 -0.0292 -0.0114 -0.0573 360 TYR A N   
3046  C CA  . TYR A 360 ? 0.1187 0.2482 0.2158 -0.0306 -0.0184 -0.0686 360 TYR A CA  
3047  C C   . TYR A 360 ? 0.1175 0.2746 0.2333 -0.0339 -0.0228 -0.0838 360 TYR A C   
3048  O O   . TYR A 360 ? 0.1155 0.2978 0.2356 -0.0301 -0.0228 -0.0855 360 TYR A O   
3049  C CB  . TYR A 360 ? 0.1141 0.2324 0.1851 -0.0187 -0.0240 -0.0685 360 TYR A CB  
3050  C CG  . TYR A 360 ? 0.1155 0.2062 0.1752 -0.0186 -0.0233 -0.0600 360 TYR A CG  
3051  C CD1 . TYR A 360 ? 0.1190 0.1966 0.1668 -0.0178 -0.0193 -0.0458 360 TYR A CD1 
3052  C CD2 . TYR A 360 ? 0.1148 0.1956 0.1757 -0.0189 -0.0269 -0.0671 360 TYR A CD2 
3053  C CE1 . TYR A 360 ? 0.1251 0.1809 0.1640 -0.0175 -0.0205 -0.0378 360 TYR A CE1 
3054  C CE2 . TYR A 360 ? 0.1712 0.2307 0.2256 -0.0180 -0.0267 -0.0596 360 TYR A CE2 
3055  C CZ  . TYR A 360 ? 0.1427 0.1901 0.1867 -0.0173 -0.0243 -0.0445 360 TYR A CZ  
3056  O OH  . TYR A 360 ? 0.1206 0.1501 0.1596 -0.0164 -0.0258 -0.0367 360 TYR A OH  
3057  N N   . GLU A 361 ? 0.1207 0.2740 0.2483 -0.0404 -0.0269 -0.0963 361 GLU A N   
3058  C CA  . GLU A 361 ? 0.1293 0.2970 0.2602 -0.0397 -0.0302 -0.1065 361 GLU A CA  
3059  C C   . GLU A 361 ? 0.1327 0.3109 0.2400 -0.0253 -0.0357 -0.1065 361 GLU A C   
3060  O O   . GLU A 361 ? 0.1707 0.3343 0.2571 -0.0178 -0.0373 -0.1033 361 GLU A O   
3061  C CB  . GLU A 361 ? 0.2482 0.3996 0.3847 -0.0453 -0.0304 -0.1156 361 GLU A CB  
3062  C CG  . GLU A 361 ? 0.4733 0.6117 0.6353 -0.0592 -0.0256 -0.1156 361 GLU A CG  
3063  C CD  . GLU A 361 ? 0.6012 0.7590 0.7830 -0.0686 -0.0234 -0.1151 361 GLU A CD  
3064  O OE1 . GLU A 361 ? 0.4573 0.6383 0.6378 -0.0654 -0.0273 -0.1220 361 GLU A OE1 
3065  O OE2 . GLU A 361 ? 0.6017 0.7518 0.8007 -0.0794 -0.0174 -0.1063 361 GLU A OE2 
3066  N N   . GLU A 362 ? 0.1293 0.3317 0.2411 -0.0218 -0.0381 -0.1086 362 GLU A N   
3067  C CA  . GLU A 362 ? 0.1313 0.3428 0.2237 -0.0080 -0.0435 -0.1066 362 GLU A CA  
3068  C C   . GLU A 362 ? 0.1234 0.3236 0.1956 0.0032  -0.0434 -0.0961 362 GLU A C   
3069  O O   . GLU A 362 ? 0.2477 0.4384 0.2987 0.0126  -0.0465 -0.0916 362 GLU A O   
3070  C CB  . GLU A 362 ? 0.1425 0.3486 0.2231 -0.0069 -0.0471 -0.1122 362 GLU A CB  
3071  C CG  . GLU A 362 ? 0.3873 0.6154 0.4663 -0.0018 -0.0533 -0.1156 362 GLU A CG  
3072  C CD  . GLU A 362 ? 0.6366 0.8591 0.6958 0.0026  -0.0567 -0.1156 362 GLU A CD  
3073  O OE1 . GLU A 362 ? 0.5071 0.7184 0.5652 -0.0037 -0.0541 -0.1217 362 GLU A OE1 
3074  O OE2 . GLU A 362 ? 0.5493 0.7790 0.5951 0.0123  -0.0617 -0.1093 362 GLU A OE2 
3075  N N   . ASN A 363 ? 0.1147 0.3159 0.1940 0.0013  -0.0393 -0.0914 363 ASN A N   
3076  C CA  . ASN A 363 ? 0.1197 0.3090 0.1788 0.0119  -0.0385 -0.0818 363 ASN A CA  
3077  C C   . ASN A 363 ? 0.1121 0.2728 0.1487 0.0133  -0.0404 -0.0780 363 ASN A C   
3078  O O   . ASN A 363 ? 0.1158 0.2620 0.1301 0.0234  -0.0415 -0.0706 363 ASN A O   
3079  C CB  . ASN A 363 ? 0.1159 0.3199 0.1672 0.0273  -0.0425 -0.0800 363 ASN A CB  
3080  C CG  . ASN A 363 ? 0.1357 0.3224 0.1682 0.0379  -0.0382 -0.0703 363 ASN A CG  
3081  O OD1 . ASN A 363 ? 0.1808 0.3619 0.2159 0.0340  -0.0289 -0.0658 363 ASN A OD1 
3082  N ND2 . ASN A 363 ? 0.2431 0.4191 0.2549 0.0505  -0.0444 -0.0668 363 ASN A ND2 
3083  N N   . GLY A 364 ? 0.1223 0.2718 0.1665 0.0031  -0.0391 -0.0823 364 GLY A N   
3084  C CA  . GLY A 364 ? 0.1204 0.2447 0.1484 0.0038  -0.0386 -0.0780 364 GLY A CA  
3085  C C   . GLY A 364 ? 0.1546 0.2738 0.1684 0.0092  -0.0398 -0.0767 364 GLY A C   
3086  O O   . GLY A 364 ? 0.2214 0.3236 0.2239 0.0092  -0.0384 -0.0724 364 GLY A O   
3087  N N   . ILE A 365 ? 0.1247 0.2607 0.1400 0.0128  -0.0425 -0.0799 365 ILE A N   
3088  C CA  . ILE A 365 ? 0.1338 0.2677 0.1354 0.0163  -0.0444 -0.0778 365 ILE A CA  
3089  C C   . ILE A 365 ? 0.1631 0.2930 0.1681 0.0092  -0.0422 -0.0850 365 ILE A C   
3090  O O   . ILE A 365 ? 0.2889 0.4082 0.2800 0.0103  -0.0412 -0.0804 365 ILE A O   
3091  C CB  . ILE A 365 ? 0.1426 0.2970 0.1454 0.0217  -0.0494 -0.0797 365 ILE A CB  
3092  C CG1 . ILE A 365 ? 0.1409 0.2990 0.1415 0.0312  -0.0509 -0.0733 365 ILE A CG1 
3093  C CG2 . ILE A 365 ? 0.1556 0.3086 0.1427 0.0243  -0.0524 -0.0764 365 ILE A CG2 
3094  C CD1 . ILE A 365 ? 0.1498 0.3312 0.1562 0.0377  -0.0563 -0.0755 365 ILE A CD1 
3095  N N   . PRO A 366 ? 0.1381 0.2760 0.1618 0.0017  -0.0411 -0.0968 366 PRO A N   
3096  C CA  . PRO A 366 ? 0.1435 0.2758 0.1711 -0.0033 -0.0382 -0.1048 366 PRO A CA  
3097  C C   . PRO A 366 ? 0.1369 0.2498 0.1615 -0.0038 -0.0346 -0.1002 366 PRO A C   
3098  O O   . PRO A 366 ? 0.1681 0.2774 0.1854 -0.0032 -0.0326 -0.1015 366 PRO A O   
3099  C CB  . PRO A 366 ? 0.1480 0.2877 0.1990 -0.0116 -0.0375 -0.1174 366 PRO A CB  
3100  C CG  . PRO A 366 ? 0.1482 0.3053 0.2041 -0.0108 -0.0412 -0.1170 366 PRO A CG  
3101  C CD  . PRO A 366 ? 0.1381 0.2913 0.1815 -0.0031 -0.0421 -0.1041 366 PRO A CD  
3102  N N   . PHE A 367 ? 0.1280 0.2306 0.1585 -0.0051 -0.0340 -0.0954 367 PHE A N   
3103  C CA  . PHE A 367 ? 0.1235 0.2088 0.1523 -0.0056 -0.0319 -0.0912 367 PHE A CA  
3104  C C   . PHE A 367 ? 0.1819 0.2606 0.1879 0.0002  -0.0321 -0.0807 367 PHE A C   
3105  O O   . PHE A 367 ? 0.1932 0.2663 0.1961 -0.0001 -0.0299 -0.0813 367 PHE A O   
3106  C CB  . PHE A 367 ? 0.1173 0.1942 0.1558 -0.0091 -0.0327 -0.0871 367 PHE A CB  
3107  C CG  . PHE A 367 ? 0.1137 0.1741 0.1472 -0.0082 -0.0330 -0.0805 367 PHE A CG  
3108  C CD1 . PHE A 367 ? 0.1271 0.1773 0.1762 -0.0112 -0.0313 -0.0853 367 PHE A CD1 
3109  C CD2 . PHE A 367 ? 0.1554 0.2094 0.1694 -0.0035 -0.0345 -0.0686 367 PHE A CD2 
3110  C CE1 . PHE A 367 ? 0.1254 0.1613 0.1717 -0.0091 -0.0311 -0.0753 367 PHE A CE1 
3111  C CE2 . PHE A 367 ? 0.1160 0.1541 0.1249 -0.0029 -0.0339 -0.0590 367 PHE A CE2 
3112  C CZ  . PHE A 367 ? 0.1201 0.1508 0.1456 -0.0056 -0.0326 -0.0617 367 PHE A CZ  
3113  N N   . LEU A 368 ? 0.1903 0.2695 0.1823 0.0051  -0.0343 -0.0716 368 LEU A N   
3114  C CA  . LEU A 368 ? 0.1586 0.2265 0.1309 0.0089  -0.0342 -0.0606 368 LEU A CA  
3115  C C   . LEU A 368 ? 0.1606 0.2334 0.1244 0.0086  -0.0337 -0.0620 368 LEU A C   
3116  O O   . LEU A 368 ? 0.1373 0.2017 0.0915 0.0074  -0.0319 -0.0579 368 LEU A O   
3117  C CB  . LEU A 368 ? 0.1307 0.1966 0.0933 0.0146  -0.0364 -0.0525 368 LEU A CB  
3118  C CG  . LEU A 368 ? 0.1833 0.2399 0.1452 0.0155  -0.0360 -0.0479 368 LEU A CG  
3119  C CD1 . LEU A 368 ? 0.2087 0.2623 0.1600 0.0228  -0.0370 -0.0413 368 LEU A CD1 
3120  C CD2 . LEU A 368 ? 0.1849 0.2256 0.1415 0.0119  -0.0346 -0.0434 368 LEU A CD2 
3121  N N   . GLU A 369 ? 0.1924 0.2805 0.1590 0.0092  -0.0357 -0.0681 369 GLU A N   
3122  C CA  . GLU A 369 ? 0.1542 0.2489 0.1106 0.0084  -0.0357 -0.0701 369 GLU A CA  
3123  C C   . GLU A 369 ? 0.1673 0.2642 0.1313 0.0040  -0.0312 -0.0796 369 GLU A C   
3124  O O   . GLU A 369 ? 0.2384 0.3349 0.1912 0.0031  -0.0290 -0.0783 369 GLU A O   
3125  C CB  . GLU A 369 ? 0.1855 0.2983 0.1436 0.0097  -0.0399 -0.0756 369 GLU A CB  
3126  C CG  . GLU A 369 ? 0.1676 0.2815 0.1176 0.0159  -0.0449 -0.0666 369 GLU A CG  
3127  C CD  . GLU A 369 ? 0.2770 0.4116 0.2283 0.0176  -0.0503 -0.0721 369 GLU A CD  
3128  O OE1 . GLU A 369 ? 0.2838 0.4318 0.2457 0.0128  -0.0498 -0.0845 369 GLU A OE1 
3129  O OE2 . GLU A 369 ? 0.3738 0.5114 0.3163 0.0237  -0.0555 -0.0645 369 GLU A OE2 
3130  N N   . LYS A 370 ? 0.1487 0.2484 0.1328 0.0011  -0.0294 -0.0901 370 LYS A N   
3131  C CA  . LYS A 370 ? 0.1860 0.2866 0.1813 -0.0019 -0.0248 -0.1006 370 LYS A CA  
3132  C C   . LYS A 370 ? 0.2475 0.3364 0.2390 -0.0012 -0.0223 -0.0944 370 LYS A C   
3133  O O   . LYS A 370 ? 0.2729 0.3665 0.2632 -0.0021 -0.0184 -0.0991 370 LYS A O   
3134  C CB  . LYS A 370 ? 0.2172 0.3175 0.2369 -0.0052 -0.0239 -0.1120 370 LYS A CB  
3135  C CG  . LYS A 370 ? 0.2377 0.3446 0.2711 -0.0080 -0.0201 -0.1278 370 LYS A CG  
3136  C CD  . LYS A 370 ? 0.3792 0.5036 0.4040 -0.0090 -0.0214 -0.1352 370 LYS A CD  
3137  C CE  . LYS A 370 ? 0.3720 0.5047 0.3926 -0.0096 -0.0170 -0.1439 370 LYS A CE  
3138  N NZ  . LYS A 370 ? 0.2873 0.4373 0.2948 -0.0108 -0.0190 -0.1497 370 LYS A NZ  
3139  N N   . LEU A 371 ? 0.1779 0.2540 0.1678 0.0000  -0.0244 -0.0848 371 LEU A N   
3140  C CA  . LEU A 371 ? 0.1573 0.2235 0.1443 0.0000  -0.0233 -0.0795 371 LEU A CA  
3141  C C   . LEU A 371 ? 0.2218 0.2877 0.1881 0.0003  -0.0224 -0.0715 371 LEU A C   
3142  O O   . LEU A 371 ? 0.2494 0.3189 0.2162 -0.0013 -0.0191 -0.0745 371 LEU A O   
3143  C CB  . LEU A 371 ? 0.1406 0.1941 0.1279 0.0007  -0.0269 -0.0711 371 LEU A CB  
3144  C CG  . LEU A 371 ? 0.1187 0.1617 0.0981 0.0006  -0.0283 -0.0630 371 LEU A CG  
3145  C CD1 . LEU A 371 ? 0.1379 0.1829 0.1359 -0.0010 -0.0271 -0.0720 371 LEU A CD1 
3146  C CD2 . LEU A 371 ? 0.1317 0.1637 0.1063 0.0015  -0.0324 -0.0540 371 LEU A CD2 
3147  N N   . TYR A 372 ? 0.2204 0.2826 0.1702 0.0021  -0.0253 -0.0620 372 TYR A N   
3148  C CA  . TYR A 372 ? 0.2379 0.2948 0.1678 0.0015  -0.0251 -0.0531 372 TYR A CA  
3149  C C   . TYR A 372 ? 0.2698 0.3412 0.1951 -0.0004 -0.0216 -0.0598 372 TYR A C   
3150  O O   . TYR A 372 ? 0.3892 0.4613 0.3046 -0.0028 -0.0186 -0.0569 372 TYR A O   
3151  C CB  . TYR A 372 ? 0.2339 0.2821 0.1502 0.0042  -0.0295 -0.0429 372 TYR A CB  
3152  C CG  . TYR A 372 ? 0.1504 0.1858 0.0687 0.0056  -0.0314 -0.0362 372 TYR A CG  
3153  C CD1 . TYR A 372 ? 0.2338 0.2639 0.1612 0.0041  -0.0303 -0.0373 372 TYR A CD1 
3154  C CD2 . TYR A 372 ? 0.1742 0.2054 0.0859 0.0090  -0.0344 -0.0296 372 TYR A CD2 
3155  C CE1 . TYR A 372 ? 0.2501 0.2705 0.1773 0.0051  -0.0317 -0.0316 372 TYR A CE1 
3156  C CE2 . TYR A 372 ? 0.1633 0.1866 0.0776 0.0112  -0.0348 -0.0255 372 TYR A CE2 
3157  C CZ  . TYR A 372 ? 0.1525 0.1702 0.0734 0.0086  -0.0331 -0.0263 372 TYR A CZ  
3158  O OH  . TYR A 372 ? 0.1737 0.1843 0.0949 0.0109  -0.0332 -0.0227 372 TYR A OH  
3159  N N   . SER A 373 ? 0.2116 0.2966 0.1436 -0.0001 -0.0217 -0.0693 373 SER A N   
3160  C CA  . SER A 373 ? 0.2765 0.3772 0.2047 -0.0024 -0.0179 -0.0778 373 SER A CA  
3161  C C   . SER A 373 ? 0.3398 0.4478 0.2831 -0.0048 -0.0112 -0.0888 373 SER A C   
3162  O O   . SER A 373 ? 0.4358 0.5546 0.3726 -0.0074 -0.0060 -0.0921 373 SER A O   
3163  C CB  . SER A 373 ? 0.2074 0.3214 0.1403 -0.0021 -0.0203 -0.0873 373 SER A CB  
3164  O OG  . SER A 373 ? 0.2808 0.3944 0.2350 -0.0018 -0.0212 -0.0951 373 SER A OG  
3165  N N   . THR A 374 ? 0.3400 0.4432 0.3044 -0.0040 -0.0111 -0.0948 374 THR A N   
3166  C CA  . THR A 374 ? 0.3242 0.4328 0.3072 -0.0050 -0.0056 -0.1063 374 THR A CA  
3167  C C   . THR A 374 ? 0.3317 0.4389 0.3074 -0.0064 -0.0030 -0.0995 374 THR A C   
3168  O O   . THR A 374 ? 0.3190 0.4397 0.2992 -0.0083 0.0037  -0.1075 374 THR A O   
3169  C CB  . THR A 374 ? 0.2884 0.3876 0.2958 -0.0034 -0.0075 -0.1123 374 THR A CB  
3170  O OG1 . THR A 374 ? 0.3250 0.4279 0.3408 -0.0039 -0.0088 -0.1203 374 THR A OG1 
3171  C CG2 . THR A 374 ? 0.2955 0.3970 0.3260 -0.0027 -0.0026 -0.1238 374 THR A CG2 
3172  N N   . LEU A 375 ? 0.3390 0.4313 0.3041 -0.0060 -0.0080 -0.0856 375 LEU A N   
3173  C CA  . LEU A 375 ? 0.3339 0.4250 0.2913 -0.0090 -0.0068 -0.0789 375 LEU A CA  
3174  C C   . LEU A 375 ? 0.3124 0.4134 0.2505 -0.0130 -0.0020 -0.0743 375 LEU A C   
3175  O O   . LEU A 375 ? 0.3305 0.4434 0.2693 -0.0177 0.0040  -0.0764 375 LEU A O   
3176  C CB  . LEU A 375 ? 0.2847 0.3560 0.2320 -0.0084 -0.0141 -0.0644 375 LEU A CB  
3177  C CG  . LEU A 375 ? 0.2214 0.2835 0.1856 -0.0061 -0.0190 -0.0663 375 LEU A CG  
3178  C CD1 . LEU A 375 ? 0.2962 0.3403 0.2465 -0.0059 -0.0251 -0.0517 375 LEU A CD1 
3179  C CD2 . LEU A 375 ? 0.1260 0.1928 0.1154 -0.0068 -0.0164 -0.0720 375 LEU A CD2 
3180  N N   . GLU A 376 ? 0.2833 0.3806 0.2047 -0.0115 -0.0045 -0.0679 376 GLU A N   
3181  C CA  . GLU A 376 ? 0.3541 0.4599 0.2564 -0.0150 -0.0007 -0.0632 376 GLU A CA  
3182  C C   . GLU A 376 ? 0.4125 0.5425 0.3243 -0.0182 0.0084  -0.0777 376 GLU A C   
3183  O O   . GLU A 376 ? 0.3935 0.5349 0.2957 -0.0236 0.0151  -0.0751 376 GLU A O   
3184  C CB  . GLU A 376 ? 0.3643 0.4634 0.2507 -0.0115 -0.0064 -0.0572 376 GLU A CB  
3185  C CG  . GLU A 376 ? 0.3732 0.4635 0.2336 -0.0128 -0.0079 -0.0422 376 GLU A CG  
3186  C CD  . GLU A 376 ? 0.5418 0.6313 0.3883 -0.0093 -0.0134 -0.0397 376 GLU A CD  
3187  O OE1 . GLU A 376 ? 0.8544 0.9616 0.7056 -0.0096 -0.0118 -0.0510 376 GLU A OE1 
3188  O OE2 . GLU A 376 ? 0.5721 0.6440 0.4037 -0.0062 -0.0198 -0.0272 376 GLU A OE2 
3189  N N   . LYS A 377 ? 0.4042 0.5420 0.3359 -0.0153 0.0093  -0.0933 377 LYS A N   
3190  C CA  . LYS A 377 ? 0.3264 0.4851 0.2692 -0.0171 0.0177  -0.1095 377 LYS A CA  
3191  C C   . LYS A 377 ? 0.2969 0.4646 0.2590 -0.0184 0.0252  -0.1172 377 LYS A C   
3192  O O   . LYS A 377 ? 0.3094 0.4958 0.2752 -0.0211 0.0342  -0.1259 377 LYS A O   
3193  C CB  . LYS A 377 ? 0.4343 0.5953 0.3938 -0.0138 0.0157  -0.1243 377 LYS A CB  
3194  C CG  . LYS A 377 ? 0.3636 0.5235 0.3075 -0.0132 0.0096  -0.1211 377 LYS A CG  
3195  C CD  . LYS A 377 ? 0.5223 0.6861 0.4365 -0.0156 0.0094  -0.1091 377 LYS A CD  
3196  C CE  . LYS A 377 ? 0.5595 0.7117 0.4589 -0.0128 0.0000  -0.0978 377 LYS A CE  
3197  N NZ  . LYS A 377 ? 0.6171 0.7626 0.4893 -0.0136 -0.0019 -0.0809 377 LYS A NZ  
3198  N N   . GLU A 378 ? 0.3368 0.4929 0.3122 -0.0163 0.0219  -0.1148 378 GLU A N   
3199  C CA  . GLU A 378 ? 0.3180 0.4833 0.3178 -0.0156 0.0284  -0.1242 378 GLU A CA  
3200  C C   . GLU A 378 ? 0.3378 0.5155 0.3249 -0.0228 0.0350  -0.1149 378 GLU A C   
3201  O O   . GLU A 378 ? 0.3596 0.5220 0.3320 -0.0267 0.0284  -0.0964 378 GLU A O   
3202  C CB  . GLU A 378 ? 0.2049 0.3518 0.2241 -0.0106 0.0209  -0.1227 378 GLU A CB  
3203  C CG  . GLU A 378 ? 0.2921 0.4294 0.3295 -0.0051 0.0172  -0.1338 378 GLU A CG  
3204  C CD  . GLU A 378 ? 0.4047 0.5550 0.4633 -0.0030 0.0244  -0.1505 378 GLU A CD  
3205  O OE1 . GLU A 378 ? 0.4087 0.5658 0.4934 0.0007  0.0300  -0.1580 378 GLU A OE1 
3206  O OE2 . GLU A 378 ? 0.4172 0.5712 0.4677 -0.0045 0.0241  -0.1556 378 GLU A OE2 
3207  N N   . GLU A 379 ? 0.2262 0.4264 0.2237 -0.0251 0.0462  -0.1229 379 GLU A N   
3208  C CA  . GLU A 379 ? 0.2024 0.4180 0.1915 -0.0342 0.0545  -0.1129 379 GLU A CA  
3209  C C   . GLU A 379 ? 0.3332 0.5388 0.3449 -0.0354 0.0490  -0.1002 379 GLU A C   
3210  O O   . GLU A 379 ? 0.4241 0.6244 0.4225 -0.0444 0.0473  -0.0829 379 GLU A O   
3211  C CB  . GLU A 379 ? 0.5161 0.7559 0.5177 -0.0354 0.0660  -0.1241 379 GLU A CB  
3212  C CG  . GLU A 379 ? 0.4554 0.7013 0.4975 -0.0258 0.0687  -0.1426 379 GLU A CG  
3213  C CD  . GLU A 379 ? 0.6469 0.9082 0.6933 -0.0244 0.0766  -0.1578 379 GLU A CD  
3214  O OE1 . GLU A 379 ? 0.6903 0.9630 0.7108 -0.0315 0.0817  -0.1538 379 GLU A OE1 
3215  O OE2 . GLU A 379 ? 0.5643 0.8251 0.6402 -0.0160 0.0775  -0.1731 379 GLU A OE2 
3216  N N   . TRP A 380 ? 0.3200 0.5212 0.3660 -0.0266 0.0450  -0.1077 380 TRP A N   
3217  C CA  . TRP A 380 ? 0.1641 0.3614 0.2359 -0.0267 0.0391  -0.0974 380 TRP A CA  
3218  C C   . TRP A 380 ? 0.2507 0.4181 0.3094 -0.0277 0.0242  -0.0803 380 TRP A C   
3219  O O   . TRP A 380 ? 0.3351 0.4987 0.4094 -0.0293 0.0175  -0.0705 380 TRP A O   
3220  C CB  . TRP A 380 ? 0.1465 0.3518 0.2607 -0.0155 0.0402  -0.1112 380 TRP A CB  
3221  C CG  . TRP A 380 ? 0.2102 0.3941 0.3279 -0.0066 0.0332  -0.1180 380 TRP A CG  
3222  C CD1 . TRP A 380 ? 0.1500 0.3345 0.2611 -0.0028 0.0380  -0.1352 380 TRP A CD1 
3223  C CD2 . TRP A 380 ? 0.2878 0.4475 0.4162 -0.0018 0.0201  -0.1076 380 TRP A CD2 
3224  N NE1 . TRP A 380 ? 0.2219 0.3834 0.3416 0.0032  0.0290  -0.1359 380 TRP A NE1 
3225  C CE2 . TRP A 380 ? 0.2684 0.4145 0.3979 0.0041  0.0185  -0.1182 380 TRP A CE2 
3226  C CE3 . TRP A 380 ? 0.3600 0.5096 0.4961 -0.0029 0.0095  -0.0905 380 TRP A CE3 
3227  C CZ2 . TRP A 380 ? 0.3151 0.4376 0.4536 0.0084  0.0080  -0.1105 380 TRP A CZ2 
3228  C CZ3 . TRP A 380 ? 0.3916 0.5186 0.5336 0.0023  -0.0014 -0.0833 380 TRP A CZ3 
3229  C CH2 . TRP A 380 ? 0.3181 0.4317 0.4615 0.0077  -0.0014 -0.0924 380 TRP A CH2 
3230  N N   . ILE A 381 ? 0.3061 0.4546 0.3374 -0.0267 0.0189  -0.0775 381 ILE A N   
3231  C CA  . ILE A 381 ? 0.1465 0.2682 0.1637 -0.0270 0.0067  -0.0634 381 ILE A CA  
3232  C C   . ILE A 381 ? 0.1556 0.2690 0.1387 -0.0351 0.0062  -0.0512 381 ILE A C   
3233  O O   . ILE A 381 ? 0.2806 0.3976 0.2412 -0.0357 0.0102  -0.0537 381 ILE A O   
3234  C CB  . ILE A 381 ? 0.1728 0.2800 0.1885 -0.0191 0.0010  -0.0689 381 ILE A CB  
3235  C CG1 . ILE A 381 ? 0.1726 0.2809 0.2233 -0.0116 -0.0002 -0.0770 381 ILE A CG1 
3236  C CG2 . ILE A 381 ? 0.1403 0.2237 0.1361 -0.0197 -0.0090 -0.0553 381 ILE A CG2 
3237  C CD1 . ILE A 381 ? 0.2322 0.3279 0.2849 -0.0060 -0.0037 -0.0836 381 ILE A CD1 
3238  N N   . GLU A 382 ? 0.1541 0.2555 0.1331 -0.0415 0.0007  -0.0379 382 GLU A N   
3239  C CA  . GLU A 382 ? 0.2041 0.2912 0.1534 -0.0492 -0.0008 -0.0252 382 GLU A CA  
3240  C C   . GLU A 382 ? 0.2808 0.3395 0.2178 -0.0462 -0.0122 -0.0173 382 GLU A C   
3241  O O   . GLU A 382 ? 0.2828 0.3336 0.2301 -0.0486 -0.0185 -0.0130 382 GLU A O   
3242  C CB  . GLU A 382 ? 0.2448 0.3415 0.1994 -0.0617 0.0038  -0.0180 382 GLU A CB  
3243  C CG  . GLU A 382 ? 0.4489 0.5356 0.3735 -0.0710 0.0067  -0.0060 382 GLU A CG  
3244  C CD  . GLU A 382 ? 0.6994 0.7948 0.6313 -0.0859 0.0116  0.0019  382 GLU A CD  
3245  O OE1 . GLU A 382 ? 0.7625 0.8461 0.6715 -0.0955 0.0138  0.0141  382 GLU A OE1 
3246  O OE2 . GLU A 382 ? 0.7480 0.8624 0.7100 -0.0882 0.0130  -0.0034 382 GLU A OE2 
3247  N N   . THR A 383 ? 0.2429 0.2889 0.1583 -0.0406 -0.0149 -0.0162 383 THR A N   
3248  C CA  . THR A 383 ? 0.1852 0.2060 0.0876 -0.0371 -0.0238 -0.0096 383 THR A CA  
3249  C C   . THR A 383 ? 0.2493 0.2519 0.1340 -0.0453 -0.0260 0.0020  383 THR A C   
3250  O O   . THR A 383 ? 0.3293 0.3340 0.2012 -0.0514 -0.0211 0.0079  383 THR A O   
3251  C CB  . THR A 383 ? 0.1882 0.2047 0.0767 -0.0280 -0.0257 -0.0125 383 THR A CB  
3252  O OG1 . THR A 383 ? 0.2008 0.2269 0.0780 -0.0279 -0.0202 -0.0119 383 THR A OG1 
3253  C CG2 . THR A 383 ? 0.1560 0.1825 0.0641 -0.0212 -0.0260 -0.0235 383 THR A CG2 
3254  N N   . LEU A 384 ? 0.1920 0.1760 0.0755 -0.0460 -0.0332 0.0054  384 LEU A N   
3255  C CA  . LEU A 384 ? 0.2157 0.1794 0.0860 -0.0549 -0.0361 0.0139  384 LEU A CA  
3256  C C   . LEU A 384 ? 0.2312 0.1685 0.0867 -0.0474 -0.0418 0.0155  384 LEU A C   
3257  O O   . LEU A 384 ? 0.2161 0.1563 0.0820 -0.0359 -0.0419 0.0099  384 LEU A O   
3258  C CB  . LEU A 384 ? 0.2089 0.1778 0.0964 -0.0648 -0.0391 0.0138  384 LEU A CB  
3259  C CG  . LEU A 384 ? 0.2017 0.1991 0.1125 -0.0725 -0.0330 0.0120  384 LEU A CG  
3260  C CD1 . LEU A 384 ? 0.1996 0.2010 0.1277 -0.0803 -0.0396 0.0121  384 LEU A CD1 
3261  C CD2 . LEU A 384 ? 0.2193 0.2206 0.1204 -0.0823 -0.0246 0.0183  384 LEU A CD2 
3262  N N   . THR A 385 ? 0.2530 0.1670 0.0915 -0.0531 -0.0436 0.0228  385 THR A N   
3263  C CA  . THR A 385 ? 0.2549 0.1435 0.0855 -0.0473 -0.0480 0.0217  385 THR A CA  
3264  C C   . THR A 385 ? 0.2597 0.1392 0.0908 -0.0567 -0.0546 0.0190  385 THR A C   
3265  O O   . THR A 385 ? 0.3556 0.2498 0.1989 -0.0678 -0.0553 0.0193  385 THR A O   
3266  C CB  . THR A 385 ? 0.2845 0.1478 0.0959 -0.0483 -0.0485 0.0300  385 THR A CB  
3267  O OG1 . THR A 385 ? 0.3318 0.1763 0.1331 -0.0650 -0.0512 0.0368  385 THR A OG1 
3268  C CG2 . THR A 385 ? 0.2988 0.1784 0.1104 -0.0445 -0.0424 0.0353  385 THR A CG2 
3269  N N   . LEU A 386 ? 0.2680 0.1284 0.0928 -0.0510 -0.0579 0.0149  386 LEU A N   
3270  C CA  . LEU A 386 ? 0.2756 0.1290 0.1012 -0.0591 -0.0635 0.0114  386 LEU A CA  
3271  C C   . LEU A 386 ? 0.3468 0.1848 0.1641 -0.0773 -0.0679 0.0149  386 LEU A C   
3272  O O   . LEU A 386 ? 0.3895 0.2395 0.2198 -0.0884 -0.0713 0.0132  386 LEU A O   
3273  C CB  . LEU A 386 ? 0.2849 0.1213 0.1022 -0.0493 -0.0641 0.0060  386 LEU A CB  
3274  C CG  . LEU A 386 ? 0.2608 0.1150 0.0909 -0.0340 -0.0582 0.0025  386 LEU A CG  
3275  C CD1 . LEU A 386 ? 0.2754 0.1140 0.0944 -0.0269 -0.0588 -0.0028 386 LEU A CD1 
3276  C CD2 . LEU A 386 ? 0.2833 0.1665 0.1351 -0.0342 -0.0564 0.0020  386 LEU A CD2 
3277  N N   . GLU A 387 ? 0.4487 0.2645 0.2535 -0.0787 -0.0651 0.0215  387 GLU A N   
3278  C CA  . GLU A 387 ? 0.4320 0.2350 0.2373 -0.0960 -0.0649 0.0274  387 GLU A CA  
3279  C C   . GLU A 387 ? 0.3325 0.1678 0.1568 -0.1068 -0.0595 0.0326  387 GLU A C   
3280  O O   . GLU A 387 ? 0.3399 0.1810 0.1759 -0.1232 -0.0610 0.0330  387 GLU A O   
3281  C CB  . GLU A 387 ? 0.4076 0.1781 0.1951 -0.0939 -0.0628 0.0363  387 GLU A CB  
3282  C CG  . GLU A 387 ? 0.5741 0.3381 0.3655 -0.1109 -0.0599 0.0448  387 GLU A CG  
3283  C CD  . GLU A 387 ? 0.8779 0.6084 0.6587 -0.1072 -0.0609 0.0471  387 GLU A CD  
3284  O OE1 . GLU A 387 ? 0.6898 0.4037 0.4591 -0.0906 -0.0623 0.0458  387 GLU A OE1 
3285  O OE2 . GLU A 387 ? 0.8968 0.6188 0.6834 -0.1207 -0.0602 0.0500  387 GLU A OE2 
3286  N N   . GLU A 388 ? 0.3372 0.1957 0.1659 -0.0983 -0.0529 0.0352  388 GLU A N   
3287  C CA  . GLU A 388 ? 0.3291 0.2209 0.1768 -0.1066 -0.0462 0.0374  388 GLU A CA  
3288  C C   . GLU A 388 ? 0.2811 0.1969 0.1528 -0.1100 -0.0504 0.0296  388 GLU A C   
3289  O O   . GLU A 388 ? 0.3923 0.3260 0.2819 -0.1235 -0.0489 0.0308  388 GLU A O   
3290  C CB  . GLU A 388 ? 0.3000 0.2112 0.1462 -0.0954 -0.0389 0.0381  388 GLU A CB  
3291  C CG  . GLU A 388 ? 0.4511 0.3629 0.2855 -0.1020 -0.0307 0.0490  388 GLU A CG  
3292  C CD  . GLU A 388 ? 0.5510 0.4691 0.3720 -0.0884 -0.0276 0.0500  388 GLU A CD  
3293  O OE1 . GLU A 388 ? 0.5997 0.5412 0.4322 -0.0790 -0.0261 0.0402  388 GLU A OE1 
3294  O OE2 . GLU A 388 ? 0.4670 0.3676 0.2693 -0.0863 -0.0271 0.0597  388 GLU A OE2 
3295  N N   . ALA A 389 ? 0.2627 0.1803 0.1360 -0.0981 -0.0560 0.0225  389 ALA A N   
3296  C CA  . ALA A 389 ? 0.2462 0.1840 0.1402 -0.1000 -0.0622 0.0176  389 ALA A CA  
3297  C C   . ALA A 389 ? 0.2929 0.2210 0.1873 -0.1146 -0.0703 0.0169  389 ALA A C   
3298  O O   . ALA A 389 ? 0.3535 0.3054 0.2707 -0.1182 -0.0726 0.0159  389 ALA A O   
3299  C CB  . ALA A 389 ? 0.2315 0.1682 0.1221 -0.0856 -0.0667 0.0128  389 ALA A CB  
3300  N N   . MET A 390 ? 0.2901 0.1857 0.1631 -0.1172 -0.0719 0.0174  390 MET A N   
3301  C CA  . MET A 390 ? 0.3100 0.1984 0.1857 -0.1262 -0.0757 0.0157  390 MET A CA  
3302  C C   . MET A 390 ? 0.3185 0.2205 0.2104 -0.1432 -0.0721 0.0207  390 MET A C   
3303  O O   . MET A 390 ? 0.3736 0.2923 0.2830 -0.1502 -0.0756 0.0181  390 MET A O   
3304  C CB  . MET A 390 ? 0.3625 0.2126 0.2135 -0.1236 -0.0772 0.0137  390 MET A CB  
3305  C CG  . MET A 390 ? 0.3330 0.1761 0.1737 -0.1084 -0.0799 0.0069  390 MET A CG  
3306  S SD  . MET A 390 ? 0.4256 0.2879 0.2794 -0.1101 -0.0859 0.0003  390 MET A SD  
3307  C CE  . MET A 390 ? 0.3709 0.2071 0.2153 -0.1227 -0.0892 -0.0049 390 MET A CE  
3308  N N   . ARG A 391 ? 0.3250 0.2223 0.2117 -0.1497 -0.0643 0.0284  391 ARG A N   
3309  C CA  . ARG A 391 ? 0.3481 0.2598 0.2493 -0.1652 -0.0575 0.0347  391 ARG A CA  
3310  C C   . ARG A 391 ? 0.3105 0.2665 0.2394 -0.1679 -0.0518 0.0346  391 ARG A C   
3311  O O   . ARG A 391 ? 0.3176 0.2932 0.2635 -0.1798 -0.0454 0.0381  391 ARG A O   
3312  C CB  . ARG A 391 ? 0.4103 0.2986 0.2919 -0.1693 -0.0494 0.0455  391 ARG A CB  
3313  C CG  . ARG A 391 ? 0.4500 0.2940 0.3072 -0.1636 -0.0540 0.0458  391 ARG A CG  
3314  C CD  . ARG A 391 ? 0.4224 0.2547 0.2853 -0.1713 -0.0603 0.0394  391 ARG A CD  
3315  N NE  . ARG A 391 ? 0.4581 0.2595 0.3030 -0.1602 -0.0671 0.0319  391 ARG A NE  
3316  C CZ  . ARG A 391 ? 0.6468 0.4493 0.4947 -0.1583 -0.0743 0.0209  391 ARG A CZ  
3317  N NH1 . ARG A 391 ? 0.5545 0.3857 0.4230 -0.1661 -0.0774 0.0168  391 ARG A NH1 
3318  N NH2 . ARG A 391 ? 0.8120 0.5884 0.6427 -0.1474 -0.0780 0.0138  391 ARG A NH2 
3319  N N   . LYS A 392 ? 0.2827 0.2563 0.2188 -0.1549 -0.0530 0.0298  392 LYS A N   
3320  C CA  . LYS A 392 ? 0.3636 0.3777 0.3260 -0.1513 -0.0449 0.0282  392 LYS A CA  
3321  C C   . LYS A 392 ? 0.4272 0.4711 0.4221 -0.1589 -0.0493 0.0249  392 LYS A C   
3322  O O   . LYS A 392 ? 0.5574 0.6018 0.5591 -0.1508 -0.0599 0.0203  392 LYS A O   
3323  C CB  . LYS A 392 ? 0.3001 0.3205 0.2624 -0.1306 -0.0449 0.0226  392 LYS A CB  
3324  C CG  . LYS A 392 ? 0.2837 0.3432 0.2761 -0.1247 -0.0378 0.0178  392 LYS A CG  
3325  C CD  . LYS A 392 ? 0.3132 0.3888 0.3058 -0.1305 -0.0226 0.0202  392 LYS A CD  
3326  C CE  . LYS A 392 ? 0.2884 0.3447 0.2509 -0.1217 -0.0172 0.0223  392 LYS A CE  
3327  N NZ  . LYS A 392 ? 0.3430 0.4177 0.3021 -0.1274 -0.0026 0.0250  392 LYS A NZ  
3328  N N   . GLU A 393 ? 0.3828 0.4519 0.3969 -0.1697 -0.0396 0.0275  393 GLU A N   
3329  C CA  . GLU A 393 ? 0.3461 0.4452 0.3936 -0.1729 -0.0418 0.0239  393 GLU A CA  
3330  C C   . GLU A 393 ? 0.3940 0.5322 0.4738 -0.1616 -0.0389 0.0183  393 GLU A C   
3331  O O   . GLU A 393 ? 0.3689 0.5324 0.4792 -0.1607 -0.0426 0.0150  393 GLU A O   
3332  C CB  . GLU A 393 ? 0.3926 0.4998 0.4472 -0.1897 -0.0325 0.0289  393 GLU A CB  
3333  C CG  . GLU A 393 ? 0.5411 0.6077 0.5658 -0.2005 -0.0337 0.0354  393 GLU A CG  
3334  C CD  . GLU A 393 ? 0.6437 0.7001 0.6482 -0.2062 -0.0204 0.0448  393 GLU A CD  
3335  O OE1 . GLU A 393 ? 0.9220 1.0096 0.9417 -0.2105 -0.0074 0.0469  393 GLU A OE1 
3336  O OE2 . GLU A 393 ? 0.6471 0.6651 0.6203 -0.2048 -0.0226 0.0501  393 GLU A OE2 
3337  N N   . ASP A 394 ? 0.4481 0.5920 0.5235 -0.1524 -0.0324 0.0162  394 ASP A N   
3338  C CA  . ASP A 394 ? 0.3031 0.4795 0.4096 -0.1387 -0.0302 0.0089  394 ASP A CA  
3339  C C   . ASP A 394 ? 0.2325 0.4014 0.3455 -0.1251 -0.0456 0.0070  394 ASP A C   
3340  O O   . ASP A 394 ? 0.1975 0.3908 0.3407 -0.1132 -0.0466 0.0026  394 ASP A O   
3341  C CB  . ASP A 394 ? 0.3283 0.5043 0.4229 -0.1265 -0.0167 0.0045  394 ASP A CB  
3342  C CG  . ASP A 394 ? 0.5168 0.7018 0.6007 -0.1384 -0.0006 0.0076  394 ASP A CG  
3343  O OD1 . ASP A 394 ? 0.5800 0.7442 0.6419 -0.1534 -0.0011 0.0169  394 ASP A OD1 
3344  O OD2 . ASP A 394 ? 0.5966 0.8085 0.6932 -0.1329 0.0129  0.0006  394 ASP A OD2 
3345  N N   . VAL A 395 ? 0.2817 0.4170 0.3669 -0.1253 -0.0566 0.0103  395 VAL A N   
3346  C CA  . VAL A 395 ? 0.2693 0.3941 0.3524 -0.1122 -0.0691 0.0098  395 VAL A CA  
3347  C C   . VAL A 395 ? 0.2499 0.3828 0.3465 -0.1148 -0.0791 0.0100  395 VAL A C   
3348  O O   . VAL A 395 ? 0.2100 0.3347 0.2979 -0.1274 -0.0803 0.0107  395 VAL A O   
3349  C CB  . VAL A 395 ? 0.2939 0.3803 0.3376 -0.1091 -0.0727 0.0114  395 VAL A CB  
3350  C CG1 . VAL A 395 ? 0.2305 0.3063 0.2682 -0.0980 -0.0834 0.0118  395 VAL A CG1 
3351  C CG2 . VAL A 395 ? 0.2623 0.3419 0.2944 -0.1007 -0.0630 0.0096  395 VAL A CG2 
3352  N N   . LYS A 396 ? 0.1829 0.3324 0.3013 -0.1031 -0.0864 0.0095  396 LYS A N   
3353  C CA  . LYS A 396 ? 0.1937 0.3549 0.3249 -0.1045 -0.0971 0.0098  396 LYS A CA  
3354  C C   . LYS A 396 ? 0.2084 0.3414 0.3063 -0.1050 -0.1064 0.0116  396 LYS A C   
3355  O O   . LYS A 396 ? 0.2043 0.3173 0.2811 -0.0958 -0.1075 0.0137  396 LYS A O   
3356  C CB  . LYS A 396 ? 0.1829 0.3704 0.3467 -0.0907 -0.1019 0.0100  396 LYS A CB  
3357  C CG  . LYS A 396 ? 0.3270 0.5524 0.5324 -0.0932 -0.0989 0.0061  396 LYS A CG  
3358  C CD  . LYS A 396 ? 0.3361 0.5736 0.5537 -0.1002 -0.0828 0.0022  396 LYS A CD  
3359  C CE  . LYS A 396 ? 0.3484 0.6263 0.6136 -0.0949 -0.0771 -0.0032 396 LYS A CE  
3360  N NZ  . LYS A 396 ? 0.3274 0.6206 0.6037 -0.1062 -0.0608 -0.0051 396 LYS A NZ  
3361  N N   . THR A 397 ? 0.2179 0.2899 0.1815 0.0447  -0.0816 -0.0073 397 THR A N   
3362  C CA  . THR A 397 ? 0.1765 0.2459 0.1413 0.0356  -0.0824 -0.0027 397 THR A CA  
3363  C C   . THR A 397 ? 0.1958 0.2748 0.1653 0.0298  -0.0874 -0.0001 397 THR A C   
3364  O O   . THR A 397 ? 0.3010 0.3915 0.2738 0.0302  -0.0903 -0.0014 397 THR A O   
3365  C CB  . THR A 397 ? 0.2063 0.2759 0.1680 0.0300  -0.0807 0.0006  397 THR A CB  
3366  O OG1 . THR A 397 ? 0.2319 0.2944 0.1876 0.0375  -0.0771 -0.0024 397 THR A OG1 
3367  C CG2 . THR A 397 ? 0.1936 0.2570 0.1546 0.0232  -0.0803 0.0036  397 THR A CG2 
3368  N N   . GLU A 398 ? 0.1777 0.2524 0.1473 0.0254  -0.0886 0.0025  398 GLU A N   
3369  C CA  . GLU A 398 ? 0.1953 0.2772 0.1672 0.0207  -0.0941 0.0046  398 GLU A CA  
3370  C C   . GLU A 398 ? 0.1770 0.2566 0.1468 0.0126  -0.0942 0.0087  398 GLU A C   
3371  O O   . GLU A 398 ? 0.1869 0.2598 0.1546 0.0119  -0.0895 0.0096  398 GLU A O   
3372  C CB  . GLU A 398 ? 0.2497 0.3301 0.2222 0.0257  -0.0969 0.0030  398 GLU A CB  
3373  C CG  . GLU A 398 ? 0.3960 0.4840 0.3712 0.0318  -0.1004 -0.0010 398 GLU A CG  
3374  C CD  . GLU A 398 ? 0.4695 0.5560 0.4445 0.0357  -0.1055 -0.0023 398 GLU A CD  
3375  O OE1 . GLU A 398 ? 0.6203 0.6967 0.5925 0.0356  -0.1049 -0.0009 398 GLU A OE1 
3376  O OE2 . GLU A 398 ? 0.3943 0.4896 0.3718 0.0394  -0.1106 -0.0054 398 GLU A OE2 
3377  N N   . VAL A 399 ? 0.1842 0.2694 0.1545 0.0078  -0.0999 0.0096  399 VAL A N   
3378  C CA  . VAL A 399 ? 0.1857 0.2669 0.1535 0.0014  -0.0990 0.0115  399 VAL A CA  
3379  C C   . VAL A 399 ? 0.1903 0.2759 0.1565 0.0018  -0.1007 0.0130  399 VAL A C   
3380  O O   . VAL A 399 ? 0.2243 0.3156 0.1912 0.0054  -0.1067 0.0118  399 VAL A O   
3381  C CB  . VAL A 399 ? 0.2791 0.3610 0.2474 -0.0011 -0.1049 0.0082  399 VAL A CB  
3382  C CG1 . VAL A 399 ? 0.2303 0.3005 0.1942 -0.0049 -0.1047 0.0077  399 VAL A CG1 
3383  C CG2 . VAL A 399 ? 0.2497 0.3354 0.2203 0.0013  -0.1041 0.0051  399 VAL A CG2 
3384  N N   . ILE A 400 ? 0.1853 0.2703 0.1489 -0.0003 -0.0954 0.0144  400 ILE A N   
3385  C CA  . ILE A 400 ? 0.1909 0.2805 0.1510 0.0016  -0.0969 0.0143  400 ILE A CA  
3386  C C   . ILE A 400 ? 0.2223 0.3180 0.1799 -0.0015 -0.0936 0.0133  400 ILE A C   
3387  O O   . ILE A 400 ? 0.2448 0.3425 0.2038 -0.0026 -0.0875 0.0116  400 ILE A O   
3388  C CB  . ILE A 400 ? 0.1867 0.2690 0.1456 0.0073  -0.0950 0.0137  400 ILE A CB  
3389  C CG1 . ILE A 400 ? 0.1746 0.2493 0.1347 0.0077  -0.0885 0.0125  400 ILE A CG1 
3390  C CG2 . ILE A 400 ? 0.2811 0.3601 0.2418 0.0118  -0.0994 0.0133  400 ILE A CG2 
3391  C CD1 . ILE A 400 ? 0.1734 0.2370 0.1317 0.0106  -0.0879 0.0117  400 ILE A CD1 
3392  N N   . GLU A 401 ? 0.2339 0.3336 0.1865 -0.0002 -0.0980 0.0126  401 GLU A N   
3393  C CA  . GLU A 401 ? 0.2693 0.3760 0.2184 -0.0006 -0.0970 0.0093  401 GLU A CA  
3394  C C   . GLU A 401 ? 0.2917 0.3902 0.2341 0.0053  -0.0961 0.0064  401 GLU A C   
3395  O O   . GLU A 401 ? 0.2293 0.3268 0.1679 0.0068  -0.0961 0.0023  401 GLU A O   
3396  C CB  . GLU A 401 ? 0.3586 0.4679 0.3042 -0.0068 -0.1078 0.0118  401 GLU A CB  
3397  C CG  . GLU A 401 ? 0.5127 0.6151 0.4627 -0.0108 -0.1160 0.0126  401 GLU A CG  
3398  C CD  . GLU A 401 ? 0.6046 0.6922 0.5559 -0.0160 -0.1185 0.0111  401 GLU A CD  
3399  O OE1 . GLU A 401 ? 0.5761 0.6637 0.5328 -0.0131 -0.1235 0.0063  401 GLU A OE1 
3400  O OE2 . GLU A 401 ? 0.5823 0.6557 0.5289 -0.0191 -0.1171 0.0115  401 GLU A OE2 
3401  N N   . SER A 402 ? 0.2555 0.3445 0.1958 0.0070  -0.0970 0.0094  402 SER A N   
3402  C CA  . SER A 402 ? 0.2093 0.2888 0.1427 0.0082  -0.0973 0.0097  402 SER A CA  
3403  C C   . SER A 402 ? 0.2345 0.3040 0.1697 0.0090  -0.0961 0.0123  402 SER A C   
3404  O O   . SER A 402 ? 0.3288 0.3982 0.2688 0.0099  -0.0967 0.0135  402 SER A O   
3405  C CB  . SER A 402 ? 0.2283 0.3104 0.1512 0.0086  -0.1042 0.0111  402 SER A CB  
3406  O OG  . SER A 402 ? 0.2384 0.3196 0.1586 0.0100  -0.1100 0.0145  402 SER A OG  
3407  N N   . VAL A 403 ? 0.2035 0.2631 0.1354 0.0080  -0.0943 0.0128  403 VAL A N   
3408  C CA  . VAL A 403 ? 0.2005 0.2486 0.1342 0.0078  -0.0934 0.0148  403 VAL A CA  
3409  C C   . VAL A 403 ? 0.3075 0.3493 0.2317 0.0065  -0.0957 0.0171  403 VAL A C   
3410  O O   . VAL A 403 ? 0.4400 0.4836 0.3576 0.0053  -0.0958 0.0165  403 VAL A O   
3411  C CB  . VAL A 403 ? 0.1850 0.2271 0.1269 0.0067  -0.0878 0.0131  403 VAL A CB  
3412  C CG1 . VAL A 403 ? 0.2347 0.2821 0.1825 0.0076  -0.0854 0.0114  403 VAL A CG1 
3413  C CG2 . VAL A 403 ? 0.2199 0.2594 0.1598 0.0043  -0.0850 0.0122  403 VAL A CG2 
3414  N N   . LYS A 404 ? 0.2178 0.2512 0.1403 0.0068  -0.0980 0.0198  404 LYS A N   
3415  C CA  . LYS A 404 ? 0.2423 0.2681 0.1553 0.0048  -0.0996 0.0228  404 LYS A CA  
3416  C C   . LYS A 404 ? 0.2524 0.2738 0.1718 0.0017  -0.0945 0.0217  404 LYS A C   
3417  O O   . LYS A 404 ? 0.3139 0.3330 0.2443 0.0022  -0.0921 0.0197  404 LYS A O   
3418  C CB  . LYS A 404 ? 0.2433 0.2610 0.1513 0.0061  -0.1046 0.0265  404 LYS A CB  
3419  C CG  . LYS A 404 ? 0.4003 0.4212 0.2996 0.0099  -0.1110 0.0279  404 LYS A CG  
3420  C CD  . LYS A 404 ? 0.4768 0.4904 0.3568 0.0103  -0.1161 0.0325  404 LYS A CD  
3421  C CE  . LYS A 404 ? 0.7053 0.7205 0.5755 0.0148  -0.1240 0.0336  404 LYS A CE  
3422  N NZ  . LYS A 404 ? 0.7621 0.7649 0.6264 0.0173  -0.1293 0.0370  404 LYS A NZ  
3423  N N   . ALA A 405 ? 0.2899 0.3104 0.2015 -0.0010 -0.0935 0.0224  405 ALA A N   
3424  C CA  . ALA A 405 ? 0.3257 0.3445 0.2433 -0.0036 -0.0892 0.0206  405 ALA A CA  
3425  C C   . ALA A 405 ? 0.2086 0.2205 0.1287 -0.0051 -0.0902 0.0228  405 ALA A C   
3426  O O   . ALA A 405 ? 0.3495 0.3557 0.2584 -0.0066 -0.0935 0.0274  405 ALA A O   
3427  C CB  . ALA A 405 ? 0.4191 0.4394 0.3265 -0.0061 -0.0881 0.0204  405 ALA A CB  
3428  N N   . GLY A 406 ? 0.1933 0.2046 0.1265 -0.0043 -0.0879 0.0196  406 GLY A N   
3429  C CA  . GLY A 406 ? 0.2093 0.2149 0.1476 -0.0052 -0.0896 0.0205  406 GLY A CA  
3430  C C   . GLY A 406 ? 0.2247 0.2297 0.1773 -0.0024 -0.0877 0.0150  406 GLY A C   
3431  O O   . GLY A 406 ? 0.2787 0.2861 0.2349 -0.0001 -0.0847 0.0113  406 GLY A O   
3432  N N   . THR A 407 ? 0.1755 0.1757 0.1356 -0.0023 -0.0902 0.0142  407 THR A N   
3433  C CA  . THR A 407 ? 0.1661 0.1618 0.1396 0.0021  -0.0903 0.0076  407 THR A CA  
3434  C C   . THR A 407 ? 0.2013 0.1860 0.1810 0.0056  -0.0944 0.0061  407 THR A C   
3435  O O   . THR A 407 ? 0.1775 0.1603 0.1518 0.0040  -0.0969 0.0108  407 THR A O   
3436  C CB  . THR A 407 ? 0.1915 0.1924 0.1721 0.0004  -0.0908 0.0049  407 THR A CB  
3437  O OG1 . THR A 407 ? 0.2696 0.2690 0.2530 -0.0028 -0.0950 0.0083  407 THR A OG1 
3438  C CG2 . THR A 407 ? 0.1789 0.1915 0.1504 -0.0040 -0.0873 0.0061  407 THR A CG2 
3439  N N   . TRP A 408 ? 0.2702 0.2458 0.2606 0.0116  -0.0959 -0.0022 408 TRP A N   
3440  C CA  . TRP A 408 ? 0.2302 0.1941 0.2268 0.0155  -0.1006 -0.0058 408 TRP A CA  
3441  C C   . TRP A 408 ? 0.2626 0.2258 0.2678 0.0125  -0.1054 -0.0034 408 TRP A C   
3442  O O   . TRP A 408 ? 0.2692 0.2222 0.2821 0.0155  -0.1103 -0.0071 408 TRP A O   
3443  C CB  . TRP A 408 ? 0.2170 0.1682 0.2200 0.0248  -0.1014 -0.0182 408 TRP A CB  
3444  C CG  . TRP A 408 ? 0.2030 0.1507 0.2169 0.0295  -0.1025 -0.0274 408 TRP A CG  
3445  C CD1 . TRP A 408 ? 0.2388 0.1962 0.2610 0.0258  -0.1028 -0.0255 408 TRP A CD1 
3446  C CD2 . TRP A 408 ? 0.2046 0.1384 0.2227 0.0400  -0.1040 -0.0420 408 TRP A CD2 
3447  N NE1 . TRP A 408 ? 0.1637 0.1153 0.1982 0.0338  -0.1043 -0.0385 408 TRP A NE1 
3448  C CE2 . TRP A 408 ? 0.1889 0.1241 0.2197 0.0431  -0.1054 -0.0493 408 TRP A CE2 
3449  C CE3 . TRP A 408 ? 0.1819 0.1059 0.1938 0.0467  -0.1035 -0.0496 408 TRP A CE3 
3450  C CZ2 . TRP A 408 ? 0.2292 0.1672 0.2650 0.0490  -0.1024 -0.0587 408 TRP A CZ2 
3451  C CZ3 . TRP A 408 ? 0.2051 0.1362 0.2206 0.0505  -0.0989 -0.0555 408 TRP A CZ3 
3452  C CH2 . TRP A 408 ? 0.2105 0.1475 0.2369 0.0514  -0.0986 -0.0597 408 TRP A CH2 
3453  N N   . PHE A 409 ? 0.2468 0.2209 0.2510 0.0065  -0.1045 0.0021  409 PHE A N   
3454  C CA  . PHE A 409 ? 0.2566 0.2328 0.2686 0.0020  -0.1089 0.0060  409 PHE A CA  
3455  C C   . PHE A 409 ? 0.3182 0.2949 0.3118 -0.0042 -0.1094 0.0172  409 PHE A C   
3456  O O   . PHE A 409 ? 0.3522 0.3360 0.3327 -0.0093 -0.1068 0.0222  409 PHE A O   
3457  C CB  . PHE A 409 ? 0.3038 0.2932 0.3278 -0.0007 -0.1077 0.0021  409 PHE A CB  
3458  C CG  . PHE A 409 ? 0.4645 0.4566 0.5129 -0.0022 -0.1125 -0.0016 409 PHE A CG  
3459  C CD1 . PHE A 409 ? 0.5045 0.4990 0.5517 -0.0102 -0.1159 0.0069  409 PHE A CD1 
3460  C CD2 . PHE A 409 ? 0.3976 0.3882 0.4721 0.0047  -0.1136 -0.0151 409 PHE A CD2 
3461  C CE1 . PHE A 409 ? 0.4581 0.4537 0.5380 -0.0146 -0.1224 0.0023  409 PHE A CE1 
3462  C CE2 . PHE A 409 ? 0.4294 0.4247 0.5347 0.0030  -0.1164 -0.0212 409 PHE A CE2 
3463  C CZ  . PHE A 409 ? 0.4247 0.4273 0.5346 -0.0084 -0.1180 -0.0128 409 PHE A CZ  
3464  N N   . ASP A 410 ? 0.3047 0.2716 0.2956 -0.0029 -0.1133 0.0197  410 ASP A N   
3465  C CA  . ASP A 410 ? 0.2917 0.2550 0.2652 -0.0063 -0.1155 0.0286  410 ASP A CA  
3466  C C   . ASP A 410 ? 0.2949 0.2631 0.2520 -0.0060 -0.1114 0.0304  410 ASP A C   
3467  O O   . ASP A 410 ? 0.3178 0.2827 0.2585 -0.0073 -0.1133 0.0366  410 ASP A O   
3468  C CB  . ASP A 410 ? 0.3776 0.3396 0.3434 -0.0125 -0.1178 0.0371  410 ASP A CB  
3469  C CG  . ASP A 410 ? 0.6022 0.5585 0.5854 -0.0130 -0.1241 0.0377  410 ASP A CG  
3470  O OD1 . ASP A 410 ? 0.7488 0.6966 0.7389 -0.0094 -0.1284 0.0351  410 ASP A OD1 
3471  O OD2 . ASP A 410 ? 0.7357 0.6956 0.7279 -0.0179 -0.1264 0.0403  410 ASP A OD2 
3472  N N   . GLY A 411 ? 0.3805 0.3555 0.3415 -0.0035 -0.1064 0.0249  411 GLY A N   
3473  C CA  . GLY A 411 ? 0.3050 0.2860 0.2546 -0.0031 -0.1034 0.0260  411 GLY A CA  
3474  C C   . GLY A 411 ? 0.2428 0.2285 0.1792 -0.0073 -0.1011 0.0298  411 GLY A C   
3475  O O   . GLY A 411 ? 0.3189 0.3078 0.2444 -0.0066 -0.1003 0.0311  411 GLY A O   
3476  N N   . ASN A 412 ? 0.2135 0.1997 0.1501 -0.0112 -0.1004 0.0310  412 ASN A N   
3477  C CA  . ASN A 412 ? 0.2366 0.2251 0.1573 -0.0154 -0.0978 0.0342  412 ASN A CA  
3478  C C   . ASN A 412 ? 0.2136 0.2098 0.1441 -0.0177 -0.0951 0.0295  412 ASN A C   
3479  O O   . ASN A 412 ? 0.2335 0.2335 0.1841 -0.0150 -0.0961 0.0236  412 ASN A O   
3480  C CB  . ASN A 412 ? 0.3263 0.3037 0.2252 -0.0185 -0.1002 0.0433  412 ASN A CB  
3481  C CG  . ASN A 412 ? 0.2908 0.2612 0.1963 -0.0203 -0.1039 0.0469  412 ASN A CG  
3482  O OD1 . ASN A 412 ? 0.2849 0.2608 0.2055 -0.0226 -0.1039 0.0437  412 ASN A OD1 
3483  N ND2 . ASN A 412 ? 0.3941 0.3532 0.2900 -0.0185 -0.1080 0.0528  412 ASN A ND2 
3484  N N   . PHE A 413 ? 0.2184 0.2165 0.1338 -0.0220 -0.0920 0.0308  413 PHE A N   
3485  C CA  . PHE A 413 ? 0.2071 0.2152 0.1302 -0.0245 -0.0898 0.0238  413 PHE A CA  
3486  C C   . PHE A 413 ? 0.2567 0.2581 0.1690 -0.0363 -0.0935 0.0287  413 PHE A C   
3487  O O   . PHE A 413 ? 0.2749 0.2769 0.1806 -0.0517 -0.0960 0.0269  413 PHE A O   
3488  C CB  . PHE A 413 ? 0.2105 0.2221 0.1221 -0.0249 -0.0852 0.0214  413 PHE A CB  
3489  C CG  . PHE A 413 ? 0.2021 0.2162 0.1203 -0.0191 -0.0845 0.0193  413 PHE A CG  
3490  C CD1 . PHE A 413 ? 0.2404 0.2490 0.1468 -0.0180 -0.0856 0.0243  413 PHE A CD1 
3491  C CD2 . PHE A 413 ? 0.1994 0.2217 0.1343 -0.0146 -0.0828 0.0116  413 PHE A CD2 
3492  C CE1 . PHE A 413 ? 0.2317 0.2442 0.1446 -0.0139 -0.0850 0.0215  413 PHE A CE1 
3493  C CE2 . PHE A 413 ? 0.2526 0.2755 0.1900 -0.0107 -0.0813 0.0107  413 PHE A CE2 
3494  C CZ  . PHE A 413 ? 0.2604 0.2791 0.1877 -0.0109 -0.0824 0.0154  413 PHE A CZ  
3495  N N   . LEU A 414 ? 0.3172 0.3011 0.2196 -0.0430 -0.1006 0.0409  414 LEU A N   
3496  C CA  . LEU A 414 ? 0.2951 0.2538 0.1679 -0.0704 -0.1100 0.0579  414 LEU A CA  
3497  C C   . LEU A 414 ? 0.2761 0.2503 0.2076 -0.0777 -0.1000 0.0383  414 LEU A C   
3498  O O   . LEU A 414 ? 0.3286 0.2931 0.2695 -0.0914 -0.0718 0.0345  414 LEU A O   
3499  C CB  . LEU A 414 ? 0.3201 0.2537 0.1801 -0.0692 -0.1131 0.0734  414 LEU A CB  
3500  C CG  . LEU A 414 ? 0.3526 0.2673 0.1742 -0.0618 -0.0985 0.0821  414 LEU A CG  
3501  C CD1 . LEU A 414 ? 0.4345 0.3129 0.2352 -0.0692 -0.0955 0.1002  414 LEU A CD1 
3502  C CD2 . LEU A 414 ? 0.4187 0.3250 0.2046 -0.0689 -0.0824 0.0851  414 LEU A CD2 
3503  N N   . LYS A 415 ? 0.2335 0.2318 0.2074 -0.0670 -0.1200 0.0236  415 LYS A N   
3504  C CA  . LYS A 415 ? 0.2424 0.2565 0.2776 -0.0698 -0.1122 0.0011  415 LYS A CA  
3505  C C   . LYS A 415 ? 0.2786 0.3076 0.3230 -0.0751 -0.0995 -0.0145 415 LYS A C   
3506  O O   . LYS A 415 ? 0.2919 0.3330 0.3864 -0.0793 -0.0885 -0.0347 415 LYS A O   
3507  C CB  . LYS A 415 ? 0.1857 0.2143 0.2428 -0.0431 -0.1115 -0.0091 415 LYS A CB  
3508  C CG  . LYS A 415 ? 0.2674 0.3069 0.3734 -0.0421 -0.1052 -0.0276 415 LYS A CG  
3509  C CD  . LYS A 415 ? 0.4032 0.4320 0.5371 -0.0421 -0.1103 -0.0266 415 LYS A CD  
3510  C CE  . LYS A 415 ? 0.5305 0.5668 0.7162 -0.0444 -0.0996 -0.0456 415 LYS A CE  
3511  N NZ  . LYS A 415 ? 0.4208 0.4596 0.6334 -0.0681 -0.0814 -0.0557 415 LYS A NZ  
3512  N N   . TRP A 416 ? 0.2770 0.3062 0.2768 -0.0746 -0.1012 -0.0073 416 TRP A N   
3513  C CA  . TRP A 416 ? 0.2391 0.2818 0.2447 -0.0784 -0.0911 -0.0221 416 TRP A CA  
3514  C C   . TRP A 416 ? 0.2952 0.3220 0.2572 -0.0905 -0.0678 -0.0118 416 TRP A C   
3515  O O   . TRP A 416 ? 0.2931 0.3284 0.2665 -0.0969 -0.0518 -0.0254 416 TRP A O   
3516  C CB  . TRP A 416 ? 0.1767 0.2345 0.1790 -0.0481 -0.0908 -0.0292 416 TRP A CB  
3517  C CG  . TRP A 416 ? 0.1817 0.2569 0.2047 -0.0373 -0.0829 -0.0321 416 TRP A CG  
3518  C CD1 . TRP A 416 ? 0.2209 0.2923 0.2645 -0.0372 -0.0829 -0.0366 416 TRP A CD1 
3519  C CD2 . TRP A 416 ? 0.1767 0.2356 0.1949 -0.0246 -0.0880 -0.0205 416 TRP A CD2 
3520  N NE1 . TRP A 416 ? 0.2281 0.2846 0.2833 -0.0185 -0.0881 -0.0367 416 TRP A NE1 
3521  C CE2 . TRP A 416 ? 0.2021 0.2510 0.2405 -0.0153 -0.0906 -0.0253 416 TRP A CE2 
3522  C CE3 . TRP A 416 ? 0.1942 0.2382 0.1931 -0.0200 -0.0910 -0.0080 416 TRP A CE3 
3523  C CZ2 . TRP A 416 ? 0.1455 0.1752 0.1849 -0.0032 -0.0945 -0.0225 416 TRP A CZ2 
3524  C CZ3 . TRP A 416 ? 0.2029 0.2324 0.2058 -0.0122 -0.0938 -0.0034 416 TRP A CZ3 
3525  C CH2 . TRP A 416 ? 0.2095 0.2322 0.2316 -0.0044 -0.0954 -0.0114 416 TRP A CH2 
3526  N N   . ILE A 417 ? 0.4022 0.4055 0.3137 -0.0924 -0.0661 0.0106  417 ILE A N   
3527  C CA  . ILE A 417 ? 0.3418 0.3270 0.2023 -0.1004 -0.0475 0.0215  417 ILE A CA  
3528  C C   . ILE A 417 ? 0.3605 0.3130 0.1824 -0.1034 -0.0405 0.0439  417 ILE A C   
3529  O O   . ILE A 417 ? 0.3517 0.2994 0.1810 -0.0970 -0.0561 0.0515  417 ILE A O   
3530  C CB  . ILE A 417 ? 0.3077 0.3031 0.1321 -0.0924 -0.0655 0.0226  417 ILE A CB  
3531  C CG1 . ILE A 417 ? 0.3942 0.3782 0.1787 -0.1002 -0.0450 0.0250  417 ILE A CG1 
3532  C CG2 . ILE A 417 ? 0.2911 0.2815 0.1218 -0.0675 -0.0735 0.0317  417 ILE A CG2 
3533  C CD1 . ILE A 417 ? 0.3182 0.3153 0.1139 -0.0804 -0.0520 0.0183  417 ILE A CD1 
3534  N N   . GLY A 418 ? 0.4146 0.3424 0.1917 -0.1118 -0.0175 0.0546  418 GLY A N   
3535  C CA  . GLY A 418 ? 0.5049 0.3958 0.2476 -0.1159 -0.0051 0.0745  418 GLY A CA  
3536  C C   . GLY A 418 ? 0.6328 0.5005 0.3711 -0.1320 0.0350  0.0761  418 GLY A C   
3537  O O   . GLY A 418 ? 0.7170 0.5739 0.4157 -0.1362 0.0518  0.0788  418 GLY A O   
3538  N N   . ASN A 419 ? 0.5935 0.4521 0.3713 -0.1412 0.0513  0.0743  419 ASN A N   
3539  C CA  . ASN A 419 ? 0.7207 0.5527 0.4946 -0.1582 0.0925  0.0778  419 ASN A CA  
3540  C C   . ASN A 419 ? 0.7001 0.5524 0.4978 -0.1679 0.1159  0.0588  419 ASN A C   
3541  O O   . ASN A 419 ? 0.6748 0.5612 0.4935 -0.1607 0.0983  0.0427  419 ASN A O   
3542  C CB  . ASN A 419 ? 0.7842 0.6090 0.6101 -0.1666 0.1031  0.0749  419 ASN A CB  
3543  C CG  . ASN A 419 ? 0.8300 0.6952 0.7294 -0.1597 0.0789  0.0533  419 ASN A CG  
3544  O OD1 . ASN A 419 ? 0.7624 0.6618 0.6894 -0.1551 0.0687  0.0346  419 ASN A OD1 
3545  N ND2 . ASN A 419 ? 0.8561 0.7153 0.7853 -0.1577 0.0690  0.0556  419 ASN A ND2 
3546  N N   . LYS A 420 ? 0.7400 0.5702 0.5338 -0.1842 0.1565  0.0605  420 LYS A N   
3547  C CA  . LYS A 420 ? 0.7735 0.6200 0.5812 -0.1932 0.1813  0.0439  420 LYS A CA  
3548  C C   . LYS A 420 ? 0.6901 0.5827 0.5822 -0.1937 0.1737  0.0134  420 LYS A C   
3549  O O   . LYS A 420 ? 0.6923 0.6108 0.5950 -0.1914 0.1722  -0.0032 420 LYS A O   
3550  C CB  . LYS A 420 ? 0.7867 0.6026 0.5815 -0.2082 0.2257  0.0501  420 LYS A CB  
3551  C CG  . LYS A 420 ? 0.8303 0.6650 0.6419 -0.2143 0.2497  0.0315  420 LYS A CG  
3552  C CD  . LYS A 420 ? 0.9052 0.7177 0.7174 -0.2218 0.2846  0.0338  420 LYS A CD  
3553  C CE  . LYS A 420 ? 0.8440 0.6861 0.7346 -0.2341 0.3069  0.0053  420 LYS A CE  
3554  N NZ  . LYS A 420 ? 0.8213 0.6471 0.7003 -0.2409 0.3411  0.0040  420 LYS A NZ  
3555  N N   . GLU A 421 ? 0.5259 0.4282 0.4780 -0.1954 0.1678  0.0046  421 GLU A N   
3556  C CA  . GLU A 421 ? 0.5867 0.5304 0.6198 -0.1944 0.1607  -0.0263 421 GLU A CA  
3557  C C   . GLU A 421 ? 0.6142 0.5879 0.6491 -0.1758 0.1209  -0.0358 421 GLU A C   
3558  O O   . GLU A 421 ? 0.5273 0.5287 0.5893 -0.1736 0.1194  -0.0573 421 GLU A O   
3559  C CB  . GLU A 421 ? 0.6678 0.6134 0.7623 -0.1984 0.1602  -0.0339 421 GLU A CB  
3560  C CG  . GLU A 421 ? 0.6909 0.6083 0.7528 -0.1926 0.1438  -0.0095 421 GLU A CG  
3561  C CD  . GLU A 421 ? 0.7404 0.6528 0.8603 -0.2007 0.1525  -0.0160 421 GLU A CD  
3562  O OE1 . GLU A 421 ? 0.6429 0.5498 0.7960 -0.2175 0.1879  -0.0252 421 GLU A OE1 
3563  O OE2 . GLU A 421 ? 0.8171 0.7318 0.9497 -0.1891 0.1235  -0.0128 421 GLU A OE2 
3564  N N   . LYS A 422 ? 0.5780 0.5456 0.5838 -0.1623 0.0890  -0.0203 422 LYS A N   
3565  C CA  . LYS A 422 ? 0.4439 0.4364 0.4477 -0.1456 0.0537  -0.0274 422 LYS A CA  
3566  C C   . LYS A 422 ? 0.3854 0.3797 0.3426 -0.1441 0.0557  -0.0255 422 LYS A C   
3567  O O   . LYS A 422 ? 0.4071 0.4255 0.3753 -0.1346 0.0362  -0.0391 422 LYS A O   
3568  C CB  . LYS A 422 ? 0.4853 0.4690 0.4634 -0.1328 0.0230  -0.0099 422 LYS A CB  
3569  C CG  . LYS A 422 ? 0.4628 0.4439 0.4835 -0.1321 0.0171  -0.0112 422 LYS A CG  
3570  C CD  . LYS A 422 ? 0.3782 0.3905 0.4546 -0.1194 -0.0092 -0.0323 422 LYS A CD  
3571  C CE  . LYS A 422 ? 0.3151 0.3232 0.4313 -0.1178 -0.0157 -0.0334 422 LYS A CE  
3572  N NZ  . LYS A 422 ? 0.3431 0.3794 0.5303 -0.1112 -0.0265 -0.0619 422 LYS A NZ  
3573  N N   . ASN A 423 ? 0.4362 0.4031 0.3396 -0.1527 0.0788  -0.0091 423 ASN A N   
3574  C CA  . ASN A 423 ? 0.5438 0.5095 0.3980 -0.1504 0.0799  -0.0063 423 ASN A CA  
3575  C C   . ASN A 423 ? 0.5439 0.5261 0.4242 -0.1588 0.1037  -0.0273 423 ASN A C   
3576  O O   . ASN A 423 ? 0.4457 0.4376 0.3021 -0.1539 0.0971  -0.0327 423 ASN A O   
3577  C CB  . ASN A 423 ? 0.5486 0.4756 0.3286 -0.1531 0.0923  0.0196  423 ASN A CB  
3578  C CG  . ASN A 423 ? 0.5439 0.4593 0.2854 -0.1402 0.0613  0.0382  423 ASN A CG  
3579  O OD1 . ASN A 423 ? 0.4441 0.3783 0.2170 -0.1313 0.0341  0.0337  423 ASN A OD1 
3580  N ND2 . ASN A 423 ? 0.5361 0.4201 0.2085 -0.1382 0.0650  0.0583  423 ASN A ND2 
3581  N N   . GLU A 424 ? 0.4988 0.4847 0.4290 -0.1713 0.1311  -0.0404 424 GLU A N   
3582  C CA  . GLU A 424 ? 0.4504 0.4545 0.4100 -0.1792 0.1545  -0.0628 424 GLU A CA  
3583  C C   . GLU A 424 ? 0.3987 0.4387 0.3951 -0.1672 0.1280  -0.0865 424 GLU A C   
3584  O O   . GLU A 424 ? 0.4006 0.4517 0.3865 -0.1662 0.1325  -0.0977 424 GLU A O   
3585  C CB  . GLU A 424 ? 0.4942 0.4991 0.5105 -0.1949 0.1873  -0.0751 424 GLU A CB  
3586  C CG  . GLU A 424 ? 0.8805 0.8868 0.9014 -0.2089 0.2271  -0.0871 424 GLU A CG  
3587  C CD  . GLU A 424 ? 0.8793 0.8641 0.8201 -0.2079 0.2362  -0.0704 424 GLU A CD  
3588  O OE1 . GLU A 424 ? 0.9694 0.9162 0.8524 -0.2130 0.2521  -0.0448 424 GLU A OE1 
3589  O OE2 . GLU A 424 ? 0.6937 0.6982 0.6284 -0.2011 0.2270  -0.0835 424 GLU A OE2 
3590  N N   . TYR A 425 ? 0.3555 0.4114 0.3921 -0.1569 0.0997  -0.0943 425 TYR A N   
3591  C CA  . TYR A 425 ? 0.3345 0.4189 0.3998 -0.1434 0.0729  -0.1151 425 TYR A CA  
3592  C C   . TYR A 425 ? 0.3269 0.4079 0.3353 -0.1337 0.0522  -0.1042 425 TYR A C   
3593  O O   . TYR A 425 ? 0.3024 0.3996 0.3159 -0.1282 0.0450  -0.1203 425 TYR A O   
3594  C CB  . TYR A 425 ? 0.3315 0.4279 0.4416 -0.1327 0.0465  -0.1226 425 TYR A CB  
3595  C CG  . TYR A 425 ? 0.2950 0.4110 0.4821 -0.1359 0.0561  -0.1500 425 TYR A CG  
3596  C CD1 . TYR A 425 ? 0.2866 0.4035 0.5009 -0.1523 0.0928  -0.1607 425 TYR A CD1 
3597  C CD2 . TYR A 425 ? 0.2616 0.3874 0.4802 -0.1129 0.0286  -0.1575 425 TYR A CD2 
3598  C CE1 . TYR A 425 ? 0.3809 0.5107 0.6554 -0.1458 0.0984  -0.1818 425 TYR A CE1 
3599  C CE2 . TYR A 425 ? 0.3225 0.4563 0.5902 -0.1032 0.0349  -0.1740 425 TYR A CE2 
3600  C CZ  . TYR A 425 ? 0.3959 0.5334 0.6941 -0.1197 0.0679  -0.1882 425 TYR A CZ  
3601  O OH  . TYR A 425 ? 0.3081 0.4536 0.6548 -0.1095 0.0727  -0.2076 425 TYR A OH  
3602  N N   . TRP A 426 ? 0.3381 0.3982 0.2937 -0.1310 0.0416  -0.0783 426 TRP A N   
3603  C CA  . TRP A 426 ? 0.3289 0.3863 0.2335 -0.1224 0.0218  -0.0689 426 TRP A CA  
3604  C C   . TRP A 426 ? 0.3597 0.4126 0.2307 -0.1284 0.0414  -0.0715 426 TRP A C   
3605  O O   . TRP A 426 ? 0.3886 0.4519 0.2458 -0.1217 0.0277  -0.0792 426 TRP A O   
3606  C CB  . TRP A 426 ? 0.3326 0.3691 0.1906 -0.1186 0.0083  -0.0426 426 TRP A CB  
3607  C CG  . TRP A 426 ? 0.4108 0.4560 0.2906 -0.1078 -0.0208 -0.0406 426 TRP A CG  
3608  C CD1 . TRP A 426 ? 0.4635 0.5023 0.3647 -0.1078 -0.0232 -0.0338 426 TRP A CD1 
3609  C CD2 . TRP A 426 ? 0.3214 0.3800 0.2054 -0.0926 -0.0490 -0.0442 426 TRP A CD2 
3610  N NE1 . TRP A 426 ? 0.3940 0.4443 0.3088 -0.0951 -0.0530 -0.0345 426 TRP A NE1 
3611  C CE2 . TRP A 426 ? 0.3643 0.4207 0.2756 -0.0786 -0.0631 -0.0378 426 TRP A CE2 
3612  C CE3 . TRP A 426 ? 0.3589 0.4158 0.2468 -0.0732 -0.0525 -0.0446 426 TRP A CE3 
3613  C CZ2 . TRP A 426 ? 0.4009 0.4500 0.3359 -0.0460 -0.0747 -0.0365 426 TRP A CZ2 
3614  C CZ3 . TRP A 426 ? 0.4178 0.4633 0.3296 -0.0444 -0.0668 -0.0410 426 TRP A CZ3 
3615  C CH2 . TRP A 426 ? 0.3523 0.3941 0.2843 -0.0325 -0.0752 -0.0386 426 TRP A CH2 
3616  N N   . LYS A 427 ? 0.3927 0.4281 0.2484 -0.1408 0.0741  -0.0649 427 LYS A N   
3617  C CA  . LYS A 427 ? 0.4259 0.4564 0.2500 -0.1461 0.0954  -0.0686 427 LYS A CA  
3618  C C   . LYS A 427 ? 0.4028 0.4617 0.2746 -0.1462 0.0999  -0.0977 427 LYS A C   
3619  O O   . LYS A 427 ? 0.4068 0.4716 0.2563 -0.1426 0.0972  -0.1051 427 LYS A O   
3620  C CB  . LYS A 427 ? 0.4806 0.4845 0.2808 -0.1596 0.1329  -0.0563 427 LYS A CB  
3621  C CG  . LYS A 427 ? 0.5180 0.4874 0.2514 -0.1574 0.1296  -0.0270 427 LYS A CG  
3622  C CD  . LYS A 427 ? 0.5934 0.5321 0.3084 -0.1706 0.1672  -0.0144 427 LYS A CD  
3623  C CE  . LYS A 427 ? 0.7908 0.6998 0.4729 -0.1679 0.1582  0.0107  427 LYS A CE  
3624  N NZ  . LYS A 427 ? 0.9083 0.7992 0.6155 -0.1816 0.1880  0.0152  427 LYS A NZ  
3625  N N   . ILE A 428 ? 0.3800 0.4564 0.3183 -0.1493 0.1057  -0.1158 428 ILE A N   
3626  C CA  . ILE A 428 ? 0.3555 0.4602 0.3438 -0.1464 0.1050  -0.1461 428 ILE A CA  
3627  C C   . ILE A 428 ? 0.3203 0.4373 0.3017 -0.1307 0.0688  -0.1525 428 ILE A C   
3628  O O   . ILE A 428 ? 0.3158 0.4454 0.2994 -0.1267 0.0664  -0.1691 428 ILE A O   
3629  C CB  . ILE A 428 ? 0.3361 0.4573 0.3994 -0.1501 0.1124  -0.1652 428 ILE A CB  
3630  C CG1 . ILE A 428 ? 0.3752 0.4822 0.4467 -0.1681 0.1521  -0.1592 428 ILE A CG1 
3631  C CG2 . ILE A 428 ? 0.3115 0.4623 0.4271 -0.1444 0.1081  -0.1990 428 ILE A CG2 
3632  C CD1 . ILE A 428 ? 0.3609 0.4880 0.5134 -0.1744 0.1655  -0.1842 428 ILE A CD1 
3633  N N   . LEU A 429 ? 0.2971 0.4095 0.2698 -0.1217 0.0409  -0.1394 429 LEU A N   
3634  C CA  . LEU A 429 ? 0.2802 0.4003 0.2451 -0.1069 0.0086  -0.1424 429 LEU A CA  
3635  C C   . LEU A 429 ? 0.2927 0.4006 0.2074 -0.1015 0.0061  -0.1271 429 LEU A C   
3636  O O   . LEU A 429 ? 0.2841 0.3925 0.2092 -0.0861 -0.0044 -0.1266 429 LEU A O   
3637  C CB  . LEU A 429 ? 0.2451 0.3546 0.2115 -0.0930 -0.0145 -0.1207 429 LEU A CB  
3638  C CG  . LEU A 429 ? 0.2219 0.3139 0.1868 -0.0656 -0.0384 -0.1016 429 LEU A CG  
3639  C CD1 . LEU A 429 ? 0.2200 0.3181 0.2154 -0.0553 -0.0393 -0.1135 429 LEU A CD1 
3640  C CD2 . LEU A 429 ? 0.2539 0.3292 0.2234 -0.0550 -0.0541 -0.0844 429 LEU A CD2 
3641  N N   . ILE A 430 ? 0.3641 0.4549 0.2249 -0.1113 0.0158  -0.1109 430 ILE A N   
3642  C CA  . ILE A 430 ? 0.3301 0.4058 0.1572 -0.0995 0.0089  -0.0925 430 ILE A CA  
3643  C C   . ILE A 430 ? 0.3839 0.4666 0.2090 -0.1035 0.0247  -0.1082 430 ILE A C   
3644  O O   . ILE A 430 ? 0.4795 0.5598 0.3078 -0.0891 0.0110  -0.1054 430 ILE A O   
3645  C CB  . ILE A 430 ? 0.3624 0.4146 0.1433 -0.1016 0.0139  -0.0691 430 ILE A CB  
3646  C CG1 . ILE A 430 ? 0.3382 0.3833 0.1278 -0.0897 -0.0076 -0.0525 430 ILE A CG1 
3647  C CG2 . ILE A 430 ? 0.3818 0.4203 0.1371 -0.0891 0.0111  -0.0593 430 ILE A CG2 
3648  C CD1 . ILE A 430 ? 0.3688 0.3948 0.1253 -0.0961 0.0004  -0.0351 430 ILE A CD1 
3649  N N   . GLU A 431 ? 0.3769 0.4644 0.1987 -0.1218 0.0573  -0.1246 431 GLU A N   
3650  C CA  . GLU A 431 ? 0.3942 0.4890 0.2203 -0.1239 0.0747  -0.1397 431 GLU A CA  
3651  C C   . GLU A 431 ? 0.4680 0.5861 0.3465 -0.1143 0.0599  -0.1613 431 GLU A C   
3652  O O   . GLU A 431 ? 0.5414 0.6627 0.4198 -0.1074 0.0575  -0.1659 431 GLU A O   
3653  C CB  . GLU A 431 ? 0.4311 0.5222 0.2597 -0.1406 0.1171  -0.1467 431 GLU A CB  
3654  C CG  . GLU A 431 ? 0.4968 0.5578 0.2667 -0.1434 0.1336  -0.1222 431 GLU A CG  
3655  C CD  . GLU A 431 ? 0.7480 0.8018 0.4884 -0.1287 0.1152  -0.1141 431 GLU A CD  
3656  O OE1 . GLU A 431 ? 0.6813 0.7512 0.4416 -0.1259 0.1154  -0.1322 431 GLU A OE1 
3657  O OE2 . GLU A 431 ? 0.7959 0.8286 0.4983 -0.1177 0.1000  -0.0909 431 GLU A OE2 
3658  N N   . ALA A 432 ? 0.3245 0.4559 0.2492 -0.1108 0.0484  -0.1716 432 ALA A N   
3659  C CA  . ALA A 432 ? 0.2926 0.4373 0.2626 -0.0934 0.0301  -0.1799 432 ALA A CA  
3660  C C   . ALA A 432 ? 0.3399 0.4649 0.2875 -0.0740 0.0033  -0.1552 432 ALA A C   
3661  O O   . ALA A 432 ? 0.4290 0.5528 0.3837 -0.0638 -0.0036 -0.1575 432 ALA A O   
3662  C CB  . ALA A 432 ? 0.2659 0.4213 0.2863 -0.0881 0.0237  -0.1882 432 ALA A CB  
3663  N N   . LYS A 433 ? 0.3686 0.4741 0.2911 -0.0694 -0.0099 -0.1320 433 LYS A N   
3664  C CA  . LYS A 433 ? 0.3650 0.4432 0.2692 -0.0535 -0.0294 -0.1103 433 LYS A CA  
3665  C C   . LYS A 433 ? 0.3887 0.4594 0.2668 -0.0529 -0.0264 -0.1094 433 LYS A C   
3666  O O   . LYS A 433 ? 0.4169 0.4775 0.2947 -0.0445 -0.0366 -0.1046 433 LYS A O   
3667  C CB  . LYS A 433 ? 0.3420 0.4011 0.2292 -0.0489 -0.0393 -0.0900 433 LYS A CB  
3668  C CG  . LYS A 433 ? 0.2967 0.3438 0.1732 -0.0404 -0.0503 -0.0771 433 LYS A CG  
3669  C CD  . LYS A 433 ? 0.2740 0.3210 0.1723 -0.0346 -0.0585 -0.0762 433 LYS A CD  
3670  C CE  . LYS A 433 ? 0.3776 0.4124 0.2649 -0.0301 -0.0659 -0.0656 433 LYS A CE  
3671  N NZ  . LYS A 433 ? 0.4496 0.4792 0.3199 -0.0285 -0.0667 -0.0568 433 LYS A NZ  
3672  N N   . LYS A 434 ? 0.4207 0.5008 0.2762 -0.0655 -0.0087 -0.1159 434 LYS A N   
3673  C CA  . LYS A 434 ? 0.4539 0.5256 0.2831 -0.0632 -0.0051 -0.1150 434 LYS A CA  
3674  C C   . LYS A 434 ? 0.5415 0.6232 0.3921 -0.0601 -0.0048 -0.1309 434 LYS A C   
3675  O O   . LYS A 434 ? 0.5982 0.6645 0.4366 -0.0509 -0.0146 -0.1254 434 LYS A O   
3676  C CB  . LYS A 434 ? 0.4512 0.5247 0.2488 -0.0771 0.0184  -0.1170 434 LYS A CB  
3677  C CG  . LYS A 434 ? 0.6445 0.7006 0.4048 -0.0693 0.0179  -0.1076 434 LYS A CG  
3678  C CD  . LYS A 434 ? 0.7667 0.8256 0.5050 -0.0812 0.0464  -0.1164 434 LYS A CD  
3679  C CE  . LYS A 434 ? 0.5924 0.6329 0.2911 -0.0700 0.0447  -0.1060 434 LYS A CE  
3680  N NZ  . LYS A 434 ? 0.4799 0.5219 0.1857 -0.0605 0.0339  -0.1153 434 LYS A NZ  
3681  N N   . LYS A 435 ? 0.3906 0.6514 0.3893 -0.0233 0.0726  -0.1272 435 LYS A N   
3682  C CA  . LYS A 435 ? 0.4169 0.6631 0.4263 -0.0124 0.0811  -0.1444 435 LYS A CA  
3683  C C   . LYS A 435 ? 0.4046 0.6278 0.4343 0.0010  0.0783  -0.1423 435 LYS A C   
3684  O O   . LYS A 435 ? 0.4171 0.6318 0.4624 0.0137  0.0834  -0.1499 435 LYS A O   
3685  C CB  . LYS A 435 ? 0.4007 0.6640 0.4136 -0.0095 0.0901  -0.1439 435 LYS A CB  
3686  C CG  . LYS A 435 ? 0.4705 0.7577 0.4597 -0.0228 0.0936  -0.1442 435 LYS A CG  
3687  C CD  . LYS A 435 ? 0.4847 0.7921 0.4769 -0.0216 0.1045  -0.1408 435 LYS A CD  
3688  C CE  . LYS A 435 ? 0.6159 0.9297 0.6232 -0.0211 0.1008  -0.1186 435 LYS A CE  
3689  N NZ  . LYS A 435 ? 0.5611 0.8772 0.5947 -0.0099 0.1088  -0.1213 435 LYS A NZ  
3690  N N   . ALA A 436 ? 0.2984 0.5136 0.3283 -0.0008 0.0706  -0.1316 436 ALA A N   
3691  C CA  . ALA A 436 ? 0.2563 0.4515 0.3014 0.0114  0.0678  -0.1277 436 ALA A CA  
3692  C C   . ALA A 436 ? 0.2531 0.4231 0.3024 0.0177  0.0715  -0.1463 436 ALA A C   
3693  O O   . ALA A 436 ? 0.2644 0.4280 0.3017 0.0079  0.0737  -0.1603 436 ALA A O   
3694  C CB  . ALA A 436 ? 0.1754 0.3704 0.2167 0.0077  0.0609  -0.1119 436 ALA A CB  
3695  N N   . LYS A 437 ? 0.2703 0.4240 0.3374 0.0339  0.0707  -0.1469 437 LYS A N   
3696  C CA  . LYS A 437 ? 0.2676 0.3888 0.3423 0.0437  0.0725  -0.1621 437 LYS A CA  
3697  C C   . LYS A 437 ? 0.2456 0.3434 0.3279 0.0525  0.0654  -0.1517 437 LYS A C   
3698  O O   . LYS A 437 ? 0.2886 0.3525 0.3633 0.0469  0.0622  -0.1506 437 LYS A O   
3699  C CB  . LYS A 437 ? 0.3393 0.4569 0.4300 0.0587  0.0768  -0.1716 437 LYS A CB  
3700  C CG  . LYS A 437 ? 0.2956 0.4401 0.3788 0.0516  0.0849  -0.1778 437 LYS A CG  
3701  C CD  . LYS A 437 ? 0.3249 0.4536 0.4100 0.0596  0.0935  -0.1999 437 LYS A CD  
3702  C CE  . LYS A 437 ? 0.4402 0.5480 0.5034 0.0464  0.0944  -0.2166 437 LYS A CE  
3703  N NZ  . LYS A 437 ? 0.3590 0.4962 0.3986 0.0272  0.0964  -0.2169 437 LYS A NZ  
3704  N N   . ASN A 438 ? 0.2237 0.3328 0.3155 0.0617  0.0588  -0.1358 438 ASN A N   
3705  C CA  . ASN A 438 ? 0.2276 0.3108 0.3169 0.0680  0.0476  -0.1173 438 ASN A CA  
3706  C C   . ASN A 438 ? 0.3015 0.3973 0.3747 0.0577  0.0440  -0.0998 438 ASN A C   
3707  O O   . ASN A 438 ? 0.3393 0.4605 0.4062 0.0466  0.0486  -0.1006 438 ASN A O   
3708  C CB  . ASN A 438 ? 0.2311 0.3149 0.3422 0.0880  0.0401  -0.1144 438 ASN A CB  
3709  C CG  . ASN A 438 ? 0.2984 0.4242 0.4265 0.0904  0.0432  -0.1189 438 ASN A CG  
3710  O OD1 . ASN A 438 ? 0.2732 0.4161 0.3991 0.0869  0.0370  -0.1072 438 ASN A OD1 
3711  N ND2 . ASN A 438 ? 0.3856 0.5195 0.5229 0.0908  0.0511  -0.1290 438 ASN A ND2 
3712  N N   . ASP A 439 ? 0.3090 0.3861 0.3742 0.0626  0.0355  -0.0838 439 ASP A N   
3713  C CA  . ASP A 439 ? 0.2716 0.3549 0.3197 0.0553  0.0340  -0.0695 439 ASP A CA  
3714  C C   . ASP A 439 ? 0.2203 0.3262 0.2714 0.0594  0.0294  -0.0663 439 ASP A C   
3715  O O   . ASP A 439 ? 0.2304 0.3390 0.2677 0.0560  0.0284  -0.0572 439 ASP A O   
3716  C CB  . ASP A 439 ? 0.3104 0.3644 0.3428 0.0576  0.0290  -0.0544 439 ASP A CB  
3717  C CG  . ASP A 439 ? 0.5891 0.6276 0.6130 0.0439  0.0360  -0.0511 439 ASP A CG  
3718  O OD1 . ASP A 439 ? 0.5552 0.6120 0.5823 0.0317  0.0428  -0.0586 439 ASP A OD1 
3719  O OD2 . ASP A 439 ? 0.7640 0.7733 0.7782 0.0440  0.0338  -0.0395 439 ASP A OD2 
3720  N N   . TYR A 440 ? 0.2486 0.3708 0.3193 0.0662  0.0273  -0.0743 440 TYR A N   
3721  C CA  . TYR A 440 ? 0.1788 0.3219 0.2551 0.0657  0.0226  -0.0712 440 TYR A CA  
3722  C C   . TYR A 440 ? 0.1321 0.2926 0.2018 0.0536  0.0297  -0.0697 440 TYR A C   
3723  O O   . TYR A 440 ? 0.2030 0.3711 0.2722 0.0514  0.0255  -0.0643 440 TYR A O   
3724  C CB  . TYR A 440 ? 0.1776 0.3409 0.2821 0.0729  0.0207  -0.0793 440 TYR A CB  
3725  C CG  . TYR A 440 ? 0.2021 0.3587 0.3155 0.0848  0.0054  -0.0741 440 TYR A CG  
3726  C CD1 . TYR A 440 ? 0.1753 0.3371 0.2841 0.0821  -0.0059 -0.0675 440 TYR A CD1 
3727  C CD2 . TYR A 440 ? 0.2608 0.4040 0.3865 0.0989  0.0004  -0.0758 440 TYR A CD2 
3728  C CE1 . TYR A 440 ? 0.1685 0.3267 0.2826 0.0914  -0.0230 -0.0632 440 TYR A CE1 
3729  C CE2 . TYR A 440 ? 0.2485 0.3883 0.3823 0.1104  -0.0168 -0.0685 440 TYR A CE2 
3730  C CZ  . TYR A 440 ? 0.2284 0.3778 0.3551 0.1057  -0.0291 -0.0623 440 TYR A CZ  
3731  O OH  . TYR A 440 ? 0.4054 0.5539 0.5374 0.1157  -0.0492 -0.0555 440 TYR A OH  
3732  N N   . ILE A 441 ? 0.1474 0.3128 0.2121 0.0455  0.0387  -0.0740 441 ILE A N   
3733  C CA  . ILE A 441 ? 0.1224 0.2978 0.1775 0.0339  0.0407  -0.0665 441 ILE A CA  
3734  C C   . ILE A 441 ? 0.1302 0.2997 0.1747 0.0359  0.0392  -0.0573 441 ILE A C   
3735  O O   . ILE A 441 ? 0.2047 0.3799 0.2462 0.0322  0.0380  -0.0493 441 ILE A O   
3736  C CB  . ILE A 441 ? 0.1292 0.3098 0.1787 0.0237  0.0461  -0.0722 441 ILE A CB  
3737  C CG1 . ILE A 441 ? 0.1245 0.3212 0.1686 0.0140  0.0452  -0.0649 441 ILE A CG1 
3738  C CG2 . ILE A 441 ? 0.2354 0.4107 0.2782 0.0206  0.0491  -0.0727 441 ILE A CG2 
3739  C CD1 . ILE A 441 ? 0.1245 0.3314 0.1756 0.0136  0.0458  -0.0646 441 ILE A CD1 
3740  N N   . LEU A 442 ? 0.1323 0.2809 0.1680 0.0407  0.0375  -0.0545 442 LEU A N   
3741  C CA  . LEU A 442 ? 0.1506 0.2909 0.1726 0.0429  0.0374  -0.0453 442 LEU A CA  
3742  C C   . LEU A 442 ? 0.1733 0.3098 0.1915 0.0496  0.0305  -0.0439 442 LEU A C   
3743  O O   . LEU A 442 ? 0.1618 0.2985 0.1729 0.0511  0.0321  -0.0401 442 LEU A O   
3744  C CB  . LEU A 442 ? 0.1547 0.2740 0.1646 0.0445  0.0384  -0.0407 442 LEU A CB  
3745  C CG  . LEU A 442 ? 0.1609 0.2793 0.1735 0.0342  0.0452  -0.0406 442 LEU A CG  
3746  C CD1 . LEU A 442 ? 0.1869 0.2799 0.1872 0.0343  0.0459  -0.0325 442 LEU A CD1 
3747  C CD2 . LEU A 442 ? 0.1611 0.3020 0.1771 0.0263  0.0513  -0.0367 442 LEU A CD2 
3748  N N   . VAL A 443 ? 0.1526 0.2858 0.1775 0.0540  0.0222  -0.0481 443 VAL A N   
3749  C CA  . VAL A 443 ? 0.1434 0.2733 0.1665 0.0572  0.0129  -0.0486 443 VAL A CA  
3750  C C   . VAL A 443 ? 0.1563 0.2997 0.1905 0.0506  0.0148  -0.0483 443 VAL A C   
3751  O O   . VAL A 443 ? 0.2696 0.4037 0.2971 0.0513  0.0107  -0.0475 443 VAL A O   
3752  C CB  . VAL A 443 ? 0.1499 0.2805 0.1847 0.0621  0.0017  -0.0522 443 VAL A CB  
3753  C CG1 . VAL A 443 ? 0.1890 0.3147 0.2189 0.0629  -0.0113 -0.0535 443 VAL A CG1 
3754  C CG2 . VAL A 443 ? 0.1843 0.2987 0.2097 0.0693  -0.0008 -0.0491 443 VAL A CG2 
3755  N N   . ALA A 444 ? 0.1378 0.3007 0.1868 0.0440  0.0210  -0.0490 444 ALA A N   
3756  C CA  . ALA A 444 ? 0.1191 0.2950 0.1765 0.0363  0.0228  -0.0445 444 ALA A CA  
3757  C C   . ALA A 444 ? 0.1336 0.3058 0.1816 0.0362  0.0263  -0.0367 444 ALA A C   
3758  O O   . ALA A 444 ? 0.2108 0.3865 0.2638 0.0319  0.0255  -0.0297 444 ALA A O   
3759  C CB  . ALA A 444 ? 0.1033 0.3038 0.1733 0.0290  0.0299  -0.0470 444 ALA A CB  
3760  N N   . GLU A 445 ? 0.1450 0.3113 0.1822 0.0410  0.0303  -0.0361 445 GLU A N   
3761  C CA  . GLU A 445 ? 0.1408 0.3094 0.1754 0.0435  0.0340  -0.0289 445 GLU A CA  
3762  C C   . GLU A 445 ? 0.1314 0.2797 0.1568 0.0534  0.0325  -0.0297 445 GLU A C   
3763  O O   . GLU A 445 ? 0.2061 0.3563 0.2318 0.0595  0.0373  -0.0253 445 GLU A O   
3764  C CB  . GLU A 445 ? 0.2305 0.4065 0.2625 0.0407  0.0397  -0.0275 445 GLU A CB  
3765  C CG  . GLU A 445 ? 0.1544 0.3400 0.1901 0.0295  0.0392  -0.0299 445 GLU A CG  
3766  C CD  . GLU A 445 ? 0.1473 0.3357 0.1815 0.0241  0.0427  -0.0303 445 GLU A CD  
3767  O OE1 . GLU A 445 ? 0.1825 0.3638 0.2130 0.0283  0.0466  -0.0281 445 GLU A OE1 
3768  O OE2 . GLU A 445 ? 0.2424 0.4430 0.2784 0.0147  0.0423  -0.0337 445 GLU A OE2 
3769  N N   . GLY A 446 ? 0.1904 0.3212 0.2080 0.0557  0.0256  -0.0364 446 GLY A N   
3770  C CA  . GLY A 446 ? 0.1838 0.2926 0.1871 0.0642  0.0235  -0.0412 446 GLY A CA  
3771  C C   . GLY A 446 ? 0.2142 0.3144 0.2268 0.0652  0.0215  -0.0384 446 GLY A C   
3772  O O   . GLY A 446 ? 0.2325 0.3384 0.2600 0.0563  0.0169  -0.0329 446 GLY A O   
3773  N N   . SER A 447 ? 0.1940 0.2790 0.1974 0.0767  0.0259  -0.0418 447 SER A N   
3774  C CA  . SER A 447 ? 0.2398 0.3099 0.2533 0.0811  0.0240  -0.0388 447 SER A CA  
3775  C C   . SER A 447 ? 0.2291 0.2742 0.2423 0.0735  0.0119  -0.0447 447 SER A C   
3776  O O   . SER A 447 ? 0.2464 0.2800 0.2734 0.0704  0.0079  -0.0373 447 SER A O   
3777  C CB  . SER A 447 ? 0.2515 0.3099 0.2567 0.0985  0.0332  -0.0450 447 SER A CB  
3778  O OG  . SER A 447 ? 0.3166 0.3580 0.2943 0.1032  0.0343  -0.0602 447 SER A OG  
3779  N N   . ASP A 448 ? 0.2368 0.2738 0.2359 0.0691  0.0044  -0.0562 448 ASP A N   
3780  C CA  . ASP A 448 ? 0.2607 0.2744 0.2601 0.0606  -0.0090 -0.0642 448 ASP A CA  
3781  C C   . ASP A 448 ? 0.2455 0.2731 0.2712 0.0440  -0.0147 -0.0530 448 ASP A C   
3782  O O   . ASP A 448 ? 0.2679 0.2756 0.3019 0.0345  -0.0239 -0.0544 448 ASP A O   
3783  C CB  . ASP A 448 ? 0.2738 0.2824 0.2523 0.0597  -0.0183 -0.0777 448 ASP A CB  
3784  C CG  . ASP A 448 ? 0.3165 0.3132 0.2629 0.0744  -0.0107 -0.0875 448 ASP A CG  
3785  O OD1 . ASP A 448 ? 0.3068 0.3228 0.2465 0.0794  -0.0012 -0.0814 448 ASP A OD1 
3786  O OD2 . ASP A 448 ? 0.3839 0.3512 0.3108 0.0800  -0.0133 -0.1019 448 ASP A OD2 
3787  N N   . TRP A 449 ? 0.2786 0.3393 0.3169 0.0391  -0.0087 -0.0428 449 TRP A N   
3788  C CA  . TRP A 449 ? 0.2529 0.3315 0.3136 0.0234  -0.0105 -0.0326 449 TRP A CA  
3789  C C   . TRP A 449 ? 0.2327 0.3040 0.3018 0.0201  -0.0074 -0.0172 449 TRP A C   
3790  O O   . TRP A 449 ? 0.3113 0.3836 0.3952 0.0052  -0.0108 -0.0079 449 TRP A O   
3791  C CB  . TRP A 449 ? 0.1959 0.3105 0.2637 0.0208  -0.0036 -0.0300 449 TRP A CB  
3792  C CG  . TRP A 449 ? 0.1966 0.3139 0.2544 0.0287  -0.0059 -0.0412 449 TRP A CG  
3793  C CD1 . TRP A 449 ? 0.1808 0.3041 0.2268 0.0377  0.0014  -0.0423 449 TRP A CD1 
3794  C CD2 . TRP A 449 ? 0.2696 0.3829 0.3286 0.0273  -0.0180 -0.0506 449 TRP A CD2 
3795  N NE1 . TRP A 449 ? 0.1723 0.2921 0.2101 0.0427  -0.0046 -0.0499 449 TRP A NE1 
3796  C CE2 . TRP A 449 ? 0.2049 0.3201 0.2501 0.0374  -0.0174 -0.0551 449 TRP A CE2 
3797  C CE3 . TRP A 449 ? 0.2728 0.3819 0.3445 0.0170  -0.0307 -0.0546 449 TRP A CE3 
3798  C CZ2 . TRP A 449 ? 0.1952 0.3085 0.2369 0.0399  -0.0302 -0.0618 449 TRP A CZ2 
3799  C CZ3 . TRP A 449 ? 0.2637 0.3749 0.3343 0.0185  -0.0440 -0.0635 449 TRP A CZ3 
3800  C CH2 . TRP A 449 ? 0.2430 0.3564 0.2976 0.0310  -0.0442 -0.0663 449 TRP A CH2 
3801  N N   . PHE A 450 ? 0.2141 0.2801 0.2760 0.0333  -0.0014 -0.0124 450 PHE A N   
3802  C CA  . PHE A 450 ? 0.2270 0.2868 0.2976 0.0334  -0.0007 0.0051  450 PHE A CA  
3803  C C   . PHE A 450 ? 0.2659 0.2817 0.3360 0.0417  -0.0062 0.0024  450 PHE A C   
3804  O O   . PHE A 450 ? 0.2867 0.2878 0.3670 0.0397  -0.0091 0.0187  450 PHE A O   
3805  C CB  . PHE A 450 ? 0.2091 0.2935 0.2782 0.0435  0.0069  0.0133  450 PHE A CB  
3806  C CG  . PHE A 450 ? 0.1781 0.2990 0.2448 0.0361  0.0123  0.0116  450 PHE A CG  
3807  C CD1 . PHE A 450 ? 0.1702 0.3159 0.2414 0.0225  0.0137  0.0233  450 PHE A CD1 
3808  C CD2 . PHE A 450 ? 0.1633 0.2910 0.2211 0.0425  0.0165  -0.0020 450 PHE A CD2 
3809  C CE1 . PHE A 450 ? 0.1486 0.3237 0.2163 0.0169  0.0195  0.0176  450 PHE A CE1 
3810  C CE2 . PHE A 450 ? 0.1797 0.3335 0.2364 0.0363  0.0209  -0.0048 450 PHE A CE2 
3811  C CZ  . PHE A 450 ? 0.1666 0.3433 0.2287 0.0242  0.0225  0.0031  450 PHE A CZ  
3812  N N   . TRP A 451 ? 0.2863 0.2786 0.3427 0.0513  -0.0079 -0.0179 451 TRP A N   
3813  C CA  . TRP A 451 ? 0.3739 0.3190 0.4269 0.0586  -0.0132 -0.0267 451 TRP A CA  
3814  C C   . TRP A 451 ? 0.3959 0.3177 0.4592 0.0381  -0.0252 -0.0242 451 TRP A C   
3815  O O   . TRP A 451 ? 0.3876 0.2737 0.4596 0.0374  -0.0298 -0.0169 451 TRP A O   
3816  C CB  . TRP A 451 ? 0.3766 0.3060 0.4056 0.0715  -0.0114 -0.0518 451 TRP A CB  
3817  C CG  . TRP A 451 ? 0.4068 0.2878 0.4273 0.0844  -0.0130 -0.0663 451 TRP A CG  
3818  C CD1 . TRP A 451 ? 0.4901 0.3606 0.5068 0.1084  -0.0020 -0.0718 451 TRP A CD1 
3819  C CD2 . TRP A 451 ? 0.4878 0.3243 0.5037 0.0743  -0.0259 -0.0798 451 TRP A CD2 
3820  N NE1 . TRP A 451 ? 0.5352 0.3545 0.5435 0.1163  -0.0060 -0.0893 451 TRP A NE1 
3821  C CE2 . TRP A 451 ? 0.5014 0.2964 0.5075 0.0943  -0.0217 -0.0949 451 TRP A CE2 
3822  C CE3 . TRP A 451 ? 0.6375 0.4666 0.6592 0.0497  -0.0407 -0.0814 451 TRP A CE3 
3823  C CZ2 . TRP A 451 ? 0.5809 0.3213 0.5789 0.0899  -0.0325 -0.1133 451 TRP A CZ2 
3824  C CZ3 . TRP A 451 ? 0.6730 0.4519 0.6894 0.0428  -0.0527 -0.0975 451 TRP A CZ3 
3825  C CH2 . TRP A 451 ? 0.6077 0.3397 0.6103 0.0625  -0.0490 -0.1141 451 TRP A CH2 
3826  N N   . TRP A 452 ? 0.4984 0.4409 0.5645 0.0209  -0.0306 -0.0287 452 TRP A N   
3827  C CA  . TRP A 452 ? 0.5088 0.4351 0.5873 -0.0008 -0.0427 -0.0301 452 TRP A CA  
3828  C C   . TRP A 452 ? 0.5305 0.4741 0.6322 -0.0200 -0.0408 -0.0048 452 TRP A C   
3829  O O   . TRP A 452 ? 0.6620 0.6080 0.7799 -0.0422 -0.0481 -0.0028 452 TRP A O   
3830  C CB  . TRP A 452 ? 0.5460 0.4934 0.6218 -0.0092 -0.0503 -0.0459 452 TRP A CB  
3831  C CG  . TRP A 452 ? 0.6224 0.5448 0.6709 0.0030  -0.0569 -0.0706 452 TRP A CG  
3832  C CD1 . TRP A 452 ? 0.6686 0.6044 0.6942 0.0198  -0.0506 -0.0799 452 TRP A CD1 
3833  C CD2 . TRP A 452 ? 0.6728 0.5519 0.7103 -0.0025 -0.0708 -0.0894 452 TRP A CD2 
3834  N NE1 . TRP A 452 ? 0.6454 0.5518 0.6435 0.0260  -0.0586 -0.1020 452 TRP A NE1 
3835  C CE2 . TRP A 452 ? 0.6536 0.5245 0.6575 0.0129  -0.0716 -0.1102 452 TRP A CE2 
3836  C CE3 . TRP A 452 ? 0.7152 0.5601 0.7666 -0.0205 -0.0828 -0.0908 452 TRP A CE3 
3837  C CZ2 . TRP A 452 ? 0.7052 0.5363 0.6852 0.0118  -0.0841 -0.1347 452 TRP A CZ2 
3838  C CZ3 . TRP A 452 ? 0.8198 0.6221 0.8512 -0.0223 -0.0964 -0.1161 452 TRP A CZ3 
3839  C CH2 . TRP A 452 ? 0.6824 0.4789 0.6767 -0.0057 -0.0970 -0.1389 452 TRP A CH2 
3840  N N   . GLN A 453 ? 0.4733 0.4322 0.5767 -0.0134 -0.0315 0.0152  453 GLN A N   
3841  C CA  . GLN A 453 ? 0.4950 0.4762 0.6128 -0.0319 -0.0280 0.0406  453 GLN A CA  
3842  C C   . GLN A 453 ? 0.5794 0.5170 0.7049 -0.0384 -0.0342 0.0587  453 GLN A C   
3843  O O   . GLN A 453 ? 0.5687 0.4876 0.6897 -0.0224 -0.0333 0.0705  453 GLN A O   
3844  C CB  . GLN A 453 ? 0.4684 0.4907 0.5798 -0.0242 -0.0170 0.0531  453 GLN A CB  
3845  C CG  . GLN A 453 ? 0.5695 0.6417 0.6870 -0.0402 -0.0092 0.0569  453 GLN A CG  
3846  C CD  . GLN A 453 ? 0.7201 0.7993 0.8524 -0.0656 -0.0083 0.0764  453 GLN A CD  
3847  O OE1 . GLN A 453 ? 0.8108 0.8535 0.9494 -0.0742 -0.0154 0.0893  453 GLN A OE1 
3848  N NE2 . GLN A 453 ? 0.5485 0.6745 0.6867 -0.0778 0.0018  0.0786  453 GLN A NE2 
3849  N N   . GLY A 454 ? 0.6875 0.6082 0.8273 -0.0621 -0.0414 0.0615  454 GLY A N   
3850  C CA  . GLY A 454 ? 0.8499 0.7395 1.0011 -0.0780 -0.0455 0.0872  454 GLY A CA  
3851  C C   . GLY A 454 ? 0.9912 0.8168 1.1389 -0.0627 -0.0529 0.0909  454 GLY A C   
3852  O O   . GLY A 454 ? 0.8893 0.6888 1.0452 -0.0727 -0.0559 0.1186  454 GLY A O   
3853  N N   . GLU A 455 ? 0.9830 0.7819 1.1187 -0.0380 -0.0552 0.0645  455 GLU A N   
3854  C CA  . GLU A 455 ? 1.0727 0.8098 1.2081 -0.0201 -0.0605 0.0646  455 GLU A CA  
3855  C C   . GLU A 455 ? 1.1081 0.7848 1.2518 -0.0391 -0.0733 0.0572  455 GLU A C   
3856  O O   . GLU A 455 ? 1.0865 0.7126 1.2397 -0.0399 -0.0789 0.0751  455 GLU A O   
3857  C CB  . GLU A 455 ? 0.9443 0.6757 1.0640 0.0127  -0.0555 0.0373  455 GLU A CB  
3858  C CG  . GLU A 455 ? 1.0880 0.7530 1.2080 0.0344  -0.0593 0.0275  455 GLU A CG  
3859  C CD  . GLU A 455 ? 1.1986 0.8530 1.3333 0.0511  -0.0582 0.0586  455 GLU A CD  
3860  O OE1 . GLU A 455 ? 1.0908 0.7396 1.2375 0.0321  -0.0639 0.0909  455 GLU A OE1 
3861  O OE2 . GLU A 455 ? 1.0633 0.7179 1.1983 0.0831  -0.0517 0.0521  455 GLU A OE2 
3862  N N   . GLU A 456 ? 1.1114 0.7917 1.2528 -0.0554 -0.0796 0.0318  456 GLU A N   
3863  C CA  . GLU A 456 ? 1.0514 0.6795 1.2014 -0.0785 -0.0941 0.0209  456 GLU A CA  
3864  C C   . GLU A 456 ? 0.9908 0.6562 1.1430 -0.0995 -0.1005 0.0008  456 GLU A C   
3865  O O   . GLU A 456 ? 1.0504 0.7482 1.1856 -0.0840 -0.0973 -0.0204 456 GLU A O   
3866  C CB  . GLU A 456 ? 1.0523 0.6081 1.1876 -0.0568 -0.1004 -0.0058 456 GLU A CB  
3867  C CG  . GLU A 456 ? 1.2004 0.6944 1.3412 -0.0813 -0.1174 -0.0227 456 GLU A CG  
3868  C CD  . GLU A 456 ? 1.2055 0.6531 1.3699 -0.1012 -0.1230 0.0091  456 GLU A CD  
3869  O OE1 . GLU A 456 ? 1.0052 0.4100 1.1704 -0.0786 -0.1197 0.0231  456 GLU A OE1 
3870  O OE2 . GLU A 456 ? 1.1479 0.6025 1.3323 -0.1396 -0.1309 0.0214  456 GLU A OE2 
3871  N N   . LYS A 457 ? 0.7933 0.4560 0.9688 -0.1352 -0.1098 0.0096  457 LYS A N   
3872  C CA  . LYS A 457 ? 0.8716 0.5799 1.0586 -0.1564 -0.1170 -0.0047 457 LYS A CA  
3873  C C   . LYS A 457 ? 0.8822 0.5714 1.0450 -0.1436 -0.1291 -0.0451 457 LYS A C   
3874  O O   . LYS A 457 ? 0.9004 0.5252 1.0509 -0.1434 -0.1410 -0.0656 457 LYS A O   
3875  C CB  . LYS A 457 ? 0.8996 0.6009 1.1196 -0.1981 -0.1268 0.0091  457 LYS A CB  
3876  C CG  . LYS A 457 ? 0.8893 0.6425 1.1294 -0.2202 -0.1363 -0.0055 457 LYS A CG  
3877  C CD  . LYS A 457 ? 0.7725 0.5724 1.0530 -0.2549 -0.1303 0.0235  457 LYS A CD  
3878  C CE  . LYS A 457 ? 0.8079 0.6485 1.1172 -0.2802 -0.1442 0.0076  457 LYS A CE  
3879  N NZ  . LYS A 457 ? 0.7400 0.5319 1.0299 -0.2795 -0.1647 -0.0261 457 LYS A NZ  
3880  N N   . ALA A 458 ? 0.9280 0.6717 1.0819 -0.1331 -0.1261 -0.0563 458 ALA A N   
3881  C CA  . ALA A 458 ? 0.8321 0.5683 0.9533 -0.1133 -0.1324 -0.0888 458 ALA A CA  
3882  C C   . ALA A 458 ? 0.8022 0.5892 0.9333 -0.1278 -0.1442 -0.0988 458 ALA A C   
3883  O O   . ALA A 458 ? 0.8102 0.6465 0.9754 -0.1465 -0.1420 -0.0802 458 ALA A O   
3884  C CB  . ALA A 458 ? 0.6539 0.4052 0.7513 -0.0784 -0.1139 -0.0862 458 ALA A CB  
3885  N N   . PRO A 459 ? 0.7821 0.5605 0.8846 -0.1193 -0.1571 -0.1277 459 PRO A N   
3886  C CA  . PRO A 459 ? 0.6322 0.4557 0.7478 -0.1346 -0.1739 -0.1359 459 PRO A CA  
3887  C C   . PRO A 459 ? 0.5688 0.4584 0.6931 -0.1210 -0.1620 -0.1222 459 PRO A C   
3888  O O   . PRO A 459 ? 0.6341 0.5279 0.7322 -0.0943 -0.1471 -0.1212 459 PRO A O   
3889  C CB  . PRO A 459 ? 0.6302 0.4190 0.7025 -0.1267 -0.1913 -0.1697 459 PRO A CB  
3890  C CG  . PRO A 459 ? 0.7439 0.4839 0.7777 -0.0993 -0.1760 -0.1791 459 PRO A CG  
3891  C CD  . PRO A 459 ? 0.7478 0.4868 0.8035 -0.0919 -0.1543 -0.1515 459 PRO A CD  
3892  N N   . PHE A 460 ? 0.5691 0.5106 0.7334 -0.1401 -0.1685 -0.1124 460 PHE A N   
3893  C CA  . PHE A 460 ? 0.4344 0.4384 0.6134 -0.1286 -0.1596 -0.1023 460 PHE A CA  
3894  C C   . PHE A 460 ? 0.3948 0.4100 0.5693 -0.1113 -0.1323 -0.0837 460 PHE A C   
3895  O O   . PHE A 460 ? 0.4037 0.4386 0.5614 -0.0892 -0.1229 -0.0840 460 PHE A O   
3896  C CB  . PHE A 460 ? 0.4342 0.4460 0.5836 -0.1109 -0.1727 -0.1200 460 PHE A CB  
3897  C CG  . PHE A 460 ? 0.5530 0.5599 0.7033 -0.1279 -0.2030 -0.1387 460 PHE A CG  
3898  C CD1 . PHE A 460 ? 0.5743 0.5238 0.6865 -0.1307 -0.2167 -0.1609 460 PHE A CD1 
3899  C CD2 . PHE A 460 ? 0.5448 0.6063 0.7346 -0.1402 -0.2185 -0.1355 460 PHE A CD2 
3900  C CE1 . PHE A 460 ? 0.5784 0.5259 0.6829 -0.1456 -0.2388 -0.1754 460 PHE A CE1 
3901  C CE2 . PHE A 460 ? 0.5588 0.6205 0.7413 -0.1532 -0.2386 -0.1464 460 PHE A CE2 
3902  C CZ  . PHE A 460 ? 0.6444 0.6496 0.7833 -0.1572 -0.2491 -0.1664 460 PHE A CZ  
3903  N N   . VAL A 461 ? 0.5133 0.5139 0.7017 -0.1228 -0.1210 -0.0665 461 VAL A N   
3904  C CA  . VAL A 461 ? 0.4453 0.4629 0.6316 -0.1106 -0.0978 -0.0470 461 VAL A CA  
3905  C C   . VAL A 461 ? 0.4134 0.4967 0.6283 -0.1144 -0.0876 -0.0367 461 VAL A C   
3906  O O   . VAL A 461 ? 0.3851 0.4913 0.5898 -0.0970 -0.0725 -0.0318 461 VAL A O   
3907  C CB  . VAL A 461 ? 0.4045 0.3891 0.5962 -0.1224 -0.0912 -0.0284 461 VAL A CB  
3908  C CG1 . VAL A 461 ? 0.3637 0.3800 0.5592 -0.1174 -0.0702 -0.0048 461 VAL A CG1 
3909  C CG2 . VAL A 461 ? 0.4355 0.3554 0.5963 -0.1073 -0.0957 -0.0393 461 VAL A CG2 
3910  N N   . GLU A 462 ? 0.3282 0.4435 0.5812 -0.1372 -0.0955 -0.0348 462 GLU A N   
3911  C CA  . GLU A 462 ? 0.2911 0.4720 0.5763 -0.1390 -0.0845 -0.0278 462 GLU A CA  
3912  C C   . GLU A 462 ? 0.2616 0.4635 0.5345 -0.1131 -0.0858 -0.0408 462 GLU A C   
3913  O O   . GLU A 462 ? 0.2296 0.4721 0.5144 -0.1035 -0.0702 -0.0360 462 GLU A O   
3914  C CB  . GLU A 462 ? 0.3514 0.5657 0.6843 -0.1666 -0.0956 -0.0265 462 GLU A CB  
3915  C CG  . GLU A 462 ? 0.6576 0.8488 1.0058 -0.1970 -0.0955 -0.0116 462 GLU A CG  
3916  C CD  . GLU A 462 ? 0.9254 1.1267 1.3113 -0.2255 -0.1168 -0.0181 462 GLU A CD  
3917  O OE1 . GLU A 462 ? 1.0533 1.2138 1.4390 -0.2477 -0.1225 -0.0129 462 GLU A OE1 
3918  O OE2 . GLU A 462 ? 0.8170 1.0616 1.2189 -0.2192 -0.1230 -0.0301 462 GLU A OE2 
3919  N N   . VAL A 463 ? 0.2776 0.4503 0.5248 -0.1019 -0.1038 -0.0573 463 VAL A N   
3920  C CA  . VAL A 463 ? 0.2574 0.4446 0.4898 -0.0784 -0.1064 -0.0662 463 VAL A CA  
3921  C C   . VAL A 463 ? 0.2387 0.4091 0.4372 -0.0574 -0.0880 -0.0625 463 VAL A C   
3922  O O   . VAL A 463 ? 0.2114 0.4075 0.4119 -0.0428 -0.0783 -0.0610 463 VAL A O   
3923  C CB  . VAL A 463 ? 0.2881 0.4514 0.4990 -0.0757 -0.1322 -0.0829 463 VAL A CB  
3924  C CG1 . VAL A 463 ? 0.2758 0.4415 0.4592 -0.0505 -0.1333 -0.0879 463 VAL A CG1 
3925  C CG2 . VAL A 463 ? 0.3014 0.4959 0.5531 -0.0958 -0.1533 -0.0867 463 VAL A CG2 
3926  N N   . PHE A 464 ? 0.2560 0.3835 0.4259 -0.0552 -0.0833 -0.0614 464 PHE A N   
3927  C CA  . PHE A 464 ? 0.2389 0.3563 0.3824 -0.0370 -0.0668 -0.0569 464 PHE A CA  
3928  C C   . PHE A 464 ? 0.2356 0.3854 0.3966 -0.0402 -0.0481 -0.0421 464 PHE A C   
3929  O O   . PHE A 464 ? 0.2473 0.4059 0.3949 -0.0263 -0.0361 -0.0404 464 PHE A O   
3930  C CB  . PHE A 464 ? 0.3126 0.3817 0.4289 -0.0325 -0.0662 -0.0586 464 PHE A CB  
3931  C CG  . PHE A 464 ? 0.3304 0.3677 0.4152 -0.0218 -0.0781 -0.0766 464 PHE A CG  
3932  C CD1 . PHE A 464 ? 0.4174 0.4303 0.5004 -0.0338 -0.0965 -0.0894 464 PHE A CD1 
3933  C CD2 . PHE A 464 ? 0.2899 0.3228 0.3453 -0.0017 -0.0706 -0.0810 464 PHE A CD2 
3934  C CE1 . PHE A 464 ? 0.4194 0.4036 0.4667 -0.0244 -0.1071 -0.1080 464 PHE A CE1 
3935  C CE2 . PHE A 464 ? 0.4466 0.4531 0.4683 0.0074  -0.0791 -0.0968 464 PHE A CE2 
3936  C CZ  . PHE A 464 ? 0.4793 0.4614 0.4943 -0.0032 -0.0973 -0.1112 464 PHE A CZ  
3937  N N   . ASP A 465 ? 0.2784 0.4461 0.4674 -0.0600 -0.0451 -0.0314 465 ASP A N   
3938  C CA  . ASP A 465 ? 0.2038 0.4085 0.4064 -0.0644 -0.0266 -0.0189 465 ASP A CA  
3939  C C   . ASP A 465 ? 0.1696 0.4181 0.3916 -0.0569 -0.0219 -0.0269 465 ASP A C   
3940  O O   . ASP A 465 ? 0.1764 0.4418 0.3903 -0.0461 -0.0077 -0.0271 465 ASP A O   
3941  C CB  . ASP A 465 ? 0.2439 0.4573 0.4694 -0.0894 -0.0232 -0.0032 465 ASP A CB  
3942  C CG  . ASP A 465 ? 0.2994 0.5542 0.5337 -0.0956 -0.0026 0.0097  465 ASP A CG  
3943  O OD1 . ASP A 465 ? 0.2381 0.4826 0.4488 -0.0918 0.0070  0.0209  465 ASP A OD1 
3944  O OD2 . ASP A 465 ? 0.3142 0.6142 0.5790 -0.1040 0.0040  0.0082  465 ASP A OD2 
3945  N N   . LYS A 466 ? 0.1905 0.4571 0.4398 -0.0619 -0.0349 -0.0345 466 LYS A N   
3946  C CA  . LYS A 466 ? 0.1540 0.4628 0.4285 -0.0518 -0.0320 -0.0416 466 LYS A CA  
3947  C C   . LYS A 466 ? 0.1910 0.4845 0.4389 -0.0273 -0.0321 -0.0501 466 LYS A C   
3948  O O   . LYS A 466 ? 0.2460 0.5640 0.5035 -0.0157 -0.0207 -0.0535 466 LYS A O   
3949  C CB  . LYS A 466 ? 0.1638 0.4938 0.4737 -0.0603 -0.0511 -0.0471 466 LYS A CB  
3950  C CG  . LYS A 466 ? 0.2030 0.5662 0.5364 -0.0445 -0.0513 -0.0513 466 LYS A CG  
3951  C CD  . LYS A 466 ? 0.2834 0.6734 0.6552 -0.0571 -0.0630 -0.0468 466 LYS A CD  
3952  C CE  . LYS A 466 ? 0.2960 0.7163 0.6918 -0.0413 -0.0542 -0.0441 466 LYS A CE  
3953  N NZ  . LYS A 466 ? 0.2116 0.6350 0.6143 -0.0287 -0.0772 -0.0485 466 LYS A NZ  
3954  N N   . LEU A 467 ? 0.2033 0.4551 0.4173 -0.0197 -0.0438 -0.0539 467 LEU A N   
3955  C CA  . LEU A 467 ? 0.1496 0.3861 0.3376 0.0005  -0.0436 -0.0591 467 LEU A CA  
3956  C C   . LEU A 467 ? 0.1357 0.3667 0.3046 0.0061  -0.0243 -0.0548 467 LEU A C   
3957  O O   . LEU A 467 ? 0.2292 0.4679 0.3958 0.0181  -0.0171 -0.0581 467 LEU A O   
3958  C CB  . LEU A 467 ? 0.1722 0.3703 0.3276 0.0054  -0.0594 -0.0643 467 LEU A CB  
3959  C CG  . LEU A 467 ? 0.1879 0.3920 0.3504 0.0084  -0.0816 -0.0709 467 LEU A CG  
3960  C CD1 . LEU A 467 ? 0.2199 0.3861 0.3458 0.0079  -0.0968 -0.0781 467 LEU A CD1 
3961  C CD2 . LEU A 467 ? 0.1791 0.3952 0.3429 0.0264  -0.0816 -0.0705 467 LEU A CD2 
3962  N N   . PHE A 468 ? 0.1656 0.3823 0.3217 -0.0025 -0.0175 -0.0472 468 PHE A N   
3963  C CA  . PHE A 468 ? 0.1634 0.3786 0.3021 0.0019  -0.0027 -0.0424 468 PHE A CA  
3964  C C   . PHE A 468 ? 0.2143 0.4654 0.3693 -0.0012 0.0116  -0.0423 468 PHE A C   
3965  O O   . PHE A 468 ? 0.2095 0.4639 0.3533 0.0070  0.0204  -0.0465 468 PHE A O   
3966  C CB  . PHE A 468 ? 0.2143 0.4099 0.3404 -0.0052 -0.0008 -0.0318 468 PHE A CB  
3967  C CG  . PHE A 468 ? 0.2780 0.4800 0.3905 -0.0029 0.0116  -0.0245 468 PHE A CG  
3968  C CD1 . PHE A 468 ? 0.2790 0.4707 0.3728 0.0095  0.0140  -0.0286 468 PHE A CD1 
3969  C CD2 . PHE A 468 ? 0.3029 0.5233 0.4207 -0.0150 0.0199  -0.0125 468 PHE A CD2 
3970  C CE1 . PHE A 468 ? 0.1836 0.3846 0.2676 0.0095  0.0226  -0.0226 468 PHE A CE1 
3971  C CE2 . PHE A 468 ? 0.2102 0.4389 0.3130 -0.0138 0.0279  -0.0059 468 PHE A CE2 
3972  C CZ  . PHE A 468 ? 0.2178 0.4375 0.3055 -0.0016 0.0283  -0.0118 468 PHE A CZ  
3973  N N   . ARG A 469 ? 0.1213 0.3999 0.3024 -0.0141 0.0151  -0.0386 469 ARG A N   
3974  C CA  . ARG A 469 ? 0.1144 0.4231 0.3063 -0.0156 0.0306  -0.0402 469 ARG A CA  
3975  C C   . ARG A 469 ? 0.1152 0.4224 0.3137 0.0000  0.0292  -0.0515 469 ARG A C   
3976  O O   . ARG A 469 ? 0.2371 0.5463 0.4288 0.0045  0.0408  -0.0552 469 ARG A O   
3977  C CB  . ARG A 469 ? 0.1254 0.4570 0.3402 -0.0330 0.0355  -0.0307 469 ARG A CB  
3978  C CG  . ARG A 469 ? 0.1523 0.4796 0.3621 -0.0508 0.0348  -0.0154 469 ARG A CG  
3979  C CD  . ARG A 469 ? 0.1487 0.4978 0.3786 -0.0708 0.0425  -0.0028 469 ARG A CD  
3980  N NE  . ARG A 469 ? 0.1789 0.5148 0.3944 -0.0865 0.0438  0.0170  469 ARG A NE  
3981  C CZ  . ARG A 469 ? 0.1732 0.5151 0.3653 -0.0898 0.0563  0.0285  469 ARG A CZ  
3982  N NH1 . ARG A 469 ? 0.1749 0.5246 0.3492 -0.0783 0.0675  0.0184  469 ARG A NH1 
3983  N NH2 . ARG A 469 ? 0.1933 0.5157 0.3722 -0.1016 0.0535  0.0500  469 ARG A NH2 
3984  N N   . SER A 470 ? 0.1226 0.4264 0.3338 0.0083  0.0137  -0.0571 470 SER A N   
3985  C CA  . SER A 470 ? 0.1649 0.4662 0.3833 0.0244  0.0103  -0.0645 470 SER A CA  
3986  C C   . SER A 470 ? 0.1253 0.4018 0.3161 0.0360  0.0147  -0.0691 470 SER A C   
3987  O O   . SER A 470 ? 0.2782 0.5519 0.4684 0.0431  0.0234  -0.0741 470 SER A O   
3988  C CB  . SER A 470 ? 0.1691 0.4729 0.4048 0.0295  -0.0112 -0.0666 470 SER A CB  
3989  O OG  . SER A 470 ? 0.3235 0.6539 0.5934 0.0236  -0.0142 -0.0642 470 SER A OG  
3990  N N   . PHE A 471 ? 0.1413 0.4003 0.3111 0.0377  0.0090  -0.0679 471 PHE A N   
3991  C CA  . PHE A 471 ? 0.1899 0.4266 0.3356 0.0462  0.0134  -0.0701 471 PHE A CA  
3992  C C   . PHE A 471 ? 0.2408 0.4752 0.3723 0.0383  0.0283  -0.0697 471 PHE A C   
3993  O O   . PHE A 471 ? 0.2312 0.4538 0.3549 0.0435  0.0330  -0.0754 471 PHE A O   
3994  C CB  . PHE A 471 ? 0.1150 0.3235 0.2322 0.0458  0.0066  -0.0638 471 PHE A CB  
3995  C CG  . PHE A 471 ? 0.1568 0.3511 0.2699 0.0502  -0.0104 -0.0626 471 PHE A CG  
3996  C CD1 . PHE A 471 ? 0.1953 0.3890 0.3171 0.0611  -0.0208 -0.0648 471 PHE A CD1 
3997  C CD2 . PHE A 471 ? 0.1971 0.3768 0.2961 0.0440  -0.0172 -0.0597 471 PHE A CD2 
3998  C CE1 . PHE A 471 ? 0.1702 0.3529 0.2834 0.0642  -0.0390 -0.0632 471 PHE A CE1 
3999  C CE2 . PHE A 471 ? 0.1543 0.3202 0.2439 0.0468  -0.0336 -0.0617 471 PHE A CE2 
4000  C CZ  . PHE A 471 ? 0.1636 0.3328 0.2586 0.0560  -0.0453 -0.0630 471 PHE A CZ  
4001  N N   . VAL A 472 ? 0.2898 0.5356 0.4184 0.0256  0.0339  -0.0632 472 VAL A N   
4002  C CA  . VAL A 472 ? 0.2178 0.4651 0.3305 0.0180  0.0443  -0.0622 472 VAL A CA  
4003  C C   . VAL A 472 ? 0.2232 0.4790 0.3445 0.0211  0.0522  -0.0717 472 VAL A C   
4004  O O   . VAL A 472 ? 0.2413 0.4901 0.3489 0.0218  0.0577  -0.0790 472 VAL A O   
4005  C CB  . VAL A 472 ? 0.2317 0.4930 0.3421 0.0050  0.0473  -0.0507 472 VAL A CB  
4006  C CG1 . VAL A 472 ? 0.2105 0.4809 0.3061 -0.0028 0.0566  -0.0499 472 VAL A CG1 
4007  C CG2 . VAL A 472 ? 0.2501 0.5017 0.3503 0.0046  0.0416  -0.0426 472 VAL A CG2 
4008  N N   . ARG A 473 ? 0.2835 0.5568 0.4301 0.0232  0.0530  -0.0729 473 ARG A N   
4009  C CA  . ARG A 473 ? 0.3082 0.5927 0.4671 0.0289  0.0623  -0.0825 473 ARG A CA  
4010  C C   . ARG A 473 ? 0.2848 0.5533 0.4508 0.0451  0.0584  -0.0925 473 ARG A C   
4011  O O   . ARG A 473 ? 0.2928 0.5578 0.4568 0.0509  0.0670  -0.1034 473 ARG A O   
4012  C CB  . ARG A 473 ? 0.3184 0.6313 0.5071 0.0259  0.0651  -0.0787 473 ARG A CB  
4013  C CG  . ARG A 473 ? 0.3745 0.7090 0.5608 0.0167  0.0808  -0.0784 473 ARG A CG  
4014  C CD  . ARG A 473 ? 0.3849 0.7140 0.5402 0.0029  0.0835  -0.0705 473 ARG A CD  
4015  N NE  . ARG A 473 ? 0.5545 0.8844 0.7131 -0.0076 0.0759  -0.0559 473 ARG A NE  
4016  C CZ  . ARG A 473 ? 0.6847 1.0174 0.8262 -0.0208 0.0784  -0.0440 473 ARG A CZ  
4017  N NH1 . ARG A 473 ? 0.5553 0.8926 0.6727 -0.0256 0.0869  -0.0443 473 ARG A NH1 
4018  N NH2 . ARG A 473 ? 0.5082 0.8402 0.6576 -0.0296 0.0713  -0.0313 473 ARG A NH2 
4019  N N   . ARG A 474 ? 0.2842 0.5424 0.4581 0.0531  0.0452  -0.0893 474 ARG A N   
4020  C CA  . ARG A 474 ? 0.3027 0.5431 0.4825 0.0693  0.0399  -0.0956 474 ARG A CA  
4021  C C   . ARG A 474 ? 0.3437 0.5594 0.4987 0.0689  0.0449  -0.1011 474 ARG A C   
4022  O O   . ARG A 474 ? 0.3455 0.5458 0.5052 0.0801  0.0470  -0.1100 474 ARG A O   
4023  C CB  . ARG A 474 ? 0.2394 0.4750 0.4273 0.0772  0.0225  -0.0891 474 ARG A CB  
4024  C CG  . ARG A 474 ? 0.1915 0.4049 0.3818 0.0950  0.0138  -0.0911 474 ARG A CG  
4025  C CD  . ARG A 474 ? 0.2984 0.5186 0.5182 0.1093  0.0132  -0.0951 474 ARG A CD  
4026  N NE  . ARG A 474 ? 0.3065 0.4970 0.5256 0.1264  0.0072  -0.0963 474 ARG A NE  
4027  C CZ  . ARG A 474 ? 0.3599 0.5304 0.5753 0.1315  0.0186  -0.1063 474 ARG A CZ  
4028  N NH1 . ARG A 474 ? 0.4111 0.5909 0.6199 0.1212  0.0358  -0.1169 474 ARG A NH1 
4029  N NH2 . ARG A 474 ? 0.3518 0.4894 0.5681 0.1470  0.0111  -0.1051 474 ARG A NH2 
4030  N N   . ALA A 475 ? 0.3522 0.5638 0.4834 0.0561  0.0462  -0.0957 475 ALA A N   
4031  C CA  . ALA A 475 ? 0.2481 0.4417 0.3590 0.0529  0.0499  -0.1001 475 ALA A CA  
4032  C C   . ALA A 475 ? 0.2499 0.4467 0.3547 0.0481  0.0605  -0.1122 475 ALA A C   
4033  O O   . ALA A 475 ? 0.2398 0.4209 0.3339 0.0471  0.0632  -0.1214 475 ALA A O   
4034  C CB  . ALA A 475 ? 0.2232 0.4164 0.3147 0.0417  0.0473  -0.0894 475 ALA A CB  
4035  N N   . GLN A 476 ? 0.2360 0.4537 0.3468 0.0445  0.0670  -0.1138 476 GLN A N   
4036  C CA  . GLN A 476 ? 0.3356 0.5593 0.4376 0.0407  0.0778  -0.1268 476 GLN A CA  
4037  C C   . GLN A 476 ? 0.3435 0.5626 0.4640 0.0558  0.0843  -0.1416 476 GLN A C   
4038  O O   . GLN A 476 ? 0.3013 0.5218 0.4137 0.0551  0.0943  -0.1562 476 GLN A O   
4039  C CB  . GLN A 476 ? 0.3350 0.5850 0.4305 0.0290  0.0835  -0.1204 476 GLN A CB  
4040  C CG  . GLN A 476 ? 0.2594 0.5121 0.3383 0.0162  0.0768  -0.1051 476 GLN A CG  
4041  C CD  . GLN A 476 ? 0.3958 0.6724 0.4701 0.0055  0.0820  -0.0962 476 GLN A CD  
4042  O OE1 . GLN A 476 ? 0.5030 0.7921 0.5624 -0.0013 0.0895  -0.1018 476 GLN A OE1 
4043  N NE2 . GLN A 476 ? 0.4438 0.7271 0.5302 0.0032  0.0783  -0.0826 476 GLN A NE2 
4044  N N   . GLU A 477 ? 0.2686 0.4826 0.4132 0.0703  0.0783  -0.1383 477 GLU A N   
4045  C CA  . GLU A 477 ? 0.2519 0.4579 0.4175 0.0882  0.0824  -0.1503 477 GLU A CA  
4046  C C   . GLU A 477 ? 0.2630 0.4324 0.4285 0.0993  0.0746  -0.1537 477 GLU A C   
4047  O O   . GLU A 477 ? 0.4111 0.5575 0.5745 0.1065  0.0801  -0.1686 477 GLU A O   
4048  C CB  . GLU A 477 ? 0.2472 0.4767 0.4454 0.0985  0.0798  -0.1431 477 GLU A CB  
4049  C CG  . GLU A 477 ? 0.4215 0.6835 0.6222 0.0844  0.0821  -0.1325 477 GLU A CG  
4050  C CD  . GLU A 477 ? 0.5703 0.8562 0.8070 0.0924  0.0767  -0.1250 477 GLU A CD  
4051  O OE1 . GLU A 477 ? 0.5392 0.8181 0.7985 0.1102  0.0701  -0.1271 477 GLU A OE1 
4052  O OE2 . GLU A 477 ? 0.6048 0.9165 0.8489 0.0806  0.0780  -0.1162 477 GLU A OE2 
4053  N N   . MET B 1   ? 0.4097 0.8480 0.4936 0.0440  -0.0861 0.0220  1   MET B N   
4054  C CA  . MET B 1   ? 0.4884 0.9113 0.5848 0.0486  -0.0850 0.0433  1   MET B CA  
4055  C C   . MET B 1   ? 0.2874 0.6819 0.3924 0.0483  -0.0805 0.0329  1   MET B C   
4056  O O   . MET B 1   ? 0.3623 0.7495 0.4546 0.0440  -0.0770 0.0130  1   MET B O   
4057  C CB  . MET B 1   ? 0.5756 1.0090 0.6571 0.0487  -0.0832 0.0588  1   MET B CB  
4058  C CG  . MET B 1   ? 0.5044 0.9328 0.5660 0.0447  -0.0780 0.0441  1   MET B CG  
4059  S SD  . MET B 1   ? 0.6565 1.0930 0.7067 0.0455  -0.0745 0.0649  1   MET B SD  
4060  C CE  . MET B 1   ? 0.5471 0.9731 0.6231 0.0510  -0.0770 0.0962  1   MET B CE  
4061  N N   . LYS B 2   ? 0.2501 0.6286 0.3783 0.0531  -0.0801 0.0457  2   LYS B N   
4062  C CA  . LYS B 2   ? 0.1877 0.5236 0.3186 0.0510  -0.0714 0.0357  2   LYS B CA  
4063  C C   . LYS B 2   ? 0.1934 0.5178 0.3095 0.0491  -0.0672 0.0395  2   LYS B C   
4064  O O   . LYS B 2   ? 0.2952 0.6334 0.4115 0.0518  -0.0698 0.0599  2   LYS B O   
4065  C CB  . LYS B 2   ? 0.1869 0.5026 0.3444 0.0558  -0.0700 0.0471  2   LYS B CB  
4066  C CG  . LYS B 2   ? 0.1806 0.4583 0.3424 0.0533  -0.0617 0.0308  2   LYS B CG  
4067  C CD  . LYS B 2   ? 0.2908 0.5424 0.4686 0.0564  -0.0578 0.0426  2   LYS B CD  
4068  C CE  . LYS B 2   ? 0.3347 0.5875 0.5423 0.0626  -0.0602 0.0537  2   LYS B CE  
4069  N NZ  . LYS B 2   ? 0.2389 0.4669 0.4655 0.0657  -0.0566 0.0643  2   LYS B NZ  
4070  N N   . LYS B 3   ? 0.2335 0.5337 0.3377 0.0444  -0.0607 0.0210  3   LYS B N   
4071  C CA  . LYS B 3   ? 0.1806 0.4712 0.2696 0.0420  -0.0567 0.0212  3   LYS B CA  
4072  C C   . LYS B 3   ? 0.1750 0.4268 0.2708 0.0412  -0.0499 0.0193  3   LYS B C   
4073  O O   . LYS B 3   ? 0.2684 0.5014 0.3785 0.0420  -0.0478 0.0151  3   LYS B O   
4074  C CB  . LYS B 3   ? 0.1791 0.4779 0.2478 0.0372  -0.0552 0.0007  3   LYS B CB  
4075  C CG  . LYS B 3   ? 0.2075 0.5478 0.2652 0.0376  -0.0614 0.0017  3   LYS B CG  
4076  C CD  . LYS B 3   ? 0.2691 0.6147 0.3089 0.0330  -0.0589 -0.0198 3   LYS B CD  
4077  C CE  . LYS B 3   ? 0.3189 0.7027 0.3448 0.0331  -0.0627 -0.0181 3   LYS B CE  
4078  N NZ  . LYS B 3   ? 0.4611 0.8449 0.4722 0.0288  -0.0580 -0.0405 3   LYS B NZ  
4079  N N   . LEU B 4   ? 0.1747 0.4168 0.2601 0.0394  -0.0466 0.0220  4   LEU B N   
4080  C CA  . LEU B 4   ? 0.1697 0.3778 0.2568 0.0374  -0.0404 0.0165  4   LEU B CA  
4081  C C   . LEU B 4   ? 0.2125 0.4155 0.2797 0.0330  -0.0367 0.0018  4   LEU B C   
4082  O O   . LEU B 4   ? 0.2637 0.4836 0.3189 0.0325  -0.0376 0.0060  4   LEU B O   
4083  C CB  . LEU B 4   ? 0.1734 0.3723 0.2721 0.0396  -0.0401 0.0355  4   LEU B CB  
4084  C CG  . LEU B 4   ? 0.1694 0.3358 0.2696 0.0371  -0.0344 0.0291  4   LEU B CG  
4085  C CD1 . LEU B 4   ? 0.1899 0.3406 0.3142 0.0400  -0.0343 0.0403  4   LEU B CD1 
4086  C CD2 . LEU B 4   ? 0.1694 0.3358 0.2553 0.0344  -0.0324 0.0314  4   LEU B CD2 
4087  N N   . PHE B 5   ? 0.1876 0.3687 0.2523 0.0300  -0.0322 -0.0147 5   PHE B N   
4088  C CA  . PHE B 5   ? 0.1577 0.3322 0.2072 0.0261  -0.0285 -0.0289 5   PHE B CA  
4089  C C   . PHE B 5   ? 0.1788 0.3304 0.2262 0.0249  -0.0244 -0.0256 5   PHE B C   
4090  O O   . PHE B 5   ? 0.1668 0.2954 0.2203 0.0240  -0.0211 -0.0294 5   PHE B O   
4091  C CB  . PHE B 5   ? 0.1854 0.3514 0.2351 0.0232  -0.0262 -0.0465 5   PHE B CB  
4092  C CG  . PHE B 5   ? 0.1565 0.3465 0.2083 0.0235  -0.0305 -0.0522 5   PHE B CG  
4093  C CD1 . PHE B 5   ? 0.1610 0.3780 0.2034 0.0235  -0.0342 -0.0534 5   PHE B CD1 
4094  C CD2 . PHE B 5   ? 0.1548 0.3425 0.2186 0.0235  -0.0309 -0.0570 5   PHE B CD2 
4095  C CE1 . PHE B 5   ? 0.1642 0.4056 0.2086 0.0233  -0.0389 -0.0600 5   PHE B CE1 
4096  C CE2 . PHE B 5   ? 0.1671 0.3781 0.2341 0.0234  -0.0354 -0.0625 5   PHE B CE2 
4097  C CZ  . PHE B 5   ? 0.1621 0.4001 0.2193 0.0231  -0.0397 -0.0644 5   PHE B CZ  
4098  N N   . LEU B 6   ? 0.2143 0.3742 0.2531 0.0248  -0.0245 -0.0188 6   LEU B N   
4099  C CA  . LEU B 6   ? 0.2073 0.3495 0.2454 0.0237  -0.0214 -0.0140 6   LEU B CA  
4100  C C   . LEU B 6   ? 0.1535 0.2877 0.1785 0.0206  -0.0177 -0.0274 6   LEU B C   
4101  O O   . LEU B 6   ? 0.1645 0.3156 0.1799 0.0203  -0.0180 -0.0334 6   LEU B O   
4102  C CB  . LEU B 6   ? 0.1614 0.3184 0.2014 0.0255  -0.0236 0.0042  6   LEU B CB  
4103  C CG  . LEU B 6   ? 0.1610 0.3018 0.2036 0.0241  -0.0210 0.0113  6   LEU B CG  
4104  C CD1 . LEU B 6   ? 0.1602 0.2771 0.2185 0.0242  -0.0203 0.0130  6   LEU B CD1 
4105  C CD2 . LEU B 6   ? 0.1665 0.3268 0.2107 0.0255  -0.0228 0.0296  6   LEU B CD2 
4106  N N   . VAL B 7   ? 0.1501 0.2601 0.1760 0.0186  -0.0142 -0.0324 7   VAL B N   
4107  C CA  . VAL B 7   ? 0.1477 0.2483 0.1641 0.0160  -0.0108 -0.0434 7   VAL B CA  
4108  C C   . VAL B 7   ? 0.1655 0.2526 0.1815 0.0150  -0.0091 -0.0373 7   VAL B C   
4109  O O   . VAL B 7   ? 0.1621 0.2328 0.1848 0.0143  -0.0085 -0.0351 7   VAL B O   
4110  C CB  . VAL B 7   ? 0.1451 0.2316 0.1625 0.0140  -0.0082 -0.0561 7   VAL B CB  
4111  C CG1 . VAL B 7   ? 0.1439 0.2220 0.1538 0.0117  -0.0049 -0.0652 7   VAL B CG1 
4112  C CG2 . VAL B 7   ? 0.1459 0.2460 0.1665 0.0145  -0.0101 -0.0621 7   VAL B CG2 
4113  N N   . PHE B 8   ? 0.1478 0.2431 0.1567 0.0149  -0.0084 -0.0355 8   PHE B N   
4114  C CA  . PHE B 8   ? 0.1470 0.2311 0.1553 0.0135  -0.0068 -0.0313 8   PHE B CA  
4115  C C   . PHE B 8   ? 0.1865 0.2580 0.1889 0.0116  -0.0039 -0.0429 8   PHE B C   
4116  O O   . PHE B 8   ? 0.1444 0.2214 0.1425 0.0117  -0.0026 -0.0527 8   PHE B O   
4117  C CB  . PHE B 8   ? 0.1495 0.2511 0.1550 0.0146  -0.0072 -0.0220 8   PHE B CB  
4118  C CG  . PHE B 8   ? 0.1531 0.2662 0.1668 0.0161  -0.0100 -0.0061 8   PHE B CG  
4119  C CD1 . PHE B 8   ? 0.1815 0.2815 0.2067 0.0152  -0.0107 0.0040  8   PHE B CD1 
4120  C CD2 . PHE B 8   ? 0.1569 0.2948 0.1679 0.0183  -0.0120 -0.0010 8   PHE B CD2 
4121  C CE1 . PHE B 8   ? 0.2449 0.3546 0.2814 0.0167  -0.0131 0.0203  8   PHE B CE1 
4122  C CE2 . PHE B 8   ? 0.1614 0.3114 0.1812 0.0200  -0.0146 0.0164  8   PHE B CE2 
4123  C CZ  . PHE B 8   ? 0.1622 0.2970 0.1959 0.0193  -0.0150 0.0277  8   PHE B CZ  
4124  N N   . TRP B 9   ? 0.1435 0.1989 0.1473 0.0099  -0.0029 -0.0415 9   TRP B N   
4125  C CA  . TRP B 9   ? 0.1422 0.1860 0.1414 0.0082  -0.0004 -0.0499 9   TRP B CA  
4126  C C   . TRP B 9   ? 0.1981 0.2338 0.1978 0.0068  -0.0005 -0.0447 9   TRP B C   
4127  O O   . TRP B 9   ? 0.2185 0.2424 0.2213 0.0051  -0.0012 -0.0437 9   TRP B O   
4128  C CB  . TRP B 9   ? 0.1418 0.1742 0.1422 0.0069  0.0007  -0.0568 9   TRP B CB  
4129  C CG  . TRP B 9   ? 0.1523 0.1771 0.1493 0.0055  0.0034  -0.0641 9   TRP B CG  
4130  C CD1 . TRP B 9   ? 0.2313 0.2568 0.2258 0.0057  0.0046  -0.0655 9   TRP B CD1 
4131  C CD2 . TRP B 9   ? 0.2167 0.2327 0.2144 0.0039  0.0055  -0.0699 9   TRP B CD2 
4132  N NE1 . TRP B 9   ? 0.2567 0.2733 0.2516 0.0044  0.0070  -0.0709 9   TRP B NE1 
4133  C CE2 . TRP B 9   ? 0.2214 0.2326 0.2177 0.0030  0.0077  -0.0732 9   TRP B CE2 
4134  C CE3 . TRP B 9   ? 0.1890 0.2016 0.1899 0.0033  0.0060  -0.0721 9   TRP B CE3 
4135  C CZ2 . TRP B 9   ? 0.1471 0.1506 0.1449 0.0012  0.0103  -0.0769 9   TRP B CZ2 
4136  C CZ3 . TRP B 9   ? 0.1439 0.1497 0.1449 0.0014  0.0090  -0.0771 9   TRP B CZ3 
4137  C CH2 . TRP B 9   ? 0.1931 0.1946 0.1925 0.0001  0.0111  -0.0787 9   TRP B CH2 
4138  N N   . TRP B 10  ? 0.2068 0.2501 0.2041 0.0074  0.0001  -0.0426 10  TRP B N   
4139  C CA  . TRP B 10  ? 0.1828 0.2216 0.1818 0.0061  -0.0004 -0.0370 10  TRP B CA  
4140  C C   . TRP B 10  ? 0.1832 0.2108 0.1792 0.0048  0.0008  -0.0426 10  TRP B C   
4141  O O   . TRP B 10  ? 0.1900 0.2188 0.1835 0.0060  0.0028  -0.0488 10  TRP B O   
4142  C CB  . TRP B 10  ? 0.2000 0.2542 0.1990 0.0075  0.0002  -0.0312 10  TRP B CB  
4143  C CG  . TRP B 10  ? 0.1445 0.2144 0.1451 0.0090  -0.0007 -0.0242 10  TRP B CG  
4144  C CD1 . TRP B 10  ? 0.1458 0.2321 0.1418 0.0113  0.0000  -0.0277 10  TRP B CD1 
4145  C CD2 . TRP B 10  ? 0.1471 0.2193 0.1557 0.0084  -0.0028 -0.0119 10  TRP B CD2 
4146  N NE1 . TRP B 10  ? 0.1484 0.2490 0.1472 0.0122  -0.0017 -0.0170 10  TRP B NE1 
4147  C CE2 . TRP B 10  ? 0.1591 0.2504 0.1669 0.0106  -0.0032 -0.0063 10  TRP B CE2 
4148  C CE3 . TRP B 10  ? 0.1885 0.2492 0.2066 0.0060  -0.0044 -0.0053 10  TRP B CE3 
4149  C CZ2 . TRP B 10  ? 0.1581 0.2567 0.1748 0.0108  -0.0051 0.0081  10  TRP B CZ2 
4150  C CZ3 . TRP B 10  ? 0.2437 0.3096 0.2724 0.0060  -0.0060 0.0073  10  TRP B CZ3 
4151  C CH2 . TRP B 10  ? 0.2408 0.3254 0.2691 0.0085  -0.0063 0.0151  10  TRP B CH2 
4152  N N   . HIS B 11  ? 0.1868 0.2047 0.1845 0.0025  -0.0007 -0.0403 11  HIS B N   
4153  C CA  . HIS B 11  ? 0.1437 0.1535 0.1383 0.0011  -0.0004 -0.0434 11  HIS B CA  
4154  C C   . HIS B 11  ? 0.1888 0.2026 0.1853 0.0011  -0.0012 -0.0386 11  HIS B C   
4155  O O   . HIS B 11  ? 0.2262 0.2413 0.2272 -0.0006 -0.0033 -0.0333 11  HIS B O   
4156  C CB  . HIS B 11  ? 0.1567 0.1567 0.1509 -0.0016 -0.0017 -0.0453 11  HIS B CB  
4157  C CG  . HIS B 11  ? 0.2003 0.1955 0.1901 -0.0032 -0.0018 -0.0469 11  HIS B CG  
4158  N ND1 . HIS B 11  ? 0.2523 0.2470 0.2392 -0.0020 0.0003  -0.0482 11  HIS B ND1 
4159  C CD2 . HIS B 11  ? 0.2426 0.2347 0.2313 -0.0059 -0.0041 -0.0470 11  HIS B CD2 
4160  C CE1 . HIS B 11  ? 0.2278 0.2198 0.2117 -0.0037 -0.0007 -0.0470 11  HIS B CE1 
4161  N NE2 . HIS B 11  ? 0.2655 0.2569 0.2491 -0.0061 -0.0035 -0.0468 11  HIS B NE2 
4162  N N   . MET B 12  ? 0.1697 0.1858 0.1653 0.0028  0.0006  -0.0406 12  MET B N   
4163  C CA  . MET B 12  ? 0.1434 0.1639 0.1422 0.0034  0.0002  -0.0366 12  MET B CA  
4164  C C   . MET B 12  ? 0.1456 0.1587 0.1434 0.0024  -0.0009 -0.0367 12  MET B C   
4165  O O   . MET B 12  ? 0.1607 0.1698 0.1579 0.0037  0.0011  -0.0399 12  MET B O   
4166  C CB  . MET B 12  ? 0.1426 0.1734 0.1437 0.0070  0.0032  -0.0390 12  MET B CB  
4167  C CG  . MET B 12  ? 0.1419 0.1833 0.1416 0.0082  0.0044  -0.0397 12  MET B CG  
4168  S SD  . MET B 12  ? 0.2584 0.3053 0.2610 0.0060  0.0019  -0.0291 12  MET B SD  
4169  C CE  . MET B 12  ? 0.1424 0.2101 0.1439 0.0089  0.0043  -0.0274 12  MET B CE  
4170  N N   . HIS B 13  ? 0.1718 0.1842 0.1706 -0.0001 -0.0041 -0.0326 13  HIS B N   
4171  C CA  . HIS B 13  ? 0.1766 0.1855 0.1735 -0.0012 -0.0059 -0.0314 13  HIS B CA  
4172  C C   . HIS B 13  ? 0.2846 0.2987 0.2856 -0.0029 -0.0095 -0.0265 13  HIS B C   
4173  O O   . HIS B 13  ? 0.2173 0.2343 0.2222 -0.0048 -0.0112 -0.0249 13  HIS B O   
4174  C CB  . HIS B 13  ? 0.1538 0.1559 0.1439 -0.0039 -0.0067 -0.0349 13  HIS B CB  
4175  C CG  . HIS B 13  ? 0.1589 0.1616 0.1455 -0.0057 -0.0092 -0.0325 13  HIS B CG  
4176  N ND1 . HIS B 13  ? 0.1610 0.1647 0.1488 -0.0037 -0.0084 -0.0283 13  HIS B ND1 
4177  C CD2 . HIS B 13  ? 0.1635 0.1676 0.1463 -0.0093 -0.0128 -0.0337 13  HIS B CD2 
4178  C CE1 . HIS B 13  ? 0.1734 0.1803 0.1570 -0.0059 -0.0115 -0.0252 13  HIS B CE1 
4179  N NE2 . HIS B 13  ? 0.2211 0.2291 0.2007 -0.0095 -0.0143 -0.0295 13  HIS B NE2 
4180  N N   . GLN B 14  ? 0.3019 0.3175 0.3036 -0.0022 -0.0109 -0.0234 14  GLN B N   
4181  C CA  . GLN B 14  ? 0.2034 0.2255 0.2095 -0.0035 -0.0149 -0.0186 14  GLN B CA  
4182  C C   . GLN B 14  ? 0.1613 0.1840 0.1642 -0.0036 -0.0171 -0.0154 14  GLN B C   
4183  O O   . GLN B 14  ? 0.2572 0.2779 0.2624 -0.0001 -0.0144 -0.0131 14  GLN B O   
4184  C CB  . GLN B 14  ? 0.2461 0.2757 0.2617 -0.0003 -0.0132 -0.0150 14  GLN B CB  
4185  C CG  . GLN B 14  ? 0.2438 0.2810 0.2660 -0.0030 -0.0165 -0.0113 14  GLN B CG  
4186  C CD  . GLN B 14  ? 0.1775 0.2137 0.2005 -0.0059 -0.0164 -0.0126 14  GLN B CD  
4187  O OE1 . GLN B 14  ? 0.2678 0.3053 0.2911 -0.0039 -0.0126 -0.0130 14  GLN B OE1 
4188  N NE2 . GLN B 14  ? 0.2700 0.3049 0.2947 -0.0108 -0.0208 -0.0133 14  GLN B NE2 
4189  N N   . PRO B 15  ? 0.1661 0.1925 0.1650 -0.0074 -0.0219 -0.0150 15  PRO B N   
4190  C CA  . PRO B 15  ? 0.1764 0.2075 0.1717 -0.0074 -0.0245 -0.0098 15  PRO B CA  
4191  C C   . PRO B 15  ? 0.2072 0.2454 0.2128 -0.0042 -0.0261 -0.0017 15  PRO B C   
4192  O O   . PRO B 15  ? 0.2937 0.3348 0.3084 -0.0027 -0.0256 -0.0012 15  PRO B O   
4193  C CB  . PRO B 15  ? 0.1783 0.2150 0.1668 -0.0128 -0.0297 -0.0138 15  PRO B CB  
4194  C CG  . PRO B 15  ? 0.1743 0.2105 0.1696 -0.0151 -0.0311 -0.0181 15  PRO B CG  
4195  C CD  . PRO B 15  ? 0.2189 0.2470 0.2179 -0.0121 -0.0255 -0.0192 15  PRO B CD  
4196  N N   . LEU B 16  ? 0.2551 0.2975 0.2602 -0.0028 -0.0277 0.0056  16  LEU B N   
4197  C CA  . LEU B 16  ? 0.1794 0.2280 0.1966 0.0012  -0.0290 0.0146  16  LEU B CA  
4198  C C   . LEU B 16  ? 0.1809 0.2420 0.2008 -0.0014 -0.0355 0.0170  16  LEU B C   
4199  O O   . LEU B 16  ? 0.2343 0.3047 0.2480 -0.0043 -0.0411 0.0203  16  LEU B O   
4200  C CB  . LEU B 16  ? 0.1866 0.2358 0.2046 0.0036  -0.0288 0.0238  16  LEU B CB  
4201  C CG  . LEU B 16  ? 0.2027 0.2561 0.2374 0.0091  -0.0291 0.0338  16  LEU B CG  
4202  C CD1 . LEU B 16  ? 0.2009 0.2479 0.2486 0.0135  -0.0236 0.0284  16  LEU B CD1 
4203  C CD2 . LEU B 16  ? 0.1965 0.2483 0.2345 0.0114  -0.0280 0.0443  16  LEU B CD2 
4204  N N   . TYR B 17  ? 0.2264 0.2899 0.2562 -0.0006 -0.0350 0.0155  17  TYR B N   
4205  C CA  . TYR B 17  ? 0.1796 0.2555 0.2159 -0.0031 -0.0408 0.0182  17  TYR B CA  
4206  C C   . TYR B 17  ? 0.1787 0.2641 0.2268 0.0014  -0.0431 0.0285  17  TYR B C   
4207  O O   . TYR B 17  ? 0.1797 0.2774 0.2351 -0.0003 -0.0484 0.0318  17  TYR B O   
4208  C CB  . TYR B 17  ? 0.1995 0.2753 0.2433 -0.0042 -0.0388 0.0140  17  TYR B CB  
4209  C CG  . TYR B 17  ? 0.2023 0.2692 0.2385 -0.0081 -0.0366 0.0057  17  TYR B CG  
4210  C CD1 . TYR B 17  ? 0.1813 0.2462 0.2078 -0.0133 -0.0404 0.0001  17  TYR B CD1 
4211  C CD2 . TYR B 17  ? 0.1964 0.2585 0.2359 -0.0062 -0.0309 0.0034  17  TYR B CD2 
4212  C CE1 . TYR B 17  ? 0.2490 0.3054 0.2717 -0.0162 -0.0383 -0.0072 17  TYR B CE1 
4213  C CE2 . TYR B 17  ? 0.2435 0.2984 0.2780 -0.0092 -0.0294 -0.0023 17  TYR B CE2 
4214  C CZ  . TYR B 17  ? 0.2400 0.2910 0.2672 -0.0140 -0.0330 -0.0074 17  TYR B CZ  
4215  O OH  . TYR B 17  ? 0.1937 0.2371 0.2190 -0.0164 -0.0313 -0.0128 17  TYR B OH  
4216  N N   . ARG B 18  ? 0.1856 0.2660 0.2384 0.0069  -0.0393 0.0338  18  ARG B N   
4217  C CA  . ARG B 18  ? 0.1831 0.2710 0.2515 0.0123  -0.0406 0.0440  18  ARG B CA  
4218  C C   . ARG B 18  ? 0.1925 0.2911 0.2567 0.0109  -0.0476 0.0543  18  ARG B C   
4219  O O   . ARG B 18  ? 0.1982 0.2930 0.2531 0.0104  -0.0472 0.0575  18  ARG B O   
4220  C CB  . ARG B 18  ? 0.1913 0.2685 0.2699 0.0188  -0.0333 0.0445  18  ARG B CB  
4221  C CG  . ARG B 18  ? 0.2360 0.3190 0.3355 0.0254  -0.0333 0.0538  18  ARG B CG  
4222  C CD  . ARG B 18  ? 0.1858 0.2568 0.2976 0.0313  -0.0258 0.0514  18  ARG B CD  
4223  N NE  . ARG B 18  ? 0.1913 0.2663 0.3255 0.0379  -0.0261 0.0616  18  ARG B NE  
4224  C CZ  . ARG B 18  ? 0.2652 0.3421 0.4041 0.0393  -0.0298 0.0754  18  ARG B CZ  
4225  N NH1 . ARG B 18  ? 0.2513 0.3278 0.3728 0.0344  -0.0330 0.0800  18  ARG B NH1 
4226  N NH2 . ARG B 18  ? 0.3936 0.4745 0.5564 0.0459  -0.0301 0.0855  18  ARG B NH2 
4227  N N   . GLU B 19  ? 0.2564 0.3705 0.3277 0.0102  -0.0542 0.0599  19  GLU B N   
4228  C CA  . GLU B 19  ? 0.2111 0.3401 0.2775 0.0084  -0.0621 0.0697  19  GLU B CA  
4229  C C   . GLU B 19  ? 0.2726 0.4008 0.3482 0.0147  -0.0607 0.0838  19  GLU B C   
4230  O O   . GLU B 19  ? 0.2875 0.4119 0.3827 0.0213  -0.0570 0.0886  19  GLU B O   
4231  C CB  . GLU B 19  ? 0.2531 0.4000 0.3285 0.0067  -0.0697 0.0727  19  GLU B CB  
4232  C CG  . GLU B 19  ? 0.3313 0.4953 0.3935 0.0002  -0.0790 0.0729  19  GLU B CG  
4233  C CD  . GLU B 19  ? 0.4475 0.6291 0.5141 0.0033  -0.0855 0.0893  19  GLU B CD  
4234  O OE1 . GLU B 19  ? 0.4092 0.5907 0.4944 0.0104  -0.0837 0.1006  19  GLU B OE1 
4235  O OE2 . GLU B 19  ? 0.4750 0.6719 0.5274 -0.0013 -0.0923 0.0909  19  GLU B OE2 
4236  N N   . PRO B 20  ? 0.3296 0.4619 0.3932 0.0130  -0.0630 0.0909  20  PRO B N   
4237  C CA  . PRO B 20  ? 0.2703 0.4001 0.3451 0.0188  -0.0607 0.1061  20  PRO B CA  
4238  C C   . PRO B 20  ? 0.3473 0.4904 0.4427 0.0243  -0.0654 0.1216  20  PRO B C   
4239  O O   . PRO B 20  ? 0.4274 0.5625 0.5434 0.0312  -0.0612 0.1302  20  PRO B O   
4240  C CB  . PRO B 20  ? 0.2651 0.4020 0.3202 0.0144  -0.0631 0.1112  20  PRO B CB  
4241  C CG  . PRO B 20  ? 0.3259 0.4755 0.3622 0.0071  -0.0692 0.1005  20  PRO B CG  
4242  C CD  . PRO B 20  ? 0.3391 0.4810 0.3804 0.0057  -0.0679 0.0860  20  PRO B CD  
4243  N N   . TYR B 21  ? 0.3331 0.4967 0.4254 0.0214  -0.0743 0.1249  21  TYR B N   
4244  C CA  . TYR B 21  ? 0.3020 0.4814 0.4136 0.0266  -0.0800 0.1417  21  TYR B CA  
4245  C C   . TYR B 21  ? 0.3019 0.4771 0.4371 0.0319  -0.0770 0.1381  21  TYR B C   
4246  O O   . TYR B 21  ? 0.3750 0.5477 0.5340 0.0398  -0.0745 0.1488  21  TYR B O   
4247  C CB  . TYR B 21  ? 0.2499 0.4559 0.3493 0.0213  -0.0913 0.1463  21  TYR B CB  
4248  C CG  . TYR B 21  ? 0.2941 0.5101 0.3721 0.0172  -0.0945 0.1527  21  TYR B CG  
4249  C CD1 . TYR B 21  ? 0.3287 0.5528 0.4132 0.0217  -0.0958 0.1742  21  TYR B CD1 
4250  C CD2 . TYR B 21  ? 0.4260 0.6440 0.4786 0.0091  -0.0956 0.1377  21  TYR B CD2 
4251  C CE1 . TYR B 21  ? 0.3423 0.5783 0.4067 0.0179  -0.0980 0.1813  21  TYR B CE1 
4252  C CE2 . TYR B 21  ? 0.4285 0.6580 0.4612 0.0056  -0.0977 0.1424  21  TYR B CE2 
4253  C CZ  . TYR B 21  ? 0.2853 0.5247 0.3230 0.0098  -0.0988 0.1646  21  TYR B CZ  
4254  O OH  . TYR B 21  ? 0.2980 0.5516 0.3152 0.0062  -0.1003 0.1705  21  TYR B OH  
4255  N N   . THR B 22  ? 0.2532 0.4282 0.3838 0.0278  -0.0768 0.1234  22  THR B N   
4256  C CA  . THR B 22  ? 0.2338 0.4088 0.3853 0.0321  -0.0738 0.1198  22  THR B CA  
4257  C C   . THR B 22  ? 0.2972 0.4517 0.4535 0.0352  -0.0627 0.1078  22  THR B C   
4258  O O   . THR B 22  ? 0.3239 0.4787 0.4994 0.0402  -0.0586 0.1055  22  THR B O   
4259  C CB  . THR B 22  ? 0.3034 0.4923 0.4506 0.0257  -0.0797 0.1123  22  THR B CB  
4260  O OG1 . THR B 22  ? 0.4330 0.6091 0.5673 0.0206  -0.0746 0.0961  22  THR B OG1 
4261  C CG2 . THR B 22  ? 0.4507 0.6589 0.5843 0.0197  -0.0908 0.1178  22  THR B CG2 
4262  N N   . GLY B 23  ? 0.2397 0.3787 0.3796 0.0324  -0.0579 0.0997  23  GLY B N   
4263  C CA  . GLY B 23  ? 0.2343 0.3564 0.3777 0.0350  -0.0481 0.0880  23  GLY B CA  
4264  C C   . GLY B 23  ? 0.2308 0.3531 0.3691 0.0314  -0.0456 0.0749  23  GLY B C   
4265  O O   . GLY B 23  ? 0.1840 0.2965 0.3257 0.0339  -0.0377 0.0655  23  GLY B O   
4266  N N   . GLU B 24  ? 0.3159 0.4503 0.4471 0.0255  -0.0522 0.0741  24  GLU B N   
4267  C CA  . GLU B 24  ? 0.3128 0.4492 0.4435 0.0219  -0.0501 0.0646  24  GLU B CA  
4268  C C   . GLU B 24  ? 0.2842 0.4093 0.3949 0.0157  -0.0482 0.0541  24  GLU B C   
4269  O O   . GLU B 24  ? 0.2293 0.3511 0.3247 0.0117  -0.0517 0.0537  24  GLU B O   
4270  C CB  . GLU B 24  ? 0.2356 0.3901 0.3727 0.0181  -0.0580 0.0686  24  GLU B CB  
4271  C CG  . GLU B 24  ? 0.3122 0.4799 0.4710 0.0245  -0.0604 0.0797  24  GLU B CG  
4272  C CD  . GLU B 24  ? 0.4976 0.6844 0.6656 0.0207  -0.0675 0.0824  24  GLU B CD  
4273  O OE1 . GLU B 24  ? 0.5784 0.7762 0.7391 0.0158  -0.0769 0.0863  24  GLU B OE1 
4274  O OE2 . GLU B 24  ? 0.5757 0.7682 0.7585 0.0224  -0.0637 0.0804  24  GLU B OE2 
4275  N N   . TYR B 25  ? 0.2453 0.3662 0.3572 0.0151  -0.0424 0.0461  25  TYR B N   
4276  C CA  . TYR B 25  ? 0.1872 0.2982 0.2838 0.0099  -0.0403 0.0372  25  TYR B CA  
4277  C C   . TYR B 25  ? 0.2094 0.3284 0.3048 0.0025  -0.0460 0.0353  25  TYR B C   
4278  O O   . TYR B 25  ? 0.2752 0.4013 0.3812 0.0016  -0.0446 0.0353  25  TYR B O   
4279  C CB  . TYR B 25  ? 0.2615 0.3660 0.3605 0.0132  -0.0315 0.0310  25  TYR B CB  
4280  C CG  . TYR B 25  ? 0.2103 0.3023 0.3048 0.0176  -0.0263 0.0279  25  TYR B CG  
4281  C CD1 . TYR B 25  ? 0.2672 0.3589 0.3751 0.0246  -0.0231 0.0309  25  TYR B CD1 
4282  C CD2 . TYR B 25  ? 0.2285 0.3090 0.3079 0.0145  -0.0245 0.0217  25  TYR B CD2 
4283  C CE1 . TYR B 25  ? 0.2631 0.3430 0.3700 0.0279  -0.0184 0.0274  25  TYR B CE1 
4284  C CE2 . TYR B 25  ? 0.3134 0.3832 0.3904 0.0179  -0.0200 0.0186  25  TYR B CE2 
4285  C CZ  . TYR B 25  ? 0.2261 0.2953 0.3170 0.0243  -0.0170 0.0213  25  TYR B CZ  
4286  O OH  . TYR B 25  ? 0.2242 0.2824 0.3157 0.0271  -0.0125 0.0176  25  TYR B OH  
4287  N N   . LEU B 26  ? 0.1777 0.2962 0.2612 -0.0030 -0.0520 0.0331  26  LEU B N   
4288  C CA  . LEU B 26  ? 0.1738 0.3002 0.2586 -0.0105 -0.0583 0.0297  26  LEU B CA  
4289  C C   . LEU B 26  ? 0.1690 0.2876 0.2540 -0.0144 -0.0545 0.0228  26  LEU B C   
4290  O O   . LEU B 26  ? 0.3465 0.4717 0.4406 -0.0198 -0.0579 0.0215  26  LEU B O   
4291  C CB  . LEU B 26  ? 0.1822 0.3118 0.2539 -0.0151 -0.0654 0.0270  26  LEU B CB  
4292  C CG  . LEU B 26  ? 0.1890 0.3283 0.2583 -0.0116 -0.0697 0.0360  26  LEU B CG  
4293  C CD1 . LEU B 26  ? 0.1987 0.3489 0.2564 -0.0178 -0.0780 0.0326  26  LEU B CD1 
4294  C CD2 . LEU B 26  ? 0.1878 0.3398 0.2753 -0.0072 -0.0715 0.0459  26  LEU B CD2 
4295  N N   . LEU B 27  ? 0.1766 0.2820 0.2535 -0.0121 -0.0478 0.0191  27  LEU B N   
4296  C CA  . LEU B 27  ? 0.2349 0.3337 0.3125 -0.0152 -0.0441 0.0147  27  LEU B CA  
4297  C C   . LEU B 27  ? 0.2680 0.3636 0.3470 -0.0093 -0.0357 0.0162  27  LEU B C   
4298  O O   . LEU B 27  ? 0.2993 0.3887 0.3715 -0.0044 -0.0322 0.0151  27  LEU B O   
4299  C CB  . LEU B 27  ? 0.2542 0.3418 0.3191 -0.0192 -0.0453 0.0069  27  LEU B CB  
4300  C CG  . LEU B 27  ? 0.1723 0.2640 0.2342 -0.0254 -0.0532 0.0020  27  LEU B CG  
4301  C CD1 . LEU B 27  ? 0.2552 0.3361 0.3037 -0.0276 -0.0527 -0.0066 27  LEU B CD1 
4302  C CD2 . LEU B 27  ? 0.2044 0.3031 0.2811 -0.0314 -0.0573 0.0009  27  LEU B CD2 
4303  N N   . PRO B 28  ? 0.2457 0.3467 0.3339 -0.0100 -0.0322 0.0183  28  PRO B N   
4304  C CA  . PRO B 28  ? 0.2293 0.3318 0.3181 -0.0045 -0.0242 0.0188  28  PRO B CA  
4305  C C   . PRO B 28  ? 0.2377 0.3301 0.3156 -0.0047 -0.0204 0.0143  28  PRO B C   
4306  O O   . PRO B 28  ? 0.2066 0.3034 0.2848 -0.0012 -0.0143 0.0143  28  PRO B O   
4307  C CB  . PRO B 28  ? 0.1467 0.2631 0.2498 -0.0060 -0.0226 0.0245  28  PRO B CB  
4308  C CG  . PRO B 28  ? 0.1491 0.2637 0.2565 -0.0140 -0.0285 0.0252  28  PRO B CG  
4309  C CD  . PRO B 28  ? 0.1889 0.2959 0.2880 -0.0163 -0.0353 0.0204  28  PRO B CD  
4310  N N   . TRP B 29  ? 0.2719 0.3530 0.3407 -0.0083 -0.0237 0.0101  29  TRP B N   
4311  C CA  . TRP B 29  ? 0.1894 0.2621 0.2508 -0.0091 -0.0208 0.0068  29  TRP B CA  
4312  C C   . TRP B 29  ? 0.2407 0.3103 0.2941 -0.0034 -0.0152 0.0034  29  TRP B C   
4313  O O   . TRP B 29  ? 0.2641 0.3324 0.3138 -0.0029 -0.0118 0.0022  29  TRP B O   
4314  C CB  . TRP B 29  ? 0.2484 0.3103 0.3031 -0.0136 -0.0253 0.0016  29  TRP B CB  
4315  C CG  . TRP B 29  ? 0.2814 0.3456 0.3456 -0.0200 -0.0305 0.0021  29  TRP B CG  
4316  C CD1 . TRP B 29  ? 0.2971 0.3606 0.3599 -0.0241 -0.0367 -0.0024 29  TRP B CD1 
4317  C CD2 . TRP B 29  ? 0.3589 0.4278 0.4369 -0.0233 -0.0302 0.0070  29  TRP B CD2 
4318  N NE1 . TRP B 29  ? 0.3766 0.4431 0.4525 -0.0299 -0.0404 -0.0025 29  TRP B NE1 
4319  C CE2 . TRP B 29  ? 0.3988 0.4677 0.4853 -0.0297 -0.0364 0.0041  29  TRP B CE2 
4320  C CE3 . TRP B 29  ? 0.3667 0.4414 0.4512 -0.0218 -0.0251 0.0139  29  TRP B CE3 
4321  C CZ2 . TRP B 29  ? 0.5022 0.5743 0.6059 -0.0347 -0.0376 0.0081  29  TRP B CZ2 
4322  C CZ3 . TRP B 29  ? 0.3415 0.4207 0.4418 -0.0266 -0.0261 0.0199  29  TRP B CZ3 
4323  C CH2 . TRP B 29  ? 0.4440 0.5206 0.5549 -0.0331 -0.0322 0.0170  29  TRP B CH2 
4324  N N   . THR B 30  ? 0.2278 0.2968 0.2802 0.0007  -0.0145 0.0021  30  THR B N   
4325  C CA  . THR B 30  ? 0.2003 0.2673 0.2493 0.0059  -0.0089 -0.0024 30  THR B CA  
4326  C C   . THR B 30  ? 0.1789 0.2590 0.2348 0.0092  -0.0037 -0.0017 30  THR B C   
4327  O O   . THR B 30  ? 0.2151 0.2973 0.2666 0.0113  0.0007  -0.0060 30  THR B O   
4328  C CB  . THR B 30  ? 0.2555 0.3179 0.3058 0.0095  -0.0092 -0.0032 30  THR B CB  
4329  O OG1 . THR B 30  ? 0.2461 0.2999 0.2886 0.0061  -0.0137 -0.0027 30  THR B OG1 
4330  C CG2 . THR B 30  ? 0.1481 0.2068 0.1974 0.0140  -0.0036 -0.0096 30  THR B CG2 
4331  N N   . PHE B 31  ? 0.1435 0.2348 0.2103 0.0096  -0.0042 0.0034  31  PHE B N   
4332  C CA  . PHE B 31  ? 0.1426 0.2493 0.2163 0.0128  0.0014  0.0040  31  PHE B CA  
4333  C C   . PHE B 31  ? 0.1519 0.2649 0.2220 0.0098  0.0033  0.0072  31  PHE B C   
4334  O O   . PHE B 31  ? 0.1874 0.3090 0.2538 0.0126  0.0085  0.0042  31  PHE B O   
4335  C CB  . PHE B 31  ? 0.1746 0.2926 0.2621 0.0135  0.0004  0.0097  31  PHE B CB  
4336  C CG  . PHE B 31  ? 0.1426 0.2790 0.2381 0.0171  0.0069  0.0100  31  PHE B CG  
4337  C CD1 . PHE B 31  ? 0.1442 0.2858 0.2445 0.0239  0.0122  0.0031  31  PHE B CD1 
4338  C CD2 . PHE B 31  ? 0.1571 0.3063 0.2566 0.0136  0.0082  0.0171  31  PHE B CD2 
4339  C CE1 . PHE B 31  ? 0.1457 0.3066 0.2530 0.0274  0.0188  0.0016  31  PHE B CE1 
4340  C CE2 . PHE B 31  ? 0.1429 0.3119 0.2487 0.0169  0.0149  0.0179  31  PHE B CE2 
4341  C CZ  . PHE B 31  ? 0.1445 0.3202 0.2534 0.0239  0.0203  0.0093  31  PHE B CZ  
4342  N N   . PHE B 32  ? 0.2251 0.3351 0.2976 0.0039  -0.0012 0.0134  32  PHE B N   
4343  C CA  . PHE B 32  ? 0.2262 0.3438 0.3007 0.0009  0.0005  0.0198  32  PHE B CA  
4344  C C   . PHE B 32  ? 0.2191 0.3309 0.2826 0.0014  0.0021  0.0167  32  PHE B C   
4345  O O   . PHE B 32  ? 0.2229 0.3456 0.2864 0.0014  0.0053  0.0219  32  PHE B O   
4346  C CB  . PHE B 32  ? 0.1739 0.2879 0.2578 -0.0058 -0.0048 0.0263  32  PHE B CB  
4347  C CG  . PHE B 32  ? 0.1433 0.2709 0.2415 -0.0071 -0.0048 0.0329  32  PHE B CG  
4348  C CD1 . PHE B 32  ? 0.1432 0.2894 0.2469 -0.0046 0.0013  0.0384  32  PHE B CD1 
4349  C CD2 . PHE B 32  ? 0.2230 0.3473 0.3293 -0.0108 -0.0108 0.0333  32  PHE B CD2 
4350  C CE1 . PHE B 32  ? 0.1434 0.3035 0.2615 -0.0058 0.0018  0.0447  32  PHE B CE1 
4351  C CE2 . PHE B 32  ? 0.1771 0.3152 0.2981 -0.0122 -0.0111 0.0394  32  PHE B CE2 
4352  C CZ  . PHE B 32  ? 0.1572 0.3126 0.2847 -0.0096 -0.0045 0.0454  32  PHE B CZ  
4353  N N   . HIS B 33  ? 0.1419 0.2384 0.1964 0.0019  -0.0001 0.0093  33  HIS B N   
4354  C CA  . HIS B 33  ? 0.1419 0.2340 0.1870 0.0029  0.0014  0.0056  33  HIS B CA  
4355  C C   . HIS B 33  ? 0.2060 0.3040 0.2450 0.0083  0.0061  -0.0023 33  HIS B C   
4356  O O   . HIS B 33  ? 0.2304 0.3314 0.2627 0.0094  0.0081  -0.0049 33  HIS B O   
4357  C CB  . HIS B 33  ? 0.1422 0.2161 0.1818 0.0002  -0.0028 0.0013  33  HIS B CB  
4358  C CG  . HIS B 33  ? 0.1821 0.2504 0.2279 -0.0052 -0.0068 0.0063  33  HIS B CG  
4359  N ND1 . HIS B 33  ? 0.2328 0.3046 0.2831 -0.0069 -0.0061 0.0126  33  HIS B ND1 
4360  C CD2 . HIS B 33  ? 0.1688 0.2293 0.2189 -0.0094 -0.0116 0.0055  33  HIS B CD2 
4361  C CE1 . HIS B 33  ? 0.2094 0.2736 0.2686 -0.0117 -0.0100 0.0150  33  HIS B CE1 
4362  N NE2 . HIS B 33  ? 0.1961 0.2538 0.2545 -0.0135 -0.0135 0.0096  33  HIS B NE2 
4363  N N   . ALA B 34  ? 0.1501 0.2502 0.1930 0.0117  0.0078  -0.0066 34  ALA B N   
4364  C CA  . ALA B 34  ? 0.1434 0.2509 0.1848 0.0169  0.0129  -0.0156 34  ALA B CA  
4365  C C   . ALA B 34  ? 0.1866 0.3164 0.2293 0.0188  0.0177  -0.0138 34  ALA B C   
4366  O O   . ALA B 34  ? 0.2302 0.3695 0.2673 0.0214  0.0213  -0.0209 34  ALA B O   
4367  C CB  . ALA B 34  ? 0.1443 0.2474 0.1936 0.0204  0.0135  -0.0200 34  ALA B CB  
4368  N N   . VAL B 35  ? 0.1448 0.2853 0.1951 0.0172  0.0179  -0.0045 35  VAL B N   
4369  C CA  . VAL B 35  ? 0.2456 0.4102 0.2975 0.0186  0.0230  -0.0006 35  VAL B CA  
4370  C C   . VAL B 35  ? 0.2694 0.4406 0.3157 0.0153  0.0224  0.0084  35  VAL B C   
4371  O O   . VAL B 35  ? 0.3459 0.5397 0.3911 0.0164  0.0267  0.0128  35  VAL B O   
4372  C CB  . VAL B 35  ? 0.1470 0.3224 0.2114 0.0180  0.0240  0.0072  35  VAL B CB  
4373  C CG1 . VAL B 35  ? 0.1548 0.3280 0.2272 0.0225  0.0253  -0.0009 35  VAL B CG1 
4374  C CG2 . VAL B 35  ? 0.2103 0.3747 0.2806 0.0118  0.0181  0.0181  35  VAL B CG2 
4375  N N   . LYS B 36  ? 0.1648 0.3185 0.2085 0.0115  0.0173  0.0117  36  LYS B N   
4376  C CA  . LYS B 36  ? 0.2570 0.4148 0.2992 0.0086  0.0162  0.0216  36  LYS B CA  
4377  C C   . LYS B 36  ? 0.2831 0.4333 0.3149 0.0096  0.0149  0.0155  36  LYS B C   
4378  O O   . LYS B 36  ? 0.3845 0.5485 0.4122 0.0101  0.0162  0.0205  36  LYS B O   
4379  C CB  . LYS B 36  ? 0.2771 0.4223 0.3297 0.0030  0.0115  0.0315  36  LYS B CB  
4380  C CG  . LYS B 36  ? 0.2240 0.3804 0.2842 0.0000  0.0119  0.0468  36  LYS B CG  
4381  C CD  . LYS B 36  ? 0.2635 0.4057 0.3378 -0.0058 0.0072  0.0540  36  LYS B CD  
4382  C CE  . LYS B 36  ? 0.2352 0.3538 0.3063 -0.0074 0.0023  0.0463  36  LYS B CE  
4383  N NZ  . LYS B 36  ? 0.3307 0.4487 0.3911 -0.0045 0.0032  0.0433  36  LYS B NZ  
4384  N N   . ASP B 37  ? 0.1893 0.3198 0.2173 0.0098  0.0123  0.0057  37  ASP B N   
4385  C CA  . ASP B 37  ? 0.2076 0.3293 0.2280 0.0098  0.0106  0.0010  37  ASP B CA  
4386  C C   . ASP B 37  ? 0.1780 0.2954 0.1917 0.0131  0.0122  -0.0133 37  ASP B C   
4387  O O   . ASP B 37  ? 0.2607 0.3841 0.2681 0.0145  0.0130  -0.0181 37  ASP B O   
4388  C CB  . ASP B 37  ? 0.2866 0.3876 0.3103 0.0059  0.0057  0.0038  37  ASP B CB  
4389  C CG  . ASP B 37  ? 0.3288 0.4322 0.3620 0.0023  0.0039  0.0170  37  ASP B CG  
4390  O OD1 . ASP B 37  ? 0.3428 0.4571 0.3763 0.0027  0.0047  0.0245  37  ASP B OD1 
4391  O OD2 . ASP B 37  ? 0.2950 0.3904 0.3367 -0.0011 0.0014  0.0202  37  ASP B OD2 
4392  N N   . TYR B 38  ? 0.1490 0.2568 0.1656 0.0142  0.0125  -0.0197 38  TYR B N   
4393  C CA  . TYR B 38  ? 0.1837 0.2837 0.1977 0.0166  0.0137  -0.0321 38  TYR B CA  
4394  C C   . TYR B 38  ? 0.2480 0.3651 0.2603 0.0204  0.0181  -0.0415 38  TYR B C   
4395  O O   . TYR B 38  ? 0.2392 0.3521 0.2494 0.0217  0.0188  -0.0521 38  TYR B O   
4396  C CB  . TYR B 38  ? 0.2295 0.3170 0.2495 0.0173  0.0130  -0.0342 38  TYR B CB  
4397  C CG  . TYR B 38  ? 0.1427 0.2149 0.1624 0.0133  0.0083  -0.0278 38  TYR B CG  
4398  C CD1 . TYR B 38  ? 0.1746 0.2390 0.1889 0.0102  0.0057  -0.0259 38  TYR B CD1 
4399  C CD2 . TYR B 38  ? 0.1595 0.2267 0.1849 0.0129  0.0063  -0.0243 38  TYR B CD2 
4400  C CE1 . TYR B 38  ? 0.1926 0.2450 0.2069 0.0067  0.0018  -0.0225 38  TYR B CE1 
4401  C CE2 . TYR B 38  ? 0.1500 0.2064 0.1741 0.0090  0.0018  -0.0201 38  TYR B CE2 
4402  C CZ  . TYR B 38  ? 0.2134 0.2625 0.2318 0.0058  -0.0003 -0.0201 38  TYR B CZ  
4403  O OH  . TYR B 38  ? 0.1792 0.2192 0.1967 0.0020  -0.0045 -0.0183 38  TYR B OH  
4404  N N   . TYR B 39  ? 0.1884 0.3261 0.2022 0.0221  0.0213  -0.0386 39  TYR B N   
4405  C CA  . TYR B 39  ? 0.1575 0.3157 0.1677 0.0254  0.0254  -0.0486 39  TYR B CA  
4406  C C   . TYR B 39  ? 0.2057 0.3806 0.2071 0.0241  0.0246  -0.0421 39  TYR B C   
4407  O O   . TYR B 39  ? 0.1952 0.3809 0.1906 0.0255  0.0254  -0.0514 39  TYR B O   
4408  C CB  . TYR B 39  ? 0.2059 0.3816 0.2223 0.0286  0.0303  -0.0513 39  TYR B CB  
4409  C CG  . TYR B 39  ? 0.1802 0.3807 0.1924 0.0319  0.0349  -0.0633 39  TYR B CG  
4410  C CD1 . TYR B 39  ? 0.2626 0.4601 0.2777 0.0347  0.0369  -0.0817 39  TYR B CD1 
4411  C CD2 . TYR B 39  ? 0.2496 0.4779 0.2555 0.0320  0.0373  -0.0564 39  TYR B CD2 
4412  C CE1 . TYR B 39  ? 0.3808 0.6026 0.3925 0.0374  0.0408  -0.0954 39  TYR B CE1 
4413  C CE2 . TYR B 39  ? 0.1817 0.4365 0.1820 0.0349  0.0414  -0.0684 39  TYR B CE2 
4414  C CZ  . TYR B 39  ? 0.3413 0.5896 0.3445 0.0369  0.0418  -0.0879 39  TYR B CZ  
4415  O OH  . TYR B 39  ? 0.4566 0.7207 0.4562 0.0370  0.0413  -0.0973 39  TYR B OH  
4416  N N   . ASP B 40  ? 0.2612 0.4392 0.2636 0.0214  0.0228  -0.0258 40  ASP B N   
4417  C CA  . ASP B 40  ? 0.1925 0.3897 0.1894 0.0207  0.0225  -0.0162 40  ASP B CA  
4418  C C   . ASP B 40  ? 0.2724 0.4592 0.2649 0.0194  0.0183  -0.0162 40  ASP B C   
4419  O O   . ASP B 40  ? 0.3584 0.5634 0.3445 0.0203  0.0181  -0.0147 40  ASP B O   
4420  C CB  . ASP B 40  ? 0.1594 0.3619 0.1630 0.0181  0.0221  0.0024  40  ASP B CB  
4421  C CG  . ASP B 40  ? 0.3307 0.5572 0.3365 0.0198  0.0273  0.0050  40  ASP B CG  
4422  O OD1 . ASP B 40  ? 0.3841 0.6381 0.3829 0.0220  0.0307  0.0041  40  ASP B OD1 
4423  O OD2 . ASP B 40  ? 0.4086 0.6286 0.4232 0.0191  0.0281  0.0076  40  ASP B OD2 
4424  N N   . MET B 41  ? 0.1960 0.3559 0.1917 0.0173  0.0150  -0.0177 41  MET B N   
4425  C CA  . MET B 41  ? 0.2318 0.3818 0.2249 0.0161  0.0115  -0.0178 41  MET B CA  
4426  C C   . MET B 41  ? 0.2457 0.4047 0.2319 0.0183  0.0123  -0.0311 41  MET B C   
4427  O O   . MET B 41  ? 0.2764 0.4472 0.2589 0.0185  0.0105  -0.0274 41  MET B O   
4428  C CB  . MET B 41  ? 0.2462 0.3680 0.2433 0.0137  0.0088  -0.0190 41  MET B CB  
4429  C CG  . MET B 41  ? 0.3431 0.4552 0.3428 0.0115  0.0052  -0.0115 41  MET B CG  
4430  S SD  . MET B 41  ? 0.2760 0.4018 0.2831 0.0103  0.0042  0.0078  41  MET B SD  
4431  C CE  . MET B 41  ? 0.2420 0.3475 0.2568 0.0080  0.0001  0.0119  41  MET B CE  
4432  N N   . PRO B 42  ? 0.1805 0.3356 0.1666 0.0200  0.0146  -0.0464 42  PRO B N   
4433  C CA  . PRO B 42  ? 0.1589 0.3249 0.1409 0.0215  0.0153  -0.0604 42  PRO B CA  
4434  C C   . PRO B 42  ? 0.2034 0.4013 0.1802 0.0239  0.0180  -0.0641 42  PRO B C   
4435  O O   . PRO B 42  ? 0.1709 0.3828 0.1434 0.0248  0.0178  -0.0753 42  PRO B O   
4436  C CB  . PRO B 42  ? 0.1580 0.3067 0.1460 0.0221  0.0172  -0.0744 42  PRO B CB  
4437  C CG  . PRO B 42  ? 0.1993 0.3420 0.1926 0.0227  0.0190  -0.0690 42  PRO B CG  
4438  C CD  . PRO B 42  ? 0.2466 0.3862 0.2388 0.0203  0.0163  -0.0516 42  PRO B CD  
4439  N N   . ALA B 43  ? 0.1980 0.4097 0.1751 0.0248  0.0206  -0.0554 43  ALA B N   
4440  C CA  . ALA B 43  ? 0.1745 0.4200 0.1458 0.0271  0.0240  -0.0586 43  ALA B CA  
4441  C C   . ALA B 43  ? 0.1925 0.4605 0.1559 0.0265  0.0214  -0.0463 43  ALA B C   
4442  O O   . ALA B 43  ? 0.2258 0.5248 0.1822 0.0282  0.0231  -0.0505 43  ALA B O   
4443  C CB  . ALA B 43  ? 0.1753 0.4299 0.1506 0.0282  0.0283  -0.0526 43  ALA B CB  
4444  N N   . TYR B 44  ? 0.2439 0.4976 0.2099 0.0242  0.0171  -0.0310 44  TYR B N   
4445  C CA  . TYR B 44  ? 0.1945 0.4674 0.1560 0.0241  0.0139  -0.0188 44  TYR B CA  
4446  C C   . TYR B 44  ? 0.2551 0.5422 0.2091 0.0253  0.0122  -0.0338 44  TYR B C   
4447  O O   . TYR B 44  ? 0.2979 0.6142 0.2451 0.0262  0.0107  -0.0278 44  TYR B O   
4448  C CB  . TYR B 44  ? 0.1741 0.4243 0.1435 0.0218  0.0096  -0.0036 44  TYR B CB  
4449  C CG  . TYR B 44  ? 0.1735 0.4198 0.1514 0.0200  0.0102  0.0159  44  TYR B CG  
4450  C CD1 . TYR B 44  ? 0.1898 0.4118 0.1753 0.0182  0.0111  0.0151  44  TYR B CD1 
4451  C CD2 . TYR B 44  ? 0.1793 0.4472 0.1593 0.0200  0.0095  0.0359  44  TYR B CD2 
4452  C CE1 . TYR B 44  ? 0.1679 0.3867 0.1632 0.0160  0.0112  0.0316  44  TYR B CE1 
4453  C CE2 . TYR B 44  ? 0.1796 0.4433 0.1706 0.0178  0.0101  0.0540  44  TYR B CE2 
4454  C CZ  . TYR B 44  ? 0.1737 0.4125 0.1726 0.0156  0.0109  0.0508  44  TYR B CZ  
4455  O OH  . TYR B 44  ? 0.2225 0.4576 0.2344 0.0129  0.0112  0.0675  44  TYR B OH  
4456  N N   . LEU B 45  ? 0.2153 0.4834 0.1716 0.0251  0.0123  -0.0527 45  LEU B N   
4457  C CA  . LEU B 45  ? 0.2770 0.5549 0.2301 0.0254  0.0102  -0.0683 45  LEU B CA  
4458  C C   . LEU B 45  ? 0.3647 0.6676 0.3191 0.0261  0.0105  -0.0761 45  LEU B C   
4459  O O   . LEU B 45  ? 0.3711 0.6877 0.3261 0.0257  0.0073  -0.0828 45  LEU B O   
4460  C CB  . LEU B 45  ? 0.1788 0.4267 0.1398 0.0243  0.0104  -0.0841 45  LEU B CB  
4461  C CG  . LEU B 45  ? 0.1708 0.3893 0.1362 0.0223  0.0078  -0.0755 45  LEU B CG  
4462  C CD1 . LEU B 45  ? 0.1699 0.3595 0.1429 0.0214  0.0099  -0.0856 45  LEU B CD1 
4463  C CD2 . LEU B 45  ? 0.2057 0.4282 0.1701 0.0216  0.0034  -0.0756 45  LEU B CD2 
4464  N N   . LYS B 46  ? 0.2721 0.5825 0.2276 0.0272  0.0143  -0.0761 46  LYS B N   
4465  C CA  . LYS B 46  ? 0.2947 0.6309 0.2510 0.0279  0.0146  -0.0842 46  LYS B CA  
4466  C C   . LYS B 46  ? 0.2159 0.5859 0.1653 0.0286  0.0135  -0.0682 46  LYS B C   
4467  O O   . LYS B 46  ? 0.3516 0.7479 0.3007 0.0292  0.0131  -0.0747 46  LYS B O   
4468  C CB  . LYS B 46  ? 0.2485 0.5794 0.2098 0.0290  0.0192  -0.0921 46  LYS B CB  
4469  C CG  . LYS B 46  ? 0.3817 0.6791 0.3520 0.0286  0.0207  -0.1039 46  LYS B CG  
4470  C CD  . LYS B 46  ? 0.5574 0.8527 0.5347 0.0302  0.0249  -0.1125 46  LYS B CD  
4471  C CE  . LYS B 46  ? 0.3603 0.6682 0.3333 0.0316  0.0285  -0.0982 46  LYS B CE  
4472  N NZ  . LYS B 46  ? 0.2978 0.5897 0.2796 0.0333  0.0329  -0.1025 46  LYS B NZ  
4473  N N   . ASP B 47  ? 0.2426 0.6134 0.1880 0.0285  0.0131  -0.0467 47  ASP B N   
4474  C CA  . ASP B 47  ? 0.2184 0.6195 0.1604 0.0289  0.0119  -0.0272 47  ASP B CA  
4475  C C   . ASP B 47  ? 0.2746 0.6793 0.2150 0.0286  0.0073  -0.0146 47  ASP B C   
4476  O O   . ASP B 47  ? 0.2242 0.6535 0.1645 0.0290  0.0060  0.0037  47  ASP B O   
4477  C CB  . ASP B 47  ? 0.2490 0.6514 0.1921 0.0288  0.0155  -0.0075 47  ASP B CB  
4478  C CG  . ASP B 47  ? 0.5555 0.9556 0.5009 0.0294  0.0202  -0.0183 47  ASP B CG  
4479  O OD1 . ASP B 47  ? 0.7536 1.1474 0.7005 0.0301  0.0206  -0.0406 47  ASP B OD1 
4480  O OD2 . ASP B 47  ? 0.7903 1.1946 0.7380 0.0292  0.0234  -0.0035 47  ASP B OD2 
4481  N N   . PHE B 48  ? 0.3034 0.6846 0.2440 0.0279  0.0048  -0.0232 48  PHE B N   
4482  C CA  . PHE B 48  ? 0.2088 0.5912 0.1487 0.0278  -0.0002 -0.0120 48  PHE B CA  
4483  C C   . PHE B 48  ? 0.2194 0.5895 0.1607 0.0272  -0.0028 -0.0325 48  PHE B C   
4484  O O   . PHE B 48  ? 0.2939 0.6368 0.2376 0.0263  -0.0014 -0.0470 48  PHE B O   
4485  C CB  . PHE B 48  ? 0.2335 0.5936 0.1763 0.0272  -0.0015 0.0070  48  PHE B CB  
4486  C CG  . PHE B 48  ? 0.2844 0.6554 0.2308 0.0270  0.0007  0.0308  48  PHE B CG  
4487  C CD1 . PHE B 48  ? 0.2337 0.6283 0.1824 0.0277  -0.0020 0.0536  48  PHE B CD1 
4488  C CD2 . PHE B 48  ? 0.2464 0.6039 0.1968 0.0260  0.0055  0.0310  48  PHE B CD2 
4489  C CE1 . PHE B 48  ? 0.2864 0.6901 0.2422 0.0271  0.0003  0.0765  48  PHE B CE1 
4490  C CE2 . PHE B 48  ? 0.2327 0.6007 0.1885 0.0253  0.0076  0.0530  48  PHE B CE2 
4491  C CZ  . PHE B 48  ? 0.2116 0.6034 0.1693 0.0257  0.0052  0.0763  48  PHE B CZ  
4492  N N   . GLU B 49  ? 0.2992 0.6894 0.2409 0.0275  -0.0064 -0.0327 49  GLU B N   
4493  C CA  . GLU B 49  ? 0.2716 0.6539 0.2168 0.0266  -0.0087 -0.0519 49  GLU B CA  
4494  C C   . GLU B 49  ? 0.2743 0.6343 0.2206 0.0261  -0.0127 -0.0475 49  GLU B C   
4495  O O   . GLU B 49  ? 0.3310 0.6993 0.2792 0.0262  -0.0169 -0.0471 49  GLU B O   
4496  C CB  . GLU B 49  ? 0.3738 0.7891 0.3193 0.0270  -0.0106 -0.0552 49  GLU B CB  
4497  C CG  . GLU B 49  ? 0.6347 1.0488 0.5862 0.0256  -0.0105 -0.0807 49  GLU B CG  
4498  C CD  . GLU B 49  ? 0.6553 1.0601 0.6109 0.0250  -0.0065 -0.0962 49  GLU B CD  
4499  O OE1 . GLU B 49  ? 0.6932 1.1068 0.6452 0.0261  -0.0037 -0.0889 49  GLU B OE1 
4500  O OE2 . GLU B 49  ? 0.6128 1.0011 0.5768 0.0233  -0.0061 -0.1148 49  GLU B OE2 
4501  N N   . ILE B 50  ? 0.2956 0.6287 0.2413 0.0256  -0.0116 -0.0445 50  ILE B N   
4502  C CA  . ILE B 50  ? 0.1895 0.4914 0.1451 0.0245  -0.0139 -0.0413 50  ILE B CA  
4503  C C   . ILE B 50  ? 0.1880 0.4586 0.1477 0.0226  -0.0102 -0.0583 50  ILE B C   
4504  O O   . ILE B 50  ? 0.1999 0.4724 0.1562 0.0226  -0.0062 -0.0705 50  ILE B O   
4505  C CB  . ILE B 50  ? 0.1836 0.4727 0.1472 0.0249  -0.0148 -0.0168 50  ILE B CB  
4506  C CG1 . ILE B 50  ? 0.1808 0.4557 0.1451 0.0241  -0.0101 -0.0123 50  ILE B CG1 
4507  C CG2 . ILE B 50  ? 0.2020 0.5228 0.1643 0.0270  -0.0184 0.0030  50  ILE B CG2 
4508  C CD1 . ILE B 50  ? 0.1745 0.4176 0.1505 0.0229  -0.0101 -0.0010 50  ILE B CD1 
4509  N N   . LYS B 51  ? 0.1766 0.4195 0.1446 0.0213  -0.0113 -0.0586 51  LYS B N   
4510  C CA  . LYS B 51  ? 0.1891 0.4030 0.1615 0.0194  -0.0080 -0.0717 51  LYS B CA  
4511  C C   . LYS B 51  ? 0.1619 0.3490 0.1392 0.0187  -0.0065 -0.0597 51  LYS B C   
4512  O O   . LYS B 51  ? 0.1896 0.3715 0.1715 0.0190  -0.0088 -0.0455 51  LYS B O   
4513  C CB  . LYS B 51  ? 0.2104 0.4157 0.1883 0.0179  -0.0097 -0.0835 51  LYS B CB  
4514  C CG  . LYS B 51  ? 0.2038 0.4269 0.1801 0.0172  -0.0099 -0.1032 51  LYS B CG  
4515  C CD  . LYS B 51  ? 0.2127 0.4658 0.1863 0.0181  -0.0149 -0.1019 51  LYS B CD  
4516  C CE  . LYS B 51  ? 0.3251 0.5887 0.3066 0.0167  -0.0136 -0.1165 51  LYS B CE  
4517  N NZ  . LYS B 51  ? 0.3920 0.6772 0.3697 0.0181  -0.0117 -0.1168 51  LYS B NZ  
4518  N N   . LEU B 52  ? 0.1825 0.3535 0.1601 0.0178  -0.0028 -0.0659 52  LEU B N   
4519  C CA  . LEU B 52  ? 0.1547 0.3014 0.1364 0.0167  -0.0016 -0.0574 52  LEU B CA  
4520  C C   . LEU B 52  ? 0.1519 0.2777 0.1361 0.0152  0.0012  -0.0694 52  LEU B C   
4521  O O   . LEU B 52  ? 0.1542 0.2852 0.1379 0.0157  0.0034  -0.0817 52  LEU B O   
4522  C CB  . LEU B 52  ? 0.1753 0.3294 0.1555 0.0174  -0.0002 -0.0462 52  LEU B CB  
4523  C CG  . LEU B 52  ? 0.1596 0.3344 0.1393 0.0186  -0.0023 -0.0300 52  LEU B CG  
4524  C CD1 . LEU B 52  ? 0.1615 0.3463 0.1397 0.0189  0.0003  -0.0222 52  LEU B CD1 
4525  C CD2 . LEU B 52  ? 0.1578 0.3186 0.1461 0.0178  -0.0052 -0.0172 52  LEU B CD2 
4526  N N   . ASN B 53  ? 0.1482 0.2514 0.1361 0.0136  0.0011  -0.0657 53  ASN B N   
4527  C CA  . ASN B 53  ? 0.1465 0.2309 0.1370 0.0121  0.0035  -0.0740 53  ASN B CA  
4528  C C   . ASN B 53  ? 0.1596 0.2303 0.1504 0.0113  0.0044  -0.0670 53  ASN B C   
4529  O O   . ASN B 53  ? 0.1952 0.2658 0.1860 0.0111  0.0029  -0.0564 53  ASN B O   
4530  C CB  . ASN B 53  ? 0.1545 0.2274 0.1484 0.0104  0.0029  -0.0772 53  ASN B CB  
4531  C CG  . ASN B 53  ? 0.1503 0.2382 0.1452 0.0110  0.0011  -0.0827 53  ASN B CG  
4532  O OD1 . ASN B 53  ? 0.1826 0.2777 0.1790 0.0107  0.0020  -0.0944 53  ASN B OD1 
4533  N ND2 . ASN B 53  ? 0.1616 0.2550 0.1575 0.0117  -0.0018 -0.0746 53  ASN B ND2 
4534  N N   . PHE B 54  ? 0.1447 0.2043 0.1374 0.0108  0.0067  -0.0729 54  PHE B N   
4535  C CA  . PHE B 54  ? 0.1437 0.1939 0.1370 0.0103  0.0072  -0.0671 54  PHE B CA  
4536  C C   . PHE B 54  ? 0.1440 0.1777 0.1398 0.0088  0.0085  -0.0703 54  PHE B C   
4537  O O   . PHE B 54  ? 0.1636 0.1947 0.1632 0.0088  0.0103  -0.0783 54  PHE B O   
4538  C CB  . PHE B 54  ? 0.1583 0.2199 0.1524 0.0125  0.0089  -0.0680 54  PHE B CB  
4539  C CG  . PHE B 54  ? 0.1754 0.2572 0.1662 0.0140  0.0083  -0.0644 54  PHE B CG  
4540  C CD1 . PHE B 54  ? 0.1489 0.2348 0.1392 0.0135  0.0069  -0.0520 54  PHE B CD1 
4541  C CD2 . PHE B 54  ? 0.1594 0.2578 0.1484 0.0155  0.0091  -0.0729 54  PHE B CD2 
4542  C CE1 . PHE B 54  ? 0.1669 0.2731 0.1550 0.0147  0.0066  -0.0460 54  PHE B CE1 
4543  C CE2 . PHE B 54  ? 0.1796 0.3003 0.1643 0.0169  0.0084  -0.0682 54  PHE B CE2 
4544  C CZ  . PHE B 54  ? 0.1747 0.2993 0.1589 0.0165  0.0074  -0.0535 54  PHE B CZ  
4545  N N   . ASN B 55  ? 0.1558 0.1796 0.1504 0.0074  0.0075  -0.0636 55  ASN B N   
4546  C CA  . ASN B 55  ? 0.1450 0.1563 0.1407 0.0060  0.0084  -0.0636 55  ASN B CA  
4547  C C   . ASN B 55  ? 0.1577 0.1684 0.1551 0.0067  0.0081  -0.0590 55  ASN B C   
4548  O O   . ASN B 55  ? 0.2173 0.2312 0.2130 0.0063  0.0060  -0.0531 55  ASN B O   
4549  C CB  . ASN B 55  ? 0.1452 0.1484 0.1373 0.0034  0.0071  -0.0609 55  ASN B CB  
4550  C CG  . ASN B 55  ? 0.1840 0.1782 0.1755 0.0017  0.0082  -0.0598 55  ASN B CG  
4551  O OD1 . ASN B 55  ? 0.2414 0.2326 0.2368 0.0019  0.0106  -0.0627 55  ASN B OD1 
4552  N ND2 . ASN B 55  ? 0.1526 0.1436 0.1403 0.0000  0.0063  -0.0553 55  ASN B ND2 
4553  N N   . LEU B 56  ? 0.1638 0.1706 0.1667 0.0078  0.0100  -0.0610 56  LEU B N   
4554  C CA  . LEU B 56  ? 0.1494 0.1560 0.1563 0.0090  0.0097  -0.0561 56  LEU B CA  
4555  C C   . LEU B 56  ? 0.1529 0.1499 0.1611 0.0076  0.0095  -0.0517 56  LEU B C   
4556  O O   . LEU B 56  ? 0.2018 0.1933 0.2156 0.0078  0.0119  -0.0544 56  LEU B O   
4557  C CB  . LEU B 56  ? 0.1507 0.1639 0.1663 0.0126  0.0124  -0.0616 56  LEU B CB  
4558  C CG  . LEU B 56  ? 0.1530 0.1793 0.1671 0.0141  0.0135  -0.0684 56  LEU B CG  
4559  C CD1 . LEU B 56  ? 0.1824 0.2146 0.2064 0.0175  0.0169  -0.0775 56  LEU B CD1 
4560  C CD2 . LEU B 56  ? 0.2011 0.2370 0.2096 0.0139  0.0117  -0.0616 56  LEU B CD2 
4561  N N   . THR B 57  ? 0.1711 0.1673 0.1749 0.0060  0.0065  -0.0446 57  THR B N   
4562  C CA  . THR B 57  ? 0.1583 0.1495 0.1621 0.0048  0.0059  -0.0388 57  THR B CA  
4563  C C   . THR B 57  ? 0.2009 0.1924 0.2160 0.0080  0.0069  -0.0351 57  THR B C   
4564  O O   . THR B 57  ? 0.2456 0.2426 0.2656 0.0104  0.0064  -0.0351 57  THR B O   
4565  C CB  . THR B 57  ? 0.1594 0.1528 0.1551 0.0020  0.0019  -0.0340 57  THR B CB  
4566  O OG1 . THR B 57  ? 0.1742 0.1735 0.1725 0.0029  -0.0005 -0.0315 57  THR B OG1 
4567  C CG2 . THR B 57  ? 0.1745 0.1663 0.1623 -0.0007 0.0014  -0.0385 57  THR B CG2 
4568  N N   . PRO B 58  ? 0.1734 0.1594 0.1947 0.0082  0.0085  -0.0313 58  PRO B N   
4569  C CA  . PRO B 58  ? 0.1703 0.1553 0.2068 0.0118  0.0097  -0.0275 58  PRO B CA  
4570  C C   . PRO B 58  ? 0.1949 0.1861 0.2325 0.0131  0.0062  -0.0192 58  PRO B C   
4571  O O   . PRO B 58  ? 0.2233 0.2163 0.2742 0.0171  0.0071  -0.0185 58  PRO B O   
4572  C CB  . PRO B 58  ? 0.1770 0.1552 0.2194 0.0107  0.0116  -0.0216 58  PRO B CB  
4573  C CG  . PRO B 58  ? 0.1752 0.1507 0.2081 0.0072  0.0131  -0.0274 58  PRO B CG  
4574  C CD  . PRO B 58  ? 0.1698 0.1507 0.1873 0.0054  0.0100  -0.0302 58  PRO B CD  
4575  N N   . VAL B 59  ? 0.2187 0.2139 0.2440 0.0100  0.0020  -0.0140 59  VAL B N   
4576  C CA  . VAL B 59  ? 0.1798 0.1826 0.2067 0.0107  -0.0021 -0.0070 59  VAL B CA  
4577  C C   . VAL B 59  ? 0.1658 0.1742 0.1946 0.0120  -0.0023 -0.0120 59  VAL B C   
4578  O O   . VAL B 59  ? 0.1684 0.1833 0.2046 0.0140  -0.0042 -0.0075 59  VAL B O   
4579  C CB  . VAL B 59  ? 0.2169 0.2243 0.2307 0.0064  -0.0068 -0.0021 59  VAL B CB  
4580  C CG1 . VAL B 59  ? 0.1709 0.1782 0.1732 0.0027  -0.0077 -0.0101 59  VAL B CG1 
4581  C CG2 . VAL B 59  ? 0.1829 0.1996 0.2002 0.0069  -0.0117 0.0063  59  VAL B CG2 
4582  N N   . LEU B 60  ? 0.1906 0.1982 0.2138 0.0109  -0.0004 -0.0202 60  LEU B N   
4583  C CA  . LEU B 60  ? 0.1563 0.1713 0.1824 0.0124  0.0004  -0.0236 60  LEU B CA  
4584  C C   . LEU B 60  ? 0.1568 0.1739 0.1949 0.0173  0.0048  -0.0285 60  LEU B C   
4585  O O   . LEU B 60  ? 0.1967 0.2225 0.2415 0.0198  0.0056  -0.0284 60  LEU B O   
4586  C CB  . LEU B 60  ? 0.1525 0.1679 0.1695 0.0098  0.0006  -0.0287 60  LEU B CB  
4587  C CG  . LEU B 60  ? 0.1489 0.1740 0.1686 0.0114  0.0023  -0.0309 60  LEU B CG  
4588  C CD1 . LEU B 60  ? 0.1480 0.1805 0.1709 0.0104  -0.0006 -0.0244 60  LEU B CD1 
4589  C CD2 . LEU B 60  ? 0.1588 0.1847 0.1715 0.0097  0.0029  -0.0346 60  LEU B CD2 
4590  N N   . ILE B 61  ? 0.1593 0.1695 0.2018 0.0185  0.0080  -0.0336 61  ILE B N   
4591  C CA  . ILE B 61  ? 0.1616 0.1732 0.2183 0.0230  0.0123  -0.0406 61  ILE B CA  
4592  C C   . ILE B 61  ? 0.2104 0.2223 0.2818 0.0265  0.0119  -0.0338 61  ILE B C   
4593  O O   . ILE B 61  ? 0.2799 0.2979 0.3638 0.0308  0.0148  -0.0385 61  ILE B O   
4594  C CB  . ILE B 61  ? 0.1644 0.1677 0.2252 0.0227  0.0153  -0.0480 61  ILE B CB  
4595  C CG1 . ILE B 61  ? 0.1604 0.1665 0.2085 0.0200  0.0156  -0.0553 61  ILE B CG1 
4596  C CG2 . ILE B 61  ? 0.1688 0.1724 0.2480 0.0271  0.0196  -0.0567 61  ILE B CG2 
4597  C CD1 . ILE B 61  ? 0.1627 0.1608 0.2127 0.0183  0.0174  -0.0609 61  ILE B CD1 
4598  N N   . ASP B 62  ? 0.2186 0.2260 0.2894 0.0250  0.0085  -0.0226 62  ASP B N   
4599  C CA  . ASP B 62  ? 0.2037 0.2132 0.2886 0.0285  0.0071  -0.0137 62  ASP B CA  
4600  C C   . ASP B 62  ? 0.2047 0.2261 0.2905 0.0298  0.0054  -0.0122 62  ASP B C   
4601  O O   . ASP B 62  ? 0.2279 0.2540 0.3300 0.0347  0.0071  -0.0120 62  ASP B O   
4602  C CB  . ASP B 62  ? 0.2209 0.2277 0.3014 0.0260  0.0029  -0.0007 62  ASP B CB  
4603  C CG  . ASP B 62  ? 0.4775 0.4740 0.5650 0.0260  0.0055  0.0017  62  ASP B CG  
4604  O OD1 . ASP B 62  ? 0.5938 0.5846 0.6986 0.0295  0.0100  -0.0041 62  ASP B OD1 
4605  O OD2 . ASP B 62  ? 0.5226 0.5176 0.5995 0.0223  0.0033  0.0090  62  ASP B OD2 
4606  N N   . GLN B 63  ? 0.2342 0.2608 0.3049 0.0256  0.0021  -0.0114 63  GLN B N   
4607  C CA  . GLN B 63  ? 0.1614 0.1996 0.2343 0.0258  0.0002  -0.0086 63  GLN B CA  
4608  C C   . GLN B 63  ? 0.1587 0.2047 0.2374 0.0291  0.0054  -0.0173 63  GLN B C   
4609  O O   . GLN B 63  ? 0.2855 0.3412 0.3756 0.0324  0.0065  -0.0158 63  GLN B O   
4610  C CB  . GLN B 63  ? 0.1585 0.1990 0.2168 0.0199  -0.0045 -0.0057 63  GLN B CB  
4611  C CG  . GLN B 63  ? 0.1627 0.1996 0.2143 0.0166  -0.0097 0.0013  63  GLN B CG  
4612  C CD  . GLN B 63  ? 0.2214 0.2611 0.2612 0.0107  -0.0143 0.0015  63  GLN B CD  
4613  O OE1 . GLN B 63  ? 0.2116 0.2599 0.2547 0.0091  -0.0184 0.0055  63  GLN B OE1 
4614  N NE2 . GLN B 63  ? 0.2424 0.2750 0.2706 0.0075  -0.0137 -0.0036 63  GLN B NE2 
4615  N N   . ILE B 64  ? 0.1569 0.2012 0.2281 0.0283  0.0088  -0.0264 64  ILE B N   
4616  C CA  . ILE B 64  ? 0.1809 0.2364 0.2558 0.0312  0.0137  -0.0351 64  ILE B CA  
4617  C C   . ILE B 64  ? 0.1904 0.2477 0.2838 0.0374  0.0180  -0.0407 64  ILE B C   
4618  O O   . ILE B 64  ? 0.2448 0.3153 0.3464 0.0408  0.0213  -0.0442 64  ILE B O   
4619  C CB  . ILE B 64  ? 0.1983 0.2530 0.2621 0.0294  0.0158  -0.0438 64  ILE B CB  
4620  C CG1 . ILE B 64  ? 0.1814 0.2385 0.2309 0.0245  0.0126  -0.0384 64  ILE B CG1 
4621  C CG2 . ILE B 64  ? 0.1981 0.2659 0.2669 0.0332  0.0214  -0.0549 64  ILE B CG2 
4622  C CD1 . ILE B 64  ? 0.2762 0.3264 0.3152 0.0219  0.0123  -0.0430 64  ILE B CD1 
4623  N N   . GLN B 65  ? 0.2267 0.2714 0.3291 0.0389  0.0183  -0.0414 65  GLN B N   
4624  C CA  . GLN B 65  ? 0.2898 0.3339 0.4144 0.0449  0.0223  -0.0466 65  GLN B CA  
4625  C C   . GLN B 65  ? 0.2960 0.3470 0.4335 0.0483  0.0208  -0.0375 65  GLN B C   
4626  O O   . GLN B 65  ? 0.2964 0.3559 0.4497 0.0536  0.0251  -0.0439 65  GLN B O   
4627  C CB  . GLN B 65  ? 0.2906 0.3186 0.4247 0.0452  0.0224  -0.0456 65  GLN B CB  
4628  C CG  . GLN B 65  ? 0.3004 0.3227 0.4295 0.0431  0.0252  -0.0577 65  GLN B CG  
4629  C CD  . GLN B 65  ? 0.3383 0.3448 0.4778 0.0424  0.0253  -0.0544 65  GLN B CD  
4630  O OE1 . GLN B 65  ? 0.3194 0.3194 0.4541 0.0399  0.0215  -0.0405 65  GLN B OE1 
4631  N NE2 . GLN B 65  ? 0.2734 0.2752 0.4280 0.0444  0.0298  -0.0674 65  GLN B NE2 
4632  N N   . GLU B 66  ? 0.2257 0.2748 0.3572 0.0453  0.0147  -0.0234 66  GLU B N   
4633  C CA  . GLU B 66  ? 0.1716 0.2281 0.3162 0.0483  0.0122  -0.0137 66  GLU B CA  
4634  C C   . GLU B 66  ? 0.1843 0.2573 0.3306 0.0496  0.0145  -0.0173 66  GLU B C   
4635  O O   . GLU B 66  ? 0.3080 0.3893 0.4725 0.0548  0.0163  -0.0163 66  GLU B O   
4636  C CB  . GLU B 66  ? 0.1713 0.2260 0.3061 0.0438  0.0046  0.0005  66  GLU B CB  
4637  C CG  . GLU B 66  ? 0.2605 0.3150 0.4125 0.0476  0.0015  0.0126  66  GLU B CG  
4638  C CD  . GLU B 66  ? 0.2820 0.3397 0.4228 0.0429  -0.0066 0.0257  66  GLU B CD  
4639  O OE1 . GLU B 66  ? 0.2919 0.3474 0.4121 0.0367  -0.0091 0.0241  66  GLU B OE1 
4640  O OE2 . GLU B 66  ? 0.3086 0.3723 0.4619 0.0456  -0.0105 0.0372  66  GLU B OE2 
4641  N N   . TYR B 67  ? 0.1819 0.2607 0.3109 0.0451  0.0147  -0.0206 67  TYR B N   
4642  C CA  . TYR B 67  ? 0.2286 0.3248 0.3593 0.0460  0.0178  -0.0231 67  TYR B CA  
4643  C C   . TYR B 67  ? 0.2683 0.3724 0.4092 0.0518  0.0257  -0.0369 67  TYR B C   
4644  O O   . TYR B 67  ? 0.2971 0.4164 0.4497 0.0556  0.0294  -0.0389 67  TYR B O   
4645  C CB  . TYR B 67  ? 0.1748 0.2747 0.2864 0.0397  0.0159  -0.0212 67  TYR B CB  
4646  C CG  . TYR B 67  ? 0.1523 0.2497 0.2579 0.0342  0.0087  -0.0096 67  TYR B CG  
4647  C CD1 . TYR B 67  ? 0.1855 0.2690 0.2829 0.0309  0.0035  -0.0058 67  TYR B CD1 
4648  C CD2 . TYR B 67  ? 0.2757 0.3859 0.3846 0.0320  0.0071  -0.0033 67  TYR B CD2 
4649  C CE1 . TYR B 67  ? 0.2657 0.3488 0.3575 0.0257  -0.0031 0.0022  67  TYR B CE1 
4650  C CE2 . TYR B 67  ? 0.2649 0.3733 0.3702 0.0264  0.0001  0.0051  67  TYR B CE2 
4651  C CZ  . TYR B 67  ? 0.2609 0.3560 0.3571 0.0234  -0.0051 0.0070  67  TYR B CZ  
4652  O OH  . TYR B 67  ? 0.3044 0.3997 0.3969 0.0178  -0.0120 0.0129  67  TYR B OH  
4653  N N   . ALA B 68  ? 0.2206 0.3164 0.3582 0.0523  0.0285  -0.0476 68  ALA B N   
4654  C CA  . ALA B 68  ? 0.2737 0.3786 0.4201 0.0571  0.0358  -0.0637 68  ALA B CA  
4655  C C   . ALA B 68  ? 0.2948 0.4000 0.4679 0.0642  0.0392  -0.0676 68  ALA B C   
4656  O O   . ALA B 68  ? 0.2912 0.4118 0.4749 0.0690  0.0452  -0.0780 68  ALA B O   
4657  C CB  . ALA B 68  ? 0.2497 0.3450 0.3888 0.0554  0.0370  -0.0746 68  ALA B CB  
4658  N N   . GLN B 69  ? 0.1806 0.2701 0.3658 0.0654  0.0355  -0.0589 69  GLN B N   
4659  C CA  . GLN B 69  ? 0.2599 0.3482 0.4737 0.0725  0.0380  -0.0595 69  GLN B CA  
4660  C C   . GLN B 69  ? 0.3304 0.4322 0.5527 0.0748  0.0365  -0.0493 69  GLN B C   
4661  O O   . GLN B 69  ? 0.2539 0.3598 0.5015 0.0817  0.0397  -0.0516 69  GLN B O   
4662  C CB  . GLN B 69  ? 0.2520 0.3204 0.4771 0.0729  0.0344  -0.0507 69  GLN B CB  
4663  C CG  . GLN B 69  ? 0.5031 0.5575 0.7188 0.0692  0.0350  -0.0579 69  GLN B CG  
4664  C CD  . GLN B 69  ? 0.5980 0.6358 0.8144 0.0666  0.0298  -0.0431 69  GLN B CD  
4665  O OE1 . GLN B 69  ? 0.5424 0.5803 0.7634 0.0672  0.0251  -0.0270 69  GLN B OE1 
4666  N NE2 . GLN B 69  ? 0.4155 0.4412 0.6268 0.0634  0.0306  -0.0482 69  GLN B NE2 
4667  N N   . GLY B 70  ? 0.2409 0.3499 0.4450 0.0693  0.0318  -0.0387 70  GLY B N   
4668  C CA  . GLY B 70  ? 0.2007 0.3230 0.4130 0.0704  0.0297  -0.0287 70  GLY B CA  
4669  C C   . GLY B 70  ? 0.1750 0.2903 0.3950 0.0701  0.0220  -0.0124 70  GLY B C   
4670  O O   . GLY B 70  ? 0.1835 0.3102 0.4174 0.0727  0.0204  -0.0049 70  GLY B O   
4671  N N   . LYS B 71  ? 0.1763 0.2755 0.3878 0.0669  0.0173  -0.0063 71  LYS B N   
4672  C CA  . LYS B 71  ? 0.1792 0.2739 0.3966 0.0666  0.0099  0.0097  71  LYS B CA  
4673  C C   . LYS B 71  ? 0.2834 0.3801 0.4785 0.0585  0.0021  0.0193  71  LYS B C   
4674  O O   . LYS B 71  ? 0.3182 0.4109 0.5113 0.0567  -0.0045 0.0311  71  LYS B O   
4675  C CB  . LYS B 71  ? 0.2110 0.2887 0.4366 0.0688  0.0102  0.0116  71  LYS B CB  
4676  C CG  . LYS B 71  ? 0.2749 0.3492 0.5305 0.0773  0.0165  0.0046  71  LYS B CG  
4677  C CD  . LYS B 71  ? 0.3431 0.3996 0.6030 0.0775  0.0193  -0.0005 71  LYS B CD  
4678  C CE  . LYS B 71  ? 0.4821 0.5346 0.7739 0.0855  0.0265  -0.0116 71  LYS B CE  
4679  N NZ  . LYS B 71  ? 0.4394 0.4741 0.7483 0.0870  0.0265  -0.0062 71  LYS B NZ  
4680  N N   . ALA B 72  ? 0.2749 0.3788 0.4543 0.0536  0.0027  0.0144  72  ALA B N   
4681  C CA  . ALA B 72  ? 0.1648 0.2690 0.3250 0.0456  -0.0041 0.0206  72  ALA B CA  
4682  C C   . ALA B 72  ? 0.2662 0.3854 0.4338 0.0442  -0.0091 0.0291  72  ALA B C   
4683  O O   . ALA B 72  ? 0.3642 0.4961 0.5412 0.0460  -0.0054 0.0266  72  ALA B O   
4684  C CB  . ALA B 72  ? 0.1711 0.2738 0.3134 0.0409  -0.0012 0.0120  72  ALA B CB  
4685  N N   . LYS B 73  ? 0.2910 0.4106 0.4543 0.0406  -0.0175 0.0389  73  LYS B N   
4686  C CA  . LYS B 73  ? 0.3585 0.4931 0.5285 0.0381  -0.0238 0.0467  73  LYS B CA  
4687  C C   . LYS B 73  ? 0.4329 0.5692 0.5867 0.0291  -0.0276 0.0444  73  LYS B C   
4688  O O   . LYS B 73  ? 0.4121 0.5484 0.5561 0.0236  -0.0351 0.0481  73  LYS B O   
4689  C CB  . LYS B 73  ? 0.3707 0.5083 0.5472 0.0396  -0.0313 0.0585  73  LYS B CB  
4690  C CG  . LYS B 73  ? 0.3806 0.5310 0.5825 0.0463  -0.0318 0.0660  73  LYS B CG  
4691  C CD  . LYS B 73  ? 0.5236 0.6668 0.7428 0.0554  -0.0233 0.0620  73  LYS B CD  
4692  C CE  . LYS B 73  ? 0.5801 0.7105 0.8013 0.0583  -0.0245 0.0682  73  LYS B CE  
4693  N NZ  . LYS B 73  ? 0.4680 0.5881 0.7059 0.0658  -0.0157 0.0607  73  LYS B NZ  
4694  N N   . ASP B 74  ? 0.3788 0.5179 0.5312 0.0278  -0.0220 0.0381  74  ASP B N   
4695  C CA  . ASP B 74  ? 0.3782 0.5174 0.5191 0.0198  -0.0242 0.0361  74  ASP B CA  
4696  C C   . ASP B 74  ? 0.3326 0.4876 0.4858 0.0163  -0.0285 0.0418  74  ASP B C   
4697  O O   . ASP B 74  ? 0.3868 0.5531 0.5514 0.0179  -0.0236 0.0423  74  ASP B O   
4698  C CB  . ASP B 74  ? 0.3908 0.5271 0.5254 0.0200  -0.0164 0.0292  74  ASP B CB  
4699  C CG  . ASP B 74  ? 0.4147 0.5405 0.5326 0.0135  -0.0183 0.0260  74  ASP B CG  
4700  O OD1 . ASP B 74  ? 0.4686 0.5961 0.5854 0.0070  -0.0243 0.0287  74  ASP B OD1 
4701  O OD2 . ASP B 74  ? 0.3506 0.4670 0.4583 0.0148  -0.0139 0.0201  74  ASP B OD2 
4702  N N   . VAL B 75  ? 0.2435 0.4009 0.3945 0.0111  -0.0376 0.0456  75  VAL B N   
4703  C CA  . VAL B 75  ? 0.3486 0.5220 0.5133 0.0074  -0.0430 0.0506  75  VAL B CA  
4704  C C   . VAL B 75  ? 0.3310 0.5086 0.4995 0.0022  -0.0398 0.0487  75  VAL B C   
4705  O O   . VAL B 75  ? 0.3323 0.5243 0.5169 0.0027  -0.0377 0.0527  75  VAL B O   
4706  C CB  . VAL B 75  ? 0.4021 0.5782 0.5612 0.0018  -0.0538 0.0525  75  VAL B CB  
4707  C CG1 . VAL B 75  ? 0.3432 0.5249 0.5072 0.0075  -0.0579 0.0598  75  VAL B CG1 
4708  C CG2 . VAL B 75  ? 0.2773 0.4388 0.4161 -0.0032 -0.0552 0.0456  75  VAL B CG2 
4709  N N   . PHE B 76  ? 0.3391 0.5050 0.4943 -0.0029 -0.0391 0.0437  76  PHE B N   
4710  C CA  . PHE B 76  ? 0.2282 0.3975 0.3887 -0.0081 -0.0362 0.0441  76  PHE B CA  
4711  C C   . PHE B 76  ? 0.2717 0.4481 0.4375 -0.0028 -0.0262 0.0457  76  PHE B C   
4712  O O   . PHE B 76  ? 0.2133 0.4025 0.3918 -0.0051 -0.0235 0.0504  76  PHE B O   
4713  C CB  . PHE B 76  ? 0.1983 0.3527 0.3453 -0.0136 -0.0374 0.0388  76  PHE B CB  
4714  C CG  . PHE B 76  ? 0.1495 0.3056 0.3031 -0.0183 -0.0339 0.0411  76  PHE B CG  
4715  C CD1 . PHE B 76  ? 0.1519 0.3132 0.3189 -0.0262 -0.0390 0.0433  76  PHE B CD1 
4716  C CD2 . PHE B 76  ? 0.2298 0.3836 0.3777 -0.0151 -0.0258 0.0416  76  PHE B CD2 
4717  C CE1 . PHE B 76  ? 0.2062 0.3689 0.3824 -0.0307 -0.0356 0.0475  76  PHE B CE1 
4718  C CE2 . PHE B 76  ? 0.1579 0.3153 0.3128 -0.0193 -0.0227 0.0464  76  PHE B CE2 
4719  C CZ  . PHE B 76  ? 0.1492 0.3103 0.3191 -0.0270 -0.0274 0.0502  76  PHE B CZ  
4720  N N   . LEU B 77  ? 0.3208 0.4905 0.4776 0.0041  -0.0205 0.0414  77  LEU B N   
4721  C CA  . LEU B 77  ? 0.2676 0.4462 0.4279 0.0092  -0.0109 0.0403  77  LEU B CA  
4722  C C   . LEU B 77  ? 0.2582 0.4544 0.4371 0.0140  -0.0083 0.0438  77  LEU B C   
4723  O O   . LEU B 77  ? 0.3112 0.5227 0.4984 0.0148  -0.0019 0.0459  77  LEU B O   
4724  C CB  . LEU B 77  ? 0.2240 0.3917 0.3720 0.0150  -0.0060 0.0326  77  LEU B CB  
4725  C CG  . LEU B 77  ? 0.1951 0.3746 0.3464 0.0207  0.0038  0.0287  77  LEU B CG  
4726  C CD1 . LEU B 77  ? 0.2171 0.4023 0.3613 0.0165  0.0075  0.0306  77  LEU B CD1 
4727  C CD2 . LEU B 77  ? 0.3068 0.4770 0.4524 0.0273  0.0077  0.0195  77  LEU B CD2 
4728  N N   . GLU B 78  ? 0.2370 0.4330 0.4234 0.0175  -0.0129 0.0452  78  GLU B N   
4729  C CA  . GLU B 78  ? 0.2131 0.4260 0.4198 0.0225  -0.0109 0.0488  78  GLU B CA  
4730  C C   . GLU B 78  ? 0.2185 0.4470 0.4385 0.0164  -0.0140 0.0560  78  GLU B C   
4731  O O   . GLU B 78  ? 0.3275 0.5735 0.5651 0.0199  -0.0103 0.0591  78  GLU B O   
4732  C CB  . GLU B 78  ? 0.3416 0.5507 0.5550 0.0276  -0.0161 0.0509  78  GLU B CB  
4733  C CG  . GLU B 78  ? 0.6057 0.8105 0.8238 0.0374  -0.0089 0.0452  78  GLU B CG  
4734  C CD  . GLU B 78  ? 0.8491 1.0335 1.0501 0.0380  -0.0087 0.0396  78  GLU B CD  
4735  O OE1 . GLU B 78  ? 0.9221 1.0963 1.1128 0.0339  -0.0164 0.0432  78  GLU B OE1 
4736  O OE2 . GLU B 78  ? 0.7139 0.8940 0.9119 0.0424  -0.0008 0.0311  78  GLU B OE2 
4737  N N   . ALA B 79  ? 0.2911 0.5141 0.5049 0.0073  -0.0205 0.0579  79  ALA B N   
4738  C CA  . ALA B 79  ? 0.1540 0.3906 0.3821 0.0003  -0.0226 0.0640  79  ALA B CA  
4739  C C   . ALA B 79  ? 0.1426 0.3873 0.3725 -0.0009 -0.0135 0.0662  79  ALA B C   
4740  O O   . ALA B 79  ? 0.2299 0.4922 0.4768 -0.0032 -0.0112 0.0726  79  ALA B O   
4741  C CB  . ALA B 79  ? 0.1465 0.3740 0.3699 -0.0091 -0.0325 0.0635  79  ALA B CB  
4742  N N   . ILE B 80  ? 0.2255 0.4595 0.4389 0.0003  -0.0084 0.0620  80  ILE B N   
4743  C CA  . ILE B 80  ? 0.1687 0.4136 0.3823 0.0002  0.0006  0.0652  80  ILE B CA  
4744  C C   . ILE B 80  ? 0.1816 0.4447 0.4029 0.0086  0.0096  0.0635  80  ILE B C   
4745  O O   . ILE B 80  ? 0.1759 0.4587 0.4068 0.0081  0.0162  0.0691  80  ILE B O   
4746  C CB  . ILE B 80  ? 0.1707 0.4011 0.3645 -0.0003 0.0028  0.0611  80  ILE B CB  
4747  C CG1 . ILE B 80  ? 0.1672 0.3788 0.3544 -0.0077 -0.0058 0.0607  80  ILE B CG1 
4748  C CG2 . ILE B 80  ? 0.1429 0.3876 0.3369 -0.0012 0.0111  0.0668  80  ILE B CG2 
4749  C CD1 . ILE B 80  ? 0.1429 0.3422 0.3144 -0.0088 -0.0036 0.0584  80  ILE B CD1 
4750  N N   . ARG B 81  ? 0.1420 0.3996 0.3609 0.0165  0.0103  0.0558  81  ARG B N   
4751  C CA  . ARG B 81  ? 0.1434 0.4162 0.3701 0.0253  0.0195  0.0509  81  ARG B CA  
4752  C C   . ARG B 81  ? 0.2406 0.5354 0.4903 0.0262  0.0211  0.0571  81  ARG B C   
4753  O O   . ARG B 81  ? 0.2654 0.5811 0.5224 0.0290  0.0303  0.0574  81  ARG B O   
4754  C CB  . ARG B 81  ? 0.1447 0.4042 0.3685 0.0330  0.0189  0.0417  81  ARG B CB  
4755  C CG  . ARG B 81  ? 0.1475 0.4199 0.3803 0.0425  0.0288  0.0331  81  ARG B CG  
4756  C CD  . ARG B 81  ? 0.2606 0.5267 0.5076 0.0499  0.0265  0.0300  81  ARG B CD  
4757  N NE  . ARG B 81  ? 0.6063 0.8869 0.8751 0.0508  0.0237  0.0381  81  ARG B NE  
4758  C CZ  . ARG B 81  ? 0.5913 0.8940 0.8779 0.0557  0.0312  0.0370  81  ARG B CZ  
4759  N NH1 . ARG B 81  ? 0.5249 0.8394 0.8096 0.0602  0.0422  0.0275  81  ARG B NH1 
4760  N NH2 . ARG B 81  ? 0.3835 0.6988 0.6907 0.0560  0.0276  0.0451  81  ARG B NH2 
4761  N N   . LYS B 82  ? 0.2240 0.5166 0.4854 0.0239  0.0123  0.0622  82  LYS B N   
4762  C CA  . LYS B 82  ? 0.1470 0.4598 0.4323 0.0265  0.0131  0.0670  82  LYS B CA  
4763  C C   . LYS B 82  ? 0.1424 0.4747 0.4386 0.0199  0.0163  0.0757  82  LYS B C   
4764  O O   . LYS B 82  ? 0.1422 0.4705 0.4291 0.0124  0.0162  0.0797  82  LYS B O   
4765  C CB  . LYS B 82  ? 0.1432 0.4500 0.4373 0.0254  0.0016  0.0708  82  LYS B CB  
4766  C CG  . LYS B 82  ? 0.1427 0.4403 0.4302 0.0146  -0.0087 0.0754  82  LYS B CG  
4767  C CD  . LYS B 82  ? 0.1460 0.4460 0.4446 0.0134  -0.0198 0.0794  82  LYS B CD  
4768  C CE  . LYS B 82  ? 0.1464 0.4333 0.4372 0.0205  -0.0231 0.0761  82  LYS B CE  
4769  N NZ  . LYS B 82  ? 0.1675 0.4556 0.4625 0.0175  -0.0357 0.0810  82  LYS B NZ  
4770  N N   . ASP B 83  ? 0.1428 0.4968 0.4612 0.0228  0.0194  0.0795  83  ASP B N   
4771  C CA  . ASP B 83  ? 0.1480 0.5149 0.4738 0.0163  0.0224  0.0865  83  ASP B CA  
4772  C C   . ASP B 83  ? 0.1984 0.5582 0.5293 0.0054  0.0114  0.0940  83  ASP B C   
4773  O O   . ASP B 83  ? 0.2314 0.5834 0.5662 0.0045  0.0012  0.0933  83  ASP B O   
4774  C CB  . ASP B 83  ? 0.1556 0.5384 0.4977 0.0220  0.0272  0.0851  83  ASP B CB  
4775  C CG  . ASP B 83  ? 0.3130 0.7119 0.6611 0.0170  0.0337  0.0914  83  ASP B CG  
4776  O OD1 . ASP B 83  ? 0.3520 0.7519 0.7097 0.0087  0.0276  0.0995  83  ASP B OD1 
4777  O OD2 . ASP B 83  ? 0.3708 0.7817 0.7141 0.0213  0.0448  0.0878  83  ASP B OD2 
4778  N N   . PRO B 84  ? 0.1505 0.5128 0.4818 -0.0031 0.0130  0.1009  84  PRO B N   
4779  C CA  . PRO B 84  ? 0.1520 0.5068 0.4910 -0.0139 0.0029  0.1059  84  PRO B CA  
4780  C C   . PRO B 84  ? 0.2175 0.5801 0.5737 -0.0152 -0.0033 0.1070  84  PRO B C   
4781  O O   . PRO B 84  ? 0.3228 0.6782 0.6837 -0.0223 -0.0141 0.1070  84  PRO B O   
4782  C CB  . PRO B 84  ? 0.1571 0.5151 0.4968 -0.0209 0.0085  0.1140  84  PRO B CB  
4783  C CG  . PRO B 84  ? 0.2200 0.5831 0.5449 -0.0144 0.0195  0.1127  84  PRO B CG  
4784  C CD  . PRO B 84  ? 0.2080 0.5797 0.5328 -0.0034 0.0240  0.1045  84  PRO B CD  
4785  N N   . ASP B 85  ? 0.1601 0.5382 0.5259 -0.0085 0.0030  0.1069  85  ASP B N   
4786  C CA  . ASP B 85  ? 0.1644 0.5507 0.5467 -0.0085 -0.0031 0.1078  85  ASP B CA  
4787  C C   . ASP B 85  ? 0.1688 0.5463 0.5483 -0.0045 -0.0130 0.1033  85  ASP B C   
4788  O O   . ASP B 85  ? 0.2633 0.6429 0.6519 -0.0080 -0.0228 0.1044  85  ASP B O   
4789  C CB  . ASP B 85  ? 0.1693 0.5740 0.5630 -0.0012 0.0065  0.1079  85  ASP B CB  
4790  C CG  . ASP B 85  ? 0.2947 0.7111 0.6906 -0.0051 0.0165  0.1135  85  ASP B CG  
4791  O OD1 . ASP B 85  ? 0.2520 0.6661 0.6523 -0.0152 0.0131  0.1204  85  ASP B OD1 
4792  O OD2 . ASP B 85  ? 0.2751 0.7029 0.6687 0.0018  0.0276  0.1109  85  ASP B OD2 
4793  N N   . ASP B 86  ? 0.1559 0.5243 0.5228 0.0029  -0.0108 0.0984  86  ASP B N   
4794  C CA  . ASP B 86  ? 0.1544 0.5138 0.5177 0.0074  -0.0194 0.0958  86  ASP B CA  
4795  C C   . ASP B 86  ? 0.1516 0.4966 0.5024 -0.0002 -0.0298 0.0951  86  ASP B C   
4796  O O   . ASP B 86  ? 0.2186 0.5567 0.5642 0.0024  -0.0378 0.0938  86  ASP B O   
4797  C CB  . ASP B 86  ? 0.1564 0.5117 0.5140 0.0189  -0.0120 0.0906  86  ASP B CB  
4798  C CG  . ASP B 86  ? 0.2101 0.5778 0.5831 0.0282  -0.0055 0.0889  86  ASP B CG  
4799  O OD1 . ASP B 86  ? 0.1621 0.5391 0.5493 0.0273  -0.0105 0.0928  86  ASP B OD1 
4800  O OD2 . ASP B 86  ? 0.3430 0.7117 0.7145 0.0365  0.0044  0.0826  86  ASP B OD2 
4801  N N   . LEU B 87  ? 0.1684 0.5087 0.5148 -0.0095 -0.0298 0.0960  87  LEU B N   
4802  C CA  . LEU B 87  ? 0.1582 0.4846 0.4937 -0.0170 -0.0391 0.0933  87  LEU B CA  
4803  C C   . LEU B 87  ? 0.2354 0.5645 0.5781 -0.0239 -0.0513 0.0926  87  LEU B C   
4804  O O   . LEU B 87  ? 0.2442 0.5834 0.6015 -0.0286 -0.0517 0.0952  87  LEU B O   
4805  C CB  . LEU B 87  ? 0.1472 0.4671 0.4786 -0.0244 -0.0348 0.0944  87  LEU B CB  
4806  C CG  . LEU B 87  ? 0.1448 0.4514 0.4555 -0.0191 -0.0261 0.0909  87  LEU B CG  
4807  C CD1 . LEU B 87  ? 0.1458 0.4443 0.4524 -0.0272 -0.0239 0.0930  87  LEU B CD1 
4808  C CD2 . LEU B 87  ? 0.1453 0.4331 0.4352 -0.0144 -0.0306 0.0831  87  LEU B CD2 
4809  N N   . GLU B 88  ? 0.2154 0.5370 0.5474 -0.0245 -0.0611 0.0888  88  GLU B N   
4810  C CA  . GLU B 88  ? 0.2226 0.5472 0.5576 -0.0321 -0.0731 0.0859  88  GLU B CA  
4811  C C   . GLU B 88  ? 0.2903 0.6051 0.6226 -0.0435 -0.0766 0.0805  88  GLU B C   
4812  O O   . GLU B 88  ? 0.2712 0.5740 0.5951 -0.0447 -0.0717 0.0795  88  GLU B O   
4813  C CB  . GLU B 88  ? 0.2671 0.5902 0.5903 -0.0280 -0.0821 0.0844  88  GLU B CB  
4814  C CG  . GLU B 88  ? 0.3197 0.6494 0.6473 -0.0162 -0.0786 0.0902  88  GLU B CG  
4815  C CD  . GLU B 88  ? 0.3359 0.6809 0.6836 -0.0142 -0.0753 0.0943  88  GLU B CD  
4816  O OE1 . GLU B 88  ? 0.2807 0.6352 0.6372 -0.0208 -0.0826 0.0937  88  GLU B OE1 
4817  O OE2 . GLU B 88  ? 0.3299 0.6782 0.6851 -0.0060 -0.0653 0.0972  88  GLU B OE2 
4818  N N   . LYS B 89  ? 0.3076 0.6276 0.6485 -0.0517 -0.0850 0.0764  89  LYS B N   
4819  C CA  . LYS B 89  ? 0.3794 0.6892 0.7210 -0.0626 -0.0886 0.0693  89  LYS B CA  
4820  C C   . LYS B 89  ? 0.2932 0.5888 0.6151 -0.0638 -0.0936 0.0618  89  LYS B C   
4821  O O   . LYS B 89  ? 0.2516 0.5342 0.5722 -0.0705 -0.0930 0.0567  89  LYS B O   
4822  C CB  . LYS B 89  ? 0.4189 0.7384 0.7742 -0.0707 -0.0972 0.0639  89  LYS B CB  
4823  C CG  . LYS B 89  ? 0.3200 0.6519 0.6969 -0.0716 -0.0918 0.0711  89  LYS B CG  
4824  C CD  . LYS B 89  ? 0.3154 0.6610 0.7060 -0.0777 -0.1010 0.0660  89  LYS B CD  
4825  C CE  . LYS B 89  ? 0.2491 0.6092 0.6604 -0.0768 -0.0956 0.0744  89  LYS B CE  
4826  N NZ  . LYS B 89  ? 0.3225 0.7008 0.7418 -0.0754 -0.1037 0.0733  89  LYS B NZ  
4827  N N   . GLU B 90  ? 0.2686 0.5661 0.5757 -0.0573 -0.0979 0.0616  90  GLU B N   
4828  C CA  . GLU B 90  ? 0.3038 0.5848 0.5869 -0.0568 -0.0997 0.0545  90  GLU B CA  
4829  C C   . GLU B 90  ? 0.3437 0.6059 0.6141 -0.0515 -0.0876 0.0559  90  GLU B C   
4830  O O   . GLU B 90  ? 0.4673 0.7122 0.7237 -0.0544 -0.0866 0.0488  90  GLU B O   
4831  C CB  . GLU B 90  ? 0.4553 0.7423 0.7246 -0.0503 -0.1057 0.0559  90  GLU B CB  
4832  C CG  . GLU B 90  ? 0.5865 0.8796 0.8600 -0.0389 -0.0995 0.0666  90  GLU B CG  
4833  C CD  . GLU B 90  ? 0.7195 1.0165 0.9812 -0.0323 -0.1051 0.0699  90  GLU B CD  
4834  O OE1 . GLU B 90  ? 0.9798 1.2830 1.2332 -0.0374 -0.1156 0.0657  90  GLU B OE1 
4835  O OE2 . GLU B 90  ? 0.4965 0.7914 0.7584 -0.0222 -0.0989 0.0768  90  GLU B OE2 
4836  N N   . GLU B 91  ? 0.3415 0.6084 0.6171 -0.0435 -0.0785 0.0642  91  GLU B N   
4837  C CA  . GLU B 91  ? 0.2543 0.5070 0.5176 -0.0382 -0.0674 0.0648  91  GLU B CA  
4838  C C   . GLU B 91  ? 0.1993 0.4474 0.4706 -0.0449 -0.0624 0.0659  91  GLU B C   
4839  O O   . GLU B 91  ? 0.1580 0.3902 0.4156 -0.0447 -0.0577 0.0630  91  GLU B O   
4840  C CB  . GLU B 91  ? 0.2426 0.5044 0.5107 -0.0279 -0.0591 0.0713  91  GLU B CB  
4841  C CG  . GLU B 91  ? 0.3072 0.5715 0.5701 -0.0200 -0.0628 0.0720  91  GLU B CG  
4842  C CD  . GLU B 91  ? 0.2723 0.5465 0.5460 -0.0099 -0.0545 0.0771  91  GLU B CD  
4843  O OE1 . GLU B 91  ? 0.3176 0.6105 0.6127 -0.0099 -0.0540 0.0826  91  GLU B OE1 
4844  O OE2 . GLU B 91  ? 0.2958 0.5595 0.5582 -0.0021 -0.0483 0.0748  91  GLU B OE2 
4845  N N   . VAL B 92  ? 0.1596 0.4224 0.4549 -0.0508 -0.0633 0.0711  92  VAL B N   
4846  C CA  . VAL B 92  ? 0.1601 0.4200 0.4670 -0.0575 -0.0584 0.0750  92  VAL B CA  
4847  C C   . VAL B 92  ? 0.2764 0.5189 0.5784 -0.0655 -0.0644 0.0664  92  VAL B C   
4848  O O   . VAL B 92  ? 0.3355 0.5656 0.6348 -0.0673 -0.0591 0.0677  92  VAL B O   
4849  C CB  . VAL B 92  ? 0.1615 0.4409 0.4967 -0.0625 -0.0583 0.0828  92  VAL B CB  
4850  C CG1 . VAL B 92  ? 0.1666 0.4392 0.5126 -0.0698 -0.0537 0.0871  92  VAL B CG1 
4851  C CG2 . VAL B 92  ? 0.1578 0.4528 0.4960 -0.0534 -0.0500 0.0902  92  VAL B CG2 
4852  N N   . GLU B 93  ? 0.2655 0.5081 0.5668 -0.0701 -0.0753 0.0572  93  GLU B N   
4853  C CA  . GLU B 93  ? 0.1960 0.4227 0.4915 -0.0770 -0.0807 0.0460  93  GLU B CA  
4854  C C   . GLU B 93  ? 0.2267 0.4342 0.4959 -0.0710 -0.0757 0.0423  93  GLU B C   
4855  O O   . GLU B 93  ? 0.2969 0.4892 0.5646 -0.0750 -0.0746 0.0375  93  GLU B O   
4856  C CB  . GLU B 93  ? 0.3638 0.5978 0.6588 -0.0817 -0.0932 0.0353  93  GLU B CB  
4857  C CG  . GLU B 93  ? 0.6250 0.8772 0.9442 -0.0878 -0.0987 0.0367  93  GLU B CG  
4858  C CD  . GLU B 93  ? 0.7717 1.0211 1.0960 -0.0973 -0.1071 0.0219  93  GLU B CD  
4859  O OE1 . GLU B 93  ? 0.8781 1.1216 1.1867 -0.0987 -0.1132 0.0102  93  GLU B OE1 
4860  O OE2 . GLU B 93  ? 0.5673 0.8217 0.9111 -0.1033 -0.1072 0.0213  93  GLU B OE2 
4861  N N   . LYS B 94  ? 0.2672 0.4754 0.5180 -0.0615 -0.0726 0.0444  94  LYS B N   
4862  C CA  . LYS B 94  ? 0.3092 0.5006 0.5370 -0.0557 -0.0672 0.0415  94  LYS B CA  
4863  C C   . LYS B 94  ? 0.3072 0.4927 0.5377 -0.0543 -0.0573 0.0481  94  LYS B C   
4864  O O   . LYS B 94  ? 0.3650 0.5350 0.5854 -0.0549 -0.0549 0.0445  94  LYS B O   
4865  C CB  . LYS B 94  ? 0.3351 0.5294 0.5477 -0.0461 -0.0656 0.0431  94  LYS B CB  
4866  C CG  . LYS B 94  ? 0.3759 0.5641 0.5707 -0.0455 -0.0725 0.0353  94  LYS B CG  
4867  C CD  . LYS B 94  ? 0.4376 0.6412 0.6412 -0.0501 -0.0832 0.0334  94  LYS B CD  
4868  C CE  . LYS B 94  ? 0.4875 0.6943 0.6750 -0.0451 -0.0878 0.0331  94  LYS B CE  
4869  N NZ  . LYS B 94  ? 0.4176 0.6454 0.6163 -0.0465 -0.0969 0.0364  94  LYS B NZ  
4870  N N   . LEU B 95  ? 0.2238 0.4235 0.4681 -0.0523 -0.0514 0.0583  95  LEU B N   
4871  C CA  . LEU B 95  ? 0.1579 0.3569 0.4044 -0.0511 -0.0419 0.0662  95  LEU B CA  
4872  C C   . LEU B 95  ? 0.1627 0.3535 0.4227 -0.0600 -0.0434 0.0677  95  LEU B C   
4873  O O   . LEU B 95  ? 0.2704 0.4509 0.5240 -0.0592 -0.0386 0.0700  95  LEU B O   
4874  C CB  . LEU B 95  ? 0.2113 0.4311 0.4714 -0.0479 -0.0353 0.0766  95  LEU B CB  
4875  C CG  . LEU B 95  ? 0.3551 0.5810 0.6018 -0.0370 -0.0284 0.0765  95  LEU B CG  
4876  C CD1 . LEU B 95  ? 0.2300 0.4788 0.4939 -0.0343 -0.0244 0.0836  95  LEU B CD1 
4877  C CD2 . LEU B 95  ? 0.2261 0.4463 0.4586 -0.0331 -0.0198 0.0779  95  LEU B CD2 
4878  N N   . ILE B 96  ? 0.2330 0.4285 0.5139 -0.0684 -0.0503 0.0664  96  ILE B N   
4879  C CA  . ILE B 96  ? 0.1742 0.3602 0.4724 -0.0774 -0.0524 0.0663  96  ILE B CA  
4880  C C   . ILE B 96  ? 0.2420 0.4075 0.5257 -0.0784 -0.0566 0.0533  96  ILE B C   
4881  O O   . ILE B 96  ? 0.1964 0.3490 0.4844 -0.0808 -0.0541 0.0546  96  ILE B O   
4882  C CB  . ILE B 96  ? 0.1786 0.3755 0.5049 -0.0865 -0.0592 0.0660  96  ILE B CB  
4883  C CG1 . ILE B 96  ? 0.1745 0.3938 0.5145 -0.0847 -0.0547 0.0784  96  ILE B CG1 
4884  C CG2 . ILE B 96  ? 0.2374 0.4233 0.5848 -0.0951 -0.0595 0.0670  96  ILE B CG2 
4885  C CD1 . ILE B 96  ? 0.1746 0.3982 0.5211 -0.0830 -0.0438 0.0935  96  ILE B CD1 
4886  N N   . GLU B 97  ? 0.3439 0.5074 0.6110 -0.0765 -0.0630 0.0415  97  GLU B N   
4887  C CA  . GLU B 97  ? 0.2783 0.4249 0.5296 -0.0769 -0.0664 0.0285  97  GLU B CA  
4888  C C   . GLU B 97  ? 0.2201 0.3539 0.4546 -0.0706 -0.0586 0.0318  97  GLU B C   
4889  O O   . GLU B 97  ? 0.2696 0.3886 0.5038 -0.0730 -0.0585 0.0265  97  GLU B O   
4890  C CB  . GLU B 97  ? 0.4240 0.5752 0.6573 -0.0743 -0.0729 0.0190  97  GLU B CB  
4891  C CG  . GLU B 97  ? 0.5770 0.7215 0.8066 -0.0801 -0.0810 0.0030  97  GLU B CG  
4892  C CD  . GLU B 97  ? 0.7771 0.9283 0.9852 -0.0764 -0.0863 -0.0033 97  GLU B CD  
4893  O OE1 . GLU B 97  ? 0.6026 0.7484 0.7993 -0.0788 -0.0908 -0.0162 97  GLU B OE1 
4894  O OE2 . GLU B 97  ? 0.8086 0.9716 1.0124 -0.0709 -0.0856 0.0052  97  GLU B OE2 
4895  N N   . PHE B 98  ? 0.1706 0.3108 0.3926 -0.0626 -0.0520 0.0398  98  PHE B N   
4896  C CA  . PHE B 98  ? 0.1739 0.3047 0.3795 -0.0565 -0.0450 0.0420  98  PHE B CA  
4897  C C   . PHE B 98  ? 0.1683 0.2969 0.3878 -0.0591 -0.0399 0.0519  98  PHE B C   
4898  O O   . PHE B 98  ? 0.2029 0.3191 0.4149 -0.0578 -0.0376 0.0507  98  PHE B O   
4899  C CB  . PHE B 98  ? 0.2510 0.3913 0.4431 -0.0477 -0.0395 0.0465  98  PHE B CB  
4900  C CG  . PHE B 98  ? 0.2014 0.3316 0.3724 -0.0412 -0.0346 0.0435  98  PHE B CG  
4901  C CD1 . PHE B 98  ? 0.2028 0.3205 0.3572 -0.0397 -0.0382 0.0332  98  PHE B CD1 
4902  C CD2 . PHE B 98  ? 0.2502 0.3855 0.4183 -0.0369 -0.0266 0.0510  98  PHE B CD2 
4903  C CE1 . PHE B 98  ? 0.2149 0.3238 0.3517 -0.0343 -0.0337 0.0305  98  PHE B CE1 
4904  C CE2 . PHE B 98  ? 0.1614 0.2888 0.3111 -0.0314 -0.0227 0.0473  98  PHE B CE2 
4905  C CZ  . PHE B 98  ? 0.2029 0.3162 0.3378 -0.0302 -0.0263 0.0370  98  PHE B CZ  
4906  N N   . THR B 99  ? 0.1690 0.3110 0.4097 -0.0627 -0.0379 0.0631  99  THR B N   
4907  C CA  . THR B 99  ? 0.1825 0.3254 0.4377 -0.0650 -0.0325 0.0759  99  THR B CA  
4908  C C   . THR B 99  ? 0.2739 0.4013 0.5466 -0.0726 -0.0371 0.0723  99  THR B C   
4909  O O   . THR B 99  ? 0.2766 0.3951 0.5512 -0.0722 -0.0339 0.0776  99  THR B O   
4910  C CB  . THR B 99  ? 0.1710 0.3344 0.4451 -0.0669 -0.0286 0.0899  99  THR B CB  
4911  O OG1 . THR B 99  ? 0.1647 0.3426 0.4235 -0.0590 -0.0233 0.0918  99  THR B OG1 
4912  C CG2 . THR B 99  ? 0.1748 0.3416 0.4644 -0.0695 -0.0228 0.1059  99  THR B CG2 
4913  N N   . LYS B 100 ? 0.2953 0.4203 0.5823 -0.0796 -0.0448 0.0627  100 LYS B N   
4914  C CA  . LYS B 100 ? 0.1925 0.3018 0.4967 -0.0866 -0.0495 0.0549  100 LYS B CA  
4915  C C   . LYS B 100 ? 0.2009 0.2930 0.4848 -0.0827 -0.0499 0.0435  100 LYS B C   
4916  O O   . LYS B 100 ? 0.3048 0.3829 0.6018 -0.0859 -0.0506 0.0405  100 LYS B O   
4917  C CB  . LYS B 100 ? 0.1985 0.3103 0.5180 -0.0945 -0.0584 0.0424  100 LYS B CB  
4918  C CG  . LYS B 100 ? 0.3142 0.4438 0.6562 -0.0993 -0.0591 0.0519  100 LYS B CG  
4919  C CD  . LYS B 100 ? 0.2923 0.4161 0.6493 -0.1063 -0.0654 0.0395  100 LYS B CD  
4920  C CE  . LYS B 100 ? 0.3997 0.5411 0.7670 -0.1089 -0.0673 0.0431  100 LYS B CE  
4921  N NZ  . LYS B 100 ? 0.5900 0.7419 0.9442 -0.1087 -0.0753 0.0304  100 LYS B NZ  
4922  N N   . LEU B 101 ? 0.2283 0.3214 0.4825 -0.0756 -0.0493 0.0373  101 LEU B N   
4923  C CA  . LEU B 101 ? 0.2761 0.3546 0.5108 -0.0718 -0.0492 0.0270  101 LEU B CA  
4924  C C   . LEU B 101 ? 0.2366 0.3094 0.4685 -0.0674 -0.0423 0.0375  101 LEU B C   
4925  O O   . LEU B 101 ? 0.3454 0.4045 0.5838 -0.0688 -0.0425 0.0341  101 LEU B O   
4926  C CB  . LEU B 101 ? 0.1984 0.2804 0.4050 -0.0659 -0.0502 0.0195  101 LEU B CB  
4927  C CG  . LEU B 101 ? 0.2279 0.2966 0.4168 -0.0642 -0.0521 0.0057  101 LEU B CG  
4928  C CD1 . LEU B 101 ? 0.2558 0.3227 0.4511 -0.0708 -0.0600 -0.0095 101 LEU B CD1 
4929  C CD2 . LEU B 101 ? 0.3125 0.3835 0.4743 -0.0565 -0.0496 0.0048  101 LEU B CD2 
4930  N N   . ASN B 102 ? 0.1784 0.2631 0.4011 -0.0620 -0.0362 0.0499  102 ASN B N   
4931  C CA  . ASN B 102 ? 0.1767 0.2611 0.3946 -0.0575 -0.0299 0.0606  102 ASN B CA  
4932  C C   . ASN B 102 ? 0.1899 0.2802 0.4338 -0.0616 -0.0271 0.0775  102 ASN B C   
4933  O O   . ASN B 102 ? 0.2201 0.3184 0.4607 -0.0578 -0.0213 0.0907  102 ASN B O   
4934  C CB  . ASN B 102 ? 0.1692 0.2660 0.3649 -0.0497 -0.0246 0.0641  102 ASN B CB  
4935  C CG  . ASN B 102 ? 0.1863 0.2799 0.3615 -0.0461 -0.0273 0.0504  102 ASN B CG  
4936  O OD1 . ASN B 102 ? 0.2263 0.3091 0.3847 -0.0428 -0.0275 0.0418  102 ASN B OD1 
4937  N ND2 . ASN B 102 ? 0.2070 0.3109 0.3848 -0.0467 -0.0292 0.0496  102 ASN B ND2 
4938  N N   . TYR B 103 ? 0.2735 0.3614 0.5441 -0.0695 -0.0312 0.0777  103 TYR B N   
4939  C CA  . TYR B 103 ? 0.2819 0.3765 0.5810 -0.0742 -0.0283 0.0957  103 TYR B CA  
4940  C C   . TYR B 103 ? 0.3143 0.3992 0.6216 -0.0731 -0.0257 0.1049  103 TYR B C   
4941  O O   . TYR B 103 ? 0.3061 0.4026 0.6220 -0.0721 -0.0204 0.1247  103 TYR B O   
4942  C CB  . TYR B 103 ? 0.2390 0.3302 0.5674 -0.0836 -0.0341 0.0910  103 TYR B CB  
4943  C CG  . TYR B 103 ? 0.2817 0.3829 0.6376 -0.0879 -0.0309 0.1096  103 TYR B CG  
4944  C CD1 . TYR B 103 ? 0.2015 0.3247 0.5536 -0.0855 -0.0252 0.1245  103 TYR B CD1 
4945  C CD2 . TYR B 103 ? 0.5996 0.6862 0.9778 -0.0913 -0.0329 0.1098  103 TYR B CD2 
4946  C CE1 . TYR B 103 ? 0.3302 0.4607 0.6992 -0.0869 -0.0218 0.1400  103 TYR B CE1 
4947  C CE2 . TYR B 103 ? 0.5564 0.6498 0.9537 -0.0927 -0.0298 0.1259  103 TYR B CE2 
4948  C CZ  . TYR B 103 ? 0.4871 0.6025 0.8792 -0.0907 -0.0244 0.1414  103 TYR B CZ  
4949  O OH  . TYR B 103 ? 0.3566 0.4796 0.7673 -0.0921 -0.0214 0.1577  103 TYR B OH  
4950  N N   . GLU B 104 ? 0.3640 0.4296 0.6690 -0.0730 -0.0293 0.0913  104 GLU B N   
4951  C CA  . GLU B 104 ? 0.3848 0.4401 0.7022 -0.0720 -0.0275 0.0995  104 GLU B CA  
4952  C C   . GLU B 104 ? 0.3717 0.4326 0.6633 -0.0635 -0.0228 0.1057  104 GLU B C   
4953  O O   . GLU B 104 ? 0.3363 0.3947 0.6379 -0.0619 -0.0206 0.1180  104 GLU B O   
4954  C CB  . GLU B 104 ? 0.5230 0.5564 0.8513 -0.0751 -0.0328 0.0812  104 GLU B CB  
4955  C CG  . GLU B 104 ? 0.6303 0.6592 0.9770 -0.0833 -0.0388 0.0674  104 GLU B CG  
4956  C CD  . GLU B 104 ? 0.8384 0.8656 1.2132 -0.0860 -0.0383 0.0774  104 GLU B CD  
4957  O OE1 . GLU B 104 ? 0.9333 0.9524 1.3200 -0.0899 -0.0426 0.0630  104 GLU B OE1 
4958  O OE2 . GLU B 104 ? 0.8678 0.9029 1.2517 -0.0839 -0.0335 0.0994  104 GLU B OE2 
4959  N N   . LYS B 105 ? 0.2754 0.3440 0.5360 -0.0581 -0.0215 0.0979  105 LYS B N   
4960  C CA  . LYS B 105 ? 0.1873 0.2616 0.4241 -0.0505 -0.0174 0.1011  105 LYS B CA  
4961  C C   . LYS B 105 ? 0.1916 0.2871 0.4319 -0.0487 -0.0116 0.1230  105 LYS B C   
4962  O O   . LYS B 105 ? 0.3553 0.4668 0.6000 -0.0503 -0.0093 0.1305  105 LYS B O   
4963  C CB  . LYS B 105 ? 0.1792 0.2557 0.3859 -0.0458 -0.0174 0.0864  105 LYS B CB  
4964  C CG  . LYS B 105 ? 0.1790 0.2369 0.3769 -0.0462 -0.0221 0.0666  105 LYS B CG  
4965  C CD  . LYS B 105 ? 0.1735 0.2344 0.3524 -0.0446 -0.0237 0.0543  105 LYS B CD  
4966  C CE  . LYS B 105 ? 0.1752 0.2205 0.3458 -0.0456 -0.0284 0.0363  105 LYS B CE  
4967  N NZ  . LYS B 105 ? 0.2313 0.2806 0.3922 -0.0464 -0.0317 0.0269  105 LYS B NZ  
4968  N N   . PRO B 106 ? 0.1910 0.2897 0.4300 -0.0452 -0.0092 0.1342  106 PRO B N   
4969  C CA  . PRO B 106 ? 0.2167 0.3390 0.4604 -0.0439 -0.0038 0.1569  106 PRO B CA  
4970  C C   . PRO B 106 ? 0.1912 0.3366 0.4118 -0.0396 0.0009  0.1566  106 PRO B C   
4971  O O   . PRO B 106 ? 0.2215 0.3898 0.4478 -0.0398 0.0057  0.1741  106 PRO B O   
4972  C CB  . PRO B 106 ? 0.1998 0.3206 0.4412 -0.0399 -0.0034 0.1650  106 PRO B CB  
4973  C CG  . PRO B 106 ? 0.3002 0.3953 0.5381 -0.0392 -0.0080 0.1461  106 PRO B CG  
4974  C CD  . PRO B 106 ? 0.2789 0.3595 0.5208 -0.0438 -0.0118 0.1287  106 PRO B CD  
4975  N N   . ILE B 107 ? 0.2451 0.3863 0.4412 -0.0356 0.0003  0.1377  107 ILE B N   
4976  C CA  . ILE B 107 ? 0.3170 0.4789 0.4951 -0.0314 0.0049  0.1355  107 ILE B CA  
4977  C C   . ILE B 107 ? 0.3381 0.5097 0.5297 -0.0352 0.0060  0.1393  107 ILE B C   
4978  O O   . ILE B 107 ? 0.3212 0.5141 0.5045 -0.0322 0.0111  0.1416  107 ILE B O   
4979  C CB  . ILE B 107 ? 0.1695 0.3224 0.3227 -0.0263 0.0038  0.1148  107 ILE B CB  
4980  C CG1 . ILE B 107 ? 0.1670 0.2971 0.3239 -0.0296 -0.0021 0.1001  107 ILE B CG1 
4981  C CG2 . ILE B 107 ? 0.1963 0.3461 0.3351 -0.0220 0.0040  0.1123  107 ILE B CG2 
4982  C CD1 . ILE B 107 ? 0.1759 0.3025 0.3129 -0.0255 -0.0025 0.0836  107 ILE B CD1 
4983  N N   . TYR B 108 ? 0.3035 0.4610 0.5169 -0.0418 0.0014  0.1390  108 TYR B N   
4984  C CA  . TYR B 108 ? 0.2349 0.4014 0.4653 -0.0466 0.0016  0.1436  108 TYR B CA  
4985  C C   . TYR B 108 ? 0.2362 0.4133 0.4943 -0.0520 0.0040  0.1657  108 TYR B C   
4986  O O   . TYR B 108 ? 0.2001 0.3795 0.4800 -0.0581 0.0027  0.1698  108 TYR B O   
4987  C CB  . TYR B 108 ? 0.1778 0.3249 0.4156 -0.0511 -0.0056 0.1279  108 TYR B CB  
4988  C CG  . TYR B 108 ? 0.2273 0.3758 0.4460 -0.0472 -0.0068 0.1125  108 TYR B CG  
4989  C CD1 . TYR B 108 ? 0.2730 0.4139 0.4661 -0.0410 -0.0068 0.0999  108 TYR B CD1 
4990  C CD2 . TYR B 108 ? 0.2350 0.3925 0.4634 -0.0498 -0.0080 0.1115  108 TYR B CD2 
4991  C CE1 . TYR B 108 ? 0.2929 0.4345 0.4717 -0.0374 -0.0078 0.0877  108 TYR B CE1 
4992  C CE2 . TYR B 108 ? 0.2433 0.4025 0.4567 -0.0458 -0.0093 0.0992  108 TYR B CE2 
4993  C CZ  . TYR B 108 ? 0.2906 0.4413 0.4797 -0.0395 -0.0091 0.0879  108 TYR B CZ  
4994  O OH  . TYR B 108 ? 0.2897 0.4415 0.4669 -0.0355 -0.0103 0.0775  108 TYR B OH  
4995  N N   . ARG B 109 ? 0.2432 0.4277 0.5024 -0.0502 0.0073  0.1810  109 ARG B N   
4996  C CA  . ARG B 109 ? 0.2858 0.4806 0.5731 -0.0553 0.0098  0.2052  109 ARG B CA  
4997  C C   . ARG B 109 ? 0.3019 0.5256 0.5803 -0.0518 0.0161  0.2164  109 ARG B C   
4998  O O   . ARG B 109 ? 0.2363 0.4779 0.5046 -0.0471 0.0202  0.2297  109 ARG B O   
4999  C CB  . ARG B 109 ? 0.2082 0.3962 0.4992 -0.0533 0.0091  0.2162  109 ARG B CB  
5000  C CG  . ARG B 109 ? 0.2637 0.4428 0.5828 -0.0556 0.0064  0.2303  109 ARG B CG  
5001  C CD  . ARG B 109 ? 0.2662 0.4318 0.5943 -0.0537 0.0038  0.2364  109 ARG B CD  
5002  N NE  . ARG B 109 ? 0.3993 0.5836 0.7060 -0.0475 0.0074  0.2456  109 ARG B NE  
5003  C CZ  . ARG B 109 ? 0.4427 0.6179 0.7407 -0.0452 0.0062  0.2410  109 ARG B CZ  
5004  N NH1 . ARG B 109 ? 0.3367 0.4838 0.6458 -0.0482 0.0017  0.2273  109 ARG B NH1 
5005  N NH2 . ARG B 109 ? 0.4422 0.6380 0.7196 -0.0395 0.0094  0.2492  109 ARG B NH2 
5006  N N   . PHE B 110 ? 0.3249 0.5538 0.6068 -0.0538 0.0164  0.2098  110 PHE B N   
5007  C CA  . PHE B 110 ? 0.2165 0.4684 0.4978 -0.0521 0.0215  0.2197  110 PHE B CA  
5008  C C   . PHE B 110 ? 0.3256 0.5685 0.6349 -0.0582 0.0182  0.2278  110 PHE B C   
5009  O O   . PHE B 110 ? 0.5130 0.7347 0.8376 -0.0636 0.0122  0.2174  110 PHE B O   
5010  C CB  . PHE B 110 ? 0.2235 0.4889 0.4907 -0.0493 0.0246  0.2064  110 PHE B CB  
5011  C CG  . PHE B 110 ? 0.2431 0.5190 0.4840 -0.0425 0.0283  0.1963  110 PHE B CG  
5012  C CD1 . PHE B 110 ? 0.3309 0.5844 0.5588 -0.0405 0.0231  0.1775  110 PHE B CD1 
5013  C CD2 . PHE B 110 ? 0.2178 0.5192 0.4403 -0.0361 0.0352  0.2002  110 PHE B CD2 
5014  C CE1 . PHE B 110 ? 0.2665 0.5228 0.4666 -0.0328 0.0251  0.1646  110 PHE B CE1 
5015  C CE2 . PHE B 110 ? 0.3326 0.6432 0.5317 -0.0297 0.0385  0.1881  110 PHE B CE2 
5016  C CZ  . PHE B 110 ? 0.3373 0.6224 0.5244 -0.0277 0.0328  0.1697  110 PHE B CZ  
5017  N N   . GLU B 111 ? 0.4044 0.6643 0.7206 -0.0572 0.0219  0.2453  111 GLU B N   
5018  C CA  . GLU B 111 ? 0.4570 0.7103 0.8012 -0.0629 0.0193  0.2532  111 GLU B CA  
5019  C C   . GLU B 111 ? 0.4283 0.6860 0.7762 -0.0658 0.0194  0.2431  111 GLU B C   
5020  O O   . GLU B 111 ? 0.5177 0.7624 0.8881 -0.0719 0.0149  0.2405  111 GLU B O   
5021  C CB  . GLU B 111 ? 0.6062 0.8777 0.9586 -0.0609 0.0230  0.2765  111 GLU B CB  
5022  C CG  . GLU B 111 ? 0.6504 0.9131 1.0357 -0.0667 0.0200  0.2865  111 GLU B CG  
5023  C CD  . GLU B 111 ? 0.8003 1.0361 1.2072 -0.0696 0.0138  0.2861  111 GLU B CD  
5024  O OE1 . GLU B 111 ? 0.8094 1.0380 1.2066 -0.0663 0.0127  0.2849  111 GLU B OE1 
5025  O OE2 . GLU B 111 ? 0.6338 0.8561 1.0682 -0.0752 0.0102  0.2861  111 GLU B OE2 
5026  N N   . ARG B 112 ? 0.3345 0.6109 0.6616 -0.0612 0.0242  0.2364  112 ARG B N   
5027  C CA  . ARG B 112 ? 0.3695 0.6511 0.7007 -0.0630 0.0240  0.2262  112 ARG B CA  
5028  C C   . ARG B 112 ? 0.3526 0.6118 0.6910 -0.0675 0.0161  0.2087  112 ARG B C   
5029  O O   . ARG B 112 ? 0.2704 0.5261 0.6241 -0.0722 0.0123  0.2034  112 ARG B O   
5030  C CB  . ARG B 112 ? 0.3832 0.6875 0.6910 -0.0558 0.0307  0.2202  112 ARG B CB  
5031  C CG  . ARG B 112 ? 0.3056 0.6171 0.6177 -0.0560 0.0308  0.2098  112 ARG B CG  
5032  C CD  . ARG B 112 ? 0.2606 0.5830 0.5916 -0.0596 0.0326  0.2215  112 ARG B CD  
5033  N NE  . ARG B 112 ? 0.2267 0.5631 0.5576 -0.0575 0.0350  0.2133  112 ARG B NE  
5034  C CZ  . ARG B 112 ? 0.3349 0.6758 0.6853 -0.0619 0.0340  0.2167  112 ARG B CZ  
5035  N NH1 . ARG B 112 ? 0.4771 0.8092 0.8491 -0.0688 0.0308  0.2275  112 ARG B NH1 
5036  N NH2 . ARG B 112 ? 0.3371 0.6914 0.6867 -0.0589 0.0362  0.2087  112 ARG B NH2 
5037  N N   . ILE B 113 ? 0.3906 0.6358 0.7178 -0.0662 0.0131  0.1992  113 ILE B N   
5038  C CA  . ILE B 113 ? 0.3168 0.5417 0.6491 -0.0703 0.0050  0.1821  113 ILE B CA  
5039  C C   . ILE B 113 ? 0.3232 0.5284 0.6808 -0.0778 -0.0012 0.1826  113 ILE B C   
5040  O O   . ILE B 113 ? 0.3365 0.5314 0.7037 -0.0826 -0.0079 0.1693  113 ILE B O   
5041  C CB  . ILE B 113 ? 0.2173 0.4332 0.5320 -0.0670 0.0040  0.1731  113 ILE B CB  
5042  C CG1 . ILE B 113 ? 0.2646 0.4988 0.5556 -0.0594 0.0093  0.1677  113 ILE B CG1 
5043  C CG2 . ILE B 113 ? 0.3612 0.5548 0.6820 -0.0718 -0.0050 0.1563  113 ILE B CG2 
5044  C CD1 . ILE B 113 ? 0.2339 0.4497 0.4979 -0.0535 0.0059  0.1500  113 ILE B CD1 
5045  N N   . ARG B 114 ? 0.3475 0.5485 0.7166 -0.0784 0.0005  0.1973  114 ARG B N   
5046  C CA  . ARG B 114 ? 0.4084 0.5911 0.8042 -0.0845 -0.0047 0.1976  114 ARG B CA  
5047  C C   . ARG B 114 ? 0.3864 0.5763 0.7998 -0.0893 -0.0058 0.1984  114 ARG B C   
5048  O O   . ARG B 114 ? 0.3231 0.4984 0.7542 -0.0952 -0.0122 0.1878  114 ARG B O   
5049  C CB  . ARG B 114 ? 0.4043 0.5846 0.8110 -0.0828 -0.0022 0.2160  114 ARG B CB  
5050  C CG  . ARG B 114 ? 0.4017 0.5561 0.8299 -0.0864 -0.0081 0.2108  114 ARG B CG  
5051  C CD  . ARG B 114 ? 0.5503 0.7000 1.0087 -0.0921 -0.0106 0.2140  114 ARG B CD  
5052  N NE  . ARG B 114 ? 0.6260 0.7979 1.0898 -0.0914 -0.0052 0.2333  114 ARG B NE  
5053  C CZ  . ARG B 114 ? 0.6015 0.7745 1.0912 -0.0960 -0.0060 0.2403  114 ARG B CZ  
5054  N NH1 . ARG B 114 ? 0.5375 0.6910 1.0509 -0.1016 -0.0119 0.2292  114 ARG B NH1 
5055  N NH2 . ARG B 114 ? 0.5594 0.7546 1.0515 -0.0948 -0.0005 0.2582  114 ARG B NH2 
5056  N N   . GLU B 115 ? 0.4519 0.6653 0.8604 -0.0866 0.0004  0.2100  115 GLU B N   
5057  C CA  . GLU B 115 ? 0.4495 0.6717 0.8751 -0.0909 -0.0001 0.2118  115 GLU B CA  
5058  C C   . GLU B 115 ? 0.3868 0.6080 0.8084 -0.0931 -0.0053 0.1926  115 GLU B C   
5059  O O   . GLU B 115 ? 0.3188 0.5346 0.7589 -0.0992 -0.0105 0.1860  115 GLU B O   
5060  C CB  . GLU B 115 ? 0.4229 0.6719 0.8429 -0.0869 0.0084  0.2284  115 GLU B CB  
5061  C CG  . GLU B 115 ? 0.5592 0.8163 0.9713 -0.0820 0.0140  0.2460  115 GLU B CG  
5062  C CD  . GLU B 115 ? 0.6446 0.9313 1.0435 -0.0768 0.0225  0.2576  115 GLU B CD  
5063  O OE1 . GLU B 115 ? 0.6279 0.9273 1.0300 -0.0778 0.0244  0.2545  115 GLU B OE1 
5064  O OE2 . GLU B 115 ? 0.5668 0.8651 0.9518 -0.0716 0.0270  0.2689  115 GLU B OE2 
5065  N N   . LEU B 116 ? 0.3622 0.5900 0.7605 -0.0879 -0.0041 0.1836  116 LEU B N   
5066  C CA  . LEU B 116 ? 0.2880 0.5182 0.6822 -0.0885 -0.0092 0.1677  116 LEU B CA  
5067  C C   . LEU B 116 ? 0.3594 0.5684 0.7610 -0.0943 -0.0192 0.1511  116 LEU B C   
5068  O O   . LEU B 116 ? 0.3795 0.5900 0.7883 -0.0979 -0.0252 0.1404  116 LEU B O   
5069  C CB  . LEU B 116 ? 0.2018 0.4431 0.5709 -0.0806 -0.0056 0.1626  116 LEU B CB  
5070  C CG  . LEU B 116 ? 0.2018 0.4666 0.5608 -0.0741 0.0046  0.1747  116 LEU B CG  
5071  C CD1 . LEU B 116 ? 0.1887 0.4644 0.5271 -0.0663 0.0072  0.1652  116 LEU B CD1 
5072  C CD2 . LEU B 116 ? 0.2978 0.5768 0.6735 -0.0767 0.0071  0.1832  116 LEU B CD2 
5073  N N   . MET B 117 ? 0.2992 0.4897 0.6987 -0.0949 -0.0211 0.1482  117 MET B N   
5074  C CA  . MET B 117 ? 0.2342 0.4049 0.6392 -0.0999 -0.0300 0.1305  117 MET B CA  
5075  C C   . MET B 117 ? 0.3798 0.5413 0.8115 -0.1071 -0.0337 0.1295  117 MET B C   
5076  O O   . MET B 117 ? 0.4503 0.6008 0.8876 -0.1119 -0.0414 0.1123  117 MET B O   
5077  C CB  . MET B 117 ? 0.4196 0.5738 0.8140 -0.0976 -0.0303 0.1266  117 MET B CB  
5078  C CG  . MET B 117 ? 0.4323 0.5904 0.8017 -0.0925 -0.0306 0.1182  117 MET B CG  
5079  S SD  . MET B 117 ? 0.5784 0.7400 0.9421 -0.0947 -0.0397 0.0986  117 MET B SD  
5080  C CE  . MET B 117 ? 0.2368 0.4248 0.5890 -0.0879 -0.0340 0.1076  117 MET B CE  
5081  N N   . ASN B 118 ? 0.4725 0.6395 0.9205 -0.1079 -0.0285 0.1471  118 ASN B N   
5082  C CA  . ASN B 118 ? 0.5274 0.6890 1.0033 -0.1146 -0.0315 0.1476  118 ASN B CA  
5083  C C   . ASN B 118 ? 0.4916 0.6712 0.9754 -0.1175 -0.0319 0.1485  118 ASN B C   
5084  O O   . ASN B 118 ? 0.4587 0.6356 0.9657 -0.1239 -0.0353 0.1462  118 ASN B O   
5085  C CB  . ASN B 118 ? 0.4363 0.5945 0.9293 -0.1140 -0.0263 0.1675  118 ASN B CB  
5086  C CG  . ASN B 118 ? 0.5540 0.6886 1.0588 -0.1153 -0.0297 0.1616  118 ASN B CG  
5087  O OD1 . ASN B 118 ? 0.6508 0.7752 1.1817 -0.1202 -0.0327 0.1596  118 ASN B OD1 
5088  N ND2 . ASN B 118 ? 0.4093 0.5353 0.8960 -0.1106 -0.0291 0.1581  118 ASN B ND2 
5089  N N   . LYS B 119 ? 0.4177 0.6158 0.8840 -0.1127 -0.0285 0.1513  119 LYS B N   
5090  C CA  . LYS B 119 ? 0.3864 0.6031 0.8595 -0.1141 -0.0283 0.1526  119 LYS B CA  
5091  C C   . LYS B 119 ? 0.4356 0.6510 0.9078 -0.1177 -0.0377 0.1324  119 LYS B C   
5092  O O   . LYS B 119 ? 0.3866 0.5939 0.8424 -0.1159 -0.0424 0.1189  119 LYS B O   
5093  C CB  . LYS B 119 ? 0.3828 0.6203 0.8379 -0.1063 -0.0204 0.1625  119 LYS B CB  
5094  C CG  . LYS B 119 ? 0.3578 0.6163 0.8218 -0.1065 -0.0179 0.1674  119 LYS B CG  
5095  C CD  . LYS B 119 ? 0.2944 0.5687 0.7594 -0.1030 -0.0075 0.1874  119 LYS B CD  
5096  C CE  . LYS B 119 ? 0.4739 0.7665 0.9549 -0.1053 -0.0055 0.1929  119 LYS B CE  
5097  N NZ  . LYS B 119 ? 0.3247 0.6078 0.8325 -0.1146 -0.0122 0.1896  119 LYS B NZ  
5098  N N   . GLU B 120 ? 0.4594 0.6843 0.9493 -0.1228 -0.0407 0.1307  120 GLU B N   
5099  C CA  . GLU B 120 ? 0.3908 0.6181 0.8810 -0.1266 -0.0502 0.1125  120 GLU B CA  
5100  C C   . GLU B 120 ? 0.3606 0.6084 0.8388 -0.1214 -0.0502 0.1119  120 GLU B C   
5101  O O   . GLU B 120 ? 0.3032 0.5527 0.7702 -0.1206 -0.0576 0.0978  120 GLU B O   
5102  C CB  . GLU B 120 ? 0.4120 0.6383 0.9296 -0.1357 -0.0547 0.1086  120 GLU B CB  
5103  C CG  . GLU B 120 ? 0.5764 0.7802 1.1060 -0.1412 -0.0582 0.1007  120 GLU B CG  
5104  C CD  . GLU B 120 ? 0.6543 0.8494 1.1985 -0.1407 -0.0506 0.1190  120 GLU B CD  
5105  O OE1 . GLU B 120 ? 0.7540 0.9624 1.3096 -0.1403 -0.0447 0.1360  120 GLU B OE1 
5106  O OE2 . GLU B 120 ? 0.5399 0.7159 1.0842 -0.1402 -0.0507 0.1168  120 GLU B OE2 
5107  N N   . LYS B 121 ? 0.3342 0.5985 0.8150 -0.1174 -0.0421 0.1268  121 LYS B N   
5108  C CA  . LYS B 121 ? 0.2659 0.5495 0.7366 -0.1109 -0.0405 0.1271  121 LYS B CA  
5109  C C   . LYS B 121 ? 0.3112 0.6026 0.7672 -0.1023 -0.0296 0.1399  121 LYS B C   
5110  O O   . LYS B 121 ? 0.3180 0.6123 0.7810 -0.1028 -0.0218 0.1541  121 LYS B O   
5111  C CB  . LYS B 121 ? 0.2417 0.5423 0.7322 -0.1144 -0.0415 0.1298  121 LYS B CB  
5112  C CG  . LYS B 121 ? 0.2446 0.5656 0.7276 -0.1069 -0.0391 0.1311  121 LYS B CG  
5113  C CD  . LYS B 121 ? 0.2241 0.5442 0.6926 -0.1035 -0.0478 0.1170  121 LYS B CD  
5114  C CE  . LYS B 121 ? 0.2230 0.5632 0.6972 -0.1002 -0.0503 0.1156  121 LYS B CE  
5115  N NZ  . LYS B 121 ? 0.2339 0.5791 0.7274 -0.1089 -0.0592 0.1088  121 LYS B NZ  
5116  N N   . LEU B 122 ? 0.2262 0.5224 0.6622 -0.0945 -0.0290 0.1348  122 LEU B N   
5117  C CA  . LEU B 122 ? 0.2060 0.5107 0.6262 -0.0858 -0.0188 0.1432  122 LEU B CA  
5118  C C   . LEU B 122 ? 0.2018 0.5273 0.6204 -0.0790 -0.0151 0.1436  122 LEU B C   
5119  O O   . LEU B 122 ? 0.2537 0.5822 0.6719 -0.0774 -0.0219 0.1341  122 LEU B O   
5120  C CB  . LEU B 122 ? 0.1956 0.4878 0.5945 -0.0814 -0.0201 0.1362  122 LEU B CB  
5121  C CG  . LEU B 122 ? 0.1987 0.4685 0.5980 -0.0875 -0.0254 0.1316  122 LEU B CG  
5122  C CD1 . LEU B 122 ? 0.1884 0.4483 0.5697 -0.0843 -0.0310 0.1191  122 LEU B CD1 
5123  C CD2 . LEU B 122 ? 0.2034 0.4684 0.6020 -0.0873 -0.0177 0.1445  122 LEU B CD2 
5124  N N   . ASN B 123 ? 0.2045 0.5449 0.6221 -0.0746 -0.0044 0.1544  123 ASN B N   
5125  C CA  . ASN B 123 ? 0.2021 0.5626 0.6189 -0.0674 0.0009  0.1543  123 ASN B CA  
5126  C C   . ASN B 123 ? 0.1922 0.5555 0.5871 -0.0572 0.0065  0.1498  123 ASN B C   
5127  O O   . ASN B 123 ? 0.1860 0.5354 0.5665 -0.0562 0.0047  0.1459  123 ASN B O   
5128  C CB  . ASN B 123 ? 0.2130 0.5904 0.6429 -0.0688 0.0092  0.1669  123 ASN B CB  
5129  C CG  . ASN B 123 ? 0.2179 0.5967 0.6384 -0.0677 0.0182  0.1784  123 ASN B CG  
5130  O OD1 . ASN B 123 ? 0.2130 0.5981 0.6149 -0.0600 0.0251  0.1774  123 ASN B OD1 
5131  N ND2 . ASN B 123 ? 0.2589 0.6328 0.6931 -0.0753 0.0181  0.1893  123 ASN B ND2 
5132  N N   . ARG B 124 ? 0.1917 0.5729 0.5852 -0.0494 0.0135  0.1493  124 ARG B N   
5133  C CA  . ARG B 124 ? 0.1836 0.5675 0.5593 -0.0391 0.0182  0.1420  124 ARG B CA  
5134  C C   . ARG B 124 ? 0.1840 0.5670 0.5427 -0.0368 0.0263  0.1460  124 ARG B C   
5135  O O   . ARG B 124 ? 0.1981 0.5728 0.5405 -0.0321 0.0263  0.1391  124 ARG B O   
5136  C CB  . ARG B 124 ? 0.1854 0.5888 0.5668 -0.0313 0.0244  0.1393  124 ARG B CB  
5137  C CG  . ARG B 124 ? 0.1787 0.5838 0.5452 -0.0203 0.0291  0.1296  124 ARG B CG  
5138  C CD  . ARG B 124 ? 0.2022 0.6275 0.5743 -0.0123 0.0381  0.1268  124 ARG B CD  
5139  N NE  . ARG B 124 ? 0.2736 0.6998 0.6318 -0.0021 0.0441  0.1166  124 ARG B NE  
5140  C CZ  . ARG B 124 ? 0.2475 0.6801 0.5907 0.0012  0.0535  0.1153  124 ARG B CZ  
5141  N NH1 . ARG B 124 ? 0.1904 0.6300 0.5298 -0.0043 0.0582  0.1256  124 ARG B NH1 
5142  N NH2 . ARG B 124 ? 0.2074 0.6396 0.5396 0.0103  0.0580  0.1036  124 ARG B NH2 
5143  N N   . GLU B 125 ? 0.1939 0.5866 0.5559 -0.0398 0.0331  0.1576  125 GLU B N   
5144  C CA  . GLU B 125 ? 0.1965 0.5916 0.5413 -0.0372 0.0404  0.1624  125 GLU B CA  
5145  C C   . GLU B 125 ? 0.2068 0.5809 0.5460 -0.0425 0.0345  0.1645  125 GLU B C   
5146  O O   . GLU B 125 ? 0.1894 0.5599 0.5107 -0.0385 0.0373  0.1623  125 GLU B O   
5147  C CB  . GLU B 125 ? 0.2102 0.6231 0.5603 -0.0389 0.0486  0.1760  125 GLU B CB  
5148  C CG  . GLU B 125 ? 0.2511 0.6880 0.6016 -0.0320 0.0573  0.1728  125 GLU B CG  
5149  C CD  . GLU B 125 ? 0.3918 0.8319 0.7601 -0.0318 0.0532  0.1665  125 GLU B CD  
5150  O OE1 . GLU B 125 ? 0.4143 0.8431 0.7980 -0.0392 0.0444  0.1689  125 GLU B OE1 
5151  O OE2 . GLU B 125 ? 0.2117 0.6660 0.5793 -0.0241 0.0586  0.1585  125 GLU B OE2 
5152  N N   . GLU B 126 ? 0.2154 0.5756 0.5707 -0.0513 0.0263  0.1676  126 GLU B N   
5153  C CA  . GLU B 126 ? 0.1937 0.5326 0.5465 -0.0564 0.0204  0.1678  126 GLU B CA  
5154  C C   . GLU B 126 ? 0.1811 0.5070 0.5220 -0.0535 0.0142  0.1538  126 GLU B C   
5155  O O   . GLU B 126 ? 0.3225 0.6363 0.6518 -0.0532 0.0133  0.1522  126 GLU B O   
5156  C CB  . GLU B 126 ? 0.2046 0.5324 0.5797 -0.0665 0.0135  0.1724  126 GLU B CB  
5157  C CG  . GLU B 126 ? 0.4286 0.7714 0.8191 -0.0692 0.0190  0.1860  126 GLU B CG  
5158  C CD  . GLU B 126 ? 0.5559 0.8868 0.9701 -0.0791 0.0128  0.1907  126 GLU B CD  
5159  O OE1 . GLU B 126 ? 0.5882 0.9093 1.0124 -0.0837 0.0039  0.1799  126 GLU B OE1 
5160  O OE2 . GLU B 126 ? 0.5039 0.8361 0.9270 -0.0821 0.0166  0.2052  126 GLU B OE2 
5161  N N   . LEU B 127 ? 0.1755 0.5043 0.5197 -0.0510 0.0097  0.1442  127 LEU B N   
5162  C CA  . LEU B 127 ? 0.1647 0.4842 0.4966 -0.0467 0.0045  0.1323  127 LEU B CA  
5163  C C   . LEU B 127 ? 0.1593 0.4866 0.4727 -0.0370 0.0130  0.1294  127 LEU B C   
5164  O O   . LEU B 127 ? 0.1847 0.5018 0.4851 -0.0341 0.0108  0.1226  127 LEU B O   
5165  C CB  . LEU B 127 ? 0.1623 0.4848 0.5026 -0.0457 -0.0026 0.1248  127 LEU B CB  
5166  C CG  . LEU B 127 ? 0.1714 0.4836 0.5255 -0.0551 -0.0138 0.1221  127 LEU B CG  
5167  C CD1 . LEU B 127 ? 0.1673 0.4893 0.5309 -0.0535 -0.0194 0.1176  127 LEU B CD1 
5168  C CD2 . LEU B 127 ? 0.1625 0.4553 0.5074 -0.0585 -0.0218 0.1143  127 LEU B CD2 
5169  N N   . LEU B 128 ? 0.1642 0.5101 0.4764 -0.0318 0.0226  0.1332  128 LEU B N   
5170  C CA  . LEU B 128 ? 0.1625 0.5168 0.4565 -0.0232 0.0314  0.1291  128 LEU B CA  
5171  C C   . LEU B 128 ? 0.1719 0.5197 0.4535 -0.0257 0.0335  0.1349  128 LEU B C   
5172  O O   . LEU B 128 ? 0.1591 0.5043 0.4240 -0.0205 0.0359  0.1283  128 LEU B O   
5173  C CB  . LEU B 128 ? 0.2407 0.6174 0.5367 -0.0182 0.0411  0.1312  128 LEU B CB  
5174  C CG  . LEU B 128 ? 0.1688 0.5557 0.4526 -0.0073 0.0483  0.1194  128 LEU B CG  
5175  C CD1 . LEU B 128 ? 0.1770 0.5845 0.4699 -0.0033 0.0556  0.1190  128 LEU B CD1 
5176  C CD2 . LEU B 128 ? 0.4251 0.8134 0.6879 -0.0044 0.0540  0.1178  128 LEU B CD2 
5177  N N   . ASP B 129 ? 0.1728 0.5177 0.4636 -0.0334 0.0325  0.1473  129 ASP B N   
5178  C CA  . ASP B 129 ? 0.1748 0.5124 0.4567 -0.0359 0.0336  0.1547  129 ASP B CA  
5179  C C   . ASP B 129 ? 0.2158 0.5309 0.4956 -0.0390 0.0254  0.1481  129 ASP B C   
5180  O O   . ASP B 129 ? 0.2523 0.5622 0.5187 -0.0373 0.0268  0.1480  129 ASP B O   
5181  C CB  . ASP B 129 ? 0.2612 0.6006 0.5572 -0.0427 0.0343  0.1708  129 ASP B CB  
5182  C CG  . ASP B 129 ? 0.3668 0.7302 0.6584 -0.0389 0.0439  0.1798  129 ASP B CG  
5183  O OD1 . ASP B 129 ? 0.3940 0.7729 0.6785 -0.0323 0.0491  0.1718  129 ASP B OD1 
5184  O OD2 . ASP B 129 ? 0.3247 0.6918 0.6207 -0.0423 0.0459  0.1948  129 ASP B OD2 
5185  N N   . LEU B 130 ? 0.1868 0.4897 0.4793 -0.0438 0.0165  0.1421  130 LEU B N   
5186  C CA  . LEU B 130 ? 0.1586 0.4368 0.4435 -0.0460 0.0080  0.1323  130 LEU B CA  
5187  C C   . LEU B 130 ? 0.1543 0.4238 0.4131 -0.0368 0.0083  0.1181  130 LEU B C   
5188  O O   . LEU B 130 ? 0.1933 0.4441 0.4357 -0.0357 0.0057  0.1115  130 LEU B O   
5189  C CB  . LEU B 130 ? 0.1591 0.4277 0.4609 -0.0530 -0.0021 0.1274  130 LEU B CB  
5190  C CG  . LEU B 130 ? 0.1607 0.4023 0.4551 -0.0569 -0.0108 0.1174  130 LEU B CG  
5191  C CD1 . LEU B 130 ? 0.1666 0.4001 0.4762 -0.0646 -0.0111 0.1265  130 LEU B CD1 
5192  C CD2 . LEU B 130 ? 0.1606 0.3963 0.4614 -0.0604 -0.0209 0.1067  130 LEU B CD2 
5193  N N   . GLN B 131 ? 0.1514 0.4343 0.4084 -0.0301 0.0115  0.1132  131 GLN B N   
5194  C CA  . GLN B 131 ? 0.1484 0.4235 0.3847 -0.0214 0.0125  0.1004  131 GLN B CA  
5195  C C   . GLN B 131 ? 0.1752 0.4534 0.3938 -0.0167 0.0201  0.0999  131 GLN B C   
5196  O O   . GLN B 131 ? 0.2217 0.4828 0.4224 -0.0139 0.0181  0.0912  131 GLN B O   
5197  C CB  . GLN B 131 ? 0.1464 0.4368 0.3898 -0.0149 0.0153  0.0964  131 GLN B CB  
5198  C CG  . GLN B 131 ? 0.1448 0.4286 0.3984 -0.0166 0.0061  0.0926  131 GLN B CG  
5199  C CD  . GLN B 131 ? 0.1438 0.4474 0.4116 -0.0111 0.0094  0.0929  131 GLN B CD  
5200  O OE1 . GLN B 131 ? 0.1444 0.4665 0.4143 -0.0058 0.0193  0.0944  131 GLN B OE1 
5201  N NE2 . GLN B 131 ? 0.1431 0.4446 0.4211 -0.0120 0.0013  0.0912  131 GLN B NE2 
5202  N N   . THR B 132 ? 0.1525 0.4546 0.3761 -0.0159 0.0288  0.1095  132 THR B N   
5203  C CA  . THR B 132 ? 0.1548 0.4659 0.3610 -0.0108 0.0362  0.1082  132 THR B CA  
5204  C C   . THR B 132 ? 0.1570 0.4551 0.3555 -0.0154 0.0335  0.1146  132 THR B C   
5205  O O   . THR B 132 ? 0.1570 0.4472 0.3366 -0.0114 0.0342  0.1073  132 THR B O   
5206  C CB  . THR B 132 ? 0.1588 0.5036 0.3719 -0.0087 0.0465  0.1169  132 THR B CB  
5207  O OG1 . THR B 132 ? 0.1568 0.5136 0.3808 -0.0045 0.0488  0.1109  132 THR B OG1 
5208  C CG2 . THR B 132 ? 0.1623 0.5204 0.3556 -0.0026 0.0539  0.1124  132 THR B CG2 
5209  N N   . LEU B 133 ? 0.1596 0.4551 0.3748 -0.0236 0.0304  0.1280  133 LEU B N   
5210  C CA  . LEU B 133 ? 0.1945 0.4769 0.4067 -0.0276 0.0279  0.1348  133 LEU B CA  
5211  C C   . LEU B 133 ? 0.1835 0.4353 0.3852 -0.0279 0.0196  0.1216  133 LEU B C   
5212  O O   . LEU B 133 ? 0.2673 0.5078 0.4591 -0.0278 0.0185  0.1218  133 LEU B O   
5213  C CB  . LEU B 133 ? 0.2115 0.4976 0.4488 -0.0364 0.0268  0.1523  133 LEU B CB  
5214  C CG  . LEU B 133 ? 0.1887 0.4986 0.4285 -0.0361 0.0348  0.1695  133 LEU B CG  
5215  C CD1 . LEU B 133 ? 0.2430 0.5424 0.5009 -0.0434 0.0314  0.1847  133 LEU B CD1 
5216  C CD2 . LEU B 133 ? 0.1776 0.4986 0.3944 -0.0296 0.0402  0.1686  133 LEU B CD2 
5217  N N   . ASN B 134 ? 0.1558 0.3958 0.3599 -0.0282 0.0138  0.1108  134 ASN B N   
5218  C CA  . ASN B 134 ? 0.1533 0.3685 0.3440 -0.0273 0.0072  0.0973  134 ASN B CA  
5219  C C   . ASN B 134 ? 0.1510 0.3650 0.3190 -0.0192 0.0110  0.0877  134 ASN B C   
5220  O O   . ASN B 134 ? 0.3139 0.5116 0.4691 -0.0185 0.0086  0.0819  134 ASN B O   
5221  C CB  . ASN B 134 ? 0.1511 0.3595 0.3483 -0.0287 0.0005  0.0893  134 ASN B CB  
5222  C CG  . ASN B 134 ? 0.1538 0.3466 0.3627 -0.0371 -0.0079 0.0885  134 ASN B CG  
5223  O OD1 . ASN B 134 ? 0.1850 0.3604 0.3868 -0.0389 -0.0110 0.0843  134 ASN B OD1 
5224  N ND2 . ASN B 134 ? 0.1550 0.3549 0.3830 -0.0421 -0.0117 0.0914  134 ASN B ND2 
5225  N N   . LEU B 135 ? 0.1947 0.4263 0.3594 -0.0130 0.0172  0.0850  135 LEU B N   
5226  C CA  . LEU B 135 ? 0.2154 0.4478 0.3616 -0.0056 0.0215  0.0747  135 LEU B CA  
5227  C C   . LEU B 135 ? 0.1891 0.4284 0.3253 -0.0054 0.0255  0.0801  135 LEU B C   
5228  O O   . LEU B 135 ? 0.1827 0.4093 0.3044 -0.0034 0.0240  0.0728  135 LEU B O   
5229  C CB  . LEU B 135 ? 0.1669 0.4189 0.3159 0.0008  0.0279  0.0699  135 LEU B CB  
5230  C CG  . LEU B 135 ? 0.1649 0.4073 0.3162 0.0049  0.0248  0.0592  135 LEU B CG  
5231  C CD1 . LEU B 135 ? 0.1473 0.4112 0.3064 0.0113  0.0320  0.0557  135 LEU B CD1 
5232  C CD2 . LEU B 135 ? 0.1450 0.3670 0.2803 0.0082  0.0222  0.0474  135 LEU B CD2 
5233  N N   . LEU B 136 ? 0.1564 0.4176 0.3011 -0.0074 0.0305  0.0939  136 LEU B N   
5234  C CA  . LEU B 136 ? 0.1942 0.4684 0.3292 -0.0064 0.0348  0.1009  136 LEU B CA  
5235  C C   . LEU B 136 ? 0.2537 0.5078 0.3868 -0.0104 0.0292  0.1055  136 LEU B C   
5236  O O   . LEU B 136 ? 0.3953 0.6524 0.5154 -0.0080 0.0306  0.1054  136 LEU B O   
5237  C CB  . LEU B 136 ? 0.1790 0.4826 0.3253 -0.0084 0.0413  0.1177  136 LEU B CB  
5238  C CG  . LEU B 136 ? 0.1795 0.5085 0.3277 -0.0037 0.0487  0.1134  136 LEU B CG  
5239  C CD1 . LEU B 136 ? 0.2020 0.5568 0.3667 -0.0077 0.0539  0.1323  136 LEU B CD1 
5240  C CD2 . LEU B 136 ? 0.1696 0.5141 0.2985 0.0038  0.0547  0.1013  136 LEU B CD2 
5241  N N   . ALA B 137 ? 0.2711 0.5058 0.4180 -0.0165 0.0227  0.1086  137 ALA B N   
5242  C CA  . ALA B 137 ? 0.2071 0.4224 0.3556 -0.0202 0.0176  0.1117  137 ALA B CA  
5243  C C   . ALA B 137 ? 0.2686 0.4668 0.3978 -0.0161 0.0150  0.0969  137 ALA B C   
5244  O O   . ALA B 137 ? 0.3882 0.5746 0.5155 -0.0174 0.0124  0.0989  137 ALA B O   
5245  C CB  . ALA B 137 ? 0.2191 0.4174 0.3871 -0.0274 0.0112  0.1134  137 ALA B CB  
5246  N N   . TRP B 138 ? 0.2589 0.4556 0.3761 -0.0112 0.0159  0.0826  138 TRP B N   
5247  C CA  . TRP B 138 ? 0.2293 0.4114 0.3297 -0.0074 0.0141  0.0688  138 TRP B CA  
5248  C C   . TRP B 138 ? 0.1930 0.3918 0.2791 -0.0012 0.0201  0.0637  138 TRP B C   
5249  O O   . TRP B 138 ? 0.2054 0.3972 0.2806 0.0030  0.0203  0.0498  138 TRP B O   
5250  C CB  . TRP B 138 ? 0.2522 0.4190 0.3513 -0.0067 0.0102  0.0568  138 TRP B CB  
5251  C CG  . TRP B 138 ? 0.2751 0.4263 0.3854 -0.0129 0.0036  0.0587  138 TRP B CG  
5252  C CD1 . TRP B 138 ? 0.1901 0.3466 0.3174 -0.0175 0.0017  0.0659  138 TRP B CD1 
5253  C CD2 . TRP B 138 ? 0.2571 0.3867 0.3632 -0.0154 -0.0020 0.0519  138 TRP B CD2 
5254  N NE1 . TRP B 138 ? 0.1912 0.3307 0.3250 -0.0229 -0.0051 0.0628  138 TRP B NE1 
5255  C CE2 . TRP B 138 ? 0.2859 0.4091 0.4064 -0.0215 -0.0073 0.0541  138 TRP B CE2 
5256  C CE3 . TRP B 138 ? 0.1526 0.2689 0.2448 -0.0131 -0.0029 0.0436  138 TRP B CE3 
5257  C CZ2 . TRP B 138 ? 0.3104 0.4153 0.4308 -0.0252 -0.0131 0.0471  138 TRP B CZ2 
5258  C CZ3 . TRP B 138 ? 0.2843 0.3824 0.3766 -0.0166 -0.0083 0.0380  138 TRP B CZ3 
5259  C CH2 . TRP B 138 ? 0.3165 0.4095 0.4223 -0.0225 -0.0132 0.0392  138 TRP B CH2 
5260  N N   . CYS B 139 ? 0.2645 0.4870 0.3517 -0.0008 0.0250  0.0746  139 CYS B N   
5261  C CA  . CYS B 139 ? 0.3820 0.6253 0.4557 0.0047  0.0307  0.0688  139 CYS B CA  
5262  C C   . CYS B 139 ? 0.3734 0.6111 0.4347 0.0057  0.0287  0.0662  139 CYS B C   
5263  O O   . CYS B 139 ? 0.3575 0.5853 0.4232 0.0021  0.0249  0.0763  139 CYS B O   
5264  C CB  . CYS B 139 ? 0.3789 0.6543 0.4572 0.0047  0.0371  0.0821  139 CYS B CB  
5265  S SG  . CYS B 139 ? 0.4154 0.7225 0.4786 0.0118  0.0452  0.0707  139 CYS B SG  
5266  N N   . GLY B 140 ? 0.3036 0.5478 0.3512 0.0107  0.0313  0.0518  140 GLY B N   
5267  C CA  . GLY B 140 ? 0.3587 0.5983 0.3947 0.0120  0.0291  0.0467  140 GLY B CA  
5268  C C   . GLY B 140 ? 0.3508 0.6202 0.3790 0.0136  0.0326  0.0542  140 GLY B C   
5269  O O   . GLY B 140 ? 0.4038 0.6991 0.4349 0.0137  0.0372  0.0641  140 GLY B O   
5270  N N   . ARG B 141 ? 0.3019 0.5691 0.3202 0.0147  0.0301  0.0496  141 ARG B N   
5271  C CA  . ARG B 141 ? 0.2478 0.5449 0.2570 0.0164  0.0322  0.0560  141 ARG B CA  
5272  C C   . ARG B 141 ? 0.3568 0.6830 0.3570 0.0206  0.0386  0.0439  141 ARG B C   
5273  O O   . ARG B 141 ? 0.3803 0.7397 0.3766 0.0213  0.0426  0.0537  141 ARG B O   
5274  C CB  . ARG B 141 ? 0.1837 0.4715 0.1849 0.0171  0.0277  0.0507  141 ARG B CB  
5275  C CG  . ARG B 141 ? 0.1867 0.5062 0.1782 0.0188  0.0285  0.0576  141 ARG B CG  
5276  C CD  . ARG B 141 ? 0.1914 0.4995 0.1782 0.0191  0.0232  0.0541  141 ARG B CD  
5277  N NE  . ARG B 141 ? 0.2977 0.6385 0.2732 0.0213  0.0234  0.0563  141 ARG B NE  
5278  C CZ  . ARG B 141 ? 0.2859 0.6437 0.2487 0.0242  0.0251  0.0371  141 ARG B CZ  
5279  N NH1 . ARG B 141 ? 0.2486 0.5926 0.2102 0.0255  0.0272  0.0151  141 ARG B NH1 
5280  N NH2 . ARG B 141 ? 0.3269 0.7134 0.2818 0.0257  0.0233  0.0396  141 ARG B NH2 
5281  N N   . THR B 142 ? 0.3677 0.6832 0.3657 0.0234  0.0399  0.0227  142 THR B N   
5282  C CA  . THR B 142 ? 0.2530 0.5945 0.2448 0.0278  0.0461  0.0075  142 THR B CA  
5283  C C   . THR B 142 ? 0.3353 0.6949 0.3344 0.0280  0.0513  0.0154  142 THR B C   
5284  O O   . THR B 142 ? 0.3653 0.7471 0.3587 0.0292  0.0523  0.0153  142 THR B O   
5285  C CB  . THR B 142 ? 0.3012 0.6226 0.2944 0.0306  0.0460  -0.0158 142 THR B CB  
5286  O OG1 . THR B 142 ? 0.3312 0.6309 0.3198 0.0293  0.0404  -0.0209 142 THR B OG1 
5287  C CG2 . THR B 142 ? 0.2294 0.5667 0.2182 0.0339  0.0484  -0.0337 142 THR B CG2 
5288  N N   . LEU B 143 ? 0.3864 0.7283 0.3988 0.0261  0.0510  0.0221  143 LEU B N   
5289  C CA  . LEU B 143 ? 0.3753 0.7348 0.3970 0.0267  0.0566  0.0273  143 LEU B CA  
5290  C C   . LEU B 143 ? 0.3516 0.7269 0.3780 0.0226  0.0570  0.0519  143 LEU B C   
5291  O O   . LEU B 143 ? 0.4040 0.7938 0.4353 0.0229  0.0602  0.0566  143 LEU B O   
5292  C CB  . LEU B 143 ? 0.2454 0.5781 0.2805 0.0262  0.0546  0.0230  143 LEU B CB  
5293  C CG  . LEU B 143 ? 0.1764 0.4999 0.2119 0.0313  0.0563  0.0001  143 LEU B CG  
5294  C CD1 . LEU B 143 ? 0.2605 0.5537 0.3079 0.0302  0.0519  -0.0006 143 LEU B CD1 
5295  C CD2 . LEU B 143 ? 0.1851 0.5345 0.2217 0.0357  0.0634  -0.0093 143 LEU B CD2 
5296  N N   . ARG B 144 ? 0.2698 0.6388 0.2964 0.0188  0.0528  0.0676  144 ARG B N   
5297  C CA  . ARG B 144 ? 0.3006 0.6854 0.3342 0.0152  0.0532  0.0922  144 ARG B CA  
5298  C C   . ARG B 144 ? 0.3929 0.8061 0.4147 0.0180  0.0541  0.0935  144 ARG B C   
5299  O O   . ARG B 144 ? 0.4472 0.8755 0.4755 0.0160  0.0545  0.1124  144 ARG B O   
5300  C CB  . ARG B 144 ? 0.3282 0.6966 0.3663 0.0112  0.0474  0.1073  144 ARG B CB  
5301  C CG  . ARG B 144 ? 0.3769 0.7139 0.4335 0.0062  0.0426  0.1149  144 ARG B CG  
5302  C CD  . ARG B 144 ? 0.4716 0.7859 0.5325 0.0033  0.0359  0.1228  144 ARG B CD  
5303  N NE  . ARG B 144 ? 0.4114 0.7123 0.4939 -0.0025 0.0333  0.1399  144 ARG B NE  
5304  C CZ  . ARG B 144 ? 0.3532 0.6233 0.4467 -0.0058 0.0284  0.1340  144 ARG B CZ  
5305  N NH1 . ARG B 144 ? 0.3006 0.5500 0.3849 -0.0038 0.0257  0.1137  144 ARG B NH1 
5306  N NH2 . ARG B 144 ? 0.4573 0.7184 0.5723 -0.0115 0.0262  0.1489  144 ARG B NH2 
5307  N N   . LYS B 145 ? 0.5039 0.9254 0.5110 0.0223  0.0540  0.0737  145 LYS B N   
5308  C CA  . LYS B 145 ? 0.3655 0.8163 0.3629 0.0250  0.0547  0.0705  145 LYS B CA  
5309  C C   . LYS B 145 ? 0.4807 0.9407 0.4803 0.0274  0.0600  0.0586  145 LYS B C   
5310  O O   . LYS B 145 ? 0.5630 1.0478 0.5624 0.0276  0.0623  0.0669  145 LYS B O   
5311  C CB  . LYS B 145 ? 0.4207 0.8761 0.4043 0.0276  0.0514  0.0536  145 LYS B CB  
5312  C CG  . LYS B 145 ? 0.4936 0.9306 0.4759 0.0259  0.0469  0.0577  145 LYS B CG  
5313  C CD  . LYS B 145 ? 0.5306 0.9655 0.5021 0.0284  0.0439  0.0359  145 LYS B CD  
5314  C CE  . LYS B 145 ? 0.5765 0.9987 0.5460 0.0269  0.0394  0.0428  145 LYS B CE  
5315  N NZ  . LYS B 145 ? 0.5832 0.9972 0.5450 0.0287  0.0366  0.0203  145 LYS B NZ  
5316  N N   . ASP B 146 ? 0.5740 1.0154 0.5772 0.0294  0.0622  0.0398  146 ASP B N   
5317  C CA  . ASP B 146 ? 0.5528 1.0012 0.5610 0.0321  0.0674  0.0282  146 ASP B CA  
5318  C C   . ASP B 146 ? 0.4118 0.8614 0.4343 0.0296  0.0704  0.0455  146 ASP B C   
5319  O O   . ASP B 146 ? 0.4729 0.9425 0.4975 0.0304  0.0744  0.0484  146 ASP B O   
5320  C CB  . ASP B 146 ? 0.5812 1.0082 0.5929 0.0354  0.0683  0.0048  146 ASP B CB  
5321  C CG  . ASP B 146 ? 0.7789 1.2064 0.7793 0.0377  0.0658  -0.0150 146 ASP B CG  
5322  O OD1 . ASP B 146 ? 0.7056 1.1561 0.6954 0.0376  0.0643  -0.0137 146 ASP B OD1 
5323  O OD2 . ASP B 146 ? 0.7929 1.1986 0.7966 0.0395  0.0650  -0.0313 146 ASP B OD2 
5324  N N   . LEU B 147 ? 0.4173 0.8463 0.4510 0.0261  0.0684  0.0567  147 LEU B N   
5325  C CA  . LEU B 147 ? 0.2935 0.7205 0.3440 0.0227  0.0699  0.0723  147 LEU B CA  
5326  C C   . LEU B 147 ? 0.4097 0.8465 0.4644 0.0178  0.0680  0.0982  147 LEU B C   
5327  O O   . LEU B 147 ? 0.3745 0.8011 0.4457 0.0130  0.0669  0.1133  147 LEU B O   
5328  C CB  . LEU B 147 ? 0.1977 0.5986 0.2617 0.0209  0.0677  0.0699  147 LEU B CB  
5329  C CG  . LEU B 147 ? 0.3019 0.6905 0.3673 0.0259  0.0690  0.0472  147 LEU B CG  
5330  C CD1 . LEU B 147 ? 0.2016 0.5642 0.2792 0.0234  0.0642  0.0486  147 LEU B CD1 
5331  C CD2 . LEU B 147 ? 0.2046 0.6050 0.2768 0.0294  0.0741  0.0394  147 LEU B CD2 
5332  N N   . LYS B 148 ? 0.3863 0.8427 0.4285 0.0187  0.0670  0.1040  148 LYS B N   
5333  C CA  . LYS B 148 ? 0.3940 0.8604 0.4425 0.0149  0.0648  0.1300  148 LYS B CA  
5334  C C   . LYS B 148 ? 0.4319 0.9104 0.4934 0.0128  0.0683  0.1433  148 LYS B C   
5335  O O   . LYS B 148 ? 0.4603 0.9336 0.5372 0.0080  0.0664  0.1645  148 LYS B O   
5336  C CB  . LYS B 148 ? 0.3638 0.8535 0.3974 0.0173  0.0627  0.1326  148 LYS B CB  
5337  C CG  . LYS B 148 ? 0.4022 0.9060 0.4441 0.0144  0.0602  0.1604  148 LYS B CG  
5338  C CD  . LYS B 148 ? 0.3311 0.8655 0.3596 0.0175  0.0585  0.1620  148 LYS B CD  
5339  C CE  . LYS B 148 ? 0.3273 0.8704 0.3662 0.0152  0.0544  0.1898  148 LYS B CE  
5340  N NZ  . LYS B 148 ? 0.3950 0.9777 0.4283 0.0175  0.0547  0.1985  148 LYS B NZ  
5341  N N   . ASP B 149 ? 0.4658 0.9599 0.5233 0.0163  0.0735  0.1305  149 ASP B N   
5342  C CA  . ASP B 149 ? 0.4094 0.9176 0.4787 0.0147  0.0775  0.1421  149 ASP B CA  
5343  C C   . ASP B 149 ? 0.4147 0.9005 0.5050 0.0101  0.0768  0.1493  149 ASP B C   
5344  O O   . ASP B 149 ? 0.4049 0.8926 0.5101 0.0055  0.0762  0.1695  149 ASP B O   
5345  C CB  . ASP B 149 ? 0.2726 0.7999 0.3344 0.0197  0.0836  0.1240  149 ASP B CB  
5346  C CG  . ASP B 149 ? 0.5420 1.1042 0.5947 0.0212  0.0858  0.1315  149 ASP B CG  
5347  O OD1 . ASP B 149 ? 0.5059 1.0780 0.5566 0.0191  0.0820  0.1500  149 ASP B OD1 
5348  O OD2 . ASP B 149 ? 0.6907 1.2714 0.7396 0.0246  0.0913  0.1191  149 ASP B OD2 
5349  N N   . LEU B 150 ? 0.3128 0.7779 0.4062 0.0113  0.0764  0.1328  150 LEU B N   
5350  C CA  . LEU B 150 ? 0.2379 0.6837 0.3520 0.0069  0.0746  0.1380  150 LEU B CA  
5351  C C   . LEU B 150 ? 0.2898 0.7167 0.4139 0.0006  0.0684  0.1540  150 LEU B C   
5352  O O   . LEU B 150 ? 0.3537 0.7714 0.4976 -0.0050 0.0663  0.1664  150 LEU B O   
5353  C CB  . LEU B 150 ? 0.2693 0.7000 0.3850 0.0103  0.0747  0.1170  150 LEU B CB  
5354  C CG  . LEU B 150 ? 0.2173 0.6614 0.3303 0.0165  0.0807  0.1000  150 LEU B CG  
5355  C CD1 . LEU B 150 ? 0.2056 0.6327 0.3191 0.0209  0.0797  0.0795  150 LEU B CD1 
5356  C CD2 . LEU B 150 ? 0.2214 0.6749 0.3517 0.0145  0.0837  0.1088  150 LEU B CD2 
5357  N N   . LEU B 151 ? 0.3037 0.7240 0.4161 0.0013  0.0653  0.1531  151 LEU B N   
5358  C CA  . LEU B 151 ? 0.2814 0.6827 0.4049 -0.0044 0.0597  0.1670  151 LEU B CA  
5359  C C   . LEU B 151 ? 0.3166 0.7258 0.4532 -0.0086 0.0587  0.1912  151 LEU B C   
5360  O O   . LEU B 151 ? 0.3806 0.7717 0.5368 -0.0146 0.0546  0.2029  151 LEU B O   
5361  C CB  . LEU B 151 ? 0.3217 0.7177 0.4296 -0.0021 0.0572  0.1613  151 LEU B CB  
5362  C CG  . LEU B 151 ? 0.4044 0.7827 0.5070 -0.0001 0.0562  0.1411  151 LEU B CG  
5363  C CD1 . LEU B 151 ? 0.4410 0.8169 0.5276 0.0023  0.0542  0.1357  151 LEU B CD1 
5364  C CD2 . LEU B 151 ? 0.3978 0.7494 0.5197 -0.0056 0.0512  0.1431  151 LEU B CD2 
5365  N N   . ASN B 152 ? 0.4036 0.8398 0.5313 -0.0056 0.0619  0.1984  152 ASN B N   
5366  C CA  . ASN B 152 ? 0.4293 0.8767 0.5706 -0.0087 0.0613  0.2223  152 ASN B CA  
5367  C C   . ASN B 152 ? 0.3773 0.8347 0.5317 -0.0106 0.0651  0.2273  152 ASN B C   
5368  O O   . ASN B 152 ? 0.4013 0.8663 0.5705 -0.0138 0.0647  0.2475  152 ASN B O   
5369  C CB  . ASN B 152 ? 0.2864 0.7610 0.4127 -0.0046 0.0617  0.2300  152 ASN B CB  
5370  C CG  . ASN B 152 ? 0.4570 0.9223 0.5764 -0.0038 0.0568  0.2314  152 ASN B CG  
5371  O OD1 . ASN B 152 ? 0.5593 0.9990 0.6923 -0.0078 0.0526  0.2373  152 ASN B OD1 
5372  N ND2 . ASN B 152 ? 0.5123 0.9990 0.6117 0.0012  0.0571  0.2252  152 ASN B ND2 
5373  N N   . LYS B 153 ? 0.3242 0.7821 0.4752 -0.0085 0.0689  0.2097  153 LYS B N   
5374  C CA  . LYS B 153 ? 0.2848 0.7489 0.4515 -0.0108 0.0720  0.2139  153 LYS B CA  
5375  C C   . LYS B 153 ? 0.3769 0.8170 0.5689 -0.0182 0.0670  0.2238  153 LYS B C   
5376  O O   . LYS B 153 ? 0.4405 0.8859 0.6501 -0.0220 0.0679  0.2365  153 LYS B O   
5377  C CB  . LYS B 153 ? 0.2671 0.7354 0.4270 -0.0062 0.0765  0.1920  153 LYS B CB  
5378  C CG  . LYS B 153 ? 0.2558 0.7382 0.4286 -0.0069 0.0812  0.1950  153 LYS B CG  
5379  C CD  . LYS B 153 ? 0.3206 0.8001 0.4932 -0.0027 0.0841  0.1736  153 LYS B CD  
5380  C CE  . LYS B 153 ? 0.3394 0.8410 0.5186 -0.0009 0.0908  0.1733  153 LYS B CE  
5381  N NZ  . LYS B 153 ? 0.4256 0.9379 0.5924 0.0068  0.0962  0.1512  153 LYS B NZ  
5382  N N   . GLY B 154 ? 0.2382 0.6524 0.4331 -0.0205 0.0616  0.2173  154 GLY B N   
5383  C CA  . GLY B 154 ? 0.2728 0.6631 0.4913 -0.0279 0.0556  0.2257  154 GLY B CA  
5384  C C   . GLY B 154 ? 0.2912 0.6722 0.5264 -0.0315 0.0541  0.2184  154 GLY B C   
5385  O O   . GLY B 154 ? 0.3164 0.6747 0.5607 -0.0352 0.0484  0.2104  154 GLY B O   
5386  N N   . ARG B 155 ? 0.2733 0.6727 0.5129 -0.0305 0.0589  0.2207  155 ARG B N   
5387  C CA  . ARG B 155 ? 0.2734 0.6672 0.5309 -0.0340 0.0573  0.2155  155 ARG B CA  
5388  C C   . ARG B 155 ? 0.3408 0.7575 0.5905 -0.0282 0.0644  0.2070  155 ARG B C   
5389  O O   . ARG B 155 ? 0.2705 0.7048 0.5006 -0.0218 0.0701  0.2025  155 ARG B O   
5390  C CB  . ARG B 155 ? 0.2381 0.6262 0.5209 -0.0416 0.0542  0.2322  155 ARG B CB  
5391  C CG  . ARG B 155 ? 0.2555 0.6628 0.5390 -0.0412 0.0586  0.2519  155 ARG B CG  
5392  C CD  . ARG B 155 ? 0.3960 0.7954 0.7078 -0.0487 0.0552  0.2681  155 ARG B CD  
5393  N NE  . ARG B 155 ? 0.5482 0.9183 0.8739 -0.0540 0.0472  0.2676  155 ARG B NE  
5394  C CZ  . ARG B 155 ? 0.4905 0.8515 0.8170 -0.0543 0.0446  0.2775  155 ARG B CZ  
5395  N NH1 . ARG B 155 ? 0.3825 0.7623 0.6961 -0.0495 0.0485  0.2896  155 ARG B NH1 
5396  N NH2 . ARG B 155 ? 0.4358 0.7692 0.7771 -0.0592 0.0375  0.2743  155 ARG B NH2 
5397  N N   . ASN B 156 ? 0.3339 0.7504 0.6002 -0.0305 0.0638  0.2039  156 ASN B N   
5398  C CA  . ASN B 156 ? 0.2820 0.7191 0.5467 -0.0254 0.0704  0.1964  156 ASN B CA  
5399  C C   . ASN B 156 ? 0.3632 0.8042 0.6081 -0.0169 0.0737  0.1774  156 ASN B C   
5400  O O   . ASN B 156 ? 0.3844 0.8449 0.6140 -0.0110 0.0806  0.1734  156 ASN B O   
5401  C CB  . ASN B 156 ? 0.2487 0.7109 0.5132 -0.0251 0.0772  0.2105  156 ASN B CB  
5402  C CG  . ASN B 156 ? 0.3343 0.7953 0.6235 -0.0327 0.0750  0.2269  156 ASN B CG  
5403  O OD1 . ASN B 156 ? 0.3880 0.8273 0.6928 -0.0392 0.0677  0.2303  156 ASN B OD1 
5404  N ND2 . ASN B 156 ? 0.4658 0.9506 0.7594 -0.0321 0.0815  0.2361  156 ASN B ND2 
5405  N N   . TYR B 157 ? 0.3262 0.7485 0.5725 -0.0162 0.0682  0.1650  157 TYR B N   
5406  C CA  . TYR B 157 ? 0.2475 0.6699 0.4789 -0.0082 0.0704  0.1466  157 TYR B CA  
5407  C C   . TYR B 157 ? 0.1996 0.6290 0.4414 -0.0037 0.0726  0.1355  157 TYR B C   
5408  O O   . TYR B 157 ? 0.2349 0.6653 0.4956 -0.0075 0.0705  0.1411  157 TYR B O   
5409  C CB  . TYR B 157 ? 0.2157 0.6150 0.4425 -0.0092 0.0633  0.1401  157 TYR B CB  
5410  C CG  . TYR B 157 ? 0.1917 0.5870 0.4042 -0.0108 0.0629  0.1469  157 TYR B CG  
5411  C CD1 . TYR B 157 ? 0.1974 0.6058 0.3888 -0.0047 0.0685  0.1411  157 TYR B CD1 
5412  C CD2 . TYR B 157 ? 0.1903 0.5693 0.4117 -0.0183 0.0566  0.1587  157 TYR B CD2 
5413  C CE1 . TYR B 157 ? 0.2635 0.6700 0.4423 -0.0059 0.0674  0.1480  157 TYR B CE1 
5414  C CE2 . TYR B 157 ? 0.2463 0.6220 0.4569 -0.0192 0.0562  0.1659  157 TYR B CE2 
5415  C CZ  . TYR B 157 ? 0.2892 0.6794 0.4780 -0.0129 0.0614  0.1612  157 TYR B CZ  
5416  O OH  . TYR B 157 ? 0.4037 0.7922 0.5820 -0.0135 0.0602  0.1688  157 TYR B OH  
5417  N N   . THR B 158 ? 0.1978 0.6318 0.4283 0.0047  0.0768  0.1192  158 THR B N   
5418  C CA  . THR B 158 ? 0.1987 0.6418 0.4384 0.0109  0.0807  0.1077  158 THR B CA  
5419  C C   . THR B 158 ? 0.2280 0.6559 0.4669 0.0165  0.0770  0.0922  158 THR B C   
5420  O O   . THR B 158 ? 0.2282 0.6448 0.4527 0.0179  0.0750  0.0866  158 THR B O   
5421  C CB  . THR B 158 ? 0.2128 0.6793 0.4421 0.0164  0.0909  0.1020  158 THR B CB  
5422  O OG1 . THR B 158 ? 0.2904 0.7731 0.5241 0.0113  0.0940  0.1182  158 THR B OG1 
5423  C CG2 . THR B 158 ? 0.2765 0.7508 0.5158 0.0239  0.0957  0.0870  158 THR B CG2 
5424  N N   . GLN B 159 ? 0.1839 0.6116 0.4395 0.0199  0.0757  0.0863  159 GLN B N   
5425  C CA  . GLN B 159 ? 0.1754 0.5903 0.4326 0.0265  0.0726  0.0726  159 GLN B CA  
5426  C C   . GLN B 159 ? 0.1923 0.6103 0.4342 0.0344  0.0796  0.0570  159 GLN B C   
5427  O O   . GLN B 159 ? 0.2129 0.6165 0.4490 0.0383  0.0767  0.0474  159 GLN B O   
5428  C CB  . GLN B 159 ? 0.1747 0.5931 0.4537 0.0300  0.0712  0.0699  159 GLN B CB  
5429  C CG  . GLN B 159 ? 0.1674 0.5723 0.4517 0.0370  0.0669  0.0588  159 GLN B CG  
5430  C CD  . GLN B 159 ? 0.1568 0.5432 0.4429 0.0320  0.0552  0.0655  159 GLN B CD  
5431  O OE1 . GLN B 159 ? 0.2037 0.5877 0.4932 0.0231  0.0495  0.0772  159 GLN B OE1 
5432  N NE2 . GLN B 159 ? 0.1510 0.5238 0.4355 0.0375  0.0514  0.0576  159 GLN B NE2 
5433  N N   . GLU B 160 ? 0.1929 0.6295 0.4281 0.0365  0.0884  0.0540  160 GLU B N   
5434  C CA  . GLU B 160 ? 0.2002 0.6403 0.4192 0.0426  0.0944  0.0385  160 GLU B CA  
5435  C C   . GLU B 160 ? 0.1986 0.6320 0.3957 0.0391  0.0918  0.0416  160 GLU B C   
5436  O O   . GLU B 160 ? 0.1978 0.6223 0.3831 0.0432  0.0918  0.0281  160 GLU B O   
5437  C CB  . GLU B 160 ? 0.3121 0.7759 0.5300 0.0453  0.1039  0.0346  160 GLU B CB  
5438  C CG  . GLU B 160 ? 0.4545 0.9243 0.6927 0.0520  0.1086  0.0239  160 GLU B CG  
5439  C CD  . GLU B 160 ? 0.4706 0.9380 0.7321 0.0494  0.1039  0.0347  160 GLU B CD  
5440  O OE1 . GLU B 160 ? 0.4165 0.8828 0.6788 0.0414  0.0987  0.0514  160 GLU B OE1 
5441  O OE2 . GLU B 160 ? 0.5567 1.0230 0.8371 0.0553  0.1049  0.0263  160 GLU B OE2 
5442  N N   . GLU B 161 ? 0.2128 0.6500 0.4058 0.0314  0.0894  0.0593  161 GLU B N   
5443  C CA  . GLU B 161 ? 0.1979 0.6288 0.3728 0.0281  0.0865  0.0642  161 GLU B CA  
5444  C C   . GLU B 161 ? 0.1828 0.5901 0.3591 0.0266  0.0788  0.0627  161 GLU B C   
5445  O O   . GLU B 161 ? 0.1806 0.5797 0.3418 0.0281  0.0776  0.0557  161 GLU B O   
5446  C CB  . GLU B 161 ? 0.2041 0.6445 0.3784 0.0206  0.0860  0.0850  161 GLU B CB  
5447  C CG  . GLU B 161 ? 0.3690 0.8350 0.5423 0.0216  0.0934  0.0891  161 GLU B CG  
5448  C CD  . GLU B 161 ? 0.3312 0.8053 0.5071 0.0144  0.0923  0.1118  161 GLU B CD  
5449  O OE1 . GLU B 161 ? 0.3402 0.7980 0.5249 0.0081  0.0858  0.1238  161 GLU B OE1 
5450  O OE2 . GLU B 161 ? 0.3198 0.8166 0.4902 0.0150  0.0977  0.1175  161 GLU B OE2 
5451  N N   . LYS B 162 ? 0.1735 0.5703 0.3676 0.0234  0.0730  0.0692  162 LYS B N   
5452  C CA  . LYS B 162 ? 0.1605 0.5365 0.3564 0.0219  0.0651  0.0677  162 LYS B CA  
5453  C C   . LYS B 162 ? 0.1775 0.5417 0.3671 0.0300  0.0652  0.0490  162 LYS B C   
5454  O O   . LYS B 162 ? 0.1783 0.5199 0.3535 0.0297  0.0603  0.0428  162 LYS B O   
5455  C CB  . LYS B 162 ? 0.1552 0.5212 0.3699 0.0168  0.0574  0.0763  162 LYS B CB  
5456  C CG  . LYS B 162 ? 0.1509 0.4835 0.3590 0.0137  0.0463  0.0728  162 LYS B CG  
5457  C CD  . LYS B 162 ? 0.1477 0.4713 0.3701 0.0144  0.0397  0.0705  162 LYS B CD  
5458  C CE  . LYS B 162 ? 0.2123 0.5582 0.4574 0.0126  0.0420  0.0797  162 LYS B CE  
5459  N NZ  . LYS B 162 ? 0.1463 0.4913 0.4054 0.0174  0.0386  0.0746  162 LYS B NZ  
5460  N N   . GLU B 163 ? 0.1944 0.5700 0.3949 0.0370  0.0704  0.0395  163 GLU B N   
5461  C CA  . GLU B 163 ? 0.1619 0.5272 0.3610 0.0451  0.0714  0.0220  163 GLU B CA  
5462  C C   . GLU B 163 ? 0.1941 0.5625 0.3735 0.0479  0.0766  0.0097  163 GLU B C   
5463  O O   . GLU B 163 ? 0.2286 0.5835 0.4033 0.0522  0.0756  -0.0036 163 GLU B O   
5464  C CB  . GLU B 163 ? 0.1663 0.5399 0.3843 0.0516  0.0754  0.0149  163 GLU B CB  
5465  C CG  . GLU B 163 ? 0.3210 0.6846 0.5581 0.0512  0.0678  0.0223  163 GLU B CG  
5466  C CD  . GLU B 163 ? 0.5044 0.8791 0.7629 0.0574  0.0718  0.0180  163 GLU B CD  
5467  O OE1 . GLU B 163 ? 0.5633 0.9425 0.8227 0.0642  0.0793  0.0036  163 GLU B OE1 
5468  O OE2 . GLU B 163 ? 0.5138 0.8905 0.7883 0.0549  0.0669  0.0284  163 GLU B OE2 
5469  N N   . TYR B 164 ? 0.1872 0.5718 0.3547 0.0450  0.0813  0.0142  164 TYR B N   
5470  C CA  . TYR B 164 ? 0.1875 0.5751 0.3341 0.0463  0.0842  0.0044  164 TYR B CA  
5471  C C   . TYR B 164 ? 0.1786 0.5518 0.3130 0.0428  0.0783  0.0080  164 TYR B C   
5472  O O   . TYR B 164 ? 0.1803 0.5452 0.3033 0.0457  0.0781  -0.0056 164 TYR B O   
5473  C CB  . TYR B 164 ? 0.2182 0.6290 0.3551 0.0439  0.0891  0.0117  164 TYR B CB  
5474  C CG  . TYR B 164 ? 0.2116 0.6291 0.3270 0.0451  0.0908  0.0021  164 TYR B CG  
5475  C CD1 . TYR B 164 ? 0.3246 0.7406 0.4365 0.0510  0.0938  -0.0194 164 TYR B CD1 
5476  C CD2 . TYR B 164 ? 0.2144 0.6394 0.3149 0.0403  0.0885  0.0150  164 TYR B CD2 
5477  C CE1 . TYR B 164 ? 0.3202 0.7434 0.4134 0.0515  0.0940  -0.0288 164 TYR B CE1 
5478  C CE2 . TYR B 164 ? 0.2854 0.7188 0.3671 0.0414  0.0888  0.0069  164 TYR B CE2 
5479  C CZ  . TYR B 164 ? 0.3018 0.7348 0.3795 0.0468  0.0912  -0.0156 164 TYR B CZ  
5480  O OH  . TYR B 164 ? 0.4576 0.9001 0.5177 0.0473  0.0903  -0.0244 164 TYR B OH  
5481  N N   . VAL B 165 ? 0.1701 0.5396 0.3084 0.0362  0.0735  0.0257  165 VAL B N   
5482  C CA  . VAL B 165 ? 0.1658 0.5115 0.2921 0.0319  0.0660  0.0288  165 VAL B CA  
5483  C C   . VAL B 165 ? 0.1615 0.4771 0.2882 0.0344  0.0600  0.0167  165 VAL B C   
5484  O O   . VAL B 165 ? 0.2316 0.5306 0.3453 0.0344  0.0568  0.0098  165 VAL B O   
5485  C CB  . VAL B 165 ? 0.1628 0.5018 0.2948 0.0235  0.0605  0.0486  165 VAL B CB  
5486  C CG1 . VAL B 165 ? 0.1601 0.4729 0.2806 0.0193  0.0529  0.0505  165 VAL B CG1 
5487  C CG2 . VAL B 165 ? 0.1682 0.5379 0.3023 0.0208  0.0670  0.0631  165 VAL B CG2 
5488  N N   . LEU B 166 ? 0.2154 0.5251 0.3578 0.0366  0.0584  0.0153  166 LEU B N   
5489  C CA  . LEU B 166 ? 0.2181 0.5009 0.3626 0.0387  0.0524  0.0074  166 LEU B CA  
5490  C C   . LEU B 166 ? 0.2711 0.5509 0.4105 0.0455  0.0565  -0.0106 166 LEU B C   
5491  O O   . LEU B 166 ? 0.2650 0.5221 0.3973 0.0453  0.0519  -0.0162 166 LEU B O   
5492  C CB  . LEU B 166 ? 0.2592 0.5411 0.4232 0.0402  0.0500  0.0112  166 LEU B CB  
5493  C CG  . LEU B 166 ? 0.2233 0.4936 0.3918 0.0327  0.0412  0.0250  166 LEU B CG  
5494  C CD1 . LEU B 166 ? 0.1487 0.4288 0.3380 0.0339  0.0402  0.0303  166 LEU B CD1 
5495  C CD2 . LEU B 166 ? 0.1471 0.3887 0.3060 0.0304  0.0327  0.0228  166 LEU B CD2 
5496  N N   . ASN B 167 ? 0.2353 0.5387 0.3798 0.0513  0.0654  -0.0206 167 ASN B N   
5497  C CA  . ASN B 167 ? 0.2553 0.5564 0.3985 0.0576  0.0695  -0.0401 167 ASN B CA  
5498  C C   . ASN B 167 ? 0.2557 0.5533 0.3783 0.0551  0.0686  -0.0452 167 ASN B C   
5499  O O   . ASN B 167 ? 0.2879 0.5657 0.4071 0.0562  0.0657  -0.0551 167 ASN B O   
5500  C CB  . ASN B 167 ? 0.1985 0.5220 0.3498 0.0631  0.0785  -0.0508 167 ASN B CB  
5501  C CG  . ASN B 167 ? 0.3301 0.6430 0.4791 0.0675  0.0809  -0.0710 167 ASN B CG  
5502  O OD1 . ASN B 167 ? 0.3441 0.6399 0.5075 0.0719  0.0796  -0.0788 167 ASN B OD1 
5503  N ND2 . ASN B 167 ? 0.3259 0.6493 0.4580 0.0661  0.0836  -0.0785 167 ASN B ND2 
5504  N N   . LYS B 168 ? 0.1932 0.5113 0.3034 0.0515  0.0710  -0.0373 168 LYS B N   
5505  C CA  . LYS B 168 ? 0.1755 0.4929 0.2669 0.0491  0.0695  -0.0401 168 LYS B CA  
5506  C C   . LYS B 168 ? 0.2050 0.4905 0.2903 0.0444  0.0604  -0.0335 168 LYS B C   
5507  O O   . LYS B 168 ? 0.3274 0.6032 0.4016 0.0441  0.0584  -0.0414 168 LYS B O   
5508  C CB  . LYS B 168 ? 0.1814 0.5217 0.2613 0.0452  0.0715  -0.0276 168 LYS B CB  
5509  C CG  . LYS B 168 ? 0.1950 0.5558 0.2763 0.0472  0.0772  -0.0303 168 LYS B CG  
5510  C CD  . LYS B 168 ? 0.2093 0.5855 0.2726 0.0470  0.0783  -0.0366 168 LYS B CD  
5511  C CE  . LYS B 168 ? 0.3523 0.7186 0.4127 0.0509  0.0782  -0.0596 168 LYS B CE  
5512  N NZ  . LYS B 168 ? 0.3898 0.7724 0.4335 0.0500  0.0775  -0.0661 168 LYS B NZ  
5513  N N   . TYR B 169 ? 0.1985 0.4688 0.2912 0.0405  0.0549  -0.0201 169 TYR B N   
5514  C CA  . TYR B 169 ? 0.2196 0.4609 0.3073 0.0363  0.0466  -0.0157 169 TYR B CA  
5515  C C   . TYR B 169 ? 0.2735 0.4943 0.3642 0.0400  0.0449  -0.0286 169 TYR B C   
5516  O O   . TYR B 169 ? 0.3284 0.5298 0.4106 0.0378  0.0403  -0.0303 169 TYR B O   
5517  C CB  . TYR B 169 ? 0.1564 0.3894 0.2526 0.0313  0.0412  -0.0007 169 TYR B CB  
5518  C CG  . TYR B 169 ? 0.1530 0.3936 0.2453 0.0251  0.0399  0.0139  169 TYR B CG  
5519  C CD1 . TYR B 169 ? 0.1573 0.4197 0.2417 0.0254  0.0450  0.0165  169 TYR B CD1 
5520  C CD2 . TYR B 169 ? 0.1497 0.3766 0.2476 0.0190  0.0333  0.0252  169 TYR B CD2 
5521  C CE1 . TYR B 169 ? 0.1783 0.4475 0.2620 0.0200  0.0438  0.0323  169 TYR B CE1 
5522  C CE2 . TYR B 169 ? 0.1505 0.3828 0.2490 0.0134  0.0322  0.0387  169 TYR B CE2 
5523  C CZ  . TYR B 169 ? 0.1940 0.4468 0.2862 0.0140  0.0376  0.0433  169 TYR B CZ  
5524  O OH  . TYR B 169 ? 0.2793 0.5375 0.3750 0.0086  0.0365  0.0590  169 TYR B OH  
5525  N N   . PHE B 170 ? 0.2628 0.4881 0.3675 0.0457  0.0487  -0.0370 170 PHE B N   
5526  C CA  . PHE B 170 ? 0.3650 0.5716 0.4764 0.0495  0.0476  -0.0480 170 PHE B CA  
5527  C C   . PHE B 170 ? 0.3393 0.5511 0.4463 0.0531  0.0525  -0.0656 170 PHE B C   
5528  O O   . PHE B 170 ? 0.3058 0.4989 0.4138 0.0539  0.0505  -0.0734 170 PHE B O   
5529  C CB  . PHE B 170 ? 0.3217 0.5290 0.4539 0.0545  0.0490  -0.0485 170 PHE B CB  
5530  C CG  . PHE B 170 ? 0.2823 0.4762 0.4197 0.0511  0.0416  -0.0340 170 PHE B CG  
5531  C CD1 . PHE B 170 ? 0.3403 0.5107 0.4774 0.0501  0.0356  -0.0322 170 PHE B CD1 
5532  C CD2 . PHE B 170 ? 0.2592 0.4660 0.4021 0.0486  0.0407  -0.0224 170 PHE B CD2 
5533  C CE1 . PHE B 170 ? 0.3609 0.5226 0.5013 0.0469  0.0285  -0.0198 170 PHE B CE1 
5534  C CE2 . PHE B 170 ? 0.4139 0.6106 0.5620 0.0451  0.0333  -0.0108 170 PHE B CE2 
5535  C CZ  . PHE B 170 ? 0.3520 0.5269 0.4979 0.0443  0.0270  -0.0099 170 PHE B CZ  
5536  N N   . GLU B 171 ? 0.3092 0.5476 0.4117 0.0549  0.0589  -0.0720 171 GLU B N   
5537  C CA  . GLU B 171 ? 0.3188 0.5654 0.4145 0.0571  0.0627  -0.0894 171 GLU B CA  
5538  C C   . GLU B 171 ? 0.2915 0.5239 0.3710 0.0523  0.0572  -0.0868 171 GLU B C   
5539  O O   . GLU B 171 ? 0.2803 0.5018 0.3595 0.0533  0.0567  -0.0998 171 GLU B O   
5540  C CB  . GLU B 171 ? 0.3516 0.6240 0.4383 0.0567  0.0671  -0.0909 171 GLU B CB  
5541  C CG  . GLU B 171 ? 0.5909 0.8644 0.6760 0.0585  0.0691  -0.1089 171 GLU B CG  
5542  C CD  . GLU B 171 ? 0.7401 1.0373 0.8080 0.0560  0.0699  -0.1094 171 GLU B CD  
5543  O OE1 . GLU B 171 ? 0.7861 1.0911 0.8402 0.0523  0.0673  -0.0974 171 GLU B OE1 
5544  O OE2 . GLU B 171 ? 0.7686 1.0779 0.8380 0.0579  0.0730  -0.1215 171 GLU B OE2 
5545  N N   . ILE B 172 ? 0.2744 0.5065 0.3426 0.0469  0.0530  -0.0700 172 ILE B N   
5546  C CA  . ILE B 172 ? 0.2479 0.4665 0.3026 0.0425  0.0478  -0.0662 172 ILE B CA  
5547  C C   . ILE B 172 ? 0.2738 0.4615 0.3330 0.0415  0.0427  -0.0673 172 ILE B C   
5548  O O   . ILE B 172 ? 0.1895 0.3659 0.2429 0.0406  0.0409  -0.0745 172 ILE B O   
5549  C CB  . ILE B 172 ? 0.3428 0.5670 0.3896 0.0373  0.0447  -0.0473 172 ILE B CB  
5550  C CG1 . ILE B 172 ? 0.2854 0.5426 0.3254 0.0380  0.0499  -0.0452 172 ILE B CG1 
5551  C CG2 . ILE B 172 ? 0.3426 0.5474 0.3800 0.0329  0.0385  -0.0421 172 ILE B CG2 
5552  C CD1 . ILE B 172 ? 0.4475 0.7134 0.4729 0.0367  0.0488  -0.0475 172 ILE B CD1 
5553  N N   . ILE B 173 ? 0.2721 0.4477 0.3418 0.0414  0.0404  -0.0595 173 ILE B N   
5554  C CA  . ILE B 173 ? 0.2944 0.4441 0.3685 0.0407  0.0358  -0.0590 173 ILE B CA  
5555  C C   . ILE B 173 ? 0.3235 0.4670 0.4069 0.0452  0.0391  -0.0746 173 ILE B C   
5556  O O   . ILE B 173 ? 0.2926 0.4188 0.3738 0.0438  0.0366  -0.0780 173 ILE B O   
5557  C CB  . ILE B 173 ? 0.1918 0.3352 0.2763 0.0403  0.0327  -0.0477 173 ILE B CB  
5558  C CG1 . ILE B 173 ? 0.1510 0.2931 0.2273 0.0343  0.0277  -0.0335 173 ILE B CG1 
5559  C CG2 . ILE B 173 ? 0.1565 0.2790 0.2489 0.0416  0.0296  -0.0486 173 ILE B CG2 
5560  C CD1 . ILE B 173 ? 0.1490 0.2858 0.2347 0.0330  0.0234  -0.0236 173 ILE B CD1 
5561  N N   . LYS B 174 ? 0.3159 0.4737 0.4115 0.0506  0.0449  -0.0848 174 LYS B N   
5562  C CA  . LYS B 174 ? 0.2857 0.4372 0.3955 0.0552  0.0484  -0.1008 174 LYS B CA  
5563  C C   . LYS B 174 ? 0.3188 0.4713 0.4199 0.0539  0.0494  -0.1145 174 LYS B C   
5564  O O   . LYS B 174 ? 0.3394 0.4796 0.4515 0.0554  0.0503  -0.1257 174 LYS B O   
5565  C CB  . LYS B 174 ? 0.2678 0.4375 0.3935 0.0614  0.0551  -0.1108 174 LYS B CB  
5566  C CG  . LYS B 174 ? 0.2376 0.4033 0.3796 0.0641  0.0543  -0.1002 174 LYS B CG  
5567  C CD  . LYS B 174 ? 0.3085 0.4836 0.4726 0.0713  0.0609  -0.1133 174 LYS B CD  
5568  C CE  . LYS B 174 ? 0.5156 0.7150 0.6796 0.0728  0.0648  -0.1095 174 LYS B CE  
5569  N NZ  . LYS B 174 ? 0.4601 0.6580 0.6338 0.0729  0.0615  -0.0928 174 LYS B NZ  
5570  N N   . LYS B 175 ? 0.2069 0.3725 0.2891 0.0504  0.0484  -0.1120 175 LYS B N   
5571  C CA  . LYS B 175 ? 0.1849 0.3519 0.2572 0.0482  0.0476  -0.1223 175 LYS B CA  
5572  C C   . LYS B 175 ? 0.2713 0.4287 0.3295 0.0436  0.0427  -0.1135 175 LYS B C   
5573  O O   . LYS B 175 ? 0.2657 0.4310 0.3129 0.0415  0.0417  -0.1185 175 LYS B O   
5574  C CB  . LYS B 175 ? 0.2007 0.3920 0.2631 0.0474  0.0493  -0.1266 175 LYS B CB  
5575  C CG  . LYS B 175 ? 0.1865 0.3994 0.2370 0.0466  0.0502  -0.1136 175 LYS B CG  
5576  C CD  . LYS B 175 ? 0.3805 0.6183 0.4262 0.0471  0.0530  -0.1174 175 LYS B CD  
5577  C CE  . LYS B 175 ? 0.5409 0.8000 0.5701 0.0443  0.0518  -0.1056 175 LYS B CE  
5578  N NZ  . LYS B 175 ? 0.4877 0.7734 0.5132 0.0451  0.0548  -0.1065 175 LYS B NZ  
5579  N N   . THR B 176 ? 0.2982 0.4369 0.3559 0.0408  0.0382  -0.0984 176 THR B N   
5580  C CA  . THR B 176 ? 0.1627 0.2897 0.2079 0.0359  0.0331  -0.0896 176 THR B CA  
5581  C C   . THR B 176 ? 0.2649 0.3765 0.3121 0.0351  0.0322  -0.0990 176 THR B C   
5582  O O   . THR B 176 ? 0.3920 0.5060 0.4294 0.0327  0.0306  -0.1017 176 THR B O   
5583  C CB  . THR B 176 ? 0.2121 0.3253 0.2568 0.0331  0.0288  -0.0735 176 THR B CB  
5584  O OG1 . THR B 176 ? 0.3144 0.4426 0.3565 0.0325  0.0292  -0.0638 176 THR B OG1 
5585  C CG2 . THR B 176 ? 0.1889 0.2876 0.2236 0.0286  0.0241  -0.0676 176 THR B CG2 
5586  N N   . LEU B 177 ? 0.3199 0.4165 0.3815 0.0370  0.0331  -0.1031 177 LEU B N   
5587  C CA  . LEU B 177 ? 0.2724 0.3541 0.3386 0.0357  0.0325  -0.1105 177 LEU B CA  
5588  C C   . LEU B 177 ? 0.2159 0.3088 0.2847 0.0364  0.0351  -0.1276 177 LEU B C   
5589  O O   . LEU B 177 ? 0.2865 0.3715 0.3533 0.0329  0.0329  -0.1306 177 LEU B O   
5590  C CB  . LEU B 177 ? 0.2263 0.2898 0.3094 0.0373  0.0328  -0.1076 177 LEU B CB  
5591  C CG  . LEU B 177 ? 0.1668 0.2188 0.2457 0.0352  0.0286  -0.0898 177 LEU B CG  
5592  C CD1 . LEU B 177 ? 0.1708 0.2077 0.2666 0.0369  0.0287  -0.0856 177 LEU B CD1 
5593  C CD2 . LEU B 177 ? 0.1621 0.2078 0.2244 0.0300  0.0247  -0.0830 177 LEU B CD2 
5594  N N   . SER B 178 ? 0.1869 0.2961 0.2583 0.0385  0.0375  -0.1332 178 SER B N   
5595  C CA  . SER B 178 ? 0.2159 0.3352 0.2869 0.0366  0.0370  -0.1443 178 SER B CA  
5596  C C   . SER B 178 ? 0.2937 0.4259 0.3475 0.0333  0.0339  -0.1426 178 SER B C   
5597  O O   . SER B 178 ? 0.3613 0.4938 0.4158 0.0305  0.0316  -0.1495 178 SER B O   
5598  C CB  . SER B 178 ? 0.2532 0.3892 0.3296 0.0397  0.0404  -0.1509 178 SER B CB  
5599  O OG  . SER B 178 ? 0.3492 0.4738 0.4434 0.0434  0.0433  -0.1514 178 SER B OG  
5600  N N   . ILE B 179 ? 0.3758 0.5202 0.4161 0.0338  0.0338  -0.1329 179 ILE B N   
5601  C CA  . ILE B 179 ? 0.3156 0.4745 0.3415 0.0313  0.0309  -0.1297 179 ILE B CA  
5602  C C   . ILE B 179 ? 0.2762 0.4187 0.2990 0.0283  0.0274  -0.1270 179 ILE B C   
5603  O O   . ILE B 179 ? 0.3816 0.5316 0.3994 0.0261  0.0245  -0.1295 179 ILE B O   
5604  C CB  . ILE B 179 ? 0.3069 0.4844 0.3215 0.0325  0.0321  -0.1181 179 ILE B CB  
5605  C CG1 . ILE B 179 ? 0.3570 0.5544 0.3589 0.0307  0.0293  -0.1146 179 ILE B CG1 
5606  C CG2 . ILE B 179 ? 0.3267 0.4890 0.3400 0.0319  0.0311  -0.1049 179 ILE B CG2 
5607  C CD1 . ILE B 179 ? 0.3130 0.5274 0.3050 0.0312  0.0303  -0.0994 179 ILE B CD1 
5608  N N   . TYR B 180 ? 0.2712 0.3931 0.2977 0.0284  0.0276  -0.1220 180 TYR B N   
5609  C CA  . TYR B 180 ? 0.2745 0.3801 0.2994 0.0253  0.0248  -0.1202 180 TYR B CA  
5610  C C   . TYR B 180 ? 0.2539 0.3524 0.2893 0.0233  0.0240  -0.1294 180 TYR B C   
5611  O O   . TYR B 180 ? 0.2004 0.2981 0.2330 0.0204  0.0215  -0.1304 180 TYR B O   
5612  C CB  . TYR B 180 ? 0.2612 0.3459 0.2890 0.0247  0.0241  -0.1104 180 TYR B CB  
5613  C CG  . TYR B 180 ? 0.2353 0.3200 0.2526 0.0229  0.0211  -0.0944 180 TYR B CG  
5614  C CD1 . TYR B 180 ? 0.2466 0.3271 0.2555 0.0199  0.0178  -0.0882 180 TYR B CD1 
5615  C CD2 . TYR B 180 ? 0.2527 0.3416 0.2711 0.0241  0.0216  -0.0862 180 TYR B CD2 
5616  C CE1 . TYR B 180 ? 0.2272 0.3067 0.2302 0.0183  0.0152  -0.0748 180 TYR B CE1 
5617  C CE2 . TYR B 180 ? 0.2888 0.3772 0.3007 0.0219  0.0188  -0.0725 180 TYR B CE2 
5618  C CZ  . TYR B 180 ? 0.2122 0.2954 0.2170 0.0190  0.0156  -0.0673 180 TYR B CZ  
5619  O OH  . TYR B 180 ? 0.1462 0.2280 0.1481 0.0168  0.0129  -0.0548 180 TYR B OH  
5620  N N   . ARG B 181 ? 0.2648 0.3589 0.3140 0.0248  0.0265  -0.1361 181 ARG B N   
5621  C CA  . ARG B 181 ? 0.2237 0.3150 0.2854 0.0229  0.0263  -0.1462 181 ARG B CA  
5622  C C   . ARG B 181 ? 0.3447 0.4573 0.4009 0.0215  0.0243  -0.1537 181 ARG B C   
5623  O O   . ARG B 181 ? 0.3293 0.4417 0.3909 0.0187  0.0226  -0.1597 181 ARG B O   
5624  C CB  . ARG B 181 ? 0.2285 0.3152 0.3071 0.0255  0.0296  -0.1524 181 ARG B CB  
5625  C CG  . ARG B 181 ? 0.2693 0.3414 0.3666 0.0238  0.0302  -0.1582 181 ARG B CG  
5626  C CD  . ARG B 181 ? 0.3413 0.4092 0.4570 0.0269  0.0335  -0.1634 181 ARG B CD  
5627  N NE  . ARG B 181 ? 0.3586 0.4086 0.4825 0.0294  0.0350  -0.1535 181 ARG B NE  
5628  C CZ  . ARG B 181 ? 0.2962 0.3478 0.4180 0.0335  0.0366  -0.1473 181 ARG B CZ  
5629  N NH1 . ARG B 181 ? 0.2360 0.3059 0.3473 0.0355  0.0373  -0.1494 181 ARG B NH1 
5630  N NH2 . ARG B 181 ? 0.2967 0.3330 0.4286 0.0358  0.0374  -0.1381 181 ARG B NH2 
5631  N N   . GLU B 182 ? 0.3818 0.5150 0.4280 0.0234  0.0246  -0.1530 182 GLU B N   
5632  C CA  . GLU B 182 ? 0.3359 0.4934 0.3773 0.0225  0.0228  -0.1601 182 GLU B CA  
5633  C C   . GLU B 182 ? 0.3392 0.5013 0.3710 0.0202  0.0190  -0.1553 182 GLU B C   
5634  O O   . GLU B 182 ? 0.4081 0.5755 0.4451 0.0180  0.0169  -0.1631 182 GLU B O   
5635  C CB  . GLU B 182 ? 0.2999 0.4795 0.3325 0.0253  0.0244  -0.1579 182 GLU B CB  
5636  C CG  . GLU B 182 ? 0.5112 0.7195 0.5403 0.0249  0.0230  -0.1661 182 GLU B CG  
5637  C CD  . GLU B 182 ? 0.6679 0.9004 0.6831 0.0268  0.0236  -0.1574 182 GLU B CD  
5638  O OE1 . GLU B 182 ? 0.7865 1.0233 0.8028 0.0292  0.0271  -0.1565 182 GLU B OE1 
5639  O OE2 . GLU B 182 ? 0.6207 0.8689 0.6251 0.0260  0.0207  -0.1506 182 GLU B OE2 
5640  N N   . ILE B 183 ? 0.2668 0.4278 0.2862 0.0208  0.0181  -0.1428 183 ILE B N   
5641  C CA  . ILE B 183 ? 0.2656 0.4338 0.2763 0.0193  0.0146  -0.1378 183 ILE B CA  
5642  C C   . ILE B 183 ? 0.3385 0.4883 0.3567 0.0164  0.0131  -0.1406 183 ILE B C   
5643  O O   . ILE B 183 ? 0.2733 0.4313 0.2893 0.0150  0.0102  -0.1414 183 ILE B O   
5644  C CB  . ILE B 183 ? 0.1765 0.3461 0.1746 0.0206  0.0145  -0.1238 183 ILE B CB  
5645  C CG1 . ILE B 183 ? 0.2424 0.3862 0.2434 0.0205  0.0162  -0.1188 183 ILE B CG1 
5646  C CG2 . ILE B 183 ? 0.2541 0.4467 0.2453 0.0230  0.0163  -0.1193 183 ILE B CG2 
5647  C CD1 . ILE B 183 ? 0.1633 0.2940 0.1603 0.0188  0.0139  -0.1129 183 ILE B CD1 
5648  N N   . LYS B 184 ? 0.3794 0.5060 0.4072 0.0157  0.0151  -0.1413 184 LYS B N   
5649  C CA  . LYS B 184 ? 0.2593 0.3702 0.2956 0.0128  0.0144  -0.1432 184 LYS B CA  
5650  C C   . LYS B 184 ? 0.2754 0.3962 0.3231 0.0111  0.0137  -0.1557 184 LYS B C   
5651  O O   . LYS B 184 ? 0.3522 0.4767 0.4015 0.0089  0.0116  -0.1580 184 LYS B O   
5652  C CB  . LYS B 184 ? 0.2542 0.3411 0.2985 0.0128  0.0170  -0.1397 184 LYS B CB  
5653  C CG  . LYS B 184 ? 0.2673 0.3392 0.3214 0.0097  0.0171  -0.1404 184 LYS B CG  
5654  C CD  . LYS B 184 ? 0.2836 0.3351 0.3370 0.0095  0.0185  -0.1312 184 LYS B CD  
5655  C CE  . LYS B 184 ? 0.2818 0.3184 0.3519 0.0080  0.0209  -0.1336 184 LYS B CE  
5656  N NZ  . LYS B 184 ? 0.3978 0.4407 0.4789 0.0053  0.0203  -0.1426 184 LYS B NZ  
5657  N N   . GLU B 185 ? 0.3444 0.4705 0.4014 0.0121  0.0157  -0.1647 185 GLU B N   
5658  C CA  . GLU B 185 ? 0.3480 0.4851 0.4179 0.0104  0.0152  -0.1786 185 GLU B CA  
5659  C C   . GLU B 185 ? 0.3212 0.4864 0.3827 0.0105  0.0122  -0.1832 185 GLU B C   
5660  O O   . GLU B 185 ? 0.3019 0.4767 0.3709 0.0084  0.0105  -0.1922 185 GLU B O   
5661  C CB  . GLU B 185 ? 0.3275 0.4639 0.4108 0.0117  0.0182  -0.1879 185 GLU B CB  
5662  C CG  . GLU B 185 ? 0.4486 0.5659 0.5524 0.0099  0.0202  -0.1926 185 GLU B CG  
5663  C CD  . GLU B 185 ? 0.6738 0.7661 0.7779 0.0105  0.0221  -0.1802 185 GLU B CD  
5664  O OE1 . GLU B 185 ? 0.7444 0.8340 0.8387 0.0134  0.0230  -0.1724 185 GLU B OE1 
5665  O OE2 . GLU B 185 ? 0.7546 0.8317 0.8695 0.0081  0.0227  -0.1784 185 GLU B OE2 
5666  N N   . GLU B 186 ? 0.4086 0.5791 0.2697 0.0709  -0.0274 -0.1414 186 GLU B N   
5667  C CA  . GLU B 186 ? 0.3521 0.5561 0.2010 0.0743  -0.0276 -0.1340 186 GLU B CA  
5668  C C   . GLU B 186 ? 0.3488 0.5729 0.2037 0.0676  -0.0353 -0.1203 186 GLU B C   
5669  O O   . GLU B 186 ? 0.3946 0.6457 0.2415 0.0694  -0.0372 -0.1141 186 GLU B O   
5670  C CB  . GLU B 186 ? 0.4335 0.6558 0.2784 0.0891  -0.0152 -0.1190 186 GLU B CB  
5671  C CG  . GLU B 186 ? 0.4910 0.7146 0.3223 0.0968  -0.0088 -0.1310 186 GLU B CG  
5672  C CD  . GLU B 186 ? 0.7662 1.0166 0.5937 0.1090  0.0023  -0.1126 186 GLU B CD  
5673  O OE1 . GLU B 186 ? 0.6139 0.8600 0.4397 0.1177  0.0120  -0.1160 186 GLU B OE1 
5674  O OE2 . GLU B 186 ? 0.8609 1.1360 0.6889 0.1099  0.0014  -0.0936 186 GLU B OE2 
5675  N N   . GLY B 187 ? 0.3710 0.5834 0.2408 0.0606  -0.0394 -0.1147 187 GLY B N   
5676  C CA  . GLY B 187 ? 0.3231 0.5541 0.2019 0.0552  -0.0457 -0.1005 187 GLY B CA  
5677  C C   . GLY B 187 ? 0.3005 0.5538 0.1826 0.0659  -0.0393 -0.0752 187 GLY B C   
5678  O O   . GLY B 187 ? 0.2712 0.5422 0.1611 0.0641  -0.0432 -0.0619 187 GLY B O   
5679  N N   . LYS B 188 ? 0.3271 0.5760 0.2090 0.0762  -0.0280 -0.0661 188 LYS B N   
5680  C CA  . LYS B 188 ? 0.2966 0.5607 0.1861 0.0849  -0.0202 -0.0399 188 LYS B CA  
5681  C C   . LYS B 188 ? 0.2345 0.4782 0.1497 0.0811  -0.0180 -0.0252 188 LYS B C   
5682  O O   . LYS B 188 ? 0.2610 0.5153 0.1854 0.0859  -0.0141 -0.0039 188 LYS B O   
5683  C CB  . LYS B 188 ? 0.3388 0.6082 0.2202 0.0960  -0.0081 -0.0353 188 LYS B CB  
5684  C CG  . LYS B 188 ? 0.3747 0.6649 0.2357 0.1006  -0.0081 -0.0450 188 LYS B CG  
5685  C CD  . LYS B 188 ? 0.4195 0.7314 0.2793 0.1111  0.0022  -0.0239 188 LYS B CD  
5686  C CE  . LYS B 188 ? 0.4859 0.8187 0.3521 0.1119  -0.0008 -0.0029 188 LYS B CE  
5687  N NZ  . LYS B 188 ? 0.4128 0.7628 0.2815 0.1214  0.0096  0.0201  188 LYS B NZ  
5688  N N   . GLY B 189 ? 0.2254 0.4398 0.1515 0.0729  -0.0202 -0.0358 189 GLY B N   
5689  C CA  . GLY B 189 ? 0.2023 0.3985 0.1499 0.0691  -0.0184 -0.0239 189 GLY B CA  
5690  C C   . GLY B 189 ? 0.1977 0.3667 0.1525 0.0588  -0.0234 -0.0376 189 GLY B C   
5691  O O   . GLY B 189 ? 0.2120 0.3690 0.1582 0.0560  -0.0257 -0.0549 189 GLY B O   
5692  N N   . SER B 190 ? 0.1802 0.3391 0.1507 0.0535  -0.0246 -0.0292 190 SER B N   
5693  C CA  . SER B 190 ? 0.1748 0.3088 0.1533 0.0438  -0.0281 -0.0375 190 SER B CA  
5694  C C   . SER B 190 ? 0.1648 0.2773 0.1534 0.0464  -0.0220 -0.0321 190 SER B C   
5695  O O   . SER B 190 ? 0.1574 0.2749 0.1522 0.0534  -0.0156 -0.0195 190 SER B O   
5696  C CB  . SER B 190 ? 0.1635 0.3022 0.1522 0.0368  -0.0326 -0.0321 190 SER B CB  
5697  O OG  . SER B 190 ? 0.1766 0.3338 0.1585 0.0316  -0.0402 -0.0399 190 SER B OG  
5698  N N   . VAL B 191 ? 0.1670 0.2562 0.1582 0.0404  -0.0245 -0.0413 191 VAL B N   
5699  C CA  . VAL B 191 ? 0.1586 0.2286 0.1598 0.0419  -0.0207 -0.0367 191 VAL B CA  
5700  C C   . VAL B 191 ? 0.1859 0.2392 0.1943 0.0322  -0.0250 -0.0370 191 VAL B C   
5701  O O   . VAL B 191 ? 0.2754 0.3184 0.2797 0.0248  -0.0300 -0.0469 191 VAL B O   
5702  C CB  . VAL B 191 ? 0.1716 0.2303 0.1684 0.0472  -0.0183 -0.0458 191 VAL B CB  
5703  C CG1 . VAL B 191 ? 0.1621 0.2061 0.1714 0.0494  -0.0152 -0.0390 191 VAL B CG1 
5704  C CG2 . VAL B 191 ? 0.1810 0.2597 0.1683 0.0568  -0.0131 -0.0464 191 VAL B CG2 
5705  N N   . SER B 192 ? 0.1375 0.1878 0.1562 0.0320  -0.0228 -0.0264 192 SER B N   
5706  C CA  . SER B 192 ? 0.1321 0.1684 0.1564 0.0243  -0.0255 -0.0253 192 SER B CA  
5707  C C   . SER B 192 ? 0.1698 0.1899 0.1998 0.0264  -0.0241 -0.0227 192 SER B C   
5708  O O   . SER B 192 ? 0.2047 0.2267 0.2375 0.0337  -0.0205 -0.0204 192 SER B O   
5709  C CB  . SER B 192 ? 0.1450 0.1920 0.1756 0.0229  -0.0244 -0.0171 192 SER B CB  
5710  O OG  . SER B 192 ? 0.2429 0.2959 0.2799 0.0303  -0.0194 -0.0080 192 SER B OG  
5711  N N   . THR B 193 ? 0.1649 0.1714 0.1969 0.0199  -0.0269 -0.0222 193 THR B N   
5712  C CA  . THR B 193 ? 0.1689 0.1627 0.2060 0.0213  -0.0272 -0.0186 193 THR B CA  
5713  C C   . THR B 193 ? 0.1665 0.1587 0.2066 0.0161  -0.0280 -0.0134 193 THR B C   
5714  O O   . THR B 193 ? 0.1758 0.1765 0.2152 0.0126  -0.0273 -0.0125 193 THR B O   
5715  C CB  . THR B 193 ? 0.1413 0.1175 0.1752 0.0205  -0.0303 -0.0239 193 THR B CB  
5716  O OG1 . THR B 193 ? 0.1721 0.1408 0.2124 0.0245  -0.0308 -0.0194 193 THR B OG1 
5717  C CG2 . THR B 193 ? 0.1489 0.1150 0.1785 0.0106  -0.0341 -0.0256 193 THR B CG2 
5718  N N   . SER B 194 ? 0.2082 0.1916 0.2519 0.0164  -0.0295 -0.0102 194 SER B N   
5719  C CA  . SER B 194 ? 0.1739 0.1557 0.2183 0.0122  -0.0305 -0.0068 194 SER B CA  
5720  C C   . SER B 194 ? 0.1572 0.1261 0.1980 0.0091  -0.0349 -0.0055 194 SER B C   
5721  O O   . SER B 194 ? 0.1960 0.1564 0.2374 0.0121  -0.0369 -0.0062 194 SER B O   
5722  C CB  . SER B 194 ? 0.1472 0.1345 0.2004 0.0159  -0.0284 -0.0036 194 SER B CB  
5723  O OG  . SER B 194 ? 0.1789 0.1769 0.2359 0.0188  -0.0239 -0.0021 194 SER B OG  
5724  N N   . PRO B 195 ? 0.1952 0.1627 0.2317 0.0038  -0.0363 -0.0033 195 PRO B N   
5725  C CA  . PRO B 195 ? 0.1993 0.1568 0.2317 0.0018  -0.0409 0.0005  195 PRO B CA  
5726  C C   . PRO B 195 ? 0.2493 0.2057 0.2893 0.0081  -0.0437 0.0021  195 PRO B C   
5727  O O   . PRO B 195 ? 0.3276 0.2924 0.3755 0.0113  -0.0421 0.0012  195 PRO B O   
5728  C CB  . PRO B 195 ? 0.2420 0.2045 0.2684 -0.0030 -0.0406 0.0018  195 PRO B CB  
5729  C CG  . PRO B 195 ? 0.1758 0.1469 0.2020 -0.0055 -0.0356 -0.0011 195 PRO B CG  
5730  C CD  . PRO B 195 ? 0.1665 0.1424 0.2004 -0.0001 -0.0333 -0.0038 195 PRO B CD  
5731  N N   . TYR B 196 ? 0.2515 0.1978 0.2904 0.0098  -0.0479 0.0055  196 TYR B N   
5732  C CA  . TYR B 196 ? 0.1585 0.1040 0.2070 0.0179  -0.0495 0.0064  196 TYR B CA  
5733  C C   . TYR B 196 ? 0.1766 0.1350 0.2352 0.0204  -0.0501 0.0071  196 TYR B C   
5734  O O   . TYR B 196 ? 0.2369 0.2031 0.3052 0.0252  -0.0464 0.0054  196 TYR B O   
5735  C CB  . TYR B 196 ? 0.1859 0.1190 0.2325 0.0199  -0.0547 0.0120  196 TYR B CB  
5736  C CG  . TYR B 196 ? 0.1833 0.1114 0.2390 0.0296  -0.0544 0.0110  196 TYR B CG  
5737  C CD1 . TYR B 196 ? 0.2391 0.1797 0.3075 0.0368  -0.0544 0.0116  196 TYR B CD1 
5738  C CD2 . TYR B 196 ? 0.2489 0.1600 0.3016 0.0315  -0.0536 0.0087  196 TYR B CD2 
5739  C CE1 . TYR B 196 ? 0.2949 0.2336 0.3724 0.0469  -0.0528 0.0105  196 TYR B CE1 
5740  C CE2 . TYR B 196 ? 0.2402 0.1459 0.3009 0.0420  -0.0524 0.0061  196 TYR B CE2 
5741  C CZ  . TYR B 196 ? 0.2554 0.1761 0.3282 0.0504  -0.0516 0.0072  196 TYR B CZ  
5742  O OH  . TYR B 196 ? 0.3327 0.2513 0.4137 0.0617  -0.0489 0.0044  196 TYR B OH  
5743  N N   . TYR B 197 ? 0.1487 0.1104 0.2053 0.0167  -0.0549 0.0097  197 TYR B N   
5744  C CA  . TYR B 197 ? 0.1391 0.1121 0.2070 0.0175  -0.0573 0.0097  197 TYR B CA  
5745  C C   . TYR B 197 ? 0.1344 0.1127 0.2026 0.0125  -0.0541 0.0052  197 TYR B C   
5746  O O   . TYR B 197 ? 0.2106 0.1951 0.2852 0.0099  -0.0575 0.0039  197 TYR B O   
5747  C CB  . TYR B 197 ? 0.1433 0.1183 0.2100 0.0170  -0.0660 0.0141  197 TYR B CB  
5748  C CG  . TYR B 197 ? 0.1575 0.1284 0.2296 0.0247  -0.0690 0.0197  197 TYR B CG  
5749  C CD1 . TYR B 197 ? 0.1471 0.1277 0.2365 0.0315  -0.0692 0.0208  197 TYR B CD1 
5750  C CD2 . TYR B 197 ? 0.2230 0.1801 0.2845 0.0255  -0.0707 0.0242  197 TYR B CD2 
5751  C CE1 . TYR B 197 ? 0.1560 0.1331 0.2518 0.0405  -0.0710 0.0253  197 TYR B CE1 
5752  C CE2 . TYR B 197 ? 0.1909 0.1411 0.2586 0.0338  -0.0729 0.0291  197 TYR B CE2 
5753  C CZ  . TYR B 197 ? 0.1744 0.1349 0.2592 0.0421  -0.0731 0.0292  197 TYR B CZ  
5754  O OH  . TYR B 197 ? 0.2296 0.1842 0.3203 0.0515  -0.0735 0.0331  197 TYR B OH  
5755  N N   . HIS B 198 ? 0.1219 0.0977 0.1844 0.0112  -0.0481 0.0027  198 HIS B N   
5756  C CA  . HIS B 198 ? 0.1490 0.1284 0.2136 0.0089  -0.0438 -0.0008 198 HIS B CA  
5757  C C   . HIS B 198 ? 0.1355 0.1143 0.1928 0.0036  -0.0470 -0.0043 198 HIS B C   
5758  O O   . HIS B 198 ? 0.1709 0.1520 0.2356 0.0019  -0.0480 -0.0076 198 HIS B O   
5759  C CB  . HIS B 198 ? 0.1667 0.1524 0.2475 0.0116  -0.0413 0.0004  198 HIS B CB  
5760  C CG  . HIS B 198 ? 0.1467 0.1339 0.2318 0.0117  -0.0350 -0.0005 198 HIS B CG  
5761  N ND1 . HIS B 198 ? 0.2249 0.2105 0.3159 0.0083  -0.0349 -0.0033 198 HIS B ND1 
5762  C CD2 . HIS B 198 ? 0.1954 0.1855 0.2801 0.0152  -0.0289 0.0014  198 HIS B CD2 
5763  C CE1 . HIS B 198 ? 0.2312 0.2168 0.3263 0.0105  -0.0285 -0.0020 198 HIS B CE1 
5764  N NE2 . HIS B 198 ? 0.1861 0.1761 0.2772 0.0148  -0.0251 0.0016  198 HIS B NE2 
5765  N N   . PRO B 199 ? 0.1444 0.1203 0.1871 0.0006  -0.0485 -0.0040 199 PRO B N   
5766  C CA  . PRO B 199 ? 0.1922 0.1696 0.2250 -0.0036 -0.0510 -0.0080 199 PRO B CA  
5767  C C   . PRO B 199 ? 0.3149 0.2935 0.3430 -0.0047 -0.0442 -0.0132 199 PRO B C   
5768  O O   . PRO B 199 ? 0.4472 0.4265 0.4774 -0.0029 -0.0385 -0.0118 199 PRO B O   
5769  C CB  . PRO B 199 ? 0.1518 0.1272 0.1714 -0.0055 -0.0553 -0.0023 199 PRO B CB  
5770  C CG  . PRO B 199 ? 0.1468 0.1169 0.1672 -0.0042 -0.0514 0.0020  199 PRO B CG  
5771  C CD  . PRO B 199 ? 0.2268 0.1978 0.2613 0.0003  -0.0478 0.0000  199 PRO B CD  
5772  N N   . LEU B 200 ? 0.2545 0.2345 0.2762 -0.0071 -0.0452 -0.0198 200 LEU B N   
5773  C CA  . LEU B 200 ? 0.1794 0.1613 0.1950 -0.0069 -0.0384 -0.0253 200 LEU B CA  
5774  C C   . LEU B 200 ? 0.2006 0.1870 0.2014 -0.0094 -0.0365 -0.0211 200 LEU B C   
5775  O O   . LEU B 200 ? 0.2529 0.2427 0.2393 -0.0122 -0.0386 -0.0227 200 LEU B O   
5776  C CB  . LEU B 200 ? 0.1975 0.1781 0.2104 -0.0081 -0.0395 -0.0359 200 LEU B CB  
5777  C CG  . LEU B 200 ? 0.1776 0.1518 0.2079 -0.0065 -0.0386 -0.0405 200 LEU B CG  
5778  C CD1 . LEU B 200 ? 0.2974 0.2671 0.3251 -0.0062 -0.0352 -0.0526 200 LEU B CD1 
5779  C CD2 . LEU B 200 ? 0.2404 0.2138 0.2841 -0.0019 -0.0326 -0.0334 200 LEU B CD2 
5780  N N   . ILE B 201 ? 0.1637 0.1512 0.1681 -0.0089 -0.0327 -0.0156 201 ILE B N   
5781  C CA  . ILE B 201 ? 0.1800 0.1710 0.1739 -0.0131 -0.0312 -0.0100 201 ILE B CA  
5782  C C   . ILE B 201 ? 0.2575 0.2576 0.2407 -0.0146 -0.0257 -0.0138 201 ILE B C   
5783  O O   . ILE B 201 ? 0.2079 0.2114 0.1776 -0.0189 -0.0263 -0.0093 201 ILE B O   
5784  C CB  . ILE B 201 ? 0.2344 0.2253 0.2361 -0.0135 -0.0287 -0.0057 201 ILE B CB  
5785  C CG1 . ILE B 201 ? 0.1747 0.1558 0.1809 -0.0127 -0.0344 -0.0014 201 ILE B CG1 
5786  C CG2 . ILE B 201 ? 0.1997 0.1968 0.1947 -0.0192 -0.0251 -0.0015 201 ILE B CG2 
5787  C CD1 . ILE B 201 ? 0.1955 0.1700 0.1925 -0.0167 -0.0389 0.0056  201 ILE B CD1 
5788  N N   . PRO B 202 ? 0.2351 0.2401 0.2234 -0.0105 -0.0196 -0.0212 202 PRO B N   
5789  C CA  . PRO B 202 ? 0.1909 0.2056 0.1684 -0.0104 -0.0135 -0.0261 202 PRO B CA  
5790  C C   . PRO B 202 ? 0.2196 0.2340 0.1803 -0.0127 -0.0175 -0.0303 202 PRO B C   
5791  O O   . PRO B 202 ? 0.2917 0.3158 0.2376 -0.0153 -0.0140 -0.0288 202 PRO B O   
5792  C CB  . PRO B 202 ? 0.1728 0.1878 0.1617 -0.0033 -0.0076 -0.0344 202 PRO B CB  
5793  C CG  . PRO B 202 ? 0.1562 0.1687 0.1608 -0.0013 -0.0083 -0.0288 202 PRO B CG  
5794  C CD  . PRO B 202 ? 0.1658 0.1691 0.1700 -0.0049 -0.0166 -0.0239 202 PRO B CD  
5795  N N   . ILE B 203 ? 0.2017 0.2074 0.1642 -0.0122 -0.0248 -0.0350 203 ILE B N   
5796  C CA  . ILE B 203 ? 0.2934 0.3014 0.2395 -0.0146 -0.0302 -0.0401 203 ILE B CA  
5797  C C   . ILE B 203 ? 0.2781 0.2896 0.2116 -0.0191 -0.0358 -0.0278 203 ILE B C   
5798  O O   . ILE B 203 ? 0.3136 0.3340 0.2279 -0.0213 -0.0357 -0.0272 203 ILE B O   
5799  C CB  . ILE B 203 ? 0.2751 0.2749 0.2296 -0.0141 -0.0375 -0.0488 203 ILE B CB  
5800  C CG1 . ILE B 203 ? 0.2679 0.2627 0.2300 -0.0102 -0.0314 -0.0623 203 ILE B CG1 
5801  C CG2 . ILE B 203 ? 0.2331 0.2378 0.1715 -0.0178 -0.0466 -0.0516 203 ILE B CG2 
5802  C CD1 . ILE B 203 ? 0.2682 0.2551 0.2358 -0.0121 -0.0383 -0.0734 203 ILE B CD1 
5803  N N   . LEU B 204 ? 0.2606 0.2651 0.2044 -0.0197 -0.0402 -0.0176 204 LEU B N   
5804  C CA  . LEU B 204 ? 0.2250 0.2291 0.1593 -0.0229 -0.0453 -0.0047 204 LEU B CA  
5805  C C   . LEU B 204 ? 0.2844 0.2958 0.2067 -0.0268 -0.0381 0.0026  204 LEU B C   
5806  O O   . LEU B 204 ? 0.2458 0.2626 0.1515 -0.0297 -0.0402 0.0102  204 LEU B O   
5807  C CB  . LEU B 204 ? 0.2058 0.1991 0.1551 -0.0217 -0.0491 0.0032  204 LEU B CB  
5808  C CG  . LEU B 204 ? 0.2221 0.2105 0.1851 -0.0179 -0.0560 0.0002  204 LEU B CG  
5809  C CD1 . LEU B 204 ? 0.1854 0.1647 0.1621 -0.0156 -0.0561 0.0065  204 LEU B CD1 
5810  C CD2 . LEU B 204 ? 0.2378 0.2303 0.1928 -0.0182 -0.0660 0.0027  204 LEU B CD2 
5811  N N   . LEU B 205 ? 0.3429 0.3566 0.2743 -0.0272 -0.0296 0.0015  205 LEU B N   
5812  C CA  . LEU B 205 ? 0.2389 0.2623 0.1629 -0.0320 -0.0221 0.0088  205 LEU B CA  
5813  C C   . LEU B 205 ? 0.3331 0.3711 0.2391 -0.0316 -0.0169 0.0035  205 LEU B C   
5814  O O   . LEU B 205 ? 0.4111 0.4573 0.3017 -0.0360 -0.0150 0.0128  205 LEU B O   
5815  C CB  . LEU B 205 ? 0.2107 0.2373 0.1506 -0.0323 -0.0151 0.0073  205 LEU B CB  
5816  C CG  . LEU B 205 ? 0.2004 0.2159 0.1537 -0.0352 -0.0185 0.0141  205 LEU B CG  
5817  C CD1 . LEU B 205 ? 0.1834 0.2030 0.1527 -0.0322 -0.0146 0.0078  205 LEU B CD1 
5818  C CD2 . LEU B 205 ? 0.3182 0.3339 0.2672 -0.0438 -0.0169 0.0267  205 LEU B CD2 
5819  N N   . ASN B 206 ? 0.3786 0.4198 0.2863 -0.0260 -0.0140 -0.0114 206 ASN B N   
5820  C CA  . ASN B 206 ? 0.3421 0.3966 0.2328 -0.0241 -0.0080 -0.0203 206 ASN B CA  
5821  C C   . ASN B 206 ? 0.3089 0.3572 0.2016 -0.0183 -0.0104 -0.0380 206 ASN B C   
5822  O O   . ASN B 206 ? 0.4713 0.5151 0.3803 -0.0134 -0.0058 -0.0458 206 ASN B O   
5823  C CB  . ASN B 206 ? 0.2641 0.3335 0.1582 -0.0237 0.0048  -0.0193 206 ASN B CB  
5824  C CG  . ASN B 206 ? 0.4033 0.4897 0.2767 -0.0220 0.0126  -0.0254 206 ASN B CG  
5825  O OD1 . ASN B 206 ? 0.3552 0.4408 0.2128 -0.0196 0.0087  -0.0359 206 ASN B OD1 
5826  N ND2 . ASN B 206 ? 0.6350 0.7389 0.5087 -0.0236 0.0237  -0.0195 206 ASN B ND2 
5827  N N   . PRO B 207 ? 0.2781 0.3262 0.1553 -0.0191 -0.0178 -0.0446 207 PRO B N   
5828  C CA  . PRO B 207 ? 0.2836 0.3244 0.1638 -0.0154 -0.0205 -0.0630 207 PRO B CA  
5829  C C   . PRO B 207 ? 0.3331 0.3791 0.2094 -0.0097 -0.0094 -0.0779 207 PRO B C   
5830  O O   . PRO B 207 ? 0.2998 0.3353 0.1834 -0.0061 -0.0100 -0.0934 207 PRO B O   
5831  C CB  . PRO B 207 ? 0.3726 0.4170 0.2339 -0.0190 -0.0317 -0.0655 207 PRO B CB  
5832  C CG  . PRO B 207 ? 0.3534 0.4010 0.2105 -0.0231 -0.0370 -0.0453 207 PRO B CG  
5833  C CD  . PRO B 207 ? 0.3500 0.4034 0.2087 -0.0236 -0.0257 -0.0344 207 PRO B CD  
5834  N N   . ASN B 208 ? 0.4164 0.4780 0.2828 -0.0086 0.0012  -0.0737 208 ASN B N   
5835  C CA  . ASN B 208 ? 0.3645 0.4329 0.2298 -0.0012 0.0132  -0.0876 208 ASN B CA  
5836  C C   . ASN B 208 ? 0.2939 0.3545 0.1862 0.0050  0.0191  -0.0889 208 ASN B C   
5837  O O   . ASN B 208 ? 0.3029 0.3665 0.1986 0.0132  0.0289  -0.1005 208 ASN B O   
5838  C CB  . ASN B 208 ? 0.3409 0.4325 0.1899 -0.0018 0.0238  -0.0808 208 ASN B CB  
5839  C CG  . ASN B 208 ? 0.3734 0.4759 0.1909 -0.0041 0.0214  -0.0857 208 ASN B CG  
5840  O OD1 . ASN B 208 ? 0.4085 0.5048 0.2152 -0.0016 0.0169  -0.1036 208 ASN B OD1 
5841  N ND2 . ASN B 208 ? 0.4176 0.5369 0.2201 -0.0094 0.0244  -0.0697 208 ASN B ND2 
5842  N N   . CYS B 209 ? 0.2896 0.3412 0.2004 0.0022  0.0137  -0.0771 209 CYS B N   
5843  C CA  . CYS B 209 ? 0.2522 0.2982 0.1873 0.0082  0.0182  -0.0766 209 CYS B CA  
5844  C C   . CYS B 209 ? 0.3447 0.3741 0.2891 0.0146  0.0176  -0.0915 209 CYS B C   
5845  O O   . CYS B 209 ? 0.4095 0.4369 0.3695 0.0228  0.0249  -0.0947 209 CYS B O   
5846  C CB  . CYS B 209 ? 0.2466 0.2869 0.1957 0.0035  0.0116  -0.0622 209 CYS B CB  
5847  S SG  . CYS B 209 ? 0.4407 0.4619 0.3930 -0.0005 -0.0020 -0.0628 209 CYS B SG  
5848  N N   . VAL B 210 ? 0.3429 0.3603 0.2794 0.0107  0.0088  -0.1001 210 VAL B N   
5849  C CA  . VAL B 210 ? 0.3148 0.3135 0.2632 0.0142  0.0071  -0.1133 210 VAL B CA  
5850  C C   . VAL B 210 ? 0.3712 0.3684 0.3155 0.0227  0.0169  -0.1304 210 VAL B C   
5851  O O   . VAL B 210 ? 0.4563 0.4358 0.4148 0.0276  0.0184  -0.1405 210 VAL B O   
5852  C CB  . VAL B 210 ? 0.3134 0.3029 0.2549 0.0063  -0.0055 -0.1194 210 VAL B CB  
5853  C CG1 . VAL B 210 ? 0.3830 0.3721 0.3337 0.0004  -0.0143 -0.1031 210 VAL B CG1 
5854  C CG2 . VAL B 210 ? 0.3608 0.3620 0.2742 0.0030  -0.0079 -0.1279 210 VAL B CG2 
5855  N N   . TYR B 211 ? 0.3143 0.3293 0.2402 0.0250  0.0243  -0.1337 211 TYR B N   
5856  C CA  . TYR B 211 ? 0.3397 0.3551 0.2596 0.0344  0.0346  -0.1516 211 TYR B CA  
5857  C C   . TYR B 211 ? 0.3315 0.3508 0.2713 0.0459  0.0467  -0.1481 211 TYR B C   
5858  O O   . TYR B 211 ? 0.4101 0.4263 0.3505 0.0562  0.0560  -0.1632 211 TYR B O   
5859  C CB  . TYR B 211 ? 0.3604 0.3968 0.2510 0.0329  0.0387  -0.1564 211 TYR B CB  
5860  C CG  . TYR B 211 ? 0.3792 0.4123 0.2472 0.0246  0.0275  -0.1656 211 TYR B CG  
5861  C CD1 . TYR B 211 ? 0.4034 0.4191 0.2679 0.0256  0.0233  -0.1878 211 TYR B CD1 
5862  C CD2 . TYR B 211 ? 0.3751 0.4223 0.2262 0.0156  0.0203  -0.1518 211 TYR B CD2 
5863  C CE1 . TYR B 211 ? 0.4218 0.4358 0.2681 0.0170  0.0116  -0.1926 211 TYR B CE1 
5864  C CE2 . TYR B 211 ? 0.3934 0.4406 0.2241 0.0089  0.0090  -0.1589 211 TYR B CE2 
5865  C CZ  . TYR B 211 ? 0.4162 0.4486 0.2441 0.0095  0.0043  -0.1806 211 TYR B CZ  
5866  O OH  . TYR B 211 ? 0.5935 0.6260 0.4047 0.0021  -0.0080 -0.1836 211 TYR B OH  
5867  N N   . GLU B 212 ? 0.3034 0.3301 0.2598 0.0449  0.0466  -0.1294 212 GLU B N   
5868  C CA  . GLU B 212 ? 0.3481 0.3846 0.3232 0.0557  0.0570  -0.1244 212 GLU B CA  
5869  C C   . GLU B 212 ? 0.3195 0.3339 0.3156 0.0654  0.0586  -0.1307 212 GLU B C   
5870  O O   . GLU B 212 ? 0.3818 0.4022 0.3921 0.0777  0.0683  -0.1308 212 GLU B O   
5871  C CB  . GLU B 212 ? 0.3823 0.4344 0.3676 0.0504  0.0549  -0.1037 212 GLU B CB  
5872  C CG  . GLU B 212 ? 0.4892 0.5664 0.4593 0.0439  0.0583  -0.0963 212 GLU B CG  
5873  C CD  . GLU B 212 ? 0.4848 0.5676 0.4585 0.0330  0.0509  -0.0785 212 GLU B CD  
5874  O OE1 . GLU B 212 ? 0.5144 0.5915 0.5064 0.0338  0.0471  -0.0706 212 GLU B OE1 
5875  O OE2 . GLU B 212 ? 0.4327 0.5248 0.3902 0.0238  0.0490  -0.0723 212 GLU B OE2 
5876  N N   . THR B 213 ? 0.3149 0.3048 0.3146 0.0603  0.0496  -0.1349 213 THR B N   
5877  C CA  . THR B 213 ? 0.3403 0.3060 0.3598 0.0680  0.0512  -0.1404 213 THR B CA  
5878  C C   . THR B 213 ? 0.4172 0.3586 0.4297 0.0651  0.0473  -0.1607 213 THR B C   
5879  O O   . THR B 213 ? 0.4240 0.3431 0.4499 0.0701  0.0490  -0.1625 213 THR B O   
5880  C CB  . THR B 213 ? 0.3797 0.3380 0.4183 0.0645  0.0446  -0.1231 213 THR B CB  
5881  O OG1 . THR B 213 ? 0.4034 0.3626 0.4320 0.0509  0.0335  -0.1177 213 THR B OG1 
5882  C CG2 . THR B 213 ? 0.3660 0.3449 0.4164 0.0705  0.0494  -0.1062 213 THR B CG2 
5883  N N   . THR B 214 ? 0.4163 0.3619 0.4060 0.0551  0.0404  -0.1696 214 THR B N   
5884  C CA  . THR B 214 ? 0.3999 0.3263 0.3795 0.0494  0.0344  -0.1853 214 THR B CA  
5885  C C   . THR B 214 ? 0.4913 0.4338 0.4405 0.0472  0.0353  -0.1965 214 THR B C   
5886  O O   . THR B 214 ? 0.5388 0.4890 0.4709 0.0367  0.0255  -0.1980 214 THR B O   
5887  C CB  . THR B 214 ? 0.4570 0.3720 0.4436 0.0368  0.0208  -0.1815 214 THR B CB  
5888  O OG1 . THR B 214 ? 0.3906 0.3250 0.3700 0.0300  0.0148  -0.1679 214 THR B OG1 
5889  C CG2 . THR B 214 ? 0.4036 0.2993 0.4188 0.0390  0.0211  -0.1708 214 THR B CG2 
5890  N N   . PRO B 215 ? 0.4194 0.3683 0.3606 0.0574  0.0470  -0.2029 215 PRO B N   
5891  C CA  . PRO B 215 ? 0.4364 0.4069 0.3485 0.0562  0.0503  -0.2090 215 PRO B CA  
5892  C C   . PRO B 215 ? 0.5328 0.4965 0.4220 0.0468  0.0404  -0.2215 215 PRO B C   
5893  O O   . PRO B 215 ? 0.5284 0.5122 0.3943 0.0407  0.0368  -0.2193 215 PRO B O   
5894  C CB  . PRO B 215 ? 0.4779 0.4510 0.3918 0.0703  0.0653  -0.2140 215 PRO B CB  
5895  C CG  . PRO B 215 ? 0.4352 0.4010 0.3799 0.0789  0.0701  -0.2030 215 PRO B CG  
5896  C CD  . PRO B 215 ? 0.4269 0.3671 0.3860 0.0713  0.0585  -0.2017 215 PRO B CD  
5897  N N   . ASN B 216 ? 0.6033 0.5406 0.4978 0.0452  0.0359  -0.2334 216 ASN B N   
5898  C CA  . ASN B 216 ? 0.6655 0.5978 0.5393 0.0357  0.0257  -0.2458 216 ASN B CA  
5899  C C   . ASN B 216 ? 0.5845 0.5071 0.4700 0.0231  0.0105  -0.2408 216 ASN B C   
5900  O O   . ASN B 216 ? 0.7305 0.6306 0.6261 0.0184  0.0048  -0.2485 216 ASN B O   
5901  C CB  . ASN B 216 ? 0.7841 0.6959 0.6528 0.0412  0.0307  -0.2643 216 ASN B CB  
5902  C CG  . ASN B 216 ? 0.8745 0.7599 0.7711 0.0487  0.0362  -0.2638 216 ASN B CG  
5903  O OD1 . ASN B 216 ? 0.9738 0.8385 0.8870 0.0418  0.0281  -0.2629 216 ASN B OD1 
5904  N ND2 . ASN B 216 ? 0.6844 0.5715 0.5866 0.0631  0.0504  -0.2629 216 ASN B ND2 
5905  N N   . VAL B 217 ? 0.4702 0.4107 0.3542 0.0173  0.0043  -0.2270 217 VAL B N   
5906  C CA  . VAL B 217 ? 0.5012 0.4372 0.3957 0.0059  -0.0099 -0.2203 217 VAL B CA  
5907  C C   . VAL B 217 ? 0.5881 0.5436 0.4571 -0.0024 -0.0205 -0.2188 217 VAL B C   
5908  O O   . VAL B 217 ? 0.4670 0.4425 0.3129 0.0004  -0.0162 -0.2166 217 VAL B O   
5909  C CB  . VAL B 217 ? 0.4129 0.3498 0.3313 0.0067  -0.0097 -0.2039 217 VAL B CB  
5910  C CG1 . VAL B 217 ? 0.4365 0.3986 0.3413 0.0052  -0.0113 -0.1923 217 VAL B CG1 
5911  C CG2 . VAL B 217 ? 0.4032 0.3257 0.3425 -0.0022 -0.0205 -0.1993 217 VAL B CG2 
5912  N N   . LYS B 218 ? 0.6369 0.5876 0.5114 -0.0128 -0.0343 -0.2180 218 LYS B N   
5913  C CA  . LYS B 218 ? 0.5268 0.4946 0.3801 -0.0208 -0.0465 -0.2154 218 LYS B CA  
5914  C C   . LYS B 218 ? 0.5583 0.5393 0.4195 -0.0243 -0.0537 -0.1965 218 LYS B C   
5915  O O   . LYS B 218 ? 0.5794 0.5536 0.4620 -0.0302 -0.0620 -0.1908 218 LYS B O   
5916  C CB  . LYS B 218 ? 0.5634 0.5202 0.4187 -0.0298 -0.0578 -0.2264 218 LYS B CB  
5917  C CG  . LYS B 218 ? 0.6774 0.6193 0.5225 -0.0276 -0.0529 -0.2469 218 LYS B CG  
5918  C CD  . LYS B 218 ? 0.6747 0.6318 0.4869 -0.0218 -0.0471 -0.2535 218 LYS B CD  
5919  C CE  . LYS B 218 ? 0.8888 0.8691 0.6773 -0.0282 -0.0589 -0.2465 218 LYS B CE  
5920  N NZ  . LYS B 218 ? 0.9395 0.9365 0.6960 -0.0221 -0.0517 -0.2496 218 LYS B NZ  
5921  N N   . ILE B 219 ? 0.6282 0.6285 0.4727 -0.0210 -0.0502 -0.1859 219 ILE B N   
5922  C CA  . ILE B 219 ? 0.6341 0.6468 0.4820 -0.0246 -0.0582 -0.1677 219 ILE B CA  
5923  C C   . ILE B 219 ? 0.6209 0.6518 0.4423 -0.0287 -0.0675 -0.1613 219 ILE B C   
5924  O O   . ILE B 219 ? 0.5619 0.6018 0.3581 -0.0261 -0.0623 -0.1662 219 ILE B O   
5925  C CB  . ILE B 219 ? 0.5260 0.5434 0.3800 -0.0189 -0.0472 -0.1523 219 ILE B CB  
5926  C CG1 . ILE B 219 ? 0.5223 0.5550 0.3515 -0.0140 -0.0359 -0.1535 219 ILE B CG1 
5927  C CG2 . ILE B 219 ? 0.5031 0.5020 0.3863 -0.0143 -0.0392 -0.1531 219 ILE B CG2 
5928  C CD1 . ILE B 219 ? 0.5149 0.5612 0.3390 -0.0143 -0.0323 -0.1293 219 ILE B CD1 
5929  N N   . PRO B 220 ? 0.5884 0.6255 0.4152 -0.0341 -0.0809 -0.1496 220 PRO B N   
5930  C CA  . PRO B 220 ? 0.5894 0.6433 0.3926 -0.0367 -0.0904 -0.1412 220 PRO B CA  
5931  C C   . PRO B 220 ? 0.6158 0.6851 0.3992 -0.0328 -0.0836 -0.1252 220 PRO B C   
5932  O O   . PRO B 220 ? 0.6098 0.6789 0.3992 -0.0296 -0.0730 -0.1195 220 PRO B O   
5933  C CB  . PRO B 220 ? 0.5386 0.5943 0.3599 -0.0417 -0.1050 -0.1307 220 PRO B CB  
5934  C CG  . PRO B 220 ? 0.3852 0.4295 0.2362 -0.0404 -0.1008 -0.1277 220 PRO B CG  
5935  C CD  . PRO B 220 ? 0.5056 0.5345 0.3624 -0.0371 -0.0877 -0.1433 220 PRO B CD  
5936  N N   . ASP B 221 ? 0.7917 0.8749 0.5517 -0.0336 -0.0899 -0.1169 221 ASP B N   
5937  C CA  . ASP B 221 ? 0.7200 0.8173 0.4614 -0.0311 -0.0838 -0.0981 221 ASP B CA  
5938  C C   . ASP B 221 ? 0.5730 0.6710 0.3292 -0.0322 -0.0881 -0.0762 221 ASP B C   
5939  O O   . ASP B 221 ? 0.6100 0.7082 0.3754 -0.0338 -0.1014 -0.0682 221 ASP B O   
5940  C CB  . ASP B 221 ? 0.6762 0.7868 0.3905 -0.0312 -0.0901 -0.0939 221 ASP B CB  
5941  C CG  . ASP B 221 ? 0.7695 0.8811 0.4648 -0.0298 -0.0839 -0.1144 221 ASP B CG  
5942  O OD1 . ASP B 221 ? 0.9868 1.0864 0.6927 -0.0285 -0.0759 -0.1325 221 ASP B OD1 
5943  O OD2 . ASP B 221 ? 0.7356 0.8595 0.4058 -0.0295 -0.0871 -0.1122 221 ASP B OD2 
5944  N N   . PHE B 222 ? 0.5004 0.5969 0.2613 -0.0309 -0.0762 -0.0657 222 PHE B N   
5945  C CA  . PHE B 222 ? 0.4970 0.5854 0.2752 -0.0310 -0.0772 -0.0424 222 PHE B CA  
5946  C C   . PHE B 222 ? 0.6244 0.7256 0.3808 -0.0319 -0.0763 -0.0210 222 PHE B C   
5947  O O   . PHE B 222 ? 0.6643 0.7648 0.4205 -0.0323 -0.0648 -0.0088 222 PHE B O   
5948  C CB  . PHE B 222 ? 0.4829 0.5565 0.2850 -0.0292 -0.0650 -0.0418 222 PHE B CB  
5949  C CG  . PHE B 222 ? 0.4596 0.5180 0.2889 -0.0282 -0.0681 -0.0533 222 PHE B CG  
5950  C CD1 . PHE B 222 ? 0.4653 0.5197 0.2971 -0.0273 -0.0658 -0.0752 222 PHE B CD1 
5951  C CD2 . PHE B 222 ? 0.4395 0.4870 0.2919 -0.0279 -0.0725 -0.0417 222 PHE B CD2 
5952  C CE1 . PHE B 222 ? 0.4419 0.4817 0.2994 -0.0271 -0.0680 -0.0833 222 PHE B CE1 
5953  C CE2 . PHE B 222 ? 0.4595 0.4954 0.3362 -0.0272 -0.0743 -0.0505 222 PHE B CE2 
5954  C CZ  . PHE B 222 ? 0.4669 0.4990 0.3466 -0.0272 -0.0720 -0.0702 222 PHE B CZ  
5955  N N   . ALA B 223 ? 0.6547 0.7663 0.3958 -0.0319 -0.0884 -0.0156 223 ALA B N   
5956  C CA  . ALA B 223 ? 0.6628 0.7825 0.3863 -0.0309 -0.0874 0.0058  223 ALA B CA  
5957  C C   . ALA B 223 ? 0.6911 0.8018 0.4279 -0.0315 -0.0896 0.0312  223 ALA B C   
5958  O O   . ALA B 223 ? 0.8112 0.9249 0.5374 -0.0304 -0.0890 0.0509  223 ALA B O   
5959  C CB  . ALA B 223 ? 0.6966 0.8254 0.4050 -0.0286 -0.0991 0.0034  223 ALA B CB  
5960  N N   . VAL B 224 ? 0.5655 0.6603 0.3294 -0.0318 -0.0905 0.0304  224 VAL B N   
5961  C CA  . VAL B 224 ? 0.4966 0.5760 0.2781 -0.0309 -0.0908 0.0509  224 VAL B CA  
5962  C C   . VAL B 224 ? 0.3646 0.4289 0.1666 -0.0323 -0.0782 0.0464  224 VAL B C   
5963  O O   . VAL B 224 ? 0.3993 0.4633 0.2078 -0.0322 -0.0723 0.0278  224 VAL B O   
5964  C CB  . VAL B 224 ? 0.4712 0.5446 0.2706 -0.0270 -0.1050 0.0541  224 VAL B CB  
5965  C CG1 . VAL B 224 ? 0.3516 0.4128 0.1785 -0.0261 -0.1037 0.0379  224 VAL B CG1 
5966  C CG2 . VAL B 224 ? 0.5460 0.6085 0.3523 -0.0245 -0.1077 0.0790  224 VAL B CG2 
5967  N N   . SER B 225 ? 0.3922 0.4437 0.2043 -0.0335 -0.0745 0.0638  225 SER B N   
5968  C CA  . SER B 225 ? 0.3513 0.3908 0.1817 -0.0357 -0.0637 0.0610  225 SER B CA  
5969  C C   . SER B 225 ? 0.3162 0.3381 0.1729 -0.0324 -0.0685 0.0588  225 SER B C   
5970  O O   . SER B 225 ? 0.3231 0.3376 0.1855 -0.0292 -0.0776 0.0690  225 SER B O   
5971  C CB  . SER B 225 ? 0.3504 0.3872 0.1763 -0.0411 -0.0556 0.0793  225 SER B CB  
5972  O OG  . SER B 225 ? 0.3304 0.3535 0.1781 -0.0435 -0.0491 0.0781  225 SER B OG  
5973  N N   . PHE B 226 ? 0.3045 0.3213 0.1770 -0.0322 -0.0619 0.0459  226 PHE B N   
5974  C CA  . PHE B 226 ? 0.2911 0.2935 0.1872 -0.0291 -0.0641 0.0430  226 PHE B CA  
5975  C C   . PHE B 226 ? 0.2929 0.2861 0.2005 -0.0322 -0.0553 0.0460  226 PHE B C   
5976  O O   . PHE B 226 ? 0.3046 0.2895 0.2297 -0.0298 -0.0545 0.0397  226 PHE B O   
5977  C CB  . PHE B 226 ? 0.2773 0.2826 0.1836 -0.0259 -0.0656 0.0256  226 PHE B CB  
5978  C CG  . PHE B 226 ? 0.2644 0.2753 0.1688 -0.0235 -0.0769 0.0224  226 PHE B CG  
5979  C CD1 . PHE B 226 ? 0.3333 0.3385 0.2494 -0.0198 -0.0854 0.0307  226 PHE B CD1 
5980  C CD2 . PHE B 226 ? 0.2753 0.2980 0.1670 -0.0247 -0.0793 0.0102  226 PHE B CD2 
5981  C CE1 . PHE B 226 ? 0.3644 0.3786 0.2813 -0.0179 -0.0965 0.0283  226 PHE B CE1 
5982  C CE2 . PHE B 226 ? 0.2936 0.3236 0.1847 -0.0240 -0.0911 0.0064  226 PHE B CE2 
5983  C CZ  . PHE B 226 ? 0.3564 0.3836 0.2610 -0.0208 -0.0999 0.0161  226 PHE B CZ  
5984  N N   . ARG B 227 ? 0.2747 0.2712 0.1727 -0.0380 -0.0489 0.0556  227 ARG B N   
5985  C CA  . ARG B 227 ? 0.2661 0.2570 0.1759 -0.0428 -0.0413 0.0574  227 ARG B CA  
5986  C C   . ARG B 227 ? 0.3316 0.3023 0.2547 -0.0428 -0.0456 0.0653  227 ARG B C   
5987  O O   . ARG B 227 ? 0.3987 0.3623 0.3368 -0.0431 -0.0433 0.0590  227 ARG B O   
5988  C CB  . ARG B 227 ? 0.2818 0.2839 0.1798 -0.0503 -0.0330 0.0665  227 ARG B CB  
5989  C CG  . ARG B 227 ? 0.3915 0.4143 0.2785 -0.0492 -0.0260 0.0559  227 ARG B CG  
5990  C CD  . ARG B 227 ? 0.4976 0.5350 0.3734 -0.0561 -0.0165 0.0659  227 ARG B CD  
5991  N NE  . ARG B 227 ? 0.5944 0.6301 0.4864 -0.0630 -0.0100 0.0704  227 ARG B NE  
5992  C CZ  . ARG B 227 ? 0.6921 0.7398 0.5952 -0.0630 -0.0023 0.0604  227 ARG B CZ  
5993  N NH1 . ARG B 227 ? 0.6641 0.7232 0.5643 -0.0555 0.0008  0.0456  227 ARG B NH1 
5994  N NH2 . ARG B 227 ? 0.7553 0.8033 0.6736 -0.0705 0.0019  0.0654  227 ARG B NH2 
5995  N N   . GLU B 228 ? 0.3741 0.3355 0.2914 -0.0416 -0.0521 0.0786  228 GLU B N   
5996  C CA  . GLU B 228 ? 0.4113 0.3512 0.3416 -0.0398 -0.0560 0.0849  228 GLU B CA  
5997  C C   . GLU B 228 ? 0.5027 0.4379 0.4472 -0.0314 -0.0606 0.0733  228 GLU B C   
5998  O O   . GLU B 228 ? 0.6048 0.5259 0.5628 -0.0300 -0.0600 0.0703  228 GLU B O   
5999  C CB  . GLU B 228 ? 0.5136 0.4448 0.4353 -0.0385 -0.0620 0.1032  228 GLU B CB  
6000  C CG  . GLU B 228 ? 0.5077 0.4461 0.4132 -0.0466 -0.0572 0.1176  228 GLU B CG  
6001  C CD  . GLU B 228 ? 0.7091 0.6431 0.6213 -0.0573 -0.0478 0.1191  228 GLU B CD  
6002  O OE1 . GLU B 228 ? 0.8772 0.7937 0.8059 -0.0587 -0.0476 0.1151  228 GLU B OE1 
6003  O OE2 . GLU B 228 ? 0.7783 0.7283 0.6795 -0.0643 -0.0407 0.1238  228 GLU B OE2 
6004  N N   . ASP B 229 ? 0.3548 0.3024 0.2965 -0.0261 -0.0650 0.0663  229 ASP B N   
6005  C CA  . ASP B 229 ? 0.3657 0.3121 0.3224 -0.0192 -0.0682 0.0561  229 ASP B CA  
6006  C C   . ASP B 229 ? 0.3380 0.2853 0.3046 -0.0206 -0.0610 0.0441  229 ASP B C   
6007  O O   . ASP B 229 ? 0.2973 0.2371 0.2773 -0.0165 -0.0609 0.0398  229 ASP B O   
6008  C CB  . ASP B 229 ? 0.4602 0.4208 0.4130 -0.0158 -0.0744 0.0509  229 ASP B CB  
6009  C CG  . ASP B 229 ? 0.5677 0.5310 0.5113 -0.0133 -0.0833 0.0631  229 ASP B CG  
6010  O OD1 . ASP B 229 ? 0.8775 0.8394 0.8069 -0.0170 -0.0824 0.0749  229 ASP B OD1 
6011  O OD2 . ASP B 229 ? 0.4735 0.4419 0.4248 -0.0077 -0.0913 0.0619  229 ASP B OD2 
6012  N N   . ALA B 230 ? 0.3105 0.2686 0.2704 -0.0254 -0.0547 0.0391  230 ALA B N   
6013  C CA  . ALA B 230 ? 0.2315 0.1927 0.2010 -0.0259 -0.0483 0.0295  230 ALA B CA  
6014  C C   . ALA B 230 ? 0.2300 0.1811 0.2068 -0.0293 -0.0458 0.0325  230 ALA B C   
6015  O O   . ALA B 230 ? 0.1888 0.1395 0.1760 -0.0274 -0.0437 0.0253  230 ALA B O   
6016  C CB  . ALA B 230 ? 0.2688 0.2447 0.2306 -0.0290 -0.0418 0.0246  230 ALA B CB  
6017  N N   . SER B 231 ? 0.3969 0.3396 0.3680 -0.0350 -0.0461 0.0430  231 SER B N   
6018  C CA  . SER B 231 ? 0.2895 0.2192 0.2683 -0.0397 -0.0449 0.0449  231 SER B CA  
6019  C C   . SER B 231 ? 0.3439 0.2557 0.3307 -0.0330 -0.0501 0.0445  231 SER B C   
6020  O O   . SER B 231 ? 0.4233 0.3271 0.4188 -0.0332 -0.0492 0.0380  231 SER B O   
6021  C CB  . SER B 231 ? 0.2490 0.1744 0.2209 -0.0493 -0.0427 0.0573  231 SER B CB  
6022  O OG  . SER B 231 ? 0.4728 0.3873 0.4537 -0.0565 -0.0409 0.0568  231 SER B OG  
6023  N N   . LYS B 232 ? 0.3098 0.2170 0.2939 -0.0266 -0.0557 0.0507  232 LYS B N   
6024  C CA  . LYS B 232 ? 0.2384 0.1314 0.2319 -0.0182 -0.0600 0.0502  232 LYS B CA  
6025  C C   . LYS B 232 ? 0.3398 0.2402 0.3432 -0.0119 -0.0585 0.0375  232 LYS B C   
6026  O O   . LYS B 232 ? 0.2956 0.1855 0.3072 -0.0075 -0.0582 0.0326  232 LYS B O   
6027  C CB  . LYS B 232 ? 0.2567 0.1491 0.2470 -0.0117 -0.0668 0.0601  232 LYS B CB  
6028  C CG  . LYS B 232 ? 0.3965 0.2757 0.3795 -0.0151 -0.0690 0.0759  232 LYS B CG  
6029  C CD  . LYS B 232 ? 0.4670 0.3488 0.4472 -0.0070 -0.0769 0.0864  232 LYS B CD  
6030  C CE  . LYS B 232 ? 0.4930 0.3647 0.4883 0.0047  -0.0807 0.0844  232 LYS B CE  
6031  N NZ  . LYS B 232 ? 0.5096 0.3539 0.5105 0.0065  -0.0802 0.0916  232 LYS B NZ  
6032  N N   . HIS B 233 ? 0.3404 0.2583 0.3427 -0.0114 -0.0571 0.0320  233 HIS B N   
6033  C CA  . HIS B 233 ? 0.2439 0.1694 0.2559 -0.0061 -0.0550 0.0225  233 HIS B CA  
6034  C C   . HIS B 233 ? 0.2417 0.1650 0.2572 -0.0083 -0.0503 0.0159  233 HIS B C   
6035  O O   . HIS B 233 ? 0.2827 0.2040 0.3055 -0.0026 -0.0495 0.0105  233 HIS B O   
6036  C CB  . HIS B 233 ? 0.2546 0.1960 0.2652 -0.0067 -0.0537 0.0185  233 HIS B CB  
6037  C CG  . HIS B 233 ? 0.2154 0.1621 0.2284 -0.0025 -0.0593 0.0200  233 HIS B CG  
6038  N ND1 . HIS B 233 ? 0.2114 0.1595 0.2370 0.0044  -0.0614 0.0185  233 HIS B ND1 
6039  C CD2 . HIS B 233 ? 0.1792 0.1324 0.1838 -0.0046 -0.0635 0.0224  233 HIS B CD2 
6040  C CE1 . HIS B 233 ? 0.2376 0.1934 0.2647 0.0055  -0.0672 0.0202  233 HIS B CE1 
6041  N NE2 . HIS B 233 ? 0.2167 0.1753 0.2302 0.0001  -0.0691 0.0220  233 HIS B NE2 
6042  N N   . VAL B 234 ? 0.2566 0.1827 0.2670 -0.0167 -0.0472 0.0161  234 VAL B N   
6043  C CA  . VAL B 234 ? 0.3018 0.2297 0.3159 -0.0199 -0.0440 0.0094  234 VAL B CA  
6044  C C   . VAL B 234 ? 0.3083 0.2179 0.3238 -0.0225 -0.0460 0.0089  234 VAL B C   
6045  O O   . VAL B 234 ? 0.3606 0.2701 0.3792 -0.0237 -0.0449 0.0010  234 VAL B O   
6046  C CB  . VAL B 234 ? 0.2397 0.1811 0.2510 -0.0278 -0.0400 0.0096  234 VAL B CB  
6047  C CG1 . VAL B 234 ? 0.2794 0.2366 0.2905 -0.0238 -0.0373 0.0075  234 VAL B CG1 
6048  C CG2 . VAL B 234 ? 0.3361 0.2719 0.3408 -0.0364 -0.0401 0.0183  234 VAL B CG2 
6049  N N   . GLU B 235 ? 0.3396 0.2329 0.3527 -0.0231 -0.0490 0.0170  235 GLU B N   
6050  C CA  . GLU B 235 ? 0.3691 0.2402 0.3850 -0.0247 -0.0508 0.0162  235 GLU B CA  
6051  C C   . GLU B 235 ? 0.3112 0.1722 0.3325 -0.0125 -0.0527 0.0117  235 GLU B C   
6052  O O   . GLU B 235 ? 0.4395 0.2892 0.4641 -0.0109 -0.0522 0.0027  235 GLU B O   
6053  C CB  . GLU B 235 ? 0.4012 0.2575 0.4131 -0.0313 -0.0524 0.0291  235 GLU B CB  
6054  C CG  . GLU B 235 ? 0.4436 0.3108 0.4511 -0.0442 -0.0491 0.0339  235 GLU B CG  
6055  C CD  . GLU B 235 ? 0.6396 0.4939 0.6425 -0.0512 -0.0498 0.0491  235 GLU B CD  
6056  O OE1 . GLU B 235 ? 0.7811 0.6267 0.7804 -0.0443 -0.0533 0.0585  235 GLU B OE1 
6057  O OE2 . GLU B 235 ? 0.7370 0.5918 0.7406 -0.0638 -0.0467 0.0527  235 GLU B OE2 
6058  N N   . LEU B 236 ? 0.2288 0.0953 0.2517 -0.0037 -0.0548 0.0170  236 LEU B N   
6059  C CA  . LEU B 236 ? 0.2487 0.1113 0.2794 0.0087  -0.0556 0.0130  236 LEU B CA  
6060  C C   . LEU B 236 ? 0.2228 0.0998 0.2568 0.0127  -0.0515 0.0017  236 LEU B C   
6061  O O   . LEU B 236 ? 0.2632 0.1354 0.3019 0.0211  -0.0501 -0.0051 236 LEU B O   
6062  C CB  . LEU B 236 ? 0.2403 0.1101 0.2740 0.0159  -0.0595 0.0219  236 LEU B CB  
6063  C CG  . LEU B 236 ? 0.2456 0.1031 0.2750 0.0142  -0.0643 0.0354  236 LEU B CG  
6064  C CD1 . LEU B 236 ? 0.2617 0.1333 0.2928 0.0201  -0.0694 0.0430  236 LEU B CD1 
6065  C CD2 . LEU B 236 ? 0.2703 0.1017 0.3044 0.0191  -0.0652 0.0372  236 LEU B CD2 
6066  N N   . ALA B 237 ? 0.1954 0.0904 0.2267 0.0077  -0.0492 0.0000  237 ALA B N   
6067  C CA  . ALA B 237 ? 0.1823 0.0913 0.2159 0.0109  -0.0452 -0.0083 237 ALA B CA  
6068  C C   . ALA B 237 ? 0.2837 0.1857 0.3141 0.0080  -0.0441 -0.0177 237 ALA B C   
6069  O O   . ALA B 237 ? 0.3037 0.2099 0.3352 0.0147  -0.0418 -0.0255 237 ALA B O   
6070  C CB  . ALA B 237 ? 0.1719 0.0989 0.2042 0.0065  -0.0431 -0.0068 237 ALA B CB  
6071  N N   . LYS B 238 ? 0.3396 0.2326 0.3660 -0.0025 -0.0457 -0.0172 238 LYS B N   
6072  C CA  . LYS B 238 ? 0.2357 0.1212 0.2601 -0.0075 -0.0460 -0.0273 238 LYS B CA  
6073  C C   . LYS B 238 ? 0.2779 0.1423 0.3038 -0.0003 -0.0469 -0.0338 238 LYS B C   
6074  O O   . LYS B 238 ? 0.4297 0.2939 0.4534 0.0025  -0.0459 -0.0461 238 LYS B O   
6075  C CB  . LYS B 238 ? 0.2270 0.1064 0.2500 -0.0217 -0.0476 -0.0239 238 LYS B CB  
6076  C CG  . LYS B 238 ? 0.2102 0.1134 0.2326 -0.0288 -0.0458 -0.0224 238 LYS B CG  
6077  C CD  . LYS B 238 ? 0.2708 0.1703 0.2941 -0.0433 -0.0467 -0.0192 238 LYS B CD  
6078  C CE  . LYS B 238 ? 0.3877 0.2862 0.4128 -0.0508 -0.0489 -0.0308 238 LYS B CE  
6079  N NZ  . LYS B 238 ? 0.4133 0.3100 0.4424 -0.0668 -0.0496 -0.0271 238 LYS B NZ  
6080  N N   . GLU B 239 ? 0.3100 0.1571 0.3391 0.0038  -0.0487 -0.0257 239 GLU B N   
6081  C CA  . GLU B 239 ? 0.3376 0.1628 0.3700 0.0125  -0.0491 -0.0310 239 GLU B CA  
6082  C C   . GLU B 239 ? 0.3571 0.1947 0.3921 0.0266  -0.0456 -0.0383 239 GLU B C   
6083  O O   . GLU B 239 ? 0.3908 0.2204 0.4243 0.0320  -0.0437 -0.0511 239 GLU B O   
6084  C CB  . GLU B 239 ? 0.2971 0.1050 0.3335 0.0155  -0.0520 -0.0176 239 GLU B CB  
6085  C CG  . GLU B 239 ? 0.5030 0.2917 0.5416 0.0224  -0.0493 -0.0204 239 GLU B CG  
6086  C CD  . GLU B 239 ? 0.8969 0.6679 0.9353 0.0175  -0.0504 -0.0074 239 GLU B CD  
6087  O OE1 . GLU B 239 ? 0.9573 0.7068 0.9960 0.0168  -0.0480 -0.0110 239 GLU B OE1 
6088  O OE2 . GLU B 239 ? 1.0099 0.7882 1.0474 0.0144  -0.0534 0.0065  239 GLU B OE2 
6089  N N   . LYS B 240 ? 0.3074 0.1652 0.3464 0.0322  -0.0443 -0.0306 240 LYS B N   
6090  C CA  . LYS B 240 ? 0.2909 0.1631 0.3346 0.0447  -0.0401 -0.0350 240 LYS B CA  
6091  C C   . LYS B 240 ? 0.3250 0.2104 0.3618 0.0441  -0.0362 -0.0466 240 LYS B C   
6092  O O   . LYS B 240 ? 0.3868 0.2746 0.4232 0.0539  -0.0323 -0.0556 240 LYS B O   
6093  C CB  . LYS B 240 ? 0.2663 0.1584 0.3171 0.0473  -0.0401 -0.0243 240 LYS B CB  
6094  C CG  . LYS B 240 ? 0.2045 0.1136 0.2634 0.0590  -0.0352 -0.0260 240 LYS B CG  
6095  C CD  . LYS B 240 ? 0.3099 0.2083 0.3773 0.0713  -0.0351 -0.0265 240 LYS B CD  
6096  C CE  . LYS B 240 ? 0.3366 0.2536 0.4117 0.0832  -0.0283 -0.0301 240 LYS B CE  
6097  N NZ  . LYS B 240 ? 0.4300 0.3464 0.5143 0.0930  -0.0263 -0.0255 240 LYS B NZ  
6098  N N   . TYR B 241 ? 0.2771 0.1729 0.3082 0.0334  -0.0372 -0.0463 241 TYR B N   
6099  C CA  . TYR B 241 ? 0.2202 0.1304 0.2440 0.0323  -0.0349 -0.0560 241 TYR B CA  
6100  C C   . TYR B 241 ? 0.3251 0.2188 0.3423 0.0313  -0.0363 -0.0709 241 TYR B C   
6101  O O   . TYR B 241 ? 0.2865 0.1900 0.2969 0.0363  -0.0337 -0.0819 241 TYR B O   
6102  C CB  . TYR B 241 ? 0.2455 0.1694 0.2668 0.0214  -0.0365 -0.0514 241 TYR B CB  
6103  C CG  . TYR B 241 ? 0.3008 0.2451 0.3157 0.0206  -0.0351 -0.0578 241 TYR B CG  
6104  C CD1 . TYR B 241 ? 0.2863 0.2284 0.2945 0.0129  -0.0385 -0.0685 241 TYR B CD1 
6105  C CD2 . TYR B 241 ? 0.2028 0.1693 0.2192 0.0270  -0.0310 -0.0522 241 TYR B CD2 
6106  C CE1 . TYR B 241 ? 0.2347 0.1988 0.2366 0.0125  -0.0384 -0.0735 241 TYR B CE1 
6107  C CE2 . TYR B 241 ? 0.2216 0.2080 0.2317 0.0272  -0.0300 -0.0555 241 TYR B CE2 
6108  C CZ  . TYR B 241 ? 0.2035 0.1899 0.2057 0.0204  -0.0341 -0.0663 241 TYR B CZ  
6109  O OH  . TYR B 241 ? 0.2167 0.2261 0.2122 0.0210  -0.0344 -0.0691 241 TYR B OH  
6110  N N   . PHE B 242 ? 0.3063 0.1744 0.3249 0.0244  -0.0402 -0.0715 242 PHE B N   
6111  C CA  . PHE B 242 ? 0.2930 0.1395 0.3073 0.0229  -0.0418 -0.0865 242 PHE B CA  
6112  C C   . PHE B 242 ? 0.3092 0.1456 0.3248 0.0387  -0.0380 -0.0944 242 PHE B C   
6113  O O   . PHE B 242 ? 0.3357 0.1648 0.3444 0.0415  -0.0369 -0.1109 242 PHE B O   
6114  C CB  . PHE B 242 ? 0.4441 0.2636 0.4622 0.0113  -0.0464 -0.0821 242 PHE B CB  
6115  C CG  . PHE B 242 ? 0.4618 0.2614 0.4758 0.0052  -0.0468 -0.0953 242 PHE B CG  
6116  C CD1 . PHE B 242 ? 0.3831 0.1618 0.3979 0.0136  -0.0430 -0.0981 242 PHE B CD1 
6117  C CD2 . PHE B 242 ? 0.4343 0.2392 0.4441 -0.0095 -0.0501 -0.1034 242 PHE B CD2 
6118  C CE1 . PHE B 242 ? 0.4011 0.1607 0.4112 0.0075  -0.0422 -0.1099 242 PHE B CE1 
6119  C CE2 . PHE B 242 ? 0.3850 0.1733 0.3906 -0.0166 -0.0499 -0.1147 242 PHE B CE2 
6120  C CZ  . PHE B 242 ? 0.4075 0.1712 0.4126 -0.0082 -0.0459 -0.1185 242 PHE B CZ  
6121  N N   . GLU B 243 ? 0.3467 0.1845 0.3713 0.0493  -0.0357 -0.0831 243 GLU B N   
6122  C CA  . GLU B 243 ? 0.3716 0.2063 0.3998 0.0650  -0.0304 -0.0878 243 GLU B CA  
6123  C C   . GLU B 243 ? 0.3644 0.2238 0.3871 0.0743  -0.0248 -0.0976 243 GLU B C   
6124  O O   . GLU B 243 ? 0.3253 0.1832 0.3451 0.0845  -0.0193 -0.1075 243 GLU B O   
6125  C CB  . GLU B 243 ? 0.3698 0.2071 0.4103 0.0720  -0.0298 -0.0710 243 GLU B CB  
6126  C CG  . GLU B 243 ? 0.4664 0.3111 0.5134 0.0878  -0.0230 -0.0715 243 GLU B CG  
6127  C CD  . GLU B 243 ? 0.4977 0.3546 0.5577 0.0931  -0.0234 -0.0548 243 GLU B CD  
6128  O OE1 . GLU B 243 ? 0.5266 0.3798 0.5886 0.0849  -0.0294 -0.0432 243 GLU B OE1 
6129  O OE2 . GLU B 243 ? 0.3482 0.2205 0.4163 0.1048  -0.0177 -0.0533 243 GLU B OE2 
6130  N N   . ILE B 244 ? 0.4040 0.2904 0.4235 0.0687  -0.0241 -0.0911 244 ILE B N   
6131  C CA  . ILE B 244 ? 0.3641 0.2782 0.3785 0.0765  -0.0177 -0.0944 244 ILE B CA  
6132  C C   . ILE B 244 ? 0.3787 0.3029 0.3774 0.0701  -0.0188 -0.1065 244 ILE B C   
6133  O O   . ILE B 244 ? 0.3640 0.3078 0.3544 0.0781  -0.0134 -0.1130 244 ILE B O   
6134  C CB  . ILE B 244 ? 0.3643 0.3023 0.3875 0.0766  -0.0154 -0.0774 244 ILE B CB  
6135  C CG1 . ILE B 244 ? 0.2524 0.1806 0.2905 0.0788  -0.0175 -0.0654 244 ILE B CG1 
6136  C CG2 . ILE B 244 ? 0.3910 0.3555 0.4134 0.0871  -0.0071 -0.0773 244 ILE B CG2 
6137  C CD1 . ILE B 244 ? 0.3507 0.2836 0.3993 0.0939  -0.0121 -0.0650 244 ILE B CD1 
6138  N N   . PHE B 245 ? 0.3985 0.3125 0.3931 0.0560  -0.0257 -0.1094 245 PHE B N   
6139  C CA  . PHE B 245 ? 0.3141 0.2429 0.2959 0.0489  -0.0283 -0.1192 245 PHE B CA  
6140  C C   . PHE B 245 ? 0.3307 0.2369 0.3071 0.0385  -0.0346 -0.1351 245 PHE B C   
6141  O O   . PHE B 245 ? 0.3867 0.3056 0.3541 0.0300  -0.0389 -0.1436 245 PHE B O   
6142  C CB  . PHE B 245 ? 0.2799 0.2301 0.2645 0.0404  -0.0303 -0.1053 245 PHE B CB  
6143  C CG  . PHE B 245 ? 0.3716 0.3448 0.3607 0.0493  -0.0241 -0.0917 245 PHE B CG  
6144  C CD1 . PHE B 245 ? 0.3552 0.3531 0.3355 0.0567  -0.0195 -0.0937 245 PHE B CD1 
6145  C CD2 . PHE B 245 ? 0.3103 0.2804 0.3124 0.0497  -0.0229 -0.0768 245 PHE B CD2 
6146  C CE1 . PHE B 245 ? 0.2436 0.2611 0.2299 0.0637  -0.0133 -0.0797 245 PHE B CE1 
6147  C CE2 . PHE B 245 ? 0.2268 0.2163 0.2351 0.0562  -0.0176 -0.0652 245 PHE B CE2 
6148  C CZ  . PHE B 245 ? 0.2323 0.2445 0.2337 0.0629  -0.0124 -0.0659 245 PHE B CZ  
6149  N N   . GLY B 246 ? 0.2057 0.1652 0.3606 -0.0128 0.0934  -0.0318 246 GLY B N   
6150  C CA  . GLY B 246 ? 0.2246 0.1805 0.3830 -0.0172 0.1019  -0.0398 246 GLY B CA  
6151  C C   . GLY B 246 ? 0.2614 0.2202 0.4178 -0.0214 0.1020  -0.0463 246 GLY B C   
6152  O O   . GLY B 246 ? 0.2542 0.2113 0.4125 -0.0267 0.1093  -0.0548 246 GLY B O   
6153  N N   . GLU B 247 ? 0.3498 0.3132 0.5032 -0.0195 0.0946  -0.0427 247 GLU B N   
6154  C CA  . GLU B 247 ? 0.3422 0.3092 0.4939 -0.0236 0.0944  -0.0485 247 GLU B CA  
6155  C C   . GLU B 247 ? 0.2592 0.2315 0.4085 -0.0205 0.0850  -0.0395 247 GLU B C   
6156  O O   . GLU B 247 ? 0.2084 0.1798 0.3584 -0.0150 0.0807  -0.0323 247 GLU B O   
6157  C CB  . GLU B 247 ? 0.3228 0.2950 0.4632 -0.0304 0.0939  -0.0574 247 GLU B CB  
6158  C CG  . GLU B 247 ? 0.3513 0.3272 0.4824 -0.0288 0.0864  -0.0545 247 GLU B CG  
6159  C CD  . GLU B 247 ? 0.5507 0.5317 0.6726 -0.0354 0.0870  -0.0625 247 GLU B CD  
6160  O OE1 . GLU B 247 ? 0.6515 0.6317 0.7739 -0.0409 0.0944  -0.0711 247 GLU B OE1 
6161  O OE2 . GLU B 247 ? 0.6401 0.6268 0.7547 -0.0356 0.0804  -0.0600 247 GLU B OE2 
6162  N N   . HIS B 248 ? 0.3110 0.2900 0.4577 -0.0249 0.0823  -0.0402 248 HIS B N   
6163  C CA  . HIS B 248 ? 0.2314 0.2156 0.3754 -0.0234 0.0748  -0.0329 248 HIS B CA  
6164  C C   . HIS B 248 ? 0.1866 0.1753 0.3199 -0.0239 0.0685  -0.0339 248 HIS B C   
6165  O O   . HIS B 248 ? 0.2449 0.2354 0.3728 -0.0272 0.0695  -0.0404 248 HIS B O   
6166  C CB  . HIS B 248 ? 0.2899 0.2803 0.4363 -0.0285 0.0752  -0.0329 248 HIS B CB  
6167  C CG  . HIS B 248 ? 0.3494 0.3378 0.5064 -0.0264 0.0776  -0.0260 248 HIS B CG  
6168  N ND1 . HIS B 248 ? 0.4151 0.4099 0.5756 -0.0311 0.0779  -0.0236 248 HIS B ND1 
6169  C CD2 . HIS B 248 ? 0.3506 0.3328 0.5165 -0.0204 0.0796  -0.0199 248 HIS B CD2 
6170  C CE1 . HIS B 248 ? 0.4349 0.4270 0.6055 -0.0281 0.0799  -0.0163 248 HIS B CE1 
6171  N NE2 . HIS B 248 ? 0.4326 0.4171 0.6072 -0.0213 0.0810  -0.0139 248 HIS B NE2 
6172  N N   . PRO B 249 ? 0.2335 0.2245 0.3641 -0.0209 0.0623  -0.0273 249 PRO B N   
6173  C CA  . PRO B 249 ? 0.1798 0.1747 0.3017 -0.0214 0.0570  -0.0279 249 PRO B CA  
6174  C C   . PRO B 249 ? 0.1205 0.1234 0.2391 -0.0265 0.0555  -0.0312 249 PRO B C   
6175  O O   . PRO B 249 ? 0.1684 0.1749 0.2901 -0.0289 0.0562  -0.0298 249 PRO B O   
6176  C CB  . PRO B 249 ? 0.1337 0.1276 0.2555 -0.0167 0.0520  -0.0196 249 PRO B CB  
6177  C CG  . PRO B 249 ? 0.1217 0.1159 0.2500 -0.0163 0.0531  -0.0149 249 PRO B CG  
6178  C CD  . PRO B 249 ? 0.2550 0.2456 0.3906 -0.0174 0.0599  -0.0186 249 PRO B CD  
6179  N N   . VAL B 250 ? 0.0875 0.0948 0.2006 -0.0285 0.0534  -0.0349 250 VAL B N   
6180  C CA  . VAL B 250 ? 0.1051 0.1219 0.2163 -0.0325 0.0512  -0.0371 250 VAL B CA  
6181  C C   . VAL B 250 ? 0.1595 0.1777 0.2667 -0.0299 0.0462  -0.0343 250 VAL B C   
6182  O O   . VAL B 250 ? 0.1527 0.1790 0.2595 -0.0323 0.0444  -0.0356 250 VAL B O   
6183  C CB  . VAL B 250 ? 0.0983 0.1232 0.2095 -0.0383 0.0533  -0.0442 250 VAL B CB  
6184  C CG1 . VAL B 250 ? 0.1274 0.1546 0.2439 -0.0429 0.0582  -0.0473 250 VAL B CG1 
6185  C CG2 . VAL B 250 ? 0.1173 0.1388 0.2254 -0.0378 0.0540  -0.0466 250 VAL B CG2 
6186  N N   . TYR B 251 ? 0.1510 0.1625 0.2562 -0.0252 0.0440  -0.0303 251 TYR B N   
6187  C CA  . TYR B 251 ? 0.1493 0.1609 0.2518 -0.0227 0.0397  -0.0270 251 TYR B CA  
6188  C C   . TYR B 251 ? 0.1397 0.1461 0.2428 -0.0187 0.0380  -0.0206 251 TYR B C   
6189  O O   . TYR B 251 ? 0.1528 0.1548 0.2583 -0.0162 0.0389  -0.0175 251 TYR B O   
6190  C CB  . TYR B 251 ? 0.1594 0.1709 0.2598 -0.0220 0.0380  -0.0270 251 TYR B CB  
6191  C CG  . TYR B 251 ? 0.1721 0.1899 0.2723 -0.0267 0.0399  -0.0326 251 TYR B CG  
6192  C CD1 . TYR B 251 ? 0.2787 0.3066 0.3804 -0.0309 0.0399  -0.0368 251 TYR B CD1 
6193  C CD2 . TYR B 251 ? 0.1735 0.1893 0.2727 -0.0276 0.0419  -0.0338 251 TYR B CD2 
6194  C CE1 . TYR B 251 ? 0.2983 0.3349 0.4007 -0.0359 0.0413  -0.0416 251 TYR B CE1 
6195  C CE2 . TYR B 251 ? 0.2179 0.2409 0.3165 -0.0329 0.0437  -0.0394 251 TYR B CE2 
6196  C CZ  . TYR B 251 ? 0.2045 0.2384 0.3049 -0.0371 0.0432  -0.0431 251 TYR B CZ  
6197  O OH  . TYR B 251 ? 0.2459 0.2896 0.3464 -0.0429 0.0446  -0.0484 251 TYR B OH  
6198  N N   . MET B 252 ? 0.0960 0.1045 0.1978 -0.0186 0.0356  -0.0188 252 MET B N   
6199  C CA  . MET B 252 ? 0.1089 0.1155 0.2108 -0.0164 0.0332  -0.0127 252 MET B CA  
6200  C C   . MET B 252 ? 0.1138 0.1205 0.2136 -0.0152 0.0299  -0.0115 252 MET B C   
6201  O O   . MET B 252 ? 0.0826 0.0919 0.1818 -0.0165 0.0299  -0.0156 252 MET B O   
6202  C CB  . MET B 252 ? 0.1040 0.1145 0.2064 -0.0193 0.0340  -0.0116 252 MET B CB  
6203  C CG  . MET B 252 ? 0.2240 0.2338 0.3283 -0.0182 0.0325  -0.0046 252 MET B CG  
6204  S SD  . MET B 252 ? 0.3306 0.3444 0.4391 -0.0215 0.0351  -0.0027 252 MET B SD  
6205  C CE  . MET B 252 ? 0.0709 0.0783 0.1865 -0.0179 0.0384  -0.0021 252 MET B CE  
6206  N N   . TRP B 253 ? 0.2100 0.2149 0.3099 -0.0131 0.0270  -0.0056 253 TRP B N   
6207  C CA  . TRP B 253 ? 0.1671 0.1726 0.2660 -0.0129 0.0239  -0.0039 253 TRP B CA  
6208  C C   . TRP B 253 ? 0.1700 0.1782 0.2671 -0.0156 0.0226  -0.0012 253 TRP B C   
6209  O O   . TRP B 253 ? 0.1779 0.1867 0.2754 -0.0160 0.0207  0.0043  253 TRP B O   
6210  C CB  . TRP B 253 ? 0.1197 0.1237 0.2198 -0.0108 0.0207  0.0010  253 TRP B CB  
6211  C CG  . TRP B 253 ? 0.1599 0.1648 0.2595 -0.0120 0.0168  0.0043  253 TRP B CG  
6212  C CD1 . TRP B 253 ? 0.1260 0.1321 0.2248 -0.0139 0.0132  0.0102  253 TRP B CD1 
6213  C CD2 . TRP B 253 ? 0.1159 0.1207 0.2166 -0.0123 0.0160  0.0015  253 TRP B CD2 
6214  N NE1 . TRP B 253 ? 0.1676 0.1736 0.2654 -0.0166 0.0102  0.0109  253 TRP B NE1 
6215  C CE2 . TRP B 253 ? 0.1009 0.1060 0.2008 -0.0150 0.0120  0.0056  253 TRP B CE2 
6216  C CE3 . TRP B 253 ? 0.1567 0.1614 0.2597 -0.0112 0.0180  -0.0042 253 TRP B CE3 
6217  C CZ2 . TRP B 253 ? 0.0709 0.0749 0.1727 -0.0163 0.0103  0.0040  253 TRP B CZ2 
6218  C CZ3 . TRP B 253 ? 0.1477 0.1523 0.2544 -0.0112 0.0164  -0.0055 253 TRP B CZ3 
6219  C CH2 . TRP B 253 ? 0.0774 0.0814 0.1839 -0.0135 0.0127  -0.0015 253 TRP B CH2 
6220  N N   . PRO B 254 ? 0.1063 0.1174 0.2020 -0.0182 0.0234  -0.0049 254 PRO B N   
6221  C CA  . PRO B 254 ? 0.0810 0.0961 0.1739 -0.0225 0.0223  -0.0025 254 PRO B CA  
6222  C C   . PRO B 254 ? 0.1201 0.1343 0.2110 -0.0243 0.0181  0.0027  254 PRO B C   
6223  O O   . PRO B 254 ? 0.1625 0.1741 0.2546 -0.0230 0.0165  0.0021  254 PRO B O   
6224  C CB  . PRO B 254 ? 0.1549 0.1736 0.2478 -0.0246 0.0245  -0.0089 254 PRO B CB  
6225  C CG  . PRO B 254 ? 0.1205 0.1361 0.2168 -0.0210 0.0254  -0.0136 254 PRO B CG  
6226  C CD  . PRO B 254 ? 0.0803 0.0918 0.1775 -0.0177 0.0249  -0.0112 254 PRO B CD  
6227  N N   . PRO B 255 ? 0.1095 0.1264 0.1980 -0.0280 0.0160  0.0080  255 PRO B N   
6228  C CA  . PRO B 255 ? 0.1441 0.1600 0.2300 -0.0314 0.0117  0.0127  255 PRO B CA  
6229  C C   . PRO B 255 ? 0.1690 0.1837 0.2507 -0.0363 0.0107  0.0097  255 PRO B C   
6230  O O   . PRO B 255 ? 0.1813 0.1994 0.2607 -0.0400 0.0123  0.0062  255 PRO B O   
6231  C CB  . PRO B 255 ? 0.0698 0.0895 0.1540 -0.0355 0.0107  0.0173  255 PRO B CB  
6232  C CG  . PRO B 255 ? 0.0970 0.1181 0.1860 -0.0313 0.0137  0.0173  255 PRO B CG  
6233  C CD  . PRO B 255 ? 0.1300 0.1506 0.2189 -0.0296 0.0173  0.0102  255 PRO B CD  
6234  N N   . GLU B 256 ? 0.1460 0.1561 0.2279 -0.0365 0.0076  0.0114  256 GLU B N   
6235  C CA  . GLU B 256 ? 0.1490 0.1547 0.2279 -0.0412 0.0060  0.0086  256 GLU B CA  
6236  C C   . GLU B 256 ? 0.1550 0.1616 0.2400 -0.0366 0.0092  0.0021  256 GLU B C   
6237  O O   . GLU B 256 ? 0.1936 0.1977 0.2781 -0.0402 0.0087  -0.0018 256 GLU B O   
6238  C CB  . GLU B 256 ? 0.2206 0.2253 0.2902 -0.0518 0.0053  0.0081  256 GLU B CB  
6239  C CG  . GLU B 256 ? 0.2459 0.2498 0.3152 -0.0542 0.0035  0.0133  256 GLU B CG  
6240  C CD  . GLU B 256 ? 0.3696 0.3670 0.4407 -0.0534 -0.0021 0.0183  256 GLU B CD  
6241  O OE1 . GLU B 256 ? 0.3288 0.3180 0.3975 -0.0560 -0.0030 0.0150  256 GLU B OE1 
6242  O OE2 . GLU B 256 ? 0.4154 0.4160 0.4901 -0.0506 -0.0062 0.0259  256 GLU B OE2 
6243  N N   . ALA B 257 ? 0.1399 0.1487 0.2310 -0.0291 0.0126  -0.0003 257 ALA B N   
6244  C CA  . ALA B 257 ? 0.0835 0.0936 0.1806 -0.0248 0.0168  -0.0079 257 ALA B CA  
6245  C C   . ALA B 257 ? 0.1261 0.1409 0.2222 -0.0281 0.0199  -0.0134 257 ALA B C   
6246  O O   . ALA B 257 ? 0.1243 0.1410 0.2258 -0.0261 0.0227  -0.0212 257 ALA B O   
6247  C CB  . ALA B 257 ? 0.1073 0.1140 0.2107 -0.0225 0.0149  -0.0098 257 ALA B CB  
6248  N N   . SER B 258 ? 0.1598 0.1780 0.2498 -0.0333 0.0190  -0.0095 258 SER B N   
6249  C CA  . SER B 258 ? 0.1342 0.1585 0.2231 -0.0375 0.0213  -0.0135 258 SER B CA  
6250  C C   . SER B 258 ? 0.1713 0.2012 0.2630 -0.0347 0.0259  -0.0190 258 SER B C   
6251  O O   . SER B 258 ? 0.1172 0.1474 0.2081 -0.0334 0.0261  -0.0156 258 SER B O   
6252  C CB  . SER B 258 ? 0.1898 0.2174 0.2721 -0.0450 0.0177  -0.0056 258 SER B CB  
6253  O OG  . SER B 258 ? 0.3216 0.3491 0.4012 -0.0444 0.0158  0.0011  258 SER B OG  
6254  N N   . VAL B 259 ? 0.2334 0.2686 0.3287 -0.0348 0.0293  -0.0278 259 VAL B N   
6255  C CA  . VAL B 259 ? 0.1801 0.2236 0.2777 -0.0344 0.0324  -0.0327 259 VAL B CA  
6256  C C   . VAL B 259 ? 0.1611 0.2160 0.2591 -0.0384 0.0349  -0.0381 259 VAL B C   
6257  O O   . VAL B 259 ? 0.1427 0.1974 0.2402 -0.0404 0.0351  -0.0413 259 VAL B O   
6258  C CB  . VAL B 259 ? 0.0770 0.1203 0.1810 -0.0302 0.0331  -0.0388 259 VAL B CB  
6259  C CG1 . VAL B 259 ? 0.1392 0.1723 0.2427 -0.0264 0.0309  -0.0338 259 VAL B CG1 
6260  C CG2 . VAL B 259 ? 0.0692 0.1146 0.1796 -0.0287 0.0334  -0.0468 259 VAL B CG2 
6261  N N   . SER B 260 ? 0.1036 0.1697 0.2029 -0.0399 0.0369  -0.0388 260 SER B N   
6262  C CA  . SER B 260 ? 0.1522 0.2342 0.2540 -0.0423 0.0399  -0.0449 260 SER B CA  
6263  C C   . SER B 260 ? 0.1648 0.2587 0.2711 -0.0421 0.0414  -0.0446 260 SER B C   
6264  O O   . SER B 260 ? 0.1964 0.2845 0.3024 -0.0413 0.0402  -0.0398 260 SER B O   
6265  C CB  . SER B 260 ? 0.2079 0.2939 0.3043 -0.0477 0.0403  -0.0411 260 SER B CB  
6266  O OG  . SER B 260 ? 0.2984 0.3839 0.3929 -0.0497 0.0388  -0.0308 260 SER B OG  
6267  N N   . ASN B 261 ? 0.1007 0.2132 0.2119 -0.0424 0.0442  -0.0500 261 ASN B N   
6268  C CA  . ASN B 261 ? 0.0915 0.2187 0.2081 -0.0427 0.0460  -0.0487 261 ASN B CA  
6269  C C   . ASN B 261 ? 0.0921 0.2156 0.2057 -0.0466 0.0459  -0.0395 261 ASN B C   
6270  O O   . ASN B 261 ? 0.1316 0.2530 0.2476 -0.0466 0.0454  -0.0362 261 ASN B O   
6271  C CB  . ASN B 261 ? 0.1967 0.3473 0.3190 -0.0418 0.0498  -0.0541 261 ASN B CB  
6272  C CG  . ASN B 261 ? 0.1372 0.2958 0.2660 -0.0352 0.0503  -0.0627 261 ASN B CG  
6273  O OD1 . ASN B 261 ? 0.2186 0.3681 0.3500 -0.0317 0.0476  -0.0640 261 ASN B OD1 
6274  N ND2 . ASN B 261 ? 0.1737 0.3507 0.3060 -0.0321 0.0543  -0.0682 261 ASN B ND2 
6275  N N   . GLU B 262 ? 0.0941 0.2176 0.2036 -0.0500 0.0461  -0.0352 262 GLU B N   
6276  C CA  . GLU B 262 ? 0.1313 0.2530 0.2410 -0.0529 0.0456  -0.0251 262 GLU B CA  
6277  C C   . GLU B 262 ? 0.1867 0.2912 0.2939 -0.0510 0.0422  -0.0193 262 GLU B C   
6278  O O   . GLU B 262 ? 0.2240 0.3278 0.3345 -0.0515 0.0421  -0.0136 262 GLU B O   
6279  C CB  . GLU B 262 ? 0.1686 0.2951 0.2752 -0.0568 0.0461  -0.0212 262 GLU B CB  
6280  C CG  . GLU B 262 ? 0.2070 0.3492 0.3127 -0.0581 0.0495  -0.0297 262 GLU B CG  
6281  C CD  . GLU B 262 ? 0.4507 0.6021 0.5531 -0.0632 0.0508  -0.0259 262 GLU B CD  
6282  O OE1 . GLU B 262 ? 0.5472 0.7014 0.6532 -0.0655 0.0512  -0.0171 262 GLU B OE1 
6283  O OE2 . GLU B 262 ? 0.4630 0.6195 0.5599 -0.0652 0.0518  -0.0322 262 GLU B OE2 
6284  N N   . ALA B 263 ? 0.1990 0.2908 0.3012 -0.0487 0.0396  -0.0211 263 ALA B N   
6285  C CA  . ALA B 263 ? 0.1346 0.2124 0.2344 -0.0462 0.0366  -0.0162 263 ALA B CA  
6286  C C   . ALA B 263 ? 0.1366 0.2117 0.2391 -0.0438 0.0376  -0.0194 263 ALA B C   
6287  O O   . ALA B 263 ? 0.1395 0.2102 0.2427 -0.0435 0.0371  -0.0149 263 ALA B O   
6288  C CB  . ALA B 263 ? 0.1626 0.2296 0.2581 -0.0441 0.0343  -0.0178 263 ALA B CB  
6289  N N   . LEU B 264 ? 0.1336 0.2130 0.2388 -0.0423 0.0389  -0.0273 264 LEU B N   
6290  C CA  . LEU B 264 ? 0.1211 0.2008 0.2295 -0.0411 0.0394  -0.0300 264 LEU B CA  
6291  C C   . LEU B 264 ? 0.1418 0.2320 0.2548 -0.0445 0.0416  -0.0273 264 LEU B C   
6292  O O   . LEU B 264 ? 0.0943 0.1815 0.2089 -0.0446 0.0419  -0.0272 264 LEU B O   
6293  C CB  . LEU B 264 ? 0.1147 0.2019 0.2273 -0.0392 0.0397  -0.0375 264 LEU B CB  
6294  C CG  . LEU B 264 ? 0.1220 0.1986 0.2329 -0.0356 0.0377  -0.0404 264 LEU B CG  
6295  C CD1 . LEU B 264 ? 0.1936 0.2816 0.3120 -0.0334 0.0376  -0.0469 264 LEU B CD1 
6296  C CD2 . LEU B 264 ? 0.0714 0.1319 0.1786 -0.0330 0.0358  -0.0366 264 LEU B CD2 
6297  N N   . GLU B 265 ? 0.1652 0.2682 0.2811 -0.0476 0.0434  -0.0252 265 GLU B N   
6298  C CA  . GLU B 265 ? 0.1443 0.2576 0.2662 -0.0511 0.0457  -0.0211 265 GLU B CA  
6299  C C   . GLU B 265 ? 0.1581 0.2619 0.2789 -0.0521 0.0447  -0.0132 265 GLU B C   
6300  O O   . GLU B 265 ? 0.0974 0.2033 0.2228 -0.0541 0.0463  -0.0115 265 GLU B O   
6301  C CB  . GLU B 265 ? 0.1082 0.2385 0.2344 -0.0538 0.0485  -0.0201 265 GLU B CB  
6302  C CG  . GLU B 265 ? 0.2323 0.3777 0.3621 -0.0525 0.0503  -0.0283 265 GLU B CG  
6303  C CD  . GLU B 265 ? 0.3738 0.5373 0.5069 -0.0544 0.0537  -0.0285 265 GLU B CD  
6304  O OE1 . GLU B 265 ? 0.5759 0.7457 0.7128 -0.0580 0.0559  -0.0222 265 GLU B OE1 
6305  O OE2 . GLU B 265 ? 0.2344 0.4066 0.3671 -0.0520 0.0545  -0.0352 265 GLU B OE2 
6306  N N   . LEU B 266 ? 0.1902 0.2851 0.3059 -0.0509 0.0422  -0.0086 266 LEU B N   
6307  C CA  . LEU B 266 ? 0.0893 0.1779 0.2046 -0.0514 0.0408  -0.0013 266 LEU B CA  
6308  C C   . LEU B 266 ? 0.1050 0.1803 0.2190 -0.0482 0.0410  -0.0053 266 LEU B C   
6309  O O   . LEU B 266 ? 0.1355 0.2084 0.2529 -0.0491 0.0426  -0.0031 266 LEU B O   
6310  C CB  . LEU B 266 ? 0.0866 0.1720 0.1971 -0.0515 0.0374  0.0045  266 LEU B CB  
6311  C CG  . LEU B 266 ? 0.0867 0.1653 0.1947 -0.0518 0.0357  0.0097  266 LEU B CG  
6312  C CD1 . LEU B 266 ? 0.0927 0.1796 0.2055 -0.0562 0.0378  0.0144  266 LEU B CD1 
6313  C CD2 . LEU B 266 ? 0.0850 0.1639 0.1869 -0.0536 0.0320  0.0140  266 LEU B CD2 
6314  N N   . TYR B 267 ? 0.0835 0.1502 0.1935 -0.0443 0.0400  -0.0111 267 TYR B N   
6315  C CA  . TYR B 267 ? 0.0821 0.1378 0.1919 -0.0410 0.0405  -0.0144 267 TYR B CA  
6316  C C   . TYR B 267 ? 0.1109 0.1728 0.2257 -0.0438 0.0434  -0.0183 267 TYR B C   
6317  O O   . TYR B 267 ? 0.1116 0.1674 0.2285 -0.0434 0.0451  -0.0189 267 TYR B O   
6318  C CB  . TYR B 267 ? 0.0771 0.1256 0.1828 -0.0371 0.0386  -0.0185 267 TYR B CB  
6319  C CG  . TYR B 267 ? 0.1795 0.2209 0.2811 -0.0344 0.0358  -0.0144 267 TYR B CG  
6320  C CD1 . TYR B 267 ? 0.1292 0.1626 0.2307 -0.0317 0.0347  -0.0096 267 TYR B CD1 
6321  C CD2 . TYR B 267 ? 0.2124 0.2566 0.3117 -0.0349 0.0344  -0.0156 267 TYR B CD2 
6322  C CE1 . TYR B 267 ? 0.1486 0.1787 0.2472 -0.0303 0.0317  -0.0052 267 TYR B CE1 
6323  C CE2 . TYR B 267 ? 0.2311 0.2705 0.3270 -0.0337 0.0318  -0.0117 267 TYR B CE2 
6324  C CZ  . TYR B 267 ? 0.2257 0.2588 0.3210 -0.0319 0.0301  -0.0061 267 TYR B CZ  
6325  O OH  . TYR B 267 ? 0.2910 0.3220 0.3833 -0.0320 0.0269  -0.0017 267 TYR B OH  
6326  N N   . TYR B 268 ? 0.0894 0.1647 0.2071 -0.0468 0.0442  -0.0213 268 TYR B N   
6327  C CA  . TYR B 268 ? 0.1162 0.2011 0.2398 -0.0505 0.0468  -0.0244 268 TYR B CA  
6328  C C   . TYR B 268 ? 0.2214 0.3089 0.3502 -0.0542 0.0493  -0.0195 268 TYR B C   
6329  O O   . TYR B 268 ? 0.2052 0.2910 0.3374 -0.0561 0.0517  -0.0216 268 TYR B O   
6330  C CB  . TYR B 268 ? 0.1667 0.2690 0.2945 -0.0524 0.0473  -0.0275 268 TYR B CB  
6331  C CG  . TYR B 268 ? 0.1042 0.2217 0.2403 -0.0573 0.0501  -0.0287 268 TYR B CG  
6332  C CD1 . TYR B 268 ? 0.1722 0.2910 0.3102 -0.0586 0.0505  -0.0335 268 TYR B CD1 
6333  C CD2 . TYR B 268 ? 0.1096 0.2414 0.2523 -0.0610 0.0525  -0.0247 268 TYR B CD2 
6334  C CE1 . TYR B 268 ? 0.1510 0.2851 0.2973 -0.0639 0.0531  -0.0346 268 TYR B CE1 
6335  C CE2 . TYR B 268 ? 0.1641 0.3108 0.3158 -0.0658 0.0553  -0.0252 268 TYR B CE2 
6336  C CZ  . TYR B 268 ? 0.1919 0.3398 0.3453 -0.0674 0.0555  -0.0304 268 TYR B CZ  
6337  O OH  . TYR B 268 ? 0.3423 0.5063 0.5053 -0.0731 0.0584  -0.0310 268 TYR B OH  
6338  N N   . GLU B 269 ? 0.2543 0.3470 0.3843 -0.0557 0.0491  -0.0126 269 GLU B N   
6339  C CA  . GLU B 269 ? 0.1928 0.2902 0.3291 -0.0597 0.0514  -0.0065 269 GLU B CA  
6340  C C   . GLU B 269 ? 0.1546 0.2368 0.2904 -0.0576 0.0524  -0.0061 269 GLU B C   
6341  O O   . GLU B 269 ? 0.2165 0.2997 0.3588 -0.0608 0.0557  -0.0047 269 GLU B O   
6342  C CB  . GLU B 269 ? 0.2004 0.3076 0.3377 -0.0617 0.0503  0.0020  269 GLU B CB  
6343  C CG  . GLU B 269 ? 0.3474 0.4729 0.4915 -0.0646 0.0523  0.0030  269 GLU B CG  
6344  C CD  . GLU B 269 ? 0.5153 0.6466 0.6586 -0.0637 0.0513  0.0074  269 GLU B CD  
6345  O OE1 . GLU B 269 ? 0.4949 0.6214 0.6347 -0.0633 0.0486  0.0141  269 GLU B OE1 
6346  O OE2 . GLU B 269 ? 0.5559 0.6979 0.7017 -0.0637 0.0535  0.0030  269 GLU B OE2 
6347  N N   . LYS B 270 ? 0.1030 0.1715 0.2330 -0.0521 0.0501  -0.0072 270 LYS B N   
6348  C CA  . LYS B 270 ? 0.1032 0.1578 0.2349 -0.0483 0.0517  -0.0068 270 LYS B CA  
6349  C C   . LYS B 270 ? 0.1097 0.1564 0.2408 -0.0462 0.0535  -0.0145 270 LYS B C   
6350  O O   . LYS B 270 ? 0.1684 0.2033 0.3000 -0.0417 0.0545  -0.0150 270 LYS B O   
6351  C CB  . LYS B 270 ? 0.0974 0.1443 0.2251 -0.0435 0.0484  -0.0022 270 LYS B CB  
6352  C CG  . LYS B 270 ? 0.0975 0.1541 0.2235 -0.0468 0.0459  0.0046  270 LYS B CG  
6353  C CD  . LYS B 270 ? 0.1210 0.1802 0.2540 -0.0492 0.0482  0.0110  270 LYS B CD  
6354  C CE  . LYS B 270 ? 0.1903 0.2653 0.3212 -0.0558 0.0469  0.0161  270 LYS B CE  
6355  N NZ  . LYS B 270 ? 0.3166 0.3985 0.4554 -0.0606 0.0507  0.0202  270 LYS B NZ  
6356  N N   . GLY B 271 ? 0.1049 0.1598 0.2356 -0.0496 0.0540  -0.0201 271 GLY B N   
6357  C CA  . GLY B 271 ? 0.1061 0.1571 0.2360 -0.0494 0.0556  -0.0273 271 GLY B CA  
6358  C C   . GLY B 271 ? 0.0987 0.1410 0.2220 -0.0441 0.0528  -0.0296 271 GLY B C   
6359  O O   . GLY B 271 ? 0.0991 0.1329 0.2220 -0.0420 0.0545  -0.0323 271 GLY B O   
6360  N N   . ILE B 272 ? 0.1334 0.1781 0.2522 -0.0422 0.0490  -0.0284 272 ILE B N   
6361  C CA  . ILE B 272 ? 0.0865 0.1247 0.2001 -0.0379 0.0464  -0.0299 272 ILE B CA  
6362  C C   . ILE B 272 ? 0.1140 0.1626 0.2275 -0.0404 0.0452  -0.0349 272 ILE B C   
6363  O O   . ILE B 272 ? 0.1666 0.2247 0.2811 -0.0418 0.0441  -0.0348 272 ILE B O   
6364  C CB  . ILE B 272 ? 0.0806 0.1138 0.1907 -0.0340 0.0432  -0.0249 272 ILE B CB  
6365  C CG1 . ILE B 272 ? 0.0960 0.1212 0.2077 -0.0312 0.0436  -0.0193 272 ILE B CG1 
6366  C CG2 . ILE B 272 ? 0.0750 0.1041 0.1812 -0.0306 0.0405  -0.0263 272 ILE B CG2 
6367  C CD1 . ILE B 272 ? 0.0816 0.0991 0.1957 -0.0288 0.0461  -0.0209 272 ILE B CD1 
6368  N N   . ASN B 273 ? 0.1357 0.1844 0.2488 -0.0410 0.0457  -0.0389 273 ASN B N   
6369  C CA  . ASN B 273 ? 0.0888 0.1507 0.2038 -0.0438 0.0444  -0.0428 273 ASN B CA  
6370  C C   . ASN B 273 ? 0.1124 0.1739 0.2253 -0.0401 0.0407  -0.0419 273 ASN B C   
6371  O O   . ASN B 273 ? 0.1651 0.2398 0.2819 -0.0413 0.0393  -0.0436 273 ASN B O   
6372  C CB  . ASN B 273 ? 0.0929 0.1576 0.2085 -0.0467 0.0459  -0.0470 273 ASN B CB  
6373  C CG  . ASN B 273 ? 0.2278 0.2921 0.3464 -0.0509 0.0504  -0.0491 273 ASN B CG  
6374  O OD1 . ASN B 273 ? 0.2329 0.3007 0.3553 -0.0530 0.0520  -0.0472 273 ASN B OD1 
6375  N ND2 . ASN B 273 ? 0.2425 0.3033 0.3601 -0.0526 0.0527  -0.0528 273 ASN B ND2 
6376  N N   . MET B 274 ? 0.1634 0.2117 0.2721 -0.0355 0.0392  -0.0388 274 MET B N   
6377  C CA  . MET B 274 ? 0.1680 0.2149 0.2759 -0.0323 0.0360  -0.0376 274 MET B CA  
6378  C C   . MET B 274 ? 0.1292 0.1634 0.2337 -0.0278 0.0349  -0.0330 274 MET B C   
6379  O O   . MET B 274 ? 0.1925 0.2185 0.2951 -0.0261 0.0359  -0.0300 274 MET B O   
6380  C CB  . MET B 274 ? 0.1939 0.2420 0.3017 -0.0321 0.0344  -0.0380 274 MET B CB  
6381  C CG  . MET B 274 ? 0.1809 0.2290 0.2900 -0.0292 0.0309  -0.0358 274 MET B CG  
6382  S SD  . MET B 274 ? 0.2544 0.2859 0.3593 -0.0240 0.0293  -0.0298 274 MET B SD  
6383  C CE  . MET B 274 ? 0.2274 0.2607 0.3311 -0.0256 0.0287  -0.0287 274 MET B CE  
6384  N N   . LEU B 275 ? 0.0659 0.1004 0.1710 -0.0260 0.0328  -0.0324 275 LEU B N   
6385  C CA  . LEU B 275 ? 0.0674 0.0919 0.1702 -0.0221 0.0312  -0.0281 275 LEU B CA  
6386  C C   . LEU B 275 ? 0.1494 0.1747 0.2552 -0.0204 0.0289  -0.0289 275 LEU B C   
6387  O O   . LEU B 275 ? 0.1794 0.2140 0.2894 -0.0220 0.0284  -0.0328 275 LEU B O   
6388  C CB  . LEU B 275 ? 0.0615 0.0854 0.1628 -0.0228 0.0319  -0.0261 275 LEU B CB  
6389  C CG  . LEU B 275 ? 0.0648 0.0982 0.1677 -0.0260 0.0329  -0.0298 275 LEU B CG  
6390  C CD1 . LEU B 275 ? 0.2174 0.2499 0.3213 -0.0245 0.0316  -0.0310 275 LEU B CD1 
6391  C CD2 . LEU B 275 ? 0.0803 0.1164 0.1820 -0.0287 0.0343  -0.0271 275 LEU B CD2 
6392  N N   . ALA B 276 ? 0.1961 0.2137 0.3013 -0.0171 0.0270  -0.0248 276 ALA B N   
6393  C CA  . ALA B 276 ? 0.1193 0.1357 0.2289 -0.0151 0.0247  -0.0249 276 ALA B CA  
6394  C C   . ALA B 276 ? 0.1256 0.1395 0.2356 -0.0144 0.0244  -0.0243 276 ALA B C   
6395  O O   . ALA B 276 ? 0.1459 0.1595 0.2516 -0.0158 0.0253  -0.0223 276 ALA B O   
6396  C CB  . ALA B 276 ? 0.0716 0.0835 0.1822 -0.0126 0.0219  -0.0196 276 ALA B CB  
6397  N N   . THR B 277 ? 0.0840 0.0974 0.2000 -0.0129 0.0227  -0.0261 277 THR B N   
6398  C CA  . THR B 277 ? 0.1136 0.1255 0.2310 -0.0131 0.0221  -0.0260 277 THR B CA  
6399  C C   . THR B 277 ? 0.1364 0.1460 0.2629 -0.0105 0.0187  -0.0263 277 THR B C   
6400  O O   . THR B 277 ? 0.1749 0.1836 0.3060 -0.0084 0.0164  -0.0252 277 THR B O   
6401  C CB  . THR B 277 ? 0.0752 0.0933 0.1918 -0.0161 0.0252  -0.0328 277 THR B CB  
6402  O OG1 . THR B 277 ? 0.1094 0.1269 0.2286 -0.0170 0.0247  -0.0344 277 THR B OG1 
6403  C CG2 . THR B 277 ? 0.0590 0.0860 0.1810 -0.0167 0.0260  -0.0400 277 THR B CG2 
6404  N N   . ASP B 278 ? 0.1915 0.2006 0.3206 -0.0119 0.0174  -0.0272 278 ASP B N   
6405  C CA  . ASP B 278 ? 0.1707 0.1767 0.3082 -0.0112 0.0121  -0.0266 278 ASP B CA  
6406  C C   . ASP B 278 ? 0.1902 0.2005 0.3403 -0.0074 0.0124  -0.0373 278 ASP B C   
6407  O O   . ASP B 278 ? 0.2223 0.2385 0.3716 -0.0081 0.0167  -0.0458 278 ASP B O   
6408  C CB  . ASP B 278 ? 0.2022 0.2005 0.3310 -0.0184 0.0080  -0.0232 278 ASP B CB  
6409  C CG  . ASP B 278 ? 0.2627 0.2450 0.3879 -0.0214 -0.0006 -0.0211 278 ASP B CG  
6410  O OD1 . ASP B 278 ? 0.2884 0.2702 0.4222 -0.0168 -0.0034 -0.0217 278 ASP B OD1 
6411  O OD2 . ASP B 278 ? 0.3102 0.2752 0.4191 -0.0289 -0.0050 -0.0187 278 ASP B OD2 
6412  N N   . GLU B 279 ? 0.1914 0.1995 0.3582 -0.0041 0.0063  -0.0385 279 GLU B N   
6413  C CA  . GLU B 279 ? 0.1795 0.1958 0.3762 0.0000  0.0036  -0.0541 279 GLU B CA  
6414  C C   . GLU B 279 ? 0.1677 0.1718 0.3629 0.0030  0.0014  -0.0660 279 GLU B C   
6415  O O   . GLU B 279 ? 0.1843 0.1901 0.3735 0.0189  0.0023  -0.0760 279 GLU B O   
6416  C CB  . GLU B 279 ? 0.1594 0.1699 0.3706 0.0029  -0.0065 -0.0526 279 GLU B CB  
6417  C CG  . GLU B 279 ? 0.2101 0.1819 0.3900 0.0085  -0.0146 -0.0452 279 GLU B CG  
6418  C CD  . GLU B 279 ? 0.3287 0.2860 0.5033 0.0237  -0.0213 -0.0439 279 GLU B CD  
6419  O OE1 . GLU B 279 ? 0.3711 0.3337 0.5451 0.0424  -0.0197 -0.0522 279 GLU B OE1 
6420  O OE2 . GLU B 279 ? 0.3716 0.3171 0.5387 0.0188  -0.0267 -0.0327 279 GLU B OE2 
6421  N N   . VAL B 280 ? 0.1654 0.1484 0.3336 -0.0044 0.0003  -0.0589 280 VAL B N   
6422  C CA  . VAL B 280 ? 0.2206 0.1832 0.3709 -0.0005 0.0003  -0.0703 280 VAL B CA  
6423  C C   . VAL B 280 ? 0.1320 0.1272 0.3031 -0.0019 0.0106  -0.0828 280 VAL B C   
6424  O O   . VAL B 280 ? 0.1587 0.1514 0.3207 0.0101  0.0134  -0.0964 280 VAL B O   
6425  C CB  . VAL B 280 ? 0.2302 0.1622 0.3437 -0.0122 -0.0047 -0.0599 280 VAL B CB  
6426  C CG1 . VAL B 280 ? 0.3174 0.2689 0.4232 -0.0254 -0.0022 -0.0437 280 VAL B CG1 
6427  C CG2 . VAL B 280 ? 0.2770 0.1881 0.3727 -0.0094 -0.0041 -0.0733 280 VAL B CG2 
6428  N N   . ILE B 281 ? 0.1077 0.1313 0.2932 -0.0099 0.0190  -0.0753 281 ILE B N   
6429  C CA  . ILE B 281 ? 0.0893 0.1234 0.2661 -0.0120 0.0263  -0.0835 281 ILE B CA  
6430  C C   . ILE B 281 ? 0.1326 0.1883 0.3128 -0.0055 0.0240  -0.0857 281 ILE B C   
6431  O O   . ILE B 281 ? 0.1470 0.2220 0.3222 0.0009  0.0281  -0.0897 281 ILE B O   
6432  C CB  . ILE B 281 ? 0.0671 0.0987 0.2076 -0.0168 0.0258  -0.0601 281 ILE B CB  
6433  C CG1 . ILE B 281 ? 0.0717 0.0963 0.2017 -0.0230 0.0253  -0.0527 281 ILE B CG1 
6434  C CG2 . ILE B 281 ? 0.1338 0.1798 0.2701 -0.0191 0.0293  -0.0634 281 ILE B CG2 
6435  C CD1 . ILE B 281 ? 0.1165 0.1314 0.2394 -0.0243 0.0212  -0.0399 281 ILE B CD1 
6436  N N   . LEU B 282 ? 0.1537 0.2085 0.3354 -0.0009 0.0196  -0.0785 282 LEU B N   
6437  C CA  . LEU B 282 ? 0.0858 0.1628 0.2642 0.0124  0.0198  -0.0756 282 LEU B CA  
6438  C C   . LEU B 282 ? 0.1701 0.2484 0.3509 0.0335  0.0206  -0.0862 282 LEU B C   
6439  O O   . LEU B 282 ? 0.2152 0.3129 0.3915 0.0438  0.0256  -0.0867 282 LEU B O   
6440  C CB  . LEU B 282 ? 0.1603 0.2350 0.3391 0.0131  0.0153  -0.0666 282 LEU B CB  
6441  C CG  . LEU B 282 ? 0.1122 0.2062 0.2934 0.0295  0.0147  -0.0644 282 LEU B CG  
6442  C CD1 . LEU B 282 ? 0.1213 0.2395 0.2997 0.0263  0.0191  -0.0607 282 LEU B CD1 
6443  C CD2 . LEU B 282 ? 0.0890 0.1761 0.2744 0.0305  0.0089  -0.0585 282 LEU B CD2 
6444  N N   . LYS B 283 ? 0.1341 0.1823 0.3127 0.0418  0.0157  -0.0919 283 LYS B N   
6445  C CA  . LYS B 283 ? 0.1750 0.2058 0.3376 0.0643  0.0162  -0.0994 283 LYS B CA  
6446  C C   . LYS B 283 ? 0.2292 0.2616 0.3814 0.0663  0.0230  -0.1099 283 LYS B C   
6447  O O   . LYS B 283 ? 0.2491 0.2819 0.3911 0.0844  0.0277  -0.1154 283 LYS B O   
6448  C CB  . LYS B 283 ? 0.2288 0.2126 0.3759 0.0693  0.0077  -0.0983 283 LYS B CB  
6449  C CG  . LYS B 283 ? 0.1993 0.1808 0.3536 0.0720  0.0011  -0.0877 283 LYS B CG  
6450  C CD  . LYS B 283 ? 0.2015 0.2120 0.3634 0.0888  0.0047  -0.0855 283 LYS B CD  
6451  C CE  . LYS B 283 ? 0.2157 0.2118 0.3765 0.0987  -0.0023 -0.0771 283 LYS B CE  
6452  N NZ  . LYS B 283 ? 0.1952 0.1798 0.3610 0.0813  -0.0098 -0.0690 283 LYS B NZ  
6453  N N   . ASN B 284 ? 0.2679 0.3016 0.4233 0.0479  0.0246  -0.1124 284 ASN B N   
6454  C CA  . ASN B 284 ? 0.1829 0.2229 0.3284 0.0478  0.0315  -0.1220 284 ASN B CA  
6455  C C   . ASN B 284 ? 0.2337 0.3157 0.3873 0.0484  0.0387  -0.1179 284 ASN B C   
6456  O O   . ASN B 284 ? 0.3408 0.4304 0.4847 0.0569  0.0450  -0.1247 284 ASN B O   
6457  C CB  . ASN B 284 ? 0.1851 0.2155 0.3315 0.0263  0.0316  -0.1238 284 ASN B CB  
6458  C CG  . ASN B 284 ? 0.3314 0.3098 0.4509 0.0247  0.0233  -0.1254 284 ASN B CG  
6459  O OD1 . ASN B 284 ? 0.5301 0.4779 0.6284 0.0410  0.0193  -0.1286 284 ASN B OD1 
6460  N ND2 . ASN B 284 ? 0.2855 0.2527 0.4009 0.0033  0.0203  -0.1186 284 ASN B ND2 
6461  N N   . SER B 285 ? 0.1840 0.2864 0.3486 0.0389  0.0372  -0.1048 285 SER B N   
6462  C CA  . SER B 285 ? 0.2086 0.3375 0.3717 0.0348  0.0415  -0.0955 285 SER B CA  
6463  C C   . SER B 285 ? 0.2633 0.4079 0.4289 0.0516  0.0444  -0.0915 285 SER B C   
6464  O O   . SER B 285 ? 0.4599 0.6207 0.6246 0.0582  0.0510  -0.0921 285 SER B O   
6465  C CB  . SER B 285 ? 0.2013 0.3291 0.3622 0.0160  0.0378  -0.0816 285 SER B CB  
6466  O OG  . SER B 285 ? 0.1965 0.3048 0.3541 0.0023  0.0356  -0.0825 285 SER B OG  
6467  N N   . VAL B 286 ? 0.2465 0.3873 0.4171 0.0579  0.0401  -0.0869 286 VAL B N   
6468  C CA  . VAL B 286 ? 0.3167 0.4726 0.4935 0.0734  0.0429  -0.0833 286 VAL B CA  
6469  C C   . VAL B 286 ? 0.3731 0.5102 0.5468 0.0949  0.0428  -0.0926 286 VAL B C   
6470  O O   . VAL B 286 ? 0.4600 0.5683 0.6263 0.0961  0.0376  -0.0989 286 VAL B O   
6471  C CB  . VAL B 286 ? 0.2539 0.4225 0.4407 0.0659  0.0376  -0.0754 286 VAL B CB  
6472  C CG1 . VAL B 286 ? 0.1898 0.3648 0.3755 0.0443  0.0360  -0.0725 286 VAL B CG1 
6473  C CG2 . VAL B 286 ? 0.3398 0.4875 0.5241 0.0686  0.0314  -0.0716 286 VAL B CG2 
6474  N N   . GLU B 287 ? 0.4076 0.5565 0.5862 0.1120  0.0483  -0.0928 287 GLU B N   
6475  C CA  . GLU B 287 ? 0.4704 0.5970 0.6423 0.1340  0.0499  -0.1018 287 GLU B CA  
6476  C C   . GLU B 287 ? 0.6793 0.7804 0.8494 0.1399  0.0414  -0.0991 287 GLU B C   
6477  O O   . GLU B 287 ? 0.7418 0.8060 0.8969 0.1418  0.0372  -0.1057 287 GLU B O   
6478  C CB  . GLU B 287 ? 0.4792 0.6274 0.6622 0.1498  0.0575  -0.1015 287 GLU B CB  
6479  C CG  . GLU B 287 ? 0.6196 0.7458 0.7921 0.1706  0.0631  -0.1137 287 GLU B CG  
6480  C CD  . GLU B 287 ? 0.7405 0.8763 0.9270 0.1904  0.0655  -0.1120 287 GLU B CD  
6481  O OE1 . GLU B 287 ? 0.6148 0.7863 0.8197 0.1892  0.0684  -0.1057 287 GLU B OE1 
6482  O OE2 . GLU B 287 ? 0.6434 0.7493 0.8227 0.2065  0.0639  -0.1168 287 GLU B OE2 
6483  N N   . ARG B 288 ? 0.6033 0.7212 0.7873 0.1416  0.0383  -0.0888 288 ARG B N   
6484  C CA  . ARG B 288 ? 0.5677 0.6647 0.7508 0.1454  0.0295  -0.0840 288 ARG B CA  
6485  C C   . ARG B 288 ? 0.5834 0.7089 0.7809 0.1349  0.0261  -0.0717 288 ARG B C   
6486  O O   . ARG B 288 ? 0.5349 0.6815 0.7460 0.1438  0.0277  -0.0660 288 ARG B O   
6487  C CB  . ARG B 288 ? 0.4895 0.5649 0.6701 0.1689  0.0297  -0.0866 288 ARG B CB  
6488  C CG  . ARG B 288 ? 0.5643 0.6682 0.7615 0.1837  0.0360  -0.0850 288 ARG B CG  
6489  C CD  . ARG B 288 ? 0.6715 0.7544 0.8610 0.2039  0.0419  -0.0955 288 ARG B CD  
6490  N NE  . ARG B 288 ? 0.7563 0.8007 0.9377 0.2176  0.0363  -0.0951 288 ARG B NE  
6491  C CZ  . ARG B 288 ? 0.6939 0.7125 0.8677 0.2357  0.0402  -0.1032 288 ARG B CZ  
6492  N NH1 . ARG B 288 ? 0.7673 0.7962 0.9407 0.2439  0.0501  -0.1133 288 ARG B NH1 
6493  N NH2 . ARG B 288 ? 0.6184 0.5992 0.7844 0.2454  0.0341  -0.1007 288 ARG B NH2 
6494  N N   . ALA B 289 ? 0.4834 0.6082 0.6783 0.1151  0.0216  -0.0681 289 ALA B N   
6495  C CA  . ALA B 289 ? 0.5347 0.6806 0.7376 0.1029  0.0190  -0.0570 289 ALA B CA  
6496  C C   . ALA B 289 ? 0.3702 0.4970 0.5687 0.0927  0.0107  -0.0549 289 ALA B C   
6497  O O   . ALA B 289 ? 0.3096 0.4101 0.5018 0.0875  0.0076  -0.0613 289 ALA B O   
6498  C CB  . ALA B 289 ? 0.4687 0.6372 0.6737 0.0856  0.0229  -0.0560 289 ALA B CB  
6499  N N   . SER B 290 ? 0.2796 0.4196 0.4836 0.0890  0.0073  -0.0454 290 SER B N   
6500  C CA  . SER B 290 ? 0.2177 0.3415 0.4194 0.0807  -0.0004 -0.0426 290 SER B CA  
6501  C C   . SER B 290 ? 0.1756 0.2939 0.3708 0.0566  0.0009  -0.0426 290 SER B C   
6502  O O   . SER B 290 ? 0.2180 0.3507 0.4103 0.0459  0.0059  -0.0423 290 SER B O   
6503  C CB  . SER B 290 ? 0.1285 0.2708 0.3366 0.0838  -0.0037 -0.0325 290 SER B CB  
6504  O OG  . SER B 290 ? 0.2558 0.3793 0.4650 0.0979  -0.0116 -0.0305 290 SER B OG  
6505  N N   . PRO B 291 ? 0.0994 0.1921 0.2952 0.0478  -0.0044 -0.0435 291 PRO B N   
6506  C CA  . PRO B 291 ? 0.0775 0.1627 0.2652 0.0260  -0.0023 -0.0394 291 PRO B CA  
6507  C C   . PRO B 291 ? 0.1296 0.2257 0.3121 0.0196  -0.0030 -0.0316 291 PRO B C   
6508  O O   . PRO B 291 ? 0.2227 0.3050 0.3970 0.0061  -0.0009 -0.0298 291 PRO B O   
6509  C CB  . PRO B 291 ? 0.0890 0.1416 0.2861 0.0209  -0.0075 -0.0412 291 PRO B CB  
6510  C CG  . PRO B 291 ? 0.1218 0.1641 0.3247 0.0392  -0.0157 -0.0406 291 PRO B CG  
6511  C CD  . PRO B 291 ? 0.1277 0.1904 0.3269 0.0586  -0.0123 -0.0448 291 PRO B CD  
6512  N N   . TYR B 292 ? 0.1202 0.2383 0.3089 0.0313  -0.0054 -0.0280 292 TYR B N   
6513  C CA  . TYR B 292 ? 0.1545 0.2854 0.3435 0.0264  -0.0075 -0.0222 292 TYR B CA  
6514  C C   . TYR B 292 ? 0.1561 0.3109 0.3476 0.0218  -0.0036 -0.0224 292 TYR B C   
6515  O O   . TYR B 292 ? 0.1418 0.3085 0.3340 0.0173  -0.0051 -0.0176 292 TYR B O   
6516  C CB  . TYR B 292 ? 0.1452 0.2839 0.3413 0.0425  -0.0143 -0.0166 292 TYR B CB  
6517  C CG  . TYR B 292 ? 0.1272 0.2324 0.3299 0.0486  -0.0216 -0.0192 292 TYR B CG  
6518  C CD1 . TYR B 292 ? 0.1371 0.2176 0.3391 0.0337  -0.0242 -0.0161 292 TYR B CD1 
6519  C CD2 . TYR B 292 ? 0.1451 0.2378 0.3510 0.0692  -0.0254 -0.0216 292 TYR B CD2 
6520  C CE1 . TYR B 292 ? 0.1864 0.2330 0.3940 0.0370  -0.0320 -0.0133 292 TYR B CE1 
6521  C CE2 . TYR B 292 ? 0.1464 0.1994 0.3487 0.0739  -0.0326 -0.0205 292 TYR B CE2 
6522  C CZ  . TYR B 292 ? 0.2269 0.2574 0.4300 0.0568  -0.0365 -0.0155 292 TYR B CZ  
6523  O OH  . TYR B 292 ? 0.3898 0.3784 0.5813 0.0581  -0.0431 -0.0110 292 TYR B OH  
6524  N N   . LEU B 293 ? 0.1325 0.2934 0.3259 0.0228  0.0011  -0.0275 293 LEU B N   
6525  C CA  . LEU B 293 ? 0.0745 0.2514 0.2698 0.0165  0.0045  -0.0288 293 LEU B CA  
6526  C C   . LEU B 293 ? 0.0685 0.2260 0.2495 0.0024  0.0081  -0.0322 293 LEU B C   
6527  O O   . LEU B 293 ? 0.1846 0.3181 0.3567 -0.0014 0.0090  -0.0340 293 LEU B O   
6528  C CB  . LEU B 293 ? 0.0831 0.2775 0.2881 0.0256  0.0077  -0.0327 293 LEU B CB  
6529  C CG  . LEU B 293 ? 0.0946 0.3135 0.3166 0.0403  0.0062  -0.0299 293 LEU B CG  
6530  C CD1 . LEU B 293 ? 0.1433 0.3558 0.3691 0.0545  0.0020  -0.0245 293 LEU B CD1 
6531  C CD2 . LEU B 293 ? 0.1041 0.3362 0.3327 0.0478  0.0111  -0.0356 293 LEU B CD2 
6532  N N   . ARG B 294 ? 0.0699 0.2367 0.2498 -0.0039 0.0103  -0.0329 294 ARG B N   
6533  C CA  . ARG B 294 ? 0.0690 0.2214 0.2373 -0.0126 0.0145  -0.0367 294 ARG B CA  
6534  C C   . ARG B 294 ? 0.0732 0.2367 0.2458 -0.0105 0.0176  -0.0413 294 ARG B C   
6535  O O   . ARG B 294 ? 0.0787 0.2666 0.2633 -0.0050 0.0176  -0.0420 294 ARG B O   
6536  C CB  . ARG B 294 ? 0.0708 0.2270 0.2355 -0.0194 0.0153  -0.0364 294 ARG B CB  
6537  C CG  . ARG B 294 ? 0.0823 0.2291 0.2380 -0.0257 0.0198  -0.0405 294 ARG B CG  
6538  C CD  . ARG B 294 ? 0.1040 0.2549 0.2569 -0.0316 0.0208  -0.0415 294 ARG B CD  
6539  N NE  . ARG B 294 ? 0.1715 0.3485 0.3361 -0.0309 0.0185  -0.0416 294 ARG B NE  
6540  C CZ  . ARG B 294 ? 0.1487 0.3317 0.3150 -0.0326 0.0159  -0.0397 294 ARG B CZ  
6541  N NH1 . ARG B 294 ? 0.1466 0.3120 0.3036 -0.0353 0.0156  -0.0372 294 ARG B NH1 
6542  N NH2 . ARG B 294 ? 0.1159 0.3249 0.2940 -0.0314 0.0134  -0.0403 294 ARG B NH2 
6543  N N   . TYR B 295 ? 0.0717 0.2186 0.2354 -0.0140 0.0204  -0.0440 295 TYR B N   
6544  C CA  . TYR B 295 ? 0.0757 0.2329 0.2427 -0.0126 0.0234  -0.0478 295 TYR B CA  
6545  C C   . TYR B 295 ? 0.0779 0.2329 0.2382 -0.0202 0.0268  -0.0492 295 TYR B C   
6546  O O   . TYR B 295 ? 0.0753 0.2101 0.2248 -0.0251 0.0276  -0.0480 295 TYR B O   
6547  C CB  . TYR B 295 ? 0.0738 0.2177 0.2381 -0.0098 0.0237  -0.0498 295 TYR B CB  
6548  C CG  . TYR B 295 ? 0.0757 0.2282 0.2501 0.0008  0.0212  -0.0499 295 TYR B CG  
6549  C CD1 . TYR B 295 ? 0.0719 0.2108 0.2456 0.0027  0.0173  -0.0469 295 TYR B CD1 
6550  C CD2 . TYR B 295 ? 0.0837 0.2583 0.2687 0.0108  0.0230  -0.0524 295 TYR B CD2 
6551  C CE1 . TYR B 295 ? 0.0764 0.2223 0.2593 0.0150  0.0146  -0.0465 295 TYR B CE1 
6552  C CE2 . TYR B 295 ? 0.0899 0.2704 0.2835 0.0249  0.0214  -0.0521 295 TYR B CE2 
6553  C CZ  . TYR B 295 ? 0.0867 0.2522 0.2787 0.0274  0.0169  -0.0490 295 TYR B CZ  
6554  O OH  . TYR B 295 ? 0.0973 0.2647 0.2959 0.0442  0.0153  -0.0481 295 TYR B OH  
6555  N N   . TYR B 296 ? 0.0838 0.2610 0.2519 -0.0199 0.0289  -0.0512 296 TYR B N   
6556  C CA  . TYR B 296 ? 0.0875 0.2665 0.2520 -0.0266 0.0322  -0.0523 296 TYR B CA  
6557  C C   . TYR B 296 ? 0.0889 0.2682 0.2525 -0.0257 0.0348  -0.0537 296 TYR B C   
6558  O O   . TYR B 296 ? 0.0932 0.2922 0.2660 -0.0203 0.0360  -0.0557 296 TYR B O   
6559  C CB  . TYR B 296 ? 0.0943 0.2994 0.2689 -0.0277 0.0330  -0.0534 296 TYR B CB  
6560  C CG  . TYR B 296 ? 0.0950 0.2998 0.2683 -0.0324 0.0316  -0.0528 296 TYR B CG  
6561  C CD1 . TYR B 296 ? 0.0910 0.2720 0.2528 -0.0364 0.0312  -0.0516 296 TYR B CD1 
6562  C CD2 . TYR B 296 ? 0.1009 0.3310 0.2849 -0.0325 0.0308  -0.0538 296 TYR B CD2 
6563  C CE1 . TYR B 296 ? 0.1467 0.3287 0.3073 -0.0405 0.0305  -0.0520 296 TYR B CE1 
6564  C CE2 . TYR B 296 ? 0.1027 0.3342 0.2853 -0.0375 0.0296  -0.0541 296 TYR B CE2 
6565  C CZ  . TYR B 296 ? 0.0988 0.3059 0.2694 -0.0416 0.0296  -0.0535 296 TYR B CZ  
6566  O OH  . TYR B 296 ? 0.1019 0.3114 0.2708 -0.0466 0.0289  -0.0546 296 TYR B OH  
6567  N N   . PHE B 297 ? 0.0864 0.2456 0.2395 -0.0299 0.0359  -0.0526 297 PHE B N   
6568  C CA  . PHE B 297 ? 0.0883 0.2494 0.2402 -0.0302 0.0384  -0.0535 297 PHE B CA  
6569  C C   . PHE B 297 ? 0.1124 0.2908 0.2689 -0.0341 0.0416  -0.0532 297 PHE B C   
6570  O O   . PHE B 297 ? 0.1278 0.2984 0.2799 -0.0396 0.0427  -0.0507 297 PHE B O   
6571  C CB  . PHE B 297 ? 0.0841 0.2203 0.2246 -0.0326 0.0382  -0.0513 297 PHE B CB  
6572  C CG  . PHE B 297 ? 0.0997 0.2390 0.2389 -0.0332 0.0404  -0.0520 297 PHE B CG  
6573  C CD1 . PHE B 297 ? 0.0862 0.2307 0.2287 -0.0288 0.0403  -0.0557 297 PHE B CD1 
6574  C CD2 . PHE B 297 ? 0.1247 0.2636 0.2605 -0.0378 0.0426  -0.0488 297 PHE B CD2 
6575  C CE1 . PHE B 297 ? 0.1081 0.2571 0.2492 -0.0296 0.0426  -0.0571 297 PHE B CE1 
6576  C CE2 . PHE B 297 ? 0.0913 0.2353 0.2261 -0.0387 0.0446  -0.0488 297 PHE B CE2 
6577  C CZ  . PHE B 297 ? 0.1004 0.2496 0.2372 -0.0349 0.0447  -0.0534 297 PHE B CZ  
6578  N N   . ARG B 298 ? 0.1413 0.3443 0.3079 -0.0304 0.0436  -0.0555 298 ARG B N   
6579  C CA  . ARG B 298 ? 0.1080 0.3301 0.2803 -0.0337 0.0473  -0.0551 298 ARG B CA  
6580  C C   . ARG B 298 ? 0.1460 0.3722 0.3205 -0.0400 0.0477  -0.0534 298 ARG B C   
6581  O O   . ARG B 298 ? 0.2738 0.5072 0.4504 -0.0452 0.0506  -0.0516 298 ARG B O   
6582  C CB  . ARG B 298 ? 0.1085 0.3225 0.2744 -0.0372 0.0497  -0.0532 298 ARG B CB  
6583  C CG  . ARG B 298 ? 0.1264 0.3410 0.2910 -0.0320 0.0504  -0.0560 298 ARG B CG  
6584  C CD  . ARG B 298 ? 0.2372 0.4646 0.4029 -0.0342 0.0546  -0.0553 298 ARG B CD  
6585  N NE  . ARG B 298 ? 0.1466 0.3565 0.3034 -0.0407 0.0545  -0.0505 298 ARG B NE  
6586  C CZ  . ARG B 298 ? 0.1264 0.3268 0.2762 -0.0411 0.0545  -0.0502 298 ARG B CZ  
6587  N NH1 . ARG B 298 ? 0.1120 0.3170 0.2620 -0.0361 0.0551  -0.0554 298 ARG B NH1 
6588  N NH2 . ARG B 298 ? 0.1630 0.3499 0.3063 -0.0461 0.0542  -0.0444 298 ARG B NH2 
6589  N N   . GLU B 299 ? 0.1086 0.3314 0.2835 -0.0397 0.0448  -0.0540 299 GLU B N   
6590  C CA  . GLU B 299 ? 0.1487 0.3741 0.3248 -0.0460 0.0451  -0.0536 299 GLU B CA  
6591  C C   . GLU B 299 ? 0.1729 0.3795 0.3408 -0.0520 0.0469  -0.0509 299 GLU B C   
6592  O O   . GLU B 299 ? 0.1769 0.3915 0.3489 -0.0577 0.0495  -0.0499 299 GLU B O   
6593  C CB  . GLU B 299 ? 0.2449 0.5012 0.4340 -0.0474 0.0472  -0.0548 299 GLU B CB  
6594  C CG  . GLU B 299 ? 0.3851 0.6638 0.5845 -0.0389 0.0462  -0.0568 299 GLU B CG  
6595  C CD  . GLU B 299 ? 0.5817 0.8921 0.7939 -0.0384 0.0495  -0.0577 299 GLU B CD  
6596  O OE1 . GLU B 299 ? 0.6555 0.9721 0.8695 -0.0463 0.0521  -0.0565 299 GLU B OE1 
6597  O OE2 . GLU B 299 ? 0.4358 0.7658 0.6571 -0.0295 0.0498  -0.0592 299 GLU B OE2 
6598  N N   . LEU B 300 ? 0.1806 0.3631 0.3383 -0.0502 0.0456  -0.0493 300 LEU B N   
6599  C CA  . LEU B 300 ? 0.1577 0.3215 0.3081 -0.0536 0.0468  -0.0461 300 LEU B CA  
6600  C C   . LEU B 300 ? 0.1638 0.3045 0.3052 -0.0516 0.0447  -0.0458 300 LEU B C   
6601  O O   . LEU B 300 ? 0.1699 0.2997 0.3083 -0.0541 0.0459  -0.0446 300 LEU B O   
6602  C CB  . LEU B 300 ? 0.2102 0.3702 0.3580 -0.0530 0.0481  -0.0428 300 LEU B CB  
6603  C CG  . LEU B 300 ? 0.1905 0.3715 0.3461 -0.0548 0.0511  -0.0419 300 LEU B CG  
6604  C CD1 . LEU B 300 ? 0.1692 0.3441 0.3202 -0.0537 0.0517  -0.0390 300 LEU B CD1 
6605  C CD2 . LEU B 300 ? 0.2330 0.4230 0.3950 -0.0610 0.0541  -0.0394 300 LEU B CD2 
6606  N N   . ILE B 301 ? 0.0936 0.2276 0.2319 -0.0469 0.0419  -0.0469 301 ILE B N   
6607  C CA  . ILE B 301 ? 0.1250 0.2371 0.2550 -0.0443 0.0402  -0.0456 301 ILE B CA  
6608  C C   . ILE B 301 ? 0.0837 0.1967 0.2149 -0.0402 0.0371  -0.0469 301 ILE B C   
6609  O O   . ILE B 301 ? 0.1254 0.2500 0.2619 -0.0377 0.0363  -0.0483 301 ILE B O   
6610  C CB  . ILE B 301 ? 0.1198 0.2166 0.2435 -0.0430 0.0406  -0.0420 301 ILE B CB  
6611  C CG1 . ILE B 301 ? 0.1025 0.1795 0.2193 -0.0391 0.0389  -0.0401 301 ILE B CG1 
6612  C CG2 . ILE B 301 ? 0.1793 0.2841 0.3049 -0.0418 0.0405  -0.0424 301 ILE B CG2 
6613  C CD1 . ILE B 301 ? 0.0778 0.1431 0.1898 -0.0375 0.0389  -0.0358 301 ILE B CD1 
6614  N N   . SER B 302 ? 0.0809 0.1831 0.2083 -0.0391 0.0356  -0.0462 302 SER B N   
6615  C CA  . SER B 302 ? 0.0768 0.1790 0.2060 -0.0354 0.0324  -0.0458 302 SER B CA  
6616  C C   . SER B 302 ? 0.0716 0.1557 0.1956 -0.0317 0.0313  -0.0435 302 SER B C   
6617  O O   . SER B 302 ? 0.0753 0.1440 0.1924 -0.0314 0.0325  -0.0412 302 SER B O   
6618  C CB  . SER B 302 ? 0.0767 0.1781 0.2051 -0.0365 0.0313  -0.0453 302 SER B CB  
6619  O OG  . SER B 302 ? 0.0825 0.2018 0.2164 -0.0405 0.0322  -0.0479 302 SER B OG  
6620  N N   . VAL B 303 ? 0.0693 0.1572 0.1979 -0.0283 0.0290  -0.0440 303 VAL B N   
6621  C CA  . VAL B 303 ? 0.0654 0.1375 0.1910 -0.0251 0.0278  -0.0425 303 VAL B CA  
6622  C C   . VAL B 303 ? 0.0628 0.1355 0.1935 -0.0220 0.0244  -0.0411 303 VAL B C   
6623  O O   . VAL B 303 ? 0.0643 0.1555 0.2041 -0.0204 0.0227  -0.0426 303 VAL B O   
6624  C CB  . VAL B 303 ? 0.0666 0.1427 0.1945 -0.0245 0.0289  -0.0454 303 VAL B CB  
6625  C CG1 . VAL B 303 ? 0.0635 0.1234 0.1891 -0.0218 0.0278  -0.0443 303 VAL B CG1 
6626  C CG2 . VAL B 303 ? 0.0695 0.1474 0.1931 -0.0280 0.0319  -0.0453 303 VAL B CG2 
6627  N N   . PHE B 304 ? 0.0649 0.1201 0.1911 -0.0203 0.0231  -0.0372 304 PHE B N   
6628  C CA  . PHE B 304 ? 0.1025 0.1556 0.2338 -0.0175 0.0195  -0.0346 304 PHE B CA  
6629  C C   . PHE B 304 ? 0.0950 0.1335 0.2271 -0.0145 0.0185  -0.0337 304 PHE B C   
6630  O O   . PHE B 304 ? 0.1363 0.1632 0.2618 -0.0140 0.0204  -0.0313 304 PHE B O   
6631  C CB  . PHE B 304 ? 0.1815 0.2291 0.3085 -0.0183 0.0183  -0.0296 304 PHE B CB  
6632  C CG  . PHE B 304 ? 0.1017 0.1650 0.2295 -0.0218 0.0187  -0.0307 304 PHE B CG  
6633  C CD1 . PHE B 304 ? 0.0852 0.1663 0.2213 -0.0214 0.0154  -0.0298 304 PHE B CD1 
6634  C CD2 . PHE B 304 ? 0.1003 0.1624 0.2222 -0.0248 0.0220  -0.0323 304 PHE B CD2 
6635  C CE1 . PHE B 304 ? 0.0840 0.1815 0.2222 -0.0246 0.0156  -0.0302 304 PHE B CE1 
6636  C CE2 . PHE B 304 ? 0.1902 0.2662 0.3138 -0.0285 0.0224  -0.0339 304 PHE B CE2 
6637  C CZ  . PHE B 304 ? 0.0906 0.1844 0.2222 -0.0286 0.0192  -0.0329 304 PHE B CZ  
6638  N N   . PHE B 305 ? 0.1531 0.1952 0.2948 -0.0118 0.0153  -0.0352 305 PHE B N   
6639  C CA  . PHE B 305 ? 0.1141 0.1430 0.2590 -0.0092 0.0137  -0.0353 305 PHE B CA  
6640  C C   . PHE B 305 ? 0.1471 0.1658 0.2953 -0.0067 0.0091  -0.0285 305 PHE B C   
6641  O O   . PHE B 305 ? 0.1501 0.1767 0.3057 -0.0058 0.0050  -0.0280 305 PHE B O   
6642  C CB  . PHE B 305 ? 0.1467 0.1881 0.3019 -0.0068 0.0124  -0.0426 305 PHE B CB  
6643  C CG  . PHE B 305 ? 0.0793 0.1347 0.2320 -0.0085 0.0168  -0.0479 305 PHE B CG  
6644  C CD1 . PHE B 305 ? 0.0857 0.1629 0.2406 -0.0079 0.0180  -0.0488 305 PHE B CD1 
6645  C CD2 . PHE B 305 ? 0.1068 0.1551 0.2554 -0.0105 0.0195  -0.0510 305 PHE B CD2 
6646  C CE1 . PHE B 305 ? 0.0763 0.1665 0.2300 -0.0093 0.0217  -0.0523 305 PHE B CE1 
6647  C CE2 . PHE B 305 ? 0.0967 0.1590 0.2432 -0.0124 0.0231  -0.0549 305 PHE B CE2 
6648  C CZ  . PHE B 305 ? 0.0667 0.1494 0.2161 -0.0117 0.0241  -0.0553 305 PHE B CZ  
6649  N N   . ARG B 306 ? 0.1900 0.1983 0.3338 -0.0051 0.0088  -0.0220 306 ARG B N   
6650  C CA  . ARG B 306 ? 0.1624 0.1665 0.3086 -0.0036 0.0035  -0.0135 306 ARG B CA  
6651  C C   . ARG B 306 ? 0.1604 0.1623 0.3190 -0.0014 -0.0032 -0.0142 306 ARG B C   
6652  O O   . ARG B 306 ? 0.1936 0.1963 0.3613 0.0000  -0.0036 -0.0213 306 ARG B O   
6653  C CB  . ARG B 306 ? 0.1332 0.1352 0.2713 -0.0053 0.0030  -0.0063 306 ARG B CB  
6654  C CG  . ARG B 306 ? 0.0924 0.0927 0.2293 -0.0079 0.0021  -0.0072 306 ARG B CG  
6655  C CD  . ARG B 306 ? 0.0806 0.0758 0.2095 -0.0128 -0.0031 0.0009  306 ARG B CD  
6656  N NE  . ARG B 306 ? 0.1413 0.1274 0.2648 -0.0186 -0.0066 -0.0003 306 ARG B NE  
6657  C CZ  . ARG B 306 ? 0.0906 0.0670 0.2027 -0.0251 -0.0109 0.0049  306 ARG B CZ  
6658  N NH1 . ARG B 306 ? 0.0883 0.0675 0.1974 -0.0257 -0.0126 0.0117  306 ARG B NH1 
6659  N NH2 . ARG B 306 ? 0.1357 0.0970 0.2377 -0.0313 -0.0136 0.0022  306 ARG B NH2 
6660  N N   . ASP B 307 ? 0.2331 0.2330 0.3951 -0.0012 -0.0097 -0.0078 307 ASP B N   
6661  C CA  . ASP B 307 ? 0.1993 0.1942 0.3818 -0.0009 -0.0205 -0.0079 307 ASP B CA  
6662  C C   . ASP B 307 ? 0.1844 0.1596 0.3335 -0.0086 -0.0215 -0.0029 307 ASP B C   
6663  O O   . ASP B 307 ? 0.2118 0.1855 0.3538 -0.0121 -0.0235 0.0053  307 ASP B O   
6664  C CB  . ASP B 307 ? 0.2158 0.2111 0.4127 0.0001  -0.0287 -0.0020 307 ASP B CB  
6665  C CG  . ASP B 307 ? 0.3728 0.3390 0.5604 0.0066  -0.0378 -0.0038 307 ASP B CG  
6666  O OD1 . ASP B 307 ? 0.4746 0.4142 0.6352 0.0080  -0.0384 -0.0040 307 ASP B OD1 
6667  O OD2 . ASP B 307 ? 0.3646 0.3341 0.5593 0.0184  -0.0417 -0.0035 307 ASP B OD2 
6668  N N   . LYS B 308 ? 0.1673 0.1271 0.3067 -0.0091 -0.0215 -0.0089 308 LYS B N   
6669  C CA  . LYS B 308 ? 0.1595 0.1022 0.2809 -0.0156 -0.0232 -0.0056 308 LYS B CA  
6670  C C   . LYS B 308 ? 0.2527 0.1717 0.3604 -0.0172 -0.0299 0.0006  308 LYS B C   
6671  O O   . LYS B 308 ? 0.3378 0.2544 0.4380 -0.0238 -0.0315 0.0068  308 LYS B O   
6672  C CB  . LYS B 308 ? 0.1431 0.0694 0.2536 -0.0151 -0.0217 -0.0144 308 LYS B CB  
6673  C CG  . LYS B 308 ? 0.1873 0.0822 0.2743 -0.0201 -0.0250 -0.0132 308 LYS B CG  
6674  C CD  . LYS B 308 ? 0.2670 0.1552 0.3441 -0.0238 -0.0217 -0.0202 308 LYS B CD  
6675  C CE  . LYS B 308 ? 0.2198 0.0808 0.2761 -0.0316 -0.0235 -0.0189 308 LYS B CE  
6676  N NZ  . LYS B 308 ? 0.2068 0.0820 0.2660 -0.0404 -0.0247 -0.0088 308 LYS B NZ  
6677  N N   . THR B 309 ? 0.3006 0.2013 0.4044 -0.0090 -0.0333 -0.0009 309 THR B N   
6678  C CA  . THR B 309 ? 0.2877 0.1635 0.3780 -0.0087 -0.0386 0.0054  309 THR B CA  
6679  C C   . THR B 309 ? 0.2127 0.1065 0.3108 -0.0155 -0.0411 0.0150  309 THR B C   
6680  O O   . THR B 309 ? 0.3397 0.2251 0.4294 -0.0218 -0.0441 0.0209  309 THR B O   
6681  C CB  . THR B 309 ? 0.3433 0.1965 0.4271 0.0070  -0.0401 0.0032  309 THR B CB  
6682  O OG1 . THR B 309 ? 0.3052 0.1504 0.3908 0.0179  -0.0389 -0.0075 309 THR B OG1 
6683  C CG2 . THR B 309 ? 0.3385 0.1600 0.4063 0.0085  -0.0443 0.0090  309 THR B CG2 
6684  N N   . LEU B 310 ? 0.2220 0.1402 0.3359 -0.0137 -0.0396 0.0161  310 LEU B N   
6685  C CA  . LEU B 310 ? 0.2634 0.1966 0.3823 -0.0181 -0.0411 0.0243  310 LEU B CA  
6686  C C   . LEU B 310 ? 0.2070 0.1540 0.3247 -0.0234 -0.0384 0.0273  310 LEU B C   
6687  O O   . LEU B 310 ? 0.2311 0.1767 0.3435 -0.0275 -0.0413 0.0339  310 LEU B O   
6688  C CB  . LEU B 310 ? 0.2206 0.1748 0.3550 -0.0145 -0.0392 0.0241  310 LEU B CB  
6689  C CG  . LEU B 310 ? 0.1393 0.0805 0.2813 -0.0075 -0.0463 0.0259  310 LEU B CG  
6690  C CD1 . LEU B 310 ? 0.1113 0.0787 0.2878 -0.0051 -0.0481 0.0250  310 LEU B CD1 
6691  C CD2 . LEU B 310 ? 0.2067 0.1330 0.3332 -0.0092 -0.0502 0.0351  310 LEU B CD2 
6692  N N   . SER B 311 ? 0.1994 0.1579 0.3207 -0.0222 -0.0326 0.0226  311 SER B N   
6693  C CA  . SER B 311 ? 0.1584 0.1261 0.2759 -0.0244 -0.0295 0.0255  311 SER B CA  
6694  C C   . SER B 311 ? 0.1953 0.1478 0.3007 -0.0311 -0.0337 0.0283  311 SER B C   
6695  O O   . SER B 311 ? 0.2086 0.1649 0.3108 -0.0340 -0.0351 0.0339  311 SER B O   
6696  C CB  . SER B 311 ? 0.1270 0.1057 0.2484 -0.0207 -0.0221 0.0199  311 SER B CB  
6697  O OG  . SER B 311 ? 0.1302 0.1189 0.2612 -0.0147 -0.0179 0.0166  311 SER B OG  
6698  N N   . ASP B 312 ? 0.2742 0.2074 0.3719 -0.0332 -0.0355 0.0241  312 ASP B N   
6699  C CA  . ASP B 312 ? 0.3008 0.2159 0.3856 -0.0398 -0.0393 0.0263  312 ASP B CA  
6700  C C   . ASP B 312 ? 0.2714 0.1707 0.3503 -0.0424 -0.0460 0.0323  312 ASP B C   
6701  O O   . ASP B 312 ? 0.3172 0.2050 0.3876 -0.0485 -0.0499 0.0360  312 ASP B O   
6702  C CB  . ASP B 312 ? 0.3049 0.2001 0.3804 -0.0406 -0.0380 0.0188  312 ASP B CB  
6703  C CG  . ASP B 312 ? 0.4109 0.3198 0.4882 -0.0418 -0.0321 0.0146  312 ASP B CG  
6704  O OD1 . ASP B 312 ? 0.4488 0.3796 0.5332 -0.0412 -0.0293 0.0182  312 ASP B OD1 
6705  O OD2 . ASP B 312 ? 0.4072 0.3025 0.4774 -0.0426 -0.0301 0.0074  312 ASP B OD2 
6706  N N   . LEU B 313 ? 0.2722 0.1701 0.3553 -0.0383 -0.0477 0.0339  313 LEU B N   
6707  C CA  . LEU B 313 ? 0.3038 0.1888 0.3816 -0.0409 -0.0537 0.0410  313 LEU B CA  
6708  C C   . LEU B 313 ? 0.2931 0.1975 0.3755 -0.0452 -0.0547 0.0480  313 LEU B C   
6709  O O   . LEU B 313 ? 0.3030 0.1983 0.3793 -0.0509 -0.0595 0.0540  313 LEU B O   
6710  C CB  . LEU B 313 ? 0.3108 0.1880 0.3906 -0.0345 -0.0549 0.0414  313 LEU B CB  
6711  C CG  . LEU B 313 ? 0.3706 0.2139 0.4387 -0.0283 -0.0567 0.0382  313 LEU B CG  
6712  C CD1 . LEU B 313 ? 0.3719 0.2132 0.4440 -0.0174 -0.0559 0.0368  313 LEU B CD1 
6713  C CD2 . LEU B 313 ? 0.3810 0.1992 0.4374 -0.0318 -0.0623 0.0449  313 LEU B CD2 
6714  N N   . ILE B 314 ? 0.2301 0.1594 0.3227 -0.0419 -0.0499 0.0474  314 ILE B N   
6715  C CA  . ILE B 314 ? 0.2039 0.1487 0.2989 -0.0438 -0.0495 0.0528  314 ILE B CA  
6716  C C   . ILE B 314 ? 0.2041 0.1487 0.2946 -0.0479 -0.0500 0.0539  314 ILE B C   
6717  O O   . ILE B 314 ? 0.1991 0.1440 0.2872 -0.0526 -0.0537 0.0601  314 ILE B O   
6718  C CB  . ILE B 314 ? 0.1767 0.1417 0.2802 -0.0377 -0.0433 0.0506  314 ILE B CB  
6719  C CG1 . ILE B 314 ? 0.2028 0.1687 0.3112 -0.0348 -0.0438 0.0504  314 ILE B CG1 
6720  C CG2 . ILE B 314 ? 0.1391 0.1150 0.2425 -0.0386 -0.0419 0.0552  314 ILE B CG2 
6721  C CD1 . ILE B 314 ? 0.1931 0.1750 0.3070 -0.0299 -0.0380 0.0488  314 ILE B CD1 
6722  N N   . GLY B 315 ? 0.1953 0.1395 0.2847 -0.0466 -0.0465 0.0484  315 GLY B N   
6723  C CA  . GLY B 315 ? 0.1586 0.1050 0.2443 -0.0502 -0.0467 0.0499  315 GLY B CA  
6724  C C   . GLY B 315 ? 0.2451 0.1729 0.3211 -0.0582 -0.0534 0.0528  315 GLY B C   
6725  O O   . GLY B 315 ? 0.3370 0.2677 0.4107 -0.0629 -0.0563 0.0574  315 GLY B O   
6726  N N   . PHE B 316 ? 0.2118 0.1183 0.2815 -0.0596 -0.0562 0.0504  316 PHE B N   
6727  C CA  . PHE B 316 ? 0.2650 0.1486 0.3231 -0.0667 -0.0617 0.0514  316 PHE B CA  
6728  C C   . PHE B 316 ? 0.2923 0.1531 0.3437 -0.0692 -0.0678 0.0550  316 PHE B C   
6729  O O   . PHE B 316 ? 0.3600 0.2017 0.4017 -0.0759 -0.0734 0.0574  316 PHE B O   
6730  C CB  . PHE B 316 ? 0.2490 0.1195 0.3012 -0.0660 -0.0583 0.0429  316 PHE B CB  
6731  C CG  . PHE B 316 ? 0.2252 0.1147 0.2820 -0.0647 -0.0524 0.0398  316 PHE B CG  
6732  C CD1 . PHE B 316 ? 0.2291 0.1218 0.2820 -0.0707 -0.0545 0.0428  316 PHE B CD1 
6733  C CD2 . PHE B 316 ? 0.3201 0.2237 0.3850 -0.0577 -0.0453 0.0345  316 PHE B CD2 
6734  C CE1 . PHE B 316 ? 0.2605 0.1689 0.3169 -0.0692 -0.0491 0.0405  316 PHE B CE1 
6735  C CE2 . PHE B 316 ? 0.3620 0.2810 0.4303 -0.0565 -0.0397 0.0320  316 PHE B CE2 
6736  C CZ  . PHE B 316 ? 0.3328 0.2536 0.3966 -0.0620 -0.0414 0.0350  316 PHE B CZ  
6737  N N   . SER B 317 ? 0.2719 0.1330 0.3275 -0.0643 -0.0673 0.0558  317 SER B N   
6738  C CA  . SER B 317 ? 0.2979 0.1338 0.3460 -0.0651 -0.0724 0.0593  317 SER B CA  
6739  C C   . SER B 317 ? 0.3042 0.1489 0.3563 -0.0677 -0.0757 0.0682  317 SER B C   
6740  O O   . SER B 317 ? 0.4159 0.2449 0.4612 -0.0738 -0.0815 0.0745  317 SER B O   
6741  C CB  . SER B 317 ? 0.3471 0.1686 0.3940 -0.0562 -0.0695 0.0534  317 SER B CB  
6742  O OG  . SER B 317 ? 0.4961 0.3144 0.5416 -0.0528 -0.0649 0.0444  317 SER B OG  
6743  N N   . TYR B 318 ? 0.2663 0.1352 0.3290 -0.0638 -0.0720 0.0688  318 TYR B N   
6744  C CA  . TYR B 318 ? 0.2668 0.1415 0.3324 -0.0653 -0.0741 0.0763  318 TYR B CA  
6745  C C   . TYR B 318 ? 0.3375 0.2202 0.4032 -0.0729 -0.0775 0.0837  318 TYR B C   
6746  O O   . TYR B 318 ? 0.3570 0.2414 0.4236 -0.0756 -0.0797 0.0907  318 TYR B O   
6747  C CB  . TYR B 318 ? 0.2631 0.1610 0.3392 -0.0595 -0.0689 0.0743  318 TYR B CB  
6748  C CG  . TYR B 318 ? 0.2798 0.1688 0.3564 -0.0529 -0.0675 0.0705  318 TYR B CG  
6749  C CD1 . TYR B 318 ? 0.3658 0.2250 0.4327 -0.0509 -0.0709 0.0709  318 TYR B CD1 
6750  C CD2 . TYR B 318 ? 0.2828 0.1913 0.3690 -0.0476 -0.0629 0.0671  318 TYR B CD2 
6751  C CE1 . TYR B 318 ? 0.3417 0.1910 0.4084 -0.0424 -0.0696 0.0683  318 TYR B CE1 
6752  C CE2 . TYR B 318 ? 0.3150 0.2161 0.4024 -0.0415 -0.0624 0.0645  318 TYR B CE2 
6753  C CZ  . TYR B 318 ? 0.3627 0.2340 0.4401 -0.0382 -0.0657 0.0652  318 TYR B CZ  
6754  O OH  . TYR B 318 ? 0.3889 0.2510 0.4662 -0.0289 -0.0651 0.0634  318 TYR B OH  
6755  N N   . HIS B 319 ? 0.3358 0.2236 0.4007 -0.0764 -0.0781 0.0830  319 HIS B N   
6756  C CA  . HIS B 319 ? 0.3064 0.2009 0.3717 -0.0836 -0.0820 0.0907  319 HIS B CA  
6757  C C   . HIS B 319 ? 0.3439 0.2152 0.4005 -0.0912 -0.0893 0.0976  319 HIS B C   
6758  O O   . HIS B 319 ? 0.4449 0.3216 0.5033 -0.0968 -0.0924 0.1058  319 HIS B O   
6759  C CB  . HIS B 319 ? 0.3663 0.2682 0.4313 -0.0858 -0.0819 0.0892  319 HIS B CB  
6760  C CG  . HIS B 319 ? 0.4169 0.2960 0.4713 -0.0905 -0.0860 0.0868  319 HIS B CG  
6761  N ND1 . HIS B 319 ? 0.3908 0.2565 0.4378 -0.1002 -0.0934 0.0929  319 HIS B ND1 
6762  C CD2 . HIS B 319 ? 0.3933 0.2595 0.4425 -0.0873 -0.0835 0.0787  319 HIS B CD2 
6763  C CE1 . HIS B 319 ? 0.4104 0.2546 0.4472 -0.1028 -0.0954 0.0883  319 HIS B CE1 
6764  N NE2 . HIS B 319 ? 0.3646 0.2087 0.4026 -0.0948 -0.0892 0.0795  319 HIS B NE2 
6765  N N   . ALA B 320 ? 0.3457 0.1896 0.3927 -0.0913 -0.0917 0.0945  320 ALA B N   
6766  C CA  . ALA B 320 ? 0.3816 0.1986 0.4188 -0.0979 -0.0985 0.1008  320 ALA B CA  
6767  C C   . ALA B 320 ? 0.3876 0.1955 0.4244 -0.0948 -0.0987 0.1056  320 ALA B C   
6768  O O   . ALA B 320 ? 0.4195 0.2084 0.4497 -0.1004 -0.1039 0.1133  320 ALA B O   
6769  C CB  . ALA B 320 ? 0.4054 0.1924 0.4308 -0.0984 -0.1007 0.0953  320 ALA B CB  
6770  N N   . TRP B 321 ? 0.3640 0.1846 0.4073 -0.0865 -0.0933 0.1019  321 TRP B N   
6771  C CA  . TRP B 321 ? 0.3752 0.1871 0.4173 -0.0828 -0.0934 0.1068  321 TRP B CA  
6772  C C   . TRP B 321 ? 0.3667 0.1971 0.4144 -0.0880 -0.0940 0.1156  321 TRP B C   
6773  O O   . TRP B 321 ? 0.4610 0.3113 0.5144 -0.0930 -0.0937 0.1173  321 TRP B O   
6774  C CB  . TRP B 321 ? 0.4204 0.2398 0.4673 -0.0726 -0.0880 0.1001  321 TRP B CB  
6775  C CG  . TRP B 321 ? 0.3672 0.1654 0.4080 -0.0658 -0.0868 0.0923  321 TRP B CG  
6776  C CD1 . TRP B 321 ? 0.3732 0.1626 0.4098 -0.0675 -0.0870 0.0860  321 TRP B CD1 
6777  C CD2 . TRP B 321 ? 0.3777 0.1606 0.4157 -0.0551 -0.0850 0.0901  321 TRP B CD2 
6778  N NE1 . TRP B 321 ? 0.3872 0.1562 0.4185 -0.0589 -0.0848 0.0793  321 TRP B NE1 
6779  C CE2 . TRP B 321 ? 0.3903 0.1551 0.4228 -0.0503 -0.0836 0.0819  321 TRP B CE2 
6780  C CE3 . TRP B 321 ? 0.3796 0.1623 0.4187 -0.0483 -0.0844 0.0950  321 TRP B CE3 
6781  C CZ2 . TRP B 321 ? 0.4049 0.1515 0.4336 -0.0376 -0.0814 0.0780  321 TRP B CZ2 
6782  C CZ3 . TRP B 321 ? 0.4123 0.1774 0.4473 -0.0356 -0.0829 0.0922  321 TRP B CZ3 
6783  C CH2 . TRP B 321 ? 0.4066 0.1539 0.4368 -0.0297 -0.0812 0.0836  321 TRP B CH2 
6784  N N   . ASN B 322 ? 0.4203 0.2432 0.4658 -0.0859 -0.0943 0.1218  322 ASN B N   
6785  C CA  . ASN B 322 ? 0.4623 0.3052 0.5135 -0.0888 -0.0929 0.1287  322 ASN B CA  
6786  C C   . ASN B 322 ? 0.4714 0.3383 0.5310 -0.0822 -0.0867 0.1225  322 ASN B C   
6787  O O   . ASN B 322 ? 0.5318 0.3943 0.5916 -0.0748 -0.0846 0.1160  322 ASN B O   
6788  C CB  . ASN B 322 ? 0.5050 0.3289 0.5487 -0.0897 -0.0959 0.1394  322 ASN B CB  
6789  C CG  . ASN B 322 ? 0.6127 0.4571 0.6608 -0.0921 -0.0935 0.1464  322 ASN B CG  
6790  O OD1 . ASN B 322 ? 0.6470 0.5030 0.6979 -0.0864 -0.0896 0.1446  322 ASN B OD1 
6791  N ND2 . ASN B 322 ? 0.7050 0.5537 0.7533 -0.1008 -0.0956 0.1547  322 ASN B ND2 
6792  N N   . ALA B 323 ? 0.3531 0.4351 0.5670 -0.1015 -0.0272 0.1630  323 ALA B N   
6793  C CA  . ALA B 323 ? 0.3461 0.4446 0.5402 -0.0957 -0.0254 0.1577  323 ALA B CA  
6794  C C   . ALA B 323 ? 0.4117 0.5107 0.5981 -0.0892 -0.0243 0.1695  323 ALA B C   
6795  O O   . ALA B 323 ? 0.3465 0.4386 0.5157 -0.0810 -0.0266 0.1555  323 ALA B O   
6796  C CB  . ALA B 323 ? 0.3386 0.4731 0.5240 -0.0956 -0.0192 0.1609  323 ALA B CB  
6797  N N   . GLU B 324 ? 0.5234 0.6299 0.7166 -0.0881 -0.0220 0.1902  324 GLU B N   
6798  C CA  . GLU B 324 ? 0.5038 0.6152 0.6906 -0.0809 -0.0221 0.2035  324 GLU B CA  
6799  C C   . GLU B 324 ? 0.4783 0.5559 0.6763 -0.0770 -0.0267 0.1990  324 GLU B C   
6800  O O   . GLU B 324 ? 0.4945 0.5734 0.6835 -0.0698 -0.0281 0.1997  324 GLU B O   
6801  C CB  . GLU B 324 ? 0.5113 0.6417 0.7039 -0.0801 -0.0191 0.2265  324 GLU B CB  
6802  C CG  . GLU B 324 ? 0.6033 0.7689 0.7842 -0.0825 -0.0134 0.2309  324 GLU B CG  
6803  C CD  . GLU B 324 ? 0.8266 1.0243 0.9921 -0.0770 -0.0110 0.2460  324 GLU B CD  
6804  O OE1 . GLU B 324 ? 0.8685 1.0638 1.0306 -0.0713 -0.0145 0.2517  324 GLU B OE1 
6805  O OE2 . GLU B 324 ? 0.7201 0.9471 0.8771 -0.0779 -0.0056 0.2514  324 GLU B OE2 
6806  N N   . ASP B 325 ? 0.4443 0.4929 0.6610 -0.0806 -0.0288 0.1926  325 ASP B N   
6807  C CA  . ASP B 325 ? 0.4434 0.4587 0.6703 -0.0755 -0.0317 0.1854  325 ASP B CA  
6808  C C   . ASP B 325 ? 0.3607 0.3650 0.5757 -0.0734 -0.0343 0.1642  325 ASP B C   
6809  O O   . ASP B 325 ? 0.3183 0.3114 0.5306 -0.0637 -0.0351 0.1596  325 ASP B O   
6810  C CB  . ASP B 325 ? 0.5608 0.5481 0.8068 -0.0810 -0.0327 0.1799  325 ASP B CB  
6811  C CG  . ASP B 325 ? 0.6907 0.6875 0.9507 -0.0844 -0.0300 0.2016  325 ASP B CG  
6812  O OD1 . ASP B 325 ? 0.7290 0.7449 0.9880 -0.0785 -0.0279 0.2220  325 ASP B OD1 
6813  O OD2 . ASP B 325 ? 0.7076 0.6941 0.9794 -0.0933 -0.0304 0.1983  325 ASP B OD2 
6814  N N   . ALA B 326 ? 0.3405 0.3515 0.5437 -0.0781 -0.0354 0.1461  326 ALA B N   
6815  C CA  . ALA B 326 ? 0.4413 0.4429 0.6277 -0.0730 -0.0378 0.1206  326 ALA B CA  
6816  C C   . ALA B 326 ? 0.4349 0.4552 0.5997 -0.0639 -0.0366 0.1183  326 ALA B C   
6817  O O   . ALA B 326 ? 0.3661 0.3758 0.5229 -0.0573 -0.0377 0.1050  326 ALA B O   
6818  C CB  . ALA B 326 ? 0.3856 0.3916 0.5666 -0.0800 -0.0398 0.1055  326 ALA B CB  
6819  N N   . VAL B 327 ? 0.4131 0.4626 0.5682 -0.0640 -0.0340 0.1301  327 VAL B N   
6820  C CA  . VAL B 327 ? 0.3429 0.4105 0.4783 -0.0573 -0.0337 0.1275  327 VAL B CA  
6821  C C   . VAL B 327 ? 0.2682 0.3341 0.4114 -0.0508 -0.0349 0.1408  327 VAL B C   
6822  O O   . VAL B 327 ? 0.2367 0.3072 0.3696 -0.0448 -0.0365 0.1335  327 VAL B O   
6823  C CB  . VAL B 327 ? 0.3261 0.4255 0.4472 -0.0594 -0.0304 0.1341  327 VAL B CB  
6824  C CG1 . VAL B 327 ? 0.2160 0.3320 0.3154 -0.0544 -0.0311 0.1272  327 VAL B CG1 
6825  C CG2 . VAL B 327 ? 0.2755 0.3771 0.3935 -0.0639 -0.0285 0.1225  327 VAL B CG2 
6826  N N   . ARG B 328 ? 0.2884 0.3486 0.4519 -0.0517 -0.0343 0.1617  328 ARG B N   
6827  C CA  . ARG B 328 ? 0.2789 0.3350 0.4542 -0.0436 -0.0355 0.1762  328 ARG B CA  
6828  C C   . ARG B 328 ? 0.2567 0.2844 0.4394 -0.0372 -0.0365 0.1595  328 ARG B C   
6829  O O   . ARG B 328 ? 0.2424 0.2749 0.4250 -0.0282 -0.0374 0.1607  328 ARG B O   
6830  C CB  . ARG B 328 ? 0.3280 0.3788 0.5262 -0.0459 -0.0341 0.2031  328 ARG B CB  
6831  C CG  . ARG B 328 ? 0.3377 0.4162 0.5356 -0.0407 -0.0345 0.2299  328 ARG B CG  
6832  C CD  . ARG B 328 ? 0.4990 0.5897 0.7052 -0.0456 -0.0315 0.2454  328 ARG B CD  
6833  N NE  . ARG B 328 ? 0.6037 0.6618 0.8345 -0.0478 -0.0304 0.2449  328 ARG B NE  
6834  C CZ  . ARG B 328 ? 0.7041 0.7611 0.9434 -0.0559 -0.0281 0.2496  328 ARG B CZ  
6835  N NH1 . ARG B 328 ? 0.7028 0.7902 0.9298 -0.0615 -0.0259 0.2558  328 ARG B NH1 
6836  N NH2 . ARG B 328 ? 0.7365 0.7621 0.9970 -0.0584 -0.0278 0.2472  328 ARG B NH2 
6837  N N   . ASP B 329 ? 0.2504 0.2507 0.4396 -0.0418 -0.0363 0.1439  329 ASP B N   
6838  C CA  . ASP B 329 ? 0.2415 0.2156 0.4347 -0.0359 -0.0362 0.1258  329 ASP B CA  
6839  C C   . ASP B 329 ? 0.2660 0.2513 0.4372 -0.0323 -0.0366 0.1069  329 ASP B C   
6840  O O   . ASP B 329 ? 0.3585 0.3372 0.5310 -0.0239 -0.0354 0.0996  329 ASP B O   
6841  C CB  . ASP B 329 ? 0.2533 0.1983 0.4560 -0.0435 -0.0369 0.1126  329 ASP B CB  
6842  C CG  . ASP B 329 ? 0.3350 0.2535 0.5390 -0.0373 -0.0361 0.0919  329 ASP B CG  
6843  O OD1 . ASP B 329 ? 0.3125 0.2335 0.4981 -0.0375 -0.0368 0.0717  329 ASP B OD1 
6844  O OD2 . ASP B 329 ? 0.3561 0.2510 0.5794 -0.0318 -0.0343 0.0961  329 ASP B OD2 
6845  N N   . PHE B 330 ? 0.3028 0.3048 0.4554 -0.0384 -0.0374 0.0994  330 PHE B N   
6846  C CA  . PHE B 330 ? 0.3063 0.3167 0.4391 -0.0363 -0.0375 0.0831  330 PHE B CA  
6847  C C   . PHE B 330 ? 0.3148 0.3451 0.4440 -0.0301 -0.0377 0.0908  330 PHE B C   
6848  O O   . PHE B 330 ? 0.2501 0.2781 0.3768 -0.0249 -0.0371 0.0814  330 PHE B O   
6849  C CB  . PHE B 330 ? 0.2115 0.2347 0.3277 -0.0429 -0.0379 0.0761  330 PHE B CB  
6850  C CG  . PHE B 330 ? 0.2352 0.2578 0.3339 -0.0420 -0.0379 0.0579  330 PHE B CG  
6851  C CD1 . PHE B 330 ? 0.2030 0.2068 0.2996 -0.0426 -0.0384 0.0427  330 PHE B CD1 
6852  C CD2 . PHE B 330 ? 0.2212 0.2618 0.3051 -0.0413 -0.0377 0.0562  330 PHE B CD2 
6853  C CE1 . PHE B 330 ? 0.2995 0.3033 0.3801 -0.0417 -0.0381 0.0290  330 PHE B CE1 
6854  C CE2 . PHE B 330 ? 0.2022 0.2398 0.2721 -0.0413 -0.0373 0.0413  330 PHE B CE2 
6855  C CZ  . PHE B 330 ? 0.1952 0.2146 0.2637 -0.0412 -0.0372 0.0291  330 PHE B CZ  
6856  N N   . ILE B 331 ? 0.2932 0.3463 0.4221 -0.0310 -0.0388 0.1084  331 ILE B N   
6857  C CA  . ILE B 331 ? 0.1869 0.2638 0.3122 -0.0265 -0.0408 0.1165  331 ILE B CA  
6858  C C   . ILE B 331 ? 0.1974 0.2661 0.3433 -0.0168 -0.0406 0.1257  331 ILE B C   
6859  O O   . ILE B 331 ? 0.2754 0.3553 0.4213 -0.0115 -0.0414 0.1229  331 ILE B O   
6860  C CB  . ILE B 331 ? 0.2163 0.3216 0.3345 -0.0299 -0.0423 0.1336  331 ILE B CB  
6861  C CG1 . ILE B 331 ? 0.1817 0.2952 0.2799 -0.0375 -0.0409 0.1222  331 ILE B CG1 
6862  C CG2 . ILE B 331 ? 0.2504 0.3837 0.3646 -0.0263 -0.0462 0.1418  331 ILE B CG2 
6863  C CD1 . ILE B 331 ? 0.1699 0.2768 0.2529 -0.0391 -0.0408 0.0987  331 ILE B CD1 
6864  N N   . GLY B 332 ? 0.2128 0.2618 0.3785 -0.0142 -0.0391 0.1371  332 GLY B N   
6865  C CA  . GLY B 332 ? 0.2270 0.2637 0.4146 -0.0030 -0.0378 0.1450  332 GLY B CA  
6866  C C   . GLY B 332 ? 0.2242 0.2450 0.4113 0.0025  -0.0348 0.1234  332 GLY B C   
6867  O O   . GLY B 332 ? 0.3137 0.3404 0.5118 0.0129  -0.0335 0.1265  332 GLY B O   
6868  N N   . ARG B 333 ? 0.2186 0.2220 0.3933 -0.0040 -0.0335 0.1023  333 ARG B N   
6869  C CA  . ARG B 333 ? 0.2172 0.2088 0.3872 0.0004  -0.0302 0.0818  333 ARG B CA  
6870  C C   . ARG B 333 ? 0.2222 0.2403 0.3787 0.0008  -0.0307 0.0773  333 ARG B C   
6871  O O   . ARG B 333 ? 0.2024 0.2237 0.3646 0.0087  -0.0275 0.0725  333 ARG B O   
6872  C CB  . ARG B 333 ? 0.2172 0.1877 0.3757 -0.0073 -0.0299 0.0626  333 ARG B CB  
6873  C CG  . ARG B 333 ? 0.2395 0.1779 0.4137 -0.0062 -0.0284 0.0585  333 ARG B CG  
6874  C CD  . ARG B 333 ? 0.2401 0.1636 0.4028 -0.0161 -0.0305 0.0414  333 ARG B CD  
6875  N NE  . ARG B 333 ? 0.3581 0.2547 0.5242 -0.0126 -0.0279 0.0232  333 ARG B NE  
6876  C CZ  . ARG B 333 ? 0.2833 0.1525 0.4651 -0.0148 -0.0282 0.0208  333 ARG B CZ  
6877  N NH1 . ARG B 333 ? 0.3263 0.1914 0.5238 -0.0210 -0.0308 0.0378  333 ARG B NH1 
6878  N NH2 . ARG B 333 ? 0.3039 0.1493 0.4853 -0.0113 -0.0256 0.0007  333 ARG B NH2 
6879  N N   . LEU B 334 ? 0.2573 0.2944 0.3968 -0.0079 -0.0342 0.0783  334 LEU B N   
6880  C CA  . LEU B 334 ? 0.2437 0.3051 0.3719 -0.0097 -0.0355 0.0747  334 LEU B CA  
6881  C C   . LEU B 334 ? 0.2319 0.3156 0.3751 -0.0021 -0.0370 0.0898  334 LEU B C   
6882  O O   . LEU B 334 ? 0.1929 0.2904 0.3374 0.0003  -0.0362 0.0851  334 LEU B O   
6883  C CB  . LEU B 334 ? 0.1680 0.2441 0.2773 -0.0196 -0.0389 0.0741  334 LEU B CB  
6884  C CG  . LEU B 334 ? 0.2241 0.2862 0.3167 -0.0265 -0.0377 0.0581  334 LEU B CG  
6885  C CD1 . LEU B 334 ? 0.1585 0.2379 0.2342 -0.0337 -0.0399 0.0571  334 LEU B CD1 
6886  C CD2 . LEU B 334 ? 0.2168 0.2681 0.3040 -0.0254 -0.0348 0.0426  334 LEU B CD2 
6887  N N   . LYS B 335 ? 0.2535 0.3432 0.4097 0.0016  -0.0394 0.1096  335 LYS B N   
6888  C CA  . LYS B 335 ? 0.1961 0.3085 0.3694 0.0105  -0.0417 0.1275  335 LYS B CA  
6889  C C   . LYS B 335 ? 0.2124 0.3146 0.4040 0.0225  -0.0365 0.1226  335 LYS B C   
6890  O O   . LYS B 335 ? 0.2285 0.3553 0.4278 0.0274  -0.0373 0.1259  335 LYS B O   
6891  C CB  . LYS B 335 ? 0.2409 0.3541 0.4271 0.0138  -0.0438 0.1513  335 LYS B CB  
6892  C CG  . LYS B 335 ? 0.3335 0.4833 0.5102 0.0090  -0.0504 0.1679  335 LYS B CG  
6893  C CD  . LYS B 335 ? 0.3362 0.4830 0.5193 0.0087  -0.0510 0.1896  335 LYS B CD  
6894  C CE  . LYS B 335 ? 0.3647 0.5427 0.5261 -0.0008 -0.0555 0.1966  335 LYS B CE  
6895  N NZ  . LYS B 335 ? 0.4416 0.6193 0.6081 -0.0021 -0.0548 0.2188  335 LYS B NZ  
6896  N N   . LYS B 336 ? 0.2714 0.3389 0.4707 0.0272  -0.0309 0.1137  336 LYS B N   
6897  C CA  . LYS B 336 ? 0.2930 0.3488 0.5097 0.0405  -0.0244 0.1078  336 LYS B CA  
6898  C C   . LYS B 336 ? 0.2879 0.3509 0.4923 0.0387  -0.0205 0.0882  336 LYS B C   
6899  O O   . LYS B 336 ? 0.3236 0.3939 0.5418 0.0496  -0.0152 0.0864  336 LYS B O   
6900  C CB  . LYS B 336 ? 0.3073 0.3222 0.5342 0.0448  -0.0199 0.1018  336 LYS B CB  
6901  C CG  . LYS B 336 ? 0.3932 0.4005 0.6425 0.0511  -0.0216 0.1254  336 LYS B CG  
6902  C CD  . LYS B 336 ? 0.2814 0.2472 0.5376 0.0487  -0.0193 0.1198  336 LYS B CD  
6903  C CE  . LYS B 336 ? 0.5197 0.4748 0.8031 0.0568  -0.0196 0.1452  336 LYS B CE  
6904  N NZ  . LYS B 336 ? 0.6050 0.5448 0.8879 0.0446  -0.0227 0.1545  336 LYS B NZ  
6905  N N   . ILE B 337 ? 0.2479 0.3098 0.4278 0.0257  -0.0222 0.0748  337 ILE B N   
6906  C CA  . ILE B 337 ? 0.1882 0.2622 0.3563 0.0222  -0.0194 0.0614  337 ILE B CA  
6907  C C   . ILE B 337 ? 0.1791 0.2908 0.3530 0.0209  -0.0233 0.0724  337 ILE B C   
6908  O O   . ILE B 337 ? 0.2276 0.3552 0.4085 0.0247  -0.0194 0.0691  337 ILE B O   
6909  C CB  . ILE B 337 ? 0.1785 0.2416 0.3208 0.0092  -0.0210 0.0475  337 ILE B CB  
6910  C CG1 . ILE B 337 ? 0.1885 0.2187 0.3262 0.0097  -0.0184 0.0360  337 ILE B CG1 
6911  C CG2 . ILE B 337 ? 0.1701 0.2457 0.3012 0.0045  -0.0183 0.0370  337 ILE B CG2 
6912  C CD1 . ILE B 337 ? 0.1804 0.2023 0.2979 -0.0020 -0.0220 0.0287  337 ILE B CD1 
6913  N N   . HIS B 338 ? 0.1751 0.3040 0.3459 0.0150  -0.0311 0.0855  338 HIS B N   
6914  C CA  . HIS B 338 ? 0.1785 0.3452 0.3512 0.0107  -0.0369 0.0941  338 HIS B CA  
6915  C C   . HIS B 338 ? 0.2402 0.4286 0.4402 0.0240  -0.0359 0.1076  338 HIS B C   
6916  O O   . HIS B 338 ? 0.2591 0.4742 0.4656 0.0228  -0.0361 0.1065  338 HIS B O   
6917  C CB  . HIS B 338 ? 0.2022 0.3822 0.3640 0.0029  -0.0451 0.1048  338 HIS B CB  
6918  C CG  . HIS B 338 ? 0.2341 0.4540 0.3944 -0.0034 -0.0528 0.1119  338 HIS B CG  
6919  N ND1 . HIS B 338 ? 0.2031 0.4527 0.3825 0.0044  -0.0577 0.1317  338 HIS B ND1 
6920  C CD2 . HIS B 338 ? 0.2257 0.4607 0.3681 -0.0172 -0.0571 0.1016  338 HIS B CD2 
6921  C CE1 . HIS B 338 ? 0.1681 0.4522 0.3402 -0.0054 -0.0656 0.1326  338 HIS B CE1 
6922  N NE2 . HIS B 338 ? 0.2543 0.5285 0.4040 -0.0190 -0.0651 0.1135  338 HIS B NE2 
6923  N N   . GLU B 339 ? 0.2610 0.4384 0.4797 0.0369  -0.0345 0.1212  339 GLU B N   
6924  C CA  . GLU B 339 ? 0.1977 0.3937 0.4457 0.0527  -0.0330 0.1361  339 GLU B CA  
6925  C C   . GLU B 339 ? 0.2079 0.3807 0.4699 0.0662  -0.0215 0.1245  339 GLU B C   
6926  O O   . GLU B 339 ? 0.4080 0.5774 0.6960 0.0831  -0.0176 0.1356  339 GLU B O   
6927  C CB  . GLU B 339 ? 0.3132 0.5123 0.5760 0.0605  -0.0380 0.1607  339 GLU B CB  
6928  C CG  . GLU B 339 ? 0.5087 0.6662 0.7697 0.0618  -0.0349 0.1609  339 GLU B CG  
6929  C CD  . GLU B 339 ? 0.5999 0.7672 0.8599 0.0584  -0.0424 0.1837  339 GLU B CD  
6930  O OE1 . GLU B 339 ? 0.4942 0.6985 0.7441 0.0510  -0.0506 0.1931  339 GLU B OE1 
6931  O OE2 . GLU B 339 ? 0.4900 0.6286 0.7591 0.0625  -0.0400 0.1922  339 GLU B OE2 
6932  N N   . SER B 340 ? 0.2376 0.3944 0.4824 0.0597  -0.0155 0.1023  340 SER B N   
6933  C CA  . SER B 340 ? 0.2677 0.4089 0.5207 0.0711  -0.0040 0.0886  340 SER B CA  
6934  C C   . SER B 340 ? 0.2692 0.4348 0.5179 0.0670  0.0006  0.0787  340 SER B C   
6935  O O   . SER B 340 ? 0.3426 0.5023 0.5981 0.0773  0.0114  0.0682  340 SER B O   
6936  C CB  . SER B 340 ? 0.2943 0.3917 0.5306 0.0684  0.0004  0.0705  340 SER B CB  
6937  O OG  . SER B 340 ? 0.2216 0.3172 0.4319 0.0551  0.0012  0.0541  340 SER B OG  
6938  N N   . VAL B 341 ? 0.2869 0.4788 0.5242 0.0520  -0.0066 0.0812  341 VAL B N   
6939  C CA  . VAL B 341 ? 0.2307 0.4457 0.4653 0.0451  -0.0028 0.0739  341 VAL B CA  
6940  C C   . VAL B 341 ? 0.2632 0.5228 0.5110 0.0392  -0.0114 0.0885  341 VAL B C   
6941  O O   . VAL B 341 ? 0.3515 0.6212 0.5987 0.0352  -0.0219 0.1005  341 VAL B O   
6942  C CB  . VAL B 341 ? 0.1701 0.3667 0.3741 0.0288  -0.0027 0.0579  341 VAL B CB  
6943  C CG1 . VAL B 341 ? 0.1796 0.3371 0.3705 0.0341  0.0045  0.0435  341 VAL B CG1 
6944  C CG2 . VAL B 341 ? 0.2057 0.4024 0.3934 0.0142  -0.0141 0.0615  341 VAL B CG2 
6945  N N   . ASP B 342 ? 0.2876 0.5763 0.5472 0.0380  -0.0070 0.0876  342 ASP B N   
6946  C CA  . ASP B 342 ? 0.2649 0.5998 0.5391 0.0305  -0.0158 0.1001  342 ASP B CA  
6947  C C   . ASP B 342 ? 0.2704 0.6113 0.5225 0.0066  -0.0234 0.0923  342 ASP B C   
6948  O O   . ASP B 342 ? 0.3591 0.7285 0.6133 -0.0035 -0.0344 0.0998  342 ASP B O   
6949  C CB  . ASP B 342 ? 0.2320 0.6000 0.5343 0.0401  -0.0074 0.1044  342 ASP B CB  
6950  C CG  . ASP B 342 ? 0.3820 0.7494 0.7113 0.0657  -0.0006 0.1141  342 ASP B CG  
6951  O OD1 . ASP B 342 ? 0.4141 0.7737 0.7470 0.0727  -0.0079 0.1259  342 ASP B OD1 
6952  O OD2 . ASP B 342 ? 0.5204 0.8906 0.8638 0.0785  0.0127  0.1087  342 ASP B OD2 
6953  N N   . PHE B 343 ? 0.1980 0.5096 0.4272 -0.0023 -0.0178 0.0766  343 PHE B N   
6954  C CA  . PHE B 343 ? 0.1440 0.4526 0.3520 -0.0234 -0.0236 0.0681  343 PHE B CA  
6955  C C   . PHE B 343 ? 0.1992 0.4815 0.3842 -0.0281 -0.0308 0.0647  343 PHE B C   
6956  O O   . PHE B 343 ? 0.2203 0.4893 0.4069 -0.0167 -0.0316 0.0704  343 PHE B O   
6957  C CB  . PHE B 343 ? 0.1450 0.4364 0.3414 -0.0292 -0.0135 0.0558  343 PHE B CB  
6958  C CG  . PHE B 343 ? 0.1609 0.4164 0.3459 -0.0169 -0.0042 0.0476  343 PHE B CG  
6959  C CD1 . PHE B 343 ? 0.1563 0.4144 0.3570 0.0002  0.0062  0.0484  343 PHE B CD1 
6960  C CD2 . PHE B 343 ? 0.2015 0.4220 0.3609 -0.0223 -0.0059 0.0382  343 PHE B CD2 
6961  C CE1 . PHE B 343 ? 0.1643 0.3895 0.3531 0.0101  0.0139  0.0383  343 PHE B CE1 
6962  C CE2 . PHE B 343 ? 0.2371 0.4278 0.3865 -0.0127 0.0010  0.0301  343 PHE B CE2 
6963  C CZ  . PHE B 343 ? 0.1633 0.3557 0.3263 0.0028  0.0105  0.0293  343 PHE B CZ  
6964  N N   . GLN B 344 ? 0.2340 0.5084 0.3987 -0.0451 -0.0353 0.0555  344 GLN B N   
6965  C CA  . GLN B 344 ? 0.1743 0.4234 0.3163 -0.0493 -0.0398 0.0501  344 GLN B CA  
6966  C C   . GLN B 344 ? 0.1966 0.4075 0.3227 -0.0472 -0.0318 0.0389  344 GLN B C   
6967  O O   . GLN B 344 ? 0.2337 0.4366 0.3513 -0.0559 -0.0279 0.0305  344 GLN B O   
6968  C CB  . GLN B 344 ? 0.1449 0.4045 0.2735 -0.0670 -0.0485 0.0446  344 GLN B CB  
6969  C CG  . GLN B 344 ? 0.2245 0.5204 0.3629 -0.0692 -0.0581 0.0546  344 GLN B CG  
6970  C CD  . GLN B 344 ? 0.2646 0.5560 0.3800 -0.0832 -0.0641 0.0446  344 GLN B CD  
6971  O OE1 . GLN B 344 ? 0.2804 0.5663 0.3798 -0.0834 -0.0682 0.0440  344 GLN B OE1 
6972  N NE2 . GLN B 344 ? 0.2512 0.5460 0.3661 -0.0947 -0.0638 0.0371  344 GLN B NE2 
6973  N N   . PRO B 345 ? 0.1646 0.3525 0.2870 -0.0366 -0.0295 0.0393  345 PRO B N   
6974  C CA  . PRO B 345 ? 0.1442 0.3002 0.2529 -0.0344 -0.0229 0.0287  345 PRO B CA  
6975  C C   . PRO B 345 ? 0.1717 0.3088 0.2582 -0.0446 -0.0263 0.0208  345 PRO B C   
6976  O O   . PRO B 345 ? 0.1689 0.3111 0.2495 -0.0498 -0.0329 0.0230  345 PRO B O   
6977  C CB  . PRO B 345 ? 0.1480 0.2892 0.2646 -0.0206 -0.0207 0.0324  345 PRO B CB  
6978  C CG  . PRO B 345 ? 0.1473 0.3046 0.2732 -0.0190 -0.0282 0.0454  345 PRO B CG  
6979  C CD  . PRO B 345 ? 0.1442 0.3352 0.2752 -0.0274 -0.0337 0.0504  345 PRO B CD  
6980  N N   . VAL B 346 ? 0.1863 0.3029 0.2605 -0.0464 -0.0211 0.0120  346 VAL B N   
6981  C CA  . VAL B 346 ? 0.1459 0.2412 0.2014 -0.0521 -0.0230 0.0051  346 VAL B CA  
6982  C C   . VAL B 346 ? 0.1620 0.2356 0.2127 -0.0437 -0.0204 0.0019  346 VAL B C   
6983  O O   . VAL B 346 ? 0.2279 0.2959 0.2807 -0.0376 -0.0149 -0.0011 346 VAL B O   
6984  C CB  . VAL B 346 ? 0.1504 0.2403 0.1960 -0.0619 -0.0206 -0.0005 346 VAL B CB  
6985  C CG1 . VAL B 346 ? 0.1752 0.2556 0.2176 -0.0579 -0.0129 -0.0030 346 VAL B CG1 
6986  C CG2 . VAL B 346 ? 0.1531 0.2260 0.1830 -0.0679 -0.0239 -0.0060 346 VAL B CG2 
6987  N N   . VAL B 347 ? 0.1664 0.2302 0.2115 -0.0436 -0.0245 0.0021  347 VAL B N   
6988  C CA  . VAL B 347 ? 0.1494 0.1951 0.1930 -0.0378 -0.0238 -0.0003 347 VAL B CA  
6989  C C   . VAL B 347 ? 0.1683 0.1998 0.1964 -0.0423 -0.0252 -0.0062 347 VAL B C   
6990  O O   . VAL B 347 ? 0.1655 0.1994 0.1887 -0.0465 -0.0283 -0.0051 347 VAL B O   
6991  C CB  . VAL B 347 ? 0.1473 0.1956 0.2023 -0.0334 -0.0269 0.0079  347 VAL B CB  
6992  C CG1 . VAL B 347 ? 0.1776 0.2062 0.2339 -0.0292 -0.0262 0.0045  347 VAL B CG1 
6993  C CG2 . VAL B 347 ? 0.1611 0.2261 0.2332 -0.0277 -0.0262 0.0165  347 VAL B CG2 
6994  N N   . PHE B 348 ? 0.2206 0.2393 0.2410 -0.0406 -0.0226 -0.0124 348 PHE B N   
6995  C CA  . PHE B 348 ? 0.1895 0.1965 0.1970 -0.0433 -0.0241 -0.0163 348 PHE B CA  
6996  C C   . PHE B 348 ? 0.2010 0.1985 0.2097 -0.0402 -0.0269 -0.0181 348 PHE B C   
6997  O O   . PHE B 348 ? 0.2217 0.2139 0.2337 -0.0364 -0.0258 -0.0216 348 PHE B O   
6998  C CB  . PHE B 348 ? 0.1615 0.1638 0.1587 -0.0443 -0.0204 -0.0196 348 PHE B CB  
6999  C CG  . PHE B 348 ? 0.1632 0.1660 0.1547 -0.0508 -0.0196 -0.0181 348 PHE B CG  
7000  C CD1 . PHE B 348 ? 0.2142 0.2288 0.2122 -0.0557 -0.0181 -0.0158 348 PHE B CD1 
7001  C CD2 . PHE B 348 ? 0.2284 0.2193 0.2097 -0.0521 -0.0207 -0.0190 348 PHE B CD2 
7002  C CE1 . PHE B 348 ? 0.2709 0.2830 0.2646 -0.0635 -0.0178 -0.0159 348 PHE B CE1 
7003  C CE2 . PHE B 348 ? 0.2086 0.1951 0.1861 -0.0579 -0.0195 -0.0182 348 PHE B CE2 
7004  C CZ  . PHE B 348 ? 0.1882 0.1839 0.1716 -0.0644 -0.0180 -0.0175 348 PHE B CZ  
7005  N N   . VAL B 349 ? 0.1774 0.1737 0.1844 -0.0421 -0.0301 -0.0166 349 VAL B N   
7006  C CA  . VAL B 349 ? 0.1645 0.1553 0.1753 -0.0412 -0.0333 -0.0170 349 VAL B CA  
7007  C C   . VAL B 349 ? 0.1969 0.1832 0.1977 -0.0418 -0.0350 -0.0200 349 VAL B C   
7008  O O   . VAL B 349 ? 0.2217 0.2110 0.2203 -0.0425 -0.0353 -0.0179 349 VAL B O   
7009  C CB  . VAL B 349 ? 0.1888 0.1871 0.2096 -0.0422 -0.0349 -0.0098 349 VAL B CB  
7010  C CG1 . VAL B 349 ? 0.1734 0.1669 0.2017 -0.0429 -0.0380 -0.0092 349 VAL B CG1 
7011  C CG2 . VAL B 349 ? 0.2341 0.2394 0.2648 -0.0405 -0.0337 -0.0039 349 VAL B CG2 
7012  N N   . VAL B 350 ? 0.1634 0.1437 0.1579 -0.0407 -0.0361 -0.0249 350 VAL B N   
7013  C CA  . VAL B 350 ? 0.1681 0.1462 0.1529 -0.0402 -0.0385 -0.0257 350 VAL B CA  
7014  C C   . VAL B 350 ? 0.1729 0.1508 0.1608 -0.0409 -0.0440 -0.0291 350 VAL B C   
7015  O O   . VAL B 350 ? 0.1808 0.1547 0.1681 -0.0413 -0.0449 -0.0353 350 VAL B O   
7016  C CB  . VAL B 350 ? 0.1763 0.1515 0.1482 -0.0395 -0.0355 -0.0269 350 VAL B CB  
7017  C CG1 . VAL B 350 ? 0.1829 0.1565 0.1459 -0.0380 -0.0381 -0.0242 350 VAL B CG1 
7018  C CG2 . VAL B 350 ? 0.1732 0.1496 0.1454 -0.0412 -0.0302 -0.0242 350 VAL B CG2 
7019  N N   . LEU B 351 ? 0.1702 0.1533 0.1623 -0.0410 -0.0477 -0.0259 351 LEU B N   
7020  C CA  . LEU B 351 ? 0.1754 0.1620 0.1724 -0.0433 -0.0543 -0.0284 351 LEU B CA  
7021  C C   . LEU B 351 ? 0.2058 0.2018 0.2055 -0.0412 -0.0571 -0.0230 351 LEU B C   
7022  O O   . LEU B 351 ? 0.1677 0.1650 0.1675 -0.0377 -0.0530 -0.0184 351 LEU B O   
7023  C CB  . LEU B 351 ? 0.2027 0.1881 0.2149 -0.0476 -0.0556 -0.0290 351 LEU B CB  
7024  C CG  . LEU B 351 ? 0.2271 0.2210 0.2528 -0.0487 -0.0541 -0.0205 351 LEU B CG  
7025  C CD1 . LEU B 351 ? 0.2088 0.2049 0.2507 -0.0548 -0.0585 -0.0194 351 LEU B CD1 
7026  C CD2 . LEU B 351 ? 0.1582 0.1508 0.1849 -0.0471 -0.0483 -0.0164 351 LEU B CD2 
7027  N N   . ASP B 352 ? 0.3313 0.3347 0.3340 -0.0433 -0.0643 -0.0245 352 ASP B N   
7028  C CA  . ASP B 352 ? 0.3141 0.3304 0.3230 -0.0402 -0.0675 -0.0184 352 ASP B CA  
7029  C C   . ASP B 352 ? 0.3112 0.3348 0.3350 -0.0397 -0.0635 -0.0131 352 ASP B C   
7030  O O   . ASP B 352 ? 0.3392 0.3656 0.3750 -0.0455 -0.0639 -0.0128 352 ASP B O   
7031  C CB  . ASP B 352 ? 0.3528 0.3803 0.3658 -0.0445 -0.0774 -0.0210 352 ASP B CB  
7032  C CG  . ASP B 352 ? 0.4986 0.5228 0.4932 -0.0445 -0.0816 -0.0266 352 ASP B CG  
7033  O OD1 . ASP B 352 ? 0.6423 0.6567 0.6299 -0.0488 -0.0813 -0.0359 352 ASP B OD1 
7034  O OD2 . ASP B 352 ? 0.5768 0.6091 0.5638 -0.0395 -0.0849 -0.0211 352 ASP B OD2 
7035  N N   . GLY B 353 ? 0.1913 0.2176 0.2141 -0.0327 -0.0590 -0.0086 353 GLY B N   
7036  C CA  . GLY B 353 ? 0.2187 0.2521 0.2509 -0.0313 -0.0532 -0.0053 353 GLY B CA  
7037  C C   . GLY B 353 ? 0.2896 0.3430 0.3392 -0.0314 -0.0549 -0.0001 353 GLY B C   
7038  O O   . GLY B 353 ? 0.3265 0.3889 0.3830 -0.0299 -0.0488 0.0031  353 GLY B O   
7039  N N   . GLU B 354 ? 0.2862 0.3501 0.3434 -0.0334 -0.0629 0.0010  354 GLU B N   
7040  C CA  . GLU B 354 ? 0.2229 0.3103 0.2997 -0.0334 -0.0647 0.0072  354 GLU B CA  
7041  C C   . GLU B 354 ? 0.2406 0.3391 0.3308 -0.0443 -0.0743 0.0069  354 GLU B C   
7042  O O   . GLU B 354 ? 0.3083 0.4295 0.4176 -0.0459 -0.0764 0.0128  354 GLU B O   
7043  C CB  . GLU B 354 ? 0.2584 0.3556 0.3366 -0.0217 -0.0644 0.0112  354 GLU B CB  
7044  C CG  . GLU B 354 ? 0.2779 0.3799 0.3530 -0.0209 -0.0748 0.0121  354 GLU B CG  
7045  C CD  . GLU B 354 ? 0.2912 0.3711 0.3437 -0.0174 -0.0743 0.0088  354 GLU B CD  
7046  O OE1 . GLU B 354 ? 0.3760 0.4413 0.4168 -0.0247 -0.0749 0.0022  354 GLU B OE1 
7047  O OE2 . GLU B 354 ? 0.2218 0.2987 0.2696 -0.0070 -0.0726 0.0137  354 GLU B OE2 
7048  N N   . ASN B 355 ? 0.2715 0.3555 0.3532 -0.0519 -0.0800 -0.0006 355 ASN B N   
7049  C CA  . ASN B 355 ? 0.2747 0.3666 0.3680 -0.0633 -0.0901 -0.0040 355 ASN B CA  
7050  C C   . ASN B 355 ? 0.3068 0.3952 0.4162 -0.0739 -0.0884 -0.0026 355 ASN B C   
7051  O O   . ASN B 355 ? 0.2452 0.3462 0.3730 -0.0843 -0.0951 -0.0016 355 ASN B O   
7052  C CB  . ASN B 355 ? 0.2805 0.3584 0.3557 -0.0662 -0.0969 -0.0150 355 ASN B CB  
7053  C CG  . ASN B 355 ? 0.3454 0.4341 0.4092 -0.0592 -0.1025 -0.0137 355 ASN B CG  
7054  O OD1 . ASN B 355 ? 0.4009 0.5126 0.4771 -0.0576 -0.1079 -0.0072 355 ASN B OD1 
7055  N ND2 . ASN B 355 ? 0.4960 0.5699 0.5369 -0.0549 -0.1013 -0.0187 355 ASN B ND2 
7056  N N   . CYS B 356 ? 0.3360 0.4080 0.4400 -0.0724 -0.0803 -0.0017 356 CYS B N   
7057  C CA  . CYS B 356 ? 0.2937 0.3572 0.4112 -0.0820 -0.0793 0.0003  356 CYS B CA  
7058  C C   . CYS B 356 ? 0.1888 0.2719 0.3272 -0.0855 -0.0750 0.0136  356 CYS B C   
7059  O O   . CYS B 356 ? 0.3117 0.3941 0.4683 -0.0965 -0.0771 0.0177  356 CYS B O   
7060  C CB  . CYS B 356 ? 0.2359 0.2777 0.3408 -0.0779 -0.0729 -0.0018 356 CYS B CB  
7061  S SG  . CYS B 356 ? 0.3165 0.3586 0.4013 -0.0647 -0.0647 -0.0003 356 CYS B SG  
7062  N N   . TRP B 357 ? 0.1581 0.2583 0.2946 -0.0764 -0.0684 0.0202  357 TRP B N   
7063  C CA  . TRP B 357 ? 0.1539 0.2727 0.3051 -0.0776 -0.0610 0.0327  357 TRP B CA  
7064  C C   . TRP B 357 ? 0.2181 0.3623 0.3950 -0.0859 -0.0648 0.0400  357 TRP B C   
7065  O O   . TRP B 357 ? 0.2951 0.4543 0.4879 -0.0908 -0.0592 0.0519  357 TRP B O   
7066  C CB  . TRP B 357 ? 0.1465 0.2743 0.2852 -0.0645 -0.0518 0.0343  357 TRP B CB  
7067  C CG  . TRP B 357 ? 0.1577 0.2628 0.2725 -0.0576 -0.0500 0.0258  357 TRP B CG  
7068  C CD1 . TRP B 357 ? 0.1719 0.2700 0.2716 -0.0485 -0.0502 0.0185  357 TRP B CD1 
7069  C CD2 . TRP B 357 ? 0.2050 0.2925 0.3106 -0.0597 -0.0478 0.0252  357 TRP B CD2 
7070  N NE1 . TRP B 357 ? 0.2122 0.2902 0.2942 -0.0464 -0.0481 0.0130  357 TRP B NE1 
7071  C CE2 . TRP B 357 ? 0.2537 0.3264 0.3392 -0.0526 -0.0468 0.0167  357 TRP B CE2 
7072  C CE3 . TRP B 357 ? 0.2380 0.3216 0.3522 -0.0666 -0.0466 0.0326  357 TRP B CE3 
7073  C CZ2 . TRP B 357 ? 0.1650 0.2227 0.2397 -0.0526 -0.0448 0.0146  357 TRP B CZ2 
7074  C CZ3 . TRP B 357 ? 0.1494 0.2171 0.2525 -0.0648 -0.0448 0.0312  357 TRP B CZ3 
7075  C CH2 . TRP B 357 ? 0.1464 0.2030 0.2304 -0.0580 -0.0441 0.0218  357 TRP B CH2 
7076  N N   . GLU B 358 ? 0.2406 0.3929 0.4226 -0.0881 -0.0743 0.0343  358 GLU B N   
7077  C CA  . GLU B 358 ? 0.1947 0.3684 0.3985 -0.0958 -0.0772 0.0393  358 GLU B CA  
7078  C C   . GLU B 358 ? 0.1829 0.3396 0.3942 -0.1085 -0.0778 0.0386  358 GLU B C   
7079  O O   . GLU B 358 ? 0.1909 0.3629 0.4208 -0.1155 -0.0761 0.0459  358 GLU B O   
7080  C CB  . GLU B 358 ? 0.1921 0.3769 0.3952 -0.0938 -0.0870 0.0322  358 GLU B CB  
7081  C CG  . GLU B 358 ? 0.2701 0.4321 0.4511 -0.0926 -0.0949 0.0189  358 GLU B CG  
7082  C CD  . GLU B 358 ? 0.3518 0.5169 0.5182 -0.0788 -0.0947 0.0192  358 GLU B CD  
7083  O OE1 . GLU B 358 ? 0.4775 0.6389 0.6306 -0.0764 -0.1029 0.0123  358 GLU B OE1 
7084  O OE2 . GLU B 358 ? 0.1978 0.3651 0.3611 -0.0681 -0.0836 0.0251  358 GLU B OE2 
7085  N N   . TYR B 359 ? 0.2052 0.3309 0.4036 -0.1112 -0.0795 0.0301  359 TYR B N   
7086  C CA  . TYR B 359 ? 0.2078 0.3138 0.4138 -0.1215 -0.0793 0.0292  359 TYR B CA  
7087  C C   . TYR B 359 ? 0.2060 0.3048 0.4170 -0.1214 -0.0706 0.0427  359 TYR B C   
7088  O O   . TYR B 359 ? 0.3054 0.3914 0.5272 -0.1294 -0.0693 0.0469  359 TYR B O   
7089  C CB  . TYR B 359 ? 0.2204 0.2977 0.4109 -0.1230 -0.0848 0.0123  359 TYR B CB  
7090  C CG  . TYR B 359 ? 0.2253 0.3115 0.4075 -0.1232 -0.0937 -0.0006 359 TYR B CG  
7091  C CD1 . TYR B 359 ? 0.2414 0.3391 0.4360 -0.1332 -0.0996 -0.0051 359 TYR B CD1 
7092  C CD2 . TYR B 359 ? 0.2522 0.3375 0.4146 -0.1137 -0.0964 -0.0071 359 TYR B CD2 
7093  C CE1 . TYR B 359 ? 0.2473 0.3571 0.4344 -0.1333 -0.1085 -0.0160 359 TYR B CE1 
7094  C CE2 . TYR B 359 ? 0.2222 0.3180 0.3763 -0.1131 -0.1047 -0.0165 359 TYR B CE2 
7095  C CZ  . TYR B 359 ? 0.2377 0.3469 0.4040 -0.1226 -0.1110 -0.0208 359 TYR B CZ  
7096  O OH  . TYR B 359 ? 0.3390 0.4621 0.4971 -0.1218 -0.1202 -0.0294 359 TYR B OH  
7097  N N   . TYR B 360 ? 0.1889 0.2960 0.3920 -0.1126 -0.0647 0.0498  360 TYR B N   
7098  C CA  . TYR B 360 ? 0.1880 0.2960 0.3950 -0.1122 -0.0563 0.0646  360 TYR B CA  
7099  C C   . TYR B 360 ? 0.1901 0.3266 0.4132 -0.1152 -0.0503 0.0795  360 TYR B C   
7100  O O   . TYR B 360 ? 0.1858 0.3460 0.4158 -0.1142 -0.0510 0.0786  360 TYR B O   
7101  C CB  . TYR B 360 ? 0.2496 0.3613 0.4416 -0.1029 -0.0520 0.0660  360 TYR B CB  
7102  C CG  . TYR B 360 ? 0.2166 0.2981 0.3910 -0.0982 -0.0539 0.0558  360 TYR B CG  
7103  C CD1 . TYR B 360 ? 0.2226 0.2888 0.3851 -0.0961 -0.0606 0.0393  360 TYR B CD1 
7104  C CD2 . TYR B 360 ? 0.1757 0.2478 0.3455 -0.0953 -0.0488 0.0639  360 TYR B CD2 
7105  C CE1 . TYR B 360 ? 0.1811 0.2233 0.3286 -0.0913 -0.0608 0.0305  360 TYR B CE1 
7106  C CE2 . TYR B 360 ? 0.1993 0.2477 0.3559 -0.0902 -0.0500 0.0554  360 TYR B CE2 
7107  C CZ  . TYR B 360 ? 0.1846 0.2182 0.3305 -0.0882 -0.0554 0.0383  360 TYR B CZ  
7108  O OH  . TYR B 360 ? 0.1809 0.1943 0.3147 -0.0827 -0.0553 0.0302  360 TYR B OH  
7109  N N   . GLU B 361 ? 0.1986 0.3340 0.4278 -0.1180 -0.0441 0.0941  361 GLU B N   
7110  C CA  . GLU B 361 ? 0.2014 0.3660 0.4418 -0.1192 -0.0363 0.1099  361 GLU B CA  
7111  C C   . GLU B 361 ? 0.1841 0.3762 0.4138 -0.1086 -0.0288 0.1121  361 GLU B C   
7112  O O   . GLU B 361 ? 0.1744 0.3615 0.3885 -0.1022 -0.0265 0.1103  361 GLU B O   
7113  C CB  . GLU B 361 ? 0.2831 0.4400 0.5292 -0.1234 -0.0316 0.1265  361 GLU B CB  
7114  C CG  . GLU B 361 ? 0.4387 0.5659 0.6966 -0.1330 -0.0377 0.1240  361 GLU B CG  
7115  C CD  . GLU B 361 ? 0.4785 0.6167 0.7563 -0.1437 -0.0393 0.1271  361 GLU B CD  
7116  O OE1 . GLU B 361 ? 0.4324 0.5986 0.7186 -0.1444 -0.0326 0.1417  361 GLU B OE1 
7117  O OE2 . GLU B 361 ? 0.5934 0.7139 0.8778 -0.1516 -0.0469 0.1142  361 GLU B OE2 
7118  N N   . GLU B 362 ? 0.2419 0.4640 0.4808 -0.1064 -0.0247 0.1152  362 GLU B N   
7119  C CA  . GLU B 362 ? 0.1703 0.4208 0.4012 -0.0948 -0.0158 0.1159  362 GLU B CA  
7120  C C   . GLU B 362 ? 0.1555 0.3961 0.3703 -0.0859 -0.0192 0.1011  362 GLU B C   
7121  O O   . GLU B 362 ? 0.1946 0.4341 0.3872 -0.0749 -0.0120 0.0969  362 GLU B O   
7122  C CB  . GLU B 362 ? 0.1756 0.4399 0.3978 -0.0922 -0.0046 0.1293  362 GLU B CB  
7123  C CG  . GLU B 362 ? 0.3473 0.6267 0.5833 -0.0985 0.0004  0.1454  362 GLU B CG  
7124  C CD  . GLU B 362 ? 0.5903 0.8514 0.8254 -0.1054 -0.0004 0.1582  362 GLU B CD  
7125  O OE1 . GLU B 362 ? 0.5228 0.7550 0.7666 -0.1135 -0.0092 0.1556  362 GLU B OE1 
7126  O OE2 . GLU B 362 ? 0.5290 0.8052 0.7542 -0.1019 0.0078  0.1704  362 GLU B OE2 
7127  N N   . ASN B 363 ? 0.1533 0.3774 0.3701 -0.0880 -0.0302 0.0895  363 ASN B N   
7128  C CA  . ASN B 363 ? 0.1480 0.3553 0.3429 -0.0763 -0.0334 0.0735  363 ASN B CA  
7129  C C   . ASN B 363 ? 0.2082 0.3885 0.3779 -0.0716 -0.0314 0.0674  363 ASN B C   
7130  O O   . ASN B 363 ? 0.2643 0.4364 0.4142 -0.0606 -0.0291 0.0576  363 ASN B O   
7131  C CB  . ASN B 363 ? 0.1445 0.3748 0.3371 -0.0625 -0.0265 0.0713  363 ASN B CB  
7132  C CG  . ASN B 363 ? 0.1733 0.3877 0.3509 -0.0522 -0.0315 0.0579  363 ASN B CG  
7133  O OD1 . ASN B 363 ? 0.1736 0.3763 0.3533 -0.0571 -0.0424 0.0526  363 ASN B OD1 
7134  N ND2 . ASN B 363 ? 0.1845 0.3981 0.3463 -0.0382 -0.0234 0.0523  363 ASN B ND2 
7135  N N   . GLY B 364 ? 0.2056 0.3724 0.3781 -0.0800 -0.0324 0.0740  364 GLY B N   
7136  C CA  . GLY B 364 ? 0.1925 0.3387 0.3451 -0.0758 -0.0310 0.0706  364 GLY B CA  
7137  C C   . GLY B 364 ? 0.2063 0.3670 0.3444 -0.0685 -0.0214 0.0752  364 GLY B C   
7138  O O   . GLY B 364 ? 0.2774 0.4258 0.4009 -0.0663 -0.0208 0.0742  364 GLY B O   
7139  N N   . ILE B 365 ? 0.1524 0.3410 0.2943 -0.0645 -0.0139 0.0796  365 ILE B N   
7140  C CA  . ILE B 365 ? 0.1561 0.3596 0.2805 -0.0571 -0.0043 0.0805  365 ILE B CA  
7141  C C   . ILE B 365 ? 0.1624 0.3685 0.2835 -0.0624 -0.0024 0.0941  365 ILE B C   
7142  O O   . ILE B 365 ? 0.1849 0.3878 0.2850 -0.0577 -0.0005 0.0897  365 ILE B O   
7143  C CB  . ILE B 365 ? 0.1587 0.3938 0.2901 -0.0516 0.0048  0.0831  365 ILE B CB  
7144  C CG1 . ILE B 365 ? 0.1578 0.3900 0.2946 -0.0447 0.0018  0.0716  365 ILE B CG1 
7145  C CG2 . ILE B 365 ? 0.1668 0.4162 0.2765 -0.0432 0.0150  0.0797  365 ILE B CG2 
7146  C CD1 . ILE B 365 ? 0.1558 0.4213 0.3103 -0.0405 0.0090  0.0773  365 ILE B CD1 
7147  N N   . PRO B 366 ? 0.1674 0.3798 0.3088 -0.0723 -0.0030 0.1116  366 PRO B N   
7148  C CA  . PRO B 366 ? 0.1757 0.3881 0.3139 -0.0759 -0.0018 0.1267  366 PRO B CA  
7149  C C   . PRO B 366 ? 0.1738 0.3567 0.3019 -0.0743 -0.0090 0.1197  366 PRO B C   
7150  O O   . PRO B 366 ? 0.2802 0.4668 0.3948 -0.0714 -0.0077 0.1252  366 PRO B O   
7151  C CB  . PRO B 366 ? 0.1833 0.4010 0.3503 -0.0878 -0.0023 0.1461  366 PRO B CB  
7152  C CG  . PRO B 366 ? 0.1794 0.4143 0.3614 -0.0897 -0.0004 0.1428  366 PRO B CG  
7153  C CD  . PRO B 366 ? 0.1683 0.3902 0.3377 -0.0813 -0.0047 0.1202  366 PRO B CD  
7154  N N   . PHE B 367 ? 0.1728 0.3294 0.3070 -0.0758 -0.0165 0.1077  367 PHE B N   
7155  C CA  . PHE B 367 ? 0.1684 0.2988 0.2946 -0.0736 -0.0220 0.1008  367 PHE B CA  
7156  C C   . PHE B 367 ? 0.2248 0.3550 0.3259 -0.0650 -0.0210 0.0870  367 PHE B C   
7157  O O   . PHE B 367 ? 0.3307 0.4580 0.4218 -0.0625 -0.0216 0.0890  367 PHE B O   
7158  C CB  . PHE B 367 ? 0.2336 0.3386 0.3709 -0.0776 -0.0293 0.0904  367 PHE B CB  
7159  C CG  . PHE B 367 ? 0.1657 0.2464 0.2920 -0.0731 -0.0334 0.0789  367 PHE B CG  
7160  C CD1 . PHE B 367 ? 0.1779 0.2440 0.3113 -0.0737 -0.0348 0.0865  367 PHE B CD1 
7161  C CD2 . PHE B 367 ? 0.1578 0.2312 0.2686 -0.0678 -0.0353 0.0618  367 PHE B CD2 
7162  C CE1 . PHE B 367 ? 0.1732 0.2204 0.2984 -0.0686 -0.0373 0.0761  367 PHE B CE1 
7163  C CE2 . PHE B 367 ? 0.1628 0.2172 0.2644 -0.0642 -0.0379 0.0525  367 PHE B CE2 
7164  C CZ  . PHE B 367 ? 0.1644 0.2070 0.2734 -0.0644 -0.0386 0.0591  367 PHE B CZ  
7165  N N   . LEU B 368 ? 0.1846 0.3178 0.2770 -0.0606 -0.0196 0.0734  368 LEU B N   
7166  C CA  . LEU B 368 ? 0.1534 0.2819 0.2240 -0.0538 -0.0186 0.0595  368 LEU B CA  
7167  C C   . LEU B 368 ? 0.1599 0.3089 0.2158 -0.0514 -0.0129 0.0633  368 LEU B C   
7168  O O   . LEU B 368 ? 0.1764 0.3212 0.2171 -0.0497 -0.0143 0.0574  368 LEU B O   
7169  C CB  . LEU B 368 ? 0.1499 0.2758 0.2172 -0.0489 -0.0179 0.0465  368 LEU B CB  
7170  C CG  . LEU B 368 ? 0.1454 0.2516 0.2200 -0.0504 -0.0249 0.0398  368 LEU B CG  
7171  C CD1 . LEU B 368 ? 0.1729 0.2865 0.2526 -0.0465 -0.0244 0.0349  368 LEU B CD1 
7172  C CD2 . LEU B 368 ? 0.1438 0.2290 0.2042 -0.0481 -0.0280 0.0295  368 LEU B CD2 
7173  N N   . GLU B 369 ? 0.1844 0.3582 0.2443 -0.0518 -0.0065 0.0729  369 GLU B N   
7174  C CA  . GLU B 369 ? 0.1811 0.3778 0.2243 -0.0497 -0.0008 0.0762  369 GLU B CA  
7175  C C   . GLU B 369 ? 0.2352 0.4340 0.2762 -0.0534 -0.0047 0.0892  369 GLU B C   
7176  O O   . GLU B 369 ? 0.1854 0.3911 0.2076 -0.0517 -0.0054 0.0844  369 GLU B O   
7177  C CB  . GLU B 369 ? 0.1823 0.4082 0.2319 -0.0496 0.0080  0.0863  369 GLU B CB  
7178  C CG  . GLU B 369 ? 0.2707 0.5030 0.3161 -0.0421 0.0144  0.0716  369 GLU B CG  
7179  C CD  . GLU B 369 ? 0.3074 0.5729 0.3603 -0.0408 0.0246  0.0819  369 GLU B CD  
7180  O OE1 . GLU B 369 ? 0.3067 0.5883 0.3724 -0.0479 0.0258  0.1023  369 GLU B OE1 
7181  O OE2 . GLU B 369 ? 0.2528 0.5286 0.3001 -0.0324 0.0321  0.0701  369 GLU B OE2 
7182  N N   . LYS B 370 ? 0.2936 0.4861 0.3549 -0.0584 -0.0078 0.1057  370 LYS B N   
7183  C CA  . LYS B 370 ? 0.2763 0.4688 0.3395 -0.0600 -0.0115 0.1204  370 LYS B CA  
7184  C C   . LYS B 370 ? 0.2695 0.4421 0.3253 -0.0571 -0.0180 0.1082  370 LYS B C   
7185  O O   . LYS B 370 ? 0.3780 0.5608 0.4234 -0.0557 -0.0202 0.1122  370 LYS B O   
7186  C CB  . LYS B 370 ? 0.2598 0.4433 0.3494 -0.0655 -0.0130 0.1394  370 LYS B CB  
7187  C CG  . LYS B 370 ? 0.2982 0.4810 0.3939 -0.0654 -0.0161 0.1581  370 LYS B CG  
7188  C CD  . LYS B 370 ? 0.4712 0.6670 0.5842 -0.0708 -0.0124 0.1849  370 LYS B CD  
7189  C CE  . LYS B 370 ? 0.3354 0.5700 0.4329 -0.0708 -0.0052 0.1942  370 LYS B CE  
7190  N NZ  . LYS B 370 ? 0.4279 0.6799 0.4979 -0.0652 -0.0066 0.1874  370 LYS B NZ  
7191  N N   . LEU B 371 ? 0.2467 0.3939 0.3079 -0.0565 -0.0210 0.0941  371 LEU B N   
7192  C CA  . LEU B 371 ? 0.1802 0.3098 0.2362 -0.0541 -0.0259 0.0835  371 LEU B CA  
7193  C C   . LEU B 371 ? 0.3036 0.4432 0.3376 -0.0520 -0.0254 0.0711  371 LEU B C   
7194  O O   . LEU B 371 ? 0.3380 0.4827 0.3664 -0.0517 -0.0287 0.0728  371 LEU B O   
7195  C CB  . LEU B 371 ? 0.1580 0.2622 0.2212 -0.0541 -0.0282 0.0707  371 LEU B CB  
7196  C CG  . LEU B 371 ? 0.1530 0.2405 0.2081 -0.0514 -0.0313 0.0567  371 LEU B CG  
7197  C CD1 . LEU B 371 ? 0.1558 0.2392 0.2183 -0.0499 -0.0339 0.0645  371 LEU B CD1 
7198  C CD2 . LEU B 371 ? 0.1490 0.2168 0.2083 -0.0516 -0.0330 0.0455  371 LEU B CD2 
7199  N N   . TYR B 372 ? 0.3729 0.5157 0.3955 -0.0508 -0.0214 0.0585  372 TYR B N   
7200  C CA  . TYR B 372 ? 0.2809 0.4286 0.2830 -0.0498 -0.0207 0.0442  372 TYR B CA  
7201  C C   . TYR B 372 ? 0.3079 0.4830 0.2976 -0.0513 -0.0200 0.0516  372 TYR B C   
7202  O O   . TYR B 372 ? 0.4186 0.5987 0.3942 -0.0530 -0.0229 0.0431  372 TYR B O   
7203  C CB  . TYR B 372 ? 0.2300 0.3736 0.2248 -0.0465 -0.0155 0.0301  372 TYR B CB  
7204  C CG  . TYR B 372 ? 0.2131 0.3326 0.2165 -0.0445 -0.0171 0.0222  372 TYR B CG  
7205  C CD1 . TYR B 372 ? 0.1779 0.2791 0.1881 -0.0462 -0.0226 0.0222  372 TYR B CD1 
7206  C CD2 . TYR B 372 ? 0.2093 0.3266 0.2134 -0.0401 -0.0129 0.0152  372 TYR B CD2 
7207  C CE1 . TYR B 372 ? 0.1513 0.2337 0.1662 -0.0446 -0.0242 0.0153  372 TYR B CE1 
7208  C CE2 . TYR B 372 ? 0.1593 0.2581 0.1703 -0.0381 -0.0154 0.0099  372 TYR B CE2 
7209  C CZ  . TYR B 372 ? 0.1527 0.2345 0.1677 -0.0409 -0.0212 0.0099  372 TYR B CZ  
7210  O OH  . TYR B 372 ? 0.1495 0.2159 0.1683 -0.0390 -0.0239 0.0050  372 TYR B OH  
7211  N N   . SER B 373 ? 0.2845 0.4795 0.2790 -0.0517 -0.0165 0.0679  373 SER B N   
7212  C CA  . SER B 373 ? 0.2905 0.5155 0.2713 -0.0530 -0.0160 0.0773  373 SER B CA  
7213  C C   . SER B 373 ? 0.3625 0.5919 0.3493 -0.0544 -0.0234 0.0915  373 SER B C   
7214  O O   . SER B 373 ? 0.4084 0.6609 0.3805 -0.0558 -0.0263 0.0942  373 SER B O   
7215  C CB  . SER B 373 ? 0.4214 0.6687 0.4066 -0.0530 -0.0091 0.0934  373 SER B CB  
7216  O OG  . SER B 373 ? 0.4142 0.6615 0.4197 -0.0552 -0.0115 0.1175  373 SER B OG  
7217  N N   . THR B 374 ? 0.3598 0.5690 0.3684 -0.0537 -0.0266 0.1006  374 THR B N   
7218  C CA  . THR B 374 ? 0.2823 0.4935 0.2998 -0.0526 -0.0328 0.1135  374 THR B CA  
7219  C C   . THR B 374 ? 0.2698 0.4738 0.2800 -0.0526 -0.0378 0.0973  374 THR B C   
7220  O O   . THR B 374 ? 0.2470 0.4683 0.2545 -0.0527 -0.0431 0.1038  374 THR B O   
7221  C CB  . THR B 374 ? 0.1902 0.3797 0.2341 -0.0509 -0.0332 0.1266  374 THR B CB  
7222  O OG1 . THR B 374 ? 0.2325 0.4350 0.2856 -0.0523 -0.0301 0.1488  374 THR B OG1 
7223  C CG2 . THR B 374 ? 0.1899 0.3724 0.2454 -0.0471 -0.0387 0.1329  374 THR B CG2 
7224  N N   . LEU B 375 ? 0.2021 0.3833 0.2097 -0.0530 -0.0363 0.0776  375 LEU B N   
7225  C CA  . LEU B 375 ? 0.1754 0.3489 0.1779 -0.0542 -0.0400 0.0635  375 LEU B CA  
7226  C C   . LEU B 375 ? 0.2864 0.4826 0.2691 -0.0587 -0.0427 0.0557  375 LEU B C   
7227  O O   . LEU B 375 ? 0.3460 0.5485 0.3285 -0.0612 -0.0480 0.0528  375 LEU B O   
7228  C CB  . LEU B 375 ? 0.1676 0.3141 0.1689 -0.0541 -0.0372 0.0460  375 LEU B CB  
7229  C CG  . LEU B 375 ? 0.1590 0.2824 0.1776 -0.0510 -0.0364 0.0491  375 LEU B CG  
7230  C CD1 . LEU B 375 ? 0.1564 0.2594 0.1703 -0.0509 -0.0341 0.0334  375 LEU B CD1 
7231  C CD2 . LEU B 375 ? 0.2114 0.3299 0.2427 -0.0488 -0.0397 0.0547  375 LEU B CD2 
7232  N N   . GLU B 376 ? 0.2963 0.5063 0.2625 -0.0600 -0.0389 0.0512  376 GLU B N   
7233  C CA  . GLU B 376 ? 0.3676 0.5991 0.3124 -0.0650 -0.0417 0.0409  376 GLU B CA  
7234  C C   . GLU B 376 ? 0.2639 0.5285 0.2075 -0.0662 -0.0478 0.0592  376 GLU B C   
7235  O O   . GLU B 376 ? 0.2764 0.5558 0.2106 -0.0709 -0.0530 0.0524  376 GLU B O   
7236  C CB  . GLU B 376 ? 0.2948 0.5309 0.2210 -0.0647 -0.0345 0.0282  376 GLU B CB  
7237  C CG  . GLU B 376 ? 0.4625 0.7179 0.3893 -0.0612 -0.0289 0.0450  376 GLU B CG  
7238  C CD  . GLU B 376 ? 0.5647 0.8167 0.4824 -0.0579 -0.0193 0.0325  376 GLU B CD  
7239  O OE1 . GLU B 376 ? 0.5270 0.7555 0.4419 -0.0568 -0.0171 0.0127  376 GLU B OE1 
7240  O OE2 . GLU B 376 ? 0.5887 0.8626 0.5033 -0.0559 -0.0134 0.0439  376 GLU B OE2 
7241  N N   . LYS B 377 ? 0.2829 0.5569 0.2386 -0.0619 -0.0464 0.0828  377 LYS B N   
7242  C CA  . LYS B 377 ? 0.3042 0.6065 0.2631 -0.0613 -0.0515 0.1035  377 LYS B CA  
7243  C C   . LYS B 377 ? 0.3485 0.6461 0.3248 -0.0597 -0.0584 0.1085  377 LYS B C   
7244  O O   . LYS B 377 ? 0.4432 0.7593 0.4188 -0.0607 -0.0616 0.1114  377 LYS B O   
7245  C CB  . LYS B 377 ? 0.3245 0.6337 0.2956 -0.0571 -0.0476 0.1295  377 LYS B CB  
7246  C CG  . LYS B 377 ? 0.3524 0.6740 0.3094 -0.0582 -0.0393 0.1279  377 LYS B CG  
7247  C CD  . LYS B 377 ? 0.4127 0.7312 0.3878 -0.0557 -0.0345 0.1521  377 LYS B CD  
7248  C CE  . LYS B 377 ? 0.5675 0.8905 0.5332 -0.0568 -0.0249 0.1469  377 LYS B CE  
7249  N NZ  . LYS B 377 ? 0.4427 0.7491 0.4335 -0.0564 -0.0203 0.1625  377 LYS B NZ  
7250  N N   . GLU B 378 ? 0.4058 0.6753 0.4002 -0.0563 -0.0578 0.1072  378 GLU B N   
7251  C CA  . GLU B 378 ? 0.2867 0.5525 0.2999 -0.0530 -0.0627 0.1127  378 GLU B CA  
7252  C C   . GLU B 378 ? 0.2445 0.5162 0.2477 -0.0595 -0.0671 0.0936  378 GLU B C   
7253  O O   . GLU B 378 ? 0.3265 0.5741 0.3264 -0.0623 -0.0638 0.0743  378 GLU B O   
7254  C CB  . GLU B 378 ? 0.2640 0.4947 0.2977 -0.0473 -0.0579 0.1127  378 GLU B CB  
7255  C CG  . GLU B 378 ? 0.3726 0.5949 0.4190 -0.0430 -0.0540 0.1310  378 GLU B CG  
7256  C CD  . GLU B 378 ? 0.4880 0.7239 0.5527 -0.0366 -0.0575 0.1575  378 GLU B CD  
7257  O OE1 . GLU B 378 ? 0.4012 0.6263 0.4804 -0.0334 -0.0544 0.1741  378 GLU B OE1 
7258  O OE2 . GLU B 378 ? 0.4187 0.6762 0.4852 -0.0347 -0.0635 0.1625  378 GLU B OE2 
7259  N N   . GLU B 379 ? 0.2771 0.5714 0.2775 -0.0611 -0.0701 0.0971  379 GLU B N   
7260  C CA  . GLU B 379 ? 0.3019 0.5996 0.2933 -0.0686 -0.0725 0.0786  379 GLU B CA  
7261  C C   . GLU B 379 ? 0.3195 0.6062 0.3286 -0.0677 -0.0744 0.0754  379 GLU B C   
7262  O O   . GLU B 379 ? 0.2892 0.5701 0.2925 -0.0750 -0.0749 0.0583  379 GLU B O   
7263  C CB  . GLU B 379 ? 0.4197 0.7475 0.4049 -0.0710 -0.0759 0.0849  379 GLU B CB  
7264  C CG  . GLU B 379 ? 0.6125 0.9567 0.6193 -0.0643 -0.0797 0.1061  379 GLU B CG  
7265  C CD  . GLU B 379 ? 0.5920 0.9362 0.6132 -0.0544 -0.0775 0.1309  379 GLU B CD  
7266  O OE1 . GLU B 379 ? 0.5425 0.8950 0.5838 -0.0470 -0.0795 0.1487  379 GLU B OE1 
7267  O OE2 . GLU B 379 ? 0.6245 0.9598 0.6386 -0.0538 -0.0735 0.1330  379 GLU B OE2 
7268  N N   . TRP B 380 ? 0.3065 0.5896 0.3384 -0.0587 -0.0747 0.0917  380 TRP B N   
7269  C CA  . TRP B 380 ? 0.1806 0.4565 0.2315 -0.0562 -0.0750 0.0892  380 TRP B CA  
7270  C C   . TRP B 380 ? 0.2210 0.4633 0.2710 -0.0570 -0.0689 0.0740  380 TRP B C   
7271  O O   . TRP B 380 ? 0.2839 0.5162 0.3462 -0.0550 -0.0663 0.0694  380 TRP B O   
7272  C CB  . TRP B 380 ? 0.2427 0.5254 0.3197 -0.0436 -0.0756 0.1113  380 TRP B CB  
7273  C CG  . TRP B 380 ? 0.1800 0.4473 0.2633 -0.0360 -0.0724 0.1249  380 TRP B CG  
7274  C CD1 . TRP B 380 ? 0.2496 0.5287 0.3257 -0.0355 -0.0734 0.1395  380 TRP B CD1 
7275  C CD2 . TRP B 380 ? 0.1823 0.4137 0.2784 -0.0288 -0.0648 0.1229  380 TRP B CD2 
7276  N NE1 . TRP B 380 ? 0.1907 0.4459 0.2778 -0.0292 -0.0683 0.1490  380 TRP B NE1 
7277  C CE2 . TRP B 380 ? 0.1821 0.4059 0.2809 -0.0253 -0.0630 0.1373  380 TRP B CE2 
7278  C CE3 . TRP B 380 ? 0.2332 0.4397 0.3379 -0.0256 -0.0595 0.1100  380 TRP B CE3 
7279  C CZ2 . TRP B 380 ? 0.2784 0.4690 0.3896 -0.0200 -0.0570 0.1379  380 TRP B CZ2 
7280  C CZ3 . TRP B 380 ? 0.1982 0.3730 0.3121 -0.0194 -0.0535 0.1097  380 TRP B CZ3 
7281  C CH2 . TRP B 380 ? 0.2782 0.4446 0.3960 -0.0172 -0.0528 0.1228  380 TRP B CH2 
7282  N N   . ILE B 381 ? 0.2994 0.5226 0.3343 -0.0587 -0.0647 0.0661  381 ILE B N   
7283  C CA  . ILE B 381 ? 0.2377 0.4272 0.2697 -0.0585 -0.0580 0.0522  381 ILE B CA  
7284  C C   . ILE B 381 ? 0.2468 0.4318 0.2582 -0.0679 -0.0578 0.0338  381 ILE B C   
7285  O O   . ILE B 381 ? 0.2645 0.4525 0.2610 -0.0698 -0.0570 0.0305  381 ILE B O   
7286  C CB  . ILE B 381 ? 0.1872 0.3580 0.2228 -0.0522 -0.0534 0.0585  381 ILE B CB  
7287  C CG1 . ILE B 381 ? 0.2627 0.4315 0.3203 -0.0431 -0.0531 0.0751  381 ILE B CG1 
7288  C CG2 . ILE B 381 ? 0.3432 0.4840 0.3738 -0.0527 -0.0482 0.0439  381 ILE B CG2 
7289  C CD1 . ILE B 381 ? 0.2347 0.3945 0.2976 -0.0395 -0.0508 0.0868  381 ILE B CD1 
7290  N N   . GLU B 382 ? 0.2116 0.3891 0.2229 -0.0735 -0.0577 0.0220  382 GLU B N   
7291  C CA  . GLU B 382 ? 0.2324 0.3973 0.2272 -0.0819 -0.0564 0.0042  382 GLU B CA  
7292  C C   . GLU B 382 ? 0.2728 0.4050 0.2668 -0.0779 -0.0496 -0.0026 382 GLU B C   
7293  O O   . GLU B 382 ? 0.3379 0.4589 0.3429 -0.0746 -0.0472 -0.0002 382 GLU B O   
7294  C CB  . GLU B 382 ? 0.2243 0.3991 0.2207 -0.0920 -0.0603 -0.0033 382 GLU B CB  
7295  C CG  . GLU B 382 ? 0.3246 0.4846 0.3041 -0.0993 -0.0582 -0.0208 382 GLU B CG  
7296  C CD  . GLU B 382 ? 0.4694 0.6332 0.4533 -0.1074 -0.0600 -0.0261 382 GLU B CD  
7297  O OE1 . GLU B 382 ? 0.4933 0.6831 0.4853 -0.1085 -0.0648 -0.0178 382 GLU B OE1 
7298  O OE2 . GLU B 382 ? 0.4570 0.5983 0.4376 -0.1128 -0.0569 -0.0374 382 GLU B OE2 
7299  N N   . THR B 383 ? 0.1812 0.3007 0.1623 -0.0774 -0.0465 -0.0107 383 THR B N   
7300  C CA  . THR B 383 ? 0.2150 0.3067 0.1946 -0.0739 -0.0412 -0.0170 383 THR B CA  
7301  C C   . THR B 383 ? 0.2320 0.3092 0.2033 -0.0810 -0.0401 -0.0309 383 THR B C   
7302  O O   . THR B 383 ? 0.2450 0.3295 0.2063 -0.0881 -0.0422 -0.0399 383 THR B O   
7303  C CB  . THR B 383 ? 0.1904 0.2776 0.1649 -0.0681 -0.0379 -0.0163 383 THR B CB  
7304  O OG1 . THR B 383 ? 0.3246 0.4140 0.2840 -0.0713 -0.0366 -0.0276 383 THR B OG1 
7305  C CG2 . THR B 383 ? 0.1991 0.3038 0.1814 -0.0639 -0.0394 -0.0016 383 THR B CG2 
7306  N N   . LEU B 384 ? 0.1803 0.2365 0.1551 -0.0795 -0.0369 -0.0324 384 LEU B N   
7307  C CA  . LEU B 384 ? 0.2024 0.2428 0.1728 -0.0866 -0.0355 -0.0418 384 LEU B CA  
7308  C C   . LEU B 384 ? 0.2161 0.2303 0.1823 -0.0812 -0.0308 -0.0451 384 LEU B C   
7309  O O   . LEU B 384 ? 0.2495 0.2590 0.2192 -0.0730 -0.0292 -0.0387 384 LEU B O   
7310  C CB  . LEU B 384 ? 0.1898 0.2351 0.1705 -0.0920 -0.0362 -0.0373 384 LEU B CB  
7311  C CG  . LEU B 384 ? 0.2247 0.2986 0.2157 -0.0937 -0.0405 -0.0295 384 LEU B CG  
7312  C CD1 . LEU B 384 ? 0.2152 0.2929 0.2185 -0.0955 -0.0386 -0.0243 384 LEU B CD1 
7313  C CD2 . LEU B 384 ? 0.1924 0.2841 0.1781 -0.1033 -0.0460 -0.0357 384 LEU B CD2 
7314  N N   . THR B 385 ? 0.2615 0.2588 0.2210 -0.0860 -0.0290 -0.0550 385 THR B N   
7315  C CA  . THR B 385 ? 0.2821 0.2537 0.2405 -0.0819 -0.0248 -0.0554 385 THR B CA  
7316  C C   . THR B 385 ? 0.3325 0.2990 0.2972 -0.0858 -0.0241 -0.0482 385 THR B C   
7317  O O   . THR B 385 ? 0.3623 0.3421 0.3324 -0.0939 -0.0259 -0.0464 385 THR B O   
7318  C CB  . THR B 385 ? 0.2598 0.2116 0.2109 -0.0852 -0.0224 -0.0678 385 THR B CB  
7319  O OG1 . THR B 385 ? 0.2596 0.2083 0.2120 -0.0987 -0.0241 -0.0730 385 THR B OG1 
7320  C CG2 . THR B 385 ? 0.2532 0.2145 0.1959 -0.0822 -0.0222 -0.0772 385 THR B CG2 
7321  N N   . LEU B 386 ? 0.3449 0.2949 0.3089 -0.0796 -0.0211 -0.0432 386 LEU B N   
7322  C CA  . LEU B 386 ? 0.2279 0.1738 0.1951 -0.0829 -0.0192 -0.0357 386 LEU B CA  
7323  C C   . LEU B 386 ? 0.3369 0.2754 0.3064 -0.0956 -0.0181 -0.0387 386 LEU B C   
7324  O O   . LEU B 386 ? 0.4142 0.3606 0.3895 -0.1018 -0.0167 -0.0326 386 LEU B O   
7325  C CB  . LEU B 386 ? 0.3185 0.2487 0.2820 -0.0745 -0.0169 -0.0295 386 LEU B CB  
7326  C CG  . LEU B 386 ? 0.2640 0.2009 0.2265 -0.0636 -0.0189 -0.0274 386 LEU B CG  
7327  C CD1 . LEU B 386 ? 0.2256 0.1489 0.1845 -0.0561 -0.0181 -0.0217 386 LEU B CD1 
7328  C CD2 . LEU B 386 ? 0.2281 0.1826 0.1943 -0.0627 -0.0204 -0.0239 386 LEU B CD2 
7329  N N   . GLU B 387 ? 0.4115 0.3355 0.3774 -0.1000 -0.0182 -0.0487 387 GLU B N   
7330  C CA  . GLU B 387 ? 0.3898 0.3074 0.3590 -0.1149 -0.0185 -0.0543 387 GLU B CA  
7331  C C   . GLU B 387 ? 0.3681 0.3162 0.3440 -0.1220 -0.0229 -0.0550 387 GLU B C   
7332  O O   . GLU B 387 ? 0.4186 0.3755 0.4038 -0.1305 -0.0227 -0.0501 387 GLU B O   
7333  C CB  . GLU B 387 ? 0.4637 0.3605 0.4275 -0.1152 -0.0179 -0.0676 387 GLU B CB  
7334  C CG  . GLU B 387 ? 0.4160 0.2870 0.3851 -0.1219 -0.0152 -0.0683 387 GLU B CG  
7335  C CD  . GLU B 387 ? 0.6619 0.5090 0.6263 -0.1176 -0.0138 -0.0817 387 GLU B CD  
7336  O OE1 . GLU B 387 ? 0.8960 0.7555 0.8541 -0.1158 -0.0166 -0.0937 387 GLU B OE1 
7337  O OE2 . GLU B 387 ? 0.7264 0.5426 0.6930 -0.1154 -0.0095 -0.0795 387 GLU B OE2 
7338  N N   . GLU B 388 ? 0.3437 0.3102 0.3160 -0.1173 -0.0267 -0.0591 388 GLU B N   
7339  C CA  . GLU B 388 ? 0.4467 0.4428 0.4253 -0.1216 -0.0314 -0.0580 388 GLU B CA  
7340  C C   . GLU B 388 ? 0.3979 0.4130 0.3878 -0.1226 -0.0312 -0.0464 388 GLU B C   
7341  O O   . GLU B 388 ? 0.4501 0.4832 0.4502 -0.1295 -0.0329 -0.0435 388 GLU B O   
7342  C CB  . GLU B 388 ? 0.4386 0.4502 0.4099 -0.1157 -0.0348 -0.0616 388 GLU B CB  
7343  C CG  . GLU B 388 ? 0.4449 0.4447 0.4050 -0.1161 -0.0348 -0.0751 388 GLU B CG  
7344  C CD  . GLU B 388 ? 0.4107 0.4282 0.3616 -0.1107 -0.0368 -0.0776 388 GLU B CD  
7345  O OE1 . GLU B 388 ? 0.3860 0.4184 0.3394 -0.1052 -0.0377 -0.0682 388 GLU B OE1 
7346  O OE2 . GLU B 388 ? 0.3852 0.4019 0.3262 -0.1122 -0.0374 -0.0889 388 GLU B OE2 
7347  N N   . ALA B 389 ? 0.3784 0.3904 0.3676 -0.1132 -0.0284 -0.0396 389 ALA B N   
7348  C CA  . ALA B 389 ? 0.2628 0.2903 0.2623 -0.1096 -0.0263 -0.0296 389 ALA B CA  
7349  C C   . ALA B 389 ? 0.3311 0.3542 0.3361 -0.1179 -0.0218 -0.0256 389 ALA B C   
7350  O O   . ALA B 389 ? 0.3664 0.4097 0.3828 -0.1193 -0.0199 -0.0191 389 ALA B O   
7351  C CB  . ALA B 389 ? 0.2010 0.2218 0.1971 -0.0956 -0.0237 -0.0250 389 ALA B CB  
7352  N N   . MET B 390 ? 0.3188 0.3163 0.3173 -0.1228 -0.0193 -0.0282 390 MET B N   
7353  C CA  . MET B 390 ? 0.3258 0.3176 0.3298 -0.1320 -0.0146 -0.0222 390 MET B CA  
7354  C C   . MET B 390 ? 0.4008 0.4044 0.4158 -0.1473 -0.0173 -0.0254 390 MET B C   
7355  O O   . MET B 390 ? 0.3426 0.3553 0.3681 -0.1552 -0.0136 -0.0180 390 MET B O   
7356  C CB  . MET B 390 ? 0.3253 0.2840 0.3202 -0.1304 -0.0110 -0.0211 390 MET B CB  
7357  C CG  . MET B 390 ? 0.4363 0.3896 0.4236 -0.1168 -0.0072 -0.0127 390 MET B CG  
7358  S SD  . MET B 390 ? 0.3862 0.3545 0.3783 -0.1191 -0.0002 0.0005  390 MET B SD  
7359  C CE  . MET B 390 ? 0.4436 0.3869 0.4367 -0.1313 0.0040  0.0077  390 MET B CE  
7360  N N   . ARG B 391 ? 0.4155 0.4209 0.4283 -0.1473 -0.0231 -0.0355 391 ARG B N   
7361  C CA  . ARG B 391 ? 0.3477 0.3648 0.3698 -0.1574 -0.0269 -0.0394 391 ARG B CA  
7362  C C   . ARG B 391 ? 0.3776 0.4315 0.4082 -0.1570 -0.0320 -0.0370 391 ARG B C   
7363  O O   . ARG B 391 ? 0.4646 0.5332 0.5042 -0.1658 -0.0358 -0.0389 391 ARG B O   
7364  C CB  . ARG B 391 ? 0.3777 0.3746 0.3911 -0.1593 -0.0303 -0.0529 391 ARG B CB  
7365  C CG  . ARG B 391 ? 0.4323 0.3920 0.4381 -0.1566 -0.0256 -0.0556 391 ARG B CG  
7366  C CD  . ARG B 391 ? 0.4788 0.4195 0.4933 -0.1680 -0.0242 -0.0567 391 ARG B CD  
7367  N NE  . ARG B 391 ? 0.6384 0.5771 0.6618 -0.1727 -0.0182 -0.0424 391 ARG B NE  
7368  C CZ  . ARG B 391 ? 0.6233 0.5466 0.6407 -0.1667 -0.0122 -0.0328 391 ARG B CZ  
7369  N NH1 . ARG B 391 ? 0.5926 0.4990 0.5969 -0.1555 -0.0117 -0.0362 391 ARG B NH1 
7370  N NH2 . ARG B 391 ? 0.6434 0.5696 0.6678 -0.1721 -0.0065 -0.0188 391 ARG B NH2 
7371  N N   . LYS B 392 ? 0.2622 0.3310 0.2915 -0.1470 -0.0325 -0.0324 392 LYS B N   
7372  C CA  . LYS B 392 ? 0.2242 0.3257 0.2612 -0.1444 -0.0380 -0.0292 392 LYS B CA  
7373  C C   . LYS B 392 ? 0.4101 0.5386 0.4664 -0.1494 -0.0370 -0.0204 392 LYS B C   
7374  O O   . LYS B 392 ? 0.4672 0.5989 0.5316 -0.1483 -0.0304 -0.0129 392 LYS B O   
7375  C CB  . LYS B 392 ? 0.2293 0.3373 0.2632 -0.1323 -0.0384 -0.0249 392 LYS B CB  
7376  C CG  . LYS B 392 ? 0.3694 0.4767 0.3909 -0.1276 -0.0434 -0.0305 392 LYS B CG  
7377  C CD  . LYS B 392 ? 0.2285 0.3642 0.2551 -0.1305 -0.0500 -0.0290 392 LYS B CD  
7378  C CE  . LYS B 392 ? 0.3686 0.5090 0.3824 -0.1252 -0.0541 -0.0316 392 LYS B CE  
7379  N NZ  . LYS B 392 ? 0.5178 0.6809 0.5307 -0.1307 -0.0605 -0.0333 392 LYS B NZ  
7380  N N   . GLU B 393 ? 0.4051 0.5557 0.4687 -0.1548 -0.0431 -0.0213 393 GLU B N   
7381  C CA  . GLU B 393 ? 0.2915 0.4718 0.3755 -0.1590 -0.0428 -0.0128 393 GLU B CA  
7382  C C   . GLU B 393 ? 0.3644 0.5749 0.4611 -0.1473 -0.0429 -0.0021 393 GLU B C   
7383  O O   . GLU B 393 ? 0.4669 0.6996 0.5821 -0.1464 -0.0387 0.0066  393 GLU B O   
7384  C CB  . GLU B 393 ? 0.3014 0.4945 0.3891 -0.1699 -0.0503 -0.0181 393 GLU B CB  
7385  C CG  . GLU B 393 ? 0.4368 0.6078 0.5238 -0.1839 -0.0492 -0.0258 393 GLU B CG  
7386  C CD  . GLU B 393 ? 0.6543 0.8404 0.7466 -0.1957 -0.0576 -0.0321 393 GLU B CD  
7387  O OE1 . GLU B 393 ? 0.7234 0.9162 0.8046 -0.1938 -0.0648 -0.0387 393 GLU B OE1 
7388  O OE2 . GLU B 393 ? 0.4787 0.6714 0.5862 -0.2073 -0.0570 -0.0302 393 GLU B OE2 
7389  N N   . ASP B 394 ? 0.2453 0.4573 0.3340 -0.1377 -0.0468 -0.0018 394 ASP B N   
7390  C CA  . ASP B 394 ? 0.2040 0.4442 0.3067 -0.1259 -0.0484 0.0093  394 ASP B CA  
7391  C C   . ASP B 394 ? 0.2859 0.5254 0.3981 -0.1157 -0.0406 0.0156  394 ASP B C   
7392  O O   . ASP B 394 ? 0.2278 0.4896 0.3560 -0.1041 -0.0403 0.0253  394 ASP B O   
7393  C CB  . ASP B 394 ? 0.3183 0.5602 0.4093 -0.1202 -0.0555 0.0090  394 ASP B CB  
7394  C CG  . ASP B 394 ? 0.4859 0.7385 0.5696 -0.1288 -0.0631 0.0041  394 ASP B CG  
7395  O OD1 . ASP B 394 ? 0.4363 0.6675 0.5034 -0.1372 -0.0641 -0.0083 394 ASP B OD1 
7396  O OD2 . ASP B 394 ? 0.6533 0.9363 0.7485 -0.1266 -0.0681 0.0127  394 ASP B OD2 
7397  N N   . VAL B 395 ? 0.3251 0.5397 0.4282 -0.1188 -0.0339 0.0106  395 VAL B N   
7398  C CA  . VAL B 395 ? 0.1609 0.3592 0.2616 -0.1029 -0.0247 0.0132  395 VAL B CA  
7399  C C   . VAL B 395 ? 0.1615 0.3768 0.2779 -0.1013 -0.0156 0.0190  395 VAL B C   
7400  O O   . VAL B 395 ? 0.2227 0.4477 0.3453 -0.1152 -0.0141 0.0197  395 VAL B O   
7401  C CB  . VAL B 395 ? 0.1653 0.3246 0.2433 -0.1028 -0.0217 0.0054  395 VAL B CB  
7402  C CG1 . VAL B 395 ? 0.1621 0.3069 0.2361 -0.0888 -0.0133 0.0065  395 VAL B CG1 
7403  C CG2 . VAL B 395 ? 0.1758 0.3222 0.2403 -0.1022 -0.0291 0.0002  395 VAL B CG2 
7404  N N   . LYS B 396 ? 0.1565 0.3755 0.2802 -0.0846 -0.0090 0.0228  396 LYS B N   
7405  C CA  . LYS B 396 ? 0.1591 0.3943 0.2958 -0.0797 0.0019  0.0270  396 LYS B CA  
7406  C C   . LYS B 396 ? 0.1667 0.3759 0.2848 -0.0809 0.0105  0.0223  396 LYS B C   
7407  O O   . LYS B 396 ? 0.1671 0.3472 0.2667 -0.0741 0.0104  0.0164  396 LYS B O   
7408  C CB  . LYS B 396 ? 0.1555 0.4018 0.3063 -0.0598 0.0063  0.0308  396 LYS B CB  
7409  C CG  . LYS B 396 ? 0.1665 0.4384 0.3356 -0.0527 0.0180  0.0353  396 LYS B CG  
7410  C CD  . LYS B 396 ? 0.1872 0.4677 0.3726 -0.0315 0.0220  0.0381  396 LYS B CD  
7411  C CE  . LYS B 396 ? 0.3246 0.6395 0.5341 -0.0237 0.0332  0.0437  396 LYS B CE  
7412  N NZ  . LYS B 396 ? 0.3233 0.6264 0.5330 -0.0027 0.0452  0.0379  396 LYS B NZ  
7413  N N   . THR B 397 ? 0.1593 0.1812 0.2111 -0.0053 0.0198  -0.0125 397 THR B N   
7414  C CA  . THR B 397 ? 0.1153 0.1276 0.1625 -0.0057 0.0269  -0.0219 397 THR B CA  
7415  C C   . THR B 397 ? 0.1625 0.1686 0.2208 0.0008  0.0314  -0.0244 397 THR B C   
7416  O O   . THR B 397 ? 0.1898 0.2052 0.2610 0.0049  0.0303  -0.0219 397 THR B O   
7417  C CB  . THR B 397 ? 0.1676 0.1865 0.2091 -0.0102 0.0280  -0.0288 397 THR B CB  
7418  O OG1 . THR B 397 ? 0.3178 0.3460 0.3506 -0.0141 0.0224  -0.0271 397 THR B OG1 
7419  C CG2 . THR B 397 ? 0.1600 0.1682 0.1920 -0.0113 0.0340  -0.0360 397 THR B CG2 
7420  N N   . GLU B 398 ? 0.1207 0.1131 0.1736 0.0023  0.0364  -0.0296 398 GLU B N   
7421  C CA  . GLU B 398 ? 0.1614 0.1479 0.2206 0.0093  0.0417  -0.0343 398 GLU B CA  
7422  C C   . GLU B 398 ? 0.1725 0.1556 0.2229 0.0071  0.0482  -0.0421 398 GLU B C   
7423  O O   . GLU B 398 ? 0.1881 0.1662 0.2270 0.0019  0.0481  -0.0439 398 GLU B O   
7424  C CB  . GLU B 398 ? 0.1684 0.1384 0.2287 0.0147  0.0400  -0.0332 398 GLU B CB  
7425  C CG  . GLU B 398 ? 0.3070 0.2683 0.3690 0.0229  0.0458  -0.0410 398 GLU B CG  
7426  C CD  . GLU B 398 ? 0.5171 0.4683 0.5882 0.0328  0.0430  -0.0392 398 GLU B CD  
7427  O OE1 . GLU B 398 ? 0.4387 0.3964 0.5196 0.0345  0.0377  -0.0307 398 GLU B OE1 
7428  O OE2 . GLU B 398 ? 0.7305 0.6686 0.7962 0.0385  0.0442  -0.0454 398 GLU B OE2 
7429  N N   . VAL B 399 ? 0.1460 0.1340 0.2023 0.0114  0.0540  -0.0456 399 VAL B N   
7430  C CA  . VAL B 399 ? 0.1580 0.1454 0.2020 0.0081  0.0541  -0.0458 399 VAL B CA  
7431  C C   . VAL B 399 ? 0.1351 0.1151 0.1722 0.0137  0.0530  -0.0464 399 VAL B C   
7432  O O   . VAL B 399 ? 0.1780 0.1592 0.2220 0.0216  0.0547  -0.0475 399 VAL B O   
7433  C CB  . VAL B 399 ? 0.1994 0.2000 0.2513 0.0065  0.0580  -0.0454 399 VAL B CB  
7434  C CG1 . VAL B 399 ? 0.2061 0.2043 0.2471 0.0044  0.0583  -0.0444 399 VAL B CG1 
7435  C CG2 . VAL B 399 ? 0.1423 0.1504 0.2005 0.0001  0.0582  -0.0468 399 VAL B CG2 
7436  N N   . ILE B 400 ? 0.1216 0.0956 0.1460 0.0108  0.0498  -0.0461 400 ILE B N   
7437  C CA  . ILE B 400 ? 0.1943 0.1625 0.2110 0.0156  0.0483  -0.0482 400 ILE B CA  
7438  C C   . ILE B 400 ? 0.2144 0.1876 0.2232 0.0139  0.0484  -0.0470 400 ILE B C   
7439  O O   . ILE B 400 ? 0.1524 0.1289 0.1600 0.0082  0.0480  -0.0441 400 ILE B O   
7440  C CB  . ILE B 400 ? 0.1641 0.1196 0.1757 0.0146  0.0440  -0.0497 400 ILE B CB  
7441  C CG1 . ILE B 400 ? 0.1401 0.0967 0.1447 0.0078  0.0416  -0.0474 400 ILE B CG1 
7442  C CG2 . ILE B 400 ? 0.1564 0.1050 0.1773 0.0150  0.0439  -0.0494 400 ILE B CG2 
7443  C CD1 . ILE B 400 ? 0.1348 0.0811 0.1374 0.0046  0.0388  -0.0484 400 ILE B CD1 
7444  N N   . GLU B 401 ? 0.3044 0.2773 0.3076 0.0200  0.0490  -0.0498 401 GLU B N   
7445  C CA  . GLU B 401 ? 0.2018 0.1808 0.1992 0.0202  0.0507  -0.0490 401 GLU B CA  
7446  C C   . GLU B 401 ? 0.1990 0.1718 0.1876 0.0179  0.0483  -0.0507 401 GLU B C   
7447  O O   . GLU B 401 ? 0.1933 0.1698 0.1785 0.0152  0.0498  -0.0489 401 GLU B O   
7448  C CB  . GLU B 401 ? 0.2575 0.2440 0.2547 0.0290  0.0551  -0.0517 401 GLU B CB  
7449  C CG  . GLU B 401 ? 0.3243 0.3226 0.3337 0.0297  0.0610  -0.0496 401 GLU B CG  
7450  C CD  . GLU B 401 ? 0.3827 0.3874 0.3958 0.0215  0.0637  -0.0450 401 GLU B CD  
7451  O OE1 . GLU B 401 ? 0.4919 0.4969 0.4975 0.0196  0.0638  -0.0438 401 GLU B OE1 
7452  O OE2 . GLU B 401 ? 0.4497 0.4587 0.4737 0.0173  0.0658  -0.0432 401 GLU B OE2 
7453  N N   . SER B 402 ? 0.1642 0.1276 0.1491 0.0192  0.0445  -0.0540 402 SER B N   
7454  C CA  . SER B 402 ? 0.2195 0.1782 0.1961 0.0179  0.0421  -0.0565 402 SER B CA  
7455  C C   . SER B 402 ? 0.2281 0.1758 0.2036 0.0160  0.0369  -0.0583 402 SER B C   
7456  O O   . SER B 402 ? 0.2644 0.2058 0.2439 0.0176  0.0350  -0.0586 402 SER B O   
7457  C CB  . SER B 402 ? 0.2705 0.2292 0.2388 0.0254  0.0438  -0.0621 402 SER B CB  
7458  O OG  . SER B 402 ? 0.3346 0.2842 0.3006 0.0330  0.0421  -0.0677 402 SER B OG  
7459  N N   . VAL B 403 ? 0.2568 0.2018 0.2267 0.0125  0.0343  -0.0595 403 VAL B N   
7460  C CA  . VAL B 403 ? 0.2598 0.1939 0.2278 0.0096  0.0287  -0.0616 403 VAL B CA  
7461  C C   . VAL B 403 ? 0.2924 0.2194 0.2503 0.0111  0.0253  -0.0677 403 VAL B C   
7462  O O   . VAL B 403 ? 0.2762 0.2109 0.2293 0.0118  0.0277  -0.0680 403 VAL B O   
7463  C CB  . VAL B 403 ? 0.2183 0.1577 0.1908 0.0017  0.0289  -0.0566 403 VAL B CB  
7464  C CG1 . VAL B 403 ? 0.1795 0.1232 0.1600 0.0003  0.0319  -0.0523 403 VAL B CG1 
7465  C CG2 . VAL B 403 ? 0.2346 0.1844 0.2040 0.0001  0.0306  -0.0540 403 VAL B CG2 
7466  N N   . LYS B 404 ? 0.3430 0.2533 0.2974 0.0111  0.0193  -0.0731 404 LYS B N   
7467  C CA  . LYS B 404 ? 0.2661 0.1665 0.2101 0.0107  0.0140  -0.0799 404 LYS B CA  
7468  C C   . LYS B 404 ? 0.3186 0.2230 0.2654 0.0001  0.0124  -0.0779 404 LYS B C   
7469  O O   . LYS B 404 ? 0.3166 0.2165 0.2709 -0.0078 0.0106  -0.0754 404 LYS B O   
7470  C CB  . LYS B 404 ? 0.3309 0.2084 0.2700 0.0131  0.0076  -0.0864 404 LYS B CB  
7471  C CG  . LYS B 404 ? 0.3876 0.2583 0.3128 0.0217  0.0073  -0.0922 404 LYS B CG  
7472  C CD  . LYS B 404 ? 0.4829 0.3253 0.3976 0.0202  0.0013  -0.0971 404 LYS B CD  
7473  C CE  . LYS B 404 ? 0.4746 0.3014 0.3789 0.0285  0.0089  -0.0979 404 LYS B CE  
7474  N NZ  . LYS B 404 ? 0.4484 0.2444 0.3455 0.0179  0.0175  -0.1028 404 LYS B NZ  
7475  N N   . ALA B 405 ? 0.2707 0.1838 0.2111 -0.0002 0.0132  -0.0787 405 ALA B N   
7476  C CA  . ALA B 405 ? 0.2432 0.1644 0.1858 -0.0094 0.0134  -0.0763 405 ALA B CA  
7477  C C   . ALA B 405 ? 0.2511 0.1602 0.1949 -0.0196 0.0059  -0.0804 405 ALA B C   
7478  O O   . ALA B 405 ? 0.3955 0.2884 0.3345 -0.0187 -0.0017 -0.0871 405 ALA B O   
7479  C CB  . ALA B 405 ? 0.3371 0.2677 0.2710 -0.0068 0.0147  -0.0772 405 ALA B CB  
7480  N N   . GLY B 406 ? 0.2062 0.1231 0.1565 -0.0298 0.0071  -0.0761 406 GLY B N   
7481  C CA  . GLY B 406 ? 0.2940 0.2031 0.2484 -0.0427 -0.0011 -0.0769 406 GLY B CA  
7482  C C   . GLY B 406 ? 0.2347 0.1588 0.1959 -0.0539 0.0022  -0.0700 406 GLY B C   
7483  O O   . GLY B 406 ? 0.2773 0.2162 0.2378 -0.0503 0.0107  -0.0674 406 GLY B O   
7484  N N   . THR B 407 ? 0.2165 0.1378 0.1848 -0.0677 -0.0058 -0.0660 407 THR B N   
7485  C CA  . THR B 407 ? 0.2495 0.1890 0.2260 -0.0805 -0.0048 -0.0562 407 THR B CA  
7486  C C   . THR B 407 ? 0.2762 0.2046 0.2639 -0.0874 -0.0099 -0.0471 407 THR B C   
7487  O O   . THR B 407 ? 0.3337 0.2392 0.3232 -0.0823 -0.0144 -0.0506 407 THR B O   
7488  C CB  . THR B 407 ? 0.2596 0.2176 0.2376 -0.0919 -0.0109 -0.0537 407 THR B CB  
7489  O OG1 . THR B 407 ? 0.3337 0.2771 0.3165 -0.0991 -0.0227 -0.0534 407 THR B OG1 
7490  C CG2 . THR B 407 ? 0.2590 0.2261 0.2253 -0.0842 -0.0072 -0.0627 407 THR B CG2 
7491  N N   . TRP B 408 ? 0.2888 0.2367 0.2854 -0.0981 -0.0095 -0.0341 408 TRP B N   
7492  C CA  . TRP B 408 ? 0.3386 0.2787 0.3463 -0.1042 -0.0145 -0.0224 408 TRP B CA  
7493  C C   . TRP B 408 ? 0.2733 0.2055 0.2893 -0.1137 -0.0254 -0.0190 408 TRP B C   
7494  O O   . TRP B 408 ? 0.3098 0.2335 0.3349 -0.1188 -0.0292 -0.0100 408 TRP B O   
7495  C CB  . TRP B 408 ? 0.2315 0.1992 0.2458 -0.1089 -0.0093 -0.0076 408 TRP B CB  
7496  C CG  . TRP B 408 ? 0.2543 0.2575 0.2734 -0.1150 -0.0084 0.0007  408 TRP B CG  
7497  C CD1 . TRP B 408 ? 0.2683 0.2811 0.2876 -0.1199 -0.0129 -0.0022 408 TRP B CD1 
7498  C CD2 . TRP B 408 ? 0.2024 0.2384 0.2269 -0.1144 -0.0023 0.0134  408 TRP B CD2 
7499  N NE1 . TRP B 408 ? 0.2387 0.2890 0.2647 -0.1223 -0.0099 0.0085  408 TRP B NE1 
7500  C CE2 . TRP B 408 ? 0.1815 0.2462 0.2100 -0.1179 -0.0029 0.0176  408 TRP B CE2 
7501  C CE3 . TRP B 408 ? 0.1690 0.2138 0.1943 -0.1094 0.0035  0.0211  408 TRP B CE3 
7502  C CZ2 . TRP B 408 ? 0.1665 0.2665 0.1990 -0.1140 0.0026  0.0281  408 TRP B CZ2 
7503  C CZ3 . TRP B 408 ? 0.1592 0.2390 0.1871 -0.1069 0.0086  0.0311  408 TRP B CZ3 
7504  C CH2 . TRP B 408 ? 0.1684 0.2740 0.1994 -0.1078 0.0084  0.0338  408 TRP B CH2 
7505  N N   . PHE B 409 ? 0.2820 0.2169 0.2943 -0.1164 -0.0300 -0.0263 409 PHE B N   
7506  C CA  . PHE B 409 ? 0.3165 0.2398 0.3346 -0.1247 -0.0401 -0.0275 409 PHE B CA  
7507  C C   . PHE B 409 ? 0.4508 0.3436 0.4627 -0.1152 -0.0421 -0.0438 409 PHE B C   
7508  O O   . PHE B 409 ? 0.4866 0.3772 0.4892 -0.1091 -0.0431 -0.0564 409 PHE B O   
7509  C CB  . PHE B 409 ? 0.2710 0.2159 0.2889 -0.1325 -0.0445 -0.0268 409 PHE B CB  
7510  C CG  . PHE B 409 ? 0.3534 0.3312 0.3820 -0.1423 -0.0436 -0.0095 409 PHE B CG  
7511  C CD1 . PHE B 409 ? 0.4176 0.3979 0.4576 -0.1541 -0.0505 0.0016  409 PHE B CD1 
7512  C CD2 . PHE B 409 ? 0.3593 0.3675 0.3862 -0.1385 -0.0352 -0.0048 409 PHE B CD2 
7513  C CE1 . PHE B 409 ? 0.5180 0.5316 0.5673 -0.1609 -0.0489 0.0180  409 PHE B CE1 
7514  C CE2 . PHE B 409 ? 0.3284 0.3706 0.3654 -0.1439 -0.0332 0.0105  409 PHE B CE2 
7515  C CZ  . PHE B 409 ? 0.3989 0.4443 0.4468 -0.1547 -0.0399 0.0221  409 PHE B CZ  
7516  N N   . ASP B 410 ? 0.4527 0.3244 0.4691 -0.1132 -0.0420 -0.0431 410 ASP B N   
7517  C CA  . ASP B 410 ? 0.3641 0.2089 0.3759 -0.1055 -0.0424 -0.0573 410 ASP B CA  
7518  C C   . ASP B 410 ? 0.4010 0.2452 0.4052 -0.0884 -0.0353 -0.0704 410 ASP B C   
7519  O O   . ASP B 410 ? 0.3929 0.2232 0.3913 -0.0816 -0.0336 -0.0840 410 ASP B O   
7520  C CB  . ASP B 410 ? 0.3803 0.2164 0.3899 -0.1136 -0.0508 -0.0650 410 ASP B CB  
7521  C CG  . ASP B 410 ? 0.5945 0.4337 0.6137 -0.1305 -0.0594 -0.0510 410 ASP B CG  
7522  O OD1 . ASP B 410 ? 0.6399 0.4894 0.6671 -0.1352 -0.0579 -0.0349 410 ASP B OD1 
7523  O OD2 . ASP B 410 ? 0.6524 0.4855 0.6713 -0.1391 -0.0677 -0.0558 410 ASP B OD2 
7524  N N   . GLY B 411 ? 0.3162 0.1759 0.3174 -0.0818 -0.0310 -0.0654 411 GLY B N   
7525  C CA  . GLY B 411 ? 0.2740 0.1319 0.2640 -0.0649 -0.0273 -0.0728 411 GLY B CA  
7526  C C   . GLY B 411 ? 0.3533 0.2154 0.3285 -0.0587 -0.0284 -0.0823 411 GLY B C   
7527  O O   . GLY B 411 ? 0.4286 0.2886 0.3913 -0.0449 -0.0241 -0.0869 411 GLY B O   
7528  N N   . ASN B 412 ? 0.3176 0.1876 0.2929 -0.0690 -0.0331 -0.0838 412 ASN B N   
7529  C CA  . ASN B 412 ? 0.3409 0.2153 0.3021 -0.0638 -0.0347 -0.0925 412 ASN B CA  
7530  C C   . ASN B 412 ? 0.3426 0.2386 0.3020 -0.0753 -0.0343 -0.0868 412 ASN B C   
7531  O O   . ASN B 412 ? 0.2864 0.1963 0.2539 -0.0848 -0.0315 -0.0761 412 ASN B O   
7532  C CB  . ASN B 412 ? 0.4167 0.2781 0.3811 -0.0628 -0.0421 -0.1052 412 ASN B CB  
7533  C CG  . ASN B 412 ? 0.3855 0.2421 0.3639 -0.0811 -0.0469 -0.1047 412 ASN B CG  
7534  O OD1 . ASN B 412 ? 0.4450 0.3140 0.4258 -0.0936 -0.0517 -0.0953 412 ASN B OD1 
7535  N ND2 . ASN B 412 ? 0.3582 0.1947 0.3381 -0.0838 -0.0445 -0.1108 412 ASN B ND2 
7536  N N   . PHE B 413 ? 0.3104 0.2117 0.2592 -0.0739 -0.0376 -0.0938 413 PHE B N   
7537  C CA  . PHE B 413 ? 0.2781 0.2031 0.2249 -0.0829 -0.0379 -0.0895 413 PHE B CA  
7538  C C   . PHE B 413 ? 0.2998 0.2256 0.2505 -0.0947 -0.0509 -0.0924 413 PHE B C   
7539  O O   . PHE B 413 ? 0.2973 0.2432 0.2446 -0.1001 -0.0534 -0.0906 413 PHE B O   
7540  C CB  . PHE B 413 ? 0.2677 0.2040 0.1999 -0.0714 -0.0300 -0.0932 413 PHE B CB  
7541  C CG  . PHE B 413 ? 0.3497 0.2895 0.2812 -0.0601 -0.0169 -0.0895 413 PHE B CG  
7542  C CD1 . PHE B 413 ? 0.3427 0.2663 0.2714 -0.0477 -0.0134 -0.0921 413 PHE B CD1 
7543  C CD2 . PHE B 413 ? 0.2859 0.2473 0.2205 -0.0616 -0.0091 -0.0832 413 PHE B CD2 
7544  C CE1 . PHE B 413 ? 0.2826 0.2118 0.2132 -0.0384 -0.0028 -0.0870 413 PHE B CE1 
7545  C CE2 . PHE B 413 ? 0.2599 0.2233 0.1954 -0.0510 0.0016  -0.0798 413 PHE B CE2 
7546  C CZ  . PHE B 413 ? 0.2573 0.2049 0.1918 -0.0401 0.0044  -0.0808 413 PHE B CZ  
7547  N N   . LEU B 414 ? 0.3215 0.2281 0.2813 -0.0988 -0.0586 -0.0971 414 LEU B N   
7548  C CA  . LEU B 414 ? 0.3456 0.2519 0.3096 -0.1102 -0.0699 -0.1018 414 LEU B CA  
7549  C C   . LEU B 414 ? 0.3398 0.2689 0.3151 -0.1267 -0.0745 -0.0872 414 LEU B C   
7550  O O   . LEU B 414 ? 0.3575 0.2926 0.3355 -0.1366 -0.0841 -0.0888 414 LEU B O   
7551  C CB  . LEU B 414 ? 0.3719 0.2534 0.3434 -0.1129 -0.0730 -0.1102 414 LEU B CB  
7552  C CG  . LEU B 414 ? 0.3815 0.2462 0.3448 -0.0980 -0.0669 -0.1265 414 LEU B CG  
7553  C CD1 . LEU B 414 ? 0.4568 0.2959 0.4227 -0.1050 -0.0668 -0.1326 414 LEU B CD1 
7554  C CD2 . LEU B 414 ? 0.3891 0.2614 0.3372 -0.0893 -0.0693 -0.1378 414 LEU B CD2 
7555  N N   . LYS B 415 ? 0.3667 0.3113 0.3493 -0.1295 -0.0676 -0.0730 415 LYS B N   
7556  C CA  . LYS B 415 ? 0.3401 0.3131 0.3358 -0.1429 -0.0701 -0.0575 415 LYS B CA  
7557  C C   . LYS B 415 ? 0.3329 0.3373 0.3238 -0.1428 -0.0692 -0.0555 415 LYS B C   
7558  O O   . LYS B 415 ? 0.3874 0.4187 0.3900 -0.1529 -0.0731 -0.0441 415 LYS B O   
7559  C CB  . LYS B 415 ? 0.4202 0.4023 0.4254 -0.1437 -0.0620 -0.0437 415 LYS B CB  
7560  C CG  . LYS B 415 ? 0.4814 0.4846 0.5035 -0.1572 -0.0654 -0.0266 415 LYS B CG  
7561  C CD  . LYS B 415 ? 0.7033 0.6866 0.7319 -0.1677 -0.0763 -0.0280 415 LYS B CD  
7562  C CE  . LYS B 415 ? 0.8663 0.8271 0.9011 -0.1692 -0.0753 -0.0228 415 LYS B CE  
7563  N NZ  . LYS B 415 ? 0.9742 0.9048 1.0094 -0.1752 -0.0845 -0.0312 415 LYS B NZ  
7564  N N   . TRP B 416 ? 0.2864 0.2901 0.2610 -0.1305 -0.0636 -0.0652 416 TRP B N   
7565  C CA  . TRP B 416 ? 0.2732 0.3079 0.2432 -0.1284 -0.0615 -0.0630 416 TRP B CA  
7566  C C   . TRP B 416 ? 0.3495 0.3772 0.3031 -0.1218 -0.0658 -0.0754 416 TRP B C   
7567  O O   . TRP B 416 ? 0.3976 0.4516 0.3489 -0.1214 -0.0670 -0.0727 416 TRP B O   
7568  C CB  . TRP B 416 ? 0.2447 0.2947 0.2116 -0.1187 -0.0480 -0.0601 416 TRP B CB  
7569  C CG  . TRP B 416 ? 0.2294 0.2898 0.2109 -0.1234 -0.0430 -0.0483 416 TRP B CG  
7570  C CD1 . TRP B 416 ? 0.2442 0.3413 0.2403 -0.1279 -0.0411 -0.0346 416 TRP B CD1 
7571  C CD2 . TRP B 416 ? 0.2482 0.2845 0.2316 -0.1220 -0.0388 -0.0481 416 TRP B CD2 
7572  N NE1 . TRP B 416 ? 0.2049 0.3020 0.2105 -0.1295 -0.0357 -0.0258 416 TRP B NE1 
7573  C CE2 . TRP B 416 ? 0.2138 0.2733 0.2117 -0.1269 -0.0347 -0.0338 416 TRP B CE2 
7574  C CE3 . TRP B 416 ? 0.3073 0.3073 0.2824 -0.1151 -0.0379 -0.0576 416 TRP B CE3 
7575  C CZ2 . TRP B 416 ? 0.3063 0.3522 0.3090 -0.1267 -0.0305 -0.0288 416 TRP B CZ2 
7576  C CZ3 . TRP B 416 ? 0.3098 0.2969 0.2914 -0.1145 -0.0339 -0.0527 416 TRP B CZ3 
7577  C CH2 . TRP B 416 ? 0.3451 0.3541 0.3395 -0.1212 -0.0306 -0.0385 416 TRP B CH2 
7578  N N   . ILE B 417 ? 0.3074 0.3032 0.2502 -0.1151 -0.0682 -0.0880 417 ILE B N   
7579  C CA  . ILE B 417 ? 0.3233 0.3126 0.2486 -0.1066 -0.0714 -0.0994 417 ILE B CA  
7580  C C   . ILE B 417 ? 0.3570 0.3152 0.2795 -0.1049 -0.0796 -0.1122 417 ILE B C   
7581  O O   . ILE B 417 ? 0.3761 0.3158 0.3078 -0.1050 -0.0783 -0.1131 417 ILE B O   
7582  C CB  . ILE B 417 ? 0.3930 0.3843 0.3036 -0.0904 -0.0582 -0.1012 417 ILE B CB  
7583  C CG1 . ILE B 417 ? 0.4256 0.4260 0.3202 -0.0842 -0.0607 -0.1061 417 ILE B CG1 
7584  C CG2 . ILE B 417 ? 0.3961 0.3590 0.3014 -0.0789 -0.0519 -0.1073 417 ILE B CG2 
7585  C CD1 . ILE B 417 ? 0.2979 0.3114 0.1841 -0.0714 -0.0478 -0.1020 417 ILE B CD1 
7586  N N   . GLY B 418 ? 0.3895 0.3444 0.3005 -0.1029 -0.0882 -0.1227 418 GLY B N   
7587  C CA  . GLY B 418 ? 0.4640 0.3938 0.3709 -0.0979 -0.0948 -0.1389 418 GLY B CA  
7588  C C   . GLY B 418 ? 0.5034 0.4335 0.4192 -0.1116 -0.1083 -0.1467 418 GLY B C   
7589  O O   . GLY B 418 ? 0.6009 0.5191 0.5099 -0.1073 -0.1122 -0.1635 418 GLY B O   
7590  N N   . ASN B 419 ? 0.5577 0.5033 0.4886 -0.1283 -0.1137 -0.1347 419 ASN B N   
7591  C CA  . ASN B 419 ? 0.5385 0.4845 0.4768 -0.1427 -0.1268 -0.1402 419 ASN B CA  
7592  C C   . ASN B 419 ? 0.5553 0.5270 0.4874 -0.1463 -0.1348 -0.1368 419 ASN B C   
7593  O O   . ASN B 419 ? 0.5324 0.5239 0.4569 -0.1396 -0.1287 -0.1278 419 ASN B O   
7594  C CB  . ASN B 419 ? 0.5076 0.4510 0.4673 -0.1595 -0.1292 -0.1282 419 ASN B CB  
7595  C CG  . ASN B 419 ? 0.6086 0.5839 0.5818 -0.1699 -0.1293 -0.1070 419 ASN B CG  
7596  O OD1 . ASN B 419 ? 0.5037 0.5054 0.4726 -0.1685 -0.1302 -0.1021 419 ASN B OD1 
7597  N ND2 . ASN B 419 ? 0.7424 0.7171 0.7323 -0.1800 -0.1276 -0.0937 419 ASN B ND2 
7598  N N   . LYS B 420 ? 0.6041 0.5761 0.5396 -0.1576 -0.1477 -0.1443 420 LYS B N   
7599  C CA  . LYS B 420 ? 0.5472 0.5416 0.4756 -0.1601 -0.1571 -0.1443 420 LYS B CA  
7600  C C   . LYS B 420 ? 0.6025 0.6322 0.5409 -0.1652 -0.1536 -0.1231 420 LYS B C   
7601  O O   . LYS B 420 ? 0.5999 0.6488 0.5265 -0.1567 -0.1503 -0.1195 420 LYS B O   
7602  C CB  . LYS B 420 ? 0.5375 0.5272 0.4727 -0.1749 -0.1719 -0.1538 420 LYS B CB  
7603  C CG  . LYS B 420 ? 0.6154 0.6325 0.5502 -0.1823 -0.1834 -0.1499 420 LYS B CG  
7604  C CD  . LYS B 420 ? 0.5882 0.5973 0.5298 -0.1981 -0.1982 -0.1605 420 LYS B CD  
7605  C CE  . LYS B 420 ? 0.5873 0.6110 0.5541 -0.2182 -0.2026 -0.1424 420 LYS B CE  
7606  N NZ  . LYS B 420 ? 0.7732 0.8294 0.7462 -0.2280 -0.2137 -0.1347 420 LYS B NZ  
7607  N N   . GLU B 421 ? 0.6015 0.6422 0.5619 -0.1784 -0.1529 -0.1085 421 GLU B N   
7608  C CA  . GLU B 421 ? 0.6169 0.6968 0.5899 -0.1829 -0.1493 -0.0891 421 GLU B CA  
7609  C C   . GLU B 421 ? 0.6182 0.7078 0.5870 -0.1702 -0.1336 -0.0810 421 GLU B C   
7610  O O   . GLU B 421 ? 0.5515 0.6727 0.5204 -0.1653 -0.1289 -0.0720 421 GLU B O   
7611  C CB  . GLU B 421 ? 0.6166 0.7073 0.6137 -0.2002 -0.1533 -0.0753 421 GLU B CB  
7612  C CG  . GLU B 421 ? 0.6574 0.7314 0.6593 -0.2143 -0.1679 -0.0841 421 GLU B CG  
7613  C CD  . GLU B 421 ? 0.9072 1.0127 0.9191 -0.2263 -0.1786 -0.0766 421 GLU B CD  
7614  O OE1 . GLU B 421 ? 0.9669 1.1096 0.9880 -0.2255 -0.1733 -0.0604 421 GLU B OE1 
7615  O OE2 . GLU B 421 ? 0.9664 1.0608 0.9773 -0.2360 -0.1921 -0.0873 421 GLU B OE2 
7616  N N   . LYS B 422 ? 0.6154 0.6795 0.5816 -0.1644 -0.1253 -0.0844 422 LYS B N   
7617  C CA  . LYS B 422 ? 0.4577 0.5299 0.4201 -0.1532 -0.1107 -0.0781 422 LYS B CA  
7618  C C   . LYS B 422 ? 0.4483 0.5225 0.3894 -0.1382 -0.1055 -0.0857 422 LYS B C   
7619  O O   . LYS B 422 ? 0.4098 0.5052 0.3497 -0.1303 -0.0952 -0.0783 422 LYS B O   
7620  C CB  . LYS B 422 ? 0.4491 0.4919 0.4127 -0.1501 -0.1039 -0.0808 422 LYS B CB  
7621  C CG  . LYS B 422 ? 0.3933 0.4425 0.3780 -0.1616 -0.1031 -0.0668 422 LYS B CG  
7622  C CD  . LYS B 422 ? 0.3902 0.4081 0.3753 -0.1581 -0.0978 -0.0702 422 LYS B CD  
7623  C CE  . LYS B 422 ? 0.4560 0.4743 0.4604 -0.1714 -0.1004 -0.0575 422 LYS B CE  
7624  N NZ  . LYS B 422 ? 0.3333 0.3905 0.3512 -0.1770 -0.0962 -0.0388 422 LYS B NZ  
7625  N N   . ASN B 423 ? 0.5528 0.6063 0.4772 -0.1334 -0.1123 -0.1004 423 ASN B N   
7626  C CA  . ASN B 423 ? 0.5160 0.5687 0.4182 -0.1184 -0.1064 -0.1064 423 ASN B CA  
7627  C C   . ASN B 423 ? 0.5313 0.6192 0.4325 -0.1180 -0.1081 -0.0984 423 ASN B C   
7628  O O   . ASN B 423 ? 0.5267 0.6239 0.4158 -0.1055 -0.0992 -0.0966 423 ASN B O   
7629  C CB  . ASN B 423 ? 0.5768 0.5993 0.4607 -0.1125 -0.1135 -0.1234 423 ASN B CB  
7630  C CG  . ASN B 423 ? 0.5682 0.5597 0.4456 -0.1019 -0.1054 -0.1309 423 ASN B CG  
7631  O OD1 . ASN B 423 ? 0.5428 0.5342 0.4282 -0.0995 -0.0942 -0.1235 423 ASN B OD1 
7632  N ND2 . ASN B 423 ? 0.5990 0.5653 0.4621 -0.0948 -0.1114 -0.1459 423 ASN B ND2 
7633  N N   . GLU B 424 ? 0.4965 0.6051 0.4115 -0.1307 -0.1193 -0.0927 424 GLU B N   
7634  C CA  . GLU B 424 ? 0.4786 0.6219 0.3940 -0.1290 -0.1219 -0.0848 424 GLU B CA  
7635  C C   . GLU B 424 ? 0.4060 0.5815 0.3342 -0.1235 -0.1106 -0.0695 424 GLU B C   
7636  O O   . GLU B 424 ? 0.3849 0.5824 0.3076 -0.1133 -0.1069 -0.0646 424 GLU B O   
7637  C CB  . GLU B 424 ? 0.5190 0.6759 0.4466 -0.1438 -0.1374 -0.0831 424 GLU B CB  
7638  C CG  . GLU B 424 ? 0.6774 0.8453 0.5910 -0.1408 -0.1466 -0.0878 424 GLU B CG  
7639  C CD  . GLU B 424 ? 0.7603 0.8961 0.6458 -0.1308 -0.1477 -0.1045 424 GLU B CD  
7640  O OE1 . GLU B 424 ? 0.8221 0.9242 0.7027 -0.1313 -0.1486 -0.1162 424 GLU B OE1 
7641  O OE2 . GLU B 424 ? 0.6481 0.7936 0.5169 -0.1216 -0.1473 -0.1051 424 GLU B OE2 
7642  N N   . TYR B 425 ? 0.4559 0.6345 0.4011 -0.1288 -0.1051 -0.0618 425 TYR B N   
7643  C CA  . TYR B 425 ? 0.3376 0.5459 0.2940 -0.1212 -0.0940 -0.0490 425 TYR B CA  
7644  C C   . TYR B 425 ? 0.2909 0.4905 0.2310 -0.1042 -0.0823 -0.0535 425 TYR B C   
7645  O O   . TYR B 425 ? 0.2865 0.5115 0.2282 -0.0927 -0.0763 -0.0458 425 TYR B O   
7646  C CB  . TYR B 425 ? 0.3784 0.5883 0.3533 -0.1294 -0.0900 -0.0410 425 TYR B CB  
7647  C CG  . TYR B 425 ? 0.4447 0.6880 0.4421 -0.1392 -0.0945 -0.0266 425 TYR B CG  
7648  C CD1 . TYR B 425 ? 0.4955 0.7511 0.4964 -0.1476 -0.1064 -0.0256 425 TYR B CD1 
7649  C CD2 . TYR B 425 ? 0.3495 0.6126 0.3638 -0.1395 -0.0864 -0.0139 425 TYR B CD2 
7650  C CE1 . TYR B 425 ? 0.5322 0.8191 0.5538 -0.1565 -0.1097 -0.0119 425 TYR B CE1 
7651  C CE2 . TYR B 425 ? 0.3296 0.6238 0.3632 -0.1471 -0.0889 0.0000  425 TYR B CE2 
7652  C CZ  . TYR B 425 ? 0.4204 0.7266 0.4579 -0.1559 -0.1004 0.0012  425 TYR B CZ  
7653  O OH  . TYR B 425 ? 0.4786 0.8168 0.5351 -0.1636 -0.1024 0.0155  425 TYR B OH  
7654  N N   . TRP B 426 ? 0.3198 0.4828 0.2449 -0.1011 -0.0786 -0.0652 426 TRP B N   
7655  C CA  . TRP B 426 ? 0.2805 0.4325 0.1896 -0.0851 -0.0673 -0.0692 426 TRP B CA  
7656  C C   . TRP B 426 ? 0.3473 0.5092 0.2424 -0.0763 -0.0695 -0.0694 426 TRP B C   
7657  O O   . TRP B 426 ? 0.3954 0.5669 0.2854 -0.0629 -0.0610 -0.0642 426 TRP B O   
7658  C CB  . TRP B 426 ? 0.2919 0.4038 0.1895 -0.0830 -0.0633 -0.0807 426 TRP B CB  
7659  C CG  . TRP B 426 ? 0.3170 0.4197 0.2252 -0.0849 -0.0557 -0.0786 426 TRP B CG  
7660  C CD1 . TRP B 426 ? 0.4109 0.5012 0.3309 -0.0969 -0.0605 -0.0787 426 TRP B CD1 
7661  C CD2 . TRP B 426 ? 0.2885 0.3932 0.1970 -0.0742 -0.0425 -0.0751 426 TRP B CD2 
7662  N NE1 . TRP B 426 ? 0.2723 0.3582 0.1991 -0.0947 -0.0509 -0.0754 426 TRP B NE1 
7663  C CE2 . TRP B 426 ? 0.2387 0.3334 0.1582 -0.0809 -0.0400 -0.0741 426 TRP B CE2 
7664  C CE3 . TRP B 426 ? 0.5058 0.6177 0.4066 -0.0594 -0.0329 -0.0719 426 TRP B CE3 
7665  C CZ2 . TRP B 426 ? 0.3742 0.4671 0.2963 -0.0730 -0.0283 -0.0714 426 TRP B CZ2 
7666  C CZ3 . TRP B 426 ? 0.5451 0.6527 0.4492 -0.0514 -0.0215 -0.0690 426 TRP B CZ3 
7667  C CH2 . TRP B 426 ? 0.3955 0.4937 0.3103 -0.0578 -0.0191 -0.0690 426 TRP B CH2 
7668  N N   . LYS B 427 ? 0.3300 0.4884 0.2187 -0.0834 -0.0815 -0.0750 427 LYS B N   
7669  C CA  . LYS B 427 ? 0.3294 0.4990 0.2045 -0.0762 -0.0848 -0.0744 427 LYS B CA  
7670  C C   . LYS B 427 ? 0.3999 0.6088 0.2878 -0.0717 -0.0842 -0.0601 427 LYS B C   
7671  O O   . LYS B 427 ? 0.3682 0.5861 0.2473 -0.0588 -0.0791 -0.0553 427 LYS B O   
7672  C CB  . LYS B 427 ? 0.3618 0.5223 0.2290 -0.0858 -0.0996 -0.0835 427 LYS B CB  
7673  C CG  . LYS B 427 ? 0.3854 0.5323 0.2270 -0.0769 -0.1003 -0.0913 427 LYS B CG  
7674  C CD  . LYS B 427 ? 0.6079 0.7327 0.4384 -0.0850 -0.1137 -0.1051 427 LYS B CD  
7675  C CE  . LYS B 427 ? 0.5503 0.6424 0.3834 -0.0888 -0.1129 -0.1145 427 LYS B CE  
7676  N NZ  . LYS B 427 ? 0.6375 0.7121 0.4683 -0.0988 -0.1292 -0.1266 427 LYS B NZ  
7677  N N   . ILE B 428 ? 0.4066 0.6392 0.3163 -0.0811 -0.0889 -0.0520 428 ILE B N   
7678  C CA  . ILE B 428 ? 0.2909 0.5622 0.2153 -0.0743 -0.0870 -0.0377 428 ILE B CA  
7679  C C   . ILE B 428 ? 0.3310 0.6045 0.2550 -0.0581 -0.0733 -0.0324 428 ILE B C   
7680  O O   . ILE B 428 ? 0.3942 0.6851 0.3172 -0.0443 -0.0699 -0.0244 428 ILE B O   
7681  C CB  . ILE B 428 ? 0.2863 0.5818 0.2356 -0.0870 -0.0923 -0.0292 428 ILE B CB  
7682  C CG1 . ILE B 428 ? 0.3130 0.5982 0.2625 -0.1044 -0.1064 -0.0357 428 ILE B CG1 
7683  C CG2 . ILE B 428 ? 0.3863 0.7234 0.3505 -0.0784 -0.0909 -0.0149 428 ILE B CG2 
7684  C CD1 . ILE B 428 ? 0.3117 0.6146 0.2854 -0.1189 -0.1110 -0.0269 428 ILE B CD1 
7685  N N   . LEU B 429 ? 0.2543 0.5083 0.1789 -0.0591 -0.0657 -0.0368 429 LEU B N   
7686  C CA  . LEU B 429 ? 0.2352 0.4871 0.1580 -0.0440 -0.0532 -0.0331 429 LEU B CA  
7687  C C   . LEU B 429 ? 0.2430 0.4755 0.1456 -0.0311 -0.0475 -0.0360 429 LEU B C   
7688  O O   . LEU B 429 ? 0.3310 0.5697 0.2326 -0.0161 -0.0403 -0.0286 429 LEU B O   
7689  C CB  . LEU B 429 ? 0.2230 0.4560 0.1495 -0.0493 -0.0471 -0.0381 429 LEU B CB  
7690  C CG  . LEU B 429 ? 0.2070 0.4280 0.1315 -0.0342 -0.0330 -0.0359 429 LEU B CG  
7691  C CD1 . LEU B 429 ? 0.1924 0.4409 0.1349 -0.0252 -0.0286 -0.0239 429 LEU B CD1 
7692  C CD2 . LEU B 429 ? 0.2023 0.3928 0.1261 -0.0397 -0.0271 -0.0433 429 LEU B CD2 
7693  N N   . ILE B 430 ? 0.2952 0.5029 0.1820 -0.0360 -0.0504 -0.0461 430 ILE B N   
7694  C CA  . ILE B 430 ? 0.3491 0.5394 0.2179 -0.0248 -0.0443 -0.0473 430 ILE B CA  
7695  C C   . ILE B 430 ? 0.3574 0.5703 0.2228 -0.0171 -0.0484 -0.0382 430 ILE B C   
7696  O O   . ILE B 430 ? 0.3986 0.6094 0.2581 -0.0041 -0.0413 -0.0313 430 ILE B O   
7697  C CB  . ILE B 430 ? 0.3641 0.5253 0.2172 -0.0307 -0.0464 -0.0600 430 ILE B CB  
7698  C CG1 . ILE B 430 ? 0.2849 0.4202 0.1410 -0.0334 -0.0395 -0.0670 430 ILE B CG1 
7699  C CG2 . ILE B 430 ? 0.3106 0.4617 0.1454 -0.0208 -0.0420 -0.0593 430 ILE B CG2 
7700  C CD1 . ILE B 430 ? 0.3233 0.4339 0.1708 -0.0414 -0.0453 -0.0795 430 ILE B CD1 
7701  N N   . GLU B 431 ? 0.3346 0.5685 0.2048 -0.0251 -0.0602 -0.0372 431 GLU B N   
7702  C CA  . GLU B 431 ? 0.3005 0.5574 0.1690 -0.0176 -0.0647 -0.0278 431 GLU B CA  
7703  C C   . GLU B 431 ? 0.2927 0.5737 0.1769 -0.0054 -0.0598 -0.0143 431 GLU B C   
7704  O O   . GLU B 431 ? 0.3414 0.6295 0.2211 0.0077  -0.0575 -0.0054 431 GLU B O   
7705  C CB  . GLU B 431 ? 0.3186 0.5921 0.1902 -0.0298 -0.0788 -0.0300 431 GLU B CB  
7706  C CG  . GLU B 431 ? 0.4401 0.7026 0.2899 -0.0305 -0.0847 -0.0363 431 GLU B CG  
7707  C CD  . GLU B 431 ? 0.6173 0.8908 0.4586 -0.0163 -0.0814 -0.0260 431 GLU B CD  
7708  O OE1 . GLU B 431 ? 0.5623 0.8625 0.4178 -0.0091 -0.0818 -0.0134 431 GLU B OE1 
7709  O OE2 . GLU B 431 ? 0.6380 0.8933 0.4589 -0.0119 -0.0782 -0.0297 431 GLU B OE2 
7710  N N   . ALA B 432 ? 0.2663 0.5597 0.1688 -0.0086 -0.0582 -0.0121 432 ALA B N   
7711  C CA  . ALA B 432 ? 0.2500 0.5649 0.1668 0.0055  -0.0527 -0.0005 432 ALA B CA  
7712  C C   . ALA B 432 ? 0.2848 0.5773 0.1913 0.0209  -0.0414 0.0012  432 ALA B C   
7713  O O   . ALA B 432 ? 0.3904 0.6916 0.2982 0.0368  -0.0385 0.0111  432 ALA B O   
7714  C CB  . ALA B 432 ? 0.2337 0.5658 0.1710 -0.0015 -0.0522 0.0009  432 ALA B CB  
7715  N N   . LYS B 433 ? 0.2688 0.5306 0.1658 0.0164  -0.0349 -0.0079 433 LYS B N   
7716  C CA  . LYS B 433 ? 0.2992 0.5366 0.1877 0.0287  -0.0238 -0.0063 433 LYS B CA  
7717  C C   . LYS B 433 ? 0.3529 0.5823 0.2272 0.0370  -0.0236 -0.0009 433 LYS B C   
7718  O O   . LYS B 433 ? 0.4001 0.6191 0.2709 0.0500  -0.0168 0.0063  433 LYS B O   
7719  C CB  . LYS B 433 ? 0.2771 0.4836 0.1604 0.0205  -0.0174 -0.0171 433 LYS B CB  
7720  C CG  . LYS B 433 ? 0.3314 0.5105 0.2085 0.0301  -0.0062 -0.0157 433 LYS B CG  
7721  C CD  . LYS B 433 ? 0.3701 0.5553 0.2568 0.0429  -0.0005 -0.0088 433 LYS B CD  
7722  C CE  . LYS B 433 ? 0.4112 0.5693 0.2909 0.0524  0.0083  -0.0057 433 LYS B CE  
7723  N NZ  . LYS B 433 ? 0.3347 0.4946 0.2228 0.0665  0.0127  0.0003  433 LYS B NZ  
7724  N N   . LYS B 434 ? 0.4228 0.6559 0.2879 0.0293  -0.0311 -0.0038 434 LYS B N   
7725  C CA  . LYS B 434 ? 0.2856 0.5168 0.1374 0.0366  -0.0318 0.0030  434 LYS B CA  
7726  C C   . LYS B 434 ? 0.3361 0.5909 0.1963 0.0501  -0.0344 0.0171  434 LYS B C   
7727  O O   . LYS B 434 ? 0.3302 0.5779 0.1825 0.0613  -0.0311 0.0264  434 LYS B O   
7728  C CB  . LYS B 434 ? 0.3048 0.5381 0.1448 0.0261  -0.0402 -0.0039 434 LYS B CB  
7729  C CG  . LYS B 434 ? 0.3510 0.5563 0.1781 0.0173  -0.0367 -0.0169 434 LYS B CG  
7730  C CD  . LYS B 434 ? 0.4466 0.6556 0.2703 0.0041  -0.0472 -0.0278 434 LYS B CD  
7731  C CE  . LYS B 434 ? 0.4396 0.6267 0.2426 0.0010  -0.0466 -0.0373 434 LYS B CE  
7732  N NZ  . LYS B 434 ? 0.4132 0.6121 0.2062 -0.0048 -0.0587 -0.0411 434 LYS B NZ  
7733  N N   . LYS B 435 ? 0.4230 0.7060 0.3001 0.0494  -0.0401 0.0197  435 LYS B N   
7734  C CA  . LYS B 435 ? 0.3724 0.6804 0.2606 0.0631  -0.0428 0.0327  435 LYS B CA  
7735  C C   . LYS B 435 ? 0.3769 0.6939 0.2816 0.0739  -0.0373 0.0366  435 LYS B C   
7736  O O   . LYS B 435 ? 0.4810 0.8238 0.3999 0.0840  -0.0396 0.0453  435 LYS B O   
7737  C CB  . LYS B 435 ? 0.3155 0.6537 0.2114 0.0550  -0.0539 0.0341  435 LYS B CB  
7738  C CG  . LYS B 435 ? 0.3763 0.7079 0.2546 0.0455  -0.0606 0.0295  435 LYS B CG  
7739  C CD  . LYS B 435 ? 0.3312 0.6935 0.2174 0.0397  -0.0722 0.0327  435 LYS B CD  
7740  C CE  . LYS B 435 ? 0.3366 0.7205 0.2309 0.0559  -0.0728 0.0478  435 LYS B CE  
7741  N NZ  . LYS B 435 ? 0.3480 0.7622 0.2496 0.0503  -0.0840 0.0513  435 LYS B NZ  
7742  N N   . ALA B 436 ? 0.3014 0.5152 0.2934 -0.0527 -0.1136 0.1645  436 ALA B N   
7743  C CA  . ALA B 436 ? 0.2834 0.4668 0.3019 -0.0439 -0.1164 0.1624  436 ALA B CA  
7744  C C   . ALA B 436 ? 0.3897 0.5458 0.4255 -0.0482 -0.1214 0.1990  436 ALA B C   
7745  O O   . ALA B 436 ? 0.5265 0.6843 0.5490 -0.0642 -0.1184 0.2236  436 ALA B O   
7746  C CB  . ALA B 436 ? 0.2545 0.4432 0.2733 -0.0468 -0.1112 0.1365  436 ALA B CB  
7747  N N   . LYS B 437 ? 0.3263 0.4493 0.3927 -0.0339 -0.1244 0.2000  437 LYS B N   
7748  C CA  . LYS B 437 ? 0.3484 0.4255 0.4384 -0.0335 -0.1197 0.2211  437 LYS B CA  
7749  C C   . LYS B 437 ? 0.3484 0.3888 0.4667 -0.0293 -0.1084 0.1946  437 LYS B C   
7750  O O   . LYS B 437 ? 0.4535 0.4506 0.5932 -0.0315 -0.1012 0.2052  437 LYS B O   
7751  C CB  . LYS B 437 ? 0.3785 0.4469 0.4816 -0.0165 -0.1287 0.2450  437 LYS B CB  
7752  C CG  . LYS B 437 ? 0.4267 0.5014 0.5064 -0.0253 -0.1299 0.2746  437 LYS B CG  
7753  C CD  . LYS B 437 ? 0.5110 0.6099 0.5839 -0.0105 -0.1397 0.2780  437 LYS B CD  
7754  C CE  . LYS B 437 ? 0.6065 0.7540 0.6482 -0.0186 -0.1409 0.2574  437 LYS B CE  
7755  N NZ  . LYS B 437 ? 0.6887 0.8556 0.6986 -0.0407 -0.1347 0.2653  437 LYS B NZ  
7756  N N   . ASN B 438 ? 0.3317 0.3855 0.4487 -0.0240 -0.1060 0.1611  438 ASN B N   
7757  C CA  . ASN B 438 ? 0.3528 0.3785 0.4891 -0.0216 -0.0954 0.1345  438 ASN B CA  
7758  C C   . ASN B 438 ? 0.3625 0.4123 0.4790 -0.0243 -0.0930 0.1033  438 ASN B C   
7759  O O   . ASN B 438 ? 0.3542 0.4363 0.4485 -0.0239 -0.0992 0.1013  438 ASN B O   
7760  C CB  . ASN B 438 ? 0.4021 0.4075 0.5686 -0.0017 -0.0961 0.1343  438 ASN B CB  
7761  C CG  . ASN B 438 ? 0.3901 0.4266 0.5517 0.0103  -0.1032 0.1252  438 ASN B CG  
7762  O OD1 . ASN B 438 ? 0.4164 0.4604 0.5668 0.0096  -0.0978 0.0991  438 ASN B OD1 
7763  N ND2 . ASN B 438 ? 0.3288 0.3839 0.4981 0.0202  -0.1158 0.1478  438 ASN B ND2 
7764  N N   . ASP B 439 ? 0.2910 0.3237 0.4149 -0.0263 -0.0843 0.0784  439 ASP B N   
7765  C CA  . ASP B 439 ? 0.3586 0.4120 0.4624 -0.0285 -0.0836 0.0522  439 ASP B CA  
7766  C C   . ASP B 439 ? 0.3240 0.3886 0.4140 -0.0142 -0.0874 0.0439  439 ASP B C   
7767  O O   . ASP B 439 ? 0.3250 0.3996 0.3968 -0.0126 -0.0873 0.0255  439 ASP B O   
7768  C CB  . ASP B 439 ? 0.4490 0.4847 0.5615 -0.0360 -0.0748 0.0283  439 ASP B CB  
7769  C CG  . ASP B 439 ? 0.6803 0.7204 0.7976 -0.0569 -0.0711 0.0258  439 ASP B CG  
7770  O OD1 . ASP B 439 ? 0.6004 0.6730 0.7047 -0.0637 -0.0753 0.0315  439 ASP B OD1 
7771  O OD2 . ASP B 439 ? 0.7655 0.7780 0.9015 -0.0679 -0.0623 0.0156  439 ASP B OD2 
7772  N N   . TYR B 440 ? 0.2676 0.3321 0.3657 -0.0046 -0.0911 0.0565  440 TYR B N   
7773  C CA  . TYR B 440 ? 0.1902 0.2672 0.2734 0.0029  -0.0935 0.0485  440 TYR B CA  
7774  C C   . TYR B 440 ? 0.2061 0.3074 0.2646 0.0001  -0.1001 0.0482  440 TYR B C   
7775  O O   . TYR B 440 ? 0.3579 0.4622 0.4008 0.0050  -0.1005 0.0382  440 TYR B O   
7776  C CB  . TYR B 440 ? 0.2135 0.2931 0.3167 0.0106  -0.0962 0.0592  440 TYR B CB  
7777  C CG  . TYR B 440 ? 0.1936 0.2576 0.3156 0.0173  -0.0860 0.0467  440 TYR B CG  
7778  C CD1 . TYR B 440 ? 0.1874 0.2505 0.2928 0.0174  -0.0788 0.0301  440 TYR B CD1 
7779  C CD2 . TYR B 440 ? 0.2245 0.2732 0.3807 0.0238  -0.0818 0.0517  440 TYR B CD2 
7780  C CE1 . TYR B 440 ? 0.1951 0.2487 0.3145 0.0208  -0.0663 0.0177  440 TYR B CE1 
7781  C CE2 . TYR B 440 ? 0.2881 0.3273 0.4638 0.0303  -0.0697 0.0359  440 TYR B CE2 
7782  C CZ  . TYR B 440 ? 0.2808 0.3257 0.4367 0.0274  -0.0612 0.0183  440 TYR B CZ  
7783  O OH  . TYR B 440 ? 0.2172 0.2574 0.3898 0.0313  -0.0461 0.0017  440 TYR B OH  
7784  N N   . ILE B 441 ? 0.1845 0.3014 0.2394 -0.0082 -0.1033 0.0584  441 ILE B N   
7785  C CA  . ILE B 441 ? 0.2045 0.3430 0.2373 -0.0093 -0.1030 0.0496  441 ILE B CA  
7786  C C   . ILE B 441 ? 0.1990 0.3389 0.2223 -0.0052 -0.1012 0.0299  441 ILE B C   
7787  O O   . ILE B 441 ? 0.2137 0.3506 0.2216 0.0026  -0.0987 0.0174  441 ILE B O   
7788  C CB  . ILE B 441 ? 0.2260 0.3847 0.2568 -0.0215 -0.1033 0.0646  441 ILE B CB  
7789  C CG1 . ILE B 441 ? 0.1952 0.3673 0.2057 -0.0195 -0.0983 0.0557  441 ILE B CG1 
7790  C CG2 . ILE B 441 ? 0.1949 0.3651 0.2314 -0.0334 -0.1007 0.0605  441 ILE B CG2 
7791  C CD1 . ILE B 441 ? 0.1973 0.3605 0.2042 -0.0129 -0.0999 0.0550  441 ILE B CD1 
7792  N N   . LEU B 442 ? 0.2307 0.3641 0.2638 -0.0098 -0.1000 0.0248  442 LEU B N   
7793  C CA  . LEU B 442 ? 0.2027 0.3428 0.2252 -0.0045 -0.1011 0.0063  442 LEU B CA  
7794  C C   . LEU B 442 ? 0.2573 0.3804 0.2625 0.0093  -0.1020 0.0008  442 LEU B C   
7795  O O   . LEU B 442 ? 0.2381 0.3566 0.2272 0.0164  -0.1003 -0.0051 442 LEU B O   
7796  C CB  . LEU B 442 ? 0.1879 0.3208 0.2227 -0.0145 -0.0970 -0.0031 442 LEU B CB  
7797  C CG  . LEU B 442 ? 0.1958 0.3451 0.2466 -0.0324 -0.0942 -0.0019 442 LEU B CG  
7798  C CD1 . LEU B 442 ? 0.2128 0.3497 0.2765 -0.0442 -0.0891 -0.0171 442 LEU B CD1 
7799  C CD2 . LEU B 442 ? 0.2032 0.3954 0.2480 -0.0319 -0.0986 -0.0098 442 LEU B CD2 
7800  N N   . VAL B 443 ? 0.1787 0.2789 0.1894 0.0098  -0.0972 0.0063  443 VAL B N   
7801  C CA  . VAL B 443 ? 0.1843 0.2675 0.1788 0.0180  -0.0944 0.0029  443 VAL B CA  
7802  C C   . VAL B 443 ? 0.1828 0.2696 0.1645 0.0235  -0.0984 0.0051  443 VAL B C   
7803  O O   . VAL B 443 ? 0.2524 0.3249 0.2134 0.0317  -0.0979 0.0012  443 VAL B O   
7804  C CB  . VAL B 443 ? 0.2550 0.3223 0.2659 0.0152  -0.0862 0.0063  443 VAL B CB  
7805  C CG1 . VAL B 443 ? 0.2654 0.3160 0.2579 0.0187  -0.0789 0.0011  443 VAL B CG1 
7806  C CG2 . VAL B 443 ? 0.2819 0.3429 0.3123 0.0103  -0.0811 0.0021  443 VAL B CG2 
7807  N N   . ALA B 444 ? 0.1959 0.2952 0.1882 0.0170  -0.0995 0.0121  444 ALA B N   
7808  C CA  . ALA B 444 ? 0.2261 0.3239 0.2089 0.0174  -0.0984 0.0097  444 ALA B CA  
7809  C C   . ALA B 444 ? 0.2443 0.3444 0.2159 0.0239  -0.0962 0.0012  444 ALA B C   
7810  O O   . ALA B 444 ? 0.2504 0.3495 0.2132 0.0295  -0.0966 -0.0057 444 ALA B O   
7811  C CB  . ALA B 444 ? 0.1781 0.2872 0.1699 0.0114  -0.1003 0.0135  444 ALA B CB  
7812  N N   . GLU B 445 ? 0.1891 0.2963 0.1631 0.0253  -0.0957 -0.0012 445 GLU B N   
7813  C CA  . GLU B 445 ? 0.1954 0.3138 0.1659 0.0346  -0.0951 -0.0100 445 GLU B CA  
7814  C C   . GLU B 445 ? 0.2434 0.3477 0.2004 0.0489  -0.0974 -0.0129 445 GLU B C   
7815  O O   . GLU B 445 ? 0.2212 0.3376 0.1784 0.0601  -0.0996 -0.0193 445 GLU B O   
7816  C CB  . GLU B 445 ? 0.1903 0.3339 0.1738 0.0276  -0.0947 -0.0127 445 GLU B CB  
7817  C CG  . GLU B 445 ? 0.1926 0.3538 0.1835 0.0170  -0.0926 -0.0092 445 GLU B CG  
7818  C CD  . GLU B 445 ? 0.3158 0.4978 0.3195 0.0048  -0.0927 -0.0065 445 GLU B CD  
7819  O OE1 . GLU B 445 ? 0.3346 0.5289 0.3448 0.0048  -0.0936 -0.0144 445 GLU B OE1 
7820  O OE2 . GLU B 445 ? 0.3634 0.5535 0.3712 -0.0063 -0.0920 0.0047  445 GLU B OE2 
7821  N N   . GLY B 446 ? 0.2477 0.3291 0.1918 0.0503  -0.0979 -0.0081 446 GLY B N   
7822  C CA  . GLY B 446 ? 0.2444 0.3067 0.1665 0.0648  -0.1011 -0.0071 446 GLY B CA  
7823  C C   . GLY B 446 ? 0.2848 0.3312 0.1954 0.0821  -0.1050 -0.0091 446 GLY B C   
7824  O O   . GLY B 446 ? 0.2958 0.3338 0.2061 0.0814  -0.1058 -0.0122 446 GLY B O   
7825  N N   . SER B 447 ? 0.3272 0.3702 0.2280 0.0996  -0.1100 -0.0086 447 SER B N   
7826  C CA  . SER B 447 ? 0.3249 0.3441 0.2128 0.1229  -0.1162 -0.0101 447 SER B CA  
7827  C C   . SER B 447 ? 0.3597 0.3230 0.2161 0.1278  -0.1171 0.0012  447 SER B C   
7828  O O   . SER B 447 ? 0.3865 0.3181 0.2406 0.1354  -0.1135 -0.0023 447 SER B O   
7829  C CB  . SER B 447 ? 0.3517 0.3787 0.2375 0.1429  -0.1224 -0.0087 447 SER B CB  
7830  O OG  . SER B 447 ? 0.3764 0.3856 0.2394 0.1428  -0.1238 0.0055  447 SER B OG  
7831  N N   . ASP B 448 ? 0.3622 0.3107 0.2024 0.1142  -0.1119 0.0118  448 ASP B N   
7832  C CA  . ASP B 448 ? 0.3965 0.2939 0.2160 0.1048  -0.0993 0.0226  448 ASP B CA  
7833  C C   . ASP B 448 ? 0.3813 0.2712 0.2207 0.0846  -0.0880 0.0134  448 ASP B C   
7834  O O   . ASP B 448 ? 0.4587 0.3112 0.2874 0.0717  -0.0757 0.0190  448 ASP B O   
7835  C CB  . ASP B 448 ? 0.4020 0.2974 0.2023 0.0935  -0.0935 0.0323  448 ASP B CB  
7836  C CG  . ASP B 448 ? 0.4096 0.3297 0.1969 0.1065  -0.1045 0.0354  448 ASP B CG  
7837  O OD1 . ASP B 448 ? 0.3696 0.3350 0.1845 0.0975  -0.1059 0.0232  448 ASP B OD1 
7838  O OD2 . ASP B 448 ? 0.4587 0.3563 0.2202 0.1184  -0.1061 0.0488  448 ASP B OD2 
7839  N N   . TRP B 449 ? 0.3584 0.2860 0.2250 0.0796  -0.0919 -0.0002 449 TRP B N   
7840  C CA  . TRP B 449 ? 0.3337 0.2629 0.2167 0.0618  -0.0852 -0.0101 449 TRP B CA  
7841  C C   . TRP B 449 ? 0.3587 0.2748 0.2431 0.0699  -0.0854 -0.0244 449 TRP B C   
7842  O O   . TRP B 449 ? 0.5345 0.4342 0.4233 0.0551  -0.0779 -0.0340 449 TRP B O   
7843  C CB  . TRP B 449 ? 0.2868 0.2658 0.1943 0.0495  -0.0893 -0.0139 449 TRP B CB  
7844  C CG  . TRP B 449 ? 0.2724 0.2641 0.1851 0.0435  -0.0885 -0.0043 449 TRP B CG  
7845  C CD1 . TRP B 449 ? 0.2709 0.2938 0.1945 0.0451  -0.0947 -0.0031 449 TRP B CD1 
7846  C CD2 . TRP B 449 ? 0.2754 0.2484 0.1848 0.0335  -0.0786 0.0021  449 TRP B CD2 
7847  N NE1 . TRP B 449 ? 0.2908 0.3115 0.2184 0.0383  -0.0897 0.0020  449 TRP B NE1 
7848  C CE2 . TRP B 449 ? 0.2546 0.2482 0.1737 0.0321  -0.0795 0.0048  449 TRP B CE2 
7849  C CE3 . TRP B 449 ? 0.3164 0.2577 0.2168 0.0236  -0.0667 0.0042  449 TRP B CE3 
7850  C CZ2 . TRP B 449 ? 0.2593 0.2456 0.1800 0.0240  -0.0690 0.0071  449 TRP B CZ2 
7851  C CZ3 . TRP B 449 ? 0.3792 0.3172 0.2806 0.0136  -0.0558 0.0087  449 TRP B CZ3 
7852  C CH2 . TRP B 449 ? 0.3786 0.3404 0.2903 0.0152  -0.0570 0.0091  449 TRP B CH2 
7853  N N   . PHE B 450 ? 0.3628 0.2894 0.2467 0.0926  -0.0932 -0.0294 450 PHE B N   
7854  C CA  . PHE B 450 ? 0.3839 0.3057 0.2743 0.1031  -0.0921 -0.0482 450 PHE B CA  
7855  C C   . PHE B 450 ? 0.4436 0.3057 0.3187 0.1250  -0.0899 -0.0450 450 PHE B C   
7856  O O   . PHE B 450 ? 0.5305 0.3788 0.4127 0.1367  -0.0870 -0.0631 450 PHE B O   
7857  C CB  . PHE B 450 ? 0.3558 0.3344 0.2623 0.1148  -0.0999 -0.0591 450 PHE B CB  
7858  C CG  . PHE B 450 ? 0.3234 0.3538 0.2422 0.0939  -0.1016 -0.0575 450 PHE B CG  
7859  C CD1 . PHE B 450 ? 0.2817 0.3305 0.2022 0.0902  -0.1066 -0.0427 450 PHE B CD1 
7860  C CD2 . PHE B 450 ? 0.3356 0.3938 0.2622 0.0778  -0.0983 -0.0705 450 PHE B CD2 
7861  C CE1 . PHE B 450 ? 0.2475 0.3328 0.1812 0.0716  -0.1062 -0.0385 450 PHE B CE1 
7862  C CE2 . PHE B 450 ? 0.2620 0.3624 0.1968 0.0606  -0.1010 -0.0631 450 PHE B CE2 
7863  C CZ  . PHE B 450 ? 0.2391 0.3477 0.1796 0.0576  -0.1033 -0.0454 450 PHE B CZ  
7864  N N   . TRP B 451 ? 0.4708 0.2953 0.3234 0.1310  -0.0903 -0.0222 451 TRP B N   
7865  C CA  . TRP B 451 ? 0.5381 0.3001 0.3713 0.1539  -0.0895 -0.0113 451 TRP B CA  
7866  C C   . TRP B 451 ? 0.6619 0.3572 0.4841 0.1351  -0.0732 -0.0107 451 TRP B C   
7867  O O   . TRP B 451 ? 0.8078 0.4464 0.6242 0.1509  -0.0690 -0.0125 451 TRP B O   
7868  C CB  . TRP B 451 ? 0.5541 0.3113 0.3618 0.1699  -0.0993 0.0157  451 TRP B CB  
7869  C CG  . TRP B 451 ? 0.7932 0.4802 0.5646 0.1677  -0.0910 0.0414  451 TRP B CG  
7870  C CD1 . TRP B 451 ? 0.7985 0.4588 0.5567 0.1365  -0.0749 0.0491  451 TRP B CD1 
7871  C CD2 . TRP B 451 ? 0.8661 0.5043 0.6093 0.1978  -0.0982 0.0649  451 TRP B CD2 
7872  N NE1 . TRP B 451 ? 0.8824 0.4782 0.6033 0.1415  -0.0688 0.0757  451 TRP B NE1 
7873  C CE2 . TRP B 451 ? 0.9185 0.4992 0.6287 0.1788  -0.0834 0.0876  451 TRP B CE2 
7874  C CE3 . TRP B 451 ? 0.7693 0.4303 0.5272 0.2264  -0.1094 0.0654  451 TRP B CE3 
7875  C CZ2 . TRP B 451 ? 0.8076 0.3530 0.4976 0.1889  -0.0813 0.1127  451 TRP B CZ2 
7876  C CZ3 . TRP B 451 ? 0.7759 0.3994 0.5150 0.2384  -0.1091 0.0907  451 TRP B CZ3 
7877  C CH2 . TRP B 451 ? 0.8262 0.3921 0.5306 0.2202  -0.0959 0.1150  451 TRP B CH2 
7878  N N   . TRP B 452 ? 0.7251 0.4258 0.5477 0.1017  -0.0631 -0.0093 452 TRP B N   
7879  C CA  . TRP B 452 ? 0.8107 0.4541 0.6261 0.0785  -0.0460 -0.0100 452 TRP B CA  
7880  C C   . TRP B 452 ? 0.8506 0.4929 0.6884 0.0656  -0.0401 -0.0417 452 TRP B C   
7881  O O   . TRP B 452 ? 0.9627 0.5421 0.7953 0.0591  -0.0279 -0.0485 452 TRP B O   
7882  C CB  . TRP B 452 ? 0.8089 0.4691 0.6233 0.0476  -0.0368 -0.0007 452 TRP B CB  
7883  C CG  . TRP B 452 ? 0.9410 0.6147 0.7347 0.0564  -0.0415 0.0232  452 TRP B CG  
7884  C CD1 . TRP B 452 ? 0.8303 0.5645 0.6344 0.0609  -0.0524 0.0227  452 TRP B CD1 
7885  C CD2 . TRP B 452 ? 0.9736 0.5985 0.7296 0.0600  -0.0344 0.0501  452 TRP B CD2 
7886  N NE1 . TRP B 452 ? 0.8952 0.6240 0.6722 0.0666  -0.0528 0.0429  452 TRP B NE1 
7887  C CE2 . TRP B 452 ? 0.9243 0.5894 0.6689 0.0665  -0.0424 0.0611  452 TRP B CE2 
7888  C CE3 . TRP B 452 ? 0.8857 0.4342 0.6138 0.0570  -0.0213 0.0667  452 TRP B CE3 
7889  C CZ2 . TRP B 452 ? 1.0858 0.7247 0.7892 0.0702  -0.0387 0.0864  452 TRP B CZ2 
7890  C CZ3 . TRP B 452 ? 0.9606 0.4792 0.6464 0.0611  -0.0174 0.0972  452 TRP B CZ3 
7891  C CH2 . TRP B 452 ? 1.0083 0.5757 0.6807 0.0677  -0.0266 0.1060  452 TRP B CH2 
7892  N N   . GLN B 453 ? 0.8370 0.5466 0.6973 0.0599  -0.0479 -0.0616 453 GLN B N   
7893  C CA  . GLN B 453 ? 0.7797 0.5010 0.6569 0.0443  -0.0434 -0.0939 453 GLN B CA  
7894  C C   . GLN B 453 ? 0.7667 0.4508 0.6440 0.0689  -0.0412 -0.1122 453 GLN B C   
7895  O O   . GLN B 453 ? 0.7599 0.4472 0.6348 0.1021  -0.0497 -0.1042 453 GLN B O   
7896  C CB  . GLN B 453 ? 0.6623 0.4672 0.5565 0.0352  -0.0536 -0.1048 453 GLN B CB  
7897  C CG  . GLN B 453 ? 0.7346 0.5747 0.6398 0.0043  -0.0533 -0.1010 453 GLN B CG  
7898  C CD  . GLN B 453 ? 0.8808 0.6938 0.7787 -0.0027 -0.0470 -0.0761 453 GLN B CD  
7899  O OE1 . GLN B 453 ? 0.7720 0.5684 0.6752 -0.0275 -0.0366 -0.0786 453 GLN B OE1 
7900  N NE2 . GLN B 453 ? 0.6782 0.4924 0.5644 0.0171  -0.0525 -0.0541 453 GLN B NE2 
7901  N N   . GLY B 454 ? 0.7780 0.4286 0.6611 0.0527  -0.0297 -0.1394 454 GLY B N   
7902  C CA  . GLY B 454 ? 0.8817 0.4919 0.7690 0.0751  -0.0246 -0.1630 454 GLY B CA  
7903  C C   . GLY B 454 ? 1.2247 0.7316 1.0992 0.0853  -0.0129 -0.1516 454 GLY B C   
7904  O O   . GLY B 454 ? 1.3496 0.8089 1.2165 0.0558  -0.0002 -0.1466 454 GLY B O   
7905  N N   . GLU B 455 ? 1.3402 0.8123 1.2136 0.1278  -0.0170 -0.1463 455 GLU B N   
7906  C CA  . GLU B 455 ? 1.4734 0.8434 1.3371 0.1435  -0.0066 -0.1345 455 GLU B CA  
7907  C C   . GLU B 455 ? 1.5609 0.8896 1.3978 0.1385  -0.0057 -0.0855 455 GLU B C   
7908  O O   . GLU B 455 ? 1.6426 0.9094 1.4805 0.1411  0.0041  -0.0669 455 GLU B O   
7909  C CB  . GLU B 455 ? 1.2291 0.6071 1.1145 0.1890  -0.0115 -0.1360 455 GLU B CB  
7910  C CG  . GLU B 455 ? 1.5173 0.8270 1.4246 0.1948  0.0061  -0.1466 455 GLU B CG  
7911  C CD  . GLU B 455 ? 1.5599 0.8801 1.4897 0.1793  0.0220  -0.2015 455 GLU B CD  
7912  O OE1 . GLU B 455 ? 1.4203 0.8049 1.3444 0.1612  0.0173  -0.2287 455 GLU B OE1 
7913  O OE2 . GLU B 455 ? 1.5672 0.8339 1.5202 0.1848  0.0389  -0.2173 455 GLU B OE2 
7914  N N   . GLU B 456 ? 1.3908 0.7671 1.2118 0.1284  -0.0151 -0.0641 456 GLU B N   
7915  C CA  . GLU B 456 ? 1.3825 0.7232 1.1708 0.1254  -0.0138 -0.0206 456 GLU B CA  
7916  C C   . GLU B 456 ? 1.4449 0.7642 1.2274 0.0761  0.0053  -0.0195 456 GLU B C   
7917  O O   . GLU B 456 ? 1.2333 0.6114 1.0378 0.0450  0.0077  -0.0435 456 GLU B O   
7918  C CB  . GLU B 456 ? 1.2425 0.6584 1.0241 0.1395  -0.0321 -0.0009 456 GLU B CB  
7919  C CG  . GLU B 456 ? 1.1908 0.6015 0.9614 0.1847  -0.0479 0.0232  456 GLU B CG  
7920  C CD  . GLU B 456 ? 1.3837 0.8281 1.1872 0.2163  -0.0575 -0.0030 456 GLU B CD  
7921  O OE1 . GLU B 456 ? 1.3651 0.8249 1.1898 0.2067  -0.0523 -0.0407 456 GLU B OE1 
7922  O OE2 . GLU B 456 ? 1.4978 0.9589 1.3076 0.2479  -0.0688 0.0125  456 GLU B OE2 
7923  N N   . LYS B 457 ? 1.4844 0.7433 1.2481 0.0673  0.0179  0.0098  457 LYS B N   
7924  C CA  . LYS B 457 ? 1.3765 0.6140 1.1379 0.0202  0.0387  0.0117  457 LYS B CA  
7925  C C   . LYS B 457 ? 1.4040 0.6401 1.1316 0.0156  0.0419  0.0534  457 LYS B C   
7926  O O   . LYS B 457 ? 1.4384 0.6466 1.1451 0.0400  0.0371  0.0852  457 LYS B O   
7927  C CB  . LYS B 457 ? 1.2717 0.4489 1.0506 0.0066  0.0535  0.0020  457 LYS B CB  
7928  C CG  . LYS B 457 ? 1.2258 0.4067 1.0374 0.0140  0.0502  -0.0425 457 LYS B CG  
7929  C CD  . LYS B 457 ? 1.1751 0.3021 0.9968 0.0483  0.0471  -0.0377 457 LYS B CD  
7930  C CE  . LYS B 457 ? 1.2696 0.3242 1.0926 0.0256  0.0624  -0.0274 457 LYS B CE  
7931  N NZ  . LYS B 457 ? 1.3445 0.3465 1.1898 0.0525  0.0596  -0.0398 457 LYS B NZ  
7932  N N   . ALA B 458 ? 1.5011 0.7723 1.2256 -0.0166 0.0502  0.0513  458 ALA B N   
7933  C CA  . ALA B 458 ? 1.4240 0.7121 1.1175 -0.0202 0.0527  0.0832  458 ALA B CA  
7934  C C   . ALA B 458 ? 1.2938 0.6235 1.0055 -0.0654 0.0695  0.0702  458 ALA B C   
7935  O O   . ALA B 458 ? 1.1439 0.5010 0.8950 -0.0890 0.0733  0.0373  458 ALA B O   
7936  C CB  . ALA B 458 ? 1.2517 0.5954 0.9373 0.0166  0.0275  0.0907  458 ALA B CB  
7937  N N   . PRO B 459 ? 1.1740 0.5201 0.8636 -0.0785 0.0797  0.0922  459 PRO B N   
7938  C CA  . PRO B 459 ? 1.1166 0.5149 0.8349 -0.1182 0.0960  0.0765  459 PRO B CA  
7939  C C   . PRO B 459 ? 1.0673 0.5621 0.8162 -0.1087 0.0794  0.0608  459 PRO B C   
7940  O O   . PRO B 459 ? 0.9505 0.4707 0.6910 -0.0755 0.0582  0.0659  459 PRO B O   
7941  C CB  . PRO B 459 ? 1.0891 0.4565 0.7677 -0.1353 0.1183  0.1073  459 PRO B CB  
7942  C CG  . PRO B 459 ? 1.1149 0.4482 0.7483 -0.0962 0.1035  0.1393  459 PRO B CG  
7943  C CD  . PRO B 459 ? 1.2276 0.5553 0.8693 -0.0584 0.0773  0.1296  459 PRO B CD  
7944  N N   . PHE B 460 ? 1.0187 0.5670 0.8065 -0.1390 0.0897  0.0413  460 PHE B N   
7945  C CA  . PHE B 460 ? 0.8003 0.4348 0.6217 -0.1334 0.0776  0.0282  460 PHE B CA  
7946  C C   . PHE B 460 ? 0.7523 0.4218 0.5931 -0.1068 0.0502  0.0140  460 PHE B C   
7947  O O   . PHE B 460 ? 0.6812 0.4037 0.5343 -0.0909 0.0366  0.0131  460 PHE B O   
7948  C CB  . PHE B 460 ? 0.6904 0.3411 0.4853 -0.1226 0.0813  0.0473  460 PHE B CB  
7949  C CG  . PHE B 460 ? 0.7996 0.4304 0.5755 -0.1514 0.1110  0.0595  460 PHE B CG  
7950  C CD1 . PHE B 460 ? 0.7907 0.4547 0.6071 -0.1861 0.1300  0.0420  460 PHE B CD1 
7951  C CD2 . PHE B 460 ? 0.8873 0.4723 0.6044 -0.1444 0.1198  0.0886  460 PHE B CD2 
7952  C CE1 . PHE B 460 ? 0.8142 0.4653 0.6151 -0.2155 0.1608  0.0516  460 PHE B CE1 
7953  C CE2 . PHE B 460 ? 0.8316 0.4002 0.5260 -0.1736 0.1499  0.1012  460 PHE B CE2 
7954  C CZ  . PHE B 460 ? 0.8210 0.4224 0.5584 -0.2102 0.1721  0.0818  460 PHE B CZ  
7955  N N   . VAL B 461 ? 0.7424 0.3816 0.5859 -0.1031 0.0440  0.0017  461 VAL B N   
7956  C CA  . VAL B 461 ? 0.6784 0.3565 0.5398 -0.0821 0.0215  -0.0141 461 VAL B CA  
7957  C C   . VAL B 461 ? 0.6354 0.3893 0.5398 -0.0979 0.0145  -0.0335 461 VAL B C   
7958  O O   . VAL B 461 ? 0.6113 0.4129 0.5287 -0.0813 -0.0036 -0.0383 461 VAL B O   
7959  C CB  . VAL B 461 ? 0.6331 0.2626 0.4882 -0.0752 0.0196  -0.0275 461 VAL B CB  
7960  C CG1 . VAL B 461 ? 0.7971 0.3425 0.6123 -0.0605 0.0283  -0.0043 461 VAL B CG1 
7961  C CG2 . VAL B 461 ? 0.6504 0.2810 0.5319 -0.1095 0.0298  -0.0550 461 VAL B CG2 
7962  N N   . GLU B 462 ? 0.5866 0.3550 0.5146 -0.1299 0.0285  -0.0433 462 GLU B N   
7963  C CA  . GLU B 462 ? 0.5831 0.4286 0.5549 -0.1420 0.0195  -0.0589 462 GLU B CA  
7964  C C   . GLU B 462 ? 0.4639 0.3553 0.4459 -0.1251 0.0122  -0.0452 462 GLU B C   
7965  O O   . GLU B 462 ? 0.3847 0.3322 0.3927 -0.1166 -0.0048 -0.0502 462 GLU B O   
7966  C CB  . GLU B 462 ? 0.5684 0.4247 0.5676 -0.1798 0.0366  -0.0731 462 GLU B CB  
7967  C CG  . GLU B 462 ? 0.7937 0.6431 0.8050 -0.2015 0.0353  -0.1003 462 GLU B CG  
7968  C CD  . GLU B 462 ? 1.0534 0.8162 1.0390 -0.2192 0.0572  -0.1008 462 GLU B CD  
7969  O OE1 . GLU B 462 ? 1.1409 0.9008 1.1472 -0.2564 0.0724  -0.1188 462 GLU B OE1 
7970  O OE2 . GLU B 462 ? 1.1340 0.8316 1.0803 -0.1959 0.0590  -0.0827 462 GLU B OE2 
7971  N N   . VAL B 463 ? 0.5033 0.3699 0.4636 -0.1209 0.0256  -0.0279 463 VAL B N   
7972  C CA  . VAL B 463 ? 0.4078 0.3121 0.3770 -0.1056 0.0211  -0.0195 463 VAL B CA  
7973  C C   . VAL B 463 ? 0.3795 0.2881 0.3346 -0.0766 0.0004  -0.0134 463 VAL B C   
7974  O O   . VAL B 463 ? 0.3559 0.3077 0.3336 -0.0659 -0.0111 -0.0139 463 VAL B O   
7975  C CB  . VAL B 463 ? 0.4401 0.3189 0.3841 -0.1111 0.0423  -0.0065 463 VAL B CB  
7976  C CG1 . VAL B 463 ? 0.4085 0.3132 0.3505 -0.0910 0.0365  -0.0008 463 VAL B CG1 
7977  C CG2 . VAL B 463 ? 0.4551 0.3532 0.4270 -0.1416 0.0644  -0.0155 463 VAL B CG2 
7978  N N   . PHE B 464 ? 0.4370 0.3010 0.3575 -0.0634 -0.0040 -0.0076 464 PHE B N   
7979  C CA  . PHE B 464 ? 0.4070 0.2826 0.3196 -0.0382 -0.0227 -0.0054 464 PHE B CA  
7980  C C   . PHE B 464 ? 0.3729 0.2936 0.3151 -0.0395 -0.0369 -0.0186 464 PHE B C   
7981  O O   . PHE B 464 ? 0.3359 0.2918 0.2889 -0.0279 -0.0490 -0.0158 464 PHE B O   
7982  C CB  . PHE B 464 ? 0.4776 0.3025 0.3558 -0.0224 -0.0249 0.0004  464 PHE B CB  
7983  C CG  . PHE B 464 ? 0.4916 0.2801 0.3328 -0.0129 -0.0183 0.0197  464 PHE B CG  
7984  C CD1 . PHE B 464 ? 0.4389 0.2519 0.2710 0.0012  -0.0259 0.0272  464 PHE B CD1 
7985  C CD2 . PHE B 464 ? 0.6838 0.4125 0.4967 -0.0197 -0.0045 0.0307  464 PHE B CD2 
7986  C CE1 . PHE B 464 ? 0.6298 0.4162 0.4231 0.0090  -0.0217 0.0439  464 PHE B CE1 
7987  C CE2 . PHE B 464 ? 0.7534 0.4503 0.5253 -0.0108 0.0003  0.0527  464 PHE B CE2 
7988  C CZ  . PHE B 464 ? 0.7465 0.4761 0.5074 0.0039  -0.0094 0.0586  464 PHE B CZ  
7989  N N   . ASP B 465 ? 0.4173 0.3370 0.3705 -0.0558 -0.0349 -0.0333 465 ASP B N   
7990  C CA  . ASP B 465 ? 0.3319 0.3002 0.3081 -0.0600 -0.0487 -0.0461 465 ASP B CA  
7991  C C   . ASP B 465 ? 0.2926 0.3147 0.3005 -0.0631 -0.0551 -0.0401 465 ASP B C   
7992  O O   . ASP B 465 ? 0.3274 0.3854 0.3439 -0.0529 -0.0696 -0.0354 465 ASP B O   
7993  C CB  . ASP B 465 ? 0.3621 0.3230 0.3451 -0.0818 -0.0440 -0.0670 465 ASP B CB  
7994  C CG  . ASP B 465 ? 0.4142 0.4332 0.4165 -0.0890 -0.0594 -0.0812 465 ASP B CG  
7995  O OD1 . ASP B 465 ? 0.4383 0.4705 0.4285 -0.0753 -0.0702 -0.0839 465 ASP B OD1 
7996  O OD2 . ASP B 465 ? 0.3768 0.4334 0.4063 -0.1085 -0.0608 -0.0893 465 ASP B OD2 
7997  N N   . LYS B 466 ? 0.2966 0.3241 0.3235 -0.0766 -0.0431 -0.0393 466 LYS B N   
7998  C CA  . LYS B 466 ? 0.2648 0.3434 0.3290 -0.0758 -0.0486 -0.0352 466 LYS B CA  
7999  C C   . LYS B 466 ? 0.2405 0.3219 0.3014 -0.0541 -0.0544 -0.0205 466 LYS B C   
8000  O O   . LYS B 466 ? 0.2245 0.3432 0.3103 -0.0460 -0.0667 -0.0144 466 LYS B O   
8001  C CB  . LYS B 466 ? 0.2773 0.3612 0.3639 -0.0927 -0.0304 -0.0397 466 LYS B CB  
8002  C CG  . LYS B 466 ? 0.2489 0.3876 0.3821 -0.0882 -0.0347 -0.0379 466 LYS B CG  
8003  C CD  . LYS B 466 ? 0.3114 0.4527 0.4632 -0.1003 -0.0115 -0.0425 466 LYS B CD  
8004  C CE  . LYS B 466 ? 0.3636 0.5714 0.5756 -0.1034 -0.0154 -0.0500 466 LYS B CE  
8005  N NZ  . LYS B 466 ? 0.2622 0.4812 0.4968 -0.1236 0.0103  -0.0611 466 LYS B NZ  
8006  N N   . LEU B 467 ? 0.3386 0.3801 0.3684 -0.0449 -0.0463 -0.0145 467 LEU B N   
8007  C CA  . LEU B 467 ? 0.2352 0.2794 0.2620 -0.0284 -0.0506 -0.0055 467 LEU B CA  
8008  C C   . LEU B 467 ? 0.2935 0.3507 0.3150 -0.0175 -0.0676 -0.0016 467 LEU B C   
8009  O O   . LEU B 467 ? 0.3363 0.4152 0.3752 -0.0105 -0.0752 0.0054  467 LEU B O   
8010  C CB  . LEU B 467 ? 0.2584 0.2647 0.2510 -0.0234 -0.0394 -0.0020 467 LEU B CB  
8011  C CG  . LEU B 467 ? 0.2730 0.2753 0.2699 -0.0318 -0.0205 -0.0033 467 LEU B CG  
8012  C CD1 . LEU B 467 ? 0.3146 0.2739 0.2659 -0.0339 -0.0086 0.0023  467 LEU B CD1 
8013  C CD2 . LEU B 467 ? 0.2534 0.2762 0.2696 -0.0224 -0.0204 -0.0045 467 LEU B CD2 
8014  N N   . PHE B 468 ? 0.2651 0.3078 0.2636 -0.0162 -0.0717 -0.0066 468 PHE B N   
8015  C CA  . PHE B 468 ? 0.2202 0.2803 0.2130 -0.0077 -0.0844 -0.0054 468 PHE B CA  
8016  C C   . PHE B 468 ? 0.2449 0.3474 0.2606 -0.0134 -0.0952 -0.0018 468 PHE B C   
8017  O O   . PHE B 468 ? 0.2911 0.4120 0.3125 -0.0077 -0.1028 0.0087  468 PHE B O   
8018  C CB  . PHE B 468 ? 0.2624 0.3033 0.2324 -0.0047 -0.0846 -0.0162 468 PHE B CB  
8019  C CG  . PHE B 468 ? 0.2282 0.2949 0.1942 0.0019  -0.0943 -0.0193 468 PHE B CG  
8020  C CD1 . PHE B 468 ? 0.2189 0.2894 0.1782 0.0145  -0.0974 -0.0141 468 PHE B CD1 
8021  C CD2 . PHE B 468 ? 0.2861 0.3785 0.2548 -0.0070 -0.0994 -0.0296 468 PHE B CD2 
8022  C CE1 . PHE B 468 ? 0.2116 0.3108 0.1695 0.0175  -0.1032 -0.0179 468 PHE B CE1 
8023  C CE2 . PHE B 468 ? 0.2261 0.3463 0.1880 -0.0031 -0.1053 -0.0331 468 PHE B CE2 
8024  C CZ  . PHE B 468 ? 0.2165 0.3379 0.1745 0.0085  -0.1050 -0.0261 468 PHE B CZ  
8025  N N   . ARG B 469 ? 0.2184 0.3375 0.2469 -0.0260 -0.0965 -0.0095 469 ARG B N   
8026  C CA  . ARG B 469 ? 0.1966 0.3620 0.2441 -0.0304 -0.1103 -0.0043 469 ARG B CA  
8027  C C   . ARG B 469 ? 0.2308 0.4125 0.3080 -0.0230 -0.1136 0.0123  469 ARG B C   
8028  O O   . ARG B 469 ? 0.3241 0.5185 0.4061 -0.0154 -0.1193 0.0224  469 ARG B O   
8029  C CB  . ARG B 469 ? 0.2105 0.3954 0.2670 -0.0472 -0.1119 -0.0202 469 ARG B CB  
8030  C CG  . ARG B 469 ? 0.2979 0.4527 0.3284 -0.0545 -0.1042 -0.0402 469 ARG B CG  
8031  C CD  . ARG B 469 ? 0.3624 0.5347 0.4022 -0.0756 -0.1048 -0.0609 469 ARG B CD  
8032  N NE  . ARG B 469 ? 0.2972 0.4501 0.3122 -0.0801 -0.1019 -0.0819 469 ARG B NE  
8033  C CZ  . ARG B 469 ? 0.3525 0.5348 0.3531 -0.0783 -0.1120 -0.0889 469 ARG B CZ  
8034  N NH1 . ARG B 469 ? 0.3657 0.5752 0.3700 -0.0681 -0.1197 -0.0667 469 ARG B NH1 
8035  N NH2 . ARG B 469 ? 0.3911 0.5519 0.3722 -0.0806 -0.1058 -0.1125 469 ARG B NH2 
8036  N N   . SER B 470 ? 0.3538 0.5163 0.4445 -0.0210 -0.1009 0.0108  470 SER B N   
8037  C CA  . SER B 470 ? 0.2708 0.4434 0.3924 -0.0110 -0.1010 0.0222  470 SER B CA  
8038  C C   . SER B 470 ? 0.2854 0.4420 0.3967 0.0000  -0.1039 0.0342  470 SER B C   
8039  O O   . SER B 470 ? 0.3381 0.5067 0.4716 0.0081  -0.1115 0.0488  470 SER B O   
8040  C CB  . SER B 470 ? 0.2638 0.4214 0.3987 -0.0131 -0.0829 0.0128  470 SER B CB  
8041  O OG  . SER B 470 ? 0.2006 0.3935 0.3796 -0.0133 -0.0837 0.0120  470 SER B OG  
8042  N N   . PHE B 471 ? 0.2849 0.4143 0.3647 0.0004  -0.0982 0.0285  471 PHE B N   
8043  C CA  . PHE B 471 ? 0.2528 0.3728 0.3252 0.0065  -0.1004 0.0360  471 PHE B CA  
8044  C C   . PHE B 471 ? 0.2394 0.3746 0.3025 0.0056  -0.1073 0.0439  471 PHE B C   
8045  O O   . PHE B 471 ? 0.2765 0.4092 0.3464 0.0079  -0.1079 0.0556  471 PHE B O   
8046  C CB  . PHE B 471 ? 0.2062 0.3022 0.2494 0.0082  -0.0936 0.0255  471 PHE B CB  
8047  C CG  . PHE B 471 ? 0.2153 0.2894 0.2556 0.0094  -0.0808 0.0174  471 PHE B CG  
8048  C CD1 . PHE B 471 ? 0.2257 0.2979 0.2897 0.0116  -0.0740 0.0172  471 PHE B CD1 
8049  C CD2 . PHE B 471 ? 0.2842 0.3380 0.2961 0.0090  -0.0747 0.0104  471 PHE B CD2 
8050  C CE1 . PHE B 471 ? 0.2724 0.3294 0.3299 0.0109  -0.0600 0.0070  471 PHE B CE1 
8051  C CE2 . PHE B 471 ? 0.2804 0.3161 0.2823 0.0082  -0.0621 0.0057  471 PHE B CE2 
8052  C CZ  . PHE B 471 ? 0.2112 0.2518 0.2348 0.0079  -0.0541 0.0025  471 PHE B CZ  
8053  N N   . VAL B 472 ? 0.2744 0.4179 0.3200 0.0013  -0.1085 0.0349  472 VAL B N   
8054  C CA  . VAL B 472 ? 0.2295 0.3827 0.2630 -0.0006 -0.1102 0.0384  472 VAL B CA  
8055  C C   . VAL B 472 ? 0.3082 0.4771 0.3579 0.0005  -0.1162 0.0534  472 VAL B C   
8056  O O   . VAL B 472 ? 0.2707 0.4428 0.3163 0.0002  -0.1181 0.0686  472 VAL B O   
8057  C CB  . VAL B 472 ? 0.2199 0.3789 0.2353 -0.0063 -0.1114 0.0238  472 VAL B CB  
8058  C CG1 . VAL B 472 ? 0.2573 0.4375 0.2657 -0.0115 -0.1154 0.0284  472 VAL B CG1 
8059  C CG2 . VAL B 472 ? 0.3367 0.4823 0.3344 -0.0040 -0.1070 0.0148  472 VAL B CG2 
8060  N N   . ARG B 473 ? 0.4075 0.5894 0.4775 0.0011  -0.1205 0.0511  473 ARG B N   
8061  C CA  . ARG B 473 ? 0.2881 0.4875 0.3779 0.0066  -0.1284 0.0650  473 ARG B CA  
8062  C C   . ARG B 473 ? 0.2466 0.4314 0.3559 0.0161  -0.1273 0.0831  473 ARG B C   
8063  O O   . ARG B 473 ? 0.3614 0.5484 0.4737 0.0207  -0.1333 0.1024  473 ARG B O   
8064  C CB  . ARG B 473 ? 0.2531 0.4756 0.3689 0.0053  -0.1326 0.0552  473 ARG B CB  
8065  C CG  . ARG B 473 ? 0.4202 0.6718 0.5494 0.0092  -0.1449 0.0625  473 ARG B CG  
8066  C CD  . ARG B 473 ? 0.5044 0.7835 0.6719 0.0091  -0.1478 0.0521  473 ARG B CD  
8067  N NE  . ARG B 473 ? 0.5562 0.8522 0.7560 0.0253  -0.1553 0.0655  473 ARG B NE  
8068  C CZ  . ARG B 473 ? 0.5227 0.8496 0.7646 0.0295  -0.1576 0.0573  473 ARG B CZ  
8069  N NH1 . ARG B 473 ? 0.6489 0.9937 0.9074 0.0143  -0.1519 0.0368  473 ARG B NH1 
8070  N NH2 . ARG B 473 ? 0.3965 0.7376 0.6676 0.0487  -0.1651 0.0701  473 ARG B NH2 
8071  N N   . ARG B 474 ? 0.2289 0.3969 0.3528 0.0186  -0.1205 0.0784  474 ARG B N   
8072  C CA  . ARG B 474 ? 0.3089 0.4592 0.4600 0.0278  -0.1194 0.0919  474 ARG B CA  
8073  C C   . ARG B 474 ? 0.3115 0.4436 0.4472 0.0237  -0.1197 0.1055  474 ARG B C   
8074  O O   . ARG B 474 ? 0.3937 0.5106 0.5509 0.0300  -0.1223 0.1241  474 ARG B O   
8075  C CB  . ARG B 474 ? 0.3196 0.4589 0.4937 0.0304  -0.1126 0.0793  474 ARG B CB  
8076  C CG  . ARG B 474 ? 0.3892 0.5032 0.5941 0.0411  -0.1049 0.0815  474 ARG B CG  
8077  C CD  . ARG B 474 ? 0.3516 0.4808 0.6008 0.0564  -0.1106 0.0933  474 ARG B CD  
8078  N NE  . ARG B 474 ? 0.4164 0.5271 0.6682 0.0631  -0.1160 0.1159  474 ARG B NE  
8079  C CZ  . ARG B 474 ? 0.4466 0.5206 0.7200 0.0695  -0.1109 0.1215  474 ARG B CZ  
8080  N NH1 . ARG B 474 ? 0.3685 0.4189 0.6459 0.0670  -0.0936 0.0956  474 ARG B NH1 
8081  N NH2 . ARG B 474 ? 0.5255 0.5800 0.7994 0.0730  -0.1157 0.1456  474 ARG B NH2 
8082  N N   . ALA B 475 ? 0.2640 0.3972 0.3671 0.0134  -0.1167 0.0967  475 ALA B N   
8083  C CA  . ALA B 475 ? 0.2389 0.3639 0.3325 0.0061  -0.1169 0.1081  475 ALA B CA  
8084  C C   . ALA B 475 ? 0.3491 0.4814 0.4376 0.0027  -0.1221 0.1329  475 ALA B C   
8085  O O   . ALA B 475 ? 0.3994 0.5217 0.4901 -0.0043 -0.1236 0.1519  475 ALA B O   
8086  C CB  . ALA B 475 ? 0.2092 0.3416 0.2732 -0.0015 -0.1116 0.0895  475 ALA B CB  
8087  N N   . GLN B 476 ? 0.3310 0.4815 0.4127 0.0060  -0.1264 0.1348  476 GLN B N   
8088  C CA  . GLN B 476 ? 0.3492 0.5104 0.4203 0.0027  -0.1328 0.1591  476 GLN B CA  
8089  C C   . GLN B 476 ? 0.4519 0.6020 0.5498 0.0159  -0.1405 0.1828  476 GLN B C   
8090  O O   . GLN B 476 ? 0.5659 0.7172 0.6555 0.0148  -0.1462 0.2089  476 GLN B O   
8091  C CB  . GLN B 476 ? 0.2936 0.4844 0.3403 -0.0015 -0.1357 0.1475  476 GLN B CB  
8092  C CG  . GLN B 476 ? 0.2803 0.4808 0.3001 -0.0132 -0.1276 0.1291  476 GLN B CG  
8093  C CD  . GLN B 476 ? 0.2777 0.4943 0.2862 -0.0139 -0.1285 0.1055  476 GLN B CD  
8094  O OE1 . GLN B 476 ? 0.3297 0.5700 0.3226 -0.0192 -0.1333 0.1086  476 GLN B OE1 
8095  N NE2 . GLN B 476 ? 0.3137 0.5179 0.3301 -0.0101 -0.1247 0.0835  476 GLN B NE2 
8096  N N   . GLU B 477 ? 0.4871 0.6269 0.6172 0.0294  -0.1401 0.1747  477 GLU B N   
8097  C CA  . GLU B 477 ? 0.4610 0.5916 0.6213 0.0464  -0.1465 0.1933  477 GLU B CA  
8098  C C   . GLU B 477 ? 0.5621 0.6488 0.7447 0.0503  -0.1416 0.2114  477 GLU B C   
8099  O O   . GLU B 477 ? 0.4869 0.5565 0.6794 0.0595  -0.1463 0.2367  477 GLU B O   
8100  C CB  . GLU B 477 ? 0.4315 0.5764 0.6221 0.0596  -0.1466 0.1743  477 GLU B CB  
8101  C CG  . GLU B 477 ? 0.3795 0.5628 0.5535 0.0534  -0.1509 0.1547  477 GLU B CG  
8102  C CD  . GLU B 477 ? 0.4792 0.6839 0.6891 0.0647  -0.1523 0.1404  477 GLU B CD  
8103  O OE1 . GLU B 477 ? 0.5345 0.7281 0.7820 0.0808  -0.1506 0.1470  477 GLU B OE1 
8104  O OE2 . GLU B 477 ? 0.4637 0.6968 0.6679 0.0568  -0.1540 0.1213  477 GLU B OE2 
8105  N N   . MET C 1   ? 1.0419 0.5907 0.6700 -0.1591 -0.0174 0.2181  1   MET C N   
8106  C CA  . MET C 1   ? 1.0081 0.5864 0.6682 -0.1656 -0.0194 0.2050  1   MET C CA  
8107  C C   . MET C 1   ? 0.9472 0.5279 0.6096 -0.1544 -0.0352 0.1884  1   MET C C   
8108  O O   . MET C 1   ? 0.9917 0.6001 0.6622 -0.1470 -0.0362 0.1782  1   MET C O   
8109  C CB  . MET C 1   ? 0.9465 0.5194 0.6340 -0.1862 -0.0181 0.2079  1   MET C CB  
8110  C CG  . MET C 1   ? 0.8661 0.4764 0.5899 -0.1957 -0.0139 0.2014  1   MET C CG  
8111  S SD  . MET C 1   ? 1.0228 0.6513 0.7659 -0.1890 -0.0312 0.1807  1   MET C SD  
8112  C CE  . MET C 1   ? 0.8331 0.4589 0.6114 -0.2115 -0.0389 0.1792  1   MET C CE  
8113  N N   . LYS C 2   ? 0.8571 0.4073 0.5118 -0.1530 -0.0463 0.1859  2   LYS C N   
8114  C CA  . LYS C 2   ? 0.8338 0.3827 0.4891 -0.1433 -0.0602 0.1709  2   LYS C CA  
8115  C C   . LYS C 2   ? 0.8298 0.3874 0.4655 -0.1242 -0.0617 0.1683  2   LYS C C   
8116  O O   . LYS C 2   ? 0.8684 0.4059 0.4809 -0.1148 -0.0621 0.1761  2   LYS C O   
8117  C CB  . LYS C 2   ? 0.9518 0.4626 0.5995 -0.1458 -0.0693 0.1694  2   LYS C CB  
8118  C CG  . LYS C 2   ? 0.8453 0.3561 0.5037 -0.1458 -0.0823 0.1533  2   LYS C CG  
8119  C CD  . LYS C 2   ? 0.9039 0.3790 0.5460 -0.1392 -0.0898 0.1489  2   LYS C CD  
8120  C CE  . LYS C 2   ? 0.9897 0.4423 0.6364 -0.1503 -0.0866 0.1531  2   LYS C CE  
8121  N NZ  . LYS C 2   ? 0.9455 0.4032 0.6135 -0.1730 -0.0880 0.1542  2   LYS C NZ  
8122  N N   . LYS C 3   ? 0.7885 0.3759 0.4343 -0.1186 -0.0630 0.1578  3   LYS C N   
8123  C CA  . LYS C 3   ? 0.7981 0.3958 0.4291 -0.1021 -0.0662 0.1528  3   LYS C CA  
8124  C C   . LYS C 3   ? 0.9256 0.5247 0.5644 -0.0958 -0.0781 0.1383  3   LYS C C   
8125  O O   . LYS C 3   ? 0.9102 0.5227 0.5698 -0.1025 -0.0810 0.1297  3   LYS C O   
8126  C CB  . LYS C 3   ? 0.7990 0.4277 0.4324 -0.1004 -0.0569 0.1520  3   LYS C CB  
8127  C CG  . LYS C 3   ? 0.8260 0.4537 0.4321 -0.0916 -0.0516 0.1609  3   LYS C CG  
8128  C CD  . LYS C 3   ? 0.7698 0.4252 0.3763 -0.0920 -0.0405 0.1593  3   LYS C CD  
8129  C CE  . LYS C 3   ? 0.7768 0.4351 0.3551 -0.0801 -0.0410 0.1612  3   LYS C CE  
8130  N NZ  . LYS C 3   ? 0.7818 0.4609 0.3535 -0.0814 -0.0281 0.1612  3   LYS C NZ  
8131  N N   . LEU C 4   ? 0.9121 0.4976 0.5348 -0.0828 -0.0847 0.1364  4   LEU C N   
8132  C CA  . LEU C 4   ? 0.8803 0.4676 0.5078 -0.0756 -0.0942 0.1234  4   LEU C CA  
8133  C C   . LEU C 4   ? 0.8385 0.4555 0.4706 -0.0683 -0.0939 0.1158  4   LEU C C   
8134  O O   . LEU C 4   ? 0.8936 0.5205 0.5138 -0.0615 -0.0901 0.1200  4   LEU C O   
8135  C CB  . LEU C 4   ? 0.7828 0.3454 0.3940 -0.0642 -0.0996 0.1246  4   LEU C CB  
8136  C CG  . LEU C 4   ? 0.7230 0.2810 0.3373 -0.0579 -0.1078 0.1121  4   LEU C CG  
8137  C CD1 . LEU C 4   ? 0.7522 0.2854 0.3633 -0.0541 -0.1087 0.1101  4   LEU C CD1 
8138  C CD2 . LEU C 4   ? 0.7002 0.2787 0.3133 -0.0444 -0.1097 0.1065  4   LEU C CD2 
8139  N N   . PHE C 5   ? 0.7004 0.3303 0.3484 -0.0700 -0.0984 0.1047  5   PHE C N   
8140  C CA  . PHE C 5   ? 0.6747 0.3310 0.3296 -0.0645 -0.0977 0.0969  5   PHE C CA  
8141  C C   . PHE C 5   ? 0.6478 0.3016 0.2975 -0.0533 -0.1057 0.0885  5   PHE C C   
8142  O O   . PHE C 5   ? 0.7176 0.3583 0.3698 -0.0536 -0.1123 0.0833  5   PHE C O   
8143  C CB  . PHE C 5   ? 0.6583 0.3328 0.3370 -0.0734 -0.0965 0.0917  5   PHE C CB  
8144  C CG  . PHE C 5   ? 0.7534 0.4363 0.4413 -0.0841 -0.0865 0.0999  5   PHE C CG  
8145  C CD1 . PHE C 5   ? 0.8219 0.5157 0.5003 -0.0817 -0.0759 0.1057  5   PHE C CD1 
8146  C CD2 . PHE C 5   ? 0.7509 0.4303 0.4562 -0.0972 -0.0876 0.1021  5   PHE C CD2 
8147  C CE1 . PHE C 5   ? 0.8155 0.5169 0.5016 -0.0915 -0.0646 0.1139  5   PHE C CE1 
8148  C CE2 . PHE C 5   ? 0.7762 0.4650 0.4929 -0.1078 -0.0773 0.1105  5   PHE C CE2 
8149  C CZ  . PHE C 5   ? 0.8095 0.5093 0.5166 -0.1046 -0.0648 0.1166  5   PHE C CZ  
8150  N N   . LEU C 6   ? 0.6631 0.3292 0.3047 -0.0441 -0.1048 0.0870  6   LEU C N   
8151  C CA  . LEU C 6   ? 0.6184 0.2837 0.2556 -0.0334 -0.1112 0.0808  6   LEU C CA  
8152  C C   . LEU C 6   ? 0.6403 0.3280 0.2866 -0.0309 -0.1113 0.0715  6   LEU C C   
8153  O O   . LEU C 6   ? 0.7740 0.4765 0.4168 -0.0298 -0.1068 0.0717  6   LEU C O   
8154  C CB  . LEU C 6   ? 0.6309 0.2899 0.2518 -0.0248 -0.1119 0.0881  6   LEU C CB  
8155  C CG  . LEU C 6   ? 0.6682 0.3298 0.2950 -0.0140 -0.1158 0.0813  6   LEU C CG  
8156  C CD1 . LEU C 6   ? 0.6408 0.2864 0.2722 -0.0150 -0.1192 0.0759  6   LEU C CD1 
8157  C CD2 . LEU C 6   ? 0.6825 0.3423 0.3066 -0.0064 -0.1143 0.0878  6   LEU C CD2 
8158  N N   . VAL C 7   ? 0.5816 0.2698 0.2376 -0.0298 -0.1163 0.0632  7   VAL C N   
8159  C CA  . VAL C 7   ? 0.5621 0.2680 0.2273 -0.0269 -0.1169 0.0545  7   VAL C CA  
8160  C C   . VAL C 7   ? 0.6236 0.3261 0.2836 -0.0181 -0.1219 0.0501  7   VAL C C   
8161  O O   . VAL C 7   ? 0.6150 0.3031 0.2734 -0.0162 -0.1258 0.0491  7   VAL C O   
8162  C CB  . VAL C 7   ? 0.5528 0.2637 0.2347 -0.0330 -0.1185 0.0496  7   VAL C CB  
8163  C CG1 . VAL C 7   ? 0.5354 0.2633 0.2268 -0.0292 -0.1183 0.0417  7   VAL C CG1 
8164  C CG2 . VAL C 7   ? 0.5681 0.2832 0.2590 -0.0426 -0.1136 0.0549  7   VAL C CG2 
8165  N N   . PHE C 8   ? 0.7023 0.4176 0.3594 -0.0130 -0.1213 0.0475  8   PHE C N   
8166  C CA  . PHE C 8   ? 0.5720 0.2914 0.2332 -0.0057 -0.1238 0.0424  8   PHE C CA  
8167  C C   . PHE C 8   ? 0.5901 0.3194 0.2595 -0.0056 -0.1250 0.0339  8   PHE C C   
8168  O O   . PHE C 8   ? 0.5287 0.2690 0.1985 -0.0076 -0.1226 0.0310  8   PHE C O   
8169  C CB  . PHE C 8   ? 0.5948 0.3247 0.2533 -0.0010 -0.1223 0.0447  8   PHE C CB  
8170  C CG  . PHE C 8   ? 0.6898 0.4104 0.3448 0.0026  -0.1222 0.0522  8   PHE C CG  
8171  C CD1 . PHE C 8   ? 0.6969 0.4123 0.3582 0.0087  -0.1237 0.0513  8   PHE C CD1 
8172  C CD2 . PHE C 8   ? 0.7367 0.4529 0.3811 0.0003  -0.1200 0.0608  8   PHE C CD2 
8173  C CE1 . PHE C 8   ? 0.7860 0.4918 0.4440 0.0134  -0.1234 0.0583  8   PHE C CE1 
8174  C CE2 . PHE C 8   ? 0.6904 0.3972 0.3323 0.0045  -0.1199 0.0683  8   PHE C CE2 
8175  C CZ  . PHE C 8   ? 0.7420 0.4436 0.3911 0.0114  -0.1218 0.0668  8   PHE C CZ  
8176  N N   . TRP C 9   ? 0.5960 0.3214 0.2734 -0.0031 -0.1267 0.0295  9   TRP C N   
8177  C CA  . TRP C 9   ? 0.5967 0.3289 0.2824 -0.0026 -0.1277 0.0225  9   TRP C CA  
8178  C C   . TRP C 9   ? 0.5735 0.3079 0.2650 0.0029  -0.1272 0.0194  9   TRP C C   
8179  O O   . TRP C 9   ? 0.5093 0.2334 0.2008 0.0050  -0.1274 0.0198  9   TRP C O   
8180  C CB  . TRP C 9   ? 0.5807 0.3044 0.2687 -0.0065 -0.1312 0.0216  9   TRP C CB  
8181  C CG  . TRP C 9   ? 0.5565 0.2902 0.2552 -0.0074 -0.1313 0.0164  9   TRP C CG  
8182  C CD1 . TRP C 9   ? 0.4838 0.2273 0.1864 -0.0045 -0.1295 0.0114  9   TRP C CD1 
8183  C CD2 . TRP C 9   ? 0.6421 0.3765 0.3510 -0.0113 -0.1335 0.0158  9   TRP C CD2 
8184  N NE1 . TRP C 9   ? 0.4779 0.2268 0.1922 -0.0054 -0.1293 0.0079  9   TRP C NE1 
8185  C CE2 . TRP C 9   ? 0.5493 0.2942 0.2686 -0.0092 -0.1322 0.0110  9   TRP C CE2 
8186  C CE3 . TRP C 9   ? 0.6293 0.3562 0.3401 -0.0167 -0.1372 0.0189  9   TRP C CE3 
8187  C CZ2 . TRP C 9   ? 0.5179 0.2673 0.2506 -0.0110 -0.1344 0.0103  9   TRP C CZ2 
8188  C CZ3 . TRP C 9   ? 0.6008 0.3339 0.3251 -0.0197 -0.1405 0.0178  9   TRP C CZ3 
8189  C CH2 . TRP C 9   ? 0.5714 0.3162 0.3071 -0.0162 -0.1392 0.0141  9   TRP C CH2 
8190  N N   . TRP C 10  ? 0.5029 0.2496 0.1974 0.0047  -0.1268 0.0163  10  TRP C N   
8191  C CA  . TRP C 10  ? 0.5685 0.3184 0.2685 0.0087  -0.1275 0.0140  10  TRP C CA  
8192  C C   . TRP C 10  ? 0.4752 0.2254 0.1808 0.0078  -0.1279 0.0082  10  TRP C C   
8193  O O   . TRP C 10  ? 0.4723 0.2274 0.1784 0.0053  -0.1281 0.0043  10  TRP C O   
8194  C CB  . TRP C 10  ? 0.5641 0.3264 0.2637 0.0102  -0.1290 0.0144  10  TRP C CB  
8195  C CG  . TRP C 10  ? 0.5413 0.3041 0.2346 0.0115  -0.1291 0.0212  10  TRP C CG  
8196  C CD1 . TRP C 10  ? 0.6679 0.4357 0.3533 0.0089  -0.1283 0.0232  10  TRP C CD1 
8197  C CD2 . TRP C 10  ? 0.5523 0.3087 0.2448 0.0163  -0.1298 0.0275  10  TRP C CD2 
8198  N NE1 . TRP C 10  ? 0.6532 0.4185 0.3336 0.0114  -0.1287 0.0310  10  TRP C NE1 
8199  C CE2 . TRP C 10  ? 0.6408 0.3990 0.3263 0.0163  -0.1298 0.0336  10  TRP C CE2 
8200  C CE3 . TRP C 10  ? 0.5374 0.2853 0.2327 0.0213  -0.1299 0.0288  10  TRP C CE3 
8201  C CZ2 . TRP C 10  ? 0.5217 0.2737 0.2051 0.0213  -0.1305 0.0412  10  TRP C CZ2 
8202  C CZ3 . TRP C 10  ? 0.6160 0.3574 0.3085 0.0268  -0.1301 0.0357  10  TRP C CZ3 
8203  C CH2 . TRP C 10  ? 0.5213 0.2649 0.2090 0.0269  -0.1306 0.0419  10  TRP C CH2 
8204  N N   . HIS C 11  ? 0.4746 0.2178 0.1821 0.0102  -0.1280 0.0079  11  HIS C N   
8205  C CA  . HIS C 11  ? 0.4680 0.2079 0.1787 0.0095  -0.1284 0.0041  11  HIS C CA  
8206  C C   . HIS C 11  ? 0.4659 0.2116 0.1794 0.0107  -0.1297 0.0014  11  HIS C C   
8207  O O   . HIS C 11  ? 0.4686 0.2124 0.1808 0.0138  -0.1302 0.0037  11  HIS C O   
8208  C CB  . HIS C 11  ? 0.5957 0.3220 0.3027 0.0106  -0.1277 0.0058  11  HIS C CB  
8209  C CG  . HIS C 11  ? 0.5018 0.2232 0.2093 0.0110  -0.1280 0.0036  11  HIS C CG  
8210  N ND1 . HIS C 11  ? 0.4686 0.1914 0.1800 0.0089  -0.1301 0.0012  11  HIS C ND1 
8211  C CD2 . HIS C 11  ? 0.4764 0.1896 0.1788 0.0136  -0.1267 0.0044  11  HIS C CD2 
8212  C CE1 . HIS C 11  ? 0.4968 0.2123 0.2058 0.0099  -0.1304 0.0008  11  HIS C CE1 
8213  N NE2 . HIS C 11  ? 0.5170 0.2265 0.2198 0.0124  -0.1279 0.0028  11  HIS C NE2 
8214  N N   . MET C 12  ? 0.5120 0.2633 0.2280 0.0083  -0.1310 -0.0037 12  MET C N   
8215  C CA  . MET C 12  ? 0.5867 0.3433 0.3070 0.0073  -0.1324 -0.0077 12  MET C CA  
8216  C C   . MET C 12  ? 0.5127 0.2624 0.2387 0.0067  -0.1303 -0.0101 12  MET C C   
8217  O O   . MET C 12  ? 0.4620 0.2089 0.1895 0.0056  -0.1297 -0.0132 12  MET C O   
8218  C CB  . MET C 12  ? 0.4909 0.2568 0.2101 0.0044  -0.1339 -0.0129 12  MET C CB  
8219  C CG  . MET C 12  ? 0.4847 0.2577 0.1990 0.0048  -0.1336 -0.0094 12  MET C CG  
8220  S SD  . MET C 12  ? 0.6712 0.4485 0.3867 0.0084  -0.1363 -0.0022 12  MET C SD  
8221  C CE  . MET C 12  ? 0.4782 0.2699 0.1903 0.0063  -0.1396 -0.0032 12  MET C CE  
8222  N N   . HIS C 13  ? 0.5066 0.2533 0.2361 0.0077  -0.1286 -0.0080 13  HIS C N   
8223  C CA  . HIS C 13  ? 0.4639 0.2022 0.1966 0.0071  -0.1261 -0.0087 13  HIS C CA  
8224  C C   . HIS C 13  ? 0.4652 0.2058 0.2050 0.0067  -0.1231 -0.0072 13  HIS C C   
8225  O O   . HIS C 13  ? 0.4653 0.2104 0.2059 0.0092  -0.1220 -0.0036 13  HIS C O   
8226  C CB  . HIS C 13  ? 0.4675 0.1930 0.1915 0.0093  -0.1258 -0.0048 13  HIS C CB  
8227  C CG  . HIS C 13  ? 0.4731 0.1884 0.1962 0.0097  -0.1231 -0.0029 13  HIS C CG  
8228  N ND1 . HIS C 13  ? 0.4746 0.1874 0.2041 0.0079  -0.1224 -0.0051 13  HIS C ND1 
8229  C CD2 . HIS C 13  ? 0.4808 0.1859 0.1954 0.0118  -0.1200 0.0013  13  HIS C CD2 
8230  C CE1 . HIS C 13  ? 0.5043 0.2063 0.2295 0.0086  -0.1195 -0.0014 13  HIS C CE1 
8231  N NE2 . HIS C 13  ? 0.4867 0.1841 0.2019 0.0109  -0.1178 0.0023  13  HIS C NE2 
8232  N N   . GLN C 14  ? 0.4674 0.2050 0.2140 0.0038  -0.1211 -0.0094 14  GLN C N   
8233  C CA  . GLN C 14  ? 0.4701 0.2094 0.2255 0.0022  -0.1169 -0.0075 14  GLN C CA  
8234  C C   . GLN C 14  ? 0.5282 0.2548 0.2836 0.0004  -0.1138 -0.0074 14  GLN C C   
8235  O O   . GLN C 14  ? 0.6014 0.3248 0.3584 -0.0016 -0.1161 -0.0120 14  GLN C O   
8236  C CB  . GLN C 14  ? 0.4681 0.2223 0.2365 -0.0023 -0.1196 -0.0112 14  GLN C CB  
8237  C CG  . GLN C 14  ? 0.5190 0.2823 0.2997 -0.0025 -0.1160 -0.0070 14  GLN C CG  
8238  C CD  . GLN C 14  ? 0.5584 0.3326 0.3398 0.0024  -0.1179 -0.0033 14  GLN C CD  
8239  O OE1 . GLN C 14  ? 0.5218 0.3059 0.3029 0.0018  -0.1247 -0.0054 14  GLN C OE1 
8240  N NE2 . GLN C 14  ? 0.4933 0.2643 0.2743 0.0077  -0.1114 0.0027  14  GLN C NE2 
8241  N N   . PRO C 15  ? 0.4833 0.2014 0.2361 0.0015  -0.1080 -0.0021 15  PRO C N   
8242  C CA  . PRO C 15  ? 0.4926 0.1966 0.2429 0.0002  -0.1054 -0.0003 15  PRO C CA  
8243  C C   . PRO C 15  ? 0.5364 0.2425 0.3010 -0.0059 -0.1040 -0.0038 15  PRO C C   
8244  O O   . PRO C 15  ? 0.5713 0.2908 0.3473 -0.0098 -0.1062 -0.0085 15  PRO C O   
8245  C CB  . PRO C 15  ? 0.5022 0.1973 0.2434 0.0027  -0.0984 0.0067  15  PRO C CB  
8246  C CG  . PRO C 15  ? 0.4972 0.2053 0.2451 0.0039  -0.0953 0.0074  15  PRO C CG  
8247  C CD  . PRO C 15  ? 0.4857 0.2057 0.2366 0.0047  -0.1027 0.0030  15  PRO C CD  
8248  N N   . LEU C 16  ? 0.5058 0.1977 0.2691 -0.0071 -0.1012 -0.0015 16  LEU C N   
8249  C CA  . LEU C 16  ? 0.5121 0.2012 0.2878 -0.0134 -0.0998 -0.0051 16  LEU C CA  
8250  C C   . LEU C 16  ? 0.5171 0.2101 0.3032 -0.0185 -0.0928 -0.0010 16  LEU C C   
8251  O O   . LEU C 16  ? 0.5270 0.2096 0.3068 -0.0172 -0.0860 0.0066  16  LEU C O   
8252  C CB  . LEU C 16  ? 0.5235 0.1941 0.2942 -0.0118 -0.0996 -0.0035 16  LEU C CB  
8253  C CG  . LEU C 16  ? 0.5318 0.1961 0.3139 -0.0174 -0.0993 -0.0094 16  LEU C CG  
8254  C CD1 . LEU C 16  ? 0.5240 0.2005 0.3117 -0.0196 -0.1045 -0.0201 16  LEU C CD1 
8255  C CD2 . LEU C 16  ? 0.5441 0.1894 0.3216 -0.0134 -0.0993 -0.0068 16  LEU C CD2 
8256  N N   . TYR C 17  ? 0.5122 0.2206 0.3139 -0.0244 -0.0946 -0.0058 17  TYR C N   
8257  C CA  . TYR C 17  ? 0.5166 0.2325 0.3343 -0.0306 -0.0885 -0.0024 17  TYR C CA  
8258  C C   . TYR C 17  ? 0.5288 0.2358 0.3577 -0.0398 -0.0871 -0.0052 17  TYR C C   
8259  O O   . TYR C 17  ? 0.5336 0.2478 0.3793 -0.0470 -0.0824 -0.0028 17  TYR C O   
8260  C CB  . TYR C 17  ? 0.5059 0.2460 0.3376 -0.0324 -0.0926 -0.0049 17  TYR C CB  
8261  C CG  . TYR C 17  ? 0.5015 0.2491 0.3236 -0.0234 -0.0935 -0.0018 17  TYR C CG  
8262  C CD1 . TYR C 17  ? 0.4995 0.2426 0.3147 -0.0175 -0.0848 0.0059  17  TYR C CD1 
8263  C CD2 . TYR C 17  ? 0.5456 0.3030 0.3639 -0.0211 -0.1023 -0.0068 17  TYR C CD2 
8264  C CE1 . TYR C 17  ? 0.4940 0.2408 0.2996 -0.0095 -0.0854 0.0080  17  TYR C CE1 
8265  C CE2 . TYR C 17  ? 0.5081 0.2701 0.3179 -0.0133 -0.1029 -0.0035 17  TYR C CE2 
8266  C CZ  . TYR C 17  ? 0.5144 0.2705 0.3183 -0.0076 -0.0946 0.0035  17  TYR C CZ  
8267  O OH  . TYR C 17  ? 0.5300 0.2876 0.3246 0.0000  -0.0949 0.0060  17  TYR C OH  
8268  N N   . ARG C 18  ? 0.5353 0.2268 0.3569 -0.0395 -0.0906 -0.0101 18  ARG C N   
8269  C CA  . ARG C 18  ? 0.5501 0.2289 0.3805 -0.0477 -0.0893 -0.0137 18  ARG C CA  
8270  C C   . ARG C 18  ? 0.5650 0.2235 0.3901 -0.0467 -0.0808 -0.0040 18  ARG C C   
8271  O O   . ARG C 18  ? 0.5692 0.2127 0.3793 -0.0390 -0.0811 -0.0004 18  ARG C O   
8272  C CB  . ARG C 18  ? 0.5530 0.2233 0.3778 -0.0465 -0.0957 -0.0238 18  ARG C CB  
8273  C CG  . ARG C 18  ? 0.5662 0.2318 0.4024 -0.0572 -0.0978 -0.0331 18  ARG C CG  
8274  C CD  . ARG C 18  ? 0.5780 0.2241 0.4063 -0.0542 -0.0991 -0.0406 18  ARG C CD  
8275  N NE  . ARG C 18  ? 0.6967 0.3189 0.5276 -0.0563 -0.0931 -0.0363 18  ARG C NE  
8276  C CZ  . ARG C 18  ? 0.6153 0.2180 0.4469 -0.0586 -0.0928 -0.0439 18  ARG C CZ  
8277  N NH1 . ARG C 18  ? 0.6181 0.2218 0.4465 -0.0592 -0.0975 -0.0571 18  ARG C NH1 
8278  N NH2 . ARG C 18  ? 0.6340 0.2139 0.4682 -0.0600 -0.0870 -0.0379 18  ARG C NH2 
8279  N N   . GLU C 19  ? 0.5745 0.2333 0.4124 -0.0547 -0.0736 0.0009  19  GLU C N   
8280  C CA  . GLU C 19  ? 0.5925 0.2310 0.4242 -0.0548 -0.0645 0.0112  19  GLU C CA  
8281  C C   . GLU C 19  ? 0.6081 0.2225 0.4356 -0.0552 -0.0668 0.0085  19  GLU C C   
8282  O O   . GLU C 19  ? 0.6108 0.2241 0.4484 -0.0612 -0.0716 -0.0017 19  GLU C O   
8283  C CB  . GLU C 19  ? 0.6607 0.3057 0.5104 -0.0649 -0.0553 0.0165  19  GLU C CB  
8284  C CG  . GLU C 19  ? 0.7928 0.4234 0.6323 -0.0631 -0.0430 0.0300  19  GLU C CG  
8285  C CD  . GLU C 19  ? 0.9119 0.5205 0.7565 -0.0713 -0.0375 0.0341  19  GLU C CD  
8286  O OE1 . GLU C 19  ? 0.8932 0.4911 0.7421 -0.0746 -0.0444 0.0261  19  GLU C OE1 
8287  O OE2 . GLU C 19  ? 0.9301 0.5305 0.7734 -0.0742 -0.0256 0.0452  19  GLU C OE2 
8288  N N   . PRO C 20  ? 0.6299 0.2236 0.4417 -0.0486 -0.0636 0.0174  20  PRO C N   
8289  C CA  . PRO C 20  ? 0.6862 0.2573 0.4948 -0.0462 -0.0664 0.0155  20  PRO C CA  
8290  C C   . PRO C 20  ? 0.7713 0.3239 0.5907 -0.0559 -0.0604 0.0172  20  PRO C C   
8291  O O   . PRO C 20  ? 0.8135 0.3484 0.6347 -0.0554 -0.0629 0.0121  20  PRO C O   
8292  C CB  . PRO C 20  ? 0.6425 0.2007 0.4306 -0.0351 -0.0668 0.0263  20  PRO C CB  
8293  C CG  . PRO C 20  ? 0.6296 0.2038 0.4079 -0.0319 -0.0653 0.0308  20  PRO C CG  
8294  C CD  . PRO C 20  ? 0.6466 0.2369 0.4407 -0.0414 -0.0590 0.0289  20  PRO C CD  
8295  N N   . TYR C 21  ? 0.7126 0.2676 0.5400 -0.0646 -0.0517 0.0244  21  TYR C N   
8296  C CA  . TYR C 21  ? 0.7526 0.2893 0.5914 -0.0754 -0.0452 0.0271  21  TYR C CA  
8297  C C   . TYR C 21  ? 0.7448 0.2950 0.6073 -0.0895 -0.0470 0.0162  21  TYR C C   
8298  O O   . TYR C 21  ? 0.8535 0.3887 0.7279 -0.1006 -0.0427 0.0164  21  TYR C O   
8299  C CB  . TYR C 21  ? 0.7638 0.2927 0.5971 -0.0775 -0.0330 0.0430  21  TYR C CB  
8300  C CG  . TYR C 21  ? 0.7508 0.2579 0.5588 -0.0660 -0.0318 0.0548  21  TYR C CG  
8301  C CD1 . TYR C 21  ? 0.7962 0.2739 0.5992 -0.0643 -0.0320 0.0591  21  TYR C CD1 
8302  C CD2 . TYR C 21  ? 0.7130 0.2281 0.5018 -0.0567 -0.0312 0.0616  21  TYR C CD2 
8303  C CE1 . TYR C 21  ? 0.7602 0.2192 0.5406 -0.0535 -0.0328 0.0709  21  TYR C CE1 
8304  C CE2 . TYR C 21  ? 0.7326 0.2283 0.4970 -0.0471 -0.0322 0.0722  21  TYR C CE2 
8305  C CZ  . TYR C 21  ? 0.7519 0.2206 0.5127 -0.0454 -0.0336 0.0773  21  TYR C CZ  
8306  O OH  . TYR C 21  ? 0.8145 0.2668 0.5526 -0.0354 -0.0362 0.0887  21  TYR C OH  
8307  N N   . THR C 22  ? 0.7181 0.2957 0.5875 -0.0899 -0.0539 0.0072  22  THR C N   
8308  C CA  . THR C 22  ? 0.6634 0.2560 0.5540 -0.1032 -0.0586 -0.0035 22  THR C CA  
8309  C C   . THR C 22  ? 0.6775 0.2828 0.5653 -0.1007 -0.0707 -0.0181 22  THR C C   
8310  O O   . THR C 22  ? 0.6733 0.2831 0.5734 -0.1118 -0.0766 -0.0291 22  THR C O   
8311  C CB  . THR C 22  ? 0.6740 0.2935 0.5824 -0.1098 -0.0536 0.0027  22  THR C CB  
8312  O OG1 . THR C 22  ? 0.7725 0.4092 0.6699 -0.0977 -0.0536 0.0072  22  THR C OG1 
8313  C CG2 . THR C 22  ? 0.6727 0.2801 0.5888 -0.1168 -0.0401 0.0156  22  THR C CG2 
8314  N N   . GLY C 23  ? 0.7086 0.3189 0.5797 -0.0873 -0.0747 -0.0186 23  GLY C N   
8315  C CA  . GLY C 23  ? 0.6781 0.3017 0.5453 -0.0848 -0.0847 -0.0311 23  GLY C CA  
8316  C C   . GLY C 23  ? 0.6291 0.2837 0.5070 -0.0890 -0.0898 -0.0333 23  GLY C C   
8317  O O   . GLY C 23  ? 0.6336 0.2994 0.5087 -0.0892 -0.0987 -0.0436 23  GLY C O   
8318  N N   . GLU C 24  ? 0.5979 0.2665 0.4878 -0.0916 -0.0839 -0.0234 24  GLU C N   
8319  C CA  . GLU C 24  ? 0.6079 0.3070 0.5125 -0.0949 -0.0882 -0.0240 24  GLU C CA  
8320  C C   . GLU C 24  ? 0.7161 0.4281 0.6083 -0.0816 -0.0883 -0.0189 24  GLU C C   
8321  O O   . GLU C 24  ? 0.7775 0.4783 0.6558 -0.0726 -0.0812 -0.0106 24  GLU C O   
8322  C CB  . GLU C 24  ? 0.5934 0.3024 0.5216 -0.1047 -0.0803 -0.0159 24  GLU C CB  
8323  C CG  . GLU C 24  ? 0.7773 0.4755 0.7213 -0.1205 -0.0811 -0.0212 24  GLU C CG  
8324  C CD  . GLU C 24  ? 0.9634 0.6749 0.9347 -0.1314 -0.0729 -0.0127 24  GLU C CD  
8325  O OE1 . GLU C 24  ? 0.9847 0.7116 0.9608 -0.1251 -0.0646 -0.0021 24  GLU C OE1 
8326  O OE2 . GLU C 24  ? 1.1415 0.8478 1.1298 -0.1465 -0.0742 -0.0167 24  GLU C OE2 
8327  N N   . TYR C 25  ? 0.6656 0.3998 0.5617 -0.0808 -0.0972 -0.0240 25  TYR C N   
8328  C CA  . TYR C 25  ? 0.5342 0.2815 0.4213 -0.0694 -0.0976 -0.0193 25  TYR C CA  
8329  C C   . TYR C 25  ? 0.5293 0.2959 0.4349 -0.0701 -0.0911 -0.0103 25  TYR C C   
8330  O O   . TYR C 25  ? 0.6582 0.4461 0.5858 -0.0775 -0.0959 -0.0120 25  TYR C O   
8331  C CB  . TYR C 25  ? 0.5794 0.3395 0.4606 -0.0676 -0.1096 -0.0279 25  TYR C CB  
8332  C CG  . TYR C 25  ? 0.5416 0.2846 0.4016 -0.0629 -0.1133 -0.0352 25  TYR C CG  
8333  C CD1 . TYR C 25  ? 0.5608 0.2875 0.4191 -0.0694 -0.1150 -0.0439 25  TYR C CD1 
8334  C CD2 . TYR C 25  ? 0.5452 0.2885 0.3886 -0.0520 -0.1144 -0.0335 25  TYR C CD2 
8335  C CE1 . TYR C 25  ? 0.5471 0.2595 0.3884 -0.0640 -0.1167 -0.0505 25  TYR C CE1 
8336  C CE2 . TYR C 25  ? 0.5434 0.2740 0.3712 -0.0478 -0.1167 -0.0395 25  TYR C CE2 
8337  C CZ  . TYR C 25  ? 0.5345 0.2503 0.3618 -0.0532 -0.1174 -0.0479 25  TYR C CZ  
8338  O OH  . TYR C 25  ? 0.5562 0.2604 0.3702 -0.0479 -0.1181 -0.0538 25  TYR C OH  
8339  N N   . LEU C 26  ? 0.5289 0.2884 0.4258 -0.0621 -0.0803 -0.0008 26  LEU C N   
8340  C CA  . LEU C 26  ? 0.5311 0.3057 0.4441 -0.0615 -0.0705 0.0082  26  LEU C CA  
8341  C C   . LEU C 26  ? 0.5140 0.3089 0.4291 -0.0526 -0.0733 0.0098  26  LEU C C   
8342  O O   . LEU C 26  ? 0.5133 0.3226 0.4436 -0.0503 -0.0647 0.0169  26  LEU C O   
8343  C CB  . LEU C 26  ? 0.5860 0.3413 0.4852 -0.0570 -0.0561 0.0176  26  LEU C CB  
8344  C CG  . LEU C 26  ? 0.5576 0.2902 0.4541 -0.0644 -0.0500 0.0201  26  LEU C CG  
8345  C CD1 . LEU C 26  ? 0.5645 0.3085 0.4913 -0.0787 -0.0485 0.0193  26  LEU C CD1 
8346  C CD2 . LEU C 26  ? 0.5636 0.2740 0.4405 -0.0626 -0.0579 0.0141  26  LEU C CD2 
8347  N N   . LEU C 27  ? 0.5533 0.3489 0.4541 -0.0472 -0.0840 0.0040  27  LEU C N   
8348  C CA  . LEU C 27  ? 0.5825 0.3950 0.4842 -0.0389 -0.0878 0.0056  27  LEU C CA  
8349  C C   . LEU C 27  ? 0.6177 0.4370 0.5150 -0.0410 -0.1028 -0.0030 27  LEU C C   
8350  O O   . LEU C 27  ? 0.6911 0.4941 0.5706 -0.0418 -0.1069 -0.0091 27  LEU C O   
8351  C CB  . LEU C 27  ? 0.5172 0.3164 0.3958 -0.0268 -0.0814 0.0102  27  LEU C CB  
8352  C CG  . LEU C 27  ? 0.5003 0.2947 0.3793 -0.0222 -0.0660 0.0189  27  LEU C CG  
8353  C CD1 . LEU C 27  ? 0.5040 0.2782 0.3530 -0.0123 -0.0621 0.0210  27  LEU C CD1 
8354  C CD2 . LEU C 27  ? 0.4968 0.3159 0.4008 -0.0196 -0.0615 0.0238  27  LEU C CD2 
8355  N N   . PRO C 28  ? 0.5189 0.3619 0.4315 -0.0415 -0.1109 -0.0031 28  PRO C N   
8356  C CA  . PRO C 28  ? 0.5569 0.4062 0.4630 -0.0445 -0.1254 -0.0109 28  PRO C CA  
8357  C C   . PRO C 28  ? 0.5880 0.4341 0.4729 -0.0342 -0.1292 -0.0105 28  PRO C C   
8358  O O   . PRO C 28  ? 0.5789 0.4335 0.4588 -0.0356 -0.1405 -0.0150 28  PRO C O   
8359  C CB  . PRO C 28  ? 0.4822 0.3599 0.4163 -0.0501 -0.1328 -0.0093 28  PRO C CB  
8360  C CG  . PRO C 28  ? 0.4769 0.3655 0.4267 -0.0421 -0.1219 0.0015  28  PRO C CG  
8361  C CD  . PRO C 28  ? 0.4797 0.3451 0.4164 -0.0386 -0.1068 0.0047  28  PRO C CD  
8362  N N   . TRP C 29  ? 0.5001 0.3332 0.3710 -0.0247 -0.1205 -0.0053 29  TRP C N   
8363  C CA  . TRP C 29  ? 0.5128 0.3442 0.3673 -0.0156 -0.1235 -0.0035 29  TRP C CA  
8364  C C   . TRP C 29  ? 0.4952 0.3182 0.3309 -0.0174 -0.1313 -0.0108 29  TRP C C   
8365  O O   . TRP C 29  ? 0.5439 0.3725 0.3709 -0.0135 -0.1376 -0.0105 29  TRP C O   
8366  C CB  . TRP C 29  ? 0.5289 0.3450 0.3707 -0.0070 -0.1129 0.0022  29  TRP C CB  
8367  C CG  . TRP C 29  ? 0.5684 0.3922 0.4253 -0.0029 -0.1033 0.0096  29  TRP C CG  
8368  C CD1 . TRP C 29  ? 0.5372 0.3513 0.3954 -0.0031 -0.0913 0.0131  29  TRP C CD1 
8369  C CD2 . TRP C 29  ? 0.6618 0.5046 0.5349 0.0027  -0.1039 0.0148  29  TRP C CD2 
8370  N NE1 . TRP C 29  ? 0.5491 0.3752 0.4231 0.0019  -0.0830 0.0196  29  TRP C NE1 
8371  C CE2 . TRP C 29  ? 0.6788 0.5232 0.5638 0.0060  -0.0906 0.0208  29  TRP C CE2 
8372  C CE3 . TRP C 29  ? 0.7137 0.5721 0.5919 0.0059  -0.1140 0.0158  29  TRP C CE3 
8373  C CZ2 . TRP C 29  ? 0.7454 0.6074 0.6500 0.0130  -0.0866 0.0272  29  TRP C CZ2 
8374  C CZ3 . TRP C 29  ? 0.6836 0.5591 0.5811 0.0128  -0.1116 0.0228  29  TRP C CZ3 
8375  C CH2 . TRP C 29  ? 0.6131 0.4908 0.5249 0.0166  -0.0977 0.0282  29  TRP C CH2 
8376  N N   . THR C 30  ? 0.5477 0.3567 0.3771 -0.0228 -0.1301 -0.0170 30  THR C N   
8377  C CA  . THR C 30  ? 0.5926 0.3942 0.4059 -0.0239 -0.1356 -0.0244 30  THR C CA  
8378  C C   . THR C 30  ? 0.5306 0.3464 0.3463 -0.0295 -0.1461 -0.0300 30  THR C C   
8379  O O   . THR C 30  ? 0.5951 0.4122 0.3962 -0.0271 -0.1511 -0.0322 30  THR C O   
8380  C CB  . THR C 30  ? 0.5726 0.3565 0.3820 -0.0278 -0.1316 -0.0297 30  THR C CB  
8381  O OG1 . THR C 30  ? 0.5569 0.3309 0.3699 -0.0256 -0.1228 -0.0233 30  THR C OG1 
8382  C CG2 . THR C 30  ? 0.5356 0.3085 0.3273 -0.0237 -0.1321 -0.0336 30  THR C CG2 
8383  N N   . PHE C 31  ? 0.5474 0.3739 0.3806 -0.0377 -0.1498 -0.0322 31  PHE C N   
8384  C CA  . PHE C 31  ? 0.5145 0.3548 0.3493 -0.0444 -0.1619 -0.0380 31  PHE C CA  
8385  C C   . PHE C 31  ? 0.5011 0.3586 0.3355 -0.0382 -0.1686 -0.0313 31  PHE C C   
8386  O O   . PHE C 31  ? 0.4978 0.3585 0.3172 -0.0385 -0.1770 -0.0347 31  PHE C O   
8387  C CB  . PHE C 31  ? 0.5012 0.3507 0.3587 -0.0553 -0.1650 -0.0406 31  PHE C CB  
8388  C CG  . PHE C 31  ? 0.6450 0.5117 0.5069 -0.0632 -0.1795 -0.0456 31  PHE C CG  
8389  C CD1 . PHE C 31  ? 0.6136 0.4714 0.4568 -0.0695 -0.1868 -0.0572 31  PHE C CD1 
8390  C CD2 . PHE C 31  ? 0.6067 0.4985 0.4914 -0.0640 -0.1860 -0.0386 31  PHE C CD2 
8391  C CE1 . PHE C 31  ? 0.5547 0.4270 0.3982 -0.0774 -0.2015 -0.0623 31  PHE C CE1 
8392  C CE2 . PHE C 31  ? 0.5202 0.4291 0.4091 -0.0716 -0.2017 -0.0426 31  PHE C CE2 
8393  C CZ  . PHE C 31  ? 0.5805 0.4789 0.4470 -0.0788 -0.2100 -0.0546 31  PHE C CZ  
8394  N N   . PHE C 32  ? 0.4815 0.3488 0.3311 -0.0319 -0.1642 -0.0213 32  PHE C N   
8395  C CA  . PHE C 32  ? 0.5431 0.4277 0.3973 -0.0256 -0.1707 -0.0140 32  PHE C CA  
8396  C C   . PHE C 32  ? 0.5383 0.4129 0.3681 -0.0174 -0.1707 -0.0118 32  PHE C C   
8397  O O   . PHE C 32  ? 0.5813 0.4653 0.4040 -0.0157 -0.1801 -0.0099 32  PHE C O   
8398  C CB  . PHE C 32  ? 0.5784 0.4734 0.4554 -0.0197 -0.1633 -0.0043 32  PHE C CB  
8399  C CG  . PHE C 32  ? 0.4744 0.3883 0.3810 -0.0278 -0.1660 -0.0040 32  PHE C CG  
8400  C CD1 . PHE C 32  ? 0.6457 0.5738 0.5590 -0.0377 -0.1803 -0.0096 32  PHE C CD1 
8401  C CD2 . PHE C 32  ? 0.4701 0.3867 0.3969 -0.0265 -0.1542 0.0015  32  PHE C CD2 
8402  C CE1 . PHE C 32  ? 0.7693 0.7158 0.7123 -0.0468 -0.1839 -0.0095 32  PHE C CE1 
8403  C CE2 . PHE C 32  ? 0.6745 0.6099 0.6315 -0.0350 -0.1559 0.0023  32  PHE C CE2 
8404  C CZ  . PHE C 32  ? 0.7553 0.7062 0.7218 -0.0456 -0.1713 -0.0032 32  PHE C CZ  
8405  N N   . HIS C 33  ? 0.5209 0.3766 0.3378 -0.0127 -0.1607 -0.0114 33  HIS C N   
8406  C CA  . HIS C 33  ? 0.5353 0.3819 0.3318 -0.0061 -0.1602 -0.0089 33  HIS C CA  
8407  C C   . HIS C 33  ? 0.5562 0.3978 0.3338 -0.0107 -0.1653 -0.0165 33  HIS C C   
8408  O O   . HIS C 33  ? 0.6581 0.4980 0.4203 -0.0069 -0.1675 -0.0139 33  HIS C O   
8409  C CB  . HIS C 33  ? 0.6201 0.4492 0.4098 -0.0007 -0.1494 -0.0062 33  HIS C CB  
8410  C CG  . HIS C 33  ? 0.5162 0.3470 0.3154 0.0067  -0.1436 0.0022  33  HIS C CG  
8411  N ND1 . HIS C 33  ? 0.5778 0.4067 0.3895 0.0067  -0.1355 0.0038  33  HIS C ND1 
8412  C CD2 . HIS C 33  ? 0.4928 0.3257 0.2901 0.0148  -0.1437 0.0094  33  HIS C CD2 
8413  C CE1 . HIS C 33  ? 0.5353 0.3654 0.3518 0.0148  -0.1301 0.0109  33  HIS C CE1 
8414  N NE2 . HIS C 33  ? 0.5005 0.3324 0.3090 0.0201  -0.1352 0.0143  33  HIS C NE2 
8415  N N   . ALA C 34  ? 0.4872 0.3253 0.2652 -0.0188 -0.1664 -0.0259 34  ALA C N   
8416  C CA  . ALA C 34  ? 0.5174 0.3505 0.2768 -0.0229 -0.1701 -0.0344 34  ALA C CA  
8417  C C   . ALA C 34  ? 0.5459 0.3934 0.2994 -0.0256 -0.1820 -0.0344 34  ALA C C   
8418  O O   . ALA C 34  ? 0.6491 0.4958 0.3848 -0.0236 -0.1827 -0.0343 34  ALA C O   
8419  C CB  . ALA C 34  ? 0.6124 0.4356 0.3739 -0.0303 -0.1676 -0.0449 34  ALA C CB  
8420  N N   . VAL C 35  ? 0.5144 0.3772 0.2855 -0.0301 -0.1900 -0.0336 35  VAL C N   
8421  C CA  . VAL C 35  ? 0.5585 0.4370 0.3256 -0.0329 -0.2038 -0.0327 35  VAL C CA  
8422  C C   . VAL C 35  ? 0.5950 0.4826 0.3615 -0.0232 -0.2065 -0.0201 35  VAL C C   
8423  O O   . VAL C 35  ? 0.7482 0.6478 0.5085 -0.0234 -0.2159 -0.0173 35  VAL C O   
8424  C CB  . VAL C 35  ? 0.5306 0.4253 0.3209 -0.0416 -0.2129 -0.0353 35  VAL C CB  
8425  C CG1 . VAL C 35  ? 0.5369 0.4192 0.3277 -0.0517 -0.2097 -0.0478 35  VAL C CG1 
8426  C CG2 . VAL C 35  ? 0.5520 0.4596 0.3720 -0.0364 -0.2090 -0.0248 35  VAL C CG2 
8427  N N   . LYS C 36  ? 0.5436 0.4255 0.3175 -0.0146 -0.1965 -0.0122 36  LYS C N   
8428  C CA  . LYS C 36  ? 0.5515 0.4381 0.3251 -0.0047 -0.1975 -0.0004 36  LYS C CA  
8429  C C   . LYS C 36  ? 0.6785 0.5478 0.4302 0.0008  -0.1902 0.0023  36  LYS C C   
8430  O O   . LYS C 36  ? 0.7595 0.6315 0.5039 0.0063  -0.1923 0.0102  36  LYS C O   
8431  C CB  . LYS C 36  ? 0.4954 0.3886 0.2948 0.0015  -0.1917 0.0072  36  LYS C CB  
8432  C CG  . LYS C 36  ? 0.5297 0.4282 0.3325 0.0125  -0.1930 0.0194  36  LYS C CG  
8433  C CD  . LYS C 36  ? 0.5697 0.4788 0.4009 0.0186  -0.1877 0.0260  36  LYS C CD  
8434  C CE  . LYS C 36  ? 0.6902 0.5803 0.5183 0.0246  -0.1723 0.0272  36  LYS C CE  
8435  N NZ  . LYS C 36  ? 0.6283 0.4974 0.4295 0.0272  -0.1688 0.0269  36  LYS C NZ  
8436  N N   . ASP C 37  ? 0.6044 0.4577 0.3493 -0.0006 -0.1803 -0.0033 37  ASP C N   
8437  C CA  . ASP C 37  ? 0.5652 0.4054 0.2963 0.0040  -0.1721 0.0001  37  ASP C CA  
8438  C C   . ASP C 37  ? 0.6197 0.4515 0.3411 -0.0004 -0.1640 -0.0079 37  ASP C C   
8439  O O   . ASP C 37  ? 0.6790 0.5077 0.3912 0.0011  -0.1583 -0.0055 37  ASP C O   
8440  C CB  . ASP C 37  ? 0.5998 0.4299 0.3381 0.0101  -0.1649 0.0053  37  ASP C CB  
8441  C CG  . ASP C 37  ? 0.6336 0.4745 0.3901 0.0155  -0.1667 0.0126  37  ASP C CG  
8442  O OD1 . ASP C 37  ? 0.7759 0.6200 0.5303 0.0218  -0.1700 0.0209  37  ASP C OD1 
8443  O OD2 . ASP C 37  ? 0.4887 0.3348 0.2624 0.0138  -0.1641 0.0105  37  ASP C OD2 
8444  N N   . TYR C 38  ? 0.5366 0.3641 0.2603 -0.0057 -0.1637 -0.0170 38  TYR C N   
8445  C CA  . TYR C 38  ? 0.5187 0.3356 0.2354 -0.0074 -0.1555 -0.0233 38  TYR C CA  
8446  C C   . TYR C 38  ? 0.6022 0.4234 0.3070 -0.0102 -0.1537 -0.0278 38  TYR C C   
8447  O O   . TYR C 38  ? 0.5700 0.3846 0.2665 -0.0091 -0.1466 -0.0289 38  TYR C O   
8448  C CB  . TYR C 38  ? 0.5700 0.3782 0.2920 -0.0113 -0.1553 -0.0311 38  TYR C CB  
8449  C CG  . TYR C 38  ? 0.6087 0.4114 0.3430 -0.0078 -0.1511 -0.0258 38  TYR C CG  
8450  C CD1 . TYR C 38  ? 0.5755 0.3740 0.3072 -0.0017 -0.1479 -0.0176 38  TYR C CD1 
8451  C CD2 . TYR C 38  ? 0.5601 0.3605 0.3077 -0.0109 -0.1491 -0.0289 38  TYR C CD2 
8452  C CE1 . TYR C 38  ? 0.5587 0.3509 0.2986 0.0014  -0.1432 -0.0135 38  TYR C CE1 
8453  C CE2 . TYR C 38  ? 0.5391 0.3340 0.2954 -0.0077 -0.1437 -0.0235 38  TYR C CE2 
8454  C CZ  . TYR C 38  ? 0.5832 0.3739 0.3345 -0.0014 -0.1408 -0.0162 38  TYR C CZ  
8455  O OH  . TYR C 38  ? 0.6378 0.4209 0.3937 0.0017  -0.1353 -0.0118 38  TYR C OH  
8456  N N   . TYR C 39  ? 0.7597 0.5919 0.4627 -0.0141 -0.1605 -0.0306 39  TYR C N   
8457  C CA  . TYR C 39  ? 0.6108 0.4468 0.2984 -0.0161 -0.1590 -0.0337 39  TYR C CA  
8458  C C   . TYR C 39  ? 0.6436 0.4862 0.3248 -0.0119 -0.1598 -0.0231 39  TYR C C   
8459  O O   . TYR C 39  ? 0.7497 0.5897 0.4162 -0.0114 -0.1544 -0.0223 39  TYR C O   
8460  C CB  . TYR C 39  ? 0.6256 0.4695 0.3114 -0.0229 -0.1663 -0.0420 39  TYR C CB  
8461  C CG  . TYR C 39  ? 0.7045 0.5532 0.3715 -0.0250 -0.1663 -0.0448 39  TYR C CG  
8462  C CD1 . TYR C 39  ? 0.7733 0.6125 0.4254 -0.0272 -0.1586 -0.0544 39  TYR C CD1 
8463  C CD2 . TYR C 39  ? 0.6407 0.5028 0.3036 -0.0243 -0.1741 -0.0378 39  TYR C CD2 
8464  C CE1 . TYR C 39  ? 0.6586 0.5008 0.2903 -0.0290 -0.1579 -0.0574 39  TYR C CE1 
8465  C CE2 . TYR C 39  ? 0.6192 0.4849 0.2622 -0.0263 -0.1743 -0.0400 39  TYR C CE2 
8466  C CZ  . TYR C 39  ? 0.7106 0.5661 0.3371 -0.0288 -0.1659 -0.0501 39  TYR C CZ  
8467  O OH  . TYR C 39  ? 0.7296 0.5873 0.3333 -0.0306 -0.1656 -0.0526 39  TYR C OH  
8468  N N   . ASP C 40  ? 0.6687 0.5186 0.3601 -0.0084 -0.1663 -0.0145 40  ASP C N   
8469  C CA  . ASP C 40  ? 0.6884 0.5449 0.3745 -0.0043 -0.1688 -0.0042 40  ASP C CA  
8470  C C   . ASP C 40  ? 0.6310 0.4767 0.3124 0.0004  -0.1602 0.0029  40  ASP C C   
8471  O O   . ASP C 40  ? 0.7168 0.5629 0.3860 0.0014  -0.1582 0.0082  40  ASP C O   
8472  C CB  . ASP C 40  ? 0.6844 0.5518 0.3845 -0.0010 -0.1789 0.0029  40  ASP C CB  
8473  C CG  . ASP C 40  ? 0.9022 0.7809 0.6105 -0.0070 -0.1887 -0.0041 40  ASP C CG  
8474  O OD1 . ASP C 40  ? 0.8506 0.7378 0.5499 -0.0117 -0.1936 -0.0082 40  ASP C OD1 
8475  O OD2 . ASP C 40  ? 0.9647 0.8430 0.6876 -0.0077 -0.1919 -0.0057 40  ASP C OD2 
8476  N N   . MET C 41  ? 0.6661 0.5016 0.3561 0.0027  -0.1555 0.0033  41  MET C N   
8477  C CA  . MET C 41  ? 0.6259 0.4507 0.3124 0.0060  -0.1488 0.0098  41  MET C CA  
8478  C C   . MET C 41  ? 0.6514 0.4713 0.3240 0.0030  -0.1422 0.0073  41  MET C C   
8479  O O   . MET C 41  ? 0.7604 0.5770 0.4244 0.0043  -0.1395 0.0147  41  MET C O   
8480  C CB  . MET C 41  ? 0.5677 0.3822 0.2644 0.0083  -0.1459 0.0095  41  MET C CB  
8481  C CG  . MET C 41  ? 0.6707 0.4860 0.3767 0.0137  -0.1504 0.0157  41  MET C CG  
8482  S SD  . MET C 41  ? 0.5663 0.3746 0.2689 0.0202  -0.1486 0.0274  41  MET C SD  
8483  C CE  . MET C 41  ? 0.6566 0.4525 0.3491 0.0163  -0.1401 0.0265  41  MET C CE  
8484  N N   . PRO C 42  ? 0.6108 0.4287 0.2796 -0.0008 -0.1391 -0.0022 42  PRO C N   
8485  C CA  . PRO C 42  ? 0.7512 0.5652 0.4039 -0.0031 -0.1330 -0.0043 42  PRO C CA  
8486  C C   . PRO C 42  ? 0.6921 0.5138 0.3290 -0.0050 -0.1346 -0.0046 42  PRO C C   
8487  O O   . PRO C 42  ? 0.7139 0.5321 0.3341 -0.0061 -0.1291 -0.0030 42  PRO C O   
8488  C CB  . PRO C 42  ? 0.7187 0.5270 0.3727 -0.0052 -0.1296 -0.0151 42  PRO C CB  
8489  C CG  . PRO C 42  ? 0.7256 0.5370 0.3939 -0.0056 -0.1349 -0.0194 42  PRO C CG  
8490  C CD  . PRO C 42  ? 0.5544 0.3702 0.2330 -0.0025 -0.1399 -0.0106 42  PRO C CD  
8491  N N   . ALA C 43  ? 0.6383 0.4703 0.2787 -0.0060 -0.1424 -0.0065 43  ALA C N   
8492  C CA  . ALA C 43  ? 0.6378 0.4779 0.2625 -0.0079 -0.1457 -0.0062 43  ALA C CA  
8493  C C   . ALA C 43  ? 0.6590 0.5014 0.2775 -0.0044 -0.1471 0.0068  43  ALA C C   
8494  O O   . ALA C 43  ? 0.6518 0.4992 0.2536 -0.0055 -0.1488 0.0089  43  ALA C O   
8495  C CB  . ALA C 43  ? 0.5875 0.4388 0.2188 -0.0106 -0.1557 -0.0116 43  ALA C CB  
8496  N N   . TYR C 44  ? 0.6109 0.4483 0.2410 -0.0001 -0.1462 0.0154  44  TYR C N   
8497  C CA  . TYR C 44  ? 0.6278 0.4631 0.2514 0.0033  -0.1459 0.0279  44  TYR C CA  
8498  C C   . TYR C 44  ? 0.6115 0.4390 0.2149 0.0007  -0.1376 0.0299  44  TYR C C   
8499  O O   . TYR C 44  ? 0.6229 0.4509 0.2134 0.0018  -0.1378 0.0389  44  TYR C O   
8500  C CB  . TYR C 44  ? 0.5737 0.4008 0.2123 0.0079  -0.1450 0.0346  44  TYR C CB  
8501  C CG  . TYR C 44  ? 0.6182 0.4527 0.2710 0.0129  -0.1533 0.0394  44  TYR C CG  
8502  C CD1 . TYR C 44  ? 0.5541 0.3927 0.2220 0.0131  -0.1571 0.0332  44  TYR C CD1 
8503  C CD2 . TYR C 44  ? 0.6512 0.4878 0.3021 0.0180  -0.1572 0.0508  44  TYR C CD2 
8504  C CE1 . TYR C 44  ? 0.5517 0.3974 0.2324 0.0182  -0.1646 0.0383  44  TYR C CE1 
8505  C CE2 . TYR C 44  ? 0.6364 0.4802 0.3011 0.0238  -0.1648 0.0559  44  TYR C CE2 
8506  C CZ  . TYR C 44  ? 0.5636 0.4124 0.2432 0.0239  -0.1685 0.0496  44  TYR C CZ  
8507  O OH  . TYR C 44  ? 0.5627 0.4194 0.2565 0.0301  -0.1762 0.0555  44  TYR C OH  
8508  N N   . LEU C 45  ? 0.6004 0.4207 0.2002 -0.0024 -0.1303 0.0224  45  LEU C N   
8509  C CA  . LEU C 45  ? 0.6184 0.4304 0.1992 -0.0050 -0.1214 0.0248  45  LEU C CA  
8510  C C   . LEU C 45  ? 0.6935 0.5105 0.2509 -0.0072 -0.1196 0.0227  45  LEU C C   
8511  O O   . LEU C 45  ? 0.8081 0.6191 0.3466 -0.0088 -0.1121 0.0282  45  LEU C O   
8512  C CB  . LEU C 45  ? 0.6181 0.4223 0.2011 -0.0071 -0.1149 0.0168  45  LEU C CB  
8513  C CG  . LEU C 45  ? 0.6521 0.4476 0.2500 -0.0061 -0.1141 0.0211  45  LEU C CG  
8514  C CD1 . LEU C 45  ? 0.6619 0.4531 0.2649 -0.0075 -0.1112 0.0116  45  LEU C CD1 
8515  C CD2 . LEU C 45  ? 0.6533 0.4399 0.2410 -0.0077 -0.1093 0.0325  45  LEU C CD2 
8516  N N   . LYS C 46  ? 0.6605 0.4873 0.2174 -0.0081 -0.1261 0.0150  46  LYS C N   
8517  C CA  . LYS C 46  ? 0.6761 0.5068 0.2088 -0.0105 -0.1253 0.0120  46  LYS C CA  
8518  C C   . LYS C 46  ? 0.7966 0.6335 0.3204 -0.0084 -0.1312 0.0242  46  LYS C C   
8519  O O   . LYS C 46  ? 0.9342 0.7723 0.4339 -0.0101 -0.1291 0.0248  46  LYS C O   
8520  C CB  . LYS C 46  ? 0.7465 0.5841 0.2810 -0.0132 -0.1309 -0.0016 46  LYS C CB  
8521  C CG  . LYS C 46  ? 0.7260 0.5553 0.2615 -0.0154 -0.1233 -0.0149 46  LYS C CG  
8522  C CD  . LYS C 46  ? 0.8887 0.7217 0.4193 -0.0190 -0.1273 -0.0287 46  LYS C CD  
8523  C CE  . LYS C 46  ? 0.7455 0.5899 0.2957 -0.0197 -0.1408 -0.0282 46  LYS C CE  
8524  N NZ  . LYS C 46  ? 0.6780 0.5229 0.2293 -0.0243 -0.1442 -0.0428 46  LYS C NZ  
8525  N N   . ASP C 47  ? 0.8136 0.6537 0.3551 -0.0043 -0.1382 0.0338  47  ASP C N   
8526  C CA  . ASP C 47  ? 0.8603 0.7054 0.3953 -0.0009 -0.1443 0.0465  47  ASP C CA  
8527  C C   . ASP C 47  ? 0.8905 0.7244 0.4255 0.0019  -0.1386 0.0600  47  ASP C C   
8528  O O   . ASP C 47  ? 0.8169 0.6522 0.3454 0.0052  -0.1424 0.0720  47  ASP C O   
8529  C CB  . ASP C 47  ? 0.8458 0.7035 0.3997 0.0025  -0.1574 0.0481  47  ASP C CB  
8530  C CG  . ASP C 47  ? 0.9666 0.8343 0.5244 -0.0015 -0.1637 0.0346  47  ASP C CG  
8531  O OD1 . ASP C 47  ? 1.1302 0.9922 0.6886 -0.0053 -0.1574 0.0230  47  ASP C OD1 
8532  O OD2 . ASP C 47  ? 1.1444 1.0252 0.7048 -0.0008 -0.1753 0.0359  47  ASP C OD2 
8533  N N   . PHE C 48  ? 0.9543 0.7764 0.4960 0.0005  -0.1301 0.0587  48  PHE C N   
8534  C CA  . PHE C 48  ? 0.8555 0.6650 0.3981 0.0018  -0.1251 0.0706  48  PHE C CA  
8535  C C   . PHE C 48  ? 0.8873 0.6853 0.4196 -0.0034 -0.1133 0.0687  48  PHE C C   
8536  O O   . PHE C 48  ? 0.8448 0.6426 0.3821 -0.0058 -0.1103 0.0578  48  PHE C O   
8537  C CB  . PHE C 48  ? 0.6605 0.4666 0.2279 0.0062  -0.1296 0.0730  48  PHE C CB  
8538  C CG  . PHE C 48  ? 0.6614 0.4773 0.2385 0.0122  -0.1399 0.0782  48  PHE C CG  
8539  C CD1 . PHE C 48  ? 0.7005 0.5130 0.2729 0.0166  -0.1419 0.0920  48  PHE C CD1 
8540  C CD2 . PHE C 48  ? 0.6638 0.4921 0.2548 0.0135  -0.1476 0.0702  48  PHE C CD2 
8541  C CE1 . PHE C 48  ? 0.7574 0.5797 0.3393 0.0230  -0.1518 0.0978  48  PHE C CE1 
8542  C CE2 . PHE C 48  ? 0.7386 0.5772 0.3391 0.0190  -0.1575 0.0761  48  PHE C CE2 
8543  C CZ  . PHE C 48  ? 0.7333 0.5694 0.3295 0.0242  -0.1597 0.0899  48  PHE C CZ  
8544  N N   . GLU C 49  ? 0.8868 0.6753 0.4050 -0.0051 -0.1065 0.0800  49  GLU C N   
8545  C CA  . GLU C 49  ? 0.8683 0.6460 0.3751 -0.0110 -0.0945 0.0809  49  GLU C CA  
8546  C C   . GLU C 49  ? 0.8204 0.5860 0.3443 -0.0121 -0.0937 0.0852  49  GLU C C   
8547  O O   . GLU C 49  ? 0.8100 0.5639 0.3309 -0.0142 -0.0898 0.0970  49  GLU C O   
8548  C CB  . GLU C 49  ? 0.9084 0.6818 0.3901 -0.0138 -0.0861 0.0914  49  GLU C CB  
8549  C CG  . GLU C 49  ? 0.9282 0.7106 0.3874 -0.0148 -0.0830 0.0844  49  GLU C CG  
8550  C CD  . GLU C 49  ? 1.1002 0.8801 0.5497 -0.0193 -0.0714 0.0738  49  GLU C CD  
8551  O OE1 . GLU C 49  ? 1.1070 0.8790 0.5401 -0.0240 -0.0575 0.0798  49  GLU C OE1 
8552  O OE2 . GLU C 49  ? 1.1737 0.9592 0.6324 -0.0182 -0.0754 0.0599  49  GLU C OE2 
8553  N N   . ILE C 50  ? 0.7176 0.4852 0.2594 -0.0112 -0.0978 0.0753  50  ILE C N   
8554  C CA  . ILE C 50  ? 0.7220 0.4787 0.2790 -0.0128 -0.0981 0.0766  50  ILE C CA  
8555  C C   . ILE C 50  ? 0.6881 0.4473 0.2506 -0.0150 -0.0970 0.0650  50  ILE C C   
8556  O O   . ILE C 50  ? 0.7502 0.5175 0.3041 -0.0152 -0.0947 0.0562  50  ILE C O   
8557  C CB  . ILE C 50  ? 0.6406 0.3956 0.2167 -0.0068 -0.1063 0.0784  50  ILE C CB  
8558  C CG1 . ILE C 50  ? 0.6274 0.3976 0.2131 -0.0016 -0.1135 0.0699  50  ILE C CG1 
8559  C CG2 . ILE C 50  ? 0.7697 0.5165 0.3406 -0.0048 -0.1062 0.0916  50  ILE C CG2 
8560  C CD1 . ILE C 50  ? 0.6070 0.3759 0.2134 0.0029  -0.1191 0.0671  50  ILE C CD1 
8561  N N   . LYS C 51  ? 0.6237 0.3775 0.2050 -0.0164 -0.0977 0.0639  51  LYS C N   
8562  C CA  . LYS C 51  ? 0.6014 0.3634 0.2024 -0.0173 -0.0955 0.0526  51  LYS C CA  
8563  C C   . LYS C 51  ? 0.5845 0.3424 0.1993 -0.0134 -0.1049 0.0488  51  LYS C C   
8564  O O   . LYS C 51  ? 0.6696 0.4162 0.2880 -0.0130 -0.1085 0.0552  51  LYS C O   
8565  C CB  . LYS C 51  ? 0.6475 0.4111 0.2634 -0.0235 -0.0860 0.0544  51  LYS C CB  
8566  C CG  . LYS C 51  ? 0.6693 0.4362 0.2732 -0.0280 -0.0741 0.0602  51  LYS C CG  
8567  C CD  . LYS C 51  ? 0.6298 0.4062 0.2191 -0.0257 -0.0688 0.0524  51  LYS C CD  
8568  C CE  . LYS C 51  ? 0.6499 0.4309 0.2309 -0.0302 -0.0535 0.0565  51  LYS C CE  
8569  N NZ  . LYS C 51  ? 0.6579 0.4499 0.2652 -0.0328 -0.0436 0.0514  51  LYS C NZ  
8570  N N   . LEU C 52  ? 0.6148 0.3803 0.2360 -0.0107 -0.1081 0.0385  52  LEU C N   
8571  C CA  . LEU C 52  ? 0.6015 0.3640 0.2361 -0.0074 -0.1150 0.0345  52  LEU C CA  
8572  C C   . LEU C 52  ? 0.5933 0.3625 0.2425 -0.0082 -0.1125 0.0244  52  LEU C C   
8573  O O   . LEU C 52  ? 0.5398 0.3169 0.1865 -0.0088 -0.1079 0.0180  52  LEU C O   
8574  C CB  . LEU C 52  ? 0.5834 0.3541 0.2246 -0.0024 -0.1190 0.0327  52  LEU C CB  
8575  C CG  . LEU C 52  ? 0.5929 0.3644 0.2281 0.0001  -0.1201 0.0415  52  LEU C CG  
8576  C CD1 . LEU C 52  ? 0.6124 0.3964 0.2533 0.0040  -0.1252 0.0387  52  LEU C CD1 
8577  C CD2 . LEU C 52  ? 0.5591 0.3177 0.1992 0.0017  -0.1206 0.0491  52  LEU C CD2 
8578  N N   . ASN C 53  ? 0.5950 0.3592 0.2578 -0.0076 -0.1156 0.0230  53  ASN C N   
8579  C CA  . ASN C 53  ? 0.5108 0.2794 0.1882 -0.0078 -0.1145 0.0154  53  ASN C CA  
8580  C C   . ASN C 53  ? 0.5671 0.3327 0.2483 -0.0040 -0.1205 0.0111  53  ASN C C   
8581  O O   . ASN C 53  ? 0.6121 0.3719 0.2918 -0.0017 -0.1242 0.0148  53  ASN C O   
8582  C CB  . ASN C 53  ? 0.5070 0.2728 0.1969 -0.0114 -0.1131 0.0182  53  ASN C CB  
8583  C CG  . ASN C 53  ? 0.5334 0.3017 0.2217 -0.0163 -0.1068 0.0243  53  ASN C CG  
8584  O OD1 . ASN C 53  ? 0.5950 0.3735 0.2865 -0.0175 -0.0992 0.0221  53  ASN C OD1 
8585  N ND2 . ASN C 53  ? 0.5261 0.2841 0.2091 -0.0190 -0.1087 0.0321  53  ASN C ND2 
8586  N N   . PHE C 54  ? 0.4936 0.2640 0.1829 -0.0032 -0.1195 0.0034  54  PHE C N   
8587  C CA  . PHE C 54  ? 0.4861 0.2545 0.1794 -0.0005 -0.1238 -0.0007 54  PHE C CA  
8588  C C   . PHE C 54  ? 0.4778 0.2442 0.1838 -0.0002 -0.1232 -0.0045 54  PHE C C   
8589  O O   . PHE C 54  ? 0.4780 0.2490 0.1910 -0.0010 -0.1190 -0.0071 54  PHE C O   
8590  C CB  . PHE C 54  ? 0.4908 0.2656 0.1781 -0.0002 -0.1246 -0.0065 54  PHE C CB  
8591  C CG  . PHE C 54  ? 0.5574 0.3380 0.2364 -0.0003 -0.1246 -0.0021 54  PHE C CG  
8592  C CD1 . PHE C 54  ? 0.5611 0.3431 0.2255 -0.0023 -0.1215 -0.0011 54  PHE C CD1 
8593  C CD2 . PHE C 54  ? 0.5421 0.3263 0.2270 0.0020  -0.1275 0.0017  54  PHE C CD2 
8594  C CE1 . PHE C 54  ? 0.5657 0.3529 0.2220 -0.0022 -0.1217 0.0040  54  PHE C CE1 
8595  C CE2 . PHE C 54  ? 0.5860 0.3761 0.2644 0.0026  -0.1287 0.0066  54  PHE C CE2 
8596  C CZ  . PHE C 54  ? 0.5944 0.3860 0.2586 0.0004  -0.1260 0.0080  54  PHE C CZ  
8597  N N   . ASN C 55  ? 0.4723 0.2320 0.1815 0.0015  -0.1270 -0.0040 55  ASN C N   
8598  C CA  . ASN C 55  ? 0.4671 0.2235 0.1858 0.0024  -0.1275 -0.0068 55  ASN C CA  
8599  C C   . ASN C 55  ? 0.4748 0.2306 0.1951 0.0038  -0.1280 -0.0114 55  ASN C C   
8600  O O   . ASN C 55  ? 0.4730 0.2272 0.1895 0.0046  -0.1299 -0.0098 55  ASN C O   
8601  C CB  . ASN C 55  ? 0.4667 0.2133 0.1850 0.0023  -0.1311 -0.0021 55  ASN C CB  
8602  C CG  . ASN C 55  ? 0.4643 0.2069 0.1901 0.0034  -0.1329 -0.0037 55  ASN C CG  
8603  O OD1 . ASN C 55  ? 0.5031 0.2498 0.2384 0.0030  -0.1329 -0.0041 55  ASN C OD1 
8604  N ND2 . ASN C 55  ? 0.4646 0.1997 0.1868 0.0052  -0.1340 -0.0037 55  ASN C ND2 
8605  N N   . LEU C 56  ? 0.4651 0.2221 0.1925 0.0042  -0.1258 -0.0168 56  LEU C N   
8606  C CA  . LEU C 56  ? 0.4656 0.2203 0.1960 0.0043  -0.1259 -0.0215 56  LEU C CA  
8607  C C   . LEU C 56  ? 0.4753 0.2222 0.2137 0.0060  -0.1260 -0.0209 56  LEU C C   
8608  O O   . LEU C 56  ? 0.5236 0.2708 0.2686 0.0076  -0.1246 -0.0215 56  LEU C O   
8609  C CB  . LEU C 56  ? 0.4721 0.2318 0.2013 0.0029  -0.1231 -0.0293 56  LEU C CB  
8610  C CG  . LEU C 56  ? 0.4775 0.2439 0.1966 0.0005  -0.1250 -0.0309 56  LEU C CG  
8611  C CD1 . LEU C 56  ? 0.4822 0.2537 0.1929 0.0004  -0.1225 -0.0288 56  LEU C CD1 
8612  C CD2 . LEU C 56  ? 0.4861 0.2527 0.2040 -0.0021 -0.1249 -0.0400 56  LEU C CD2 
8613  N N   . THR C 57  ? 0.4639 0.2041 0.2018 0.0062  -0.1273 -0.0189 57  THR C N   
8614  C CA  . THR C 57  ? 0.4662 0.1975 0.2093 0.0078  -0.1275 -0.0177 57  THR C CA  
8615  C C   . THR C 57  ? 0.4708 0.2001 0.2207 0.0074  -0.1246 -0.0239 57  THR C C   
8616  O O   . THR C 57  ? 0.4725 0.2051 0.2217 0.0044  -0.1236 -0.0286 57  THR C O   
8617  C CB  . THR C 57  ? 0.4679 0.1907 0.2056 0.0081  -0.1284 -0.0126 57  THR C CB  
8618  O OG1 . THR C 57  ? 0.5020 0.2276 0.2403 0.0063  -0.1264 -0.0142 57  THR C OG1 
8619  C CG2 . THR C 57  ? 0.5250 0.2456 0.2539 0.0087  -0.1310 -0.0076 57  THR C CG2 
8620  N N   . PRO C 58  ? 0.4748 0.1985 0.2319 0.0101  -0.1238 -0.0242 58  PRO C N   
8621  C CA  . PRO C 58  ? 0.4826 0.2010 0.2458 0.0102  -0.1203 -0.0307 58  PRO C CA  
8622  C C   . PRO C 58  ? 0.4870 0.1978 0.2498 0.0067  -0.1198 -0.0313 58  PRO C C   
8623  O O   . PRO C 58  ? 0.4946 0.2019 0.2605 0.0042  -0.1174 -0.0383 58  PRO C O   
8624  C CB  . PRO C 58  ? 0.5471 0.2599 0.3192 0.0154  -0.1203 -0.0279 58  PRO C CB  
8625  C CG  . PRO C 58  ? 0.4863 0.2075 0.2586 0.0170  -0.1236 -0.0226 58  PRO C CG  
8626  C CD  . PRO C 58  ? 0.4743 0.1967 0.2352 0.0135  -0.1266 -0.0188 58  PRO C CD  
8627  N N   . VAL C 59  ? 0.4847 0.1921 0.2436 0.0061  -0.1213 -0.0244 59  VAL C N   
8628  C CA  . VAL C 59  ? 0.4894 0.1915 0.2500 0.0023  -0.1193 -0.0240 59  VAL C CA  
8629  C C   . VAL C 59  ? 0.4887 0.2019 0.2506 -0.0025 -0.1197 -0.0289 59  VAL C C   
8630  O O   . VAL C 59  ? 0.5606 0.2724 0.3284 -0.0074 -0.1186 -0.0328 59  VAL C O   
8631  C CB  . VAL C 59  ? 0.4906 0.1861 0.2452 0.0036  -0.1190 -0.0151 59  VAL C CB  
8632  C CG1 . VAL C 59  ? 0.4897 0.1931 0.2366 0.0046  -0.1207 -0.0121 59  VAL C CG1 
8633  C CG2 . VAL C 59  ? 0.4973 0.1873 0.2558 -0.0004 -0.1149 -0.0137 59  VAL C CG2 
8634  N N   . LEU C 60  ? 0.4971 0.2213 0.2537 -0.0017 -0.1221 -0.0284 60  LEU C N   
8635  C CA  . LEU C 60  ? 0.5352 0.2711 0.2923 -0.0056 -0.1242 -0.0324 60  LEU C CA  
8636  C C   . LEU C 60  ? 0.4906 0.2272 0.2474 -0.0085 -0.1246 -0.0420 60  LEU C C   
8637  O O   . LEU C 60  ? 0.5323 0.2718 0.2923 -0.0141 -0.1265 -0.0474 60  LEU C O   
8638  C CB  . LEU C 60  ? 0.5346 0.2795 0.2847 -0.0030 -0.1266 -0.0283 60  LEU C CB  
8639  C CG  . LEU C 60  ? 0.4716 0.2293 0.2206 -0.0057 -0.1303 -0.0305 60  LEU C CG  
8640  C CD1 . LEU C 60  ? 0.5156 0.2788 0.2740 -0.0081 -0.1311 -0.0280 60  LEU C CD1 
8641  C CD2 . LEU C 60  ? 0.4681 0.2311 0.2085 -0.0023 -0.1320 -0.0259 60  LEU C CD2 
8642  N N   . ILE C 61  ? 0.5625 0.2965 0.3156 -0.0051 -0.1228 -0.0447 61  ILE C N   
8643  C CA  . ILE C 61  ? 0.4984 0.2313 0.2484 -0.0068 -0.1211 -0.0546 61  ILE C CA  
8644  C C   . ILE C 61  ? 0.5098 0.2307 0.2662 -0.0099 -0.1193 -0.0606 61  ILE C C   
8645  O O   . ILE C 61  ? 0.5268 0.2460 0.2797 -0.0147 -0.1198 -0.0701 61  ILE C O   
8646  C CB  . ILE C 61  ? 0.4984 0.2313 0.2467 -0.0014 -0.1172 -0.0549 61  ILE C CB  
8647  C CG1 . ILE C 61  ? 0.4904 0.2344 0.2318 -0.0002 -0.1188 -0.0495 61  ILE C CG1 
8648  C CG2 . ILE C 61  ? 0.5133 0.2421 0.2581 -0.0017 -0.1128 -0.0657 61  ILE C CG2 
8649  C CD1 . ILE C 61  ? 0.4865 0.2318 0.2315 0.0045  -0.1158 -0.0457 61  ILE C CD1 
8650  N N   . ASP C 62  ? 0.5088 0.2195 0.2728 -0.0077 -0.1173 -0.0553 62  ASP C N   
8651  C CA  . ASP C 62  ? 0.5214 0.2185 0.2917 -0.0112 -0.1153 -0.0592 62  ASP C CA  
8652  C C   . ASP C 62  ? 0.5955 0.2973 0.3686 -0.0200 -0.1184 -0.0619 62  ASP C C   
8653  O O   . ASP C 62  ? 0.6565 0.3508 0.4317 -0.0259 -0.1183 -0.0704 62  ASP C O   
8654  C CB  . ASP C 62  ? 0.5349 0.2208 0.3108 -0.0072 -0.1132 -0.0503 62  ASP C CB  
8655  C CG  . ASP C 62  ? 0.7052 0.3809 0.4840 -0.0001 -0.1103 -0.0507 62  ASP C CG  
8656  O OD1 . ASP C 62  ? 0.7485 0.4248 0.5264 0.0016  -0.1080 -0.0591 62  ASP C OD1 
8657  O OD2 . ASP C 62  ? 0.6560 0.3234 0.4377 0.0042  -0.1103 -0.0424 62  ASP C OD2 
8658  N N   . GLN C 63  ? 0.5127 0.2268 0.2871 -0.0210 -0.1211 -0.0549 63  GLN C N   
8659  C CA  . GLN C 63  ? 0.5410 0.2634 0.3227 -0.0289 -0.1243 -0.0559 63  GLN C CA  
8660  C C   . GLN C 63  ? 0.6440 0.3774 0.4202 -0.0335 -0.1304 -0.0644 63  GLN C C   
8661  O O   . GLN C 63  ? 0.7141 0.4491 0.4957 -0.0420 -0.1340 -0.0705 63  GLN C O   
8662  C CB  . GLN C 63  ? 0.6724 0.4045 0.4585 -0.0268 -0.1240 -0.0454 63  GLN C CB  
8663  C CG  . GLN C 63  ? 0.6035 0.3233 0.3920 -0.0238 -0.1180 -0.0374 63  GLN C CG  
8664  C CD  . GLN C 63  ? 0.5522 0.2786 0.3392 -0.0197 -0.1163 -0.0279 63  GLN C CD  
8665  O OE1 . GLN C 63  ? 0.5517 0.2842 0.3478 -0.0227 -0.1139 -0.0240 63  GLN C OE1 
8666  N NE2 . GLN C 63  ? 0.5293 0.2542 0.3055 -0.0129 -0.1168 -0.0244 63  GLN C NE2 
8667  N N   . ILE C 64  ? 0.6141 0.3545 0.3787 -0.0288 -0.1319 -0.0646 64  ILE C N   
8668  C CA  . ILE C 64  ? 0.5640 0.3132 0.3190 -0.0328 -0.1376 -0.0719 64  ILE C CA  
8669  C C   . ILE C 64  ? 0.5443 0.2807 0.2934 -0.0373 -0.1364 -0.0848 64  ILE C C   
8670  O O   . ILE C 64  ? 0.5917 0.3312 0.3364 -0.0450 -0.1425 -0.0929 64  ILE C O   
8671  C CB  . ILE C 64  ? 0.5865 0.3431 0.3287 -0.0266 -0.1377 -0.0685 64  ILE C CB  
8672  C CG1 . ILE C 64  ? 0.5961 0.3636 0.3428 -0.0229 -0.1397 -0.0570 64  ILE C CG1 
8673  C CG2 . ILE C 64  ? 0.5675 0.3305 0.2955 -0.0306 -0.1429 -0.0760 64  ILE C CG2 
8674  C CD1 . ILE C 64  ? 0.5437 0.3123 0.2809 -0.0163 -0.1372 -0.0516 64  ILE C CD1 
8675  N N   . GLN C 65  ? 0.5813 0.3025 0.3303 -0.0325 -0.1289 -0.0870 65  GLN C N   
8676  C CA  . GLN C 65  ? 0.5698 0.2755 0.3138 -0.0354 -0.1259 -0.0996 65  GLN C CA  
8677  C C   . GLN C 65  ? 0.5816 0.2790 0.3350 -0.0449 -0.1288 -0.1041 65  GLN C C   
8678  O O   . GLN C 65  ? 0.6029 0.2927 0.3492 -0.0521 -0.1312 -0.1163 65  GLN C O   
8679  C CB  . GLN C 65  ? 0.5766 0.2688 0.3229 -0.0265 -0.1171 -0.0989 65  GLN C CB  
8680  C CG  . GLN C 65  ? 0.5736 0.2705 0.3093 -0.0196 -0.1127 -0.1010 65  GLN C CG  
8681  C CD  . GLN C 65  ? 0.6080 0.2944 0.3510 -0.0106 -0.1044 -0.0998 65  GLN C CD  
8682  O OE1 . GLN C 65  ? 0.6105 0.2902 0.3658 -0.0076 -0.1037 -0.0925 65  GLN C OE1 
8683  N NE2 . GLN C 65  ? 0.6556 0.3409 0.3910 -0.0060 -0.0979 -0.1065 65  GLN C NE2 
8684  N N   . GLU C 66  ? 0.6027 0.3002 0.3713 -0.0458 -0.1280 -0.0947 66  GLU C N   
8685  C CA  . GLU C 66  ? 0.6759 0.3660 0.4560 -0.0558 -0.1296 -0.0975 66  GLU C CA  
8686  C C   . GLU C 66  ? 0.6547 0.3604 0.4364 -0.0662 -0.1393 -0.1022 66  GLU C C   
8687  O O   . GLU C 66  ? 0.7787 0.4767 0.5620 -0.0766 -0.1429 -0.1120 66  GLU C O   
8688  C CB  . GLU C 66  ? 0.6208 0.3093 0.4151 -0.0542 -0.1254 -0.0849 66  GLU C CB  
8689  C CG  . GLU C 66  ? 0.7249 0.4034 0.5326 -0.0647 -0.1247 -0.0866 66  GLU C CG  
8690  C CD  . GLU C 66  ? 0.7589 0.4265 0.5754 -0.0616 -0.1173 -0.0751 66  GLU C CD  
8691  O OE1 . GLU C 66  ? 0.7360 0.4072 0.5486 -0.0521 -0.1144 -0.0654 66  GLU C OE1 
8692  O OE2 . GLU C 66  ? 0.7192 0.3731 0.5451 -0.0692 -0.1145 -0.0758 66  GLU C OE2 
8693  N N   . TYR C 67  ? 0.5711 0.2984 0.3529 -0.0639 -0.1444 -0.0950 67  TYR C N   
8694  C CA  . TYR C 67  ? 0.5761 0.3208 0.3604 -0.0725 -0.1553 -0.0980 67  TYR C CA  
8695  C C   . TYR C 67  ? 0.5972 0.3377 0.3609 -0.0764 -0.1609 -0.1115 67  TYR C C   
8696  O O   . TYR C 67  ? 0.6128 0.3588 0.3794 -0.0867 -0.1680 -0.1188 67  TYR C O   
8697  C CB  . TYR C 67  ? 0.5723 0.3393 0.3608 -0.0669 -0.1587 -0.0864 67  TYR C CB  
8698  C CG  . TYR C 67  ? 0.5414 0.3162 0.3512 -0.0663 -0.1550 -0.0749 67  TYR C CG  
8699  C CD1 . TYR C 67  ? 0.5750 0.3410 0.3856 -0.0577 -0.1454 -0.0663 67  TYR C CD1 
8700  C CD2 . TYR C 67  ? 0.5419 0.3335 0.3710 -0.0743 -0.1611 -0.0724 67  TYR C CD2 
8701  C CE1 . TYR C 67  ? 0.5556 0.3269 0.3817 -0.0568 -0.1406 -0.0563 67  TYR C CE1 
8702  C CE2 . TYR C 67  ? 0.5304 0.3294 0.3791 -0.0731 -0.1554 -0.0618 67  TYR C CE2 
8703  C CZ  . TYR C 67  ? 0.5203 0.3079 0.3655 -0.0642 -0.1445 -0.0540 67  TYR C CZ  
8704  O OH  . TYR C 67  ? 0.5493 0.3423 0.4102 -0.0628 -0.1375 -0.0439 67  TYR C OH  
8705  N N   . ALA C 68  ? 0.6031 0.3396 0.3509 -0.0672 -0.1543 -0.1128 68  ALA C N   
8706  C CA  . ALA C 68  ? 0.6125 0.3539 0.3451 -0.0676 -0.1532 -0.1214 68  ALA C CA  
8707  C C   . ALA C 68  ? 0.6373 0.3618 0.3672 -0.0730 -0.1484 -0.1348 68  ALA C C   
8708  O O   . ALA C 68  ? 0.7048 0.4312 0.4205 -0.0748 -0.1477 -0.1439 68  ALA C O   
8709  C CB  . ALA C 68  ? 0.6481 0.3904 0.3667 -0.0567 -0.1461 -0.1179 68  ALA C CB  
8710  N N   . GLN C 69  ? 0.6406 0.3471 0.3824 -0.0754 -0.1446 -0.1362 69  GLN C N   
8711  C CA  . GLN C 69  ? 0.8619 0.5509 0.6032 -0.0809 -0.1399 -0.1486 69  GLN C CA  
8712  C C   . GLN C 69  ? 0.7759 0.4603 0.5351 -0.0929 -0.1451 -0.1492 69  GLN C C   
8713  O O   . GLN C 69  ? 0.7479 0.4138 0.5109 -0.0978 -0.1404 -0.1574 69  GLN C O   
8714  C CB  . GLN C 69  ? 0.8501 0.5174 0.5873 -0.0707 -0.1274 -0.1508 69  GLN C CB  
8715  C CG  . GLN C 69  ? 1.1335 0.7774 0.8723 -0.0738 -0.1202 -0.1626 69  GLN C CG  
8716  C CD  . GLN C 69  ? 1.2358 0.8664 0.9615 -0.0640 -0.1092 -0.1706 69  GLN C CD  
8717  O OE1 . GLN C 69  ? 1.2055 0.8260 0.9230 -0.0674 -0.1055 -0.1839 69  GLN C OE1 
8718  N NE2 . GLN C 69  ? 1.3205 0.9500 1.0448 -0.0519 -0.1040 -0.1631 69  GLN C NE2 
8719  N N   . GLY C 70  ? 0.6921 0.3925 0.4635 -0.0982 -0.1545 -0.1405 70  GLY C N   
8720  C CA  . GLY C 70  ? 0.6665 0.3681 0.4558 -0.1122 -0.1613 -0.1418 70  GLY C CA  
8721  C C   . GLY C 70  ? 0.7338 0.4170 0.5389 -0.1148 -0.1559 -0.1361 70  GLY C C   
8722  O O   . GLY C 70  ? 0.7048 0.3880 0.5268 -0.1278 -0.1603 -0.1368 70  GLY C O   
8723  N N   . LYS C 71  ? 0.6766 0.3442 0.4774 -0.1035 -0.1465 -0.1298 71  LYS C N   
8724  C CA  . LYS C 71  ? 0.7418 0.3969 0.5592 -0.1037 -0.1383 -0.1209 71  LYS C CA  
8725  C C   . LYS C 71  ? 0.8256 0.5016 0.6596 -0.1015 -0.1370 -0.1048 71  LYS C C   
8726  O O   . LYS C 71  ? 0.9982 0.6657 0.8454 -0.1032 -0.1302 -0.0965 71  LYS C O   
8727  C CB  . LYS C 71  ? 0.7301 0.3625 0.5389 -0.0913 -0.1277 -0.1192 71  LYS C CB  
8728  C CG  . LYS C 71  ? 0.7572 0.3774 0.5513 -0.0869 -0.1240 -0.1321 71  LYS C CG  
8729  C CD  . LYS C 71  ? 0.8459 0.4545 0.6334 -0.0715 -0.1157 -0.1273 71  LYS C CD  
8730  C CE  . LYS C 71  ? 1.0332 0.6444 0.8061 -0.0643 -0.1121 -0.1369 71  LYS C CE  
8731  N NZ  . LYS C 71  ? 0.9081 0.5417 0.6712 -0.0605 -0.1175 -0.1332 71  LYS C NZ  
8732  N N   . ALA C 72  ? 0.7213 0.4224 0.5537 -0.0973 -0.1425 -0.1000 72  ALA C N   
8733  C CA  . ALA C 72  ? 0.5873 0.3065 0.4342 -0.0938 -0.1400 -0.0855 72  ALA C CA  
8734  C C   . ALA C 72  ? 0.6489 0.3782 0.5200 -0.1068 -0.1421 -0.0830 72  ALA C C   
8735  O O   . ALA C 72  ? 0.6613 0.4022 0.5389 -0.1177 -0.1523 -0.0905 72  ALA C O   
8736  C CB  . ALA C 72  ? 0.6092 0.3512 0.4494 -0.0866 -0.1456 -0.0817 72  ALA C CB  
8737  N N   . LYS C 73  ? 0.6493 0.3746 0.5335 -0.1061 -0.1325 -0.0720 73  LYS C N   
8738  C CA  . LYS C 73  ? 0.6474 0.3800 0.5567 -0.1184 -0.1311 -0.0680 73  LYS C CA  
8739  C C   . LYS C 73  ? 0.6320 0.3898 0.5573 -0.1143 -0.1275 -0.0549 73  LYS C C   
8740  O O   . LYS C 73  ? 0.6118 0.3694 0.5527 -0.1173 -0.1180 -0.0456 73  LYS C O   
8741  C CB  . LYS C 73  ? 0.6105 0.3155 0.5224 -0.1223 -0.1209 -0.0657 73  LYS C CB  
8742  C CG  . LYS C 73  ? 0.7397 0.4173 0.6382 -0.1262 -0.1232 -0.0790 73  LYS C CG  
8743  C CD  . LYS C 73  ? 0.7595 0.4076 0.6599 -0.1278 -0.1127 -0.0747 73  LYS C CD  
8744  C CE  . LYS C 73  ? 0.7894 0.4198 0.6711 -0.1118 -0.1058 -0.0696 73  LYS C CE  
8745  N NZ  . LYS C 73  ? 0.7206 0.3238 0.6042 -0.1120 -0.0960 -0.0621 73  LYS C NZ  
8746  N N   . ASP C 74  ? 0.5882 0.3664 0.5087 -0.1069 -0.1340 -0.0538 74  ASP C N   
8747  C CA  . ASP C 74  ? 0.5887 0.3897 0.5225 -0.1006 -0.1304 -0.0421 74  ASP C CA  
8748  C C   . ASP C 74  ? 0.6423 0.4625 0.6087 -0.1120 -0.1300 -0.0378 74  ASP C C   
8749  O O   . ASP C 74  ? 0.7294 0.5653 0.7097 -0.1227 -0.1420 -0.0442 74  ASP C O   
8750  C CB  . ASP C 74  ? 0.6064 0.4253 0.5311 -0.0930 -0.1402 -0.0434 74  ASP C CB  
8751  C CG  . ASP C 74  ? 0.6679 0.4988 0.5945 -0.0806 -0.1336 -0.0317 74  ASP C CG  
8752  O OD1 . ASP C 74  ? 0.7429 0.5749 0.6828 -0.0796 -0.1224 -0.0228 74  ASP C OD1 
8753  O OD2 . ASP C 74  ? 0.7107 0.5484 0.6242 -0.0719 -0.1389 -0.0314 74  ASP C OD2 
8754  N N   . VAL C 75  ? 0.6527 0.4723 0.6311 -0.1101 -0.1162 -0.0267 75  VAL C N   
8755  C CA  . VAL C 75  ? 0.6888 0.5275 0.7013 -0.1209 -0.1130 -0.0212 75  VAL C CA  
8756  C C   . VAL C 75  ? 0.5354 0.4092 0.5689 -0.1168 -0.1173 -0.0154 75  VAL C C   
8757  O O   . VAL C 75  ? 0.5379 0.4339 0.6046 -0.1259 -0.1170 -0.0113 75  VAL C O   
8758  C CB  . VAL C 75  ? 0.6900 0.5150 0.7071 -0.1204 -0.0946 -0.0107 75  VAL C CB  
8759  C CG1 . VAL C 75  ? 0.6615 0.4549 0.6679 -0.1286 -0.0918 -0.0155 75  VAL C CG1 
8760  C CG2 . VAL C 75  ? 0.6027 0.4203 0.5988 -0.1035 -0.0844 -0.0024 75  VAL C CG2 
8761  N N   . PHE C 76  ? 0.5222 0.4018 0.5392 -0.1032 -0.1211 -0.0144 76  PHE C N   
8762  C CA  . PHE C 76  ? 0.6350 0.5467 0.6712 -0.0989 -0.1280 -0.0097 76  PHE C CA  
8763  C C   . PHE C 76  ? 0.6435 0.5680 0.6785 -0.1052 -0.1484 -0.0190 76  PHE C C   
8764  O O   . PHE C 76  ? 0.6733 0.6270 0.7353 -0.1104 -0.1580 -0.0169 76  PHE C O   
8765  C CB  . PHE C 76  ? 0.6762 0.5873 0.6966 -0.0810 -0.1213 -0.0026 76  PHE C CB  
8766  C CG  . PHE C 76  ? 0.4907 0.4331 0.5332 -0.0747 -0.1257 0.0042  76  PHE C CG  
8767  C CD1 . PHE C 76  ? 0.4893 0.4512 0.5634 -0.0739 -0.1149 0.0138  76  PHE C CD1 
8768  C CD2 . PHE C 76  ? 0.5758 0.5282 0.6084 -0.0693 -0.1400 0.0015  76  PHE C CD2 
8769  C CE1 . PHE C 76  ? 0.5148 0.5063 0.6122 -0.0668 -0.1186 0.0206  76  PHE C CE1 
8770  C CE2 . PHE C 76  ? 0.5254 0.5059 0.5792 -0.0626 -0.1447 0.0089  76  PHE C CE2 
8771  C CZ  . PHE C 76  ? 0.5286 0.5291 0.6160 -0.0609 -0.1342 0.0183  76  PHE C CZ  
8772  N N   . LEU C 77  ? 0.6673 0.5710 0.6712 -0.1046 -0.1551 -0.0289 77  LEU C N   
8773  C CA  . LEU C 77  ? 0.5928 0.5039 0.5901 -0.1120 -0.1734 -0.0391 77  LEU C CA  
8774  C C   . LEU C 77  ? 0.7208 0.6390 0.7407 -0.1307 -0.1814 -0.0456 77  LEU C C   
8775  O O   . LEU C 77  ? 0.6418 0.5798 0.6708 -0.1385 -0.1980 -0.0500 77  LEU C O   
8776  C CB  . LEU C 77  ? 0.5361 0.4203 0.4959 -0.1082 -0.1751 -0.0489 77  LEU C CB  
8777  C CG  . LEU C 77  ? 0.6309 0.5198 0.5681 -0.0969 -0.1819 -0.0487 77  LEU C CG  
8778  C CD1 . LEU C 77  ? 0.6309 0.4941 0.5350 -0.0954 -0.1822 -0.0592 77  LEU C CD1 
8779  C CD2 . LEU C 77  ? 0.7471 0.6633 0.6954 -0.1015 -0.1989 -0.0492 77  LEU C CD2 
8780  N N   . GLU C 78  ? 0.7762 0.6775 0.8044 -0.1386 -0.1704 -0.0458 78  GLU C N   
8781  C CA  . GLU C 78  ? 0.7244 0.6304 0.7765 -0.1578 -0.1764 -0.0512 78  GLU C CA  
8782  C C   . GLU C 78  ? 0.7704 0.7149 0.8637 -0.1633 -0.1812 -0.0426 78  GLU C C   
8783  O O   . GLU C 78  ? 0.7853 0.7448 0.8984 -0.1791 -0.1952 -0.0484 78  GLU C O   
8784  C CB  . GLU C 78  ? 0.6178 0.4964 0.6706 -0.1631 -0.1610 -0.0502 78  GLU C CB  
8785  C CG  . GLU C 78  ? 0.7822 0.6469 0.8420 -0.1826 -0.1674 -0.0613 78  GLU C CG  
8786  C CD  . GLU C 78  ? 0.9772 0.8310 1.0116 -0.1871 -0.1834 -0.0776 78  GLU C CD  
8787  O OE1 . GLU C 78  ? 0.9881 0.8179 0.9892 -0.1767 -0.1802 -0.0830 78  GLU C OE1 
8788  O OE2 . GLU C 78  ? 0.8958 0.7647 0.9435 -0.2015 -0.1992 -0.0850 78  GLU C OE2 
8789  N N   . ALA C 79  ? 0.7181 0.6791 0.8252 -0.1506 -0.1701 -0.0291 79  ALA C N   
8790  C CA  . ALA C 79  ? 0.6955 0.6953 0.8440 -0.1524 -0.1727 -0.0194 79  ALA C CA  
8791  C C   . ALA C 79  ? 0.6682 0.6940 0.8179 -0.1466 -0.1909 -0.0195 79  ALA C C   
8792  O O   . ALA C 79  ? 0.6361 0.6958 0.8196 -0.1440 -0.1935 -0.0099 79  ALA C O   
8793  C CB  . ALA C 79  ? 0.6725 0.6766 0.8335 -0.1399 -0.1511 -0.0053 79  ALA C CB  
8794  N N   . ILE C 80  ? 0.6815 0.6922 0.7954 -0.1438 -0.2029 -0.0291 80  ILE C N   
8795  C CA  . ILE C 80  ? 0.7284 0.7600 0.8380 -0.1404 -0.2221 -0.0299 80  ILE C CA  
8796  C C   . ILE C 80  ? 0.8174 0.8482 0.9198 -0.1577 -0.2426 -0.0437 80  ILE C C   
8797  O O   . ILE C 80  ? 0.9075 0.9675 1.0311 -0.1650 -0.2605 -0.0429 80  ILE C O   
8798  C CB  . ILE C 80  ? 0.6373 0.6535 0.7092 -0.1227 -0.2194 -0.0289 80  ILE C CB  
8799  C CG1 . ILE C 80  ? 0.6046 0.6176 0.6802 -0.1066 -0.1994 -0.0168 80  ILE C CG1 
8800  C CG2 . ILE C 80  ? 0.5358 0.5733 0.6031 -0.1188 -0.2387 -0.0277 80  ILE C CG2 
8801  C CD1 . ILE C 80  ? 0.5718 0.6143 0.6689 -0.0945 -0.2016 -0.0045 80  ILE C CD1 
8802  N N   . ARG C 81  ? 0.8246 0.8216 0.8968 -0.1642 -0.2405 -0.0566 81  ARG C N   
8803  C CA  . ARG C 81  ? 0.8000 0.7908 0.8615 -0.1812 -0.2582 -0.0716 81  ARG C CA  
8804  C C   . ARG C 81  ? 0.8371 0.8427 0.9372 -0.2011 -0.2638 -0.0731 81  ARG C C   
8805  O O   . ARG C 81  ? 1.0011 1.0092 1.0996 -0.2171 -0.2821 -0.0845 81  ARG C O   
8806  C CB  . ARG C 81  ? 0.6482 0.5972 0.6693 -0.1813 -0.2514 -0.0847 81  ARG C CB  
8807  C CG  . ARG C 81  ? 0.8740 0.7983 0.9023 -0.1858 -0.2336 -0.0852 81  ARG C CG  
8808  C CD  . ARG C 81  ? 0.9258 0.8211 0.9371 -0.2006 -0.2382 -0.1021 81  ARG C CD  
8809  N NE  . ARG C 81  ? 0.8585 0.7639 0.9015 -0.2212 -0.2458 -0.1052 81  ARG C NE  
8810  C CZ  . ARG C 81  ? 0.9528 0.8341 0.9879 -0.2373 -0.2503 -0.1197 81  ARG C CZ  
8811  N NH1 . ARG C 81  ? 1.0393 0.8857 1.0366 -0.2334 -0.2459 -0.1321 81  ARG C NH1 
8812  N NH2 . ARG C 81  ? 1.0401 0.9332 1.1074 -0.2571 -0.2579 -0.1215 81  ARG C NH2 
8813  N N   . LYS C 82  ? 0.7888 0.8042 0.9230 -0.2010 -0.2484 -0.0619 82  LYS C N   
8814  C CA  . LYS C 82  ? 0.7630 0.7917 0.9367 -0.2204 -0.2507 -0.0619 82  LYS C CA  
8815  C C   . LYS C 82  ? 0.7324 0.8059 0.9423 -0.2279 -0.2706 -0.0574 82  LYS C C   
8816  O O   . LYS C 82  ? 0.6015 0.7004 0.8169 -0.2140 -0.2757 -0.0480 82  LYS C O   
8817  C CB  . LYS C 82  ? 0.7935 0.8204 0.9915 -0.2163 -0.2262 -0.0493 82  LYS C CB  
8818  C CG  . LYS C 82  ? 0.8723 0.8985 1.1020 -0.2370 -0.2223 -0.0504 82  LYS C CG  
8819  C CD  . LYS C 82  ? 0.8265 0.8354 1.0614 -0.2311 -0.1953 -0.0402 82  LYS C CD  
8820  C CE  . LYS C 82  ? 0.6859 0.6995 0.9587 -0.2512 -0.1894 -0.0376 82  LYS C CE  
8821  N NZ  . LYS C 82  ? 0.7078 0.6816 0.9651 -0.2543 -0.1706 -0.0377 82  LYS C NZ  
8822  N N   . ASP C 83  ? 0.8208 0.9032 1.0558 -0.2504 -0.2826 -0.0641 83  ASP C N   
8823  C CA  . ASP C 83  ? 0.6968 0.8249 0.9744 -0.2600 -0.3016 -0.0587 83  ASP C CA  
8824  C C   . ASP C 83  ? 0.6914 0.8523 1.0163 -0.2505 -0.2859 -0.0395 83  ASP C C   
8825  O O   . ASP C 83  ? 0.7265 0.8752 1.0642 -0.2505 -0.2628 -0.0337 83  ASP C O   
8826  C CB  . ASP C 83  ? 0.8129 0.9405 1.1088 -0.2882 -0.3160 -0.0704 83  ASP C CB  
8827  C CG  . ASP C 83  ? 0.8902 1.0670 1.2320 -0.2977 -0.3333 -0.0650 83  ASP C CG  
8828  O OD1 . ASP C 83  ? 0.8938 1.1061 1.2867 -0.2957 -0.3282 -0.0485 83  ASP C OD1 
8829  O OD2 . ASP C 83  ? 0.7942 0.9740 1.1183 -0.3042 -0.3477 -0.0774 83  ASP C OD2 
8830  N N   . PRO C 84  ? 0.6853 0.8871 1.0362 -0.2418 -0.2971 -0.0289 84  PRO C N   
8831  C CA  . PRO C 84  ? 0.7405 0.9722 1.1345 -0.2295 -0.2797 -0.0106 84  PRO C CA  
8832  C C   . PRO C 84  ? 0.7423 0.9935 1.1894 -0.2464 -0.2706 -0.0051 84  PRO C C   
8833  O O   . PRO C 84  ? 0.7549 1.0200 1.2307 -0.2364 -0.2485 0.0087  84  PRO C O   
8834  C CB  . PRO C 84  ? 0.7448 1.0163 1.1561 -0.2193 -0.2990 -0.0025 84  PRO C CB  
8835  C CG  . PRO C 84  ? 0.7576 1.0079 1.1168 -0.2176 -0.3185 -0.0146 84  PRO C CG  
8836  C CD  . PRO C 84  ? 0.7621 0.9801 1.0972 -0.2386 -0.3236 -0.0322 84  PRO C CD  
8837  N N   . ASP C 85  ? 0.6639 0.9164 1.1250 -0.2718 -0.2861 -0.0153 85  ASP C N   
8838  C CA  . ASP C 85  ? 0.7055 0.9712 1.2148 -0.2896 -0.2753 -0.0104 85  ASP C CA  
8839  C C   . ASP C 85  ? 0.7867 1.0068 1.2726 -0.2942 -0.2516 -0.0145 85  ASP C C   
8840  O O   . ASP C 85  ? 0.7632 0.9895 1.2835 -0.3009 -0.2323 -0.0054 85  ASP C O   
8841  C CB  . ASP C 85  ? 0.6618 0.9484 1.1995 -0.3170 -0.3026 -0.0193 85  ASP C CB  
8842  C CG  . ASP C 85  ? 0.7921 1.1191 1.3427 -0.3124 -0.3291 -0.0172 85  ASP C CG  
8843  O OD1 . ASP C 85  ? 0.7660 1.0751 1.2666 -0.3070 -0.3443 -0.0295 85  ASP C OD1 
8844  O OD2 . ASP C 85  ? 0.8570 1.2315 1.4620 -0.3104 -0.3298 -0.0035 85  ASP C OD2 
8845  N N   . ASP C 86  ? 0.7948 0.9694 1.2235 -0.2903 -0.2523 -0.0274 86  ASP C N   
8846  C CA  . ASP C 86  ? 0.8218 0.9513 1.2269 -0.2946 -0.2327 -0.0318 86  ASP C CA  
8847  C C   . ASP C 86  ? 0.7640 0.8818 1.1606 -0.2742 -0.2033 -0.0185 86  ASP C C   
8848  O O   . ASP C 86  ? 0.8430 0.9342 1.2364 -0.2789 -0.1840 -0.0162 86  ASP C O   
8849  C CB  . ASP C 86  ? 0.7930 0.8797 1.1419 -0.2958 -0.2432 -0.0498 86  ASP C CB  
8850  C CG  . ASP C 86  ? 0.9097 0.9641 1.2542 -0.3182 -0.2434 -0.0618 86  ASP C CG  
8851  O OD1 . ASP C 86  ? 0.7786 0.8441 1.1641 -0.3344 -0.2365 -0.0560 86  ASP C OD1 
8852  O OD2 . ASP C 86  ? 0.9670 0.9840 1.2674 -0.3193 -0.2494 -0.0769 86  ASP C OD2 
8853  N N   . LEU C 87  ? 0.6301 0.7657 1.0222 -0.2520 -0.2000 -0.0095 87  LEU C N   
8854  C CA  . LEU C 87  ? 0.6426 0.7602 1.0143 -0.2315 -0.1748 -0.0001 87  LEU C CA  
8855  C C   . LEU C 87  ? 0.6654 0.7911 1.0722 -0.2351 -0.1502 0.0131  87  LEU C C   
8856  O O   . LEU C 87  ? 0.6348 0.7885 1.0893 -0.2513 -0.1520 0.0174  87  LEU C O   
8857  C CB  . LEU C 87  ? 0.6866 0.8246 1.0523 -0.2087 -0.1768 0.0072  87  LEU C CB  
8858  C CG  . LEU C 87  ? 0.6883 0.8251 1.0227 -0.2020 -0.1995 -0.0018 87  LEU C CG  
8859  C CD1 . LEU C 87  ? 0.6056 0.7849 0.9676 -0.1905 -0.2089 0.0081  87  LEU C CD1 
8860  C CD2 . LEU C 87  ? 0.5856 0.6833 0.8655 -0.1860 -0.1907 -0.0062 87  LEU C CD2 
8861  N N   . GLU C 88  ? 0.7843 0.8850 1.1658 -0.2199 -0.1271 0.0197  88  GLU C N   
8862  C CA  . GLU C 88  ? 0.7748 0.8775 1.1787 -0.2197 -0.1005 0.0329  88  GLU C CA  
8863  C C   . GLU C 88  ? 0.7409 0.8697 1.1590 -0.1992 -0.0872 0.0457  88  GLU C C   
8864  O O   . GLU C 88  ? 0.7047 0.8393 1.1047 -0.1827 -0.0960 0.0444  88  GLU C O   
8865  C CB  . GLU C 88  ? 0.6567 0.7106 1.0199 -0.2173 -0.0833 0.0319  88  GLU C CB  
8866  C CG  . GLU C 88  ? 0.6156 0.6601 1.0010 -0.2342 -0.0671 0.0379  88  GLU C CG  
8867  C CD  . GLU C 88  ? 0.7963 0.8250 1.1846 -0.2574 -0.0825 0.0259  88  GLU C CD  
8868  O OE1 . GLU C 88  ? 0.8277 0.8176 1.1743 -0.2565 -0.0883 0.0153  88  GLU C OE1 
8869  O OE2 . GLU C 88  ? 0.8769 0.9319 1.3102 -0.2765 -0.0886 0.0268  88  GLU C OE2 
8870  N N   . LYS C 89  ? 0.6284 0.7715 1.0789 -0.2004 -0.0646 0.0584  89  LYS C N   
8871  C CA  . LYS C 89  ? 0.6546 0.8196 1.1187 -0.1806 -0.0481 0.0706  89  LYS C CA  
8872  C C   . LYS C 89  ? 0.6427 0.7734 1.0524 -0.1591 -0.0375 0.0699  89  LYS C C   
8873  O O   . LYS C 89  ? 0.6558 0.7986 1.0604 -0.1404 -0.0374 0.0731  89  LYS C O   
8874  C CB  . LYS C 89  ? 0.6609 0.8420 1.1647 -0.1867 -0.0224 0.0837  89  LYS C CB  
8875  C CG  . LYS C 89  ? 0.5501 0.7374 1.0530 -0.1649 0.0032  0.0955  89  LYS C CG  
8876  C CD  . LYS C 89  ? 0.6386 0.8420 1.1810 -0.1723 0.0300  0.1083  89  LYS C CD  
8877  C CE  . LYS C 89  ? 0.7395 0.9000 1.2502 -0.1810 0.0477  0.1095  89  LYS C CE  
8878  N NZ  . LYS C 89  ? 0.7163 0.8508 1.1886 -0.1616 0.0736  0.1162  89  LYS C NZ  
8879  N N   . GLU C 90  ? 0.6951 0.7825 1.0645 -0.1618 -0.0293 0.0661  90  GLU C N   
8880  C CA  . GLU C 90  ? 0.7260 0.7803 1.0437 -0.1432 -0.0212 0.0651  90  GLU C CA  
8881  C C   . GLU C 90  ? 0.6946 0.7445 0.9849 -0.1346 -0.0436 0.0549  90  GLU C C   
8882  O O   . GLU C 90  ? 0.7760 0.8189 1.0410 -0.1161 -0.0401 0.0563  90  GLU C O   
8883  C CB  . GLU C 90  ? 0.7388 0.7499 1.0229 -0.1492 -0.0103 0.0638  90  GLU C CB  
8884  C CG  . GLU C 90  ? 0.7794 0.7900 1.0846 -0.1573 0.0139  0.0752  90  GLU C CG  
8885  C CD  . GLU C 90  ? 0.8421 0.8635 1.1843 -0.1817 0.0080  0.0738  90  GLU C CD  
8886  O OE1 . GLU C 90  ? 0.8082 0.8479 1.1690 -0.1917 -0.0151 0.0648  90  GLU C OE1 
8887  O OE2 . GLU C 90  ? 0.8561 0.8668 1.2076 -0.1914 0.0263  0.0818  90  GLU C OE2 
8888  N N   . GLU C 91  ? 0.6527 0.7050 0.9458 -0.1482 -0.0661 0.0443  91  GLU C N   
8889  C CA  . GLU C 91  ? 0.5933 0.6443 0.8620 -0.1409 -0.0870 0.0352  91  GLU C CA  
8890  C C   . GLU C 91  ? 0.5566 0.6464 0.8519 -0.1309 -0.0952 0.0407  91  GLU C C   
8891  O O   . GLU C 91  ? 0.5493 0.6358 0.8203 -0.1166 -0.1031 0.0388  91  GLU C O   
8892  C CB  . GLU C 91  ? 0.5363 0.5791 0.7999 -0.1584 -0.1079 0.0221  91  GLU C CB  
8893  C CG  . GLU C 91  ? 0.6596 0.6635 0.9001 -0.1683 -0.1004 0.0166  91  GLU C CG  
8894  C CD  . GLU C 91  ? 0.7982 0.7930 1.0353 -0.1860 -0.1198 0.0028  91  GLU C CD  
8895  O OE1 . GLU C 91  ? 0.8756 0.8670 1.0894 -0.1824 -0.1370 -0.0070 91  GLU C OE1 
8896  O OE2 . GLU C 91  ? 0.7197 0.7093 0.9763 -0.2038 -0.1171 0.0016  91  GLU C OE2 
8897  N N   . VAL C 92  ? 0.6148 0.7416 0.9613 -0.1381 -0.0935 0.0483  92  VAL C N   
8898  C CA  . VAL C 92  ? 0.5787 0.7440 0.9552 -0.1266 -0.0991 0.0558  92  VAL C CA  
8899  C C   . VAL C 92  ? 0.5595 0.7163 0.9193 -0.1035 -0.0792 0.0639  92  VAL C C   
8900  O O   . VAL C 92  ? 0.4892 0.6537 0.8401 -0.0881 -0.0868 0.0653  92  VAL C O   
8901  C CB  . VAL C 92  ? 0.5251 0.7329 0.9642 -0.1392 -0.0986 0.0634  92  VAL C CB  
8902  C CG1 . VAL C 92  ? 0.4969 0.7423 0.9704 -0.1226 -0.0940 0.0752  92  VAL C CG1 
8903  C CG2 . VAL C 92  ? 0.5144 0.7373 0.9704 -0.1599 -0.1262 0.0544  92  VAL C CG2 
8904  N N   . GLU C 93  ? 0.5890 0.7273 0.9416 -0.1010 -0.0536 0.0694  93  GLU C N   
8905  C CA  . GLU C 93  ? 0.5899 0.7144 0.9202 -0.0801 -0.0341 0.0755  93  GLU C CA  
8906  C C   . GLU C 93  ? 0.6761 0.7662 0.9513 -0.0697 -0.0422 0.0675  93  GLU C C   
8907  O O   . GLU C 93  ? 0.6719 0.7586 0.9314 -0.0518 -0.0381 0.0702  93  GLU C O   
8908  C CB  . GLU C 93  ? 0.5465 0.6551 0.8751 -0.0815 -0.0060 0.0822  93  GLU C CB  
8909  C CG  . GLU C 93  ? 0.6948 0.7833 0.9935 -0.0613 0.0148  0.0870  93  GLU C CG  
8910  C CD  . GLU C 93  ? 0.8326 0.8763 1.0834 -0.0623 0.0266  0.0845  93  GLU C CD  
8911  O OE1 . GLU C 93  ? 0.8341 0.8604 1.0621 -0.0492 0.0465  0.0892  93  GLU C OE1 
8912  O OE2 . GLU C 93  ? 0.7261 0.7511 0.9616 -0.0758 0.0157  0.0778  93  GLU C OE2 
8913  N N   . LYS C 94  ? 0.6577 0.7219 0.9046 -0.0809 -0.0531 0.0578  94  LYS C N   
8914  C CA  . LYS C 94  ? 0.6133 0.6479 0.8120 -0.0723 -0.0615 0.0503  94  LYS C CA  
8915  C C   . LYS C 94  ? 0.5950 0.6473 0.7942 -0.0645 -0.0806 0.0479  94  LYS C C   
8916  O O   . LYS C 94  ? 0.6476 0.6852 0.8169 -0.0503 -0.0808 0.0473  94  LYS C O   
8917  C CB  . LYS C 94  ? 0.6327 0.6402 0.8075 -0.0861 -0.0698 0.0404  94  LYS C CB  
8918  C CG  . LYS C 94  ? 0.6759 0.6482 0.8222 -0.0851 -0.0525 0.0418  94  LYS C CG  
8919  C CD  . LYS C 94  ? 0.6885 0.6297 0.7994 -0.0899 -0.0630 0.0314  94  LYS C CD  
8920  C CE  . LYS C 94  ? 0.6923 0.6213 0.8119 -0.1073 -0.0616 0.0286  94  LYS C CE  
8921  N NZ  . LYS C 94  ? 0.6404 0.5472 0.7499 -0.1063 -0.0407 0.0364  94  LYS C NZ  
8922  N N   . LEU C 95  ? 0.6439 0.7275 0.8763 -0.0742 -0.0974 0.0470  95  LEU C N   
8923  C CA  . LEU C 95  ? 0.6522 0.7519 0.8829 -0.0680 -0.1176 0.0453  95  LEU C CA  
8924  C C   . LEU C 95  ? 0.5589 0.6784 0.8063 -0.0494 -0.1105 0.0561  95  LEU C C   
8925  O O   . LEU C 95  ? 0.5745 0.6892 0.8008 -0.0370 -0.1185 0.0560  95  LEU C O   
8926  C CB  . LEU C 95  ? 0.7503 0.8768 1.0096 -0.0846 -0.1393 0.0411  95  LEU C CB  
8927  C CG  . LEU C 95  ? 0.7150 0.8184 0.9451 -0.0991 -0.1540 0.0274  95  LEU C CG  
8928  C CD1 . LEU C 95  ? 0.6721 0.7932 0.9343 -0.1207 -0.1650 0.0231  95  LEU C CD1 
8929  C CD2 . LEU C 95  ? 0.5178 0.6172 0.7184 -0.0926 -0.1727 0.0218  95  LEU C CD2 
8930  N N   . ILE C 96  ? 0.4725 0.6140 0.7584 -0.0471 -0.0946 0.0656  96  ILE C N   
8931  C CA  . ILE C 96  ? 0.5427 0.7024 0.8463 -0.0281 -0.0862 0.0756  96  ILE C CA  
8932  C C   . ILE C 96  ? 0.6344 0.7596 0.8970 -0.0118 -0.0687 0.0759  96  ILE C C   
8933  O O   . ILE C 96  ? 0.6099 0.7332 0.8610 0.0041  -0.0710 0.0787  96  ILE C O   
8934  C CB  . ILE C 96  ? 0.4714 0.6658 0.8301 -0.0294 -0.0724 0.0858  96  ILE C CB  
8935  C CG1 . ILE C 96  ? 0.4786 0.6614 0.8417 -0.0434 -0.0555 0.0849  96  ILE C CG1 
8936  C CG2 . ILE C 96  ? 0.5152 0.7538 0.9205 -0.0374 -0.0943 0.0887  96  ILE C CG2 
8937  C CD1 . ILE C 96  ? 0.4824 0.6987 0.8997 -0.0454 -0.0388 0.0955  96  ILE C CD1 
8938  N N   . GLU C 97  ? 0.6369 0.7333 0.8760 -0.0157 -0.0519 0.0734  97  GLU C N   
8939  C CA  . GLU C 97  ? 0.7250 0.7886 0.9245 -0.0015 -0.0361 0.0735  97  GLU C CA  
8940  C C   . GLU C 97  ? 0.6356 0.6745 0.7922 0.0028  -0.0510 0.0660  97  GLU C C   
8941  O O   . GLU C 97  ? 0.6445 0.6664 0.7766 0.0174  -0.0446 0.0672  97  GLU C O   
8942  C CB  . GLU C 97  ? 0.7089 0.7476 0.8915 -0.0078 -0.0169 0.0731  97  GLU C CB  
8943  C CG  . GLU C 97  ? 0.7174 0.7696 0.9278 -0.0031 0.0078  0.0825  97  GLU C CG  
8944  C CD  . GLU C 97  ? 0.8323 0.8615 1.0138 0.0148  0.0274  0.0852  97  GLU C CD  
8945  O OE1 . GLU C 97  ? 0.7994 0.8370 0.9852 0.0298  0.0263  0.0875  97  GLU C OE1 
8946  O OE2 . GLU C 97  ? 0.8317 0.8329 0.9852 0.0137  0.0435  0.0851  97  GLU C OE2 
8947  N N   . PHE C 98  ? 0.5217 0.5574 0.6684 -0.0100 -0.0698 0.0581  98  PHE C N   
8948  C CA  . PHE C 98  ? 0.5784 0.5954 0.6887 -0.0060 -0.0838 0.0518  98  PHE C CA  
8949  C C   . PHE C 98  ? 0.6302 0.6674 0.7514 0.0046  -0.0958 0.0561  98  PHE C C   
8950  O O   . PHE C 98  ? 0.5826 0.6030 0.6760 0.0157  -0.0975 0.0558  98  PHE C O   
8951  C CB  . PHE C 98  ? 0.5950 0.6041 0.6927 -0.0216 -0.0995 0.0420  98  PHE C CB  
8952  C CG  . PHE C 98  ? 0.5516 0.5408 0.6116 -0.0179 -0.1111 0.0355  98  PHE C CG  
8953  C CD1 . PHE C 98  ? 0.5694 0.5280 0.5942 -0.0101 -0.1018 0.0340  98  PHE C CD1 
8954  C CD2 . PHE C 98  ? 0.4650 0.4667 0.5248 -0.0224 -0.1314 0.0313  98  PHE C CD2 
8955  C CE1 . PHE C 98  ? 0.5410 0.4834 0.5347 -0.0073 -0.1115 0.0287  98  PHE C CE1 
8956  C CE2 . PHE C 98  ? 0.4646 0.4484 0.4900 -0.0190 -0.1401 0.0261  98  PHE C CE2 
8957  C CZ  . PHE C 98  ? 0.4634 0.4183 0.4575 -0.0115 -0.1297 0.0250  98  PHE C CZ  
8958  N N   . THR C 99  ? 0.6578 0.7309 0.8200 0.0010  -0.1050 0.0608  99  THR C N   
8959  C CA  . THR C 99  ? 0.5687 0.6631 0.7448 0.0122  -0.1166 0.0670  99  THR C CA  
8960  C C   . THR C 99  ? 0.5598 0.6566 0.7471 0.0309  -0.0988 0.0764  99  THR C C   
8961  O O   . THR C 99  ? 0.5841 0.6849 0.7692 0.0442  -0.1049 0.0813  99  THR C O   
8962  C CB  . THR C 99  ? 0.4620 0.5957 0.6798 0.0021  -0.1338 0.0694  99  THR C CB  
8963  O OG1 . THR C 99  ? 0.4821 0.6112 0.6941 -0.0177 -0.1439 0.0598  99  THR C OG1 
8964  C CG2 . THR C 99  ? 0.4633 0.6124 0.6813 0.0096  -0.1542 0.0731  99  THR C CG2 
8965  N N   . LYS C 100 ? 0.4894 0.5820 0.6870 0.0326  -0.0762 0.0791  100 LYS C N   
8966  C CA  . LYS C 100 ? 0.5931 0.6829 0.7959 0.0509  -0.0567 0.0864  100 LYS C CA  
8967  C C   . LYS C 100 ? 0.5684 0.6175 0.7212 0.0609  -0.0497 0.0822  100 LYS C C   
8968  O O   . LYS C 100 ? 0.4869 0.5307 0.6346 0.0772  -0.0452 0.0865  100 LYS C O   
8969  C CB  . LYS C 100 ? 0.6485 0.7462 0.8759 0.0489  -0.0335 0.0906  100 LYS C CB  
8970  C CG  . LYS C 100 ? 0.5260 0.6700 0.8134 0.0453  -0.0355 0.0985  100 LYS C CG  
8971  C CD  . LYS C 100 ? 0.4857 0.6363 0.7964 0.0421  -0.0105 0.1029  100 LYS C CD  
8972  C CE  . LYS C 100 ? 0.5663 0.7038 0.8694 0.0617  0.0157  0.1080  100 LYS C CE  
8973  N NZ  . LYS C 100 ? 0.5874 0.7320 0.9123 0.0588  0.0419  0.1130  100 LYS C NZ  
8974  N N   . LEU C 101 ? 0.6418 0.6617 0.7585 0.0514  -0.0492 0.0741  101 LEU C N   
8975  C CA  . LEU C 101 ? 0.7233 0.7056 0.7937 0.0589  -0.0440 0.0698  101 LEU C CA  
8976  C C   . LEU C 101 ? 0.6305 0.6070 0.6820 0.0629  -0.0620 0.0679  101 LEU C C   
8977  O O   . LEU C 101 ? 0.6533 0.6052 0.6760 0.0728  -0.0576 0.0672  101 LEU C O   
8978  C CB  . LEU C 101 ? 0.7688 0.7250 0.8104 0.0473  -0.0397 0.0628  101 LEU C CB  
8979  C CG  . LEU C 101 ? 0.8526 0.7698 0.8472 0.0515  -0.0341 0.0580  101 LEU C CG  
8980  C CD1 . LEU C 101 ? 0.7770 0.6820 0.7460 0.0471  -0.0525 0.0517  101 LEU C CD1 
8981  C CD2 . LEU C 101 ? 0.7793 0.6833 0.7629 0.0679  -0.0200 0.0616  101 LEU C CD2 
8982  N N   . ASN C 102 ? 0.6478 0.6456 0.7136 0.0549  -0.0820 0.0671  102 ASN C N   
8983  C CA  . ASN C 102 ? 0.6125 0.6070 0.6610 0.0581  -0.0991 0.0665  102 ASN C CA  
8984  C C   . ASN C 102 ? 0.5570 0.5782 0.6340 0.0689  -0.1068 0.0758  102 ASN C C   
8985  O O   . ASN C 102 ? 0.6170 0.6406 0.6839 0.0704  -0.1231 0.0769  102 ASN C O   
8986  C CB  . ASN C 102 ? 0.5293 0.5260 0.5677 0.0425  -0.1169 0.0588  102 ASN C CB  
8987  C CG  . ASN C 102 ? 0.5241 0.4942 0.5353 0.0330  -0.1106 0.0501  102 ASN C CG  
8988  O OD1 . ASN C 102 ? 0.6353 0.5843 0.6315 0.0378  -0.0948 0.0500  102 ASN C OD1 
8989  N ND2 . ASN C 102 ? 0.5278 0.4981 0.5316 0.0199  -0.1233 0.0427  102 ASN C ND2 
8990  N N   . TYR C 103 ? 0.5167 0.5577 0.6287 0.0770  -0.0947 0.0833  103 TYR C N   
8991  C CA  . TYR C 103 ? 0.5602 0.6339 0.7090 0.0859  -0.1036 0.0931  103 TYR C CA  
8992  C C   . TYR C 103 ? 0.6225 0.6833 0.7529 0.1009  -0.1089 0.0980  103 TYR C C   
8993  O O   . TYR C 103 ? 0.5964 0.6732 0.7332 0.1018  -0.1284 0.1024  103 TYR C O   
8994  C CB  . TYR C 103 ? 0.5696 0.6638 0.7587 0.0937  -0.0850 0.1003  103 TYR C CB  
8995  C CG  . TYR C 103 ? 0.6596 0.7942 0.8966 0.1020  -0.0936 0.1113  103 TYR C CG  
8996  C CD1 . TYR C 103 ? 0.5503 0.6848 0.7925 0.1219  -0.0912 0.1198  103 TYR C CD1 
8997  C CD2 . TYR C 103 ? 0.7287 0.9014 1.0072 0.0899  -0.1045 0.1135  103 TYR C CD2 
8998  C CE1 . TYR C 103 ? 0.5233 0.6959 0.8116 0.1308  -0.0997 0.1311  103 TYR C CE1 
8999  C CE2 . TYR C 103 ? 0.7634 0.9758 1.0886 0.0973  -0.1140 0.1243  103 TYR C CE2 
9000  C CZ  . TYR C 103 ? 0.6133 0.8261 0.9436 0.1184  -0.1116 0.1335  103 TYR C CZ  
9001  O OH  . TYR C 103 ? 0.5611 0.8146 0.9400 0.1270  -0.1218 0.1454  103 TYR C OH  
9002  N N   . GLU C 104 ? 0.6568 0.6869 0.7623 0.1124  -0.0923 0.0974  104 GLU C N   
9003  C CA  . GLU C 104 ? 0.5473 0.5651 0.6422 0.1287  -0.0932 0.1036  104 GLU C CA  
9004  C C   . GLU C 104 ? 0.6516 0.6468 0.7071 0.1246  -0.1079 0.0999  104 GLU C C   
9005  O O   . GLU C 104 ? 0.5905 0.5764 0.6374 0.1365  -0.1115 0.1061  104 GLU C O   
9006  C CB  . GLU C 104 ? 0.6177 0.6097 0.7015 0.1421  -0.0688 0.1035  104 GLU C CB  
9007  C CG  . GLU C 104 ? 0.6576 0.6662 0.7730 0.1445  -0.0496 0.1054  104 GLU C CG  
9008  C CD  . GLU C 104 ? 0.9160 0.8951 1.0135 0.1572  -0.0245 0.1038  104 GLU C CD  
9009  O OE1 . GLU C 104 ? 0.9473 0.8984 1.0178 0.1677  -0.0228 0.1034  104 GLU C OE1 
9010  O OE2 . GLU C 104 ? 0.8815 0.8640 0.9903 0.1561  -0.0061 0.1027  104 GLU C OE2 
9011  N N   . LYS C 105 ? 0.7299 0.7158 0.7623 0.1086  -0.1155 0.0907  105 LYS C N   
9012  C CA  . LYS C 105 ? 0.6082 0.5721 0.6032 0.1048  -0.1263 0.0871  105 LYS C CA  
9013  C C   . LYS C 105 ? 0.6657 0.6499 0.6682 0.1049  -0.1473 0.0933  105 LYS C C   
9014  O O   . LYS C 105 ? 0.6652 0.6807 0.6958 0.0993  -0.1586 0.0955  105 LYS C O   
9015  C CB  . LYS C 105 ? 0.4925 0.4429 0.4642 0.0888  -0.1277 0.0758  105 LYS C CB  
9016  C CG  . LYS C 105 ? 0.5730 0.5028 0.5344 0.0878  -0.1089 0.0703  105 LYS C CG  
9017  C CD  . LYS C 105 ? 0.6200 0.5398 0.5634 0.0725  -0.1116 0.0605  105 LYS C CD  
9018  C CE  . LYS C 105 ? 0.5580 0.4583 0.4912 0.0716  -0.0942 0.0565  105 LYS C CE  
9019  N NZ  . LYS C 105 ? 0.6061 0.4874 0.5127 0.0604  -0.0969 0.0480  105 LYS C NZ  
9020  N N   . PRO C 106 ? 0.6552 0.6216 0.6321 0.1106  -0.1534 0.0967  106 PRO C N   
9021  C CA  . PRO C 106 ? 0.6266 0.6105 0.6072 0.1120  -0.1732 0.1043  106 PRO C CA  
9022  C C   . PRO C 106 ? 0.6002 0.6013 0.5783 0.0957  -0.1901 0.0982  106 PRO C C   
9023  O O   . PRO C 106 ? 0.6252 0.6528 0.6210 0.0952  -0.2066 0.1043  106 PRO C O   
9024  C CB  . PRO C 106 ? 0.6928 0.6464 0.6381 0.1178  -0.1731 0.1069  106 PRO C CB  
9025  C CG  . PRO C 106 ? 0.6685 0.5945 0.6045 0.1255  -0.1528 0.1044  106 PRO C CG  
9026  C CD  . PRO C 106 ? 0.6806 0.6119 0.6300 0.1191  -0.1409 0.0963  106 PRO C CD  
9027  N N   . ILE C 107 ? 0.6801 0.6661 0.6361 0.0825  -0.1871 0.0863  107 ILE C N   
9028  C CA  . ILE C 107 ? 0.6268 0.6256 0.5785 0.0671  -0.2017 0.0791  107 ILE C CA  
9029  C C   . ILE C 107 ? 0.6232 0.6518 0.6120 0.0601  -0.2054 0.0778  107 ILE C C   
9030  O O   . ILE C 107 ? 0.6194 0.6621 0.6094 0.0475  -0.2200 0.0726  107 ILE C O   
9031  C CB  . ILE C 107 ? 0.6855 0.6593 0.6056 0.0562  -0.1962 0.0668  107 ILE C CB  
9032  C CG1 . ILE C 107 ? 0.5883 0.5579 0.5202 0.0509  -0.1820 0.0599  107 ILE C CG1 
9033  C CG2 . ILE C 107 ? 0.6157 0.5604 0.5039 0.0627  -0.1896 0.0682  107 ILE C CG2 
9034  C CD1 . ILE C 107 ? 0.5049 0.4542 0.4111 0.0398  -0.1788 0.0484  107 ILE C CD1 
9035  N N   . TYR C 108 ? 0.6758 0.7135 0.6944 0.0675  -0.1921 0.0824  108 TYR C N   
9036  C CA  . TYR C 108 ? 0.7100 0.7784 0.7695 0.0617  -0.1936 0.0833  108 TYR C CA  
9037  C C   . TYR C 108 ? 0.7116 0.8104 0.8083 0.0736  -0.2001 0.0965  108 TYR C C   
9038  O O   . TYR C 108 ? 0.7511 0.8721 0.8869 0.0760  -0.1922 0.1007  108 TYR C O   
9039  C CB  . TYR C 108 ? 0.5355 0.5946 0.6044 0.0605  -0.1721 0.0793  108 TYR C CB  
9040  C CG  . TYR C 108 ? 0.5858 0.6383 0.6467 0.0431  -0.1716 0.0679  108 TYR C CG  
9041  C CD1 . TYR C 108 ? 0.7055 0.7265 0.7277 0.0380  -0.1673 0.0589  108 TYR C CD1 
9042  C CD2 . TYR C 108 ? 0.5268 0.6046 0.6206 0.0319  -0.1752 0.0666  108 TYR C CD2 
9043  C CE1 . TYR C 108 ? 0.6742 0.6877 0.6898 0.0235  -0.1664 0.0491  108 TYR C CE1 
9044  C CE2 . TYR C 108 ? 0.5469 0.6156 0.6330 0.0161  -0.1742 0.0564  108 TYR C CE2 
9045  C CZ  . TYR C 108 ? 0.6075 0.6435 0.6541 0.0127  -0.1697 0.0478  108 TYR C CZ  
9046  O OH  . TYR C 108 ? 0.5518 0.5775 0.5915 -0.0016 -0.1684 0.0383  108 TYR C OH  
9047  N N   . ARG C 109 ? 0.5325 0.6332 0.6188 0.0816  -0.2138 0.1040  109 ARG C N   
9048  C CA  . ARG C 109 ? 0.5126 0.6385 0.6316 0.0961  -0.2198 0.1183  109 ARG C CA  
9049  C C   . ARG C 109 ? 0.6009 0.7597 0.7367 0.0875  -0.2463 0.1214  109 ARG C C   
9050  O O   . ARG C 109 ? 0.5322 0.6885 0.6460 0.0888  -0.2632 0.1254  109 ARG C O   
9051  C CB  . ARG C 109 ? 0.6020 0.7048 0.6979 0.1125  -0.2163 0.1262  109 ARG C CB  
9052  C CG  . ARG C 109 ? 0.7660 0.8869 0.8969 0.1318  -0.2140 0.1409  109 ARG C CG  
9053  C CD  . ARG C 109 ? 0.8187 0.9080 0.9239 0.1479  -0.2052 0.1470  109 ARG C CD  
9054  N NE  . ARG C 109 ? 0.7932 0.8593 0.8544 0.1436  -0.2167 0.1460  109 ARG C NE  
9055  C CZ  . ARG C 109 ? 0.9081 0.9874 0.9592 0.1362  -0.2393 0.1487  109 ARG C CZ  
9056  N NH1 . ARG C 109 ? 0.9006 1.0178 0.9832 0.1324  -0.2566 0.1532  109 ARG C NH1 
9057  N NH2 . ARG C 109 ? 0.8363 0.8903 0.8443 0.1325  -0.2448 0.1471  109 ARG C NH2 
9058  N N   . PHE C 110 ? 0.7092 0.8988 0.8840 0.0783  -0.2498 0.1201  110 PHE C N   
9059  C CA  . PHE C 110 ? 0.6639 0.8872 0.8590 0.0678  -0.2756 0.1220  110 PHE C CA  
9060  C C   . PHE C 110 ? 0.6132 0.8779 0.8689 0.0751  -0.2766 0.1335  110 PHE C C   
9061  O O   . PHE C 110 ? 0.5082 0.7758 0.7907 0.0822  -0.2548 0.1357  110 PHE C O   
9062  C CB  . PHE C 110 ? 0.5168 0.7382 0.7007 0.0446  -0.2822 0.1069  110 PHE C CB  
9063  C CG  . PHE C 110 ? 0.5236 0.7127 0.6519 0.0365  -0.2878 0.0964  110 PHE C CG  
9064  C CD1 . PHE C 110 ? 0.5406 0.7285 0.6429 0.0385  -0.3071 0.1003  110 PHE C CD1 
9065  C CD2 . PHE C 110 ? 0.5867 0.7469 0.6892 0.0273  -0.2732 0.0833  110 PHE C CD2 
9066  C CE1 . PHE C 110 ? 0.5485 0.7075 0.6005 0.0313  -0.3101 0.0908  110 PHE C CE1 
9067  C CE2 . PHE C 110 ? 0.5483 0.6809 0.6033 0.0207  -0.2771 0.0739  110 PHE C CE2 
9068  C CZ  . PHE C 110 ? 0.5381 0.6704 0.5682 0.0226  -0.2947 0.0774  110 PHE C CZ  
9069  N N   . GLU C 111 ? 0.6027 0.9002 0.8796 0.0733  -0.3023 0.1412  111 GLU C N   
9070  C CA  . GLU C 111 ? 0.5845 0.9259 0.9231 0.0811  -0.3060 0.1539  111 GLU C CA  
9071  C C   . GLU C 111 ? 0.6817 1.0448 1.0597 0.0667  -0.2972 0.1477  111 GLU C C   
9072  O O   . GLU C 111 ? 0.6864 1.0689 1.1089 0.0764  -0.2804 0.1552  111 GLU C O   
9073  C CB  . GLU C 111 ? 0.7213 1.0935 1.0718 0.0800  -0.3389 0.1630  111 GLU C CB  
9074  C CG  . GLU C 111 ? 0.7956 1.1561 1.1025 0.0608  -0.3614 0.1518  111 GLU C CG  
9075  C CD  . GLU C 111 ? 0.7375 1.1103 1.0306 0.0639  -0.3801 0.1553  111 GLU C CD  
9076  O OE1 . GLU C 111 ? 0.8508 1.2089 1.1227 0.0813  -0.3773 0.1641  111 GLU C OE1 
9077  O OE2 . GLU C 111 ? 0.6971 1.0923 0.9990 0.0489  -0.3962 0.1485  111 GLU C OE2 
9078  N N   . ARG C 112 ? 0.7406 1.0994 1.1025 0.0438  -0.3071 0.1341  112 ARG C N   
9079  C CA  . ARG C 112 ? 0.6298 1.0099 1.0300 0.0279  -0.3017 0.1288  112 ARG C CA  
9080  C C   . ARG C 112 ? 0.7811 1.1363 1.1768 0.0294  -0.2690 0.1233  112 ARG C C   
9081  O O   . ARG C 112 ? 0.7495 1.1255 1.1872 0.0239  -0.2569 0.1247  112 ARG C O   
9082  C CB  . ARG C 112 ? 0.5229 0.9025 0.9051 0.0027  -0.3230 0.1154  112 ARG C CB  
9083  C CG  . ARG C 112 ? 0.6991 1.1213 1.1143 -0.0064 -0.3542 0.1205  112 ARG C CG  
9084  C CD  . ARG C 112 ? 0.6604 1.1282 1.1477 -0.0062 -0.3501 0.1306  112 ARG C CD  
9085  N NE  . ARG C 112 ? 0.5666 1.0386 1.0736 -0.0276 -0.3430 0.1203  112 ARG C NE  
9086  C CZ  . ARG C 112 ? 0.5885 1.0787 1.1073 -0.0507 -0.3657 0.1127  112 ARG C CZ  
9087  N NH1 . ARG C 112 ? 0.6319 1.1353 1.1389 -0.0552 -0.3950 0.1122  112 ARG C NH1 
9088  N NH2 . ARG C 112 ? 0.5491 1.0391 1.0859 -0.0693 -0.3559 0.1040  112 ARG C NH2 
9089  N N   . ILE C 113 ? 0.8603 1.1717 1.2057 0.0361  -0.2548 0.1173  113 ILE C N   
9090  C CA  . ILE C 113 ? 0.7886 1.0746 1.1255 0.0382  -0.2251 0.1126  113 ILE C CA  
9091  C C   . ILE C 113 ? 0.7035 1.0040 1.0775 0.0571  -0.2045 0.1247  113 ILE C C   
9092  O O   . ILE C 113 ? 0.6430 0.9433 1.0354 0.0556  -0.1823 0.1238  113 ILE C O   
9093  C CB  . ILE C 113 ? 0.6971 0.9349 0.9729 0.0414  -0.2173 0.1042  113 ILE C CB  
9094  C CG1 . ILE C 113 ? 0.6353 0.8605 0.8756 0.0247  -0.2374 0.0929  113 ILE C CG1 
9095  C CG2 . ILE C 113 ? 0.5810 0.7924 0.8454 0.0412  -0.1897 0.0986  113 ILE C CG2 
9096  C CD1 . ILE C 113 ? 0.6445 0.8250 0.8305 0.0243  -0.2276 0.0832  113 ILE C CD1 
9097  N N   . ARG C 114 ? 0.5914 0.9033 0.9759 0.0756  -0.2106 0.1363  114 ARG C N   
9098  C CA  . ARG C 114 ? 0.5679 0.8909 0.9858 0.0959  -0.1901 0.1476  114 ARG C CA  
9099  C C   . ARG C 114 ? 0.6358 1.0046 1.1189 0.0917  -0.1866 0.1542  114 ARG C C   
9100  O O   . ARG C 114 ? 0.6398 1.0129 1.1485 0.1023  -0.1608 0.1589  114 ARG C O   
9101  C CB  . ARG C 114 ? 0.6569 0.9825 1.0734 0.1163  -0.2002 0.1593  114 ARG C CB  
9102  C CG  . ARG C 114 ? 0.6368 0.9207 1.0162 0.1342  -0.1800 0.1594  114 ARG C CG  
9103  C CD  . ARG C 114 ? 0.6098 0.8504 0.9257 0.1247  -0.1836 0.1475  114 ARG C CD  
9104  N NE  . ARG C 114 ? 0.7123 0.9165 0.9943 0.1415  -0.1715 0.1495  114 ARG C NE  
9105  C CZ  . ARG C 114 ? 0.7897 0.9830 1.0496 0.1501  -0.1854 0.1553  114 ARG C CZ  
9106  N NH1 . ARG C 114 ? 0.7173 0.9328 0.9821 0.1444  -0.2123 0.1599  114 ARG C NH1 
9107  N NH2 . ARG C 114 ? 0.8216 0.9798 1.0524 0.1642  -0.1721 0.1565  114 ARG C NH2 
9108  N N   . GLU C 115 ? 0.5445 0.9475 1.0549 0.0759  -0.2115 0.1545  115 GLU C N   
9109  C CA  . GLU C 115 ? 0.4790 0.9306 1.0566 0.0707  -0.2117 0.1620  115 GLU C CA  
9110  C C   . GLU C 115 ? 0.5679 1.0207 1.1551 0.0477  -0.2034 0.1523  115 GLU C C   
9111  O O   . GLU C 115 ? 0.6574 1.1365 1.2933 0.0469  -0.1871 0.1579  115 GLU C O   
9112  C CB  . GLU C 115 ? 0.6336 1.1267 1.2422 0.0667  -0.2460 0.1696  115 GLU C CB  
9113  C CG  . GLU C 115 ? 0.5670 1.0434 1.1289 0.0512  -0.2745 0.1597  115 GLU C CG  
9114  C CD  . GLU C 115 ? 0.7500 1.2500 1.3191 0.0591  -0.3045 0.1701  115 GLU C CD  
9115  O OE1 . GLU C 115 ? 0.7719 1.2608 1.3290 0.0814  -0.3005 0.1796  115 GLU C OE1 
9116  O OE2 . GLU C 115 ? 0.6945 1.2230 1.2805 0.0428  -0.3325 0.1690  115 GLU C OE2 
9117  N N   . LEU C 116 ? 0.6101 1.0347 1.1529 0.0293  -0.2133 0.1383  116 LEU C N   
9118  C CA  . LEU C 116 ? 0.6718 1.0929 1.2208 0.0075  -0.2054 0.1290  116 LEU C CA  
9119  C C   . LEU C 116 ? 0.6149 1.0150 1.1612 0.0143  -0.1695 0.1293  116 LEU C C   
9120  O O   . LEU C 116 ? 0.5349 0.9457 1.1086 0.0012  -0.1572 0.1282  116 LEU C O   
9121  C CB  . LEU C 116 ? 0.6677 1.0561 1.1638 -0.0099 -0.2205 0.1138  116 LEU C CB  
9122  C CG  . LEU C 116 ? 0.5809 0.9913 1.0932 -0.0342 -0.2471 0.1071  116 LEU C CG  
9123  C CD1 . LEU C 116 ? 0.4866 0.9402 1.0342 -0.0305 -0.2737 0.1170  116 LEU C CD1 
9124  C CD2 . LEU C 116 ? 0.4860 0.8581 0.9390 -0.0467 -0.2589 0.0917  116 LEU C CD2 
9125  N N   . MET C 117 ? 0.6023 0.9716 1.1149 0.0339  -0.1527 0.1307  117 MET C N   
9126  C CA  . MET C 117 ? 0.5663 0.9114 1.0684 0.0414  -0.1194 0.1303  117 MET C CA  
9127  C C   . MET C 117 ? 0.5369 0.9138 1.0936 0.0540  -0.0987 0.1426  117 MET C C   
9128  O O   . MET C 117 ? 0.5762 0.9367 1.1284 0.0587  -0.0696 0.1428  117 MET C O   
9129  C CB  . MET C 117 ? 0.6592 0.9593 1.1047 0.0569  -0.1103 0.1266  117 MET C CB  
9130  C CG  . MET C 117 ? 0.6413 0.9021 1.0321 0.0433  -0.1157 0.1133  117 MET C CG  
9131  S SD  . MET C 117 ? 0.8637 1.1109 1.2551 0.0280  -0.0931 0.1077  117 MET C SD  
9132  C CE  . MET C 117 ? 0.4626 0.6743 0.8008 0.0105  -0.1087 0.0928  117 MET C CE  
9133  N N   . ASN C 118 ? 0.5415 0.9633 1.1492 0.0600  -0.1127 0.1532  118 ASN C N   
9134  C CA  . ASN C 118 ? 0.6077 1.0643 1.2734 0.0729  -0.0932 0.1657  118 ASN C CA  
9135  C C   . ASN C 118 ? 0.4710 0.9695 1.1946 0.0541  -0.0941 0.1689  118 ASN C C   
9136  O O   . ASN C 118 ? 0.4679 0.9846 1.2306 0.0596  -0.0681 0.1762  118 ASN C O   
9137  C CB  . ASN C 118 ? 0.5765 1.0592 1.2692 0.0938  -0.1058 0.1777  118 ASN C CB  
9138  C CG  . ASN C 118 ? 0.7044 1.1456 1.3412 0.1111  -0.1070 0.1752  118 ASN C CG  
9139  O OD1 . ASN C 118 ? 0.6444 1.0411 1.2337 0.1152  -0.0872 0.1677  118 ASN C OD1 
9140  N ND2 . ASN C 118 ? 0.4936 0.9492 1.1357 0.1207  -0.1311 0.1821  118 ASN C ND2 
9141  N N   . LYS C 119 ? 0.5324 1.0457 1.2618 0.0317  -0.1224 0.1634  119 LYS C N   
9142  C CA  . LYS C 119 ? 0.4619 1.0096 1.2416 0.0102  -0.1238 0.1646  119 LYS C CA  
9143  C C   . LYS C 119 ? 0.5367 1.0515 1.2911 -0.0032 -0.0997 0.1564  119 LYS C C   
9144  O O   . LYS C 119 ? 0.7180 1.1858 1.4109 -0.0072 -0.0990 0.1452  119 LYS C O   
9145  C CB  . LYS C 119 ? 0.4631 1.0306 1.2500 -0.0107 -0.1623 0.1593  119 LYS C CB  
9146  C CG  . LYS C 119 ? 0.4651 1.0708 1.2824 0.0002  -0.1892 0.1691  119 LYS C CG  
9147  C CD  . LYS C 119 ? 0.4843 1.0606 1.2425 0.0029  -0.2141 0.1618  119 LYS C CD  
9148  C CE  . LYS C 119 ? 0.4757 1.0919 1.2620 0.0011  -0.2506 0.1684  119 LYS C CE  
9149  N NZ  . LYS C 119 ? 0.4834 1.0720 1.2112 -0.0075 -0.2779 0.1577  119 LYS C NZ  
9150  N N   . GLU C 120 ? 0.6925 1.2329 1.4957 -0.0099 -0.0793 0.1630  120 GLU C N   
9151  C CA  . GLU C 120 ? 0.8202 1.3303 1.6018 -0.0211 -0.0537 0.1578  120 GLU C CA  
9152  C C   . GLU C 120 ? 0.8489 1.3490 1.6191 -0.0506 -0.0712 0.1472  120 GLU C C   
9153  O O   . GLU C 120 ? 0.8807 1.3394 1.6080 -0.0589 -0.0583 0.1393  120 GLU C O   
9154  C CB  . GLU C 120 ? 0.6666 1.2058 1.5027 -0.0171 -0.0228 0.1696  120 GLU C CB  
9155  C CG  . GLU C 120 ? 0.7340 1.2739 1.5743 0.0132  0.0016  0.1785  120 GLU C CG  
9156  C CD  . GLU C 120 ? 0.7672 1.2481 1.5344 0.0265  0.0199  0.1711  120 GLU C CD  
9157  O OE1 . GLU C 120 ? 0.7314 1.1874 1.4549 0.0360  0.0032  0.1653  120 GLU C OE1 
9158  O OE2 . GLU C 120 ? 0.6167 1.0763 1.3699 0.0270  0.0507  0.1714  120 GLU C OE2 
9159  N N   . LYS C 121 ? 0.8051 1.3410 1.6118 -0.0665 -0.1007 0.1468  121 LYS C N   
9160  C CA  . LYS C 121 ? 0.7078 1.2353 1.5066 -0.0952 -0.1189 0.1359  121 LYS C CA  
9161  C C   . LYS C 121 ? 0.6869 1.2125 1.4600 -0.0997 -0.1565 0.1274  121 LYS C C   
9162  O O   . LYS C 121 ? 0.6770 1.2312 1.4692 -0.0871 -0.1736 0.1340  121 LYS C O   
9163  C CB  . LYS C 121 ? 0.5812 1.1539 1.4518 -0.1149 -0.1170 0.1428  121 LYS C CB  
9164  C CG  . LYS C 121 ? 0.5716 1.1411 1.4461 -0.1476 -0.1355 0.1325  121 LYS C CG  
9165  C CD  . LYS C 121 ? 0.5676 1.1445 1.4307 -0.1594 -0.1770 0.1229  121 LYS C CD  
9166  C CE  . LYS C 121 ? 0.5829 1.1519 1.4480 -0.1914 -0.1916 0.1116  121 LYS C CE  
9167  N NZ  . LYS C 121 ? 0.5156 1.1071 1.3885 -0.2041 -0.2320 0.1052  121 LYS C NZ  
9168  N N   . LEU C 122 ? 0.8334 1.3234 1.5610 -0.1167 -0.1685 0.1130  122 LEU C N   
9169  C CA  . LEU C 122 ? 0.8898 1.3714 1.5847 -0.1227 -0.2018 0.1029  122 LEU C CA  
9170  C C   . LEU C 122 ? 0.7944 1.2837 1.5035 -0.1529 -0.2224 0.0932  122 LEU C C   
9171  O O   . LEU C 122 ? 0.7548 1.2216 1.4571 -0.1686 -0.2090 0.0871  122 LEU C O   
9172  C CB  . LEU C 122 ? 0.7618 1.1889 1.3819 -0.1132 -0.1973 0.0929  122 LEU C CB  
9173  C CG  . LEU C 122 ? 0.7091 1.1295 1.3063 -0.0856 -0.1933 0.0993  122 LEU C CG  
9174  C CD1 . LEU C 122 ? 0.6559 1.0647 1.2554 -0.0683 -0.1581 0.1074  122 LEU C CD1 
9175  C CD2 . LEU C 122 ? 0.7222 1.1013 1.2524 -0.0829 -0.2054 0.0879  122 LEU C CD2 
9176  N N   . ASN C 123 ? 0.7516 1.2711 1.4789 -0.1611 -0.2553 0.0919  123 ASN C N   
9177  C CA  . ASN C 123 ? 0.5862 1.1098 1.3199 -0.1901 -0.2793 0.0806  123 ASN C CA  
9178  C C   . ASN C 123 ? 0.6275 1.1071 1.2911 -0.1947 -0.2963 0.0640  123 ASN C C   
9179  O O   . ASN C 123 ? 0.6511 1.0967 1.2641 -0.1769 -0.2864 0.0618  123 ASN C O   
9180  C CB  . ASN C 123 ? 0.5514 1.1327 1.3439 -0.1984 -0.3068 0.0878  123 ASN C CB  
9181  C CG  . ASN C 123 ? 0.5229 1.1298 1.3228 -0.1735 -0.3172 0.0997  123 ASN C CG  
9182  O OD1 . ASN C 123 ? 0.5207 1.0996 1.2668 -0.1591 -0.3233 0.0958  123 ASN C OD1 
9183  N ND2 . ASN C 123 ? 0.5219 1.1828 1.3904 -0.1685 -0.3189 0.1149  123 ASN C ND2 
9184  N N   . ARG C 124 ? 0.6302 1.1100 1.2906 -0.2191 -0.3216 0.0517  124 ARG C N   
9185  C CA  . ARG C 124 ? 0.6046 1.0415 1.1989 -0.2247 -0.3355 0.0348  124 ARG C CA  
9186  C C   . ARG C 124 ? 0.6600 1.0978 1.2209 -0.2067 -0.3529 0.0365  124 ARG C C   
9187  O O   . ARG C 124 ? 0.6596 1.0574 1.1622 -0.1961 -0.3473 0.0294  124 ARG C O   
9188  C CB  . ARG C 124 ? 0.6077 1.0440 1.2046 -0.2541 -0.3581 0.0205  124 ARG C CB  
9189  C CG  . ARG C 124 ? 0.6094 0.9917 1.1396 -0.2616 -0.3605 0.0014  124 ARG C CG  
9190  C CD  . ARG C 124 ? 0.6691 1.0451 1.1694 -0.2739 -0.3803 -0.0155 124 ARG C CD  
9191  N NE  . ARG C 124 ? 0.6639 0.9911 1.0958 -0.2732 -0.3815 -0.0319 124 ARG C NE  
9192  C CZ  . ARG C 124 ? 0.6966 1.0142 1.0829 -0.2608 -0.3929 -0.0366 124 ARG C CZ  
9193  N NH1 . ARG C 124 ? 0.6694 1.0204 1.0677 -0.2485 -0.4061 -0.0267 124 ARG C NH1 
9194  N NH2 . ARG C 124 ? 0.7526 1.0256 1.0802 -0.2600 -0.3894 -0.0510 124 ARG C NH2 
9195  N N   . GLU C 125 ? 0.6695 1.1530 1.2673 -0.2028 -0.3739 0.0466  125 GLU C N   
9196  C CA  . GLU C 125 ? 0.6597 1.1406 1.2204 -0.1847 -0.3880 0.0484  125 GLU C CA  
9197  C C   . GLU C 125 ? 0.5732 1.0435 1.1225 -0.1573 -0.3681 0.0603  125 GLU C C   
9198  O O   . GLU C 125 ? 0.5522 1.0023 1.0554 -0.1437 -0.3747 0.0591  125 GLU C O   
9199  C CB  . GLU C 125 ? 0.7263 1.2491 1.3161 -0.1822 -0.4054 0.0541  125 GLU C CB  
9200  C CG  . GLU C 125 ? 0.7729 1.3436 1.4385 -0.1784 -0.3962 0.0705  125 GLU C CG  
9201  C CD  . GLU C 125 ? 0.7730 1.3715 1.4580 -0.1521 -0.3979 0.0876  125 GLU C CD  
9202  O OE1 . GLU C 125 ? 0.8364 1.4177 1.4754 -0.1388 -0.4088 0.0866  125 GLU C OE1 
9203  O OE2 . GLU C 125 ? 0.5764 1.2129 1.3223 -0.1444 -0.3870 0.1021  125 GLU C OE2 
9204  N N   . GLU C 126 ? 0.5962 1.0759 1.1810 -0.1476 -0.3398 0.0706  126 GLU C N   
9205  C CA  . GLU C 126 ? 0.5158 0.9761 1.0802 -0.1213 -0.3150 0.0786  126 GLU C CA  
9206  C C   . GLU C 126 ? 0.5130 0.9176 1.0171 -0.1205 -0.2971 0.0667  126 GLU C C   
9207  O O   . GLU C 126 ? 0.6265 1.0050 1.0880 -0.1034 -0.2917 0.0669  126 GLU C O   
9208  C CB  . GLU C 126 ? 0.5315 1.0189 1.1512 -0.1110 -0.2900 0.0928  126 GLU C CB  
9209  C CG  . GLU C 126 ? 0.7177 1.2430 1.3736 -0.0899 -0.2951 0.1093  126 GLU C CG  
9210  C CD  . GLU C 126 ? 0.6544 1.2291 1.3873 -0.0914 -0.2867 0.1221  126 GLU C CD  
9211  O OE1 . GLU C 126 ? 0.4907 1.0649 1.2452 -0.1052 -0.2690 0.1195  126 GLU C OE1 
9212  O OE2 . GLU C 126 ? 0.4923 1.1069 1.2653 -0.0783 -0.2975 0.1354  126 GLU C OE2 
9213  N N   . LEU C 127 ? 0.5173 0.9031 1.0182 -0.1391 -0.2881 0.0567  127 LEU C N   
9214  C CA  . LEU C 127 ? 0.5747 0.9095 1.0235 -0.1378 -0.2700 0.0469  127 LEU C CA  
9215  C C   . LEU C 127 ? 0.5846 0.8893 0.9748 -0.1376 -0.2866 0.0350  127 LEU C C   
9216  O O   . LEU C 127 ? 0.6265 0.8942 0.9720 -0.1269 -0.2728 0.0311  127 LEU C O   
9217  C CB  . LEU C 127 ? 0.5751 0.8969 1.0344 -0.1587 -0.2598 0.0393  127 LEU C CB  
9218  C CG  . LEU C 127 ? 0.6015 0.9389 1.1058 -0.1583 -0.2341 0.0502  127 LEU C CG  
9219  C CD1 . LEU C 127 ? 0.7079 1.0369 1.2266 -0.1832 -0.2309 0.0429  127 LEU C CD1 
9220  C CD2 . LEU C 127 ? 0.5006 0.8101 0.9783 -0.1378 -0.2050 0.0555  127 LEU C CD2 
9221  N N   . LEU C 128 ? 0.6404 0.9605 1.0296 -0.1497 -0.3159 0.0292  128 LEU C N   
9222  C CA  . LEU C 128 ? 0.6015 0.8926 0.9335 -0.1508 -0.3307 0.0172  128 LEU C CA  
9223  C C   . LEU C 128 ? 0.5500 0.8327 0.8529 -0.1271 -0.3275 0.0250  128 LEU C C   
9224  O O   . LEU C 128 ? 0.5472 0.7940 0.7987 -0.1219 -0.3234 0.0173  128 LEU C O   
9225  C CB  . LEU C 128 ? 0.5779 0.8895 0.9155 -0.1687 -0.3633 0.0102  128 LEU C CB  
9226  C CG  . LEU C 128 ? 0.5986 0.8817 0.9098 -0.1913 -0.3697 -0.0089 128 LEU C CG  
9227  C CD1 . LEU C 128 ? 0.6307 0.9176 0.9170 -0.1992 -0.3913 -0.0196 128 LEU C CD1 
9228  C CD2 . LEU C 128 ? 0.5945 0.8280 0.8528 -0.1842 -0.3505 -0.0180 128 LEU C CD2 
9229  N N   . ASP C 129 ? 0.5451 0.8602 0.8817 -0.1122 -0.3288 0.0406  129 ASP C N   
9230  C CA  . ASP C 129 ? 0.5285 0.8336 0.8407 -0.0890 -0.3231 0.0491  129 ASP C CA  
9231  C C   . ASP C 129 ? 0.5120 0.7861 0.8066 -0.0764 -0.2921 0.0501  129 ASP C C   
9232  O O   . ASP C 129 ? 0.5100 0.7546 0.7610 -0.0649 -0.2862 0.0483  129 ASP C O   
9233  C CB  . ASP C 129 ? 0.5991 0.9463 0.9548 -0.0760 -0.3321 0.0659  129 ASP C CB  
9234  C CG  . ASP C 129 ? 0.6935 1.0758 1.0726 -0.0896 -0.3643 0.0661  129 ASP C CG  
9235  O OD1 . ASP C 129 ? 0.7435 1.1265 1.1259 -0.1121 -0.3747 0.0545  129 ASP C OD1 
9236  O OD2 . ASP C 129 ? 0.7141 1.1221 1.1070 -0.0780 -0.3801 0.0779  129 ASP C OD2 
9237  N N   . LEU C 130 ? 0.5479 0.8279 0.8750 -0.0791 -0.2722 0.0531  130 LEU C N   
9238  C CA  . LEU C 130 ? 0.4907 0.7395 0.7980 -0.0691 -0.2437 0.0532  130 LEU C CA  
9239  C C   . LEU C 130 ? 0.4948 0.7009 0.7509 -0.0771 -0.2411 0.0390  130 LEU C C   
9240  O O   . LEU C 130 ? 0.4932 0.6690 0.7145 -0.0653 -0.2270 0.0382  130 LEU C O   
9241  C CB  . LEU C 130 ? 0.4845 0.7473 0.8344 -0.0733 -0.2238 0.0586  130 LEU C CB  
9242  C CG  . LEU C 130 ? 0.4746 0.7182 0.8175 -0.0576 -0.1936 0.0646  130 LEU C CG  
9243  C CD1 . LEU C 130 ? 0.4695 0.7285 0.8249 -0.0351 -0.1890 0.0770  130 LEU C CD1 
9244  C CD2 . LEU C 130 ? 0.5084 0.7605 0.8855 -0.0668 -0.1745 0.0674  130 LEU C CD2 
9245  N N   . GLN C 131 ? 0.5070 0.7101 0.7592 -0.0972 -0.2546 0.0276  131 GLN C N   
9246  C CA  . GLN C 131 ? 0.5570 0.7205 0.7626 -0.1044 -0.2529 0.0137  131 GLN C CA  
9247  C C   . GLN C 131 ? 0.5193 0.6677 0.6809 -0.0964 -0.2652 0.0097  131 GLN C C   
9248  O O   . GLN C 131 ? 0.5160 0.6317 0.6387 -0.0898 -0.2546 0.0049  131 GLN C O   
9249  C CB  . GLN C 131 ? 0.5876 0.7511 0.8019 -0.1280 -0.2641 0.0021  131 GLN C CB  
9250  C CG  . GLN C 131 ? 0.5269 0.6789 0.7587 -0.1372 -0.2449 0.0010  131 GLN C CG  
9251  C CD  . GLN C 131 ? 0.5778 0.7292 0.8203 -0.1613 -0.2567 -0.0102 131 GLN C CD  
9252  O OE1 . GLN C 131 ? 0.6536 0.8203 0.8985 -0.1720 -0.2804 -0.0162 131 GLN C OE1 
9253  N NE2 . GLN C 131 ? 0.7169 0.8490 0.9644 -0.1703 -0.2405 -0.0129 131 GLN C NE2 
9254  N N   . THR C 132 ? 0.5716 0.7443 0.7392 -0.0971 -0.2878 0.0123  132 THR C N   
9255  C CA  . THR C 132 ? 0.5762 0.7345 0.7001 -0.0921 -0.3008 0.0082  132 THR C CA  
9256  C C   . THR C 132 ? 0.5560 0.7094 0.6668 -0.0703 -0.2919 0.0195  132 THR C C   
9257  O O   . THR C 132 ? 0.6026 0.7287 0.6709 -0.0641 -0.2886 0.0155  132 THR C O   
9258  C CB  . THR C 132 ? 0.6100 0.7940 0.7408 -0.1021 -0.3297 0.0068  132 THR C CB  
9259  O OG1 . THR C 132 ? 0.5696 0.7661 0.7271 -0.1225 -0.3378 -0.0009 132 THR C OG1 
9260  C CG2 . THR C 132 ? 0.5785 0.7399 0.6562 -0.1035 -0.3421 -0.0026 132 THR C CG2 
9261  N N   . LEU C 133 ? 0.5189 0.6980 0.6662 -0.0585 -0.2878 0.0337  133 LEU C N   
9262  C CA  . LEU C 133 ? 0.5120 0.6847 0.6471 -0.0377 -0.2799 0.0444  133 LEU C CA  
9263  C C   . LEU C 133 ? 0.5492 0.6864 0.6573 -0.0300 -0.2560 0.0413  133 LEU C C   
9264  O O   . LEU C 133 ? 0.5670 0.6859 0.6464 -0.0174 -0.2517 0.0444  133 LEU C O   
9265  C CB  . LEU C 133 ? 0.5057 0.7119 0.6882 -0.0260 -0.2780 0.0595  133 LEU C CB  
9266  C CG  . LEU C 133 ? 0.5186 0.7597 0.7224 -0.0275 -0.3045 0.0664  133 LEU C CG  
9267  C CD1 . LEU C 133 ? 0.5628 0.8414 0.8244 -0.0194 -0.3012 0.0800  133 LEU C CD1 
9268  C CD2 . LEU C 133 ? 0.5290 0.7592 0.6974 -0.0156 -0.3156 0.0713  133 LEU C CD2 
9269  N N   . ASN C 134 ? 0.5109 0.6381 0.6280 -0.0379 -0.2408 0.0358  134 ASN C N   
9270  C CA  . ASN C 134 ? 0.5398 0.6317 0.6268 -0.0332 -0.2216 0.0313  134 ASN C CA  
9271  C C   . ASN C 134 ? 0.5701 0.6355 0.6120 -0.0384 -0.2287 0.0204  134 ASN C C   
9272  O O   . ASN C 134 ? 0.6036 0.6446 0.6152 -0.0291 -0.2198 0.0202  134 ASN C O   
9273  C CB  . ASN C 134 ? 0.5148 0.6016 0.6195 -0.0419 -0.2061 0.0282  134 ASN C CB  
9274  C CG  . ASN C 134 ? 0.4733 0.5777 0.6143 -0.0329 -0.1907 0.0396  134 ASN C CG  
9275  O OD1 . ASN C 134 ? 0.5250 0.6502 0.6848 -0.0211 -0.1937 0.0495  134 ASN C OD1 
9276  N ND2 . ASN C 134 ? 0.4706 0.5659 0.6210 -0.0379 -0.1735 0.0386  134 ASN C ND2 
9277  N N   . LEU C 135 ? 0.5379 0.6075 0.5752 -0.0534 -0.2445 0.0108  135 LEU C N   
9278  C CA  . LEU C 135 ? 0.5355 0.5807 0.5303 -0.0582 -0.2504 -0.0003 135 LEU C CA  
9279  C C   . LEU C 135 ? 0.5219 0.5655 0.4914 -0.0472 -0.2585 0.0049  135 LEU C C   
9280  O O   . LEU C 135 ? 0.5211 0.5400 0.4572 -0.0416 -0.2512 0.0020  135 LEU C O   
9281  C CB  . LEU C 135 ? 0.6273 0.6780 0.6226 -0.0765 -0.2663 -0.0118 135 LEU C CB  
9282  C CG  . LEU C 135 ? 0.5386 0.5668 0.5261 -0.0893 -0.2585 -0.0246 135 LEU C CG  
9283  C CD1 . LEU C 135 ? 0.5582 0.5979 0.5557 -0.1077 -0.2759 -0.0342 135 LEU C CD1 
9284  C CD2 . LEU C 135 ? 0.6083 0.6036 0.5527 -0.0856 -0.2513 -0.0330 135 LEU C CD2 
9285  N N   . LEU C 136 ? 0.5285 0.5991 0.5147 -0.0440 -0.2738 0.0135  136 LEU C N   
9286  C CA  . LEU C 136 ? 0.5376 0.6067 0.4994 -0.0341 -0.2830 0.0198  136 LEU C CA  
9287  C C   . LEU C 136 ? 0.5784 0.6355 0.5353 -0.0166 -0.2674 0.0300  136 LEU C C   
9288  O O   . LEU C 136 ? 0.5323 0.5787 0.4620 -0.0087 -0.2704 0.0340  136 LEU C O   
9289  C CB  . LEU C 136 ? 0.6014 0.7034 0.5845 -0.0346 -0.3046 0.0279  136 LEU C CB  
9290  C CG  . LEU C 136 ? 0.6286 0.7499 0.6267 -0.0524 -0.3229 0.0198  136 LEU C CG  
9291  C CD1 . LEU C 136 ? 0.5768 0.7376 0.6162 -0.0499 -0.3386 0.0320  136 LEU C CD1 
9292  C CD2 . LEU C 136 ? 0.5880 0.6948 0.5436 -0.0615 -0.3341 0.0082  136 LEU C CD2 
9293  N N   . ALA C 137 ? 0.5694 0.6266 0.5503 -0.0109 -0.2506 0.0341  137 ALA C N   
9294  C CA  . ALA C 137 ? 0.5202 0.5650 0.4965 0.0054  -0.2361 0.0430  137 ALA C CA  
9295  C C   . ALA C 137 ? 0.5218 0.5333 0.4573 0.0073  -0.2273 0.0372  137 ALA C C   
9296  O O   . ALA C 137 ? 0.6193 0.6193 0.5387 0.0186  -0.2238 0.0439  137 ALA C O   
9297  C CB  . ALA C 137 ? 0.5986 0.6481 0.6052 0.0097  -0.2189 0.0467  137 ALA C CB  
9298  N N   . TRP C 138 ? 0.5830 0.5787 0.5029 -0.0038 -0.2236 0.0253  138 TRP C N   
9299  C CA  . TRP C 138 ? 0.6165 0.5831 0.5026 -0.0028 -0.2147 0.0195  138 TRP C CA  
9300  C C   . TRP C 138 ? 0.6894 0.6496 0.5454 -0.0086 -0.2262 0.0132  138 TRP C C   
9301  O O   . TRP C 138 ? 0.6970 0.6374 0.5303 -0.0133 -0.2207 0.0042  138 TRP C O   
9302  C CB  . TRP C 138 ? 0.5898 0.5415 0.4772 -0.0093 -0.2021 0.0113  138 TRP C CB  
9303  C CG  . TRP C 138 ? 0.6740 0.6306 0.5877 -0.0048 -0.1895 0.0170  138 TRP C CG  
9304  C CD1 . TRP C 138 ? 0.7034 0.6822 0.6510 -0.0087 -0.1908 0.0199  138 TRP C CD1 
9305  C CD2 . TRP C 138 ? 0.6579 0.5967 0.5654 0.0041  -0.1733 0.0205  138 TRP C CD2 
9306  N NE1 . TRP C 138 ? 0.7365 0.7122 0.6987 -0.0022 -0.1746 0.0252  138 TRP C NE1 
9307  C CE2 . TRP C 138 ? 0.7316 0.6817 0.6675 0.0058  -0.1641 0.0253  138 TRP C CE2 
9308  C CE3 . TRP C 138 ? 0.6620 0.5765 0.5424 0.0101  -0.1658 0.0200  138 TRP C CE3 
9309  C CZ2 . TRP C 138 ? 0.6792 0.6151 0.6133 0.0138  -0.1475 0.0290  138 TRP C CZ2 
9310  C CZ3 . TRP C 138 ? 0.7349 0.6360 0.6148 0.0173  -0.1513 0.0235  138 TRP C CZ3 
9311  C CH2 . TRP C 138 ? 0.6687 0.5794 0.5733 0.0193  -0.1421 0.0277  138 TRP C CH2 
9312  N N   . CYS C 139 ? 0.5515 0.5281 0.4066 -0.0079 -0.2418 0.0182  139 CYS C N   
9313  C CA  . CYS C 139 ? 0.5842 0.5550 0.4079 -0.0136 -0.2528 0.0125  139 CYS C CA  
9314  C C   . CYS C 139 ? 0.6228 0.5756 0.4189 -0.0047 -0.2450 0.0174  139 CYS C C   
9315  O O   . CYS C 139 ? 0.6867 0.6410 0.4871 0.0066  -0.2444 0.0295  139 CYS C O   
9316  C CB  . CYS C 139 ? 0.6608 0.6566 0.4932 -0.0166 -0.2720 0.0166  139 CYS C CB  
9317  S SG  . CYS C 139 ? 0.8141 0.8090 0.6192 -0.0271 -0.2733 0.0045  139 CYS C SG  
9318  N N   . GLY C 140 ? 0.6693 0.6066 0.4421 -0.0095 -0.2349 0.0081  140 GLY C N   
9319  C CA  . GLY C 140 ? 0.6378 0.5599 0.3909 -0.0032 -0.2226 0.0115  140 GLY C CA  
9320  C C   . GLY C 140 ? 0.7671 0.6976 0.5076 -0.0007 -0.2257 0.0175  140 GLY C C   
9321  O O   . GLY C 140 ? 0.8230 0.7718 0.5691 -0.0026 -0.2379 0.0198  140 GLY C O   
9322  N N   . ARG C 141 ? 0.7185 0.6356 0.4419 0.0032  -0.2147 0.0204  141 ARG C N   
9323  C CA  . ARG C 141 ? 0.7248 0.6468 0.4343 0.0063  -0.2164 0.0279  141 ARG C CA  
9324  C C   . ARG C 141 ? 0.6431 0.5741 0.3384 -0.0016 -0.2222 0.0203  141 ARG C C   
9325  O O   . ARG C 141 ? 0.6348 0.5793 0.3263 -0.0003 -0.2317 0.0264  141 ARG C O   
9326  C CB  . ARG C 141 ? 0.6511 0.5556 0.3458 0.0100  -0.2031 0.0315  141 ARG C CB  
9327  C CG  . ARG C 141 ? 0.6549 0.5615 0.3403 0.0160  -0.2044 0.0438  141 ARG C CG  
9328  C CD  . ARG C 141 ? 0.5964 0.4858 0.2666 0.0169  -0.1916 0.0460  141 ARG C CD  
9329  N NE  . ARG C 141 ? 0.6085 0.4955 0.2586 0.0101  -0.1873 0.0383  141 ARG C NE  
9330  C CZ  . ARG C 141 ? 0.7139 0.5967 0.3447 0.0103  -0.1832 0.0435  141 ARG C CZ  
9331  N NH1 . ARG C 141 ? 0.8213 0.7009 0.4506 0.0164  -0.1830 0.0566  141 ARG C NH1 
9332  N NH2 . ARG C 141 ? 0.7699 0.6506 0.3820 0.0044  -0.1789 0.0356  141 ARG C NH2 
9333  N N   . THR C 142 ? 0.7460 0.6689 0.4324 -0.0094 -0.2166 0.0071  142 THR C N   
9334  C CA  . THR C 142 ? 0.7954 0.7227 0.4642 -0.0165 -0.2202 -0.0016 142 THR C CA  
9335  C C   . THR C 142 ? 0.7842 0.7289 0.4648 -0.0224 -0.2354 -0.0056 142 THR C C   
9336  O O   . THR C 142 ? 0.8649 0.8209 0.5346 -0.0245 -0.2444 -0.0052 142 THR C O   
9337  C CB  . THR C 142 ? 0.8629 0.7745 0.5195 -0.0218 -0.2087 -0.0145 142 THR C CB  
9338  O OG1 . THR C 142 ? 0.9020 0.8031 0.5396 -0.0184 -0.1978 -0.0113 142 THR C OG1 
9339  C CG2 . THR C 142 ? 0.8593 0.7749 0.5059 -0.0307 -0.2142 -0.0275 142 THR C CG2 
9340  N N   . LEU C 143 ? 0.7496 0.6969 0.4524 -0.0254 -0.2391 -0.0092 143 LEU C N   
9341  C CA  . LEU C 143 ? 0.8427 0.8072 0.5601 -0.0327 -0.2538 -0.0134 143 LEU C CA  
9342  C C   . LEU C 143 ? 0.8242 0.8102 0.5593 -0.0269 -0.2673 -0.0001 143 LEU C C   
9343  O O   . LEU C 143 ? 0.7660 0.7703 0.5113 -0.0326 -0.2815 -0.0019 143 LEU C O   
9344  C CB  . LEU C 143 ? 0.8410 0.8004 0.5771 -0.0389 -0.2529 -0.0215 143 LEU C CB  
9345  C CG  . LEU C 143 ? 0.8570 0.7975 0.5780 -0.0458 -0.2424 -0.0363 143 LEU C CG  
9346  C CD1 . LEU C 143 ? 0.7875 0.7209 0.5271 -0.0508 -0.2409 -0.0420 143 LEU C CD1 
9347  C CD2 . LEU C 143 ? 0.7638 0.7082 0.4687 -0.0543 -0.2480 -0.0469 143 LEU C CD2 
9348  N N   . ARG C 144 ? 0.8434 0.8274 0.5836 -0.0156 -0.2632 0.0133  144 ARG C N   
9349  C CA  . ARG C 144 ? 0.7774 0.7808 0.5320 -0.0080 -0.2749 0.0271  144 ARG C CA  
9350  C C   . ARG C 144 ? 0.7801 0.7923 0.5145 -0.0086 -0.2819 0.0292  144 ARG C C   
9351  O O   . ARG C 144 ? 0.8733 0.9071 0.6193 -0.0084 -0.2969 0.0341  144 ARG C O   
9352  C CB  . ARG C 144 ? 0.8012 0.7961 0.5617 0.0049  -0.2670 0.0403  144 ARG C CB  
9353  C CG  . ARG C 144 ? 0.8264 0.8240 0.6159 0.0093  -0.2681 0.0442  144 ARG C CG  
9354  C CD  . ARG C 144 ? 0.8772 0.8540 0.6615 0.0191  -0.2543 0.0504  144 ARG C CD  
9355  N NE  . ARG C 144 ? 0.8411 0.8173 0.6492 0.0245  -0.2542 0.0539  144 ARG C NE  
9356  C CZ  . ARG C 144 ? 0.7314 0.7150 0.5592 0.0368  -0.2574 0.0669  144 ARG C CZ  
9357  N NH1 . ARG C 144 ? 0.5767 0.5688 0.4043 0.0449  -0.2613 0.0781  144 ARG C NH1 
9358  N NH2 . ARG C 144 ? 0.7472 0.7317 0.6001 0.0411  -0.2483 0.0675  144 ARG C NH2 
9359  N N   . LYS C 145 ? 0.7529 0.7493 0.4575 -0.0092 -0.2714 0.0258  145 LYS C N   
9360  C CA  . LYS C 145 ? 0.7145 0.7166 0.3954 -0.0105 -0.2771 0.0267  145 LYS C CA  
9361  C C   . LYS C 145 ? 0.8612 0.8715 0.5355 -0.0220 -0.2867 0.0128  145 LYS C C   
9362  O O   . LYS C 145 ? 0.9638 0.9830 0.6213 -0.0234 -0.2958 0.0134  145 LYS C O   
9363  C CB  . LYS C 145 ? 0.7004 0.6831 0.3526 -0.0086 -0.2624 0.0267  145 LYS C CB  
9364  C CG  . LYS C 145 ? 0.6928 0.6685 0.3461 0.0023  -0.2555 0.0420  145 LYS C CG  
9365  C CD  . LYS C 145 ? 0.8437 0.7969 0.4862 0.0024  -0.2376 0.0388  145 LYS C CD  
9366  C CE  . LYS C 145 ? 0.9995 0.9440 0.6106 -0.0005 -0.2308 0.0362  145 LYS C CE  
9367  N NZ  . LYS C 145 ? 0.9450 0.8698 0.5484 -0.0007 -0.2142 0.0332  145 LYS C NZ  
9368  N N   . ASP C 146 ? 0.9150 0.9212 0.6011 -0.0302 -0.2849 0.0005  146 ASP C N   
9369  C CA  . ASP C 146 ? 0.9056 0.9155 0.5857 -0.0422 -0.2923 -0.0143 146 ASP C CA  
9370  C C   . ASP C 146 ? 0.7212 0.7539 0.4304 -0.0473 -0.3097 -0.0138 146 ASP C C   
9371  O O   . ASP C 146 ? 0.7477 0.7933 0.4515 -0.0536 -0.3230 -0.0186 146 ASP C O   
9372  C CB  . ASP C 146 ? 1.0459 1.0354 0.7206 -0.0487 -0.2791 -0.0287 146 ASP C CB  
9373  C CG  . ASP C 146 ? 1.1372 1.1109 0.7776 -0.0510 -0.2694 -0.0380 146 ASP C CG  
9374  O OD1 . ASP C 146 ? 1.1705 1.1422 0.7913 -0.0446 -0.2656 -0.0301 146 ASP C OD1 
9375  O OD2 . ASP C 146 ? 1.2260 1.1889 0.8595 -0.0591 -0.2652 -0.0530 146 ASP C OD2 
9376  N N   . LEU C 147 ? 0.7596 0.7979 0.5003 -0.0448 -0.3102 -0.0081 147 LEU C N   
9377  C CA  . LEU C 147 ? 0.8007 0.8625 0.5752 -0.0498 -0.3256 -0.0065 147 LEU C CA  
9378  C C   . LEU C 147 ? 0.8098 0.8932 0.6051 -0.0385 -0.3354 0.0114  147 LEU C C   
9379  O O   . LEU C 147 ? 0.7781 0.8777 0.6095 -0.0368 -0.3416 0.0180  147 LEU C O   
9380  C CB  . LEU C 147 ? 0.8208 0.8764 0.6192 -0.0551 -0.3202 -0.0116 147 LEU C CB  
9381  C CG  . LEU C 147 ? 0.8573 0.8857 0.6365 -0.0616 -0.3057 -0.0261 147 LEU C CG  
9382  C CD1 . LEU C 147 ? 0.7968 0.8158 0.5966 -0.0607 -0.2977 -0.0250 147 LEU C CD1 
9383  C CD2 . LEU C 147 ? 0.6960 0.7242 0.4681 -0.0759 -0.3118 -0.0420 147 LEU C CD2 
9384  N N   . LYS C 148 ? 0.8434 0.9274 0.6177 -0.0300 -0.3364 0.0199  148 LYS C N   
9385  C CA  . LYS C 148 ? 0.8123 0.9128 0.6040 -0.0169 -0.3434 0.0379  148 LYS C CA  
9386  C C   . LYS C 148 ? 0.7317 0.8641 0.5559 -0.0195 -0.3630 0.0417  148 LYS C C   
9387  O O   . LYS C 148 ? 0.7912 0.9399 0.6507 -0.0115 -0.3670 0.0533  148 LYS C O   
9388  C CB  . LYS C 148 ? 0.8421 0.9359 0.6021 -0.0091 -0.3414 0.0454  148 LYS C CB  
9389  C CG  . LYS C 148 ? 0.8078 0.9110 0.5813 0.0065  -0.3442 0.0649  148 LYS C CG  
9390  C CD  . LYS C 148 ? 0.8903 0.9903 0.6930 0.0143  -0.3362 0.0720  148 LYS C CD  
9391  C CE  . LYS C 148 ? 0.7775 0.8474 0.5604 0.0170  -0.3164 0.0702  148 LYS C CE  
9392  N NZ  . LYS C 148 ? 0.8637 0.9291 0.6717 0.0264  -0.3094 0.0782  148 LYS C NZ  
9393  N N   . ASP C 149 ? 0.7786 0.9210 0.5930 -0.0304 -0.3754 0.0319  149 ASP C N   
9394  C CA  . ASP C 149 ? 0.8351 1.0095 0.6812 -0.0338 -0.3951 0.0351  149 ASP C CA  
9395  C C   . ASP C 149 ? 0.7278 0.9141 0.6165 -0.0407 -0.3963 0.0325  149 ASP C C   
9396  O O   . ASP C 149 ? 0.7238 0.9387 0.6525 -0.0375 -0.4077 0.0422  149 ASP C O   
9397  C CB  . ASP C 149 ? 0.8035 0.9828 0.6271 -0.0456 -0.4078 0.0231  149 ASP C CB  
9398  C CG  . ASP C 149 ? 1.0505 1.2418 0.8575 -0.0370 -0.4199 0.0333  149 ASP C CG  
9399  O OD1 . ASP C 149 ? 1.1589 1.3767 0.9958 -0.0299 -0.4335 0.0459  149 ASP C OD1 
9400  O OD2 . ASP C 149 ? 1.1135 1.2881 0.8785 -0.0370 -0.4157 0.0291  149 ASP C OD2 
9401  N N   . LEU C 150 ? 0.7122 0.8779 0.5946 -0.0499 -0.3843 0.0201  150 LEU C N   
9402  C CA  . LEU C 150 ? 0.6883 0.8626 0.6100 -0.0563 -0.3836 0.0187  150 LEU C CA  
9403  C C   . LEU C 150 ? 0.6937 0.8723 0.6422 -0.0418 -0.3766 0.0344  150 LEU C C   
9404  O O   . LEU C 150 ? 0.6457 0.8475 0.6393 -0.0420 -0.3819 0.0412  150 LEU C O   
9405  C CB  . LEU C 150 ? 0.7071 0.8546 0.6117 -0.0683 -0.3717 0.0021  150 LEU C CB  
9406  C CG  . LEU C 150 ? 0.7090 0.8518 0.5947 -0.0842 -0.3777 -0.0154 150 LEU C CG  
9407  C CD1 . LEU C 150 ? 0.7313 0.8537 0.5678 -0.0814 -0.3719 -0.0217 150 LEU C CD1 
9408  C CD2 . LEU C 150 ? 0.6981 0.8257 0.5920 -0.0971 -0.3699 -0.0286 150 LEU C CD2 
9409  N N   . LEU C 151 ? 0.7135 0.8702 0.6363 -0.0294 -0.3638 0.0403  151 LEU C N   
9410  C CA  . LEU C 151 ? 0.6307 0.7881 0.5750 -0.0143 -0.3568 0.0549  151 LEU C CA  
9411  C C   . LEU C 151 ? 0.7135 0.9004 0.6868 -0.0023 -0.3682 0.0712  151 LEU C C   
9412  O O   . LEU C 151 ? 0.6409 0.8446 0.6553 0.0054  -0.3683 0.0818  151 LEU C O   
9413  C CB  . LEU C 151 ? 0.6259 0.7514 0.5338 -0.0049 -0.3405 0.0565  151 LEU C CB  
9414  C CG  . LEU C 151 ? 0.7210 0.8173 0.6110 -0.0109 -0.3256 0.0451  151 LEU C CG  
9415  C CD1 . LEU C 151 ? 0.6562 0.7270 0.5010 -0.0107 -0.3145 0.0391  151 LEU C CD1 
9416  C CD2 . LEU C 151 ? 0.6441 0.7324 0.5529 -0.0006 -0.3165 0.0535  151 LEU C CD2 
9417  N N   . ASN C 152 ? 0.6827 0.8762 0.6359 0.0002  -0.3774 0.0738  152 ASN C N   
9418  C CA  . ASN C 152 ? 0.7704 0.9915 0.7494 0.0122  -0.3893 0.0891  152 ASN C CA  
9419  C C   . ASN C 152 ? 0.8251 1.0823 0.8516 0.0049  -0.4039 0.0895  152 ASN C C   
9420  O O   . ASN C 152 ? 0.6769 0.9601 0.7393 0.0164  -0.4108 0.1035  152 ASN C O   
9421  C CB  . ASN C 152 ? 0.7234 0.9428 0.6676 0.0151  -0.3973 0.0910  152 ASN C CB  
9422  C CG  . ASN C 152 ? 0.7993 0.9897 0.7063 0.0257  -0.3831 0.0964  152 ASN C CG  
9423  O OD1 . ASN C 152 ? 0.7743 0.9422 0.6417 0.0185  -0.3756 0.0864  152 ASN C OD1 
9424  N ND2 . ASN C 152 ? 0.8404 1.0312 0.7617 0.0429  -0.3783 0.1123  152 ASN C ND2 
9425  N N   . LYS C 153 ? 0.8944 1.1536 0.9231 -0.0139 -0.4080 0.0744  153 LYS C N   
9426  C CA  . LYS C 153 ? 0.6784 0.9715 0.7527 -0.0237 -0.4213 0.0736  153 LYS C CA  
9427  C C   . LYS C 153 ? 0.7835 1.0972 0.9125 -0.0148 -0.4158 0.0865  153 LYS C C   
9428  O O   . LYS C 153 ? 0.7280 1.0736 0.8961 -0.0059 -0.4243 0.0991  153 LYS C O   
9429  C CB  . LYS C 153 ? 0.7185 1.0021 0.7833 -0.0455 -0.4219 0.0545  153 LYS C CB  
9430  C CG  . LYS C 153 ? 0.8197 1.1318 0.9082 -0.0598 -0.4399 0.0485  153 LYS C CG  
9431  C CD  . LYS C 153 ? 0.8085 1.1049 0.8854 -0.0806 -0.4375 0.0291  153 LYS C CD  
9432  C CE  . LYS C 153 ? 0.9430 1.2664 1.0450 -0.0964 -0.4549 0.0223  153 LYS C CE  
9433  N NZ  . LYS C 153 ? 1.0430 1.3530 1.1471 -0.1161 -0.4502 0.0059  153 LYS C NZ  
9434  N N   . GLY C 154 ? 0.7175 1.0136 0.8511 -0.0165 -0.4010 0.0836  154 GLY C N   
9435  C CA  . GLY C 154 ? 0.7349 1.0471 0.9174 -0.0066 -0.3926 0.0962  154 GLY C CA  
9436  C C   . GLY C 154 ? 0.8034 1.1511 1.0422 -0.0184 -0.3985 0.0961  154 GLY C C   
9437  O O   . GLY C 154 ? 0.7412 1.0965 1.0172 -0.0177 -0.3877 0.1007  154 GLY C O   
9438  N N   . ARG C 155 ? 0.8529 1.2225 1.0989 -0.0295 -0.4149 0.0910  155 ARG C N   
9439  C CA  . ARG C 155 ? 0.8380 1.2440 1.1386 -0.0415 -0.4219 0.0912  155 ARG C CA  
9440  C C   . ARG C 155 ? 0.7988 1.1917 1.0851 -0.0663 -0.4244 0.0723  155 ARG C C   
9441  O O   . ARG C 155 ? 0.7050 1.0608 0.9425 -0.0722 -0.4185 0.0599  155 ARG C O   
9442  C CB  . ARG C 155 ? 0.8614 1.3019 1.1837 -0.0366 -0.4392 0.0990  155 ARG C CB  
9443  C CG  . ARG C 155 ? 0.7642 1.2270 1.1241 -0.0130 -0.4341 0.1192  155 ARG C CG  
9444  C CD  . ARG C 155 ? 0.8179 1.2830 1.2161 -0.0071 -0.4139 0.1263  155 ARG C CD  
9445  N NE  . ARG C 155 ? 0.9215 1.3929 1.3406 0.0187  -0.4027 0.1438  155 ARG C NE  
9446  C CZ  . ARG C 155 ? 0.8997 1.4038 1.3802 0.0290  -0.3936 0.1565  155 ARG C CZ  
9447  N NH1 . ARG C 155 ? 0.8118 1.3485 1.3420 0.0151  -0.3948 0.1548  155 ARG C NH1 
9448  N NH2 . ARG C 155 ? 0.7670 1.2699 1.2593 0.0539  -0.3812 0.1708  155 ARG C NH2 
9449  N N   . ASN C 156 ? 0.8141 1.2373 1.1441 -0.0806 -0.4322 0.0701  156 ASN C N   
9450  C CA  . ASN C 156 ? 0.8979 1.3128 1.2309 -0.1041 -0.4311 0.0549  156 ASN C CA  
9451  C C   . ASN C 156 ? 0.8351 1.2091 1.1036 -0.1144 -0.4322 0.0362  156 ASN C C   
9452  O O   . ASN C 156 ? 0.7304 1.1006 0.9651 -0.1151 -0.4445 0.0302  156 ASN C O   
9453  C CB  . ASN C 156 ? 0.7139 1.1669 1.0904 -0.1177 -0.4452 0.0538  156 ASN C CB  
9454  C CG  . ASN C 156 ? 0.7132 1.1808 1.1401 -0.1320 -0.4355 0.0534  156 ASN C CG  
9455  O OD1 . ASN C 156 ? 0.7195 1.1602 1.1350 -0.1394 -0.4219 0.0466  156 ASN C OD1 
9456  N ND2 . ASN C 156 ? 0.6282 1.1386 1.1120 -0.1359 -0.4419 0.0611  156 ASN C ND2 
9457  N N   . TYR C 157 ? 0.7880 1.1318 1.0405 -0.1218 -0.4184 0.0273  157 TYR C N   
9458  C CA  . TYR C 157 ? 0.8039 1.1083 1.0011 -0.1319 -0.4155 0.0089  157 TYR C CA  
9459  C C   . TYR C 157 ? 0.7295 1.0325 0.9411 -0.1550 -0.4172 -0.0052 157 TYR C C   
9460  O O   . TYR C 157 ? 0.6397 0.9608 0.8997 -0.1628 -0.4131 -0.0004 157 TYR C O   
9461  C CB  . TYR C 157 ? 0.6231 0.8910 0.7890 -0.1232 -0.3983 0.0080  157 TYR C CB  
9462  C CG  . TYR C 157 ? 0.7056 0.9675 0.8491 -0.1014 -0.3950 0.0197  157 TYR C CG  
9463  C CD1 . TYR C 157 ? 0.6767 0.9563 0.8547 -0.0858 -0.3903 0.0375  157 TYR C CD1 
9464  C CD2 . TYR C 157 ? 0.8714 1.1096 0.9606 -0.0963 -0.3951 0.0134  157 TYR C CD2 
9465  C CE1 . TYR C 157 ? 0.7140 0.9851 0.8707 -0.0659 -0.3865 0.0480  157 TYR C CE1 
9466  C CE2 . TYR C 157 ? 0.7922 1.0236 0.8614 -0.0775 -0.3909 0.0244  157 TYR C CE2 
9467  C CZ  . TYR C 157 ? 0.7429 0.9894 0.8448 -0.0625 -0.3870 0.0414  157 TYR C CZ  
9468  O OH  . TYR C 157 ? 0.7226 0.9594 0.8039 -0.0440 -0.3821 0.0521  157 TYR C OH  
9469  N N   . THR C 158 ? 0.7553 1.0369 0.9258 -0.1656 -0.4222 -0.0222 158 THR C N   
9470  C CA  . THR C 158 ? 0.7004 0.9735 0.8769 -0.1871 -0.4227 -0.0375 158 THR C CA  
9471  C C   . THR C 158 ? 0.6903 0.9212 0.8389 -0.1909 -0.4050 -0.0479 158 THR C C   
9472  O O   . THR C 158 ? 0.7055 0.9119 0.8210 -0.1777 -0.3945 -0.0462 158 THR C O   
9473  C CB  . THR C 158 ? 0.7415 1.0138 0.8902 -0.1967 -0.4375 -0.0512 158 THR C CB  
9474  O OG1 . THR C 158 ? 0.7530 1.0087 0.8517 -0.1833 -0.4382 -0.0523 158 THR C OG1 
9475  C CG2 . THR C 158 ? 0.7557 1.0723 0.9468 -0.2018 -0.4562 -0.0444 158 THR C CG2 
9476  N N   . GLN C 159 ? 0.6980 0.9203 0.8615 -0.2091 -0.4015 -0.0584 159 GLN C N   
9477  C CA  . GLN C 159 ? 0.6922 0.8738 0.8315 -0.2132 -0.3848 -0.0684 159 GLN C CA  
9478  C C   . GLN C 159 ? 0.7863 0.9331 0.8645 -0.2087 -0.3810 -0.0825 159 GLN C C   
9479  O O   . GLN C 159 ? 0.7711 0.8849 0.8218 -0.2029 -0.3660 -0.0865 159 GLN C O   
9480  C CB  . GLN C 159 ? 0.7028 0.8815 0.8695 -0.2342 -0.3823 -0.0771 159 GLN C CB  
9481  C CG  . GLN C 159 ? 0.7065 0.8400 0.8450 -0.2401 -0.3663 -0.0899 159 GLN C CG  
9482  C CD  . GLN C 159 ? 0.8640 0.9827 1.0085 -0.2310 -0.3506 -0.0801 159 GLN C CD  
9483  O OE1 . GLN C 159 ? 0.8944 1.0361 1.0644 -0.2204 -0.3511 -0.0640 159 GLN C OE1 
9484  N NE2 . GLN C 159 ? 0.7667 0.8458 0.8874 -0.2347 -0.3364 -0.0899 159 GLN C NE2 
9485  N N   . GLU C 160 ? 0.7733 0.9279 0.8311 -0.2107 -0.3940 -0.0896 160 GLU C N   
9486  C CA  . GLU C 160 ? 0.8374 0.9624 0.8399 -0.2061 -0.3896 -0.1022 160 GLU C CA  
9487  C C   . GLU C 160 ? 0.8428 0.9618 0.8190 -0.1859 -0.3831 -0.0919 160 GLU C C   
9488  O O   . GLU C 160 ? 0.7462 0.8342 0.6847 -0.1795 -0.3696 -0.0985 160 GLU C O   
9489  C CB  . GLU C 160 ? 0.8151 0.9516 0.8047 -0.2147 -0.4061 -0.1123 160 GLU C CB  
9490  C CG  . GLU C 160 ? 0.9891 1.1237 0.9958 -0.2357 -0.4109 -0.1263 160 GLU C CG  
9491  C CD  . GLU C 160 ? 1.0000 1.1721 1.0639 -0.2455 -0.4224 -0.1167 160 GLU C CD  
9492  O OE1 . GLU C 160 ? 1.0164 1.2217 1.0954 -0.2435 -0.4393 -0.1094 160 GLU C OE1 
9493  O OE2 . GLU C 160 ? 0.9331 1.1022 1.0281 -0.2549 -0.4139 -0.1159 160 GLU C OE2 
9494  N N   . GLU C 161 ? 0.9162 1.0646 0.9134 -0.1754 -0.3918 -0.0754 161 GLU C N   
9495  C CA  . GLU C 161 ? 0.9494 1.0917 0.9233 -0.1563 -0.3854 -0.0647 161 GLU C CA  
9496  C C   . GLU C 161 ? 0.7649 0.8863 0.7393 -0.1488 -0.3682 -0.0600 161 GLU C C   
9497  O O   . GLU C 161 ? 0.7857 0.8829 0.7246 -0.1382 -0.3566 -0.0610 161 GLU C O   
9498  C CB  . GLU C 161 ? 0.8455 1.0235 0.8447 -0.1463 -0.3986 -0.0477 161 GLU C CB  
9499  C CG  . GLU C 161 ? 0.8695 1.0603 0.8483 -0.1459 -0.4135 -0.0500 161 GLU C CG  
9500  C CD  . GLU C 161 ? 1.0019 1.2329 1.0175 -0.1402 -0.4294 -0.0346 161 GLU C CD  
9501  O OE1 . GLU C 161 ? 0.9866 1.2421 1.0512 -0.1467 -0.4341 -0.0293 161 GLU C OE1 
9502  O OE2 . GLU C 161 ? 1.0046 1.2431 1.0017 -0.1289 -0.4366 -0.0273 161 GLU C OE2 
9503  N N   . LYS C 162 ? 0.7767 0.9080 0.7921 -0.1542 -0.3663 -0.0545 162 LYS C N   
9504  C CA  . LYS C 162 ? 0.8951 1.0062 0.9111 -0.1479 -0.3513 -0.0503 162 LYS C CA  
9505  C C   . LYS C 162 ? 0.7718 0.8429 0.7514 -0.1525 -0.3376 -0.0658 162 LYS C C   
9506  O O   . LYS C 162 ? 0.7552 0.8027 0.7110 -0.1420 -0.3249 -0.0647 162 LYS C O   
9507  C CB  . LYS C 162 ? 0.8423 0.9728 0.9114 -0.1550 -0.3517 -0.0420 162 LYS C CB  
9508  C CG  . LYS C 162 ? 0.8795 0.9904 0.9489 -0.1423 -0.3240 -0.0365 162 LYS C CG  
9509  C CD  . LYS C 162 ? 0.9063 1.0026 0.9914 -0.1544 -0.3100 -0.0433 162 LYS C CD  
9510  C CE  . LYS C 162 ? 0.7977 0.9248 0.9313 -0.1698 -0.3199 -0.0410 162 LYS C CE  
9511  N NZ  . LYS C 162 ? 0.8655 0.9790 1.0179 -0.1809 -0.3040 -0.0446 162 LYS C NZ  
9512  N N   . GLU C 163 ? 0.6696 0.7329 0.6462 -0.1678 -0.3397 -0.0801 163 GLU C N   
9513  C CA  . GLU C 163 ? 0.6812 0.7073 0.6252 -0.1713 -0.3265 -0.0950 163 GLU C CA  
9514  C C   . GLU C 163 ? 0.7422 0.7531 0.6402 -0.1607 -0.3218 -0.1004 163 GLU C C   
9515  O O   . GLU C 163 ? 0.6939 0.6755 0.5651 -0.1563 -0.3073 -0.1074 163 GLU C O   
9516  C CB  . GLU C 163 ? 0.8322 0.8549 0.7864 -0.1899 -0.3306 -0.1087 163 GLU C CB  
9517  C CG  . GLU C 163 ? 0.7631 0.7478 0.6925 -0.1942 -0.3163 -0.1235 163 GLU C CG  
9518  C CD  . GLU C 163 ? 0.8566 0.8379 0.7963 -0.2125 -0.3212 -0.1370 163 GLU C CD  
9519  O OE1 . GLU C 163 ? 0.7415 0.7320 0.7183 -0.2242 -0.3231 -0.1336 163 GLU C OE1 
9520  O OE2 . GLU C 163 ? 1.1362 1.1056 1.0476 -0.2155 -0.3227 -0.1508 163 GLU C OE2 
9521  N N   . TYR C 164 ? 0.8071 0.8387 0.6975 -0.1565 -0.3336 -0.0963 164 TYR C N   
9522  C CA  . TYR C 164 ? 0.7509 0.7707 0.6000 -0.1463 -0.3288 -0.0988 164 TYR C CA  
9523  C C   . TYR C 164 ? 0.7121 0.7201 0.5497 -0.1306 -0.3156 -0.0885 164 TYR C C   
9524  O O   . TYR C 164 ? 0.7074 0.6929 0.5132 -0.1244 -0.3030 -0.0938 164 TYR C O   
9525  C CB  . TYR C 164 ? 0.7599 0.8057 0.6063 -0.1449 -0.3452 -0.0941 164 TYR C CB  
9526  C CG  . TYR C 164 ? 0.8365 0.8740 0.6433 -0.1341 -0.3412 -0.0935 164 TYR C CG  
9527  C CD1 . TYR C 164 ? 0.7984 0.8190 0.5713 -0.1388 -0.3383 -0.1082 164 TYR C CD1 
9528  C CD2 . TYR C 164 ? 0.8959 0.9423 0.7001 -0.1195 -0.3401 -0.0778 164 TYR C CD2 
9529  C CE1 . TYR C 164 ? 0.8283 0.8424 0.5664 -0.1297 -0.3342 -0.1070 164 TYR C CE1 
9530  C CE2 . TYR C 164 ? 0.9991 1.0379 0.7685 -0.1107 -0.3359 -0.0764 164 TYR C CE2 
9531  C CZ  . TYR C 164 ? 1.0142 1.0377 0.7511 -0.1161 -0.3329 -0.0908 164 TYR C CZ  
9532  O OH  . TYR C 164 ? 0.9719 0.9886 0.6752 -0.1080 -0.3282 -0.0888 164 TYR C OH  
9533  N N   . VAL C 165 ? 0.6816 0.7049 0.5462 -0.1240 -0.3183 -0.0738 165 VAL C N   
9534  C CA  . VAL C 165 ? 0.6714 0.6825 0.5268 -0.1097 -0.3064 -0.0643 165 VAL C CA  
9535  C C   . VAL C 165 ? 0.6341 0.6153 0.4803 -0.1113 -0.2909 -0.0724 165 VAL C C   
9536  O O   . VAL C 165 ? 0.6269 0.5887 0.4491 -0.1016 -0.2779 -0.0721 165 VAL C O   
9537  C CB  . VAL C 165 ? 0.6218 0.6556 0.5109 -0.1027 -0.3132 -0.0477 165 VAL C CB  
9538  C CG1 . VAL C 165 ? 0.6000 0.6183 0.4784 -0.0883 -0.3010 -0.0390 165 VAL C CG1 
9539  C CG2 . VAL C 165 ? 0.6332 0.6963 0.5315 -0.0989 -0.3280 -0.0386 165 VAL C CG2 
9540  N N   . LEU C 166 ? 0.6349 0.6122 0.5015 -0.1238 -0.2918 -0.0792 166 LEU C N   
9541  C CA  . LEU C 166 ? 0.6275 0.5760 0.4878 -0.1253 -0.2776 -0.0858 166 LEU C CA  
9542  C C   . LEU C 166 ? 0.7610 0.6852 0.5859 -0.1233 -0.2662 -0.0981 166 LEU C C   
9543  O O   . LEU C 166 ? 0.7512 0.6539 0.5611 -0.1155 -0.2524 -0.0988 166 LEU C O   
9544  C CB  . LEU C 166 ? 0.6308 0.5798 0.5201 -0.1407 -0.2809 -0.0907 166 LEU C CB  
9545  C CG  . LEU C 166 ? 0.7088 0.6722 0.6363 -0.1374 -0.2739 -0.0774 166 LEU C CG  
9546  C CD1 . LEU C 166 ? 0.6971 0.6619 0.6543 -0.1530 -0.2730 -0.0817 166 LEU C CD1 
9547  C CD2 . LEU C 166 ? 0.5842 0.5287 0.5010 -0.1224 -0.2530 -0.0713 166 LEU C CD2 
9548  N N   . ASN C 167 ? 0.8074 0.7357 0.6200 -0.1302 -0.2722 -0.1079 167 ASN C N   
9549  C CA  . ASN C 167 ? 0.8254 0.7326 0.6058 -0.1283 -0.2619 -0.1198 167 ASN C CA  
9550  C C   . ASN C 167 ? 0.8212 0.7259 0.5779 -0.1139 -0.2542 -0.1129 167 ASN C C   
9551  O O   . ASN C 167 ? 0.7898 0.6739 0.5292 -0.1078 -0.2399 -0.1168 167 ASN C O   
9552  C CB  . ASN C 167 ? 0.7311 0.6447 0.5028 -0.1389 -0.2719 -0.1316 167 ASN C CB  
9553  C CG  . ASN C 167 ? 0.8455 0.7372 0.5850 -0.1378 -0.2617 -0.1452 167 ASN C CG  
9554  O OD1 . ASN C 167 ? 0.7710 0.6576 0.4875 -0.1273 -0.2538 -0.1426 167 ASN C OD1 
9555  N ND2 . ASN C 167 ? 1.1501 1.0287 0.8890 -0.1488 -0.2615 -0.1599 167 ASN C ND2 
9556  N N   . LYS C 168 ? 0.7806 0.7066 0.5381 -0.1084 -0.2633 -0.1020 168 LYS C N   
9557  C CA  . LYS C 168 ? 0.6873 0.6112 0.4238 -0.0957 -0.2560 -0.0944 168 LYS C CA  
9558  C C   . LYS C 168 ? 0.7829 0.6944 0.5240 -0.0863 -0.2438 -0.0866 168 LYS C C   
9559  O O   . LYS C 168 ? 0.8113 0.7098 0.5333 -0.0784 -0.2318 -0.0861 168 LYS C O   
9560  C CB  . LYS C 168 ? 0.6823 0.6308 0.4221 -0.0916 -0.2687 -0.0828 168 LYS C CB  
9561  C CG  . LYS C 168 ? 0.7074 0.6681 0.4368 -0.0992 -0.2811 -0.0897 168 LYS C CG  
9562  C CD  . LYS C 168 ? 0.8399 0.7848 0.5337 -0.0982 -0.2725 -0.0996 168 LYS C CD  
9563  C CE  . LYS C 168 ? 0.9062 0.8555 0.5891 -0.1091 -0.2833 -0.1123 168 LYS C CE  
9564  N NZ  . LYS C 168 ? 0.8862 0.8132 0.5602 -0.1168 -0.2745 -0.1295 168 LYS C NZ  
9565  N N   . TYR C 169 ? 0.7759 0.6919 0.5428 -0.0873 -0.2474 -0.0804 169 TYR C N   
9566  C CA  . TYR C 169 ? 0.6392 0.5428 0.4095 -0.0786 -0.2371 -0.0735 169 TYR C CA  
9567  C C   . TYR C 169 ? 0.7122 0.5900 0.4692 -0.0786 -0.2227 -0.0831 169 TYR C C   
9568  O O   . TYR C 169 ? 0.7732 0.6395 0.5191 -0.0693 -0.2117 -0.0793 169 TYR C O   
9569  C CB  . TYR C 169 ? 0.6526 0.5644 0.4524 -0.0815 -0.2443 -0.0670 169 TYR C CB  
9570  C CG  . TYR C 169 ? 0.6738 0.6072 0.4876 -0.0740 -0.2535 -0.0524 169 TYR C CG  
9571  C CD1 . TYR C 169 ? 0.6436 0.5876 0.4440 -0.0666 -0.2560 -0.0462 169 TYR C CD1 
9572  C CD2 . TYR C 169 ? 0.6454 0.5922 0.4936 -0.0709 -0.2483 -0.0429 169 TYR C CD2 
9573  C CE1 . TYR C 169 ? 0.6969 0.6591 0.5110 -0.0584 -0.2637 -0.0322 169 TYR C CE1 
9574  C CE2 . TYR C 169 ? 0.5490 0.5164 0.4139 -0.0615 -0.2520 -0.0292 169 TYR C CE2 
9575  C CZ  . TYR C 169 ? 0.5668 0.5406 0.4136 -0.0555 -0.2624 -0.0240 169 TYR C CZ  
9576  O OH  . TYR C 169 ? 0.6084 0.6009 0.4723 -0.0451 -0.2659 -0.0098 169 TYR C OH  
9577  N N   . PHE C 170 ? 0.7049 0.5733 0.4642 -0.0888 -0.2226 -0.0952 170 PHE C N   
9578  C CA  . PHE C 170 ? 0.8611 0.7048 0.6106 -0.0880 -0.2092 -0.1039 170 PHE C CA  
9579  C C   . PHE C 170 ? 0.8401 0.6760 0.5635 -0.0833 -0.2008 -0.1102 170 PHE C C   
9580  O O   . PHE C 170 ? 0.7791 0.5969 0.4941 -0.0785 -0.1885 -0.1138 170 PHE C O   
9581  C CB  . PHE C 170 ? 0.8086 0.6428 0.5701 -0.1003 -0.2111 -0.1144 170 PHE C CB  
9582  C CG  . PHE C 170 ? 0.7814 0.6124 0.5666 -0.1038 -0.2126 -0.1089 170 PHE C CG  
9583  C CD1 . PHE C 170 ? 0.7654 0.6167 0.5738 -0.1106 -0.2256 -0.1025 170 PHE C CD1 
9584  C CD2 . PHE C 170 ? 0.7395 0.5479 0.5248 -0.1004 -0.2012 -0.1095 170 PHE C CD2 
9585  C CE1 . PHE C 170 ? 0.7689 0.6228 0.6052 -0.1117 -0.2197 -0.0949 170 PHE C CE1 
9586  C CE2 . PHE C 170 ? 0.7509 0.5600 0.5610 -0.1018 -0.1969 -0.1019 170 PHE C CE2 
9587  C CZ  . PHE C 170 ? 0.8083 0.6410 0.6446 -0.1070 -0.2041 -0.0943 170 PHE C CZ  
9588  N N   . GLU C 171 ? 0.7993 0.6486 0.5101 -0.0847 -0.2074 -0.1112 171 GLU C N   
9589  C CA  . GLU C 171 ? 0.7398 0.5829 0.4248 -0.0794 -0.1991 -0.1149 171 GLU C CA  
9590  C C   . GLU C 171 ? 0.7097 0.5524 0.3900 -0.0679 -0.1912 -0.1033 171 GLU C C   
9591  O O   . GLU C 171 ? 0.7807 0.6119 0.4452 -0.0629 -0.1800 -0.1063 171 GLU C O   
9592  C CB  . GLU C 171 ? 0.7320 0.5893 0.4029 -0.0834 -0.2089 -0.1175 171 GLU C CB  
9593  C CG  . GLU C 171 ? 0.7446 0.5948 0.4061 -0.0934 -0.2116 -0.1336 171 GLU C CG  
9594  C CD  . GLU C 171 ? 0.9839 0.8532 0.6451 -0.1009 -0.2279 -0.1346 171 GLU C CD  
9595  O OE1 . GLU C 171 ? 1.0145 0.9010 0.6735 -0.0961 -0.2349 -0.1233 171 GLU C OE1 
9596  O OE2 . GLU C 171 ? 1.0200 0.8864 0.6823 -0.1113 -0.2339 -0.1467 171 GLU C OE2 
9597  N N   . ILE C 172 ? 0.7380 0.5929 0.4322 -0.0638 -0.1968 -0.0904 172 ILE C N   
9598  C CA  . ILE C 172 ? 0.7458 0.5991 0.4374 -0.0535 -0.1896 -0.0794 172 ILE C CA  
9599  C C   . ILE C 172 ? 0.7792 0.6149 0.4759 -0.0500 -0.1789 -0.0809 172 ILE C C   
9600  O O   . ILE C 172 ? 0.7906 0.6185 0.4781 -0.0433 -0.1693 -0.0781 172 ILE C O   
9601  C CB  . ILE C 172 ? 0.6125 0.4818 0.3180 -0.0498 -0.1987 -0.0661 172 ILE C CB  
9602  C CG1 . ILE C 172 ? 0.6107 0.4954 0.3053 -0.0488 -0.2059 -0.0611 172 ILE C CG1 
9603  C CG2 . ILE C 172 ? 0.6075 0.4702 0.3175 -0.0407 -0.1912 -0.0562 172 ILE C CG2 
9604  C CD1 . ILE C 172 ? 0.7564 0.6349 0.4286 -0.0436 -0.1965 -0.0597 172 ILE C CD1 
9605  N N   . ILE C 173 ? 0.7129 0.5420 0.4245 -0.0548 -0.1808 -0.0849 173 ILE C N   
9606  C CA  . ILE C 173 ? 0.6289 0.4404 0.3449 -0.0515 -0.1717 -0.0860 173 ILE C CA  
9607  C C   . ILE C 173 ? 0.6468 0.4431 0.3493 -0.0511 -0.1618 -0.0965 173 ILE C C   
9608  O O   . ILE C 173 ? 0.6336 0.4186 0.3331 -0.0445 -0.1528 -0.0952 173 ILE C O   
9609  C CB  . ILE C 173 ? 0.6838 0.4908 0.4181 -0.0577 -0.1765 -0.0873 173 ILE C CB  
9610  C CG1 . ILE C 173 ? 0.6858 0.5096 0.4337 -0.0582 -0.1872 -0.0775 173 ILE C CG1 
9611  C CG2 . ILE C 173 ? 0.6470 0.4353 0.3848 -0.0534 -0.1677 -0.0866 173 ILE C CG2 
9612  C CD1 . ILE C 173 ? 0.5508 0.3755 0.3236 -0.0629 -0.1868 -0.0753 173 ILE C CD1 
9613  N N   . LYS C 174 ? 0.6714 0.4671 0.3658 -0.0578 -0.1637 -0.1074 174 LYS C N   
9614  C CA  . LYS C 174 ? 0.6278 0.4084 0.3073 -0.0568 -0.1540 -0.1184 174 LYS C CA  
9615  C C   . LYS C 174 ? 0.6859 0.4682 0.3481 -0.0493 -0.1469 -0.1151 174 LYS C C   
9616  O O   . LYS C 174 ? 0.8649 0.6334 0.5175 -0.0455 -0.1367 -0.1214 174 LYS C O   
9617  C CB  . LYS C 174 ? 0.6559 0.4356 0.3277 -0.0658 -0.1581 -0.1312 174 LYS C CB  
9618  C CG  . LYS C 174 ? 0.7114 0.4852 0.3998 -0.0748 -0.1633 -0.1369 174 LYS C CG  
9619  C CD  . LYS C 174 ? 0.8072 0.5872 0.4896 -0.0852 -0.1718 -0.1469 174 LYS C CD  
9620  C CE  . LYS C 174 ? 0.7819 0.5465 0.4740 -0.0941 -0.1713 -0.1582 174 LYS C CE  
9621  N NZ  . LYS C 174 ? 0.6898 0.4613 0.4065 -0.1014 -0.1803 -0.1523 174 LYS C NZ  
9622  N N   . LYS C 175 ? 0.7224 0.5206 0.3809 -0.0471 -0.1519 -0.1051 175 LYS C N   
9623  C CA  . LYS C 175 ? 0.6832 0.4834 0.3247 -0.0415 -0.1458 -0.1009 175 LYS C CA  
9624  C C   . LYS C 175 ? 0.7266 0.5278 0.3757 -0.0341 -0.1424 -0.0885 175 LYS C C   
9625  O O   . LYS C 175 ? 0.7075 0.5125 0.3452 -0.0303 -0.1390 -0.0823 175 LYS C O   
9626  C CB  . LYS C 175 ? 0.7822 0.5977 0.4117 -0.0442 -0.1533 -0.0980 175 LYS C CB  
9627  C CG  . LYS C 175 ? 0.8260 0.6369 0.4312 -0.0471 -0.1495 -0.1090 175 LYS C CG  
9628  C CD  . LYS C 175 ? 0.8737 0.6994 0.4701 -0.0520 -0.1609 -0.1082 175 LYS C CD  
9629  C CE  . LYS C 175 ? 0.8733 0.7097 0.4593 -0.0469 -0.1618 -0.0955 175 LYS C CE  
9630  N NZ  . LYS C 175 ? 0.8070 0.6362 0.3652 -0.0451 -0.1523 -0.0996 175 LYS C NZ  
9631  N N   . THR C 176 ? 0.8100 0.6067 0.4769 -0.0326 -0.1433 -0.0848 176 THR C N   
9632  C CA  . THR C 176 ? 0.6519 0.4501 0.3262 -0.0263 -0.1417 -0.0731 176 THR C CA  
9633  C C   . THR C 176 ? 0.6473 0.4331 0.3165 -0.0212 -0.1323 -0.0742 176 THR C C   
9634  O O   . THR C 176 ? 0.6902 0.4783 0.3544 -0.0172 -0.1294 -0.0666 176 THR C O   
9635  C CB  . THR C 176 ? 0.7064 0.5052 0.3992 -0.0268 -0.1472 -0.0683 176 THR C CB  
9636  O OG1 . THR C 176 ? 0.5938 0.4074 0.2915 -0.0287 -0.1563 -0.0623 176 THR C OG1 
9637  C CG2 . THR C 176 ? 0.6404 0.4333 0.3389 -0.0205 -0.1432 -0.0600 176 THR C CG2 
9638  N N   . LEU C 177 ? 0.6941 0.4660 0.3652 -0.0214 -0.1279 -0.0833 177 LEU C N   
9639  C CA  . LEU C 177 ? 0.6188 0.3793 0.2847 -0.0159 -0.1199 -0.0850 177 LEU C CA  
9640  C C   . LEU C 177 ? 0.6857 0.4468 0.3312 -0.0149 -0.1135 -0.0888 177 LEU C C   
9641  O O   . LEU C 177 ? 0.6674 0.4323 0.3143 -0.0105 -0.1066 -0.0823 177 LEU C O   
9642  C CB  . LEU C 177 ? 0.7387 0.4863 0.4161 -0.0147 -0.1146 -0.0928 177 LEU C CB  
9643  C CG  . LEU C 177 ? 0.5784 0.3231 0.2767 -0.0136 -0.1169 -0.0866 177 LEU C CG  
9644  C CD1 . LEU C 177 ? 0.5300 0.2832 0.2360 -0.0096 -0.1180 -0.0734 177 LEU C CD1 
9645  C CD2 . LEU C 177 ? 0.7163 0.4604 0.4185 -0.0205 -0.1251 -0.0891 177 LEU C CD2 
9646  N N   . SER C 178 ? 0.7629 0.5258 0.3966 -0.0192 -0.1131 -0.0971 178 SER C N   
9647  C CA  . SER C 178 ? 0.8168 0.5780 0.4275 -0.0183 -0.1054 -0.1019 178 SER C CA  
9648  C C   . SER C 178 ? 0.8134 0.5857 0.4152 -0.0170 -0.1061 -0.0899 178 SER C C   
9649  O O   . SER C 178 ? 0.8495 0.6179 0.4335 -0.0147 -0.0974 -0.0905 178 SER C O   
9650  C CB  . SER C 178 ? 0.7261 0.4882 0.3253 -0.0241 -0.1067 -0.1124 178 SER C CB  
9651  O OG  . SER C 178 ? 0.9999 0.7545 0.6121 -0.0275 -0.1098 -0.1205 178 SER C OG  
9652  N N   . ILE C 179 ? 0.7280 0.5129 0.3415 -0.0183 -0.1152 -0.0790 179 ILE C N   
9653  C CA  . ILE C 179 ? 0.6063 0.3994 0.2125 -0.0167 -0.1155 -0.0671 179 ILE C CA  
9654  C C   . ILE C 179 ? 0.6571 0.4448 0.2694 -0.0124 -0.1116 -0.0595 179 ILE C C   
9655  O O   . ILE C 179 ? 0.7524 0.5403 0.3527 -0.0112 -0.1073 -0.0528 179 ILE C O   
9656  C CB  . ILE C 179 ? 0.5958 0.4028 0.2113 -0.0183 -0.1259 -0.0586 179 ILE C CB  
9657  C CG1 . ILE C 179 ? 0.8298 0.6427 0.4384 -0.0159 -0.1257 -0.0459 179 ILE C CG1 
9658  C CG2 . ILE C 179 ? 0.6017 0.4099 0.2406 -0.0175 -0.1317 -0.0551 179 ILE C CG2 
9659  C CD1 . ILE C 179 ? 0.8288 0.6532 0.4490 -0.0154 -0.1353 -0.0367 179 ILE C CD1 
9660  N N   . TYR C 180 ? 0.5717 0.3538 0.2012 -0.0106 -0.1133 -0.0604 180 TYR C N   
9661  C CA  . TYR C 180 ? 0.6373 0.4203 0.2831 -0.0068 -0.1072 -0.0528 180 TYR C CA  
9662  C C   . TYR C 180 ? 0.6409 0.4231 0.2865 -0.0046 -0.0942 -0.0570 180 TYR C C   
9663  O O   . TYR C 180 ? 0.6391 0.4257 0.2896 -0.0033 -0.0885 -0.0495 180 TYR C O   
9664  C CB  . TYR C 180 ? 0.6343 0.4141 0.3018 -0.0052 -0.1107 -0.0519 180 TYR C CB  
9665  C CG  . TYR C 180 ? 0.5341 0.3163 0.2058 -0.0060 -0.1203 -0.0446 180 TYR C CG  
9666  C CD1 . TYR C 180 ? 0.5511 0.3353 0.2247 -0.0043 -0.1218 -0.0339 180 TYR C CD1 
9667  C CD2 . TYR C 180 ? 0.5781 0.3612 0.2549 -0.0083 -0.1265 -0.0483 180 TYR C CD2 
9668  C CE1 . TYR C 180 ? 0.5578 0.3454 0.2396 -0.0036 -0.1272 -0.0272 180 TYR C CE1 
9669  C CE2 . TYR C 180 ? 0.5109 0.3003 0.1983 -0.0079 -0.1317 -0.0407 180 TYR C CE2 
9670  C CZ  . TYR C 180 ? 0.5202 0.3114 0.2097 -0.0049 -0.1315 -0.0305 180 TYR C CZ  
9671  O OH  . TYR C 180 ? 0.4939 0.2890 0.1922 -0.0034 -0.1357 -0.0239 180 TYR C OH  
9672  N N   . ARG C 181 ? 0.6588 0.4351 0.2999 -0.0042 -0.0889 -0.0690 181 ARG C N   
9673  C CA  . ARG C 181 ? 0.6761 0.4521 0.3151 -0.0012 -0.0747 -0.0736 181 ARG C CA  
9674  C C   . ARG C 181 ? 0.7365 0.5166 0.3519 -0.0032 -0.0696 -0.0707 181 ARG C C   
9675  O O   . ARG C 181 ? 0.7815 0.5668 0.4005 -0.0012 -0.0585 -0.0663 181 ARG C O   
9676  C CB  . ARG C 181 ? 0.7382 0.5039 0.3738 0.0001  -0.0694 -0.0882 181 ARG C CB  
9677  C CG  . ARG C 181 ? 0.7179 0.4759 0.3633 -0.0016 -0.0788 -0.0929 181 ARG C CG  
9678  C CD  . ARG C 181 ? 0.8011 0.5458 0.4428 -0.0005 -0.0725 -0.1076 181 ARG C CD  
9679  N NE  . ARG C 181 ? 0.9247 0.6609 0.5721 -0.0044 -0.0821 -0.1122 181 ARG C NE  
9680  C CZ  . ARG C 181 ? 1.1037 0.8277 0.7636 -0.0021 -0.0787 -0.1190 181 ARG C CZ  
9681  N NH1 . ARG C 181 ? 1.1068 0.8260 0.7762 0.0053  -0.0664 -0.1221 181 ARG C NH1 
9682  N NH2 . ARG C 181 ? 1.0787 0.7953 0.7432 -0.0071 -0.0874 -0.1220 181 ARG C NH2 
9683  N N   . GLU C 182 ? 0.6667 0.4450 0.2581 -0.0074 -0.0780 -0.0722 182 GLU C N   
9684  C CA  . GLU C 182 ? 0.6484 0.4285 0.2127 -0.0093 -0.0737 -0.0691 182 GLU C CA  
9685  C C   . GLU C 182 ? 0.6664 0.4537 0.2367 -0.0091 -0.0727 -0.0536 182 GLU C C   
9686  O O   . GLU C 182 ? 0.8092 0.5988 0.3700 -0.0090 -0.0613 -0.0497 182 GLU C O   
9687  C CB  . GLU C 182 ? 0.6938 0.4716 0.2329 -0.0139 -0.0859 -0.0726 182 GLU C CB  
9688  C CG  . GLU C 182 ? 0.7868 0.5660 0.2977 -0.0157 -0.0790 -0.0738 182 GLU C CG  
9689  C CD  . GLU C 182 ? 0.8381 0.6287 0.3463 -0.0196 -0.0899 -0.0729 182 GLU C CD  
9690  O OE1 . GLU C 182 ? 0.7244 0.5168 0.2437 -0.0221 -0.0974 -0.0811 182 GLU C OE1 
9691  O OE2 . GLU C 182 ? 0.8205 0.6178 0.3150 -0.0203 -0.0911 -0.0638 182 GLU C OE2 
9692  N N   . ILE C 183 ? 0.6201 0.4099 0.2056 -0.0092 -0.0836 -0.0448 183 ILE C N   
9693  C CA  . ILE C 183 ? 0.6979 0.4912 0.2871 -0.0095 -0.0833 -0.0308 183 ILE C CA  
9694  C C   . ILE C 183 ? 0.7040 0.5009 0.3133 -0.0082 -0.0717 -0.0278 183 ILE C C   
9695  O O   . ILE C 183 ? 0.6849 0.4846 0.2914 -0.0099 -0.0652 -0.0189 183 ILE C O   
9696  C CB  . ILE C 183 ? 0.6545 0.4475 0.2542 -0.0091 -0.0967 -0.0233 183 ILE C CB  
9697  C CG1 . ILE C 183 ? 0.5642 0.3562 0.1900 -0.0072 -0.0990 -0.0264 183 ILE C CG1 
9698  C CG2 . ILE C 183 ? 0.5961 0.3919 0.1847 -0.0102 -0.1071 -0.0245 183 ILE C CG2 
9699  C CD1 . ILE C 183 ? 0.5627 0.3546 0.2055 -0.0065 -0.0985 -0.0169 183 ILE C CD1 
9700  N N   . LYS C 184 ? 0.6075 0.4049 0.2384 -0.0055 -0.0692 -0.0343 184 LYS C N   
9701  C CA  . LYS C 184 ? 0.6081 0.4115 0.2608 -0.0041 -0.0593 -0.0313 184 LYS C CA  
9702  C C   . LYS C 184 ? 0.7426 0.5496 0.3877 -0.0029 -0.0433 -0.0362 184 LYS C C   
9703  O O   . LYS C 184 ? 0.7905 0.6051 0.4453 -0.0038 -0.0335 -0.0295 184 LYS C O   
9704  C CB  . LYS C 184 ? 0.7055 0.5084 0.3837 -0.0007 -0.0627 -0.0354 184 LYS C CB  
9705  C CG  . LYS C 184 ? 0.7084 0.5197 0.4125 0.0005  -0.0564 -0.0301 184 LYS C CG  
9706  C CD  . LYS C 184 ? 0.5602 0.3705 0.2877 0.0043  -0.0613 -0.0324 184 LYS C CD  
9707  C CE  . LYS C 184 ? 0.5968 0.4023 0.3247 0.0092  -0.0561 -0.0441 184 LYS C CE  
9708  N NZ  . LYS C 184 ? 0.6540 0.4615 0.4092 0.0141  -0.0564 -0.0441 184 LYS C NZ  
9709  N N   . GLU C 185 ? 0.7090 0.5102 0.3369 -0.0013 -0.0396 -0.0481 185 GLU C N   
9710  C CA  . GLU C 185 ? 0.6391 0.4415 0.2551 0.0004  -0.0227 -0.0538 185 GLU C CA  
9711  C C   . GLU C 185 ? 0.6586 0.4629 0.2501 -0.0037 -0.0176 -0.0456 185 GLU C C   
9712  O O   . GLU C 185 ? 0.6698 0.4804 0.2636 -0.0034 -0.0021 -0.0422 185 GLU C O   
9713  C CB  . GLU C 185 ? 0.6594 0.4511 0.2571 0.0022  -0.0211 -0.0695 185 GLU C CB  
9714  C CG  . GLU C 185 ? 0.6585 0.4486 0.2771 0.0085  -0.0109 -0.0791 185 GLU C CG  
9715  C CD  . GLU C 185 ? 0.8834 0.6770 0.5368 0.0111  -0.0192 -0.0747 185 GLU C CD  
9716  O OE1 . GLU C 185 ? 0.9182 0.7058 0.5719 0.0090  -0.0336 -0.0753 185 GLU C OE1 
9717  O OE2 . GLU C 185 ? 1.0134 0.8163 0.6937 0.0151  -0.0113 -0.0702 185 GLU C OE2 
9718  N N   . GLU C 186 ? 0.7844 0.5838 0.3537 -0.0073 -0.0302 -0.0413 186 GLU C N   
9719  C CA  . GLU C 186 ? 0.7245 0.5235 0.2678 -0.0109 -0.0274 -0.0320 186 GLU C CA  
9720  C C   . GLU C 186 ? 0.6701 0.4743 0.2297 -0.0133 -0.0277 -0.0163 186 GLU C C   
9721  O O   . GLU C 186 ? 0.8090 0.6118 0.3494 -0.0164 -0.0247 -0.0065 186 GLU C O   
9722  C CB  . GLU C 186 ? 0.7007 0.4930 0.2153 -0.0131 -0.0423 -0.0326 186 GLU C CB  
9723  C CG  . GLU C 186 ? 0.8629 0.6483 0.3532 -0.0130 -0.0421 -0.0480 186 GLU C CG  
9724  C CD  . GLU C 186 ? 0.9340 0.7147 0.3866 -0.0164 -0.0521 -0.0462 186 GLU C CD  
9725  O OE1 . GLU C 186 ? 1.0379 0.8245 0.4971 -0.0174 -0.0637 -0.0337 186 GLU C OE1 
9726  O OE2 . GLU C 186 ? 0.8809 0.6586 0.3110 -0.0174 -0.0472 -0.0563 186 GLU C OE2 
9727  N N   . GLY C 187 ? 0.6661 0.4747 0.2587 -0.0124 -0.0317 -0.0137 187 GLY C N   
9728  C CA  . GLY C 187 ? 0.6836 0.4959 0.2930 -0.0157 -0.0315 -0.0007 187 GLY C CA  
9729  C C   . GLY C 187 ? 0.6727 0.4777 0.2740 -0.0179 -0.0454 0.0090  187 GLY C C   
9730  O O   . GLY C 187 ? 0.6234 0.4277 0.2312 -0.0216 -0.0443 0.0203  187 GLY C O   
9731  N N   . LYS C 188 ? 0.6544 0.4540 0.2432 -0.0158 -0.0581 0.0051  188 LYS C N   
9732  C CA  . LYS C 188 ? 0.6195 0.4130 0.2022 -0.0162 -0.0706 0.0144  188 LYS C CA  
9733  C C   . LYS C 188 ? 0.5966 0.3881 0.2041 -0.0151 -0.0791 0.0160  188 LYS C C   
9734  O O   . LYS C 188 ? 0.6810 0.4662 0.2868 -0.0150 -0.0870 0.0244  188 LYS C O   
9735  C CB  . LYS C 188 ? 0.6541 0.4450 0.2143 -0.0144 -0.0809 0.0105  188 LYS C CB  
9736  C CG  . LYS C 188 ? 0.6639 0.4535 0.1914 -0.0161 -0.0761 0.0122  188 LYS C CG  
9737  C CD  . LYS C 188 ? 0.8782 0.6666 0.4002 -0.0190 -0.0640 0.0235  188 LYS C CD  
9738  C CE  . LYS C 188 ? 1.1050 0.8865 0.6084 -0.0196 -0.0712 0.0377  188 LYS C CE  
9739  N NZ  . LYS C 188 ? 0.9752 0.7536 0.4765 -0.0235 -0.0596 0.0500  188 LYS C NZ  
9740  N N   . GLY C 189 ? 0.5915 0.3869 0.2205 -0.0139 -0.0775 0.0085  189 GLY C N   
9741  C CA  . GLY C 189 ? 0.5549 0.3473 0.2038 -0.0131 -0.0853 0.0101  189 GLY C CA  
9742  C C   . GLY C 189 ? 0.6109 0.4082 0.2812 -0.0115 -0.0824 0.0023  189 GLY C C   
9743  O O   . GLY C 189 ? 0.6587 0.4609 0.3290 -0.0098 -0.0750 -0.0056 189 GLY C O   
9744  N N   . SER C 190 ? 0.6215 0.4160 0.3086 -0.0116 -0.0885 0.0048  190 SER C N   
9745  C CA  . SER C 190 ? 0.5129 0.3112 0.2210 -0.0097 -0.0882 -0.0002 190 SER C CA  
9746  C C   . SER C 190 ? 0.5021 0.2937 0.2116 -0.0066 -0.0974 -0.0045 190 SER C C   
9747  O O   . SER C 190 ? 0.4988 0.2831 0.2022 -0.0069 -0.1048 -0.0005 190 SER C O   
9748  C CB  . SER C 190 ? 0.5068 0.3075 0.2330 -0.0132 -0.0887 0.0063  190 SER C CB  
9749  O OG  . SER C 190 ? 0.5826 0.3931 0.3150 -0.0161 -0.0782 0.0093  190 SER C OG  
9750  N N   . VAL C 191 ? 0.4984 0.2917 0.2165 -0.0034 -0.0958 -0.0123 191 VAL C N   
9751  C CA  . VAL C 191 ? 0.4898 0.2767 0.2110 -0.0010 -0.1028 -0.0160 191 VAL C CA  
9752  C C   . VAL C 191 ? 0.4805 0.2672 0.2207 0.0006  -0.1047 -0.0149 191 VAL C C   
9753  O O   . VAL C 191 ? 0.4817 0.2743 0.2348 0.0026  -0.0991 -0.0176 191 VAL C O   
9754  C CB  . VAL C 191 ? 0.4964 0.2822 0.2108 0.0008  -0.1008 -0.0254 191 VAL C CB  
9755  C CG1 . VAL C 191 ? 0.5426 0.3270 0.2392 -0.0010 -0.1055 -0.0255 191 VAL C CG1 
9756  C CG2 . VAL C 191 ? 0.5461 0.3371 0.2608 0.0019  -0.0904 -0.0310 191 VAL C CG2 
9757  N N   . SER C 192 ? 0.4735 0.2531 0.2148 0.0000  -0.1125 -0.0107 192 SER C N   
9758  C CA  . SER C 192 ? 0.4902 0.2676 0.2451 0.0013  -0.1168 -0.0090 192 SER C CA  
9759  C C   . SER C 192 ? 0.4650 0.2341 0.2182 0.0043  -0.1203 -0.0125 192 SER C C   
9760  O O   . SER C 192 ? 0.4660 0.2318 0.2093 0.0044  -0.1203 -0.0154 192 SER C O   
9761  C CB  . SER C 192 ? 0.4668 0.2396 0.2208 -0.0023 -0.1229 -0.0020 192 SER C CB  
9762  O OG  . SER C 192 ? 0.4664 0.2276 0.2084 -0.0018 -0.1281 -0.0010 192 SER C OG  
9763  N N   . THR C 193 ? 0.4629 0.2293 0.2270 0.0064  -0.1235 -0.0113 193 THR C N   
9764  C CA  . THR C 193 ? 0.4655 0.2226 0.2282 0.0088  -0.1264 -0.0129 193 THR C CA  
9765  C C   . THR C 193 ? 0.5405 0.2899 0.3023 0.0084  -0.1338 -0.0070 193 THR C C   
9766  O O   . THR C 193 ? 0.5044 0.2569 0.2709 0.0065  -0.1377 -0.0028 193 THR C O   
9767  C CB  . THR C 193 ? 0.5097 0.2673 0.2835 0.0129  -0.1224 -0.0178 193 THR C CB  
9768  O OG1 . THR C 193 ? 0.4679 0.2150 0.2379 0.0139  -0.1239 -0.0195 193 THR C OG1 
9769  C CG2 . THR C 193 ? 0.5851 0.3470 0.3753 0.0157  -0.1245 -0.0140 193 THR C CG2 
9770  N N   . SER C 194 ? 0.5126 0.2515 0.2674 0.0096  -0.1358 -0.0068 194 SER C N   
9771  C CA  . SER C 194 ? 0.6431 0.3717 0.3922 0.0097  -0.1421 -0.0019 194 SER C CA  
9772  C C   . SER C 194 ? 0.5860 0.3097 0.3422 0.0133  -0.1435 -0.0011 194 SER C C   
9773  O O   . SER C 194 ? 0.4731 0.1993 0.2382 0.0157  -0.1388 -0.0052 194 SER C O   
9774  C CB  . SER C 194 ? 0.5378 0.2570 0.2715 0.0088  -0.1414 -0.0011 194 SER C CB  
9775  O OG  . SER C 194 ? 0.5220 0.2399 0.2472 0.0063  -0.1431 0.0010  194 SER C OG  
9776  N N   . PRO C 195 ? 0.3607 0.3574 0.3339 0.0644  -0.0837 -0.0245 195 PRO C N   
9777  C CA  . PRO C 195 ? 0.3328 0.3138 0.2933 0.0686  -0.0786 -0.0287 195 PRO C CA  
9778  C C   . PRO C 195 ? 0.3714 0.3355 0.3161 0.0614  -0.0778 -0.0365 195 PRO C C   
9779  O O   . PRO C 195 ? 0.2969 0.2664 0.2477 0.0529  -0.0833 -0.0394 195 PRO C O   
9780  C CB  . PRO C 195 ? 0.2955 0.2830 0.2691 0.0682  -0.0829 -0.0276 195 PRO C CB  
9781  C CG  . PRO C 195 ? 0.2777 0.2849 0.2695 0.0686  -0.0868 -0.0211 195 PRO C CG  
9782  C CD  . PRO C 195 ? 0.2992 0.3102 0.2922 0.0641  -0.0886 -0.0197 195 PRO C CD  
9783  N N   . TYR C 196 ? 0.4244 0.3678 0.3493 0.0649  -0.0708 -0.0398 196 TYR C N   
9784  C CA  . TYR C 196 ? 0.3347 0.2598 0.2394 0.0571  -0.0682 -0.0474 196 TYR C CA  
9785  C C   . TYR C 196 ? 0.3067 0.2354 0.2167 0.0441  -0.0740 -0.0522 196 TYR C C   
9786  O O   . TYR C 196 ? 0.2856 0.2195 0.1938 0.0354  -0.0777 -0.0557 196 TYR C O   
9787  C CB  . TYR C 196 ? 0.3301 0.2268 0.2126 0.0628  -0.0597 -0.0501 196 TYR C CB  
9788  C CG  . TYR C 196 ? 0.3471 0.2220 0.2045 0.0573  -0.0545 -0.0579 196 TYR C CG  
9789  C CD1 . TYR C 196 ? 0.3991 0.2654 0.2465 0.0415  -0.0573 -0.0651 196 TYR C CD1 
9790  C CD2 . TYR C 196 ? 0.3672 0.2317 0.2106 0.0670  -0.0464 -0.0590 196 TYR C CD2 
9791  C CE1 . TYR C 196 ? 0.4382 0.2844 0.2608 0.0339  -0.0533 -0.0732 196 TYR C CE1 
9792  C CE2 . TYR C 196 ? 0.4377 0.2798 0.2548 0.0609  -0.0411 -0.0680 196 TYR C CE2 
9793  C CZ  . TYR C 196 ? 0.5586 0.3907 0.3644 0.0434  -0.0452 -0.0751 196 TYR C CZ  
9794  O OH  . TYR C 196 ? 0.7048 0.5143 0.4825 0.0348  -0.0408 -0.0849 196 TYR C OH  
9795  N N   . TYR C 197 ? 0.2971 0.2255 0.2137 0.0427  -0.0749 -0.0524 197 TYR C N   
9796  C CA  . TYR C 197 ? 0.2895 0.2226 0.2112 0.0308  -0.0780 -0.0580 197 TYR C CA  
9797  C C   . TYR C 197 ? 0.3418 0.2981 0.2892 0.0311  -0.0841 -0.0566 197 TYR C C   
9798  O O   . TYR C 197 ? 0.3484 0.3098 0.3024 0.0250  -0.0845 -0.0608 197 TYR C O   
9799  C CB  . TYR C 197 ? 0.2904 0.2032 0.1960 0.0262  -0.0727 -0.0608 197 TYR C CB  
9800  C CG  . TYR C 197 ? 0.3422 0.2270 0.2207 0.0229  -0.0668 -0.0643 197 TYR C CG  
9801  C CD1 . TYR C 197 ? 0.3320 0.2145 0.2020 0.0094  -0.0677 -0.0713 197 TYR C CD1 
9802  C CD2 . TYR C 197 ? 0.4050 0.2656 0.2665 0.0335  -0.0606 -0.0609 197 TYR C CD2 
9803  C CE1 . TYR C 197 ? 0.3645 0.2181 0.2071 0.0045  -0.0621 -0.0761 197 TYR C CE1 
9804  C CE2 . TYR C 197 ? 0.3748 0.2048 0.2100 0.0313  -0.0543 -0.0653 197 TYR C CE2 
9805  C CZ  . TYR C 197 ? 0.3870 0.2120 0.2114 0.0158  -0.0548 -0.0736 197 TYR C CZ  
9806  O OH  . TYR C 197 ? 0.4246 0.2157 0.2199 0.0117  -0.0483 -0.0795 197 TYR C OH  
9807  N N   . HIS C 198 ? 0.3154 0.2848 0.2764 0.0375  -0.0881 -0.0511 198 HIS C N   
9808  C CA  . HIS C 198 ? 0.3453 0.3320 0.3293 0.0379  -0.0941 -0.0501 198 HIS C CA  
9809  C C   . HIS C 198 ? 0.3468 0.3352 0.3376 0.0375  -0.0932 -0.0529 198 HIS C C   
9810  O O   . HIS C 198 ? 0.4341 0.4313 0.4372 0.0332  -0.0950 -0.0583 198 HIS C O   
9811  C CB  . HIS C 198 ? 0.3479 0.3454 0.3413 0.0319  -0.0993 -0.0533 198 HIS C CB  
9812  C CG  . HIS C 198 ? 0.3385 0.3499 0.3537 0.0354  -0.1061 -0.0497 198 HIS C CG  
9813  N ND1 . HIS C 198 ? 0.3214 0.3421 0.3547 0.0351  -0.1085 -0.0542 198 HIS C ND1 
9814  C CD2 . HIS C 198 ? 0.2728 0.2879 0.2932 0.0393  -0.1105 -0.0419 198 HIS C CD2 
9815  C CE1 . HIS C 198 ? 0.3477 0.3745 0.3967 0.0396  -0.1145 -0.0494 198 HIS C CE1 
9816  N NE2 . HIS C 198 ? 0.3771 0.4004 0.4181 0.0413  -0.1162 -0.0412 198 HIS C NE2 
9817  N N   . PRO C 199 ? 0.3628 0.3449 0.3465 0.0421  -0.0904 -0.0496 199 PRO C N   
9818  C CA  . PRO C 199 ? 0.3349 0.3191 0.3216 0.0404  -0.0902 -0.0520 199 PRO C CA  
9819  C C   . PRO C 199 ? 0.3689 0.3652 0.3718 0.0431  -0.0949 -0.0497 199 PRO C C   
9820  O O   . PRO C 199 ? 0.4077 0.4099 0.4193 0.0464  -0.0980 -0.0446 199 PRO C O   
9821  C CB  . PRO C 199 ? 0.3705 0.3406 0.3383 0.0440  -0.0861 -0.0480 199 PRO C CB  
9822  C CG  . PRO C 199 ? 0.3448 0.3126 0.3095 0.0524  -0.0852 -0.0417 199 PRO C CG  
9823  C CD  . PRO C 199 ? 0.3481 0.3227 0.3207 0.0498  -0.0874 -0.0433 199 PRO C CD  
9824  N N   . LEU C 200 ? 0.4081 0.4070 0.4129 0.0400  -0.0951 -0.0538 200 LEU C N   
9825  C CA  . LEU C 200 ? 0.3255 0.3327 0.3415 0.0404  -0.0994 -0.0528 200 LEU C CA  
9826  C C   . LEU C 200 ? 0.3504 0.3591 0.3580 0.0441  -0.1002 -0.0454 200 LEU C C   
9827  O O   . LEU C 200 ? 0.3584 0.3655 0.3558 0.0422  -0.0998 -0.0461 200 LEU C O   
9828  C CB  . LEU C 200 ? 0.2867 0.2962 0.3075 0.0349  -0.0990 -0.0624 200 LEU C CB  
9829  C CG  . LEU C 200 ? 0.2505 0.2628 0.2855 0.0339  -0.0986 -0.0698 200 LEU C CG  
9830  C CD1 . LEU C 200 ? 0.3113 0.3260 0.3485 0.0296  -0.0953 -0.0809 200 LEU C CD1 
9831  C CD2 . LEU C 200 ? 0.2685 0.2826 0.3191 0.0374  -0.1041 -0.0658 200 LEU C CD2 
9832  N N   . ILE C 201 ? 0.3396 0.3533 0.3515 0.0495  -0.1014 -0.0375 201 ILE C N   
9833  C CA  . ILE C 201 ? 0.2487 0.2695 0.2577 0.0553  -0.1023 -0.0294 201 ILE C CA  
9834  C C   . ILE C 201 ? 0.3687 0.4004 0.3824 0.0506  -0.1076 -0.0297 201 ILE C C   
9835  O O   . ILE C 201 ? 0.3595 0.3942 0.3648 0.0537  -0.1088 -0.0253 201 ILE C O   
9836  C CB  . ILE C 201 ? 0.2424 0.2724 0.2598 0.0606  -0.1018 -0.0222 201 ILE C CB  
9837  C CG1 . ILE C 201 ? 0.3036 0.3217 0.3113 0.0646  -0.0962 -0.0228 201 ILE C CG1 
9838  C CG2 . ILE C 201 ? 0.2438 0.2872 0.2631 0.0676  -0.1024 -0.0140 201 ILE C CG2 
9839  C CD1 . ILE C 201 ? 0.4374 0.4408 0.4271 0.0710  -0.0910 -0.0224 201 ILE C CD1 
9840  N N   . PRO C 202 ? 0.3067 0.3432 0.3322 0.0431  -0.1114 -0.0347 202 PRO C N   
9841  C CA  . PRO C 202 ? 0.2266 0.2713 0.2527 0.0364  -0.1164 -0.0370 202 PRO C CA  
9842  C C   . PRO C 202 ? 0.2601 0.2991 0.2700 0.0340  -0.1152 -0.0416 202 PRO C C   
9843  O O   . PRO C 202 ? 0.2891 0.3371 0.2930 0.0319  -0.1197 -0.0384 202 PRO C O   
9844  C CB  . PRO C 202 ? 0.1985 0.2398 0.2365 0.0290  -0.1184 -0.0445 202 PRO C CB  
9845  C CG  . PRO C 202 ? 0.1908 0.2305 0.2385 0.0330  -0.1173 -0.0394 202 PRO C CG  
9846  C CD  . PRO C 202 ? 0.1889 0.2232 0.2270 0.0406  -0.1121 -0.0369 202 PRO C CD  
9847  N N   . ILE C 203 ? 0.2706 0.2968 0.2729 0.0331  -0.1096 -0.0484 203 ILE C N   
9848  C CA  . ILE C 203 ? 0.2503 0.2709 0.2351 0.0291  -0.1071 -0.0521 203 ILE C CA  
9849  C C   . ILE C 203 ? 0.2544 0.2711 0.2243 0.0357  -0.1072 -0.0412 203 ILE C C   
9850  O O   . ILE C 203 ? 0.2590 0.2780 0.2158 0.0337  -0.1102 -0.0378 203 ILE C O   
9851  C CB  . ILE C 203 ? 0.3414 0.3526 0.3241 0.0254  -0.1002 -0.0617 203 ILE C CB  
9852  C CG1 . ILE C 203 ? 0.3015 0.3161 0.3014 0.0224  -0.1003 -0.0717 203 ILE C CG1 
9853  C CG2 . ILE C 203 ? 0.3317 0.3383 0.2951 0.0191  -0.0964 -0.0652 203 ILE C CG2 
9854  C CD1 . ILE C 203 ? 0.2293 0.2479 0.2285 0.0159  -0.1028 -0.0789 203 ILE C CD1 
9855  N N   . LEU C 204 ? 0.3026 0.3121 0.2729 0.0439  -0.1041 -0.0355 204 LEU C N   
9856  C CA  . LEU C 204 ? 0.2801 0.2805 0.2358 0.0524  -0.1029 -0.0259 204 LEU C CA  
9857  C C   . LEU C 204 ? 0.2648 0.2818 0.2258 0.0595  -0.1095 -0.0158 204 LEU C C   
9858  O O   . LEU C 204 ? 0.2793 0.2932 0.2270 0.0641  -0.1117 -0.0081 204 LEU C O   
9859  C CB  . LEU C 204 ? 0.2950 0.2827 0.2494 0.0594  -0.0972 -0.0244 204 LEU C CB  
9860  C CG  . LEU C 204 ? 0.2866 0.2632 0.2390 0.0519  -0.0921 -0.0337 204 LEU C CG  
9861  C CD1 . LEU C 204 ? 0.3511 0.3168 0.3004 0.0577  -0.0879 -0.0321 204 LEU C CD1 
9862  C CD2 . LEU C 204 ? 0.3113 0.2746 0.2459 0.0438  -0.0885 -0.0373 204 LEU C CD2 
9863  N N   . LEU C 205 ? 0.2742 0.3097 0.2547 0.0601  -0.1130 -0.0148 205 LEU C N   
9864  C CA  . LEU C 205 ? 0.2412 0.2987 0.2305 0.0652  -0.1196 -0.0053 205 LEU C CA  
9865  C C   . LEU C 205 ? 0.2747 0.3423 0.2576 0.0565  -0.1272 -0.0059 205 LEU C C   
9866  O O   . LEU C 205 ? 0.3372 0.4132 0.3135 0.0622  -0.1324 0.0035  205 LEU C O   
9867  C CB  . LEU C 205 ? 0.2641 0.3398 0.2752 0.0639  -0.1209 -0.0046 205 LEU C CB  
9868  C CG  . LEU C 205 ? 0.2993 0.3728 0.3160 0.0745  -0.1143 -0.0005 205 LEU C CG  
9869  C CD1 . LEU C 205 ? 0.3113 0.4030 0.3474 0.0694  -0.1144 0.0012  205 LEU C CD1 
9870  C CD2 . LEU C 205 ? 0.4170 0.4932 0.4294 0.0895  -0.1118 0.0094  205 LEU C CD2 
9871  N N   . ASN C 206 ? 0.3041 0.3706 0.2880 0.0432  -0.1282 -0.0170 206 ASN C N   
9872  C CA  . ASN C 206 ? 0.2536 0.3275 0.2281 0.0326  -0.1345 -0.0206 206 ASN C CA  
9873  C C   . ASN C 206 ? 0.2708 0.3310 0.2395 0.0214  -0.1297 -0.0358 206 ASN C C   
9874  O O   . ASN C 206 ? 0.2841 0.3449 0.2664 0.0159  -0.1293 -0.0441 206 ASN C O   
9875  C CB  . ASN C 206 ? 0.3546 0.4539 0.3437 0.0271  -0.1434 -0.0175 206 ASN C CB  
9876  C CG  . ASN C 206 ? 0.4402 0.5469 0.4171 0.0137  -0.1495 -0.0222 206 ASN C CG  
9877  O OD1 . ASN C 206 ? 0.4406 0.5374 0.3961 0.0116  -0.1497 -0.0249 206 ASN C OD1 
9878  N ND2 . ASN C 206 ? 0.5271 0.6506 0.5155 0.0027  -0.1536 -0.0230 206 ASN C ND2 
9879  N N   . PRO C 207 ? 0.2796 0.3272 0.2284 0.0182  -0.1255 -0.0396 207 PRO C N   
9880  C CA  . PRO C 207 ? 0.2853 0.3236 0.2307 0.0089  -0.1192 -0.0549 207 PRO C CA  
9881  C C   . PRO C 207 ? 0.3031 0.3492 0.2500 -0.0023 -0.1232 -0.0653 207 PRO C C   
9882  O O   . PRO C 207 ? 0.2785 0.3171 0.2266 -0.0080 -0.1173 -0.0795 207 PRO C O   
9883  C CB  . PRO C 207 ? 0.2883 0.3158 0.2096 0.0064  -0.1142 -0.0541 207 PRO C CB  
9884  C CG  . PRO C 207 ? 0.3154 0.3388 0.2297 0.0172  -0.1166 -0.0380 207 PRO C CG  
9885  C CD  . PRO C 207 ? 0.2847 0.3261 0.2133 0.0231  -0.1258 -0.0295 207 PRO C CD  
9886  N N   . ASN C 208 ? 0.3455 0.4069 0.2929 -0.0056 -0.1330 -0.0594 208 ASN C N   
9887  C CA  . ASN C 208 ? 0.2943 0.3616 0.2413 -0.0185 -0.1376 -0.0699 208 ASN C CA  
9888  C C   . ASN C 208 ? 0.3262 0.3883 0.2943 -0.0202 -0.1364 -0.0775 208 ASN C C   
9889  O O   . ASN C 208 ? 0.4782 0.5379 0.4457 -0.0315 -0.1366 -0.0869 208 ASN C O   
9890  C CB  . ASN C 208 ? 0.3012 0.3896 0.2448 -0.0231 -0.1484 -0.0593 208 ASN C CB  
9891  C CG  . ASN C 208 ? 0.3209 0.4132 0.2389 -0.0246 -0.1521 -0.0538 208 ASN C CG  
9892  O OD1 . ASN C 208 ? 0.3354 0.4160 0.2335 -0.0309 -0.1471 -0.0640 208 ASN C OD1 
9893  N ND2 . ASN C 208 ? 0.4808 0.5904 0.3996 -0.0188 -0.1598 -0.0368 208 ASN C ND2 
9894  N N   . CYS C 209 ? 0.2626 0.3203 0.2471 -0.0102 -0.1329 -0.0718 209 CYS C N   
9895  C CA  . CYS C 209 ? 0.2551 0.3069 0.2583 -0.0114 -0.1326 -0.0759 209 CYS C CA  
9896  C C   . CYS C 209 ? 0.2620 0.2958 0.2663 -0.0135 -0.1256 -0.0917 209 CYS C C   
9897  O O   . CYS C 209 ? 0.3451 0.3699 0.3615 -0.0163 -0.1264 -0.0969 209 CYS C O   
9898  C CB  . CYS C 209 ? 0.2367 0.2903 0.2540 -0.0005 -0.1310 -0.0645 209 CYS C CB  
9899  S SG  . CYS C 209 ? 0.3446 0.3862 0.3569 0.0104  -0.1220 -0.0641 209 CYS C SG  
9900  N N   . VAL C 210 ? 0.2661 0.2946 0.2584 -0.0121 -0.1185 -0.0988 210 VAL C N   
9901  C CA  . VAL C 210 ? 0.2740 0.2902 0.2692 -0.0131 -0.1110 -0.1148 210 VAL C CA  
9902  C C   . VAL C 210 ? 0.3099 0.3202 0.2991 -0.0239 -0.1116 -0.1263 210 VAL C C   
9903  O O   . VAL C 210 ? 0.3049 0.3016 0.3020 -0.0233 -0.1063 -0.1381 210 VAL C O   
9904  C CB  . VAL C 210 ? 0.2773 0.2939 0.2599 -0.0118 -0.1022 -0.1199 210 VAL C CB  
9905  C CG1 . VAL C 210 ? 0.2608 0.2795 0.2467 -0.0034 -0.1004 -0.1080 210 VAL C CG1 
9906  C CG2 . VAL C 210 ? 0.2956 0.3178 0.2530 -0.0211 -0.1033 -0.1214 210 VAL C CG2 
9907  N N   . TYR C 211 ? 0.3559 0.3756 0.3309 -0.0336 -0.1175 -0.1218 211 TYR C N   
9908  C CA  . TYR C 211 ? 0.3369 0.3508 0.2995 -0.0468 -0.1171 -0.1321 211 TYR C CA  
9909  C C   . TYR C 211 ? 0.3964 0.4038 0.3710 -0.0531 -0.1225 -0.1326 211 TYR C C   
9910  O O   . TYR C 211 ? 0.5292 0.5262 0.4933 -0.0647 -0.1215 -0.1429 211 TYR C O   
9911  C CB  . TYR C 211 ? 0.3460 0.3742 0.2861 -0.0561 -0.1227 -0.1264 211 TYR C CB  
9912  C CG  . TYR C 211 ? 0.3495 0.3794 0.2720 -0.0531 -0.1170 -0.1274 211 TYR C CG  
9913  C CD1 . TYR C 211 ? 0.3624 0.3804 0.2771 -0.0539 -0.1051 -0.1420 211 TYR C CD1 
9914  C CD2 . TYR C 211 ? 0.3424 0.3859 0.2564 -0.0491 -0.1231 -0.1134 211 TYR C CD2 
9915  C CE1 . TYR C 211 ? 0.3676 0.3885 0.2658 -0.0534 -0.0991 -0.1426 211 TYR C CE1 
9916  C CE2 . TYR C 211 ? 0.3498 0.3923 0.2451 -0.0481 -0.1181 -0.1140 211 TYR C CE2 
9917  C CZ  . TYR C 211 ? 0.3620 0.3939 0.2492 -0.0516 -0.1058 -0.1286 211 TYR C CZ  
9918  O OH  . TYR C 211 ? 0.3713 0.4036 0.2393 -0.0529 -0.0996 -0.1286 211 TYR C OH  
9919  N N   . GLU C 212 ? 0.4084 0.4200 0.4024 -0.0470 -0.1280 -0.1216 212 GLU C N   
9920  C CA  . GLU C 212 ? 0.5041 0.5059 0.5098 -0.0538 -0.1322 -0.1223 212 GLU C CA  
9921  C C   . GLU C 212 ? 0.4909 0.4647 0.5004 -0.0517 -0.1251 -0.1373 212 GLU C C   
9922  O O   . GLU C 212 ? 0.4293 0.3876 0.4347 -0.0625 -0.1253 -0.1454 212 GLU C O   
9923  C CB  . GLU C 212 ? 0.4355 0.4457 0.4606 -0.0468 -0.1379 -0.1074 212 GLU C CB  
9924  C CG  . GLU C 212 ? 0.4681 0.5029 0.4957 -0.0543 -0.1459 -0.0937 212 GLU C CG  
9925  C CD  . GLU C 212 ? 0.6793 0.7363 0.7057 -0.0438 -0.1467 -0.0806 212 GLU C CD  
9926  O OE1 . GLU C 212 ? 0.7423 0.7946 0.7592 -0.0354 -0.1419 -0.0839 212 GLU C OE1 
9927  O OE2 . GLU C 212 ? 0.7707 0.8494 0.8059 -0.0438 -0.1513 -0.0672 212 GLU C OE2 
9928  N N   . THR C 213 ? 0.4111 0.3784 0.4284 -0.0379 -0.1184 -0.1413 213 THR C N   
9929  C CA  . THR C 213 ? 0.3787 0.3228 0.4056 -0.0311 -0.1119 -0.1532 213 THR C CA  
9930  C C   . THR C 213 ? 0.4173 0.3559 0.4315 -0.0305 -0.1004 -0.1689 213 THR C C   
9931  O O   . THR C 213 ? 0.5771 0.4949 0.5923 -0.0301 -0.0947 -0.1811 213 THR C O   
9932  C CB  . THR C 213 ? 0.4708 0.4146 0.5179 -0.0159 -0.1128 -0.1470 213 THR C CB  
9933  O OG1 . THR C 213 ? 0.3811 0.3471 0.4255 -0.0121 -0.1138 -0.1345 213 THR C OG1 
9934  C CG2 . THR C 213 ? 0.3956 0.3272 0.4567 -0.0159 -0.1193 -0.1366 213 THR C CG2 
9935  N N   . THR C 214 ? 0.4987 0.4542 0.5006 -0.0303 -0.0963 -0.1687 214 THR C N   
9936  C CA  . THR C 214 ? 0.4046 0.3582 0.3939 -0.0305 -0.0846 -0.1826 214 THR C CA  
9937  C C   . THR C 214 ? 0.4345 0.4001 0.3967 -0.0429 -0.0858 -0.1806 214 THR C C   
9938  O O   . THR C 214 ? 0.5254 0.5054 0.4801 -0.0409 -0.0838 -0.1756 214 THR C O   
9939  C CB  . THR C 214 ? 0.3565 0.3183 0.3596 -0.0170 -0.0771 -0.1846 214 THR C CB  
9940  O OG1 . THR C 214 ? 0.4023 0.3802 0.4064 -0.0147 -0.0827 -0.1706 214 THR C OG1 
9941  C CG2 . THR C 214 ? 0.3536 0.3028 0.3829 -0.0041 -0.0764 -0.1880 214 THR C CG2 
9942  N N   . PRO C 215 ? 0.4097 0.3682 0.3550 -0.0564 -0.0898 -0.1842 215 PRO C N   
9943  C CA  . PRO C 215 ? 0.4201 0.3912 0.3402 -0.0681 -0.0955 -0.1788 215 PRO C CA  
9944  C C   . PRO C 215 ? 0.4361 0.4095 0.3356 -0.0691 -0.0865 -0.1867 215 PRO C C   
9945  O O   . PRO C 215 ? 0.4478 0.4303 0.3256 -0.0772 -0.0922 -0.1816 215 PRO C O   
9946  C CB  . PRO C 215 ? 0.4483 0.4082 0.3575 -0.0824 -0.1028 -0.1827 215 PRO C CB  
9947  C CG  . PRO C 215 ? 0.4435 0.3891 0.3750 -0.0790 -0.1029 -0.1843 215 PRO C CG  
9948  C CD  . PRO C 215 ? 0.4599 0.3979 0.4087 -0.0623 -0.0919 -0.1909 215 PRO C CD  
9949  N N   . ASN C 216 ? 0.4917 0.4593 0.3982 -0.0607 -0.0730 -0.1985 216 ASN C N   
9950  C CA  . ASN C 216 ? 0.5411 0.5136 0.4287 -0.0631 -0.0629 -0.2067 216 ASN C CA  
9951  C C   . ASN C 216 ? 0.6190 0.6048 0.5165 -0.0543 -0.0545 -0.2043 216 ASN C C   
9952  O O   . ASN C 216 ? 0.7006 0.6921 0.5860 -0.0564 -0.0437 -0.2120 216 ASN C O   
9953  C CB  . ASN C 216 ? 0.6603 0.6171 0.5429 -0.0637 -0.0521 -0.2258 216 ASN C CB  
9954  C CG  . ASN C 216 ? 0.7681 0.7296 0.6222 -0.0723 -0.0458 -0.2335 216 ASN C CG  
9955  O OD1 . ASN C 216 ? 0.7027 0.6746 0.5368 -0.0810 -0.0537 -0.2239 216 ASN C OD1 
9956  N ND2 . ASN C 216 ? 0.8645 0.8199 0.7178 -0.0691 -0.0313 -0.2505 216 ASN C ND2 
9957  N N   . VAL C 217 ? 0.4801 0.4717 0.3986 -0.0456 -0.0593 -0.1940 217 VAL C N   
9958  C CA  . VAL C 217 ? 0.3843 0.3876 0.3110 -0.0389 -0.0525 -0.1920 217 VAL C CA  
9959  C C   . VAL C 217 ? 0.5130 0.5257 0.4142 -0.0471 -0.0544 -0.1825 217 VAL C C   
9960  O O   . VAL C 217 ? 0.4830 0.4961 0.3686 -0.0531 -0.0654 -0.1720 217 VAL C O   
9961  C CB  . VAL C 217 ? 0.3532 0.3583 0.3068 -0.0276 -0.0585 -0.1834 217 VAL C CB  
9962  C CG1 . VAL C 217 ? 0.4907 0.4876 0.4703 -0.0175 -0.0544 -0.1936 217 VAL C CG1 
9963  C CG2 . VAL C 217 ? 0.3418 0.3459 0.2940 -0.0295 -0.0728 -0.1686 217 VAL C CG2 
9964  N N   . LYS C 218 ? 0.5179 0.5390 0.4150 -0.0475 -0.0438 -0.1860 218 LYS C N   
9965  C CA  . LYS C 218 ? 0.4026 0.4297 0.2750 -0.0551 -0.0442 -0.1764 218 LYS C CA  
9966  C C   . LYS C 218 ? 0.3704 0.4009 0.2540 -0.0491 -0.0480 -0.1657 218 LYS C C   
9967  O O   . LYS C 218 ? 0.3559 0.3912 0.2604 -0.0430 -0.0412 -0.1713 218 LYS C O   
9968  C CB  . LYS C 218 ? 0.4590 0.4928 0.3167 -0.0625 -0.0293 -0.1864 218 LYS C CB  
9969  C CG  . LYS C 218 ? 0.5781 0.6091 0.4346 -0.0642 -0.0210 -0.2029 218 LYS C CG  
9970  C CD  . LYS C 218 ? 0.5897 0.6267 0.4180 -0.0758 -0.0111 -0.2076 218 LYS C CD  
9971  C CE  . LYS C 218 ? 0.5749 0.6210 0.4153 -0.0738 0.0071  -0.2259 218 LYS C CE  
9972  N NZ  . LYS C 218 ? 0.5746 0.6302 0.3885 -0.0862 0.0186  -0.2294 218 LYS C NZ  
9973  N N   . ILE C 219 ? 0.3789 0.4077 0.2492 -0.0501 -0.0594 -0.1507 219 ILE C N   
9974  C CA  . ILE C 219 ? 0.4275 0.4526 0.3066 -0.0425 -0.0623 -0.1350 219 ILE C CA  
9975  C C   . ILE C 219 ? 0.4345 0.4550 0.2842 -0.0485 -0.0638 -0.1210 219 ILE C C   
9976  O O   . ILE C 219 ? 0.4656 0.4874 0.2911 -0.0562 -0.0678 -0.1189 219 ILE C O   
9977  C CB  . ILE C 219 ? 0.3278 0.3502 0.2264 -0.0322 -0.0739 -0.1252 219 ILE C CB  
9978  C CG1 . ILE C 219 ? 0.3367 0.3605 0.2202 -0.0342 -0.0858 -0.1136 219 ILE C CG1 
9979  C CG2 . ILE C 219 ? 0.3178 0.3408 0.2411 -0.0278 -0.0734 -0.1378 219 ILE C CG2 
9980  C CD1 . ILE C 219 ? 0.3174 0.3416 0.2176 -0.0240 -0.0954 -0.1001 219 ILE C CD1 
9981  N N   . PRO C 220 ? 0.3935 0.4071 0.2430 -0.0458 -0.0610 -0.1109 220 PRO C N   
9982  C CA  . PRO C 220 ? 0.3831 0.3866 0.2028 -0.0516 -0.0611 -0.0974 220 PRO C CA  
9983  C C   . PRO C 220 ? 0.3916 0.3912 0.1979 -0.0470 -0.0746 -0.0818 220 PRO C C   
9984  O O   . PRO C 220 ? 0.4437 0.4498 0.2658 -0.0394 -0.0840 -0.0803 220 PRO C O   
9985  C CB  . PRO C 220 ? 0.3737 0.3670 0.2013 -0.0479 -0.0569 -0.0907 220 PRO C CB  
9986  C CG  . PRO C 220 ? 0.3575 0.3624 0.2142 -0.0457 -0.0503 -0.1054 220 PRO C CG  
9987  C CD  . PRO C 220 ? 0.3395 0.3530 0.2134 -0.0394 -0.0564 -0.1132 220 PRO C CD  
9988  N N   . ASP C 221 ? 0.4628 0.4525 0.2394 -0.0520 -0.0756 -0.0693 221 ASP C N   
9989  C CA  . ASP C 221 ? 0.5220 0.5093 0.2837 -0.0468 -0.0887 -0.0523 221 ASP C CA  
9990  C C   . ASP C 221 ? 0.5165 0.4904 0.2884 -0.0321 -0.0929 -0.0375 221 ASP C C   
9991  O O   . ASP C 221 ? 0.5540 0.5081 0.3094 -0.0316 -0.0894 -0.0272 221 ASP C O   
9992  C CB  . ASP C 221 ? 0.5483 0.5293 0.2718 -0.0580 -0.0882 -0.0444 221 ASP C CB  
9993  C CG  . ASP C 221 ? 0.7715 0.7545 0.4800 -0.0523 -0.1036 -0.0265 221 ASP C CG  
9994  O OD1 . ASP C 221 ? 0.7102 0.7114 0.4309 -0.0497 -0.1135 -0.0293 221 ASP C OD1 
9995  O OD2 . ASP C 221 ? 0.9326 0.8992 0.6173 -0.0507 -0.1060 -0.0092 221 ASP C OD2 
9996  N N   . PHE C 222 ? 0.4476 0.4310 0.2457 -0.0206 -0.0999 -0.0370 222 PHE C N   
9997  C CA  . PHE C 222 ? 0.5438 0.5171 0.3526 -0.0057 -0.1029 -0.0247 222 PHE C CA  
9998  C C   . PHE C 222 ? 0.5536 0.5224 0.3456 0.0026  -0.1126 -0.0056 222 PHE C C   
9999  O O   . PHE C 222 ? 0.4992 0.4830 0.3052 0.0128  -0.1225 0.0016  222 PHE C O   
10000 C CB  . PHE C 222 ? 0.5061 0.4935 0.3469 0.0028  -0.1066 -0.0296 222 PHE C CB  
10001 C CG  . PHE C 222 ? 0.3761 0.3639 0.2356 -0.0006 -0.0981 -0.0445 222 PHE C CG  
10002 C CD1 . PHE C 222 ? 0.3339 0.3309 0.1969 -0.0111 -0.0938 -0.0599 222 PHE C CD1 
10003 C CD2 . PHE C 222 ? 0.4432 0.4228 0.3168 0.0074  -0.0948 -0.0430 222 PHE C CD2 
10004 C CE1 . PHE C 222 ? 0.3350 0.3339 0.2177 -0.0117 -0.0869 -0.0723 222 PHE C CE1 
10005 C CE2 . PHE C 222 ? 0.3935 0.3761 0.2847 0.0048  -0.0889 -0.0550 222 PHE C CE2 
10006 C CZ  . PHE C 222 ? 0.3009 0.2936 0.1980 -0.0039 -0.0853 -0.0689 222 PHE C CZ  
10007 N N   . ALA C 223 ? 0.4640 0.4133 0.2267 -0.0016 -0.1100 0.0035  223 ALA C N   
10008 C CA  . ALA C 223 ? 0.4977 0.4393 0.2421 0.0075  -0.1195 0.0236  223 ALA C CA  
10009 C C   . ALA C 223 ? 0.5679 0.4900 0.3190 0.0259  -0.1195 0.0356  223 ALA C C   
10010 O O   . ALA C 223 ? 0.6786 0.5863 0.4125 0.0357  -0.1252 0.0531  223 ALA C O   
10011 C CB  . ALA C 223 ? 0.6714 0.5964 0.3782 -0.0053 -0.1167 0.0299  223 ALA C CB  
10012 N N   . VAL C 224 ? 0.6092 0.5295 0.3833 0.0313  -0.1132 0.0266  224 VAL C N   
10013 C CA  . VAL C 224 ? 0.5300 0.4330 0.3113 0.0484  -0.1116 0.0345  224 VAL C CA  
10014 C C   . VAL C 224 ? 0.4276 0.3539 0.2424 0.0566  -0.1132 0.0273  224 VAL C C   
10015 O O   . VAL C 224 ? 0.4659 0.4118 0.2965 0.0467  -0.1124 0.0143  224 VAL C O   
10016 C CB  . VAL C 224 ? 0.5332 0.4019 0.2996 0.0427  -0.0999 0.0307  224 VAL C CB  
10017 C CG1 . VAL C 224 ? 0.4680 0.3465 0.2527 0.0322  -0.0921 0.0126  224 VAL C CG1 
10018 C CG2 . VAL C 224 ? 0.5203 0.3622 0.2832 0.0604  -0.0984 0.0410  224 VAL C CG2 
10019 N N   . SER C 225 ? 0.4698 0.3933 0.2949 0.0749  -0.1148 0.0362  225 SER C N   
10020 C CA  . SER C 225 ? 0.5285 0.4773 0.3839 0.0833  -0.1170 0.0327  225 SER C CA  
10021 C C   . SER C 225 ? 0.4982 0.4324 0.3619 0.0856  -0.1071 0.0241  225 SER C C   
10022 O O   . SER C 225 ? 0.4537 0.3601 0.3049 0.0941  -0.1013 0.0281  225 SER C O   
10023 C CB  . SER C 225 ? 0.5281 0.4911 0.3926 0.1025  -0.1247 0.0477  225 SER C CB  
10024 O OG  . SER C 225 ? 0.5590 0.5504 0.4530 0.1082  -0.1263 0.0447  225 SER C OG  
10025 N N   . PHE C 226 ? 0.5390 0.4905 0.4221 0.0776  -0.1057 0.0123  226 PHE C N   
10026 C CA  . PHE C 226 ? 0.4182 0.3633 0.3119 0.0798  -0.0988 0.0051  226 PHE C CA  
10027 C C   . PHE C 226 ? 0.4016 0.3678 0.3179 0.0916  -0.1010 0.0086  226 PHE C C   
10028 O O   . PHE C 226 ? 0.4589 0.4251 0.3852 0.0918  -0.0963 0.0027  226 PHE C O   
10029 C CB  . PHE C 226 ? 0.3876 0.3375 0.2884 0.0644  -0.0959 -0.0087 226 PHE C CB  
10030 C CG  . PHE C 226 ? 0.4085 0.3405 0.2903 0.0518  -0.0908 -0.0141 226 PHE C CG  
10031 C CD1 . PHE C 226 ? 0.4388 0.3459 0.3073 0.0498  -0.0835 -0.0159 226 PHE C CD1 
10032 C CD2 . PHE C 226 ? 0.4721 0.4134 0.3487 0.0404  -0.0927 -0.0183 226 PHE C CD2 
10033 C CE1 . PHE C 226 ? 0.4033 0.2971 0.2556 0.0359  -0.0784 -0.0207 226 PHE C CE1 
10034 C CE2 . PHE C 226 ? 0.4470 0.3756 0.3070 0.0279  -0.0865 -0.0235 226 PHE C CE2 
10035 C CZ  . PHE C 226 ? 0.3509 0.2568 0.1997 0.0253  -0.0795 -0.0242 226 PHE C CZ  
10036 N N   . ARG C 227 ? 0.4920 0.4789 0.4167 0.1002  -0.1083 0.0184  227 ARG C N   
10037 C CA  . ARG C 227 ? 0.4470 0.4602 0.3957 0.1090  -0.1101 0.0217  227 ARG C CA  
10038 C C   . ARG C 227 ? 0.4498 0.4496 0.3984 0.1240  -0.1015 0.0237  227 ARG C C   
10039 O O   . ARG C 227 ? 0.4388 0.4505 0.4024 0.1252  -0.0979 0.0201  227 ARG C O   
10040 C CB  . ARG C 227 ? 0.4046 0.4457 0.3633 0.1140  -0.1190 0.0325  227 ARG C CB  
10041 C CG  . ARG C 227 ? 0.4819 0.5556 0.4699 0.1125  -0.1177 0.0346  227 ARG C CG  
10042 C CD  . ARG C 227 ? 0.5583 0.6591 0.5576 0.0977  -0.1266 0.0346  227 ARG C CD  
10043 N NE  . ARG C 227 ? 0.7230 0.8453 0.7452 0.0907  -0.1254 0.0322  227 ARG C NE  
10044 C CZ  . ARG C 227 ? 0.6817 0.8277 0.7168 0.0781  -0.1325 0.0329  227 ARG C CZ  
10045 N NH1 . ARG C 227 ? 0.6158 0.7694 0.6439 0.0706  -0.1415 0.0352  227 ARG C NH1 
10046 N NH2 . ARG C 227 ? 0.5994 0.7599 0.6527 0.0719  -0.1313 0.0312  227 ARG C NH2 
10047 N N   . GLU C 228 ? 0.4952 0.4676 0.4248 0.1349  -0.0978 0.0292  228 GLU C N   
10048 C CA  . GLU C 228 ? 0.5135 0.4678 0.4392 0.1494  -0.0884 0.0292  228 GLU C CA  
10049 C C   . GLU C 228 ? 0.5107 0.4427 0.4265 0.1385  -0.0804 0.0169  228 GLU C C   
10050 O O   . GLU C 228 ? 0.5689 0.4947 0.4857 0.1459  -0.0729 0.0134  228 GLU C O   
10051 C CB  . GLU C 228 ? 0.5417 0.4677 0.4480 0.1646  -0.0868 0.0386  228 GLU C CB  
10052 C CG  . GLU C 228 ? 0.6668 0.5732 0.5511 0.1545  -0.0918 0.0423  228 GLU C CG  
10053 C CD  . GLU C 228 ? 0.8214 0.7566 0.7141 0.1552  -0.1034 0.0528  228 GLU C CD  
10054 O OE1 . GLU C 228 ? 0.6495 0.6199 0.5622 0.1454  -0.1090 0.0493  228 GLU C OE1 
10055 O OE2 . GLU C 228 ? 0.8821 0.8052 0.7630 0.1615  -0.1053 0.0639  228 GLU C OE2 
10056 N N   . ASP C 229 ? 0.5186 0.4405 0.4247 0.1209  -0.0818 0.0100  229 ASP C N   
10057 C CA  . ASP C 229 ? 0.4848 0.3912 0.3843 0.1098  -0.0758 -0.0011 229 ASP C CA  
10058 C C   . ASP C 229 ? 0.3457 0.2778 0.2665 0.1044  -0.0772 -0.0067 229 ASP C C   
10059 O O   . ASP C 229 ? 0.3487 0.2736 0.2674 0.1025  -0.0723 -0.0126 229 ASP C O   
10060 C CB  . ASP C 229 ? 0.5888 0.4806 0.4740 0.0935  -0.0762 -0.0063 229 ASP C CB  
10061 C CG  . ASP C 229 ? 0.5924 0.4470 0.4501 0.0948  -0.0713 -0.0033 229 ASP C CG  
10062 O OD1 . ASP C 229 ? 0.5484 0.3897 0.3989 0.1110  -0.0701 0.0054  229 ASP C OD1 
10063 O OD2 . ASP C 229 ? 0.4665 0.3050 0.3105 0.0798  -0.0685 -0.0093 229 ASP C OD2 
10064 N N   . ALA C 230 ? 0.2838 0.2444 0.2232 0.1008  -0.0843 -0.0046 230 ALA C N   
10065 C CA  . ALA C 230 ? 0.3869 0.3694 0.3459 0.0970  -0.0858 -0.0074 230 ALA C CA  
10066 C C   . ALA C 230 ? 0.5062 0.4961 0.4713 0.1095  -0.0810 -0.0031 230 ALA C C   
10067 O O   . ALA C 230 ? 0.5103 0.5076 0.4827 0.1063  -0.0788 -0.0060 230 ALA C O   
10068 C CB  . ALA C 230 ? 0.3353 0.3430 0.3108 0.0906  -0.0940 -0.0057 230 ALA C CB  
10069 N N   . SER C 231 ? 0.4608 0.4496 0.4228 0.1245  -0.0790 0.0043  231 SER C N   
10070 C CA  . SER C 231 ? 0.3428 0.3380 0.3096 0.1386  -0.0719 0.0072  231 SER C CA  
10071 C C   . SER C 231 ? 0.4132 0.3774 0.3597 0.1405  -0.0624 -0.0001 231 SER C C   
10072 O O   . SER C 231 ? 0.4011 0.3706 0.3498 0.1433  -0.0562 -0.0028 231 SER C O   
10073 C CB  . SER C 231 ? 0.3728 0.3769 0.3442 0.1564  -0.0727 0.0173  231 SER C CB  
10074 O OG  . SER C 231 ? 0.6072 0.6386 0.5972 0.1657  -0.0679 0.0213  231 SER C OG  
10075 N N   . LYS C 232 ? 0.4254 0.3567 0.3500 0.1373  -0.0610 -0.0034 232 LYS C N   
10076 C CA  . LYS C 232 ? 0.4251 0.3246 0.3279 0.1361  -0.0526 -0.0113 232 LYS C CA  
10077 C C   . LYS C 232 ? 0.4399 0.3459 0.3449 0.1208  -0.0532 -0.0196 232 LYS C C   
10078 O O   . LYS C 232 ? 0.4918 0.3884 0.3869 0.1215  -0.0467 -0.0251 232 LYS C O   
10079 C CB  . LYS C 232 ? 0.4668 0.3305 0.3460 0.1317  -0.0518 -0.0127 232 LYS C CB  
10080 C CG  . LYS C 232 ? 0.5518 0.3773 0.4069 0.1415  -0.0421 -0.0156 232 LYS C CG  
10081 C CD  . LYS C 232 ? 0.7816 0.5728 0.6154 0.1417  -0.0421 -0.0115 232 LYS C CD  
10082 C CE  . LYS C 232 ? 0.6894 0.4941 0.5335 0.1561  -0.0479 0.0019  232 LYS C CE  
10083 N NZ  . LYS C 232 ? 0.7316 0.5092 0.5558 0.1508  -0.0509 0.0075  232 LYS C NZ  
10084 N N   . HIS C 233 ? 0.3860 0.3077 0.3029 0.1074  -0.0611 -0.0207 233 HIS C N   
10085 C CA  . HIS C 233 ? 0.2917 0.2210 0.2132 0.0947  -0.0632 -0.0268 233 HIS C CA  
10086 C C   . HIS C 233 ? 0.3139 0.2628 0.2463 0.0990  -0.0615 -0.0244 233 HIS C C   
10087 O O   . HIS C 233 ? 0.3715 0.3155 0.2954 0.0946  -0.0587 -0.0289 233 HIS C O   
10088 C CB  . HIS C 233 ? 0.3041 0.2479 0.2397 0.0834  -0.0713 -0.0277 233 HIS C CB  
10089 C CG  . HIS C 233 ? 0.3675 0.2943 0.2910 0.0733  -0.0715 -0.0334 233 HIS C CG  
10090 N ND1 . HIS C 233 ? 0.4502 0.3756 0.3725 0.0711  -0.0738 -0.0317 233 HIS C ND1 
10091 C CD2 . HIS C 233 ? 0.3648 0.2780 0.2767 0.0632  -0.0695 -0.0406 233 HIS C CD2 
10092 C CE1 . HIS C 233 ? 0.3900 0.3014 0.3007 0.0602  -0.0721 -0.0375 233 HIS C CE1 
10093 N NE2 . HIS C 233 ? 0.3645 0.2691 0.2700 0.0551  -0.0697 -0.0430 233 HIS C NE2 
10094 N N   . VAL C 234 ? 0.3317 0.3044 0.2821 0.1061  -0.0634 -0.0169 234 VAL C N   
10095 C CA  . VAL C 234 ? 0.3333 0.3272 0.2947 0.1082  -0.0612 -0.0135 234 VAL C CA  
10096 C C   . VAL C 234 ? 0.3498 0.3343 0.2977 0.1200  -0.0502 -0.0151 234 VAL C C   
10097 O O   . VAL C 234 ? 0.3192 0.3073 0.2621 0.1172  -0.0459 -0.0173 234 VAL C O   
10098 C CB  . VAL C 234 ? 0.2498 0.2734 0.2346 0.1103  -0.0661 -0.0054 234 VAL C CB  
10099 C CG1 . VAL C 234 ? 0.3067 0.3530 0.3019 0.1132  -0.0615 -0.0007 234 VAL C CG1 
10100 C CG2 . VAL C 234 ? 0.2670 0.2973 0.2631 0.0970  -0.0759 -0.0061 234 VAL C CG2 
10101 N N   . GLU C 235 ? 0.4142 0.3852 0.3544 0.1337  -0.0452 -0.0141 235 GLU C N   
10102 C CA  . GLU C 235 ? 0.3362 0.2974 0.2649 0.1480  -0.0333 -0.0163 235 GLU C CA  
10103 C C   . GLU C 235 ? 0.3709 0.3004 0.2720 0.1414  -0.0274 -0.0270 235 GLU C C   
10104 O O   . GLU C 235 ? 0.5037 0.4342 0.3961 0.1432  -0.0195 -0.0313 235 GLU C O   
10105 C CB  . GLU C 235 ? 0.4934 0.4450 0.4213 0.1662  -0.0302 -0.0116 235 GLU C CB  
10106 C CG  . GLU C 235 ? 0.6112 0.6007 0.5658 0.1785  -0.0314 -0.0016 235 GLU C CG  
10107 C CD  . GLU C 235 ? 0.8671 0.8641 0.8233 0.1971  -0.0185 -0.0019 235 GLU C CD  
10108 O OE1 . GLU C 235 ? 0.9048 0.8723 0.8443 0.2123  -0.0104 -0.0050 235 GLU C OE1 
10109 O OE2 . GLU C 235 ? 0.8973 0.9285 0.8708 0.1964  -0.0156 0.0008  235 GLU C OE2 
10110 N N   . LEU C 236 ? 0.4076 0.3100 0.2936 0.1323  -0.0311 -0.0317 236 LEU C N   
10111 C CA  . LEU C 236 ? 0.4028 0.2756 0.2622 0.1233  -0.0267 -0.0423 236 LEU C CA  
10112 C C   . LEU C 236 ? 0.4587 0.3477 0.3196 0.1091  -0.0303 -0.0456 236 LEU C C   
10113 O O   . LEU C 236 ? 0.5618 0.4347 0.4011 0.1037  -0.0254 -0.0538 236 LEU C O   
10114 C CB  . LEU C 236 ? 0.3961 0.2422 0.2424 0.1134  -0.0306 -0.0455 236 LEU C CB  
10115 C CG  . LEU C 236 ? 0.4483 0.2563 0.2736 0.1235  -0.0237 -0.0465 236 LEU C CG  
10116 C CD1 . LEU C 236 ? 0.4458 0.2616 0.2820 0.1467  -0.0193 -0.0381 236 LEU C CD1 
10117 C CD2 . LEU C 236 ? 0.5978 0.3904 0.4176 0.1125  -0.0296 -0.0451 236 LEU C CD2 
10118 N N   . ALA C 237 ? 0.4097 0.3283 0.2938 0.1027  -0.0393 -0.0391 237 ALA C N   
10119 C CA  . ALA C 237 ? 0.3511 0.2853 0.2379 0.0914  -0.0436 -0.0394 237 ALA C CA  
10120 C C   . ALA C 237 ? 0.4142 0.3596 0.2967 0.0978  -0.0354 -0.0381 237 ALA C C   
10121 O O   . ALA C 237 ? 0.4656 0.4101 0.3342 0.0896  -0.0347 -0.0416 237 ALA C O   
10122 C CB  . ALA C 237 ? 0.3633 0.3216 0.2757 0.0849  -0.0544 -0.0324 237 ALA C CB  
10123 N N   . LYS C 238 ? 0.4178 0.3768 0.3123 0.1119  -0.0292 -0.0327 238 LYS C N   
10124 C CA  . LYS C 238 ? 0.4157 0.3881 0.3069 0.1188  -0.0190 -0.0320 238 LYS C CA  
10125 C C   . LYS C 238 ? 0.5140 0.4581 0.3750 0.1241  -0.0071 -0.0432 238 LYS C C   
10126 O O   . LYS C 238 ? 0.5631 0.5120 0.4109 0.1221  0.0002  -0.0465 238 LYS C O   
10127 C CB  . LYS C 238 ? 0.4806 0.4784 0.3951 0.1331  -0.0149 -0.0238 238 LYS C CB  
10128 C CG  . LYS C 238 ? 0.4471 0.4735 0.3892 0.1254  -0.0260 -0.0138 238 LYS C CG  
10129 C CD  . LYS C 238 ? 0.4212 0.4732 0.3864 0.1379  -0.0239 -0.0061 238 LYS C CD  
10130 C CE  . LYS C 238 ? 0.4473 0.5230 0.4172 0.1463  -0.0117 -0.0039 238 LYS C CE  
10131 N NZ  . LYS C 238 ? 0.6316 0.7302 0.6222 0.1631  -0.0079 0.0019  238 LYS C NZ  
10132 N N   . GLU C 239 ? 0.4884 0.4011 0.3361 0.1300  -0.0045 -0.0491 239 GLU C N   
10133 C CA  . GLU C 239 ? 0.4808 0.3591 0.2964 0.1328  0.0063  -0.0613 239 GLU C CA  
10134 C C   . GLU C 239 ? 0.6258 0.4942 0.4200 0.1125  0.0018  -0.0691 239 GLU C C   
10135 O O   . GLU C 239 ? 0.5861 0.4475 0.3581 0.1104  0.0099  -0.0769 239 GLU C O   
10136 C CB  . GLU C 239 ? 0.5242 0.3670 0.3292 0.1408  0.0084  -0.0644 239 GLU C CB  
10137 C CG  . GLU C 239 ? 0.7856 0.6102 0.5813 0.1636  0.0230  -0.0677 239 GLU C CG  
10138 C CD  . GLU C 239 ? 0.9340 0.7123 0.7101 0.1689  0.0254  -0.0718 239 GLU C CD  
10139 O OE1 . GLU C 239 ? 0.7497 0.5202 0.5289 0.1584  0.0149  -0.0678 239 GLU C OE1 
10140 O OE2 . GLU C 239 ? 0.9433 0.6915 0.6999 0.1834  0.0384  -0.0793 239 GLU C OE2 
10141 N N   . LYS C 240 ? 0.5783 0.4480 0.3791 0.0975  -0.0114 -0.0671 240 LYS C N   
10142 C CA  . LYS C 240 ? 0.5424 0.4083 0.3271 0.0784  -0.0179 -0.0730 240 LYS C CA  
10143 C C   . LYS C 240 ? 0.5315 0.4258 0.3202 0.0731  -0.0204 -0.0680 240 LYS C C   
10144 O O   . LYS C 240 ? 0.6188 0.5086 0.3856 0.0615  -0.0212 -0.0739 240 LYS C O   
10145 C CB  . LYS C 240 ? 0.5285 0.3965 0.3255 0.0659  -0.0309 -0.0710 240 LYS C CB  
10146 C CG  . LYS C 240 ? 0.5166 0.3890 0.3043 0.0468  -0.0401 -0.0751 240 LYS C CG  
10147 C CD  . LYS C 240 ? 0.6180 0.4613 0.3697 0.0384  -0.0337 -0.0883 240 LYS C CD  
10148 C CE  . LYS C 240 ? 0.6885 0.4979 0.4271 0.0362  -0.0300 -0.0956 240 LYS C CE  
10149 N NZ  . LYS C 240 ? 0.6225 0.4085 0.3303 0.0184  -0.0299 -0.1082 240 LYS C NZ  
10150 N N   . TYR C 241 ? 0.4460 0.3692 0.2609 0.0800  -0.0222 -0.0566 241 TYR C N   
10151 C CA  . TYR C 241 ? 0.4837 0.4316 0.3007 0.0753  -0.0228 -0.0503 241 TYR C CA  
10152 C C   . TYR C 241 ? 0.5034 0.4464 0.2971 0.0817  -0.0074 -0.0568 241 TYR C C   
10153 O O   . TYR C 241 ? 0.5300 0.4782 0.3054 0.0720  -0.0070 -0.0581 241 TYR C O   
10154 C CB  . TYR C 241 ? 0.5084 0.4853 0.3578 0.0799  -0.0271 -0.0371 241 TYR C CB  
10155 C CG  . TYR C 241 ? 0.5353 0.5357 0.3892 0.0711  -0.0313 -0.0277 241 TYR C CG  
10156 C CD1 . TYR C 241 ? 0.4746 0.4814 0.3375 0.0592  -0.0459 -0.0212 241 TYR C CD1 
10157 C CD2 . TYR C 241 ? 0.4398 0.4560 0.2894 0.0753  -0.0202 -0.0245 241 TYR C CD2 
10158 C CE1 . TYR C 241 ? 0.5855 0.6097 0.4508 0.0515  -0.0504 -0.0108 241 TYR C CE1 
10159 C CE2 . TYR C 241 ? 0.3913 0.4272 0.2427 0.0656  -0.0239 -0.0144 241 TYR C CE2 
10160 C CZ  . TYR C 241 ? 0.5328 0.5707 0.3912 0.0537  -0.0395 -0.0070 241 TYR C CZ  
10161 O OH  . TYR C 241 ? 0.4812 0.5347 0.3396 0.0444  -0.0438 0.0048  241 TYR C OH  
10162 N N   . PHE C 242 ? 0.4731 0.4062 0.2665 0.0988  0.0055  -0.0610 242 PHE C N   
10163 C CA  . PHE C 242 ? 0.5152 0.4423 0.2871 0.1076  0.0225  -0.0693 242 PHE C CA  
10164 C C   . PHE C 242 ? 0.5183 0.4119 0.2509 0.0980  0.0260  -0.0843 242 PHE C C   
10165 O O   . PHE C 242 ? 0.5483 0.4391 0.2564 0.0976  0.0372  -0.0921 242 PHE C O   
10166 C CB  . PHE C 242 ? 0.4874 0.4103 0.2704 0.1307  0.0348  -0.0703 242 PHE C CB  
10167 C CG  . PHE C 242 ? 0.5515 0.4807 0.3233 0.1437  0.0537  -0.0762 242 PHE C CG  
10168 C CD1 . PHE C 242 ? 0.5623 0.4565 0.3000 0.1488  0.0669  -0.0922 242 PHE C CD1 
10169 C CD2 . PHE C 242 ? 0.6556 0.6256 0.4503 0.1499  0.0591  -0.0666 242 PHE C CD2 
10170 C CE1 . PHE C 242 ? 0.6210 0.5212 0.3479 0.1620  0.0860  -0.0992 242 PHE C CE1 
10171 C CE2 . PHE C 242 ? 0.6421 0.6221 0.4281 0.1620  0.0781  -0.0725 242 PHE C CE2 
10172 C CZ  . PHE C 242 ? 0.5734 0.5185 0.3255 0.1691  0.0920  -0.0892 242 PHE C CZ  
10173 N N   . GLU C 243 ? 0.5873 0.4559 0.3121 0.0888  0.0169  -0.0893 243 GLU C N   
10174 C CA  . GLU C 243 ? 0.6268 0.4641 0.3145 0.0760  0.0187  -0.1038 243 GLU C CA  
10175 C C   . GLU C 243 ? 0.6269 0.4807 0.3022 0.0556  0.0084  -0.1028 243 GLU C C   
10176 O O   . GLU C 243 ? 0.6960 0.5316 0.3365 0.0452  0.0124  -0.1150 243 GLU C O   
10177 C CB  . GLU C 243 ? 0.6185 0.4263 0.3031 0.0705  0.0123  -0.1085 243 GLU C CB  
10178 C CG  . GLU C 243 ? 0.8544 0.6226 0.4989 0.0589  0.0171  -0.1253 243 GLU C CG  
10179 C CD  . GLU C 243 ? 0.9639 0.7069 0.6063 0.0488  0.0097  -0.1283 243 GLU C CD  
10180 O OE1 . GLU C 243 ? 0.8363 0.5987 0.5078 0.0471  -0.0015 -0.1175 243 GLU C OE1 
10181 O OE2 . GLU C 243 ? 1.0597 0.7695 0.6784 0.0406  0.0154  -0.1396 243 GLU C OE2 
10182 N N   . ILE C 244 ? 0.5194 0.4056 0.2208 0.0497  -0.0050 -0.0885 244 ILE C N   
10183 C CA  . ILE C 244 ? 0.5188 0.4202 0.2113 0.0314  -0.0177 -0.0849 244 ILE C CA  
10184 C C   . ILE C 244 ? 0.5546 0.4809 0.2439 0.0320  -0.0134 -0.0769 244 ILE C C   
10185 O O   . ILE C 244 ? 0.6520 0.5820 0.3160 0.0191  -0.0163 -0.0787 244 ILE C O   
10186 C CB  . ILE C 244 ? 0.5093 0.4266 0.2309 0.0242  -0.0359 -0.0746 244 ILE C CB  
10187 C CG1 . ILE C 244 ? 0.5302 0.4243 0.2491 0.0191  -0.0396 -0.0837 244 ILE C CG1 
10188 C CG2 . ILE C 244 ? 0.6688 0.6074 0.3874 0.0095  -0.0500 -0.0668 244 ILE C CG2 
10189 C CD1 . ILE C 244 ? 0.8119 0.6996 0.5081 -0.0007 -0.0485 -0.0917 244 ILE C CD1 
10190 N N   . PHE C 245 ? 0.5016 0.4461 0.2152 0.0456  -0.0066 -0.0676 245 PHE C N   
10191 C CA  . PHE C 245 ? 0.5031 0.4737 0.2169 0.0449  -0.0020 -0.0582 245 PHE C CA  
10192 C C   . PHE C 245 ? 0.5201 0.4944 0.2302 0.0602  0.0190  -0.0630 245 PHE C C   
10193 O O   . PHE C 245 ? 0.5285 0.5244 0.2336 0.0583  0.0261  -0.0573 245 PHE C O   
10194 C CB  . PHE C 245 ? 0.4641 0.4610 0.2130 0.0431  -0.0144 -0.0401 245 PHE C CB  
10195 C CG  . PHE C 245 ? 0.4754 0.4714 0.2329 0.0314  -0.0342 -0.0347 245 PHE C CG  
10196 C CD1 . PHE C 245 ? 0.5169 0.5173 0.2557 0.0169  -0.0444 -0.0314 245 PHE C CD1 
10197 C CD2 . PHE C 245 ? 0.4881 0.4808 0.2726 0.0354  -0.0426 -0.0329 245 PHE C CD2 
10198 C CE1 . PHE C 245 ? 0.4467 0.4499 0.1969 0.0083  -0.0627 -0.0261 245 PHE C CE1 
10199 C CE2 . PHE C 245 ? 0.4033 0.3979 0.1979 0.0262  -0.0592 -0.0290 245 PHE C CE2 
10200 C CZ  . PHE C 245 ? 0.4172 0.4177 0.1963 0.0136  -0.0693 -0.0255 245 PHE C CZ  
10201 N N   . GLY C 246 ? 0.6456 0.6004 0.3583 0.0758  0.0293  -0.0726 246 GLY C N   
10202 C CA  . GLY C 246 ? 0.6154 0.5722 0.3238 0.0930  0.0501  -0.0791 246 GLY C CA  
10203 C C   . GLY C 246 ? 0.6398 0.6349 0.3804 0.1026  0.0552  -0.0658 246 GLY C C   
10204 O O   . GLY C 246 ? 0.6205 0.6283 0.3570 0.1134  0.0728  -0.0694 246 GLY C O   
10205 N N   . GLU C 247 ? 0.6535 0.6682 0.4262 0.0983  0.0408  -0.0512 247 GLU C N   
10206 C CA  . GLU C 247 ? 0.6445 0.6968 0.4473 0.1028  0.0439  -0.0380 247 GLU C CA  
10207 C C   . GLU C 247 ? 0.5013 0.5614 0.3387 0.1160  0.0403  -0.0328 247 GLU C C   
10208 O O   . GLU C 247 ? 0.5218 0.6000 0.3745 0.1317  0.0527  -0.0322 247 GLU C O   
10209 C CB  . GLU C 247 ? 0.6518 0.7230 0.4602 0.0838  0.0307  -0.0239 247 GLU C CB  
10210 C CG  . GLU C 247 ? 0.6570 0.7597 0.4662 0.0799  0.0413  -0.0157 247 GLU C CG  
10211 C CD  . GLU C 247 ? 0.8750 0.9934 0.6939 0.0624  0.0273  0.0011  247 GLU C CD  
10212 O OE1 . GLU C 247 ? 0.6968 0.7986 0.5115 0.0524  0.0105  0.0038  247 GLU C OE1 
10213 O OE2 . GLU C 247 ? 1.2134 1.3606 1.0448 0.0586  0.0333  0.0117  247 GLU C OE2 
10214 N N   . HIS C 248 ? 0.4779 0.5260 0.3272 0.1103  0.0239  -0.0292 248 HIS C N   
10215 C CA  . HIS C 248 ? 0.4734 0.5298 0.3538 0.1162  0.0152  -0.0222 248 HIS C CA  
10216 C C   . HIS C 248 ? 0.4842 0.5616 0.3847 0.1016  0.0016  -0.0092 248 HIS C C   
10217 O O   . HIS C 248 ? 0.5546 0.6559 0.4592 0.0949  0.0049  -0.0014 248 HIS C O   
10218 C CB  . HIS C 248 ? 0.4065 0.4827 0.3071 0.1351  0.0263  -0.0202 248 HIS C CB  
10219 C CG  . HIS C 248 ? 0.5340 0.5838 0.4282 0.1523  0.0315  -0.0288 248 HIS C CG  
10220 N ND1 . HIS C 248 ? 0.7108 0.7661 0.6082 0.1733  0.0466  -0.0323 248 HIS C ND1 
10221 C CD2 . HIS C 248 ? 0.5262 0.5431 0.4107 0.1518  0.0237  -0.0338 248 HIS C CD2 
10222 C CE1 . HIS C 248 ? 0.6888 0.7121 0.5774 0.1856  0.0473  -0.0384 248 HIS C CE1 
10223 N NE2 . HIS C 248 ? 0.6831 0.6827 0.5630 0.1716  0.0337  -0.0393 248 HIS C NE2 
10224 N N   . PRO C 249 ? 0.4304 0.4986 0.3429 0.0962  -0.0127 -0.0068 249 PRO C N   
10225 C CA  . PRO C 249 ? 0.4258 0.5071 0.3542 0.0826  -0.0254 0.0038  249 PRO C CA  
10226 C C   . PRO C 249 ? 0.4035 0.5122 0.3611 0.0844  -0.0260 0.0133  249 PRO C C   
10227 O O   . PRO C 249 ? 0.3380 0.4553 0.3088 0.0965  -0.0214 0.0120  249 PRO C O   
10228 C CB  . PRO C 249 ? 0.3353 0.3954 0.2648 0.0784  -0.0382 -0.0001 249 PRO C CB  
10229 C CG  . PRO C 249 ? 0.3967 0.4421 0.3235 0.0911  -0.0328 -0.0084 249 PRO C CG  
10230 C CD  . PRO C 249 ? 0.4548 0.4996 0.3666 0.1024  -0.0169 -0.0137 249 PRO C CD  
10231 N N   . VAL C 250 ? 0.3240 0.4462 0.2910 0.0713  -0.0326 0.0235  250 VAL C N   
10232 C CA  . VAL C 250 ? 0.2709 0.4165 0.2648 0.0675  -0.0360 0.0326  250 VAL C CA  
10233 C C   . VAL C 250 ? 0.2580 0.3942 0.2615 0.0549  -0.0511 0.0381  250 VAL C C   
10234 O O   . VAL C 250 ? 0.2938 0.4438 0.3177 0.0492  -0.0557 0.0443  250 VAL C O   
10235 C CB  . VAL C 250 ? 0.2991 0.4740 0.2973 0.0632  -0.0259 0.0409  250 VAL C CB  
10236 C CG1 . VAL C 250 ? 0.2935 0.4816 0.2876 0.0789  -0.0094 0.0347  250 VAL C CG1 
10237 C CG2 . VAL C 250 ? 0.3688 0.5374 0.3482 0.0497  -0.0273 0.0469  250 VAL C CG2 
10238 N N   . TYR C 251 ? 0.2809 0.3945 0.2706 0.0502  -0.0588 0.0356  251 TYR C N   
10239 C CA  . TYR C 251 ? 0.2583 0.3598 0.2577 0.0421  -0.0725 0.0387  251 TYR C CA  
10240 C C   . TYR C 251 ? 0.3098 0.3921 0.3058 0.0478  -0.0776 0.0282  251 TYR C C   
10241 O O   . TYR C 251 ? 0.3055 0.3771 0.2835 0.0520  -0.0738 0.0210  251 TYR C O   
10242 C CB  . TYR C 251 ? 0.3382 0.4339 0.3277 0.0316  -0.0784 0.0476  251 TYR C CB  
10243 C CG  . TYR C 251 ? 0.3455 0.4591 0.3300 0.0251  -0.0705 0.0576  251 TYR C CG  
10244 C CD1 . TYR C 251 ? 0.4173 0.5481 0.4198 0.0189  -0.0690 0.0655  251 TYR C CD1 
10245 C CD2 . TYR C 251 ? 0.3754 0.4901 0.3361 0.0235  -0.0642 0.0587  251 TYR C CD2 
10246 C CE1 . TYR C 251 ? 0.4280 0.5780 0.4269 0.0112  -0.0607 0.0749  251 TYR C CE1 
10247 C CE2 . TYR C 251 ? 0.5270 0.6599 0.4819 0.0167  -0.0555 0.0677  251 TYR C CE2 
10248 C CZ  . TYR C 251 ? 0.4957 0.6470 0.4708 0.0105  -0.0534 0.0761  251 TYR C CZ  
10249 O OH  . TYR C 251 ? 0.4847 0.6570 0.4552 0.0020  -0.0438 0.0855  251 TYR C OH  
10250 N N   . MET C 252 ? 0.3649 0.4427 0.3767 0.0466  -0.0854 0.0266  252 MET C N   
10251 C CA  . MET C 252 ? 0.3222 0.3845 0.3324 0.0504  -0.0896 0.0171  252 MET C CA  
10252 C C   . MET C 252 ? 0.2585 0.3130 0.2812 0.0445  -0.1003 0.0180  252 MET C C   
10253 O O   . MET C 252 ? 0.4473 0.5062 0.4824 0.0388  -0.1042 0.0245  252 MET C O   
10254 C CB  . MET C 252 ? 0.3621 0.4269 0.3772 0.0582  -0.0854 0.0116  252 MET C CB  
10255 C CG  . MET C 252 ? 0.5447 0.6082 0.5455 0.0680  -0.0750 0.0076  252 MET C CG  
10256 S SD  . MET C 252 ? 0.6793 0.7273 0.6749 0.0763  -0.0738 -0.0012 252 MET C SD  
10257 C CE  . MET C 252 ? 0.3789 0.4166 0.3523 0.0867  -0.0611 -0.0058 252 MET C CE  
10258 N N   . TRP C 253 ? 0.2623 0.3049 0.2817 0.0457  -0.1045 0.0109  253 TRP C N   
10259 C CA  . TRP C 253 ? 0.2307 0.2665 0.2637 0.0433  -0.1129 0.0090  253 TRP C CA  
10260 C C   . TRP C 253 ? 0.2380 0.2702 0.2747 0.0464  -0.1114 -0.0011 253 TRP C C   
10261 O O   . TRP C 253 ? 0.3459 0.3728 0.3731 0.0486  -0.1091 -0.0080 253 TRP C O   
10262 C CB  . TRP C 253 ? 0.2141 0.2444 0.2440 0.0421  -0.1194 0.0096  253 TRP C CB  
10263 C CG  . TRP C 253 ? 0.2087 0.2333 0.2534 0.0431  -0.1261 0.0047  253 TRP C CG  
10264 C CD1 . TRP C 253 ? 0.2603 0.2838 0.3061 0.0449  -0.1267 -0.0046 253 TRP C CD1 
10265 C CD2 . TRP C 253 ? 0.2355 0.2546 0.2960 0.0422  -0.1317 0.0080  253 TRP C CD2 
10266 N NE1 . TRP C 253 ? 0.2023 0.2223 0.2636 0.0455  -0.1284 -0.0075 253 TRP C NE1 
10267 C CE2 . TRP C 253 ? 0.2072 0.2222 0.2769 0.0446  -0.1318 -0.0005 253 TRP C CE2 
10268 C CE3 . TRP C 253 ? 0.3024 0.3181 0.3683 0.0380  -0.1337 0.0169  253 TRP C CE3 
10269 C CZ2 . TRP C 253 ? 0.2118 0.2180 0.2965 0.0460  -0.1361 -0.0014 253 TRP C CZ2 
10270 C CZ3 . TRP C 253 ? 0.2495 0.2537 0.3294 0.0378  -0.1391 0.0166  253 TRP C CZ3 
10271 C CH2 . TRP C 253 ? 0.2206 0.2194 0.3102 0.0432  -0.1412 0.0070  253 TRP C CH2 
10272 N N   . PRO C 254 ? 0.1926 0.2271 0.2406 0.0453  -0.1124 -0.0021 254 PRO C N   
10273 C CA  . PRO C 254 ? 0.1868 0.2181 0.2354 0.0472  -0.1113 -0.0110 254 PRO C CA  
10274 C C   . PRO C 254 ? 0.2139 0.2371 0.2654 0.0466  -0.1144 -0.0185 254 PRO C C   
10275 O O   . PRO C 254 ? 0.1926 0.2129 0.2545 0.0451  -0.1198 -0.0173 254 PRO C O   
10276 C CB  . PRO C 254 ? 0.2327 0.2693 0.2927 0.0433  -0.1138 -0.0098 254 PRO C CB  
10277 C CG  . PRO C 254 ? 0.1898 0.2261 0.2579 0.0381  -0.1179 -0.0022 254 PRO C CG  
10278 C CD  . PRO C 254 ? 0.2077 0.2472 0.2667 0.0400  -0.1153 0.0049  254 PRO C CD  
10279 N N   . PRO C 255 ? 0.2230 0.2426 0.2662 0.0480  -0.1109 -0.0259 255 PRO C N   
10280 C CA  . PRO C 255 ? 0.2463 0.2635 0.2934 0.0466  -0.1128 -0.0331 255 PRO C CA  
10281 C C   . PRO C 255 ? 0.2453 0.2623 0.3081 0.0460  -0.1160 -0.0378 255 PRO C C   
10282 O O   . PRO C 255 ? 0.3082 0.3241 0.3721 0.0446  -0.1147 -0.0408 255 PRO C O   
10283 C CB  . PRO C 255 ? 0.2735 0.2863 0.3070 0.0459  -0.1071 -0.0394 255 PRO C CB  
10284 C CG  . PRO C 255 ? 0.2630 0.2727 0.2827 0.0492  -0.1027 -0.0340 255 PRO C CG  
10285 C CD  . PRO C 255 ? 0.2302 0.2477 0.2596 0.0509  -0.1048 -0.0270 255 PRO C CD  
10286 N N   . GLU C 256 ? 0.2755 0.2934 0.3498 0.0473  -0.1204 -0.0388 256 GLU C N   
10287 C CA  . GLU C 256 ? 0.2013 0.2163 0.2915 0.0490  -0.1228 -0.0440 256 GLU C CA  
10288 C C   . GLU C 256 ? 0.1904 0.1978 0.2845 0.0472  -0.1251 -0.0398 256 GLU C C   
10289 O O   . GLU C 256 ? 0.1997 0.2012 0.3005 0.0463  -0.1247 -0.0469 256 GLU C O   
10290 C CB  . GLU C 256 ? 0.3127 0.3299 0.4033 0.0479  -0.1175 -0.0564 256 GLU C CB  
10291 C CG  . GLU C 256 ? 0.3817 0.4060 0.4646 0.0459  -0.1138 -0.0604 256 GLU C CG  
10292 C CD  . GLU C 256 ? 0.4170 0.4513 0.5141 0.0484  -0.1166 -0.0632 256 GLU C CD  
10293 O OE1 . GLU C 256 ? 0.3479 0.3821 0.4604 0.0540  -0.1222 -0.0601 256 GLU C OE1 
10294 O OE2 . GLU C 256 ? 0.4073 0.4499 0.5006 0.0445  -0.1135 -0.0680 256 GLU C OE2 
10295 N N   . ALA C 257 ? 0.1918 0.1998 0.2805 0.0453  -0.1268 -0.0288 257 ALA C N   
10296 C CA  . ALA C 257 ? 0.2356 0.2396 0.3272 0.0406  -0.1287 -0.0231 257 ALA C CA  
10297 C C   . ALA C 257 ? 0.2677 0.2749 0.3564 0.0365  -0.1258 -0.0291 257 ALA C C   
10298 O O   . ALA C 257 ? 0.2566 0.2609 0.3495 0.0306  -0.1281 -0.0276 257 ALA C O   
10299 C CB  . ALA C 257 ? 0.2106 0.2009 0.3144 0.0408  -0.1341 -0.0219 257 ALA C CB  
10300 N N   . SER C 258 ? 0.2234 0.2361 0.3037 0.0384  -0.1215 -0.0351 258 SER C N   
10301 C CA  . SER C 258 ? 0.1880 0.2042 0.2639 0.0350  -0.1200 -0.0400 258 SER C CA  
10302 C C   . SER C 258 ? 0.1877 0.2140 0.2630 0.0317  -0.1212 -0.0313 258 SER C C   
10303 O O   . SER C 258 ? 0.1839 0.2181 0.2552 0.0352  -0.1190 -0.0233 258 SER C O   
10304 C CB  . SER C 258 ? 0.3041 0.3226 0.3683 0.0377  -0.1152 -0.0449 258 SER C CB  
10305 O OG  . SER C 258 ? 0.2905 0.3068 0.3524 0.0343  -0.1140 -0.0547 258 SER C OG  
10306 N N   . VAL C 259 ? 0.2515 0.2790 0.3309 0.0245  -0.1244 -0.0335 259 VAL C N   
10307 C CA  . VAL C 259 ? 0.2642 0.3057 0.3468 0.0192  -0.1266 -0.0254 259 VAL C CA  
10308 C C   . VAL C 259 ? 0.2796 0.3276 0.3597 0.0128  -0.1294 -0.0311 259 VAL C C   
10309 O O   . VAL C 259 ? 0.2679 0.3045 0.3446 0.0095  -0.1299 -0.0420 259 VAL C O   
10310 C CB  . VAL C 259 ? 0.2971 0.3337 0.3890 0.0122  -0.1297 -0.0191 259 VAL C CB  
10311 C CG1 . VAL C 259 ? 0.2951 0.3183 0.3909 0.0026  -0.1339 -0.0267 259 VAL C CG1 
10312 C CG2 . VAL C 259 ? 0.2005 0.2571 0.2961 0.0088  -0.1292 -0.0077 259 VAL C CG2 
10313 N N   . SER C 260 ? 0.1975 0.2658 0.2790 0.0113  -0.1309 -0.0238 260 SER C N   
10314 C CA  . SER C 260 ? 0.2036 0.2838 0.2828 0.0043  -0.1356 -0.0266 260 SER C CA  
10315 C C   . SER C 260 ? 0.2507 0.3585 0.3386 0.0033  -0.1378 -0.0152 260 SER C C   
10316 O O   . SER C 260 ? 0.3710 0.4874 0.4642 0.0102  -0.1337 -0.0065 260 SER C O   
10317 C CB  . SER C 260 ? 0.2594 0.3369 0.3248 0.0102  -0.1340 -0.0320 260 SER C CB  
10318 O OG  . SER C 260 ? 0.2801 0.3672 0.3417 0.0217  -0.1309 -0.0237 260 SER C OG  
10319 N N   . ASN C 261 ? 0.2963 0.4783 0.2813 0.0049  -0.0466 0.0449  261 ASN C N   
10320 C CA  . ASN C 261 ? 0.2464 0.4512 0.2365 0.0039  -0.0442 0.0465  261 ASN C CA  
10321 C C   . ASN C 261 ? 0.3662 0.5727 0.3553 0.0168  -0.0361 0.0595  261 ASN C C   
10322 O O   . ASN C 261 ? 0.4212 0.6271 0.4123 0.0156  -0.0307 0.0618  261 ASN C O   
10323 C CB  . ASN C 261 ? 0.3827 0.6264 0.3790 0.0039  -0.0495 0.0394  261 ASN C CB  
10324 C CG  . ASN C 261 ? 0.4344 0.6730 0.4317 -0.0099 -0.0570 0.0238  261 ASN C CG  
10325 O OD1 . ASN C 261 ? 0.4511 0.6873 0.4539 -0.0236 -0.0590 0.0174  261 ASN C OD1 
10326 N ND2 . ASN C 261 ? 0.4765 0.7120 0.4686 -0.0063 -0.0602 0.0176  261 ASN C ND2 
10327 N N   . GLU C 262 ? 0.3699 0.5772 0.3559 0.0293  -0.0339 0.0680  262 GLU C N   
10328 C CA  . GLU C 262 ? 0.3529 0.5563 0.3381 0.0425  -0.0262 0.0806  262 GLU C CA  
10329 C C   . GLU C 262 ? 0.3631 0.5262 0.3412 0.0395  -0.0214 0.0826  262 GLU C C   
10330 O O   . GLU C 262 ? 0.4856 0.6408 0.4624 0.0463  -0.0143 0.0877  262 GLU C O   
10331 C CB  . GLU C 262 ? 0.4375 0.6521 0.4204 0.0555  -0.0251 0.0911  262 GLU C CB  
10332 C CG  . GLU C 262 ? 0.4727 0.7309 0.4596 0.0630  -0.0294 0.0928  262 GLU C CG  
10333 C CD  . GLU C 262 ? 0.5529 0.8269 0.5348 0.0576  -0.0362 0.0844  262 GLU C CD  
10334 O OE1 . GLU C 262 ? 0.5737 0.8263 0.5531 0.0475  -0.0375 0.0752  262 GLU C OE1 
10335 O OE2 . GLU C 262 ? 0.4684 0.7761 0.4485 0.0643  -0.0401 0.0862  262 GLU C OE2 
10336 N N   . ALA C 263 ? 0.2850 0.4234 0.2585 0.0301  -0.0257 0.0779  263 ALA C N   
10337 C CA  . ALA C 263 ? 0.2857 0.3881 0.2511 0.0254  -0.0241 0.0784  263 ALA C CA  
10338 C C   . ALA C 263 ? 0.3179 0.4130 0.2772 0.0182  -0.0220 0.0738  263 ALA C C   
10339 O O   . ALA C 263 ? 0.3231 0.4012 0.2744 0.0210  -0.0156 0.0760  263 ALA C O   
10340 C CB  . ALA C 263 ? 0.2229 0.3069 0.1881 0.0173  -0.0314 0.0744  263 ALA C CB  
10341 N N   . LEU C 264 ? 0.2467 0.3538 0.2090 0.0082  -0.0264 0.0670  264 LEU C N   
10342 C CA  . LEU C 264 ? 0.2359 0.3392 0.1928 -0.0006 -0.0228 0.0643  264 LEU C CA  
10343 C C   . LEU C 264 ? 0.2652 0.3902 0.2272 0.0086  -0.0123 0.0677  264 LEU C C   
10344 O O   . LEU C 264 ? 0.3377 0.4542 0.2920 0.0056  -0.0048 0.0671  264 LEU C O   
10345 C CB  . LEU C 264 ? 0.2336 0.3471 0.1958 -0.0139 -0.0289 0.0575  264 LEU C CB  
10346 C CG  . LEU C 264 ? 0.2362 0.3237 0.1936 -0.0221 -0.0387 0.0537  264 LEU C CG  
10347 C CD1 . LEU C 264 ? 0.2447 0.3410 0.2095 -0.0330 -0.0446 0.0459  264 LEU C CD1 
10348 C CD2 . LEU C 264 ? 0.2524 0.3056 0.1933 -0.0285 -0.0392 0.0568  264 LEU C CD2 
10349 N N   . GLU C 265 ? 0.3288 0.4834 0.3035 0.0209  -0.0115 0.0715  265 GLU C N   
10350 C CA  . GLU C 265 ? 0.3563 0.5308 0.3385 0.0341  -0.0021 0.0764  265 GLU C CA  
10351 C C   . GLU C 265 ? 0.3346 0.4778 0.3060 0.0445  0.0057  0.0812  265 GLU C C   
10352 O O   . GLU C 265 ? 0.3904 0.5286 0.3585 0.0483  0.0156  0.0800  265 GLU C O   
10353 C CB  . GLU C 265 ? 0.2315 0.4443 0.2283 0.0460  -0.0057 0.0813  265 GLU C CB  
10354 C CG  . GLU C 265 ? 0.3206 0.5681 0.3288 0.0354  -0.0135 0.0740  265 GLU C CG  
10355 C CD  . GLU C 265 ? 0.5211 0.8065 0.5389 0.0466  -0.0196 0.0781  265 GLU C CD  
10356 O OE1 . GLU C 265 ? 0.5925 0.8707 0.6044 0.0603  -0.0192 0.0875  265 GLU C OE1 
10357 O OE2 . GLU C 265 ? 0.4572 0.7796 0.4876 0.0406  -0.0252 0.0723  265 GLU C OE2 
10358 N N   . LEU C 266 ? 0.3353 0.4567 0.3011 0.0482  0.0020  0.0855  266 LEU C N   
10359 C CA  . LEU C 266 ? 0.3114 0.4010 0.2685 0.0567  0.0085  0.0895  266 LEU C CA  
10360 C C   . LEU C 266 ? 0.3676 0.4258 0.3079 0.0470  0.0117  0.0818  266 LEU C C   
10361 O O   . LEU C 266 ? 0.3833 0.4254 0.3165 0.0548  0.0212  0.0807  266 LEU C O   
10362 C CB  . LEU C 266 ? 0.3086 0.3816 0.2646 0.0572  0.0035  0.0952  266 LEU C CB  
10363 C CG  . LEU C 266 ? 0.3025 0.3407 0.2518 0.0637  0.0093  0.0998  266 LEU C CG  
10364 C CD1 . LEU C 266 ? 0.4363 0.4844 0.3941 0.0819  0.0152  0.1125  266 LEU C CD1 
10365 C CD2 . LEU C 266 ? 0.3166 0.3300 0.2619 0.0523  0.0025  0.0990  266 LEU C CD2 
10366 N N   . TYR C 267 ? 0.3654 0.4136 0.2977 0.0309  0.0037  0.0763  267 TYR C N   
10367 C CA  . TYR C 267 ? 0.3507 0.3712 0.2633 0.0211  0.0051  0.0703  267 TYR C CA  
10368 C C   . TYR C 267 ? 0.3705 0.4054 0.2799 0.0223  0.0166  0.0673  267 TYR C C   
10369 O O   . TYR C 267 ? 0.4056 0.4205 0.2984 0.0235  0.0248  0.0632  267 TYR C O   
10370 C CB  . TYR C 267 ? 0.3556 0.3651 0.2618 0.0054  -0.0071 0.0676  267 TYR C CB  
10371 C CG  . TYR C 267 ? 0.2983 0.2920 0.2077 0.0041  -0.0170 0.0693  267 TYR C CG  
10372 C CD1 . TYR C 267 ? 0.3554 0.3223 0.2566 0.0060  -0.0168 0.0693  267 TYR C CD1 
10373 C CD2 . TYR C 267 ? 0.2684 0.2750 0.1906 0.0006  -0.0259 0.0697  267 TYR C CD2 
10374 C CE1 . TYR C 267 ? 0.3854 0.3420 0.2936 0.0032  -0.0252 0.0711  267 TYR C CE1 
10375 C CE2 . TYR C 267 ? 0.2642 0.2609 0.1924 0.0000  -0.0331 0.0711  267 TYR C CE2 
10376 C CZ  . TYR C 267 ? 0.3457 0.3192 0.2684 0.0008  -0.0327 0.0726  267 TYR C CZ  
10377 O OH  . TYR C 267 ? 0.5016 0.4693 0.4343 -0.0014 -0.0392 0.0743  267 TYR C OH  
10378 N N   . TYR C 268 ? 0.4008 0.4722 0.3266 0.0214  0.0177  0.0683  268 TYR C N   
10379 C CA  . TYR C 268 ? 0.3744 0.4669 0.3032 0.0219  0.0299  0.0662  268 TYR C CA  
10380 C C   . TYR C 268 ? 0.3758 0.4753 0.3111 0.0419  0.0425  0.0676  268 TYR C C   
10381 O O   . TYR C 268 ? 0.4121 0.5110 0.3404 0.0447  0.0556  0.0635  268 TYR C O   
10382 C CB  . TYR C 268 ? 0.3692 0.5022 0.3186 0.0149  0.0268  0.0665  268 TYR C CB  
10383 C CG  . TYR C 268 ? 0.3184 0.4886 0.2842 0.0216  0.0395  0.0664  268 TYR C CG  
10384 C CD1 . TYR C 268 ? 0.3019 0.4727 0.2594 0.0125  0.0512  0.0632  268 TYR C CD1 
10385 C CD2 . TYR C 268 ? 0.3526 0.5595 0.3426 0.0374  0.0399  0.0703  268 TYR C CD2 
10386 C CE1 . TYR C 268 ? 0.3051 0.5144 0.2814 0.0188  0.0643  0.0628  268 TYR C CE1 
10387 C CE2 . TYR C 268 ? 0.3039 0.5495 0.3134 0.0448  0.0508  0.0703  268 TYR C CE2 
10388 C CZ  . TYR C 268 ? 0.3375 0.5853 0.3420 0.0354  0.0636  0.0661  268 TYR C CZ  
10389 O OH  . TYR C 268 ? 0.3709 0.6617 0.3987 0.0429  0.0760  0.0658  268 TYR C OH  
10390 N N   . GLU C 269 ? 0.4145 0.5202 0.3627 0.0568  0.0395  0.0738  269 GLU C N   
10391 C CA  . GLU C 269 ? 0.4023 0.5101 0.3577 0.0782  0.0505  0.0769  269 GLU C CA  
10392 C C   . GLU C 269 ? 0.4364 0.4992 0.3696 0.0812  0.0587  0.0711  269 GLU C C   
10393 O O   . GLU C 269 ? 0.4220 0.4831 0.3577 0.0974  0.0716  0.0695  269 GLU C O   
10394 C CB  . GLU C 269 ? 0.4588 0.5748 0.4277 0.0923  0.0445  0.0875  269 GLU C CB  
10395 C CG  . GLU C 269 ? 0.5965 0.7574 0.5841 0.0912  0.0353  0.0922  269 GLU C CG  
10396 C CD  . GLU C 269 ? 0.7135 0.8801 0.7080 0.1050  0.0298  0.1040  269 GLU C CD  
10397 O OE1 . GLU C 269 ? 0.7813 0.9209 0.7712 0.1185  0.0354  0.1104  269 GLU C OE1 
10398 O OE2 . GLU C 269 ? 0.6388 0.8348 0.6413 0.1016  0.0201  0.1067  269 GLU C OE2 
10399 N N   . LYS C 270 ? 0.3973 0.4246 0.3096 0.0665  0.0510  0.0670  270 LYS C N   
10400 C CA  . LYS C 270 ? 0.4424 0.4254 0.3322 0.0670  0.0553  0.0601  270 LYS C CA  
10401 C C   . LYS C 270 ? 0.5124 0.4821 0.3769 0.0548  0.0604  0.0499  270 LYS C C   
10402 O O   . LYS C 270 ? 0.4528 0.3850 0.2933 0.0514  0.0612  0.0420  270 LYS C O   
10403 C CB  . LYS C 270 ? 0.5277 0.4814 0.4121 0.0591  0.0424  0.0625  270 LYS C CB  
10404 C CG  . LYS C 270 ? 0.4635 0.4278 0.3686 0.0703  0.0391  0.0740  270 LYS C CG  
10405 C CD  . LYS C 270 ? 0.3947 0.3338 0.2999 0.0865  0.0485  0.0761  270 LYS C CD  
10406 C CE  . LYS C 270 ? 0.3853 0.3441 0.3115 0.1021  0.0487  0.0908  270 LYS C CE  
10407 N NZ  . LYS C 270 ? 0.4702 0.4346 0.4052 0.1249  0.0613  0.0941  270 LYS C NZ  
10408 N N   . GLY C 271 ? 0.5413 0.5406 0.4095 0.0470  0.0636  0.0501  271 GLY C N   
10409 C CA  . GLY C 271 ? 0.4965 0.4864 0.3394 0.0355  0.0707  0.0430  271 GLY C CA  
10410 C C   . GLY C 271 ? 0.4325 0.4067 0.2567 0.0143  0.0570  0.0441  271 GLY C C   
10411 O O   . GLY C 271 ? 0.4385 0.3985 0.2351 0.0042  0.0614  0.0397  271 GLY C O   
10412 N N   . ILE C 272 ? 0.3880 0.3643 0.2252 0.0083  0.0411  0.0499  272 ILE C N   
10413 C CA  . ILE C 272 ? 0.3984 0.3596 0.2216 -0.0092 0.0271  0.0517  272 ILE C CA  
10414 C C   . ILE C 272 ? 0.3955 0.3813 0.2246 -0.0201 0.0298  0.0553  272 ILE C C   
10415 O O   . ILE C 272 ? 0.4846 0.5032 0.3405 -0.0170 0.0316  0.0581  272 ILE C O   
10416 C CB  . ILE C 272 ? 0.3657 0.3208 0.2033 -0.0099 0.0109  0.0554  272 ILE C CB  
10417 C CG1 . ILE C 272 ? 0.3734 0.3079 0.2105 0.0001  0.0106  0.0532  272 ILE C CG1 
10418 C CG2 . ILE C 272 ? 0.3700 0.3065 0.1940 -0.0249 -0.0041 0.0568  272 ILE C CG2 
10419 C CD1 . ILE C 272 ? 0.4077 0.3072 0.2148 -0.0043 0.0111  0.0456  272 ILE C CD1 
10420 N N   . ASN C 273 ? 0.4841 0.4534 0.2870 -0.0340 0.0295  0.0558  273 ASN C N   
10421 C CA  . ASN C 273 ? 0.5530 0.5397 0.3587 -0.0474 0.0331  0.0605  273 ASN C CA  
10422 C C   . ASN C 273 ? 0.4827 0.4573 0.2902 -0.0601 0.0158  0.0660  273 ASN C C   
10423 O O   . ASN C 273 ? 0.4392 0.4296 0.2583 -0.0706 0.0167  0.0697  273 ASN C O   
10424 C CB  . ASN C 273 ? 0.4406 0.4176 0.2148 -0.0555 0.0462  0.0600  273 ASN C CB  
10425 C CG  . ASN C 273 ? 0.5032 0.4897 0.2738 -0.0415 0.0652  0.0524  273 ASN C CG  
10426 O OD1 . ASN C 273 ? 0.5400 0.5519 0.3391 -0.0271 0.0718  0.0503  273 ASN C OD1 
10427 N ND2 . ASN C 273 ? 0.6203 0.5860 0.3545 -0.0447 0.0740  0.0482  273 ASN C ND2 
10428 N N   . MET C 274 ? 0.3968 0.3445 0.1953 -0.0595 0.0003  0.0661  274 MET C N   
10429 C CA  . MET C 274 ? 0.3940 0.3281 0.1942 -0.0690 -0.0159 0.0711  274 MET C CA  
10430 C C   . MET C 274 ? 0.4160 0.3372 0.2246 -0.0617 -0.0306 0.0692  274 MET C C   
10431 O O   . MET C 274 ? 0.4442 0.3548 0.2448 -0.0547 -0.0304 0.0655  274 MET C O   
10432 C CB  . MET C 274 ? 0.5438 0.4524 0.3116 -0.0824 -0.0191 0.0773  274 MET C CB  
10433 C CG  . MET C 274 ? 0.5064 0.4013 0.2781 -0.0920 -0.0337 0.0843  274 MET C CG  
10434 S SD  . MET C 274 ? 0.6376 0.5037 0.4023 -0.0879 -0.0567 0.0858  274 MET C SD  
10435 C CE  . MET C 274 ? 0.4794 0.3202 0.1969 -0.0932 -0.0566 0.0885  274 MET C CE  
10436 N N   . LEU C 275 ? 0.3950 0.3170 0.2206 -0.0640 -0.0427 0.0712  275 LEU C N   
10437 C CA  . LEU C 275 ? 0.3915 0.3051 0.2284 -0.0582 -0.0561 0.0700  275 LEU C CA  
10438 C C   . LEU C 275 ? 0.4081 0.3167 0.2563 -0.0630 -0.0682 0.0724  275 LEU C C   
10439 O O   . LEU C 275 ? 0.4160 0.3274 0.2651 -0.0708 -0.0656 0.0742  275 LEU C O   
10440 C CB  . LEU C 275 ? 0.3293 0.2636 0.1884 -0.0461 -0.0507 0.0662  275 LEU C CB  
10441 C CG  . LEU C 275 ? 0.3206 0.2820 0.2059 -0.0421 -0.0494 0.0645  275 LEU C CG  
10442 C CD1 . LEU C 275 ? 0.3680 0.3445 0.2680 -0.0297 -0.0451 0.0637  275 LEU C CD1 
10443 C CD2 . LEU C 275 ? 0.4081 0.3893 0.2960 -0.0469 -0.0398 0.0640  275 LEU C CD2 
10444 N N   . ALA C 276 ? 0.3603 0.2610 0.2187 -0.0584 -0.0810 0.0719  276 ALA C N   
10445 C CA  . ALA C 276 ? 0.3770 0.2682 0.2454 -0.0603 -0.0935 0.0736  276 ALA C CA  
10446 C C   . ALA C 276 ? 0.3304 0.2373 0.2273 -0.0507 -0.0971 0.0682  276 ALA C C   
10447 O O   . ALA C 276 ? 0.3993 0.3179 0.3048 -0.0439 -0.0939 0.0660  276 ALA C O   
10448 C CB  . ALA C 276 ? 0.4415 0.3052 0.2919 -0.0641 -0.1079 0.0802  276 ALA C CB  
10449 N N   . THR C 277 ? 0.3221 0.2272 0.2327 -0.0504 -0.1031 0.0660  277 THR C N   
10450 C CA  . THR C 277 ? 0.3754 0.2958 0.3116 -0.0412 -0.1054 0.0595  277 THR C CA  
10451 C C   . THR C 277 ? 0.3362 0.2402 0.2810 -0.0407 -0.1162 0.0583  277 THR C C   
10452 O O   . THR C 277 ? 0.3418 0.2211 0.2723 -0.0477 -0.1227 0.0646  277 THR C O   
10453 C CB  . THR C 277 ? 0.3424 0.2910 0.2890 -0.0382 -0.0936 0.0529  277 THR C CB  
10454 O OG1 . THR C 277 ? 0.3744 0.3355 0.3411 -0.0308 -0.0955 0.0454  277 THR C OG1 
10455 C CG2 . THR C 277 ? 0.2921 0.2419 0.2308 -0.0477 -0.0881 0.0518  277 THR C CG2 
10456 N N   . ASP C 278 ? 0.3057 0.2224 0.2731 -0.0318 -0.1174 0.0506  278 ASP C N   
10457 C CA  . ASP C 278 ? 0.3369 0.2378 0.3169 -0.0268 -0.1281 0.0486  278 ASP C CA  
10458 C C   . ASP C 278 ? 0.5235 0.4134 0.5043 -0.0312 -0.1268 0.0419  278 ASP C C   
10459 O O   . ASP C 278 ? 0.5031 0.4075 0.4816 -0.0367 -0.1173 0.0356  278 ASP C O   
10460 C CB  . ASP C 278 ? 0.3958 0.3164 0.4014 -0.0142 -0.1286 0.0421  278 ASP C CB  
10461 C CG  . ASP C 278 ? 0.4797 0.3853 0.5017 -0.0059 -0.1403 0.0406  278 ASP C CG  
10462 O OD1 . ASP C 278 ? 0.3961 0.2780 0.4102 -0.0077 -0.1528 0.0503  278 ASP C OD1 
10463 O OD2 . ASP C 278 ? 0.3755 0.2930 0.4174 0.0034  -0.1369 0.0297  278 ASP C OD2 
10464 N N   . GLU C 279 ? 0.5204 0.3840 0.5063 -0.0283 -0.1374 0.0434  279 GLU C N   
10465 C CA  . GLU C 279 ? 0.4109 0.2560 0.3992 -0.0326 -0.1377 0.0365  279 GLU C CA  
10466 C C   . GLU C 279 ? 0.5094 0.3759 0.5157 -0.0258 -0.1307 0.0184  279 GLU C C   
10467 O O   . GLU C 279 ? 0.6361 0.5005 0.6406 -0.0338 -0.1262 0.0089  279 GLU C O   
10468 C CB  . GLU C 279 ? 0.5076 0.3168 0.4985 -0.0278 -0.1514 0.0435  279 GLU C CB  
10469 C CG  . GLU C 279 ? 0.7195 0.5020 0.7160 -0.0301 -0.1528 0.0357  279 GLU C CG  
10470 C CD  . GLU C 279 ? 0.6374 0.3757 0.6223 -0.0336 -0.1644 0.0508  279 GLU C CD  
10471 O OE1 . GLU C 279 ? 0.5809 0.3124 0.5573 -0.0295 -0.1742 0.0657  279 GLU C OE1 
10472 O OE2 . GLU C 279 ? 0.5360 0.2453 0.5195 -0.0408 -0.1644 0.0480  279 GLU C OE2 
10473 N N   . VAL C 280 ? 0.5302 0.4184 0.5534 -0.0120 -0.1296 0.0130  280 VAL C N   
10474 C CA  . VAL C 280 ? 0.4035 0.3125 0.4403 -0.0046 -0.1222 -0.0043 280 VAL C CA  
10475 C C   . VAL C 280 ? 0.3216 0.2607 0.3493 -0.0112 -0.1112 -0.0092 280 VAL C C   
10476 O O   . VAL C 280 ? 0.3371 0.2898 0.3679 -0.0101 -0.1062 -0.0242 280 VAL C O   
10477 C CB  . VAL C 280 ? 0.3304 0.2574 0.3885 0.0116  -0.1219 -0.0075 280 VAL C CB  
10478 C CG1 . VAL C 280 ? 0.3147 0.2758 0.3724 0.0126  -0.1134 -0.0027 280 VAL C CG1 
10479 C CG2 . VAL C 280 ? 0.3426 0.2739 0.4147 0.0216  -0.1177 -0.0266 280 VAL C CG2 
10480 N N   . ILE C 281 ? 0.3746 0.3248 0.3907 -0.0170 -0.1079 0.0027  281 ILE C N   
10481 C CA  . ILE C 281 ? 0.3195 0.2964 0.3277 -0.0224 -0.0989 0.0002  281 ILE C CA  
10482 C C   . ILE C 281 ? 0.3072 0.2740 0.3077 -0.0363 -0.0993 -0.0042 281 ILE C C   
10483 O O   . ILE C 281 ? 0.3147 0.3026 0.3162 -0.0398 -0.0953 -0.0148 281 ILE C O   
10484 C CB  . ILE C 281 ? 0.3883 0.3765 0.3881 -0.0228 -0.0946 0.0135  281 ILE C CB  
10485 C CG1 . ILE C 281 ? 0.3302 0.3386 0.3400 -0.0112 -0.0906 0.0148  281 ILE C CG1 
10486 C CG2 . ILE C 281 ? 0.3362 0.3434 0.3268 -0.0299 -0.0873 0.0143  281 ILE C CG2 
10487 C CD1 . ILE C 281 ? 0.2883 0.2991 0.2915 -0.0114 -0.0878 0.0273  281 ILE C CD1 
10488 N N   . LEU C 282 ? 0.3780 0.3137 0.3705 -0.0454 -0.1047 0.0045  282 LEU C N   
10489 C CA  . LEU C 282 ? 0.3942 0.3169 0.3816 -0.0610 -0.1046 0.0017  282 LEU C CA  
10490 C C   . LEU C 282 ? 0.4765 0.3917 0.4742 -0.0616 -0.1074 -0.0159 282 LEU C C   
10491 O O   . LEU C 282 ? 0.5014 0.4229 0.4992 -0.0744 -0.1052 -0.0247 282 LEU C O   
10492 C CB  . LEU C 282 ? 0.3694 0.2552 0.3446 -0.0695 -0.1100 0.0161  282 LEU C CB  
10493 C CG  . LEU C 282 ? 0.4504 0.3194 0.4187 -0.0886 -0.1083 0.0180  282 LEU C CG  
10494 C CD1 . LEU C 282 ? 0.3798 0.2769 0.3409 -0.0987 -0.0981 0.0231  282 LEU C CD1 
10495 C CD2 . LEU C 282 ? 0.5071 0.3318 0.4636 -0.0935 -0.1157 0.0320  282 LEU C CD2 
10496 N N   . LYS C 283 ? 0.4805 0.3832 0.4882 -0.0482 -0.1119 -0.0226 283 LYS C N   
10497 C CA  . LYS C 283 ? 0.3917 0.2838 0.4082 -0.0467 -0.1136 -0.0420 283 LYS C CA  
10498 C C   . LYS C 283 ? 0.3784 0.3090 0.3957 -0.0467 -0.1072 -0.0584 283 LYS C C   
10499 O O   . LYS C 283 ? 0.3983 0.3253 0.4160 -0.0557 -0.1080 -0.0746 283 LYS C O   
10500 C CB  . LYS C 283 ? 0.4374 0.3133 0.4667 -0.0288 -0.1181 -0.0458 283 LYS C CB  
10501 C CG  . LYS C 283 ? 0.6556 0.4824 0.6879 -0.0300 -0.1271 -0.0434 283 LYS C CG  
10502 C CD  . LYS C 283 ? 0.5842 0.4001 0.6342 -0.0103 -0.1300 -0.0546 283 LYS C CD  
10503 C CE  . LYS C 283 ? 0.6970 0.4900 0.7536 0.0001  -0.1399 -0.0370 283 LYS C CE  
10504 N NZ  . LYS C 283 ? 0.6394 0.4357 0.7190 0.0222  -0.1413 -0.0465 283 LYS C NZ  
10505 N N   . ASN C 284 ? 0.3488 0.3154 0.3651 -0.0375 -0.1014 -0.0540 284 ASN C N   
10506 C CA  . ASN C 284 ? 0.3385 0.3436 0.3525 -0.0357 -0.0961 -0.0663 284 ASN C CA  
10507 C C   . ASN C 284 ? 0.4303 0.4588 0.4375 -0.0489 -0.0944 -0.0623 284 ASN C C   
10508 O O   . ASN C 284 ? 0.4346 0.4985 0.4390 -0.0472 -0.0917 -0.0700 284 ASN C O   
10509 C CB  . ASN C 284 ? 0.3154 0.3482 0.3311 -0.0198 -0.0899 -0.0611 284 ASN C CB  
10510 C CG  . ASN C 284 ? 0.3196 0.3351 0.3469 -0.0067 -0.0910 -0.0606 284 ASN C CG  
10511 O OD1 . ASN C 284 ? 0.3979 0.3878 0.4323 -0.0043 -0.0952 -0.0719 284 ASN C OD1 
10512 N ND2 . ASN C 284 ? 0.2990 0.3286 0.3304 0.0020  -0.0873 -0.0478 284 ASN C ND2 
10513 N N   . SER C 285 ? 0.4121 0.4245 0.4169 -0.0613 -0.0956 -0.0501 285 SER C N   
10514 C CA  . SER C 285 ? 0.3412 0.3801 0.3434 -0.0719 -0.0922 -0.0444 285 SER C CA  
10515 C C   . SER C 285 ? 0.4326 0.4594 0.4374 -0.0926 -0.0946 -0.0490 285 SER C C   
10516 O O   . SER C 285 ? 0.5590 0.6172 0.5674 -0.1019 -0.0930 -0.0523 285 SER C O   
10517 C CB  . SER C 285 ? 0.4316 0.4721 0.4283 -0.0680 -0.0875 -0.0241 285 SER C CB  
10518 O OG  . SER C 285 ? 0.4577 0.5011 0.4537 -0.0516 -0.0860 -0.0188 285 SER C OG  
10519 N N   . VAL C 286 ? 0.5378 0.5207 0.5420 -0.1004 -0.0987 -0.0481 286 VAL C N   
10520 C CA  . VAL C 286 ? 0.4652 0.4313 0.4724 -0.1222 -0.1003 -0.0519 286 VAL C CA  
10521 C C   . VAL C 286 ? 0.5088 0.4352 0.5194 -0.1240 -0.1069 -0.0664 286 VAL C C   
10522 O O   . VAL C 286 ? 0.6997 0.6053 0.7100 -0.1078 -0.1098 -0.0681 286 VAL C O   
10523 C CB  . VAL C 286 ? 0.5227 0.4689 0.5228 -0.1334 -0.0968 -0.0313 286 VAL C CB  
10524 C CG1 . VAL C 286 ? 0.6375 0.6248 0.6369 -0.1350 -0.0886 -0.0215 286 VAL C CG1 
10525 C CG2 . VAL C 286 ? 0.5388 0.4498 0.5292 -0.1212 -0.0999 -0.0178 286 VAL C CG2 
10526 N N   . GLU C 287 ? 0.4585 0.3746 0.4742 -0.1441 -0.1091 -0.0776 287 GLU C N   
10527 C CA  . GLU C 287 ? 0.6810 0.5553 0.7002 -0.1468 -0.1150 -0.0938 287 GLU C CA  
10528 C C   . GLU C 287 ? 0.7364 0.5541 0.7519 -0.1505 -0.1175 -0.0781 287 GLU C C   
10529 O O   . GLU C 287 ? 0.7278 0.5094 0.7447 -0.1372 -0.1223 -0.0824 287 GLU C O   
10530 C CB  . GLU C 287 ? 0.5915 0.4744 0.6179 -0.1684 -0.1174 -0.1141 287 GLU C CB  
10531 C CG  . GLU C 287 ? 0.6596 0.4986 0.6889 -0.1705 -0.1231 -0.1357 287 GLU C CG  
10532 C CD  . GLU C 287 ? 0.9405 0.7649 0.9770 -0.2000 -0.1259 -0.1478 287 GLU C CD  
10533 O OE1 . GLU C 287 ? 1.0854 0.9118 1.1251 -0.2200 -0.1228 -0.1313 287 GLU C OE1 
10534 O OE2 . GLU C 287 ? 1.1084 0.9193 1.1475 -0.2041 -0.1307 -0.1748 287 GLU C OE2 
10535 N N   . ARG C 288 ? 0.7350 0.5455 0.7457 -0.1674 -0.1142 -0.0592 288 ARG C N   
10536 C CA  . ARG C 288 ? 0.7478 0.5053 0.7503 -0.1727 -0.1166 -0.0408 288 ARG C CA  
10537 C C   . ARG C 288 ? 0.6602 0.4221 0.6505 -0.1573 -0.1157 -0.0188 288 ARG C C   
10538 O O   . ARG C 288 ? 0.6122 0.3814 0.5917 -0.1668 -0.1103 -0.0006 288 ARG C O   
10539 C CB  . ARG C 288 ? 0.7743 0.5200 0.7765 -0.2023 -0.1124 -0.0331 288 ARG C CB  
10540 C CG  . ARG C 288 ? 0.8480 0.5834 0.8634 -0.2207 -0.1149 -0.0556 288 ARG C CG  
10541 C CD  . ARG C 288 ? 0.9803 0.6474 0.9945 -0.2253 -0.1200 -0.0543 288 ARG C CD  
10542 N NE  . ARG C 288 ? 1.1414 0.7903 1.1520 -0.2435 -0.1112 -0.0340 288 ARG C NE  
10543 C CZ  . ARG C 288 ? 1.1543 0.8227 1.1760 -0.2677 -0.1034 -0.0377 288 ARG C CZ  
10544 N NH1 . ARG C 288 ? 1.0224 0.7302 1.0598 -0.2770 -0.1045 -0.0614 288 ARG C NH1 
10545 N NH2 . ARG C 288 ? 1.1879 0.8383 1.2054 -0.2822 -0.0948 -0.0171 288 ARG C NH2 
10546 N N   . ALA C 289 ? 0.8369 0.5947 0.8293 -0.1337 -0.1209 -0.0217 289 ALA C N   
10547 C CA  . ALA C 289 ? 0.8585 0.6280 0.8426 -0.1181 -0.1213 -0.0057 289 ALA C CA  
10548 C C   . ALA C 289 ? 0.8771 0.6042 0.8471 -0.1208 -0.1267 0.0167  289 ALA C C   
10549 O O   . ALA C 289 ? 1.0409 0.7372 1.0128 -0.1072 -0.1360 0.0210  289 ALA C O   
10550 C CB  . ALA C 289 ? 0.6983 0.4806 0.6931 -0.0943 -0.1247 -0.0165 289 ALA C CB  
10551 N N   . SER C 290 ? 0.7263 0.4543 0.6816 -0.1381 -0.1208 0.0318  290 SER C N   
10552 C CA  . SER C 290 ? 0.8691 0.5652 0.8039 -0.1409 -0.1244 0.0555  290 SER C CA  
10553 C C   . SER C 290 ? 0.6705 0.3952 0.5922 -0.1324 -0.1214 0.0654  290 SER C C   
10554 O O   . SER C 290 ? 0.6206 0.3805 0.5401 -0.1399 -0.1104 0.0637  290 SER C O   
10555 C CB  . SER C 290 ? 0.9556 0.6314 0.8794 -0.1666 -0.1180 0.0666  290 SER C CB  
10556 O OG  . SER C 290 ? 0.8950 0.5293 0.8273 -0.1747 -0.1231 0.0617  290 SER C OG  
10557 N N   . PRO C 291 ? 0.5370 0.2496 0.4520 -0.1166 -0.1311 0.0744  291 PRO C N   
10558 C CA  . PRO C 291 ? 0.5582 0.2955 0.4608 -0.1096 -0.1291 0.0813  291 PRO C CA  
10559 C C   . PRO C 291 ? 0.6698 0.3899 0.5416 -0.1194 -0.1285 0.1014  291 PRO C C   
10560 O O   . PRO C 291 ? 0.7384 0.4706 0.5974 -0.1124 -0.1298 0.1065  291 PRO C O   
10561 C CB  . PRO C 291 ? 0.4961 0.2314 0.4111 -0.0886 -0.1412 0.0783  291 PRO C CB  
10562 C CG  . PRO C 291 ? 0.5346 0.2297 0.4567 -0.0853 -0.1520 0.0804  291 PRO C CG  
10563 C CD  . PRO C 291 ? 0.6069 0.2860 0.5300 -0.1027 -0.1450 0.0757  291 PRO C CD  
10564 N N   . TYR C 292 ? 0.6653 0.3570 0.5234 -0.1360 -0.1261 0.1127  292 TYR C N   
10565 C CA  . TYR C 292 ? 0.6557 0.3296 0.4812 -0.1441 -0.1253 0.1327  292 TYR C CA  
10566 C C   . TYR C 292 ? 0.6294 0.3221 0.4408 -0.1630 -0.1074 0.1367  292 TYR C C   
10567 O O   . TYR C 292 ? 0.6362 0.3211 0.4260 -0.1701 -0.1010 0.1482  292 TYR C O   
10568 C CB  . TYR C 292 ? 0.6895 0.3296 0.5116 -0.1429 -0.1317 0.1413  292 TYR C CB  
10569 C CG  . TYR C 292 ? 0.6471 0.2718 0.4863 -0.1230 -0.1481 0.1373  292 TYR C CG  
10570 C CD1 . TYR C 292 ? 0.6298 0.2667 0.4676 -0.1065 -0.1586 0.1380  292 TYR C CD1 
10571 C CD2 . TYR C 292 ? 0.6674 0.2672 0.5262 -0.1207 -0.1522 0.1314  292 TYR C CD2 
10572 C CE1 . TYR C 292 ? 0.6306 0.2592 0.4882 -0.0883 -0.1725 0.1342  292 TYR C CE1 
10573 C CE2 . TYR C 292 ? 0.6703 0.2584 0.5468 -0.1007 -0.1656 0.1270  292 TYR C CE2 
10574 C CZ  . TYR C 292 ? 0.6508 0.2552 0.5277 -0.0845 -0.1756 0.1291  292 TYR C CZ  
10575 O OH  . TYR C 292 ? 0.7205 0.3186 0.6191 -0.0645 -0.1880 0.1247  292 TYR C OH  
10576 N N   . LEU C 293 ? 0.5706 0.3038 0.4013 -0.1640 -0.0959 0.1214  293 LEU C N   
10577 C CA  . LEU C 293 ? 0.5922 0.3520 0.4169 -0.1788 -0.0780 0.1230  293 LEU C CA  
10578 C C   . LEU C 293 ? 0.5194 0.3225 0.3513 -0.1667 -0.0704 0.1120  293 LEU C C   
10579 O O   . LEU C 293 ? 0.4880 0.3058 0.3379 -0.1512 -0.0770 0.1000  293 LEU C O   
10580 C CB  . LEU C 293 ? 0.6202 0.3868 0.4661 -0.1971 -0.0704 0.1166  293 LEU C CB  
10581 C CG  . LEU C 293 ? 0.7286 0.5150 0.6082 -0.1928 -0.0741 0.0958  293 LEU C CG  
10582 C CD1 . LEU C 293 ? 0.7826 0.5851 0.6785 -0.2152 -0.0641 0.0906  293 LEU C CD1 
10583 C CD2 . LEU C 293 ? 0.6662 0.4157 0.5530 -0.1839 -0.0898 0.0917  293 LEU C CD2 
10584 N N   . ARG C 294 ? 0.5218 0.3443 0.3392 -0.1735 -0.0555 0.1169  294 ARG C N   
10585 C CA  . ARG C 294 ? 0.4875 0.3479 0.3111 -0.1618 -0.0467 0.1077  294 ARG C CA  
10586 C C   . ARG C 294 ? 0.5135 0.4125 0.3708 -0.1626 -0.0404 0.0942  294 ARG C C   
10587 O O   . ARG C 294 ? 0.5746 0.4859 0.4429 -0.1790 -0.0321 0.0942  294 ARG C O   
10588 C CB  . ARG C 294 ? 0.5052 0.3729 0.3028 -0.1678 -0.0314 0.1158  294 ARG C CB  
10589 C CG  . ARG C 294 ? 0.4765 0.3809 0.2811 -0.1556 -0.0198 0.1064  294 ARG C CG  
10590 C CD  . ARG C 294 ? 0.5932 0.4958 0.3658 -0.1583 -0.0063 0.1131  294 ARG C CD  
10591 N NE  . ARG C 294 ? 0.7344 0.6317 0.4941 -0.1785 0.0049  0.1243  294 ARG C NE  
10592 C CZ  . ARG C 294 ? 0.8504 0.7694 0.6008 -0.1851 0.0255  0.1264  294 ARG C CZ  
10593 N NH1 . ARG C 294 ? 0.9286 0.8741 0.6808 -0.1716 0.0369  0.1172  294 ARG C NH1 
10594 N NH2 . ARG C 294 ? 0.7291 0.6424 0.4689 -0.2057 0.0359  0.1382  294 ARG C NH2 
10595 N N   . TYR C 295 ? 0.4274 0.3468 0.3010 -0.1459 -0.0449 0.0832  295 TYR C N   
10596 C CA  . TYR C 295 ? 0.3972 0.3540 0.2999 -0.1444 -0.0419 0.0708  295 TYR C CA  
10597 C C   . TYR C 295 ? 0.4615 0.4572 0.3690 -0.1362 -0.0290 0.0689  295 TYR C C   
10598 O O   . TYR C 295 ? 0.5071 0.5018 0.4042 -0.1215 -0.0283 0.0700  295 TYR C O   
10599 C CB  . TYR C 295 ? 0.3776 0.3330 0.2947 -0.1311 -0.0544 0.0606  295 TYR C CB  
10600 C CG  . TYR C 295 ? 0.4216 0.3468 0.3434 -0.1388 -0.0652 0.0577  295 TYR C CG  
10601 C CD1 . TYR C 295 ? 0.4218 0.3563 0.3609 -0.1519 -0.0649 0.0486  295 TYR C CD1 
10602 C CD2 . TYR C 295 ? 0.4254 0.3124 0.3357 -0.1326 -0.0763 0.0635  295 TYR C CD2 
10603 C CE1 . TYR C 295 ? 0.4643 0.3661 0.4074 -0.1584 -0.0742 0.0444  295 TYR C CE1 
10604 C CE2 . TYR C 295 ? 0.4607 0.3175 0.3767 -0.1370 -0.0858 0.0609  295 TYR C CE2 
10605 C CZ  . TYR C 295 ? 0.4561 0.3180 0.3878 -0.1498 -0.0841 0.0509  295 TYR C CZ  
10606 O OH  . TYR C 295 ? 0.4752 0.3021 0.4123 -0.1537 -0.0930 0.0468  295 TYR C OH  
10607 N N   . TYR C 296 ? 0.4412 0.4708 0.3661 -0.1458 -0.0193 0.0658  296 TYR C N   
10608 C CA  . TYR C 296 ? 0.3535 0.4255 0.2902 -0.1358 -0.0078 0.0632  296 TYR C CA  
10609 C C   . TYR C 296 ? 0.4205 0.5215 0.3807 -0.1239 -0.0153 0.0529  296 TYR C C   
10610 O O   . TYR C 296 ? 0.4287 0.5446 0.4071 -0.1335 -0.0209 0.0454  296 TYR C O   
10611 C CB  . TYR C 296 ? 0.4169 0.5172 0.3643 -0.1515 0.0064  0.0656  296 TYR C CB  
10612 C CG  . TYR C 296 ? 0.6960 0.7853 0.6194 -0.1553 0.0209  0.0754  296 TYR C CG  
10613 C CD1 . TYR C 296 ? 0.6117 0.7197 0.5305 -0.1395 0.0327  0.0751  296 TYR C CD1 
10614 C CD2 . TYR C 296 ? 0.6757 0.7343 0.5791 -0.1743 0.0234  0.0851  296 TYR C CD2 
10615 C CE1 . TYR C 296 ? 0.8755 0.9734 0.7692 -0.1426 0.0471  0.0816  296 TYR C CE1 
10616 C CE2 . TYR C 296 ? 0.6644 0.7140 0.5411 -0.1781 0.0374  0.0941  296 TYR C CE2 
10617 C CZ  . TYR C 296 ? 1.0203 1.0905 0.8918 -0.1622 0.0495  0.0911  296 TYR C CZ  
10618 O OH  . TYR C 296 ? 1.0803 1.1415 0.9223 -0.1656 0.0646  0.0977  296 TYR C OH  
10619 N N   . PHE C 297 ? 0.4590 0.5665 0.4169 -0.1038 -0.0155 0.0526  297 PHE C N   
10620 C CA  . PHE C 297 ? 0.3041 0.4402 0.2801 -0.0911 -0.0213 0.0457  297 PHE C CA  
10621 C C   . PHE C 297 ? 0.3131 0.4968 0.3076 -0.0860 -0.0118 0.0455  297 PHE C C   
10622 O O   . PHE C 297 ? 0.3127 0.5030 0.3029 -0.0732 -0.0021 0.0506  297 PHE C O   
10623 C CB  . PHE C 297 ? 0.2721 0.3917 0.2383 -0.0731 -0.0257 0.0474  297 PHE C CB  
10624 C CG  . PHE C 297 ? 0.2525 0.4013 0.2335 -0.0598 -0.0297 0.0432  297 PHE C CG  
10625 C CD1 . PHE C 297 ? 0.2642 0.4218 0.2548 -0.0640 -0.0393 0.0344  297 PHE C CD1 
10626 C CD2 . PHE C 297 ? 0.2425 0.4089 0.2261 -0.0429 -0.0236 0.0479  297 PHE C CD2 
10627 C CE1 . PHE C 297 ? 0.2353 0.4211 0.2349 -0.0520 -0.0428 0.0311  297 PHE C CE1 
10628 C CE2 . PHE C 297 ? 0.2292 0.4218 0.2234 -0.0305 -0.0274 0.0468  297 PHE C CE2 
10629 C CZ  . PHE C 297 ? 0.2255 0.4293 0.2264 -0.0354 -0.0371 0.0386  297 PHE C CZ  
10630 N N   . ARG C 298 ? 0.3420 0.5587 0.3580 -0.0957 -0.0151 0.0389  298 ARG C N   
10631 C CA  . ARG C 298 ? 0.2608 0.5304 0.3002 -0.0907 -0.0092 0.0382  298 ARG C CA  
10632 C C   . ARG C 298 ? 0.2703 0.5506 0.3108 -0.0927 0.0075  0.0449  298 ARG C C   
10633 O O   . ARG C 298 ? 0.2796 0.5966 0.3353 -0.0791 0.0152  0.0470  298 ARG C O   
10634 C CB  . ARG C 298 ? 0.2429 0.5329 0.2868 -0.0667 -0.0128 0.0393  298 ARG C CB  
10635 C CG  . ARG C 298 ? 0.2353 0.5274 0.2803 -0.0647 -0.0273 0.0319  298 ARG C CG  
10636 C CD  . ARG C 298 ? 0.2337 0.5527 0.2834 -0.0425 -0.0297 0.0355  298 ARG C CD  
10637 N NE  . ARG C 298 ? 0.2188 0.5325 0.2618 -0.0393 -0.0411 0.0296  298 ARG C NE  
10638 C CZ  . ARG C 298 ? 0.3174 0.6292 0.3522 -0.0214 -0.0426 0.0351  298 ARG C CZ  
10639 N NH1 . ARG C 298 ? 0.4000 0.7122 0.4332 -0.0046 -0.0347 0.0468  298 ARG C NH1 
10640 N NH2 . ARG C 298 ? 0.3427 0.6509 0.3706 -0.0205 -0.0511 0.0287  298 ARG C NH2 
10641 N N   . GLU C 299 ? 0.2906 0.5392 0.3143 -0.1085 0.0135  0.0488  299 GLU C N   
10642 C CA  . GLU C 299 ? 0.3375 0.5908 0.3549 -0.1111 0.0313  0.0550  299 GLU C CA  
10643 C C   . GLU C 299 ? 0.3702 0.6214 0.3772 -0.0868 0.0394  0.0578  299 GLU C C   
10644 O O   . GLU C 299 ? 0.4498 0.7267 0.4646 -0.0798 0.0547  0.0594  299 GLU C O   
10645 C CB  . GLU C 299 ? 0.4383 0.7431 0.4863 -0.1230 0.0407  0.0535  299 GLU C CB  
10646 C CG  . GLU C 299 ? 0.5443 0.8490 0.6033 -0.1511 0.0348  0.0505  299 GLU C CG  
10647 C CD  . GLU C 299 ? 0.6672 1.0332 0.7655 -0.1606 0.0378  0.0457  299 GLU C CD  
10648 O OE1 . GLU C 299 ? 0.5193 0.9225 0.6324 -0.1551 0.0534  0.0492  299 GLU C OE1 
10649 O OE2 . GLU C 299 ? 0.6248 1.0030 0.7402 -0.1735 0.0244  0.0374  299 GLU C OE2 
10650 N N   . LEU C 300 ? 0.3046 0.5248 0.2955 -0.0738 0.0297  0.0578  300 LEU C N   
10651 C CA  . LEU C 300 ? 0.2909 0.5036 0.2726 -0.0518 0.0355  0.0597  300 LEU C CA  
10652 C C   . LEU C 300 ? 0.3600 0.5213 0.3084 -0.0513 0.0339  0.0617  300 LEU C C   
10653 O O   . LEU C 300 ? 0.4295 0.5793 0.3626 -0.0429 0.0450  0.0623  300 LEU C O   
10654 C CB  . LEU C 300 ? 0.2695 0.4998 0.2668 -0.0343 0.0262  0.0588  300 LEU C CB  
10655 C CG  . LEU C 300 ? 0.2577 0.5437 0.2865 -0.0268 0.0282  0.0582  300 LEU C CG  
10656 C CD1 . LEU C 300 ? 0.2427 0.5405 0.2793 -0.0084 0.0185  0.0600  300 LEU C CD1 
10657 C CD2 . LEU C 300 ? 0.2907 0.5990 0.3280 -0.0176 0.0459  0.0603  300 LEU C CD2 
10658 N N   . ILE C 301 ? 0.3322 0.4634 0.2698 -0.0595 0.0198  0.0617  301 ILE C N   
10659 C CA  . ILE C 301 ? 0.3172 0.4041 0.2271 -0.0580 0.0147  0.0636  301 ILE C CA  
10660 C C   . ILE C 301 ? 0.3890 0.4490 0.2889 -0.0742 0.0029  0.0654  301 ILE C C   
10661 O O   . ILE C 301 ? 0.4347 0.5017 0.3506 -0.0785 -0.0068 0.0627  301 ILE C O   
10662 C CB  . ILE C 301 ? 0.3025 0.3820 0.2153 -0.0409 0.0082  0.0626  301 ILE C CB  
10663 C CG1 . ILE C 301 ? 0.3302 0.3674 0.2182 -0.0416 0.0013  0.0636  301 ILE C CG1 
10664 C CG2 . ILE C 301 ? 0.2800 0.3772 0.2138 -0.0387 -0.0027 0.0606  301 ILE C CG2 
10665 C CD1 . ILE C 301 ? 0.3218 0.3510 0.2148 -0.0282 -0.0044 0.0632  301 ILE C CD1 
10666 N N   . SER C 302 ? 0.4693 0.4980 0.3415 -0.0824 0.0037  0.0699  302 SER C N   
10667 C CA  . SER C 302 ? 0.3956 0.3955 0.2569 -0.0962 -0.0077 0.0742  302 SER C CA  
10668 C C   . SER C 302 ? 0.3730 0.3515 0.2351 -0.0883 -0.0242 0.0726  302 SER C C   
10669 O O   . SER C 302 ? 0.4663 0.4351 0.3201 -0.0773 -0.0264 0.0716  302 SER C O   
10670 C CB  . SER C 302 ? 0.4747 0.4492 0.3031 -0.1066 -0.0025 0.0817  302 SER C CB  
10671 O OG  . SER C 302 ? 0.6519 0.6496 0.4800 -0.1132 0.0158  0.0829  302 SER C OG  
10672 N N   . VAL C 303 ? 0.4233 0.3947 0.2971 -0.0941 -0.0351 0.0717  303 VAL C N   
10673 C CA  . VAL C 303 ? 0.3840 0.3384 0.2626 -0.0866 -0.0496 0.0697  303 VAL C CA  
10674 C C   . VAL C 303 ? 0.3704 0.2913 0.2375 -0.0965 -0.0604 0.0755  303 VAL C C   
10675 O O   . VAL C 303 ? 0.5028 0.4203 0.3737 -0.1088 -0.0593 0.0767  303 VAL C O   
10676 C CB  . VAL C 303 ? 0.3216 0.3004 0.2271 -0.0797 -0.0526 0.0611  303 VAL C CB  
10677 C CG1 . VAL C 303 ? 0.3206 0.2860 0.2316 -0.0702 -0.0643 0.0589  303 VAL C CG1 
10678 C CG2 . VAL C 303 ? 0.2999 0.3135 0.2164 -0.0704 -0.0421 0.0582  303 VAL C CG2 
10679 N N   . PHE C 304 ? 0.3798 0.2761 0.2342 -0.0914 -0.0713 0.0796  304 PHE C N   
10680 C CA  . PHE C 304 ? 0.4102 0.2748 0.2564 -0.0964 -0.0845 0.0863  304 PHE C CA  
10681 C C   . PHE C 304 ? 0.4051 0.2680 0.2730 -0.0853 -0.0968 0.0805  304 PHE C C   
10682 O O   . PHE C 304 ? 0.3925 0.2724 0.2724 -0.0743 -0.0967 0.0747  304 PHE C O   
10683 C CB  . PHE C 304 ? 0.4724 0.3123 0.2868 -0.0989 -0.0897 0.0963  304 PHE C CB  
10684 C CG  . PHE C 304 ? 0.4867 0.3183 0.2749 -0.1128 -0.0794 0.1049  304 PHE C CG  
10685 C CD1 . PHE C 304 ? 0.4885 0.3009 0.2716 -0.1252 -0.0811 0.1136  304 PHE C CD1 
10686 C CD2 . PHE C 304 ? 0.4964 0.3381 0.2649 -0.1134 -0.0667 0.1043  304 PHE C CD2 
10687 C CE1 . PHE C 304 ? 0.5186 0.3248 0.2774 -0.1395 -0.0698 0.1232  304 PHE C CE1 
10688 C CE2 . PHE C 304 ? 0.4968 0.3340 0.2409 -0.1260 -0.0548 0.1120  304 PHE C CE2 
10689 C CZ  . PHE C 304 ? 0.5761 0.3969 0.3154 -0.1398 -0.0560 0.1222  304 PHE C CZ  
10690 N N   . PHE C 305 ? 0.4131 0.2552 0.2870 -0.0879 -0.1063 0.0821  305 PHE C N   
10691 C CA  . PHE C 305 ? 0.4182 0.2593 0.3147 -0.0765 -0.1163 0.0753  305 PHE C CA  
10692 C C   . PHE C 305 ? 0.5087 0.3193 0.3978 -0.0728 -0.1321 0.0847  305 PHE C C   
10693 O O   . PHE C 305 ? 0.6087 0.3910 0.4826 -0.0812 -0.1368 0.0946  305 PHE C O   
10694 C CB  . PHE C 305 ? 0.3933 0.2382 0.3081 -0.0797 -0.1137 0.0653  305 PHE C CB  
10695 C CG  . PHE C 305 ? 0.3646 0.2466 0.2925 -0.0785 -0.1025 0.0542  305 PHE C CG  
10696 C CD1 . PHE C 305 ? 0.3917 0.2954 0.3371 -0.0656 -0.1027 0.0446  305 PHE C CD1 
10697 C CD2 . PHE C 305 ? 0.3750 0.2725 0.2978 -0.0900 -0.0917 0.0545  305 PHE C CD2 
10698 C CE1 . PHE C 305 ? 0.3618 0.2994 0.3159 -0.0637 -0.0937 0.0365  305 PHE C CE1 
10699 C CE2 . PHE C 305 ? 0.4188 0.3529 0.3545 -0.0873 -0.0835 0.0455  305 PHE C CE2 
10700 C CZ  . PHE C 305 ? 0.4051 0.3581 0.3548 -0.0739 -0.0852 0.0371  305 PHE C CZ  
10701 N N   . ARG C 306 ? 0.4065 0.2240 0.3073 -0.0606 -0.1406 0.0827  306 ARG C N   
10702 C CA  . ARG C 306 ? 0.4930 0.2889 0.3890 -0.0556 -0.1575 0.0920  306 ARG C CA  
10703 C C   . ARG C 306 ? 0.4422 0.2217 0.3583 -0.0479 -0.1671 0.0905  306 ARG C C   
10704 O O   . ARG C 306 ? 0.4392 0.2321 0.3794 -0.0417 -0.1619 0.0779  306 ARG C O   
10705 C CB  . ARG C 306 ? 0.5059 0.3194 0.4105 -0.0472 -0.1628 0.0898  306 ARG C CB  
10706 C CG  . ARG C 306 ? 0.4828 0.3198 0.4223 -0.0351 -0.1616 0.0788  306 ARG C CG  
10707 C CD  . ARG C 306 ? 0.4026 0.2426 0.3579 -0.0260 -0.1764 0.0815  306 ARG C CD  
10708 N NE  . ARG C 306 ? 0.3638 0.2251 0.3540 -0.0141 -0.1743 0.0717  306 ARG C NE  
10709 C CZ  . ARG C 306 ? 0.4298 0.3056 0.4433 -0.0056 -0.1829 0.0714  306 ARG C CZ  
10710 N NH1 . ARG C 306 ? 0.5575 0.4290 0.5641 -0.0082 -0.1965 0.0794  306 ARG C NH1 
10711 N NH2 . ARG C 306 ? 0.4552 0.3525 0.4998 0.0050  -0.1776 0.0621  306 ARG C NH2 
10712 N N   . ASP C 307 ? 0.5623 0.3116 0.4666 -0.0476 -0.1813 0.1035  307 ASP C N   
10713 C CA  . ASP C 307 ? 0.6800 0.4082 0.6032 -0.0377 -0.1920 0.1038  307 ASP C CA  
10714 C C   . ASP C 307 ? 0.6374 0.3849 0.5895 -0.0204 -0.2017 0.0983  307 ASP C C   
10715 O O   . ASP C 307 ? 0.6176 0.3743 0.5673 -0.0176 -0.2093 0.1028  307 ASP C O   
10716 C CB  . ASP C 307 ? 0.6099 0.3113 0.5135 -0.0423 -0.1981 0.1165  307 ASP C CB  
10717 C CG  . ASP C 307 ? 0.6702 0.3459 0.5906 -0.0346 -0.2040 0.1160  307 ASP C CG  
10718 O OD1 . ASP C 307 ? 0.7041 0.3852 0.6517 -0.0178 -0.2128 0.1106  307 ASP C OD1 
10719 O OD2 . ASP C 307 ? 0.5938 0.2446 0.5017 -0.0454 -0.1985 0.1204  307 ASP C OD2 
10720 N N   . LYS C 308 ? 0.6052 0.4144 0.4156 0.0061  -0.1105 -0.0100 308 LYS C N   
10721 C CA  . LYS C 308 ? 0.5815 0.3914 0.3949 0.0133  -0.1051 -0.0119 308 LYS C CA  
10722 C C   . LYS C 308 ? 0.6221 0.4180 0.4500 0.0207  -0.1011 -0.0116 308 LYS C C   
10723 O O   . LYS C 308 ? 0.6823 0.4832 0.5204 0.0285  -0.1002 -0.0073 308 LYS C O   
10724 C CB  . LYS C 308 ? 0.6515 0.4626 0.4517 0.0086  -0.0998 -0.0226 308 LYS C CB  
10725 C CG  . LYS C 308 ? 0.6432 0.4574 0.4452 0.0147  -0.0926 -0.0244 308 LYS C CG  
10726 C CD  . LYS C 308 ? 0.5481 0.3606 0.3353 0.0092  -0.0851 -0.0367 308 LYS C CD  
10727 C CE  . LYS C 308 ? 0.7515 0.5752 0.5321 0.0114  -0.0805 -0.0348 308 LYS C CE  
10728 N NZ  . LYS C 308 ? 0.6416 0.4801 0.4103 0.0083  -0.0884 -0.0257 308 LYS C NZ  
10729 N N   . THR C 309 ? 0.6923 0.4710 0.5232 0.0185  -0.0988 -0.0159 309 THR C N   
10730 C CA  . THR C 309 ? 0.6483 0.4125 0.4950 0.0269  -0.0950 -0.0152 309 THR C CA  
10731 C C   . THR C 309 ? 0.6116 0.3803 0.4695 0.0340  -0.1019 -0.0015 309 THR C C   
10732 O O   . THR C 309 ? 0.6126 0.3829 0.4846 0.0433  -0.1008 0.0010  309 THR C O   
10733 C CB  . THR C 309 ? 0.6129 0.3549 0.4611 0.0228  -0.0915 -0.0211 309 THR C CB  
10734 O OG1 . THR C 309 ? 0.6545 0.3942 0.4965 0.0150  -0.0978 -0.0146 309 THR C OG1 
10735 C CG2 . THR C 309 ? 0.5841 0.3214 0.4218 0.0159  -0.0835 -0.0376 309 THR C CG2 
10736 N N   . LEU C 310 ? 0.6432 0.4157 0.4949 0.0292  -0.1090 0.0068  310 LEU C N   
10737 C CA  . LEU C 310 ? 0.5606 0.3389 0.4188 0.0343  -0.1158 0.0189  310 LEU C CA  
10738 C C   . LEU C 310 ? 0.5496 0.3467 0.4105 0.0385  -0.1173 0.0203  310 LEU C C   
10739 O O   . LEU C 310 ? 0.5721 0.3737 0.4443 0.0456  -0.1201 0.0255  310 LEU C O   
10740 C CB  . LEU C 310 ? 0.5126 0.2915 0.3617 0.0268  -0.1209 0.0258  310 LEU C CB  
10741 C CG  . LEU C 310 ? 0.5964 0.3569 0.4421 0.0200  -0.1191 0.0253  310 LEU C CG  
10742 C CD1 . LEU C 310 ? 0.5476 0.3103 0.3870 0.0141  -0.1239 0.0352  310 LEU C CD1 
10743 C CD2 . LEU C 310 ? 0.5956 0.3353 0.4528 0.0267  -0.1161 0.0260  310 LEU C CD2 
10744 N N   . SER C 311 ? 0.4852 0.2935 0.3365 0.0339  -0.1160 0.0160  311 SER C N   
10745 C CA  . SER C 311 ? 0.4698 0.2933 0.3235 0.0369  -0.1169 0.0180  311 SER C CA  
10746 C C   . SER C 311 ? 0.5074 0.3321 0.3715 0.0431  -0.1111 0.0139  311 SER C C   
10747 O O   . SER C 311 ? 0.5392 0.3739 0.4122 0.0470  -0.1123 0.0171  311 SER C O   
10748 C CB  . SER C 311 ? 0.4740 0.3072 0.3160 0.0313  -0.1170 0.0161  311 SER C CB  
10749 O OG  . SER C 311 ? 0.5257 0.3609 0.3618 0.0258  -0.1216 0.0192  311 SER C OG  
10750 N N   . ASP C 312 ? 0.5850 0.4005 0.4490 0.0433  -0.1040 0.0059  312 ASP C N   
10751 C CA  . ASP C 312 ? 0.5625 0.3801 0.4379 0.0490  -0.0966 0.0008  312 ASP C CA  
10752 C C   . ASP C 312 ? 0.5550 0.3673 0.4510 0.0576  -0.0975 0.0034  312 ASP C C   
10753 O O   . ASP C 312 ? 0.5962 0.4152 0.5075 0.0635  -0.0928 0.0010  312 ASP C O   
10754 C CB  . ASP C 312 ? 0.5800 0.3914 0.4458 0.0452  -0.0871 -0.0106 312 ASP C CB  
10755 C CG  . ASP C 312 ? 0.6801 0.5014 0.5276 0.0385  -0.0861 -0.0119 312 ASP C CG  
10756 O OD1 . ASP C 312 ? 0.6667 0.4987 0.5127 0.0382  -0.0914 -0.0041 312 ASP C OD1 
10757 O OD2 . ASP C 312 ? 0.9087 0.7267 0.7429 0.0335  -0.0801 -0.0207 312 ASP C OD2 
10758 N N   . LEU C 313 ? 0.5777 0.3788 0.4756 0.0586  -0.1034 0.0091  313 LEU C N   
10759 C CA  . LEU C 313 ? 0.5704 0.3675 0.4882 0.0678  -0.1067 0.0148  313 LEU C CA  
10760 C C   . LEU C 313 ? 0.5293 0.3438 0.4558 0.0712  -0.1145 0.0230  313 LEU C C   
10761 O O   . LEU C 313 ? 0.5204 0.3426 0.4668 0.0790  -0.1144 0.0235  313 LEU C O   
10762 C CB  . LEU C 313 ? 0.5190 0.2984 0.4339 0.0670  -0.1113 0.0211  313 LEU C CB  
10763 C CG  . LEU C 313 ? 0.5405 0.2985 0.4560 0.0662  -0.1033 0.0128  313 LEU C CG  
10764 C CD1 . LEU C 313 ? 0.5523 0.2945 0.4574 0.0600  -0.1077 0.0190  313 LEU C CD1 
10765 C CD2 . LEU C 313 ? 0.5538 0.3038 0.4935 0.0778  -0.0988 0.0107  313 LEU C CD2 
10766 N N   . ILE C 314 ? 0.4786 0.3003 0.3914 0.0652  -0.1211 0.0285  314 ILE C N   
10767 C CA  . ILE C 314 ? 0.4661 0.3041 0.3848 0.0665  -0.1279 0.0339  314 ILE C CA  
10768 C C   . ILE C 314 ? 0.4932 0.3443 0.4201 0.0672  -0.1219 0.0276  314 ILE C C   
10769 O O   . ILE C 314 ? 0.5227 0.3863 0.4654 0.0711  -0.1247 0.0292  314 ILE C O   
10770 C CB  . ILE C 314 ? 0.4594 0.3009 0.3609 0.0592  -0.1337 0.0386  314 ILE C CB  
10771 C CG1 . ILE C 314 ? 0.4872 0.3175 0.3818 0.0580  -0.1395 0.0465  314 ILE C CG1 
10772 C CG2 . ILE C 314 ? 0.4477 0.3059 0.3532 0.0588  -0.1387 0.0406  314 ILE C CG2 
10773 C CD1 . ILE C 314 ? 0.4674 0.3023 0.3459 0.0505  -0.1437 0.0504  314 ILE C CD1 
10774 N N   . GLY C 315 ? 0.4915 0.3405 0.4078 0.0628  -0.1137 0.0209  315 GLY C N   
10775 C CA  . GLY C 315 ? 0.4478 0.3077 0.3682 0.0618  -0.1075 0.0168  315 GLY C CA  
10776 C C   . GLY C 315 ? 0.4663 0.3291 0.4046 0.0672  -0.0992 0.0110  315 GLY C C   
10777 O O   . GLY C 315 ? 0.5451 0.4200 0.4941 0.0673  -0.0954 0.0095  315 GLY C O   
10778 N N   . PHE C 316 ? 0.5110 0.3625 0.4541 0.0714  -0.0950 0.0069  316 PHE C N   
10779 C CA  . PHE C 316 ? 0.5497 0.4038 0.5088 0.0760  -0.0840 -0.0011 316 PHE C CA  
10780 C C   . PHE C 316 ? 0.5667 0.4161 0.5497 0.0861  -0.0846 -0.0013 316 PHE C C   
10781 O O   . PHE C 316 ? 0.6760 0.5350 0.6818 0.0920  -0.0783 -0.0056 316 PHE C O   
10782 C CB  . PHE C 316 ? 0.4863 0.3320 0.4274 0.0704  -0.0727 -0.0106 316 PHE C CB  
10783 C CG  . PHE C 316 ? 0.5062 0.3582 0.4268 0.0620  -0.0715 -0.0094 316 PHE C CG  
10784 C CD1 . PHE C 316 ? 0.6122 0.4774 0.5392 0.0609  -0.0671 -0.0085 316 PHE C CD1 
10785 C CD2 . PHE C 316 ? 0.6550 0.5000 0.5517 0.0554  -0.0749 -0.0086 316 PHE C CD2 
10786 C CE1 . PHE C 316 ? 0.5789 0.4476 0.4882 0.0540  -0.0660 -0.0055 316 PHE C CE1 
10787 C CE2 . PHE C 316 ? 0.6337 0.4848 0.5138 0.0492  -0.0747 -0.0058 316 PHE C CE2 
10788 C CZ  . PHE C 316 ? 0.5509 0.4126 0.4369 0.0489  -0.0703 -0.0037 316 PHE C CZ  
10789 N N   . SER C 317 ? 0.5348 0.3697 0.5149 0.0884  -0.0915 0.0038  317 SER C N   
10790 C CA  . SER C 317 ? 0.6147 0.4411 0.6176 0.0989  -0.0915 0.0045  317 SER C CA  
10791 C C   . SER C 317 ? 0.6398 0.4722 0.6567 0.1055  -0.1060 0.0180  317 SER C C   
10792 O O   . SER C 317 ? 0.7060 0.5439 0.7504 0.1160  -0.1073 0.0199  317 SER C O   
10793 C CB  . SER C 317 ? 0.6461 0.4477 0.6382 0.0975  -0.0872 0.0003  317 SER C CB  
10794 O OG  . SER C 317 ? 0.6109 0.4056 0.5771 0.0879  -0.0934 0.0049  317 SER C OG  
10795 N N   . TYR C 318 ? 0.5808 0.4135 0.5797 0.0996  -0.1169 0.0274  318 TYR C N   
10796 C CA  . TYR C 318 ? 0.5006 0.3379 0.5073 0.1044  -0.1310 0.0407  318 TYR C CA  
10797 C C   . TYR C 318 ? 0.5340 0.3960 0.5615 0.1088  -0.1368 0.0428  318 TYR C C   
10798 O O   . TYR C 318 ? 0.5530 0.4221 0.5893 0.1136  -0.1496 0.0536  318 TYR C O   
10799 C CB  . TYR C 318 ? 0.4968 0.3308 0.4771 0.0953  -0.1392 0.0483  318 TYR C CB  
10800 C CG  . TYR C 318 ? 0.5541 0.3646 0.5192 0.0922  -0.1383 0.0515  318 TYR C CG  
10801 C CD1 . TYR C 318 ? 0.6094 0.4013 0.5872 0.0996  -0.1356 0.0528  318 TYR C CD1 
10802 C CD2 . TYR C 318 ? 0.5481 0.3551 0.4883 0.0816  -0.1398 0.0529  318 TYR C CD2 
10803 C CE1 . TYR C 318 ? 0.5482 0.3173 0.5130 0.0952  -0.1342 0.0554  318 TYR C CE1 
10804 C CE2 . TYR C 318 ? 0.5221 0.3093 0.4501 0.0773  -0.1385 0.0555  318 TYR C CE2 
10805 C CZ  . TYR C 318 ? 0.5427 0.3102 0.4823 0.0834  -0.1357 0.0567  318 TYR C CZ  
10806 O OH  . TYR C 318 ? 0.5592 0.3055 0.4872 0.0777  -0.1338 0.0589  318 TYR C OH  
10807 N N   . HIS C 319 ? 0.5750 0.4510 0.6099 0.1065  -0.1282 0.0331  319 HIS C N   
10808 C CA  . HIS C 319 ? 0.5759 0.4763 0.6327 0.1090  -0.1329 0.0338  319 HIS C CA  
10809 C C   . HIS C 319 ? 0.6183 0.5254 0.7093 0.1220  -0.1350 0.0358  319 HIS C C   
10810 O O   . HIS C 319 ? 0.5454 0.4719 0.6549 0.1260  -0.1462 0.0419  319 HIS C O   
10811 C CB  . HIS C 319 ? 0.5374 0.4486 0.5939 0.1023  -0.1213 0.0235  319 HIS C CB  
10812 C CG  . HIS C 319 ? 0.5738 0.4901 0.6541 0.1081  -0.1083 0.0144  319 HIS C CG  
10813 N ND1 . HIS C 319 ? 0.5135 0.4142 0.5867 0.1085  -0.0946 0.0060  319 HIS C ND1 
10814 C CD2 . HIS C 319 ? 0.4672 0.4040 0.5789 0.1131  -0.1061 0.0113  319 HIS C CD2 
10815 C CE1 . HIS C 319 ? 0.4764 0.3868 0.5745 0.1137  -0.0835 -0.0021 319 HIS C CE1 
10816 N NE2 . HIS C 319 ? 0.4681 0.4009 0.5913 0.1168  -0.0902 0.0013  319 HIS C NE2 
10817 N N   . ALA C 320 ? 0.5457 0.4382 0.6469 0.1289  -0.1244 0.0302  320 ALA C N   
10818 C CA  . ALA C 320 ? 0.5126 0.4085 0.6491 0.1431  -0.1250 0.0319  320 ALA C CA  
10819 C C   . ALA C 320 ? 0.6007 0.4787 0.7372 0.1508  -0.1361 0.0449  320 ALA C C   
10820 O O   . ALA C 320 ? 0.5394 0.4078 0.7001 0.1629  -0.1330 0.0453  320 ALA C O   
10821 C CB  . ALA C 320 ? 0.5218 0.4109 0.6716 0.1467  -0.1057 0.0171  320 ALA C CB  
10822 N N   . TRP C 321 ? 0.6212 0.4936 0.7313 0.1439  -0.1482 0.0558  321 TRP C N   
10823 C CA  . TRP C 321 ? 0.7331 0.5856 0.8359 0.1481  -0.1575 0.0695  321 TRP C CA  
10824 C C   . TRP C 321 ? 0.7359 0.6047 0.8401 0.1501  -0.1771 0.0854  321 TRP C C   
10825 O O   . TRP C 321 ? 0.6760 0.5673 0.7740 0.1431  -0.1831 0.0843  321 TRP C O   
10826 C CB  . TRP C 321 ? 0.5797 0.4102 0.6463 0.1363  -0.1536 0.0687  321 TRP C CB  
10827 C CG  . TRP C 321 ? 0.5868 0.3918 0.6505 0.1363  -0.1392 0.0588  321 TRP C CG  
10828 C CD1 . TRP C 321 ? 0.6778 0.4824 0.7499 0.1366  -0.1237 0.0425  321 TRP C CD1 
10829 C CD2 . TRP C 321 ? 0.5743 0.3507 0.6239 0.1342  -0.1386 0.0637  321 TRP C CD2 
10830 N NE1 . TRP C 321 ? 0.5694 0.3473 0.6330 0.1349  -0.1140 0.0358  321 TRP C NE1 
10831 C CE2 . TRP C 321 ? 0.6311 0.3910 0.6823 0.1333  -0.1229 0.0486  321 TRP C CE2 
10832 C CE3 . TRP C 321 ? 0.7010 0.4642 0.7365 0.1321  -0.1492 0.0793  321 TRP C CE3 
10833 C CZ2 . TRP C 321 ? 0.7136 0.4440 0.7542 0.1300  -0.1180 0.0476  321 TRP C CZ2 
10834 C CZ3 . TRP C 321 ? 0.7393 0.4729 0.7647 0.1289  -0.1436 0.0797  321 TRP C CZ3 
10835 C CH2 . TRP C 321 ? 0.7426 0.4600 0.7716 0.1278  -0.1284 0.0635  321 TRP C CH2 
10836 N N   . ASN C 322 ? 0.6138 0.4704 0.7256 0.1593  -0.1869 0.1003  322 ASN C N   
10837 C CA  . ASN C 322 ? 0.6894 0.5556 0.7908 0.1585  -0.2060 0.1177  322 ASN C CA  
10838 C C   . ASN C 322 ? 0.7339 0.5901 0.7934 0.1433  -0.2067 0.1199  322 ASN C C   
10839 O O   . ASN C 322 ? 0.7334 0.5669 0.7754 0.1371  -0.1955 0.1143  322 ASN C O   
10840 C CB  . ASN C 322 ? 0.6018 0.4536 0.7197 0.1723  -0.2155 0.1351  322 ASN C CB  
10841 C CG  . ASN C 322 ? 0.8576 0.7159 0.9528 0.1671  -0.2295 0.1532  322 ASN C CG  
10842 O OD1 . ASN C 322 ? 0.9639 0.8454 1.0433 0.1578  -0.2375 0.1534  322 ASN C OD1 
10843 N ND2 . ASN C 322 ? 0.9274 0.7662 1.0194 0.1717  -0.2291 0.1668  322 ASN C ND2 
10844 N N   . ALA C 323 ? 0.7679 0.6429 0.8125 0.1367  -0.2198 0.1270  323 ALA C N   
10845 C CA  . ALA C 323 ? 0.6778 0.5471 0.6849 0.1223  -0.2196 0.1276  323 ALA C CA  
10846 C C   . ALA C 323 ? 0.7312 0.5727 0.7197 0.1210  -0.2202 0.1402  323 ALA C C   
10847 O O   . ALA C 323 ? 0.6327 0.4575 0.6005 0.1119  -0.2101 0.1345  323 ALA C O   
10848 C CB  . ALA C 323 ? 0.7703 0.6652 0.7663 0.1160  -0.2333 0.1320  323 ALA C CB  
10849 N N   . GLU C 324 ? 0.8655 0.7050 0.8618 0.1285  -0.2282 0.1560  324 GLU C N   
10850 C CA  . GLU C 324 ? 0.8760 0.6903 0.8555 0.1258  -0.2253 0.1680  324 GLU C CA  
10851 C C   . GLU C 324 ? 0.7852 0.5664 0.7743 0.1306  -0.2150 0.1629  324 GLU C C   
10852 O O   . GLU C 324 ? 0.8122 0.5689 0.7819 0.1233  -0.2100 0.1668  324 GLU C O   
10853 C CB  . GLU C 324 ? 0.8920 0.7134 0.8792 0.1334  -0.2333 0.1854  324 GLU C CB  
10854 C CG  . GLU C 324 ? 0.9260 0.7769 0.8968 0.1267  -0.2438 0.1912  324 GLU C CG  
10855 C CD  . GLU C 324 ? 1.0356 0.8774 0.9735 0.1170  -0.2447 0.2039  324 GLU C CD  
10856 O OE1 . GLU C 324 ? 1.1114 0.9241 1.0405 0.1149  -0.2373 0.2089  324 GLU C OE1 
10857 O OE2 . GLU C 324 ? 0.9804 0.8441 0.9016 0.1111  -0.2524 0.2083  324 GLU C OE2 
10858 N N   . ASP C 325 ? 0.7279 0.5089 0.7473 0.1418  -0.2101 0.1528  325 ASP C N   
10859 C CA  . ASP C 325 ? 0.6386 0.3937 0.6651 0.1429  -0.1940 0.1412  325 ASP C CA  
10860 C C   . ASP C 325 ? 0.7034 0.4583 0.7070 0.1283  -0.1818 0.1244  325 ASP C C   
10861 O O   . ASP C 325 ? 0.6266 0.3578 0.6191 0.1222  -0.1719 0.1192  325 ASP C O   
10862 C CB  . ASP C 325 ? 0.7173 0.4776 0.7820 0.1573  -0.1882 0.1321  325 ASP C CB  
10863 C CG  . ASP C 325 ? 0.9486 0.7096 1.0410 0.1738  -0.2007 0.1492  325 ASP C CG  
10864 O OD1 . ASP C 325 ? 0.8666 0.6225 0.9440 0.1711  -0.2061 0.1658  325 ASP C OD1 
10865 O OD2 . ASP C 325 ? 1.0009 0.7748 1.1282 0.1865  -0.1989 0.1434  325 ASP C OD2 
10866 N N   . ALA C 326 ? 0.6690 0.4501 0.6661 0.1223  -0.1827 0.1160  326 ALA C N   
10867 C CA  . ALA C 326 ? 0.5985 0.3811 0.5766 0.1101  -0.1720 0.1013  326 ALA C CA  
10868 C C   . ALA C 326 ? 0.6597 0.4329 0.6073 0.0976  -0.1736 0.1070  326 ALA C C   
10869 O O   . ALA C 326 ? 0.6605 0.4209 0.5954 0.0895  -0.1640 0.0985  326 ALA C O   
10870 C CB  . ALA C 326 ? 0.5536 0.3645 0.5349 0.1078  -0.1727 0.0926  326 ALA C CB  
10871 N N   . VAL C 327 ? 0.5911 0.3723 0.5267 0.0953  -0.1856 0.1209  327 VAL C N   
10872 C CA  . VAL C 327 ? 0.5883 0.3631 0.4953 0.0829  -0.1858 0.1261  327 VAL C CA  
10873 C C   . VAL C 327 ? 0.6123 0.3570 0.5148 0.0811  -0.1808 0.1322  327 VAL C C   
10874 O O   . VAL C 327 ? 0.6297 0.3649 0.5167 0.0702  -0.1729 0.1262  327 VAL C O   
10875 C CB  . VAL C 327 ? 0.7795 0.5698 0.6732 0.0805  -0.1991 0.1393  327 VAL C CB  
10876 C CG1 . VAL C 327 ? 0.6452 0.4249 0.5111 0.0689  -0.1987 0.1478  327 VAL C CG1 
10877 C CG2 . VAL C 327 ? 0.5831 0.4015 0.4765 0.0776  -0.2013 0.1292  327 VAL C CG2 
10878 N N   . ARG C 328 ? 0.6361 0.3651 0.5542 0.0917  -0.1852 0.1438  328 ARG C N   
10879 C CA  . ARG C 328 ? 0.6629 0.3599 0.5784 0.0898  -0.1799 0.1501  328 ARG C CA  
10880 C C   . ARG C 328 ? 0.6992 0.3808 0.6230 0.0879  -0.1654 0.1320  328 ARG C C   
10881 O O   . ARG C 328 ? 0.7410 0.3984 0.6567 0.0805  -0.1587 0.1320  328 ARG C O   
10882 C CB  . ARG C 328 ? 0.6923 0.3747 0.6248 0.1031  -0.1884 0.1681  328 ARG C CB  
10883 C CG  . ARG C 328 ? 0.7665 0.4457 0.6793 0.0977  -0.1962 0.1890  328 ARG C CG  
10884 C CD  . ARG C 328 ? 0.7348 0.4238 0.6656 0.1105  -0.2026 0.2034  328 ARG C CD  
10885 N NE  . ARG C 328 ? 0.8592 0.5374 0.8240 0.1259  -0.1990 0.1982  328 ARG C NE  
10886 C CZ  . ARG C 328 ? 0.9435 0.6432 0.9333 0.1392  -0.2046 0.1985  328 ARG C CZ  
10887 N NH1 . ARG C 328 ? 0.9292 0.6617 0.9138 0.1387  -0.2149 0.2041  328 ARG C NH1 
10888 N NH2 . ARG C 328 ? 0.8222 0.5106 0.8439 0.1527  -0.1990 0.1920  328 ARG C NH2 
10889 N N   . ASP C 329 ? 0.6501 0.3451 0.5889 0.0932  -0.1601 0.1165  329 ASP C N   
10890 C CA  . ASP C 329 ? 0.7172 0.4019 0.6573 0.0886  -0.1464 0.0978  329 ASP C CA  
10891 C C   . ASP C 329 ? 0.6572 0.3520 0.5733 0.0736  -0.1427 0.0892  329 ASP C C   
10892 O O   . ASP C 329 ? 0.6876 0.3680 0.5952 0.0646  -0.1347 0.0807  329 ASP C O   
10893 C CB  . ASP C 329 ? 0.6545 0.3512 0.6162 0.0983  -0.1410 0.0847  329 ASP C CB  
10894 C CG  . ASP C 329 ? 0.6400 0.3292 0.5988 0.0925  -0.1270 0.0649  329 ASP C CG  
10895 O OD1 . ASP C 329 ? 0.7151 0.3785 0.6777 0.0919  -0.1196 0.0603  329 ASP C OD1 
10896 O OD2 . ASP C 329 ? 0.6108 0.3193 0.5628 0.0880  -0.1235 0.0540  329 ASP C OD2 
10897 N N   . PHE C 330 ? 0.6600 0.3802 0.5667 0.0707  -0.1487 0.0908  330 PHE C N   
10898 C CA  . PHE C 330 ? 0.5784 0.3097 0.4654 0.0581  -0.1459 0.0839  330 PHE C CA  
10899 C C   . PHE C 330 ? 0.5933 0.3122 0.4632 0.0476  -0.1465 0.0923  330 PHE C C   
10900 O O   . PHE C 330 ? 0.6313 0.3467 0.4914 0.0372  -0.1402 0.0841  330 PHE C O   
10901 C CB  . PHE C 330 ? 0.5817 0.3400 0.4650 0.0585  -0.1519 0.0845  330 PHE C CB  
10902 C CG  . PHE C 330 ? 0.5378 0.3090 0.4064 0.0484  -0.1483 0.0761  330 PHE C CG  
10903 C CD1 . PHE C 330 ? 0.5220 0.3015 0.3939 0.0482  -0.1421 0.0630  330 PHE C CD1 
10904 C CD2 . PHE C 330 ? 0.5779 0.3536 0.4298 0.0395  -0.1510 0.0817  330 PHE C CD2 
10905 C CE1 . PHE C 330 ? 0.5416 0.3328 0.4019 0.0404  -0.1399 0.0571  330 PHE C CE1 
10906 C CE2 . PHE C 330 ? 0.5225 0.3108 0.3647 0.0317  -0.1475 0.0740  330 PHE C CE2 
10907 C CZ  . PHE C 330 ? 0.5682 0.3640 0.4154 0.0327  -0.1427 0.0623  330 PHE C CZ  
10908 N N   . ILE C 331 ? 0.6242 0.3374 0.4904 0.0495  -0.1542 0.1090  331 ILE C N   
10909 C CA  . ILE C 331 ? 0.6280 0.3289 0.4773 0.0386  -0.1537 0.1185  331 ILE C CA  
10910 C C   . ILE C 331 ? 0.7380 0.4098 0.5922 0.0353  -0.1458 0.1159  331 ILE C C   
10911 O O   . ILE C 331 ? 0.7615 0.4259 0.6041 0.0225  -0.1404 0.1138  331 ILE C O   
10912 C CB  . ILE C 331 ? 0.6529 0.3543 0.4948 0.0415  -0.1641 0.1384  331 ILE C CB  
10913 C CG1 . ILE C 331 ? 0.6249 0.3560 0.4607 0.0426  -0.1715 0.1380  331 ILE C CG1 
10914 C CG2 . ILE C 331 ? 0.6674 0.3550 0.4903 0.0293  -0.1621 0.1493  331 ILE C CG2 
10915 C CD1 . ILE C 331 ? 0.6050 0.3526 0.4259 0.0312  -0.1664 0.1277  331 ILE C CD1 
10916 N N   . GLY C 332 ? 0.7212 0.3765 0.5945 0.0464  -0.1444 0.1151  332 GLY C N   
10917 C CA  . GLY C 332 ? 0.7259 0.3511 0.6054 0.0433  -0.1359 0.1108  332 GLY C CA  
10918 C C   . GLY C 332 ? 0.7275 0.3548 0.6029 0.0332  -0.1262 0.0903  332 GLY C C   
10919 O O   . GLY C 332 ? 0.7329 0.3425 0.6028 0.0221  -0.1200 0.0866  332 GLY C O   
10920 N N   . ARG C 333 ? 0.6696 0.3187 0.5475 0.0363  -0.1250 0.0770  333 ARG C N   
10921 C CA  . ARG C 333 ? 0.7023 0.3570 0.5736 0.0266  -0.1176 0.0591  333 ARG C CA  
10922 C C   . ARG C 333 ? 0.7281 0.3941 0.5822 0.0124  -0.1188 0.0604  333 ARG C C   
10923 O O   . ARG C 333 ? 0.7844 0.4448 0.6333 0.0010  -0.1135 0.0506  333 ARG C O   
10924 C CB  . ARG C 333 ? 0.6156 0.2918 0.4914 0.0330  -0.1166 0.0479  333 ARG C CB  
10925 C CG  . ARG C 333 ? 0.6251 0.2908 0.5187 0.0440  -0.1110 0.0399  333 ARG C CG  
10926 C CD  . ARG C 333 ? 0.6016 0.2911 0.4995 0.0504  -0.1108 0.0331  333 ARG C CD  
10927 N NE  . ARG C 333 ? 0.6096 0.2932 0.5277 0.0623  -0.1055 0.0275  333 ARG C NE  
10928 C CZ  . ARG C 333 ? 0.6195 0.2947 0.5412 0.0617  -0.0948 0.0113  333 ARG C CZ  
10929 N NH1 . ARG C 333 ? 0.6242 0.2950 0.5297 0.0495  -0.0894 -0.0006 333 ARG C NH1 
10930 N NH2 . ARG C 333 ? 0.6263 0.2988 0.5685 0.0734  -0.0891 0.0062  333 ARG C NH2 
10931 N N   . LEU C 334 ? 0.6808 0.3642 0.5269 0.0125  -0.1256 0.0714  334 LEU C N   
10932 C CA  . LEU C 334 ? 0.7654 0.4586 0.5974 -0.0004 -0.1256 0.0738  334 LEU C CA  
10933 C C   . LEU C 334 ? 0.8143 0.4838 0.6426 -0.0100 -0.1221 0.0807  334 LEU C C   
10934 O O   . LEU C 334 ? 0.8495 0.5206 0.6720 -0.0232 -0.1177 0.0748  334 LEU C O   
10935 C CB  . LEU C 334 ? 0.7277 0.4405 0.5518 0.0018  -0.1324 0.0842  334 LEU C CB  
10936 C CG  . LEU C 334 ? 0.6538 0.3932 0.4785 0.0064  -0.1349 0.0771  334 LEU C CG  
10937 C CD1 . LEU C 334 ? 0.5814 0.3368 0.3956 0.0042  -0.1397 0.0857  334 LEU C CD1 
10938 C CD2 . LEU C 334 ? 0.6576 0.4078 0.4813 0.0000  -0.1301 0.0629  334 LEU C CD2 
10939 N N   . LYS C 335 ? 0.7814 0.4289 0.6144 -0.0035 -0.1242 0.0939  335 LYS C N   
10940 C CA  . LYS C 335 ? 0.7970 0.4175 0.6272 -0.0122 -0.1203 0.1025  335 LYS C CA  
10941 C C   . LYS C 335 ? 0.8172 0.4199 0.6545 -0.0197 -0.1115 0.0869  335 LYS C C   
10942 O O   . LYS C 335 ? 0.8742 0.4670 0.7062 -0.0342 -0.1064 0.0859  335 LYS C O   
10943 C CB  . LYS C 335 ? 0.8374 0.4368 0.6736 -0.0010 -0.1252 0.1207  335 LYS C CB  
10944 C CG  . LYS C 335 ? 0.7584 0.3324 0.5869 -0.0099 -0.1233 0.1367  335 LYS C CG  
10945 C CD  . LYS C 335 ? 0.8729 0.4365 0.7019 0.0018  -0.1322 0.1594  335 LYS C CD  
10946 C CE  . LYS C 335 ? 0.8544 0.4042 0.7065 0.0194  -0.1342 0.1579  335 LYS C CE  
10947 N NZ  . LYS C 335 ? 0.8285 0.3876 0.6837 0.0339  -0.1465 0.1753  335 LYS C NZ  
10948 N N   . LYS C 336 ? 0.7971 0.3964 0.6464 -0.0109 -0.1090 0.0737  336 LYS C N   
10949 C CA  . LYS C 336 ? 0.8124 0.3969 0.6664 -0.0187 -0.1005 0.0561  336 LYS C CA  
10950 C C   . LYS C 336 ? 0.8627 0.4693 0.7064 -0.0330 -0.0990 0.0429  336 LYS C C   
10951 O O   . LYS C 336 ? 0.9532 0.5486 0.7961 -0.0462 -0.0933 0.0328  336 LYS C O   
10952 C CB  . LYS C 336 ? 0.8543 0.4344 0.7212 -0.0062 -0.0973 0.0438  336 LYS C CB  
10953 C CG  . LYS C 336 ? 0.8244 0.3789 0.7076 0.0079  -0.0971 0.0537  336 LYS C CG  
10954 C CD  . LYS C 336 ? 1.1007 0.6584 0.9983 0.0209  -0.0934 0.0408  336 LYS C CD  
10955 C CE  . LYS C 336 ? 1.0601 0.6063 0.9581 0.0127  -0.0825 0.0176  336 LYS C CE  
10956 N NZ  . LYS C 336 ? 0.9778 0.5325 0.8856 0.0233  -0.0775 0.0034  336 LYS C NZ  
10957 N N   . ILE C 337 ? 0.8340 0.4721 0.6713 -0.0305 -0.1043 0.0427  337 ILE C N   
10958 C CA  . ILE C 337 ? 0.7449 0.4063 0.5750 -0.0421 -0.1042 0.0323  337 ILE C CA  
10959 C C   . ILE C 337 ? 0.6867 0.3491 0.5112 -0.0561 -0.1032 0.0397  337 ILE C C   
10960 O O   . ILE C 337 ? 0.7567 0.4255 0.5802 -0.0696 -0.1005 0.0298  337 ILE C O   
10961 C CB  . ILE C 337 ? 0.8121 0.5041 0.6392 -0.0343 -0.1096 0.0315  337 ILE C CB  
10962 C CG1 . ILE C 337 ? 0.7898 0.4834 0.6215 -0.0250 -0.1082 0.0204  337 ILE C CG1 
10963 C CG2 . ILE C 337 ? 0.7099 0.4272 0.5313 -0.0447 -0.1110 0.0264  337 ILE C CG2 
10964 C CD1 . ILE C 337 ? 0.6039 0.3152 0.4371 -0.0124 -0.1128 0.0254  337 ILE C CD1 
10965 N N   . HIS C 338 ? 0.7454 0.4027 0.5659 -0.0536 -0.1054 0.0571  338 HIS C N   
10966 C CA  . HIS C 338 ? 0.7304 0.3895 0.5441 -0.0673 -0.1031 0.0652  338 HIS C CA  
10967 C C   . HIS C 338 ? 0.7387 0.3722 0.5559 -0.0808 -0.0960 0.0615  338 HIS C C   
10968 O O   . HIS C 338 ? 0.7123 0.3547 0.5282 -0.0963 -0.0924 0.0574  338 HIS C O   
10969 C CB  . HIS C 338 ? 0.6869 0.3419 0.4926 -0.0619 -0.1066 0.0853  338 HIS C CB  
10970 C CG  . HIS C 338 ? 0.8377 0.5036 0.6332 -0.0748 -0.1039 0.0932  338 HIS C CG  
10971 N ND1 . HIS C 338 ? 0.8786 0.5231 0.6698 -0.0865 -0.0986 0.1034  338 HIS C ND1 
10972 C CD2 . HIS C 338 ? 0.7748 0.4704 0.5643 -0.0780 -0.1047 0.0921  338 HIS C CD2 
10973 C CE1 . HIS C 338 ? 0.7979 0.4600 0.5799 -0.0970 -0.0957 0.1081  338 HIS C CE1 
10974 N NE2 . HIS C 338 ? 0.7222 0.4156 0.5037 -0.0916 -0.0992 0.1007  338 HIS C NE2 
10975 N N   . GLU C 339 ? 0.8859 0.4879 0.7098 -0.0754 -0.0936 0.0621  339 GLU C N   
10976 C CA  . GLU C 339 ? 0.9562 0.5281 0.7848 -0.0877 -0.0861 0.0591  339 GLU C CA  
10977 C C   . GLU C 339 ? 0.9789 0.5489 0.8140 -0.0944 -0.0819 0.0358  339 GLU C C   
10978 O O   . GLU C 339 ? 0.9278 0.4730 0.7676 -0.1062 -0.0751 0.0296  339 GLU C O   
10979 C CB  . GLU C 339 ? 0.8829 0.4179 0.7168 -0.0780 -0.0850 0.0733  339 GLU C CB  
10980 C CG  . GLU C 339 ? 0.9956 0.5208 0.8408 -0.0611 -0.0859 0.0655  339 GLU C CG  
10981 C CD  . GLU C 339 ? 1.1861 0.6711 1.0420 -0.0532 -0.0831 0.0763  339 GLU C CD  
10982 O OE1 . GLU C 339 ? 1.0840 0.5638 0.9387 -0.0429 -0.0890 0.0976  339 GLU C OE1 
10983 O OE2 . GLU C 339 ? 1.3134 0.7722 1.1794 -0.0571 -0.0752 0.0635  339 GLU C OE2 
10984 N N   . SER C 340 ? 0.9063 0.5012 0.7407 -0.0881 -0.0856 0.0228  340 SER C N   
10985 C CA  . SER C 340 ? 0.9119 0.5093 0.7483 -0.0955 -0.0826 0.0007  340 SER C CA  
10986 C C   . SER C 340 ? 0.9315 0.5586 0.7640 -0.1106 -0.0848 -0.0084 340 SER C C   
10987 O O   . SER C 340 ? 0.9844 0.6140 0.8175 -0.1208 -0.0830 -0.0263 340 SER C O   
10988 C CB  . SER C 340 ? 0.8815 0.4881 0.7182 -0.0808 -0.0847 -0.0082 340 SER C CB  
10989 O OG  . SER C 340 ? 0.8194 0.4600 0.6505 -0.0744 -0.0918 -0.0040 340 SER C OG  
10990 N N   . VAL C 341 ? 0.9004 0.5511 0.7297 -0.1121 -0.0886 0.0027  341 VAL C N   
10991 C CA  . VAL C 341 ? 0.8846 0.5668 0.7142 -0.1244 -0.0911 -0.0045 341 VAL C CA  
10992 C C   . VAL C 341 ? 0.9574 0.6386 0.7885 -0.1371 -0.0871 0.0062  341 VAL C C   
10993 O O   . VAL C 341 ? 1.0435 0.7103 0.8707 -0.1325 -0.0853 0.0229  341 VAL C O   
10994 C CB  . VAL C 341 ? 0.8214 0.5383 0.6482 -0.1134 -0.0984 -0.0035 341 VAL C CB  
10995 C CG1 . VAL C 341 ? 0.8742 0.5881 0.6981 -0.0995 -0.1009 -0.0100 341 VAL C CG1 
10996 C CG2 . VAL C 341 ? 0.8433 0.5682 0.6673 -0.1061 -0.0997 0.0136  341 VAL C CG2 
10997 N N   . ASP C 342 ? 0.9266 0.6240 0.7633 -0.1540 -0.0858 -0.0034 342 ASP C N   
10998 C CA  . ASP C 342 ? 0.9862 0.6862 0.8260 -0.1686 -0.0805 0.0046  342 ASP C CA  
10999 C C   . ASP C 342 ? 0.8664 0.6083 0.7098 -0.1700 -0.0837 0.0056  342 ASP C C   
11000 O O   . ASP C 342 ? 0.8012 0.5567 0.6519 -0.1853 -0.0795 0.0047  342 ASP C O   
11001 C CB  . ASP C 342 ? 1.0723 0.7577 0.9196 -0.1890 -0.0746 -0.0067 342 ASP C CB  
11002 C CG  . ASP C 342 ? 1.2550 0.9621 1.1079 -0.1958 -0.0796 -0.0278 342 ASP C CG  
11003 O OD1 . ASP C 342 ? 1.1836 0.8821 1.0319 -0.1869 -0.0827 -0.0374 342 ASP C OD1 
11004 O OD2 . ASP C 342 ? 1.3549 1.0889 1.2167 -0.2103 -0.0804 -0.0348 342 ASP C OD2 
11005 N N   . PHE C 343 ? 0.8877 0.6499 0.7280 -0.1541 -0.0904 0.0069  343 PHE C N   
11006 C CA  . PHE C 343 ? 0.7702 0.5672 0.6140 -0.1513 -0.0927 0.0102  343 PHE C CA  
11007 C C   . PHE C 343 ? 0.8129 0.6059 0.6467 -0.1352 -0.0941 0.0234  343 PHE C C   
11008 O O   . PHE C 343 ? 0.7889 0.5546 0.6147 -0.1270 -0.0941 0.0305  343 PHE C O   
11009 C CB  . PHE C 343 ? 0.7171 0.5463 0.5688 -0.1487 -0.1002 -0.0024 343 PHE C CB  
11010 C CG  . PHE C 343 ? 0.7609 0.5834 0.6061 -0.1359 -0.1064 -0.0081 343 PHE C CG  
11011 C CD1 . PHE C 343 ? 0.8525 0.6545 0.6949 -0.1409 -0.1059 -0.0183 343 PHE C CD1 
11012 C CD2 . PHE C 343 ? 0.7936 0.6299 0.6356 -0.1197 -0.1115 -0.0040 343 PHE C CD2 
11013 C CE1 . PHE C 343 ? 0.8738 0.6707 0.7093 -0.1299 -0.1099 -0.0243 343 PHE C CE1 
11014 C CE2 . PHE C 343 ? 0.7492 0.5799 0.5850 -0.1091 -0.1158 -0.0088 343 PHE C CE2 
11015 C CZ  . PHE C 343 ? 0.8461 0.6578 0.6782 -0.1141 -0.1147 -0.0189 343 PHE C CZ  
11016 N N   . GLN C 344 ? 0.6842 0.5051 0.5201 -0.1306 -0.0952 0.0261  344 GLN C N   
11017 C CA  . GLN C 344 ? 0.6669 0.4865 0.4933 -0.1164 -0.0971 0.0362  344 GLN C CA  
11018 C C   . GLN C 344 ? 0.6939 0.5213 0.5211 -0.1014 -0.1046 0.0305  344 GLN C C   
11019 O O   . GLN C 344 ? 0.7712 0.6253 0.6058 -0.0980 -0.1078 0.0244  344 GLN C O   
11020 C CB  . GLN C 344 ? 0.5883 0.4310 0.4153 -0.1189 -0.0931 0.0408  344 GLN C CB  
11021 C CG  . GLN C 344 ? 0.6301 0.4562 0.4435 -0.1232 -0.0873 0.0549  344 GLN C CG  
11022 C CD  . GLN C 344 ? 0.6244 0.4742 0.4363 -0.1266 -0.0817 0.0575  344 GLN C CD  
11023 O OE1 . GLN C 344 ? 0.7676 0.6461 0.5922 -0.1256 -0.0815 0.0483  344 GLN C OE1 
11024 N NE2 . GLN C 344 ? 0.6223 0.4601 0.4185 -0.1306 -0.0769 0.0701  344 GLN C NE2 
11025 N N   . PRO C 345 ? 0.6341 0.4390 0.4551 -0.0920 -0.1070 0.0328  345 PRO C N   
11026 C CA  . PRO C 345 ? 0.6619 0.4733 0.4840 -0.0799 -0.1126 0.0264  345 PRO C CA  
11027 C C   . PRO C 345 ? 0.6109 0.4392 0.4317 -0.0683 -0.1156 0.0311  345 PRO C C   
11028 O O   . PRO C 345 ? 0.6831 0.5104 0.4988 -0.0665 -0.1140 0.0403  345 PRO C O   
11029 C CB  . PRO C 345 ? 0.6558 0.4373 0.4738 -0.0742 -0.1121 0.0281  345 PRO C CB  
11030 C CG  . PRO C 345 ? 0.6603 0.4236 0.4733 -0.0762 -0.1090 0.0415  345 PRO C CG  
11031 C CD  . PRO C 345 ? 0.6910 0.4649 0.5048 -0.0909 -0.1046 0.0430  345 PRO C CD  
11032 N N   . VAL C 346 ? 0.6512 0.4947 0.4756 -0.0611 -0.1198 0.0246  346 VAL C N   
11033 C CA  . VAL C 346 ? 0.5681 0.4243 0.3926 -0.0495 -0.1225 0.0276  346 VAL C CA  
11034 C C   . VAL C 346 ? 0.6339 0.4807 0.4559 -0.0395 -0.1253 0.0253  346 VAL C C   
11035 O O   . VAL C 346 ? 0.5908 0.4401 0.4135 -0.0402 -0.1270 0.0177  346 VAL C O   
11036 C CB  . VAL C 346 ? 0.4900 0.3740 0.3232 -0.0497 -0.1241 0.0234  346 VAL C CB  
11037 C CG1 . VAL C 346 ? 0.4754 0.3691 0.3094 -0.0400 -0.1243 0.0273  346 VAL C CG1 
11038 C CG2 . VAL C 346 ? 0.5766 0.4718 0.4161 -0.0622 -0.1204 0.0221  346 VAL C CG2 
11039 N N   . VAL C 347 ? 0.6383 0.4760 0.4573 -0.0308 -0.1258 0.0316  347 VAL C N   
11040 C CA  . VAL C 347 ? 0.5615 0.3910 0.3805 -0.0212 -0.1273 0.0298  347 VAL C CA  
11041 C C   . VAL C 347 ? 0.5780 0.4225 0.3991 -0.0127 -0.1295 0.0312  347 VAL C C   
11042 O O   . VAL C 347 ? 0.6101 0.4590 0.4305 -0.0105 -0.1300 0.0367  347 VAL C O   
11043 C CB  . VAL C 347 ? 0.5107 0.3184 0.3286 -0.0174 -0.1265 0.0357  347 VAL C CB  
11044 C CG1 . VAL C 347 ? 0.5344 0.3381 0.3559 -0.0068 -0.1272 0.0335  347 VAL C CG1 
11045 C CG2 . VAL C 347 ? 0.5628 0.3517 0.3801 -0.0256 -0.1232 0.0336  347 VAL C CG2 
11046 N N   . PHE C 348 ? 0.5986 0.4504 0.4212 -0.0088 -0.1305 0.0260  348 PHE C N   
11047 C CA  . PHE C 348 ? 0.4597 0.3221 0.2851 -0.0009 -0.1318 0.0273  348 PHE C CA  
11048 C C   . PHE C 348 ? 0.4743 0.3265 0.3002 0.0065  -0.1309 0.0275  348 PHE C C   
11049 O O   . PHE C 348 ? 0.4685 0.3137 0.2925 0.0068  -0.1291 0.0227  348 PHE C O   
11050 C CB  . PHE C 348 ? 0.6168 0.4939 0.4436 -0.0010 -0.1334 0.0238  348 PHE C CB  
11051 C CG  . PHE C 348 ? 0.5518 0.4452 0.3847 -0.0021 -0.1343 0.0254  348 PHE C CG  
11052 C CD1 . PHE C 348 ? 0.4544 0.3533 0.2896 -0.0100 -0.1336 0.0248  348 PHE C CD1 
11053 C CD2 . PHE C 348 ? 0.4610 0.3639 0.2991 0.0047  -0.1349 0.0270  348 PHE C CD2 
11054 C CE1 . PHE C 348 ? 0.4375 0.3530 0.2808 -0.0105 -0.1330 0.0251  348 PHE C CE1 
11055 C CE2 . PHE C 348 ? 0.4868 0.4040 0.3332 0.0048  -0.1346 0.0273  348 PHE C CE2 
11056 C CZ  . PHE C 348 ? 0.5088 0.4333 0.3583 -0.0025 -0.1335 0.0260  348 PHE C CZ  
11057 N N   . VAL C 349 ? 0.5356 0.3883 0.3646 0.0118  -0.1319 0.0320  349 VAL C N   
11058 C CA  . VAL C 349 ? 0.5051 0.3527 0.3386 0.0190  -0.1314 0.0322  349 VAL C CA  
11059 C C   . VAL C 349 ? 0.4730 0.3325 0.3100 0.0229  -0.1313 0.0315  349 VAL C C   
11060 O O   . VAL C 349 ? 0.5013 0.3674 0.3408 0.0241  -0.1329 0.0340  349 VAL C O   
11061 C CB  . VAL C 349 ? 0.5016 0.3422 0.3377 0.0217  -0.1338 0.0382  349 VAL C CB  
11062 C CG1 . VAL C 349 ? 0.5275 0.3643 0.3724 0.0293  -0.1334 0.0377  349 VAL C CG1 
11063 C CG2 . VAL C 349 ? 0.5415 0.3688 0.3735 0.0169  -0.1338 0.0412  349 VAL C CG2 
11064 N N   . VAL C 350 ? 0.5009 0.3624 0.3371 0.0241  -0.1290 0.0280  350 VAL C N   
11065 C CA  . VAL C 350 ? 0.5224 0.3929 0.3612 0.0270  -0.1283 0.0286  350 VAL C CA  
11066 C C   . VAL C 350 ? 0.5249 0.3920 0.3671 0.0312  -0.1246 0.0273  350 VAL C C   
11067 O O   . VAL C 350 ? 0.4707 0.3318 0.3093 0.0309  -0.1215 0.0237  350 VAL C O   
11068 C CB  . VAL C 350 ? 0.4294 0.3071 0.2633 0.0245  -0.1291 0.0280  350 VAL C CB  
11069 C CG1 . VAL C 350 ? 0.5573 0.4410 0.3945 0.0284  -0.1281 0.0306  350 VAL C CG1 
11070 C CG2 . VAL C 350 ? 0.4263 0.3102 0.2606 0.0202  -0.1319 0.0286  350 VAL C CG2 
11071 N N   . LEU C 351 ? 0.5010 0.3725 0.3508 0.0344  -0.1241 0.0289  351 LEU C N   
11072 C CA  . LEU C 351 ? 0.4482 0.3184 0.3050 0.0378  -0.1203 0.0275  351 LEU C CA  
11073 C C   . LEU C 351 ? 0.5074 0.3838 0.3717 0.0390  -0.1194 0.0289  351 LEU C C   
11074 O O   . LEU C 351 ? 0.5187 0.3990 0.3850 0.0381  -0.1226 0.0299  351 LEU C O   
11075 C CB  . LEU C 351 ? 0.4836 0.3494 0.3477 0.0404  -0.1219 0.0273  351 LEU C CB  
11076 C CG  . LEU C 351 ? 0.5251 0.3913 0.4007 0.0446  -0.1177 0.0250  351 LEU C CG  
11077 C CD1 . LEU C 351 ? 0.5037 0.3670 0.3739 0.0438  -0.1101 0.0207  351 LEU C CD1 
11078 C CD2 . LEU C 351 ? 0.4994 0.3605 0.3833 0.0484  -0.1206 0.0260  351 LEU C CD2 
11079 N N   . ASP C 352 ? 0.5071 0.3840 0.3756 0.0401  -0.1140 0.0281  352 ASP C N   
11080 C CA  . ASP C 352 ? 0.4128 0.2939 0.2911 0.0403  -0.1121 0.0286  352 ASP C CA  
11081 C C   . ASP C 352 ? 0.4641 0.3498 0.3539 0.0412  -0.1161 0.0270  352 ASP C C   
11082 O O   . ASP C 352 ? 0.5515 0.4387 0.4497 0.0435  -0.1155 0.0255  352 ASP C O   
11083 C CB  . ASP C 352 ? 0.5589 0.4396 0.4396 0.0401  -0.1043 0.0284  352 ASP C CB  
11084 C CG  . ASP C 352 ? 0.8142 0.6913 0.6800 0.0388  -0.1012 0.0307  352 ASP C CG  
11085 O OD1 . ASP C 352 ? 0.8070 0.6831 0.6630 0.0382  -0.1059 0.0320  352 ASP C OD1 
11086 O OD2 . ASP C 352 ? 0.8512 0.7276 0.7147 0.0378  -0.0941 0.0311  352 ASP C OD2 
11087 N N   . GLY C 353 ? 0.4265 0.3157 0.3172 0.0395  -0.1204 0.0269  353 GLY C N   
11088 C CA  . GLY C 353 ? 0.4813 0.3759 0.3775 0.0394  -0.1263 0.0260  353 GLY C CA  
11089 C C   . GLY C 353 ? 0.5133 0.4159 0.4234 0.0384  -0.1266 0.0230  353 GLY C C   
11090 O O   . GLY C 353 ? 0.5246 0.4337 0.4365 0.0364  -0.1325 0.0216  353 GLY C O   
11091 N N   . GLU C 354 ? 0.4940 0.3974 0.4137 0.0387  -0.1203 0.0218  354 GLU C N   
11092 C CA  . GLU C 354 ? 0.4598 0.3726 0.3958 0.0366  -0.1203 0.0183  354 GLU C CA  
11093 C C   . GLU C 354 ? 0.4883 0.4059 0.4385 0.0389  -0.1153 0.0174  354 GLU C C   
11094 O O   . GLU C 354 ? 0.4627 0.3917 0.4297 0.0377  -0.1173 0.0144  354 GLU C O   
11095 C CB  . GLU C 354 ? 0.4023 0.3127 0.3402 0.0319  -0.1155 0.0158  354 GLU C CB  
11096 C CG  . GLU C 354 ? 0.4915 0.3944 0.4282 0.0317  -0.1059 0.0186  354 GLU C CG  
11097 C CD  . GLU C 354 ? 0.5276 0.4206 0.4501 0.0325  -0.1046 0.0225  354 GLU C CD  
11098 O OE1 . GLU C 354 ? 0.6894 0.5796 0.6001 0.0354  -0.1068 0.0253  354 GLU C OE1 
11099 O OE2 . GLU C 354 ? 0.5195 0.4076 0.4443 0.0304  -0.1014 0.0227  354 GLU C OE2 
11100 N N   . ASN C 355 ? 0.5206 0.4316 0.4656 0.0415  -0.1088 0.0188  355 ASN C N   
11101 C CA  . ASN C 355 ? 0.5129 0.4288 0.4714 0.0426  -0.1009 0.0165  355 ASN C CA  
11102 C C   . ASN C 355 ? 0.5514 0.4718 0.5211 0.0488  -0.1033 0.0153  355 ASN C C   
11103 O O   . ASN C 355 ? 0.6926 0.6198 0.6782 0.0506  -0.0966 0.0121  355 ASN C O   
11104 C CB  . ASN C 355 ? 0.5097 0.4168 0.4554 0.0412  -0.0907 0.0176  355 ASN C CB  
11105 C CG  . ASN C 355 ? 0.6528 0.5655 0.6109 0.0388  -0.0797 0.0153  355 ASN C CG  
11106 O OD1 . ASN C 355 ? 0.6412 0.5646 0.6190 0.0370  -0.0796 0.0127  355 ASN C OD1 
11107 N ND2 . ASN C 355 ? 0.5727 0.4796 0.5189 0.0378  -0.0703 0.0159  355 ASN C ND2 
11108 N N   . CYS C 356 ? 0.5160 0.4324 0.4792 0.0523  -0.1120 0.0181  356 CYS C N   
11109 C CA  . CYS C 356 ? 0.5025 0.4194 0.4767 0.0592  -0.1143 0.0184  356 CYS C CA  
11110 C C   . CYS C 356 ? 0.4833 0.4123 0.4731 0.0622  -0.1255 0.0212  356 CYS C C   
11111 O O   . CYS C 356 ? 0.5152 0.4479 0.5213 0.0693  -0.1275 0.0222  356 CYS C O   
11112 C CB  . CYS C 356 ? 0.5104 0.4122 0.4674 0.0611  -0.1157 0.0208  356 CYS C CB  
11113 S SG  . CYS C 356 ? 0.5305 0.4276 0.4691 0.0575  -0.1265 0.0265  356 CYS C SG  
11114 N N   . TRP C 357 ? 0.4104 0.3463 0.3961 0.0572  -0.1329 0.0222  357 TRP C N   
11115 C CA  . TRP C 357 ? 0.4126 0.3614 0.4087 0.0588  -0.1452 0.0251  357 TRP C CA  
11116 C C   . TRP C 357 ? 0.5528 0.5204 0.5769 0.0599  -0.1455 0.0215  357 TRP C C   
11117 O O   . TRP C 357 ? 0.5963 0.5775 0.6333 0.0629  -0.1568 0.0246  357 TRP C O   
11118 C CB  . TRP C 357 ? 0.4134 0.3639 0.3938 0.0517  -0.1520 0.0253  357 TRP C CB  
11119 C CG  . TRP C 357 ? 0.4501 0.3850 0.4060 0.0498  -0.1504 0.0278  357 TRP C CG  
11120 C CD1 . TRP C 357 ? 0.5747 0.5046 0.5171 0.0438  -0.1464 0.0248  357 TRP C CD1 
11121 C CD2 . TRP C 357 ? 0.4640 0.3869 0.4087 0.0537  -0.1523 0.0337  357 TRP C CD2 
11122 N NE1 . TRP C 357 ? 0.5132 0.4315 0.4377 0.0439  -0.1462 0.0282  357 TRP C NE1 
11123 C CE2 . TRP C 357 ? 0.4170 0.3305 0.3419 0.0490  -0.1496 0.0334  357 TRP C CE2 
11124 C CE3 . TRP C 357 ? 0.4354 0.3541 0.3870 0.0607  -0.1558 0.0390  357 TRP C CE3 
11125 C CZ2 . TRP C 357 ? 0.4455 0.3470 0.3568 0.0497  -0.1501 0.0378  357 TRP C CZ2 
11126 C CZ3 . TRP C 357 ? 0.4783 0.3818 0.4152 0.0615  -0.1559 0.0436  357 TRP C CZ3 
11127 C CH2 . TRP C 357 ? 0.6028 0.4986 0.5196 0.0553  -0.1531 0.0428  357 TRP C CH2 
11128 N N   . GLU C 358 ? 0.6159 0.5860 0.6500 0.0572  -0.1337 0.0157  358 GLU C N   
11129 C CA  . GLU C 358 ? 0.5381 0.5274 0.6014 0.0574  -0.1320 0.0115  358 GLU C CA  
11130 C C   . GLU C 358 ? 0.4398 0.4339 0.5242 0.0674  -0.1294 0.0121  358 GLU C C   
11131 O O   . GLU C 358 ? 0.4330 0.4460 0.5461 0.0689  -0.1285 0.0087  358 GLU C O   
11132 C CB  . GLU C 358 ? 0.5636 0.5527 0.6293 0.0495  -0.1187 0.0058  358 GLU C CB  
11133 C CG  . GLU C 358 ? 0.5752 0.5455 0.6214 0.0492  -0.1062 0.0063  358 GLU C CG  
11134 C CD  . GLU C 358 ? 0.6853 0.6498 0.7224 0.0403  -0.0979 0.0049  358 GLU C CD  
11135 O OE1 . GLU C 358 ? 0.6784 0.6506 0.7310 0.0360  -0.0886 0.0015  358 GLU C OE1 
11136 O OE2 . GLU C 358 ? 0.6922 0.6440 0.7079 0.0376  -0.1003 0.0075  358 GLU C OE2 
11137 N N   . TYR C 359 ? 0.4686 0.4463 0.5414 0.0739  -0.1275 0.0153  359 TYR C N   
11138 C CA  . TYR C 359 ? 0.4915 0.4703 0.5845 0.0843  -0.1244 0.0150  359 TYR C CA  
11139 C C   . TYR C 359 ? 0.4503 0.4263 0.5461 0.0929  -0.1382 0.0236  359 TYR C C   
11140 O O   . TYR C 359 ? 0.4379 0.4175 0.5571 0.1031  -0.1383 0.0246  359 TYR C O   
11141 C CB  . TYR C 359 ? 0.4404 0.4012 0.5204 0.0850  -0.1094 0.0104  359 TYR C CB  
11142 C CG  . TYR C 359 ? 0.4250 0.3892 0.5034 0.0776  -0.0948 0.0035  359 TYR C CG  
11143 C CD1 . TYR C 359 ? 0.5157 0.4708 0.5685 0.0685  -0.0922 0.0042  359 TYR C CD1 
11144 C CD2 . TYR C 359 ? 0.4566 0.4333 0.5599 0.0798  -0.0833 -0.0030 359 TYR C CD2 
11145 C CE1 . TYR C 359 ? 0.5758 0.5324 0.6260 0.0617  -0.0793 0.0004  359 TYR C CE1 
11146 C CE2 . TYR C 359 ? 0.4435 0.4227 0.5434 0.0719  -0.0692 -0.0080 359 TYR C CE2 
11147 C CZ  . TYR C 359 ? 0.5245 0.4926 0.5968 0.0628  -0.0677 -0.0054 359 TYR C CZ  
11148 O OH  . TYR C 359 ? 0.4306 0.3994 0.4983 0.0550  -0.0540 -0.0080 359 TYR C OH  
11149 N N   . TYR C 360 ? 0.4783 0.4473 0.5513 0.0891  -0.1491 0.0302  360 TYR C N   
11150 C CA  . TYR C 360 ? 0.4610 0.4291 0.5346 0.0955  -0.1635 0.0405  360 TYR C CA  
11151 C C   . TYR C 360 ? 0.4558 0.4499 0.5521 0.0974  -0.1766 0.0435  360 TYR C C   
11152 O O   . TYR C 360 ? 0.5063 0.5177 0.6109 0.0903  -0.1760 0.0370  360 TYR C O   
11153 C CB  . TYR C 360 ? 0.5200 0.4749 0.5606 0.0890  -0.1698 0.0461  360 TYR C CB  
11154 C CG  . TYR C 360 ? 0.5079 0.4381 0.5275 0.0883  -0.1617 0.0462  360 TYR C CG  
11155 C CD1 . TYR C 360 ? 0.4402 0.3622 0.4529 0.0845  -0.1477 0.0377  360 TYR C CD1 
11156 C CD2 . TYR C 360 ? 0.4612 0.3770 0.4664 0.0902  -0.1684 0.0553  360 TYR C CD2 
11157 C CE1 . TYR C 360 ? 0.4446 0.3468 0.4382 0.0829  -0.1416 0.0370  360 TYR C CE1 
11158 C CE2 . TYR C 360 ? 0.4625 0.3572 0.4500 0.0880  -0.1611 0.0544  360 TYR C CE2 
11159 C CZ  . TYR C 360 ? 0.4551 0.3440 0.4372 0.0843  -0.1482 0.0447  360 TYR C CZ  
11160 O OH  . TYR C 360 ? 0.4602 0.3307 0.4251 0.0813  -0.1422 0.0430  360 TYR C OH  
11161 N N   . GLU C 361 ? 0.4541 0.4508 0.5607 0.1066  -0.1890 0.0538  361 GLU C N   
11162 C CA  . GLU C 361 ? 0.5411 0.5638 0.6651 0.1080  -0.2053 0.0587  361 GLU C CA  
11163 C C   . GLU C 361 ? 0.5489 0.5759 0.6449 0.0964  -0.2154 0.0606  361 GLU C C   
11164 O O   . GLU C 361 ? 0.5589 0.5681 0.6253 0.0935  -0.2176 0.0666  361 GLU C O   
11165 C CB  . GLU C 361 ? 0.7106 0.7335 0.8509 0.1217  -0.2171 0.0718  361 GLU C CB  
11166 C CG  . GLU C 361 ? 0.7368 0.7894 0.9182 0.1299  -0.2258 0.0727  361 GLU C CG  
11167 C CD  . GLU C 361 ? 0.6888 0.7468 0.9020 0.1351  -0.2092 0.0612  361 GLU C CD  
11168 O OE1 . GLU C 361 ? 0.7572 0.7962 0.9772 0.1444  -0.1988 0.0610  361 GLU C OE1 
11169 O OE2 . GLU C 361 ? 0.6214 0.7023 0.8525 0.1290  -0.2057 0.0516  361 GLU C OE2 
11170 N N   . GLU C 362 ? 0.4813 0.5321 0.5875 0.0889  -0.2204 0.0541  362 GLU C N   
11171 C CA  . GLU C 362 ? 0.4547 0.5126 0.5376 0.0772  -0.2296 0.0529  362 GLU C CA  
11172 C C   . GLU C 362 ? 0.4481 0.4841 0.4992 0.0683  -0.2182 0.0475  362 GLU C C   
11173 O O   . GLU C 362 ? 0.4842 0.5120 0.5074 0.0636  -0.2236 0.0519  362 GLU C O   
11174 C CB  . GLU C 362 ? 0.5533 0.6166 0.6248 0.0804  -0.2486 0.0665  362 GLU C CB  
11175 C CG  . GLU C 362 ? 0.6748 0.7690 0.7734 0.0844  -0.2653 0.0705  362 GLU C CG  
11176 C CD  . GLU C 362 ? 0.8786 0.9733 1.0042 0.1011  -0.2702 0.0820  362 GLU C CD  
11177 O OE1 . GLU C 362 ? 0.8775 0.9484 0.9888 0.1082  -0.2694 0.0929  362 GLU C OE1 
11178 O OE2 . GLU C 362 ? 0.8168 0.9355 0.9795 0.1071  -0.2745 0.0800  362 GLU C OE2 
11179 N N   . ASN C 363 ? 0.5271 0.5548 0.5832 0.0661  -0.2020 0.0385  363 ASN C N   
11180 C CA  . ASN C 363 ? 0.4973 0.5076 0.5287 0.0581  -0.1912 0.0330  363 ASN C CA  
11181 C C   . ASN C 363 ? 0.4687 0.4567 0.4753 0.0609  -0.1896 0.0401  363 ASN C C   
11182 O O   . ASN C 363 ? 0.4643 0.4404 0.4488 0.0546  -0.1843 0.0374  363 ASN C O   
11183 C CB  . ASN C 363 ? 0.6003 0.6199 0.6203 0.0465  -0.1958 0.0266  363 ASN C CB  
11184 C CG  . ASN C 363 ? 0.5706 0.5744 0.5730 0.0394  -0.1836 0.0199  363 ASN C CG  
11185 O OD1 . ASN C 363 ? 0.4509 0.4416 0.4540 0.0418  -0.1714 0.0189  363 ASN C OD1 
11186 N ND2 . ASN C 363 ? 0.6327 0.6383 0.6193 0.0307  -0.1869 0.0153  363 ASN C ND2 
11187 N N   . GLY C 364 ? 0.4420 0.4237 0.4536 0.0703  -0.1938 0.0490  364 GLY C N   
11188 C CA  . GLY C 364 ? 0.5052 0.4664 0.4940 0.0714  -0.1933 0.0559  364 GLY C CA  
11189 C C   . GLY C 364 ? 0.5609 0.5236 0.5267 0.0656  -0.2040 0.0622  364 GLY C C   
11190 O O   . GLY C 364 ? 0.5412 0.4876 0.4865 0.0643  -0.2026 0.0677  364 GLY C O   
11191 N N   . ILE C 365 ? 0.5635 0.5460 0.5314 0.0609  -0.2140 0.0608  365 ILE C N   
11192 C CA  . ILE C 365 ? 0.5632 0.5490 0.5069 0.0546  -0.2242 0.0663  365 ILE C CA  
11193 C C   . ILE C 365 ? 0.6184 0.5957 0.5548 0.0612  -0.2333 0.0822  365 ILE C C   
11194 O O   . ILE C 365 ? 0.5905 0.5564 0.5005 0.0563  -0.2335 0.0877  365 ILE C O   
11195 C CB  . ILE C 365 ? 0.5304 0.5409 0.4791 0.0480  -0.2340 0.0605  365 ILE C CB  
11196 C CG1 . ILE C 365 ? 0.4643 0.4771 0.4161 0.0398  -0.2230 0.0449  365 ILE C CG1 
11197 C CG2 . ILE C 365 ? 0.5477 0.5636 0.4696 0.0414  -0.2455 0.0666  365 ILE C CG2 
11198 C CD1 . ILE C 365 ? 0.4652 0.5018 0.4319 0.0338  -0.2300 0.0366  365 ILE C CD1 
11199 N N   . PRO C 366 ? 0.5338 0.5154 0.4929 0.0721  -0.2405 0.0906  366 PRO C N   
11200 C CA  . PRO C 366 ? 0.5644 0.5322 0.5165 0.0790  -0.2476 0.1071  366 PRO C CA  
11201 C C   . PRO C 366 ? 0.5625 0.5019 0.5022 0.0795  -0.2350 0.1083  366 PRO C C   
11202 O O   . PRO C 366 ? 0.5386 0.4642 0.4585 0.0778  -0.2380 0.1195  366 PRO C O   
11203 C CB  . PRO C 366 ? 0.5263 0.5042 0.5130 0.0924  -0.2549 0.1130  366 PRO C CB  
11204 C CG  . PRO C 366 ? 0.5112 0.5000 0.5220 0.0926  -0.2446 0.0975  366 PRO C CG  
11205 C CD  . PRO C 366 ? 0.4941 0.4937 0.4878 0.0789  -0.2428 0.0865  366 PRO C CD  
11206 N N   . PHE C 367 ? 0.5045 0.4354 0.4544 0.0805  -0.2207 0.0969  367 PHE C N   
11207 C CA  . PHE C 367 ? 0.5060 0.4118 0.4455 0.0805  -0.2099 0.0969  367 PHE C CA  
11208 C C   . PHE C 367 ? 0.5049 0.4040 0.4144 0.0690  -0.2061 0.0952  367 PHE C C   
11209 O O   . PHE C 367 ? 0.5400 0.4223 0.4342 0.0669  -0.2049 0.1027  367 PHE C O   
11210 C CB  . PHE C 367 ? 0.4909 0.3919 0.4464 0.0835  -0.1963 0.0848  367 PHE C CB  
11211 C CG  . PHE C 367 ? 0.4895 0.3696 0.4296 0.0794  -0.1849 0.0808  367 PHE C CG  
11212 C CD1 . PHE C 367 ? 0.5052 0.3645 0.4440 0.0835  -0.1833 0.0872  367 PHE C CD1 
11213 C CD2 . PHE C 367 ? 0.4745 0.3559 0.4026 0.0714  -0.1765 0.0708  367 PHE C CD2 
11214 C CE1 . PHE C 367 ? 0.5052 0.3472 0.4307 0.0782  -0.1736 0.0824  367 PHE C CE1 
11215 C CE2 . PHE C 367 ? 0.4742 0.3396 0.3894 0.0674  -0.1678 0.0674  367 PHE C CE2 
11216 C CZ  . PHE C 367 ? 0.4892 0.3358 0.4028 0.0702  -0.1664 0.0725  367 PHE C CZ  
11217 N N   . LEU C 368 ? 0.5005 0.4124 0.4033 0.0612  -0.2034 0.0851  368 LEU C N   
11218 C CA  . LEU C 368 ? 0.5219 0.4289 0.4004 0.0513  -0.1982 0.0818  368 LEU C CA  
11219 C C   . LEU C 368 ? 0.6041 0.5138 0.4615 0.0460  -0.2073 0.0916  368 LEU C C   
11220 O O   . LEU C 368 ? 0.6177 0.5162 0.4562 0.0404  -0.2032 0.0951  368 LEU C O   
11221 C CB  . LEU C 368 ? 0.4724 0.3907 0.3522 0.0457  -0.1925 0.0685  368 LEU C CB  
11222 C CG  . LEU C 368 ? 0.4569 0.3672 0.3456 0.0474  -0.1804 0.0602  368 LEU C CG  
11223 C CD1 . LEU C 368 ? 0.4437 0.3647 0.3382 0.0435  -0.1759 0.0495  368 LEU C CD1 
11224 C CD2 . LEU C 368 ? 0.4579 0.3532 0.3311 0.0439  -0.1735 0.0608  368 LEU C CD2 
11225 N N   . GLU C 369 ? 0.6288 0.5547 0.4888 0.0469  -0.2195 0.0961  369 GLU C N   
11226 C CA  . GLU C 369 ? 0.5392 0.4697 0.3776 0.0413  -0.2270 0.1060  369 GLU C CA  
11227 C C   . GLU C 369 ? 0.5576 0.4717 0.3930 0.0457  -0.2264 0.1209  369 GLU C C   
11228 O O   . GLU C 369 ? 0.5733 0.4816 0.3867 0.0388  -0.2240 0.1275  369 GLU C O   
11229 C CB  . GLU C 369 ? 0.5831 0.5381 0.4285 0.0413  -0.2377 0.1063  369 GLU C CB  
11230 C CG  . GLU C 369 ? 0.6044 0.5749 0.4461 0.0330  -0.2387 0.0914  369 GLU C CG  
11231 C CD  . GLU C 369 ? 0.7643 0.7594 0.6046 0.0292  -0.2493 0.0914  369 GLU C CD  
11232 O OE1 . GLU C 369 ? 0.7990 0.8048 0.6578 0.0370  -0.2579 0.0992  369 GLU C OE1 
11233 O OE2 . GLU C 369 ? 0.8191 0.8235 0.6402 0.0184  -0.2490 0.0829  369 GLU C OE2 
11234 N N   . LYS C 370 ? 0.5925 0.4979 0.4505 0.0570  -0.2283 0.1262  370 LYS C N   
11235 C CA  . LYS C 370 ? 0.6279 0.5131 0.4853 0.0617  -0.2269 0.1395  370 LYS C CA  
11236 C C   . LYS C 370 ? 0.6287 0.4910 0.4708 0.0558  -0.2174 0.1374  370 LYS C C   
11237 O O   . LYS C 370 ? 0.7179 0.5670 0.5446 0.0514  -0.2155 0.1475  370 LYS C O   
11238 C CB  . LYS C 370 ? 0.5783 0.4579 0.4660 0.0758  -0.2297 0.1429  370 LYS C CB  
11239 C CG  . LYS C 370 ? 0.6053 0.4708 0.4972 0.0827  -0.2320 0.1591  370 LYS C CG  
11240 C CD  . LYS C 370 ? 0.7812 0.6682 0.6815 0.0880  -0.2429 0.1688  370 LYS C CD  
11241 C CE  . LYS C 370 ? 0.7659 0.6712 0.6976 0.0975  -0.2480 0.1617  370 LYS C CE  
11242 N NZ  . LYS C 370 ? 0.7696 0.7056 0.7020 0.0959  -0.2592 0.1636  370 LYS C NZ  
11243 N N   . LEU C 371 ? 0.5538 0.4136 0.4016 0.0547  -0.2091 0.1234  371 LEU C N   
11244 C CA  . LEU C 371 ? 0.5505 0.3942 0.3882 0.0485  -0.1973 0.1186  371 LEU C CA  
11245 C C   . LEU C 371 ? 0.5770 0.4256 0.3895 0.0363  -0.1951 0.1183  371 LEU C C   
11246 O O   . LEU C 371 ? 0.6493 0.4842 0.4480 0.0304  -0.1912 0.1244  371 LEU C O   
11247 C CB  . LEU C 371 ? 0.5267 0.3719 0.3782 0.0501  -0.1873 0.1030  371 LEU C CB  
11248 C CG  . LEU C 371 ? 0.5192 0.3559 0.3601 0.0423  -0.1765 0.0953  371 LEU C CG  
11249 C CD1 . LEU C 371 ? 0.6024 0.4164 0.4439 0.0428  -0.1724 0.1000  371 LEU C CD1 
11250 C CD2 . LEU C 371 ? 0.4968 0.3412 0.3473 0.0431  -0.1694 0.0813  371 LEU C CD2 
11251 N N   . TYR C 372 ? 0.5429 0.4109 0.3500 0.0320  -0.1966 0.1103  372 TYR C N   
11252 C CA  . TYR C 372 ? 0.5518 0.4257 0.3374 0.0208  -0.1921 0.1066  372 TYR C CA  
11253 C C   . TYR C 372 ? 0.6537 0.5246 0.4172 0.0152  -0.1980 0.1210  372 TYR C C   
11254 O O   . TYR C 372 ? 0.7747 0.6402 0.5214 0.0063  -0.1912 0.1224  372 TYR C O   
11255 C CB  . TYR C 372 ? 0.5311 0.4245 0.3175 0.0179  -0.1921 0.0941  372 TYR C CB  
11256 C CG  . TYR C 372 ? 0.5062 0.4008 0.3088 0.0205  -0.1835 0.0805  372 TYR C CG  
11257 C CD1 . TYR C 372 ? 0.4980 0.3795 0.3070 0.0223  -0.1755 0.0786  372 TYR C CD1 
11258 C CD2 . TYR C 372 ? 0.4944 0.4029 0.3049 0.0202  -0.1835 0.0698  372 TYR C CD2 
11259 C CE1 . TYR C 372 ? 0.4788 0.3619 0.2995 0.0243  -0.1686 0.0679  372 TYR C CE1 
11260 C CE2 . TYR C 372 ? 0.5491 0.4571 0.3729 0.0224  -0.1756 0.0596  372 TYR C CE2 
11261 C CZ  . TYR C 372 ? 0.5029 0.3987 0.3309 0.0247  -0.1686 0.0595  372 TYR C CZ  
11262 O OH  . TYR C 372 ? 0.4515 0.3474 0.2901 0.0266  -0.1617 0.0511  372 TYR C OH  
11263 N N   . SER C 373 ? 0.5871 0.4655 0.3543 0.0200  -0.2071 0.1304  373 SER C N   
11264 C CA  . SER C 373 ? 0.6155 0.4932 0.3650 0.0154  -0.2093 0.1442  373 SER C CA  
11265 C C   . SER C 373 ? 0.7066 0.5586 0.4543 0.0163  -0.2060 0.1567  373 SER C C   
11266 O O   . SER C 373 ? 0.8976 0.7434 0.6252 0.0086  -0.2038 0.1668  373 SER C O   
11267 C CB  . SER C 373 ? 0.6277 0.5215 0.3847 0.0217  -0.2196 0.1512  373 SER C CB  
11268 O OG  . SER C 373 ? 0.7523 0.6422 0.5370 0.0343  -0.2241 0.1534  373 SER C OG  
11269 N N   . THR C 374 ? 0.6225 0.4586 0.3904 0.0249  -0.2051 0.1559  374 THR C N   
11270 C CA  . THR C 374 ? 0.6396 0.4480 0.4066 0.0249  -0.2015 0.1659  374 THR C CA  
11271 C C   . THR C 374 ? 0.6759 0.4757 0.4288 0.0133  -0.1910 0.1593  374 THR C C   
11272 O O   . THR C 374 ? 0.7048 0.4896 0.4439 0.0058  -0.1872 0.1693  374 THR C O   
11273 C CB  . THR C 374 ? 0.6330 0.4271 0.4262 0.0373  -0.2024 0.1642  374 THR C CB  
11274 O OG1 . THR C 374 ? 0.7674 0.5781 0.5793 0.0479  -0.2099 0.1654  374 THR C OG1 
11275 C CG2 . THR C 374 ? 0.6812 0.4459 0.4762 0.0389  -0.2001 0.1766  374 THR C CG2 
11276 N N   . LEU C 375 ? 0.7307 0.5427 0.4907 0.0114  -0.1837 0.1414  375 LEU C N   
11277 C CA  . LEU C 375 ? 0.7416 0.5539 0.4933 0.0007  -0.1723 0.1328  375 LEU C CA  
11278 C C   . LEU C 375 ? 0.7432 0.5644 0.4704 -0.0105 -0.1711 0.1379  375 LEU C C   
11279 O O   . LEU C 375 ? 0.6608 0.4771 0.3788 -0.0205 -0.1624 0.1378  375 LEU C O   
11280 C CB  . LEU C 375 ? 0.7089 0.5355 0.4725 0.0022  -0.1670 0.1148  375 LEU C CB  
11281 C CG  . LEU C 375 ? 0.6684 0.4864 0.4493 0.0062  -0.1611 0.1054  375 LEU C CG  
11282 C CD1 . LEU C 375 ? 0.5613 0.3639 0.3559 0.0159  -0.1652 0.1111  375 LEU C CD1 
11283 C CD2 . LEU C 375 ? 0.5269 0.3612 0.3168 0.0088  -0.1586 0.0914  375 LEU C CD2 
11284 N N   . GLU C 376 ? 0.7392 0.5747 0.4556 -0.0099 -0.1794 0.1415  376 GLU C N   
11285 C CA  . GLU C 376 ? 0.7931 0.6386 0.4832 -0.0211 -0.1780 0.1451  376 GLU C CA  
11286 C C   . GLU C 376 ? 0.8991 0.7276 0.5718 -0.0275 -0.1779 0.1637  376 GLU C C   
11287 O O   . GLU C 376 ? 0.9871 0.8169 0.6420 -0.0397 -0.1692 0.1645  376 GLU C O   
11288 C CB  . GLU C 376 ? 0.8296 0.6940 0.5127 -0.0189 -0.1881 0.1445  376 GLU C CB  
11289 C CG  . GLU C 376 ? 0.9538 0.8374 0.6213 -0.0284 -0.1830 0.1317  376 GLU C CG  
11290 C CD  . GLU C 376 ? 0.9201 0.8234 0.5847 -0.0266 -0.1910 0.1287  376 GLU C CD  
11291 O OE1 . GLU C 376 ? 0.9209 0.8259 0.5998 -0.0172 -0.1996 0.1362  376 GLU C OE1 
11292 O OE2 . GLU C 376 ? 0.9799 0.8981 0.6297 -0.0348 -0.1879 0.1177  376 GLU C OE2 
11293 N N   . LYS C 377 ? 0.7823 0.5957 0.4632 -0.0191 -0.1856 0.1781  377 LYS C N   
11294 C CA  . LYS C 377 ? 0.7229 0.5199 0.3921 -0.0232 -0.1845 0.1964  377 LYS C CA  
11295 C C   . LYS C 377 ? 0.8297 0.5973 0.5040 -0.0262 -0.1785 0.2013  377 LYS C C   
11296 O O   . LYS C 377 ? 0.8457 0.5948 0.5124 -0.0299 -0.1768 0.2171  377 LYS C O   
11297 C CB  . LYS C 377 ? 0.7508 0.5499 0.4308 -0.0112 -0.1938 0.2083  377 LYS C CB  
11298 C CG  . LYS C 377 ? 0.7940 0.6225 0.4694 -0.0088 -0.2008 0.2036  377 LYS C CG  
11299 C CD  . LYS C 377 ? 0.8710 0.7054 0.5700 0.0065  -0.2111 0.2074  377 LYS C CD  
11300 C CE  . LYS C 377 ? 0.7688 0.6328 0.4633 0.0074  -0.2188 0.2019  377 LYS C CE  
11301 N NZ  . LYS C 377 ? 0.7078 0.5878 0.4076 0.0046  -0.2165 0.1815  377 LYS C NZ  
11302 N N   . GLU C 378 ? 0.9257 0.6943 0.6201 -0.0243 -0.1707 0.1836  378 GLU C N   
11303 C CA  . GLU C 378 ? 0.9011 0.6486 0.6066 -0.0277 -0.1615 0.1814  378 GLU C CA  
11304 C C   . GLU C 378 ? 0.9102 0.6653 0.6051 -0.0431 -0.1492 0.1737  378 GLU C C   
11305 O O   . GLU C 378 ? 0.8124 0.5878 0.5122 -0.0450 -0.1444 0.1571  378 GLU C O   
11306 C CB  . GLU C 378 ? 0.8008 0.5464 0.5324 -0.0176 -0.1606 0.1667  378 GLU C CB  
11307 C CG  . GLU C 378 ? 0.7234 0.4403 0.4689 -0.0142 -0.1582 0.1709  378 GLU C CG  
11308 C CD  . GLU C 378 ? 0.9735 0.6757 0.7259 -0.0016 -0.1684 0.1865  378 GLU C CD  
11309 O OE1 . GLU C 378 ? 0.9812 0.6985 0.7412 0.0091  -0.1772 0.1852  378 GLU C OE1 
11310 O OE2 . GLU C 378 ? 1.0308 0.7064 0.7827 -0.0025 -0.1676 0.2002  378 GLU C OE2 
11311 N N   . GLU C 379 ? 0.9597 0.6986 0.6416 -0.0539 -0.1439 0.1863  379 GLU C N   
11312 C CA  . GLU C 379 ? 0.9397 0.6883 0.6115 -0.0696 -0.1317 0.1807  379 GLU C CA  
11313 C C   . GLU C 379 ? 0.9412 0.6896 0.6331 -0.0733 -0.1228 0.1643  379 GLU C C   
11314 O O   . GLU C 379 ? 0.9488 0.7171 0.6418 -0.0813 -0.1147 0.1520  379 GLU C O   
11315 C CB  . GLU C 379 ? 0.9444 0.6755 0.5957 -0.0813 -0.1280 0.2004  379 GLU C CB  
11316 C CG  . GLU C 379 ? 1.2486 0.9454 0.9071 -0.0769 -0.1316 0.2155  379 GLU C CG  
11317 C CD  . GLU C 379 ? 1.4202 1.1085 1.0715 -0.0647 -0.1459 0.2337  379 GLU C CD  
11318 O OE1 . GLU C 379 ? 1.4595 1.1409 1.0873 -0.0705 -0.1487 0.2538  379 GLU C OE1 
11319 O OE2 . GLU C 379 ? 1.3429 1.0326 1.0124 -0.0495 -0.1545 0.2283  379 GLU C OE2 
11320 N N   . TRP C 380 ? 0.8533 0.5808 0.5618 -0.0677 -0.1241 0.1633  380 TRP C N   
11321 C CA  . TRP C 380 ? 0.7739 0.5015 0.4993 -0.0725 -0.1168 0.1478  380 TRP C CA  
11322 C C   . TRP C 380 ? 0.7022 0.4513 0.4415 -0.0639 -0.1190 0.1299  380 TRP C C   
11323 O O   . TRP C 380 ? 0.7015 0.4579 0.4524 -0.0686 -0.1138 0.1165  380 TRP C O   
11324 C CB  . TRP C 380 ? 0.7915 0.4880 0.5282 -0.0709 -0.1163 0.1512  380 TRP C CB  
11325 C CG  . TRP C 380 ? 0.7172 0.3996 0.4611 -0.0547 -0.1255 0.1573  380 TRP C CG  
11326 C CD1 . TRP C 380 ? 0.7829 0.4535 0.5183 -0.0479 -0.1332 0.1761  380 TRP C CD1 
11327 C CD2 . TRP C 380 ? 0.7079 0.3884 0.4705 -0.0433 -0.1280 0.1448  380 TRP C CD2 
11328 N NE1 . TRP C 380 ? 0.8438 0.5061 0.5945 -0.0322 -0.1402 0.1755  380 TRP C NE1 
11329 C CE2 . TRP C 380 ? 0.7820 0.4499 0.5490 -0.0295 -0.1362 0.1559  380 TRP C CE2 
11330 C CE3 . TRP C 380 ? 0.6760 0.3653 0.4513 -0.0436 -0.1241 0.1256  380 TRP C CE3 
11331 C CZ2 . TRP C 380 ? 0.6971 0.3612 0.4823 -0.0165 -0.1389 0.1473  380 TRP C CZ2 
11332 C CZ3 . TRP C 380 ? 0.7562 0.4406 0.5457 -0.0314 -0.1269 0.1177  380 TRP C CZ3 
11333 C CH2 . TRP C 380 ? 0.6751 0.3471 0.4701 -0.0181 -0.1334 0.1279  380 TRP C CH2 
11334 N N   . ILE C 381 ? 0.7454 0.5050 0.4841 -0.0522 -0.1269 0.1299  381 ILE C N   
11335 C CA  . ILE C 381 ? 0.6906 0.4694 0.4412 -0.0445 -0.1285 0.1147  381 ILE C CA  
11336 C C   . ILE C 381 ? 0.6822 0.4861 0.4241 -0.0483 -0.1263 0.1099  381 ILE C C   
11337 O O   . ILE C 381 ? 0.7618 0.5703 0.4888 -0.0487 -0.1295 0.1182  381 ILE C O   
11338 C CB  . ILE C 381 ? 0.6164 0.3910 0.3750 -0.0298 -0.1372 0.1159  381 ILE C CB  
11339 C CG1 . ILE C 381 ? 0.6761 0.4232 0.4420 -0.0254 -0.1388 0.1233  381 ILE C CG1 
11340 C CG2 . ILE C 381 ? 0.5753 0.3649 0.3473 -0.0233 -0.1370 0.1005  381 ILE C CG2 
11341 C CD1 . ILE C 381 ? 0.6164 0.3609 0.3955 -0.0107 -0.1455 0.1223  381 ILE C CD1 
11342 N N   . GLU C 382 ? 0.5813 0.4018 0.3328 -0.0512 -0.1209 0.0964  382 GLU C N   
11343 C CA  . GLU C 382 ? 0.5895 0.4337 0.3383 -0.0528 -0.1177 0.0890  382 GLU C CA  
11344 C C   . GLU C 382 ? 0.5994 0.4549 0.3631 -0.0428 -0.1204 0.0771  382 GLU C C   
11345 O O   . GLU C 382 ? 0.6712 0.5306 0.4480 -0.0430 -0.1182 0.0690  382 GLU C O   
11346 C CB  . GLU C 382 ? 0.6988 0.5540 0.4477 -0.0652 -0.1077 0.0848  382 GLU C CB  
11347 C CG  . GLU C 382 ? 0.8348 0.7138 0.5823 -0.0667 -0.1025 0.0765  382 GLU C CG  
11348 C CD  . GLU C 382 ? 0.8969 0.7895 0.6489 -0.0783 -0.0917 0.0715  382 GLU C CD  
11349 O OE1 . GLU C 382 ? 0.6942 0.5766 0.4441 -0.0881 -0.0878 0.0775  382 GLU C OE1 
11350 O OE2 . GLU C 382 ? 0.9864 0.8997 0.7459 -0.0776 -0.0864 0.0612  382 GLU C OE2 
11351 N N   . THR C 383 ? 0.5545 0.4156 0.3160 -0.0350 -0.1256 0.0765  383 THR C N   
11352 C CA  . THR C 383 ? 0.5482 0.4200 0.3228 -0.0268 -0.1270 0.0661  383 THR C CA  
11353 C C   . THR C 383 ? 0.5096 0.3999 0.2895 -0.0304 -0.1201 0.0565  383 THR C C   
11354 O O   . THR C 383 ? 0.6121 0.5108 0.3827 -0.0374 -0.1150 0.0564  383 THR C O   
11355 C CB  . THR C 383 ? 0.5215 0.3954 0.2937 -0.0192 -0.1335 0.0672  383 THR C CB  
11356 O OG1 . THR C 383 ? 0.5732 0.4537 0.3295 -0.0246 -0.1335 0.0708  383 THR C OG1 
11357 C CG2 . THR C 383 ? 0.5132 0.3715 0.2880 -0.0126 -0.1405 0.0749  383 THR C CG2 
11358 N N   . LEU C 384 ? 0.4821 0.3789 0.2770 -0.0256 -0.1196 0.0486  384 LEU C N   
11359 C CA  . LEU C 384 ? 0.5276 0.4419 0.3324 -0.0271 -0.1138 0.0403  384 LEU C CA  
11360 C C   . LEU C 384 ? 0.5257 0.4467 0.3407 -0.0176 -0.1155 0.0338  384 LEU C C   
11361 O O   . LEU C 384 ? 0.4819 0.3949 0.2990 -0.0108 -0.1208 0.0351  384 LEU C O   
11362 C CB  . LEU C 384 ? 0.4969 0.4150 0.3123 -0.0313 -0.1118 0.0380  384 LEU C CB  
11363 C CG  . LEU C 384 ? 0.5546 0.4666 0.3635 -0.0426 -0.1083 0.0429  384 LEU C CG  
11364 C CD1 . LEU C 384 ? 0.4824 0.3981 0.3037 -0.0464 -0.1084 0.0390  384 LEU C CD1 
11365 C CD2 . LEU C 384 ? 0.6002 0.5237 0.4034 -0.0508 -0.1003 0.0426  384 LEU C CD2 
11366 N N   . THR C 385 ? 0.5295 0.4649 0.3519 -0.0176 -0.1099 0.0268  385 THR C N   
11367 C CA  . THR C 385 ? 0.4824 0.4236 0.3186 -0.0090 -0.1103 0.0210  385 THR C CA  
11368 C C   . THR C 385 ? 0.4781 0.4251 0.3287 -0.0064 -0.1116 0.0204  385 THR C C   
11369 O O   . THR C 385 ? 0.5288 0.4777 0.3799 -0.0123 -0.1115 0.0222  385 THR C O   
11370 C CB  . THR C 385 ? 0.4410 0.3935 0.2811 -0.0091 -0.1032 0.0131  385 THR C CB  
11371 O OG1 . THR C 385 ? 0.4951 0.4613 0.3455 -0.0128 -0.0967 0.0094  385 THR C OG1 
11372 C CG2 . THR C 385 ? 0.4548 0.4046 0.2766 -0.0149 -0.1019 0.0133  385 THR C CG2 
11373 N N   . LEU C 386 ? 0.5068 0.4565 0.3690 0.0020  -0.1131 0.0181  386 LEU C N   
11374 C CA  . LEU C 386 ? 0.5028 0.4602 0.3776 0.0050  -0.1158 0.0186  386 LEU C CA  
11375 C C   . LEU C 386 ? 0.5573 0.5327 0.4456 0.0020  -0.1111 0.0147  386 LEU C C   
11376 O O   . LEU C 386 ? 0.5774 0.5616 0.4730 -0.0006 -0.1138 0.0156  386 LEU C O   
11377 C CB  . LEU C 386 ? 0.5309 0.4861 0.4137 0.0147  -0.1185 0.0191  386 LEU C CB  
11378 C CG  . LEU C 386 ? 0.4592 0.3992 0.3318 0.0174  -0.1222 0.0224  386 LEU C CG  
11379 C CD1 . LEU C 386 ? 0.4465 0.3846 0.3273 0.0256  -0.1231 0.0235  386 LEU C CD1 
11380 C CD2 . LEU C 386 ? 0.4702 0.4032 0.3338 0.0138  -0.1265 0.0258  386 LEU C CD2 
11381 N N   . GLU C 387 ? 0.5427 0.5249 0.4350 0.0018  -0.1037 0.0093  387 GLU C N   
11382 C CA  . GLU C 387 ? 0.4869 0.4875 0.3932 -0.0017 -0.0971 0.0046  387 GLU C CA  
11383 C C   . GLU C 387 ? 0.4862 0.4889 0.3835 -0.0137 -0.0952 0.0066  387 GLU C C   
11384 O O   . GLU C 387 ? 0.4810 0.4972 0.3909 -0.0176 -0.0951 0.0060  387 GLU C O   
11385 C CB  . GLU C 387 ? 0.4551 0.4610 0.3652 -0.0003 -0.0877 -0.0034 387 GLU C CB  
11386 C CG  . GLU C 387 ? 0.5784 0.6045 0.5142 0.0034  -0.0812 -0.0097 387 GLU C CG  
11387 C CD  . GLU C 387 ? 0.9603 1.0010 0.8972 -0.0072 -0.0724 -0.0136 387 GLU C CD  
11388 O OE1 . GLU C 387 ? 1.0143 1.0482 0.9308 -0.0178 -0.0716 -0.0102 387 GLU C OE1 
11389 O OE2 . GLU C 387 ? 1.0042 1.0638 0.9646 -0.0043 -0.0656 -0.0200 387 GLU C OE2 
11390 N N   . GLU C 388 ? 0.5353 0.5250 0.4116 -0.0202 -0.0937 0.0095  388 GLU C N   
11391 C CA  . GLU C 388 ? 0.4492 0.4369 0.3154 -0.0321 -0.0912 0.0132  388 GLU C CA  
11392 C C   . GLU C 388 ? 0.5291 0.5124 0.3987 -0.0345 -0.0978 0.0170  388 GLU C C   
11393 O O   . GLU C 388 ? 0.6262 0.6162 0.4999 -0.0440 -0.0950 0.0169  388 GLU C O   
11394 C CB  . GLU C 388 ? 0.4674 0.4391 0.3096 -0.0365 -0.0911 0.0185  388 GLU C CB  
11395 C CG  . GLU C 388 ? 0.4705 0.4487 0.3048 -0.0386 -0.0834 0.0138  388 GLU C CG  
11396 C CD  . GLU C 388 ? 0.6076 0.5714 0.4182 -0.0404 -0.0869 0.0197  388 GLU C CD  
11397 O OE1 . GLU C 388 ? 0.6985 0.6477 0.4983 -0.0430 -0.0927 0.0292  388 GLU C OE1 
11398 O OE2 . GLU C 388 ? 0.5743 0.5416 0.3778 -0.0394 -0.0841 0.0146  388 GLU C OE2 
11399 N N   . ALA C 389 ? 0.5237 0.4960 0.3913 -0.0271 -0.1060 0.0194  389 ALA C N   
11400 C CA  . ALA C 389 ? 0.4578 0.4265 0.3274 -0.0295 -0.1119 0.0208  389 ALA C CA  
11401 C C   . ALA C 389 ? 0.5775 0.5675 0.4666 -0.0293 -0.1136 0.0167  389 ALA C C   
11402 O O   . ALA C 389 ? 0.7152 0.7071 0.6065 -0.0349 -0.1177 0.0161  389 ALA C O   
11403 C CB  . ALA C 389 ? 0.4353 0.3890 0.2977 -0.0216 -0.1186 0.0232  389 ALA C CB  
11404 N N   . MET C 390 ? 0.6133 0.6199 0.5178 -0.0229 -0.1109 0.0135  390 MET C N   
11405 C CA  . MET C 390 ? 0.5578 0.5872 0.4843 -0.0210 -0.1134 0.0108  390 MET C CA  
11406 C C   . MET C 390 ? 0.6221 0.6703 0.5615 -0.0306 -0.1061 0.0066  390 MET C C   
11407 O O   . MET C 390 ? 0.6838 0.7503 0.6394 -0.0340 -0.1096 0.0048  390 MET C O   
11408 C CB  . MET C 390 ? 0.5817 0.6190 0.5225 -0.0076 -0.1143 0.0102  390 MET C CB  
11409 C CG  . MET C 390 ? 0.6032 0.6360 0.5434 0.0008  -0.1243 0.0149  390 MET C CG  
11410 S SD  . MET C 390 ? 0.7941 0.8410 0.7395 -0.0054 -0.1341 0.0158  390 MET C SD  
11411 C CE  . MET C 390 ? 0.6499 0.7289 0.6284 0.0009  -0.1351 0.0144  390 MET C CE  
11412 N N   . ARG C 391 ? 0.5713 0.6167 0.5036 -0.0356 -0.0959 0.0049  391 ARG C N   
11413 C CA  . ARG C 391 ? 0.5941 0.6567 0.5367 -0.0461 -0.0866 0.0010  391 ARG C CA  
11414 C C   . ARG C 391 ? 0.6158 0.6666 0.5427 -0.0611 -0.0845 0.0045  391 ARG C C   
11415 O O   . ARG C 391 ? 0.7080 0.7700 0.6398 -0.0722 -0.0753 0.0024  391 ARG C O   
11416 C CB  . ARG C 391 ? 0.6084 0.6765 0.5512 -0.0444 -0.0750 -0.0037 391 ARG C CB  
11417 C CG  . ARG C 391 ? 0.7703 0.8654 0.7355 -0.0498 -0.0644 -0.0106 391 ARG C CG  
11418 C CD  . ARG C 391 ? 0.8749 0.9931 0.8729 -0.0391 -0.0689 -0.0144 391 ARG C CD  
11419 N NE  . ARG C 391 ? 0.8727 1.0174 0.8942 -0.0474 -0.0658 -0.0179 391 ARG C NE  
11420 C CZ  . ARG C 391 ? 0.7331 0.8913 0.7708 -0.0475 -0.0764 -0.0162 391 ARG C CZ  
11421 N NH1 . ARG C 391 ? 0.5728 0.7201 0.6039 -0.0399 -0.0903 -0.0109 391 ARG C NH1 
11422 N NH2 . ARG C 391 ? 0.5457 0.7305 0.6065 -0.0564 -0.0728 -0.0205 391 ARG C NH2 
11423 N N   . LYS C 392 ? 0.5667 0.5944 0.4760 -0.0617 -0.0917 0.0098  392 LYS C N   
11424 C CA  . LYS C 392 ? 0.6432 0.6557 0.5393 -0.0749 -0.0900 0.0137  392 LYS C CA  
11425 C C   . LYS C 392 ? 0.7171 0.7460 0.6305 -0.0849 -0.0909 0.0094  392 LYS C C   
11426 O O   . LYS C 392 ? 0.8584 0.8907 0.7788 -0.0823 -0.1001 0.0071  392 LYS C O   
11427 C CB  . LYS C 392 ? 0.6634 0.6485 0.5416 -0.0710 -0.0975 0.0189  392 LYS C CB  
11428 C CG  . LYS C 392 ? 0.5619 0.5271 0.4194 -0.0684 -0.0953 0.0255  392 LYS C CG  
11429 C CD  . LYS C 392 ? 0.6624 0.6193 0.5082 -0.0816 -0.0875 0.0309  392 LYS C CD  
11430 C CE  . LYS C 392 ? 0.6606 0.6035 0.4859 -0.0788 -0.0862 0.0380  392 LYS C CE  
11431 N NZ  . LYS C 392 ? 0.8081 0.7683 0.6351 -0.0747 -0.0809 0.0331  392 LYS C NZ  
11432 N N   . GLU C 393 ? 0.6195 0.6601 0.5395 -0.0974 -0.0811 0.0079  393 GLU C N   
11433 C CA  . GLU C 393 ? 0.5429 0.6007 0.4811 -0.1094 -0.0811 0.0031  393 GLU C CA  
11434 C C   . GLU C 393 ? 0.5068 0.5415 0.4317 -0.1226 -0.0819 0.0060  393 GLU C C   
11435 O O   . GLU C 393 ? 0.6805 0.7261 0.6189 -0.1330 -0.0841 0.0009  393 GLU C O   
11436 C CB  . GLU C 393 ? 0.7579 0.8408 0.7126 -0.1179 -0.0687 -0.0007 393 GLU C CB  
11437 C CG  . GLU C 393 ? 0.9621 1.0754 0.9421 -0.1062 -0.0683 -0.0069 393 GLU C CG  
11438 C CD  . GLU C 393 ? 1.0159 1.1497 1.0080 -0.1127 -0.0528 -0.0112 393 GLU C CD  
11439 O OE1 . GLU C 393 ? 0.7522 0.9062 0.7629 -0.1019 -0.0496 -0.0166 393 GLU C OE1 
11440 O OE2 . GLU C 393 ? 0.9912 1.1200 0.9743 -0.1287 -0.0430 -0.0093 393 GLU C OE2 
11441 N N   . ASP C 394 ? 0.5890 0.5924 0.4893 -0.1223 -0.0805 0.0138  394 ASP C N   
11442 C CA  . ASP C 394 ? 0.6079 0.5852 0.4961 -0.1341 -0.0795 0.0178  394 ASP C CA  
11443 C C   . ASP C 394 ? 0.5984 0.5538 0.4776 -0.1268 -0.0894 0.0175  394 ASP C C   
11444 O O   . ASP C 394 ? 0.6059 0.5314 0.4701 -0.1299 -0.0886 0.0233  394 ASP C O   
11445 C CB  . ASP C 394 ? 0.6394 0.5963 0.5075 -0.1393 -0.0708 0.0283  394 ASP C CB  
11446 C CG  . ASP C 394 ? 0.8065 0.7572 0.6750 -0.1588 -0.0617 0.0309  394 ASP C CG  
11447 O OD1 . ASP C 394 ? 0.6751 0.6313 0.5581 -0.1685 -0.0632 0.0239  394 ASP C OD1 
11448 O OD2 . ASP C 394 ? 0.7465 0.6869 0.6002 -0.1653 -0.0529 0.0401  394 ASP C OD2 
11449 N N   . VAL C 395 ? 0.6185 0.5879 0.5067 -0.1171 -0.0984 0.0113  395 VAL C N   
11450 C CA  . VAL C 395 ? 0.6303 0.5817 0.5092 -0.1101 -0.1065 0.0099  395 VAL C CA  
11451 C C   . VAL C 395 ? 0.5307 0.4974 0.4215 -0.1158 -0.1133 0.0003  395 VAL C C   
11452 O O   . VAL C 395 ? 0.5113 0.5081 0.4201 -0.1188 -0.1150 -0.0042 395 VAL C O   
11453 C CB  . VAL C 395 ? 0.6425 0.5931 0.5155 -0.0923 -0.1113 0.0129  395 VAL C CB  
11454 C CG1 . VAL C 395 ? 0.5059 0.4408 0.3654 -0.0879 -0.1061 0.0216  395 VAL C CG1 
11455 C CG2 . VAL C 395 ? 0.5972 0.5787 0.4867 -0.0851 -0.1143 0.0093  395 VAL C CG2 
11456 N N   . LYS C 396 ? 0.5349 0.4816 0.4159 -0.1173 -0.1173 -0.0032 396 LYS C N   
11457 C CA  . LYS C 396 ? 0.5462 0.5055 0.4336 -0.1238 -0.1244 -0.0134 396 LYS C CA  
11458 C C   . LYS C 396 ? 0.5148 0.4968 0.4066 -0.1111 -0.1338 -0.0144 396 LYS C C   
11459 O O   . LYS C 396 ? 0.5035 0.4781 0.3872 -0.0968 -0.1350 -0.0089 396 LYS C O   
11460 C CB  . LYS C 396 ? 0.6335 0.5628 0.5072 -0.1285 -0.1245 -0.0182 396 LYS C CB  
11461 C CG  . LYS C 396 ? 0.5712 0.5022 0.4510 -0.1468 -0.1246 -0.0290 396 LYS C CG  
11462 C CD  . LYS C 396 ? 0.6378 0.5520 0.5057 -0.1476 -0.1286 -0.0385 396 LYS C CD  
11463 C CE  . LYS C 396 ? 0.7304 0.6332 0.6009 -0.1671 -0.1255 -0.0495 396 LYS C CE  
11464 N NZ  . LYS C 396 ? 0.6258 0.5141 0.4843 -0.1685 -0.1286 -0.0615 396 LYS C NZ  
11465 N N   . THR C 397 ? 0.4842 0.6156 0.3020 -0.0631 -0.0665 0.2161  397 THR C N   
11466 C CA  . THR C 397 ? 0.4523 0.5949 0.2793 -0.0546 -0.0688 0.1977  397 THR C CA  
11467 C C   . THR C 397 ? 0.4277 0.5816 0.2846 -0.0652 -0.0750 0.1998  397 THR C C   
11468 O O   . THR C 397 ? 0.4343 0.6079 0.3060 -0.0805 -0.0716 0.2177  397 THR C O   
11469 C CB  . THR C 397 ? 0.4577 0.6271 0.2732 -0.0495 -0.0562 0.1955  397 THR C CB  
11470 O OG1 . THR C 397 ? 0.6634 0.8563 0.4792 -0.0615 -0.0428 0.2166  397 THR C OG1 
11471 C CG2 . THR C 397 ? 0.4800 0.6287 0.2629 -0.0353 -0.0551 0.1829  397 THR C CG2 
11472 N N   . GLU C 398 ? 0.4390 0.5784 0.3035 -0.0578 -0.0837 0.1820  398 GLU C N   
11473 C CA  . GLU C 398 ? 0.4401 0.5836 0.3262 -0.0663 -0.0914 0.1802  398 GLU C CA  
11474 C C   . GLU C 398 ? 0.4291 0.5802 0.3175 -0.0551 -0.0919 0.1608  398 GLU C C   
11475 O O   . GLU C 398 ? 0.3569 0.4941 0.2318 -0.0398 -0.0896 0.1448  398 GLU C O   
11476 C CB  . GLU C 398 ? 0.5520 0.6635 0.4430 -0.0692 -0.1007 0.1776  398 GLU C CB  
11477 C CG  . GLU C 398 ? 0.5528 0.6632 0.4612 -0.0864 -0.1095 0.1865  398 GLU C CG  
11478 C CD  . GLU C 398 ? 0.7411 0.8169 0.6514 -0.0898 -0.1173 0.1868  398 GLU C CD  
11479 O OE1 . GLU C 398 ? 0.6867 0.7482 0.6009 -0.0924 -0.1250 0.1771  398 GLU C OE1 
11480 O OE2 . GLU C 398 ? 0.6804 0.7420 0.5869 -0.0895 -0.1158 0.1967  398 GLU C OE2 
11481 N N   . VAL C 399 ? 0.4797 0.6508 0.3855 -0.0633 -0.0964 0.1630  399 VAL C N   
11482 C CA  . VAL C 399 ? 0.3350 0.5116 0.2451 -0.0532 -0.0982 0.1456  399 VAL C CA  
11483 C C   . VAL C 399 ? 0.3482 0.4936 0.2595 -0.0520 -0.1066 0.1310  399 VAL C C   
11484 O O   . VAL C 399 ? 0.3446 0.4790 0.2626 -0.0653 -0.1142 0.1382  399 VAL C O   
11485 C CB  . VAL C 399 ? 0.3898 0.6091 0.3202 -0.0612 -0.0999 0.1563  399 VAL C CB  
11486 C CG1 . VAL C 399 ? 0.3156 0.5385 0.2504 -0.0484 -0.1020 0.1382  399 VAL C CG1 
11487 C CG2 . VAL C 399 ? 0.4017 0.6568 0.3297 -0.0635 -0.0879 0.1754  399 VAL C CG2 
11488 N N   . ILE C 400 ? 0.3598 0.4891 0.2628 -0.0365 -0.1049 0.1114  400 ILE C N   
11489 C CA  . ILE C 400 ? 0.4322 0.5356 0.3334 -0.0334 -0.1097 0.0976  400 ILE C CA  
11490 C C   . ILE C 400 ? 0.3962 0.5028 0.2984 -0.0239 -0.1107 0.0842  400 ILE C C   
11491 O O   . ILE C 400 ? 0.3880 0.5035 0.2866 -0.0139 -0.1065 0.0801  400 ILE C O   
11492 C CB  . ILE C 400 ? 0.4060 0.4834 0.2960 -0.0232 -0.1062 0.0894  400 ILE C CB  
11493 C CG1 . ILE C 400 ? 0.4491 0.5244 0.3281 -0.0078 -0.1003 0.0805  400 ILE C CG1 
11494 C CG2 . ILE C 400 ? 0.3618 0.4325 0.2530 -0.0329 -0.1079 0.1036  400 ILE C CG2 
11495 C CD1 . ILE C 400 ? 0.4474 0.5014 0.3199 0.0041  -0.0987 0.0682  400 ILE C CD1 
11496 N N   . GLU C 401 ? 0.3544 0.4515 0.2596 -0.0280 -0.1172 0.0780  401 GLU C N   
11497 C CA  . GLU C 401 ? 0.3999 0.4983 0.3058 -0.0193 -0.1200 0.0667  401 GLU C CA  
11498 C C   . GLU C 401 ? 0.3628 0.4369 0.2553 -0.0056 -0.1159 0.0511  401 GLU C C   
11499 O O   . GLU C 401 ? 0.4317 0.5048 0.3216 0.0052  -0.1168 0.0419  401 GLU C O   
11500 C CB  . GLU C 401 ? 0.3710 0.4778 0.2885 -0.0327 -0.1309 0.0704  401 GLU C CB  
11501 C CG  . GLU C 401 ? 0.4312 0.5711 0.3694 -0.0472 -0.1356 0.0875  401 GLU C CG  
11502 C CD  . GLU C 401 ? 0.5397 0.7113 0.4874 -0.0386 -0.1300 0.0921  401 GLU C CD  
11503 O OE1 . GLU C 401 ? 0.5733 0.7450 0.5206 -0.0260 -0.1309 0.0817  401 GLU C OE1 
11504 O OE2 . GLU C 401 ? 0.7000 0.8968 0.6542 -0.0445 -0.1246 0.1072  401 GLU C OE2 
11505 N N   . SER C 402 ? 0.2843 0.3425 0.1705 -0.0066 -0.1118 0.0502  402 SER C N   
11506 C CA  . SER C 402 ? 0.3320 0.3787 0.2112 0.0029  -0.1060 0.0396  402 SER C CA  
11507 C C   . SER C 402 ? 0.4129 0.4485 0.2903 0.0012  -0.1017 0.0426  402 SER C C   
11508 O O   . SER C 402 ? 0.4072 0.4370 0.2862 -0.0093 -0.1056 0.0524  402 SER C O   
11509 C CB  . SER C 402 ? 0.3749 0.4129 0.2507 -0.0051 -0.1102 0.0361  402 SER C CB  
11510 O OG  . SER C 402 ? 0.3398 0.3594 0.2113 -0.0213 -0.1164 0.0420  402 SER C OG  
11511 N N   . VAL C 403 ? 0.4349 0.4682 0.3104 0.0080  -0.0962 0.0374  403 VAL C N   
11512 C CA  . VAL C 403 ? 0.3893 0.4125 0.2659 0.0070  -0.0933 0.0394  403 VAL C CA  
11513 C C   . VAL C 403 ? 0.4186 0.4274 0.2908 0.0036  -0.0915 0.0342  403 VAL C C   
11514 O O   . VAL C 403 ? 0.3900 0.3996 0.2581 0.0038  -0.0909 0.0293  403 VAL C O   
11515 C CB  . VAL C 403 ? 0.3024 0.3343 0.1810 0.0154  -0.0907 0.0403  403 VAL C CB  
11516 C CG1 . VAL C 403 ? 0.3357 0.3719 0.2114 0.0176  -0.0935 0.0452  403 VAL C CG1 
11517 C CG2 . VAL C 403 ? 0.4134 0.4554 0.2928 0.0201  -0.0868 0.0343  403 VAL C CG2 
11518 N N   . LYS C 404 ? 0.4190 0.4036 0.2862 -0.0021 -0.0948 0.0369  404 LYS C N   
11519 C CA  . LYS C 404 ? 0.3562 0.3146 0.2111 -0.0048 -0.0949 0.0315  404 LYS C CA  
11520 C C   . LYS C 404 ? 0.3525 0.3168 0.2148 0.0022  -0.0908 0.0301  404 LYS C C   
11521 O O   . LYS C 404 ? 0.3892 0.3616 0.2621 0.0054  -0.0922 0.0354  404 LYS C O   
11522 C CB  . LYS C 404 ? 0.4352 0.3555 0.2737 -0.0137 -0.1028 0.0342  404 LYS C CB  
11523 C CG  . LYS C 404 ? 0.4170 0.3041 0.2282 -0.0198 -0.1032 0.0261  404 LYS C CG  
11524 C CD  . LYS C 404 ? 0.6451 0.4906 0.4313 -0.0299 -0.1107 0.0275  404 LYS C CD  
11525 C CE  . LYS C 404 ? 0.7997 0.6102 0.5515 -0.0369 -0.1078 0.0161  404 LYS C CE  
11526 N NZ  . LYS C 404 ? 0.8523 0.6276 0.5911 -0.0342 -0.0938 0.0082  404 LYS C NZ  
11527 N N   . ALA C 405 ? 0.3852 0.3437 0.2414 0.0036  -0.0869 0.0237  405 ALA C N   
11528 C CA  . ALA C 405 ? 0.3198 0.2852 0.1835 0.0085  -0.0840 0.0223  405 ALA C CA  
11529 C C   . ALA C 405 ? 0.3523 0.2913 0.2111 0.0093  -0.0899 0.0238  405 ALA C C   
11530 O O   . ALA C 405 ? 0.5054 0.4093 0.3441 0.0067  -0.0932 0.0220  405 ALA C O   
11531 C CB  . ALA C 405 ? 0.3253 0.2868 0.1822 0.0089  -0.0798 0.0164  405 ALA C CB  
11532 N N   . GLY C 406 ? 0.4066 0.3604 0.2812 0.0134  -0.0917 0.0272  406 GLY C N   
11533 C CA  . GLY C 406 ? 0.4443 0.3788 0.3233 0.0160  -0.1001 0.0305  406 GLY C CA  
11534 C C   . GLY C 406 ? 0.3513 0.3093 0.2501 0.0195  -0.1018 0.0335  406 GLY C C   
11535 O O   . GLY C 406 ? 0.3752 0.3590 0.2764 0.0199  -0.0954 0.0319  406 GLY C O   
11536 N N   . THR C 407 ? 0.3071 0.2551 0.2215 0.0222  -0.1113 0.0387  407 THR C N   
11537 C CA  . THR C 407 ? 0.4165 0.3833 0.3489 0.0246  -0.1152 0.0416  407 THR C CA  
11538 C C   . THR C 407 ? 0.4019 0.3681 0.3538 0.0255  -0.1225 0.0519  407 THR C C   
11539 O O   . THR C 407 ? 0.3646 0.3134 0.3213 0.0249  -0.1249 0.0574  407 THR C O   
11540 C CB  . THR C 407 ? 0.3782 0.3369 0.3212 0.0269  -0.1214 0.0379  407 THR C CB  
11541 O OG1 . THR C 407 ? 0.4001 0.3349 0.3615 0.0303  -0.1287 0.0423  407 THR C OG1 
11542 C CG2 . THR C 407 ? 0.3370 0.2930 0.2596 0.0260  -0.1145 0.0285  407 THR C CG2 
11543 N N   . TRP C 408 ? 0.3269 0.3092 0.2892 0.0270  -0.1263 0.0551  408 TRP C N   
11544 C CA  . TRP C 408 ? 0.4444 0.4253 0.4272 0.0280  -0.1339 0.0654  408 TRP C CA  
11545 C C   . TRP C 408 ? 0.4608 0.4282 0.4808 0.0306  -0.1413 0.0699  408 TRP C C   
11546 O O   . TRP C 408 ? 0.4709 0.4361 0.5165 0.0322  -0.1458 0.0792  408 TRP C O   
11547 C CB  . TRP C 408 ? 0.3882 0.3867 0.3669 0.0292  -0.1372 0.0676  408 TRP C CB  
11548 C CG  . TRP C 408 ? 0.3723 0.3779 0.3563 0.0300  -0.1423 0.0628  408 TRP C CG  
11549 C CD1 . TRP C 408 ? 0.4399 0.4391 0.4338 0.0294  -0.1441 0.0567  408 TRP C CD1 
11550 C CD2 . TRP C 408 ? 0.3388 0.3568 0.3170 0.0310  -0.1482 0.0640  408 TRP C CD2 
11551 N NE1 . TRP C 408 ? 0.3922 0.3993 0.3889 0.0291  -0.1508 0.0540  408 TRP C NE1 
11552 C CE2 . TRP C 408 ? 0.3907 0.4093 0.3766 0.0299  -0.1536 0.0583  408 TRP C CE2 
11553 C CE3 . TRP C 408 ? 0.3114 0.3378 0.2772 0.0327  -0.1506 0.0697  408 TRP C CE3 
11554 C CZ2 . TRP C 408 ? 0.3588 0.3860 0.3399 0.0297  -0.1619 0.0578  408 TRP C CZ2 
11555 C CZ3 . TRP C 408 ? 0.3709 0.4038 0.3303 0.0326  -0.1600 0.0698  408 TRP C CZ3 
11556 C CH2 . TRP C 408 ? 0.3915 0.4255 0.3584 0.0311  -0.1653 0.0636  408 TRP C CH2 
11557 N N   . PHE C 409 ? 0.4476 0.4063 0.4760 0.0324  -0.1412 0.0640  409 PHE C N   
11558 C CA  . PHE C 409 ? 0.4341 0.3791 0.5079 0.0378  -0.1415 0.0677  409 PHE C CA  
11559 C C   . PHE C 409 ? 0.4088 0.3309 0.4729 0.0362  -0.1198 0.0622  409 PHE C C   
11560 O O   . PHE C 409 ? 0.4525 0.3610 0.4936 0.0333  -0.1046 0.0508  409 PHE C O   
11561 C CB  . PHE C 409 ? 0.4576 0.4040 0.5428 0.0377  -0.1383 0.0589  409 PHE C CB  
11562 C CG  . PHE C 409 ? 0.4620 0.4279 0.5687 0.0367  -0.1528 0.0612  409 PHE C CG  
11563 C CD1 . PHE C 409 ? 0.4660 0.4437 0.5358 0.0321  -0.1565 0.0560  409 PHE C CD1 
11564 C CD2 . PHE C 409 ? 0.4799 0.4511 0.6427 0.0392  -0.1551 0.0661  409 PHE C CD2 
11565 C CE1 . PHE C 409 ? 0.4354 0.4248 0.5171 0.0300  -0.1660 0.0561  409 PHE C CE1 
11566 C CE2 . PHE C 409 ? 0.5089 0.4955 0.6850 0.0354  -0.1670 0.0665  409 PHE C CE2 
11567 C CZ  . PHE C 409 ? 0.4772 0.4701 0.6094 0.0308  -0.1737 0.0615  409 PHE C CZ  
11568 N N   . ASP C 410 ? 0.5251 0.4405 0.6035 0.0374  -0.1187 0.0701  410 ASP C N   
11569 C CA  . ASP C 410 ? 0.5820 0.4725 0.6558 0.0354  -0.0982 0.0645  410 ASP C CA  
11570 C C   . ASP C 410 ? 0.5109 0.3909 0.5329 0.0286  -0.0936 0.0571  410 ASP C C   
11571 O O   . ASP C 410 ? 0.5551 0.4110 0.5646 0.0252  -0.0768 0.0491  410 ASP C O   
11572 C CB  . ASP C 410 ? 0.6833 0.5584 0.7853 0.0379  -0.0748 0.0547  410 ASP C CB  
11573 C CG  . ASP C 410 ? 0.9580 0.8110 1.0823 0.0402  -0.0578 0.0544  410 ASP C CG  
11574 O OD1 . ASP C 410 ? 1.1968 1.0563 1.3568 0.0453  -0.0674 0.0662  410 ASP C OD1 
11575 O OD2 . ASP C 410 ? 0.9852 0.8121 1.0893 0.0371  -0.0352 0.0422  410 ASP C OD2 
11576 N N   . GLY C 411 ? 0.4479 0.3447 0.4400 0.0265  -0.1085 0.0591  411 GLY C N   
11577 C CA  . GLY C 411 ? 0.3739 0.2658 0.3245 0.0206  -0.1077 0.0548  411 GLY C CA  
11578 C C   . GLY C 411 ? 0.3996 0.2794 0.3227 0.0182  -0.0972 0.0417  411 GLY C C   
11579 O O   . GLY C 411 ? 0.3996 0.2738 0.2908 0.0132  -0.0974 0.0381  411 GLY C O   
11580 N N   . ASN C 412 ? 0.3699 0.2457 0.3053 0.0211  -0.0890 0.0355  412 ASN C N   
11581 C CA  . ASN C 412 ? 0.3571 0.2171 0.2649 0.0186  -0.0777 0.0245  412 ASN C CA  
11582 C C   . ASN C 412 ? 0.3733 0.2450 0.2907 0.0221  -0.0818 0.0228  412 ASN C C   
11583 O O   . ASN C 412 ? 0.4698 0.3630 0.4063 0.0256  -0.0968 0.0291  412 ASN C O   
11584 C CB  . ASN C 412 ? 0.3354 0.1650 0.2444 0.0161  -0.0545 0.0166  412 ASN C CB  
11585 C CG  . ASN C 412 ? 0.3416 0.1708 0.2990 0.0207  -0.0434 0.0184  412 ASN C CG  
11586 O OD1 . ASN C 412 ? 0.3721 0.2082 0.3505 0.0232  -0.0399 0.0171  412 ASN C OD1 
11587 N ND2 . ASN C 412 ? 0.4475 0.2688 0.4262 0.0219  -0.0382 0.0217  412 ASN C ND2 
11588 N N   . PHE C 413 ? 0.3130 0.1678 0.2137 0.0202  -0.0691 0.0142  413 PHE C N   
11589 C CA  . PHE C 413 ? 0.3073 0.1683 0.2139 0.0220  -0.0716 0.0118  413 PHE C CA  
11590 C C   . PHE C 413 ? 0.3174 0.1649 0.2518 0.0210  -0.0518 0.0078  413 PHE C C   
11591 O O   . PHE C 413 ? 0.3199 0.1643 0.2538 0.0201  -0.0483 0.0043  413 PHE C O   
11592 C CB  . PHE C 413 ? 0.3130 0.1671 0.1766 0.0208  -0.0753 0.0070  413 PHE C CB  
11593 C CG  . PHE C 413 ? 0.3031 0.1740 0.1451 0.0225  -0.0930 0.0107  413 PHE C CG  
11594 C CD1 . PHE C 413 ? 0.3101 0.1751 0.1306 0.0191  -0.0927 0.0113  413 PHE C CD1 
11595 C CD2 . PHE C 413 ? 0.3721 0.2714 0.2294 0.0245  -0.0999 0.0116  413 PHE C CD2 
11596 C CE1 . PHE C 413 ? 0.2899 0.1904 0.1293 0.0167  -0.0890 0.0123  413 PHE C CE1 
11597 C CE2 . PHE C 413 ? 0.3091 0.2390 0.1765 0.0219  -0.0928 0.0126  413 PHE C CE2 
11598 C CZ  . PHE C 413 ? 0.3069 0.2390 0.1679 0.0186  -0.0880 0.0136  413 PHE C CZ  
11599 N N   . LEU C 414 ? 0.3251 0.1641 0.2861 0.0214  -0.0374 0.0084  414 LEU C N   
11600 C CA  . LEU C 414 ? 0.3546 0.1799 0.3434 0.0207  -0.0136 0.0041  414 LEU C CA  
11601 C C   . LEU C 414 ? 0.3234 0.1706 0.3644 0.0232  -0.0200 0.0084  414 LEU C C   
11602 O O   . LEU C 414 ? 0.3529 0.1927 0.4209 0.0219  -0.0005 0.0052  414 LEU C O   
11603 C CB  . LEU C 414 ? 0.3540 0.1631 0.3581 0.0217  0.0049  0.0026  414 LEU C CB  
11604 C CG  . LEU C 414 ? 0.3803 0.1585 0.3311 0.0168  0.0173  -0.0051 414 LEU C CG  
11605 C CD1 . LEU C 414 ? 0.3936 0.1584 0.3555 0.0179  0.0269  -0.0057 414 LEU C CD1 
11606 C CD2 . LEU C 414 ? 0.4072 0.1586 0.3342 0.0126  0.0416  -0.0137 414 LEU C CD2 
11607 N N   . LYS C 415 ? 0.3139 0.1870 0.3692 0.0260  -0.0466 0.0156  415 LYS C N   
11608 C CA  . LYS C 415 ? 0.3195 0.2125 0.4193 0.0268  -0.0577 0.0192  415 LYS C CA  
11609 C C   . LYS C 415 ? 0.2947 0.1861 0.3762 0.0230  -0.0613 0.0138  415 LYS C C   
11610 O O   . LYS C 415 ? 0.4121 0.3135 0.5313 0.0213  -0.0643 0.0143  415 LYS C O   
11611 C CB  . LYS C 415 ? 0.3279 0.2451 0.4428 0.0304  -0.0862 0.0289  415 LYS C CB  
11612 C CG  . LYS C 415 ? 0.3399 0.2770 0.5124 0.0316  -0.0989 0.0347  415 LYS C CG  
11613 C CD  . LYS C 415 ? 0.5279 0.4620 0.7563 0.0338  -0.0782 0.0360  415 LYS C CD  
11614 C CE  . LYS C 415 ? 0.5945 0.5481 0.8831 0.0329  -0.0875 0.0395  415 LYS C CE  
11615 N NZ  . LYS C 415 ? 0.5583 0.5045 0.8475 0.0267  -0.0728 0.0309  415 LYS C NZ  
11616 N N   . TRP C 416 ? 0.2992 0.1780 0.3265 0.0216  -0.0619 0.0091  416 TRP C N   
11617 C CA  . TRP C 416 ? 0.3031 0.1769 0.3099 0.0191  -0.0657 0.0044  416 TRP C CA  
11618 C C   . TRP C 416 ? 0.3235 0.1688 0.2965 0.0154  -0.0439 -0.0016 416 TRP C C   
11619 O O   . TRP C 416 ? 0.3770 0.2139 0.3392 0.0127  -0.0431 -0.0046 416 TRP C O   
11620 C CB  . TRP C 416 ? 0.2944 0.1797 0.2671 0.0221  -0.0896 0.0049  416 TRP C CB  
11621 C CG  . TRP C 416 ? 0.2813 0.1910 0.2753 0.0251  -0.1116 0.0111  416 TRP C CG  
11622 C CD1 . TRP C 416 ? 0.3555 0.2792 0.3671 0.0247  -0.1302 0.0116  416 TRP C CD1 
11623 C CD2 . TRP C 416 ? 0.2916 0.2116 0.2886 0.0279  -0.1183 0.0183  416 TRP C CD2 
11624 N NE1 . TRP C 416 ? 0.3488 0.2907 0.3708 0.0274  -0.1485 0.0191  416 TRP C NE1 
11625 C CE2 . TRP C 416 ? 0.2839 0.2240 0.2983 0.0295  -0.1409 0.0240  416 TRP C CE2 
11626 C CE3 . TRP C 416 ? 0.3375 0.2495 0.3224 0.0283  -0.1080 0.0205  416 TRP C CE3 
11627 C CZ2 . TRP C 416 ? 0.3426 0.2951 0.3615 0.0314  -0.1500 0.0327  416 TRP C CZ2 
11628 C CZ3 . TRP C 416 ? 0.2713 0.1957 0.2647 0.0305  -0.1192 0.0291  416 TRP C CZ3 
11629 C CH2 . TRP C 416 ? 0.3343 0.2785 0.3443 0.0326  -0.1408 0.0361  416 TRP C CH2 
11630 N N   . ILE C 417 ? 0.3368 0.1641 0.2900 0.0146  -0.0269 -0.0031 417 ILE C N   
11631 C CA  . ILE C 417 ? 0.3629 0.1597 0.2733 0.0106  -0.0090 -0.0082 417 ILE C CA  
11632 C C   . ILE C 417 ? 0.3878 0.1649 0.2942 0.0089  0.0138  -0.0108 417 ILE C C   
11633 O O   . ILE C 417 ? 0.3909 0.1782 0.3204 0.0117  0.0118  -0.0085 417 ILE C O   
11634 C CB  . ILE C 417 ? 0.3783 0.1715 0.2369 0.0120  -0.0255 -0.0088 417 ILE C CB  
11635 C CG1 . ILE C 417 ? 0.3912 0.1559 0.2113 0.0082  -0.0142 -0.0120 417 ILE C CG1 
11636 C CG2 . ILE C 417 ? 0.3987 0.1911 0.2351 0.0128  -0.0299 -0.0080 417 ILE C CG2 
11637 C CD1 . ILE C 417 ? 0.4134 0.1760 0.1900 0.0109  -0.0318 -0.0116 417 ILE C CD1 
11638 N N   . GLY C 418 ? 0.4136 0.1593 0.2880 0.0040  0.0360  -0.0156 418 GLY C N   
11639 C CA  . GLY C 418 ? 0.4414 0.1610 0.3000 0.0016  0.0596  -0.0204 418 GLY C CA  
11640 C C   . GLY C 418 ? 0.5023 0.2103 0.3953 -0.0002 0.0915  -0.0231 418 GLY C C   
11641 O O   . GLY C 418 ? 0.6768 0.3549 0.5461 -0.0030 0.1166  -0.0290 418 GLY C O   
11642 N N   . ASN C 419 ? 0.6207 0.3506 0.5687 0.0010  0.0917  -0.0195 419 ASN C N   
11643 C CA  . ASN C 419 ? 0.6116 0.3355 0.6022 -0.0008 0.1225  -0.0211 419 ASN C CA  
11644 C C   . ASN C 419 ? 0.5759 0.2848 0.5515 -0.0077 0.1355  -0.0214 419 ASN C C   
11645 O O   . ASN C 419 ? 0.5825 0.2931 0.5301 -0.0094 0.1154  -0.0193 419 ASN C O   
11646 C CB  . ASN C 419 ? 0.6265 0.3864 0.6967 0.0042  0.1133  -0.0156 419 ASN C CB  
11647 C CG  . ASN C 419 ? 0.9709 0.7429 1.0588 0.0112  0.1022  -0.0134 419 ASN C CG  
11648 O OD1 . ASN C 419 ? 1.0152 0.7859 1.1433 0.0150  0.1214  -0.0142 419 ASN C OD1 
11649 N ND2 . ASN C 419 ? 0.8711 0.6542 0.9308 0.0132  0.0722  -0.0103 419 ASN C ND2 
11650 N N   . LYS C 420 ? 0.6080 0.3008 0.6034 -0.0114 0.1711  -0.0239 420 LYS C N   
11651 C CA  . LYS C 420 ? 0.6174 0.2928 0.5989 -0.0193 0.1875  -0.0231 420 LYS C CA  
11652 C C   . LYS C 420 ? 0.5477 0.2519 0.5705 -0.0207 0.1642  -0.0176 420 LYS C C   
11653 O O   . LYS C 420 ? 0.5013 0.1954 0.4882 -0.0245 0.1518  -0.0160 420 LYS C O   
11654 C CB  . LYS C 420 ? 0.5849 0.2435 0.5926 -0.0231 0.2322  -0.0260 420 LYS C CB  
11655 C CG  . LYS C 420 ? 0.5938 0.2255 0.5730 -0.0329 0.2541  -0.0246 420 LYS C CG  
11656 C CD  . LYS C 420 ? 0.6036 0.2431 0.6497 -0.0372 0.2876  -0.0231 420 LYS C CD  
11657 C CE  . LYS C 420 ? 0.6146 0.2544 0.6974 -0.0318 0.3180  -0.0282 420 LYS C CE  
11658 N NZ  . LYS C 420 ? 0.5926 0.2680 0.7768 -0.0305 0.3285  -0.0244 420 LYS C NZ  
11659 N N   . GLU C 421 ? 0.5148 0.2535 0.6126 -0.0175 0.1563  -0.0146 421 GLU C N   
11660 C CA  . GLU C 421 ? 0.6065 0.3710 0.7446 -0.0202 0.1329  -0.0104 421 GLU C CA  
11661 C C   . GLU C 421 ? 0.6002 0.3768 0.7055 -0.0161 0.0928  -0.0096 421 GLU C C   
11662 O O   . GLU C 421 ? 0.5758 0.3555 0.6753 -0.0196 0.0756  -0.0088 421 GLU C O   
11663 C CB  . GLU C 421 ? 0.5217 0.3199 0.7489 -0.0182 0.1324  -0.0069 421 GLU C CB  
11664 C CG  . GLU C 421 ? 0.9254 0.7386 1.2057 -0.0263 0.1308  -0.0039 421 GLU C CG  
11665 C CD  . GLU C 421 ? 0.9875 0.7699 1.2353 -0.0362 0.1563  -0.0053 421 GLU C CD  
11666 O OE1 . GLU C 421 ? 0.8528 0.6085 1.0786 -0.0380 0.1934  -0.0076 421 GLU C OE1 
11667 O OE2 . GLU C 421 ? 0.8149 0.5971 1.0560 -0.0424 0.1394  -0.0042 421 GLU C OE2 
11668 N N   . LYS C 422 ? 0.5608 0.3433 0.6454 -0.0089 0.0789  -0.0099 422 LYS C N   
11669 C CA  . LYS C 422 ? 0.5412 0.3356 0.5944 -0.0049 0.0445  -0.0089 422 LYS C CA  
11670 C C   . LYS C 422 ? 0.5112 0.2795 0.4953 -0.0067 0.0430  -0.0114 422 LYS C C   
11671 O O   . LYS C 422 ? 0.4532 0.2290 0.4173 -0.0047 0.0184  -0.0112 422 LYS C O   
11672 C CB  . LYS C 422 ? 0.5282 0.3358 0.5810 0.0022  0.0323  -0.0072 422 LYS C CB  
11673 C CG  . LYS C 422 ? 0.5235 0.3531 0.6441 0.0053  0.0349  -0.0034 422 LYS C CG  
11674 C CD  . LYS C 422 ? 0.3833 0.2338 0.5097 0.0119  0.0092  0.0014  422 LYS C CD  
11675 C CE  . LYS C 422 ? 0.4766 0.3514 0.6755 0.0152  0.0050  0.0075  422 LYS C CE  
11676 N NZ  . LYS C 422 ? 0.6642 0.5368 0.8738 0.0212  0.0125  0.0099  422 LYS C NZ  
11677 N N   . ASN C 423 ? 0.6105 0.3468 0.5570 -0.0103 0.0689  -0.0138 423 ASN C N   
11678 C CA  . ASN C 423 ? 0.5963 0.3060 0.4773 -0.0120 0.0660  -0.0147 423 ASN C CA  
11679 C C   . ASN C 423 ? 0.5261 0.2232 0.4049 -0.0176 0.0698  -0.0131 423 ASN C C   
11680 O O   . ASN C 423 ? 0.4872 0.1673 0.3188 -0.0172 0.0594  -0.0124 423 ASN C O   
11681 C CB  . ASN C 423 ? 0.5804 0.2565 0.4149 -0.0148 0.0898  -0.0174 423 ASN C CB  
11682 C CG  . ASN C 423 ? 0.5579 0.2386 0.3712 -0.0101 0.0782  -0.0193 423 ASN C CG  
11683 O OD1 . ASN C 423 ? 0.5070 0.2117 0.3238 -0.0048 0.0506  -0.0174 423 ASN C OD1 
11684 N ND2 . ASN C 423 ? 0.6076 0.2636 0.3980 -0.0127 0.1003  -0.0234 423 ASN C ND2 
11685 N N   . GLU C 424 ? 0.5324 0.2369 0.4632 -0.0228 0.0840  -0.0121 424 GLU C N   
11686 C CA  . GLU C 424 ? 0.4897 0.1810 0.4206 -0.0297 0.0875  -0.0103 424 GLU C CA  
11687 C C   . GLU C 424 ? 0.4674 0.1760 0.4029 -0.0265 0.0537  -0.0106 424 GLU C C   
11688 O O   . GLU C 424 ? 0.4843 0.1736 0.3884 -0.0285 0.0480  -0.0099 424 GLU C O   
11689 C CB  . GLU C 424 ? 0.4964 0.1930 0.4876 -0.0374 0.1127  -0.0089 424 GLU C CB  
11690 C CG  . GLU C 424 ? 0.6054 0.2816 0.5963 -0.0475 0.1251  -0.0061 424 GLU C CG  
11691 C CD  . GLU C 424 ? 0.9657 0.6004 0.8796 -0.0495 0.1314  -0.0042 424 GLU C CD  
11692 O OE1 . GLU C 424 ? 0.9411 0.5608 0.8495 -0.0556 0.1296  -0.0013 424 GLU C OE1 
11693 O OE2 . GLU C 424 ? 1.0396 0.6543 0.9008 -0.0461 0.1386  -0.0051 424 GLU C OE2 
11694 N N   . TYR C 425 ? 0.4339 0.1761 0.4058 -0.0215 0.0313  -0.0116 425 TYR C N   
11695 C CA  . TYR C 425 ? 0.4182 0.1745 0.3890 -0.0184 0.0002  -0.0133 425 TYR C CA  
11696 C C   . TYR C 425 ? 0.4236 0.1683 0.3333 -0.0112 -0.0141 -0.0146 425 TYR C C   
11697 O O   . TYR C 425 ? 0.4563 0.1927 0.3465 -0.0101 -0.0279 -0.0164 425 TYR C O   
11698 C CB  . TYR C 425 ? 0.4521 0.2441 0.4682 -0.0150 -0.0202 -0.0132 425 TYR C CB  
11699 C CG  . TYR C 425 ? 0.3843 0.1916 0.4642 -0.0224 -0.0210 -0.0124 425 TYR C CG  
11700 C CD1 . TYR C 425 ? 0.4116 0.2080 0.5225 -0.0307 0.0073  -0.0105 425 TYR C CD1 
11701 C CD2 . TYR C 425 ? 0.4402 0.2720 0.5490 -0.0218 -0.0501 -0.0134 425 TYR C CD2 
11702 C CE1 . TYR C 425 ? 0.4334 0.2465 0.6093 -0.0383 0.0061  -0.0092 425 TYR C CE1 
11703 C CE2 . TYR C 425 ? 0.4018 0.2483 0.5712 -0.0297 -0.0543 -0.0124 425 TYR C CE2 
11704 C CZ  . TYR C 425 ? 0.3996 0.2383 0.6057 -0.0380 -0.0263 -0.0101 425 TYR C CZ  
11705 O OH  . TYR C 425 ? 0.4998 0.3559 0.7729 -0.0466 -0.0309 -0.0086 425 TYR C OH  
11706 N N   . TRP C 426 ? 0.4943 0.2379 0.3759 -0.0063 -0.0113 -0.0138 426 TRP C N   
11707 C CA  . TRP C 426 ? 0.4727 0.2058 0.3004 -0.0001 -0.0234 -0.0141 426 TRP C CA  
11708 C C   . TRP C 426 ? 0.5100 0.2079 0.2986 -0.0036 -0.0124 -0.0126 426 TRP C C   
11709 O O   . TRP C 426 ? 0.5500 0.2398 0.3081 0.0013  -0.0273 -0.0126 426 TRP C O   
11710 C CB  . TRP C 426 ? 0.4204 0.1568 0.2285 0.0032  -0.0209 -0.0133 426 TRP C CB  
11711 C CG  . TRP C 426 ? 0.3892 0.1580 0.2262 0.0078  -0.0359 -0.0131 426 TRP C CG  
11712 C CD1 . TRP C 426 ? 0.4267 0.2091 0.3025 0.0065  -0.0279 -0.0119 426 TRP C CD1 
11713 C CD2 . TRP C 426 ? 0.4297 0.2197 0.2583 0.0148  -0.0605 -0.0132 426 TRP C CD2 
11714 N NE1 . TRP C 426 ? 0.4577 0.2670 0.3475 0.0117  -0.0478 -0.0101 426 TRP C NE1 
11715 C CE2 . TRP C 426 ? 0.4512 0.2657 0.3110 0.0163  -0.0669 -0.0111 426 TRP C CE2 
11716 C CE3 . TRP C 426 ? 0.3994 0.1895 0.1978 0.0204  -0.0765 -0.0145 426 TRP C CE3 
11717 C CZ2 . TRP C 426 ? 0.4375 0.2750 0.2949 0.0220  -0.0878 -0.0098 426 TRP C CZ2 
11718 C CZ3 . TRP C 426 ? 0.3514 0.1662 0.1507 0.0268  -0.0955 -0.0145 426 TRP C CZ3 
11719 C CH2 . TRP C 426 ? 0.4595 0.2971 0.2859 0.0269  -0.1005 -0.0120 426 TRP C CH2 
11720 N N   . LYS C 427 ? 0.5419 0.2173 0.3311 -0.0117 0.0146  -0.0107 427 LYS C N   
11721 C CA  . LYS C 427 ? 0.5236 0.1623 0.2752 -0.0165 0.0267  -0.0076 427 LYS C CA  
11722 C C   . LYS C 427 ? 0.5593 0.1958 0.3266 -0.0181 0.0162  -0.0075 427 LYS C C   
11723 O O   . LYS C 427 ? 0.6432 0.2573 0.3735 -0.0159 0.0086  -0.0052 427 LYS C O   
11724 C CB  . LYS C 427 ? 0.5832 0.1993 0.3363 -0.0259 0.0611  -0.0057 427 LYS C CB  
11725 C CG  . LYS C 427 ? 0.6711 0.2600 0.3684 -0.0264 0.0739  -0.0049 427 LYS C CG  
11726 C CD  . LYS C 427 ? 0.8066 0.3637 0.4934 -0.0363 0.1107  -0.0031 427 LYS C CD  
11727 C CE  . LYS C 427 ? 0.6882 0.2573 0.4102 -0.0379 0.1332  -0.0075 427 LYS C CE  
11728 N NZ  . LYS C 427 ? 0.7839 0.3487 0.4716 -0.0337 0.1299  -0.0113 427 LYS C NZ  
11729 N N   . ILE C 428 ? 0.5057 0.1641 0.3287 -0.0221 0.0144  -0.0098 428 ILE C N   
11730 C CA  . ILE C 428 ? 0.5087 0.1651 0.3493 -0.0250 0.0023  -0.0114 428 ILE C CA  
11731 C C   . ILE C 428 ? 0.4969 0.1608 0.3134 -0.0145 -0.0269 -0.0152 428 ILE C C   
11732 O O   . ILE C 428 ? 0.5344 0.1787 0.3314 -0.0134 -0.0347 -0.0158 428 ILE C O   
11733 C CB  . ILE C 428 ? 0.4897 0.1718 0.3974 -0.0318 0.0019  -0.0135 428 ILE C CB  
11734 C CG1 . ILE C 428 ? 0.5049 0.1792 0.4419 -0.0418 0.0345  -0.0095 428 ILE C CG1 
11735 C CG2 . ILE C 428 ? 0.5349 0.2152 0.4593 -0.0355 -0.0152 -0.0169 428 ILE C CG2 
11736 C CD1 . ILE C 428 ? 0.4894 0.1893 0.4993 -0.0492 0.0343  -0.0103 428 ILE C CD1 
11737 N N   . LEU C 429 ? 0.5291 0.2204 0.3474 -0.0063 -0.0419 -0.0178 429 LEU C N   
11738 C CA  . LEU C 429 ? 0.4580 0.1594 0.2557 0.0042  -0.0664 -0.0217 429 LEU C CA  
11739 C C   . LEU C 429 ? 0.5038 0.1819 0.2505 0.0108  -0.0676 -0.0189 429 LEU C C   
11740 O O   . LEU C 429 ? 0.4949 0.1664 0.2253 0.0177  -0.0819 -0.0216 429 LEU C O   
11741 C CB  . LEU C 429 ? 0.4268 0.1615 0.2369 0.0100  -0.0783 -0.0232 429 LEU C CB  
11742 C CG  . LEU C 429 ? 0.4157 0.1654 0.2105 0.0202  -0.1012 -0.0276 429 LEU C CG  
11743 C CD1 . LEU C 429 ? 0.4144 0.1717 0.2343 0.0178  -0.1151 -0.0337 429 LEU C CD1 
11744 C CD2 . LEU C 429 ? 0.3919 0.1679 0.1865 0.0255  -0.1076 -0.0260 429 LEU C CD2 
11745 N N   . ILE C 430 ? 0.5408 0.2054 0.2619 0.0092  -0.0536 -0.0138 430 ILE C N   
11746 C CA  . ILE C 430 ? 0.5125 0.1565 0.1854 0.0153  -0.0583 -0.0099 430 ILE C CA  
11747 C C   . ILE C 430 ? 0.5664 0.1763 0.2203 0.0134  -0.0555 -0.0068 430 ILE C C   
11748 O O   . ILE C 430 ? 0.6307 0.2316 0.2611 0.0223  -0.0701 -0.0060 430 ILE C O   
11749 C CB  . ILE C 430 ? 0.5248 0.1581 0.1719 0.0116  -0.0447 -0.0058 430 ILE C CB  
11750 C CG1 . ILE C 430 ? 0.5155 0.1802 0.1720 0.0165  -0.0543 -0.0083 430 ILE C CG1 
11751 C CG2 . ILE C 430 ? 0.5608 0.1626 0.1562 0.0138  -0.0468 0.0001  430 ILE C CG2 
11752 C CD1 . ILE C 430 ? 0.5365 0.1959 0.1878 0.0101  -0.0371 -0.0074 430 ILE C CD1 
11753 N N   . GLU C 431 ? 0.6958 0.2863 0.3623 0.0020  -0.0361 -0.0044 431 GLU C N   
11754 C CA  . GLU C 431 ? 0.6051 0.1614 0.2563 -0.0015 -0.0323 -0.0005 431 GLU C CA  
11755 C C   . GLU C 431 ? 0.5924 0.1560 0.2629 0.0038  -0.0514 -0.0067 431 GLU C C   
11756 O O   . GLU C 431 ? 0.6155 0.1568 0.2616 0.0096  -0.0604 -0.0048 431 GLU C O   
11757 C CB  . GLU C 431 ? 0.6354 0.1735 0.3036 -0.0163 -0.0053 0.0033  431 GLU C CB  
11758 C CG  . GLU C 431 ? 0.8750 0.3750 0.5023 -0.0216 0.0104  0.0125  431 GLU C CG  
11759 C CD  . GLU C 431 ? 1.0557 0.5451 0.6325 -0.0172 0.0115  0.0167  431 GLU C CD  
11760 O OE1 . GLU C 431 ? 1.0968 0.5994 0.6739 -0.0157 0.0127  0.0137  431 GLU C OE1 
11761 O OE2 . GLU C 431 ? 0.9990 0.4667 0.5366 -0.0158 0.0098  0.0224  431 GLU C OE2 
11762 N N   . ALA C 432 ? 0.5621 0.1558 0.2753 0.0021  -0.0585 -0.0143 432 ALA C N   
11763 C CA  . ALA C 432 ? 0.5574 0.1568 0.2851 0.0064  -0.0774 -0.0223 432 ALA C CA  
11764 C C   . ALA C 432 ? 0.5641 0.1718 0.2648 0.0223  -0.0963 -0.0258 432 ALA C C   
11765 O O   . ALA C 432 ? 0.6898 0.2845 0.3821 0.0288  -0.1079 -0.0304 432 ALA C O   
11766 C CB  . ALA C 432 ? 0.5347 0.1648 0.3095 0.0005  -0.0832 -0.0290 432 ALA C CB  
11767 N N   . LYS C 433 ? 0.5297 0.1587 0.2193 0.0288  -0.0985 -0.0238 433 LYS C N   
11768 C CA  . LYS C 433 ? 0.5225 0.1630 0.1914 0.0435  -0.1142 -0.0260 433 LYS C CA  
11769 C C   . LYS C 433 ? 0.5898 0.1993 0.2261 0.0508  -0.1171 -0.0211 433 LYS C C   
11770 O O   . LYS C 433 ? 0.6179 0.2319 0.2559 0.0624  -0.1276 -0.0235 433 LYS C O   
11771 C CB  . LYS C 433 ? 0.5236 0.1954 0.1993 0.0457  -0.1100 -0.0207 433 LYS C CB  
11772 C CG  . LYS C 433 ? 0.4604 0.1716 0.1642 0.0555  -0.1111 -0.0214 433 LYS C CG  
11773 C CD  . LYS C 433 ? 0.5018 0.2173 0.2143 0.0632  -0.1204 -0.0278 433 LYS C CD  
11774 C CE  . LYS C 433 ? 0.5840 0.3344 0.3177 0.0708  -0.1175 -0.0294 433 LYS C CE  
11775 N NZ  . LYS C 433 ? 0.6154 0.4004 0.3741 0.0663  -0.1143 -0.0305 433 LYS C NZ  
11776 N N   . LYS C 434 ? 0.6951 0.2768 0.3093 0.0444  -0.1048 -0.0116 434 LYS C N   
11777 C CA  . LYS C 434 ? 0.6093 0.1697 0.1945 0.0502  -0.1079 -0.0064 434 LYS C CA  
11778 C C   . LYS C 434 ? 0.6456 0.1908 0.2343 0.0547  -0.1148 -0.0089 434 LYS C C   
11779 O O   . LYS C 434 ? 0.7119 0.2529 0.2883 0.0642  -0.1228 -0.0094 434 LYS C O   
11780 C CB  . LYS C 434 ? 0.6369 0.1737 0.1994 0.0389  -0.0911 0.0027  434 LYS C CB  
11781 C CG  . LYS C 434 ? 0.6733 0.2282 0.2338 0.0371  -0.0857 0.0026  434 LYS C CG  
11782 C CD  . LYS C 434 ? 0.7069 0.2329 0.2367 0.0270  -0.0704 0.0095  434 LYS C CD  
11783 C CE  . LYS C 434 ? 0.8215 0.3294 0.3490 0.0144  -0.0495 0.0142  434 LYS C CE  
11784 N NZ  . LYS C 434 ? 0.9506 0.4374 0.4497 0.0046  -0.0303 0.0183  434 LYS C NZ  
11785 N N   . LYS C 435 ? 0.6271 0.1700 0.2422 0.0464  -0.1101 -0.0134 435 LYS C N   
11786 C CA  . LYS C 435 ? 0.6838 0.2156 0.3076 0.0488  -0.1157 -0.0177 435 LYS C CA  
11787 C C   . LYS C 435 ? 0.6223 0.1763 0.2760 0.0493  -0.1247 -0.0303 435 LYS C C   
11788 O O   . LYS C 435 ? 0.7173 0.2621 0.3880 0.0433  -0.1250 -0.0352 435 LYS C O   
11789 C CB  . LYS C 435 ? 0.8053 0.3085 0.4313 0.0352  -0.1010 -0.0110 435 LYS C CB  
11790 C CG  . LYS C 435 ? 0.8655 0.3467 0.4586 0.0322  -0.0900 0.0017  435 LYS C CG  
11791 C CD  . LYS C 435 ? 0.9632 0.4292 0.5309 0.0439  -0.1006 0.0055  435 LYS C CD  
11792 C CE  . LYS C 435 ? 0.9050 0.3436 0.4436 0.0370  -0.0891 0.0176  435 LYS C CE  
11793 N NZ  . LYS C 435 ? 0.8993 0.3414 0.4116 0.0468  -0.0991 0.0203  435 LYS C NZ  
11794 N N   . ALA C 436 ? 0.3686 0.3751 0.2912 -0.1087 -0.0431 0.0273  436 ALA C N   
11795 C CA  . ALA C 436 ? 0.3076 0.3345 0.2370 -0.1043 -0.0367 0.0206  436 ALA C CA  
11796 C C   . ALA C 436 ? 0.3468 0.3969 0.3005 -0.1018 -0.0313 0.0173  436 ALA C C   
11797 O O   . ALA C 436 ? 0.4095 0.4686 0.3765 -0.1054 -0.0339 0.0245  436 ALA C O   
11798 C CB  . ALA C 436 ? 0.3760 0.4027 0.2914 -0.1088 -0.0411 0.0275  436 ALA C CB  
11799 N N   . LYS C 437 ? 0.4042 0.4639 0.3663 -0.0958 -0.0234 0.0054  437 LYS C N   
11800 C CA  . LYS C 437 ? 0.3775 0.4549 0.3633 -0.0925 -0.0160 -0.0010 437 LYS C CA  
11801 C C   . LYS C 437 ? 0.3475 0.4428 0.3307 -0.0920 -0.0076 -0.0087 437 LYS C C   
11802 O O   . LYS C 437 ? 0.4108 0.5202 0.4122 -0.0894 0.0016  -0.0166 437 LYS C O   
11803 C CB  . LYS C 437 ? 0.3103 0.3812 0.3073 -0.0872 -0.0128 -0.0098 437 LYS C CB  
11804 C CG  . LYS C 437 ? 0.2526 0.3170 0.2680 -0.0869 -0.0168 -0.0036 437 LYS C CG  
11805 C CD  . LYS C 437 ? 0.3221 0.3610 0.3183 -0.0918 -0.0264 0.0067  437 LYS C CD  
11806 C CE  . LYS C 437 ? 0.6050 0.6310 0.6132 -0.0916 -0.0323 0.0120  437 LYS C CE  
11807 N NZ  . LYS C 437 ? 0.5161 0.5158 0.5006 -0.0991 -0.0441 0.0246  437 LYS C NZ  
11808 N N   . ASN C 438 ? 0.3825 0.4753 0.3422 -0.0949 -0.0106 -0.0067 438 ASN C N   
11809 C CA  . ASN C 438 ? 0.2738 0.3788 0.2220 -0.0968 -0.0042 -0.0121 438 ASN C CA  
11810 C C   . ASN C 438 ? 0.3019 0.4004 0.2253 -0.1029 -0.0110 -0.0013 438 ASN C C   
11811 O O   . ASN C 438 ? 0.4355 0.5219 0.3552 -0.1051 -0.0193 0.0090  438 ASN C O   
11812 C CB  . ASN C 438 ? 0.3303 0.4358 0.2738 -0.0921 -0.0028 -0.0265 438 ASN C CB  
11813 C CG  . ASN C 438 ? 0.3536 0.4456 0.2871 -0.0897 -0.0136 -0.0262 438 ASN C CG  
11814 O OD1 . ASN C 438 ? 0.3538 0.4402 0.2683 -0.0921 -0.0215 -0.0203 438 ASN C OD1 
11815 N ND2 . ASN C 438 ? 0.3836 0.4698 0.3324 -0.0852 -0.0135 -0.0325 438 ASN C ND2 
11816 N N   . ASP C 439 ? 0.3208 0.4243 0.2243 -0.1064 -0.0076 -0.0037 439 ASP C N   
11817 C CA  . ASP C 439 ? 0.4376 0.5342 0.3164 -0.1137 -0.0130 0.0081  439 ASP C CA  
11818 C C   . ASP C 439 ? 0.3582 0.4380 0.2195 -0.1111 -0.0282 0.0113  439 ASP C C   
11819 O O   . ASP C 439 ? 0.3310 0.4010 0.1727 -0.1164 -0.0352 0.0223  439 ASP C O   
11820 C CB  . ASP C 439 ? 0.4256 0.5310 0.2849 -0.1204 -0.0024 0.0055  439 ASP C CB  
11821 C CG  . ASP C 439 ? 0.6791 0.8004 0.5576 -0.1257 0.0138  0.0071  439 ASP C CG  
11822 O OD1 . ASP C 439 ? 0.6807 0.8031 0.5792 -0.1274 0.0108  0.0169  439 ASP C OD1 
11823 O OD2 . ASP C 439 ? 0.6433 0.7754 0.5178 -0.1285 0.0294  -0.0020 439 ASP C OD2 
11824 N N   . TYR C 440 ? 0.3024 0.3783 0.1737 -0.1034 -0.0331 0.0022  440 TYR C N   
11825 C CA  . TYR C 440 ? 0.3118 0.3739 0.1763 -0.0999 -0.0466 0.0044  440 TYR C CA  
11826 C C   . TYR C 440 ? 0.3580 0.4052 0.2230 -0.1010 -0.0516 0.0152  440 TYR C C   
11827 O O   . TYR C 440 ? 0.4141 0.4483 0.2717 -0.0994 -0.0622 0.0196  440 TYR C O   
11828 C CB  . TYR C 440 ? 0.4130 0.4761 0.2959 -0.0921 -0.0479 -0.0084 440 TYR C CB  
11829 C CG  . TYR C 440 ? 0.4568 0.5268 0.3328 -0.0911 -0.0522 -0.0183 440 TYR C CG  
11830 C CD1 . TYR C 440 ? 0.5281 0.5910 0.3932 -0.0900 -0.0679 -0.0164 440 TYR C CD1 
11831 C CD2 . TYR C 440 ? 0.4173 0.4991 0.2982 -0.0912 -0.0421 -0.0298 440 TYR C CD2 
11832 C CE1 . TYR C 440 ? 0.5468 0.6138 0.4025 -0.0904 -0.0754 -0.0251 440 TYR C CE1 
11833 C CE2 . TYR C 440 ? 0.4729 0.5581 0.3434 -0.0916 -0.0469 -0.0401 440 TYR C CE2 
11834 C CZ  . TYR C 440 ? 0.6332 0.7108 0.4895 -0.0917 -0.0645 -0.0375 440 TYR C CZ  
11835 O OH  . TYR C 440 ? 0.6240 0.7028 0.4670 -0.0934 -0.0727 -0.0475 440 TYR C OH  
11836 N N   . ILE C 441 ? 0.3403 0.3876 0.2146 -0.1039 -0.0455 0.0192  441 ILE C N   
11837 C CA  . ILE C 441 ? 0.3704 0.4008 0.2401 -0.1070 -0.0509 0.0289  441 ILE C CA  
11838 C C   . ILE C 441 ? 0.3295 0.3537 0.1801 -0.1136 -0.0572 0.0407  441 ILE C C   
11839 O O   . ILE C 441 ? 0.3189 0.3247 0.1618 -0.1147 -0.0648 0.0472  441 ILE C O   
11840 C CB  . ILE C 441 ? 0.3860 0.4174 0.2669 -0.1105 -0.0466 0.0319  441 ILE C CB  
11841 C CG1 . ILE C 441 ? 0.2772 0.2863 0.1493 -0.1142 -0.0532 0.0392  441 ILE C CG1 
11842 C CG2 . ILE C 441 ? 0.4241 0.4728 0.3107 -0.1169 -0.0414 0.0372  441 ILE C CG2 
11843 C CD1 . ILE C 441 ? 0.2737 0.2661 0.1462 -0.1089 -0.0520 0.0317  441 ILE C CD1 
11844 N N   . LEU C 442 ? 0.3378 0.3749 0.1790 -0.1187 -0.0529 0.0431  442 LEU C N   
11845 C CA  . LEU C 442 ? 0.3294 0.3584 0.1482 -0.1264 -0.0582 0.0550  442 LEU C CA  
11846 C C   . LEU C 442 ? 0.3450 0.3584 0.1496 -0.1218 -0.0720 0.0563  442 LEU C C   
11847 O O   . LEU C 442 ? 0.3866 0.3824 0.1852 -0.1229 -0.0794 0.0656  442 LEU C O   
11848 C CB  . LEU C 442 ? 0.3866 0.4312 0.1948 -0.1338 -0.0472 0.0555  442 LEU C CB  
11849 C CG  . LEU C 442 ? 0.3717 0.4338 0.2005 -0.1391 -0.0333 0.0556  442 LEU C CG  
11850 C CD1 . LEU C 442 ? 0.3529 0.4257 0.1679 -0.1491 -0.0204 0.0586  442 LEU C CD1 
11851 C CD2 . LEU C 442 ? 0.3393 0.3929 0.1801 -0.1432 -0.0390 0.0656  442 LEU C CD2 
11852 N N   . VAL C 443 ? 0.3416 0.3607 0.1505 -0.1143 -0.0747 0.0455  443 VAL C N   
11853 C CA  . VAL C 443 ? 0.3563 0.3628 0.1598 -0.1089 -0.0905 0.0463  443 VAL C CA  
11854 C C   . VAL C 443 ? 0.3474 0.3389 0.1691 -0.1023 -0.0958 0.0463  443 VAL C C   
11855 O O   . VAL C 443 ? 0.3644 0.3398 0.1826 -0.0998 -0.1090 0.0527  443 VAL C O   
11856 C CB  . VAL C 443 ? 0.3542 0.3719 0.1635 -0.1032 -0.0932 0.0334  443 VAL C CB  
11857 C CG1 . VAL C 443 ? 0.4260 0.4320 0.2265 -0.0996 -0.1121 0.0369  443 VAL C CG1 
11858 C CG2 . VAL C 443 ? 0.4383 0.4716 0.2347 -0.1092 -0.0808 0.0279  443 VAL C CG2 
11859 N N   . ALA C 444 ? 0.3252 0.3192 0.1653 -0.0996 -0.0854 0.0392  444 ALA C N   
11860 C CA  . ALA C 444 ? 0.3217 0.2992 0.1750 -0.0945 -0.0862 0.0368  444 ALA C CA  
11861 C C   . ALA C 444 ? 0.3366 0.2943 0.1765 -0.1003 -0.0901 0.0483  444 ALA C C   
11862 O O   . ALA C 444 ? 0.3414 0.2809 0.1882 -0.0966 -0.0911 0.0461  444 ALA C O   
11863 C CB  . ALA C 444 ? 0.3170 0.2987 0.1851 -0.0927 -0.0734 0.0269  444 ALA C CB  
11864 N N   . GLU C 445 ? 0.3496 0.3097 0.1718 -0.1099 -0.0911 0.0596  445 GLU C N   
11865 C CA  . GLU C 445 ? 0.3625 0.3039 0.1725 -0.1173 -0.0955 0.0711  445 GLU C CA  
11866 C C   . GLU C 445 ? 0.3886 0.3167 0.1853 -0.1183 -0.1077 0.0814  445 GLU C C   
11867 O O   . GLU C 445 ? 0.4485 0.3617 0.2397 -0.1240 -0.1095 0.0900  445 GLU C O   
11868 C CB  . GLU C 445 ? 0.3573 0.3099 0.1658 -0.1274 -0.0873 0.0766  445 GLU C CB  
11869 C CG  . GLU C 445 ? 0.3517 0.3129 0.1714 -0.1278 -0.0799 0.0700  445 GLU C CG  
11870 C CD  . GLU C 445 ? 0.4544 0.4355 0.2797 -0.1358 -0.0732 0.0743  445 GLU C CD  
11871 O OE1 . GLU C 445 ? 0.5250 0.5190 0.3655 -0.1334 -0.0669 0.0676  445 GLU C OE1 
11872 O OE2 . GLU C 445 ? 0.4383 0.4221 0.2597 -0.1432 -0.0727 0.0827  445 GLU C OE2 
11873 N N   . GLY C 446 ? 0.3960 0.3286 0.1914 -0.1124 -0.1157 0.0796  446 GLY C N   
11874 C CA  . GLY C 446 ? 0.4242 0.3412 0.2104 -0.1117 -0.1284 0.0890  446 GLY C CA  
11875 C C   . GLY C 446 ? 0.4375 0.3272 0.2274 -0.1084 -0.1404 0.0940  446 GLY C C   
11876 O O   . GLY C 446 ? 0.4227 0.3097 0.2365 -0.0993 -0.1359 0.0822  446 GLY C O   
11877 N N   . SER C 447 ? 0.4629 0.3347 0.2426 -0.1131 -0.1464 0.1055  447 SER C N   
11878 C CA  . SER C 447 ? 0.4812 0.3224 0.2636 -0.1099 -0.1585 0.1111  447 SER C CA  
11879 C C   . SER C 447 ? 0.4861 0.3223 0.2943 -0.0947 -0.1701 0.1041  447 SER C C   
11880 O O   . SER C 447 ? 0.4878 0.3067 0.3175 -0.0866 -0.1702 0.0980  447 SER C O   
11881 C CB  . SER C 447 ? 0.5086 0.3343 0.2798 -0.1176 -0.1618 0.1226  447 SER C CB  
11882 O OG  . SER C 447 ? 0.5317 0.3555 0.2969 -0.1152 -0.1735 0.1289  447 SER C OG  
11883 N N   . ASP C 448 ? 0.5095 0.3603 0.3176 -0.0910 -0.1798 0.1039  448 ASP C N   
11884 C CA  . ASP C 448 ? 0.4931 0.3408 0.3300 -0.0773 -0.1952 0.0990  448 ASP C CA  
11885 C C   . ASP C 448 ? 0.4647 0.3221 0.3423 -0.0659 -0.1820 0.0794  448 ASP C C   
11886 O O   . ASP C 448 ? 0.5475 0.3982 0.4595 -0.0538 -0.1909 0.0740  448 ASP C O   
11887 C CB  . ASP C 448 ? 0.5036 0.3652 0.3274 -0.0782 -0.2094 0.1022  448 ASP C CB  
11888 C CG  . ASP C 448 ? 0.5276 0.3864 0.3161 -0.0900 -0.2041 0.1130  448 ASP C CG  
11889 O OD1 . ASP C 448 ? 0.5137 0.3869 0.2868 -0.0991 -0.1836 0.1104  448 ASP C OD1 
11890 O OD2 . ASP C 448 ? 0.5615 0.4041 0.3425 -0.0897 -0.2190 0.1227  448 ASP C OD2 
11891 N N   . TRP C 449 ? 0.4371 0.3095 0.3132 -0.0697 -0.1608 0.0690  449 TRP C N   
11892 C CA  . TRP C 449 ? 0.4155 0.2944 0.3245 -0.0612 -0.1462 0.0512  449 TRP C CA  
11893 C C   . TRP C 449 ? 0.4426 0.2971 0.3597 -0.0592 -0.1361 0.0467  449 TRP C C   
11894 O O   . TRP C 449 ? 0.4634 0.3153 0.4121 -0.0501 -0.1267 0.0328  449 TRP C O   
11895 C CB  . TRP C 449 ? 0.3885 0.2890 0.2902 -0.0664 -0.1292 0.0429  449 TRP C CB  
11896 C CG  . TRP C 449 ? 0.3852 0.3061 0.2711 -0.0709 -0.1359 0.0470  449 TRP C CG  
11897 C CD1 . TRP C 449 ? 0.3830 0.3124 0.2400 -0.0816 -0.1304 0.0538  449 TRP C CD1 
11898 C CD2 . TRP C 449 ? 0.3879 0.3219 0.2863 -0.0653 -0.1489 0.0435  449 TRP C CD2 
11899 N NE1 . TRP C 449 ? 0.3859 0.3313 0.2333 -0.0831 -0.1364 0.0535  449 TRP C NE1 
11900 C CE2 . TRP C 449 ? 0.3900 0.3374 0.2597 -0.0737 -0.1493 0.0476  449 TRP C CE2 
11901 C CE3 . TRP C 449 ? 0.3910 0.3266 0.3241 -0.0543 -0.1605 0.0367  449 TRP C CE3 
11902 C CZ2 . TRP C 449 ? 0.3982 0.3573 0.2658 -0.0725 -0.1614 0.0448  449 TRP C CZ2 
11903 C CZ3 . TRP C 449 ? 0.3966 0.3461 0.3321 -0.0530 -0.1754 0.0351  449 TRP C CZ3 
11904 C CH2 . TRP C 449 ? 0.4036 0.3630 0.3029 -0.0625 -0.1761 0.0390  449 TRP C CH2 
11905 N N   . PHE C 450 ? 0.4857 0.3215 0.3752 -0.0684 -0.1367 0.0572  450 PHE C N   
11906 C CA  . PHE C 450 ? 0.4920 0.3002 0.3831 -0.0683 -0.1285 0.0526  450 PHE C CA  
11907 C C   . PHE C 450 ? 0.5567 0.3397 0.4589 -0.0621 -0.1436 0.0595  450 PHE C C   
11908 O O   . PHE C 450 ? 0.4967 0.2555 0.4093 -0.0584 -0.1361 0.0518  450 PHE C O   
11909 C CB  . PHE C 450 ? 0.4548 0.2546 0.3118 -0.0828 -0.1217 0.0589  450 PHE C CB  
11910 C CG  . PHE C 450 ? 0.4293 0.2542 0.2751 -0.0896 -0.1120 0.0568  450 PHE C CG  
11911 C CD1 . PHE C 450 ? 0.4158 0.2431 0.2660 -0.0891 -0.0958 0.0435  450 PHE C CD1 
11912 C CD2 . PHE C 450 ? 0.4757 0.3197 0.3063 -0.0968 -0.1182 0.0680  450 PHE C CD2 
11913 C CE1 . PHE C 450 ? 0.4126 0.2608 0.2552 -0.0946 -0.0889 0.0425  450 PHE C CE1 
11914 C CE2 . PHE C 450 ? 0.4360 0.3027 0.2619 -0.1018 -0.1088 0.0650  450 PHE C CE2 
11915 C CZ  . PHE C 450 ? 0.3860 0.2548 0.2194 -0.1001 -0.0956 0.0528  450 PHE C CZ  
11916 N N   . TRP C 451 ? 0.5448 0.3304 0.4431 -0.0612 -0.1648 0.0738  451 TRP C N   
11917 C CA  . TRP C 451 ? 0.5552 0.3151 0.4657 -0.0547 -0.1828 0.0825  451 TRP C CA  
11918 C C   . TRP C 451 ? 0.5770 0.3354 0.5386 -0.0374 -0.1829 0.0683  451 TRP C C   
11919 O O   . TRP C 451 ? 0.6671 0.3999 0.6486 -0.0306 -0.1817 0.0641  451 TRP C O   
11920 C CB  . TRP C 451 ? 0.5457 0.3077 0.4357 -0.0589 -0.2066 0.1019  451 TRP C CB  
11921 C CG  . TRP C 451 ? 0.6441 0.3731 0.5248 -0.0603 -0.2248 0.1183  451 TRP C CG  
11922 C CD1 . TRP C 451 ? 0.7354 0.4457 0.5803 -0.0744 -0.2255 0.1327  451 TRP C CD1 
11923 C CD2 . TRP C 451 ? 0.6113 0.3212 0.5221 -0.0472 -0.2459 0.1226  451 TRP C CD2 
11924 N NE1 . TRP C 451 ? 0.6692 0.3479 0.5162 -0.0716 -0.2451 0.1461  451 TRP C NE1 
11925 C CE2 . TRP C 451 ? 0.6479 0.3253 0.5356 -0.0543 -0.2587 0.1404  451 TRP C CE2 
11926 C CE3 . TRP C 451 ? 0.6086 0.3261 0.5680 -0.0303 -0.2561 0.1133  451 TRP C CE3 
11927 C CZ2 . TRP C 451 ? 0.6831 0.3332 0.5924 -0.0443 -0.2821 0.1498  451 TRP C CZ2 
11928 C CZ3 . TRP C 451 ? 0.6421 0.3350 0.6270 -0.0199 -0.2798 0.1222  451 TRP C CZ3 
11929 C CH2 . TRP C 451 ? 0.7431 0.4017 0.7019 -0.0266 -0.2930 0.1406  451 TRP C CH2 
11930 N N   . TRP C 452 ? 0.5360 0.3218 0.5225 -0.0305 -0.1831 0.0596  452 TRP C N   
11931 C CA  . TRP C 452 ? 0.6109 0.4011 0.6533 -0.0144 -0.1873 0.0482  452 TRP C CA  
11932 C C   . TRP C 452 ? 0.6544 0.4453 0.7259 -0.0090 -0.1580 0.0259  452 TRP C C   
11933 O O   . TRP C 452 ? 0.6264 0.4321 0.7464 0.0021  -0.1543 0.0129  452 TRP C O   
11934 C CB  . TRP C 452 ? 0.6403 0.4592 0.6971 -0.0109 -0.2027 0.0491  452 TRP C CB  
11935 C CG  . TRP C 452 ? 0.6971 0.5096 0.7367 -0.0123 -0.2359 0.0691  452 TRP C CG  
11936 C CD1 . TRP C 452 ? 0.5461 0.3706 0.5450 -0.0227 -0.2473 0.0803  452 TRP C CD1 
11937 C CD2 . TRP C 452 ? 0.7410 0.5306 0.8012 -0.0036 -0.2618 0.0803  452 TRP C CD2 
11938 N NE1 . TRP C 452 ? 0.6883 0.4971 0.6752 -0.0225 -0.2786 0.0983  452 TRP C NE1 
11939 C CE2 . TRP C 452 ? 0.8160 0.6031 0.8410 -0.0105 -0.2897 0.0997  452 TRP C CE2 
11940 C CE3 . TRP C 452 ? 0.7919 0.5607 0.8964 0.0092  -0.2636 0.0756  452 TRP C CE3 
11941 C CZ2 . TRP C 452 ? 0.9624 0.7258 0.9930 -0.0055 -0.3221 0.1166  452 TRP C CZ2 
11942 C CZ3 . TRP C 452 ? 0.8569 0.6042 0.9735 0.0158  -0.2955 0.0914  452 TRP C CZ3 
11943 C CH2 . TRP C 452 ? 0.9893 0.7335 1.0681 0.0083  -0.3257 0.1127  452 TRP C CH2 
11944 N N   . GLN C 453 ? 0.7543 0.5285 0.7964 -0.0178 -0.1373 0.0212  453 GLN C N   
11945 C CA  . GLN C 453 ? 0.7847 0.5545 0.8425 -0.0157 -0.1077 0.0004  453 GLN C CA  
11946 C C   . GLN C 453 ? 0.7386 0.4766 0.8199 -0.0077 -0.1011 -0.0079 453 GLN C C   
11947 O O   . GLN C 453 ? 0.6901 0.4013 0.7447 -0.0146 -0.0855 -0.0133 453 GLN C O   
11948 C CB  . GLN C 453 ? 0.6202 0.3881 0.6298 -0.0308 -0.0906 -0.0006 453 GLN C CB  
11949 C CG  . GLN C 453 ? 0.5056 0.3042 0.5129 -0.0342 -0.0817 -0.0054 453 GLN C CG  
11950 C CD  . GLN C 453 ? 0.6338 0.4519 0.6928 -0.0223 -0.0760 -0.0190 453 GLN C CD  
11951 O OE1 . GLN C 453 ? 0.8270 0.6388 0.9068 -0.0192 -0.0527 -0.0358 453 GLN C OE1 
11952 N NE2 . GLN C 453 ? 0.5725 0.4134 0.6516 -0.0169 -0.0968 -0.0122 453 GLN C NE2 
11953 N N   . GLY C 454 ? 0.7288 0.4692 0.8626 0.0073  -0.1142 -0.0095 454 GLY C N   
11954 C CA  . GLY C 454 ? 0.7854 0.4990 0.9557 0.0182  -0.1066 -0.0202 454 GLY C CA  
11955 C C   . GLY C 454 ? 0.9819 0.6675 1.1449 0.0204  -0.1316 -0.0037 454 GLY C C   
11956 O O   . GLY C 454 ? 0.9317 0.6222 1.0749 0.0168  -0.1601 0.0175  454 GLY C O   
11957 N N   . GLU C 455 ? 1.1067 0.7598 1.2865 0.0262  -0.1194 -0.0144 455 GLU C N   
11958 C CA  . GLU C 455 ? 1.1923 0.8108 1.3706 0.0292  -0.1381 -0.0027 455 GLU C CA  
11959 C C   . GLU C 455 ? 1.0281 0.6515 1.2631 0.0461  -0.1676 0.0065  455 GLU C C   
11960 O O   . GLU C 455 ? 1.0911 0.6842 1.3442 0.0537  -0.1820 0.0126  455 GLU C O   
11961 C CB  . GLU C 455 ? 1.1534 0.7611 1.2650 0.0116  -0.1537 0.0194  455 GLU C CB  
11962 C CG  . GLU C 455 ? 1.1784 0.7452 1.2793 0.0107  -0.1687 0.0310  455 GLU C CG  
11963 C CD  . GLU C 455 ? 1.2888 0.8205 1.3859 0.0095  -0.1434 0.0122  455 GLU C CD  
11964 O OE1 . GLU C 455 ? 1.2605 0.7903 1.3158 -0.0044 -0.1222 0.0035  455 GLU C OE1 
11965 O OE2 . GLU C 455 ? 1.0673 0.5716 1.2028 0.0222  -0.1453 0.0058  455 GLU C OE2 
11966 N N   . GLU C 456 ? 0.9926 0.6524 1.2586 0.0523  -0.1773 0.0065  456 GLU C N   
11967 C CA  . GLU C 456 ? 1.0733 0.7421 1.3994 0.0686  -0.2067 0.0132  456 GLU C CA  
11968 C C   . GLU C 456 ? 0.9834 0.6954 1.3366 0.0711  -0.2073 0.0068  456 GLU C C   
11969 O O   . GLU C 456 ? 0.9147 0.6467 1.2210 0.0578  -0.2027 0.0108  456 GLU C O   
11970 C CB  . GLU C 456 ? 1.1204 0.7713 1.4171 0.0652  -0.2470 0.0424  456 GLU C CB  
11971 C CG  . GLU C 456 ? 0.9692 0.6411 1.2117 0.0511  -0.2651 0.0609  456 GLU C CG  
11972 C CD  . GLU C 456 ? 0.8991 0.5822 1.1672 0.0590  -0.3045 0.0761  456 GLU C CD  
11973 O OE1 . GLU C 456 ? 0.8678 0.5686 1.0953 0.0484  -0.3187 0.0883  456 GLU C OE1 
11974 O OE2 . GLU C 456 ? 0.8227 0.4968 1.1510 0.0753  -0.3213 0.0749  456 GLU C OE2 
11975 N N   . LYS C 457 ? 0.7813 0.5082 1.2131 0.0880  -0.2121 -0.0042 457 LYS C N   
11976 C CA  . LYS C 457 ? 0.8664 0.6340 1.3283 0.0897  -0.2131 -0.0114 457 LYS C CA  
11977 C C   . LYS C 457 ? 0.9174 0.6966 1.3626 0.0874  -0.2577 0.0119  457 LYS C C   
11978 O O   . LYS C 457 ? 0.8853 0.6501 1.3558 0.0968  -0.2923 0.0262  457 LYS C O   
11979 C CB  . LYS C 457 ? 0.9028 0.6848 1.4594 0.1070  -0.2000 -0.0329 457 LYS C CB  
11980 C CG  . LYS C 457 ? 0.7805 0.6046 1.3703 0.1068  -0.1954 -0.0432 457 LYS C CG  
11981 C CD  . LYS C 457 ? 0.6443 0.4804 1.1700 0.0892  -0.1672 -0.0486 457 LYS C CD  
11982 C CE  . LYS C 457 ? 0.5739 0.3931 1.0868 0.0848  -0.1198 -0.0685 457 LYS C CE  
11983 N NZ  . LYS C 457 ? 0.8324 0.6545 1.4278 0.0990  -0.0961 -0.0912 457 LYS C NZ  
11984 N N   . ALA C 458 ? 0.9472 0.7497 1.3480 0.0745  -0.2568 0.0153  458 ALA C N   
11985 C CA  . ALA C 458 ? 0.8414 0.6505 1.2004 0.0664  -0.2915 0.0364  458 ALA C CA  
11986 C C   . ALA C 458 ? 0.9114 0.7563 1.3054 0.0692  -0.3022 0.0291  458 ALA C C   
11987 O O   . ALA C 458 ? 0.8671 0.7344 1.3041 0.0733  -0.2760 0.0081  458 ALA C O   
11988 C CB  . ALA C 458 ? 0.8036 0.6079 1.0765 0.0472  -0.2779 0.0451  458 ALA C CB  
11989 N N   . PRO C 459 ? 0.9730 0.8220 1.3475 0.0660  -0.3404 0.0460  459 PRO C N   
11990 C CA  . PRO C 459 ? 0.8296 0.7110 1.2347 0.0672  -0.3530 0.0385  459 PRO C CA  
11991 C C   . PRO C 459 ? 0.7606 0.6633 1.1197 0.0531  -0.3280 0.0299  459 PRO C C   
11992 O O   . PRO C 459 ? 0.6772 0.5703 0.9628 0.0393  -0.3216 0.0400  459 PRO C O   
11993 C CB  . PRO C 459 ? 0.7445 0.6139 1.1169 0.0605  -0.3911 0.0575  459 PRO C CB  
11994 C CG  . PRO C 459 ? 0.9140 0.7536 1.2101 0.0495  -0.3945 0.0770  459 PRO C CG  
11995 C CD  . PRO C 459 ? 0.7954 0.6203 1.1000 0.0554  -0.3692 0.0724  459 PRO C CD  
11996 N N   . PHE C 460 ? 0.7458 0.6773 1.1538 0.0568  -0.3124 0.0106  460 PHE C N   
11997 C CA  . PHE C 460 ? 0.7268 0.6801 1.1027 0.0450  -0.2906 0.0009  460 PHE C CA  
11998 C C   . PHE C 460 ? 0.6799 0.6215 1.0035 0.0355  -0.2538 -0.0017 460 PHE C C   
11999 O O   . PHE C 460 ? 0.6548 0.5950 0.9138 0.0227  -0.2508 0.0063  460 PHE C O   
12000 C CB  . PHE C 460 ? 0.7621 0.7206 1.0887 0.0349  -0.3208 0.0139  460 PHE C CB  
12001 C CG  . PHE C 460 ? 0.8169 0.7694 1.1648 0.0403  -0.3613 0.0244  460 PHE C CG  
12002 C CD1 . PHE C 460 ? 0.6794 0.6487 1.0932 0.0480  -0.3664 0.0123  460 PHE C CD1 
12003 C CD2 . PHE C 460 ? 0.8541 0.7780 1.1436 0.0335  -0.3808 0.0450  460 PHE C CD2 
12004 C CE1 . PHE C 460 ? 0.6892 0.6469 1.1106 0.0495  -0.3947 0.0210  460 PHE C CE1 
12005 C CE2 . PHE C 460 ? 0.9332 0.8455 1.2298 0.0348  -0.4075 0.0533  460 PHE C CE2 
12006 C CZ  . PHE C 460 ? 0.7918 0.7208 1.1543 0.0430  -0.4163 0.0416  460 PHE C CZ  
12007 N N   . VAL C 461 ? 0.6794 0.6119 1.0336 0.0417  -0.2256 -0.0137 461 VAL C N   
12008 C CA  . VAL C 461 ? 0.5841 0.5052 0.8924 0.0322  -0.1914 -0.0181 461 VAL C CA  
12009 C C   . VAL C 461 ? 0.4291 0.3729 0.7280 0.0242  -0.1681 -0.0305 461 VAL C C   
12010 O O   . VAL C 461 ? 0.5387 0.4783 0.7837 0.0128  -0.1521 -0.0280 461 VAL C O   
12011 C CB  . VAL C 461 ? 0.5152 0.4159 0.8522 0.0395  -0.1674 -0.0289 461 VAL C CB  
12012 C CG1 . VAL C 461 ? 0.7826 0.6520 1.0980 0.0416  -0.1844 -0.0136 461 VAL C CG1 
12013 C CG2 . VAL C 461 ? 0.7138 0.6284 1.1361 0.0535  -0.1620 -0.0454 461 VAL C CG2 
12014 N N   . GLU C 462 ? 0.3822 0.3499 0.7364 0.0297  -0.1668 -0.0435 462 GLU C N   
12015 C CA  . GLU C 462 ? 0.4778 0.4655 0.8257 0.0219  -0.1460 -0.0548 462 GLU C CA  
12016 C C   . GLU C 462 ? 0.4226 0.4181 0.7147 0.0113  -0.1616 -0.0440 462 GLU C C   
12017 O O   . GLU C 462 ? 0.4560 0.4558 0.7136 0.0019  -0.1416 -0.0475 462 GLU C O   
12018 C CB  . GLU C 462 ? 0.5329 0.5448 0.9556 0.0292  -0.1446 -0.0701 462 GLU C CB  
12019 C CG  . GLU C 462 ? 0.7072 0.7412 1.1268 0.0208  -0.1321 -0.0796 462 GLU C CG  
12020 C CD  . GLU C 462 ? 0.8174 0.8682 1.2299 0.0181  -0.1657 -0.0730 462 GLU C CD  
12021 O OE1 . GLU C 462 ? 0.8701 0.9123 1.2621 0.0200  -0.1980 -0.0583 462 GLU C OE1 
12022 O OE2 . GLU C 462 ? 0.7217 0.7915 1.1452 0.0129  -0.1593 -0.0826 462 GLU C OE2 
12023 N N   . VAL C 463 ? 0.5003 0.4958 0.7822 0.0124  -0.1971 -0.0310 463 VAL C N   
12024 C CA  . VAL C 463 ? 0.4419 0.4433 0.6699 0.0018  -0.2101 -0.0225 463 VAL C CA  
12025 C C   . VAL C 463 ? 0.3716 0.3580 0.5354 -0.0081 -0.1948 -0.0132 463 VAL C C   
12026 O O   . VAL C 463 ? 0.4269 0.4220 0.5564 -0.0172 -0.1825 -0.0152 463 VAL C O   
12027 C CB  . VAL C 463 ? 0.4055 0.4038 0.6283 0.0035  -0.2515 -0.0095 463 VAL C CB  
12028 C CG1 . VAL C 463 ? 0.4931 0.4915 0.6493 -0.0092 -0.2602 -0.0008 463 VAL C CG1 
12029 C CG2 . VAL C 463 ? 0.4028 0.4199 0.6904 0.0116  -0.2701 -0.0191 463 VAL C CG2 
12030 N N   . PHE C 464 ? 0.3872 0.3508 0.5373 -0.0065 -0.1961 -0.0032 464 PHE C N   
12031 C CA  . PHE C 464 ? 0.4132 0.3628 0.5083 -0.0165 -0.1827 0.0057  464 PHE C CA  
12032 C C   . PHE C 464 ? 0.3702 0.3242 0.4621 -0.0207 -0.1496 -0.0065 464 PHE C C   
12033 O O   . PHE C 464 ? 0.3959 0.3521 0.4475 -0.0305 -0.1394 -0.0030 464 PHE C O   
12034 C CB  . PHE C 464 ? 0.4110 0.3334 0.4983 -0.0140 -0.1903 0.0172  464 PHE C CB  
12035 C CG  . PHE C 464 ? 0.4509 0.3616 0.5034 -0.0184 -0.2188 0.0368  464 PHE C CG  
12036 C CD1 . PHE C 464 ? 0.4560 0.3645 0.4514 -0.0317 -0.2165 0.0477  464 PHE C CD1 
12037 C CD2 . PHE C 464 ? 0.6130 0.5139 0.6906 -0.0098 -0.2477 0.0445  464 PHE C CD2 
12038 C CE1 . PHE C 464 ? 0.5797 0.4752 0.5388 -0.0377 -0.2396 0.0657  464 PHE C CE1 
12039 C CE2 . PHE C 464 ? 0.6677 0.5535 0.7070 -0.0155 -0.2747 0.0641  464 PHE C CE2 
12040 C CZ  . PHE C 464 ? 0.7252 0.6076 0.7025 -0.0302 -0.2692 0.0746  464 PHE C CZ  
12041 N N   . ASP C 465 ? 0.3800 0.3342 0.5147 -0.0138 -0.1324 -0.0207 465 ASP C N   
12042 C CA  . ASP C 465 ? 0.4388 0.3930 0.5665 -0.0189 -0.1017 -0.0317 465 ASP C CA  
12043 C C   . ASP C 465 ? 0.3902 0.3672 0.5157 -0.0238 -0.0964 -0.0380 465 ASP C C   
12044 O O   . ASP C 465 ? 0.4024 0.3791 0.4948 -0.0323 -0.0825 -0.0372 465 ASP C O   
12045 C CB  . ASP C 465 ? 0.4747 0.4213 0.6466 -0.0116 -0.0822 -0.0461 465 ASP C CB  
12046 C CG  . ASP C 465 ? 0.4976 0.4399 0.6570 -0.0185 -0.0503 -0.0571 465 ASP C CG  
12047 O OD1 . ASP C 465 ? 0.4911 0.4237 0.6017 -0.0282 -0.0441 -0.0504 465 ASP C OD1 
12048 O OD2 . ASP C 465 ? 0.5234 0.4709 0.7222 -0.0150 -0.0319 -0.0718 465 ASP C OD2 
12049 N N   . LYS C 466 ? 0.3137 0.3097 0.4761 -0.0186 -0.1092 -0.0440 466 LYS C N   
12050 C CA  . LYS C 466 ? 0.2974 0.3133 0.4600 -0.0233 -0.1052 -0.0512 466 LYS C CA  
12051 C C   . LYS C 466 ? 0.2976 0.3153 0.4074 -0.0319 -0.1128 -0.0412 466 LYS C C   
12052 O O   . LYS C 466 ? 0.3365 0.3604 0.4290 -0.0382 -0.0980 -0.0452 466 LYS C O   
12053 C CB  . LYS C 466 ? 0.2985 0.3328 0.5084 -0.0171 -0.1237 -0.0582 466 LYS C CB  
12054 C CG  . LYS C 466 ? 0.2873 0.3402 0.4934 -0.0228 -0.1253 -0.0649 466 LYS C CG  
12055 C CD  . LYS C 466 ? 0.2919 0.3617 0.5465 -0.0177 -0.1464 -0.0719 466 LYS C CD  
12056 C CE  . LYS C 466 ? 0.2891 0.3763 0.5626 -0.0223 -0.1356 -0.0856 466 LYS C CE  
12057 N NZ  . LYS C 466 ? 0.2760 0.3795 0.6183 -0.0165 -0.1448 -0.0965 466 LYS C NZ  
12058 N N   . LEU C 467 ? 0.3511 0.3624 0.4362 -0.0326 -0.1352 -0.0281 467 LEU C N   
12059 C CA  . LEU C 467 ? 0.3211 0.3334 0.3567 -0.0416 -0.1395 -0.0190 467 LEU C CA  
12060 C C   . LEU C 467 ? 0.3151 0.3189 0.3217 -0.0481 -0.1187 -0.0153 467 LEU C C   
12061 O O   . LEU C 467 ? 0.4041 0.4167 0.3910 -0.0544 -0.1086 -0.0170 467 LEU C O   
12062 C CB  . LEU C 467 ? 0.3498 0.3514 0.3617 -0.0425 -0.1651 -0.0043 467 LEU C CB  
12063 C CG  . LEU C 467 ? 0.3677 0.3780 0.3750 -0.0434 -0.1893 -0.0041 467 LEU C CG  
12064 C CD1 . LEU C 467 ? 0.4025 0.3959 0.3925 -0.0430 -0.2168 0.0117  467 LEU C CD1 
12065 C CD2 . LEU C 467 ? 0.3666 0.3864 0.3354 -0.0532 -0.1818 -0.0063 467 LEU C CD2 
12066 N N   . PHE C 468 ? 0.3623 0.3481 0.3681 -0.0468 -0.1130 -0.0105 468 PHE C N   
12067 C CA  . PHE C 468 ? 0.3127 0.2881 0.2897 -0.0541 -0.0978 -0.0057 468 PHE C CA  
12068 C C   . PHE C 468 ? 0.3192 0.3004 0.3029 -0.0563 -0.0768 -0.0163 468 PHE C C   
12069 O O   . PHE C 468 ? 0.3686 0.3516 0.3288 -0.0634 -0.0691 -0.0129 468 PHE C O   
12070 C CB  . PHE C 468 ? 0.3272 0.2789 0.3023 -0.0527 -0.0969 -0.0006 468 PHE C CB  
12071 C CG  . PHE C 468 ? 0.3255 0.2641 0.2759 -0.0604 -0.0817 0.0016  468 PHE C CG  
12072 C CD1 . PHE C 468 ? 0.3282 0.2661 0.2460 -0.0695 -0.0852 0.0135  468 PHE C CD1 
12073 C CD2 . PHE C 468 ? 0.3968 0.3232 0.3564 -0.0597 -0.0639 -0.0082 468 PHE C CD2 
12074 C CE1 . PHE C 468 ? 0.3284 0.2548 0.2270 -0.0770 -0.0749 0.0160  468 PHE C CE1 
12075 C CE2 . PHE C 468 ? 0.3291 0.2403 0.2614 -0.0681 -0.0536 -0.0055 468 PHE C CE2 
12076 C CZ  . PHE C 468 ? 0.3300 0.2419 0.2337 -0.0764 -0.0609 0.0069  468 PHE C CZ  
12077 N N   . ARG C 469 ? 0.3370 0.3201 0.3544 -0.0508 -0.0673 -0.0288 469 ARG C N   
12078 C CA  . ARG C 469 ? 0.2762 0.2613 0.2973 -0.0542 -0.0472 -0.0378 469 ARG C CA  
12079 C C   . ARG C 469 ? 0.3670 0.3715 0.3854 -0.0569 -0.0488 -0.0405 469 ARG C C   
12080 O O   . ARG C 469 ? 0.4661 0.4698 0.4715 -0.0621 -0.0368 -0.0414 469 ARG C O   
12081 C CB  . ARG C 469 ? 0.2771 0.2597 0.3364 -0.0489 -0.0342 -0.0509 469 ARG C CB  
12082 C CG  . ARG C 469 ? 0.3929 0.3552 0.4591 -0.0451 -0.0304 -0.0510 469 ARG C CG  
12083 C CD  . ARG C 469 ? 0.4743 0.4151 0.5273 -0.0502 -0.0056 -0.0570 469 ARG C CD  
12084 N NE  . ARG C 469 ? 0.4985 0.4203 0.5654 -0.0454 0.0006  -0.0615 469 ARG C NE  
12085 C CZ  . ARG C 469 ? 0.4742 0.3702 0.5235 -0.0501 0.0210  -0.0669 469 ARG C CZ  
12086 N NH1 . ARG C 469 ? 0.5627 0.4477 0.5786 -0.0602 0.0353  -0.0671 469 ARG C NH1 
12087 N NH2 . ARG C 469 ? 0.4690 0.3474 0.5331 -0.0448 0.0265  -0.0723 469 ARG C NH2 
12088 N N   . SER C 470 ? 0.3008 0.3205 0.3307 -0.0538 -0.0647 -0.0420 470 SER C N   
12089 C CA  . SER C 470 ? 0.2558 0.2912 0.2787 -0.0570 -0.0665 -0.0457 470 SER C CA  
12090 C C   . SER C 470 ? 0.2628 0.2975 0.2483 -0.0633 -0.0663 -0.0360 470 SER C C   
12091 O O   . SER C 470 ? 0.2967 0.3381 0.2761 -0.0667 -0.0569 -0.0392 470 SER C O   
12092 C CB  . SER C 470 ? 0.2668 0.3146 0.3043 -0.0537 -0.0859 -0.0496 470 SER C CB  
12093 O OG  . SER C 470 ? 0.4445 0.5060 0.4905 -0.0556 -0.0831 -0.0600 470 SER C OG  
12094 N N   . PHE C 471 ? 0.3188 0.3451 0.2824 -0.0650 -0.0761 -0.0241 471 PHE C N   
12095 C CA  . PHE C 471 ? 0.3076 0.3341 0.2407 -0.0720 -0.0738 -0.0147 471 PHE C CA  
12096 C C   . PHE C 471 ? 0.3939 0.4139 0.3237 -0.0755 -0.0591 -0.0132 471 PHE C C   
12097 O O   . PHE C 471 ? 0.4357 0.4633 0.3566 -0.0798 -0.0529 -0.0117 471 PHE C O   
12098 C CB  . PHE C 471 ? 0.3408 0.3566 0.2529 -0.0744 -0.0862 -0.0015 471 PHE C CB  
12099 C CG  . PHE C 471 ? 0.3378 0.3571 0.2416 -0.0737 -0.1035 0.0006  471 PHE C CG  
12100 C CD1 . PHE C 471 ? 0.4450 0.4777 0.3386 -0.0766 -0.1046 -0.0053 471 PHE C CD1 
12101 C CD2 . PHE C 471 ? 0.3304 0.3368 0.2344 -0.0707 -0.1199 0.0084  471 PHE C CD2 
12102 C CE1 . PHE C 471 ? 0.4109 0.4428 0.2895 -0.0777 -0.1225 -0.0032 471 PHE C CE1 
12103 C CE2 . PHE C 471 ? 0.3537 0.3600 0.2465 -0.0709 -0.1395 0.0121  471 PHE C CE2 
12104 C CZ  . PHE C 471 ? 0.4131 0.4314 0.2903 -0.0751 -0.1413 0.0064  471 PHE C CZ  
12105 N N   . VAL C 472 ? 0.3737 0.3780 0.3105 -0.0740 -0.0537 -0.0137 472 VAL C N   
12106 C CA  . VAL C 472 ? 0.3500 0.3433 0.2787 -0.0785 -0.0420 -0.0124 472 VAL C CA  
12107 C C   . VAL C 472 ? 0.3549 0.3571 0.2957 -0.0783 -0.0321 -0.0210 472 VAL C C   
12108 O O   . VAL C 472 ? 0.4067 0.4096 0.3391 -0.0826 -0.0280 -0.0175 472 VAL C O   
12109 C CB  . VAL C 472 ? 0.4065 0.3774 0.3358 -0.0777 -0.0366 -0.0138 472 VAL C CB  
12110 C CG1 . VAL C 472 ? 0.3821 0.3402 0.3058 -0.0819 -0.0226 -0.0176 472 VAL C CG1 
12111 C CG2 . VAL C 472 ? 0.4585 0.4149 0.3679 -0.0812 -0.0447 -0.0028 472 VAL C CG2 
12112 N N   . ARG C 473 ? 0.3175 0.3263 0.2816 -0.0735 -0.0292 -0.0319 473 ARG C N   
12113 C CA  . ARG C 473 ? 0.3195 0.3347 0.2968 -0.0739 -0.0197 -0.0404 473 ARG C CA  
12114 C C   . ARG C 473 ? 0.3474 0.3791 0.3211 -0.0748 -0.0234 -0.0407 473 ARG C C   
12115 O O   . ARG C 473 ? 0.3837 0.4155 0.3578 -0.0770 -0.0163 -0.0415 473 ARG C O   
12116 C CB  . ARG C 473 ? 0.3841 0.4047 0.3915 -0.0694 -0.0170 -0.0523 473 ARG C CB  
12117 C CG  . ARG C 473 ? 0.4223 0.4465 0.4461 -0.0708 -0.0057 -0.0616 473 ARG C CG  
12118 C CD  . ARG C 473 ? 0.4704 0.5038 0.5295 -0.0669 -0.0054 -0.0733 473 ARG C CD  
12119 N NE  . ARG C 473 ? 0.7730 0.8004 0.8430 -0.0630 -0.0079 -0.0727 473 ARG C NE  
12120 C CZ  . ARG C 473 ? 0.8450 0.8840 0.9429 -0.0574 -0.0198 -0.0776 473 ARG C CZ  
12121 N NH1 . ARG C 473 ? 0.6670 0.7233 0.7811 -0.0562 -0.0313 -0.0838 473 ARG C NH1 
12122 N NH2 . ARG C 473 ? 0.5867 0.6181 0.6970 -0.0529 -0.0215 -0.0764 473 ARG C NH2 
12123 N N   . ARG C 474 ? 0.2947 0.3380 0.2637 -0.0735 -0.0343 -0.0403 474 ARG C N   
12124 C CA  . ARG C 474 ? 0.3062 0.3637 0.2698 -0.0749 -0.0348 -0.0433 474 ARG C CA  
12125 C C   . ARG C 474 ? 0.3806 0.4385 0.3296 -0.0791 -0.0303 -0.0344 474 ARG C C   
12126 O O   . ARG C 474 ? 0.3836 0.4505 0.3371 -0.0797 -0.0241 -0.0385 474 ARG C O   
12127 C CB  . ARG C 474 ? 0.4193 0.4844 0.3737 -0.0744 -0.0476 -0.0447 474 ARG C CB  
12128 C CG  . ARG C 474 ? 0.4407 0.5173 0.3831 -0.0771 -0.0462 -0.0499 474 ARG C CG  
12129 C CD  . ARG C 474 ? 0.3441 0.4273 0.3061 -0.0753 -0.0395 -0.0641 474 ARG C CD  
12130 N NE  . ARG C 474 ? 0.4370 0.5285 0.3867 -0.0776 -0.0415 -0.0729 474 ARG C NE  
12131 C CZ  . ARG C 474 ? 0.4707 0.5669 0.4043 -0.0809 -0.0330 -0.0728 474 ARG C CZ  
12132 N NH1 . ARG C 474 ? 0.3513 0.4476 0.2846 -0.0820 -0.0240 -0.0633 474 ARG C NH1 
12133 N NH2 . ARG C 474 ? 0.4669 0.5674 0.3853 -0.0837 -0.0334 -0.0830 474 ARG C NH2 
12134 N N   . ALA C 475 ? 0.4435 0.4919 0.3786 -0.0820 -0.0335 -0.0227 475 ALA C N   
12135 C CA  . ALA C 475 ? 0.3633 0.4136 0.2900 -0.0869 -0.0310 -0.0137 475 ALA C CA  
12136 C C   . ALA C 475 ? 0.3460 0.3918 0.2836 -0.0875 -0.0245 -0.0136 475 ALA C C   
12137 O O   . ALA C 475 ? 0.2860 0.3379 0.2267 -0.0903 -0.0231 -0.0082 475 ALA C O   
12138 C CB  . ALA C 475 ? 0.3120 0.3506 0.2226 -0.0910 -0.0375 -0.0014 475 ALA C CB  
12139 N N   . GLN C 476 ? 0.3886 0.4232 0.3333 -0.0855 -0.0209 -0.0188 476 GLN C N   
12140 C CA  . GLN C 476 ? 0.3416 0.3667 0.2915 -0.0870 -0.0163 -0.0175 476 GLN C CA  
12141 C C   . GLN C 476 ? 0.2683 0.3042 0.2370 -0.0837 -0.0106 -0.0268 476 GLN C C   
12142 O O   . GLN C 476 ? 0.2200 0.2471 0.1945 -0.0847 -0.0080 -0.0250 476 GLN C O   
12143 C CB  . GLN C 476 ? 0.2829 0.2857 0.2252 -0.0887 -0.0124 -0.0181 476 GLN C CB  
12144 C CG  . GLN C 476 ? 0.2469 0.2314 0.1676 -0.0937 -0.0168 -0.0085 476 GLN C CG  
12145 C CD  . GLN C 476 ? 0.5862 0.5455 0.4919 -0.0994 -0.0138 -0.0045 476 GLN C CD  
12146 O OE1 . GLN C 476 ? 0.7896 0.7470 0.7000 -0.1006 -0.0130 -0.0031 476 GLN C OE1 
12147 N NE2 . GLN C 476 ? 0.6477 0.5847 0.5331 -0.1035 -0.0123 -0.0026 476 GLN C NE2 
12148 N N   . GLU C 477 ? 0.3288 0.3803 0.3048 -0.0804 -0.0098 -0.0365 477 GLU C N   
12149 C CA  . GLU C 477 ? 0.3209 0.3808 0.3138 -0.0777 -0.0043 -0.0473 477 GLU C CA  
12150 C C   . GLU C 477 ? 0.3678 0.4389 0.3674 -0.0774 -0.0015 -0.0458 477 GLU C C   
12151 O O   . GLU C 477 ? 0.4350 0.5137 0.4260 -0.0796 -0.0033 -0.0392 477 GLU C O   
12152 C CB  . GLU C 477 ? 0.3061 0.3762 0.3017 -0.0755 -0.0062 -0.0594 477 GLU C CB  
12153 C CG  . GLU C 477 ? 0.4634 0.5267 0.4615 -0.0748 -0.0100 -0.0615 477 GLU C CG  
12154 C CD  . GLU C 477 ? 0.5968 0.6544 0.6149 -0.0743 -0.0031 -0.0702 477 GLU C CD  
12155 O OE1 . GLU C 477 ? 0.7429 0.8076 0.7737 -0.0734 -0.0008 -0.0804 477 GLU C OE1 
12156 O OE2 . GLU C 477 ? 0.5087 0.5533 0.5292 -0.0756 0.0013  -0.0675 477 GLU C OE2 
12157 N N   . LEU C 478 ? 0.3408 0.4124 0.3587 -0.0749 0.0039  -0.0524 478 LEU C N   
12158 C CA  . LEU C 478 ? 0.2375 0.3197 0.2707 -0.0731 0.0083  -0.0529 478 LEU C CA  
12159 C C   . LEU C 478 ? 0.2649 0.3636 0.2950 -0.0724 0.0145  -0.0646 478 LEU C C   
12160 O O   . LEU C 478 ? 0.2717 0.3716 0.2904 -0.0727 0.0133  -0.0741 478 LEU C O   
12161 C CB  . LEU C 478 ? 0.3100 0.3841 0.3655 -0.0700 0.0111  -0.0560 478 LEU C CB  
12162 C CG  . LEU C 478 ? 0.3528 0.4103 0.4107 -0.0719 0.0042  -0.0414 478 LEU C CG  
12163 C CD1 . LEU C 478 ? 0.4235 0.4615 0.4587 -0.0765 0.0006  -0.0353 478 LEU C CD1 
12164 C CD2 . LEU C 478 ? 0.3451 0.3951 0.4269 -0.0684 0.0057  -0.0435 478 LEU C CD2 
12165 N N   . GLU C 479 ? 0.2792 0.3898 0.3200 -0.0721 0.0211  -0.0642 479 GLU C N   
12166 C CA  . GLU C 479 ? 0.3533 0.4772 0.3839 -0.0737 0.0301  -0.0738 479 GLU C CA  
12167 C C   . GLU C 479 ? 0.4024 0.5283 0.4403 -0.0707 0.0387  -0.0928 479 GLU C C   
12168 O O   . GLU C 479 ? 0.4360 0.5686 0.4573 -0.0734 0.0463  -0.1031 479 GLU C O   
12169 C CB  . GLU C 479 ? 0.4009 0.5375 0.4450 -0.0753 0.0379  -0.0676 479 GLU C CB  
12170 C CG  . GLU C 479 ? 0.5221 0.6690 0.5436 -0.0812 0.0468  -0.0707 479 GLU C CG  
12171 C CD  . GLU C 479 ? 0.5094 0.6696 0.5490 -0.0801 0.0660  -0.0834 479 GLU C CD  
12172 O OE1 . GLU C 479 ? 0.6210 0.7847 0.6985 -0.0737 0.0705  -0.0870 479 GLU C OE1 
12173 O OE2 . GLU C 479 ? 0.4190 0.5844 0.4347 -0.0859 0.0770  -0.0896 479 GLU C OE2 
12174 N N   . HIS C 480 ? 0.4194 0.5370 0.4781 -0.0663 0.0378  -0.0979 480 HIS C N   
12175 C CA  . HIS C 480 ? 0.2726 0.3901 0.3415 -0.0636 0.0460  -0.1165 480 HIS C CA  
12176 C C   . HIS C 480 ? 0.2390 0.3435 0.3140 -0.0627 0.0394  -0.1208 480 HIS C C   
12177 O O   . HIS C 480 ? 0.3119 0.4064 0.3929 -0.0626 0.0328  -0.1090 480 HIS C O   
12178 C CB  . HIS C 480 ? 0.2457 0.3678 0.3476 -0.0583 0.0572  -0.1206 480 HIS C CB  
12179 C CG  . HIS C 480 ? 0.3081 0.4455 0.4091 -0.0597 0.0704  -0.1245 480 HIS C CG  
12180 N ND1 . HIS C 480 ? 0.4711 0.6129 0.5426 -0.0645 0.0789  -0.1372 480 HIS C ND1 
12181 C CD2 . HIS C 480 ? 0.3234 0.4720 0.4491 -0.0580 0.0770  -0.1171 480 HIS C CD2 
12182 C CE1 . HIS C 480 ? 0.4036 0.5578 0.4794 -0.0663 0.0933  -0.1379 480 HIS C CE1 
12183 N NE2 . HIS C 480 ? 0.3804 0.5410 0.4933 -0.0619 0.0927  -0.1262 480 HIS C NE2 
12184 N N   . HIS C 481 ? 0.2515 0.3550 0.3233 -0.0632 0.0419  -0.1382 481 HIS C N   
12185 C CA  . HIS C 481 ? 0.2969 0.3895 0.3821 -0.0630 0.0381  -0.1447 481 HIS C CA  
12186 C C   . HIS C 481 ? 0.3449 0.4279 0.4596 -0.0587 0.0432  -0.1417 481 HIS C C   
12187 O O   . HIS C 481 ? 0.3804 0.4659 0.5116 -0.0546 0.0521  -0.1494 481 HIS C O   
12188 C CB  . HIS C 481 ? 0.2677 0.3610 0.3454 -0.0653 0.0390  -0.1653 481 HIS C CB  
12189 C CG  . HIS C 481 ? 0.3860 0.4849 0.4334 -0.0703 0.0293  -0.1673 481 HIS C CG  
12190 N ND1 . HIS C 481 ? 0.4774 0.5830 0.4968 -0.0730 0.0323  -0.1692 481 HIS C ND1 
12191 C CD2 . HIS C 481 ? 0.4452 0.5429 0.4872 -0.0733 0.0160  -0.1670 481 HIS C CD2 
12192 C CE1 . HIS C 481 ? 0.5876 0.6935 0.5818 -0.0776 0.0189  -0.1687 481 HIS C CE1 
12193 N NE2 . HIS C 481 ? 0.5257 0.6281 0.5363 -0.0771 0.0081  -0.1675 481 HIS C NE2 
12194 N N   . HIS C 482 ? 0.2711 0.3413 0.3922 -0.0598 0.0379  -0.1304 482 HIS C N   
12195 C CA  . HIS C 482 ? 0.3140 0.3706 0.4566 -0.0569 0.0390  -0.1224 482 HIS C CA  
12196 C C   . HIS C 482 ? 0.2396 0.2779 0.3861 -0.0607 0.0372  -0.1204 482 HIS C C   
12197 O O   . HIS C 482 ? 0.3224 0.3597 0.4559 -0.0654 0.0348  -0.1193 482 HIS C O   
12198 C CB  . HIS C 482 ? 0.2788 0.3350 0.4182 -0.0563 0.0337  -0.1030 482 HIS C CB  
12199 C CG  . HIS C 482 ? 0.2623 0.3112 0.3787 -0.0617 0.0268  -0.0900 482 HIS C CG  
12200 N ND1 . HIS C 482 ? 0.2721 0.3321 0.3673 -0.0641 0.0244  -0.0889 482 HIS C ND1 
12201 C CD2 . HIS C 482 ? 0.2288 0.2577 0.3384 -0.0655 0.0231  -0.0783 482 HIS C CD2 
12202 C CE1 . HIS C 482 ? 0.3681 0.4165 0.4486 -0.0681 0.0199  -0.0782 482 HIS C CE1 
12203 N NE2 . HIS C 482 ? 0.3635 0.3929 0.4503 -0.0695 0.0201  -0.0721 482 HIS C NE2 
12204 N N   . HIS C 483 ? 0.2488 0.2719 0.4157 -0.0588 0.0392  -0.1199 483 HIS C N   
12205 C CA  . HIS C 483 ? 0.2567 0.2572 0.4260 -0.0636 0.0388  -0.1133 483 HIS C CA  
12206 C C   . HIS C 483 ? 0.2654 0.2481 0.4379 -0.0623 0.0331  -0.0950 483 HIS C C   
12207 O O   . HIS C 483 ? 0.2628 0.2537 0.4435 -0.0568 0.0290  -0.0892 483 HIS C O   
12208 C CB  . HIS C 483 ? 0.3250 0.3179 0.5139 -0.0643 0.0443  -0.1292 483 HIS C CB  
12209 C CG  . HIS C 483 ? 0.2774 0.2666 0.4905 -0.0572 0.0466  -0.1356 483 HIS C CG  
12210 N ND1 . HIS C 483 ? 0.2940 0.2597 0.5248 -0.0564 0.0456  -0.1291 483 HIS C ND1 
12211 C CD2 . HIS C 483 ? 0.3097 0.3143 0.5330 -0.0507 0.0509  -0.1482 483 HIS C CD2 
12212 C CE1 . HIS C 483 ? 0.4139 0.3818 0.6696 -0.0483 0.0482  -0.1378 483 HIS C CE1 
12213 N NE2 . HIS C 483 ? 0.3263 0.3183 0.5781 -0.0449 0.0531  -0.1504 483 HIS C NE2 
12214 N N   . HIS C 484 ? 0.2793 0.2366 0.4452 -0.0684 0.0325  -0.0853 484 HIS C N   
12215 C CA  . HIS C 484 ? 0.2958 0.2303 0.4601 -0.0688 0.0238  -0.0667 484 HIS C CA  
12216 C C   . HIS C 484 ? 0.3074 0.2340 0.5043 -0.0620 0.0223  -0.0706 484 HIS C C   
12217 O O   . HIS C 484 ? 0.3290 0.2280 0.5291 -0.0653 0.0200  -0.0632 484 HIS C O   
12218 C CB  . HIS C 484 ? 0.3149 0.2202 0.4539 -0.0795 0.0250  -0.0546 484 HIS C CB  
12219 C CG  . HIS C 484 ? 0.3244 0.2165 0.4338 -0.0840 0.0157  -0.0353 484 HIS C CG  
12220 N ND1 . HIS C 484 ? 0.3087 0.2175 0.4008 -0.0842 0.0144  -0.0340 484 HIS C ND1 
12221 C CD2 . HIS C 484 ? 0.3524 0.2135 0.4442 -0.0892 0.0057  -0.0164 484 HIS C CD2 
12222 C CE1 . HIS C 484 ? 0.3256 0.2148 0.3914 -0.0895 0.0049  -0.0165 484 HIS C CE1 
12223 N NE2 . HIS C 484 ? 0.3533 0.2132 0.4167 -0.0929 -0.0013 -0.0053 484 HIS C NE2 
12224 N N   . MET D 1   ? 1.9194 1.0295 0.8680 -0.0831 0.0962  -0.3073 1   MET D N   
12225 C CA  . MET D 1   ? 1.8156 0.9028 0.7753 -0.0703 0.1137  -0.3013 1   MET D CA  
12226 C C   . MET D 1   ? 1.7040 0.8039 0.6819 -0.0647 0.1076  -0.2803 1   MET D C   
12227 O O   . MET D 1   ? 1.7314 0.8614 0.7078 -0.0651 0.0962  -0.2690 1   MET D O   
12228 C CB  . MET D 1   ? 1.9205 1.0046 0.8657 -0.0599 0.1308  -0.3061 1   MET D CB  
12229 C CG  . MET D 1   ? 1.9132 0.9795 0.8719 -0.0453 0.1493  -0.2987 1   MET D CG  
12230 S SD  . MET D 1   ? 2.1331 1.1988 1.0744 -0.0344 0.1691  -0.3045 1   MET D SD  
12231 C CE  . MET D 1   ? 1.7801 0.8847 0.7176 -0.0324 0.1574  -0.2865 1   MET D CE  
12232 N N   . LYS D 2   ? 1.7521 0.8291 0.7482 -0.0589 0.1150  -0.2752 2   LYS D N   
12233 C CA  . LYS D 2   ? 1.6756 0.7608 0.6897 -0.0535 0.1089  -0.2563 2   LYS D CA  
12234 C C   . LYS D 2   ? 1.7310 0.8233 0.7460 -0.0393 0.1206  -0.2464 2   LYS D C   
12235 O O   . LYS D 2   ? 1.7229 0.7960 0.7396 -0.0293 0.1395  -0.2519 2   LYS D O   
12236 C CB  . LYS D 2   ? 1.6906 0.7485 0.7249 -0.0520 0.1124  -0.2551 2   LYS D CB  
12237 C CG  . LYS D 2   ? 1.5793 0.6461 0.6304 -0.0525 0.0990  -0.2381 2   LYS D CG  
12238 C CD  . LYS D 2   ? 1.7359 0.8363 0.7794 -0.0622 0.0795  -0.2308 2   LYS D CD  
12239 C CE  . LYS D 2   ? 1.7125 0.8141 0.7557 -0.0781 0.0656  -0.2379 2   LYS D CE  
12240 N NZ  . LYS D 2   ? 1.8626 1.0006 0.9019 -0.0866 0.0470  -0.2313 2   LYS D NZ  
12241 N N   . LYS D 3   ? 1.7394 0.8599 0.7552 -0.0382 0.1099  -0.2319 3   LYS D N   
12242 C CA  . LYS D 3   ? 1.6712 0.8014 0.6879 -0.0259 0.1197  -0.2218 3   LYS D CA  
12243 C C   . LYS D 3   ? 1.5207 0.6522 0.5574 -0.0188 0.1162  -0.2049 3   LYS D C   
12244 O O   . LYS D 3   ? 1.6207 0.7641 0.6649 -0.0254 0.0991  -0.1961 3   LYS D O   
12245 C CB  . LYS D 3   ? 1.6912 0.8541 0.6943 -0.0286 0.1115  -0.2179 3   LYS D CB  
12246 C CG  . LYS D 3   ? 1.8736 1.0460 0.8594 -0.0400 0.1032  -0.2315 3   LYS D CG  
12247 C CD  . LYS D 3   ? 1.7974 1.0006 0.7877 -0.0496 0.0805  -0.2238 3   LYS D CD  
12248 C CE  . LYS D 3   ? 1.8578 1.0754 0.8329 -0.0597 0.0715  -0.2368 3   LYS D CE  
12249 N NZ  . LYS D 3   ? 1.7214 0.9638 0.7067 -0.0697 0.0502  -0.2310 3   LYS D NZ  
12250 N N   . LEU D 4   ? 1.5908 0.7108 0.6370 -0.0052 0.1325  -0.2007 4   LEU D N   
12251 C CA  . LEU D 4   ? 1.5480 0.6711 0.6126 0.0036  0.1307  -0.1848 4   LEU D CA  
12252 C C   . LEU D 4   ? 1.5445 0.6961 0.6038 0.0069  0.1275  -0.1730 4   LEU D C   
12253 O O   . LEU D 4   ? 1.5644 0.7173 0.6202 0.0154  0.1427  -0.1735 4   LEU D O   
12254 C CB  . LEU D 4   ? 1.5811 0.6800 0.6638 0.0174  0.1499  -0.1862 4   LEU D CB  
12255 C CG  . LEU D 4   ? 1.5253 0.6273 0.6294 0.0279  0.1483  -0.1704 4   LEU D CG  
12256 C CD1 . LEU D 4   ? 1.4517 0.5305 0.5812 0.0333  0.1509  -0.1702 4   LEU D CD1 
12257 C CD2 . LEU D 4   ? 1.4721 0.5816 0.5803 0.0406  0.1643  -0.1655 4   LEU D CD2 
12258 N N   . PHE D 5   ? 1.4602 0.6356 0.5209 0.0002  0.1080  -0.1621 5   PHE D N   
12259 C CA  . PHE D 5   ? 1.4428 0.6479 0.5032 0.0030  0.1030  -0.1496 5   PHE D CA  
12260 C C   . PHE D 5   ? 1.4202 0.6217 0.4949 0.0158  0.1114  -0.1375 5   PHE D C   
12261 O O   . PHE D 5   ? 1.5165 0.7097 0.6050 0.0183  0.1055  -0.1304 5   PHE D O   
12262 C CB  . PHE D 5   ? 1.5120 0.7455 0.5764 -0.0072 0.0799  -0.1412 5   PHE D CB  
12263 C CG  . PHE D 5   ? 1.5808 0.8224 0.6332 -0.0193 0.0713  -0.1530 5   PHE D CG  
12264 C CD1 . PHE D 5   ? 1.5058 0.7442 0.5411 -0.0198 0.0817  -0.1659 5   PHE D CD1 
12265 C CD2 . PHE D 5   ? 1.6071 0.8599 0.6658 -0.0300 0.0532  -0.1515 5   PHE D CD2 
12266 C CE1 . PHE D 5   ? 1.5672 0.8134 0.5910 -0.0304 0.0734  -0.1774 5   PHE D CE1 
12267 C CE2 . PHE D 5   ? 1.5150 0.7763 0.5639 -0.0409 0.0457  -0.1629 5   PHE D CE2 
12268 C CZ  . PHE D 5   ? 1.6673 0.9252 0.6983 -0.0409 0.0554  -0.1761 5   PHE D CZ  
12269 N N   . LEU D 6   ? 1.3916 0.5993 0.4636 0.0240  0.1253  -0.1354 6   LEU D N   
12270 C CA  . LEU D 6   ? 1.3773 0.5813 0.4632 0.0369  0.1369  -0.1260 6   LEU D CA  
12271 C C   . LEU D 6   ? 1.3263 0.5607 0.4146 0.0381  0.1303  -0.1118 6   LEU D C   
12272 O O   . LEU D 6   ? 1.3317 0.5848 0.4097 0.0336  0.1282  -0.1128 6   LEU D O   
12273 C CB  . LEU D 6   ? 1.4937 0.6782 0.5797 0.0464  0.1621  -0.1358 6   LEU D CB  
12274 C CG  . LEU D 6   ? 1.3884 0.5614 0.4964 0.0609  0.1769  -0.1303 6   LEU D CG  
12275 C CD1 . LEU D 6   ? 1.4432 0.6043 0.5689 0.0627  0.1666  -0.1259 6   LEU D CD1 
12276 C CD2 . LEU D 6   ? 1.5274 0.6817 0.6405 0.0690  0.2009  -0.1420 6   LEU D CD2 
12277 N N   . VAL D 7   ? 1.3904 0.6303 0.4941 0.0443  0.1263  -0.0986 7   VAL D N   
12278 C CA  . VAL D 7   ? 1.4022 0.6710 0.5135 0.0460  0.1202  -0.0841 7   VAL D CA  
12279 C C   . VAL D 7   ? 1.3320 0.5934 0.4554 0.0592  0.1352  -0.0772 7   VAL D C   
12280 O O   . VAL D 7   ? 1.3656 0.6104 0.4996 0.0656  0.1365  -0.0758 7   VAL D O   
12281 C CB  . VAL D 7   ? 1.3139 0.6060 0.4365 0.0386  0.0956  -0.0728 7   VAL D CB  
12282 C CG1 . VAL D 7   ? 1.2518 0.5782 0.3864 0.0390  0.0891  -0.0604 7   VAL D CG1 
12283 C CG2 . VAL D 7   ? 1.2350 0.5308 0.3497 0.0262  0.0819  -0.0810 7   VAL D CG2 
12284 N N   . PHE D 8   ? 1.2536 0.5277 0.3771 0.0635  0.1463  -0.0731 8   PHE D N   
12285 C CA  . PHE D 8   ? 1.2472 0.5197 0.3841 0.0753  0.1611  -0.0657 8   PHE D CA  
12286 C C   . PHE D 8   ? 1.2241 0.5265 0.3722 0.0740  0.1489  -0.0496 8   PHE D C   
12287 O O   . PHE D 8   ? 1.1984 0.5236 0.3437 0.0670  0.1396  -0.0468 8   PHE D O   
12288 C CB  . PHE D 8   ? 1.2898 0.5536 0.4224 0.0815  0.1861  -0.0734 8   PHE D CB  
12289 C CG  . PHE D 8   ? 1.3312 0.5665 0.4658 0.0870  0.2026  -0.0876 8   PHE D CG  
12290 C CD1 . PHE D 8   ? 1.4680 0.6910 0.5877 0.0794  0.1993  -0.1006 8   PHE D CD1 
12291 C CD2 . PHE D 8   ? 1.3146 0.5377 0.4714 0.1001  0.2210  -0.0880 8   PHE D CD2 
12292 C CE1 . PHE D 8   ? 1.5891 0.7873 0.7149 0.0844  0.2139  -0.1132 8   PHE D CE1 
12293 C CE2 . PHE D 8   ? 1.3855 0.5861 0.5534 0.1058  0.2350  -0.1002 8   PHE D CE2 
12294 C CZ  . PHE D 8   ? 1.5101 0.6977 0.6615 0.0977  0.2315  -0.1126 8   PHE D CZ  
12295 N N   . TRP D 9   ? 1.2235 0.5268 0.3871 0.0815  0.1488  -0.0394 9   TRP D N   
12296 C CA  . TRP D 9   ? 1.2231 0.5553 0.4029 0.0804  0.1365  -0.0237 9   TRP D CA  
12297 C C   . TRP D 9   ? 1.1359 0.4638 0.3281 0.0923  0.1523  -0.0166 9   TRP D C   
12298 O O   . TRP D 9   ? 1.1902 0.5135 0.4020 0.0977  0.1491  -0.0121 9   TRP D O   
12299 C CB  . TRP D 9   ? 1.2476 0.5936 0.4385 0.0736  0.1108  -0.0165 9   TRP D CB  
12300 C CG  . TRP D 9   ? 1.1266 0.5106 0.3394 0.0682  0.0944  -0.0053 9   TRP D CG  
12301 C CD1 . TRP D 9   ? 1.0609 0.4643 0.2835 0.0701  0.1002  0.0004  9   TRP D CD1 
12302 C CD2 . TRP D 9   ? 1.0405 0.4492 0.2722 0.0602  0.0710  -0.0001 9   TRP D CD2 
12303 N NE1 . TRP D 9   ? 1.0217 0.4600 0.2682 0.0641  0.0817  0.0081  9   TRP D NE1 
12304 C CE2 . TRP D 9   ? 1.0055 0.4492 0.2598 0.0581  0.0643  0.0077  9   TRP D CE2 
12305 C CE3 . TRP D 9   ? 1.0367 0.4419 0.2703 0.0545  0.0562  -0.0017 9   TRP D CE3 
12306 C CZ2 . TRP D 9   ? 0.9659 0.4429 0.2467 0.0512  0.0448  0.0128  9   TRP D CZ2 
12307 C CZ3 . TRP D 9   ? 1.0025 0.4410 0.2624 0.0472  0.0367  0.0043  9   TRP D CZ3 
12308 C CH2 . TRP D 9   ? 0.9586 0.4335 0.2429 0.0460  0.0318  0.0110  9   TRP D CH2 
12309 N N   . TRP D 10  ? 1.1406 0.4776 0.3358 0.0952  0.1669  -0.0142 10  TRP D N   
12310 C CA  . TRP D 10  ? 1.1747 0.5128 0.3852 0.1055  0.1826  -0.0064 10  TRP D CA  
12311 C C   . TRP D 10  ? 1.1658 0.5335 0.3948 0.1018  0.1659  0.0096  10  TRP D C   
12312 O O   . TRP D 10  ? 1.1370 0.5262 0.3684 0.0939  0.1548  0.0115  10  TRP D O   
12313 C CB  . TRP D 10  ? 1.1584 0.4908 0.3667 0.1103  0.2089  -0.0127 10  TRP D CB  
12314 C CG  . TRP D 10  ? 1.2812 0.5893 0.4784 0.1127  0.2242  -0.0294 10  TRP D CG  
12315 C CD1 . TRP D 10  ? 1.2804 0.5856 0.4588 0.1059  0.2259  -0.0385 10  TRP D CD1 
12316 C CD2 . TRP D 10  ? 1.2032 0.4972 0.4274 0.1210  0.2347  -0.0365 10  TRP D CD2 
12317 N NE1 . TRP D 10  ? 1.3227 0.6047 0.4991 0.1103  0.2409  -0.0527 10  TRP D NE1 
12318 C CE2 . TRP D 10  ? 1.2455 0.5156 0.4448 0.1210  0.2489  -0.0534 10  TRP D CE2 
12319 C CE3 . TRP D 10  ? 1.1734 0.4783 0.4499 0.1275  0.2301  -0.0287 10  TRP D CE3 
12320 C CZ2 . TRP D 10  ? 1.2602 0.5145 0.4831 0.1279  0.2600  -0.0630 10  TRP D CZ2 
12321 C CZ3 . TRP D 10  ? 1.1872 0.4782 0.4885 0.1346  0.2402  -0.0374 10  TRP D CZ3 
12322 C CH2 . TRP D 10  ? 1.2301 0.4958 0.5049 0.1348  0.2553  -0.0543 10  TRP D CH2 
12323 N N   . HIS D 11  ? 1.1361 0.5093 0.3872 0.1074  0.1627  0.0203  11  HIS D N   
12324 C CA  . HIS D 11  ? 1.0271 0.4270 0.2983 0.1044  0.1467  0.0347  11  HIS D CA  
12325 C C   . HIS D 11  ? 1.0248 0.4302 0.3092 0.1111  0.1652  0.0423  11  HIS D C   
12326 O O   . HIS D 11  ? 1.0532 0.4606 0.3766 0.1178  0.1752  0.0414  11  HIS D O   
12327 C CB  . HIS D 11  ? 1.0536 0.4577 0.3424 0.1046  0.1271  0.0431  11  HIS D CB  
12328 C CG  . HIS D 11  ? 0.9788 0.4146 0.3018 0.1023  0.1114  0.0552  11  HIS D CG  
12329 N ND1 . HIS D 11  ? 1.0100 0.4783 0.3498 0.0925  0.0932  0.0541  11  HIS D ND1 
12330 C CD2 . HIS D 11  ? 0.9538 0.3971 0.3032 0.1082  0.1114  0.0674  11  HIS D CD2 
12331 C CE1 . HIS D 11  ? 0.9660 0.4601 0.3381 0.0921  0.0840  0.0629  11  HIS D CE1 
12332 N NE2 . HIS D 11  ? 0.9973 0.4777 0.3763 0.1010  0.0936  0.0705  11  HIS D NE2 
12333 N N   . MET D 12  ? 1.0081 0.4370 0.3041 0.1060  0.1606  0.0461  12  MET D N   
12334 C CA  . MET D 12  ? 1.1254 0.5595 0.4330 0.1108  0.1789  0.0525  12  MET D CA  
12335 C C   . MET D 12  ? 1.0394 0.5030 0.3764 0.1067  0.1603  0.0635  12  MET D C   
12336 O O   . MET D 12  ? 0.9440 0.4297 0.2877 0.0984  0.1406  0.0620  12  MET D O   
12337 C CB  . MET D 12  ? 1.1423 0.5753 0.4346 0.1081  0.1922  0.0451  12  MET D CB  
12338 C CG  . MET D 12  ? 1.0731 0.4818 0.3401 0.1097  0.2051  0.0316  12  MET D CG  
12339 S SD  . MET D 12  ? 1.4688 0.8493 0.7316 0.1214  0.2387  0.0221  12  MET D SD  
12340 C CE  . MET D 12  ? 1.3246 0.7158 0.6077 0.1262  0.2623  0.0299  12  MET D CE  
12341 N N   . HIS D 13  ? 1.0733 0.5394 0.4311 0.1125  0.1667  0.0739  13  HIS D N   
12342 C CA  . HIS D 13  ? 0.9581 0.4530 0.3475 0.1084  0.1479  0.0825  13  HIS D CA  
12343 C C   . HIS D 13  ? 0.9742 0.4689 0.3846 0.1149  0.1628  0.0937  13  HIS D C   
12344 O O   . HIS D 13  ? 1.1123 0.6006 0.5460 0.1213  0.1733  0.0920  13  HIS D O   
12345 C CB  . HIS D 13  ? 0.8806 0.3865 0.2855 0.1053  0.1220  0.0835  13  HIS D CB  
12346 C CG  . HIS D 13  ? 0.8398 0.3720 0.2822 0.1038  0.1075  0.0923  13  HIS D CG  
12347 N ND1 . HIS D 13  ? 0.8125 0.3732 0.2726 0.0970  0.0990  0.0938  13  HIS D ND1 
12348 C CD2 . HIS D 13  ? 0.8218 0.3570 0.2897 0.1079  0.0997  0.0996  13  HIS D CD2 
12349 C CE1 . HIS D 13  ? 0.7804 0.3601 0.2723 0.0964  0.0875  0.1005  13  HIS D CE1 
12350 N NE2 . HIS D 13  ? 0.7844 0.3508 0.2830 0.1028  0.0868  0.1040  13  HIS D NE2 
12351 N N   . GLN D 14  ? 0.8829 0.4007 0.3130 0.1106  0.1580  0.0982  14  GLN D N   
12352 C CA  . GLN D 14  ? 0.8712 0.3948 0.3286 0.1145  0.1665  0.1094  14  GLN D CA  
12353 C C   . GLN D 14  ? 0.9153 0.4705 0.4004 0.1074  0.1419  0.1127  14  GLN D C   
12354 O O   . GLN D 14  ? 0.9717 0.5443 0.4533 0.0996  0.1302  0.1078  14  GLN D O   
12355 C CB  . GLN D 14  ? 0.9095 0.4267 0.3618 0.1162  0.1945  0.1108  14  GLN D CB  
12356 C CG  . GLN D 14  ? 1.1288 0.6301 0.5772 0.1214  0.2182  0.1015  14  GLN D CG  
12357 C CD  . GLN D 14  ? 1.1214 0.6337 0.6254 0.1272  0.2243  0.0989  14  GLN D CD  
12358 O OE1 . GLN D 14  ? 1.1023 0.6288 0.6401 0.1278  0.2319  0.1042  14  GLN D OE1 
12359 N NE2 . GLN D 14  ? 1.0716 0.5772 0.5857 0.1316  0.2210  0.0907  14  GLN D NE2 
12360 N N   . PRO D 15  ? 0.8049 0.3693 0.3208 0.1099  0.1336  0.1210  15  PRO D N   
12361 C CA  . PRO D 15  ? 0.7664 0.3613 0.3089 0.1026  0.1145  0.1236  15  PRO D CA  
12362 C C   . PRO D 15  ? 0.8161 0.4162 0.3602 0.1003  0.1279  0.1269  15  PRO D C   
12363 O O   . PRO D 15  ? 0.8726 0.4547 0.4031 0.1045  0.1531  0.1282  15  PRO D O   
12364 C CB  . PRO D 15  ? 0.7480 0.3475 0.3231 0.1073  0.1061  0.1312  15  PRO D CB  
12365 C CG  . PRO D 15  ? 0.7802 0.3504 0.3532 0.1187  0.1293  0.1361  15  PRO D CG  
12366 C CD  . PRO D 15  ? 0.8191 0.3696 0.3550 0.1191  0.1404  0.1270  15  PRO D CD  
12367 N N   . LEU D 16  ? 0.8658 0.4915 0.4282 0.0928  0.1118  0.1279  16  LEU D N   
12368 C CA  . LEU D 16  ? 0.7811 0.4130 0.3447 0.0892  0.1209  0.1303  16  LEU D CA  
12369 C C   . LEU D 16  ? 0.7551 0.3819 0.3393 0.0934  0.1357  0.1402  16  LEU D C   
12370 O O   . LEU D 16  ? 0.7206 0.3625 0.3317 0.0914  0.1226  0.1452  16  LEU D O   
12371 C CB  . LEU D 16  ? 0.7092 0.3689 0.2858 0.0799  0.0992  0.1280  16  LEU D CB  
12372 C CG  . LEU D 16  ? 0.7169 0.3807 0.2847 0.0758  0.1060  0.1273  16  LEU D CG  
12373 C CD1 . LEU D 16  ? 0.7526 0.4012 0.2908 0.0778  0.1173  0.1214  16  LEU D CD1 
12374 C CD2 . LEU D 16  ? 0.6824 0.3742 0.2667 0.0672  0.0852  0.1259  16  LEU D CD2 
12375 N N   . TYR D 17  ? 0.7798 0.3866 0.3546 0.0987  0.1640  0.1429  17  TYR D N   
12376 C CA  . TYR D 17  ? 0.7934 0.3969 0.3934 0.1015  0.1823  0.1527  17  TYR D CA  
12377 C C   . TYR D 17  ? 0.8162 0.4309 0.4218 0.0948  0.1861  0.1546  17  TYR D C   
12378 O O   . TYR D 17  ? 0.8460 0.4618 0.4771 0.0950  0.1988  0.1627  17  TYR D O   
12379 C CB  . TYR D 17  ? 0.8204 0.4072 0.4220 0.1076  0.2119  0.1510  17  TYR D CB  
12380 C CG  . TYR D 17  ? 0.8151 0.3993 0.4257 0.1134  0.2061  0.1424  17  TYR D CG  
12381 C CD1 . TYR D 17  ? 0.7931 0.3910 0.4413 0.1163  0.1877  0.1426  17  TYR D CD1 
12382 C CD2 . TYR D 17  ? 0.8441 0.4113 0.4251 0.1160  0.2195  0.1340  17  TYR D CD2 
12383 C CE1 . TYR D 17  ? 0.7912 0.3850 0.4472 0.1220  0.1831  0.1353  17  TYR D CE1 
12384 C CE2 . TYR D 17  ? 0.8467 0.4096 0.4357 0.1211  0.2151  0.1259  17  TYR D CE2 
12385 C CZ  . TYR D 17  ? 0.8202 0.3961 0.4470 0.1242  0.1972  0.1268  17  TYR D CZ  
12386 O OH  . TYR D 17  ? 0.8247 0.3945 0.4588 0.1297  0.1933  0.1193  17  TYR D OH  
12387 N N   . ARG D 18  ? 0.7761 0.3991 0.3624 0.0890  0.1755  0.1479  18  ARG D N   
12388 C CA  . ARG D 18  ? 0.7751 0.4060 0.3647 0.0834  0.1791  0.1497  18  ARG D CA  
12389 C C   . ARG D 18  ? 0.7415 0.3919 0.3560 0.0783  0.1589  0.1539  18  ARG D C   
12390 O O   . ARG D 18  ? 0.7406 0.4072 0.3566 0.0742  0.1342  0.1498  18  ARG D O   
12391 C CB  . ARG D 18  ? 0.8104 0.4437 0.3749 0.0798  0.1732  0.1422  18  ARG D CB  
12392 C CG  . ARG D 18  ? 0.9216 0.5636 0.4893 0.0743  0.1734  0.1444  18  ARG D CG  
12393 C CD  . ARG D 18  ? 0.9416 0.5925 0.4927 0.0705  0.1592  0.1384  18  ARG D CD  
12394 N NE  . ARG D 18  ? 0.9264 0.5909 0.4865 0.0649  0.1513  0.1411  18  ARG D NE  
12395 C CZ  . ARG D 18  ? 0.9259 0.5841 0.4872 0.0640  0.1667  0.1457  18  ARG D CZ  
12396 N NH1 . ARG D 18  ? 1.0505 0.6907 0.6060 0.0677  0.1923  0.1478  18  ARG D NH1 
12397 N NH2 . ARG D 18  ? 0.8942 0.5646 0.4642 0.0590  0.1573  0.1481  18  ARG D NH2 
12398 N N   . GLU D 19  ? 0.7419 0.3919 0.3788 0.0778  0.1706  0.1618  19  GLU D N   
12399 C CA  . GLU D 19  ? 0.7136 0.3802 0.3735 0.0727  0.1530  0.1658  19  GLU D CA  
12400 C C   . GLU D 19  ? 0.7446 0.4234 0.3945 0.0655  0.1408  0.1618  19  GLU D C   
12401 O O   . GLU D 19  ? 0.9440 0.6157 0.5772 0.0646  0.1540  0.1600  19  GLU D O   
12402 C CB  . GLU D 19  ? 0.8187 0.4808 0.5063 0.0732  0.1710  0.1752  19  GLU D CB  
12403 C CG  . GLU D 19  ? 0.7113 0.3859 0.4295 0.0717  0.1534  0.1805  19  GLU D CG  
12404 C CD  . GLU D 19  ? 0.7908 0.4778 0.5128 0.0635  0.1411  0.1807  19  GLU D CD  
12405 O OE1 . GLU D 19  ? 0.8674 0.5503 0.5787 0.0597  0.1543  0.1803  19  GLU D OE1 
12406 O OE2 . GLU D 19  ? 0.8023 0.5030 0.5383 0.0607  0.1182  0.1809  19  GLU D OE2 
12407 N N   . PRO D 20  ? 0.7072 0.4050 0.3684 0.0603  0.1161  0.1603  20  PRO D N   
12408 C CA  . PRO D 20  ? 0.6760 0.3866 0.3323 0.0538  0.1057  0.1572  20  PRO D CA  
12409 C C   . PRO D 20  ? 0.6679 0.3763 0.3318 0.0503  0.1153  0.1627  20  PRO D C   
12410 O O   . PRO D 20  ? 0.6802 0.3865 0.3312 0.0484  0.1215  0.1615  20  PRO D O   
12411 C CB  . PRO D 20  ? 0.6236 0.3567 0.2955 0.0491  0.0791  0.1541  20  PRO D CB  
12412 C CG  . PRO D 20  ? 0.6157 0.3470 0.3047 0.0521  0.0752  0.1580  20  PRO D CG  
12413 C CD  . PRO D 20  ? 0.6455 0.3547 0.3255 0.0602  0.0966  0.1608  20  PRO D CD  
12414 N N   . TYR D 21  ? 0.6615 0.3697 0.3471 0.0496  0.1166  0.1690  21  TYR D N   
12415 C CA  . TYR D 21  ? 0.6648 0.3725 0.3602 0.0448  0.1226  0.1739  21  TYR D CA  
12416 C C   . TYR D 21  ? 0.7138 0.4046 0.4040 0.0462  0.1518  0.1774  21  TYR D C   
12417 O O   . TYR D 21  ? 0.8649 0.5542 0.5551 0.0419  0.1582  0.1794  21  TYR D O   
12418 C CB  . TYR D 21  ? 0.6482 0.3610 0.3708 0.0430  0.1145  0.1795  21  TYR D CB  
12419 C CG  . TYR D 21  ? 0.6152 0.3472 0.3454 0.0386  0.0859  0.1761  21  TYR D CG  
12420 C CD1 . TYR D 21  ? 0.6035 0.3456 0.3342 0.0323  0.0763  0.1751  21  TYR D CD1 
12421 C CD2 . TYR D 21  ? 0.6721 0.4129 0.4112 0.0407  0.0698  0.1740  21  TYR D CD2 
12422 C CE1 . TYR D 21  ? 0.5720 0.3341 0.3141 0.0278  0.0530  0.1721  21  TYR D CE1 
12423 C CE2 . TYR D 21  ? 0.6160 0.3771 0.3661 0.0356  0.0459  0.1707  21  TYR D CE2 
12424 C CZ  . TYR D 21  ? 0.6842 0.4567 0.4369 0.0290  0.0385  0.1699  21  TYR D CZ  
12425 O OH  . TYR D 21  ? 0.7439 0.5395 0.5124 0.0240  0.0183  0.1672  21  TYR D OH  
12426 N N   . THR D 22  ? 0.7668 0.4454 0.4541 0.0517  0.1704  0.1779  22  THR D N   
12427 C CA  . THR D 22  ? 0.7859 0.4505 0.4714 0.0523  0.2002  0.1803  22  THR D CA  
12428 C C   . THR D 22  ? 0.8663 0.5206 0.5235 0.0567  0.2107  0.1745  22  THR D C   
12429 O O   . THR D 22  ? 0.9490 0.5931 0.5995 0.0564  0.2326  0.1748  22  THR D O   
12430 C CB  . THR D 22  ? 0.7540 0.4138 0.4711 0.0538  0.2200  0.1870  22  THR D CB  
12431 O OG1 . THR D 22  ? 0.8785 0.5373 0.5987 0.0603  0.2146  0.1866  22  THR D OG1 
12432 C CG2 . THR D 22  ? 0.7363 0.4048 0.4847 0.0483  0.2132  0.1932  22  THR D CG2 
12433 N N   . GLY D 23  ? 0.8156 0.4723 0.4572 0.0603  0.1959  0.1690  23  GLY D N   
12434 C CA  . GLY D 23  ? 0.7855 0.4320 0.4001 0.0641  0.2041  0.1631  23  GLY D CA  
12435 C C   . GLY D 23  ? 0.8174 0.4489 0.4325 0.0698  0.2282  0.1637  23  GLY D C   
12436 O O   . GLY D 23  ? 0.8855 0.5069 0.4770 0.0732  0.2356  0.1582  23  GLY D O   
12437 N N   . GLU D 24  ? 0.8059 0.4365 0.4496 0.0708  0.2409  0.1702  24  GLU D N   
12438 C CA  . GLU D 24  ? 0.8909 0.5096 0.5430 0.0756  0.2683  0.1714  24  GLU D CA  
12439 C C   . GLU D 24  ? 0.9468 0.5608 0.5916 0.0822  0.2604  0.1691  24  GLU D C   
12440 O O   . GLU D 24  ? 0.9321 0.5540 0.5890 0.0832  0.2391  0.1717  24  GLU D O   
12441 C CB  . GLU D 24  ? 0.8243 0.4474 0.5193 0.0731  0.2861  0.1798  24  GLU D CB  
12442 C CG  . GLU D 24  ? 0.8629 0.4899 0.5671 0.0658  0.2947  0.1819  24  GLU D CG  
12443 C CD  . GLU D 24  ? 0.9276 0.5637 0.6793 0.0611  0.3035  0.1899  24  GLU D CD  
12444 O OE1 . GLU D 24  ? 0.8490 0.4974 0.6343 0.0639  0.2932  0.1892  24  GLU D OE1 
12445 O OE2 . GLU D 24  ? 0.9778 0.6164 0.7414 0.0544  0.3139  0.1915  24  GLU D OE2 
12446 N N   . TYR D 25  ? 0.9147 0.5152 0.5395 0.0867  0.2771  0.1637  25  TYR D N   
12447 C CA  . TYR D 25  ? 0.8943 0.4864 0.5116 0.0934  0.2749  0.1614  25  TYR D CA  
12448 C C   . TYR D 25  ? 0.8898 0.4940 0.5602 0.0963  0.2837  0.1603  25  TYR D C   
12449 O O   . TYR D 25  ? 0.8721 0.4774 0.5619 0.0975  0.3079  0.1554  25  TYR D O   
12450 C CB  . TYR D 25  ? 0.9443 0.5221 0.5276 0.0964  0.2871  0.1520  25  TYR D CB  
12451 C CG  . TYR D 25  ? 0.8776 0.4576 0.4290 0.0942  0.2618  0.1444  25  TYR D CG  
12452 C CD1 . TYR D 25  ? 0.8796 0.4655 0.4187 0.0889  0.2551  0.1423  25  TYR D CD1 
12453 C CD2 . TYR D 25  ? 0.9864 0.5634 0.5236 0.0970  0.2453  0.1397  25  TYR D CD2 
12454 C CE1 . TYR D 25  ? 0.8729 0.4644 0.3906 0.0864  0.2332  0.1362  25  TYR D CE1 
12455 C CE2 . TYR D 25  ? 0.9640 0.5467 0.4794 0.0937  0.2234  0.1326  25  TYR D CE2 
12456 C CZ  . TYR D 25  ? 0.9082 0.4992 0.4158 0.0884  0.2177  0.1312  25  TYR D CZ  
12457 O OH  . TYR D 25  ? 0.8559 0.4555 0.3484 0.0849  0.1972  0.1253  25  TYR D OH  
12458 N N   . LEU D 26  ? 0.8100 0.4299 0.5115 0.0972  0.2597  0.1611  26  LEU D N   
12459 C CA  . LEU D 26  ? 0.7933 0.4339 0.5554 0.0996  0.2602  0.1570  26  LEU D CA  
12460 C C   . LEU D 26  ? 0.8672 0.5069 0.6425 0.1075  0.2661  0.1474  26  LEU D C   
12461 O O   . LEU D 26  ? 1.0061 0.6614 0.8305 0.1105  0.2737  0.1431  26  LEU D O   
12462 C CB  . LEU D 26  ? 0.8149 0.4720 0.6037 0.0984  0.2319  0.1615  26  LEU D CB  
12463 C CG  . LEU D 26  ? 0.7465 0.4128 0.5496 0.0908  0.2293  0.1690  26  LEU D CG  
12464 C CD1 . LEU D 26  ? 0.7450 0.3983 0.5009 0.0869  0.2158  0.1768  26  LEU D CD1 
12465 C CD2 . LEU D 26  ? 0.7173 0.4075 0.5742 0.0910  0.2124  0.1688  26  LEU D CD2 
12466 N N   . LEU D 27  ? 0.8660 0.4883 0.6000 0.1109  0.2627  0.1436  27  LEU D N   
12467 C CA  . LEU D 27  ? 0.9376 0.5560 0.6804 0.1183  0.2686  0.1341  27  LEU D CA  
12468 C C   . LEU D 27  ? 0.9803 0.5761 0.6764 0.1191  0.2893  0.1288  27  LEU D C   
12469 O O   . LEU D 27  ? 1.0704 0.6510 0.7158 0.1159  0.2837  0.1319  27  LEU D O   
12470 C CB  . LEU D 27  ? 0.9018 0.5208 0.6435 0.1221  0.2416  0.1331  27  LEU D CB  
12471 C CG  . LEU D 27  ? 0.8253 0.4665 0.6163 0.1235  0.2215  0.1366  27  LEU D CG  
12472 C CD1 . LEU D 27  ? 0.8001 0.4390 0.5905 0.1289  0.2000  0.1343  27  LEU D CD1 
12473 C CD2 . LEU D 27  ? 0.7726 0.4315 0.6193 0.1265  0.2367  0.1332  27  LEU D CD2 
12474 N N   . PRO D 28  ? 0.8843 0.4776 0.5953 0.1235  0.3130  0.1208  28  PRO D N   
12475 C CA  . PRO D 28  ? 0.9222 0.4938 0.5886 0.1243  0.3347  0.1153  28  PRO D CA  
12476 C C   . PRO D 28  ? 0.9365 0.4919 0.5737 0.1292  0.3289  0.1067  28  PRO D C   
12477 O O   . PRO D 28  ? 0.9698 0.5084 0.5767 0.1309  0.3486  0.0999  28  PRO D O   
12478 C CB  . PRO D 28  ? 0.9372 0.5158 0.6395 0.1268  0.3638  0.1106  28  PRO D CB  
12479 C CG  . PRO D 28  ? 0.9099 0.5103 0.6731 0.1314  0.3532  0.1086  28  PRO D CG  
12480 C CD  . PRO D 28  ? 0.8755 0.4877 0.6472 0.1275  0.3232  0.1172  28  PRO D CD  
12481 N N   . TRP D 29  ? 0.9144 0.4736 0.5590 0.1312  0.3033  0.1065  29  TRP D N   
12482 C CA  . TRP D 29  ? 0.9293 0.4719 0.5462 0.1350  0.2980  0.0981  29  TRP D CA  
12483 C C   . TRP D 29  ? 0.9850 0.5080 0.5376 0.1305  0.2962  0.0982  29  TRP D C   
12484 O O   . TRP D 29  ? 1.0841 0.5901 0.6072 0.1327  0.3004  0.0892  29  TRP D O   
12485 C CB  . TRP D 29  ? 0.9014 0.4519 0.5400 0.1376  0.2709  0.0990  29  TRP D CB  
12486 C CG  . TRP D 29  ? 0.8745 0.4476 0.5743 0.1411  0.2654  0.1020  29  TRP D CG  
12487 C CD1 . TRP D 29  ? 0.8498 0.4402 0.5733 0.1384  0.2446  0.1109  29  TRP D CD1 
12488 C CD2 . TRP D 29  ? 0.8862 0.4677 0.6314 0.1484  0.2803  0.0957  29  TRP D CD2 
12489 N NE1 . TRP D 29  ? 0.8443 0.4538 0.6248 0.1433  0.2449  0.1105  29  TRP D NE1 
12490 C CE2 . TRP D 29  ? 0.8476 0.4527 0.6434 0.1497  0.2666  0.1015  29  TRP D CE2 
12491 C CE3 . TRP D 29  ? 0.9830 0.5546 0.7310 0.1542  0.3040  0.0856  29  TRP D CE3 
12492 C CZ2 . TRP D 29  ? 0.8432 0.4635 0.6929 0.1568  0.2751  0.0978  29  TRP D CZ2 
12493 C CZ3 . TRP D 29  ? 0.9500 0.5362 0.7521 0.1615  0.3134  0.0820  29  TRP D CZ3 
12494 C CH2 . TRP D 29  ? 0.8764 0.4873 0.7292 0.1628  0.2985  0.0882  29  TRP D CH2 
12495 N N   . THR D 30  ? 0.9988 0.5238 0.5292 0.1244  0.2893  0.1078  30  THR D N   
12496 C CA  . THR D 30  ? 1.0238 0.5312 0.4933 0.1209  0.2894  0.1083  30  THR D CA  
12497 C C   . THR D 30  ? 1.0819 0.5746 0.5268 0.1222  0.3184  0.1017  30  THR D C   
12498 O O   . THR D 30  ? 1.0448 0.5278 0.4608 0.1210  0.3130  0.0921  30  THR D O   
12499 C CB  . THR D 30  ? 1.1150 0.6359 0.5830 0.1142  0.2719  0.1165  30  THR D CB  
12500 O OG1 . THR D 30  ? 1.0062 0.5360 0.5041 0.1137  0.2861  0.1257  30  THR D OG1 
12501 C CG2 . THR D 30  ? 0.9983 0.5301 0.4714 0.1120  0.2394  0.1190  30  THR D CG2 
12502 N N   . PHE D 31  ? 1.1283 0.6275 0.6010 0.1230  0.3411  0.1034  31  PHE D N   
12503 C CA  . PHE D 31  ? 1.0474 0.5365 0.5052 0.1234  0.3659  0.0967  31  PHE D CA  
12504 C C   . PHE D 31  ? 1.0719 0.5481 0.5269 0.1304  0.3836  0.0846  31  PHE D C   
12505 O O   . PHE D 31  ? 1.1006 0.5638 0.5265 0.1297  0.3871  0.0758  31  PHE D O   
12506 C CB  . PHE D 31  ? 1.0469 0.5465 0.5356 0.1219  0.3870  0.1028  31  PHE D CB  
12507 C CG  . PHE D 31  ? 1.0808 0.5731 0.5617 0.1213  0.4087  0.0963  31  PHE D CG  
12508 C CD1 . PHE D 31  ? 1.1709 0.6614 0.6279 0.1154  0.4002  0.0971  31  PHE D CD1 
12509 C CD2 . PHE D 31  ? 1.1001 0.5889 0.6003 0.1272  0.4370  0.0891  31  PHE D CD2 
12510 C CE1 . PHE D 31  ? 1.2332 0.7160 0.6810 0.1149  0.4197  0.0926  31  PHE D CE1 
12511 C CE2 . PHE D 31  ? 1.1325 0.6144 0.6252 0.1261  0.4556  0.0837  31  PHE D CE2 
12512 C CZ  . PHE D 31  ? 1.2588 0.7366 0.7233 0.1198  0.4471  0.0862  31  PHE D CZ  
12513 N N   . PHE D 32  ? 1.0512 0.5408 0.5584 0.1350  0.3796  0.0809  32  PHE D N   
12514 C CA  . PHE D 32  ? 1.0723 0.5550 0.5940 0.1418  0.3975  0.0687  32  PHE D CA  
12515 C C   . PHE D 32  ? 1.0885 0.5525 0.5747 0.1440  0.3878  0.0590  32  PHE D C   
12516 O O   . PHE D 32  ? 1.2162 0.6650 0.6872 0.1480  0.4068  0.0480  32  PHE D O   
12517 C CB  . PHE D 32  ? 1.0460 0.5496 0.6356 0.1469  0.3959  0.0683  32  PHE D CB  
12518 C CG  . PHE D 32  ? 1.0452 0.5637 0.6724 0.1464  0.4176  0.0720  32  PHE D CG  
12519 C CD1 . PHE D 32  ? 1.0801 0.5876 0.6867 0.1461  0.4479  0.0688  32  PHE D CD1 
12520 C CD2 . PHE D 32  ? 1.0110 0.5544 0.6934 0.1460  0.4079  0.0786  32  PHE D CD2 
12521 C CE1 . PHE D 32  ? 1.0805 0.6016 0.7223 0.1449  0.4689  0.0722  32  PHE D CE1 
12522 C CE2 . PHE D 32  ? 1.0109 0.5688 0.7293 0.1447  0.4279  0.0814  32  PHE D CE2 
12523 C CZ  . PHE D 32  ? 1.0454 0.5922 0.7442 0.1440  0.4588  0.0783  32  PHE D CZ  
12524 N N   . HIS D 33  ? 1.1697 0.6343 0.6430 0.1411  0.3591  0.0624  33  HIS D N   
12525 C CA  . HIS D 33  ? 1.2100 0.6564 0.6468 0.1416  0.3495  0.0534  33  HIS D CA  
12526 C C   . HIS D 33  ? 1.1155 0.5439 0.4876 0.1370  0.3545  0.0517  33  HIS D C   
12527 O O   . HIS D 33  ? 1.1368 0.5508 0.4821 0.1363  0.3502  0.0415  33  HIS D O   
12528 C CB  . HIS D 33  ? 1.2089 0.6628 0.6566 0.1400  0.3177  0.0575  33  HIS D CB  
12529 C CG  . HIS D 33  ? 1.1423 0.6122 0.6497 0.1454  0.3108  0.0587  33  HIS D CG  
12530 N ND1 . HIS D 33  ? 1.1746 0.6401 0.6948 0.1492  0.2975  0.0531  33  HIS D ND1 
12531 C CD2 . HIS D 33  ? 1.1363 0.6266 0.6939 0.1476  0.3150  0.0649  33  HIS D CD2 
12532 C CE1 . HIS D 33  ? 1.1674 0.6498 0.7422 0.1544  0.2936  0.0563  33  HIS D CE1 
12533 N NE2 . HIS D 33  ? 1.1563 0.6548 0.7552 0.1534  0.3037  0.0632  33  HIS D NE2 
12534 N N   . ALA D 34  ? 1.1082 0.5479 0.4790 0.1307  0.3500  0.0604  34  ALA D N   
12535 C CA  . ALA D 34  ? 1.1243 0.5630 0.4674 0.1236  0.3395  0.0574  34  ALA D CA  
12536 C C   . ALA D 34  ? 1.2715 0.6987 0.6052 0.1254  0.3634  0.0487  34  ALA D C   
12537 O O   . ALA D 34  ? 1.3042 0.7226 0.6100 0.1226  0.3579  0.0408  34  ALA D O   
12538 C CB  . ALA D 34  ? 1.1048 0.5603 0.4549 0.1178  0.3280  0.0677  34  ALA D CB  
12539 N N   . VAL D 35  ? 1.2931 0.7217 0.6525 0.1300  0.3900  0.0497  35  VAL D N   
12540 C CA  . VAL D 35  ? 1.3011 0.7215 0.6569 0.1314  0.4138  0.0425  35  VAL D CA  
12541 C C   . VAL D 35  ? 1.2798 0.6874 0.6395 0.1382  0.4269  0.0301  35  VAL D C   
12542 O O   . VAL D 35  ? 1.3525 0.7535 0.7159 0.1409  0.4486  0.0228  35  VAL D O   
12543 C CB  . VAL D 35  ? 1.3152 0.7461 0.7019 0.1321  0.4355  0.0493  35  VAL D CB  
12544 C CG1 . VAL D 35  ? 1.3470 0.7899 0.7315 0.1255  0.4203  0.0611  35  VAL D CG1 
12545 C CG2 . VAL D 35  ? 1.2352 0.6744 0.6655 0.1394  0.4499  0.0500  35  VAL D CG2 
12546 N N   . LYS D 36  ? 1.2073 0.6112 0.5677 0.1414  0.4137  0.0273  36  LYS D N   
12547 C CA  . LYS D 36  ? 1.2731 0.6635 0.6375 0.1483  0.4234  0.0142  36  LYS D CA  
12548 C C   . LYS D 36  ? 1.3061 0.6840 0.6391 0.1455  0.4010  0.0077  36  LYS D C   
12549 O O   . LYS D 36  ? 1.3750 0.7384 0.6939 0.1465  0.4063  -0.0042 36  LYS D O   
12550 C CB  . LYS D 36  ? 1.2013 0.6010 0.6158 0.1581  0.4333  0.0143  36  LYS D CB  
12551 C CG  . LYS D 36  ? 1.2168 0.6067 0.6506 0.1659  0.4426  0.0010  36  LYS D CG  
12552 C CD  . LYS D 36  ? 1.1888 0.5995 0.6921 0.1725  0.4436  0.0040  36  LYS D CD  
12553 C CE  . LYS D 36  ? 1.2060 0.6220 0.7313 0.1739  0.4148  0.0057  36  LYS D CE  
12554 N NZ  . LYS D 36  ? 1.2501 0.6925 0.8261 0.1742  0.3987  0.0175  36  LYS D NZ  
12555 N N   . ASP D 37  ? 1.2922 0.6760 0.6153 0.1413  0.3759  0.0154  37  ASP D N   
12556 C CA  . ASP D 37  ? 1.2754 0.6488 0.5745 0.1385  0.3547  0.0093  37  ASP D CA  
12557 C C   . ASP D 37  ? 1.3203 0.7026 0.5949 0.1282  0.3264  0.0154  37  ASP D C   
12558 O O   . ASP D 37  ? 1.2312 0.6062 0.4817 0.1234  0.3135  0.0079  37  ASP D O   
12559 C CB  . ASP D 37  ? 1.2386 0.6138 0.5660 0.1445  0.3457  0.0100  37  ASP D CB  
12560 C CG  . ASP D 37  ? 1.3885 0.7629 0.7592 0.1532  0.3621  0.0022  37  ASP D CG  
12561 O OD1 . ASP D 37  ? 1.4836 0.8387 0.8360 0.1564  0.3782  -0.0112 37  ASP D OD1 
12562 O OD2 . ASP D 37  ? 1.2378 0.6311 0.6612 0.1571  0.3588  0.0093  37  ASP D OD2 
12563 N N   . TYR D 38  ? 1.3295 0.7293 0.6141 0.1247  0.3164  0.0279  38  TYR D N   
12564 C CA  . TYR D 38  ? 1.2623 0.6756 0.5346 0.1162  0.2878  0.0328  38  TYR D CA  
12565 C C   . TYR D 38  ? 1.2063 0.6178 0.4529 0.1106  0.2847  0.0257  38  TYR D C   
12566 O O   . TYR D 38  ? 1.1694 0.5875 0.4031 0.1046  0.2623  0.0237  38  TYR D O   
12567 C CB  . TYR D 38  ? 1.3575 0.7905 0.6497 0.1142  0.2817  0.0457  38  TYR D CB  
12568 C CG  . TYR D 38  ? 1.2854 0.7256 0.5994 0.1167  0.2718  0.0540  38  TYR D CG  
12569 C CD1 . TYR D 38  ? 1.2438 0.6812 0.5531 0.1160  0.2526  0.0523  38  TYR D CD1 
12570 C CD2 . TYR D 38  ? 1.2230 0.6723 0.5624 0.1196  0.2819  0.0638  38  TYR D CD2 
12571 C CE1 . TYR D 38  ? 1.1583 0.6019 0.4861 0.1184  0.2427  0.0607  38  TYR D CE1 
12572 C CE2 . TYR D 38  ? 1.2411 0.6972 0.6003 0.1219  0.2726  0.0724  38  TYR D CE2 
12573 C CZ  . TYR D 38  ? 1.2337 0.6867 0.5863 0.1216  0.2528  0.0712  38  TYR D CZ  
12574 O OH  . TYR D 38  ? 1.3278 0.7906 0.7062 0.1229  0.2378  0.0796  38  TYR D OH  
12575 N N   . TYR D 39  ? 1.2556 0.6593 0.4961 0.1128  0.3072  0.0215  39  TYR D N   
12576 C CA  . TYR D 39  ? 1.3614 0.7621 0.5758 0.1085  0.3066  0.0148  39  TYR D CA  
12577 C C   . TYR D 39  ? 1.4384 0.8198 0.6356 0.1102  0.3159  0.0010  39  TYR D C   
12578 O O   . TYR D 39  ? 1.4753 0.8553 0.6493 0.1053  0.3049  -0.0056 39  TYR D O   
12579 C CB  . TYR D 39  ? 1.4223 0.8259 0.6372 0.1092  0.3249  0.0185  39  TYR D CB  
12580 C CG  . TYR D 39  ? 1.4482 0.8449 0.6354 0.1069  0.3305  0.0105  39  TYR D CG  
12581 C CD1 . TYR D 39  ? 1.4269 0.8354 0.5969 0.1012  0.3128  0.0123  39  TYR D CD1 
12582 C CD2 . TYR D 39  ? 1.4978 0.8776 0.6778 0.1108  0.3538  0.0010  39  TYR D CD2 
12583 C CE1 . TYR D 39  ? 1.3912 0.7941 0.5350 0.0995  0.3179  0.0053  39  TYR D CE1 
12584 C CE2 . TYR D 39  ? 1.5314 0.9049 0.6846 0.1087  0.3586  -0.0064 39  TYR D CE2 
12585 C CZ  . TYR D 39  ? 1.5241 0.9089 0.6583 0.1031  0.3405  -0.0040 39  TYR D CZ  
12586 O OH  . TYR D 39  ? 1.5969 0.9761 0.7038 0.1015  0.3454  -0.0111 39  TYR D OH  
12587 N N   . ASP D 40  ? 1.3296 0.6977 0.5404 0.1172  0.3364  -0.0039 40  ASP D N   
12588 C CA  . ASP D 40  ? 1.3092 0.6594 0.5072 0.1195  0.3503  -0.0178 40  ASP D CA  
12589 C C   . ASP D 40  ? 1.4357 0.7764 0.6202 0.1169  0.3334  -0.0262 40  ASP D C   
12590 O O   . ASP D 40  ? 1.4270 0.7569 0.5902 0.1144  0.3344  -0.0372 40  ASP D O   
12591 C CB  . ASP D 40  ? 1.3444 0.6868 0.5685 0.1285  0.3781  -0.0210 40  ASP D CB  
12592 C CG  . ASP D 40  ? 1.6359 0.9784 0.8604 0.1298  0.4010  -0.0217 40  ASP D CG  
12593 O OD1 . ASP D 40  ? 1.6325 0.9681 0.8303 0.1263  0.4026  -0.0286 40  ASP D OD1 
12594 O OD2 . ASP D 40  ? 1.7286 1.0788 0.9802 0.1340  0.4172  -0.0150 40  ASP D OD2 
12595 N N   . MET D 41  ? 1.4852 0.8294 0.6814 0.1174  0.3180  -0.0212 41  MET D N   
12596 C CA  . MET D 41  ? 1.2785 0.6128 0.4633 0.1147  0.3022  -0.0290 41  MET D CA  
12597 C C   . MET D 41  ? 1.3186 0.6583 0.4775 0.1050  0.2828  -0.0327 41  MET D C   
12598 O O   . MET D 41  ? 1.3799 0.7061 0.5226 0.1028  0.2821  -0.0447 41  MET D O   
12599 C CB  . MET D 41  ? 1.2420 0.5813 0.4431 0.1164  0.2873  -0.0210 41  MET D CB  
12600 C CG  . MET D 41  ? 1.3519 0.6821 0.5778 0.1271  0.3055  -0.0223 41  MET D CG  
12601 S SD  . MET D 41  ? 1.5383 0.8435 0.7588 0.1302  0.3090  -0.0392 41  MET D SD  
12602 C CE  . MET D 41  ? 1.2329 0.5391 0.4932 0.1404  0.3077  -0.0344 41  MET D CE  
12603 N N   . PRO D 42  ? 1.2854 0.6457 0.4419 0.0993  0.2668  -0.0237 42  PRO D N   
12604 C CA  . PRO D 42  ? 1.2813 0.6494 0.4164 0.0915  0.2520  -0.0285 42  PRO D CA  
12605 C C   . PRO D 42  ? 1.3723 0.7337 0.4883 0.0920  0.2687  -0.0357 42  PRO D C   
12606 O O   . PRO D 42  ? 1.5142 0.8780 0.6097 0.0865  0.2596  -0.0425 42  PRO D O   
12607 C CB  . PRO D 42  ? 1.3788 0.7735 0.5251 0.0873  0.2324  -0.0163 42  PRO D CB  
12608 C CG  . PRO D 42  ? 1.3308 0.7288 0.4972 0.0929  0.2447  -0.0063 42  PRO D CG  
12609 C CD  . PRO D 42  ? 1.2833 0.6625 0.4596 0.0997  0.2595  -0.0095 42  PRO D CD  
12610 N N   . ALA D 43  ? 1.4030 0.7570 0.5258 0.0982  0.2930  -0.0344 43  ALA D N   
12611 C CA  . ALA D 43  ? 1.3773 0.7230 0.4819 0.0989  0.3104  -0.0419 43  ALA D CA  
12612 C C   . ALA D 43  ? 1.4098 0.7346 0.5021 0.1002  0.3204  -0.0571 43  ALA D C   
12613 O O   . ALA D 43  ? 1.4454 0.7641 0.5159 0.0986  0.3275  -0.0657 43  ALA D O   
12614 C CB  . ALA D 43  ? 1.4205 0.7660 0.5393 0.1048  0.3340  -0.0358 43  ALA D CB  
12615 N N   . TYR D 44  ? 1.4041 0.7177 0.5101 0.1034  0.3211  -0.0610 44  TYR D N   
12616 C CA  . TYR D 44  ? 1.4349 0.7290 0.5305 0.1036  0.3262  -0.0759 44  TYR D CA  
12617 C C   . TYR D 44  ? 1.4732 0.7696 0.5422 0.0948  0.3070  -0.0830 44  TYR D C   
12618 O O   . TYR D 44  ? 1.5443 0.8271 0.5958 0.0936  0.3140  -0.0961 44  TYR D O   
12619 C CB  . TYR D 44  ? 1.4591 0.7433 0.5746 0.1077  0.3242  -0.0774 44  TYR D CB  
12620 C CG  . TYR D 44  ? 1.4610 0.7383 0.6052 0.1182  0.3474  -0.0767 44  TYR D CG  
12621 C CD1 . TYR D 44  ? 1.5323 0.8222 0.6950 0.1225  0.3586  -0.0655 44  TYR D CD1 
12622 C CD2 . TYR D 44  ? 1.4192 0.6792 0.5760 0.1240  0.3577  -0.0873 44  TYR D CD2 
12623 C CE1 . TYR D 44  ? 1.5090 0.7961 0.7031 0.1322  0.3798  -0.0651 44  TYR D CE1 
12624 C CE2 . TYR D 44  ? 1.4155 0.6731 0.6052 0.1345  0.3780  -0.0868 44  TYR D CE2 
12625 C CZ  . TYR D 44  ? 1.3982 0.6704 0.6073 0.1386  0.3891  -0.0758 44  TYR D CZ  
12626 O OH  . TYR D 44  ? 1.3926 0.6655 0.6396 0.1491  0.4089  -0.0757 44  TYR D OH  
12627 N N   . LEU D 45  ? 1.4814 0.7964 0.5492 0.0887  0.2830  -0.0746 45  LEU D N   
12628 C CA  . LEU D 45  ? 1.5372 0.8589 0.5858 0.0802  0.2629  -0.0805 45  LEU D CA  
12629 C C   . LEU D 45  ? 1.5513 0.8738 0.5749 0.0781  0.2694  -0.0877 45  LEU D C   
12630 O O   . LEU D 45  ? 1.5677 0.8903 0.5730 0.0722  0.2587  -0.0970 45  LEU D O   
12631 C CB  . LEU D 45  ? 1.5328 0.8796 0.5915 0.0753  0.2383  -0.0686 45  LEU D CB  
12632 C CG  . LEU D 45  ? 1.4068 0.7563 0.4746 0.0708  0.2178  -0.0682 45  LEU D CG  
12633 C CD1 . LEU D 45  ? 1.3780 0.7545 0.4629 0.0679  0.1978  -0.0544 45  LEU D CD1 
12634 C CD2 . LEU D 45  ? 1.3732 0.7186 0.4216 0.0637  0.2076  -0.0808 45  LEU D CD2 
12635 N N   . LYS D 46  ? 1.4699 0.7934 0.4925 0.0827  0.2868  -0.0835 46  LYS D N   
12636 C CA  . LYS D 46  ? 1.5098 0.8331 0.5072 0.0814  0.2940  -0.0898 46  LYS D CA  
12637 C C   . LYS D 46  ? 1.5500 0.8496 0.5352 0.0845  0.3142  -0.1046 46  LYS D C   
12638 O O   . LYS D 46  ? 1.5835 0.8789 0.5438 0.0811  0.3131  -0.1153 46  LYS D O   
12639 C CB  . LYS D 46  ? 1.5168 0.8509 0.5175 0.0847  0.3039  -0.0788 46  LYS D CB  
12640 C CG  . LYS D 46  ? 1.4602 0.8148 0.4815 0.0838  0.2890  -0.0634 46  LYS D CG  
12641 C CD  . LYS D 46  ? 1.4611 0.8220 0.4884 0.0876  0.3028  -0.0533 46  LYS D CD  
12642 C CE  . LYS D 46  ? 1.4669 0.8464 0.4797 0.0838  0.2906  -0.0484 46  LYS D CE  
12643 N NZ  . LYS D 46  ? 1.4430 0.8355 0.4713 0.0857  0.2926  -0.0344 46  LYS D NZ  
12644 N N   . ASP D 47  ? 1.5838 0.8686 0.5876 0.0911  0.3329  -0.1058 47  ASP D N   
12645 C CA  . ASP D 47  ? 1.6932 0.9567 0.6901 0.0949  0.3536  -0.1197 47  ASP D CA  
12646 C C   . ASP D 47  ? 1.7241 0.9744 0.7131 0.0911  0.3440  -0.1330 47  ASP D C   
12647 O O   . ASP D 47  ? 1.6990 0.9345 0.6721 0.0911  0.3543  -0.1468 47  ASP D O   
12648 C CB  . ASP D 47  ? 1.6049 0.8602 0.6296 0.1039  0.3769  -0.1167 47  ASP D CB  
12649 C CG  . ASP D 47  ? 1.6436 0.9114 0.6780 0.1072  0.3878  -0.1040 47  ASP D CG  
12650 O OD1 . ASP D 47  ? 1.6240 0.9071 0.6458 0.1026  0.3748  -0.0960 47  ASP D OD1 
12651 O OD2 . ASP D 47  ? 1.7382 1.0014 0.7945 0.1143  0.4096  -0.1023 47  ASP D OD2 
12652 N N   . PHE D 48  ? 1.5676 0.8224 0.5677 0.0877  0.3248  -0.1291 48  PHE D N   
12653 C CA  . PHE D 48  ? 1.5752 0.8182 0.5689 0.0830  0.3137  -0.1406 48  PHE D CA  
12654 C C   . PHE D 48  ? 1.5506 0.8115 0.5373 0.0741  0.2852  -0.1357 48  PHE D C   
12655 O O   . PHE D 48  ? 1.5536 0.8302 0.5558 0.0738  0.2731  -0.1222 48  PHE D O   
12656 C CB  . PHE D 48  ? 1.5772 0.8053 0.5961 0.0885  0.3203  -0.1419 48  PHE D CB  
12657 C CG  . PHE D 48  ? 1.6062 0.8264 0.6454 0.0990  0.3467  -0.1404 48  PHE D CG  
12658 C CD1 . PHE D 48  ? 1.5370 0.7698 0.5975 0.1042  0.3515  -0.1262 48  PHE D CD1 
12659 C CD2 . PHE D 48  ? 1.6270 0.8286 0.6665 0.1038  0.3668  -0.1535 48  PHE D CD2 
12660 C CE1 . PHE D 48  ? 1.5762 0.8044 0.6591 0.1137  0.3760  -0.1250 48  PHE D CE1 
12661 C CE2 . PHE D 48  ? 1.6077 0.8052 0.6705 0.1137  0.3911  -0.1521 48  PHE D CE2 
12662 C CZ  . PHE D 48  ? 1.5767 0.7883 0.6620 0.1185  0.3958  -0.1379 48  PHE D CZ  
12663 N N   . GLU D 49  ? 1.6927 0.9526 0.6579 0.0669  0.2746  -0.1467 49  GLU D N   
12664 C CA  . GLU D 49  ? 1.7574 1.0373 0.7176 0.0583  0.2481  -0.1432 49  GLU D CA  
12665 C C   . GLU D 49  ? 1.7320 1.0057 0.7040 0.0541  0.2338  -0.1452 49  GLU D C   
12666 O O   . GLU D 49  ? 1.7781 1.0534 0.7394 0.0463  0.2194  -0.1535 49  GLU D O   
12667 C CB  . GLU D 49  ? 1.6449 0.9298 0.5775 0.0527  0.2430  -0.1538 49  GLU D CB  
12668 C CG  . GLU D 49  ? 1.6232 0.9032 0.5386 0.0575  0.2625  -0.1575 49  GLU D CG  
12669 C CD  . GLU D 49  ? 1.8425 1.1375 0.7671 0.0625  0.2682  -0.1421 49  GLU D CD  
12670 O OE1 . GLU D 49  ? 1.8824 1.2004 0.8161 0.0597  0.2507  -0.1303 49  GLU D OE1 
12671 O OE2 . GLU D 49  ? 1.8461 1.1302 0.7700 0.0691  0.2904  -0.1421 49  GLU D OE2 
12672 N N   . ILE D 50  ? 1.7279 0.9951 0.7224 0.0593  0.2378  -0.1375 50  ILE D N   
12673 C CA  . ILE D 50  ? 1.5870 0.8497 0.5945 0.0561  0.2236  -0.1364 50  ILE D CA  
12674 C C   . ILE D 50  ? 1.4807 0.7651 0.5062 0.0562  0.2093  -0.1192 50  ILE D C   
12675 O O   . ILE D 50  ? 1.4416 0.7344 0.4771 0.0623  0.2179  -0.1088 50  ILE D O   
12676 C CB  . ILE D 50  ? 1.5638 0.7994 0.5837 0.0627  0.2395  -0.1430 50  ILE D CB  
12677 C CG1 . ILE D 50  ? 1.4859 0.7186 0.5223 0.0739  0.2604  -0.1357 50  ILE D CG1 
12678 C CG2 . ILE D 50  ? 1.5854 0.8002 0.5897 0.0608  0.2493  -0.1611 50  ILE D CG2 
12679 C CD1 . ILE D 50  ? 1.4460 0.6827 0.5072 0.0787  0.2556  -0.1231 50  ILE D CD1 
12680 N N   . LYS D 51  ? 1.5741 0.8681 0.6051 0.0493  0.1876  -0.1164 51  LYS D N   
12681 C CA  . LYS D 51  ? 1.5667 0.8860 0.6143 0.0480  0.1710  -0.1009 51  LYS D CA  
12682 C C   . LYS D 51  ? 1.4812 0.7939 0.5495 0.0556  0.1767  -0.0908 51  LYS D C   
12683 O O   . LYS D 51  ? 1.4357 0.7257 0.5085 0.0593  0.1844  -0.0958 51  LYS D O   
12684 C CB  . LYS D 51  ? 1.4201 0.7530 0.4695 0.0384  0.1470  -0.1015 51  LYS D CB  
12685 C CG  . LYS D 51  ? 1.4793 0.8201 0.5091 0.0314  0.1415  -0.1122 51  LYS D CG  
12686 C CD  . LYS D 51  ? 1.5341 0.9026 0.5621 0.0318  0.1380  -0.1050 51  LYS D CD  
12687 C CE  . LYS D 51  ? 1.4344 0.8229 0.4534 0.0235  0.1214  -0.1106 51  LYS D CE  
12688 N NZ  . LYS D 51  ? 1.5729 0.9657 0.6059 0.0174  0.1046  -0.1093 51  LYS D NZ  
12689 N N   . LEU D 52  ? 1.3256 0.6586 0.4074 0.0584  0.1735  -0.0769 52  LEU D N   
12690 C CA  . LEU D 52  ? 1.3180 0.6505 0.4205 0.0649  0.1758  -0.0658 52  LEU D CA  
12691 C C   . LEU D 52  ? 1.2383 0.6005 0.3572 0.0610  0.1549  -0.0522 52  LEU D C   
12692 O O   . LEU D 52  ? 1.2532 0.6382 0.3703 0.0565  0.1461  -0.0497 52  LEU D O   
12693 C CB  . LEU D 52  ? 1.2915 0.6172 0.3985 0.0743  0.1994  -0.0629 52  LEU D CB  
12694 C CG  . LEU D 52  ? 1.3306 0.6301 0.4296 0.0801  0.2237  -0.0755 52  LEU D CG  
12695 C CD1 . LEU D 52  ? 1.3350 0.6348 0.4437 0.0887  0.2458  -0.0705 52  LEU D CD1 
12696 C CD2 . LEU D 52  ? 1.3321 0.6100 0.4392 0.0835  0.2256  -0.0816 52  LEU D CD2 
12697 N N   . ASN D 53  ? 1.2082 0.5711 0.3449 0.0634  0.1472  -0.0439 53  ASN D N   
12698 C CA  . ASN D 53  ? 1.1648 0.5567 0.3224 0.0603  0.1282  -0.0312 53  ASN D CA  
12699 C C   . ASN D 53  ? 1.1888 0.5820 0.3645 0.0682  0.1351  -0.0201 53  ASN D C   
12700 O O   . ASN D 53  ? 1.2900 0.6604 0.4646 0.0756  0.1491  -0.0216 53  ASN D O   
12701 C CB  . ASN D 53  ? 1.1452 0.5426 0.3100 0.0535  0.1074  -0.0312 53  ASN D CB  
12702 C CG  . ASN D 53  ? 1.1652 0.5648 0.3144 0.0450  0.0996  -0.0418 53  ASN D CG  
12703 O OD1 . ASN D 53  ? 1.1709 0.5885 0.3148 0.0417  0.0975  -0.0433 53  ASN D OD1 
12704 N ND2 . ASN D 53  ? 1.1774 0.5584 0.3190 0.0414  0.0953  -0.0493 53  ASN D ND2 
12705 N N   . PHE D 54  ? 1.1108 0.5322 0.3050 0.0669  0.1258  -0.0095 54  PHE D N   
12706 C CA  . PHE D 54  ? 1.0911 0.5171 0.3028 0.0736  0.1330  0.0009  54  PHE D CA  
12707 C C   . PHE D 54  ? 1.1118 0.5672 0.3514 0.0700  0.1123  0.0114  54  PHE D C   
12708 O O   . PHE D 54  ? 1.1029 0.5816 0.3501 0.0627  0.0956  0.0114  54  PHE D O   
12709 C CB  . PHE D 54  ? 1.1069 0.5361 0.3138 0.0767  0.1496  0.0021  54  PHE D CB  
12710 C CG  . PHE D 54  ? 1.1518 0.5552 0.3361 0.0805  0.1720  -0.0084 54  PHE D CG  
12711 C CD1 . PHE D 54  ? 1.2046 0.5879 0.3912 0.0893  0.1938  -0.0093 54  PHE D CD1 
12712 C CD2 . PHE D 54  ? 1.1795 0.5810 0.3431 0.0756  0.1719  -0.0180 54  PHE D CD2 
12713 C CE1 . PHE D 54  ? 1.2051 0.5678 0.3768 0.0930  0.2154  -0.0200 54  PHE D CE1 
12714 C CE2 . PHE D 54  ? 1.2204 0.5998 0.3658 0.0789  0.1924  -0.0285 54  PHE D CE2 
12715 C CZ  . PHE D 54  ? 1.2615 0.6217 0.4122 0.0875  0.2143  -0.0297 54  PHE D CZ  
12716 N N   . ASN D 55  ? 1.1282 0.5843 0.3855 0.0756  0.1146  0.0199  55  ASN D N   
12717 C CA  . ASN D 55  ? 1.0156 0.5010 0.3036 0.0729  0.0975  0.0295  55  ASN D CA  
12718 C C   . ASN D 55  ? 1.0039 0.4958 0.3051 0.0783  0.1084  0.0376  55  ASN D C   
12719 O O   . ASN D 55  ? 0.9835 0.4548 0.2796 0.0861  0.1252  0.0392  55  ASN D O   
12720 C CB  . ASN D 55  ? 0.9571 0.4395 0.2576 0.0731  0.0850  0.0320  55  ASN D CB  
12721 C CG  . ASN D 55  ? 0.9805 0.4977 0.3165 0.0689  0.0667  0.0401  55  ASN D CG  
12722 O OD1 . ASN D 55  ? 1.0418 0.5810 0.3900 0.0614  0.0509  0.0389  55  ASN D OD1 
12723 N ND2 . ASN D 55  ? 0.9438 0.4678 0.2985 0.0737  0.0699  0.0481  55  ASN D ND2 
12724 N N   . LEU D 56  ? 0.9670 0.4876 0.2858 0.0742  0.1003  0.0426  56  LEU D N   
12725 C CA  . LEU D 56  ? 1.0041 0.5331 0.3368 0.0777  0.1090  0.0503  56  LEU D CA  
12726 C C   . LEU D 56  ? 1.0336 0.5937 0.3999 0.0737  0.0908  0.0574  56  LEU D C   
12727 O O   . LEU D 56  ? 0.9978 0.5829 0.3755 0.0670  0.0761  0.0571  56  LEU D O   
12728 C CB  . LEU D 56  ? 1.0078 0.5405 0.3282 0.0767  0.1192  0.0491  56  LEU D CB  
12729 C CG  . LEU D 56  ? 1.2476 0.7537 0.5413 0.0816  0.1433  0.0440  56  LEU D CG  
12730 C CD1 . LEU D 56  ? 1.1952 0.6927 0.4970 0.0883  0.1625  0.0500  56  LEU D CD1 
12731 C CD2 . LEU D 56  ? 1.1477 0.6279 0.4193 0.0833  0.1496  0.0346  56  LEU D CD2 
12732 N N   . THR D 57  ? 0.9695 0.5295 0.3531 0.0778  0.0926  0.0637  57  THR D N   
12733 C CA  . THR D 57  ? 0.8497 0.4401 0.2669 0.0737  0.0765  0.0698  57  THR D CA  
12734 C C   . THR D 57  ? 0.8694 0.4793 0.2961 0.0709  0.0782  0.0735  57  THR D C   
12735 O O   . THR D 57  ? 0.8814 0.4779 0.2949 0.0749  0.0952  0.0749  57  THR D O   
12736 C CB  . THR D 57  ? 0.8105 0.3967 0.2441 0.0787  0.0777  0.0758  57  THR D CB  
12737 O OG1 . THR D 57  ? 0.8956 0.4604 0.3171 0.0864  0.0996  0.0790  57  THR D OG1 
12738 C CG2 . THR D 57  ? 0.8127 0.3854 0.2427 0.0805  0.0708  0.0732  57  THR D CG2 
12739 N N   . PRO D 58  ? 0.7787 0.4200 0.2287 0.0642  0.0623  0.0754  58  PRO D N   
12740 C CA  . PRO D 58  ? 0.7712 0.4295 0.2285 0.0617  0.0638  0.0791  58  PRO D CA  
12741 C C   . PRO D 58  ? 0.7704 0.4245 0.2358 0.0654  0.0741  0.0853  58  PRO D C   
12742 O O   . PRO D 58  ? 0.8159 0.4692 0.2746 0.0658  0.0835  0.0876  58  PRO D O   
12743 C CB  . PRO D 58  ? 0.7898 0.4774 0.2708 0.0555  0.0459  0.0801  58  PRO D CB  
12744 C CG  . PRO D 58  ? 0.7365 0.4231 0.2168 0.0535  0.0365  0.0753  58  PRO D CG  
12745 C CD  . PRO D 58  ? 0.7465 0.4088 0.2168 0.0586  0.0441  0.0741  58  PRO D CD  
12746 N N   . VAL D 59  ? 0.7564 0.4079 0.2365 0.0680  0.0728  0.0885  59  VAL D N   
12747 C CA  . VAL D 59  ? 0.7828 0.4298 0.2713 0.0716  0.0836  0.0949  59  VAL D CA  
12748 C C   . VAL D 59  ? 0.8314 0.4496 0.2943 0.0784  0.1077  0.0947  59  VAL D C   
12749 O O   . VAL D 59  ? 0.8093 0.4251 0.2734 0.0799  0.1206  0.0991  59  VAL D O   
12750 C CB  . VAL D 59  ? 0.7418 0.3930 0.2521 0.0732  0.0763  0.0988  59  VAL D CB  
12751 C CG1 . VAL D 59  ? 0.8231 0.4527 0.3199 0.0784  0.0791  0.0958  59  VAL D CG1 
12752 C CG2 . VAL D 59  ? 0.8231 0.4710 0.3441 0.0767  0.0876  0.1063  59  VAL D CG2 
12753 N N   . LEU D 60  ? 0.8684 0.4643 0.3085 0.0822  0.1154  0.0893  60  LEU D N   
12754 C CA  . LEU D 60  ? 0.9028 0.4727 0.3195 0.0880  0.1404  0.0879  60  LEU D CA  
12755 C C   . LEU D 60  ? 0.9120 0.4847 0.3142 0.0850  0.1461  0.0854  60  LEU D C   
12756 O O   . LEU D 60  ? 0.9119 0.4725 0.3055 0.0882  0.1666  0.0869  60  LEU D O   
12757 C CB  . LEU D 60  ? 0.8946 0.4405 0.2903 0.0922  0.1468  0.0816  60  LEU D CB  
12758 C CG  . LEU D 60  ? 0.9378 0.4574 0.3113 0.0982  0.1748  0.0784  60  LEU D CG  
12759 C CD1 . LEU D 60  ? 0.9414 0.4555 0.3294 0.1041  0.1952  0.0861  60  LEU D CD1 
12760 C CD2 . LEU D 60  ? 0.9929 0.4904 0.3467 0.1015  0.1785  0.0711  60  LEU D CD2 
12761 N N   . ILE D 61  ? 0.8966 0.4864 0.2980 0.0788  0.1290  0.0822  61  ILE D N   
12762 C CA  . ILE D 61  ? 0.8914 0.4852 0.2790 0.0763  0.1329  0.0809  61  ILE D CA  
12763 C C   . ILE D 61  ? 0.9043 0.5072 0.3040 0.0760  0.1390  0.0879  61  ILE D C   
12764 O O   . ILE D 61  ? 0.9414 0.5332 0.3268 0.0780  0.1556  0.0885  61  ILE D O   
12765 C CB  . ILE D 61  ? 0.8791 0.4937 0.2688 0.0700  0.1130  0.0777  61  ILE D CB  
12766 C CG1 . ILE D 61  ? 0.8759 0.4833 0.2587 0.0694  0.1050  0.0714  61  ILE D CG1 
12767 C CG2 . ILE D 61  ? 0.8998 0.5150 0.2700 0.0685  0.1182  0.0758  61  ILE D CG2 
12768 C CD1 . ILE D 61  ? 0.9190 0.4983 0.2708 0.0731  0.1201  0.0646  61  ILE D CD1 
12769 N N   . ASP D 62  ? 0.8482 0.4709 0.2747 0.0731  0.1261  0.0929  62  ASP D N   
12770 C CA  . ASP D 62  ? 0.9245 0.5562 0.3629 0.0719  0.1302  0.0993  62  ASP D CA  
12771 C C   . ASP D 62  ? 0.9350 0.5463 0.3680 0.0772  0.1542  0.1027  62  ASP D C   
12772 O O   . ASP D 62  ? 0.9094 0.5199 0.3407 0.0769  0.1647  0.1063  62  ASP D O   
12773 C CB  . ASP D 62  ? 0.9281 0.5829 0.3969 0.0679  0.1132  0.1034  62  ASP D CB  
12774 C CG  . ASP D 62  ? 0.9533 0.6320 0.4331 0.0620  0.0919  0.1006  62  ASP D CG  
12775 O OD1 . ASP D 62  ? 1.1025 0.7808 0.5656 0.0612  0.0907  0.0976  62  ASP D OD1 
12776 O OD2 . ASP D 62  ? 0.7859 0.4796 0.2879 0.0595  0.0782  0.1015  62  ASP D OD2 
12777 N N   . GLN D 63  ? 0.8818 0.4769 0.3137 0.0822  0.1644  0.1020  63  GLN D N   
12778 C CA  . GLN D 63  ? 0.8970 0.4757 0.3299 0.0872  0.1895  0.1059  63  GLN D CA  
12779 C C   . GLN D 63  ? 1.0053 0.5653 0.4136 0.0899  0.2109  0.1016  63  GLN D C   
12780 O O   . GLN D 63  ? 1.0422 0.5970 0.4516 0.0907  0.2294  0.1049  63  GLN D O   
12781 C CB  . GLN D 63  ? 0.8903 0.4608 0.3347 0.0921  0.1936  0.1079  63  GLN D CB  
12782 C CG  . GLN D 63  ? 0.8495 0.4399 0.3203 0.0891  0.1725  0.1128  63  GLN D CG  
12783 C CD  . GLN D 63  ? 0.9165 0.5004 0.3978 0.0939  0.1709  0.1150  63  GLN D CD  
12784 O OE1 . GLN D 63  ? 0.8948 0.4763 0.3944 0.0973  0.1812  0.1225  63  GLN D OE1 
12785 N NE2 . GLN D 63  ? 0.8999 0.4813 0.3715 0.0939  0.1576  0.1094  63  GLN D NE2 
12786 N N   . ILE D 64  ? 0.9925 0.5430 0.3794 0.0906  0.2086  0.0940  64  ILE D N   
12787 C CA  . ILE D 64  ? 0.9960 0.5306 0.3590 0.0922  0.2269  0.0891  64  ILE D CA  
12788 C C   . ILE D 64  ? 1.0020 0.5466 0.3585 0.0883  0.2242  0.0913  64  ILE D C   
12789 O O   . ILE D 64  ? 1.0309 0.5655 0.3776 0.0897  0.2437  0.0917  64  ILE D O   
12790 C CB  . ILE D 64  ? 1.0123 0.5362 0.3537 0.0928  0.2224  0.0801  64  ILE D CB  
12791 C CG1 . ILE D 64  ? 1.0036 0.5182 0.3517 0.0967  0.2220  0.0785  64  ILE D CG1 
12792 C CG2 . ILE D 64  ? 1.0601 0.5662 0.3783 0.0951  0.2439  0.0743  64  ILE D CG2 
12793 C CD1 . ILE D 64  ? 1.0039 0.5156 0.3375 0.0947  0.2061  0.0710  64  ILE D CD1 
12794 N N   . GLN D 65  ? 0.9896 0.5547 0.3526 0.0834  0.2008  0.0927  65  GLN D N   
12795 C CA  . GLN D 65  ? 1.0022 0.5781 0.3610 0.0801  0.1975  0.0957  65  GLN D CA  
12796 C C   . GLN D 65  ? 0.9795 0.5547 0.3513 0.0807  0.2107  0.1030  65  GLN D C   
12797 O O   . GLN D 65  ? 1.1000 0.6692 0.4603 0.0810  0.2237  0.1048  65  GLN D O   
12798 C CB  . GLN D 65  ? 1.0404 0.6411 0.4103 0.0749  0.1712  0.0963  65  GLN D CB  
12799 C CG  . GLN D 65  ? 1.0373 0.6417 0.3966 0.0731  0.1579  0.0894  65  GLN D CG  
12800 C CD  . GLN D 65  ? 1.1346 0.7646 0.5016 0.0677  0.1375  0.0903  65  GLN D CD  
12801 O OE1 . GLN D 65  ? 1.3248 0.9693 0.7098 0.0658  0.1291  0.0956  65  GLN D OE1 
12802 N NE2 . GLN D 65  ? 1.1894 0.8220 0.5409 0.0660  0.1308  0.0849  65  GLN D NE2 
12803 N N   . GLU D 66  ? 1.0346 0.6160 0.4306 0.0808  0.2076  0.1074  66  GLU D N   
12804 C CA  . GLU D 66  ? 1.0115 0.5931 0.4222 0.0806  0.2199  0.1144  66  GLU D CA  
12805 C C   . GLU D 66  ? 1.0276 0.5890 0.4317 0.0846  0.2497  0.1145  66  GLU D C   
12806 O O   . GLU D 66  ? 1.0508 0.6091 0.4565 0.0839  0.2641  0.1186  66  GLU D O   
12807 C CB  . GLU D 66  ? 0.9166 0.5097 0.3549 0.0796  0.2099  0.1187  66  GLU D CB  
12808 C CG  . GLU D 66  ? 1.0182 0.6175 0.4736 0.0772  0.2151  0.1259  66  GLU D CG  
12809 C CD  . GLU D 66  ? 1.1140 0.7249 0.5965 0.0759  0.2049  0.1301  66  GLU D CD  
12810 O OE1 . GLU D 66  ? 1.1132 0.7312 0.6012 0.0760  0.1888  0.1275  66  GLU D OE1 
12811 O OE2 . GLU D 66  ? 1.1227 0.7356 0.6211 0.0743  0.2128  0.1361  66  GLU D OE2 
12812 N N   . TYR D 67  ? 1.0317 0.5797 0.4301 0.0888  0.2603  0.1098  67  TYR D N   
12813 C CA  . TYR D 67  ? 1.1393 0.6703 0.5345 0.0925  0.2902  0.1087  67  TYR D CA  
12814 C C   . TYR D 67  ? 1.1521 0.6746 0.5217 0.0919  0.2994  0.1053  67  TYR D C   
12815 O O   . TYR D 67  ? 1.1447 0.6593 0.5153 0.0926  0.3218  0.1072  67  TYR D O   
12816 C CB  . TYR D 67  ? 1.0392 0.5586 0.4343 0.0973  0.2988  0.1037  67  TYR D CB  
12817 C CG  . TYR D 67  ? 1.0184 0.5411 0.4429 0.0998  0.3054  0.1091  67  TYR D CG  
12818 C CD1 . TYR D 67  ? 1.0262 0.5478 0.4729 0.1009  0.3301  0.1138  67  TYR D CD1 
12819 C CD2 . TYR D 67  ? 1.0142 0.5427 0.4467 0.1008  0.2870  0.1099  67  TYR D CD2 
12820 C CE1 . TYR D 67  ? 1.0064 0.5338 0.4840 0.1029  0.3365  0.1196  67  TYR D CE1 
12821 C CE2 . TYR D 67  ? 1.0133 0.5454 0.4730 0.1033  0.2923  0.1162  67  TYR D CE2 
12822 C CZ  . TYR D 67  ? 0.9802 0.5124 0.4633 0.1044  0.3173  0.1213  67  TYR D CZ  
12823 O OH  . TYR D 67  ? 1.0032 0.5414 0.5179 0.1066  0.3230  0.1288  67  TYR D OH  
12824 N N   . ALA D 68  ? 1.0935 0.6187 0.4416 0.0903  0.2826  0.1005  68  ALA D N   
12825 C CA  . ALA D 68  ? 1.1061 0.6240 0.4284 0.0900  0.2901  0.0974  68  ALA D CA  
12826 C C   . ALA D 68  ? 1.1512 0.6773 0.4736 0.0871  0.2883  0.1040  68  ALA D C   
12827 O O   . ALA D 68  ? 1.2668 0.7839 0.5732 0.0877  0.3033  0.1041  68  ALA D O   
12828 C CB  . ALA D 68  ? 1.1087 0.6290 0.4103 0.0888  0.2726  0.0906  68  ALA D CB  
12829 N N   . GLN D 69  ? 1.0939 0.6366 0.4336 0.0841  0.2706  0.1093  69  GLN D N   
12830 C CA  . GLN D 69  ? 1.0738 0.6246 0.4141 0.0814  0.2673  0.1154  69  GLN D CA  
12831 C C   . GLN D 69  ? 1.1840 0.7276 0.5378 0.0817  0.2883  0.1213  69  GLN D C   
12832 O O   . GLN D 69  ? 1.3315 0.8785 0.6845 0.0797  0.2888  0.1265  69  GLN D O   
12833 C CB  . GLN D 69  ? 1.0334 0.6058 0.3892 0.0778  0.2408  0.1180  69  GLN D CB  
12834 C CG  . GLN D 69  ? 1.1120 0.6964 0.4533 0.0755  0.2231  0.1162  69  GLN D CG  
12835 C CD  . GLN D 69  ? 1.2073 0.8151 0.5683 0.0717  0.1980  0.1178  69  GLN D CD  
12836 O OE1 . GLN D 69  ? 1.1381 0.7556 0.5122 0.0695  0.1933  0.1234  69  GLN D OE1 
12837 N NE2 . GLN D 69  ? 1.1748 0.7914 0.5384 0.0706  0.1826  0.1128  69  GLN D NE2 
12838 N N   . GLY D 70  ? 1.2242 0.7588 0.5918 0.0839  0.3060  0.1208  70  GLY D N   
12839 C CA  . GLY D 70  ? 1.2155 0.7463 0.6020 0.0833  0.3261  0.1264  70  GLY D CA  
12840 C C   . GLY D 70  ? 1.1858 0.7302 0.5991 0.0804  0.3148  0.1324  70  GLY D C   
12841 O O   . GLY D 70  ? 1.1430 0.6860 0.5751 0.0789  0.3306  0.1374  70  GLY D O   
12842 N N   . LYS D 71  ? 1.0398 0.5983 0.4569 0.0790  0.2884  0.1318  71  LYS D N   
12843 C CA  . LYS D 71  ? 1.0343 0.6070 0.4753 0.0757  0.2753  0.1370  71  LYS D CA  
12844 C C   . LYS D 71  ? 1.0446 0.6180 0.5106 0.0769  0.2815  0.1387  71  LYS D C   
12845 O O   . LYS D 71  ? 1.1584 0.7391 0.6470 0.0742  0.2815  0.1443  71  LYS D O   
12846 C CB  . LYS D 71  ? 1.0616 0.6512 0.5004 0.0734  0.2452  0.1353  71  LYS D CB  
12847 C CG  . LYS D 71  ? 1.0669 0.6647 0.4987 0.0704  0.2360  0.1381  71  LYS D CG  
12848 C CD  . LYS D 71  ? 0.9759 0.5845 0.3940 0.0696  0.2157  0.1338  71  LYS D CD  
12849 C CE  . LYS D 71  ? 1.1021 0.7171 0.5111 0.0675  0.2104  0.1371  71  LYS D CE  
12850 N NZ  . LYS D 71  ? 1.0567 0.6547 0.4515 0.0691  0.2330  0.1404  71  LYS D NZ  
12851 N N   . ALA D 72  ? 1.0490 0.6149 0.5118 0.0809  0.2871  0.1343  72  ALA D N   
12852 C CA  . ALA D 72  ? 1.0064 0.5748 0.4928 0.0827  0.2894  0.1363  72  ALA D CA  
12853 C C   . ALA D 72  ? 0.9673 0.5332 0.4792 0.0820  0.3143  0.1420  72  ALA D C   
12854 O O   . ALA D 72  ? 0.9962 0.5529 0.5047 0.0820  0.3369  0.1416  72  ALA D O   
12855 C CB  . ALA D 72  ? 0.9695 0.5277 0.4453 0.0878  0.2938  0.1304  72  ALA D CB  
12856 N N   . LYS D 73  ? 0.9406 0.5163 0.4809 0.0809  0.3096  0.1473  73  LYS D N   
12857 C CA  . LYS D 73  ? 0.9519 0.5293 0.5250 0.0793  0.3319  0.1531  73  LYS D CA  
12858 C C   . LYS D 73  ? 0.9295 0.5086 0.5252 0.0834  0.3372  0.1548  73  LYS D C   
12859 O O   . LYS D 73  ? 0.9012 0.4905 0.5175 0.0822  0.3228  0.1602  73  LYS D O   
12860 C CB  . LYS D 73  ? 0.9568 0.5458 0.5477 0.0731  0.3217  0.1595  73  LYS D CB  
12861 C CG  . LYS D 73  ? 1.1023 0.6951 0.6694 0.0702  0.3005  0.1580  73  LYS D CG  
12862 C CD  . LYS D 73  ? 1.1043 0.7049 0.6882 0.0642  0.2978  0.1638  73  LYS D CD  
12863 C CE  . LYS D 73  ? 0.9482 0.5577 0.5678 0.0619  0.2983  0.1695  73  LYS D CE  
12864 N NZ  . LYS D 73  ? 0.8732 0.4902 0.5071 0.0555  0.2921  0.1743  73  LYS D NZ  
12865 N N   . ASP D 74  ? 1.0355 0.6046 0.6282 0.0883  0.3581  0.1502  74  ASP D N   
12866 C CA  . ASP D 74  ? 0.9436 0.5136 0.5590 0.0933  0.3673  0.1516  74  ASP D CA  
12867 C C   . ASP D 74  ? 1.0197 0.6001 0.6833 0.0914  0.3931  0.1559  74  ASP D C   
12868 O O   . ASP D 74  ? 1.1422 0.7195 0.8104 0.0902  0.4181  0.1528  74  ASP D O   
12869 C CB  . ASP D 74  ? 0.9675 0.5237 0.5586 0.0997  0.3770  0.1426  74  ASP D CB  
12870 C CG  . ASP D 74  ? 1.0079 0.5709 0.6277 0.1056  0.3725  0.1387  74  ASP D CG  
12871 O OD1 . ASP D 74  ? 1.0823 0.6654 0.7586 0.1058  0.3731  0.1378  74  ASP D OD1 
12872 O OD2 . ASP D 74  ? 1.0221 0.5753 0.6158 0.1098  0.3618  0.1330  74  ASP D OD2 
12873 N N   . VAL D 75  ? 0.9558 0.5579 0.6685 0.0907  0.3747  0.1562  75  VAL D N   
12874 C CA  . VAL D 75  ? 0.9664 0.5884 0.7381 0.0877  0.3872  0.1553  75  VAL D CA  
12875 C C   . VAL D 75  ? 0.9383 0.5657 0.7388 0.0936  0.4079  0.1454  75  VAL D C   
12876 O O   . VAL D 75  ? 1.0005 0.6346 0.8293 0.0912  0.4328  0.1441  75  VAL D O   
12877 C CB  . VAL D 75  ? 0.9374 0.5815 0.7519 0.0858  0.3602  0.1579  75  VAL D CB  
12878 C CG1 . VAL D 75  ? 0.8456 0.5021 0.6883 0.0935  0.3434  0.1508  75  VAL D CG1 
12879 C CG2 . VAL D 75  ? 0.8510 0.5131 0.7155 0.0792  0.3717  0.1600  75  VAL D CG2 
12880 N N   . PHE D 76  ? 0.9335 0.5574 0.7272 0.1014  0.3990  0.1381  76  PHE D N   
12881 C CA  . PHE D 76  ? 0.9256 0.5534 0.7458 0.1081  0.4183  0.1282  76  PHE D CA  
12882 C C   . PHE D 76  ? 0.9675 0.5734 0.7464 0.1090  0.4478  0.1248  76  PHE D C   
12883 O O   . PHE D 76  ? 0.9849 0.5950 0.7887 0.1110  0.4742  0.1196  76  PHE D O   
12884 C CB  . PHE D 76  ? 0.9120 0.5422 0.7401 0.1163  0.3987  0.1216  76  PHE D CB  
12885 C CG  . PHE D 76  ? 1.0176 0.6538 0.8796 0.1241  0.4161  0.1116  76  PHE D CG  
12886 C CD1 . PHE D 76  ? 1.0923 0.7539 1.0196 0.1257  0.4208  0.1099  76  PHE D CD1 
12887 C CD2 . PHE D 76  ? 1.1174 0.7341 0.9463 0.1302  0.4278  0.1035  76  PHE D CD2 
12888 C CE1 . PHE D 76  ? 1.0045 0.6724 0.9645 0.1338  0.4371  0.1008  76  PHE D CE1 
12889 C CE2 . PHE D 76  ? 0.9909 0.6120 0.8508 0.1380  0.4446  0.0941  76  PHE D CE2 
12890 C CZ  . PHE D 76  ? 1.0113 0.6582 0.9371 0.1402  0.4494  0.0930  76  PHE D CZ  
12891 N N   . LEU D 77  ? 0.9851 0.5682 0.7007 0.1080  0.4436  0.1276  77  LEU D N   
12892 C CA  . LEU D 77  ? 1.0273 0.5886 0.6986 0.1087  0.4707  0.1250  77  LEU D CA  
12893 C C   . LEU D 77  ? 1.0433 0.6076 0.7283 0.1026  0.4931  0.1292  77  LEU D C   
12894 O O   . LEU D 77  ? 1.1828 0.7404 0.8648 0.1036  0.5130  0.1227  77  LEU D O   
12895 C CB  . LEU D 77  ? 1.1659 0.7086 0.7755 0.1074  0.4506  0.1258  77  LEU D CB  
12896 C CG  . LEU D 77  ? 1.1665 0.6924 0.7385 0.1084  0.4572  0.1170  77  LEU D CG  
12897 C CD1 . LEU D 77  ? 1.0917 0.6104 0.6651 0.1160  0.4727  0.1068  77  LEU D CD1 
12898 C CD2 . LEU D 77  ? 1.1745 0.6920 0.7009 0.1058  0.4287  0.1166  77  LEU D CD2 
12899 N N   . GLU D 78  ? 1.0660 0.6410 0.7693 0.0956  0.4844  0.1385  78  GLU D N   
12900 C CA  . GLU D 78  ? 1.0851 0.6665 0.8127 0.0892  0.5012  0.1407  78  GLU D CA  
12901 C C   . GLU D 78  ? 1.0634 0.6630 0.8504 0.0907  0.5281  0.1376  78  GLU D C   
12902 O O   . GLU D 78  ? 1.0985 0.6983 0.8988 0.0886  0.5493  0.1339  78  GLU D O   
12903 C CB  . GLU D 78  ? 1.0093 0.5977 0.7429 0.0814  0.4839  0.1502  78  GLU D CB  
12904 C CG  . GLU D 78  ? 1.1077 0.6892 0.8263 0.0753  0.4889  0.1514  78  GLU D CG  
12905 C CD  . GLU D 78  ? 1.1681 0.7300 0.8325 0.0782  0.4839  0.1464  78  GLU D CD  
12906 O OE1 . GLU D 78  ? 1.2333 0.7885 0.8638 0.0816  0.4618  0.1448  78  GLU D OE1 
12907 O OE2 . GLU D 78  ? 1.1104 0.6646 0.7679 0.0767  0.5018  0.1441  78  GLU D OE2 
12908 N N   . ALA D 79  ? 1.0349 0.6554 0.8675 0.0946  0.5084  0.1331  79  ALA D N   
12909 C CA  . ALA D 79  ? 1.0396 0.6840 0.9389 0.0968  0.5203  0.1268  79  ALA D CA  
12910 C C   . ALA D 79  ? 1.0826 0.7193 0.9795 0.1036  0.5490  0.1176  79  ALA D C   
12911 O O   . ALA D 79  ? 1.0994 0.7542 1.0488 0.1051  0.5662  0.1127  79  ALA D O   
12912 C CB  . ALA D 79  ? 0.9900 0.6557 0.9312 0.1014  0.4905  0.1237  79  ALA D CB  
12913 N N   . ILE D 80  ? 1.2069 0.8177 1.0449 0.1077  0.5544  0.1148  80  ILE D N   
12914 C CA  . ILE D 80  ? 1.0817 0.6806 0.9076 0.1133  0.5848  0.1064  80  ILE D CA  
12915 C C   . ILE D 80  ? 1.1146 0.6990 0.9114 0.1057  0.5937  0.1085  80  ILE D C   
12916 O O   . ILE D 80  ? 1.2869 0.8750 1.1066 0.1050  0.6159  0.1043  80  ILE D O   
12917 C CB  . ILE D 80  ? 1.0943 0.6742 0.8769 0.1213  0.5749  0.0989  80  ILE D CB  
12918 C CG1 . ILE D 80  ? 1.0949 0.6898 0.9106 0.1269  0.5454  0.0950  80  ILE D CG1 
12919 C CG2 . ILE D 80  ? 1.1311 0.7005 0.9071 0.1254  0.5957  0.0886  80  ILE D CG2 
12920 C CD1 . ILE D 80  ? 1.0978 0.7196 0.9866 0.1309  0.5511  0.0904  80  ILE D CD1 
12921 N N   . ARG D 81  ? 1.1196 0.6883 0.8672 0.1008  0.5754  0.1144  81  ARG D N   
12922 C CA  . ARG D 81  ? 1.1657 0.7194 0.8805 0.0958  0.5811  0.1156  81  ARG D CA  
12923 C C   . ARG D 81  ? 1.1555 0.7210 0.9089 0.0889  0.5986  0.1196  81  ARG D C   
12924 O O   . ARG D 81  ? 1.3235 0.8788 1.0624 0.0863  0.6129  0.1186  81  ARG D O   
12925 C CB  . ARG D 81  ? 1.1519 0.6927 0.8165 0.0929  0.5544  0.1209  81  ARG D CB  
12926 C CG  . ARG D 81  ? 1.2215 0.7495 0.8546 0.0883  0.5568  0.1233  81  ARG D CG  
12927 C CD  . ARG D 81  ? 1.2259 0.7460 0.8161 0.0867  0.5282  0.1273  81  ARG D CD  
12928 N NE  . ARG D 81  ? 1.3192 0.8480 0.9150 0.0877  0.5052  0.1301  81  ARG D NE  
12929 C CZ  . ARG D 81  ? 1.4463 0.9689 1.0079 0.0904  0.4814  0.1281  81  ARG D CZ  
12930 N NH1 . ARG D 81  ? 1.4960 1.0050 1.0167 0.0922  0.4766  0.1232  81  ARG D NH1 
12931 N NH2 . ARG D 81  ? 1.3324 0.8638 0.9027 0.0909  0.4615  0.1313  81  ARG D NH2 
12932 N N   . LYS D 82  ? 1.1233 0.7106 0.9267 0.0856  0.5981  0.1241  82  LYS D N   
12933 C CA  . LYS D 82  ? 1.1250 0.7249 0.9681 0.0779  0.6132  0.1274  82  LYS D CA  
12934 C C   . LYS D 82  ? 1.1953 0.8073 1.0827 0.0803  0.6401  0.1199  82  LYS D C   
12935 O O   . LYS D 82  ? 1.1378 0.7543 1.0380 0.0886  0.6455  0.1125  82  LYS D O   
12936 C CB  . LYS D 82  ? 1.0852 0.7058 0.9685 0.0724  0.6014  0.1345  82  LYS D CB  
12937 C CG  . LYS D 82  ? 1.0970 0.7085 0.9422 0.0706  0.5727  0.1417  82  LYS D CG  
12938 C CD  . LYS D 82  ? 1.2562 0.8643 1.0935 0.0614  0.5667  0.1487  82  LYS D CD  
12939 C CE  . LYS D 82  ? 1.3308 0.9194 1.1303 0.0603  0.5773  0.1471  82  LYS D CE  
12940 N NZ  . LYS D 82  ? 1.1148 0.7029 0.9185 0.0516  0.5776  0.1531  82  LYS D NZ  
12941 N N   . ASP D 83  ? 1.2988 0.9159 1.2097 0.0732  0.6564  0.1216  83  ASP D N   
12942 C CA  . ASP D 83  ? 1.1716 0.8037 1.1316 0.0736  0.6812  0.1154  83  ASP D CA  
12943 C C   . ASP D 83  ? 1.2087 0.8744 1.2411 0.0734  0.6801  0.1145  83  ASP D C   
12944 O O   . ASP D 83  ? 1.2071 0.8844 1.2567 0.0678  0.6656  0.1210  83  ASP D O   
12945 C CB  . ASP D 83  ? 1.2720 0.8980 1.2313 0.0653  0.6975  0.1182  83  ASP D CB  
12946 C CG  . ASP D 83  ? 1.4002 1.0363 1.3979 0.0662  0.7241  0.1113  83  ASP D CG  
12947 O OD1 . ASP D 83  ? 1.3834 1.0465 1.4455 0.0631  0.7315  0.1098  83  ASP D OD1 
12948 O OD2 . ASP D 83  ? 1.3931 1.0109 1.3574 0.0700  0.7368  0.1072  83  ASP D OD2 
12949 N N   . PRO D 84  ? 1.2014 0.8841 1.2783 0.0798  0.6936  0.1062  84  PRO D N   
12950 C CA  . PRO D 84  ? 1.1990 0.9171 1.3495 0.0810  0.6900  0.1043  84  PRO D CA  
12951 C C   . PRO D 84  ? 1.1586 0.8976 1.3575 0.0696  0.6938  0.1086  84  PRO D C   
12952 O O   . PRO D 84  ? 1.2961 1.0628 1.5468 0.0682  0.6825  0.1098  84  PRO D O   
12953 C CB  . PRO D 84  ? 1.1336 0.8618 1.3159 0.0905  0.7055  0.0937  84  PRO D CB  
12954 C CG  . PRO D 84  ? 1.2053 0.9019 1.3220 0.0967  0.7081  0.0904  84  PRO D CG  
12955 C CD  . PRO D 84  ? 1.2098 0.8802 1.2691 0.0880  0.7082  0.0975  84  PRO D CD  
12956 N N   . ASP D 85  ? 1.1061 0.8333 1.2917 0.0614  0.7088  0.1105  85  ASP D N   
12957 C CA  . ASP D 85  ? 1.0960 0.8406 1.3238 0.0496  0.7112  0.1144  85  ASP D CA  
12958 C C   . ASP D 85  ? 1.1519 0.8891 1.3550 0.0424  0.6907  0.1237  85  ASP D C   
12959 O O   . ASP D 85  ? 1.1649 0.9223 1.4114 0.0338  0.6848  0.1266  85  ASP D O   
12960 C CB  . ASP D 85  ? 1.2731 1.0062 1.4933 0.0434  0.7341  0.1135  85  ASP D CB  
12961 C CG  . ASP D 85  ? 1.2467 0.9881 1.4939 0.0498  0.7550  0.1045  85  ASP D CG  
12962 O OD1 . ASP D 85  ? 1.1411 0.9139 1.4568 0.0494  0.7599  0.0997  85  ASP D OD1 
12963 O OD2 . ASP D 85  ? 1.2190 0.9363 1.4196 0.0552  0.7656  0.1021  85  ASP D OD2 
12964 N N   . ASP D 86  ? 1.2698 0.9788 1.4044 0.0458  0.6784  0.1280  86  ASP D N   
12965 C CA  . ASP D 86  ? 1.0990 0.7999 1.2066 0.0403  0.6567  0.1367  86  ASP D CA  
12966 C C   . ASP D 86  ? 1.2322 0.9518 1.3654 0.0432  0.6367  0.1387  86  ASP D C   
12967 O O   . ASP D 86  ? 1.3522 1.0756 1.4879 0.0364  0.6198  0.1457  86  ASP D O   
12968 C CB  . ASP D 86  ? 1.0926 0.7590 1.1198 0.0434  0.6484  0.1399  86  ASP D CB  
12969 C CG  . ASP D 86  ? 1.2730 0.9208 1.2734 0.0407  0.6668  0.1389  86  ASP D CG  
12970 O OD1 . ASP D 86  ? 1.3338 0.9909 1.3682 0.0402  0.6892  0.1336  86  ASP D OD1 
12971 O OD2 . ASP D 86  ? 1.4146 1.0394 1.3611 0.0394  0.6584  0.1434  86  ASP D OD2 
12972 N N   . LEU D 87  ? 1.1913 0.9220 1.3430 0.0536  0.6378  0.1327  87  LEU D N   
12973 C CA  . LEU D 87  ? 1.0515 0.7997 1.2267 0.0582  0.6087  0.1322  87  LEU D CA  
12974 C C   . LEU D 87  ? 1.0012 0.7849 1.2524 0.0524  0.5995  0.1303  87  LEU D C   
12975 O O   . LEU D 87  ? 0.9511 0.7514 1.2487 0.0478  0.6236  0.1274  87  LEU D O   
12976 C CB  . LEU D 87  ? 1.0987 0.8471 1.2711 0.0721  0.6036  0.1234  87  LEU D CB  
12977 C CG  . LEU D 87  ? 1.1504 0.8660 1.2487 0.0787  0.6039  0.1236  87  LEU D CG  
12978 C CD1 . LEU D 87  ? 0.9841 0.7033 1.0870 0.0913  0.5878  0.1154  87  LEU D CD1 
12979 C CD2 . LEU D 87  ? 1.1174 0.8132 1.1613 0.0733  0.5837  0.1331  87  LEU D CD2 
12980 N N   . GLU D 88  ? 1.0418 0.8375 1.3054 0.0527  0.5638  0.1317  88  GLU D N   
12981 C CA  . GLU D 88  ? 1.0450 0.8733 1.3746 0.0470  0.5490  0.1303  88  GLU D CA  
12982 C C   . GLU D 88  ? 0.9754 0.8236 1.3347 0.0576  0.5197  0.1247  88  GLU D C   
12983 O O   . GLU D 88  ? 0.8475 0.6805 1.1678 0.0667  0.5042  0.1244  88  GLU D O   
12984 C CB  . GLU D 88  ? 1.0577 0.8804 1.3729 0.0350  0.5339  0.1387  88  GLU D CB  
12985 C CG  . GLU D 88  ? 1.1022 0.9552 1.4738 0.0301  0.5082  0.1373  88  GLU D CG  
12986 C CD  . GLU D 88  ? 1.0785 0.9492 1.4994 0.0171  0.5264  0.1370  88  GLU D CD  
12987 O OE1 . GLU D 88  ? 0.9325 0.8023 1.3655 0.0150  0.5602  0.1350  88  GLU D OE1 
12988 O OE2 . GLU D 88  ? 0.9477 0.8330 1.3955 0.0089  0.5070  0.1385  88  GLU D OE2 
12989 N N   . LYS D 89  ? 0.9861 0.8687 1.4155 0.0563  0.5123  0.1204  89  LYS D N   
12990 C CA  . LYS D 89  ? 0.8641 0.7693 1.3306 0.0666  0.4861  0.1153  89  LYS D CA  
12991 C C   . LYS D 89  ? 0.8371 0.7278 1.2604 0.0717  0.4524  0.1191  89  LYS D C   
12992 O O   . LYS D 89  ? 0.9169 0.8108 1.3429 0.0836  0.4375  0.1154  89  LYS D O   
12993 C CB  . LYS D 89  ? 0.9050 0.8475 1.4443 0.0607  0.4755  0.1128  89  LYS D CB  
12994 C CG  . LYS D 89  ? 0.9031 0.8691 1.5012 0.0598  0.5045  0.1064  89  LYS D CG  
12995 C CD  . LYS D 89  ? 0.8053 0.8077 1.4725 0.0515  0.4940  0.1042  89  LYS D CD  
12996 C CE  . LYS D 89  ? 0.7373 0.7623 1.4351 0.0601  0.4571  0.1018  89  LYS D CE  
12997 N NZ  . LYS D 89  ? 0.7172 0.7787 1.4819 0.0521  0.4452  0.0991  89  LYS D NZ  
12998 N N   . GLU D 90  ? 0.8369 0.7109 1.2199 0.0629  0.4410  0.1267  90  GLU D N   
12999 C CA  . GLU D 90  ? 0.8877 0.7489 1.2305 0.0667  0.4094  0.1308  90  GLU D CA  
13000 C C   . GLU D 90  ? 0.9707 0.8031 1.2535 0.0754  0.4131  0.1308  90  GLU D C   
13001 O O   . GLU D 90  ? 0.8907 0.7159 1.1482 0.0812  0.3873  0.1322  90  GLU D O   
13002 C CB  . GLU D 90  ? 0.9560 0.8074 1.2734 0.0551  0.3982  0.1388  90  GLU D CB  
13003 C CG  . GLU D 90  ? 0.8641 0.7387 1.2186 0.0518  0.3678  0.1393  90  GLU D CG  
13004 C CD  . GLU D 90  ? 0.8774 0.7462 1.2049 0.0598  0.3352  0.1411  90  GLU D CD  
13005 O OE1 . GLU D 90  ? 0.7529 0.5949 1.0202 0.0604  0.3307  0.1462  90  GLU D OE1 
13006 O OE2 . GLU D 90  ? 0.9028 0.7942 1.2695 0.0656  0.3141  0.1376  90  GLU D OE2 
13007 N N   . GLU D 91  ? 1.0581 0.8735 1.3166 0.0760  0.4442  0.1293  91  GLU D N   
13008 C CA  . GLU D 91  ? 0.9653 0.7540 1.1681 0.0840  0.4488  0.1279  91  GLU D CA  
13009 C C   . GLU D 91  ? 0.8895 0.6830 1.1138 0.0946  0.4662  0.1189  91  GLU D C   
13010 O O   . GLU D 91  ? 0.9497 0.7212 1.1304 0.1014  0.4720  0.1162  91  GLU D O   
13011 C CB  . GLU D 91  ? 1.0176 0.7772 1.1616 0.0776  0.4690  0.1335  91  GLU D CB  
13012 C CG  . GLU D 91  ? 1.1414 0.9048 1.3059 0.0685  0.4999  0.1351  91  GLU D CG  
13013 C CD  . GLU D 91  ? 1.2172 0.9566 1.3312 0.0593  0.5078  0.1443  91  GLU D CD  
13014 O OE1 . GLU D 91  ? 1.2765 1.0241 1.4143 0.0489  0.5142  0.1485  91  GLU D OE1 
13015 O OE2 . GLU D 91  ? 1.3706 1.0831 1.4219 0.0625  0.5078  0.1471  91  GLU D OE2 
13016 N N   . VAL D 92  ? 0.8389 0.6607 1.1293 0.0962  0.4746  0.1137  92  VAL D N   
13017 C CA  . VAL D 92  ? 0.8524 0.6797 1.1664 0.1072  0.4917  0.1050  92  VAL D CA  
13018 C C   . VAL D 92  ? 0.8365 0.6654 1.1516 0.1193  0.4662  0.1014  92  VAL D C   
13019 O O   . VAL D 92  ? 0.8544 0.6671 1.1450 0.1285  0.4747  0.0963  92  VAL D O   
13020 C CB  . VAL D 92  ? 0.8665 0.7252 1.2532 0.1054  0.5090  0.1007  92  VAL D CB  
13021 C CG1 . VAL D 92  ? 0.8734 0.7317 1.2741 0.1152  0.5367  0.0923  92  VAL D CG1 
13022 C CG2 . VAL D 92  ? 0.8589 0.7183 1.2486 0.0913  0.5276  0.1056  92  VAL D CG2 
13023 N N   . GLU D 93  ? 0.8567 0.7042 1.1996 0.1194  0.4349  0.1041  93  GLU D N   
13024 C CA  . GLU D 93  ? 0.8310 0.6816 1.1803 0.1311  0.4110  0.1013  93  GLU D CA  
13025 C C   . GLU D 93  ? 0.8696 0.6888 1.1510 0.1340  0.3994  0.1032  93  GLU D C   
13026 O O   . GLU D 93  ? 0.8448 0.6593 1.1225 0.1444  0.3876  0.0996  93  GLU D O   
13027 C CB  . GLU D 93  ? 0.7976 0.6744 1.1887 0.1302  0.3799  0.1044  93  GLU D CB  
13028 C CG  . GLU D 93  ? 0.9221 0.7914 1.2816 0.1202  0.3578  0.1126  93  GLU D CG  
13029 C CD  . GLU D 93  ? 0.9714 0.8560 1.3579 0.1074  0.3652  0.1156  93  GLU D CD  
13030 O OE1 . GLU D 93  ? 0.9473 0.8573 1.3916 0.1069  0.3776  0.1114  93  GLU D OE1 
13031 O OE2 . GLU D 93  ? 0.8994 0.7707 1.2504 0.0978  0.3582  0.1221  93  GLU D OE2 
13032 N N   . LYS D 94  ? 0.9446 0.7422 1.1729 0.1251  0.4026  0.1088  94  LYS D N   
13033 C CA  . LYS D 94  ? 0.8588 0.6267 1.0217 0.1276  0.3953  0.1098  94  LYS D CA  
13034 C C   . LYS D 94  ? 0.9691 0.7210 1.1146 0.1359  0.4183  0.1017  94  LYS D C   
13035 O O   . LYS D 94  ? 0.9546 0.6888 1.0657 0.1423  0.4084  0.0990  94  LYS D O   
13036 C CB  . LYS D 94  ? 0.8282 0.5771 0.9396 0.1170  0.3983  0.1172  94  LYS D CB  
13037 C CG  . LYS D 94  ? 0.8010 0.5549 0.9057 0.1102  0.3693  0.1254  94  LYS D CG  
13038 C CD  . LYS D 94  ? 0.7903 0.5756 0.9586 0.1091  0.3537  0.1259  94  LYS D CD  
13039 C CE  . LYS D 94  ? 0.7491 0.5373 0.9074 0.1014  0.3283  0.1337  94  LYS D CE  
13040 N NZ  . LYS D 94  ? 0.7635 0.5352 0.8840 0.0912  0.3410  0.1399  94  LYS D NZ  
13041 N N   . LEU D 95  ? 1.0017 0.7592 1.1706 0.1357  0.4494  0.0975  95  LEU D N   
13042 C CA  . LEU D 95  ? 0.9001 0.6430 1.0549 0.1439  0.4736  0.0891  95  LEU D CA  
13043 C C   . LEU D 95  ? 0.9941 0.7505 1.1912 0.1564  0.4666  0.0819  95  LEU D C   
13044 O O   . LEU D 95  ? 1.0335 0.7719 1.2045 0.1648  0.4678  0.0761  95  LEU D O   
13045 C CB  . LEU D 95  ? 0.9241 0.6692 1.0912 0.1395  0.5100  0.0873  95  LEU D CB  
13046 C CG  . LEU D 95  ? 0.9805 0.6948 1.0809 0.1347  0.5296  0.0889  95  LEU D CG  
13047 C CD1 . LEU D 95  ? 0.9889 0.7021 1.1013 0.1356  0.5686  0.0837  95  LEU D CD1 
13048 C CD2 . LEU D 95  ? 1.0687 0.7575 1.1152 0.1412  0.5178  0.0854  95  LEU D CD2 
13049 N N   . ILE D 96  ? 0.9460 0.7339 1.2089 0.1581  0.4593  0.0821  96  ILE D N   
13050 C CA  . ILE D 96  ? 0.9321 0.7344 1.2391 0.1711  0.4543  0.0758  96  ILE D CA  
13051 C C   . ILE D 96  ? 1.0677 0.8614 1.3553 0.1771  0.4219  0.0774  96  ILE D C   
13052 O O   . ILE D 96  ? 1.0916 0.8774 1.3799 0.1885  0.4213  0.0716  96  ILE D O   
13053 C CB  . ILE D 96  ? 0.8419 0.6822 1.2253 0.1712  0.4544  0.0757  96  ILE D CB  
13054 C CG1 . ILE D 96  ? 0.8251 0.6837 1.2279 0.1659  0.4211  0.0830  96  ILE D CG1 
13055 C CG2 . ILE D 96  ? 0.8581 0.7059 1.2574 0.1628  0.4862  0.0751  96  ILE D CG2 
13056 C CD1 . ILE D 96  ? 0.8341 0.7093 1.2736 0.1771  0.3949  0.0820  96  ILE D CD1 
13057 N N   . GLU D 97  ? 1.0086 0.8026 1.2780 0.1697  0.3955  0.0854  97  GLU D N   
13058 C CA  . GLU D 97  ? 1.0248 0.8112 1.2763 0.1747  0.3647  0.0877  97  GLU D CA  
13059 C C   . GLU D 97  ? 0.9358 0.6881 1.1219 0.1761  0.3666  0.0853  97  GLU D C   
13060 O O   . GLU D 97  ? 0.8663 0.6094 1.0391 0.1823  0.3470  0.0848  97  GLU D O   
13061 C CB  . GLU D 97  ? 1.0513 0.8484 1.3027 0.1662  0.3369  0.0967  97  GLU D CB  
13062 C CG  . GLU D 97  ? 1.2535 1.0589 1.5202 0.1732  0.3045  0.0991  97  GLU D CG  
13063 C CD  . GLU D 97  ? 1.3580 1.1978 1.6935 0.1766  0.2946  0.0995  97  GLU D CD  
13064 O OE1 . GLU D 97  ? 1.3680 1.2265 1.7397 0.1720  0.3116  0.0982  97  GLU D OE1 
13065 O OE2 . GLU D 97  ? 1.2550 1.1035 1.6083 0.1838  0.2697  0.1013  97  GLU D OE2 
13066 N N   . PHE D 98  ? 0.9111 0.6442 1.0558 0.1702  0.3896  0.0840  98  PHE D N   
13067 C CA  . PHE D 98  ? 0.9566 0.6581 1.0399 0.1717  0.3926  0.0804  98  PHE D CA  
13068 C C   . PHE D 98  ? 0.9367 0.6286 1.0263 0.1824  0.4124  0.0699  98  PHE D C   
13069 O O   . PHE D 98  ? 0.9117 0.5841 0.9713 0.1878  0.4046  0.0656  98  PHE D O   
13070 C CB  . PHE D 98  ? 0.8950 0.5789 0.9273 0.1617  0.4073  0.0836  98  PHE D CB  
13071 C CG  . PHE D 98  ? 0.9465 0.6023 0.9125 0.1600  0.3971  0.0836  98  PHE D CG  
13072 C CD1 . PHE D 98  ? 0.9559 0.6104 0.9038 0.1571  0.3661  0.0899  98  PHE D CD1 
13073 C CD2 . PHE D 98  ? 1.0469 0.6783 0.9692 0.1615  0.4182  0.0770  98  PHE D CD2 
13074 C CE1 . PHE D 98  ? 1.0999 0.7306 0.9895 0.1553  0.3565  0.0897  98  PHE D CE1 
13075 C CE2 . PHE D 98  ? 1.1379 0.7450 1.0005 0.1597  0.4078  0.0763  98  PHE D CE2 
13076 C CZ  . PHE D 98  ? 1.2999 0.9072 1.1472 0.1565  0.3768  0.0827  98  PHE D CZ  
13077 N N   . THR D 99  ? 0.9692 0.6743 1.0977 0.1856  0.4385  0.0653  99  THR D N   
13078 C CA  . THR D 99  ? 0.9381 0.6357 1.0775 0.1968  0.4577  0.0550  99  THR D CA  
13079 C C   . THR D 99  ? 0.9387 0.6512 1.1243 0.2083  0.4397  0.0531  99  THR D C   
13080 O O   . THR D 99  ? 1.0613 0.7590 1.2393 0.2181  0.4429  0.0458  99  THR D O   
13081 C CB  . THR D 99  ? 0.9857 0.6932 1.1525 0.1968  0.4926  0.0508  99  THR D CB  
13082 O OG1 . THR D 99  ? 0.9691 0.7057 1.1820 0.1903  0.4900  0.0573  99  THR D OG1 
13083 C CG2 . THR D 99  ? 0.9914 0.6727 1.0998 0.1904  0.5163  0.0490  99  THR D CG2 
13084 N N   . LYS D 100 ? 0.8877 0.6286 1.1209 0.2074  0.4208  0.0594  100 LYS D N   
13085 C CA  . LYS D 100 ? 0.8875 0.6419 1.1600 0.2181  0.3993  0.0594  100 LYS D CA  
13086 C C   . LYS D 100 ? 0.9474 0.6792 1.1768 0.2200  0.3750  0.0609  100 LYS D C   
13087 O O   . LYS D 100 ? 0.9492 0.6779 1.1931 0.2312  0.3659  0.0578  100 LYS D O   
13088 C CB  . LYS D 100 ? 0.8362 0.6250 1.1618 0.2151  0.3818  0.0664  100 LYS D CB  
13089 C CG  . LYS D 100 ? 0.8111 0.6132 1.1657 0.2232  0.3501  0.0700  100 LYS D CG  
13090 C CD  . LYS D 100 ? 1.1032 0.8925 1.4155 0.2166  0.3204  0.0775  100 LYS D CD  
13091 C CE  . LYS D 100 ? 0.9767 0.7880 1.3256 0.2203  0.2895  0.0836  100 LYS D CE  
13092 N NZ  . LYS D 100 ? 0.7508 0.5464 1.0548 0.2149  0.2631  0.0902  100 LYS D NZ  
13093 N N   . LEU D 101 ? 1.0329 0.7484 1.2095 0.2094  0.3647  0.0658  101 LEU D N   
13094 C CA  . LEU D 101 ? 0.9014 0.5989 1.0402 0.2097  0.3394  0.0683  101 LEU D CA  
13095 C C   . LEU D 101 ? 0.9508 0.6183 1.0509 0.2153  0.3510  0.0594  101 LEU D C   
13096 O O   . LEU D 101 ? 1.0934 0.7530 1.1974 0.2237  0.3385  0.0570  101 LEU D O   
13097 C CB  . LEU D 101 ? 0.8948 0.5866 0.9921 0.1967  0.3252  0.0764  101 LEU D CB  
13098 C CG  . LEU D 101 ? 0.9045 0.5782 0.9583 0.1947  0.2995  0.0797  101 LEU D CG  
13099 C CD1 . LEU D 101 ? 0.8096 0.4940 0.8560 0.1850  0.2782  0.0899  101 LEU D CD1 
13100 C CD2 . LEU D 101 ? 0.9479 0.5905 0.9404 0.1920  0.3102  0.0742  101 LEU D CD2 
13101 N N   . ASN D 102 ? 0.9906 0.6404 1.0531 0.2107  0.3752  0.0544  102 ASN D N   
13102 C CA  . ASN D 102 ? 1.0085 0.6288 1.0298 0.2147  0.3873  0.0450  102 ASN D CA  
13103 C C   . ASN D 102 ? 1.0085 0.6290 1.0617 0.2262  0.4116  0.0352  102 ASN D C   
13104 O O   . ASN D 102 ? 1.0358 0.6332 1.0559 0.2281  0.4318  0.0261  102 ASN D O   
13105 C CB  . ASN D 102 ? 1.0056 0.6056 0.9674 0.2049  0.4011  0.0439  102 ASN D CB  
13106 C CG  . ASN D 102 ? 1.0564 0.6602 0.9926 0.1934  0.3814  0.0544  102 ASN D CG  
13107 O OD1 . ASN D 102 ? 1.0095 0.6339 0.9717 0.1883  0.3805  0.0617  102 ASN D OD1 
13108 N ND2 . ASN D 102 ? 0.9707 0.5544 0.8560 0.1892  0.3657  0.0550  102 ASN D ND2 
13109 N N   . TYR D 103 ? 0.9971 0.6438 1.1135 0.2341  0.4094  0.0367  103 TYR D N   
13110 C CA  . TYR D 103 ? 0.9986 0.6516 1.1546 0.2454  0.4337  0.0284  103 TYR D CA  
13111 C C   . TYR D 103 ? 1.0526 0.6779 1.1852 0.2547  0.4405  0.0184  103 TYR D C   
13112 O O   . TYR D 103 ? 1.0845 0.6922 1.1944 0.2563  0.4675  0.0092  103 TYR D O   
13113 C CB  . TYR D 103 ? 1.0514 0.7377 1.2782 0.2530  0.4217  0.0329  103 TYR D CB  
13114 C CG  . TYR D 103 ? 1.0291 0.7384 1.3083 0.2578  0.4475  0.0290  103 TYR D CG  
13115 C CD1 . TYR D 103 ? 1.0602 0.7560 1.3269 0.2603  0.4812  0.0198  103 TYR D CD1 
13116 C CD2 . TYR D 103 ? 0.9234 0.6682 1.2654 0.2601  0.4382  0.0343  103 TYR D CD2 
13117 C CE1 . TYR D 103 ? 1.0069 0.7244 1.3232 0.2648  0.5057  0.0163  103 TYR D CE1 
13118 C CE2 . TYR D 103 ? 0.9293 0.6969 1.3220 0.2642  0.4618  0.0305  103 TYR D CE2 
13119 C CZ  . TYR D 103 ? 1.0590 0.8130 1.4390 0.2664  0.4960  0.0217  103 TYR D CZ  
13120 O OH  . TYR D 103 ? 1.0705 0.8475 1.5015 0.2704  0.5208  0.0179  103 TYR D OH  
13121 N N   . GLU D 104 ? 1.0729 0.6927 1.2092 0.2608  0.4165  0.0200  104 GLU D N   
13122 C CA  . GLU D 104 ? 1.1102 0.7061 1.2357 0.2713  0.4218  0.0107  104 GLU D CA  
13123 C C   . GLU D 104 ? 1.1836 0.7449 1.2384 0.2639  0.4189  0.0063  104 GLU D C   
13124 O O   . GLU D 104 ? 1.0973 0.6433 1.1325 0.2648  0.3985  0.0070  104 GLU D O   
13125 C CB  . GLU D 104 ? 0.9942 0.6001 1.1590 0.2819  0.3985  0.0149  104 GLU D CB  
13126 C CG  . GLU D 104 ? 0.9954 0.6397 1.2233 0.2851  0.3890  0.0231  104 GLU D CG  
13127 C CD  . GLU D 104 ? 0.9692 0.6232 1.2113 0.2867  0.3541  0.0327  104 GLU D CD  
13128 O OE1 . GLU D 104 ? 0.9366 0.5853 1.1974 0.2989  0.3452  0.0316  104 GLU D OE1 
13129 O OE2 . GLU D 104 ? 0.9073 0.5733 1.1411 0.2761  0.3360  0.0416  104 GLU D OE2 
13130 N N   . LYS D 105 ? 1.1761 0.7253 1.1927 0.2563  0.4402  0.0017  105 LYS D N   
13131 C CA  . LYS D 105 ? 1.1811 0.6992 1.1300 0.2489  0.4392  -0.0033 105 LYS D CA  
13132 C C   . LYS D 105 ? 1.1318 0.6299 1.0548 0.2511  0.4720  -0.0157 105 LYS D C   
13133 O O   . LYS D 105 ? 1.1311 0.6416 1.0750 0.2523  0.4963  -0.0171 105 LYS D O   
13134 C CB  . LYS D 105 ? 1.1834 0.7052 1.0972 0.2346  0.4255  0.0059  105 LYS D CB  
13135 C CG  . LYS D 105 ? 1.0240 0.5589 0.9499 0.2315  0.3912  0.0170  105 LYS D CG  
13136 C CD  . LYS D 105 ? 1.0066 0.5473 0.9032 0.2183  0.3794  0.0264  105 LYS D CD  
13137 C CE  . LYS D 105 ? 1.0154 0.5659 0.9193 0.2155  0.3454  0.0363  105 LYS D CE  
13138 N NZ  . LYS D 105 ? 1.0001 0.5563 0.8766 0.2034  0.3333  0.0455  105 LYS D NZ  
13139 N N   . PRO D 106 ? 1.1999 0.6667 1.0769 0.2514  0.4740  -0.0253 106 PRO D N   
13140 C CA  . PRO D 106 ? 1.3559 0.8016 1.2045 0.2537  0.5051  -0.0382 106 PRO D CA  
13141 C C   . PRO D 106 ? 1.3232 0.7649 1.1295 0.2430  0.5196  -0.0371 106 PRO D C   
13142 O O   . PRO D 106 ? 1.3230 0.7511 1.1022 0.2411  0.5407  -0.0458 106 PRO D O   
13143 C CB  . PRO D 106 ? 1.3175 0.7314 1.1263 0.2549  0.4969  -0.0478 106 PRO D CB  
13144 C CG  . PRO D 106 ? 1.2240 0.6446 1.0553 0.2569  0.4654  -0.0401 106 PRO D CG  
13145 C CD  . PRO D 106 ? 1.1461 0.5958 0.9985 0.2501  0.4483  -0.0254 106 PRO D CD  
13146 N N   . ILE D 107 ? 1.1874 0.6442 0.9872 0.2330  0.5039  -0.0251 107 ILE D N   
13147 C CA  . ILE D 107 ? 1.2756 0.7333 1.0466 0.2243  0.5197  -0.0220 107 ILE D CA  
13148 C C   . ILE D 107 ? 1.2541 0.7405 1.0781 0.2259  0.5348  -0.0158 107 ILE D C   
13149 O O   . ILE D 107 ? 1.3041 0.7893 1.1183 0.2237  0.5616  -0.0178 107 ILE D O   
13150 C CB  . ILE D 107 ? 1.2071 0.6618 0.9351 0.2122  0.4958  -0.0129 107 ILE D CB  
13151 C CG1 . ILE D 107 ? 1.1365 0.6179 0.9042 0.2097  0.4696  0.0004  107 ILE D CG1 
13152 C CG2 . ILE D 107 ? 1.3550 0.7829 1.0333 0.2102  0.4812  -0.0198 107 ILE D CG2 
13153 C CD1 . ILE D 107 ? 1.1112 0.5892 0.8399 0.1993  0.4436  0.0088  107 ILE D CD1 
13154 N N   . TYR D 108 ? 1.1602 0.6724 1.0405 0.2296  0.5182  -0.0085 108 TYR D N   
13155 C CA  . TYR D 108 ? 1.1272 0.6689 1.0667 0.2324  0.5315  -0.0043 108 TYR D CA  
13156 C C   . TYR D 108 ? 1.2387 0.7850 1.2236 0.2463  0.5488  -0.0133 108 TYR D C   
13157 O O   . TYR D 108 ? 1.3044 0.8760 1.3498 0.2531  0.5416  -0.0099 108 TYR D O   
13158 C CB  . TYR D 108 ? 1.1337 0.7024 1.1099 0.2286  0.5037  0.0081  108 TYR D CB  
13159 C CG  . TYR D 108 ? 1.1154 0.6888 1.0651 0.2153  0.4962  0.0181  108 TYR D CG  
13160 C CD1 . TYR D 108 ? 1.1406 0.6907 1.0247 0.2072  0.4888  0.0190  108 TYR D CD1 
13161 C CD2 . TYR D 108 ? 1.0440 0.6454 1.0351 0.2110  0.4965  0.0266  108 TYR D CD2 
13162 C CE1 . TYR D 108 ? 1.0872 0.6412 0.9473 0.1961  0.4820  0.0285  108 TYR D CE1 
13163 C CE2 . TYR D 108 ? 1.1062 0.7103 1.0732 0.1991  0.4902  0.0357  108 TYR D CE2 
13164 C CZ  . TYR D 108 ? 1.1970 0.7770 1.0983 0.1922  0.4831  0.0369  108 TYR D CZ  
13165 O OH  . TYR D 108 ? 1.2236 0.8056 1.1006 0.1813  0.4771  0.0464  108 TYR D OH  
13166 N N   . ARG D 109 ? 1.2895 0.8123 1.2446 0.2498  0.5697  -0.0248 109 ARG D N   
13167 C CA  . ARG D 109 ? 1.2668 0.7948 1.2574 0.2584  0.5797  -0.0325 109 ARG D CA  
13168 C C   . ARG D 109 ? 1.3080 0.8444 1.3087 0.2553  0.6084  -0.0358 109 ARG D C   
13169 O O   . ARG D 109 ? 1.3004 0.8348 1.3156 0.2611  0.6209  -0.0439 109 ARG D O   
13170 C CB  . ARG D 109 ? 1.2232 0.7218 1.1759 0.2613  0.5732  -0.0421 109 ARG D CB  
13171 C CG  . ARG D 109 ? 1.3598 0.8315 1.2466 0.2526  0.5864  -0.0491 109 ARG D CG  
13172 C CD  . ARG D 109 ? 1.3269 0.7765 1.1949 0.2570  0.5891  -0.0611 109 ARG D CD  
13173 N NE  . ARG D 109 ? 1.4161 0.8734 1.3129 0.2620  0.6117  -0.0674 109 ARG D NE  
13174 C CZ  . ARG D 109 ? 1.3471 0.8044 1.2296 0.2567  0.6344  -0.0694 109 ARG D CZ  
13175 N NH1 . ARG D 109 ? 1.3529 0.8029 1.1918 0.2458  0.6376  -0.0653 109 ARG D NH1 
13176 N NH2 . ARG D 109 ? 1.3694 0.8341 1.2818 0.2624  0.6538  -0.0752 109 ARG D NH2 
13177 N N   . PHE D 110 ? 1.2613 0.8065 1.2541 0.2462  0.6190  -0.0294 110 PHE D N   
13178 C CA  . PHE D 110 ? 1.3178 0.8701 1.3193 0.2424  0.6456  -0.0315 110 PHE D CA  
13179 C C   . PHE D 110 ? 1.3474 0.9322 1.4252 0.2495  0.6523  -0.0305 110 PHE D C   
13180 O O   . PHE D 110 ? 1.2315 0.8389 1.3551 0.2537  0.6368  -0.0244 110 PHE D O   
13181 C CB  . PHE D 110 ? 1.2695 0.8223 1.2431 0.2301  0.6537  -0.0237 110 PHE D CB  
13182 C CG  . PHE D 110 ? 1.3923 0.9151 1.2889 0.2219  0.6486  -0.0242 110 PHE D CG  
13183 C CD1 . PHE D 110 ? 1.4480 0.9507 1.3089 0.2242  0.6287  -0.0275 110 PHE D CD1 
13184 C CD2 . PHE D 110 ? 1.4909 1.0056 1.3512 0.2118  0.6627  -0.0213 110 PHE D CD2 
13185 C CE1 . PHE D 110 ? 1.4275 0.9052 1.2197 0.2161  0.6226  -0.0281 110 PHE D CE1 
13186 C CE2 . PHE D 110 ? 1.5399 1.0294 1.3314 0.2043  0.6554  -0.0211 110 PHE D CE2 
13187 C CZ  . PHE D 110 ? 1.5259 0.9979 1.2840 0.2064  0.6352  -0.0248 110 PHE D CZ  
13188 N N   . GLU D 111 ? 1.4362 1.0237 1.5275 0.2509  0.6750  -0.0366 111 GLU D N   
13189 C CA  . GLU D 111 ? 1.3822 1.0008 1.5448 0.2575  0.6827  -0.0365 111 GLU D CA  
13190 C C   . GLU D 111 ? 1.3352 0.9827 1.5362 0.2507  0.6855  -0.0270 111 GLU D C   
13191 O O   . GLU D 111 ? 1.3080 0.9862 1.5739 0.2558  0.6833  -0.0251 111 GLU D O   
13192 C CB  . GLU D 111 ? 1.2934 0.9062 1.4564 0.2599  0.7077  -0.0452 111 GLU D CB  
13193 C CG  . GLU D 111 ? 1.3149 0.9291 1.4650 0.2496  0.7311  -0.0429 111 GLU D CG  
13194 C CD  . GLU D 111 ? 1.3493 0.9677 1.5210 0.2538  0.7553  -0.0503 111 GLU D CD  
13195 O OE1 . GLU D 111 ? 1.3777 0.9772 1.5291 0.2604  0.7594  -0.0595 111 GLU D OE1 
13196 O OE2 . GLU D 111 ? 1.3485 0.9893 1.5584 0.2504  0.7701  -0.0469 111 GLU D OE2 
13197 N N   . ARG D 112 ? 1.3259 0.9646 1.4885 0.2391  0.6893  -0.0211 112 ARG D N   
13198 C CA  . ARG D 112 ? 1.2408 0.9040 1.4351 0.2312  0.6928  -0.0121 112 ARG D CA  
13199 C C   . ARG D 112 ? 1.2261 0.9031 1.4389 0.2315  0.6679  -0.0041 112 ARG D C   
13200 O O   . ARG D 112 ? 1.1865 0.8749 1.4042 0.2227  0.6675  0.0041  112 ARG D O   
13201 C CB  . ARG D 112 ? 1.2277 0.8741 1.3718 0.2185  0.7089  -0.0088 112 ARG D CB  
13202 C CG  . ARG D 112 ? 1.2252 0.8950 1.4075 0.2106  0.7249  -0.0033 112 ARG D CG  
13203 C CD  . ARG D 112 ? 1.2660 0.9171 1.4050 0.2014  0.7470  -0.0034 112 ARG D CD  
13204 N NE  . ARG D 112 ? 1.2628 0.9355 1.4392 0.1933  0.7610  0.0022  112 ARG D NE  
13205 C CZ  . ARG D 112 ? 1.3090 0.9881 1.5062 0.1922  0.7839  -0.0012 112 ARG D CZ  
13206 N NH1 . ARG D 112 ? 1.4115 1.0774 1.5961 0.1989  0.7967  -0.0103 112 ARG D NH1 
13207 N NH2 . ARG D 112 ? 1.3178 1.0163 1.5490 0.1839  0.7945  0.0044  112 ARG D NH2 
13208 N N   . ILE D 113 ? 1.2114 0.8865 1.4333 0.2415  0.6467  -0.0061 113 ILE D N   
13209 C CA  . ILE D 113 ? 1.2882 0.9747 1.5274 0.2434  0.6207  0.0013  113 ILE D CA  
13210 C C   . ILE D 113 ? 1.2673 0.9875 1.5828 0.2525  0.6082  0.0026  113 ILE D C   
13211 O O   . ILE D 113 ? 1.1082 0.8567 1.4674 0.2492  0.6022  0.0094  113 ILE D O   
13212 C CB  . ILE D 113 ? 1.4695 1.1260 1.6557 0.2468  0.6017  -0.0002 113 ILE D CB  
13213 C CG1 . ILE D 113 ? 1.3671 0.9991 1.4822 0.2344  0.6031  0.0029  113 ILE D CG1 
13214 C CG2 . ILE D 113 ? 1.3735 1.0458 1.5839 0.2471  0.5646  0.0079  113 ILE D CG2 
13215 C CD1 . ILE D 113 ? 1.1612 0.8066 1.2732 0.2223  0.5798  0.0155  113 ILE D CD1 
13216 N N   . ARG D 114 ? 1.2724 0.9904 1.6044 0.2635  0.6037  -0.0040 114 ARG D N   
13217 C CA  . ARG D 114 ? 1.1734 0.9208 1.5711 0.2731  0.5861  -0.0020 114 ARG D CA  
13218 C C   . ARG D 114 ? 1.1020 0.8851 1.5615 0.2711  0.5997  -0.0012 114 ARG D C   
13219 O O   . ARG D 114 ? 1.1145 0.9289 1.6286 0.2734  0.5836  0.0040  114 ARG D O   
13220 C CB  . ARG D 114 ? 1.2306 0.9651 1.6275 0.2851  0.5797  -0.0091 114 ARG D CB  
13221 C CG  . ARG D 114 ? 1.0849 0.7955 1.4450 0.2889  0.5549  -0.0076 114 ARG D CG  
13222 C CD  . ARG D 114 ? 1.0263 0.7598 1.4334 0.2964  0.5252  -0.0008 114 ARG D CD  
13223 N NE  . ARG D 114 ? 1.0289 0.7388 1.4053 0.3016  0.5025  -0.0004 114 ARG D NE  
13224 C CZ  . ARG D 114 ? 1.0355 0.7398 1.4225 0.3118  0.4942  -0.0047 114 ARG D CZ  
13225 N NH1 . ARG D 114 ? 1.0727 0.7932 1.5000 0.3190  0.5064  -0.0098 114 ARG D NH1 
13226 N NH2 . ARG D 114 ? 1.0331 0.7149 1.3893 0.3146  0.4734  -0.0036 114 ARG D NH2 
13227 N N   . GLU D 115 ? 1.1408 0.9197 1.5922 0.2666  0.6282  -0.0063 115 GLU D N   
13228 C CA  . GLU D 115 ? 1.1763 0.9878 1.6856 0.2645  0.6423  -0.0063 115 GLU D CA  
13229 C C   . GLU D 115 ? 1.1062 0.9362 1.6306 0.2521  0.6430  0.0018  115 GLU D C   
13230 O O   . GLU D 115 ? 1.0396 0.9045 1.6249 0.2510  0.6400  0.0044  115 GLU D O   
13231 C CB  . GLU D 115 ? 1.1259 0.9249 1.6192 0.2634  0.6724  -0.0140 115 GLU D CB  
13232 C CG  . GLU D 115 ? 1.1631 0.9553 1.6650 0.2766  0.6741  -0.0225 115 GLU D CG  
13233 C CD  . GLU D 115 ? 1.1568 0.9148 1.6052 0.2820  0.6615  -0.0259 115 GLU D CD  
13234 O OE1 . GLU D 115 ? 1.2404 0.9756 1.6355 0.2746  0.6570  -0.0230 115 GLU D OE1 
13235 O OE2 . GLU D 115 ? 1.1670 0.9209 1.6266 0.2935  0.6557  -0.0314 115 GLU D OE2 
13236 N N   . LEU D 116 ? 1.1429 0.9500 1.6120 0.2426  0.6465  0.0057  116 LEU D N   
13237 C CA  . LEU D 116 ? 1.0452 0.8658 1.5219 0.2298  0.6502  0.0133  116 LEU D CA  
13238 C C   . LEU D 116 ? 0.9998 0.8427 1.5108 0.2305  0.6229  0.0206  116 LEU D C   
13239 O O   . LEU D 116 ? 0.9801 0.8515 1.5349 0.2234  0.6224  0.0252  116 LEU D O   
13240 C CB  . LEU D 116 ? 1.0656 0.8533 1.4686 0.2197  0.6617  0.0156  116 LEU D CB  
13241 C CG  . LEU D 116 ? 1.1447 0.9160 1.5171 0.2131  0.6910  0.0117  116 LEU D CG  
13242 C CD1 . LEU D 116 ? 1.1410 0.8977 1.5033 0.2231  0.7003  0.0017  116 LEU D CD1 
13243 C CD2 . LEU D 116 ? 1.1247 0.8664 1.4254 0.2026  0.6961  0.0162  116 LEU D CD2 
13244 N N   . MET D 117 ? 0.9840 0.8139 1.4752 0.2387  0.5993  0.0217  117 MET D N   
13245 C CA  . MET D 117 ? 0.9848 0.8309 1.4907 0.2340  0.5628  0.0304  117 MET D CA  
13246 C C   . MET D 117 ? 0.9571 0.8414 1.5409 0.2425  0.5494  0.0306  117 MET D C   
13247 O O   . MET D 117 ? 0.8897 0.7932 1.4944 0.2374  0.5218  0.0376  117 MET D O   
13248 C CB  . MET D 117 ? 0.9414 0.7604 1.3946 0.2363  0.5357  0.0324  117 MET D CB  
13249 C CG  . MET D 117 ? 0.9771 0.7796 1.3747 0.2220  0.5218  0.0401  117 MET D CG  
13250 S SD  . MET D 117 ? 1.0126 0.8477 1.4491 0.2091  0.5064  0.0499  117 MET D SD  
13251 C CE  . MET D 117 ? 0.9716 0.8116 1.4092 0.2123  0.4599  0.0562  117 MET D CE  
13252 N N   . ASN D 118 ? 1.1018 0.9975 1.7239 0.2530  0.5638  0.0234  118 ASN D N   
13253 C CA  . ASN D 118 ? 1.0748 1.0062 1.7654 0.2601  0.5470  0.0236  118 ASN D CA  
13254 C C   . ASN D 118 ? 1.0228 0.9889 1.7678 0.2518  0.5599  0.0238  118 ASN D C   
13255 O O   . ASN D 118 ? 0.9544 0.9507 1.7566 0.2576  0.5515  0.0220  118 ASN D O   
13256 C CB  . ASN D 118 ? 1.0603 0.9853 1.7572 0.2736  0.5476  0.0166  118 ASN D CB  
13257 C CG  . ASN D 118 ? 1.1724 1.0736 1.8358 0.2831  0.5245  0.0176  118 ASN D CG  
13258 O OD1 . ASN D 118 ? 1.2108 1.1274 1.9054 0.2916  0.4986  0.0203  118 ASN D OD1 
13259 N ND2 . ASN D 118 ? 1.0431 0.9061 1.6409 0.2810  0.5331  0.0155  118 ASN D ND2 
13260 N N   . LYS D 119 ? 0.9657 0.9277 1.6933 0.2381  0.5793  0.0259  119 LYS D N   
13261 C CA  . LYS D 119 ? 0.9482 0.9394 1.7231 0.2286  0.5941  0.0256  119 LYS D CA  
13262 C C   . LYS D 119 ? 1.0538 1.0689 1.8573 0.2186  0.5781  0.0328  119 LYS D C   
13263 O O   . LYS D 119 ? 1.0155 1.0178 1.7877 0.2156  0.5636  0.0387  119 LYS D O   
13264 C CB  . LYS D 119 ? 0.9570 0.9277 1.6957 0.2190  0.6284  0.0230  119 LYS D CB  
13265 C CG  . LYS D 119 ? 0.9947 0.9389 1.6986 0.2275  0.6456  0.0155  119 LYS D CG  
13266 C CD  . LYS D 119 ? 1.1474 1.1131 1.9030 0.2383  0.6478  0.0090  119 LYS D CD  
13267 C CE  . LYS D 119 ? 0.9933 1.0005 1.8193 0.2331  0.6493  0.0097  119 LYS D CE  
13268 N NZ  . LYS D 119 ? 1.0148 1.0211 1.8358 0.2192  0.6774  0.0097  119 LYS D NZ  
13269 N N   . GLU D 120 ? 0.9814 1.0318 1.8452 0.2130  0.5804  0.0319  120 GLU D N   
13270 C CA  . GLU D 120 ? 0.8479 0.9251 1.7469 0.2031  0.5639  0.0375  120 GLU D CA  
13271 C C   . GLU D 120 ? 0.8948 0.9560 1.7569 0.1872  0.5796  0.0425  120 GLU D C   
13272 O O   . GLU D 120 ? 0.8286 0.8866 1.6723 0.1798  0.5585  0.0491  120 GLU D O   
13273 C CB  . GLU D 120 ? 0.8450 0.9629 1.8160 0.2006  0.5633  0.0341  120 GLU D CB  
13274 C CG  . GLU D 120 ? 0.8348 0.9728 1.8326 0.1831  0.5685  0.0370  120 GLU D CG  
13275 C CD  . GLU D 120 ? 0.8338 1.0118 1.9022 0.1813  0.5663  0.0327  120 GLU D CD  
13276 O OE1 . GLU D 120 ? 0.9034 1.0852 1.9879 0.1882  0.5820  0.0266  120 GLU D OE1 
13277 O OE2 . GLU D 120 ? 0.8094 1.0151 1.9168 0.1730  0.5489  0.0350  120 GLU D OE2 
13278 N N   . LYS D 121 ? 1.1109 1.1577 1.9517 0.1794  0.6107  0.0400  121 LYS D N   
13279 C CA  . LYS D 121 ? 1.1078 1.1378 1.9115 0.1637  0.6269  0.0451  121 LYS D CA  
13280 C C   . LYS D 121 ? 1.1017 1.0884 1.8299 0.1651  0.6463  0.0445  121 LYS D C   
13281 O O   . LYS D 121 ? 1.1185 1.0900 1.8277 0.1770  0.6499  0.0391  121 LYS D O   
13282 C CB  . LYS D 121 ? 0.9882 1.0383 1.8307 0.1507  0.6454  0.0438  121 LYS D CB  
13283 C CG  . LYS D 121 ? 0.9921 1.0350 1.8337 0.1536  0.6725  0.0372  121 LYS D CG  
13284 C CD  . LYS D 121 ? 1.0028 1.0227 1.8047 0.1400  0.7002  0.0395  121 LYS D CD  
13285 C CE  . LYS D 121 ? 1.1436 1.1547 1.9415 0.1440  0.7266  0.0329  121 LYS D CE  
13286 N NZ  . LYS D 121 ? 1.0778 1.0628 1.8309 0.1321  0.7524  0.0354  121 LYS D NZ  
13287 N N   . LEU D 122 ? 1.0052 0.9717 1.6889 0.1522  0.6578  0.0502  122 LEU D N   
13288 C CA  . LEU D 122 ? 1.0960 1.0209 1.7029 0.1516  0.6738  0.0506  122 LEU D CA  
13289 C C   . LEU D 122 ? 1.0317 0.9453 1.6150 0.1354  0.6940  0.0551  122 LEU D C   
13290 O O   . LEU D 122 ? 0.9758 0.8875 1.5458 0.1249  0.6868  0.0627  122 LEU D O   
13291 C CB  . LEU D 122 ? 0.9998 0.9020 1.5542 0.1554  0.6522  0.0549  122 LEU D CB  
13292 C CG  . LEU D 122 ? 0.9495 0.8495 1.5036 0.1700  0.6271  0.0511  122 LEU D CG  
13293 C CD1 . LEU D 122 ? 0.9304 0.8391 1.4867 0.1670  0.5854  0.0576  122 LEU D CD1 
13294 C CD2 . LEU D 122 ? 1.0607 0.9217 1.5456 0.1763  0.6353  0.0477  122 LEU D CD2 
13295 N N   . ASN D 123 ? 1.0284 0.9335 1.6060 0.1335  0.7186  0.0507  123 ASN D N   
13296 C CA  . ASN D 123 ? 1.2163 1.1096 1.7729 0.1192  0.7378  0.0548  123 ASN D CA  
13297 C C   . ASN D 123 ? 1.2454 1.0970 1.7168 0.1158  0.7416  0.0597  123 ASN D C   
13298 O O   . ASN D 123 ? 1.0930 0.9258 1.5228 0.1241  0.7309  0.0591  123 ASN D O   
13299 C CB  . ASN D 123 ? 1.0876 0.9870 1.6691 0.1192  0.7622  0.0484  123 ASN D CB  
13300 C CG  . ASN D 123 ? 1.1777 1.0594 1.7330 0.1319  0.7718  0.0411  123 ASN D CG  
13301 O OD1 . ASN D 123 ? 1.1226 0.9753 1.6190 0.1370  0.7670  0.0414  123 ASN D OD1 
13302 N ND2 . ASN D 123 ? 1.1640 1.0629 1.7627 0.1368  0.7851  0.0341  123 ASN D ND2 
13303 N N   . ARG D 124 ? 1.2787 1.1156 1.7235 0.1036  0.7561  0.0644  124 ARG D N   
13304 C CA  . ARG D 124 ? 1.1222 0.9215 1.4876 0.0993  0.7564  0.0702  124 ARG D CA  
13305 C C   . ARG D 124 ? 1.1733 0.9451 1.4867 0.1093  0.7624  0.0647  124 ARG D C   
13306 O O   . ARG D 124 ? 1.1841 0.9341 1.4451 0.1130  0.7492  0.0668  124 ARG D O   
13307 C CB  . ARG D 124 ? 1.1500 0.9386 1.5004 0.0863  0.7725  0.0750  124 ARG D CB  
13308 C CG  . ARG D 124 ? 1.2354 0.9855 1.5044 0.0818  0.7720  0.0814  124 ARG D CG  
13309 C CD  . ARG D 124 ? 1.2850 1.0079 1.5064 0.0862  0.7897  0.0770  124 ARG D CD  
13310 N NE  . ARG D 124 ? 1.3614 1.0539 1.5190 0.0794  0.7914  0.0837  124 ARG D NE  
13311 C CZ  . ARG D 124 ? 1.3100 0.9720 1.4002 0.0836  0.7890  0.0835  124 ARG D CZ  
13312 N NH1 . ARG D 124 ? 1.2809 0.9360 1.3550 0.0938  0.7870  0.0765  124 ARG D NH1 
13313 N NH2 . ARG D 124 ? 1.4079 1.0462 1.4467 0.0774  0.7883  0.0900  124 ARG D NH2 
13314 N N   . GLU D 125 ? 1.1796 0.9529 1.5083 0.1138  0.7816  0.0573  125 GLU D N   
13315 C CA  . GLU D 125 ? 1.2165 0.9600 1.4899 0.1204  0.7913  0.0523  125 GLU D CA  
13316 C C   . GLU D 125 ? 1.2019 0.9392 1.4600 0.1327  0.7754  0.0474  125 GLU D C   
13317 O O   . GLU D 125 ? 1.2236 0.9309 1.4188 0.1356  0.7736  0.0461  125 GLU D O   
13318 C CB  . GLU D 125 ? 1.2502 0.9986 1.5479 0.1222  0.8161  0.0455  125 GLU D CB  
13319 C CG  . GLU D 125 ? 1.2909 1.0189 1.5522 0.1129  0.8356  0.0490  125 GLU D CG  
13320 C CD  . GLU D 125 ? 1.3130 1.0537 1.5987 0.1001  0.8363  0.0568  125 GLU D CD  
13321 O OE1 . GLU D 125 ? 1.3495 1.1214 1.6960 0.0982  0.8275  0.0575  125 GLU D OE1 
13322 O OE2 . GLU D 125 ? 1.3823 1.1014 1.6260 0.0921  0.8445  0.0622  125 GLU D OE2 
13323 N N   . GLU D 126 ? 1.1671 0.9319 1.4811 0.1402  0.7627  0.0445  126 GLU D N   
13324 C CA  . GLU D 126 ? 1.2292 0.9873 1.5291 0.1521  0.7458  0.0404  126 GLU D CA  
13325 C C   . GLU D 126 ? 1.2253 0.9784 1.5007 0.1504  0.7225  0.0474  126 GLU D C   
13326 O O   . GLU D 126 ? 1.1108 0.8534 1.3647 0.1596  0.7077  0.0446  126 GLU D O   
13327 C CB  . GLU D 126 ? 1.1336 0.9213 1.5019 0.1631  0.7407  0.0337  126 GLU D CB  
13328 C CG  . GLU D 126 ? 1.2531 1.0461 1.6462 0.1670  0.7625  0.0260  126 GLU D CG  
13329 C CD  . GLU D 126 ? 1.2483 1.0653 1.6982 0.1800  0.7542  0.0192  126 GLU D CD  
13330 O OE1 . GLU D 126 ? 1.1543 0.9892 1.6349 0.1848  0.7313  0.0214  126 GLU D OE1 
13331 O OE2 . GLU D 126 ? 1.1753 0.9926 1.6381 0.1859  0.7699  0.0119  126 GLU D OE2 
13332 N N   . LEU D 127 ? 1.2612 1.0208 1.5390 0.1390  0.7187  0.0563  127 LEU D N   
13333 C CA  . LEU D 127 ? 1.0796 0.8313 1.3267 0.1367  0.6979  0.0637  127 LEU D CA  
13334 C C   . LEU D 127 ? 1.1355 0.8487 1.2988 0.1369  0.6954  0.0645  127 LEU D C   
13335 O O   . LEU D 127 ? 1.1894 0.8926 1.3229 0.1409  0.6768  0.0664  127 LEU D O   
13336 C CB  . LEU D 127 ? 1.0638 0.8277 1.3268 0.1232  0.6960  0.0731  127 LEU D CB  
13337 C CG  . LEU D 127 ? 1.0167 0.8139 1.3395 0.1229  0.6767  0.0763  127 LEU D CG  
13338 C CD1 . LEU D 127 ? 1.0033 0.8320 1.3991 0.1320  0.6785  0.0684  127 LEU D CD1 
13339 C CD2 . LEU D 127 ? 1.0071 0.8147 1.3457 0.1080  0.6783  0.0847  127 LEU D CD2 
13340 N N   . LEU D 128 ? 1.2088 0.9005 1.3335 0.1325  0.7127  0.0629  128 LEU D N   
13341 C CA  . LEU D 128 ? 1.2304 0.8869 1.2768 0.1324  0.7089  0.0630  128 LEU D CA  
13342 C C   . LEU D 128 ? 1.2099 0.8542 1.2390 0.1440  0.7070  0.0532  128 LEU D C   
13343 O O   . LEU D 128 ? 1.2431 0.8640 1.2158 0.1458  0.6944  0.0528  128 LEU D O   
13344 C CB  . LEU D 128 ? 1.2166 0.8551 1.2290 0.1245  0.7263  0.0648  128 LEU D CB  
13345 C CG  . LEU D 128 ? 1.2136 0.8645 1.2523 0.1134  0.7343  0.0724  128 LEU D CG  
13346 C CD1 . LEU D 128 ? 1.2206 0.8943 1.3215 0.1137  0.7552  0.0673  128 LEU D CD1 
13347 C CD2 . LEU D 128 ? 1.2865 0.9115 1.2669 0.1051  0.7369  0.0786  128 LEU D CD2 
13348 N N   . ASP D 129 ? 1.1901 0.8499 1.2666 0.1518  0.7181  0.0449  129 ASP D N   
13349 C CA  . ASP D 129 ? 1.1988 0.8479 1.2637 0.1633  0.7142  0.0354  129 ASP D CA  
13350 C C   . ASP D 129 ? 1.1644 0.8146 1.2260 0.1696  0.6892  0.0366  129 ASP D C   
13351 O O   . ASP D 129 ? 1.1818 0.8087 1.1960 0.1741  0.6795  0.0326  129 ASP D O   
13352 C CB  . ASP D 129 ? 1.2803 0.9497 1.4046 0.1710  0.7277  0.0275  129 ASP D CB  
13353 C CG  . ASP D 129 ? 1.3680 1.0346 1.4933 0.1657  0.7536  0.0256  129 ASP D CG  
13354 O OD1 . ASP D 129 ? 1.3246 1.0029 1.4686 0.1562  0.7616  0.0321  129 ASP D OD1 
13355 O OD2 . ASP D 129 ? 1.4765 1.1284 1.5828 0.1708  0.7658  0.0176  129 ASP D OD2 
13356 N N   . LEU D 130 ? 1.1239 0.8009 1.2355 0.1697  0.6780  0.0419  130 LEU D N   
13357 C CA  . LEU D 130 ? 1.0906 0.7693 1.1990 0.1739  0.6484  0.0446  130 LEU D CA  
13358 C C   . LEU D 130 ? 1.0953 0.7485 1.1325 0.1659  0.6338  0.0511  130 LEU D C   
13359 O O   . LEU D 130 ? 1.1136 0.7517 1.1168 0.1692  0.6112  0.0497  130 LEU D O   
13360 C CB  . LEU D 130 ? 1.0497 0.7632 1.2228 0.1705  0.6294  0.0508  130 LEU D CB  
13361 C CG  . LEU D 130 ? 1.0119 0.7382 1.2064 0.1743  0.5904  0.0533  130 LEU D CG  
13362 C CD1 . LEU D 130 ? 0.9802 0.7435 1.2460 0.1718  0.5811  0.0572  130 LEU D CD1 
13363 C CD2 . LEU D 130 ? 1.1080 0.8164 1.2475 0.1675  0.5634  0.0606  130 LEU D CD2 
13364 N N   . GLN D 131 ? 1.1061 0.7539 1.1201 0.1555  0.6469  0.0585  131 GLN D N   
13365 C CA  . GLN D 131 ? 1.1124 0.7366 1.0591 0.1485  0.6341  0.0653  131 GLN D CA  
13366 C C   . GLN D 131 ? 1.1480 0.7411 1.0318 0.1518  0.6369  0.0585  131 GLN D C   
13367 O O   . GLN D 131 ? 1.1432 0.7209 0.9860 0.1542  0.6191  0.0582  131 GLN D O   
13368 C CB  . GLN D 131 ? 1.1794 0.8033 1.1164 0.1362  0.6442  0.0744  131 GLN D CB  
13369 C CG  . GLN D 131 ? 1.1559 0.8075 1.1452 0.1302  0.6366  0.0823  131 GLN D CG  
13370 C CD  . GLN D 131 ? 1.2699 0.9239 1.2656 0.1191  0.6535  0.0882  131 GLN D CD  
13371 O OE1 . GLN D 131 ? 1.2943 0.9257 1.2370 0.1124  0.6525  0.0925  131 GLN D OE1 
13372 N NE2 . GLN D 131 ? 1.1610 0.8429 1.2233 0.1169  0.6643  0.0877  131 GLN D NE2 
13373 N N   . THR D 132 ? 1.2425 0.8268 1.1193 0.1512  0.6562  0.0527  132 THR D N   
13374 C CA  . THR D 132 ? 1.2845 0.8398 1.1001 0.1517  0.6566  0.0469  132 THR D CA  
13375 C C   . THR D 132 ? 1.3593 0.9062 1.1670 0.1618  0.6467  0.0376  132 THR D C   
13376 O O   . THR D 132 ? 1.4567 0.9812 1.2092 0.1614  0.6338  0.0354  132 THR D O   
13377 C CB  . THR D 132 ? 1.2978 0.8484 1.1155 0.1502  0.6810  0.0421  132 THR D CB  
13378 O OG1 . THR D 132 ? 1.4588 1.0282 1.3356 0.1577  0.6948  0.0351  132 THR D OG1 
13379 C CG2 . THR D 132 ? 1.2684 0.8229 1.0875 0.1401  0.6903  0.0510  132 THR D CG2 
13380 N N   . LEU D 133 ? 1.3119 0.8771 1.1764 0.1710  0.6511  0.0320  133 LEU D N   
13381 C CA  . LEU D 133 ? 1.2937 0.8509 1.1580 0.1816  0.6431  0.0223  133 LEU D CA  
13382 C C   . LEU D 133 ? 1.1754 0.7268 1.0201 0.1845  0.6176  0.0249  133 LEU D C   
13383 O O   . LEU D 133 ? 1.1862 0.7182 0.9976 0.1889  0.6073  0.0181  133 LEU D O   
13384 C CB  . LEU D 133 ? 1.2437 0.8242 1.1789 0.1907  0.6531  0.0167  133 LEU D CB  
13385 C CG  . LEU D 133 ? 1.2797 0.8698 1.2540 0.2033  0.6390  0.0116  133 LEU D CG  
13386 C CD1 . LEU D 133 ? 1.2806 0.8432 1.2108 0.2084  0.6317  0.0027  133 LEU D CD1 
13387 C CD2 . LEU D 133 ? 1.1796 0.7946 1.2227 0.2096  0.6526  0.0075  133 LEU D CD2 
13388 N N   . ASN D 134 ? 1.1393 0.7095 1.0057 0.1778  0.5968  0.0359  134 ASN D N   
13389 C CA  . ASN D 134 ? 1.1139 0.6801 0.9565 0.1744  0.5612  0.0415  134 ASN D CA  
13390 C C   . ASN D 134 ? 1.1922 0.7283 0.9577 0.1704  0.5594  0.0405  134 ASN D C   
13391 O O   . ASN D 134 ? 1.2373 0.7593 0.9745 0.1728  0.5408  0.0365  134 ASN D O   
13392 C CB  . ASN D 134 ? 1.0788 0.6666 0.9474 0.1661  0.5445  0.0539  134 ASN D CB  
13393 C CG  . ASN D 134 ? 1.0423 0.6591 0.9794 0.1704  0.5277  0.0554  134 ASN D CG  
13394 O OD1 . ASN D 134 ? 1.0283 0.6456 0.9756 0.1770  0.5075  0.0522  134 ASN D OD1 
13395 N ND2 . ASN D 134 ? 1.0278 0.6686 1.0119 0.1664  0.5358  0.0603  134 ASN D ND2 
13396 N N   . LEU D 135 ? 1.1681 0.6940 0.8990 0.1641  0.5791  0.0442  135 LEU D N   
13397 C CA  . LEU D 135 ? 1.1887 0.6894 0.8490 0.1584  0.5709  0.0447  135 LEU D CA  
13398 C C   . LEU D 135 ? 1.3162 0.7972 0.9487 0.1627  0.5746  0.0322  135 LEU D C   
13399 O O   . LEU D 135 ? 1.2360 0.7000 0.8235 0.1618  0.5575  0.0293  135 LEU D O   
13400 C CB  . LEU D 135 ? 1.2060 0.7050 0.8478 0.1483  0.5781  0.0522  135 LEU D CB  
13401 C CG  . LEU D 135 ? 1.2419 0.7532 0.8918 0.1407  0.5693  0.0655  135 LEU D CG  
13402 C CD1 . LEU D 135 ? 1.4177 0.9184 1.0208 0.1367  0.5412  0.0711  135 LEU D CD1 
13403 C CD2 . LEU D 135 ? 1.2537 0.7909 0.9662 0.1440  0.5738  0.0694  135 LEU D CD2 
13404 N N   . LEU D 136 ? 1.3550 0.8390 1.0151 0.1670  0.5964  0.0248  136 LEU D N   
13405 C CA  . LEU D 136 ? 1.2950 0.7602 0.9294 0.1705  0.6019  0.0129  136 LEU D CA  
13406 C C   . LEU D 136 ? 1.2649 0.7235 0.9016 0.1787  0.5880  0.0051  136 LEU D C   
13407 O O   . LEU D 136 ? 1.2889 0.7273 0.8861 0.1788  0.5823  -0.0030 136 LEU D O   
13408 C CB  . LEU D 136 ? 1.4075 0.8795 1.0760 0.1738  0.6283  0.0073  136 LEU D CB  
13409 C CG  . LEU D 136 ? 1.3764 0.8471 1.0310 0.1658  0.6440  0.0121  136 LEU D CG  
13410 C CD1 . LEU D 136 ? 1.4389 0.9290 1.1512 0.1685  0.6673  0.0114  136 LEU D CD1 
13411 C CD2 . LEU D 136 ? 1.4855 0.9322 1.0858 0.1634  0.6473  0.0053  136 LEU D CD2 
13412 N N   . ALA D 137 ? 1.2575 0.7329 0.9415 0.1858  0.5818  0.0072  137 ALA D N   
13413 C CA  . ALA D 137 ? 1.2174 0.6863 0.9077 0.1941  0.5659  0.0005  137 ALA D CA  
13414 C C   . ALA D 137 ? 1.2142 0.6665 0.8501 0.1878  0.5396  0.0025  137 ALA D C   
13415 O O   . ALA D 137 ? 1.2273 0.6617 0.8397 0.1911  0.5314  -0.0063 137 ALA D O   
13416 C CB  . ALA D 137 ? 1.1747 0.6725 0.9335 0.1976  0.5490  0.0067  137 ALA D CB  
13417 N N   . TRP D 138 ? 1.2102 0.6682 0.8261 0.1788  0.5265  0.0140  138 TRP D N   
13418 C CA  . TRP D 138 ? 1.2935 0.7385 0.8590 0.1726  0.5015  0.0170  138 TRP D CA  
13419 C C   . TRP D 138 ? 1.2747 0.6986 0.7788 0.1666  0.5090  0.0134  138 TRP D C   
13420 O O   . TRP D 138 ? 1.3892 0.8122 0.8606 0.1579  0.4955  0.0216  138 TRP D O   
13421 C CB  . TRP D 138 ? 1.1556 0.6191 0.7333 0.1655  0.4797  0.0316  138 TRP D CB  
13422 C CG  . TRP D 138 ? 1.1154 0.6045 0.7585 0.1687  0.4650  0.0366  138 TRP D CG  
13423 C CD1 . TRP D 138 ? 1.1034 0.6138 0.8019 0.1713  0.4786  0.0391  138 TRP D CD1 
13424 C CD2 . TRP D 138 ? 1.0928 0.5893 0.7520 0.1695  0.4337  0.0397  138 TRP D CD2 
13425 N NE1 . TRP D 138 ? 1.0664 0.5972 0.8139 0.1740  0.4570  0.0434  138 TRP D NE1 
13426 C CE2 . TRP D 138 ? 1.0935 0.6155 0.8171 0.1731  0.4296  0.0441  138 TRP D CE2 
13427 C CE3 . TRP D 138 ? 1.1584 0.6427 0.7840 0.1672  0.4091  0.0392  138 TRP D CE3 
13428 C CZ2 . TRP D 138 ? 1.1163 0.6509 0.8692 0.1752  0.4017  0.0483  138 TRP D CZ2 
13429 C CZ3 . TRP D 138 ? 1.0951 0.5917 0.7509 0.1689  0.3824  0.0435  138 TRP D CZ3 
13430 C CH2 . TRP D 138 ? 1.0399 0.5608 0.7575 0.1731  0.3789  0.0481  138 TRP D CH2 
13431 N N   . CYS D 139 ? 1.2650 0.6768 0.7617 0.1690  0.5218  0.0023  139 CYS D N   
13432 C CA  . CYS D 139 ? 1.3011 0.6980 0.7508 0.1620  0.5223  -0.0014 139 CYS D CA  
13433 C C   . CYS D 139 ? 1.3296 0.7090 0.7400 0.1606  0.5033  -0.0093 139 CYS D C   
13434 O O   . CYS D 139 ? 1.3923 0.7662 0.8159 0.1670  0.4996  -0.0166 139 CYS D O   
13435 C CB  . CYS D 139 ? 1.4550 0.8491 0.9181 0.1649  0.5487  -0.0089 139 CYS D CB  
13436 S SG  . CYS D 139 ? 1.5176 0.8935 0.9249 0.1580  0.5513  -0.0144 139 CYS D SG  
13437 N N   . GLY D 140 ? 1.3275 0.6992 0.6925 0.1522  0.4905  -0.0080 140 GLY D N   
13438 C CA  . GLY D 140 ? 1.3372 0.6953 0.6655 0.1490  0.4709  -0.0150 140 GLY D CA  
13439 C C   . GLY D 140 ? 1.4339 0.7767 0.7385 0.1486  0.4813  -0.0274 140 GLY D C   
13440 O O   . GLY D 140 ? 1.5205 0.8630 0.8293 0.1496  0.5020  -0.0291 140 GLY D O   
13441 N N   . ARG D 141 ? 1.3895 0.7196 0.6690 0.1469  0.4665  -0.0361 141 ARG D N   
13442 C CA  . ARG D 141 ? 1.4576 0.7727 0.7135 0.1462  0.4748  -0.0489 141 ARG D CA  
13443 C C   . ARG D 141 ? 1.5092 0.8249 0.7347 0.1401  0.4770  -0.0467 141 ARG D C   
13444 O O   . ARG D 141 ? 1.6867 0.9946 0.9049 0.1417  0.4954  -0.0539 141 ARG D O   
13445 C CB  . ARG D 141 ? 1.5254 0.8280 0.7583 0.1436  0.4556  -0.0578 141 ARG D CB  
13446 C CG  . ARG D 141 ? 1.5855 0.8717 0.7986 0.1438  0.4654  -0.0725 141 ARG D CG  
13447 C CD  . ARG D 141 ? 1.4808 0.7546 0.6746 0.1407  0.4469  -0.0818 141 ARG D CD  
13448 N NE  . ARG D 141 ? 1.4748 0.7531 0.6359 0.1312  0.4221  -0.0782 141 ARG D NE  
13449 C CZ  . ARG D 141 ? 1.5034 0.7748 0.6312 0.1253  0.4149  -0.0865 141 ARG D CZ  
13450 N NH1 . ARG D 141 ? 1.5952 0.8526 0.7135 0.1274  0.4306  -0.0992 141 ARG D NH1 
13451 N NH2 . ARG D 141 ? 1.4928 0.7731 0.5982 0.1173  0.3913  -0.0823 141 ARG D NH2 
13452 N N   . THR D 142 ? 1.4968 0.8221 0.7055 0.1337  0.4578  -0.0370 142 THR D N   
13453 C CA  . THR D 142 ? 1.4675 0.7943 0.6476 0.1285  0.4568  -0.0350 142 THR D CA  
13454 C C   . THR D 142 ? 1.5259 0.8562 0.7205 0.1311  0.4817  -0.0304 142 THR D C   
13455 O O   . THR D 142 ? 1.7415 1.0672 0.9135 0.1293  0.4901  -0.0329 142 THR D O   
13456 C CB  . THR D 142 ? 1.5713 0.9108 0.7381 0.1221  0.4299  -0.0251 142 THR D CB  
13457 O OG1 . THR D 142 ? 1.8453 1.1859 0.9818 0.1177  0.4258  -0.0256 142 THR D OG1 
13458 C CG2 . THR D 142 ? 1.4863 0.8402 0.6808 0.1229  0.4303  -0.0114 142 THR D CG2 
13459 N N   . LEU D 143 ? 1.4550 0.7939 0.6878 0.1353  0.4940  -0.0238 143 LEU D N   
13460 C CA  . LEU D 143 ? 1.4663 0.8104 0.7186 0.1372  0.5181  -0.0191 143 LEU D CA  
13461 C C   . LEU D 143 ? 1.4788 0.8198 0.7635 0.1446  0.5433  -0.0267 143 LEU D C   
13462 O O   . LEU D 143 ? 1.4981 0.8491 0.8172 0.1473  0.5614  -0.0216 143 LEU D O   
13463 C CB  . LEU D 143 ? 1.4468 0.8067 0.7217 0.1353  0.5132  -0.0049 143 LEU D CB  
13464 C CG  . LEU D 143 ? 1.6432 1.0085 0.8985 0.1295  0.5074  0.0043  143 LEU D CG  
13465 C CD1 . LEU D 143 ? 1.6427 1.0026 0.8549 0.1248  0.4861  0.0011  143 LEU D CD1 
13466 C CD2 . LEU D 143 ? 1.4534 0.8338 0.7314 0.1275  0.4975  0.0173  143 LEU D CD2 
13467 N N   . ARG D 144 ? 1.4952 0.8236 0.7719 0.1478  0.5444  -0.0393 144 ARG D N   
13468 C CA  . ARG D 144 ? 1.5049 0.8315 0.8155 0.1556  0.5666  -0.0472 144 ARG D CA  
13469 C C   . ARG D 144 ? 1.6274 0.9485 0.9319 0.1565  0.5908  -0.0521 144 ARG D C   
13470 O O   . ARG D 144 ? 1.6774 1.0069 1.0180 0.1608  0.6126  -0.0506 144 ARG D O   
13471 C CB  . ARG D 144 ? 1.5363 0.8512 0.8438 0.1592  0.5581  -0.0589 144 ARG D CB  
13472 C CG  . ARG D 144 ? 1.4982 0.8199 0.8560 0.1682  0.5667  -0.0609 144 ARG D CG  
13473 C CD  . ARG D 144 ? 1.4656 0.7806 0.8224 0.1701  0.5468  -0.0653 144 ARG D CD  
13474 N NE  . ARG D 144 ? 1.6188 0.9431 0.9744 0.1666  0.5258  -0.0545 144 ARG D NE  
13475 C CZ  . ARG D 144 ? 1.5448 0.8824 0.9401 0.1719  0.5240  -0.0478 144 ARG D CZ  
13476 N NH1 . ARG D 144 ? 1.6847 1.0310 1.1285 0.1809  0.5412  -0.0501 144 ARG D NH1 
13477 N NH2 . ARG D 144 ? 1.3594 0.7034 0.7475 0.1684  0.5036  -0.0387 144 ARG D NH2 
13478 N N   . LYS D 145 ? 1.6289 0.9369 0.8892 0.1525  0.5873  -0.0582 145 LYS D N   
13479 C CA  . LYS D 145 ? 1.6233 0.9255 0.8725 0.1529  0.6092  -0.0618 145 LYS D CA  
13480 C C   . LYS D 145 ? 1.6826 0.9918 0.9191 0.1478  0.6106  -0.0502 145 LYS D C   
13481 O O   . LYS D 145 ? 1.8112 1.1171 1.0422 0.1482  0.6304  -0.0512 145 LYS D O   
13482 C CB  . LYS D 145 ? 1.6960 0.9807 0.9049 0.1519  0.6071  -0.0748 145 LYS D CB  
13483 C CG  . LYS D 145 ? 1.7270 1.0079 0.8910 0.1447  0.5819  -0.0737 145 LYS D CG  
13484 C CD  . LYS D 145 ? 1.7161 0.9831 0.8404 0.1432  0.5872  -0.0842 145 LYS D CD  
13485 C CE  . LYS D 145 ? 1.7401 0.9934 0.8689 0.1481  0.5987  -0.0995 145 LYS D CE  
13486 N NZ  . LYS D 145 ? 1.7122 0.9637 0.8543 0.1491  0.5827  -0.1038 145 LYS D NZ  
13487 N N   . ASP D 146 ? 1.7216 1.0400 0.9534 0.1432  0.5900  -0.0395 146 ASP D N   
13488 C CA  . ASP D 146 ? 1.7426 1.0691 0.9702 0.1391  0.5915  -0.0276 146 ASP D CA  
13489 C C   . ASP D 146 ? 1.6843 1.0232 0.9584 0.1416  0.6106  -0.0203 146 ASP D C   
13490 O O   . ASP D 146 ? 1.5923 0.9336 0.8687 0.1401  0.6261  -0.0149 146 ASP D O   
13491 C CB  . ASP D 146 ? 1.6158 0.9490 0.8255 0.1337  0.5624  -0.0191 146 ASP D CB  
13492 C CG  . ASP D 146 ? 1.7908 1.1246 0.9708 0.1290  0.5579  -0.0125 146 ASP D CG  
13493 O OD1 . ASP D 146 ? 1.6595 0.9892 0.8365 0.1298  0.5790  -0.0123 146 ASP D OD1 
13494 O OD2 . ASP D 146 ? 1.8129 1.1519 0.9737 0.1248  0.5333  -0.0074 146 ASP D OD2 
13495 N N   . LEU D 147 ? 1.6782 1.0258 0.9905 0.1455  0.6097  -0.0201 147 LEU D N   
13496 C CA  . LEU D 147 ? 1.6139 0.9758 0.9770 0.1486  0.6284  -0.0152 147 LEU D CA  
13497 C C   . LEU D 147 ? 1.6622 1.0228 1.0547 0.1559  0.6501  -0.0257 147 LEU D C   
13498 O O   . LEU D 147 ? 1.7582 1.1335 1.2004 0.1598  0.6632  -0.0234 147 LEU D O   
13499 C CB  . LEU D 147 ? 1.4754 0.8516 0.8675 0.1488  0.6134  -0.0072 147 LEU D CB  
13500 C CG  . LEU D 147 ? 1.4525 0.8326 0.8226 0.1423  0.5899  0.0036  147 LEU D CG  
13501 C CD1 . LEU D 147 ? 1.4116 0.7983 0.7950 0.1438  0.5697  0.0059  147 LEU D CD1 
13502 C CD2 . LEU D 147 ? 1.6876 1.0791 1.0760 0.1386  0.5996  0.0149  147 LEU D CD2 
13503 N N   . LYS D 148 ? 1.5756 0.9201 0.9401 0.1578  0.6532  -0.0374 148 LYS D N   
13504 C CA  . LYS D 148 ? 1.5969 0.9378 0.9839 0.1648  0.6731  -0.0486 148 LYS D CA  
13505 C C   . LYS D 148 ? 1.5996 0.9542 1.0311 0.1676  0.6990  -0.0452 148 LYS D C   
13506 O O   . LYS D 148 ? 1.5811 0.9480 1.0617 0.1738  0.7077  -0.0473 148 LYS D O   
13507 C CB  . LYS D 148 ? 1.6810 1.0020 1.0215 0.1638  0.6766  -0.0591 148 LYS D CB  
13508 C CG  . LYS D 148 ? 1.6781 0.9910 1.0300 0.1704  0.6977  -0.0720 148 LYS D CG  
13509 C CD  . LYS D 148 ? 1.6559 0.9784 1.0604 0.1786  0.7044  -0.0763 148 LYS D CD  
13510 C CE  . LYS D 148 ? 1.6933 1.0076 1.1070 0.1851  0.7259  -0.0888 148 LYS D CE  
13511 N NZ  . LYS D 148 ? 1.7088 1.0335 1.1506 0.1867  0.7523  -0.0856 148 LYS D NZ  
13512 N N   . ASP D 149 ? 1.6212 0.9752 1.0379 0.1628  0.7102  -0.0393 149 ASP D N   
13513 C CA  . ASP D 149 ? 1.6467 1.0107 1.0994 0.1646  0.7372  -0.0377 149 ASP D CA  
13514 C C   . ASP D 149 ? 1.5927 0.9800 1.1070 0.1671  0.7407  -0.0316 149 ASP D C   
13515 O O   . ASP D 149 ? 1.5967 0.9952 1.1550 0.1719  0.7607  -0.0349 149 ASP D O   
13516 C CB  . ASP D 149 ? 1.6586 1.0184 1.0839 0.1581  0.7446  -0.0301 149 ASP D CB  
13517 C CG  . ASP D 149 ? 1.6674 1.0393 1.1322 0.1585  0.7709  -0.0264 149 ASP D CG  
13518 O OD1 . ASP D 149 ? 1.6984 1.0667 1.1730 0.1629  0.7920  -0.0347 149 ASP D OD1 
13519 O OD2 . ASP D 149 ? 1.7772 1.1622 1.2638 0.1542  0.7704  -0.0155 149 ASP D OD2 
13520 N N   . LEU D 150 ? 1.5528 0.9488 1.0722 0.1640  0.7209  -0.0229 150 LEU D N   
13521 C CA  . LEU D 150 ? 1.5994 1.0188 1.1766 0.1657  0.7228  -0.0165 150 LEU D CA  
13522 C C   . LEU D 150 ? 1.5366 0.9637 1.1476 0.1738  0.7148  -0.0225 150 LEU D C   
13523 O O   . LEU D 150 ? 1.4911 0.9393 1.1598 0.1781  0.7223  -0.0209 150 LEU D O   
13524 C CB  . LEU D 150 ? 1.5480 0.9742 1.1173 0.1587  0.7066  -0.0037 150 LEU D CB  
13525 C CG  . LEU D 150 ? 1.5049 0.9290 1.0579 0.1515  0.7173  0.0039  150 LEU D CG  
13526 C CD1 . LEU D 150 ? 1.5089 0.9198 1.0068 0.1452  0.6968  0.0098  150 LEU D CD1 
13527 C CD2 . LEU D 150 ? 1.4788 0.9250 1.0836 0.1492  0.7266  0.0125  150 LEU D CD2 
13528 N N   . LEU D 151 ? 1.5089 0.9202 1.0873 0.1761  0.6991  -0.0295 151 LEU D N   
13529 C CA  . LEU D 151 ? 1.4651 0.8817 1.0738 0.1841  0.6899  -0.0351 151 LEU D CA  
13530 C C   . LEU D 151 ? 1.5550 0.9768 1.2034 0.1928  0.7094  -0.0445 151 LEU D C   
13531 O O   . LEU D 151 ? 1.5603 0.9977 1.2588 0.2002  0.7076  -0.0457 151 LEU D O   
13532 C CB  . LEU D 151 ? 1.4689 0.8656 1.0306 0.1834  0.6685  -0.0406 151 LEU D CB  
13533 C CG  . LEU D 151 ? 1.5051 0.9055 1.0590 0.1807  0.6431  -0.0328 151 LEU D CG  
13534 C CD1 . LEU D 151 ? 1.5600 0.9453 1.0907 0.1836  0.6248  -0.0409 151 LEU D CD1 
13535 C CD2 . LEU D 151 ? 1.4575 0.8827 1.0698 0.1845  0.6436  -0.0251 151 LEU D CD2 
13536 N N   . ASN D 152 ? 1.5637 0.9733 1.1913 0.1924  0.7272  -0.0513 152 ASN D N   
13537 C CA  . ASN D 152 ? 1.5449 0.9589 1.2079 0.2005  0.7470  -0.0603 152 ASN D CA  
13538 C C   . ASN D 152 ? 1.5437 0.9789 1.2539 0.2005  0.7683  -0.0552 152 ASN D C   
13539 O O   . ASN D 152 ? 1.5491 0.9953 1.3033 0.2080  0.7825  -0.0609 152 ASN D O   
13540 C CB  . ASN D 152 ? 1.5951 0.9849 1.2121 0.2004  0.7562  -0.0709 152 ASN D CB  
13541 C CG  . ASN D 152 ? 1.6004 0.9688 1.1624 0.1971  0.7347  -0.0747 152 ASN D CG  
13542 O OD1 . ASN D 152 ? 1.6776 1.0428 1.2075 0.1896  0.7193  -0.0671 152 ASN D OD1 
13543 N ND2 . ASN D 152 ? 1.6198 0.9737 1.1708 0.2023  0.7332  -0.0868 152 ASN D ND2 
13544 N N   . LYS D 153 ? 1.5384 0.9793 1.2405 0.1921  0.7706  -0.0448 153 LYS D N   
13545 C CA  . LYS D 153 ? 1.5859 1.0489 1.3372 0.1911  0.7889  -0.0392 153 LYS D CA  
13546 C C   . LYS D 153 ? 1.5329 1.0229 1.3519 0.1974  0.7839  -0.0376 153 LYS D C   
13547 O O   . LYS D 153 ? 1.4927 1.0001 1.3628 0.2027  0.7996  -0.0407 153 LYS D O   
13548 C CB  . LYS D 153 ? 1.5288 0.9927 1.2599 0.1807  0.7878  -0.0275 153 LYS D CB  
13549 C CG  . LYS D 153 ? 1.5761 1.0219 1.2624 0.1755  0.8026  -0.0282 153 LYS D CG  
13550 C CD  . LYS D 153 ? 1.5719 1.0218 1.2502 0.1662  0.8038  -0.0161 153 LYS D CD  
13551 C CE  . LYS D 153 ? 1.5400 1.0180 1.2833 0.1653  0.8111  -0.0095 153 LYS D CE  
13552 N NZ  . LYS D 153 ? 1.5357 1.0167 1.2714 0.1558  0.8115  0.0021  153 LYS D NZ  
13553 N N   . GLY D 154 ? 1.5892 1.0839 1.4101 0.1973  0.7610  -0.0327 154 GLY D N   
13554 C CA  . GLY D 154 ? 1.4331 0.9521 1.3150 0.2044  0.7524  -0.0317 154 GLY D CA  
13555 C C   . GLY D 154 ? 1.4028 0.9512 1.3403 0.2013  0.7605  -0.0234 154 GLY D C   
13556 O O   . GLY D 154 ? 1.3476 0.9121 1.3098 0.2001  0.7457  -0.0160 154 GLY D O   
13557 N N   . ARG D 155 ? 1.6243 1.1799 1.5820 0.1998  0.7839  -0.0249 155 ARG D N   
13558 C CA  . ARG D 155 ? 1.6021 1.1874 1.6196 0.1972  0.7940  -0.0190 155 ARG D CA  
13559 C C   . ARG D 155 ? 1.5868 1.1677 1.5797 0.1850  0.8030  -0.0104 155 ARG D C   
13560 O O   . ARG D 155 ? 1.5888 1.1444 1.5235 0.1803  0.8085  -0.0108 155 ARG D O   
13561 C CB  . ARG D 155 ? 1.4152 1.0135 1.4772 0.2040  0.8146  -0.0266 155 ARG D CB  
13562 C CG  . ARG D 155 ? 1.4081 1.0110 1.4978 0.2170  0.8071  -0.0352 155 ARG D CG  
13563 C CD  . ARG D 155 ? 1.3628 0.9981 1.5208 0.2225  0.7933  -0.0319 155 ARG D CD  
13564 N NE  . ARG D 155 ? 1.4927 1.1574 1.7121 0.2219  0.8090  -0.0305 155 ARG D NE  
13565 C CZ  . ARG D 155 ? 1.3786 1.0764 1.6637 0.2251  0.7995  -0.0271 155 ARG D CZ  
13566 N NH1 . ARG D 155 ? 1.2865 0.9924 1.5860 0.2297  0.7745  -0.0244 155 ARG D NH1 
13567 N NH2 . ARG D 155 ? 1.4118 1.1354 1.7493 0.2234  0.8147  -0.0265 155 ARG D NH2 
13568 N N   . ASN D 156 ? 1.4408 1.0469 1.4798 0.1801  0.8036  -0.0026 156 ASN D N   
13569 C CA  . ASN D 156 ? 1.3945 1.0033 1.4326 0.1696  0.8185  0.0042  156 ASN D CA  
13570 C C   . ASN D 156 ? 1.4151 0.9984 1.3850 0.1608  0.8114  0.0110  156 ASN D C   
13571 O O   . ASN D 156 ? 1.4793 1.0412 1.4045 0.1578  0.8234  0.0097  156 ASN D O   
13572 C CB  . ASN D 156 ? 1.4331 1.0417 1.4839 0.1711  0.8455  -0.0018 156 ASN D CB  
13573 C CG  . ASN D 156 ? 1.4205 1.0576 1.5434 0.1791  0.8528  -0.0075 156 ASN D CG  
13574 O OD1 . ASN D 156 ? 1.4079 1.0651 1.5719 0.1843  0.8367  -0.0072 156 ASN D OD1 
13575 N ND2 . ASN D 156 ? 1.4543 1.0936 1.5928 0.1807  0.8764  -0.0127 156 ASN D ND2 
13576 N N   . TYR D 157 ? 1.5031 1.0891 1.4650 0.1574  0.7903  0.0184  157 TYR D N   
13577 C CA  . TYR D 157 ? 1.5010 1.0670 1.4050 0.1489  0.7806  0.0262  157 TYR D CA  
13578 C C   . TYR D 157 ? 1.3711 0.9494 1.2960 0.1390  0.7870  0.0359  157 TYR D C   
13579 O O   . TYR D 157 ? 1.3402 0.9454 1.3238 0.1380  0.7869  0.0387  157 TYR D O   
13580 C CB  . TYR D 157 ? 1.3476 0.9082 1.2276 0.1505  0.7536  0.0290  157 TYR D CB  
13581 C CG  . TYR D 157 ? 1.4064 0.9489 1.2525 0.1583  0.7453  0.0199  157 TYR D CG  
13582 C CD1 . TYR D 157 ? 1.4848 1.0366 1.3675 0.1683  0.7494  0.0107  157 TYR D CD1 
13583 C CD2 . TYR D 157 ? 1.4012 0.9176 1.1797 0.1557  0.7324  0.0203  157 TYR D CD2 
13584 C CE1 . TYR D 157 ? 1.4671 1.0007 1.3186 0.1750  0.7419  0.0020  157 TYR D CE1 
13585 C CE2 . TYR D 157 ? 1.3893 0.8892 1.1374 0.1618  0.7246  0.0114  157 TYR D CE2 
13586 C CZ  . TYR D 157 ? 1.3942 0.9018 1.1782 0.1713  0.7299  0.0022  157 TYR D CZ  
13587 O OH  . TYR D 157 ? 1.4000 0.8898 1.1541 0.1770  0.7220  -0.0071 157 TYR D OH  
13588 N N   . THR D 158 ? 1.4003 0.9593 1.2786 0.1318  0.7918  0.0409  158 THR D N   
13589 C CA  . THR D 158 ? 1.3935 0.9629 1.2919 0.1224  0.7971  0.0500  158 THR D CA  
13590 C C   . THR D 158 ? 1.3683 0.9335 1.2413 0.1163  0.7751  0.0598  158 THR D C   
13591 O O   . THR D 158 ? 1.3273 0.9113 1.2355 0.1159  0.7623  0.0631  158 THR D O   
13592 C CB  . THR D 158 ? 1.5615 1.1156 1.4338 0.1179  0.8177  0.0507  158 THR D CB  
13593 O OG1 . THR D 158 ? 1.6631 1.1883 1.4643 0.1184  0.8097  0.0505  158 THR D OG1 
13594 C CG2 . THR D 158 ? 1.7096 1.2715 1.6148 0.1228  0.8418  0.0420  158 THR D CG2 
13595 N N   . GLN D 159 ? 1.3916 0.9330 1.2043 0.1121  0.7690  0.0643  159 GLN D N   
13596 C CA  . GLN D 159 ? 1.3682 0.9036 1.1506 0.1083  0.7442  0.0723  159 GLN D CA  
13597 C C   . GLN D 159 ? 1.3914 0.9002 1.1033 0.1099  0.7308  0.0714  159 GLN D C   
13598 O O   . GLN D 159 ? 1.3734 0.8773 1.0631 0.1134  0.7104  0.0700  159 GLN D O   
13599 C CB  . GLN D 159 ? 1.3633 0.9043 1.1570 0.0989  0.7460  0.0821  159 GLN D CB  
13600 C CG  . GLN D 159 ? 1.3221 0.8720 1.1216 0.0948  0.7230  0.0903  159 GLN D CG  
13601 C CD  . GLN D 159 ? 1.5206 1.0513 1.2589 0.0947  0.6982  0.0945  159 GLN D CD  
13602 O OE1 . GLN D 159 ? 1.5564 1.0699 1.2510 0.0994  0.6924  0.0897  159 GLN D OE1 
13603 N NE2 . GLN D 159 ? 1.4520 0.9869 1.1896 0.0890  0.6827  0.1032  159 GLN D NE2 
13604 N N   . GLU D 160 ? 1.6218 0.9768 0.9946 0.0045  0.6321  0.1489  160 GLU D N   
13605 C CA  . GLU D 160 ? 1.6392 0.9917 0.9591 0.0061  0.6174  0.1580  160 GLU D CA  
13606 C C   . GLU D 160 ? 1.6732 1.0309 0.9660 0.0076  0.6056  0.1435  160 GLU D C   
13607 O O   . GLU D 160 ? 1.6366 0.9952 0.8930 0.0100  0.5873  0.1479  160 GLU D O   
13608 C CB  . GLU D 160 ? 1.6347 0.9816 0.9186 0.0022  0.6336  0.1720  160 GLU D CB  
13609 C CG  . GLU D 160 ? 1.6647 1.0086 0.9029 0.0041  0.6181  0.1884  160 GLU D CG  
13610 C CD  . GLU D 160 ? 1.7469 1.0885 0.9390 0.0002  0.6327  0.1983  160 GLU D CD  
13611 O OE1 . GLU D 160 ? 1.7626 1.1069 0.9479 -0.0035 0.6509  0.1876  160 GLU D OE1 
13612 O OE2 . GLU D 160 ? 1.7632 1.1008 0.9260 0.0008  0.6260  0.2171  160 GLU D OE2 
13613 N N   . GLU D 161 ? 1.6097 0.9714 0.9216 0.0061  0.6155  0.1262  161 GLU D N   
13614 C CA  . GLU D 161 ? 1.5461 0.9129 0.8405 0.0072  0.6041  0.1106  161 GLU D CA  
13615 C C   . GLU D 161 ? 1.4950 0.8652 0.8051 0.0118  0.5789  0.1079  161 GLU D C   
13616 O O   . GLU D 161 ? 1.5335 0.9070 0.8141 0.0135  0.5617  0.1031  161 GLU D O   
13617 C CB  . GLU D 161 ? 1.6919 1.0615 1.0108 0.0047  0.6214  0.0938  161 GLU D CB  
13618 C CG  . GLU D 161 ? 1.8317 1.1984 1.1581 0.0004  0.6489  0.0975  161 GLU D CG  
13619 C CD  . GLU D 161 ? 1.9192 1.2889 1.2444 -0.0025 0.6657  0.0810  161 GLU D CD  
13620 O OE1 . GLU D 161 ? 1.7992 1.1700 1.0791 -0.0043 0.6682  0.0771  161 GLU D OE1 
13621 O OE2 . GLU D 161 ? 1.8393 1.2113 1.2096 -0.0029 0.6762  0.0718  161 GLU D OE2 
13622 N N   . LYS D 162 ? 1.4953 0.8662 0.8520 0.0137  0.5765  0.1103  162 LYS D N   
13623 C CA  . LYS D 162 ? 1.4037 0.7788 0.7757 0.0180  0.5533  0.1080  162 LYS D CA  
13624 C C   . LYS D 162 ? 1.4149 0.7880 0.7542 0.0208  0.5348  0.1216  162 LYS D C   
13625 O O   . LYS D 162 ? 1.4392 0.8162 0.7621 0.0236  0.5145  0.1175  162 LYS D O   
13626 C CB  . LYS D 162 ? 1.3739 0.7524 0.8029 0.0191  0.5555  0.1075  162 LYS D CB  
13627 C CG  . LYS D 162 ? 1.3494 0.7259 0.7931 0.0205  0.5515  0.1227  162 LYS D CG  
13628 C CD  . LYS D 162 ? 1.4234 0.8072 0.9224 0.0221  0.5482  0.1185  162 LYS D CD  
13629 C CE  . LYS D 162 ? 1.4766 0.8594 1.0077 0.0195  0.5647  0.1264  162 LYS D CE  
13630 N NZ  . LYS D 162 ? 1.2540 0.6470 0.8416 0.0202  0.5647  0.1191  162 LYS D NZ  
13631 N N   . GLU D 163 ? 1.4440 0.8113 0.7733 0.0200  0.5414  0.1382  163 GLU D N   
13632 C CA  . GLU D 163 ? 1.4581 0.8233 0.7568 0.0229  0.5239  0.1524  163 GLU D CA  
13633 C C   . GLU D 163 ? 1.4898 0.8577 0.7368 0.0231  0.5138  0.1494  163 GLU D C   
13634 O O   . GLU D 163 ? 1.4858 0.8561 0.7119 0.0266  0.4924  0.1544  163 GLU D O   
13635 C CB  . GLU D 163 ? 1.4917 0.8494 0.7865 0.0213  0.5354  0.1714  163 GLU D CB  
13636 C CG  . GLU D 163 ? 1.4589 0.8151 0.7915 0.0235  0.5291  0.1805  163 GLU D CG  
13637 C CD  . GLU D 163 ? 1.6370 0.9861 0.9819 0.0202  0.5477  0.1944  163 GLU D CD  
13638 O OE1 . GLU D 163 ? 1.6826 1.0256 0.9906 0.0184  0.5540  0.2077  163 GLU D OE1 
13639 O OE2 . GLU D 163 ? 1.5864 0.9368 0.9779 0.0191  0.5560  0.1923  163 GLU D OE2 
13640 N N   . TYR D 164 ? 1.5215 0.8903 0.7487 0.0193  0.5286  0.1403  164 TYR D N   
13641 C CA  . TYR D 164 ? 1.5498 0.9238 0.7308 0.0189  0.5193  0.1337  164 TYR D CA  
13642 C C   . TYR D 164 ? 1.6330 1.0137 0.8220 0.0214  0.4999  0.1189  164 TYR D C   
13643 O O   . TYR D 164 ? 1.6766 1.0625 0.8342 0.0233  0.4808  0.1189  164 TYR D O   
13644 C CB  . TYR D 164 ? 1.5904 0.9648 0.7536 0.0140  0.5412  0.1250  164 TYR D CB  
13645 C CG  . TYR D 164 ? 1.6274 1.0087 0.7402 0.0129  0.5337  0.1183  164 TYR D CG  
13646 C CD1 . TYR D 164 ? 1.6618 1.0454 0.7317 0.0142  0.5210  0.1322  164 TYR D CD1 
13647 C CD2 . TYR D 164 ? 1.7024 1.0888 0.8118 0.0105  0.5390  0.0980  164 TYR D CD2 
13648 C CE1 . TYR D 164 ? 1.6964 1.0890 0.7207 0.0131  0.5134  0.1254  164 TYR D CE1 
13649 C CE2 . TYR D 164 ? 1.7694 1.1637 0.8337 0.0092  0.5321  0.0903  164 TYR D CE2 
13650 C CZ  . TYR D 164 ? 1.7243 1.1225 0.7459 0.0104  0.5191  0.1038  164 TYR D CZ  
13651 O OH  . TYR D 164 ? 1.8066 1.2151 0.7837 0.0091  0.5114  0.0956  164 TYR D OH  
13652 N N   . VAL D 165 ? 1.6045 0.9862 0.8362 0.0213  0.5043  0.1063  165 VAL D N   
13653 C CA  . VAL D 165 ? 1.5820 0.9700 0.8222 0.0232  0.4868  0.0927  165 VAL D CA  
13654 C C   . VAL D 165 ? 1.4532 0.8432 0.7025 0.0279  0.4642  0.1012  165 VAL D C   
13655 O O   . VAL D 165 ? 1.4689 0.8648 0.7061 0.0298  0.4447  0.0949  165 VAL D O   
13656 C CB  . VAL D 165 ? 1.5975 0.9867 0.8803 0.0218  0.4979  0.0778  165 VAL D CB  
13657 C CG1 . VAL D 165 ? 1.6832 1.0699 0.9625 0.0174  0.5229  0.0714  165 VAL D CG1 
13658 C CG2 . VAL D 165 ? 1.4686 0.8574 0.8013 0.0240  0.4977  0.0826  165 VAL D CG2 
13659 N N   . LEU D 166 ? 1.3835 0.7692 0.6549 0.0297  0.4666  0.1149  166 LEU D N   
13660 C CA  . LEU D 166 ? 1.4774 0.8649 0.7548 0.0343  0.4457  0.1239  166 LEU D CA  
13661 C C   . LEU D 166 ? 1.5688 0.9579 0.7991 0.0361  0.4296  0.1326  166 LEU D C   
13662 O O   . LEU D 166 ? 1.5226 0.9174 0.7463 0.0394  0.4078  0.1308  166 LEU D O   
13663 C CB  . LEU D 166 ? 1.5659 0.9487 0.8744 0.0352  0.4530  0.1369  166 LEU D CB  
13664 C CG  . LEU D 166 ? 1.5879 0.9740 0.9510 0.0355  0.4574  0.1302  166 LEU D CG  
13665 C CD1 . LEU D 166 ? 1.4634 0.8487 0.8489 0.0315  0.4803  0.1209  166 LEU D CD1 
13666 C CD2 . LEU D 166 ? 1.5108 0.8951 0.8984 0.0373  0.4557  0.1437  166 LEU D CD2 
13667 N N   . ASN D 167 ? 1.5703 0.9554 0.7674 0.0340  0.4400  0.1423  167 ASN D N   
13668 C CA  . ASN D 167 ? 1.6726 1.0609 0.8237 0.0356  0.4250  0.1514  167 ASN D CA  
13669 C C   . ASN D 167 ? 1.5533 0.9513 0.6789 0.0349  0.4128  0.1358  167 ASN D C   
13670 O O   . ASN D 167 ? 1.5264 0.9311 0.6291 0.0378  0.3914  0.1385  167 ASN D O   
13671 C CB  . ASN D 167 ? 1.6131 0.9963 0.7344 0.0328  0.4408  0.1649  167 ASN D CB  
13672 C CG  . ASN D 167 ? 1.6815 1.0671 0.7632 0.0355  0.4249  0.1811  167 ASN D CG  
13673 O OD1 . ASN D 167 ? 1.6537 1.0344 0.7440 0.0387  0.4181  0.1978  167 ASN D OD1 
13674 N ND2 . ASN D 167 ? 1.6777 1.0716 0.7166 0.0341  0.4189  0.1762  167 ASN D ND2 
13675 N N   . LYS D 168 ? 1.4802 0.8795 0.6104 0.0310  0.4262  0.1191  168 LYS D N   
13676 C CA  . LYS D 168 ? 1.4804 0.8888 0.5914 0.0297  0.4155  0.1022  168 LYS D CA  
13677 C C   . LYS D 168 ? 1.5410 0.9547 0.6750 0.0330  0.3946  0.0951  168 LYS D C   
13678 O O   . LYS D 168 ? 1.5490 0.9716 0.6608 0.0339  0.3757  0.0897  168 LYS D O   
13679 C CB  . LYS D 168 ? 1.5688 0.9765 0.6871 0.0250  0.4356  0.0857  168 LYS D CB  
13680 C CG  . LYS D 168 ? 1.6602 1.0690 0.7383 0.0212  0.4498  0.0857  168 LYS D CG  
13681 C CD  . LYS D 168 ? 1.5761 0.9963 0.6100 0.0209  0.4331  0.0796  168 LYS D CD  
13682 C CE  . LYS D 168 ? 1.6380 1.0606 0.6261 0.0192  0.4399  0.0909  168 LYS D CE  
13683 N NZ  . LYS D 168 ? 1.6557 1.0878 0.6085 0.0219  0.4163  0.0997  168 LYS D NZ  
13684 N N   . TYR D 169 ? 1.5077 0.9172 0.6865 0.0345  0.3979  0.0949  169 TYR D N   
13685 C CA  . TYR D 169 ? 1.3441 0.7590 0.5459 0.0374  0.3792  0.0889  169 TYR D CA  
13686 C C   . TYR D 169 ? 1.3325 0.7508 0.5209 0.0421  0.3574  0.1017  169 TYR D C   
13687 O O   . TYR D 169 ? 1.3397 0.7662 0.5241 0.0440  0.3373  0.0958  169 TYR D O   
13688 C CB  . TYR D 169 ? 1.2913 0.7028 0.5437 0.0379  0.3885  0.0868  169 TYR D CB  
13689 C CG  . TYR D 169 ? 1.3958 0.8067 0.6686 0.0341  0.4051  0.0719  169 TYR D CG  
13690 C CD1 . TYR D 169 ? 1.3826 0.7960 0.6305 0.0306  0.4091  0.0592  169 TYR D CD1 
13691 C CD2 . TYR D 169 ? 1.3568 0.7659 0.6752 0.0341  0.4164  0.0701  169 TYR D CD2 
13692 C CE1 . TYR D 169 ? 1.3740 0.7865 0.6424 0.0274  0.4244  0.0457  169 TYR D CE1 
13693 C CE2 . TYR D 169 ? 1.2652 0.6744 0.6046 0.0311  0.4311  0.0575  169 TYR D CE2 
13694 C CZ  . TYR D 169 ? 1.2972 0.7075 0.6118 0.0278  0.4352  0.0455  169 TYR D CZ  
13695 O OH  . TYR D 169 ? 1.3180 0.7282 0.6551 0.0250  0.4499  0.0331  169 TYR D OH  
13696 N N   . PHE D 170 ? 1.3955 0.8078 0.5790 0.0440  0.3612  0.1195  170 PHE D N   
13697 C CA  . PHE D 170 ? 1.3908 0.8058 0.5635 0.0489  0.3409  0.1328  170 PHE D CA  
13698 C C   . PHE D 170 ? 1.3874 0.8106 0.5142 0.0492  0.3262  0.1334  170 PHE D C   
13699 O O   . PHE D 170 ? 1.3773 0.8075 0.4969 0.0531  0.3042  0.1371  170 PHE D O   
13700 C CB  . PHE D 170 ? 1.5470 0.9529 0.7279 0.0505  0.3497  0.1520  170 PHE D CB  
13701 C CG  . PHE D 170 ? 1.5654 0.9678 0.7941 0.0521  0.3531  0.1533  170 PHE D CG  
13702 C CD1 . PHE D 170 ? 1.5399 0.9479 0.7878 0.0564  0.3341  0.1529  170 PHE D CD1 
13703 C CD2 . PHE D 170 ? 1.6253 1.0209 0.8807 0.0491  0.3754  0.1542  170 PHE D CD2 
13704 C CE1 . PHE D 170 ? 1.5390 0.9461 0.8304 0.0575  0.3371  0.1533  170 PHE D CE1 
13705 C CE2 . PHE D 170 ? 1.6182 1.0135 0.9186 0.0502  0.3780  0.1545  170 PHE D CE2 
13706 C CZ  . PHE D 170 ? 1.5106 0.9119 0.8284 0.0543  0.3588  0.1539  170 PHE D CZ  
13707 N N   . GLU D 171 ? 1.4303 0.8541 0.5262 0.0450  0.3379  0.1296  171 GLU D N   
13708 C CA  . GLU D 171 ? 1.4690 0.9038 0.5218 0.0447  0.3239  0.1276  171 GLU D CA  
13709 C C   . GLU D 171 ? 1.4383 0.8840 0.4939 0.0437  0.3095  0.1080  171 GLU D C   
13710 O O   . GLU D 171 ? 1.4450 0.9023 0.4792 0.0454  0.2887  0.1072  171 GLU D O   
13711 C CB  . GLU D 171 ? 1.5199 0.9540 0.5390 0.0401  0.3413  0.1277  171 GLU D CB  
13712 C CG  . GLU D 171 ? 1.5957 1.0417 0.5665 0.0402  0.3274  0.1319  171 GLU D CG  
13713 C CD  . GLU D 171 ? 1.7435 1.1927 0.6808 0.0349  0.3437  0.1253  171 GLU D CD  
13714 O OE1 . GLU D 171 ? 1.6820 1.1237 0.6348 0.0313  0.3656  0.1163  171 GLU D OE1 
13715 O OE2 . GLU D 171 ? 1.6563 1.1166 0.5522 0.0345  0.3344  0.1289  171 GLU D OE2 
13716 N N   . ILE D 172 ? 1.4088 0.8518 0.4922 0.0409  0.3202  0.0924  172 ILE D N   
13717 C CA  . ILE D 172 ? 1.3834 0.8358 0.4726 0.0395  0.3077  0.0741  172 ILE D CA  
13718 C C   . ILE D 172 ? 1.4171 0.8730 0.5330 0.0438  0.2886  0.0759  172 ILE D C   
13719 O O   . ILE D 172 ? 1.3789 0.8450 0.4946 0.0433  0.2728  0.0641  172 ILE D O   
13720 C CB  . ILE D 172 ? 1.4935 0.9419 0.6028 0.0349  0.3260  0.0573  172 ILE D CB  
13721 C CG1 . ILE D 172 ? 1.5112 0.9704 0.6092 0.0318  0.3162  0.0377  172 ILE D CG1 
13722 C CG2 . ILE D 172 ? 1.3639 0.8055 0.5213 0.0364  0.3316  0.0572  172 ILE D CG2 
13723 C CD1 . ILE D 172 ? 1.4181 0.8881 0.4694 0.0305  0.3063  0.0364  172 ILE D CD1 
13724 N N   . ILE D 173 ? 1.4381 0.8866 0.5778 0.0476  0.2901  0.0897  173 ILE D N   
13725 C CA  . ILE D 173 ? 1.2746 0.7275 0.4355 0.0522  0.2711  0.0931  173 ILE D CA  
13726 C C   . ILE D 173 ? 1.3044 0.7667 0.4365 0.0557  0.2490  0.1013  173 ILE D C   
13727 O O   . ILE D 173 ? 1.2692 0.7414 0.4071 0.0579  0.2290  0.0965  173 ILE D O   
13728 C CB  . ILE D 173 ? 1.2502 0.6937 0.4447 0.0551  0.2797  0.1048  173 ILE D CB  
13729 C CG1 . ILE D 173 ? 1.2188 0.6585 0.4506 0.0525  0.2946  0.0938  173 ILE D CG1 
13730 C CG2 . ILE D 173 ? 1.2588 0.7070 0.4659 0.0607  0.2594  0.1129  173 ILE D CG2 
13731 C CD1 . ILE D 173 ? 1.2005 0.6321 0.4641 0.0538  0.3081  0.1038  173 ILE D CD1 
13732 N N   . LYS D 174 ? 1.3402 0.8004 0.4414 0.0562  0.2522  0.1142  174 LYS D N   
13733 C CA  . LYS D 174 ? 1.3623 0.8321 0.4366 0.0599  0.2314  0.1243  174 LYS D CA  
13734 C C   . LYS D 174 ? 1.3727 0.8585 0.4231 0.0573  0.2169  0.1095  174 LYS D C   
13735 O O   . LYS D 174 ? 1.3621 0.8599 0.4096 0.0604  0.1944  0.1097  174 LYS D O   
13736 C CB  . LYS D 174 ? 1.4123 0.8763 0.4591 0.0605  0.2399  0.1424  174 LYS D CB  
13737 C CG  . LYS D 174 ? 1.4040 0.8541 0.4745 0.0636  0.2497  0.1595  174 LYS D CG  
13738 C CD  . LYS D 174 ? 1.4555 0.8977 0.5009 0.0622  0.2645  0.1752  174 LYS D CD  
13739 C CE  . LYS D 174 ? 1.4449 0.8721 0.5204 0.0627  0.2815  0.1866  174 LYS D CE  
13740 N NZ  . LYS D 174 ? 1.4511 0.8745 0.5303 0.0682  0.2707  0.2072  174 LYS D NZ  
13741 N N   . LYS D 175 ? 1.3938 0.8810 0.4286 0.0515  0.2295  0.0958  175 LYS D N   
13742 C CA  . LYS D 175 ? 1.4047 0.9075 0.4187 0.0483  0.2171  0.0796  175 LYS D CA  
13743 C C   . LYS D 175 ? 1.3569 0.8649 0.4003 0.0471  0.2082  0.0629  175 LYS D C   
13744 O O   . LYS D 175 ? 1.3608 0.8826 0.3923 0.0443  0.1964  0.0484  175 LYS D O   
13745 C CB  . LYS D 175 ? 1.4450 0.9477 0.4334 0.0424  0.2345  0.0695  175 LYS D CB  
13746 C CG  . LYS D 175 ? 1.5015 1.0056 0.4503 0.0426  0.2389  0.0838  175 LYS D CG  
13747 C CD  . LYS D 175 ? 1.5325 1.0566 0.4454 0.0421  0.2191  0.0802  175 LYS D CD  
13748 C CE  . LYS D 175 ? 1.5800 1.1068 0.4592 0.0447  0.2161  0.1014  175 LYS D CE  
13749 N NZ  . LYS D 175 ? 1.6256 1.1458 0.4804 0.0409  0.2392  0.1044  175 LYS D NZ  
13750 N N   . THR D 176 ? 1.3944 0.8926 0.4760 0.0490  0.2136  0.0645  176 THR D N   
13751 C CA  . THR D 176 ? 1.3001 0.8030 0.4103 0.0477  0.2064  0.0499  176 THR D CA  
13752 C C   . THR D 176 ? 1.2540 0.7724 0.3619 0.0503  0.1796  0.0485  176 THR D C   
13753 O O   . THR D 176 ? 1.2589 0.7878 0.3716 0.0471  0.1704  0.0326  176 THR D O   
13754 C CB  . THR D 176 ? 1.2280 0.7191 0.3782 0.0497  0.2170  0.0542  176 THR D CB  
13755 O OG1 . THR D 176 ? 1.3754 0.8541 0.5309 0.0467  0.2421  0.0533  176 THR D OG1 
13756 C CG2 . THR D 176 ? 1.1908 0.6877 0.3700 0.0485  0.2091  0.0408  176 THR D CG2 
13757 N N   . LEU D 177 ? 1.2579 0.7785 0.3606 0.0561  0.1669  0.0647  177 LEU D N   
13758 C CA  . LEU D 177 ? 1.2873 0.8237 0.3904 0.0589  0.1414  0.0637  177 LEU D CA  
13759 C C   . LEU D 177 ? 1.3176 0.8703 0.3854 0.0564  0.1292  0.0581  177 LEU D C   
13760 O O   . LEU D 177 ? 1.2693 0.8381 0.3390 0.0553  0.1115  0.0473  177 LEU D O   
13761 C CB  . LEU D 177 ? 1.3683 0.9019 0.4811 0.0664  0.1318  0.0827  177 LEU D CB  
13762 C CG  . LEU D 177 ? 1.1941 0.7381 0.3316 0.0702  0.1117  0.0808  177 LEU D CG  
13763 C CD1 . LEU D 177 ? 1.1486 0.6840 0.3231 0.0699  0.1211  0.0754  177 LEU D CD1 
13764 C CD2 . LEU D 177 ? 1.2316 0.7771 0.3670 0.0777  0.0987  0.0992  177 LEU D CD2 
13765 N N   . SER D 178 ? 1.3809 0.9309 0.4164 0.0553  0.1384  0.0650  178 SER D N   
13766 C CA  . SER D 178 ? 1.4181 0.9851 0.4182 0.0525  0.1278  0.0587  178 SER D CA  
13767 C C   . SER D 178 ? 1.4325 1.0074 0.4331 0.0455  0.1305  0.0342  178 SER D C   
13768 O O   . SER D 178 ? 1.4531 1.0469 0.4390 0.0431  0.1147  0.0235  178 SER D O   
13769 C CB  . SER D 178 ? 1.4258 0.9882 0.3909 0.0522  0.1397  0.0709  178 SER D CB  
13770 O OG  . SER D 178 ? 1.4353 0.9869 0.3965 0.0471  0.1634  0.0616  178 SER D OG  
13771 N N   . ILE D 179 ? 1.3887 0.9498 0.4083 0.0422  0.1501  0.0249  179 ILE D N   
13772 C CA  . ILE D 179 ? 1.3518 0.9178 0.3744 0.0358  0.1550  0.0020  179 ILE D CA  
13773 C C   . ILE D 179 ? 1.4159 0.9931 0.4630 0.0348  0.1379  -0.0103 179 ILE D C   
13774 O O   . ILE D 179 ? 1.4187 1.0016 0.4696 0.0294  0.1393  -0.0298 179 ILE D O   
13775 C CB  . ILE D 179 ? 1.3366 0.8843 0.3761 0.0331  0.1811  -0.0029 179 ILE D CB  
13776 C CG1 . ILE D 179 ? 1.3663 0.9177 0.3884 0.0268  0.1918  -0.0221 179 ILE D CG1 
13777 C CG2 . ILE D 179 ? 1.2826 0.8230 0.3652 0.0338  0.1824  -0.0064 179 ILE D CG2 
13778 C CD1 . ILE D 179 ? 1.4734 1.0287 0.4533 0.0259  0.1975  -0.0178 179 ILE D CD1 
13779 N N   . TYR D 180 ? 1.4201 1.0015 0.4839 0.0398  0.1217  0.0003  180 TYR D N   
13780 C CA  . TYR D 180 ? 1.2683 0.8638 0.3522 0.0389  0.1034  -0.0102 180 TYR D CA  
13781 C C   . TYR D 180 ? 1.3271 0.9443 0.3922 0.0402  0.0797  -0.0087 180 TYR D C   
13782 O O   . TYR D 180 ? 1.2481 0.8814 0.3199 0.0367  0.0662  -0.0234 180 TYR D O   
13783 C CB  . TYR D 180 ? 1.3563 0.9440 0.4766 0.0432  0.1012  -0.0020 180 TYR D CB  
13784 C CG  . TYR D 180 ? 1.2192 0.7912 0.3655 0.0408  0.1207  -0.0080 180 TYR D CG  
13785 C CD1 . TYR D 180 ? 1.2223 0.7975 0.3832 0.0351  0.1233  -0.0264 180 TYR D CD1 
13786 C CD2 . TYR D 180 ? 1.1605 0.7152 0.3182 0.0441  0.1366  0.0050  180 TYR D CD2 
13787 C CE1 . TYR D 180 ? 1.1298 0.6915 0.3156 0.0332  0.1408  -0.0307 180 TYR D CE1 
13788 C CE2 . TYR D 180 ? 1.1375 0.6799 0.3205 0.0420  0.1540  -0.0001 180 TYR D CE2 
13789 C CZ  . TYR D 180 ? 1.1223 0.6684 0.3192 0.0367  0.1559  -0.0175 180 TYR D CZ  
13790 O OH  . TYR D 180 ? 1.1004 0.6352 0.3239 0.0349  0.1731  -0.0216 180 TYR D OH  
13791 N N   . ARG D 181 ? 1.3411 0.9597 0.3841 0.0450  0.0744  0.0088  181 ARG D N   
13792 C CA  . ARG D 181 ? 1.3050 0.9453 0.3313 0.0467  0.0514  0.0116  181 ARG D CA  
13793 C C   . ARG D 181 ? 1.4330 1.0897 0.4296 0.0404  0.0483  -0.0040 181 ARG D C   
13794 O O   . ARG D 181 ? 1.5678 1.2462 0.5634 0.0383  0.0295  -0.0138 181 ARG D O   
13795 C CB  . ARG D 181 ? 1.3289 0.9658 0.3388 0.0536  0.0472  0.0355  181 ARG D CB  
13796 C CG  . ARG D 181 ? 1.3022 0.9196 0.3359 0.0597  0.0555  0.0515  181 ARG D CG  
13797 C CD  . ARG D 181 ? 1.4180 1.0329 0.4324 0.0658  0.0513  0.0741  181 ARG D CD  
13798 N NE  . ARG D 181 ? 1.3052 0.9067 0.3463 0.0727  0.0523  0.0892  181 ARG D NE  
13799 C CZ  . ARG D 181 ? 1.3172 0.8999 0.3569 0.0757  0.0678  0.1049  181 ARG D CZ  
13800 N NH1 . ARG D 181 ? 1.3561 0.9305 0.3696 0.0724  0.0844  0.1082  181 ARG D NH1 
13801 N NH2 . ARG D 181 ? 1.2905 0.8631 0.3565 0.0818  0.0669  0.1170  181 ARG D NH2 
13802 N N   . GLU D 182 ? 1.5700 1.2182 0.5422 0.0373  0.0663  -0.0068 182 GLU D N   
13803 C CA  . GLU D 182 ? 1.5406 1.2050 0.4846 0.0313  0.0644  -0.0239 182 GLU D CA  
13804 C C   . GLU D 182 ? 1.5616 1.2350 0.5264 0.0255  0.0597  -0.0484 182 GLU D C   
13805 O O   . GLU D 182 ? 1.5639 1.2597 0.5257 0.0235  0.0406  -0.0578 182 GLU D O   
13806 C CB  . GLU D 182 ? 1.5794 1.2312 0.4984 0.0288  0.0877  -0.0248 182 GLU D CB  
13807 C CG  . GLU D 182 ? 1.7569 1.3970 0.6581 0.0340  0.0955  0.0004  182 GLU D CG  
13808 C CD  . GLU D 182 ? 1.7836 1.3993 0.6907 0.0335  0.1228  0.0044  182 GLU D CD  
13809 O OE1 . GLU D 182 ? 1.7207 1.3291 0.6416 0.0291  0.1367  -0.0127 182 GLU D OE1 
13810 O OE2 . GLU D 182 ? 1.8255 1.4297 0.7246 0.0376  0.1304  0.0250  182 GLU D OE2 
13811 N N   . ILE D 183 ? 1.5193 1.1756 0.5106 0.0234  0.0756  -0.0569 183 ILE D N   
13812 C CA  . ILE D 183 ? 1.4631 1.1253 0.4728 0.0174  0.0744  -0.0806 183 ILE D CA  
13813 C C   . ILE D 183 ? 1.3550 1.0369 0.3819 0.0172  0.0503  -0.0851 183 ILE D C   
13814 O O   . ILE D 183 ? 1.3155 1.0105 0.3478 0.0118  0.0435  -0.1053 183 ILE D O   
13815 C CB  . ILE D 183 ? 1.3092 0.9492 0.3505 0.0163  0.0936  -0.0844 183 ILE D CB  
13816 C CG1 . ILE D 183 ? 1.3713 1.0050 0.4470 0.0206  0.0874  -0.0722 183 ILE D CG1 
13817 C CG2 . ILE D 183 ? 1.3329 0.9540 0.3609 0.0170  0.1174  -0.0775 183 ILE D CG2 
13818 C CD1 . ILE D 183 ? 1.3536 0.9938 0.4609 0.0170  0.0792  -0.0868 183 ILE D CD1 
13819 N N   . LYS D 184 ? 1.3031 0.9877 0.3401 0.0231  0.0375  -0.0670 184 LYS D N   
13820 C CA  . LYS D 184 ? 1.3331 1.0390 0.3840 0.0231  0.0140  -0.0701 184 LYS D CA  
13821 C C   . LYS D 184 ? 1.4335 1.1641 0.4535 0.0214  -0.0019 -0.0738 184 LYS D C   
13822 O O   . LYS D 184 ? 1.4424 1.1944 0.4694 0.0173  -0.0176 -0.0878 184 LYS D O   
13823 C CB  . LYS D 184 ? 1.2442 0.9451 0.3159 0.0306  0.0060  -0.0500 184 LYS D CB  
13824 C CG  . LYS D 184 ? 1.2186 0.9405 0.3102 0.0310  -0.0170 -0.0526 184 LYS D CG  
13825 C CD  . LYS D 184 ? 1.1799 0.8933 0.2990 0.0382  -0.0208 -0.0364 184 LYS D CD  
13826 C CE  . LYS D 184 ? 1.1658 0.9020 0.2977 0.0403  -0.0448 -0.0342 184 LYS D CE  
13827 N NZ  . LYS D 184 ? 1.1758 0.9335 0.3112 0.0322  -0.0551 -0.0553 184 LYS D NZ  
13828 N N   . GLU D 185 ? 1.4916 1.2208 0.4777 0.0241  0.0018  -0.0612 185 GLU D N   
13829 C CA  . GLU D 185 ? 1.4025 1.1563 0.3564 0.0224  -0.0129 -0.0635 185 GLU D CA  
13830 C C   . GLU D 185 ? 1.4313 1.1956 0.3676 0.0148  -0.0076 -0.0888 185 GLU D C   
13831 O O   . GLU D 185 ? 1.4431 1.2325 0.3737 0.0107  -0.0238 -0.1029 185 GLU D O   
13832 C CB  . GLU D 185 ? 1.4405 1.1890 0.3630 0.0277  -0.0099 -0.0408 185 GLU D CB  
13833 C CG  . GLU D 185 ? 1.4710 1.2195 0.4042 0.0355  -0.0238 -0.0172 185 GLU D CG  
13834 C CD  . GLU D 185 ? 1.5965 1.3621 0.5592 0.0355  -0.0446 -0.0230 185 GLU D CD  
13835 O OE1 . GLU D 185 ? 1.6588 1.4506 0.6101 0.0322  -0.0624 -0.0307 185 GLU D OE1 
13836 O OE2 . GLU D 185 ? 1.5097 1.2635 0.5070 0.0385  -0.0430 -0.0200 185 GLU D OE2 
13837 N N   . GLU D 186 ? 1.4617 1.2074 0.3903 0.0129  0.0150  -0.0958 186 GLU D N   
13838 C CA  . GLU D 186 ? 1.5734 1.3271 0.4883 0.0066  0.0209  -0.1215 186 GLU D CA  
13839 C C   . GLU D 186 ? 1.5727 1.3319 0.5194 0.0018  0.0150  -0.1436 186 GLU D C   
13840 O O   . GLU D 186 ? 1.6024 1.3719 0.5398 -0.0031 0.0153  -0.1668 186 GLU D O   
13841 C CB  . GLU D 186 ? 1.6400 1.3711 0.5438 0.0058  0.0476  -0.1244 186 GLU D CB  
13842 C CG  . GLU D 186 ? 1.5626 1.2669 0.4860 0.0101  0.0625  -0.1054 186 GLU D CG  
13843 C CD  . GLU D 186 ? 1.7008 1.3973 0.5942 0.0139  0.0722  -0.0857 186 GLU D CD  
13844 O OE1 . GLU D 186 ? 1.7916 1.4998 0.6659 0.0174  0.0586  -0.0695 186 GLU D OE1 
13845 O OE2 . GLU D 186 ? 1.8292 1.5063 0.7211 0.0134  0.0946  -0.0849 186 GLU D OE2 
13846 N N   . GLY D 187 ? 1.3873 1.1400 0.3708 0.0033  0.0100  -0.1375 187 GLY D N   
13847 C CA  . GLY D 187 ? 1.3568 1.1145 0.3710 -0.0015 0.0048  -0.1569 187 GLY D CA  
13848 C C   . GLY D 187 ? 1.3490 1.0847 0.3805 -0.0046 0.0253  -0.1702 187 GLY D C   
13849 O O   . GLY D 187 ? 1.3953 1.1337 0.4508 -0.0090 0.0223  -0.1877 187 GLY D O   
13850 N N   . LYS D 188 ? 1.3563 1.0701 0.3779 -0.0027 0.0464  -0.1623 188 LYS D N   
13851 C CA  . LYS D 188 ? 1.3456 1.0383 0.3852 -0.0056 0.0670  -0.1737 188 LYS D CA  
13852 C C   . LYS D 188 ? 1.4179 1.0953 0.4976 -0.0042 0.0713  -0.1651 188 LYS D C   
13853 O O   . LYS D 188 ? 1.3468 1.0074 0.4460 -0.0067 0.0874  -0.1733 188 LYS D O   
13854 C CB  . LYS D 188 ? 1.3786 1.0551 0.3946 -0.0043 0.0888  -0.1687 188 LYS D CB  
13855 C CG  . LYS D 188 ? 1.5342 1.2254 0.5058 -0.0045 0.0859  -0.1724 188 LYS D CG  
13856 C CD  . LYS D 188 ? 1.6844 1.3622 0.6324 -0.0011 0.1026  -0.1552 188 LYS D CD  
13857 C CE  . LYS D 188 ? 1.5410 1.2003 0.4881 -0.0036 0.1281  -0.1658 188 LYS D CE  
13858 N NZ  . LYS D 188 ? 1.4826 1.1244 0.4229 0.0000  0.1453  -0.1450 188 LYS D NZ  
13859 N N   . GLY D 189 ? 1.3551 1.0383 0.4479 -0.0002 0.0576  -0.1489 189 GLY D N   
13860 C CA  . GLY D 189 ? 1.2639 0.9344 0.3934 0.0015  0.0612  -0.1411 189 GLY D CA  
13861 C C   . GLY D 189 ? 1.2883 0.9707 0.4296 0.0059  0.0422  -0.1267 189 GLY D C   
13862 O O   . GLY D 189 ? 1.3344 1.0317 0.4552 0.0086  0.0281  -0.1188 189 GLY D O   
13863 N N   . SER D 190 ? 1.1413 0.8174 0.3167 0.0067  0.0420  -0.1234 190 SER D N   
13864 C CA  . SER D 190 ? 1.1102 0.7948 0.3021 0.0114  0.0266  -0.1098 190 SER D CA  
13865 C C   . SER D 190 ? 1.0976 0.7624 0.3056 0.0170  0.0386  -0.0931 190 SER D C   
13866 O O   . SER D 190 ? 1.1650 0.8140 0.3899 0.0152  0.0548  -0.0967 190 SER D O   
13867 C CB  . SER D 190 ? 1.0796 0.7783 0.2993 0.0073  0.0135  -0.1216 190 SER D CB  
13868 O OG  . SER D 190 ? 1.2411 0.9509 0.4753 0.0120  -0.0024 -0.1091 190 SER D OG  
13869 N N   . VAL D 191 ? 1.0801 0.7463 0.2839 0.0239  0.0307  -0.0750 191 VAL D N   
13870 C CA  . VAL D 191 ? 1.0558 0.7053 0.2754 0.0298  0.0401  -0.0590 191 VAL D CA  
13871 C C   . VAL D 191 ? 1.0510 0.7109 0.2968 0.0334  0.0243  -0.0534 191 VAL D C   
13872 O O   . VAL D 191 ? 1.0878 0.7647 0.3286 0.0358  0.0059  -0.0498 191 VAL D O   
13873 C CB  . VAL D 191 ? 1.0844 0.7242 0.2794 0.0354  0.0460  -0.0422 191 VAL D CB  
13874 C CG1 . VAL D 191 ? 1.0661 0.6844 0.2765 0.0392  0.0634  -0.0307 191 VAL D CG1 
13875 C CG2 . VAL D 191 ? 1.1314 0.7710 0.2931 0.0316  0.0539  -0.0490 191 VAL D CG2 
13876 N N   . SER D 192 ? 0.9810 0.6321 0.2554 0.0336  0.0316  -0.0529 192 SER D N   
13877 C CA  . SER D 192 ? 0.9787 0.6389 0.2797 0.0370  0.0191  -0.0482 192 SER D CA  
13878 C C   . SER D 192 ? 0.9950 0.6406 0.3059 0.0441  0.0272  -0.0320 192 SER D C   
13879 O O   . SER D 192 ? 0.9608 0.5897 0.2589 0.0460  0.0424  -0.0244 192 SER D O   
13880 C CB  . SER D 192 ? 0.9143 0.5791 0.2412 0.0310  0.0194  -0.0617 192 SER D CB  
13881 O OG  . SER D 192 ? 0.9042 0.5506 0.2422 0.0296  0.0392  -0.0624 192 SER D OG  
13882 N N   . THR D 193 ? 0.8930 0.5460 0.2279 0.0478  0.0173  -0.0273 193 THR D N   
13883 C CA  . THR D 193 ? 0.9736 0.6149 0.3222 0.0542  0.0242  -0.0142 193 THR D CA  
13884 C C   . THR D 193 ? 0.9426 0.5910 0.3231 0.0537  0.0202  -0.0180 193 THR D C   
13885 O O   . THR D 193 ? 0.8974 0.5576 0.2887 0.0481  0.0141  -0.0301 193 THR D O   
13886 C CB  . THR D 193 ? 0.9331 0.5764 0.2713 0.0620  0.0141  0.0002  193 THR D CB  
13887 O OG1 . THR D 193 ? 0.8770 0.5044 0.2238 0.0675  0.0255  0.0126  193 THR D OG1 
13888 C CG2 . THR D 193 ? 0.8679 0.5323 0.2201 0.0647  -0.0077 -0.0005 193 THR D CG2 
13889 N N   . SER D 194 ? 0.9933 0.6347 0.3890 0.0592  0.0245  -0.0078 194 SER D N   
13890 C CA  . SER D 194 ? 0.8352 0.4837 0.2600 0.0595  0.0216  -0.0099 194 SER D CA  
13891 C C   . SER D 194 ? 0.8336 0.4869 0.2680 0.0676  0.0117  0.0011  194 SER D C   
13892 O O   . SER D 194 ? 0.9194 0.5669 0.3384 0.0728  0.0098  0.0110  194 SER D O   
13893 C CB  . SER D 194 ? 0.7600 0.3940 0.1971 0.0571  0.0415  -0.0109 194 SER D CB  
13894 O OG  . SER D 194 ? 0.7722 0.4065 0.2111 0.0496  0.0473  -0.0235 194 SER D OG  
13895 N N   . PRO D 195 ? 0.8379 0.5018 0.2975 0.0690  0.0052  -0.0001 195 PRO D N   
13896 C CA  . PRO D 195 ? 0.7132 0.3794 0.1831 0.0770  -0.0016 0.0100  195 PRO D CA  
13897 C C   . PRO D 195 ? 0.7240 0.3691 0.1881 0.0810  0.0146  0.0212  195 PRO D C   
13898 O O   . PRO D 195 ? 0.7643 0.3964 0.2285 0.0774  0.0321  0.0201  195 PRO D O   
13899 C CB  . PRO D 195 ? 0.7484 0.4281 0.2461 0.0760  -0.0064 0.0047  195 PRO D CB  
13900 C CG  . PRO D 195 ? 0.6714 0.3634 0.1720 0.0682  -0.0114 -0.0080 195 PRO D CG  
13901 C CD  . PRO D 195 ? 0.7368 0.4140 0.2158 0.0633  0.0010  -0.0112 195 PRO D CD  
13902 N N   . TYR D 196 ? 0.7329 0.3751 0.1941 0.0883  0.0089  0.0322  196 TYR D N   
13903 C CA  . TYR D 196 ? 0.7559 0.3784 0.2051 0.0914  0.0225  0.0439  196 TYR D CA  
13904 C C   . TYR D 196 ? 0.7476 0.3555 0.2061 0.0885  0.0439  0.0451  196 TYR D C   
13905 O O   . TYR D 196 ? 0.7696 0.3639 0.2140 0.0854  0.0590  0.0464  196 TYR D O   
13906 C CB  . TYR D 196 ? 0.7566 0.3790 0.2129 0.0999  0.0139  0.0554  196 TYR D CB  
13907 C CG  . TYR D 196 ? 0.8179 0.4245 0.2555 0.1030  0.0217  0.0676  196 TYR D CG  
13908 C CD1 . TYR D 196 ? 0.7974 0.3862 0.2375 0.1019  0.0416  0.0743  196 TYR D CD1 
13909 C CD2 . TYR D 196 ? 0.9122 0.5233 0.3311 0.1063  0.0095  0.0725  196 TYR D CD2 
13910 C CE1 . TYR D 196 ? 0.8298 0.4051 0.2540 0.1040  0.0494  0.0856  196 TYR D CE1 
13911 C CE2 . TYR D 196 ? 0.9153 0.5125 0.3161 0.1088  0.0168  0.0847  196 TYR D CE2 
13912 C CZ  . TYR D 196 ? 0.8576 0.4367 0.2611 0.1075  0.0369  0.0912  196 TYR D CZ  
13913 O OH  . TYR D 196 ? 0.8919 0.4580 0.2787 0.1094  0.0448  0.1036  196 TYR D OH  
13914 N N   . TYR D 197 ? 0.7168 0.3286 0.2001 0.0893  0.0458  0.0447  197 TYR D N   
13915 C CA  . TYR D 197 ? 0.7075 0.3079 0.2045 0.0870  0.0657  0.0475  197 TYR D CA  
13916 C C   . TYR D 197 ? 0.6844 0.2934 0.1978 0.0807  0.0713  0.0364  197 TYR D C   
13917 O O   . TYR D 197 ? 0.7026 0.3160 0.2476 0.0786  0.0808  0.0361  197 TYR D O   
13918 C CB  . TYR D 197 ? 0.6876 0.2905 0.2130 0.0913  0.0651  0.0552  197 TYR D CB  
13919 C CG  . TYR D 197 ? 0.7127 0.3034 0.2255 0.0973  0.0636  0.0674  197 TYR D CG  
13920 C CD1 . TYR D 197 ? 0.7355 0.3103 0.2415 0.0961  0.0803  0.0745  197 TYR D CD1 
13921 C CD2 . TYR D 197 ? 0.7116 0.3109 0.2263 0.1037  0.0454  0.0705  197 TYR D CD2 
13922 C CE1 . TYR D 197 ? 0.7575 0.3246 0.2573 0.1006  0.0789  0.0852  197 TYR D CE1 
13923 C CE2 . TYR D 197 ? 0.7333 0.3244 0.2429 0.1088  0.0440  0.0812  197 TYR D CE2 
13924 C CZ  . TYR D 197 ? 0.7566 0.3314 0.2583 0.1070  0.0608  0.0889  197 TYR D CZ  
13925 O OH  . TYR D 197 ? 0.8799 0.4466 0.3768 0.1117  0.0597  0.1004  197 TYR D OH  
13926 N N   . HIS D 198 ? 0.6909 0.3053 0.1893 0.0770  0.0646  0.0265  198 HIS D N   
13927 C CA  . HIS D 198 ? 0.7033 0.3236 0.2152 0.0708  0.0702  0.0159  198 HIS D CA  
13928 C C   . HIS D 198 ? 0.6832 0.3245 0.2376 0.0699  0.0639  0.0135  198 HIS D C   
13929 O O   . HIS D 198 ? 0.7005 0.3433 0.2798 0.0672  0.0758  0.0127  198 HIS D O   
13930 C CB  . HIS D 198 ? 0.6879 0.2912 0.1966 0.0678  0.0933  0.0164  198 HIS D CB  
13931 C CG  . HIS D 198 ? 0.6867 0.2909 0.1987 0.0616  0.0994  0.0049  198 HIS D CG  
13932 N ND1 . HIS D 198 ? 0.6637 0.2714 0.2057 0.0589  0.1104  0.0021  198 HIS D ND1 
13933 C CD2 . HIS D 198 ? 0.7368 0.3420 0.2341 0.0570  0.0950  -0.0040 198 HIS D CD2 
13934 C CE1 . HIS D 198 ? 0.6914 0.2957 0.2273 0.0542  0.1149  -0.0081 198 HIS D CE1 
13935 N NE2 . HIS D 198 ? 0.6951 0.2993 0.2070 0.0522  0.1051  -0.0121 198 HIS D NE2 
13936 N N   . PRO D 199 ? 0.6339 0.2928 0.1980 0.0721  0.0456  0.0122  199 PRO D N   
13937 C CA  . PRO D 199 ? 0.5901 0.2701 0.1925 0.0712  0.0400  0.0098  199 PRO D CA  
13938 C C   . PRO D 199 ? 0.6300 0.3238 0.2417 0.0655  0.0344  0.0001  199 PRO D C   
13939 O O   . PRO D 199 ? 0.7187 0.4087 0.3083 0.0625  0.0303  -0.0062 199 PRO D O   
13940 C CB  . PRO D 199 ? 0.5696 0.2604 0.1762 0.0770  0.0242  0.0135  199 PRO D CB  
13941 C CG  . PRO D 199 ? 0.6022 0.2839 0.1722 0.0797  0.0156  0.0142  199 PRO D CG  
13942 C CD  . PRO D 199 ? 0.6318 0.2935 0.1729 0.0761  0.0289  0.0129  199 PRO D CD  
13943 N N   . LEU D 200 ? 0.6106 0.3208 0.2558 0.0636  0.0342  -0.0009 200 LEU D N   
13944 C CA  . LEU D 200 ? 0.6099 0.3353 0.2691 0.0583  0.0287  -0.0081 200 LEU D CA  
13945 C C   . LEU D 200 ? 0.6095 0.3534 0.2700 0.0595  0.0098  -0.0113 200 LEU D C   
13946 O O   . LEU D 200 ? 0.6106 0.3731 0.2947 0.0611  0.0027  -0.0101 200 LEU D O   
13947 C CB  . LEU D 200 ? 0.4907 0.2272 0.1836 0.0563  0.0357  -0.0061 200 LEU D CB  
13948 C CG  . LEU D 200 ? 0.5049 0.2272 0.2021 0.0539  0.0535  -0.0051 200 LEU D CG  
13949 C CD1 . LEU D 200 ? 0.4628 0.2008 0.1922 0.0510  0.0555  -0.0047 200 LEU D CD1 
13950 C CD2 . LEU D 200 ? 0.5184 0.2230 0.1886 0.0507  0.0591  -0.0111 200 LEU D CD2 
13951 N N   . ILE D 201 ? 0.5248 0.2645 0.1597 0.0585  0.0018  -0.0162 201 ILE D N   
13952 C CA  . ILE D 201 ? 0.5210 0.2774 0.1550 0.0607  -0.0165 -0.0189 201 ILE D CA  
13953 C C   . ILE D 201 ? 0.5483 0.3295 0.2107 0.0568  -0.0242 -0.0236 201 ILE D C   
13954 O O   . ILE D 201 ? 0.5916 0.3901 0.2690 0.0606  -0.0344 -0.0225 201 ILE D O   
13955 C CB  . ILE D 201 ? 0.5522 0.3004 0.1532 0.0597  -0.0238 -0.0239 201 ILE D CB  
13956 C CG1 . ILE D 201 ? 0.5833 0.3090 0.1544 0.0646  -0.0172 -0.0172 201 ILE D CG1 
13957 C CG2 . ILE D 201 ? 0.5477 0.3157 0.1509 0.0618  -0.0433 -0.0272 201 ILE D CG2 
13958 C CD1 . ILE D 201 ? 0.6516 0.3784 0.2251 0.0732  -0.0230 -0.0078 201 ILE D CD1 
13959 N N   . PRO D 202 ? 0.4842 0.2683 0.1558 0.0496  -0.0194 -0.0285 202 PRO D N   
13960 C CA  . PRO D 202 ? 0.4579 0.2662 0.1556 0.0458  -0.0267 -0.0315 202 PRO D CA  
13961 C C   . PRO D 202 ? 0.4313 0.2545 0.1556 0.0490  -0.0258 -0.0260 202 PRO D C   
13962 O O   . PRO D 202 ? 0.4440 0.2899 0.1851 0.0486  -0.0355 -0.0280 202 PRO D O   
13963 C CB  . PRO D 202 ? 0.4837 0.2861 0.1860 0.0380  -0.0177 -0.0353 202 PRO D CB  
13964 C CG  . PRO D 202 ? 0.5979 0.3765 0.2710 0.0371  -0.0115 -0.0388 202 PRO D CG  
13965 C CD  . PRO D 202 ? 0.5049 0.2706 0.1638 0.0445  -0.0074 -0.0320 202 PRO D CD  
13966 N N   . ILE D 203 ? 0.4281 0.2404 0.1572 0.0517  -0.0142 -0.0200 203 ILE D N   
13967 C CA  . ILE D 203 ? 0.4047 0.2310 0.1578 0.0547  -0.0140 -0.0159 203 ILE D CA  
13968 C C   . ILE D 203 ? 0.4047 0.2375 0.1559 0.0611  -0.0243 -0.0157 203 ILE D C   
13969 O O   . ILE D 203 ? 0.3846 0.2385 0.1554 0.0623  -0.0314 -0.0172 203 ILE D O   
13970 C CB  . ILE D 203 ? 0.4047 0.2174 0.1639 0.0556  0.0008  -0.0102 203 ILE D CB  
13971 C CG1 . ILE D 203 ? 0.4014 0.2112 0.1691 0.0501  0.0105  -0.0100 203 ILE D CG1 
13972 C CG2 . ILE D 203 ? 0.3872 0.2137 0.1691 0.0589  0.0001  -0.0072 203 ILE D CG2 
13973 C CD1 . ILE D 203 ? 0.4165 0.2252 0.2033 0.0509  0.0222  -0.0044 203 ILE D CD1 
13974 N N   . LEU D 204 ? 0.4657 0.2806 0.1933 0.0655  -0.0250 -0.0137 204 LEU D N   
13975 C CA  . LEU D 204 ? 0.4324 0.2500 0.1587 0.0727  -0.0339 -0.0118 204 LEU D CA  
13976 C C   . LEU D 204 ? 0.4255 0.2640 0.1565 0.0735  -0.0498 -0.0175 204 LEU D C   
13977 O O   . LEU D 204 ? 0.4450 0.2945 0.1876 0.0790  -0.0574 -0.0175 204 LEU D O   
13978 C CB  . LEU D 204 ? 0.4637 0.2564 0.1614 0.0771  -0.0308 -0.0065 204 LEU D CB  
13979 C CG  . LEU D 204 ? 0.4701 0.2455 0.1690 0.0806  -0.0187 0.0011  204 LEU D CG  
13980 C CD1 . LEU D 204 ? 0.4524 0.2292 0.1711 0.0758  -0.0055 0.0013  204 LEU D CD1 
13981 C CD2 . LEU D 204 ? 0.5048 0.2544 0.1709 0.0827  -0.0129 0.0065  204 LEU D CD2 
13982 N N   . LEU D 205 ? 0.4381 0.2823 0.1617 0.0680  -0.0545 -0.0229 205 LEU D N   
13983 C CA  . LEU D 205 ? 0.4219 0.2881 0.1528 0.0678  -0.0691 -0.0289 205 LEU D CA  
13984 C C   . LEU D 205 ? 0.4491 0.3400 0.2089 0.0636  -0.0696 -0.0321 205 LEU D C   
13985 O O   . LEU D 205 ? 0.4699 0.3804 0.2458 0.0669  -0.0777 -0.0345 205 LEU D O   
13986 C CB  . LEU D 205 ? 0.4404 0.3029 0.1518 0.0630  -0.0744 -0.0342 205 LEU D CB  
13987 C CG  . LEU D 205 ? 0.4733 0.3146 0.1522 0.0668  -0.0762 -0.0319 205 LEU D CG  
13988 C CD1 . LEU D 205 ? 0.4908 0.3248 0.1516 0.0593  -0.0754 -0.0384 205 LEU D CD1 
13989 C CD2 . LEU D 205 ? 0.4800 0.3317 0.1580 0.0739  -0.0904 -0.0309 205 LEU D CD2 
13990 N N   . ASN D 206 ? 0.4363 0.3266 0.2028 0.0565  -0.0606 -0.0320 206 ASN D N   
13991 C CA  . ASN D 206 ? 0.3594 0.2725 0.1505 0.0517  -0.0604 -0.0335 206 ASN D CA  
13992 C C   . ASN D 206 ? 0.3750 0.2800 0.1741 0.0487  -0.0470 -0.0282 206 ASN D C   
13993 O O   . ASN D 206 ? 0.4291 0.3226 0.2224 0.0435  -0.0400 -0.0276 206 ASN D O   
13994 C CB  . ASN D 206 ? 0.4321 0.3575 0.2246 0.0447  -0.0666 -0.0391 206 ASN D CB  
13995 C CG  . ASN D 206 ? 0.5564 0.5058 0.3732 0.0395  -0.0660 -0.0393 206 ASN D CG  
13996 O OD1 . ASN D 206 ? 0.4164 0.3776 0.2487 0.0419  -0.0635 -0.0365 206 ASN D OD1 
13997 N ND2 . ASN D 206 ? 0.6389 0.5960 0.4588 0.0320  -0.0681 -0.0428 206 ASN D ND2 
13998 N N   . PRO D 207 ? 0.3517 0.2629 0.1656 0.0520  -0.0431 -0.0248 207 PRO D N   
13999 C CA  . PRO D 207 ? 0.3312 0.2360 0.1542 0.0499  -0.0311 -0.0194 207 PRO D CA  
14000 C C   . PRO D 207 ? 0.3203 0.2369 0.1559 0.0431  -0.0284 -0.0181 207 PRO D C   
14001 O O   . PRO D 207 ? 0.3411 0.2488 0.1815 0.0411  -0.0184 -0.0133 207 PRO D O   
14002 C CB  . PRO D 207 ? 0.3165 0.2325 0.1557 0.0542  -0.0310 -0.0182 207 PRO D CB  
14003 C CG  . PRO D 207 ? 0.3241 0.2389 0.1555 0.0602  -0.0396 -0.0216 207 PRO D CG  
14004 C CD  . PRO D 207 ? 0.3439 0.2672 0.1676 0.0580  -0.0494 -0.0263 207 PRO D CD  
14005 N N   . ASN D 208 ? 0.3124 0.2485 0.1545 0.0395  -0.0366 -0.0218 208 ASN D N   
14006 C CA  . ASN D 208 ? 0.3614 0.3088 0.2159 0.0326  -0.0340 -0.0194 208 ASN D CA  
14007 C C   . ASN D 208 ? 0.3399 0.2674 0.1841 0.0277  -0.0279 -0.0192 208 ASN D C   
14008 O O   . ASN D 208 ? 0.3300 0.2631 0.1851 0.0220  -0.0246 -0.0163 208 ASN D O   
14009 C CB  . ASN D 208 ? 0.3989 0.3724 0.2628 0.0297  -0.0437 -0.0237 208 ASN D CB  
14010 C CG  . ASN D 208 ? 0.3362 0.3319 0.2131 0.0338  -0.0483 -0.0249 208 ASN D CG  
14011 O OD1 . ASN D 208 ? 0.3599 0.3674 0.2502 0.0333  -0.0442 -0.0205 208 ASN D OD1 
14012 N ND2 . ASN D 208 ? 0.3457 0.3478 0.2191 0.0381  -0.0571 -0.0313 208 ASN D ND2 
14013 N N   . CYS D 209 ? 0.3518 0.2561 0.1753 0.0297  -0.0261 -0.0222 209 CYS D N   
14014 C CA  . CYS D 209 ? 0.4664 0.3513 0.2796 0.0249  -0.0195 -0.0240 209 CYS D CA  
14015 C C   . CYS D 209 ? 0.4614 0.3357 0.2850 0.0239  -0.0063 -0.0173 209 CYS D C   
14016 O O   . CYS D 209 ? 0.5172 0.3800 0.3406 0.0190  -0.0001 -0.0181 209 CYS D O   
14017 C CB  . CYS D 209 ? 0.5199 0.3833 0.3062 0.0276  -0.0201 -0.0289 209 CYS D CB  
14018 S SG  . CYS D 209 ? 0.8437 0.6912 0.6203 0.0360  -0.0133 -0.0237 209 CYS D SG  
14019 N N   . VAL D 210 ? 0.3822 0.2603 0.2164 0.0286  -0.0019 -0.0111 210 VAL D N   
14020 C CA  . VAL D 210 ? 0.3806 0.2522 0.2281 0.0284  0.0096  -0.0041 210 VAL D CA  
14021 C C   . VAL D 210 ? 0.3724 0.2589 0.2389 0.0234  0.0094  0.0005  210 VAL D C   
14022 O O   . VAL D 210 ? 0.3544 0.2320 0.2306 0.0220  0.0187  0.0059  210 VAL D O   
14023 C CB  . VAL D 210 ? 0.3296 0.2065 0.1870 0.0340  0.0125  0.0007  210 VAL D CB  
14024 C CG1 . VAL D 210 ? 0.3423 0.2035 0.1815 0.0387  0.0131  -0.0026 210 VAL D CG1 
14025 C CG2 . VAL D 210 ? 0.3215 0.2275 0.1950 0.0344  0.0037  0.0023  210 VAL D CG2 
14026 N N   . TYR D 211 ? 0.4068 0.3158 0.2794 0.0207  -0.0004 -0.0009 211 TYR D N   
14027 C CA  . TYR D 211 ? 0.3758 0.3015 0.2661 0.0158  -0.0006 0.0051  211 TYR D CA  
14028 C C   . TYR D 211 ? 0.3738 0.2897 0.2618 0.0087  0.0010  0.0024  211 TYR D C   
14029 O O   . TYR D 211 ? 0.3604 0.2862 0.2634 0.0041  0.0027  0.0087  211 TYR D O   
14030 C CB  . TYR D 211 ? 0.2909 0.2464 0.1893 0.0157  -0.0105 0.0045  211 TYR D CB  
14031 C CG  . TYR D 211 ? 0.2775 0.2446 0.1822 0.0216  -0.0115 0.0068  211 TYR D CG  
14032 C CD1 . TYR D 211 ? 0.2701 0.2415 0.1886 0.0231  -0.0055 0.0155  211 TYR D CD1 
14033 C CD2 . TYR D 211 ? 0.2736 0.2474 0.1718 0.0257  -0.0187 -0.0001 211 TYR D CD2 
14034 C CE1 . TYR D 211 ? 0.2719 0.2549 0.1974 0.0277  -0.0068 0.0162  211 TYR D CE1 
14035 C CE2 . TYR D 211 ? 0.3046 0.2881 0.2102 0.0305  -0.0191 0.0007  211 TYR D CE2 
14036 C CZ  . TYR D 211 ? 0.3076 0.2960 0.2266 0.0310  -0.0133 0.0083  211 TYR D CZ  
14037 O OH  . TYR D 211 ? 0.3244 0.3234 0.2518 0.0349  -0.0141 0.0077  211 TYR D OH  
14038 N N   . GLU D 212 ? 0.4644 0.3616 0.3343 0.0075  0.0007  -0.0065 212 GLU D N   
14039 C CA  . GLU D 212 ? 0.4108 0.2980 0.2789 0.0000  0.0023  -0.0111 212 GLU D CA  
14040 C C   . GLU D 212 ? 0.4176 0.2837 0.2923 -0.0014 0.0154  -0.0067 212 GLU D C   
14041 O O   . GLU D 212 ? 0.5185 0.3811 0.4026 -0.0079 0.0185  -0.0062 212 GLU D O   
14042 C CB  . GLU D 212 ? 0.5050 0.3812 0.3504 -0.0010 -0.0036 -0.0233 212 GLU D CB  
14043 C CG  . GLU D 212 ? 0.6954 0.5935 0.5410 -0.0038 -0.0169 -0.0290 212 GLU D CG  
14044 C CD  . GLU D 212 ? 0.8790 0.7673 0.7068 -0.0077 -0.0227 -0.0409 212 GLU D CD  
14045 O OE1 . GLU D 212 ? 0.8570 0.7355 0.6643 -0.0026 -0.0262 -0.0456 212 GLU D OE1 
14046 O OE2 . GLU D 212 ? 0.7071 0.5978 0.5416 -0.0161 -0.0238 -0.0454 212 GLU D OE2 
14047 N N   . THR D 213 ? 0.4166 0.2685 0.2882 0.0046  0.0236  -0.0037 213 THR D N   
14048 C CA  . THR D 213 ? 0.3790 0.2128 0.2606 0.0047  0.0367  0.0011  213 THR D CA  
14049 C C   . THR D 213 ? 0.4304 0.2759 0.3335 0.0092  0.0408  0.0143  213 THR D C   
14050 O O   . THR D 213 ? 0.5429 0.3837 0.4629 0.0080  0.0482  0.0218  213 THR D O   
14051 C CB  . THR D 213 ? 0.3991 0.2064 0.2622 0.0077  0.0452  -0.0059 213 THR D CB  
14052 O OG1 . THR D 213 ? 0.4215 0.2226 0.2605 0.0050  0.0384  -0.0178 213 THR D OG1 
14053 C CG2 . THR D 213 ? 0.4800 0.2659 0.3518 0.0059  0.0587  -0.0054 213 THR D CG2 
14054 N N   . THR D 214 ? 0.4120 0.2728 0.3156 0.0144  0.0359  0.0171  214 THR D N   
14055 C CA  . THR D 214 ? 0.3851 0.2613 0.3087 0.0184  0.0376  0.0285  214 THR D CA  
14056 C C   . THR D 214 ? 0.4152 0.3216 0.3440 0.0178  0.0262  0.0306  214 THR D C   
14057 O O   . THR D 214 ? 0.4810 0.3961 0.4027 0.0212  0.0205  0.0262  214 THR D O   
14058 C CB  . THR D 214 ? 0.3309 0.1976 0.2531 0.0248  0.0441  0.0289  214 THR D CB  
14059 O OG1 . THR D 214 ? 0.4831 0.3476 0.3863 0.0268  0.0389  0.0205  214 THR D OG1 
14060 C CG2 . THR D 214 ? 0.4159 0.2552 0.3372 0.0256  0.0575  0.0280  214 THR D CG2 
14061 N N   . PRO D 215 ? 0.3777 0.3005 0.3191 0.0135  0.0231  0.0372  215 PRO D N   
14062 C CA  . PRO D 215 ? 0.3708 0.3226 0.3144 0.0120  0.0127  0.0371  215 PRO D CA  
14063 C C   . PRO D 215 ? 0.4092 0.3830 0.3634 0.0166  0.0098  0.0430  215 PRO D C   
14064 O O   . PRO D 215 ? 0.4345 0.4297 0.3868 0.0166  0.0016  0.0390  215 PRO D O   
14065 C CB  . PRO D 215 ? 0.3717 0.3316 0.3252 0.0052  0.0127  0.0433  215 PRO D CB  
14066 C CG  . PRO D 215 ? 0.3033 0.2432 0.2667 0.0054  0.0233  0.0513  215 PRO D CG  
14067 C CD  . PRO D 215 ? 0.3707 0.2837 0.3220 0.0089  0.0293  0.0431  215 PRO D CD  
14068 N N   . ASN D 216 ? 0.4021 0.3726 0.3682 0.0203  0.0161  0.0516  216 ASN D N   
14069 C CA  . ASN D 216 ? 0.4942 0.4893 0.4721 0.0235  0.0123  0.0573  216 ASN D CA  
14070 C C   . ASN D 216 ? 0.4852 0.4726 0.4649 0.0293  0.0159  0.0549  216 ASN D C   
14071 O O   . ASN D 216 ? 0.5162 0.5126 0.5110 0.0323  0.0180  0.0628  216 ASN D O   
14072 C CB  . ASN D 216 ? 0.5924 0.5997 0.5873 0.0225  0.0143  0.0719  216 ASN D CB  
14073 C CG  . ASN D 216 ? 0.6586 0.6899 0.6546 0.0174  0.0077  0.0757  216 ASN D CG  
14074 O OD1 . ASN D 216 ? 0.4398 0.4970 0.4356 0.0176  0.0005  0.0737  216 ASN D OD1 
14075 N ND2 . ASN D 216 ? 0.5243 0.5469 0.5219 0.0123  0.0110  0.0805  216 ASN D ND2 
14076 N N   . VAL D 217 ? 0.3644 0.3360 0.3294 0.0309  0.0163  0.0445  217 VAL D N   
14077 C CA  . VAL D 217 ? 0.3622 0.3226 0.3275 0.0356  0.0213  0.0420  217 VAL D CA  
14078 C C   . VAL D 217 ? 0.4855 0.4614 0.4482 0.0374  0.0136  0.0350  217 VAL D C   
14079 O O   . VAL D 217 ? 0.4787 0.4614 0.4312 0.0359  0.0061  0.0283  217 VAL D O   
14080 C CB  . VAL D 217 ? 0.3426 0.2709 0.2923 0.0362  0.0293  0.0367  217 VAL D CB  
14081 C CG1 . VAL D 217 ? 0.3935 0.3160 0.3233 0.0335  0.0231  0.0280  217 VAL D CG1 
14082 C CG2 . VAL D 217 ? 0.3670 0.2840 0.3156 0.0406  0.0351  0.0342  217 VAL D CG2 
14083 N N   . LYS D 218 ? 0.4559 0.4376 0.4300 0.0407  0.0155  0.0360  218 LYS D N   
14084 C CA  . LYS D 218 ? 0.4504 0.4463 0.4258 0.0423  0.0093  0.0290  218 LYS D CA  
14085 C C   . LYS D 218 ? 0.4227 0.3958 0.3841 0.0447  0.0123  0.0217  218 LYS D C   
14086 O O   . LYS D 218 ? 0.3315 0.2849 0.2927 0.0467  0.0215  0.0233  218 LYS D O   
14087 C CB  . LYS D 218 ? 0.4778 0.4908 0.4733 0.0438  0.0099  0.0327  218 LYS D CB  
14088 C CG  . LYS D 218 ? 0.3176 0.3580 0.3199 0.0435  0.0009  0.0266  218 LYS D CG  
14089 C CD  . LYS D 218 ? 0.4256 0.4822 0.4194 0.0409  -0.0076 0.0231  218 LYS D CD  
14090 C CE  . LYS D 218 ? 0.6124 0.7014 0.6161 0.0401  -0.0154 0.0188  218 LYS D CE  
14091 N NZ  . LYS D 218 ? 0.5942 0.6992 0.5900 0.0379  -0.0226 0.0132  218 LYS D NZ  
14092 N N   . ILE D 219 ? 0.4421 0.4180 0.3920 0.0449  0.0050  0.0142  219 ILE D N   
14093 C CA  . ILE D 219 ? 0.4382 0.3951 0.3750 0.0480  0.0061  0.0083  219 ILE D CA  
14094 C C   . ILE D 219 ? 0.3622 0.3363 0.3042 0.0496  -0.0021 0.0013  219 ILE D C   
14095 O O   . ILE D 219 ? 0.4094 0.4086 0.3588 0.0478  -0.0096 -0.0009 219 ILE D O   
14096 C CB  . ILE D 219 ? 0.4540 0.3917 0.3689 0.0474  0.0055  0.0062  219 ILE D CB  
14097 C CG1 . ILE D 219 ? 0.4595 0.4147 0.3715 0.0449  -0.0047 0.0025  219 ILE D CG1 
14098 C CG2 . ILE D 219 ? 0.4806 0.3994 0.3908 0.0456  0.0150  0.0113  219 ILE D CG2 
14099 C CD1 . ILE D 219 ? 0.3593 0.3002 0.2510 0.0453  -0.0087 -0.0024 219 ILE D CD1 
14100 N N   . PRO D 220 ? 0.3373 0.2983 0.2760 0.0530  -0.0003 -0.0025 220 PRO D N   
14101 C CA  . PRO D 220 ? 0.3484 0.3241 0.2956 0.0549  -0.0069 -0.0099 220 PRO D CA  
14102 C C   . PRO D 220 ? 0.4031 0.3877 0.3416 0.0557  -0.0166 -0.0157 220 PRO D C   
14103 O O   . PRO D 220 ? 0.4433 0.4219 0.3684 0.0546  -0.0187 -0.0143 220 PRO D O   
14104 C CB  . PRO D 220 ? 0.4070 0.3600 0.3515 0.0582  -0.0007 -0.0106 220 PRO D CB  
14105 C CG  . PRO D 220 ? 0.3693 0.3011 0.3078 0.0575  0.0103  -0.0032 220 PRO D CG  
14106 C CD  . PRO D 220 ? 0.2691 0.2007 0.1973 0.0551  0.0091  0.0001  220 PRO D CD  
14107 N N   . ASP D 221 ? 0.3348 0.3347 0.2831 0.0575  -0.0223 -0.0233 221 ASP D N   
14108 C CA  . ASP D 221 ? 0.3577 0.3699 0.3027 0.0590  -0.0314 -0.0301 221 ASP D CA  
14109 C C   . ASP D 221 ? 0.4306 0.4202 0.3632 0.0643  -0.0327 -0.0319 221 ASP D C   
14110 O O   . ASP D 221 ? 0.3956 0.3772 0.3341 0.0679  -0.0311 -0.0348 221 ASP D O   
14111 C CB  . ASP D 221 ? 0.4413 0.4813 0.4035 0.0587  -0.0362 -0.0384 221 ASP D CB  
14112 C CG  . ASP D 221 ? 0.6215 0.6778 0.5829 0.0600  -0.0447 -0.0458 221 ASP D CG  
14113 O OD1 . ASP D 221 ? 0.6024 0.6666 0.5571 0.0572  -0.0476 -0.0433 221 ASP D OD1 
14114 O OD2 . ASP D 221 ? 0.6123 0.6734 0.5814 0.0637  -0.0480 -0.0545 221 ASP D OD2 
14115 N N   . PHE D 222 ? 0.4037 0.3837 0.3198 0.0647  -0.0358 -0.0299 222 PHE D N   
14116 C CA  . PHE D 222 ? 0.2963 0.2560 0.1978 0.0701  -0.0385 -0.0302 222 PHE D CA  
14117 C C   . PHE D 222 ? 0.3756 0.3512 0.2848 0.0741  -0.0482 -0.0382 222 PHE D C   
14118 O O   . PHE D 222 ? 0.3539 0.3392 0.2583 0.0743  -0.0558 -0.0409 222 PHE D O   
14119 C CB  . PHE D 222 ? 0.3703 0.3154 0.2509 0.0686  -0.0388 -0.0260 222 PHE D CB  
14120 C CG  . PHE D 222 ? 0.3639 0.2855 0.2337 0.0668  -0.0281 -0.0191 222 PHE D CG  
14121 C CD1 . PHE D 222 ? 0.3825 0.3090 0.2624 0.0623  -0.0207 -0.0156 222 PHE D CD1 
14122 C CD2 . PHE D 222 ? 0.3233 0.2185 0.1728 0.0701  -0.0252 -0.0157 222 PHE D CD2 
14123 C CE1 . PHE D 222 ? 0.3190 0.2244 0.1911 0.0611  -0.0101 -0.0099 222 PHE D CE1 
14124 C CE2 . PHE D 222 ? 0.3352 0.2095 0.1746 0.0683  -0.0141 -0.0102 222 PHE D CE2 
14125 C CZ  . PHE D 222 ? 0.3243 0.2037 0.1761 0.0640  -0.0062 -0.0078 222 PHE D CZ  
14126 N N   . ALA D 223 ? 0.4677 0.4462 0.3910 0.0773  -0.0474 -0.0427 223 ALA D N   
14127 C CA  . ALA D 223 ? 0.4121 0.4038 0.3457 0.0821  -0.0552 -0.0512 223 ALA D CA  
14128 C C   . ALA D 223 ? 0.4420 0.4116 0.3657 0.0897  -0.0582 -0.0491 223 ALA D C   
14129 O O   . ALA D 223 ? 0.4301 0.4033 0.3655 0.0951  -0.0620 -0.0551 223 ALA D O   
14130 C CB  . ALA D 223 ? 0.5385 0.5452 0.4938 0.0815  -0.0530 -0.0588 223 ALA D CB  
14131 N N   . VAL D 224 ? 0.4091 0.3559 0.3113 0.0903  -0.0564 -0.0406 224 VAL D N   
14132 C CA  . VAL D 224 ? 0.3395 0.2658 0.2279 0.0975  -0.0602 -0.0367 224 VAL D CA  
14133 C C   . VAL D 224 ? 0.3357 0.2532 0.2001 0.0959  -0.0632 -0.0316 224 VAL D C   
14134 O O   . VAL D 224 ? 0.4081 0.3247 0.2653 0.0894  -0.0580 -0.0292 224 VAL D O   
14135 C CB  . VAL D 224 ? 0.3684 0.2685 0.2549 0.1006  -0.0515 -0.0307 224 VAL D CB  
14136 C CG1 . VAL D 224 ? 0.4250 0.3043 0.2928 0.0966  -0.0419 -0.0220 224 VAL D CG1 
14137 C CG2 . VAL D 224 ? 0.4302 0.3154 0.3112 0.1096  -0.0570 -0.0279 224 VAL D CG2 
14138 N N   . SER D 225 ? 0.3513 0.2630 0.2043 0.1020  -0.0720 -0.0304 225 SER D N   
14139 C CA  . SER D 225 ? 0.3643 0.2704 0.1949 0.1005  -0.0769 -0.0276 225 SER D CA  
14140 C C   . SER D 225 ? 0.4103 0.2855 0.2156 0.1029  -0.0714 -0.0183 225 SER D C   
14141 O O   . SER D 225 ? 0.4255 0.2851 0.2281 0.1097  -0.0708 -0.0134 225 SER D O   
14142 C CB  . SER D 225 ? 0.4914 0.4125 0.3241 0.1054  -0.0910 -0.0321 225 SER D CB  
14143 O OG  . SER D 225 ? 0.6540 0.5814 0.4734 0.1006  -0.0965 -0.0335 225 SER D OG  
14144 N N   . PHE D 226 ? 0.4154 0.2813 0.2024 0.0971  -0.0667 -0.0160 226 PHE D N   
14145 C CA  . PHE D 226 ? 0.4259 0.2644 0.1848 0.0985  -0.0615 -0.0084 226 PHE D CA  
14146 C C   . PHE D 226 ? 0.4561 0.2935 0.1918 0.0990  -0.0717 -0.0091 226 PHE D C   
14147 O O   . PHE D 226 ? 0.5974 0.4140 0.3062 0.0993  -0.0680 -0.0039 226 PHE D O   
14148 C CB  . PHE D 226 ? 0.4430 0.2693 0.1974 0.0918  -0.0470 -0.0059 226 PHE D CB  
14149 C CG  . PHE D 226 ? 0.4162 0.2365 0.1873 0.0920  -0.0358 -0.0029 226 PHE D CG  
14150 C CD1 . PHE D 226 ? 0.3891 0.2296 0.1878 0.0889  -0.0345 -0.0079 226 PHE D CD1 
14151 C CD2 . PHE D 226 ? 0.4367 0.2320 0.1958 0.0949  -0.0263 0.0048  226 PHE D CD2 
14152 C CE1 . PHE D 226 ? 0.3820 0.2187 0.1969 0.0887  -0.0251 -0.0063 226 PHE D CE1 
14153 C CE2 . PHE D 226 ? 0.4292 0.2198 0.2059 0.0943  -0.0159 0.0068  226 PHE D CE2 
14154 C CZ  . PHE D 226 ? 0.4036 0.2153 0.2088 0.0912  -0.0158 0.0008  226 PHE D CZ  
14155 N N   . ARG D 227 ? 0.4333 0.2937 0.1788 0.0988  -0.0842 -0.0160 227 ARG D N   
14156 C CA  . ARG D 227 ? 0.4495 0.3121 0.1756 0.0981  -0.0946 -0.0183 227 ARG D CA  
14157 C C   . ARG D 227 ? 0.5453 0.3916 0.2487 0.1066  -0.1011 -0.0112 227 ARG D C   
14158 O O   . ARG D 227 ? 0.5077 0.3453 0.1846 0.1054  -0.1051 -0.0105 227 ARG D O   
14159 C CB  . ARG D 227 ? 0.5486 0.4411 0.2939 0.0966  -0.1067 -0.0269 227 ARG D CB  
14160 C CG  . ARG D 227 ? 0.5697 0.4757 0.3238 0.0860  -0.1029 -0.0332 227 ARG D CG  
14161 C CD  . ARG D 227 ? 0.6200 0.5507 0.3851 0.0823  -0.1140 -0.0404 227 ARG D CD  
14162 N NE  . ARG D 227 ? 0.8235 0.7663 0.5986 0.0722  -0.1098 -0.0452 227 ARG D NE  
14163 C CZ  . ARG D 227 ? 0.8722 0.8200 0.6442 0.0639  -0.1116 -0.0491 227 ARG D CZ  
14164 N NH1 . ARG D 227 ? 0.7593 0.7035 0.5192 0.0639  -0.1176 -0.0494 227 ARG D NH1 
14165 N NH2 . ARG D 227 ? 0.7301 0.6869 0.5110 0.0557  -0.1078 -0.0528 227 ARG D NH2 
14166 N N   . GLU D 228 ? 0.6408 0.4824 0.3537 0.1152  -0.1022 -0.0060 228 GLU D N   
14167 C CA  . GLU D 228 ? 0.6212 0.4449 0.3126 0.1239  -0.1073 0.0034  228 GLU D CA  
14168 C C   . GLU D 228 ? 0.5739 0.3683 0.2393 0.1223  -0.0938 0.0122  228 GLU D C   
14169 O O   . GLU D 228 ? 0.5672 0.3474 0.2022 0.1251  -0.0972 0.0183  228 GLU D O   
14170 C CB  . GLU D 228 ? 0.5747 0.4005 0.2868 0.1336  -0.1114 0.0067  228 GLU D CB  
14171 C CG  . GLU D 228 ? 0.6499 0.4956 0.3715 0.1406  -0.1290 0.0031  228 GLU D CG  
14172 C CD  . GLU D 228 ? 0.8888 0.7647 0.6421 0.1370  -0.1327 -0.0092 228 GLU D CD  
14173 O OE1 . GLU D 228 ? 0.8053 0.6867 0.5703 0.1287  -0.1224 -0.0142 228 GLU D OE1 
14174 O OE2 . GLU D 228 ? 0.7811 0.6760 0.5477 0.1425  -0.1458 -0.0134 228 GLU D OE2 
14175 N N   . ASP D 229 ? 0.5491 0.3355 0.2259 0.1178  -0.0785 0.0129  229 ASP D N   
14176 C CA  . ASP D 229 ? 0.5441 0.3038 0.1993 0.1160  -0.0641 0.0208  229 ASP D CA  
14177 C C   . ASP D 229 ? 0.5706 0.3248 0.1999 0.1091  -0.0610 0.0176  229 ASP D C   
14178 O O   . ASP D 229 ? 0.6554 0.3878 0.2571 0.1090  -0.0529 0.0241  229 ASP D O   
14179 C CB  . ASP D 229 ? 0.5844 0.3403 0.2623 0.1125  -0.0491 0.0211  229 ASP D CB  
14180 C CG  . ASP D 229 ? 0.6246 0.3710 0.3160 0.1195  -0.0466 0.0278  229 ASP D CG  
14181 O OD1 . ASP D 229 ? 0.7399 0.4855 0.4277 0.1276  -0.0575 0.0317  229 ASP D OD1 
14182 O OD2 . ASP D 229 ? 0.5666 0.3063 0.2734 0.1168  -0.0339 0.0290  229 ASP D OD2 
14183 N N   . ALA D 230 ? 0.5388 0.3122 0.1770 0.1028  -0.0666 0.0075  230 ALA D N   
14184 C CA  . ALA D 230 ? 0.5517 0.3200 0.1679 0.0958  -0.0640 0.0027  230 ALA D CA  
14185 C C   . ALA D 230 ? 0.5827 0.3462 0.1722 0.0981  -0.0728 0.0047  230 ALA D C   
14186 O O   . ALA D 230 ? 0.7273 0.4764 0.2948 0.0942  -0.0647 0.0057  230 ALA D O   
14187 C CB  . ALA D 230 ? 0.5263 0.3172 0.1616 0.0886  -0.0689 -0.0080 230 ALA D CB  
14188 N N   . SER D 231 ? 0.6062 0.3860 0.2057 0.1030  -0.0878 0.0046  231 SER D N   
14189 C CA  . SER D 231 ? 0.6795 0.4606 0.2627 0.1041  -0.0958 0.0070  231 SER D CA  
14190 C C   . SER D 231 ? 0.6562 0.4140 0.2181 0.1112  -0.0903 0.0199  231 SER D C   
14191 O O   . SER D 231 ? 0.8044 0.5555 0.3436 0.1099  -0.0902 0.0229  231 SER D O   
14192 C CB  . SER D 231 ? 0.6016 0.4084 0.2041 0.1072  -0.1128 0.0035  231 SER D CB  
14193 O OG  . SER D 231 ? 0.6401 0.4429 0.2473 0.1182  -0.1182 0.0123  231 SER D OG  
14194 N N   . LYS D 232 ? 0.6324 0.3784 0.2021 0.1183  -0.0854 0.0277  232 LYS D N   
14195 C CA  . LYS D 232 ? 0.6599 0.3815 0.2119 0.1235  -0.0766 0.0408  232 LYS D CA  
14196 C C   . LYS D 232 ? 0.7077 0.4099 0.2376 0.1168  -0.0595 0.0421  232 LYS D C   
14197 O O   . LYS D 232 ? 0.7036 0.3879 0.2148 0.1189  -0.0516 0.0518  232 LYS D O   
14198 C CB  . LYS D 232 ? 0.6490 0.3614 0.2188 0.1310  -0.0727 0.0482  232 LYS D CB  
14199 C CG  . LYS D 232 ? 0.6519 0.3814 0.2452 0.1391  -0.0882 0.0473  232 LYS D CG  
14200 C CD  . LYS D 232 ? 0.6646 0.3786 0.2706 0.1477  -0.0837 0.0577  232 LYS D CD  
14201 C CE  . LYS D 232 ? 0.8843 0.5842 0.4738 0.1525  -0.0837 0.0705  232 LYS D CE  
14202 N NZ  . LYS D 232 ? 0.8698 0.5473 0.4666 0.1562  -0.0708 0.0815  232 LYS D NZ  
14203 N N   . HIS D 233 ? 0.6751 0.3811 0.2086 0.1088  -0.0530 0.0324  233 HIS D N   
14204 C CA  . HIS D 233 ? 0.6737 0.3633 0.1885 0.1023  -0.0369 0.0317  233 HIS D CA  
14205 C C   . HIS D 233 ? 0.7043 0.3990 0.1994 0.0973  -0.0417 0.0263  233 HIS D C   
14206 O O   . HIS D 233 ? 0.7789 0.4584 0.2511 0.0958  -0.0321 0.0303  233 HIS D O   
14207 C CB  . HIS D 233 ? 0.6481 0.3390 0.1765 0.0963  -0.0273 0.0242  233 HIS D CB  
14208 C CG  . HIS D 233 ? 0.6338 0.3150 0.1803 0.0979  -0.0138 0.0304  233 HIS D CG  
14209 N ND1 . HIS D 233 ? 0.6527 0.3116 0.1870 0.0979  0.0034  0.0383  233 HIS D ND1 
14210 C CD2 . HIS D 233 ? 0.5999 0.2955 0.1835 0.0981  -0.0144 0.0284  233 HIS D CD2 
14211 C CE1 . HIS D 233 ? 0.6305 0.2904 0.1949 0.0978  0.0122  0.0408  233 HIS D CE1 
14212 N NE2 . HIS D 233 ? 0.6334 0.3156 0.2272 0.0980  0.0013  0.0346  233 HIS D NE2 
14213 N N   . VAL D 234 ? 0.6847 0.4017 0.1894 0.0944  -0.0562 0.0171  234 VAL D N   
14214 C CA  . VAL D 234 ? 0.7055 0.4298 0.1936 0.0889  -0.0616 0.0109  234 VAL D CA  
14215 C C   . VAL D 234 ? 0.7476 0.4725 0.2187 0.0948  -0.0710 0.0195  234 VAL D C   
14216 O O   . VAL D 234 ? 0.7660 0.4834 0.2117 0.0924  -0.0674 0.0210  234 VAL D O   
14217 C CB  . VAL D 234 ? 0.6836 0.4324 0.1905 0.0828  -0.0729 -0.0016 234 VAL D CB  
14218 C CG1 . VAL D 234 ? 0.7067 0.4635 0.1968 0.0766  -0.0785 -0.0087 234 VAL D CG1 
14219 C CG2 . VAL D 234 ? 0.6570 0.4045 0.1799 0.0770  -0.0632 -0.0087 234 VAL D CG2 
14220 N N   . GLU D 235 ? 0.8849 0.6195 0.3700 0.1026  -0.0832 0.0252  235 GLU D N   
14221 C CA  . GLU D 235 ? 0.8967 0.6341 0.3683 0.1087  -0.0937 0.0340  235 GLU D CA  
14222 C C   . GLU D 235 ? 0.8465 0.5594 0.2952 0.1128  -0.0821 0.0474  235 GLU D C   
14223 O O   . GLU D 235 ? 0.9426 0.6534 0.3673 0.1131  -0.0846 0.0525  235 GLU D O   
14224 C CB  . GLU D 235 ? 0.7889 0.5412 0.2842 0.1167  -0.1081 0.0371  235 GLU D CB  
14225 C CG  . GLU D 235 ? 0.8288 0.6099 0.3389 0.1134  -0.1240 0.0268  235 GLU D CG  
14226 C CD  . GLU D 235 ? 0.8915 0.6822 0.3856 0.1154  -0.1364 0.0310  235 GLU D CD  
14227 O OE1 . GLU D 235 ? 0.9964 0.7741 0.4614 0.1142  -0.1311 0.0366  235 GLU D OE1 
14228 O OE2 . GLU D 235 ? 0.8090 0.6213 0.3197 0.1180  -0.1513 0.0287  235 GLU D OE2 
14229 N N   . LEU D 236 ? 0.8284 0.5235 0.2845 0.1157  -0.0690 0.0535  236 LEU D N   
14230 C CA  . LEU D 236 ? 0.8122 0.4838 0.2493 0.1181  -0.0552 0.0660  236 LEU D CA  
14231 C C   . LEU D 236 ? 0.9419 0.6046 0.3534 0.1103  -0.0435 0.0619  236 LEU D C   
14232 O O   . LEU D 236 ? 1.1423 0.7940 0.5301 0.1113  -0.0383 0.0707  236 LEU D O   
14233 C CB  . LEU D 236 ? 0.9092 0.5654 0.3632 0.1206  -0.0420 0.0712  236 LEU D CB  
14234 C CG  . LEU D 236 ? 0.9917 0.6415 0.4583 0.1300  -0.0449 0.0839  236 LEU D CG  
14235 C CD1 . LEU D 236 ? 1.0524 0.7215 0.5452 0.1352  -0.0616 0.0792  236 LEU D CD1 
14236 C CD2 . LEU D 236 ? 1.0701 0.7001 0.5465 0.1297  -0.0263 0.0900  236 LEU D CD2 
14237 N N   . ALA D 237 ? 0.8075 0.4752 0.2242 0.1024  -0.0389 0.0486  237 ALA D N   
14238 C CA  . ALA D 237 ? 0.8279 0.4882 0.2230 0.0949  -0.0280 0.0427  237 ALA D CA  
14239 C C   . ALA D 237 ? 0.8656 0.5372 0.2382 0.0934  -0.0394 0.0411  237 ALA D C   
14240 O O   . ALA D 237 ? 0.8908 0.5527 0.2373 0.0909  -0.0310 0.0433  237 ALA D O   
14241 C CB  . ALA D 237 ? 0.8016 0.4668 0.2108 0.0872  -0.0228 0.0286  237 ALA D CB  
14242 N N   . LYS D 238 ? 0.9034 0.5970 0.2861 0.0946  -0.0585 0.0368  238 LYS D N   
14243 C CA  . LYS D 238 ? 0.9329 0.6405 0.2961 0.0927  -0.0706 0.0347  238 LYS D CA  
14244 C C   . LYS D 238 ? 1.0368 0.7355 0.3768 0.0992  -0.0715 0.0503  238 LYS D C   
14245 O O   . LYS D 238 ? 1.0932 0.7942 0.4062 0.0963  -0.0727 0.0505  238 LYS D O   
14246 C CB  . LYS D 238 ? 0.8599 0.5939 0.2431 0.0930  -0.0903 0.0280  238 LYS D CB  
14247 C CG  . LYS D 238 ? 0.9880 0.7353 0.3858 0.0837  -0.0913 0.0109  238 LYS D CG  
14248 C CD  . LYS D 238 ? 0.9319 0.7065 0.3502 0.0834  -0.1101 0.0048  238 LYS D CD  
14249 C CE  . LYS D 238 ? 1.0842 0.8728 0.4843 0.0843  -0.1240 0.0073  238 LYS D CE  
14250 N NZ  . LYS D 238 ? 1.0798 0.8966 0.4985 0.0804  -0.1400 -0.0026 238 LYS D NZ  
14251 N N   . GLU D 239 ? 0.9369 0.6261 0.2873 0.1078  -0.0710 0.0636  239 GLU D N   
14252 C CA  . GLU D 239 ? 0.9461 0.6266 0.2772 0.1143  -0.0719 0.0802  239 GLU D CA  
14253 C C   . GLU D 239 ? 0.9707 0.6278 0.2801 0.1120  -0.0516 0.0870  239 GLU D C   
14254 O O   . GLU D 239 ? 1.0141 0.6667 0.2976 0.1135  -0.0509 0.0972  239 GLU D O   
14255 C CB  . GLU D 239 ? 0.9416 0.6205 0.2942 0.1243  -0.0789 0.0918  239 GLU D CB  
14256 C CG  . GLU D 239 ? 1.0985 0.7980 0.4820 0.1266  -0.0943 0.0833  239 GLU D CG  
14257 C CD  . GLU D 239 ? 1.1046 0.8306 0.4866 0.1234  -0.1122 0.0740  239 GLU D CD  
14258 O OE1 . GLU D 239 ? 1.1610 0.8912 0.5177 0.1178  -0.1130 0.0709  239 GLU D OE1 
14259 O OE2 . GLU D 239 ? 1.0173 0.7612 0.4245 0.1260  -0.1252 0.0691  239 GLU D OE2 
14260 N N   . LYS D 240 ? 0.9499 0.5931 0.2698 0.1084  -0.0347 0.0820  240 LYS D N   
14261 C CA  . LYS D 240 ? 0.9728 0.5965 0.2735 0.1047  -0.0144 0.0856  240 LYS D CA  
14262 C C   . LYS D 240 ? 0.9969 0.6266 0.2720 0.0971  -0.0130 0.0753  240 LYS D C   
14263 O O   . LYS D 240 ? 1.0792 0.6993 0.3280 0.0956  -0.0033 0.0812  240 LYS D O   
14264 C CB  . LYS D 240 ? 0.9437 0.5535 0.2648 0.1023  0.0029  0.0818  240 LYS D CB  
14265 C CG  . LYS D 240 ? 0.9654 0.5546 0.2724 0.0994  0.0254  0.0870  240 LYS D CG  
14266 C CD  . LYS D 240 ? 1.1193 0.7008 0.4028 0.1033  0.0265  0.1028  240 LYS D CD  
14267 C CE  . LYS D 240 ? 1.0180 0.5784 0.3025 0.1033  0.0480  0.1129  240 LYS D CE  
14268 N NZ  . LYS D 240 ? 1.1170 0.6715 0.4311 0.1086  0.0492  0.1206  240 LYS D NZ  
14269 N N   . TYR D 241 ? 0.9967 0.6431 0.2798 0.0918  -0.0222 0.0597  241 TYR D N   
14270 C CA  . TYR D 241 ? 1.0373 0.6926 0.2974 0.0846  -0.0236 0.0488  241 TYR D CA  
14271 C C   . TYR D 241 ? 1.1117 0.7775 0.3462 0.0875  -0.0366 0.0570  241 TYR D C   
14272 O O   . TYR D 241 ? 1.0776 0.7429 0.2831 0.0834  -0.0319 0.0553  241 TYR D O   
14273 C CB  . TYR D 241 ? 0.9754 0.6482 0.2531 0.0786  -0.0326 0.0312  241 TYR D CB  
14274 C CG  . TYR D 241 ? 0.9938 0.6708 0.2541 0.0695  -0.0278 0.0165  241 TYR D CG  
14275 C CD1 . TYR D 241 ? 1.0259 0.6891 0.2892 0.0639  -0.0095 0.0078  241 TYR D CD1 
14276 C CD2 . TYR D 241 ? 1.1148 0.8103 0.3567 0.0666  -0.0413 0.0108  241 TYR D CD2 
14277 C CE1 . TYR D 241 ? 1.1163 0.7828 0.3651 0.0559  -0.0045 -0.0065 241 TYR D CE1 
14278 C CE2 . TYR D 241 ? 1.0382 0.7381 0.2644 0.0581  -0.0367 -0.0041 241 TYR D CE2 
14279 C CZ  . TYR D 241 ? 1.0625 0.7473 0.2925 0.0530  -0.0181 -0.0130 241 TYR D CZ  
14280 O OH  . TYR D 241 ? 1.1414 0.8301 0.3571 0.0451  -0.0131 -0.0287 241 TYR D OH  
14281 N N   . PHE D 242 ? 1.1433 0.8197 0.3886 0.0947  -0.0532 0.0661  242 PHE D N   
14282 C CA  . PHE D 242 ? 1.0736 0.7601 0.2968 0.0985  -0.0663 0.0765  242 PHE D CA  
14283 C C   . PHE D 242 ? 1.2067 0.8743 0.4045 0.1014  -0.0535 0.0927  242 PHE D C   
14284 O O   . PHE D 242 ? 1.3121 0.9845 0.4789 0.0995  -0.0555 0.0960  242 PHE D O   
14285 C CB  . PHE D 242 ? 1.1570 0.8560 0.4018 0.1066  -0.0847 0.0843  242 PHE D CB  
14286 C CG  . PHE D 242 ? 1.2469 0.9653 0.4757 0.1089  -0.1034 0.0894  242 PHE D CG  
14287 C CD1 . PHE D 242 ? 1.1591 0.8711 0.3684 0.1154  -0.1056 0.1085  242 PHE D CD1 
14288 C CD2 . PHE D 242 ? 1.1829 0.9268 0.4175 0.1041  -0.1190 0.0758  242 PHE D CD2 
14289 C CE1 . PHE D 242 ? 1.1552 0.8861 0.3499 0.1176  -0.1236 0.1143  242 PHE D CE1 
14290 C CE2 . PHE D 242 ? 1.1990 0.9622 0.4200 0.1058  -0.1366 0.0804  242 PHE D CE2 
14291 C CZ  . PHE D 242 ? 1.2064 0.9634 0.4070 0.1128  -0.1394 0.0999  242 PHE D CZ  
14292 N N   . GLU D 243 ? 1.2433 0.8902 0.4539 0.1055  -0.0398 0.1025  243 GLU D N   
14293 C CA  . GLU D 243 ? 1.2454 0.8739 0.4364 0.1082  -0.0266 0.1191  243 GLU D CA  
14294 C C   . GLU D 243 ? 1.1666 0.7871 0.3300 0.1007  -0.0101 0.1135  243 GLU D C   
14295 O O   . GLU D 243 ? 1.1964 0.8047 0.3385 0.1018  0.0002  0.1267  243 GLU D O   
14296 C CB  . GLU D 243 ? 1.2324 0.8416 0.4480 0.1128  -0.0142 0.1281  243 GLU D CB  
14297 C CG  . GLU D 243 ? 1.3425 0.9560 0.5813 0.1218  -0.0284 0.1383  243 GLU D CG  
14298 C CD  . GLU D 243 ? 1.5003 1.0933 0.7550 0.1264  -0.0150 0.1518  243 GLU D CD  
14299 O OE1 . GLU D 243 ? 1.4089 0.9913 0.6815 0.1233  -0.0005 0.1452  243 GLU D OE1 
14300 O OE2 . GLU D 243 ? 1.4732 1.0610 0.7237 0.1328  -0.0189 0.1692  243 GLU D OE2 
14301 N N   . ILE D 244 ? 1.1524 0.7793 0.3168 0.0930  -0.0068 0.0944  244 ILE D N   
14302 C CA  . ILE D 244 ? 1.2497 0.8693 0.3912 0.0857  0.0097  0.0867  244 ILE D CA  
14303 C C   . ILE D 244 ? 1.1985 0.8376 0.3148 0.0803  -0.0012 0.0756  244 ILE D C   
14304 O O   . ILE D 244 ? 1.2955 0.9329 0.3805 0.0774  0.0061  0.0774  244 ILE D O   
14305 C CB  . ILE D 244 ? 1.2606 0.8693 0.4239 0.0808  0.0257  0.0735  244 ILE D CB  
14306 C CG1 . ILE D 244 ? 1.1091 0.7017 0.2995 0.0858  0.0351  0.0836  244 ILE D CG1 
14307 C CG2 . ILE D 244 ? 1.2208 0.8199 0.3628 0.0741  0.0449  0.0666  244 ILE D CG2 
14308 C CD1 . ILE D 244 ? 1.2058 0.7829 0.3845 0.0904  0.0451  0.1029  244 ILE D CD1 
14309 N N   . PHE D 245 ? 1.2158 0.8749 0.3457 0.0786  -0.0185 0.0635  245 PHE D N   
14310 C CA  . PHE D 245 ? 1.2487 0.9280 0.3593 0.0722  -0.0285 0.0496  245 PHE D CA  
14311 C C   . PHE D 245 ? 1.2169 0.9194 0.3240 0.0755  -0.0530 0.0544  245 PHE D C   
14312 O O   . PHE D 245 ? 1.2309 0.9542 0.3283 0.0699  -0.0641 0.0412  245 PHE D O   
14313 C CB  . PHE D 245 ? 1.1675 0.8520 0.2975 0.0647  -0.0256 0.0277  245 PHE D CB  
14314 C CG  . PHE D 245 ? 1.2419 0.9050 0.3774 0.0611  -0.0020 0.0222  245 PHE D CG  
14315 C CD1 . PHE D 245 ? 1.2546 0.9050 0.3634 0.0590  0.0148  0.0248  245 PHE D CD1 
14316 C CD2 . PHE D 245 ? 1.1725 0.8291 0.3405 0.0600  0.0034  0.0150  245 PHE D CD2 
14317 C CE1 . PHE D 245 ? 1.2361 0.8678 0.3526 0.0559  0.0368  0.0198  245 PHE D CE1 
14318 C CE2 . PHE D 245 ? 1.1046 0.7427 0.2795 0.0569  0.0247  0.0107  245 PHE D CE2 
14319 C CZ  . PHE D 245 ? 1.1396 0.7651 0.2897 0.0549  0.0415  0.0129  245 PHE D CZ  
14320 N N   . GLY D 246 ? 1.2059 0.9058 0.3220 0.0845  -0.0614 0.0724  246 GLY D N   
14321 C CA  . GLY D 246 ? 1.2769 0.9980 0.3898 0.0886  -0.0842 0.0792  246 GLY D CA  
14322 C C   . GLY D 246 ? 1.2943 1.0390 0.4288 0.0850  -0.1009 0.0633  246 GLY D C   
14323 O O   . GLY D 246 ? 1.3230 1.0901 0.4482 0.0845  -0.1188 0.0626  246 GLY D O   
14324 N N   . GLU D 247 ? 1.2224 0.9636 0.3861 0.0821  -0.0954 0.0507  247 GLU D N   
14325 C CA  . GLU D 247 ? 1.2612 1.0244 0.4468 0.0773  -0.1089 0.0346  247 GLU D CA  
14326 C C   . GLU D 247 ? 1.2150 0.9690 0.4354 0.0773  -0.1013 0.0283  247 GLU D C   
14327 O O   . GLU D 247 ? 1.1187 0.8502 0.3420 0.0784  -0.0838 0.0319  247 GLU D O   
14328 C CB  . GLU D 247 ? 1.2593 1.0355 0.4263 0.0666  -0.1085 0.0161  247 GLU D CB  
14329 C CG  . GLU D 247 ? 1.2769 1.0793 0.4625 0.0607  -0.1246 0.0003  247 GLU D CG  
14330 C CD  . GLU D 247 ? 1.2950 1.1010 0.4778 0.0496  -0.1166 -0.0219 247 GLU D CD  
14331 O OE1 . GLU D 247 ? 1.1526 0.9501 0.3074 0.0459  -0.1049 -0.0259 247 GLU D OE1 
14332 O OE2 . GLU D 247 ? 1.2275 1.0446 0.4370 0.0446  -0.1215 -0.0354 247 GLU D OE2 
14333 N N   . HIS D 248 ? 1.1997 0.9726 0.4469 0.0758  -0.1148 0.0192  248 HIS D N   
14334 C CA  . HIS D 248 ? 1.1062 0.8757 0.3868 0.0747  -0.1100 0.0120  248 HIS D CA  
14335 C C   . HIS D 248 ? 1.1147 0.8845 0.3971 0.0640  -0.1007 -0.0069 248 HIS D C   
14336 O O   . HIS D 248 ? 1.0627 0.8487 0.3345 0.0569  -0.1075 -0.0191 248 HIS D O   
14337 C CB  . HIS D 248 ? 1.0351 0.8259 0.3443 0.0777  -0.1281 0.0109  248 HIS D CB  
14338 C CG  . HIS D 248 ? 1.1413 0.9275 0.4606 0.0892  -0.1341 0.0281  248 HIS D CG  
14339 N ND1 . HIS D 248 ? 1.1562 0.9215 0.4587 0.0961  -0.1249 0.0441  248 HIS D ND1 
14340 C CD2 . HIS D 248 ? 1.1473 0.9473 0.4933 0.0951  -0.1475 0.0313  248 HIS D CD2 
14341 C CE1 . HIS D 248 ? 1.1673 0.9328 0.4856 0.1058  -0.1328 0.0564  248 HIS D CE1 
14342 N NE2 . HIS D 248 ? 1.2690 1.0555 0.6137 0.1057  -0.1466 0.0486  248 HIS D NE2 
14343 N N   . PRO D 249 ? 1.1199 0.8724 0.4163 0.0627  -0.0851 -0.0097 249 PRO D N   
14344 C CA  . PRO D 249 ? 1.0271 0.7782 0.3272 0.0532  -0.0755 -0.0268 249 PRO D CA  
14345 C C   . PRO D 249 ? 1.1122 0.8840 0.4391 0.0480  -0.0873 -0.0396 249 PRO D C   
14346 O O   . PRO D 249 ? 0.9647 0.7487 0.3137 0.0522  -0.0993 -0.0350 249 PRO D O   
14347 C CB  . PRO D 249 ? 0.9653 0.6918 0.2748 0.0549  -0.0564 -0.0225 249 PRO D CB  
14348 C CG  . PRO D 249 ? 1.0134 0.7369 0.3396 0.0641  -0.0611 -0.0079 249 PRO D CG  
14349 C CD  . PRO D 249 ? 1.0120 0.7469 0.3242 0.0699  -0.0764 0.0022  249 PRO D CD  
14350 N N   . VAL D 250 ? 1.0858 0.8616 0.4114 0.0386  -0.0830 -0.0565 250 VAL D N   
14351 C CA  . VAL D 250 ? 1.0546 0.8493 0.4044 0.0320  -0.0923 -0.0702 250 VAL D CA  
14352 C C   . VAL D 250 ? 1.0534 0.8349 0.4172 0.0261  -0.0775 -0.0807 250 VAL D C   
14353 O O   . VAL D 250 ? 0.9979 0.7903 0.3848 0.0205  -0.0817 -0.0911 250 VAL D O   
14354 C CB  . VAL D 250 ? 1.0574 0.8738 0.3935 0.0253  -0.1048 -0.0821 250 VAL D CB  
14355 C CG1 . VAL D 250 ? 1.0357 0.8721 0.3730 0.0303  -0.1239 -0.0728 250 VAL D CG1 
14356 C CG2 . VAL D 250 ? 0.9720 0.7789 0.2733 0.0229  -0.0957 -0.0860 250 VAL D CG2 
14357 N N   . TYR D 251 ? 1.0804 0.8382 0.4307 0.0272  -0.0597 -0.0775 251 TYR D N   
14358 C CA  . TYR D 251 ? 0.9730 0.7153 0.3359 0.0227  -0.0438 -0.0852 251 TYR D CA  
14359 C C   . TYR D 251 ? 0.9209 0.6434 0.2910 0.0293  -0.0313 -0.0710 251 TYR D C   
14360 O O   . TYR D 251 ? 0.9607 0.6714 0.3122 0.0348  -0.0255 -0.0596 251 TYR D O   
14361 C CB  . TYR D 251 ? 0.9364 0.6694 0.2782 0.0165  -0.0321 -0.0975 251 TYR D CB  
14362 C CG  . TYR D 251 ? 1.2031 0.9558 0.5291 0.0113  -0.0445 -0.1099 251 TYR D CG  
14363 C CD1 . TYR D 251 ? 1.1419 0.9124 0.4853 0.0045  -0.0551 -0.1244 251 TYR D CD1 
14364 C CD2 . TYR D 251 ? 1.2773 1.0314 0.5709 0.0128  -0.0455 -0.1075 251 TYR D CD2 
14365 C CE1 . TYR D 251 ? 1.1982 0.9880 0.5284 -0.0007 -0.0664 -0.1369 251 TYR D CE1 
14366 C CE2 . TYR D 251 ? 1.2653 1.0394 0.5438 0.0078  -0.0572 -0.1195 251 TYR D CE2 
14367 C CZ  . TYR D 251 ? 1.1943 0.9864 0.4918 0.0010  -0.0677 -0.1347 251 TYR D CZ  
14368 O OH  . TYR D 251 ? 1.2779 1.0913 0.5618 -0.0044 -0.0794 -0.1477 251 TYR D OH  
14369 N N   . MET D 252 ? 0.8509 0.5704 0.2479 0.0285  -0.0272 -0.0719 252 MET D N   
14370 C CA  . MET D 252 ? 0.8199 0.5243 0.2278 0.0345  -0.0168 -0.0597 252 MET D CA  
14371 C C   . MET D 252 ? 0.7909 0.4833 0.2151 0.0299  -0.0020 -0.0661 252 MET D C   
14372 O O   . MET D 252 ? 0.7942 0.4946 0.2319 0.0234  -0.0051 -0.0778 252 MET D O   
14373 C CB  . MET D 252 ? 0.8617 0.5793 0.2894 0.0405  -0.0304 -0.0511 252 MET D CB  
14374 C CG  . MET D 252 ? 0.9472 0.6519 0.3749 0.0492  -0.0246 -0.0357 252 MET D CG  
14375 S SD  . MET D 252 ? 0.9864 0.7077 0.4262 0.0577  -0.0435 -0.0256 252 MET D SD  
14376 C CE  . MET D 252 ? 0.8386 0.5560 0.2461 0.0624  -0.0479 -0.0167 252 MET D CE  
14377 N N   . TRP D 253 ? 0.7878 0.4609 0.2116 0.0330  0.0147  -0.0583 253 TRP D N   
14378 C CA  . TRP D 253 ? 0.8000 0.4621 0.2419 0.0298  0.0293  -0.0623 253 TRP D CA  
14379 C C   . TRP D 253 ? 0.7971 0.4610 0.2618 0.0347  0.0285  -0.0531 253 TRP D C   
14380 O O   . TRP D 253 ? 0.7976 0.4552 0.2590 0.0413  0.0313  -0.0412 253 TRP D O   
14381 C CB  . TRP D 253 ? 0.7913 0.4329 0.2211 0.0293  0.0500  -0.0613 253 TRP D CB  
14382 C CG  . TRP D 253 ? 0.7855 0.4161 0.2375 0.0278  0.0660  -0.0622 253 TRP D CG  
14383 C CD1 . TRP D 253 ? 0.7934 0.4127 0.2552 0.0323  0.0793  -0.0521 253 TRP D CD1 
14384 C CD2 . TRP D 253 ? 0.7621 0.3927 0.2309 0.0216  0.0704  -0.0736 253 TRP D CD2 
14385 N NE1 . TRP D 253 ? 0.7432 0.3573 0.2276 0.0296  0.0913  -0.0562 253 TRP D NE1 
14386 C CE2 . TRP D 253 ? 0.7447 0.3645 0.2335 0.0232  0.0863  -0.0689 253 TRP D CE2 
14387 C CE3 . TRP D 253 ? 0.7677 0.4064 0.2380 0.0147  0.0629  -0.0874 253 TRP D CE3 
14388 C CZ2 . TRP D 253 ? 0.7332 0.3497 0.2434 0.0188  0.0945  -0.0764 253 TRP D CZ2 
14389 C CZ3 . TRP D 253 ? 0.7642 0.3975 0.2549 0.0098  0.0716  -0.0953 253 TRP D CZ3 
14390 C CH2 . TRP D 253 ? 0.7402 0.3623 0.2506 0.0122  0.0872  -0.0892 253 TRP D CH2 
14391 N N   . PRO D 254 ? 0.7098 0.3821 0.1973 0.0315  0.0250  -0.0584 254 PRO D N   
14392 C CA  . PRO D 254 ? 0.6982 0.3744 0.2069 0.0360  0.0241  -0.0507 254 PRO D CA  
14393 C C   . PRO D 254 ? 0.7120 0.3709 0.2277 0.0379  0.0440  -0.0455 254 PRO D C   
14394 O O   . PRO D 254 ? 0.7823 0.4307 0.3012 0.0333  0.0576  -0.0517 254 PRO D O   
14395 C CB  . PRO D 254 ? 0.6576 0.3477 0.1859 0.0307  0.0156  -0.0594 254 PRO D CB  
14396 C CG  . PRO D 254 ? 0.6768 0.3602 0.1984 0.0229  0.0219  -0.0714 254 PRO D CG  
14397 C CD  . PRO D 254 ? 0.7097 0.3882 0.2045 0.0234  0.0221  -0.0722 254 PRO D CD  
14398 N N   . PRO D 255 ? 0.6622 0.3184 0.1825 0.0445  0.0467  -0.0345 255 PRO D N   
14399 C CA  . PRO D 255 ? 0.6576 0.2994 0.1868 0.0463  0.0662  -0.0294 255 PRO D CA  
14400 C C   . PRO D 255 ? 0.6361 0.2816 0.1934 0.0424  0.0734  -0.0344 255 PRO D C   
14401 O O   . PRO D 255 ? 0.6923 0.3563 0.2740 0.0411  0.0623  -0.0349 255 PRO D O   
14402 C CB  . PRO D 255 ? 0.6473 0.2934 0.1849 0.0532  0.0624  -0.0179 255 PRO D CB  
14403 C CG  . PRO D 255 ? 0.6816 0.3339 0.2001 0.0563  0.0455  -0.0157 255 PRO D CG  
14404 C CD  . PRO D 255 ? 0.6735 0.3396 0.1920 0.0508  0.0325  -0.0265 255 PRO D CD  
14405 N N   . GLU D 256 ? 0.6794 0.3098 0.2382 0.0404  0.0920  -0.0368 256 GLU D N   
14406 C CA  . GLU D 256 ? 0.6562 0.2898 0.2460 0.0369  0.1001  -0.0400 256 GLU D CA  
14407 C C   . GLU D 256 ? 0.6235 0.2657 0.2176 0.0310  0.0894  -0.0498 256 GLU D C   
14408 O O   . GLU D 256 ? 0.6004 0.2523 0.2249 0.0287  0.0895  -0.0494 256 GLU D O   
14409 C CB  . GLU D 256 ? 0.5914 0.2396 0.2185 0.0401  0.1004  -0.0299 256 GLU D CB  
14410 C CG  . GLU D 256 ? 0.5896 0.2361 0.2149 0.0457  0.1033  -0.0199 256 GLU D CG  
14411 C CD  . GLU D 256 ? 0.6225 0.2530 0.2497 0.0470  0.1242  -0.0168 256 GLU D CD  
14412 O OE1 . GLU D 256 ? 0.6493 0.2676 0.2725 0.0441  0.1366  -0.0234 256 GLU D OE1 
14413 O OE2 . GLU D 256 ? 0.7198 0.3497 0.3536 0.0507  0.1288  -0.0083 256 GLU D OE2 
14414 N N   . ALA D 257 ? 0.6473 0.2869 0.2118 0.0284  0.0799  -0.0580 257 ALA D N   
14415 C CA  . ALA D 257 ? 0.6461 0.2952 0.2128 0.0222  0.0678  -0.0681 257 ALA D CA  
14416 C C   . ALA D 257 ? 0.6759 0.3490 0.2696 0.0227  0.0528  -0.0628 257 ALA D C   
14417 O O   . ALA D 257 ? 0.6404 0.3233 0.2492 0.0171  0.0465  -0.0687 257 ALA D O   
14418 C CB  . ALA D 257 ? 0.6533 0.2918 0.2317 0.0160  0.0800  -0.0774 257 ALA D CB  
14419 N N   . SER D 258 ? 0.6389 0.3217 0.2397 0.0291  0.0478  -0.0521 258 SER D N   
14420 C CA  . SER D 258 ? 0.6181 0.3246 0.2445 0.0299  0.0347  -0.0476 258 SER D CA  
14421 C C   . SER D 258 ? 0.6119 0.3312 0.2278 0.0271  0.0169  -0.0548 258 SER D C   
14422 O O   . SER D 258 ? 0.5869 0.3033 0.1760 0.0298  0.0087  -0.0562 258 SER D O   
14423 C CB  . SER D 258 ? 0.6100 0.3223 0.2431 0.0373  0.0331  -0.0367 258 SER D CB  
14424 O OG  . SER D 258 ? 0.7279 0.4322 0.3313 0.0417  0.0279  -0.0354 258 SER D OG  
14425 N N   . VAL D 259 ? 0.6050 0.3389 0.2425 0.0216  0.0111  -0.0588 259 VAL D N   
14426 C CA  . VAL D 259 ? 0.6215 0.3699 0.2541 0.0178  -0.0052 -0.0664 259 VAL D CA  
14427 C C   . VAL D 259 ? 0.6086 0.3812 0.2737 0.0159  -0.0126 -0.0633 259 VAL D C   
14428 O O   . VAL D 259 ? 0.5574 0.3327 0.2468 0.0148  -0.0040 -0.0579 259 VAL D O   
14429 C CB  . VAL D 259 ? 0.5865 0.3239 0.2047 0.0096  -0.0034 -0.0796 259 VAL D CB  
14430 C CG1 . VAL D 259 ? 0.5642 0.3049 0.2105 0.0022  0.0026  -0.0823 259 VAL D CG1 
14431 C CG2 . VAL D 259 ? 0.6090 0.3572 0.2093 0.0076  -0.0208 -0.0878 259 VAL D CG2 
14432 N N   . SER D 260 ? 0.5232 0.3143 0.1881 0.0160  -0.0288 -0.0663 260 SER D N   
14433 C CA  . SER D 260 ? 0.4935 0.3094 0.1861 0.0131  -0.0368 -0.0655 260 SER D CA  
14434 C C   . SER D 260 ? 0.4973 0.3275 0.1819 0.0108  -0.0532 -0.0738 260 SER D C   
14435 O O   . SER D 260 ? 0.6205 0.4431 0.2788 0.0135  -0.0596 -0.0778 260 SER D O   
14436 C CB  . SER D 260 ? 0.5185 0.3483 0.2292 0.0200  -0.0377 -0.0555 260 SER D CB  
14437 O OG  . SER D 260 ? 0.4787 0.3086 0.1742 0.0279  -0.0454 -0.0532 260 SER D OG  
14438 N N   . ASN D 261 ? 0.5157 0.3677 0.2234 0.0056  -0.0600 -0.0761 261 ASN D N   
14439 C CA  . ASN D 261 ? 0.4983 0.3676 0.2033 0.0034  -0.0760 -0.0842 261 ASN D CA  
14440 C C   . ASN D 261 ? 0.5544 0.4320 0.2494 0.0135  -0.0874 -0.0805 261 ASN D C   
14441 O O   . ASN D 261 ? 0.5930 0.4760 0.2777 0.0141  -0.0958 -0.0840 261 ASN D O   
14442 C CB  . ASN D 261 ? 0.4633 0.3563 0.1979 -0.0034 -0.0798 -0.0858 261 ASN D CB  
14443 C CG  . ASN D 261 ? 0.4783 0.3626 0.2225 -0.0141 -0.0704 -0.0900 261 ASN D CG  
14444 O OD1 . ASN D 261 ? 0.6097 0.4716 0.3373 -0.0172 -0.0633 -0.0951 261 ASN D OD1 
14445 N ND2 . ASN D 261 ? 0.5343 0.4361 0.3055 -0.0198 -0.0698 -0.0879 261 ASN D ND2 
14446 N N   . GLU D 262 ? 0.5502 0.4335 0.2581 0.0206  -0.0845 -0.0712 262 GLU D N   
14447 C CA  . GLU D 262 ? 0.4841 0.3743 0.1879 0.0303  -0.0932 -0.0667 262 GLU D CA  
14448 C C   . GLU D 262 ? 0.5010 0.3709 0.1797 0.0348  -0.0895 -0.0630 262 GLU D C   
14449 O O   . GLU D 262 ? 0.5528 0.4301 0.2278 0.0389  -0.0977 -0.0612 262 GLU D O   
14450 C CB  . GLU D 262 ? 0.5364 0.4345 0.2592 0.0360  -0.0893 -0.0591 262 GLU D CB  
14451 C CG  . GLU D 262 ? 0.7028 0.6254 0.4555 0.0307  -0.0900 -0.0605 262 GLU D CG  
14452 C CD  . GLU D 262 ? 0.7846 0.7006 0.5492 0.0251  -0.0758 -0.0565 262 GLU D CD  
14453 O OE1 . GLU D 262 ? 0.7638 0.6657 0.5260 0.0291  -0.0658 -0.0499 262 GLU D OE1 
14454 O OE2 . GLU D 262 ? 0.7435 0.6688 0.5212 0.0167  -0.0746 -0.0594 262 GLU D OE2 
14455 N N   . ALA D 263 ? 0.5188 0.3627 0.1800 0.0342  -0.0766 -0.0615 263 ALA D N   
14456 C CA  . ALA D 263 ? 0.5263 0.3511 0.1633 0.0380  -0.0714 -0.0577 263 ALA D CA  
14457 C C   . ALA D 263 ? 0.5501 0.3772 0.1734 0.0330  -0.0770 -0.0648 263 ALA D C   
14458 O O   . ALA D 263 ? 0.6050 0.4307 0.2138 0.0374  -0.0814 -0.0612 263 ALA D O   
14459 C CB  . ALA D 263 ? 0.5339 0.3320 0.1583 0.0378  -0.0542 -0.0552 263 ALA D CB  
14460 N N   . LEU D 264 ? 0.5852 0.4156 0.2122 0.0237  -0.0771 -0.0750 264 LEU D N   
14461 C CA  . LEU D 264 ? 0.5760 0.4099 0.1906 0.0180  -0.0823 -0.0837 264 LEU D CA  
14462 C C   . LEU D 264 ? 0.5768 0.4344 0.1968 0.0207  -0.0979 -0.0827 264 LEU D C   
14463 O O   . LEU D 264 ? 0.6011 0.4584 0.2033 0.0215  -0.1023 -0.0835 264 LEU D O   
14464 C CB  . LEU D 264 ? 0.5833 0.4183 0.2060 0.0071  -0.0809 -0.0957 264 LEU D CB  
14465 C CG  . LEU D 264 ? 0.6137 0.4213 0.2257 0.0026  -0.0647 -0.0997 264 LEU D CG  
14466 C CD1 . LEU D 264 ? 0.5853 0.3926 0.2096 -0.0081 -0.0638 -0.1104 264 LEU D CD1 
14467 C CD2 . LEU D 264 ? 0.6191 0.4125 0.2060 0.0024  -0.0589 -0.1030 264 LEU D CD2 
14468 N N   . GLU D 265 ? 0.5519 0.4305 0.1963 0.0222  -0.1062 -0.0808 265 GLU D N   
14469 C CA  . GLU D 265 ? 0.5521 0.4526 0.2044 0.0254  -0.1199 -0.0792 265 GLU D CA  
14470 C C   . GLU D 265 ? 0.5629 0.4550 0.2021 0.0363  -0.1214 -0.0685 265 GLU D C   
14471 O O   . GLU D 265 ? 0.6679 0.5675 0.2984 0.0387  -0.1308 -0.0672 265 GLU D O   
14472 C CB  . GLU D 265 ? 0.5737 0.4975 0.2566 0.0247  -0.1260 -0.0796 265 GLU D CB  
14473 C CG  . GLU D 265 ? 0.6037 0.5304 0.2991 0.0151  -0.1217 -0.0876 265 GLU D CG  
14474 C CD  . GLU D 265 ? 0.6132 0.5664 0.3376 0.0126  -0.1286 -0.0892 265 GLU D CD  
14475 O OE1 . GLU D 265 ? 0.5475 0.5066 0.2867 0.0181  -0.1266 -0.0831 265 GLU D OE1 
14476 O OE2 . GLU D 265 ? 0.8557 0.8243 0.5884 0.0046  -0.1355 -0.0971 265 GLU D OE2 
14477 N N   . LEU D 266 ? 0.5545 0.4303 0.1914 0.0427  -0.1124 -0.0605 266 LEU D N   
14478 C CA  . LEU D 266 ? 0.5672 0.4315 0.1907 0.0529  -0.1127 -0.0502 266 LEU D CA  
14479 C C   . LEU D 266 ? 0.6021 0.4523 0.1954 0.0524  -0.1112 -0.0494 266 LEU D C   
14480 O O   . LEU D 266 ? 0.6533 0.5057 0.2362 0.0583  -0.1191 -0.0438 266 LEU D O   
14481 C CB  . LEU D 266 ? 0.5647 0.4118 0.1894 0.0581  -0.1014 -0.0432 266 LEU D CB  
14482 C CG  . LEU D 266 ? 0.5720 0.4018 0.1798 0.0678  -0.0992 -0.0324 266 LEU D CG  
14483 C CD1 . LEU D 266 ? 0.5621 0.4056 0.1856 0.0764  -0.1102 -0.0274 266 LEU D CD1 
14484 C CD2 . LEU D 266 ? 0.5701 0.3765 0.1702 0.0696  -0.0838 -0.0272 266 LEU D CD2 
14485 N N   . TYR D 267 ? 0.6142 0.4498 0.1929 0.0457  -0.1008 -0.0551 267 TYR D N   
14486 C CA  . TYR D 267 ? 0.6487 0.4734 0.1988 0.0441  -0.0987 -0.0563 267 TYR D CA  
14487 C C   . TYR D 267 ? 0.6987 0.5445 0.2469 0.0406  -0.1132 -0.0624 267 TYR D C   
14488 O O   . TYR D 267 ? 0.6896 0.5346 0.2179 0.0441  -0.1185 -0.0582 267 TYR D O   
14489 C CB  . TYR D 267 ? 0.6576 0.4652 0.1968 0.0367  -0.0846 -0.0638 267 TYR D CB  
14490 C CG  . TYR D 267 ? 0.6536 0.4370 0.1878 0.0404  -0.0684 -0.0567 267 TYR D CG  
14491 C CD1 . TYR D 267 ? 0.7449 0.5090 0.2550 0.0446  -0.0597 -0.0497 267 TYR D CD1 
14492 C CD2 . TYR D 267 ? 0.6266 0.4074 0.1802 0.0392  -0.0615 -0.0569 267 TYR D CD2 
14493 C CE1 . TYR D 267 ? 0.6749 0.4180 0.1824 0.0473  -0.0439 -0.0434 267 TYR D CE1 
14494 C CE2 . TYR D 267 ? 0.6235 0.3839 0.1738 0.0422  -0.0466 -0.0507 267 TYR D CE2 
14495 C CZ  . TYR D 267 ? 0.6472 0.3888 0.1752 0.0461  -0.0375 -0.0442 267 TYR D CZ  
14496 O OH  . TYR D 267 ? 0.6442 0.3667 0.1710 0.0487  -0.0216 -0.0381 267 TYR D OH  
14497 N N   . TYR D 268 ? 0.6789 0.5441 0.2475 0.0335  -0.1198 -0.0720 268 TYR D N   
14498 C CA  . TYR D 268 ? 0.6589 0.5463 0.2289 0.0293  -0.1338 -0.0782 268 TYR D CA  
14499 C C   . TYR D 268 ? 0.7293 0.6289 0.3040 0.0384  -0.1461 -0.0684 268 TYR D C   
14500 O O   . TYR D 268 ? 0.8202 0.7293 0.3825 0.0388  -0.1562 -0.0683 268 TYR D O   
14501 C CB  . TYR D 268 ? 0.6623 0.5673 0.2565 0.0199  -0.1373 -0.0893 268 TYR D CB  
14502 C CG  . TYR D 268 ? 0.7110 0.6410 0.3119 0.0152  -0.1522 -0.0952 268 TYR D CG  
14503 C CD1 . TYR D 268 ? 0.7529 0.6861 0.3367 0.0073  -0.1555 -0.1053 268 TYR D CD1 
14504 C CD2 . TYR D 268 ? 0.6675 0.6182 0.2923 0.0183  -0.1625 -0.0914 268 TYR D CD2 
14505 C CE1 . TYR D 268 ? 0.7283 0.6844 0.3180 0.0022  -0.1694 -0.1107 268 TYR D CE1 
14506 C CE2 . TYR D 268 ? 0.6384 0.6111 0.2699 0.0138  -0.1758 -0.0963 268 TYR D CE2 
14507 C CZ  . TYR D 268 ? 0.6667 0.6419 0.2804 0.0055  -0.1796 -0.1056 268 TYR D CZ  
14508 O OH  . TYR D 268 ? 0.7732 0.7700 0.3935 0.0004  -0.1934 -0.1103 268 TYR D OH  
14509 N N   . GLU D 269 ? 0.6464 0.5462 0.2392 0.0460  -0.1454 -0.0604 269 GLU D N   
14510 C CA  . GLU D 269 ? 0.6378 0.5458 0.2357 0.0560  -0.1558 -0.0512 269 GLU D CA  
14511 C C   . GLU D 269 ? 0.6685 0.5584 0.2374 0.0635  -0.1545 -0.0412 269 GLU D C   
14512 O O   . GLU D 269 ? 0.8062 0.7041 0.3691 0.0691  -0.1657 -0.0356 269 GLU D O   
14513 C CB  . GLU D 269 ? 0.6933 0.6037 0.3163 0.0624  -0.1538 -0.0464 269 GLU D CB  
14514 C CG  . GLU D 269 ? 0.6423 0.5739 0.2952 0.0558  -0.1561 -0.0547 269 GLU D CG  
14515 C CD  . GLU D 269 ? 0.7384 0.6676 0.4105 0.0593  -0.1489 -0.0519 269 GLU D CD  
14516 O OE1 . GLU D 269 ? 0.6978 0.6144 0.3659 0.0689  -0.1463 -0.0433 269 GLU D OE1 
14517 O OE2 . GLU D 269 ? 0.7603 0.7004 0.4510 0.0523  -0.1460 -0.0582 269 GLU D OE2 
14518 N N   . LYS D 270 ? 0.6766 0.5419 0.2271 0.0637  -0.1406 -0.0382 270 LYS D N   
14519 C CA  . LYS D 270 ? 0.7238 0.5700 0.2458 0.0700  -0.1369 -0.0282 270 LYS D CA  
14520 C C   . LYS D 270 ? 0.8190 0.6635 0.3132 0.0637  -0.1368 -0.0333 270 LYS D C   
14521 O O   . LYS D 270 ? 0.8051 0.6304 0.2731 0.0660  -0.1284 -0.0271 270 LYS D O   
14522 C CB  . LYS D 270 ? 0.7002 0.5208 0.2170 0.0734  -0.1208 -0.0218 270 LYS D CB  
14523 C CG  . LYS D 270 ? 0.6701 0.4916 0.2118 0.0800  -0.1205 -0.0168 270 LYS D CG  
14524 C CD  . LYS D 270 ? 0.6746 0.5051 0.2231 0.0898  -0.1331 -0.0084 270 LYS D CD  
14525 C CE  . LYS D 270 ? 0.6411 0.4827 0.2211 0.0941  -0.1363 -0.0090 270 LYS D CE  
14526 N NZ  . LYS D 270 ? 0.8524 0.7110 0.4459 0.1015  -0.1511 -0.0056 270 LYS D NZ  
14527 N N   . GLY D 271 ? 0.8111 0.6755 0.3103 0.0554  -0.1453 -0.0448 271 GLY D N   
14528 C CA  . GLY D 271 ? 0.7770 0.6438 0.2505 0.0493  -0.1476 -0.0510 271 GLY D CA  
14529 C C   . GLY D 271 ? 0.7994 0.6471 0.2534 0.0432  -0.1321 -0.0577 271 GLY D C   
14530 O O   . GLY D 271 ? 0.9183 0.7570 0.3431 0.0435  -0.1289 -0.0557 271 GLY D O   
14531 N N   . ILE D 272 ? 0.8131 0.6546 0.2828 0.0378  -0.1220 -0.0654 272 ILE D N   
14532 C CA  . ILE D 272 ? 0.8211 0.6457 0.2767 0.0314  -0.1073 -0.0740 272 ILE D CA  
14533 C C   . ILE D 272 ? 0.9094 0.7487 0.3724 0.0203  -0.1115 -0.0913 272 ILE D C   
14534 O O   . ILE D 272 ? 0.9798 0.8362 0.4682 0.0168  -0.1195 -0.0962 272 ILE D O   
14535 C CB  . ILE D 272 ? 0.8287 0.6332 0.2958 0.0333  -0.0921 -0.0699 272 ILE D CB  
14536 C CG1 . ILE D 272 ? 0.7756 0.5650 0.2349 0.0437  -0.0874 -0.0537 272 ILE D CG1 
14537 C CG2 . ILE D 272 ? 0.8226 0.6098 0.2783 0.0265  -0.0766 -0.0793 272 ILE D CG2 
14538 C CD1 . ILE D 272 ? 0.7912 0.5623 0.2186 0.0453  -0.0777 -0.0492 272 ILE D CD1 
14539 N N   . ASN D 273 ? 0.8162 0.6496 0.2572 0.0144  -0.1060 -0.1012 273 ASN D N   
14540 C CA  . ASN D 273 ? 0.9268 0.7722 0.3729 0.0036  -0.1091 -0.1195 273 ASN D CA  
14541 C C   . ASN D 273 ? 0.9088 0.7364 0.3618 -0.0020 -0.0936 -0.1294 273 ASN D C   
14542 O O   . ASN D 273 ? 0.9250 0.7607 0.3970 -0.0096 -0.0957 -0.1415 273 ASN D O   
14543 C CB  . ASN D 273 ? 0.9521 0.8059 0.3705 0.0002  -0.1147 -0.1269 273 ASN D CB  
14544 C CG  . ASN D 273 ? 1.0235 0.9018 0.4410 0.0019  -0.1336 -0.1219 273 ASN D CG  
14545 O OD1 . ASN D 273 ? 1.0355 0.9122 0.4356 0.0096  -0.1379 -0.1087 273 ASN D OD1 
14546 N ND2 . ASN D 273 ? 1.2098 1.1102 0.6468 -0.0055 -0.1448 -0.1320 273 ASN D ND2 
14547 N N   . MET D 274 ? 0.8309 0.6547 0.2796 0.1060  0.1208  -0.0965 274 MET D N   
14548 C CA  . MET D 274 ? 0.8601 0.6492 0.3136 0.0984  0.1268  -0.1081 274 MET D CA  
14549 C C   . MET D 274 ? 0.8608 0.6274 0.3351 0.1068  0.1407  -0.0919 274 MET D C   
14550 O O   . MET D 274 ? 1.0232 0.7996 0.5037 0.1196  0.1485  -0.0748 274 MET D O   
14551 C CB  . MET D 274 ? 0.9782 0.7674 0.4148 0.0989  0.1284  -0.1236 274 MET D CB  
14552 C CG  . MET D 274 ? 1.0030 0.7567 0.4455 0.0920  0.1348  -0.1358 274 MET D CG  
14553 S SD  . MET D 274 ? 1.0919 0.8230 0.5490 0.1060  0.1524  -0.1223 274 MET D SD  
14554 C CE  . MET D 274 ? 0.9074 0.6675 0.3504 0.1221  0.1572  -0.1108 274 MET D CE  
14555 N N   . LEU D 275 ? 0.8108 0.5479 0.2979 0.0988  0.1436  -0.0976 275 LEU D N   
14556 C CA  . LEU D 275 ? 0.7983 0.5153 0.3056 0.1059  0.1565  -0.0877 275 LEU D CA  
14557 C C   . LEU D 275 ? 0.8074 0.4958 0.3200 0.0979  0.1575  -0.1011 275 LEU D C   
14558 O O   . LEU D 275 ? 0.8402 0.5212 0.3435 0.0854  0.1491  -0.1162 275 LEU D O   
14559 C CB  . LEU D 275 ? 0.7658 0.4847 0.2972 0.1076  0.1589  -0.0712 275 LEU D CB  
14560 C CG  . LEU D 275 ? 0.7421 0.4646 0.2926 0.0940  0.1463  -0.0706 275 LEU D CG  
14561 C CD1 . LEU D 275 ? 0.8158 0.5273 0.3966 0.0949  0.1519  -0.0599 275 LEU D CD1 
14562 C CD2 . LEU D 275 ? 0.7470 0.4977 0.2922 0.0939  0.1379  -0.0637 275 LEU D CD2 
14563 N N   . ALA D 276 ? 0.8014 0.4751 0.3313 0.1049  0.1681  -0.0950 276 ALA D N   
14564 C CA  . ALA D 276 ? 0.8864 0.5348 0.4248 0.1008  0.1702  -0.1043 276 ALA D CA  
14565 C C   . ALA D 276 ? 0.8360 0.4732 0.4024 0.1021  0.1737  -0.0945 276 ALA D C   
14566 O O   . ALA D 276 ? 0.8119 0.4607 0.3928 0.1075  0.1775  -0.0811 276 ALA D O   
14567 C CB  . ALA D 276 ? 0.8970 0.5413 0.4306 0.1088  0.1787  -0.1082 276 ALA D CB  
14568 N N   . THR D 277 ? 0.8061 0.4221 0.3813 0.0971  0.1722  -0.1012 277 THR D N   
14569 C CA  . THR D 277 ? 0.7665 0.3746 0.3688 0.0992  0.1739  -0.0928 277 THR D CA  
14570 C C   . THR D 277 ? 0.8473 0.4340 0.4553 0.0982  0.1746  -0.0998 277 THR D C   
14571 O O   . THR D 277 ? 0.9623 0.5385 0.5538 0.0947  0.1745  -0.1116 277 THR D O   
14572 C CB  . THR D 277 ? 0.7535 0.3661 0.3634 0.0911  0.1653  -0.0881 277 THR D CB  
14573 O OG1 . THR D 277 ? 0.8065 0.4149 0.4428 0.0946  0.1668  -0.0800 277 THR D OG1 
14574 C CG2 . THR D 277 ? 0.7598 0.3624 0.3574 0.0770  0.1552  -0.0990 277 THR D CG2 
14575 N N   . ASP D 278 ? 0.7655 0.3478 0.3975 0.1018  0.1754  -0.0924 278 ASP D N   
14576 C CA  . ASP D 278 ? 0.8037 0.3697 0.4441 0.1047  0.1773  -0.0954 278 ASP D CA  
14577 C C   . ASP D 278 ? 0.8726 0.4173 0.5048 0.0945  0.1710  -0.1024 278 ASP D C   
14578 O O   . ASP D 278 ? 0.8892 0.4332 0.5202 0.0862  0.1644  -0.1010 278 ASP D O   
14579 C CB  . ASP D 278 ? 0.7905 0.3655 0.4601 0.1136  0.1797  -0.0847 278 ASP D CB  
14580 C CG  . ASP D 278 ? 0.7712 0.3366 0.4491 0.1210  0.1840  -0.0866 278 ASP D CG  
14581 O OD1 . ASP D 278 ? 0.7984 0.3517 0.4603 0.1209  0.1877  -0.0954 278 ASP D OD1 
14582 O OD2 . ASP D 278 ? 0.7570 0.3284 0.4571 0.1276  0.1838  -0.0800 278 ASP D OD2 
14583 N N   . GLU D 279 ? 0.8694 0.3962 0.4969 0.0950  0.1741  -0.1098 279 GLU D N   
14584 C CA  . GLU D 279 ? 0.8401 0.3441 0.4610 0.0851  0.1707  -0.1163 279 GLU D CA  
14585 C C   . GLU D 279 ? 0.8855 0.3824 0.5246 0.0877  0.1682  -0.1058 279 GLU D C   
14586 O O   . GLU D 279 ? 0.8403 0.3192 0.4750 0.0788  0.1655  -0.1084 279 GLU D O   
14587 C CB  . GLU D 279 ? 0.8745 0.3608 0.4858 0.0857  0.1764  -0.1270 279 GLU D CB  
14588 C CG  . GLU D 279 ? 0.8760 0.3627 0.5010 0.1007  0.1836  -0.1213 279 GLU D CG  
14589 C CD  . GLU D 279 ? 1.0073 0.4689 0.6296 0.1016  0.1882  -0.1273 279 GLU D CD  
14590 O OE1 . GLU D 279 ? 1.1581 0.6012 0.7684 0.0897  0.1866  -0.1363 279 GLU D OE1 
14591 O OE2 . GLU D 279 ? 1.1218 0.5828 0.7545 0.1140  0.1940  -0.1234 279 GLU D OE2 
14592 N N   . VAL D 280 ? 0.8301 0.3421 0.4895 0.0994  0.1693  -0.0945 280 VAL D N   
14593 C CA  . VAL D 280 ? 0.7976 0.3086 0.4731 0.1024  0.1654  -0.0846 280 VAL D CA  
14594 C C   . VAL D 280 ? 0.8050 0.3202 0.4780 0.0921  0.1582  -0.0820 280 VAL D C   
14595 O O   . VAL D 280 ? 0.8550 0.3610 0.5321 0.0892  0.1542  -0.0772 280 VAL D O   
14596 C CB  . VAL D 280 ? 0.7674 0.2986 0.4666 0.1167  0.1676  -0.0756 280 VAL D CB  
14597 C CG1 . VAL D 280 ? 0.7376 0.2943 0.4461 0.1168  0.1668  -0.0715 280 VAL D CG1 
14598 C CG2 . VAL D 280 ? 0.8291 0.3573 0.5422 0.1227  0.1641  -0.0674 280 VAL D CG2 
14599 N N   . ILE D 281 ? 0.7600 0.2894 0.4253 0.0873  0.1569  -0.0847 281 ILE D N   
14600 C CA  . ILE D 281 ? 0.7480 0.2805 0.4074 0.0767  0.1504  -0.0842 281 ILE D CA  
14601 C C   . ILE D 281 ? 0.7735 0.2864 0.4143 0.0620  0.1474  -0.0947 281 ILE D C   
14602 O O   . ILE D 281 ? 0.8067 0.3127 0.4473 0.0526  0.1424  -0.0932 281 ILE D O   
14603 C CB  . ILE D 281 ? 0.7303 0.2865 0.3869 0.0773  0.1504  -0.0830 281 ILE D CB  
14604 C CG1 . ILE D 281 ? 0.7039 0.2783 0.3833 0.0893  0.1543  -0.0725 281 ILE D CG1 
14605 C CG2 . ILE D 281 ? 0.7160 0.2883 0.3713 0.0634  0.1397  -0.0810 281 ILE D CG2 
14606 C CD1 . ILE D 281 ? 0.6851 0.2856 0.3677 0.0898  0.1551  -0.0676 281 ILE D CD1 
14607 N N   . LEU D 282 ? 0.8187 0.3233 0.4447 0.0590  0.1510  -0.1062 282 LEU D N   
14608 C CA  . LEU D 282 ? 0.8273 0.3139 0.4392 0.0440  0.1493  -0.1183 282 LEU D CA  
14609 C C   . LEU D 282 ? 0.8389 0.3027 0.4600 0.0429  0.1510  -0.1135 282 LEU D C   
14610 O O   . LEU D 282 ? 0.8497 0.3013 0.4665 0.0292  0.1484  -0.1172 282 LEU D O   
14611 C CB  . LEU D 282 ? 0.8578 0.3410 0.4551 0.0432  0.1537  -0.1318 282 LEU D CB  
14612 C CG  . LEU D 282 ? 0.8860 0.3554 0.4691 0.0269  0.1527  -0.1483 282 LEU D CG  
14613 C CD1 . LEU D 282 ? 0.8795 0.3631 0.4531 0.0115  0.1444  -0.1552 282 LEU D CD1 
14614 C CD2 . LEU D 282 ? 0.9652 0.4354 0.5360 0.0301  0.1573  -0.1605 282 LEU D CD2 
14615 N N   . LYS D 283 ? 0.8869 0.3464 0.5206 0.0576  0.1556  -0.1047 283 LYS D N   
14616 C CA  . LYS D 283 ? 0.9497 0.3894 0.5906 0.0600  0.1579  -0.0982 283 LYS D CA  
14617 C C   . LYS D 283 ? 0.8829 0.3261 0.5322 0.0570  0.1521  -0.0877 283 LYS D C   
14618 O O   . LYS D 283 ? 0.8472 0.2719 0.4949 0.0507  0.1529  -0.0855 283 LYS D O   
14619 C CB  . LYS D 283 ? 0.9555 0.3961 0.6082 0.0783  0.1631  -0.0911 283 LYS D CB  
14620 C CG  . LYS D 283 ? 1.0182 0.4338 0.6712 0.0823  0.1684  -0.0884 283 LYS D CG  
14621 C CD  . LYS D 283 ? 1.1350 0.5590 0.8043 0.1012  0.1694  -0.0757 283 LYS D CD  
14622 C CE  . LYS D 283 ? 1.0913 0.5389 0.7703 0.1123  0.1704  -0.0759 283 LYS D CE  
14623 N NZ  . LYS D 283 ? 1.0113 0.4793 0.7104 0.1267  0.1676  -0.0643 283 LYS D NZ  
14624 N N   . ASN D 284 ? 0.9056 0.3719 0.5639 0.0616  0.1472  -0.0808 284 ASN D N   
14625 C CA  . ASN D 284 ? 0.8259 0.2979 0.4930 0.0600  0.1415  -0.0709 284 ASN D CA  
14626 C C   . ASN D 284 ? 0.7773 0.2479 0.4337 0.0421  0.1365  -0.0765 284 ASN D C   
14627 O O   . ASN D 284 ? 0.8500 0.3269 0.5140 0.0387  0.1313  -0.0682 284 ASN D O   
14628 C CB  . ASN D 284 ? 0.7772 0.2755 0.4608 0.0721  0.1390  -0.0621 284 ASN D CB  
14629 C CG  . ASN D 284 ? 0.8491 0.3540 0.5461 0.0890  0.1433  -0.0575 284 ASN D CG  
14630 O OD1 . ASN D 284 ? 0.9507 0.4387 0.6447 0.0937  0.1476  -0.0583 284 ASN D OD1 
14631 N ND2 . ASN D 284 ? 0.7178 0.2478 0.4306 0.0980  0.1427  -0.0531 284 ASN D ND2 
14632 N N   . SER D 285 ? 0.8099 0.2779 0.4510 0.0303  0.1370  -0.0902 285 SER D N   
14633 C CA  . SER D 285 ? 0.7849 0.2678 0.4223 0.0126  0.1292  -0.0949 285 SER D CA  
14634 C C   . SER D 285 ? 0.8630 0.3223 0.4855 -0.0044 0.1321  -0.1094 285 SER D C   
14635 O O   . SER D 285 ? 0.8795 0.3423 0.5043 -0.0191 0.1275  -0.1098 285 SER D O   
14636 C CB  . SER D 285 ? 0.7650 0.2818 0.4014 0.0129  0.1240  -0.0974 285 SER D CB  
14637 O OG  . SER D 285 ? 0.7516 0.2851 0.4010 0.0286  0.1250  -0.0864 285 SER D OG  
14638 N N   . VAL D 286 ? 0.9359 0.3810 0.5497 -0.0038 0.1384  -0.1199 286 VAL D N   
14639 C CA  . VAL D 286 ? 1.0775 0.5072 0.6834 -0.0205 0.1410  -0.1339 286 VAL D CA  
14640 C C   . VAL D 286 ? 1.0967 0.4992 0.7068 -0.0134 0.1501  -0.1302 286 VAL D C   
14641 O O   . VAL D 286 ? 0.9075 0.3082 0.5217 0.0039  0.1540  -0.1237 286 VAL D O   
14642 C CB  . VAL D 286 ? 1.0137 0.4573 0.6053 -0.0281 0.1390  -0.1521 286 VAL D CB  
14643 C CG1 . VAL D 286 ? 1.0725 0.5124 0.6592 -0.0506 0.1377  -0.1680 286 VAL D CG1 
14644 C CG2 . VAL D 286 ? 0.9540 0.4276 0.5401 -0.0240 0.1320  -0.1507 286 VAL D CG2 
14645 N N   . GLU D 287 ? 1.1126 0.4952 0.7223 -0.0267 0.1541  -0.1345 287 GLU D N   
14646 C CA  . GLU D 287 ? 1.1042 0.4592 0.7179 -0.0196 0.1635  -0.1274 287 GLU D CA  
14647 C C   . GLU D 287 ? 1.3202 0.6636 0.9292 -0.0100 0.1706  -0.1341 287 GLU D C   
14648 O O   . GLU D 287 ? 1.4682 0.8093 1.0825 0.0090  0.1736  -0.1232 287 GLU D O   
14649 C CB  . GLU D 287 ? 1.1441 0.4804 0.7570 -0.0380 0.1681  -0.1329 287 GLU D CB  
14650 C CG  . GLU D 287 ? 1.3317 0.6764 0.9502 -0.0475 0.1627  -0.1249 287 GLU D CG  
14651 C CD  . GLU D 287 ? 1.4207 0.7421 1.0412 -0.0596 0.1707  -0.1239 287 GLU D CD  
14652 O OE1 . GLU D 287 ? 1.3861 0.6936 1.0026 -0.0727 0.1772  -0.1386 287 GLU D OE1 
14653 O OE2 . GLU D 287 ? 1.4041 0.7216 1.0303 -0.0557 0.1711  -0.1086 287 GLU D OE2 
14654 N N   . ARG D 288 ? 1.2825 0.6205 0.8822 -0.0232 0.1732  -0.1527 288 ARG D N   
14655 C CA  . ARG D 288 ? 1.2297 0.5563 0.8236 -0.0161 0.1801  -0.1616 288 ARG D CA  
14656 C C   . ARG D 288 ? 1.1382 0.4858 0.7217 -0.0245 0.1747  -0.1795 288 ARG D C   
14657 O O   . ARG D 288 ? 1.3207 0.6651 0.8974 -0.0410 0.1755  -0.1973 288 ARG D O   
14658 C CB  . ARG D 288 ? 1.2147 0.5088 0.8069 -0.0230 0.1910  -0.1671 288 ARG D CB  
14659 C CG  . ARG D 288 ? 1.0810 0.3549 0.6807 -0.0177 0.1965  -0.1501 288 ARG D CG  
14660 C CD  . ARG D 288 ? 1.2097 0.4595 0.8075 -0.0359 0.2044  -0.1584 288 ARG D CD  
14661 N NE  . ARG D 288 ? 1.4069 0.6727 1.0052 -0.0577 0.1975  -0.1686 288 ARG D NE  
14662 C CZ  . ARG D 288 ? 1.2499 0.5246 0.8431 -0.0752 0.1953  -0.1901 288 ARG D CZ  
14663 N NH1 . ARG D 288 ? 1.1949 0.4626 0.7810 -0.0742 0.1997  -0.2043 288 ARG D NH1 
14664 N NH2 . ARG D 288 ? 1.1085 0.4019 0.7041 -0.0940 0.1882  -0.1980 288 ARG D NH2 
14665 N N   . ALA D 289 ? 1.0033 0.3741 0.5856 -0.0125 0.1696  -0.1748 289 ALA D N   
14666 C CA  . ALA D 289 ? 1.0377 0.4327 0.6083 -0.0172 0.1640  -0.1887 289 ALA D CA  
14667 C C   . ALA D 289 ? 1.0161 0.4136 0.5822 -0.0013 0.1687  -0.1898 289 ALA D C   
14668 O O   . ALA D 289 ? 0.9869 0.3863 0.5616 0.0159  0.1710  -0.1749 289 ALA D O   
14669 C CB  . ALA D 289 ? 1.1734 0.5961 0.7445 -0.0178 0.1545  -0.1818 289 ALA D CB  
14670 N N   . SER D 290 ? 1.0312 0.4308 0.5848 -0.0072 0.1700  -0.2079 290 SER D N   
14671 C CA  . SER D 290 ? 1.0953 0.5007 0.6428 0.0070  0.1741  -0.2102 290 SER D CA  
14672 C C   . SER D 290 ? 1.0624 0.4979 0.6074 0.0167  0.1688  -0.2020 290 SER D C   
14673 O O   . SER D 290 ? 1.1267 0.5811 0.6689 0.0092  0.1608  -0.2014 290 SER D O   
14674 C CB  . SER D 290 ? 1.1293 0.5341 0.6623 -0.0021 0.1755  -0.2328 290 SER D CB  
14675 O OG  . SER D 290 ? 1.1278 0.5027 0.6631 -0.0007 0.1852  -0.2373 290 SER D OG  
14676 N N   . PRO D 291 ? 0.9974 0.4379 0.5446 0.0338  0.1739  -0.1946 291 PRO D N   
14677 C CA  . PRO D 291 ? 0.9720 0.4408 0.5154 0.0426  0.1709  -0.1880 291 PRO D CA  
14678 C C   . PRO D 291 ? 1.0975 0.5858 0.6205 0.0381  0.1679  -0.2033 291 PRO D C   
14679 O O   . PRO D 291 ? 1.0945 0.6085 0.6109 0.0422  0.1640  -0.1985 291 PRO D O   
14680 C CB  . PRO D 291 ? 0.9643 0.4310 0.5192 0.0611  0.1789  -0.1761 291 PRO D CB  
14681 C CG  . PRO D 291 ? 1.1210 0.5598 0.6865 0.0627  0.1842  -0.1742 291 PRO D CG  
14682 C CD  . PRO D 291 ? 1.1143 0.5361 0.6690 0.0463  0.1831  -0.1903 291 PRO D CD  
14683 N N   . TYR D 292 ? 1.0510 0.5293 0.5638 0.0304  0.1697  -0.2213 292 TYR D N   
14684 C CA  . TYR D 292 ? 1.0406 0.5395 0.5337 0.0283  0.1671  -0.2372 292 TYR D CA  
14685 C C   . TYR D 292 ? 1.0488 0.5624 0.5327 0.0100  0.1569  -0.2526 292 TYR D C   
14686 O O   . TYR D 292 ? 1.0800 0.5911 0.5555 -0.0006 0.1558  -0.2724 292 TYR D O   
14687 C CB  . TYR D 292 ? 1.1286 0.6112 0.6164 0.0321  0.1752  -0.2493 292 TYR D CB  
14688 C CG  . TYR D 292 ? 1.1256 0.5844 0.6285 0.0450  0.1851  -0.2362 292 TYR D CG  
14689 C CD1 . TYR D 292 ? 1.1460 0.6150 0.6541 0.0621  0.1900  -0.2221 292 TYR D CD1 
14690 C CD2 . TYR D 292 ? 1.0911 0.5190 0.6036 0.0404  0.1898  -0.2376 292 TYR D CD2 
14691 C CE1 . TYR D 292 ? 1.1734 0.6257 0.6969 0.0739  0.1980  -0.2111 292 TYR D CE1 
14692 C CE2 . TYR D 292 ? 1.0904 0.5005 0.6161 0.0537  0.1980  -0.2253 292 TYR D CE2 
14693 C CZ  . TYR D 292 ? 1.1661 0.5901 0.6977 0.0703  0.2014  -0.2127 292 TYR D CZ  
14694 O OH  . TYR D 292 ? 1.2475 0.6585 0.7939 0.0834  0.2086  -0.2015 292 TYR D OH  
14695 N N   . LEU D 293 ? 1.0212 0.5518 0.5078 0.0060  0.1493  -0.2438 293 LEU D N   
14696 C CA  . LEU D 293 ? 1.0244 0.5798 0.5020 -0.0089 0.1383  -0.2568 293 LEU D CA  
14697 C C   . LEU D 293 ? 1.0545 0.6424 0.5257 -0.0012 0.1319  -0.2448 293 LEU D C   
14698 O O   . LEU D 293 ? 1.0673 0.6555 0.5426 0.0143  0.1369  -0.2266 293 LEU D O   
14699 C CB  . LEU D 293 ? 1.0257 0.5660 0.5157 -0.0277 0.1350  -0.2609 293 LEU D CB  
14700 C CG  . LEU D 293 ? 1.1804 0.6824 0.6816 -0.0352 0.1431  -0.2654 293 LEU D CG  
14701 C CD1 . LEU D 293 ? 1.0403 0.5179 0.5566 -0.0246 0.1498  -0.2439 293 LEU D CD1 
14702 C CD2 . LEU D 293 ? 1.2722 0.7730 0.7786 -0.0579 0.1382  -0.2784 293 LEU D CD2 
14703 N N   . ARG D 294 ? 1.0722 0.6893 0.5347 -0.0121 0.1209  -0.2550 294 ARG D N   
14704 C CA  . ARG D 294 ? 0.9801 0.6309 0.4357 -0.0059 0.1137  -0.2442 294 ARG D CA  
14705 C C   . ARG D 294 ? 0.9528 0.6043 0.4205 -0.0197 0.1070  -0.2399 294 ARG D C   
14706 O O   . ARG D 294 ? 0.9690 0.6307 0.4382 -0.0374 0.0992  -0.2553 294 ARG D O   
14707 C CB  . ARG D 294 ? 0.9900 0.6801 0.4260 -0.0053 0.1054  -0.2581 294 ARG D CB  
14708 C CG  . ARG D 294 ? 0.9687 0.6968 0.3968 0.0019  0.0974  -0.2464 294 ARG D CG  
14709 C CD  . ARG D 294 ? 0.9922 0.7576 0.3990 0.0122  0.0930  -0.2538 294 ARG D CD  
14710 N NE  . ARG D 294 ? 1.1348 0.9250 0.5346 -0.0014 0.0808  -0.2774 294 ARG D NE  
14711 C CZ  . ARG D 294 ? 1.1816 0.9929 0.5637 0.0036  0.0769  -0.2933 294 ARG D CZ  
14712 N NH1 . ARG D 294 ? 1.1063 0.9196 0.4767 0.0196  0.0856  -0.2893 294 ARG D NH1 
14713 N NH2 . ARG D 294 ? 1.1756 1.0047 0.5520 -0.0085 0.0643  -0.3127 294 ARG D NH2 
14714 N N   . TYR D 295 ? 0.9239 0.5662 0.4015 -0.0118 0.1101  -0.2195 295 TYR D N   
14715 C CA  . TYR D 295 ? 0.9022 0.5467 0.3935 -0.0229 0.1039  -0.2128 295 TYR D CA  
14716 C C   . TYR D 295 ? 0.8852 0.5748 0.3779 -0.0184 0.0933  -0.2024 295 TYR D C   
14717 O O   . TYR D 295 ? 0.9232 0.6307 0.4076 -0.0016 0.0950  -0.1919 295 TYR D O   
14718 C CB  . TYR D 295 ? 0.8795 0.4978 0.3920 -0.0160 0.1104  -0.1939 295 TYR D CB  
14719 C CG  . TYR D 295 ? 0.9014 0.4772 0.4167 -0.0176 0.1205  -0.1999 295 TYR D CG  
14720 C CD1 . TYR D 295 ? 0.9111 0.4752 0.4251 -0.0030 0.1292  -0.1974 295 TYR D CD1 
14721 C CD2 . TYR D 295 ? 0.9094 0.4634 0.4359 -0.0325 0.1206  -0.2042 295 TYR D CD2 
14722 C CE1 . TYR D 295 ? 0.9280 0.4610 0.4511 -0.0026 0.1368  -0.1993 295 TYR D CE1 
14723 C CE2 . TYR D 295 ? 0.9277 0.4488 0.4627 -0.0314 0.1290  -0.2048 295 TYR D CE2 
14724 C CZ  . TYR D 295 ? 0.9368 0.4482 0.4697 -0.0161 0.1367  -0.2024 295 TYR D CZ  
14725 O OH  . TYR D 295 ? 1.0253 0.5062 0.5663 -0.0138 0.1450  -0.2022 295 TYR D OH  
14726 N N   . TYR D 296 ? 0.8668 0.5740 0.3702 -0.0331 0.0834  -0.2049 296 TYR D N   
14727 C CA  . TYR D 296 ? 0.9080 0.6565 0.4166 -0.0291 0.0733  -0.1934 296 TYR D CA  
14728 C C   . TYR D 296 ? 0.8856 0.6279 0.4196 -0.0324 0.0719  -0.1764 296 TYR D C   
14729 O O   . TYR D 296 ? 0.8122 0.5402 0.3571 -0.0490 0.0704  -0.1831 296 TYR D O   
14730 C CB  . TYR D 296 ? 0.8926 0.6753 0.3918 -0.0429 0.0618  -0.2123 296 TYR D CB  
14731 C CG  . TYR D 296 ? 1.0251 0.8184 0.4978 -0.0404 0.0619  -0.2315 296 TYR D CG  
14732 C CD1 . TYR D 296 ? 1.0608 0.8484 0.5174 -0.0207 0.0698  -0.2246 296 TYR D CD1 
14733 C CD2 . TYR D 296 ? 1.0990 0.9093 0.5634 -0.0580 0.0545  -0.2575 296 TYR D CD2 
14734 C CE1 . TYR D 296 ? 0.9733 0.7727 0.4064 -0.0172 0.0696  -0.2415 296 TYR D CE1 
14735 C CE2 . TYR D 296 ? 1.0405 0.8669 0.4901 -0.0526 0.0520  -0.2722 296 TYR D CE2 
14736 C CZ  . TYR D 296 ? 0.9550 0.7760 0.3876 -0.0321 0.0595  -0.2644 296 TYR D CZ  
14737 O OH  . TYR D 296 ? 0.9803 0.8170 0.3961 -0.0258 0.0570  -0.2790 296 TYR D OH  
14738 N N   . PHE D 297 ? 0.8232 0.5752 0.3661 -0.0169 0.0735  -0.1551 297 PHE D N   
14739 C CA  . PHE D 297 ? 0.7508 0.5012 0.3171 -0.0186 0.0718  -0.1390 297 PHE D CA  
14740 C C   . PHE D 297 ? 0.7975 0.5836 0.3688 -0.0274 0.0602  -0.1397 297 PHE D C   
14741 O O   . PHE D 297 ? 0.8509 0.6682 0.4183 -0.0167 0.0562  -0.1311 297 PHE D O   
14742 C CB  . PHE D 297 ? 0.7277 0.4766 0.3027 0.0000  0.0786  -0.1185 297 PHE D CB  
14743 C CG  . PHE D 297 ? 0.7498 0.4961 0.3486 -0.0012 0.0776  -0.1036 297 PHE D CG  
14744 C CD1 . PHE D 297 ? 0.6959 0.4140 0.3069 -0.0087 0.0801  -0.1039 297 PHE D CD1 
14745 C CD2 . PHE D 297 ? 0.6926 0.4645 0.3005 0.0061  0.0747  -0.0891 297 PHE D CD2 
14746 C CE1 . PHE D 297 ? 0.6695 0.3876 0.3007 -0.0091 0.0788  -0.0907 297 PHE D CE1 
14747 C CE2 . PHE D 297 ? 0.6462 0.4163 0.2754 0.0047  0.0739  -0.0769 297 PHE D CE2 
14748 C CZ  . PHE D 297 ? 0.6442 0.3886 0.2848 -0.0030 0.0755  -0.0780 297 PHE D CZ  
14749 N N   . ARG D 298 ? 0.8485 0.6297 0.4281 -0.0464 0.0556  -0.1499 298 ARG D N   
14750 C CA  . ARG D 298 ? 0.8369 0.6516 0.4244 -0.0572 0.0450  -0.1521 298 ARG D CA  
14751 C C   . ARG D 298 ? 0.8286 0.6825 0.3994 -0.0558 0.0368  -0.1640 298 ARG D C   
14752 O O   . ARG D 298 ? 0.9496 0.8408 0.5248 -0.0547 0.0281  -0.1595 298 ARG D O   
14753 C CB  . ARG D 298 ? 0.8002 0.6280 0.4051 -0.0487 0.0431  -0.1303 298 ARG D CB  
14754 C CG  . ARG D 298 ? 0.6823 0.4765 0.3019 -0.0449 0.0511  -0.1169 298 ARG D CG  
14755 C CD  . ARG D 298 ? 0.6495 0.4591 0.2869 -0.0394 0.0486  -0.0987 298 ARG D CD  
14756 N NE  . ARG D 298 ? 0.6364 0.4178 0.2884 -0.0385 0.0544  -0.0888 298 ARG D NE  
14757 C CZ  . ARG D 298 ? 0.6124 0.3945 0.2765 -0.0263 0.0578  -0.0727 298 ARG D CZ  
14758 N NH1 . ARG D 298 ? 0.5993 0.4046 0.2632 -0.0141 0.0577  -0.0633 298 ARG D NH1 
14759 N NH2 . ARG D 298 ? 0.6034 0.3625 0.2799 -0.0259 0.0620  -0.0661 298 ARG D NH2 
14760 N N   . GLU D 299 ? 0.8526 0.6994 0.4036 -0.0549 0.0396  -0.1794 299 GLU D N   
14761 C CA  . GLU D 299 ? 0.9935 0.8781 0.5250 -0.0510 0.0323  -0.1915 299 GLU D CA  
14762 C C   . GLU D 299 ? 0.8408 0.7545 0.3670 -0.0284 0.0305  -0.1717 299 GLU D C   
14763 O O   . GLU D 299 ? 0.8247 0.7809 0.3430 -0.0246 0.0210  -0.1743 299 GLU D O   
14764 C CB  . GLU D 299 ? 1.1135 1.0282 0.6490 -0.0711 0.0211  -0.2108 299 GLU D CB  
14765 C CG  . GLU D 299 ? 1.2248 1.1094 0.7668 -0.0953 0.0248  -0.2308 299 GLU D CG  
14766 C CD  . GLU D 299 ? 1.3227 1.2386 0.8734 -0.1169 0.0149  -0.2491 299 GLU D CD  
14767 O OE1 . GLU D 299 ? 1.3333 1.2888 0.8930 -0.1137 0.0055  -0.2405 299 GLU D OE1 
14768 O OE2 . GLU D 299 ? 1.1241 1.0252 0.6734 -0.1372 0.0174  -0.2727 299 GLU D OE2 
14769 N N   . LEU D 300 ? 0.7613 0.6524 0.2923 -0.0131 0.0403  -0.1518 300 LEU D N   
14770 C CA  . LEU D 300 ? 0.7463 0.6572 0.2742 0.0082  0.0423  -0.1312 300 LEU D CA  
14771 C C   . LEU D 300 ? 0.7939 0.6875 0.3067 0.0260  0.0541  -0.1242 300 LEU D C   
14772 O O   . LEU D 300 ? 0.8726 0.7882 0.3707 0.0433  0.0555  -0.1150 300 LEU D O   
14773 C CB  . LEU D 300 ? 0.7884 0.6936 0.3412 0.0098  0.0441  -0.1115 300 LEU D CB  
14774 C CG  . LEU D 300 ? 0.7287 0.6523 0.2984 -0.0055 0.0338  -0.1143 300 LEU D CG  
14775 C CD1 . LEU D 300 ? 0.6666 0.5750 0.2601 -0.0048 0.0378  -0.0968 300 LEU D CD1 
14776 C CD2 . LEU D 300 ? 0.7587 0.7303 0.3207 -0.0001 0.0237  -0.1146 300 LEU D CD2 
14777 N N   . ILE D 301 ? 0.7887 0.6438 0.3045 0.0233  0.0634  -0.1275 301 ILE D N   
14778 C CA  . ILE D 301 ? 0.7725 0.6104 0.2771 0.0397  0.0759  -0.1208 301 ILE D CA  
14779 C C   . ILE D 301 ? 0.8144 0.6185 0.3139 0.0317  0.0816  -0.1366 301 ILE D C   
14780 O O   . ILE D 301 ? 0.8680 0.6511 0.3809 0.0167  0.0801  -0.1439 301 ILE D O   
14781 C CB  . ILE D 301 ? 0.7446 0.5712 0.2679 0.0517  0.0851  -0.0976 301 ILE D CB  
14782 C CG1 . ILE D 301 ? 0.7549 0.5642 0.2691 0.0675  0.0995  -0.0911 301 ILE D CG1 
14783 C CG2 . ILE D 301 ? 0.7232 0.5270 0.2723 0.0398  0.0848  -0.0951 301 ILE D CG2 
14784 C CD1 . ILE D 301 ? 0.7399 0.5589 0.2594 0.0842  0.1079  -0.0696 301 ILE D CD1 
14785 N N   . SER D 302 ? 0.8646 0.6628 0.3436 0.0426  0.0893  -0.1413 302 SER D N   
14786 C CA  . SER D 302 ? 0.8819 0.6493 0.3529 0.0371  0.0957  -0.1573 302 SER D CA  
14787 C C   . SER D 302 ? 0.8308 0.5659 0.3151 0.0464  0.1090  -0.1451 302 SER D C   
14788 O O   . SER D 302 ? 0.8621 0.6018 0.3493 0.0621  0.1167  -0.1284 302 SER D O   
14789 C CB  . SER D 302 ? 0.9139 0.6933 0.3544 0.0436  0.0970  -0.1712 302 SER D CB  
14790 O OG  . SER D 302 ? 0.9242 0.7296 0.3532 0.0308  0.0845  -0.1899 302 SER D OG  
14791 N N   . VAL D 303 ? 0.8376 0.5406 0.3305 0.0369  0.1123  -0.1538 303 VAL D N   
14792 C CA  . VAL D 303 ? 0.8297 0.5036 0.3361 0.0455  0.1239  -0.1445 303 VAL D CA  
14793 C C   . VAL D 303 ? 0.8625 0.5079 0.3553 0.0445  0.1317  -0.1608 303 VAL D C   
14794 O O   . VAL D 303 ? 0.8825 0.5169 0.3703 0.0301  0.1275  -0.1776 303 VAL D O   
14795 C CB  . VAL D 303 ? 0.8039 0.4649 0.3371 0.0384  0.1213  -0.1351 303 VAL D CB  
14796 C CG1 . VAL D 303 ? 0.8448 0.4830 0.3926 0.0497  0.1324  -0.1251 303 VAL D CG1 
14797 C CG2 . VAL D 303 ? 0.7739 0.4631 0.3198 0.0376  0.1132  -0.1213 303 VAL D CG2 
14798 N N   . PHE D 304 ? 0.8720 0.5109 0.3669 0.0589  0.1420  -0.1542 304 PHE D N   
14799 C CA  . PHE D 304 ? 0.8874 0.5055 0.3832 0.0600  0.1486  -0.1637 304 PHE D CA  
14800 C C   . PHE D 304 ? 0.8966 0.4930 0.4154 0.0676  0.1567  -0.1514 304 PHE D C   
14801 O O   . PHE D 304 ? 0.8929 0.4973 0.4243 0.0771  0.1604  -0.1355 304 PHE D O   
14802 C CB  . PHE D 304 ? 0.9771 0.6108 0.4577 0.0708  0.1532  -0.1665 304 PHE D CB  
14803 C CG  . PHE D 304 ? 1.1540 0.8151 0.6121 0.0656  0.1444  -0.1787 304 PHE D CG  
14804 C CD1 . PHE D 304 ? 1.1761 0.8395 0.6286 0.0485  0.1342  -0.1950 304 PHE D CD1 
14805 C CD2 . PHE D 304 ? 1.1297 0.8167 0.5740 0.0777  0.1463  -0.1738 304 PHE D CD2 
14806 C CE1 . PHE D 304 ? 1.2551 0.9495 0.6892 0.0438  0.1249  -0.2076 304 PHE D CE1 
14807 C CE2 . PHE D 304 ? 1.1331 0.8501 0.5573 0.0744  0.1373  -0.1849 304 PHE D CE2 
14808 C CZ  . PHE D 304 ? 1.2414 0.9639 0.6606 0.0576  0.1260  -0.2025 304 PHE D CZ  
14809 N N   . PHE D 305 ? 0.9540 0.5250 0.4799 0.0635  0.1594  -0.1585 305 PHE D N   
14810 C CA  . PHE D 305 ? 0.9034 0.4573 0.4520 0.0707  0.1651  -0.1472 305 PHE D CA  
14811 C C   . PHE D 305 ? 0.9545 0.5011 0.5054 0.0813  0.1743  -0.1487 305 PHE D C   
14812 O O   . PHE D 305 ? 1.0964 0.6285 0.6388 0.0771  0.1759  -0.1616 305 PHE D O   
14813 C CB  . PHE D 305 ? 0.9036 0.4353 0.4608 0.0598  0.1614  -0.1501 305 PHE D CB  
14814 C CG  . PHE D 305 ? 0.8537 0.3917 0.4154 0.0520  0.1540  -0.1441 305 PHE D CG  
14815 C CD1 . PHE D 305 ? 0.8611 0.4071 0.4085 0.0375  0.1461  -0.1545 305 PHE D CD1 
14816 C CD2 . PHE D 305 ? 0.8462 0.3855 0.4274 0.0589  0.1546  -0.1288 305 PHE D CD2 
14817 C CE1 . PHE D 305 ? 0.8396 0.3948 0.3934 0.0299  0.1388  -0.1482 305 PHE D CE1 
14818 C CE2 . PHE D 305 ? 0.8056 0.3515 0.3913 0.0519  0.1479  -0.1234 305 PHE D CE2 
14819 C CZ  . PHE D 305 ? 0.8095 0.3674 0.3857 0.0369  0.1387  -0.1309 305 PHE D CZ  
14820 N N   . ARG D 306 ? 0.9146 0.4720 0.4780 0.0943  0.1807  -0.1359 306 ARG D N   
14821 C CA  . ARG D 306 ? 1.0496 0.6033 0.6164 0.1046  0.1898  -0.1364 306 ARG D CA  
14822 C C   . ARG D 306 ? 0.9465 0.4775 0.5261 0.1051  0.1919  -0.1384 306 ARG D C   
14823 O O   . ARG D 306 ? 0.9090 0.4336 0.5055 0.1045  0.1891  -0.1305 306 ARG D O   
14824 C CB  . ARG D 306 ? 0.9873 0.5584 0.5694 0.1165  0.1966  -0.1218 306 ARG D CB  
14825 C CG  . ARG D 306 ? 0.9084 0.4805 0.5191 0.1201  0.1967  -0.1093 306 ARG D CG  
14826 C CD  . ARG D 306 ? 0.8391 0.4186 0.4687 0.1315  0.2060  -0.1024 306 ARG D CD  
14827 N NE  . ARG D 306 ? 0.8076 0.3867 0.4640 0.1347  0.2048  -0.0954 306 ARG D NE  
14828 C CZ  . ARG D 306 ? 0.7974 0.3871 0.4756 0.1434  0.2111  -0.0894 306 ARG D CZ  
14829 N NH1 . ARG D 306 ? 0.8039 0.4031 0.4814 0.1493  0.2200  -0.0886 306 ARG D NH1 
14830 N NH2 . ARG D 306 ? 0.7815 0.3738 0.4827 0.1462  0.2082  -0.0845 306 ARG D NH2 
14831 N N   . ASP D 307 ? 0.9906 0.5100 0.5611 0.1070  0.1970  -0.1489 307 ASP D N   
14832 C CA  . ASP D 307 ? 1.0109 0.5090 0.5925 0.1098  0.2005  -0.1499 307 ASP D CA  
14833 C C   . ASP D 307 ? 0.9177 0.4248 0.5221 0.1235  0.2061  -0.1364 307 ASP D C   
14834 O O   . ASP D 307 ? 0.9405 0.4574 0.5454 0.1322  0.2131  -0.1358 307 ASP D O   
14835 C CB  . ASP D 307 ? 0.9890 0.4725 0.5546 0.1081  0.2051  -0.1654 307 ASP D CB  
14836 C CG  . ASP D 307 ? 1.0214 0.4783 0.5942 0.1075  0.2078  -0.1681 307 ASP D CG  
14837 O OD1 . ASP D 307 ? 1.1248 0.5758 0.7138 0.1090  0.2055  -0.1572 307 ASP D OD1 
14838 O OD2 . ASP D 307 ? 1.0627 0.5047 0.6244 0.1058  0.2123  -0.1810 307 ASP D OD2 
14839 N N   . LYS D 308 ? 0.8975 0.4032 0.5213 0.1252  0.2028  -0.1263 308 LYS D N   
14840 C CA  . LYS D 308 ? 0.8745 0.3954 0.5227 0.1368  0.2060  -0.1144 308 LYS D CA  
14841 C C   . LYS D 308 ? 0.8935 0.4086 0.5476 0.1473  0.2139  -0.1168 308 LYS D C   
14842 O O   . LYS D 308 ? 0.8835 0.4153 0.5502 0.1561  0.2196  -0.1122 308 LYS D O   
14843 C CB  . LYS D 308 ? 0.8533 0.3743 0.5189 0.1364  0.1997  -0.1053 308 LYS D CB  
14844 C CG  . LYS D 308 ? 0.8473 0.3727 0.5356 0.1485  0.2023  -0.0983 308 LYS D CG  
14845 C CD  . LYS D 308 ? 0.8508 0.3729 0.5500 0.1477  0.1953  -0.0910 308 LYS D CD  
14846 C CE  . LYS D 308 ? 1.1650 0.7060 0.8909 0.1596  0.1953  -0.0823 308 LYS D CE  
14847 N NZ  . LYS D 308 ? 1.1588 0.6900 0.8907 0.1626  0.1902  -0.0766 308 LYS D NZ  
14848 N N   . THR D 309 ? 0.9539 0.4451 0.5996 0.1463  0.2153  -0.1241 309 THR D N   
14849 C CA  . THR D 309 ? 0.9637 0.4488 0.6156 0.1574  0.2231  -0.1259 309 THR D CA  
14850 C C   . THR D 309 ? 0.9533 0.4475 0.5953 0.1608  0.2303  -0.1321 309 THR D C   
14851 O O   . THR D 309 ? 0.9449 0.4543 0.6011 0.1709  0.2361  -0.1271 309 THR D O   
14852 C CB  . THR D 309 ? 0.9755 0.4306 0.6179 0.1553  0.2245  -0.1330 309 THR D CB  
14853 O OG1 . THR D 309 ? 1.0945 0.5415 0.7337 0.1637  0.2333  -0.1394 309 THR D OG1 
14854 C CG2 . THR D 309 ? 0.9918 0.4316 0.6124 0.1394  0.2204  -0.1440 309 THR D CG2 
14855 N N   . LEU D 310 ? 0.9712 0.4596 0.5893 0.1521  0.2297  -0.1429 310 LEU D N   
14856 C CA  . LEU D 310 ? 1.0081 0.5045 0.6138 0.1561  0.2367  -0.1494 310 LEU D CA  
14857 C C   . LEU D 310 ? 1.0033 0.5260 0.6188 0.1616  0.2396  -0.1389 310 LEU D C   
14858 O O   . LEU D 310 ? 0.9784 0.5095 0.5953 0.1697  0.2481  -0.1388 310 LEU D O   
14859 C CB  . LEU D 310 ? 1.0111 0.5004 0.5886 0.1455  0.2340  -0.1641 310 LEU D CB  
14860 C CG  . LEU D 310 ? 1.0491 0.5130 0.6144 0.1410  0.2358  -0.1790 310 LEU D CG  
14861 C CD1 . LEU D 310 ? 1.1249 0.5680 0.6984 0.1350  0.2315  -0.1775 310 LEU D CD1 
14862 C CD2 . LEU D 310 ? 1.1431 0.6083 0.6816 0.1316  0.2337  -0.1959 310 LEU D CD2 
14863 N N   . SER D 311 ? 1.0523 0.5875 0.6748 0.1571  0.2336  -0.1303 311 SER D N   
14864 C CA  . SER D 311 ? 0.9064 0.4651 0.5414 0.1618  0.2374  -0.1195 311 SER D CA  
14865 C C   . SER D 311 ? 0.8899 0.4582 0.5547 0.1706  0.2416  -0.1113 311 SER D C   
14866 O O   . SER D 311 ? 0.8847 0.4683 0.5597 0.1768  0.2497  -0.1069 311 SER D O   
14867 C CB  . SER D 311 ? 0.8813 0.4498 0.5161 0.1546  0.2301  -0.1130 311 SER D CB  
14868 O OG  . SER D 311 ? 0.8974 0.4585 0.5056 0.1460  0.2247  -0.1221 311 SER D OG  
14869 N N   . ASP D 312 ? 0.9162 0.4767 0.5950 0.1714  0.2365  -0.1095 312 ASP D N   
14870 C CA  . ASP D 312 ? 0.9514 0.5248 0.6588 0.1804  0.2389  -0.1030 312 ASP D CA  
14871 C C   . ASP D 312 ? 1.0230 0.5948 0.7332 0.1901  0.2481  -0.1074 312 ASP D C   
14872 O O   . ASP D 312 ? 1.0071 0.5974 0.7397 0.1974  0.2530  -0.1030 312 ASP D O   
14873 C CB  . ASP D 312 ? 0.8986 0.4638 0.6169 0.1807  0.2310  -0.1001 312 ASP D CB  
14874 C CG  . ASP D 312 ? 1.0021 0.5817 0.7335 0.1758  0.2236  -0.0920 312 ASP D CG  
14875 O OD1 . ASP D 312 ? 1.2475 0.8460 0.9857 0.1736  0.2258  -0.0879 312 ASP D OD1 
14876 O OD2 . ASP D 312 ? 0.9078 0.4789 0.6423 0.1741  0.2164  -0.0897 312 ASP D OD2 
14877 N N   . LEU D 313 ? 0.9646 0.5155 0.6541 0.1902  0.2509  -0.1170 313 LEU D N   
14878 C CA  . LEU D 313 ? 0.9449 0.4940 0.6376 0.2001  0.2601  -0.1212 313 LEU D CA  
14879 C C   . LEU D 313 ? 0.9793 0.5474 0.6742 0.2030  0.2687  -0.1193 313 LEU D C   
14880 O O   . LEU D 313 ? 1.0490 0.6306 0.7630 0.2116  0.2755  -0.1168 313 LEU D O   
14881 C CB  . LEU D 313 ? 0.9837 0.5064 0.6526 0.1988  0.2623  -0.1331 313 LEU D CB  
14882 C CG  . LEU D 313 ? 1.0118 0.5076 0.6709 0.1946  0.2575  -0.1385 313 LEU D CG  
14883 C CD1 . LEU D 313 ? 1.1551 0.6347 0.7845 0.1827  0.2555  -0.1509 313 LEU D CD1 
14884 C CD2 . LEU D 313 ? 1.0262 0.5101 0.6941 0.2062  0.2636  -0.1402 313 LEU D CD2 
14885 N N   . ILE D 314 ? 0.9423 0.5124 0.6176 0.1964  0.2690  -0.1205 314 ILE D N   
14886 C CA  . ILE D 314 ? 0.9424 0.5283 0.6167 0.1996  0.2783  -0.1174 314 ILE D CA  
14887 C C   . ILE D 314 ? 0.9102 0.5191 0.6141 0.2014  0.2805  -0.1063 314 ILE D C   
14888 O O   . ILE D 314 ? 1.0086 0.6304 0.7269 0.2075  0.2900  -0.1040 314 ILE D O   
14889 C CB  . ILE D 314 ? 0.9511 0.5359 0.5973 0.1933  0.2772  -0.1196 314 ILE D CB  
14890 C CG1 . ILE D 314 ? 0.9807 0.5446 0.5999 0.1888  0.2726  -0.1331 314 ILE D CG1 
14891 C CG2 . ILE D 314 ? 0.9691 0.5661 0.6094 0.1986  0.2886  -0.1168 314 ILE D CG2 
14892 C CD1 . ILE D 314 ? 0.9942 0.5610 0.5844 0.1840  0.2713  -0.1381 314 ILE D CD1 
14893 N N   . GLY D 315 ? 0.8830 0.4977 0.5972 0.1955  0.2721  -0.1002 315 GLY D N   
14894 C CA  . GLY D 315 ? 0.9251 0.5624 0.6664 0.1952  0.2741  -0.0912 315 GLY D CA  
14895 C C   . GLY D 315 ? 0.9102 0.5600 0.6827 0.2018  0.2745  -0.0907 315 GLY D C   
14896 O O   . GLY D 315 ? 0.9072 0.5783 0.7039 0.2025  0.2794  -0.0861 315 GLY D O   
14897 N N   . PHE D 316 ? 0.8534 0.4910 0.6263 0.2068  0.2700  -0.0956 316 PHE D N   
14898 C CA  . PHE D 316 ? 0.9050 0.5565 0.7069 0.2148  0.2690  -0.0949 316 PHE D CA  
14899 C C   . PHE D 316 ? 1.0574 0.6982 0.8582 0.2253  0.2726  -0.1009 316 PHE D C   
14900 O O   . PHE D 316 ? 1.0900 0.7458 0.9154 0.2340  0.2733  -0.1007 316 PHE D O   
14901 C CB  . PHE D 316 ? 0.9484 0.6009 0.7602 0.2122  0.2572  -0.0912 316 PHE D CB  
14902 C CG  . PHE D 316 ? 0.9793 0.6537 0.8093 0.2059  0.2548  -0.0853 316 PHE D CG  
14903 C CD1 . PHE D 316 ? 0.9670 0.6669 0.8220 0.2078  0.2620  -0.0842 316 PHE D CD1 
14904 C CD2 . PHE D 316 ? 0.8998 0.5690 0.7224 0.1976  0.2459  -0.0816 316 PHE D CD2 
14905 C CE1 . PHE D 316 ? 0.7475 0.4662 0.6199 0.2011  0.2608  -0.0797 316 PHE D CE1 
14906 C CE2 . PHE D 316 ? 0.8406 0.5291 0.6801 0.1919  0.2443  -0.0766 316 PHE D CE2 
14907 C CZ  . PHE D 316 ? 0.7347 0.4475 0.5992 0.1935  0.2519  -0.0758 316 PHE D CZ  
14908 N N   . SER D 317 ? 1.0566 0.6734 0.8307 0.2252  0.2751  -0.1069 317 SER D N   
14909 C CA  . SER D 317 ? 1.0054 0.6078 0.7772 0.2348  0.2781  -0.1125 317 SER D CA  
14910 C C   . SER D 317 ? 1.0749 0.6735 0.8359 0.2395  0.2895  -0.1188 317 SER D C   
14911 O O   . SER D 317 ? 1.0784 0.6790 0.8505 0.2501  0.2950  -0.1215 317 SER D O   
14912 C CB  . SER D 317 ? 0.9662 0.5394 0.7173 0.2310  0.2713  -0.1157 317 SER D CB  
14913 O OG  . SER D 317 ? 1.0925 0.6676 0.8491 0.2249  0.2611  -0.1097 317 SER D OG  
14914 N N   . TYR D 318 ? 1.1300 0.7238 0.8690 0.2327  0.2932  -0.1212 318 TYR D N   
14915 C CA  . TYR D 318 ? 1.0925 0.6807 0.8168 0.2370  0.3038  -0.1279 318 TYR D CA  
14916 C C   . TYR D 318 ? 1.0756 0.6874 0.8188 0.2428  0.3143  -0.1243 318 TYR D C   
14917 O O   . TYR D 318 ? 1.1433 0.7528 0.8738 0.2460  0.3240  -0.1286 318 TYR D O   
14918 C CB  . TYR D 318 ? 1.0860 0.6625 0.7782 0.2287  0.3037  -0.1323 318 TYR D CB  
14919 C CG  . TYR D 318 ? 1.0262 0.5771 0.6964 0.2230  0.2963  -0.1405 318 TYR D CG  
14920 C CD1 . TYR D 318 ? 1.0401 0.5740 0.7153 0.2272  0.2940  -0.1442 318 TYR D CD1 
14921 C CD2 . TYR D 318 ? 1.0324 0.5765 0.6770 0.2135  0.2921  -0.1449 318 TYR D CD2 
14922 C CE1 . TYR D 318 ? 1.0600 0.5688 0.7160 0.2208  0.2887  -0.1519 318 TYR D CE1 
14923 C CE2 . TYR D 318 ? 1.0509 0.5729 0.6771 0.2067  0.2857  -0.1542 318 TYR D CE2 
14924 C CZ  . TYR D 318 ? 1.0649 0.5682 0.6973 0.2097  0.2845  -0.1576 318 TYR D CZ  
14925 O OH  . TYR D 318 ? 1.0863 0.5662 0.7014 0.2017  0.2796  -0.1670 318 TYR D OH  
14926 N N   . HIS D 319 ? 1.0786 0.7133 0.8517 0.2437  0.3130  -0.1175 319 HIS D N   
14927 C CA  . HIS D 319 ? 1.0745 0.7318 0.8680 0.2484  0.3238  -0.1156 319 HIS D CA  
14928 C C   . HIS D 319 ? 1.0841 0.7439 0.8906 0.2606  0.3295  -0.1213 319 HIS D C   
14929 O O   . HIS D 319 ? 1.1111 0.7796 0.9213 0.2652  0.3411  -0.1233 319 HIS D O   
14930 C CB  . HIS D 319 ? 0.9689 0.6516 0.7916 0.2442  0.3210  -0.1086 319 HIS D CB  
14931 C CG  . HIS D 319 ? 0.9287 0.6206 0.7752 0.2487  0.3118  -0.1088 319 HIS D CG  
14932 N ND1 . HIS D 319 ? 1.0453 0.7194 0.8811 0.2484  0.3007  -0.1092 319 HIS D ND1 
14933 C CD2 . HIS D 319 ? 0.8811 0.5992 0.7613 0.2541  0.3121  -0.1089 319 HIS D CD2 
14934 C CE1 . HIS D 319 ? 1.2140 0.9021 1.0747 0.2544  0.2947  -0.1083 319 HIS D CE1 
14935 N NE2 . HIS D 319 ? 1.0855 0.8017 0.9737 0.2582  0.3010  -0.1089 319 HIS D NE2 
14936 N N   . ALA D 320 ? 1.0221 0.6738 0.8349 0.2666  0.3222  -0.1235 320 ALA D N   
14937 C CA  . ALA D 320 ? 1.0598 0.7113 0.8830 0.2798  0.3270  -0.1286 320 ALA D CA  
14938 C C   . ALA D 320 ? 1.0904 0.7108 0.8851 0.2828  0.3297  -0.1356 320 ALA D C   
14939 O O   . ALA D 320 ? 1.0524 0.6665 0.8522 0.2940  0.3330  -0.1397 320 ALA D O   
14940 C CB  . ALA D 320 ? 0.9782 0.6401 0.8259 0.2870  0.3186  -0.1262 320 ALA D CB  
14941 N N   . TRP D 321 ? 1.2186 0.8202 0.9838 0.2732  0.3285  -0.1379 321 TRP D N   
14942 C CA  . TRP D 321 ? 1.2166 0.7889 0.9537 0.2736  0.3305  -0.1468 321 TRP D CA  
14943 C C   . TRP D 321 ? 1.2152 0.7878 0.9352 0.2738  0.3415  -0.1524 321 TRP D C   
14944 O O   . TRP D 321 ? 1.2474 0.8313 0.9608 0.2671  0.3434  -0.1488 321 TRP D O   
14945 C CB  . TRP D 321 ? 1.1861 0.7384 0.9019 0.2624  0.3205  -0.1479 321 TRP D CB  
14946 C CG  . TRP D 321 ? 1.2169 0.7534 0.9376 0.2644  0.3128  -0.1467 321 TRP D CG  
14947 C CD1 . TRP D 321 ? 1.1379 0.6869 0.8845 0.2711  0.3080  -0.1393 321 TRP D CD1 
14948 C CD2 . TRP D 321 ? 1.3135 0.8188 1.0123 0.2599  0.3094  -0.1533 321 TRP D CD2 
14949 N NE1 . TRP D 321 ? 1.2569 0.7832 0.9975 0.2720  0.3023  -0.1393 321 TRP D NE1 
14950 C CE2 . TRP D 321 ? 1.3696 0.8680 1.0817 0.2646  0.3035  -0.1477 321 TRP D CE2 
14951 C CE3 . TRP D 321 ? 1.2446 0.7281 0.9143 0.2523  0.3111  -0.1642 321 TRP D CE3 
14952 C CZ2 . TRP D 321 ? 1.4016 0.8695 1.0986 0.2614  0.3005  -0.1514 321 TRP D CZ2 
14953 C CZ3 . TRP D 321 ? 1.2181 0.6729 0.8746 0.2481  0.3075  -0.1697 321 TRP D CZ3 
14954 C CH2 . TRP D 321 ? 1.3395 0.7855 1.0096 0.2524  0.3028  -0.1626 321 TRP D CH2 
14955 N N   . ASN D 322 ? 1.1427 0.7024 0.8545 0.2821  0.3493  -0.1607 322 ASN D N   
14956 C CA  . ASN D 322 ? 1.1589 0.7180 0.8527 0.2832  0.3600  -0.1669 322 ASN D CA  
14957 C C   . ASN D 322 ? 1.2363 0.7814 0.8974 0.2725  0.3563  -0.1722 322 ASN D C   
14958 O O   . ASN D 322 ? 1.2657 0.7936 0.9150 0.2656  0.3470  -0.1755 322 ASN D O   
14959 C CB  . ASN D 322 ? 1.1954 0.7413 0.8859 0.2942  0.3685  -0.1761 322 ASN D CB  
14960 C CG  . ASN D 322 ? 1.1955 0.7632 0.9070 0.3045  0.3798  -0.1739 322 ASN D CG  
14961 O OD1 . ASN D 322 ? 1.1667 0.7581 0.9068 0.3067  0.3788  -0.1658 322 ASN D OD1 
14962 N ND2 . ASN D 322 ? 1.2289 0.7900 0.9266 0.3103  0.3908  -0.1821 322 ASN D ND2 
14963 N N   . ALA D 323 ? 1.4185 0.7537 0.9343 0.2131  0.4858  -0.1640 323 ALA D N   
14964 C CA  . ALA D 323 ? 1.4328 0.7646 0.8938 0.2088  0.4785  -0.1612 323 ALA D CA  
14965 C C   . ALA D 323 ? 1.4655 0.7689 0.8880 0.2086  0.4600  -0.1787 323 ALA D C   
14966 O O   . ALA D 323 ? 1.4585 0.7527 0.8572 0.1992  0.4411  -0.1775 323 ALA D O   
14967 C CB  . ALA D 323 ? 1.4531 0.8014 0.8947 0.2146  0.4963  -0.1547 323 ALA D CB  
14968 N N   . GLU D 324 ? 1.5013 0.7921 0.9203 0.2177  0.4633  -0.1949 324 GLU D N   
14969 C CA  . GLU D 324 ? 1.5377 0.8007 0.9183 0.2172  0.4460  -0.2128 324 GLU D CA  
14970 C C   . GLU D 324 ? 1.5426 0.7823 0.9397 0.2096  0.4243  -0.2192 324 GLU D C   
14971 O O   . GLU D 324 ? 1.5730 0.7948 0.9419 0.2030  0.4023  -0.2293 324 GLU D O   
14972 C CB  . GLU D 324 ? 1.5856 0.8414 0.9600 0.2294  0.4556  -0.2291 324 GLU D CB  
14973 C CG  . GLU D 324 ? 1.5916 0.8714 0.9617 0.2375  0.4790  -0.2216 324 GLU D CG  
14974 C CD  . GLU D 324 ? 1.6030 0.8939 1.0207 0.2470  0.4976  -0.2226 324 GLU D CD  
14975 O OE1 . GLU D 324 ? 1.5493 0.8541 1.0128 0.2440  0.5027  -0.2106 324 GLU D OE1 
14976 O OE2 . GLU D 324 ? 1.6264 0.9128 1.0357 0.2575  0.5069  -0.2357 324 GLU D OE2 
14977 N N   . ASP D 325 ? 1.5803 0.8327 1.0327 0.2058  0.4214  -0.2087 325 ASP D N   
14978 C CA  . ASP D 325 ? 1.6029 0.8504 1.0822 0.1927  0.3912  -0.2057 325 ASP D CA  
14979 C C   . ASP D 325 ? 1.4718 0.7369 0.9436 0.1753  0.3708  -0.1885 325 ASP D C   
14980 O O   . ASP D 325 ? 1.4271 0.6834 0.8917 0.1630  0.3436  -0.1891 325 ASP D O   
14981 C CB  . ASP D 325 ? 1.5214 0.7763 1.0618 0.1961  0.3950  -0.2012 325 ASP D CB  
14982 C CG  . ASP D 325 ? 1.5031 0.7415 1.0561 0.2138  0.4139  -0.2182 325 ASP D CG  
14983 O OD1 . ASP D 325 ? 1.5119 0.7224 1.0403 0.2182  0.4071  -0.2358 325 ASP D OD1 
14984 O OD2 . ASP D 325 ? 1.4707 0.7239 1.0590 0.2232  0.4357  -0.2143 325 ASP D OD2 
14985 N N   . ALA D 326 ? 1.4035 0.6932 0.8777 0.1743  0.3842  -0.1731 326 ALA D N   
14986 C CA  . ALA D 326 ? 1.3683 0.6762 0.8378 0.1593  0.3669  -0.1565 326 ALA D CA  
14987 C C   . ALA D 326 ? 1.3917 0.6928 0.8077 0.1540  0.3539  -0.1604 326 ALA D C   
14988 O O   . ALA D 326 ? 1.3819 0.6861 0.7937 0.1398  0.3282  -0.1547 326 ALA D O   
14989 C CB  . ALA D 326 ? 1.3392 0.6721 0.8231 0.1610  0.3864  -0.1405 326 ALA D CB  
14990 N N   . VAL D 327 ? 1.4296 0.7226 0.8040 0.1652  0.3713  -0.1697 327 VAL D N   
14991 C CA  . VAL D 327 ? 1.4549 0.7430 0.7769 0.1610  0.3588  -0.1740 327 VAL D CA  
14992 C C   . VAL D 327 ? 1.5252 0.7919 0.8393 0.1526  0.3322  -0.1879 327 VAL D C   
14993 O O   . VAL D 327 ? 1.4719 0.7419 0.7666 0.1399  0.3091  -0.1848 327 VAL D O   
14994 C CB  . VAL D 327 ? 1.5217 0.8035 0.7997 0.1761  0.3833  -0.1825 327 VAL D CB  
14995 C CG1 . VAL D 327 ? 1.5126 0.7994 0.7396 0.1715  0.3720  -0.1799 327 VAL D CG1 
14996 C CG2 . VAL D 327 ? 1.4820 0.7794 0.7778 0.1861  0.4139  -0.1710 327 VAL D CG2 
14997 N N   . ARG D 328 ? 1.6547 0.8992 0.9851 0.1596  0.3352  -0.2033 328 ARG D N   
14998 C CA  . ARG D 328 ? 1.6988 0.9197 1.0254 0.1515  0.3104  -0.2166 328 ARG D CA  
14999 C C   . ARG D 328 ? 1.5931 0.8232 0.9526 0.1339  0.2843  -0.2028 328 ARG D C   
15000 O O   . ARG D 328 ? 1.4855 0.7085 0.8296 0.1207  0.2594  -0.2052 328 ARG D O   
15001 C CB  . ARG D 328 ? 1.5482 0.7433 0.8908 0.1641  0.3207  -0.2346 328 ARG D CB  
15002 C CG  . ARG D 328 ? 1.6022 0.7792 0.9019 0.1793  0.3390  -0.2544 328 ARG D CG  
15003 C CD  . ARG D 328 ? 1.6403 0.7851 0.9492 0.1871  0.3378  -0.2756 328 ARG D CD  
15004 N NE  . ARG D 328 ? 1.8701 1.0174 1.2357 0.1924  0.3452  -0.2703 328 ARG D NE  
15005 C CZ  . ARG D 328 ? 1.8845 1.0223 1.2862 0.1839  0.3245  -0.2680 328 ARG D CZ  
15006 N NH1 . ARG D 328 ? 1.9168 1.0410 1.3058 0.1688  0.2958  -0.2703 328 ARG D NH1 
15007 N NH2 . ARG D 328 ? 1.9079 1.0506 1.3602 0.1906  0.3327  -0.2626 328 ARG D NH2 
15008 N N   . ASP D 329 ? 1.4820 0.7287 0.8872 0.1333  0.2895  -0.1884 329 ASP D N   
15009 C CA  . ASP D 329 ? 1.4288 0.6864 0.8639 0.1173  0.2661  -0.1740 329 ASP D CA  
15010 C C   . ASP D 329 ? 1.3891 0.6673 0.8007 0.1046  0.2535  -0.1609 329 ASP D C   
15011 O O   . ASP D 329 ? 1.4073 0.6856 0.8195 0.0895  0.2285  -0.1565 329 ASP D O   
15012 C CB  . ASP D 329 ? 1.3609 0.6345 0.8463 0.1203  0.2759  -0.1616 329 ASP D CB  
15013 C CG  . ASP D 329 ? 1.3211 0.6088 0.8351 0.1045  0.2534  -0.1452 329 ASP D CG  
15014 O OD1 . ASP D 329 ? 1.2951 0.6048 0.7998 0.0954  0.2482  -0.1314 329 ASP D OD1 
15015 O OD2 . ASP D 329 ? 1.3361 0.6130 0.8815 0.1017  0.2413  -0.1459 329 ASP D OD2 
15016 N N   . PHE D 330 ? 1.3738 0.6698 0.7654 0.1108  0.2710  -0.1541 330 PHE D N   
15017 C CA  . PHE D 330 ? 1.3550 0.6724 0.7259 0.1010  0.2611  -0.1407 330 PHE D CA  
15018 C C   . PHE D 330 ? 1.4869 0.7940 0.8185 0.0930  0.2413  -0.1501 330 PHE D C   
15019 O O   . PHE D 330 ? 1.3853 0.7023 0.7183 0.0780  0.2187  -0.1419 330 PHE D O   
15020 C CB  . PHE D 330 ? 1.3512 0.6847 0.7059 0.1117  0.2861  -0.1330 330 PHE D CB  
15021 C CG  . PHE D 330 ? 1.3336 0.6894 0.6672 0.1045  0.2788  -0.1187 330 PHE D CG  
15022 C CD1 . PHE D 330 ? 1.3615 0.7155 0.6490 0.1033  0.2702  -0.1239 330 PHE D CD1 
15023 C CD2 . PHE D 330 ? 1.2908 0.6694 0.6506 0.0995  0.2803  -0.1006 330 PHE D CD2 
15024 C CE1 . PHE D 330 ? 1.3457 0.7215 0.6158 0.0979  0.2635  -0.1102 330 PHE D CE1 
15025 C CE2 . PHE D 330 ? 1.3143 0.7129 0.6558 0.0941  0.2743  -0.0876 330 PHE D CE2 
15026 C CZ  . PHE D 330 ? 1.4455 0.8432 0.7429 0.0936  0.2660  -0.0920 330 PHE D CZ  
15027 N N   . ILE D 331 ? 1.5430 0.8308 0.8394 0.1028  0.2494  -0.1677 331 ILE D N   
15028 C CA  . ILE D 331 ? 1.4633 0.7403 0.7218 0.0951  0.2298  -0.1789 331 ILE D CA  
15029 C C   . ILE D 331 ? 1.4677 0.7263 0.7462 0.0822  0.2054  -0.1858 331 ILE D C   
15030 O O   . ILE D 331 ? 1.4894 0.7478 0.7522 0.0684  0.1822  -0.1873 331 ILE D O   
15031 C CB  . ILE D 331 ? 1.5213 0.7806 0.7363 0.1094  0.2448  -0.1976 331 ILE D CB  
15032 C CG1 . ILE D 331 ? 1.5111 0.7859 0.7132 0.1241  0.2736  -0.1893 331 ILE D CG1 
15033 C CG2 . ILE D 331 ? 1.5746 0.8296 0.7458 0.1014  0.2248  -0.2069 331 ILE D CG2 
15034 C CD1 . ILE D 331 ? 1.5006 0.7996 0.6743 0.1207  0.2702  -0.1755 331 ILE D CD1 
15035 N N   . GLY D 332 ? 1.4637 0.7071 0.7781 0.0863  0.2100  -0.1896 332 GLY D N   
15036 C CA  . GLY D 332 ? 1.5555 0.7824 0.8939 0.0739  0.1872  -0.1922 332 GLY D CA  
15037 C C   . GLY D 332 ? 1.5051 0.7544 0.8662 0.0567  0.1681  -0.1720 332 GLY D C   
15038 O O   . GLY D 332 ? 1.4253 0.6654 0.7914 0.0419  0.1447  -0.1723 332 GLY D O   
15039 N N   . ARG D 333 ? 1.5345 0.8126 0.9101 0.0582  0.1785  -0.1542 333 ARG D N   
15040 C CA  . ARG D 333 ? 1.3973 0.6989 0.7903 0.0428  0.1620  -0.1352 333 ARG D CA  
15041 C C   . ARG D 333 ? 1.3641 0.6787 0.7230 0.0325  0.1479  -0.1328 333 ARG D C   
15042 O O   . ARG D 333 ? 1.3352 0.6571 0.7017 0.0161  0.1260  -0.1251 333 ARG D O   
15043 C CB  . ARG D 333 ? 1.2995 0.6265 0.7171 0.0481  0.1776  -0.1187 333 ARG D CB  
15044 C CG  . ARG D 333 ? 1.2886 0.6075 0.7459 0.0563  0.1887  -0.1191 333 ARG D CG  
15045 C CD  . ARG D 333 ? 1.2448 0.5828 0.7400 0.0473  0.1800  -0.1011 333 ARG D CD  
15046 N NE  . ARG D 333 ? 1.2298 0.5691 0.7608 0.0574  0.1952  -0.0994 333 ARG D NE  
15047 C CZ  . ARG D 333 ? 1.2005 0.5489 0.7692 0.0520  0.1872  -0.0882 333 ARG D CZ  
15048 N NH1 . ARG D 333 ? 1.1818 0.5393 0.7567 0.0369  0.1658  -0.0766 333 ARG D NH1 
15049 N NH2 . ARG D 333 ? 1.1912 0.5404 0.7922 0.0621  0.2008  -0.0886 333 ARG D NH2 
15050 N N   . LEU D 334 ? 1.4269 0.7457 0.7485 0.0419  0.1600  -0.1389 334 LEU D N   
15051 C CA  . LEU D 334 ? 1.4099 0.7420 0.6982 0.0334  0.1461  -0.1375 334 LEU D CA  
15052 C C   . LEU D 334 ? 1.4506 0.7606 0.7225 0.0231  0.1248  -0.1534 334 LEU D C   
15053 O O   . LEU D 334 ? 1.4494 0.7709 0.7146 0.0079  0.1038  -0.1487 334 LEU D O   
15054 C CB  . LEU D 334 ? 1.3947 0.7351 0.6451 0.0472  0.1640  -0.1400 334 LEU D CB  
15055 C CG  . LEU D 334 ? 1.3678 0.7276 0.6255 0.0589  0.1878  -0.1261 334 LEU D CG  
15056 C CD1 . LEU D 334 ? 1.4994 0.8514 0.7186 0.0753  0.2081  -0.1361 334 LEU D CD1 
15057 C CD2 . LEU D 334 ? 1.3334 0.7244 0.5934 0.0507  0.1797  -0.1068 334 LEU D CD2 
15058 N N   . LYS D 335 ? 1.4519 0.7303 0.7172 0.0311  0.1304  -0.1727 335 LYS D N   
15059 C CA  . LYS D 335 ? 1.4918 0.7458 0.7401 0.0215  0.1107  -0.1898 335 LYS D CA  
15060 C C   . LYS D 335 ? 1.5109 0.7623 0.7909 0.0024  0.0872  -0.1817 335 LYS D C   
15061 O O   . LYS D 335 ? 1.5757 0.8220 0.8430 -0.0124 0.0656  -0.1872 335 LYS D O   
15062 C CB  . LYS D 335 ? 1.5354 0.7540 0.7738 0.0349  0.1225  -0.2123 335 LYS D CB  
15063 C CG  . LYS D 335 ? 1.5260 0.7258 0.8060 0.0386  0.1273  -0.2126 335 LYS D CG  
15064 C CD  . LYS D 335 ? 1.5779 0.7375 0.8491 0.0435  0.1253  -0.2367 335 LYS D CD  
15065 C CE  . LYS D 335 ? 1.5814 0.7218 0.8745 0.0264  0.0998  -0.2375 335 LYS D CE  
15066 N NZ  . LYS D 335 ? 1.6379 0.7381 0.9126 0.0281  0.0935  -0.2630 335 LYS D NZ  
15067 N N   . LYS D 336 ? 1.5322 0.7882 0.8532 0.0020  0.0909  -0.1682 336 LYS D N   
15068 C CA  . LYS D 336 ? 1.4567 0.7139 0.8074 -0.0159 0.0699  -0.1568 336 LYS D CA  
15069 C C   . LYS D 336 ? 1.4612 0.7511 0.8064 -0.0306 0.0559  -0.1409 336 LYS D C   
15070 O O   . LYS D 336 ? 1.4504 0.7390 0.8008 -0.0485 0.0340  -0.1382 336 LYS D O   
15071 C CB  . LYS D 336 ? 1.4309 0.6896 0.8240 -0.0112 0.0780  -0.1447 336 LYS D CB  
15072 C CG  . LYS D 336 ? 1.4134 0.6363 0.8246 -0.0050 0.0793  -0.1575 336 LYS D CG  
15073 C CD  . LYS D 336 ? 1.3804 0.6086 0.8349 -0.0006 0.0855  -0.1442 336 LYS D CD  
15074 C CE  . LYS D 336 ? 1.3340 0.5949 0.8067 -0.0126 0.0771  -0.1208 336 LYS D CE  
15075 N NZ  . LYS D 336 ? 1.3352 0.5915 0.8164 -0.0326 0.0519  -0.1135 336 LYS D NZ  
15076 N N   . ILE D 337 ? 1.5020 0.8214 0.8380 -0.0234 0.0688  -0.1299 337 ILE D N   
15077 C CA  . ILE D 337 ? 1.4862 0.8383 0.8163 -0.0350 0.0574  -0.1151 337 ILE D CA  
15078 C C   . ILE D 337 ? 1.5119 0.8622 0.8086 -0.0436 0.0414  -0.1263 337 ILE D C   
15079 O O   . ILE D 337 ? 1.3705 0.7360 0.6708 -0.0606 0.0218  -0.1187 337 ILE D O   
15080 C CB  . ILE D 337 ? 1.3980 0.7779 0.7231 -0.0228 0.0766  -0.1027 337 ILE D CB  
15081 C CG1 . ILE D 337 ? 1.2910 0.6729 0.6514 -0.0157 0.0909  -0.0926 337 ILE D CG1 
15082 C CG2 . ILE D 337 ? 1.4763 0.8901 0.7951 -0.0329 0.0655  -0.0877 337 ILE D CG2 
15083 C CD1 . ILE D 337 ? 1.2686 0.6644 0.6227 0.0005  0.1154  -0.0874 337 ILE D CD1 
15084 N N   . HIS D 338 ? 1.5793 0.9119 0.8431 -0.0322 0.0496  -0.1448 338 HIS D N   
15085 C CA  . HIS D 338 ? 1.5218 0.8533 0.7503 -0.0389 0.0349  -0.1573 338 HIS D CA  
15086 C C   . HIS D 338 ? 1.6030 0.9134 0.8402 -0.0574 0.0108  -0.1668 338 HIS D C   
15087 O O   . HIS D 338 ? 1.6541 0.9724 0.8736 -0.0702 -0.0079 -0.1710 338 HIS D O   
15088 C CB  . HIS D 338 ? 1.5813 0.8955 0.7721 -0.0210 0.0508  -0.1759 338 HIS D CB  
15089 C CG  . HIS D 338 ? 1.6060 0.9145 0.7576 -0.0264 0.0357  -0.1922 338 HIS D CG  
15090 N ND1 . HIS D 338 ? 1.6800 0.9562 0.8237 -0.0338 0.0220  -0.2129 338 HIS D ND1 
15091 C CD2 . HIS D 338 ? 1.5575 0.8882 0.6751 -0.0248 0.0319  -0.1914 338 HIS D CD2 
15092 C CE1 . HIS D 338 ? 1.6672 0.9465 0.7737 -0.0376 0.0097  -0.2249 338 HIS D CE1 
15093 N NE2 . HIS D 338 ? 1.6229 0.9360 0.7129 -0.0320 0.0152  -0.2118 338 HIS D NE2 
15094 N N   . GLU D 339 ? 1.5760 0.8597 0.8412 -0.0592 0.0104  -0.1697 339 GLU D N   
15095 C CA  . GLU D 339 ? 1.5722 0.8299 0.8469 -0.0756 -0.0107 -0.1790 339 GLU D CA  
15096 C C   . GLU D 339 ? 1.5698 0.8383 0.8825 -0.0931 -0.0248 -0.1596 339 GLU D C   
15097 O O   . GLU D 339 ? 1.5221 0.7714 0.8442 -0.1092 -0.0435 -0.1642 339 GLU D O   
15098 C CB  . GLU D 339 ? 1.5390 0.7537 0.8163 -0.0648 -0.0023 -0.1978 339 GLU D CB  
15099 C CG  . GLU D 339 ? 1.5530 0.7672 0.8582 -0.0499 0.0182  -0.1883 339 GLU D CG  
15100 C CD  . GLU D 339 ? 1.6370 0.8134 0.9649 -0.0466 0.0186  -0.1979 339 GLU D CD  
15101 O OE1 . GLU D 339 ? 1.5762 0.7206 0.8843 -0.0398 0.0204  -0.2205 339 GLU D OE1 
15102 O OE2 . GLU D 339 ? 1.6354 0.8141 1.0004 -0.0496 0.0174  -0.1828 339 GLU D OE2 
15103 N N   . SER D 340 ? 1.5274 0.8248 0.8614 -0.0906 -0.0163 -0.1383 340 SER D N   
15104 C CA  . SER D 340 ? 1.5334 0.8423 0.9017 -0.1059 -0.0282 -0.1192 340 SER D CA  
15105 C C   . SER D 340 ? 1.4756 0.8186 0.8409 -0.1226 -0.0434 -0.1061 340 SER D C   
15106 O O   . SER D 340 ? 1.3560 0.7095 0.7471 -0.1375 -0.0548 -0.0905 340 SER D O   
15107 C CB  . SER D 340 ? 1.5618 0.8836 0.9564 -0.0950 -0.0119 -0.1035 340 SER D CB  
15108 O OG  . SER D 340 ? 1.7526 1.0535 1.1452 -0.0756 0.0072  -0.1151 340 SER D OG  
15109 N N   . VAL D 341 ? 1.5249 0.8865 0.8596 -0.1200 -0.0437 -0.1115 341 VAL D N   
15110 C CA  . VAL D 341 ? 1.4453 0.8445 0.7776 -0.1326 -0.0556 -0.0983 341 VAL D CA  
15111 C C   . VAL D 341 ? 1.4063 0.8035 0.7090 -0.1406 -0.0707 -0.1140 341 VAL D C   
15112 O O   . VAL D 341 ? 1.4441 0.8166 0.7200 -0.1312 -0.0668 -0.1344 341 VAL D O   
15113 C CB  . VAL D 341 ? 1.3305 0.7649 0.6584 -0.1193 -0.0393 -0.0839 341 VAL D CB  
15114 C CG1 . VAL D 341 ? 1.2998 0.7304 0.6521 -0.1078 -0.0216 -0.0739 341 VAL D CG1 
15115 C CG2 . VAL D 341 ? 1.4246 0.8611 0.7143 -0.1040 -0.0291 -0.0961 341 VAL D CG2 
15116 N N   . ASP D 342 ? 1.5319 0.9563 0.8397 -0.1582 -0.0883 -0.1045 342 ASP D N   
15117 C CA  . ASP D 342 ? 1.5613 0.9885 0.8459 -0.1694 -0.1064 -0.1176 342 ASP D CA  
15118 C C   . ASP D 342 ? 1.5631 1.0276 0.8228 -0.1614 -0.1039 -0.1135 342 ASP D C   
15119 O O   . ASP D 342 ? 1.5012 0.9886 0.7546 -0.1747 -0.1214 -0.1129 342 ASP D O   
15120 C CB  . ASP D 342 ? 1.4874 0.9196 0.7960 -0.1959 -0.1292 -0.1110 342 ASP D CB  
15121 C CG  . ASP D 342 ? 1.4547 0.9294 0.7877 -0.2042 -0.1309 -0.0851 342 ASP D CG  
15122 O OD1 . ASP D 342 ? 1.3930 0.8710 0.7480 -0.1983 -0.1185 -0.0702 342 ASP D OD1 
15123 O OD2 . ASP D 342 ? 1.4043 0.9100 0.7345 -0.2164 -0.1448 -0.0803 342 ASP D OD2 
15124 N N   . PHE D 343 ? 1.5630 1.0343 0.8092 -0.1397 -0.0823 -0.1101 343 PHE D N   
15125 C CA  . PHE D 343 ? 1.4794 0.9852 0.7033 -0.1297 -0.0773 -0.1032 343 PHE D CA  
15126 C C   . PHE D 343 ? 1.4647 0.9591 0.6667 -0.1048 -0.0525 -0.1080 343 PHE D C   
15127 O O   . PHE D 343 ? 1.4492 0.9127 0.6566 -0.0963 -0.0396 -0.1160 343 PHE D O   
15128 C CB  . PHE D 343 ? 1.3524 0.8991 0.6011 -0.1355 -0.0783 -0.0785 343 PHE D CB  
15129 C CG  . PHE D 343 ? 1.3568 0.9000 0.6383 -0.1334 -0.0657 -0.0641 343 PHE D CG  
15130 C CD1 . PHE D 343 ? 1.3116 0.8370 0.6220 -0.1483 -0.0747 -0.0620 343 PHE D CD1 
15131 C CD2 . PHE D 343 ? 1.3376 0.8969 0.6213 -0.1171 -0.0457 -0.0515 343 PHE D CD2 
15132 C CE1 . PHE D 343 ? 1.2783 0.8027 0.6173 -0.1459 -0.0642 -0.0483 343 PHE D CE1 
15133 C CE2 . PHE D 343 ? 1.2526 0.8100 0.5656 -0.1155 -0.0352 -0.0392 343 PHE D CE2 
15134 C CZ  . PHE D 343 ? 1.3107 0.8515 0.6508 -0.1296 -0.0448 -0.0376 343 PHE D CZ  
15135 N N   . GLN D 344 ? 1.3984 0.9190 0.5769 -0.0930 -0.0456 -0.1023 344 GLN D N   
15136 C CA  . GLN D 344 ? 1.4150 0.9276 0.5709 -0.0698 -0.0215 -0.1048 344 GLN D CA  
15137 C C   . GLN D 344 ? 1.5029 1.0281 0.6851 -0.0613 -0.0027 -0.0857 344 GLN D C   
15138 O O   . GLN D 344 ? 1.4511 1.0096 0.6449 -0.0641 -0.0049 -0.0679 344 GLN D O   
15139 C CB  . GLN D 344 ? 1.4860 1.0194 0.6038 -0.0606 -0.0226 -0.1062 344 GLN D CB  
15140 C CG  . GLN D 344 ? 1.5098 1.0274 0.5969 -0.0664 -0.0392 -0.1280 344 GLN D CG  
15141 C CD  . GLN D 344 ? 1.5563 1.0911 0.6011 -0.0551 -0.0398 -0.1310 344 GLN D CD  
15142 O OE1 . GLN D 344 ? 1.5603 1.0746 0.5697 -0.0483 -0.0399 -0.1501 344 GLN D OE1 
15143 N NE2 . GLN D 344 ? 1.5142 1.0869 0.5614 -0.0521 -0.0400 -0.1122 344 GLN D NE2 
15144 N N   . PRO D 345 ? 1.5251 1.0261 0.7180 -0.0509 0.0157  -0.0889 345 PRO D N   
15145 C CA  . PRO D 345 ? 1.3499 0.8622 0.5707 -0.0448 0.0317  -0.0718 345 PRO D CA  
15146 C C   . PRO D 345 ? 1.4003 0.9283 0.6020 -0.0264 0.0519  -0.0638 345 PRO D C   
15147 O O   . PRO D 345 ? 1.5289 1.0556 0.6947 -0.0163 0.0559  -0.0717 345 PRO D O   
15148 C CB  . PRO D 345 ? 1.3145 0.7931 0.5528 -0.0409 0.0418  -0.0811 345 PRO D CB  
15149 C CG  . PRO D 345 ? 1.4465 0.8988 0.6515 -0.0327 0.0446  -0.1027 345 PRO D CG  
15150 C CD  . PRO D 345 ? 1.5340 0.9965 0.7143 -0.0438 0.0228  -0.1092 345 PRO D CD  
15151 N N   . VAL D 346 ? 1.3789 0.9212 0.6049 -0.0223 0.0644  -0.0476 346 VAL D N   
15152 C CA  . VAL D 346 ? 1.2530 0.8038 0.4672 -0.0044 0.0871  -0.0397 346 VAL D CA  
15153 C C   . VAL D 346 ? 1.2254 0.7670 0.4707 0.0007  0.1045  -0.0339 346 VAL D C   
15154 O O   . VAL D 346 ? 1.1897 0.7465 0.4645 -0.0061 0.1021  -0.0206 346 VAL D O   
15155 C CB  . VAL D 346 ? 1.2358 0.8218 0.4421 -0.0038 0.0831  -0.0240 346 VAL D CB  
15156 C CG1 . VAL D 346 ? 1.1954 0.8040 0.4363 -0.0164 0.0737  -0.0086 346 VAL D CG1 
15157 C CG2 . VAL D 346 ? 1.2347 0.8253 0.4240 0.0155  0.1066  -0.0169 346 VAL D CG2 
15158 N N   . VAL D 347 ? 1.2433 0.7603 0.4827 0.0126  0.1218  -0.0445 347 VAL D N   
15159 C CA  . VAL D 347 ? 1.2211 0.7283 0.4913 0.0176  0.1378  -0.0412 347 VAL D CA  
15160 C C   . VAL D 347 ? 1.2676 0.7873 0.5338 0.0316  0.1604  -0.0301 347 VAL D C   
15161 O O   . VAL D 347 ? 1.2889 0.8024 0.5263 0.0449  0.1752  -0.0347 347 VAL D O   
15162 C CB  . VAL D 347 ? 1.2713 0.7462 0.5420 0.0229  0.1451  -0.0584 347 VAL D CB  
15163 C CG1 . VAL D 347 ? 1.3230 0.7914 0.6256 0.0300  0.1633  -0.0544 347 VAL D CG1 
15164 C CG2 . VAL D 347 ? 1.2829 0.7427 0.5610 0.0086  0.1226  -0.0687 347 VAL D CG2 
15165 N N   . PHE D 348 ? 1.2635 0.7999 0.5579 0.0285  0.1633  -0.0155 348 PHE D N   
15166 C CA  . PHE D 348 ? 1.1523 0.6997 0.4477 0.0401  0.1839  -0.0043 348 PHE D CA  
15167 C C   . PHE D 348 ? 1.1405 0.6740 0.4635 0.0458  0.2018  -0.0060 348 PHE D C   
15168 O O   . PHE D 348 ? 1.1214 0.6517 0.4763 0.0373  0.1944  -0.0060 348 PHE D O   
15169 C CB  . PHE D 348 ? 1.1205 0.6957 0.4277 0.0338  0.1761  0.0120  348 PHE D CB  
15170 C CG  . PHE D 348 ? 1.1298 0.7215 0.4072 0.0414  0.1790  0.0194  348 PHE D CG  
15171 C CD1 . PHE D 348 ? 1.1514 0.7540 0.4064 0.0356  0.1604  0.0174  348 PHE D CD1 
15172 C CD2 . PHE D 348 ? 1.1237 0.7203 0.3965 0.0543  0.1998  0.0287  348 PHE D CD2 
15173 C CE1 . PHE D 348 ? 1.1564 0.7753 0.3840 0.0435  0.1618  0.0244  348 PHE D CE1 
15174 C CE2 . PHE D 348 ? 1.1345 0.7455 0.3794 0.0624  0.2020  0.0366  348 PHE D CE2 
15175 C CZ  . PHE D 348 ? 1.1727 0.7957 0.3949 0.0575  0.1826  0.0346  348 PHE D CZ  
15176 N N   . VAL D 349 ? 1.1532 0.6794 0.4642 0.0601  0.2253  -0.0069 349 VAL D N   
15177 C CA  . VAL D 349 ? 1.1449 0.6597 0.4817 0.0666  0.2447  -0.0088 349 VAL D CA  
15178 C C   . VAL D 349 ? 1.1612 0.6888 0.5010 0.0744  0.2634  0.0045  349 VAL D C   
15179 O O   . VAL D 349 ? 1.1522 0.6765 0.4660 0.0863  0.2804  0.0056  349 VAL D O   
15180 C CB  . VAL D 349 ? 1.1799 0.6712 0.5019 0.0765  0.2577  -0.0239 349 VAL D CB  
15181 C CG1 . VAL D 349 ? 1.1693 0.6519 0.5232 0.0825  0.2772  -0.0253 349 VAL D CG1 
15182 C CG2 . VAL D 349 ? 1.2007 0.6775 0.5156 0.0689  0.2381  -0.0379 349 VAL D CG2 
15183 N N   . VAL D 350 ? 1.1072 0.6484 0.4775 0.0679  0.2603  0.0147  350 VAL D N   
15184 C CA  . VAL D 350 ? 1.0766 0.6294 0.4532 0.0735  0.2759  0.0272  350 VAL D CA  
15185 C C   . VAL D 350 ? 1.0553 0.6043 0.4716 0.0726  0.2869  0.0274  350 VAL D C   
15186 O O   . VAL D 350 ? 1.1523 0.7035 0.5965 0.0628  0.2732  0.0259  350 VAL D O   
15187 C CB  . VAL D 350 ? 1.0557 0.6308 0.4302 0.0668  0.2617  0.0393  350 VAL D CB  
15188 C CG1 . VAL D 350 ? 1.0474 0.6310 0.4197 0.0753  0.2793  0.0512  350 VAL D CG1 
15189 C CG2 . VAL D 350 ? 1.1078 0.6891 0.4504 0.0641  0.2446  0.0375  350 VAL D CG2 
15190 N N   . LEU D 351 ? 1.0602 0.6042 0.4793 0.0825  0.3113  0.0299  351 LEU D N   
15191 C CA  . LEU D 351 ? 1.0415 0.5838 0.4992 0.0821  0.3235  0.0302  351 LEU D CA  
15192 C C   . LEU D 351 ? 1.0493 0.5895 0.5022 0.0925  0.3502  0.0366  351 LEU D C   
15193 O O   . LEU D 351 ? 1.0709 0.6093 0.4895 0.1008  0.3590  0.0406  351 LEU D O   
15194 C CB  . LEU D 351 ? 1.0496 0.5777 0.5266 0.0819  0.3237  0.0176  351 LEU D CB  
15195 C CG  . LEU D 351 ? 1.0844 0.5958 0.5404 0.0935  0.3412  0.0083  351 LEU D CG  
15196 C CD1 . LEU D 351 ? 1.0837 0.5860 0.5732 0.0967  0.3543  0.0006  351 LEU D CD1 
15197 C CD2 . LEU D 351 ? 1.1092 0.6117 0.5344 0.0924  0.3255  -0.0011 351 LEU D CD2 
15198 N N   . ASP D 352 ? 1.0332 0.5736 0.5212 0.0918  0.3628  0.0378  352 ASP D N   
15199 C CA  . ASP D 352 ? 1.0453 0.5825 0.5356 0.1000  0.3893  0.0439  352 ASP D CA  
15200 C C   . ASP D 352 ? 1.0682 0.5921 0.5516 0.1093  0.4057  0.0361  352 ASP D C   
15201 O O   . ASP D 352 ? 1.0685 0.5853 0.5768 0.1100  0.4166  0.0286  352 ASP D O   
15202 C CB  . ASP D 352 ? 1.1114 0.6550 0.6451 0.0942  0.3942  0.0468  352 ASP D CB  
15203 C CG  . ASP D 352 ? 1.2358 0.7940 0.7812 0.0840  0.3736  0.0523  352 ASP D CG  
15204 O OD1 . ASP D 352 ? 1.1946 0.7579 0.7269 0.0787  0.3518  0.0508  352 ASP D OD1 
15205 O OD2 . ASP D 352 ? 1.3109 0.8755 0.8787 0.0811  0.3794  0.0578  352 ASP D OD2 
15206 N N   . GLY D 353 ? 1.0899 0.6149 0.5466 0.1157  0.4025  0.0379  353 GLY D N   
15207 C CA  . GLY D 353 ? 1.1188 0.6335 0.5671 0.1243  0.4155  0.0315  353 GLY D CA  
15208 C C   . GLY D 353 ? 1.1213 0.6384 0.5922 0.1288  0.4324  0.0382  353 GLY D C   
15209 O O   . GLY D 353 ? 1.1763 0.6923 0.6301 0.1361  0.4376  0.0405  353 GLY D O   
15210 N N   . GLU D 354 ? 1.0985 0.6186 0.6066 0.1241  0.4410  0.0415  354 GLU D N   
15211 C CA  . GLU D 354 ? 1.1026 0.6225 0.6348 0.1269  0.4583  0.0469  354 GLU D CA  
15212 C C   . GLU D 354 ? 1.0901 0.6079 0.6627 0.1233  0.4724  0.0419  354 GLU D C   
15213 O O   . GLU D 354 ? 1.1023 0.6176 0.6919 0.1267  0.4889  0.0426  354 GLU D O   
15214 C CB  . GLU D 354 ? 1.2115 0.7399 0.7498 0.1251  0.4543  0.0592  354 GLU D CB  
15215 C CG  . GLU D 354 ? 1.2586 0.7957 0.8077 0.1168  0.4409  0.0617  354 GLU D CG  
15216 C CD  . GLU D 354 ? 1.2669 0.8061 0.8542 0.1114  0.4503  0.0652  354 GLU D CD  
15217 O OE1 . GLU D 354 ? 1.3723 0.9061 0.9804 0.1132  0.4675  0.0650  354 GLU D OE1 
15218 O OE2 . GLU D 354 ? 1.2413 0.7881 0.8376 0.1052  0.4404  0.0683  354 GLU D OE2 
15219 N N   . ASN D 355 ? 1.0679 0.5874 0.6571 0.1169  0.4670  0.0367  355 ASN D N   
15220 C CA  . ASN D 355 ? 1.0507 0.5730 0.6842 0.1126  0.4786  0.0338  355 ASN D CA  
15221 C C   . ASN D 355 ? 1.0973 0.6135 0.7443 0.1150  0.4833  0.0202  355 ASN D C   
15222 O O   . ASN D 355 ? 1.1899 0.7122 0.8807 0.1112  0.4867  0.0167  355 ASN D O   
15223 C CB  . ASN D 355 ? 1.0210 0.5523 0.6699 0.1036  0.4698  0.0391  355 ASN D CB  
15224 C CG  . ASN D 355 ? 1.1847 0.7179 0.8044 0.1002  0.4490  0.0397  355 ASN D CG  
15225 O OD1 . ASN D 355 ? 1.2458 0.7832 0.8414 0.1005  0.4391  0.0477  355 ASN D OD1 
15226 N ND2 . ASN D 355 ? 1.2282 0.7644 0.8629 0.0944  0.4282  0.0318  355 ASN D ND2 
15227 N N   . CYS D 356 ? 1.0739 0.5805 0.6905 0.1201  0.4761  0.0124  356 CYS D N   
15228 C CA  . CYS D 356 ? 1.0775 0.5796 0.7125 0.1211  0.4686  -0.0003 356 CYS D CA  
15229 C C   . CYS D 356 ? 1.1880 0.6793 0.8163 0.1331  0.4930  -0.0079 356 CYS D C   
15230 O O   . CYS D 356 ? 1.3418 0.8314 0.9984 0.1353  0.4941  -0.0176 356 CYS D O   
15231 C CB  . CYS D 356 ? 1.0793 0.5768 0.6895 0.1173  0.4411  -0.0054 356 CYS D CB  
15232 S SG  . CYS D 356 ? 1.2331 0.7203 0.7786 0.1243  0.4416  -0.0052 356 CYS D SG  
15233 N N   . TRP D 357 ? 1.1542 0.6462 0.7570 0.1369  0.4979  -0.0008 357 TRP D N   
15234 C CA  . TRP D 357 ? 1.1608 0.6478 0.7579 0.1453  0.5106  -0.0059 357 TRP D CA  
15235 C C   . TRP D 357 ? 1.1572 0.6517 0.7985 0.1458  0.5294  -0.0041 357 TRP D C   
15236 O O   . TRP D 357 ? 1.1813 0.6730 0.8241 0.1527  0.5412  -0.0096 357 TRP D O   
15237 C CB  . TRP D 357 ? 1.1849 0.6711 0.7419 0.1494  0.5093  0.0018  357 TRP D CB  
15238 C CG  . TRP D 357 ? 1.1829 0.6671 0.7033 0.1471  0.4900  0.0029  357 TRP D CG  
15239 C CD1 . TRP D 357 ? 1.1683 0.6608 0.6787 0.1426  0.4801  0.0150  357 TRP D CD1 
15240 C CD2 . TRP D 357 ? 1.1968 0.6703 0.6867 0.1488  0.4773  -0.0089 357 TRP D CD2 
15241 N NE1 . TRP D 357 ? 1.1707 0.6611 0.6475 0.1411  0.4620  0.0123  357 TRP D NE1 
15242 C CE2 . TRP D 357 ? 1.1891 0.6668 0.6514 0.1444  0.4602  -0.0024 357 TRP D CE2 
15243 C CE3 . TRP D 357 ? 1.2167 0.6764 0.7006 0.1537  0.4782  -0.0251 357 TRP D CE3 
15244 C CZ2 . TRP D 357 ? 1.2118 0.6807 0.6398 0.1436  0.4444  -0.0111 357 TRP D CZ2 
15245 C CZ3 . TRP D 357 ? 1.2628 0.7106 0.7115 0.1534  0.4623  -0.0346 357 TRP D CZ3 
15246 C CH2 . TRP D 357 ? 1.2580 0.7106 0.6786 0.1478  0.4458  -0.0274 357 TRP D CH2 
15247 N N   . GLU D 358 ? 1.1318 0.6361 0.8085 0.1384  0.5325  0.0029  358 GLU D N   
15248 C CA  . GLU D 358 ? 1.1256 0.6379 0.8480 0.1377  0.5493  0.0032  358 GLU D CA  
15249 C C   . GLU D 358 ? 1.1156 0.6297 0.8737 0.1393  0.5499  -0.0097 358 GLU D C   
15250 O O   . GLU D 358 ? 1.1318 0.6547 0.9312 0.1395  0.5631  -0.0110 358 GLU D O   
15251 C CB  . GLU D 358 ? 1.1736 0.6951 0.9221 0.1288  0.5523  0.0144  358 GLU D CB  
15252 C CG  . GLU D 358 ? 1.1245 0.6497 0.8785 0.1214  0.5375  0.0149  358 GLU D CG  
15253 C CD  . GLU D 358 ? 1.0997 0.6249 0.8290 0.1172  0.5295  0.0270  358 GLU D CD  
15254 O OE1 . GLU D 358 ? 1.1672 0.6864 0.8537 0.1214  0.5207  0.0298  358 GLU D OE1 
15255 O OE2 . GLU D 358 ? 1.0860 0.6178 0.8402 0.1101  0.5314  0.0332  358 GLU D OE2 
15256 N N   . TYR D 359 ? 1.1112 0.6167 0.8557 0.1409  0.5352  -0.0191 359 TYR D N   
15257 C CA  . TYR D 359 ? 1.1070 0.6095 0.8818 0.1449  0.5326  -0.0324 359 TYR D CA  
15258 C C   . TYR D 359 ? 1.1912 0.6791 0.9394 0.1544  0.5309  -0.0441 359 TYR D C   
15259 O O   . TYR D 359 ? 1.1393 0.6237 0.9124 0.1582  0.5257  -0.0548 359 TYR D O   
15260 C CB  . TYR D 359 ? 1.0751 0.5846 0.8659 0.1330  0.4996  -0.0306 359 TYR D CB  
15261 C CG  . TYR D 359 ? 1.0444 0.5697 0.8636 0.1225  0.4970  -0.0202 359 TYR D CG  
15262 C CD1 . TYR D 359 ? 1.0381 0.5643 0.8296 0.1174  0.4955  -0.0098 359 TYR D CD1 
15263 C CD2 . TYR D 359 ? 1.0237 0.5630 0.8975 0.1181  0.4959  -0.0214 359 TYR D CD2 
15264 C CE1 . TYR D 359 ? 1.0534 0.5922 0.8699 0.1082  0.4935  -0.0016 359 TYR D CE1 
15265 C CE2 . TYR D 359 ? 0.9983 0.5513 0.8971 0.1081  0.4930  -0.0135 359 TYR D CE2 
15266 C CZ  . TYR D 359 ? 1.0079 0.5596 0.8773 0.1032  0.4922  -0.0040 359 TYR D CZ  
15267 O OH  . TYR D 359 ? 1.0389 0.6022 0.9320 0.0936  0.4895  0.0026  359 TYR D OH  
15268 N N   . TYR D 360 ? 1.2990 0.7798 0.9994 0.1574  0.5314  -0.0416 360 TYR D N   
15269 C CA  . TYR D 360 ? 1.1988 0.6668 0.8715 0.1665  0.5320  -0.0528 360 TYR D CA  
15270 C C   . TYR D 360 ? 1.2194 0.6950 0.9080 0.1727  0.5520  -0.0523 360 TYR D C   
15271 O O   . TYR D 360 ? 1.2853 0.7743 0.9971 0.1692  0.5649  -0.0415 360 TYR D O   
15272 C CB  . TYR D 360 ? 1.2237 0.6822 0.8379 0.1671  0.5225  -0.0508 360 TYR D CB  
15273 C CG  . TYR D 360 ? 1.2320 0.6788 0.8214 0.1628  0.5022  -0.0555 360 TYR D CG  
15274 C CD1 . TYR D 360 ? 1.2123 0.6675 0.8326 0.1525  0.4854  -0.0510 360 TYR D CD1 
15275 C CD2 . TYR D 360 ? 1.2374 0.6708 0.7775 0.1655  0.4915  -0.0620 360 TYR D CD2 
15276 C CE1 . TYR D 360 ? 1.1621 0.6158 0.7680 0.1433  0.4556  -0.0506 360 TYR D CE1 
15277 C CE2 . TYR D 360 ? 1.2272 0.6559 0.7510 0.1575  0.4652  -0.0636 360 TYR D CE2 
15278 C CZ  . TYR D 360 ? 1.1884 0.6291 0.7473 0.1455  0.4459  -0.0566 360 TYR D CZ  
15279 O OH  . TYR D 360 ? 1.1776 0.6179 0.7241 0.1354  0.4168  -0.0559 360 TYR D OH  
15280 N N   . GLU D 361 ? 1.3062 0.7721 0.9807 0.1818  0.5546  -0.0646 361 GLU D N   
15281 C CA  . GLU D 361 ? 1.3890 0.8613 1.0727 0.1888  0.5739  -0.0653 361 GLU D CA  
15282 C C   . GLU D 361 ? 1.4126 0.8845 1.0540 0.1901  0.5803  -0.0560 361 GLU D C   
15283 O O   . GLU D 361 ? 1.3750 0.8354 0.9692 0.1928  0.5701  -0.0598 361 GLU D O   
15284 C CB  . GLU D 361 ? 1.5167 0.9786 1.1998 0.1988  0.5740  -0.0825 361 GLU D CB  
15285 C CG  . GLU D 361 ? 1.5663 1.0292 1.2976 0.1995  0.5684  -0.0912 361 GLU D CG  
15286 C CD  . GLU D 361 ? 1.7474 1.2302 1.5337 0.1999  0.5850  -0.0869 361 GLU D CD  
15287 O OE1 . GLU D 361 ? 1.7817 1.2758 1.5686 0.1988  0.6017  -0.0771 361 GLU D OE1 
15288 O OE2 . GLU D 361 ? 1.8445 1.3313 1.6745 0.2013  0.5807  -0.0933 361 GLU D OE2 
15289 N N   . GLU D 362 ? 1.4378 0.9216 1.0973 0.1883  0.5965  -0.0440 362 GLU D N   
15290 C CA  . GLU D 362 ? 1.4246 0.9081 1.0503 0.1901  0.6039  -0.0334 362 GLU D CA  
15291 C C   . GLU D 362 ? 1.3146 0.7931 0.9019 0.1857  0.5870  -0.0260 362 GLU D C   
15292 O O   . GLU D 362 ? 1.3404 0.8143 0.8856 0.1899  0.5851  -0.0231 362 GLU D O   
15293 C CB  . GLU D 362 ? 1.3664 0.8444 0.9663 0.2012  0.6143  -0.0422 362 GLU D CB  
15294 C CG  . GLU D 362 ? 1.3942 0.8589 0.9399 0.2069  0.6017  -0.0512 362 GLU D CG  
15295 C CD  . GLU D 362 ? 1.5118 0.9743 1.0293 0.2168  0.6152  -0.0547 362 GLU D CD  
15296 O OE1 . GLU D 362 ? 1.5936 1.0566 1.1277 0.2236  0.6274  -0.0649 362 GLU D OE1 
15297 O OE2 . GLU D 362 ? 1.6257 1.0867 1.1051 0.2182  0.6136  -0.0469 362 GLU D OE2 
15298 N N   . ASN D 363 ? 1.2786 0.7599 0.8830 0.1771  0.5750  -0.0224 363 ASN D N   
15299 C CA  . ASN D 363 ? 1.2658 0.7461 0.8427 0.1718  0.5598  -0.0134 363 ASN D CA  
15300 C C   . ASN D 363 ? 1.3269 0.7963 0.8581 0.1751  0.5432  -0.0224 363 ASN D C   
15301 O O   . ASN D 363 ? 1.4377 0.9065 0.9327 0.1752  0.5342  -0.0161 363 ASN D O   
15302 C CB  . ASN D 363 ? 1.3544 0.8394 0.9202 0.1718  0.5677  0.0020  363 ASN D CB  
15303 C CG  . ASN D 363 ? 1.4218 0.9088 0.9700 0.1662  0.5525  0.0124  363 ASN D CG  
15304 O OD1 . ASN D 363 ? 1.4266 0.9103 0.9340 0.1694  0.5416  0.0137  363 ASN D OD1 
15305 N ND2 . ASN D 363 ? 1.2849 0.7781 0.8647 0.1580  0.5506  0.0187  363 ASN D ND2 
15306 N N   . GLY D 364 ? 1.3226 0.7830 0.8569 0.1778  0.5384  -0.0379 364 GLY D N   
15307 C CA  . GLY D 364 ? 1.3411 0.7889 0.8364 0.1787  0.5208  -0.0477 364 GLY D CA  
15308 C C   . GLY D 364 ? 1.3593 0.8018 0.8065 0.1853  0.5195  -0.0502 364 GLY D C   
15309 O O   . GLY D 364 ? 1.3485 0.7826 0.7587 0.1847  0.5034  -0.0561 364 GLY D O   
15310 N N   . ILE D 365 ? 1.4357 0.8834 0.8826 0.1914  0.5362  -0.0459 365 ILE D N   
15311 C CA  . ILE D 365 ? 1.4350 0.8783 0.8368 0.1988  0.5363  -0.0492 365 ILE D CA  
15312 C C   . ILE D 365 ? 1.4403 0.8686 0.8200 0.2044  0.5300  -0.0696 365 ILE D C   
15313 O O   . ILE D 365 ? 1.4492 0.8705 0.7859 0.2055  0.5163  -0.0752 365 ILE D O   
15314 C CB  . ILE D 365 ? 1.4459 0.8967 0.8540 0.2044  0.5572  -0.0409 365 ILE D CB  
15315 C CG1 . ILE D 365 ? 1.3974 0.8592 0.8225 0.1987  0.5612  -0.0213 365 ILE D CG1 
15316 C CG2 . ILE D 365 ? 1.4803 0.9266 0.8412 0.2129  0.5580  -0.0456 365 ILE D CG2 
15317 C CD1 . ILE D 365 ? 1.4057 0.8698 0.7935 0.1988  0.5502  -0.0114 365 ILE D CD1 
15318 N N   . PRO D 366 ? 1.4318 0.8544 0.8390 0.2081  0.5382  -0.0817 366 PRO D N   
15319 C CA  . PRO D 366 ? 1.4602 0.8655 0.8455 0.2135  0.5299  -0.1021 366 PRO D CA  
15320 C C   . PRO D 366 ? 1.4497 0.8414 0.8169 0.2071  0.5068  -0.1096 366 PRO D C   
15321 O O   . PRO D 366 ? 1.4805 0.8584 0.8087 0.2097  0.4957  -0.1225 366 PRO D O   
15322 C CB  . PRO D 366 ? 1.4592 0.8638 0.8877 0.2185  0.5433  -0.1109 366 PRO D CB  
15323 C CG  . PRO D 366 ? 1.4210 0.8418 0.8960 0.2127  0.5529  -0.0960 366 PRO D CG  
15324 C CD  . PRO D 366 ? 1.4180 0.8500 0.8748 0.2093  0.5564  -0.0784 366 PRO D CD  
15325 N N   . PHE D 367 ? 1.4234 0.8180 0.8162 0.1985  0.4989  -0.1027 367 PHE D N   
15326 C CA  . PHE D 367 ? 1.4450 0.8263 0.8180 0.1918  0.4772  -0.1089 367 PHE D CA  
15327 C C   . PHE D 367 ? 1.4996 0.8849 0.8263 0.1884  0.4649  -0.1020 367 PHE D C   
15328 O O   . PHE D 367 ? 1.6021 0.9734 0.8925 0.1873  0.4491  -0.1134 367 PHE D O   
15329 C CB  . PHE D 367 ? 1.3585 0.7440 0.7693 0.1838  0.4731  -0.1017 367 PHE D CB  
15330 C CG  . PHE D 367 ? 1.4277 0.8033 0.8183 0.1751  0.4511  -0.1037 367 PHE D CG  
15331 C CD1 . PHE D 367 ? 1.4551 0.8166 0.8480 0.1707  0.4289  -0.1168 367 PHE D CD1 
15332 C CD2 . PHE D 367 ? 1.5218 0.9133 0.9060 0.1664  0.4419  -0.0876 367 PHE D CD2 
15333 C CE1 . PHE D 367 ? 1.3973 0.7617 0.7867 0.1570  0.3988  -0.1134 367 PHE D CE1 
15334 C CE2 . PHE D 367 ? 1.4051 0.8007 0.7856 0.1537  0.4120  -0.0847 367 PHE D CE2 
15335 C CZ  . PHE D 367 ? 1.3112 0.6936 0.6945 0.1485  0.3906  -0.0973 367 PHE D CZ  
15336 N N   . LEU D 368 ? 1.4592 0.8637 0.7889 0.1863  0.4702  -0.0834 368 LEU D N   
15337 C CA  . LEU D 368 ? 1.4049 0.8166 0.6972 0.1832  0.4569  -0.0750 368 LEU D CA  
15338 C C   . LEU D 368 ? 1.4456 0.8533 0.6957 0.1907  0.4560  -0.0828 368 LEU D C   
15339 O O   . LEU D 368 ? 1.4575 0.8654 0.6707 0.1885  0.4396  -0.0839 368 LEU D O   
15340 C CB  . LEU D 368 ? 1.4186 0.8502 0.7286 0.1803  0.4631  -0.0537 368 LEU D CB  
15341 C CG  . LEU D 368 ? 1.4058 0.8450 0.7375 0.1706  0.4539  -0.0435 368 LEU D CG  
15342 C CD1 . LEU D 368 ? 1.3075 0.7611 0.6749 0.1691  0.4675  -0.0274 368 LEU D CD1 
15343 C CD2 . LEU D 368 ? 1.4165 0.8609 0.7148 0.1658  0.4336  -0.0386 368 LEU D CD2 
15344 N N   . GLU D 369 ? 1.5093 0.9148 0.7643 0.1994  0.4730  -0.0885 369 GLU D N   
15345 C CA  . GLU D 369 ? 1.5357 0.9365 0.7496 0.2070  0.4727  -0.0979 369 GLU D CA  
15346 C C   . GLU D 369 ? 1.5422 0.9221 0.7324 0.2074  0.4591  -0.1202 369 GLU D C   
15347 O O   . GLU D 369 ? 1.5697 0.9455 0.7176 0.2075  0.4452  -0.1271 369 GLU D O   
15348 C CB  . GLU D 369 ? 1.6607 1.0658 0.8864 0.2162  0.4961  -0.0970 369 GLU D CB  
15349 C CG  . GLU D 369 ? 1.5328 0.9550 0.7620 0.2174  0.5071  -0.0767 369 GLU D CG  
15350 C CD  . GLU D 369 ? 1.7220 1.1459 0.9337 0.2274  0.5237  -0.0783 369 GLU D CD  
15351 O OE1 . GLU D 369 ? 2.0438 1.4677 1.2128 0.2314  0.5168  -0.0810 369 GLU D OE1 
15352 O OE2 . GLU D 369 ? 1.8509 1.2771 1.0919 0.2311  0.5435  -0.0767 369 GLU D OE2 
15353 N N   . LYS D 370 ? 1.5349 0.9009 0.7529 0.2074  0.4618  -0.1320 370 LYS D N   
15354 C CA  . LYS D 370 ? 1.5672 0.9094 0.7663 0.2070  0.4475  -0.1538 370 LYS D CA  
15355 C C   . LYS D 370 ? 1.6499 0.9848 0.8288 0.1962  0.4236  -0.1542 370 LYS D C   
15356 O O   . LYS D 370 ? 1.6353 0.9550 0.7783 0.1944  0.4073  -0.1687 370 LYS D O   
15357 C CB  . LYS D 370 ? 1.5528 0.8820 0.7918 0.2100  0.4552  -0.1648 370 LYS D CB  
15358 C CG  . LYS D 370 ? 1.6385 0.9454 0.8603 0.2165  0.4515  -0.1885 370 LYS D CG  
15359 C CD  . LYS D 370 ? 1.6399 0.9515 0.8226 0.2244  0.4579  -0.1933 370 LYS D CD  
15360 C CE  . LYS D 370 ? 1.6845 0.9743 0.8527 0.2315  0.4557  -0.2179 370 LYS D CE  
15361 N NZ  . LYS D 370 ? 1.7239 1.0219 0.8712 0.2423  0.4714  -0.2216 370 LYS D NZ  
15362 N N   . LEU D 371 ? 1.6182 0.9640 0.8200 0.1885  0.4209  -0.1389 371 LEU D N   
15363 C CA  . LEU D 371 ? 1.6020 0.9442 0.7836 0.1778  0.3989  -0.1373 371 LEU D CA  
15364 C C   . LEU D 371 ? 1.6328 0.9856 0.7697 0.1773  0.3874  -0.1337 371 LEU D C   
15365 O O   . LEU D 371 ? 1.7062 1.0450 0.8081 0.1744  0.3702  -0.1479 371 LEU D O   
15366 C CB  . LEU D 371 ? 1.4801 0.8365 0.6940 0.1706  0.4003  -0.1197 371 LEU D CB  
15367 C CG  . LEU D 371 ? 1.4171 0.7864 0.6242 0.1571  0.3748  -0.1094 371 LEU D CG  
15368 C CD1 . LEU D 371 ? 1.4159 0.7755 0.6322 0.1451  0.3458  -0.1205 371 LEU D CD1 
15369 C CD2 . LEU D 371 ? 1.3684 0.7579 0.6144 0.1510  0.3778  -0.0901 371 LEU D CD2 
15370 N N   . TYR D 372 ? 1.6144 0.9911 0.7532 0.1807  0.3967  -0.1158 372 TYR D N   
15371 C CA  . TYR D 372 ? 1.6058 0.9963 0.7079 0.1806  0.3850  -0.1095 372 TYR D CA  
15372 C C   . TYR D 372 ? 1.6586 1.0379 0.7210 0.1863  0.3799  -0.1272 372 TYR D C   
15373 O O   . TYR D 372 ? 1.7119 1.0952 0.7392 0.1831  0.3620  -0.1298 372 TYR D O   
15374 C CB  . TYR D 372 ? 1.5983 1.0123 0.7135 0.1853  0.3985  -0.0887 372 TYR D CB  
15375 C CG  . TYR D 372 ? 1.4699 0.8991 0.6147 0.1783  0.3969  -0.0699 372 TYR D CG  
15376 C CD1 . TYR D 372 ? 1.4289 0.8514 0.5913 0.1693  0.3882  -0.0717 372 TYR D CD1 
15377 C CD2 . TYR D 372 ? 1.4451 0.8940 0.5994 0.1808  0.4039  -0.0511 372 TYR D CD2 
15378 C CE1 . TYR D 372 ? 1.3875 0.8247 0.5761 0.1630  0.3868  -0.0552 372 TYR D CE1 
15379 C CE2 . TYR D 372 ? 1.4040 0.8658 0.5859 0.1746  0.4019  -0.0353 372 TYR D CE2 
15380 C CZ  . TYR D 372 ? 1.3749 0.8319 0.5739 0.1657  0.3933  -0.0375 372 TYR D CZ  
15381 O OH  . TYR D 372 ? 1.3355 0.8062 0.5613 0.1597  0.3912  -0.0225 372 TYR D OH  
15382 N N   . SER D 373 ? 1.5952 0.9617 0.6633 0.1946  0.3949  -0.1398 373 SER D N   
15383 C CA  . SER D 373 ? 1.7032 1.0584 0.7335 0.2003  0.3905  -0.1581 373 SER D CA  
15384 C C   . SER D 373 ? 1.6815 1.0128 0.6927 0.1931  0.3692  -0.1786 373 SER D C   
15385 O O   . SER D 373 ? 1.7021 1.0281 0.6739 0.1925  0.3547  -0.1909 373 SER D O   
15386 C CB  . SER D 373 ? 1.8531 1.2026 0.8967 0.2114  0.4132  -0.1658 373 SER D CB  
15387 O OG  . SER D 373 ? 1.8039 1.1356 0.8790 0.2110  0.4179  -0.1769 373 SER D OG  
15388 N N   . THR D 374 ? 1.6386 0.9542 0.6778 0.1871  0.3663  -0.1828 374 THR D N   
15389 C CA  . THR D 374 ? 1.6554 0.9443 0.6791 0.1789  0.3453  -0.2020 374 THR D CA  
15390 C C   . THR D 374 ? 1.8113 1.1064 0.8049 0.1674  0.3205  -0.1980 374 THR D C   
15391 O O   . THR D 374 ? 1.8810 1.1577 0.8466 0.1609  0.3004  -0.2153 374 THR D O   
15392 C CB  . THR D 374 ? 1.6973 0.9684 0.7606 0.1750  0.3477  -0.2052 374 THR D CB  
15393 O OG1 . THR D 374 ? 1.6872 0.9658 0.7885 0.1850  0.3727  -0.1997 374 THR D OG1 
15394 C CG2 . THR D 374 ? 1.6541 0.8979 0.7170 0.1694  0.3289  -0.2272 374 THR D CG2 
15395 N N   . LEU D 375 ? 1.7752 1.0964 0.7761 0.1640  0.3206  -0.1757 375 LEU D N   
15396 C CA  . LEU D 375 ? 1.6142 0.9464 0.5889 0.1537  0.2969  -0.1704 375 LEU D CA  
15397 C C   . LEU D 375 ? 1.6906 1.0319 0.6246 0.1573  0.2873  -0.1766 375 LEU D C   
15398 O O   . LEU D 375 ? 1.6636 1.0089 0.5718 0.1482  0.2638  -0.1793 375 LEU D O   
15399 C CB  . LEU D 375 ? 1.5679 0.9285 0.5631 0.1505  0.2996  -0.1444 375 LEU D CB  
15400 C CG  . LEU D 375 ? 1.5153 0.8826 0.5631 0.1418  0.2995  -0.1323 375 LEU D CG  
15401 C CD1 . LEU D 375 ? 1.5786 0.9338 0.6539 0.1279  0.2765  -0.1438 375 LEU D CD1 
15402 C CD2 . LEU D 375 ? 1.4990 0.8648 0.5750 0.1523  0.3297  -0.1251 375 LEU D CD2 
15403 N N   . GLU D 376 ? 1.7883 1.1346 0.7164 0.1700  0.3044  -0.1785 376 GLU D N   
15404 C CA  . GLU D 376 ? 1.7423 1.0971 0.6305 0.1741  0.2960  -0.1852 376 GLU D CA  
15405 C C   . GLU D 376 ? 1.7668 1.0945 0.6274 0.1716  0.2823  -0.2133 376 GLU D C   
15406 O O   . GLU D 376 ? 1.8923 1.2237 0.7178 0.1676  0.2628  -0.2219 376 GLU D O   
15407 C CB  . GLU D 376 ? 1.8299 1.1991 0.7197 0.1878  0.3194  -0.1765 376 GLU D CB  
15408 C CG  . GLU D 376 ? 1.8386 1.2315 0.7583 0.1900  0.3334  -0.1497 376 GLU D CG  
15409 C CD  . GLU D 376 ? 1.7095 1.1163 0.6243 0.2018  0.3525  -0.1406 376 GLU D CD  
15410 O OE1 . GLU D 376 ? 1.7402 1.1347 0.6503 0.2099  0.3670  -0.1529 376 GLU D OE1 
15411 O OE2 . GLU D 376 ? 1.6953 1.1247 0.6108 0.2028  0.3528  -0.1214 376 GLU D OE2 
15412 N N   . LYS D 377 ? 1.7744 1.0753 0.6524 0.1739  0.2915  -0.2283 377 LYS D N   
15413 C CA  . LYS D 377 ? 1.9717 1.2445 0.8277 0.1718  0.2789  -0.2559 377 LYS D CA  
15414 C C   . LYS D 377 ? 1.9936 1.2486 0.8418 0.1552  0.2505  -0.2653 377 LYS D C   
15415 O O   . LYS D 377 ? 2.1414 1.3827 0.9602 0.1494  0.2309  -0.2845 377 LYS D O   
15416 C CB  . LYS D 377 ? 2.0504 1.3014 0.9314 0.1807  0.2980  -0.2684 377 LYS D CB  
15417 C CG  . LYS D 377 ? 1.9197 1.1592 0.8449 0.1768  0.3045  -0.2622 377 LYS D CG  
15418 C CD  . LYS D 377 ? 1.7925 1.0220 0.7486 0.1886  0.3279  -0.2687 377 LYS D CD  
15419 C CE  . LYS D 377 ? 1.7940 1.0490 0.7529 0.2015  0.3525  -0.2558 377 LYS D CE  
15420 N NZ  . LYS D 377 ? 1.7809 1.0339 0.7817 0.2106  0.3764  -0.2544 377 LYS D NZ  
15421 N N   . GLU D 378 ? 1.7741 1.0294 0.6483 0.1464  0.2475  -0.2524 378 GLU D N   
15422 C CA  . GLU D 378 ? 1.7547 1.0108 0.6501 0.1259  0.2156  -0.2535 378 GLU D CA  
15423 C C   . GLU D 378 ? 1.7947 1.0763 0.6638 0.1173  0.1953  -0.2439 378 GLU D C   
15424 O O   . GLU D 378 ? 1.7176 1.0266 0.5943 0.1184  0.2007  -0.2215 378 GLU D O   
15425 C CB  . GLU D 378 ? 1.7456 1.0100 0.7021 0.1174  0.2155  -0.2373 378 GLU D CB  
15426 C CG  . GLU D 378 ? 1.7500 0.9955 0.7364 0.1280  0.2382  -0.2427 378 GLU D CG  
15427 C CD  . GLU D 378 ? 1.7694 0.9920 0.7883 0.1178  0.2224  -0.2549 378 GLU D CD  
15428 O OE1 . GLU D 378 ? 1.9199 1.1312 0.9245 0.1055  0.1972  -0.2671 378 GLU D OE1 
15429 O OE2 . GLU D 378 ? 1.7699 0.9854 0.8291 0.1221  0.2350  -0.2520 378 GLU D OE2 
15430 N N   . GLU D 379 ? 1.9045 1.1770 0.7434 0.1088  0.1717  -0.2612 379 GLU D N   
15431 C CA  . GLU D 379 ? 1.9354 1.2330 0.7492 0.1004  0.1503  -0.2540 379 GLU D CA  
15432 C C   . GLU D 379 ? 1.9613 1.2792 0.8159 0.0799  0.1265  -0.2393 379 GLU D C   
15433 O O   . GLU D 379 ? 1.9663 1.3131 0.8115 0.0745  0.1136  -0.2260 379 GLU D O   
15434 C CB  . GLU D 379 ? 2.0164 1.2979 0.7819 0.0986  0.1334  -0.2791 379 GLU D CB  
15435 C CG  . GLU D 379 ? 2.0663 1.3288 0.8495 0.0795  0.1063  -0.2962 379 GLU D CG  
15436 C CD  . GLU D 379 ? 2.0395 1.2665 0.8470 0.0826  0.1176  -0.3111 379 GLU D CD  
15437 O OE1 . GLU D 379 ? 2.0198 1.2301 0.8099 0.1013  0.1435  -0.3198 379 GLU D OE1 
15438 O OE2 . GLU D 379 ? 1.9070 1.1234 0.7516 0.0668  0.1008  -0.3133 379 GLU D OE2 
15439 N N   . TRP D 380 ? 1.8449 1.1490 0.7441 0.0691  0.1208  -0.2409 380 TRP D N   
15440 C CA  . TRP D 380 ? 1.6784 1.0025 0.6174 0.0505  0.1011  -0.2248 380 TRP D CA  
15441 C C   . TRP D 380 ? 1.6594 1.0105 0.6256 0.0554  0.1165  -0.1983 380 TRP D C   
15442 O O   . TRP D 380 ? 1.5886 0.9674 0.5707 0.0444  0.1026  -0.1816 380 TRP D O   
15443 C CB  . TRP D 380 ? 1.7243 1.0241 0.7007 0.0377  0.0901  -0.2338 380 TRP D CB  
15444 C CG  . TRP D 380 ? 1.7321 1.0079 0.7301 0.0501  0.1133  -0.2385 380 TRP D CG  
15445 C CD1 . TRP D 380 ? 1.7349 0.9833 0.7093 0.0653  0.1303  -0.2578 380 TRP D CD1 
15446 C CD2 . TRP D 380 ? 1.6214 0.8998 0.6697 0.0483  0.1216  -0.2241 380 TRP D CD2 
15447 N NE1 . TRP D 380 ? 1.8386 1.0737 0.8477 0.0733  0.1489  -0.2558 380 TRP D NE1 
15448 C CE2 . TRP D 380 ? 1.6377 0.8907 0.6922 0.0629  0.1432  -0.2353 380 TRP D CE2 
15449 C CE3 . TRP D 380 ? 1.5696 0.8701 0.6575 0.0361  0.1128  -0.2030 380 TRP D CE3 
15450 C CZ2 . TRP D 380 ? 1.6032 0.8535 0.7034 0.0655  0.1550  -0.2259 380 TRP D CZ2 
15451 C CZ3 . TRP D 380 ? 1.5368 0.8331 0.6673 0.0386  0.1245  -0.1941 380 TRP D CZ3 
15452 C CH2 . TRP D 380 ? 1.5534 0.8252 0.6903 0.0531  0.1448  -0.2055 380 TRP D CH2 
15453 N N   . ILE D 381 ? 1.7307 1.0746 0.7031 0.0715  0.1451  -0.1944 381 ILE D N   
15454 C CA  . ILE D 381 ? 1.7240 1.0907 0.7220 0.0766  0.1613  -0.1708 381 ILE D CA  
15455 C C   . ILE D 381 ? 1.6803 1.0688 0.6409 0.0868  0.1685  -0.1604 381 ILE D C   
15456 O O   . ILE D 381 ? 1.7986 1.1792 0.7295 0.1036  0.1901  -0.1641 381 ILE D O   
15457 C CB  . ILE D 381 ? 1.5593 0.9109 0.5816 0.0888  0.1885  -0.1706 381 ILE D CB  
15458 C CG1 . ILE D 381 ? 1.5519 0.8810 0.6100 0.0800  0.1802  -0.1811 381 ILE D CG1 
15459 C CG2 . ILE D 381 ? 1.5095 0.8847 0.5586 0.0922  0.2032  -0.1469 381 ILE D CG2 
15460 C CD1 . ILE D 381 ? 1.5736 0.8883 0.6576 0.0922  0.2055  -0.1826 381 ILE D CD1 
15461 N N   . GLU D 382 ? 1.5867 1.0029 0.5487 0.0772  0.1509  -0.1467 382 GLU D N   
15462 C CA  . GLU D 382 ? 1.5599 0.9998 0.4927 0.0868  0.1566  -0.1331 382 GLU D CA  
15463 C C   . GLU D 382 ? 1.5074 0.9666 0.4736 0.0894  0.1707  -0.1095 382 GLU D C   
15464 O O   . GLU D 382 ? 1.4686 0.9449 0.4680 0.0763  0.1567  -0.0983 382 GLU D O   
15465 C CB  . GLU D 382 ? 1.7006 1.1603 0.6131 0.0760  0.1281  -0.1337 382 GLU D CB  
15466 C CG  . GLU D 382 ? 1.7150 1.2082 0.6203 0.0803  0.1278  -0.1120 382 GLU D CG  
15467 C CD  . GLU D 382 ? 1.9245 1.4339 0.7911 0.0783  0.1067  -0.1162 382 GLU D CD  
15468 O OE1 . GLU D 382 ? 1.8755 1.3834 0.7435 0.0628  0.0813  -0.1291 382 GLU D OE1 
15469 O OE2 . GLU D 382 ? 1.9458 1.4732 0.7890 0.0913  0.1144  -0.1058 382 GLU D OE2 
15470 N N   . THR D 383 ? 1.5381 0.9935 0.4963 0.1059  0.1990  -0.1025 383 THR D N   
15471 C CA  . THR D 383 ? 1.4667 0.9389 0.4531 0.1093  0.2137  -0.0810 383 THR D CA  
15472 C C   . THR D 383 ? 1.4591 0.9617 0.4313 0.1116  0.2062  -0.0645 383 THR D C   
15473 O O   . THR D 383 ? 1.6825 1.1977 0.6323 0.1177  0.2011  -0.0665 383 THR D O   
15474 C CB  . THR D 383 ? 1.4687 0.9296 0.4628 0.1241  0.2452  -0.0787 383 THR D CB  
15475 O OG1 . THR D 383 ? 1.5523 1.0264 0.5302 0.1352  0.2510  -0.0771 383 THR D OG1 
15476 C CG2 . THR D 383 ? 1.4804 0.9120 0.4878 0.1239  0.2532  -0.0962 383 THR D CG2 
15477 N N   . LEU D 384 ? 1.4204 0.9415 0.4186 0.1055  0.2029  -0.0477 384 LEU D N   
15478 C CA  . LEU D 384 ? 1.4070 0.9641 0.4094 0.1053  0.1912  -0.0316 384 LEU D CA  
15479 C C   . LEU D 384 ? 1.3633 0.9398 0.4026 0.1123  0.2078  -0.0120 384 LEU D C   
15480 O O   . LEU D 384 ? 1.3475 0.9107 0.4102 0.1156  0.2269  -0.0102 384 LEU D O   
15481 C CB  . LEU D 384 ? 1.3855 0.9545 0.3911 0.0896  0.1662  -0.0292 384 LEU D CB  
15482 C CG  . LEU D 384 ? 1.4084 0.9712 0.4053 0.0760  0.1407  -0.0469 384 LEU D CG  
15483 C CD1 . LEU D 384 ? 1.3716 0.9459 0.4100 0.0571  0.1220  -0.0428 384 LEU D CD1 
15484 C CD2 . LEU D 384 ? 1.4413 1.0192 0.3972 0.0786  0.1254  -0.0490 384 LEU D CD2 
15485 N N   . THR D 385 ? 1.3509 0.9587 0.3952 0.1140  0.1994  0.0018  385 THR D N   
15486 C CA  . THR D 385 ? 1.3146 0.9430 0.3932 0.1180  0.2091  0.0202  385 THR D CA  
15487 C C   . THR D 385 ? 1.2832 0.9334 0.3777 0.1081  0.1931  0.0301  385 THR D C   
15488 O O   . THR D 385 ? 1.2929 0.9469 0.3690 0.0989  0.1732  0.0247  385 THR D O   
15489 C CB  . THR D 385 ? 1.3829 1.0281 0.4543 0.1294  0.2140  0.0281  385 THR D CB  
15490 O OG1 . THR D 385 ? 1.3972 1.0624 0.4444 0.1270  0.1934  0.0278  385 THR D OG1 
15491 C CG2 . THR D 385 ? 1.3634 0.9876 0.4175 0.1386  0.2298  0.0184  385 THR D CG2 
15492 N N   . LEU D 386 ? 1.2469 0.9110 0.3761 0.1096  0.2015  0.0443  386 LEU D N   
15493 C CA  . LEU D 386 ? 1.2145 0.8985 0.3632 0.1003  0.1890  0.0536  386 LEU D CA  
15494 C C   . LEU D 386 ? 1.3446 1.0573 0.4792 0.0985  0.1695  0.0587  386 LEU D C   
15495 O O   . LEU D 386 ? 1.3788 1.1059 0.5186 0.0886  0.1542  0.0623  386 LEU D O   
15496 C CB  . LEU D 386 ? 1.2202 0.9131 0.4078 0.1035  0.2022  0.0662  386 LEU D CB  
15497 C CG  . LEU D 386 ? 1.1708 0.8378 0.3750 0.1052  0.2215  0.0618  386 LEU D CG  
15498 C CD1 . LEU D 386 ? 1.1407 0.8161 0.3806 0.1092  0.2340  0.0731  386 LEU D CD1 
15499 C CD2 . LEU D 386 ? 1.1654 0.8141 0.3685 0.0940  0.2171  0.0540  386 LEU D CD2 
15500 N N   . GLU D 387 ? 1.4939 1.2160 0.6109 0.1078  0.1696  0.0596  387 GLU D N   
15501 C CA  . GLU D 387 ? 1.4694 1.2173 0.5686 0.1057  0.1498  0.0623  387 GLU D CA  
15502 C C   . GLU D 387 ? 1.4985 1.2358 0.5638 0.0978  0.1327  0.0471  387 GLU D C   
15503 O O   . GLU D 387 ? 1.4402 1.1947 0.4992 0.0886  0.1123  0.0479  387 GLU D O   
15504 C CB  . GLU D 387 ? 1.3589 1.1196 0.4483 0.1177  0.1543  0.0688  387 GLU D CB  
15505 C CG  . GLU D 387 ? 1.5687 1.3079 0.6358 0.1273  0.1677  0.0605  387 GLU D CG  
15506 C CD  . GLU D 387 ? 1.4659 1.1835 0.5548 0.1329  0.1914  0.0619  387 GLU D CD  
15507 O OE1 . GLU D 387 ? 1.3052 1.0230 0.4256 0.1288  0.1969  0.0680  387 GLU D OE1 
15508 O OE2 . GLU D 387 ? 1.4437 1.1455 0.5183 0.1413  0.2045  0.0572  387 GLU D OE2 
15509 N N   . GLU D 388 ? 1.3257 1.0339 0.3690 0.1006  0.1401  0.0325  388 GLU D N   
15510 C CA  . GLU D 388 ? 1.3548 1.0487 0.3638 0.0927  0.1229  0.0156  388 GLU D CA  
15511 C C   . GLU D 388 ? 1.3817 1.0610 0.3955 0.0773  0.1120  0.0106  388 GLU D C   
15512 O O   . GLU D 388 ? 1.3714 1.0523 0.3688 0.0653  0.0893  0.0021  388 GLU D O   
15513 C CB  . GLU D 388 ? 1.4338 1.0986 0.4188 0.1000  0.1345  -0.0001 388 GLU D CB  
15514 C CG  . GLU D 388 ? 1.4681 1.1464 0.4312 0.1104  0.1343  -0.0002 388 GLU D CG  
15515 C CD  . GLU D 388 ? 1.4463 1.1006 0.3993 0.1210  0.1549  -0.0084 388 GLU D CD  
15516 O OE1 . GLU D 388 ? 1.4869 1.1121 0.4437 0.1188  0.1649  -0.0186 388 GLU D OE1 
15517 O OE2 . GLU D 388 ? 1.4662 1.1304 0.4078 0.1313  0.1613  -0.0042 388 GLU D OE2 
15518 N N   . ALA D 389 ? 1.3532 1.0193 0.3939 0.0756  0.1266  0.0157  389 ALA D N   
15519 C CA  . ALA D 389 ? 1.2892 0.9546 0.3611 0.0577  0.1133  0.0134  389 ALA D CA  
15520 C C   . ALA D 389 ? 1.3179 1.0181 0.4076 0.0487  0.0962  0.0267  389 ALA D C   
15521 O O   . ALA D 389 ? 1.2456 0.9529 0.3585 0.0311  0.0778  0.0235  389 ALA D O   
15522 C CB  . ALA D 389 ? 1.2575 0.9064 0.3618 0.0583  0.1319  0.0162  389 ALA D CB  
15523 N N   . MET D 390 ? 1.4046 1.1264 0.4844 0.0605  0.1025  0.0418  390 MET D N   
15524 C CA  . MET D 390 ? 1.3241 1.0809 0.4207 0.0543  0.0885  0.0551  390 MET D CA  
15525 C C   . MET D 390 ? 1.3354 1.1140 0.4106 0.0498  0.0649  0.0516  390 MET D C   
15526 O O   . MET D 390 ? 1.2362 1.0423 0.3312 0.0375  0.0470  0.0572  390 MET D O   
15527 C CB  . MET D 390 ? 1.2807 1.0632 0.4079 0.0659  0.1027  0.0711  390 MET D CB  
15528 C CG  . MET D 390 ? 1.1579 0.9439 0.3209 0.0614  0.1107  0.0809  390 MET D CG  
15529 S SD  . MET D 390 ? 1.3192 1.1199 0.4900 0.0426  0.0889  0.0845  390 MET D SD  
15530 C CE  . MET D 390 ? 1.1302 0.9790 0.3101 0.0479  0.0797  0.0996  390 MET D CE  
15531 N N   . ARG D 391 ? 1.3847 1.1563 0.4272 0.0583  0.0641  0.0423  391 ARG D N   
15532 C CA  . ARG D 391 ? 1.4617 1.2538 0.4798 0.0552  0.0415  0.0382  391 ARG D CA  
15533 C C   . ARG D 391 ? 1.4555 1.2315 0.4635 0.0391  0.0220  0.0180  391 ARG D C   
15534 O O   . ARG D 391 ? 1.5132 1.3098 0.5122 0.0305  -0.0014 0.0138  391 ARG D O   
15535 C CB  . ARG D 391 ? 1.3817 1.1867 0.3872 0.0705  0.0485  0.0396  391 ARG D CB  
15536 C CG  . ARG D 391 ? 1.3902 1.2281 0.4202 0.0798  0.0559  0.0591  391 ARG D CG  
15537 C CD  . ARG D 391 ? 1.5023 1.3327 0.5674 0.0844  0.0782  0.0697  391 ARG D CD  
15538 N NE  . ARG D 391 ? 1.5750 1.4296 0.6617 0.0925  0.0848  0.0859  391 ARG D NE  
15539 C CZ  . ARG D 391 ? 1.3769 1.2603 0.4807 0.0885  0.0744  0.0973  391 ARG D CZ  
15540 N NH1 . ARG D 391 ? 1.3035 1.1998 0.4072 0.0760  0.0564  0.0959  391 ARG D NH1 
15541 N NH2 . ARG D 391 ? 1.2249 1.1226 0.3458 0.0974  0.0822  0.1103  391 ARG D NH2 
15542 N N   . LYS D 392 ? 1.3627 1.1047 0.3777 0.0344  0.0304  0.0051  392 LYS D N   
15543 C CA  . LYS D 392 ? 1.4333 1.1568 0.4419 0.0202  0.0136  -0.0156 392 LYS D CA  
15544 C C   . LYS D 392 ? 1.4083 1.1509 0.4489 -0.0026 -0.0107 -0.0149 392 LYS D C   
15545 O O   . LYS D 392 ? 1.4741 1.2155 0.5520 -0.0125 -0.0081 -0.0086 392 LYS D O   
15546 C CB  . LYS D 392 ? 1.4022 1.0858 0.4161 0.0217  0.0300  -0.0277 392 LYS D CB  
15547 C CG  . LYS D 392 ? 1.4209 1.0780 0.4153 0.0141  0.0182  -0.0514 392 LYS D CG  
15548 C CD  . LYS D 392 ? 1.4655 1.1312 0.4149 0.0197  0.0058  -0.0601 392 LYS D CD  
15549 C CE  . LYS D 392 ? 1.4948 1.1448 0.4040 0.0424  0.0281  -0.0622 392 LYS D CE  
15550 N NZ  . LYS D 392 ? 1.5191 1.1300 0.4278 0.0469  0.0462  -0.0758 392 LYS D NZ  
15551 N N   . GLU D 393 ? 1.4260 1.1874 0.4523 -0.0112 -0.0344 -0.0210 393 GLU D N   
15552 C CA  . GLU D 393 ? 1.4040 1.1896 0.4609 -0.0328 -0.0574 -0.0179 393 GLU D CA  
15553 C C   . GLU D 393 ? 1.3638 1.1220 0.4423 -0.0518 -0.0656 -0.0313 393 GLU D C   
15554 O O   . GLU D 393 ? 1.3359 1.1060 0.4509 -0.0684 -0.0747 -0.0240 393 GLU D O   
15555 C CB  . GLU D 393 ? 1.3910 1.2035 0.4261 -0.0368 -0.0808 -0.0222 393 GLU D CB  
15556 C CG  . GLU D 393 ? 1.4044 1.2354 0.4066 -0.0148 -0.0730 -0.0131 393 GLU D CG  
15557 C CD  . GLU D 393 ? 1.4491 1.3249 0.4504 -0.0188 -0.0949 -0.0053 393 GLU D CD  
15558 O OE1 . GLU D 393 ? 1.3819 1.2825 0.4190 -0.0358 -0.1089 0.0014  393 GLU D OE1 
15559 O OE2 . GLU D 393 ? 1.4375 1.3246 0.4030 -0.0049 -0.0982 -0.0057 393 GLU D OE2 
15560 N N   . ASP D 394 ? 1.3980 1.1191 0.4541 -0.0489 -0.0618 -0.0506 394 ASP D N   
15561 C CA  . ASP D 394 ? 1.4082 1.0999 0.4804 -0.0658 -0.0710 -0.0655 394 ASP D CA  
15562 C C   . ASP D 394 ? 1.4548 1.1244 0.5549 -0.0629 -0.0513 -0.0598 394 ASP D C   
15563 O O   . ASP D 394 ? 1.4613 1.0979 0.5500 -0.0525 -0.0355 -0.0702 394 ASP D O   
15564 C CB  . ASP D 394 ? 1.6351 1.2969 0.6701 -0.0631 -0.0761 -0.0899 394 ASP D CB  
15565 C CG  . ASP D 394 ? 1.7336 1.4176 0.7363 -0.0632 -0.0945 -0.0959 394 ASP D CG  
15566 O OD1 . ASP D 394 ? 1.5783 1.2908 0.5669 -0.0499 -0.0895 -0.0824 394 ASP D OD1 
15567 O OD2 . ASP D 394 ? 1.8804 1.5527 0.8718 -0.0765 -0.1145 -0.1145 394 ASP D OD2 
15568 N N   . VAL D 395 ? 1.4740 1.1635 0.6115 -0.0722 -0.0527 -0.0430 395 VAL D N   
15569 C CA  . VAL D 395 ? 1.3061 0.9781 0.4742 -0.0730 -0.0387 -0.0371 395 VAL D CA  
15570 C C   . VAL D 395 ? 1.2706 0.9686 0.4762 -0.0897 -0.0499 -0.0216 395 VAL D C   
15571 O O   . VAL D 395 ? 1.3086 1.0432 0.5168 -0.0921 -0.0580 -0.0097 395 VAL D O   
15572 C CB  . VAL D 395 ? 1.2890 0.9571 0.4511 -0.0512 -0.0110 -0.0285 395 VAL D CB  
15573 C CG1 . VAL D 395 ? 1.2647 0.9703 0.4268 -0.0431 -0.0068 -0.0097 395 VAL D CG1 
15574 C CG2 . VAL D 395 ? 1.2629 0.9108 0.4556 -0.0519 0.0024  -0.0251 395 VAL D CG2 
15575 N N   . LYS D 396 ? 1.2714 0.9509 0.5057 -0.1008 -0.0505 -0.0214 396 LYS D N   
15576 C CA  . LYS D 396 ? 1.2381 0.9398 0.5066 -0.1177 -0.0613 -0.0071 396 LYS D CA  
15577 C C   . LYS D 396 ? 1.1860 0.9119 0.4700 -0.1079 -0.0459 0.0124  396 LYS D C   
15578 O O   . LYS D 396 ? 1.1820 0.8936 0.4654 -0.0930 -0.0258 0.0141  396 LYS D O   
15579 C CB  . LYS D 396 ? 1.2610 0.9344 0.5541 -0.1322 -0.0671 -0.0117 396 LYS D CB  
15580 C CG  . LYS D 396 ? 1.2255 0.9159 0.5406 -0.1563 -0.0890 -0.0060 396 LYS D CG  
15581 C CD  . LYS D 396 ? 1.2118 0.8849 0.5586 -0.1692 -0.0911 -0.0005 396 LYS D CD  
15582 C CE  . LYS D 396 ? 1.3357 0.9633 0.6795 -0.1618 -0.0817 -0.0139 396 LYS D CE  
15583 N NZ  . LYS D 396 ? 1.2111 0.8254 0.5868 -0.1717 -0.0823 -0.0052 396 LYS D NZ  
15584 N N   . THR D 397 ? 1.0445 0.8624 0.6331 -0.0985 -0.1175 -0.3481 397 THR D N   
15585 C CA  . THR D 397 ? 0.9444 0.8041 0.5551 -0.0955 -0.1143 -0.3229 397 THR D CA  
15586 C C   . THR D 397 ? 0.8777 0.7542 0.5441 -0.1137 -0.1152 -0.3192 397 THR D C   
15587 O O   . THR D 397 ? 0.8746 0.7458 0.5652 -0.1335 -0.1301 -0.3315 397 THR D O   
15588 C CB  . THR D 397 ? 1.0436 0.9296 0.6371 -0.0957 -0.1341 -0.3123 397 THR D CB  
15589 O OG1 . THR D 397 ? 1.1192 1.0129 0.7345 -0.1157 -0.1590 -0.3234 397 THR D OG1 
15590 C CG2 . THR D 397 ? 1.1120 0.9756 0.6445 -0.0830 -0.1325 -0.3148 397 THR D CG2 
15591 N N   . GLU D 398 ? 0.8686 0.7639 0.5541 -0.1088 -0.0986 -0.3012 398 GLU D N   
15592 C CA  . GLU D 398 ? 0.8199 0.7318 0.5521 -0.1271 -0.0961 -0.2937 398 GLU D CA  
15593 C C   . GLU D 398 ? 0.7675 0.7228 0.5103 -0.1205 -0.0927 -0.2700 398 GLU D C   
15594 O O   . GLU D 398 ? 0.7493 0.7105 0.4671 -0.1001 -0.0832 -0.2575 398 GLU D O   
15595 C CB  . GLU D 398 ? 0.7641 0.6398 0.5102 -0.1290 -0.0761 -0.2934 398 GLU D CB  
15596 C CG  . GLU D 398 ? 0.9078 0.7808 0.7018 -0.1501 -0.0771 -0.2826 398 GLU D CG  
15597 C CD  . GLU D 398 ? 1.1621 1.0084 0.9722 -0.1439 -0.0570 -0.2631 398 GLU D CD  
15598 O OE1 . GLU D 398 ? 1.4203 1.2403 1.2092 -0.1253 -0.0445 -0.2664 398 GLU D OE1 
15599 O OE2 . GLU D 398 ? 1.0734 0.9259 0.9177 -0.1575 -0.0537 -0.2443 398 GLU D OE2 
15600 N N   . VAL D 399 ? 0.6920 0.6761 0.4755 -0.1367 -0.0995 -0.2612 399 VAL D N   
15601 C CA  . VAL D 399 ? 0.6536 0.6794 0.4537 -0.1300 -0.0978 -0.2383 399 VAL D CA  
15602 C C   . VAL D 399 ? 0.6513 0.6721 0.4753 -0.1281 -0.0766 -0.2149 399 VAL D C   
15603 O O   . VAL D 399 ? 0.6143 0.6153 0.4624 -0.1424 -0.0704 -0.2133 399 VAL D O   
15604 C CB  . VAL D 399 ? 0.6121 0.6772 0.4452 -0.1458 -0.1179 -0.2419 399 VAL D CB  
15605 C CG1 . VAL D 399 ? 0.6371 0.7429 0.4771 -0.1323 -0.1198 -0.2231 399 VAL D CG1 
15606 C CG2 . VAL D 399 ? 0.6609 0.7139 0.4797 -0.1476 -0.1396 -0.2581 399 VAL D CG2 
15607 N N   . ILE D 400 ? 0.6520 0.6890 0.4676 -0.1110 -0.0663 -0.1961 400 ILE D N   
15608 C CA  . ILE D 400 ? 0.5965 0.6334 0.4304 -0.1078 -0.0488 -0.1733 400 ILE D CA  
15609 C C   . ILE D 400 ? 0.5262 0.6054 0.3752 -0.1036 -0.0502 -0.1581 400 ILE D C   
15610 O O   . ILE D 400 ? 0.5560 0.6598 0.3968 -0.0979 -0.0631 -0.1630 400 ILE D O   
15611 C CB  . ILE D 400 ? 0.6113 0.6211 0.4218 -0.0897 -0.0330 -0.1665 400 ILE D CB  
15612 C CG1 . ILE D 400 ? 0.4966 0.5258 0.2830 -0.0710 -0.0317 -0.1600 400 ILE D CG1 
15613 C CG2 . ILE D 400 ? 0.7554 0.7252 0.5473 -0.0894 -0.0323 -0.1864 400 ILE D CG2 
15614 C CD1 . ILE D 400 ? 0.5303 0.5391 0.2991 -0.0540 -0.0155 -0.1534 400 ILE D CD1 
15615 N N   . GLU D 401 ? 0.4477 0.5334 0.3176 -0.1059 -0.0372 -0.1397 401 GLU D N   
15616 C CA  . GLU D 401 ? 0.4147 0.5388 0.3026 -0.1031 -0.0363 -0.1271 401 GLU D CA  
15617 C C   . GLU D 401 ? 0.3860 0.5094 0.2653 -0.0886 -0.0223 -0.1085 401 GLU D C   
15618 O O   . GLU D 401 ? 0.3573 0.5098 0.2464 -0.0829 -0.0218 -0.1002 401 GLU D O   
15619 C CB  . GLU D 401 ? 0.4075 0.5505 0.3334 -0.1234 -0.0346 -0.1245 401 GLU D CB  
15620 C CG  . GLU D 401 ? 0.5015 0.6763 0.4487 -0.1323 -0.0517 -0.1384 401 GLU D CG  
15621 C CD  . GLU D 401 ? 0.7179 0.8899 0.6939 -0.1573 -0.0544 -0.1472 401 GLU D CD  
15622 O OE1 . GLU D 401 ? 0.7179 0.8640 0.6982 -0.1682 -0.0409 -0.1390 401 GLU D OE1 
15623 O OE2 . GLU D 401 ? 0.7866 0.9803 0.7802 -0.1662 -0.0716 -0.1621 401 GLU D OE2 
15624 N N   . SER D 402 ? 0.3915 0.4834 0.2559 -0.0824 -0.0118 -0.1026 402 SER D N   
15625 C CA  . SER D 402 ? 0.3673 0.4594 0.2257 -0.0695 -0.0008 -0.0857 402 SER D CA  
15626 C C   . SER D 402 ? 0.3820 0.4417 0.2215 -0.0583 0.0057  -0.0858 402 SER D C   
15627 O O   . SER D 402 ? 0.4637 0.4965 0.2993 -0.0628 0.0050  -0.0966 402 SER D O   
15628 C CB  . SER D 402 ? 0.3546 0.4522 0.2318 -0.0793 0.0080  -0.0708 402 SER D CB  
15629 O OG  . SER D 402 ? 0.4340 0.5047 0.3182 -0.0930 0.0111  -0.0703 402 SER D OG  
15630 N N   . VAL D 403 ? 0.3626 0.4259 0.1935 -0.0435 0.0124  -0.0748 403 VAL D N   
15631 C CA  . VAL D 403 ? 0.3719 0.4107 0.1925 -0.0316 0.0205  -0.0728 403 VAL D CA  
15632 C C   . VAL D 403 ? 0.4455 0.4886 0.2744 -0.0254 0.0272  -0.0540 403 VAL D C   
15633 O O   . VAL D 403 ? 0.3916 0.4585 0.2239 -0.0244 0.0264  -0.0455 403 VAL D O   
15634 C CB  . VAL D 403 ? 0.3802 0.4197 0.1780 -0.0186 0.0212  -0.0822 403 VAL D CB  
15635 C CG1 . VAL D 403 ? 0.4154 0.4407 0.1990 -0.0238 0.0151  -0.1029 403 VAL D CG1 
15636 C CG2 . VAL D 403 ? 0.3981 0.4666 0.1904 -0.0135 0.0169  -0.0763 403 VAL D CG2 
15637 N N   . LYS D 404 ? 0.4268 0.4459 0.2596 -0.0210 0.0326  -0.0482 404 LYS D N   
15638 C CA  . LYS D 404 ? 0.3973 0.4193 0.2365 -0.0138 0.0364  -0.0313 404 LYS D CA  
15639 C C   . LYS D 404 ? 0.3482 0.3827 0.1810 0.0010  0.0403  -0.0311 404 LYS D C   
15640 O O   . LYS D 404 ? 0.4200 0.4438 0.2465 0.0099  0.0451  -0.0402 404 LYS D O   
15641 C CB  . LYS D 404 ? 0.4718 0.4643 0.3196 -0.0122 0.0383  -0.0246 404 LYS D CB  
15642 C CG  . LYS D 404 ? 0.4839 0.4788 0.3384 -0.0082 0.0380  -0.0055 404 LYS D CG  
15643 C CD  . LYS D 404 ? 0.5727 0.5388 0.4339 -0.0135 0.0355  0.0049  404 LYS D CD  
15644 C CE  . LYS D 404 ? 0.5931 0.5510 0.4529 -0.0326 0.0342  0.0034  404 LYS D CE  
15645 N NZ  . LYS D 404 ? 0.5852 0.5738 0.4409 -0.0434 0.0348  0.0045  404 LYS D NZ  
15646 N N   . ALA D 405 ? 0.3392 0.3956 0.1733 0.0029  0.0393  -0.0216 405 ALA D N   
15647 C CA  . ALA D 405 ? 0.3045 0.3728 0.1337 0.0144  0.0427  -0.0201 405 ALA D CA  
15648 C C   . ALA D 405 ? 0.3459 0.4021 0.1829 0.0250  0.0496  -0.0163 405 ALA D C   
15649 O O   . ALA D 405 ? 0.3707 0.4159 0.2204 0.0253  0.0485  -0.0080 405 ALA D O   
15650 C CB  . ALA D 405 ? 0.2816 0.3692 0.1160 0.0136  0.0394  -0.0103 405 ALA D CB  
15651 N N   . GLY D 406 ? 0.2989 0.3577 0.1289 0.0340  0.0566  -0.0217 406 GLY D N   
15652 C CA  . GLY D 406 ? 0.3422 0.3943 0.1848 0.0447  0.0654  -0.0196 406 GLY D CA  
15653 C C   . GLY D 406 ? 0.4008 0.4582 0.2311 0.0521  0.0763  -0.0268 406 GLY D C   
15654 O O   . GLY D 406 ? 0.4973 0.5572 0.3138 0.0453  0.0722  -0.0302 406 GLY D O   
15655 N N   . THR D 407 ? 0.3207 0.3749 0.1658 0.0620  0.0872  -0.0271 407 THR D N   
15656 C CA  . THR D 407 ? 0.3350 0.3932 0.1719 0.0680  0.1013  -0.0335 407 THR D CA  
15657 C C   . THR D 407 ? 0.4183 0.4599 0.2585 0.0771  0.1130  -0.0478 407 THR D C   
15658 O O   . THR D 407 ? 0.4685 0.4918 0.3168 0.0758  0.1062  -0.0525 407 THR D O   
15659 C CB  . THR D 407 ? 0.3160 0.3903 0.1759 0.0701  0.1052  -0.0206 407 THR D CB  
15660 O OG1 . THR D 407 ? 0.3662 0.4427 0.2560 0.0798  0.1083  -0.0153 407 THR D OG1 
15661 C CG2 . THR D 407 ? 0.2907 0.3735 0.1522 0.0600  0.0909  -0.0087 407 THR D CG2 
15662 N N   . TRP D 408 ? 0.3890 0.4340 0.2288 0.0821  0.1280  -0.0545 408 TRP D N   
15663 C CA  . TRP D 408 ? 0.4109 0.4411 0.2567 0.0943  0.1426  -0.0701 408 TRP D CA  
15664 C C   . TRP D 408 ? 0.4440 0.4811 0.3346 0.1058  0.1493  -0.0627 408 TRP D C   
15665 O O   . TRP D 408 ? 0.5506 0.5763 0.4574 0.1166  0.1600  -0.0748 408 TRP D O   
15666 C CB  . TRP D 408 ? 0.5122 0.5435 0.3409 0.0881  0.1516  -0.0837 408 TRP D CB  
15667 C CG  . TRP D 408 ? 0.4322 0.4842 0.2686 0.0826  0.1589  -0.0746 408 TRP D CG  
15668 C CD1 . TRP D 408 ? 0.4043 0.4729 0.2664 0.0836  0.1592  -0.0578 408 TRP D CD1 
15669 C CD2 . TRP D 408 ? 0.4592 0.5156 0.2749 0.0749  0.1674  -0.0825 408 TRP D CD2 
15670 N NE1 . TRP D 408 ? 0.4465 0.5270 0.3059 0.0768  0.1678  -0.0549 408 TRP D NE1 
15671 C CE2 . TRP D 408 ? 0.5045 0.5781 0.3343 0.0716  0.1735  -0.0691 408 TRP D CE2 
15672 C CE3 . TRP D 408 ? 0.5205 0.5683 0.3056 0.0705  0.1702  -0.0999 408 TRP D CE3 
15673 C CZ2 . TRP D 408 ? 0.5287 0.6102 0.3413 0.0643  0.1836  -0.0713 408 TRP D CZ2 
15674 C CZ3 . TRP D 408 ? 0.5892 0.6475 0.3566 0.0636  0.1795  -0.1020 408 TRP D CZ3 
15675 C CH2 . TRP D 408 ? 0.5795 0.6539 0.3599 0.0606  0.1866  -0.0872 408 TRP D CH2 
15676 N N   . PHE D 409 ? 0.4071 0.4626 0.3201 0.1038  0.1416  -0.0442 409 PHE D N   
15677 C CA  . PHE D 409 ? 0.4523 0.5153 0.4113 0.1127  0.1405  -0.0353 409 PHE D CA  
15678 C C   . PHE D 409 ? 0.5628 0.6100 0.5312 0.1092  0.1195  -0.0268 409 PHE D C   
15679 O O   . PHE D 409 ? 0.5965 0.6502 0.5586 0.0997  0.1050  -0.0138 409 PHE D O   
15680 C CB  . PHE D 409 ? 0.4984 0.5892 0.4760 0.1111  0.1425  -0.0210 409 PHE D CB  
15681 C CG  . PHE D 409 ? 0.4906 0.5968 0.4729 0.1147  0.1646  -0.0266 409 PHE D CG  
15682 C CD1 . PHE D 409 ? 0.4647 0.5705 0.4141 0.0997  0.1649  -0.0290 409 PHE D CD1 
15683 C CD2 . PHE D 409 ? 0.4307 0.5481 0.4553 0.1253  0.1763  -0.0295 409 PHE D CD2 
15684 C CE1 . PHE D 409 ? 0.5632 0.6792 0.5163 0.0957  0.1789  -0.0333 409 PHE D CE1 
15685 C CE2 . PHE D 409 ? 0.6134 0.7442 0.6435 0.1204  0.1904  -0.0357 409 PHE D CE2 
15686 C CZ  . PHE D 409 ? 0.6746 0.8045 0.6665 0.1057  0.1928  -0.0372 409 PHE D CZ  
15687 N N   . ASP D 410 ? 0.5576 0.5822 0.5392 0.1167  0.1187  -0.0345 410 ASP D N   
15688 C CA  . ASP D 410 ? 0.5337 0.5383 0.5240 0.1138  0.1003  -0.0251 410 ASP D CA  
15689 C C   . ASP D 410 ? 0.5015 0.4946 0.4575 0.0977  0.0895  -0.0241 410 ASP D C   
15690 O O   . ASP D 410 ? 0.6140 0.5901 0.5715 0.0920  0.0760  -0.0153 410 ASP D O   
15691 C CB  . ASP D 410 ? 0.5456 0.5652 0.5641 0.1158  0.0873  -0.0051 410 ASP D CB  
15692 C CG  . ASP D 410 ? 0.7047 0.7432 0.7640 0.1304  0.0966  -0.0051 410 ASP D CG  
15693 O OD1 . ASP D 410 ? 0.8465 0.8723 0.9337 0.1439  0.0994  -0.0104 410 ASP D OD1 
15694 O OD2 . ASP D 410 ? 0.8114 0.8774 0.8779 0.1283  0.1012  0.0002  410 ASP D OD2 
15695 N N   . GLY D 411 ? 0.4274 0.4299 0.3535 0.0901  0.0952  -0.0324 411 GLY D N   
15696 C CA  . GLY D 411 ? 0.3693 0.3682 0.2694 0.0753  0.0847  -0.0313 411 GLY D CA  
15697 C C   . GLY D 411 ? 0.3670 0.3839 0.2671 0.0673  0.0739  -0.0146 411 GLY D C   
15698 O O   . GLY D 411 ? 0.4530 0.4678 0.3384 0.0554  0.0652  -0.0124 411 GLY D O   
15699 N N   . ASN D 412 ? 0.4086 0.4436 0.3263 0.0730  0.0745  -0.0039 412 ASN D N   
15700 C CA  . ASN D 412 ? 0.2904 0.3407 0.2078 0.0661  0.0641  0.0099  412 ASN D CA  
15701 C C   . ASN D 412 ? 0.3591 0.4323 0.2826 0.0696  0.0703  0.0129  412 ASN D C   
15702 O O   . ASN D 412 ? 0.3633 0.4413 0.2897 0.0763  0.0838  0.0058  412 ASN D O   
15703 C CB  . ASN D 412 ? 0.2920 0.3348 0.2274 0.0671  0.0521  0.0233  412 ASN D CB  
15704 C CG  . ASN D 412 ? 0.2967 0.3421 0.2648 0.0806  0.0543  0.0264  412 ASN D CG  
15705 O OD1 . ASN D 412 ? 0.2829 0.3487 0.2661 0.0854  0.0596  0.0277  412 ASN D OD1 
15706 N ND2 . ASN D 412 ? 0.3892 0.4137 0.3715 0.0867  0.0498  0.0282  412 ASN D ND2 
15707 N N   . PHE D 413 ? 0.2613 0.3473 0.1858 0.0642  0.0613  0.0232  413 PHE D N   
15708 C CA  . PHE D 413 ? 0.2381 0.3430 0.1679 0.0647  0.0649  0.0271  413 PHE D CA  
15709 C C   . PHE D 413 ? 0.2612 0.3766 0.2223 0.0692  0.0604  0.0363  413 PHE D C   
15710 O O   . PHE D 413 ? 0.2994 0.4291 0.2674 0.0667  0.0592  0.0413  413 PHE D O   
15711 C CB  . PHE D 413 ? 0.2248 0.3363 0.1352 0.0559  0.0576  0.0294  413 PHE D CB  
15712 C CG  . PHE D 413 ? 0.2315 0.3372 0.1162 0.0513  0.0590  0.0207  413 PHE D CG  
15713 C CD1 . PHE D 413 ? 0.3007 0.3961 0.1765 0.0454  0.0529  0.0179  413 PHE D CD1 
15714 C CD2 . PHE D 413 ? 0.2710 0.3718 0.1517 0.0473  0.0601  0.0148  413 PHE D CD2 
15715 C CE1 . PHE D 413 ? 0.2442 0.3346 0.1050 0.0389  0.0514  0.0089  413 PHE D CE1 
15716 C CE2 . PHE D 413 ? 0.2948 0.3858 0.1610 0.0407  0.0559  0.0068  413 PHE D CE2 
15717 C CZ  . PHE D 413 ? 0.2459 0.3333 0.1042 0.0367  0.0516  0.0031  413 PHE D CZ  
15718 N N   . LEU D 414 ? 0.2433 0.3512 0.2254 0.0758  0.0566  0.0387  414 LEU D N   
15719 C CA  . LEU D 414 ? 0.2350 0.3544 0.2491 0.0800  0.0477  0.0480  414 LEU D CA  
15720 C C   . LEU D 414 ? 0.2305 0.3688 0.2739 0.0862  0.0605  0.0462  414 LEU D C   
15721 O O   . LEU D 414 ? 0.2241 0.3770 0.2986 0.0882  0.0528  0.0533  414 LEU D O   
15722 C CB  . LEU D 414 ? 0.2513 0.3561 0.2809 0.0866  0.0377  0.0526  414 LEU D CB  
15723 C CG  . LEU D 414 ? 0.2573 0.3478 0.2644 0.0783  0.0209  0.0613  414 LEU D CG  
15724 C CD1 . LEU D 414 ? 0.2791 0.3526 0.3018 0.0854  0.0097  0.0692  414 LEU D CD1 
15725 C CD2 . LEU D 414 ? 0.2436 0.3487 0.2450 0.0707  0.0092  0.0686  414 LEU D CD2 
15726 N N   . LYS D 415 ? 0.2368 0.3762 0.2709 0.0884  0.0796  0.0372  415 LYS D N   
15727 C CA  . LYS D 415 ? 0.2429 0.4012 0.3006 0.0919  0.0955  0.0364  415 LYS D CA  
15728 C C   . LYS D 415 ? 0.2613 0.4314 0.3096 0.0822  0.0961  0.0424  415 LYS D C   
15729 O O   . LYS D 415 ? 0.3511 0.5377 0.4219 0.0822  0.1080  0.0449  415 LYS D O   
15730 C CB  . LYS D 415 ? 0.3118 0.4644 0.3583 0.0982  0.1175  0.0241  415 LYS D CB  
15731 C CG  . LYS D 415 ? 0.3531 0.5239 0.4369 0.1066  0.1363  0.0214  415 LYS D CG  
15732 C CD  . LYS D 415 ? 0.4309 0.6062 0.5613 0.1174  0.1280  0.0232  415 LYS D CD  
15733 C CE  . LYS D 415 ? 0.6112 0.8125 0.7886 0.1247  0.1458  0.0217  415 LYS D CE  
15734 N NZ  . LYS D 415 ? 0.5677 0.7906 0.7536 0.1138  0.1489  0.0310  415 LYS D NZ  
15735 N N   . TRP D 416 ? 0.2149 0.3767 0.2333 0.0740  0.0844  0.0445  416 TRP D N   
15736 C CA  . TRP D 416 ? 0.2063 0.3746 0.2148 0.0661  0.0837  0.0493  416 TRP D CA  
15737 C C   . TRP D 416 ? 0.1948 0.3641 0.2047 0.0598  0.0643  0.0547  416 TRP D C   
15738 O O   . TRP D 416 ? 0.2473 0.4223 0.2595 0.0540  0.0624  0.0585  416 TRP D O   
15739 C CB  . TRP D 416 ? 0.2137 0.3718 0.1823 0.0633  0.0899  0.0448  416 TRP D CB  
15740 C CG  . TRP D 416 ? 0.2346 0.3829 0.1940 0.0650  0.1037  0.0364  416 TRP D CG  
15741 C CD1 . TRP D 416 ? 0.2875 0.4341 0.2452 0.0607  0.1141  0.0362  416 TRP D CD1 
15742 C CD2 . TRP D 416 ? 0.2489 0.3865 0.1976 0.0704  0.1087  0.0262  416 TRP D CD2 
15743 N NE1 . TRP D 416 ? 0.3729 0.5099 0.3177 0.0623  0.1249  0.0257  416 TRP D NE1 
15744 C CE2 . TRP D 416 ? 0.3564 0.4873 0.2966 0.0686  0.1216  0.0187  416 TRP D CE2 
15745 C CE3 . TRP D 416 ? 0.2582 0.3895 0.2028 0.0757  0.1036  0.0225  416 TRP D CE3 
15746 C CZ2 . TRP D 416 ? 0.3818 0.5017 0.3096 0.0726  0.1297  0.0059  416 TRP D CZ2 
15747 C CZ3 . TRP D 416 ? 0.3332 0.4518 0.2671 0.0809  0.1122  0.0107  416 TRP D CZ3 
15748 C CH2 . TRP D 416 ? 0.3830 0.4963 0.3087 0.0795  0.1249  0.0016  416 TRP D CH2 
15749 N N   . ILE D 417 ? 0.2168 0.3788 0.2234 0.0602  0.0505  0.0550  417 ILE D N   
15750 C CA  . ILE D 417 ? 0.2100 0.3708 0.2074 0.0537  0.0337  0.0581  417 ILE D CA  
15751 C C   . ILE D 417 ? 0.1937 0.3489 0.1967 0.0558  0.0204  0.0619  417 ILE D C   
15752 O O   . ILE D 417 ? 0.2030 0.3493 0.2080 0.0615  0.0239  0.0610  417 ILE D O   
15753 C CB  . ILE D 417 ? 0.3039 0.4567 0.2667 0.0486  0.0338  0.0536  417 ILE D CB  
15754 C CG1 . ILE D 417 ? 0.2465 0.4015 0.2025 0.0422  0.0214  0.0545  417 ILE D CG1 
15755 C CG2 . ILE D 417 ? 0.2609 0.4017 0.2045 0.0490  0.0337  0.0500  417 ILE D CG2 
15756 C CD1 . ILE D 417 ? 0.1774 0.3293 0.1097 0.0391  0.0238  0.0494  417 ILE D CD1 
15757 N N   . GLY D 418 ? 0.2483 0.4063 0.2522 0.0512  0.0043  0.0663  418 GLY D N   
15758 C CA  . GLY D 418 ? 0.2579 0.4077 0.2564 0.0514  -0.0107 0.0720  418 GLY D CA  
15759 C C   . GLY D 418 ? 0.2902 0.4484 0.3195 0.0553  -0.0257 0.0792  418 GLY D C   
15760 O O   . GLY D 418 ? 0.3889 0.5374 0.4145 0.0576  -0.0384 0.0862  418 GLY D O   
15761 N N   . ASN D 419 ? 0.2502 0.4258 0.3107 0.0555  -0.0257 0.0787  419 ASN D N   
15762 C CA  . ASN D 419 ? 0.2697 0.4574 0.3634 0.0577  -0.0431 0.0846  419 ASN D CA  
15763 C C   . ASN D 419 ? 0.3739 0.5755 0.4801 0.0494  -0.0486 0.0819  419 ASN D C   
15764 O O   . ASN D 419 ? 0.3769 0.5784 0.4727 0.0441  -0.0356 0.0766  419 ASN D O   
15765 C CB  . ASN D 419 ? 0.2853 0.4836 0.4236 0.0692  -0.0360 0.0865  419 ASN D CB  
15766 C CG  . ASN D 419 ? 0.3444 0.5559 0.5031 0.0700  -0.0123 0.0806  419 ASN D CG  
15767 O OD1 . ASN D 419 ? 0.3814 0.5832 0.5167 0.0706  0.0061  0.0753  419 ASN D OD1 
15768 N ND2 . ASN D 419 ? 0.3684 0.6024 0.5702 0.0691  -0.0129 0.0818  419 ASN D ND2 
15769 N N   . LYS D 420 ? 0.3158 0.5280 0.4453 0.0481  -0.0696 0.0858  420 LYS D N   
15770 C CA  . LYS D 420 ? 0.3300 0.5518 0.4687 0.0383  -0.0796 0.0820  420 LYS D CA  
15771 C C   . LYS D 420 ? 0.3359 0.5703 0.5036 0.0352  -0.0606 0.0787  420 LYS D C   
15772 O O   . LYS D 420 ? 0.3928 0.6254 0.5538 0.0259  -0.0608 0.0742  420 LYS D O   
15773 C CB  . LYS D 420 ? 0.4729 0.7073 0.6397 0.0381  -0.1065 0.0865  420 LYS D CB  
15774 C CG  . LYS D 420 ? 0.4534 0.6941 0.6243 0.0262  -0.1218 0.0806  420 LYS D CG  
15775 C CD  . LYS D 420 ? 0.6921 0.9303 0.8483 0.0237  -0.1535 0.0829  420 LYS D CD  
15776 C CE  . LYS D 420 ? 0.6257 0.8402 0.7181 0.0224  -0.1560 0.0828  420 LYS D CE  
15777 N NZ  . LYS D 420 ? 0.4835 0.6879 0.5534 0.0218  -0.1810 0.0845  420 LYS D NZ  
15778 N N   . GLU D 421 ? 0.2894 0.5344 0.4876 0.0428  -0.0431 0.0810  421 GLU D N   
15779 C CA  . GLU D 421 ? 0.3566 0.6133 0.5789 0.0389  -0.0225 0.0798  421 GLU D CA  
15780 C C   . GLU D 421 ? 0.3873 0.6281 0.5708 0.0383  -0.0014 0.0770  421 GLU D C   
15781 O O   . GLU D 421 ? 0.4422 0.6803 0.6193 0.0303  0.0058  0.0763  421 GLU D O   
15782 C CB  . GLU D 421 ? 0.5235 0.8020 0.7974 0.0469  -0.0109 0.0824  421 GLU D CB  
15783 C CG  . GLU D 421 ? 0.6120 0.9109 0.9267 0.0390  0.0024  0.0835  421 GLU D CG  
15784 C CD  . GLU D 421 ? 0.5407 0.8379 0.8545 0.0246  -0.0130 0.0829  421 GLU D CD  
15785 O OE1 . GLU D 421 ? 0.5794 0.8632 0.8673 0.0169  -0.0019 0.0821  421 GLU D OE1 
15786 O OE2 . GLU D 421 ? 0.6685 0.9762 1.0070 0.0214  -0.0376 0.0829  421 GLU D OE2 
15787 N N   . LYS D 422 ? 0.6027 0.3789 0.5797 0.0891  0.0252  -0.0081 422 LYS D N   
15788 C CA  . LYS D 422 ? 0.5718 0.3540 0.5293 0.0858  0.0383  -0.0139 422 LYS D CA  
15789 C C   . LYS D 422 ? 0.5369 0.3183 0.4677 0.0867  0.0379  -0.0146 422 LYS D C   
15790 O O   . LYS D 422 ? 0.5489 0.3401 0.4715 0.0854  0.0433  -0.0185 422 LYS D O   
15791 C CB  . LYS D 422 ? 0.5328 0.3055 0.4810 0.0820  0.0502  -0.0167 422 LYS D CB  
15792 C CG  . LYS D 422 ? 0.5857 0.3591 0.5525 0.0827  0.0548  -0.0177 422 LYS D CG  
15793 C CD  . LYS D 422 ? 0.5797 0.3405 0.5347 0.0787  0.0661  -0.0224 422 LYS D CD  
15794 C CE  . LYS D 422 ? 0.5408 0.2968 0.5120 0.0818  0.0704  -0.0218 422 LYS D CE  
15795 N NZ  . LYS D 422 ? 0.4857 0.2473 0.4553 0.0834  0.0812  -0.0260 422 LYS D NZ  
15796 N N   . ASN D 423 ? 0.5096 0.2779 0.4234 0.0905  0.0317  -0.0103 423 ASN D N   
15797 C CA  . ASN D 423 ? 0.4679 0.2332 0.3524 0.0946  0.0312  -0.0106 423 ASN D CA  
15798 C C   . ASN D 423 ? 0.4697 0.2456 0.3611 0.0973  0.0208  -0.0126 423 ASN D C   
15799 O O   . ASN D 423 ? 0.4457 0.2244 0.3177 0.1004  0.0222  -0.0146 423 ASN D O   
15800 C CB  . ASN D 423 ? 0.4113 0.1545 0.2674 0.1008  0.0281  -0.0048 423 ASN D CB  
15801 C CG  . ASN D 423 ? 0.5028 0.2325 0.3468 0.0983  0.0424  -0.0013 423 ASN D CG  
15802 O OD1 . ASN D 423 ? 0.5741 0.3105 0.4288 0.0914  0.0536  -0.0053 423 ASN D OD1 
15803 N ND2 . ASN D 423 ? 0.4478 0.1558 0.2684 0.1040  0.0418  0.0065  423 ASN D ND2 
15804 N N   . GLU D 424 ? 0.3825 0.1639 0.3050 0.0963  0.0112  -0.0112 424 GLU D N   
15805 C CA  . GLU D 424 ? 0.3529 0.1409 0.2859 0.0979  0.0013  -0.0119 424 GLU D CA  
15806 C C   . GLU D 424 ? 0.4588 0.2638 0.4030 0.0950  0.0095  -0.0151 424 GLU D C   
15807 O O   . GLU D 424 ? 0.4971 0.3057 0.4341 0.0970  0.0056  -0.0168 424 GLU D O   
15808 C CB  . GLU D 424 ? 0.4350 0.2221 0.4031 0.0976  -0.0089 -0.0064 424 GLU D CB  
15809 C CG  . GLU D 424 ? 0.5683 0.3547 0.5399 0.0998  -0.0214 -0.0061 424 GLU D CG  
15810 C CD  . GLU D 424 ? 0.7049 0.4785 0.6304 0.1055  -0.0312 -0.0124 424 GLU D CD  
15811 O OE1 . GLU D 424 ? 0.6635 0.4184 0.5578 0.1108  -0.0399 -0.0126 424 GLU D OE1 
15812 O OE2 . GLU D 424 ? 0.5967 0.3772 0.5157 0.1060  -0.0290 -0.0163 424 GLU D OE2 
15813 N N   . TYR D 425 ? 0.4012 0.2140 0.3587 0.0914  0.0199  -0.0160 425 TYR D N   
15814 C CA  . TYR D 425 ? 0.3686 0.1938 0.3263 0.0902  0.0278  -0.0184 425 TYR D CA  
15815 C C   . TYR D 425 ? 0.4109 0.2379 0.3389 0.0909  0.0333  -0.0213 425 TYR D C   
15816 O O   . TYR D 425 ? 0.4857 0.3215 0.4114 0.0923  0.0333  -0.0221 425 TYR D O   
15817 C CB  . TYR D 425 ? 0.4769 0.3044 0.4421 0.0883  0.0385  -0.0190 425 TYR D CB  
15818 C CG  . TYR D 425 ? 0.5668 0.3999 0.5586 0.0903  0.0377  -0.0154 425 TYR D CG  
15819 C CD1 . TYR D 425 ? 0.5257 0.3578 0.5442 0.0922  0.0224  -0.0121 425 TYR D CD1 
15820 C CD2 . TYR D 425 ? 0.5707 0.4074 0.5586 0.0910  0.0520  -0.0146 425 TYR D CD2 
15821 C CE1 . TYR D 425 ? 0.5338 0.3679 0.5703 0.0956  0.0215  -0.0073 425 TYR D CE1 
15822 C CE2 . TYR D 425 ? 0.5304 0.3707 0.5390 0.0941  0.0559  -0.0085 425 TYR D CE2 
15823 C CZ  . TYR D 425 ? 0.5875 0.4279 0.6217 0.0960  0.0416  -0.0042 425 TYR D CZ  
15824 O OH  . TYR D 425 ? 0.6775 0.5220 0.7338 0.0987  0.0483  0.0042  425 TYR D OH  
15825 N N   . TRP D 426 ? 0.3437 0.1621 0.2521 0.0903  0.0381  -0.0222 426 TRP D N   
15826 C CA  . TRP D 426 ? 0.3228 0.1437 0.2100 0.0914  0.0440  -0.0239 426 TRP D CA  
15827 C C   . TRP D 426 ? 0.3462 0.1671 0.2213 0.0977  0.0372  -0.0226 426 TRP D C   
15828 O O   . TRP D 426 ? 0.4335 0.2648 0.3036 0.0997  0.0399  -0.0237 426 TRP D O   
15829 C CB  . TRP D 426 ? 0.3382 0.1465 0.2116 0.0898  0.0519  -0.0235 426 TRP D CB  
15830 C CG  . TRP D 426 ? 0.3382 0.1458 0.2179 0.0832  0.0598  -0.0276 426 TRP D CG  
15831 C CD1 . TRP D 426 ? 0.3442 0.1416 0.2321 0.0797  0.0616  -0.0277 426 TRP D CD1 
15832 C CD2 . TRP D 426 ? 0.3369 0.1525 0.2132 0.0799  0.0656  -0.0334 426 TRP D CD2 
15833 N NE1 . TRP D 426 ? 0.4005 0.1967 0.2872 0.0744  0.0684  -0.0340 426 TRP D NE1 
15834 C CE2 . TRP D 426 ? 0.3694 0.1756 0.2477 0.0742  0.0700  -0.0380 426 TRP D CE2 
15835 C CE3 . TRP D 426 ? 0.3322 0.1611 0.2034 0.0820  0.0664  -0.0355 426 TRP D CE3 
15836 C CZ2 . TRP D 426 ? 0.3783 0.1846 0.2489 0.0701  0.0736  -0.0462 426 TRP D CZ2 
15837 C CZ3 . TRP D 426 ? 0.3380 0.1697 0.2046 0.0784  0.0702  -0.0425 426 TRP D CZ3 
15838 C CH2 . TRP D 426 ? 0.3667 0.1852 0.2305 0.0722  0.0729  -0.0486 426 TRP D CH2 
15839 N N   . LYS D 427 ? 0.4019 0.2100 0.2712 0.1016  0.0274  -0.0208 427 LYS D N   
15840 C CA  . LYS D 427 ? 0.4858 0.2886 0.3375 0.1087  0.0194  -0.0213 427 LYS D CA  
15841 C C   . LYS D 427 ? 0.3379 0.1531 0.2072 0.1078  0.0141  -0.0233 427 LYS D C   
15842 O O   . LYS D 427 ? 0.3428 0.1607 0.1997 0.1126  0.0139  -0.0245 427 LYS D O   
15843 C CB  . LYS D 427 ? 0.4688 0.2517 0.3086 0.1132  0.0062  -0.0203 427 LYS D CB  
15844 C CG  . LYS D 427 ? 0.5458 0.3114 0.3453 0.1240  0.0024  -0.0207 427 LYS D CG  
15845 C CD  . LYS D 427 ? 0.6280 0.3690 0.4083 0.1294  -0.0130 -0.0203 427 LYS D CD  
15846 C CE  . LYS D 427 ? 0.6953 0.4303 0.4823 0.1258  -0.0083 -0.0153 427 LYS D CE  
15847 N NZ  . LYS D 427 ? 0.5805 0.3023 0.3743 0.1263  -0.0275 -0.0143 427 LYS D NZ  
15848 N N   . ILE D 428 ? 0.3220 0.1440 0.2217 0.1026  0.0116  -0.0225 428 ILE D N   
15849 C CA  . ILE D 428 ? 0.3098 0.1418 0.2285 0.1019  0.0095  -0.0224 428 ILE D CA  
15850 C C   . ILE D 428 ? 0.3013 0.1460 0.2118 0.1024  0.0198  -0.0230 428 ILE D C   
15851 O O   . ILE D 428 ? 0.4251 0.2747 0.3346 0.1054  0.0179  -0.0233 428 ILE D O   
15852 C CB  . ILE D 428 ? 0.2980 0.1339 0.2535 0.0976  0.0086  -0.0189 428 ILE D CB  
15853 C CG1 . ILE D 428 ? 0.3080 0.1327 0.2787 0.0976  -0.0033 -0.0161 428 ILE D CG1 
15854 C CG2 . ILE D 428 ? 0.3060 0.1514 0.2807 0.0975  0.0102  -0.0168 428 ILE D CG2 
15855 C CD1 . ILE D 428 ? 0.2978 0.1272 0.3121 0.0942  -0.0005 -0.0094 428 ILE D CD1 
15856 N N   . LEU D 429 ? 0.2980 0.1469 0.2033 0.0995  0.0298  -0.0234 429 LEU D N   
15857 C CA  . LEU D 429 ? 0.2940 0.1541 0.1924 0.1000  0.0376  -0.0243 429 LEU D CA  
15858 C C   . LEU D 429 ? 0.3007 0.1645 0.1841 0.1049  0.0383  -0.0248 429 LEU D C   
15859 O O   . LEU D 429 ? 0.3724 0.2465 0.2567 0.1083  0.0393  -0.0244 429 LEU D O   
15860 C CB  . LEU D 429 ? 0.2961 0.1558 0.1904 0.0955  0.0462  -0.0265 429 LEU D CB  
15861 C CG  . LEU D 429 ? 0.2979 0.1674 0.1837 0.0960  0.0519  -0.0293 429 LEU D CG  
15862 C CD1 . LEU D 429 ? 0.3277 0.2038 0.2175 0.0993  0.0514  -0.0273 429 LEU D CD1 
15863 C CD2 . LEU D 429 ? 0.3073 0.1710 0.1862 0.0907  0.0581  -0.0344 429 LEU D CD2 
15864 N N   . ILE D 430 ? 0.3532 0.2080 0.2227 0.1068  0.0393  -0.0246 430 ILE D N   
15865 C CA  . ILE D 430 ? 0.3766 0.2350 0.2325 0.1128  0.0446  -0.0236 430 ILE D CA  
15866 C C   . ILE D 430 ? 0.4952 0.3531 0.3477 0.1192  0.0376  -0.0235 430 ILE D C   
15867 O O   . ILE D 430 ? 0.5540 0.4234 0.4077 0.1236  0.0420  -0.0228 430 ILE D O   
15868 C CB  . ILE D 430 ? 0.3654 0.2098 0.2032 0.1153  0.0497  -0.0214 430 ILE D CB  
15869 C CG1 . ILE D 430 ? 0.3412 0.1835 0.1838 0.1086  0.0574  -0.0219 430 ILE D CG1 
15870 C CG2 . ILE D 430 ? 0.3881 0.2369 0.2133 0.1230  0.0592  -0.0184 430 ILE D CG2 
15871 C CD1 . ILE D 430 ? 0.3631 0.1883 0.1881 0.1113  0.0645  -0.0182 430 ILE D CD1 
15872 N N   . GLU D 431 ? 0.4803 0.3244 0.3305 0.1201  0.0262  -0.0249 431 GLU D N   
15873 C CA  . GLU D 431 ? 0.4015 0.2416 0.2487 0.1255  0.0184  -0.0267 431 GLU D CA  
15874 C C   . GLU D 431 ? 0.4131 0.2666 0.2824 0.1231  0.0182  -0.0261 431 GLU D C   
15875 O O   . GLU D 431 ? 0.6289 0.4841 0.4969 0.1282  0.0168  -0.0267 431 GLU D O   
15876 C CB  . GLU D 431 ? 0.4334 0.2540 0.2752 0.1266  0.0037  -0.0296 431 GLU D CB  
15877 C CG  . GLU D 431 ? 0.7295 0.5379 0.5564 0.1344  -0.0052 -0.0333 431 GLU D CG  
15878 C CD  . GLU D 431 ? 0.9815 0.7706 0.7684 0.1449  -0.0056 -0.0343 431 GLU D CD  
15879 O OE1 . GLU D 431 ? 1.0521 0.8477 0.8265 0.1494  0.0092  -0.0304 431 GLU D OE1 
15880 O OE2 . GLU D 431 ? 0.9648 0.7312 0.7331 0.1492  -0.0209 -0.0384 431 GLU D OE2 
15881 N N   . ALA D 432 ? 0.3088 0.1696 0.1961 0.1166  0.0205  -0.0244 432 ALA D N   
15882 C CA  . ALA D 432 ? 0.3057 0.1772 0.2078 0.1164  0.0227  -0.0220 432 ALA D CA  
15883 C C   . ALA D 432 ? 0.3900 0.2750 0.2842 0.1208  0.0303  -0.0211 432 ALA D C   
15884 O O   . ALA D 432 ? 0.4614 0.3526 0.3602 0.1254  0.0297  -0.0192 432 ALA D O   
15885 C CB  . ALA D 432 ? 0.2874 0.1606 0.2040 0.1111  0.0259  -0.0198 432 ALA D CB  
15886 N N   . LYS D 433 ? 0.3371 0.2271 0.2230 0.1197  0.0372  -0.0220 433 LYS D N   
15887 C CA  . LYS D 433 ? 0.3422 0.2479 0.2274 0.1242  0.0440  -0.0214 433 LYS D CA  
15888 C C   . LYS D 433 ? 0.3372 0.2468 0.2199 0.1321  0.0451  -0.0200 433 LYS D C   
15889 O O   . LYS D 433 ? 0.3669 0.2914 0.2565 0.1382  0.0482  -0.0179 433 LYS D O   
15890 C CB  . LYS D 433 ? 0.3158 0.2248 0.1970 0.1205  0.0516  -0.0236 433 LYS D CB  
15891 C CG  . LYS D 433 ? 0.3403 0.2688 0.2260 0.1257  0.0591  -0.0236 433 LYS D CG  
15892 C CD  . LYS D 433 ? 0.4538 0.3936 0.3433 0.1304  0.0554  -0.0236 433 LYS D CD  
15893 C CE  . LYS D 433 ? 0.4567 0.4204 0.3588 0.1228  0.0534  -0.0221 433 LYS D CE  
15894 N NZ  . LYS D 433 ? 0.5413 0.5182 0.4570 0.1216  0.0610  -0.0187 433 LYS D NZ  
15895 N N   . LYS D 434 ? 0.4053 0.3008 0.2765 0.1338  0.0427  -0.0210 434 LYS D N   
15896 C CA  . LYS D 434 ? 0.4240 0.3186 0.2874 0.1428  0.0454  -0.0202 434 LYS D CA  
15897 C C   . LYS D 434 ? 0.4706 0.3659 0.3422 0.1466  0.0393  -0.0204 434 LYS D C   
15898 O O   . LYS D 434 ? 0.4542 0.3587 0.3292 0.1542  0.0442  -0.0185 434 LYS D O   
15899 C CB  . LYS D 434 ? 0.3572 0.2305 0.1981 0.1458  0.0427  -0.0221 434 LYS D CB  
15900 C CG  . LYS D 434 ? 0.5194 0.3907 0.3489 0.1458  0.0525  -0.0195 434 LYS D CG  
15901 C CD  . LYS D 434 ? 0.4905 0.3471 0.2944 0.1563  0.0575  -0.0180 434 LYS D CD  
15902 C CE  . LYS D 434 ? 0.5040 0.3472 0.2888 0.1567  0.0631  -0.0150 434 LYS D CE  
15903 N NZ  . LYS D 434 ? 0.6929 0.5127 0.4613 0.1551  0.0475  -0.0188 434 LYS D NZ  
15904 N N   . LYS D 435 ? 0.4112 0.2971 0.2894 0.1417  0.0296  -0.0220 435 LYS D N   
15905 C CA  . LYS D 435 ? 0.3653 0.2493 0.2545 0.1442  0.0241  -0.0215 435 LYS D CA  
15906 C C   . LYS D 435 ? 0.4418 0.3379 0.3470 0.1417  0.0254  -0.0166 435 LYS D C   
15907 O O   . LYS D 435 ? 0.5439 0.4365 0.4619 0.1420  0.0210  -0.0144 435 LYS D O   
15908 C CB  . LYS D 435 ? 0.5155 0.3796 0.4055 0.1416  0.0128  -0.0255 435 LYS D CB  
15909 C CG  . LYS D 435 ? 0.6029 0.4502 0.4719 0.1493  0.0088  -0.0308 435 LYS D CG  
15910 C CD  . LYS D 435 ? 0.6651 0.4915 0.5361 0.1472  -0.0058 -0.0356 435 LYS D CD  
15911 C CE  . LYS D 435 ? 0.6916 0.5121 0.5622 0.1404  -0.0115 -0.0362 435 LYS D CE  
15912 N NZ  . LYS D 435 ? 0.6362 0.4359 0.4735 0.1467  -0.0187 -0.0414 435 LYS D NZ  
15913 N N   . ALA D 436 ? 0.3840 0.2925 0.2877 0.1404  0.0314  -0.0147 436 ALA D N   
15914 C CA  . ALA D 436 ? 0.3656 0.2815 0.2752 0.1405  0.0328  -0.0103 436 ALA D CA  
15915 C C   . ALA D 436 ? 0.3605 0.2873 0.2755 0.1493  0.0328  -0.0052 436 ALA D C   
15916 O O   . ALA D 436 ? 0.4004 0.3364 0.3168 0.1555  0.0346  -0.0053 436 ALA D O   
15917 C CB  . ALA D 436 ? 0.3988 0.3222 0.3008 0.1385  0.0381  -0.0119 436 ALA D CB  
15918 N N   . LYS D 437 ? 0.3600 0.2858 0.2792 0.1508  0.0321  0.0007  437 LYS D N   
15919 C CA  . LYS D 437 ? 0.3076 0.2423 0.2321 0.1596  0.0311  0.0077  437 LYS D CA  
15920 C C   . LYS D 437 ? 0.3134 0.2551 0.2289 0.1663  0.0331  0.0149  437 LYS D C   
15921 O O   . LYS D 437 ? 0.4454 0.3983 0.3631 0.1754  0.0304  0.0220  437 LYS D O   
15922 C CB  . LYS D 437 ? 0.3118 0.2342 0.2503 0.1578  0.0271  0.0103  437 LYS D CB  
15923 C CG  . LYS D 437 ? 0.3511 0.2685 0.2942 0.1594  0.0238  0.0046  437 LYS D CG  
15924 C CD  . LYS D 437 ? 0.5510 0.4494 0.5017 0.1525  0.0178  -0.0007 437 LYS D CD  
15925 C CE  . LYS D 437 ? 0.5631 0.4531 0.5022 0.1545  0.0162  -0.0092 437 LYS D CE  
15926 N NZ  . LYS D 437 ? 0.3826 0.2544 0.3233 0.1484  0.0087  -0.0147 437 LYS D NZ  
15927 N N   . ASN D 438 ? 0.3192 0.2536 0.2230 0.1633  0.0373  0.0138  438 ASN D N   
15928 C CA  . ASN D 438 ? 0.3307 0.2678 0.2171 0.1695  0.0394  0.0193  438 ASN D CA  
15929 C C   . ASN D 438 ? 0.3376 0.2722 0.2083 0.1590  0.0419  0.0106  438 ASN D C   
15930 O O   . ASN D 438 ? 0.3626 0.2899 0.2382 0.1537  0.0449  0.0030  438 ASN D O   
15931 C CB  . ASN D 438 ? 0.3399 0.2637 0.2263 0.1745  0.0454  0.0312  438 ASN D CB  
15932 C CG  . ASN D 438 ? 0.3311 0.2416 0.2321 0.1625  0.0508  0.0299  438 ASN D CG  
15933 O OD1 . ASN D 438 ? 0.3365 0.2386 0.2278 0.1607  0.0591  0.0295  438 ASN D OD1 
15934 N ND2 . ASN D 438 ? 0.4078 0.3159 0.3335 0.1553  0.0449  0.0286  438 ASN D ND2 
15935 N N   . ASP D 439 ? 0.3488 0.2864 0.1976 0.1568  0.0396  0.0117  439 ASP D N   
15936 C CA  . ASP D 439 ? 0.3580 0.2914 0.1883 0.1472  0.0394  0.0020  439 ASP D CA  
15937 C C   . ASP D 439 ? 0.3953 0.3077 0.2192 0.1456  0.0524  0.0000  439 ASP D C   
15938 O O   . ASP D 439 ? 0.3961 0.3005 0.2025 0.1391  0.0539  -0.0083 439 ASP D O   
15939 C CB  . ASP D 439 ? 0.5677 0.5051 0.3710 0.1471  0.0301  0.0027  439 ASP D CB  
15940 C CG  . ASP D 439 ? 0.8300 0.7892 0.6430 0.1408  0.0139  -0.0022 439 ASP D CG  
15941 O OD1 . ASP D 439 ? 0.8185 0.7947 0.6602 0.1432  0.0119  0.0009  439 ASP D OD1 
15942 O OD2 . ASP D 439 ? 0.8983 0.8565 0.6917 0.1339  0.0033  -0.0090 439 ASP D OD2 
15943 N N   . TYR D 440 ? 0.4029 0.3056 0.2439 0.1511  0.0610  0.0074  440 TYR D N   
15944 C CA  . TYR D 440 ? 0.3581 0.2451 0.2049 0.1484  0.0720  0.0068  440 TYR D CA  
15945 C C   . TYR D 440 ? 0.3336 0.2219 0.1915 0.1361  0.0665  -0.0030 440 TYR D C   
15946 O O   . TYR D 440 ? 0.4119 0.2916 0.2752 0.1293  0.0715  -0.0041 440 TYR D O   
15947 C CB  . TYR D 440 ? 0.4037 0.2879 0.2796 0.1478  0.0748  0.0186  440 TYR D CB  
15948 C CG  . TYR D 440 ? 0.4159 0.2914 0.2845 0.1561  0.0891  0.0316  440 TYR D CG  
15949 C CD1 . TYR D 440 ? 0.4211 0.2869 0.2917 0.1532  0.1025  0.0352  440 TYR D CD1 
15950 C CD2 . TYR D 440 ? 0.4792 0.3562 0.3400 0.1679  0.0906  0.0424  440 TYR D CD2 
15951 C CE1 . TYR D 440 ? 0.4947 0.3519 0.3578 0.1622  0.1197  0.0493  440 TYR D CE1 
15952 C CE2 . TYR D 440 ? 0.5046 0.3718 0.3562 0.1770  0.1065  0.0571  440 TYR D CE2 
15953 C CZ  . TYR D 440 ? 0.5144 0.3716 0.3664 0.1743  0.1225  0.0606  440 TYR D CZ  
15954 O OH  . TYR D 440 ? 0.4752 0.3223 0.3173 0.1848  0.1425  0.0773  440 TYR D OH  
15955 N N   . ILE D 441 ? 0.3225 0.2215 0.1850 0.1349  0.0580  -0.0086 441 ILE D N   
15956 C CA  . ILE D 441 ? 0.3961 0.2951 0.2637 0.1254  0.0552  -0.0163 441 ILE D CA  
15957 C C   . ILE D 441 ? 0.3586 0.2518 0.2069 0.1204  0.0584  -0.0243 441 ILE D C   
15958 O O   . ILE D 441 ? 0.3968 0.2829 0.2501 0.1120  0.0598  -0.0282 441 ILE D O   
15959 C CB  . ILE D 441 ? 0.3276 0.2392 0.2015 0.1278  0.0497  -0.0185 441 ILE D CB  
15960 C CG1 . ILE D 441 ? 0.2969 0.2047 0.1777 0.1198  0.0489  -0.0222 441 ILE D CG1 
15961 C CG2 . ILE D 441 ? 0.3628 0.2910 0.2286 0.1282  0.0459  -0.0207 441 ILE D CG2 
15962 C CD1 . ILE D 441 ? 0.2893 0.1879 0.1827 0.1168  0.0449  -0.0190 441 ILE D CD1 
15963 N N   . LEU D 442 ? 0.3678 0.2645 0.1950 0.1224  0.0561  -0.0261 442 LEU D N   
15964 C CA  . LEU D 442 ? 0.3773 0.2654 0.1834 0.1148  0.0547  -0.0352 442 LEU D CA  
15965 C C   . LEU D 442 ? 0.4187 0.2868 0.2173 0.1148  0.0662  -0.0349 442 LEU D C   
15966 O O   . LEU D 442 ? 0.4539 0.3118 0.2480 0.1069  0.0671  -0.0424 442 LEU D O   
15967 C CB  . LEU D 442 ? 0.3899 0.2855 0.1752 0.1147  0.0437  -0.0360 442 LEU D CB  
15968 C CG  . LEU D 442 ? 0.4440 0.3654 0.2464 0.1138  0.0304  -0.0324 442 LEU D CG  
15969 C CD1 . LEU D 442 ? 0.5329 0.4581 0.3123 0.1141  0.0166  -0.0329 442 LEU D CD1 
15970 C CD2 . LEU D 442 ? 0.4398 0.3728 0.2645 0.1036  0.0261  -0.0375 442 LEU D CD2 
15971 N N   . VAL D 443 ? 0.4719 0.3369 0.2758 0.1216  0.0741  -0.0241 443 VAL D N   
15972 C CA  . VAL D 443 ? 0.3864 0.2386 0.1948 0.1203  0.0855  -0.0199 443 VAL D CA  
15973 C C   . VAL D 443 ? 0.3628 0.2159 0.2010 0.1127  0.0849  -0.0204 443 VAL D C   
15974 O O   . VAL D 443 ? 0.4065 0.2503 0.2461 0.1088  0.0903  -0.0229 443 VAL D O   
15975 C CB  . VAL D 443 ? 0.4002 0.2497 0.2116 0.1304  0.0963  -0.0059 443 VAL D CB  
15976 C CG1 . VAL D 443 ? 0.4434 0.2797 0.2554 0.1312  0.1112  -0.0008 443 VAL D CG1 
15977 C CG2 . VAL D 443 ? 0.4311 0.2812 0.2111 0.1397  0.0948  -0.0037 443 VAL D CG2 
15978 N N   . ALA D 444 ? 0.3501 0.2132 0.2100 0.1116  0.0773  -0.0181 444 ALA D N   
15979 C CA  . ALA D 444 ? 0.3296 0.1925 0.2121 0.1053  0.0736  -0.0188 444 ALA D CA  
15980 C C   . ALA D 444 ? 0.3646 0.2247 0.2393 0.0985  0.0704  -0.0278 444 ALA D C   
15981 O O   . ALA D 444 ? 0.4481 0.3049 0.3363 0.0944  0.0685  -0.0279 444 ALA D O   
15982 C CB  . ALA D 444 ? 0.3045 0.1752 0.2049 0.1064  0.0647  -0.0153 444 ALA D CB  
15983 N N   . GLU D 445 ? 0.3431 0.2035 0.1968 0.0975  0.0692  -0.0352 445 GLU D N   
15984 C CA  . GLU D 445 ? 0.3632 0.2182 0.2104 0.0906  0.0676  -0.0439 445 GLU D CA  
15985 C C   . GLU D 445 ? 0.4199 0.2597 0.2539 0.0867  0.0722  -0.0503 445 GLU D C   
15986 O O   . GLU D 445 ? 0.4357 0.2665 0.2633 0.0805  0.0707  -0.0585 445 GLU D O   
15987 C CB  . GLU D 445 ? 0.3615 0.2239 0.1953 0.0915  0.0626  -0.0501 445 GLU D CB  
15988 C CG  . GLU D 445 ? 0.3919 0.2694 0.2392 0.0965  0.0598  -0.0445 445 GLU D CG  
15989 C CD  . GLU D 445 ? 0.4776 0.3756 0.3249 0.0965  0.0521  -0.0436 445 GLU D CD  
15990 O OE1 . GLU D 445 ? 0.4995 0.3986 0.3340 0.0918  0.0460  -0.0481 445 GLU D OE1 
15991 O OE2 . GLU D 445 ? 0.4376 0.3496 0.2975 0.1015  0.0507  -0.0383 445 GLU D OE2 
15992 N N   . GLY D 446 ? 0.5972 0.2923 0.1583 0.0540  0.0486  0.0025  446 GLY D N   
15993 C CA  . GLY D 446 ? 0.6293 0.3028 0.1718 0.0652  0.0642  0.0015  446 GLY D CA  
15994 C C   . GLY D 446 ? 0.6544 0.2935 0.1793 0.0680  0.0699  0.0061  446 GLY D C   
15995 O O   . GLY D 446 ? 0.6540 0.2849 0.1789 0.0711  0.0653  0.0198  446 GLY D O   
15996 N N   . SER D 447 ? 0.6792 0.2980 0.1895 0.0671  0.0782  -0.0040 447 SER D N   
15997 C CA  . SER D 447 ? 0.7113 0.2899 0.1988 0.0703  0.0842  -0.0009 447 SER D CA  
15998 C C   . SER D 447 ? 0.7343 0.2951 0.2136 0.0944  0.0969  0.0186  447 SER D C   
15999 O O   . SER D 447 ? 0.7500 0.2918 0.2364 0.0982  0.0916  0.0272  447 SER D O   
16000 C CB  . SER D 447 ? 0.7341 0.2971 0.2117 0.0642  0.0925  -0.0145 447 SER D CB  
16001 O OG  . SER D 447 ? 0.7558 0.3127 0.2264 0.0808  0.1090  -0.0125 447 SER D OG  
16002 N N   . ASP D 448 ? 0.7264 0.3087 0.2252 0.1080  0.1077  0.0268  448 ASP D N   
16003 C CA  . ASP D 448 ? 0.7323 0.3184 0.2664 0.1272  0.1179  0.0431  448 ASP D CA  
16004 C C   . ASP D 448 ? 0.7073 0.3126 0.2861 0.1284  0.1003  0.0591  448 ASP D C   
16005 O O   . ASP D 448 ? 0.7184 0.3180 0.3235 0.1418  0.0997  0.0687  448 ASP D O   
16006 C CB  . ASP D 448 ? 0.7335 0.3362 0.2751 0.1382  0.1371  0.0466  448 ASP D CB  
16007 C CG  . ASP D 448 ? 0.7626 0.3466 0.2558 0.1381  0.1519  0.0297  448 ASP D CG  
16008 O OD1 . ASP D 448 ? 0.7416 0.3446 0.2370 0.1218  0.1349  0.0183  448 ASP D OD1 
16009 O OD2 . ASP D 448 ? 0.7949 0.3596 0.2792 0.1501  0.1713  0.0270  448 ASP D OD2 
16010 N N   . TRP D 449 ? 0.6756 0.3043 0.2647 0.1154  0.0847  0.0610  449 TRP D N   
16011 C CA  . TRP D 449 ? 0.6523 0.3020 0.2847 0.1156  0.0676  0.0744  449 TRP D CA  
16012 C C   . TRP D 449 ? 0.6692 0.2945 0.2934 0.1145  0.0512  0.0761  449 TRP D C   
16013 O O   . TRP D 449 ? 0.6678 0.3017 0.3281 0.1249  0.0400  0.0877  449 TRP D O   
16014 C CB  . TRP D 449 ? 0.6191 0.2939 0.2581 0.1002  0.0551  0.0735  449 TRP D CB  
16015 C CG  . TRP D 449 ? 0.6125 0.3004 0.2419 0.1002  0.0688  0.0700  449 TRP D CG  
16016 C CD1 . TRP D 449 ? 0.6087 0.2955 0.2045 0.0886  0.0653  0.0569  449 TRP D CD1 
16017 C CD2 . TRP D 449 ? 0.6147 0.3164 0.2661 0.1134  0.0881  0.0792  449 TRP D CD2 
16018 N NE1 . TRP D 449 ? 0.6111 0.3079 0.2023 0.0959  0.0783  0.0588  449 TRP D NE1 
16019 C CE2 . TRP D 449 ? 0.6165 0.3200 0.2385 0.1101  0.0944  0.0730  449 TRP D CE2 
16020 C CE3 . TRP D 449 ? 0.6187 0.3306 0.3122 0.1279  0.1015  0.0910  449 TRP D CE3 
16021 C CZ2 . TRP D 449 ? 0.6765 0.3855 0.3016 0.1204  0.1146  0.0804  449 TRP D CZ2 
16022 C CZ3 . TRP D 449 ? 0.6257 0.3463 0.3281 0.1359  0.1245  0.0965  449 TRP D CZ3 
16023 C CH2 . TRP D 449 ? 0.6622 0.3783 0.3265 0.1320  0.1314  0.0923  449 TRP D CH2 
16024 N N   . PHE D 450 ? 0.6896 0.2827 0.2655 0.1020  0.0494  0.0638  450 PHE D N   
16025 C CA  . PHE D 450 ? 0.7163 0.2761 0.2725 0.1000  0.0365  0.0659  450 PHE D CA  
16026 C C   . PHE D 450 ? 0.7567 0.2841 0.3045 0.1184  0.0471  0.0691  450 PHE D C   
16027 O O   . PHE D 450 ? 0.7871 0.2889 0.3293 0.1253  0.0343  0.0769  450 PHE D O   
16028 C CB  . PHE D 450 ? 0.7257 0.2614 0.2340 0.0763  0.0340  0.0502  450 PHE D CB  
16029 C CG  . PHE D 450 ? 0.6880 0.2555 0.2034 0.0591  0.0272  0.0428  450 PHE D CG  
16030 C CD1 . PHE D 450 ? 0.6665 0.2504 0.1998 0.0504  0.0081  0.0495  450 PHE D CD1 
16031 C CD2 . PHE D 450 ? 0.6765 0.2577 0.1820 0.0532  0.0387  0.0284  450 PHE D CD2 
16032 C CE1 . PHE D 450 ? 0.6303 0.2459 0.1780 0.0352  0.0026  0.0409  450 PHE D CE1 
16033 C CE2 . PHE D 450 ? 0.6372 0.2546 0.1662 0.0395  0.0300  0.0201  450 PHE D CE2 
16034 C CZ  . PHE D 450 ? 0.6155 0.2476 0.1623 0.0307  0.0135  0.0267  450 PHE D CZ  
16035 N N   . TRP D 451 ? 0.8378 0.3630 0.3818 0.1274  0.0696  0.0631  451 TRP D N   
16036 C CA  . TRP D 451 ? 0.8559 0.3511 0.3957 0.1460  0.0819  0.0652  451 TRP D CA  
16037 C C   . TRP D 451 ? 0.8414 0.3566 0.4363 0.1689  0.0753  0.0812  451 TRP D C   
16038 O O   . TRP D 451 ? 0.8342 0.3228 0.4303 0.1843  0.0695  0.0873  451 TRP D O   
16039 C CB  . TRP D 451 ? 0.8689 0.3592 0.3912 0.1489  0.1085  0.0530  451 TRP D CB  
16040 C CG  . TRP D 451 ? 1.0235 0.4699 0.5205 0.1595  0.1232  0.0477  451 TRP D CG  
16041 C CD1 . TRP D 451 ? 1.0533 0.4583 0.4992 0.1470  0.1308  0.0326  451 TRP D CD1 
16042 C CD2 . TRP D 451 ? 1.0665 0.5053 0.5907 0.1844  0.1336  0.0559  451 TRP D CD2 
16043 N NE1 . TRP D 451 ? 1.0599 0.4290 0.4963 0.1626  0.1454  0.0320  451 TRP D NE1 
16044 C CE2 . TRP D 451 ? 1.1128 0.5021 0.5969 0.1866  0.1468  0.0463  451 TRP D CE2 
16045 C CE3 . TRP D 451 ? 1.0744 0.5439 0.6563 0.2045  0.1343  0.0686  451 TRP D CE3 
16046 C CZ2 . TRP D 451 ? 1.1463 0.5150 0.6447 0.2099  0.1595  0.0501  451 TRP D CZ2 
16047 C CZ3 . TRP D 451 ? 1.2429 0.6953 0.8425 0.2274  0.1469  0.0710  451 TRP D CZ3 
16048 C CH2 . TRP D 451 ? 1.1397 0.5415 0.6969 0.2307  0.1588  0.0624  451 TRP D CH2 
16049 N N   . TRP D 452 ? 0.8463 0.4075 0.4885 0.1719  0.0762  0.0872  452 TRP D N   
16050 C CA  . TRP D 452 ? 0.7589 0.3465 0.4634 0.1924  0.0742  0.0984  452 TRP D CA  
16051 C C   . TRP D 452 ? 0.8406 0.4452 0.5751 0.1920  0.0433  0.1077  452 TRP D C   
16052 O O   . TRP D 452 ? 0.7968 0.4435 0.5848 0.1938  0.0378  0.1131  452 TRP D O   
16053 C CB  . TRP D 452 ? 0.7340 0.3586 0.4734 0.1943  0.0954  0.0987  452 TRP D CB  
16054 C CG  . TRP D 452 ? 0.8204 0.4288 0.5414 0.2030  0.1261  0.0915  452 TRP D CG  
16055 C CD1 . TRP D 452 ? 0.7584 0.3658 0.4466 0.1941  0.1455  0.0835  452 TRP D CD1 
16056 C CD2 . TRP D 452 ? 0.8291 0.4184 0.5614 0.2235  0.1403  0.0907  452 TRP D CD2 
16057 N NE1 . TRP D 452 ? 0.9695 0.5579 0.6453 0.2065  0.1714  0.0774  452 TRP D NE1 
16058 C CE2 . TRP D 452 ? 0.8980 0.4753 0.6022 0.2241  0.1700  0.0815  452 TRP D CE2 
16059 C CE3 . TRP D 452 ? 0.8780 0.4582 0.6407 0.2427  0.1295  0.0963  452 TRP D CE3 
16060 C CZ2 . TRP D 452 ? 1.0021 0.5589 0.7088 0.2415  0.1917  0.0772  452 TRP D CZ2 
16061 C CZ3 . TRP D 452 ? 0.9807 0.5410 0.7485 0.2614  0.1501  0.0925  452 TRP D CZ3 
16062 C CH2 . TRP D 452 ? 1.0576 0.6066 0.7983 0.2599  0.1822  0.0828  452 TRP D CH2 
16063 N N   . GLN D 453 ? 0.9867 0.5557 0.6843 0.1892  0.0237  0.1090  453 GLN D N   
16064 C CA  . GLN D 453 ? 0.8271 0.4042 0.5398 0.1884  -0.0078 0.1168  453 GLN D CA  
16065 C C   . GLN D 453 ? 0.8148 0.3503 0.5029 0.2013  -0.0227 0.1207  453 GLN D C   
16066 O O   . GLN D 453 ? 1.0086 0.5100 0.6644 0.2043  -0.0074 0.1154  453 GLN D O   
16067 C CB  . GLN D 453 ? 0.8774 0.4565 0.5585 0.1611  -0.0185 0.1125  453 GLN D CB  
16068 C CG  . GLN D 453 ? 0.8636 0.4922 0.5820 0.1497  -0.0131 0.1110  453 GLN D CG  
16069 C CD  . GLN D 453 ? 0.9199 0.5903 0.7042 0.1586  -0.0299 0.1192  453 GLN D CD  
16070 O OE1 . GLN D 453 ? 0.9202 0.5937 0.7065 0.1527  -0.0560 0.1221  453 GLN D OE1 
16071 N NE2 . GLN D 453 ? 0.8816 0.5838 0.7199 0.1717  -0.0137 0.1214  453 GLN D NE2 
16072 N N   . GLY D 454 ? 0.8938 0.4417 0.6029 0.2044  -0.0524 0.1270  454 GLY D N   
16073 C CA  . GLY D 454 ? 0.9411 0.4626 0.6353 0.2133  -0.0684 0.1295  454 GLY D CA  
16074 C C   . GLY D 454 ? 1.2307 0.7690 0.9833 0.2446  -0.0762 0.1358  454 GLY D C   
16075 O O   . GLY D 454 ? 1.2967 0.8745 1.1109 0.2589  -0.0739 0.1378  454 GLY D O   
16076 N N   . GLU D 455 ? 1.5088 1.0161 1.2431 0.2559  -0.0838 0.1377  455 GLU D N   
16077 C CA  . GLU D 455 ? 1.5206 1.0422 1.3104 0.2860  -0.0948 0.1424  455 GLU D CA  
16078 C C   . GLU D 455 ? 1.5912 1.1185 1.4136 0.3029  -0.0660 0.1380  455 GLU D C   
16079 O O   . GLU D 455 ? 1.5781 1.1237 1.4578 0.3283  -0.0715 0.1391  455 GLU D O   
16080 C CB  . GLU D 455 ? 1.4144 0.8963 1.1677 0.2929  -0.1110 0.1465  455 GLU D CB  
16081 C CG  . GLU D 455 ? 1.5402 1.0433 1.3507 0.3218  -0.1360 0.1527  455 GLU D CG  
16082 C CD  . GLU D 455 ? 1.3702 0.9251 1.2338 0.3240  -0.1619 0.1549  455 GLU D CD  
16083 O OE1 . GLU D 455 ? 1.4913 1.0395 1.3215 0.3119  -0.1842 0.1573  455 GLU D OE1 
16084 O OE2 . GLU D 455 ? 1.1621 0.7643 1.1009 0.3377  -0.1582 0.1523  455 GLU D OE2 
16085 N N   . GLU D 456 ? 1.5486 1.0626 1.3379 0.2895  -0.0347 0.1315  456 GLU D N   
16086 C CA  . GLU D 456 ? 1.6388 1.1587 1.4540 0.3034  -0.0029 0.1261  456 GLU D CA  
16087 C C   . GLU D 456 ? 1.5922 1.1666 1.4800 0.3134  0.0036  0.1273  456 GLU D C   
16088 O O   . GLU D 456 ? 1.4714 1.0641 1.3552 0.2982  0.0191  0.1261  456 GLU D O   
16089 C CB  . GLU D 456 ? 1.5734 1.0625 1.3270 0.2851  0.0276  0.1179  456 GLU D CB  
16090 C CG  . GLU D 456 ? 1.3653 0.8513 1.0745 0.2571  0.0236  0.1162  456 GLU D CG  
16091 C CD  . GLU D 456 ? 1.3908 0.8425 1.0376 0.2396  0.0489  0.1051  456 GLU D CD  
16092 O OE1 . GLU D 456 ? 1.0805 0.5306 0.7307 0.2469  0.0770  0.0992  456 GLU D OE1 
16093 O OE2 . GLU D 456 ? 1.4633 0.8903 1.0589 0.2182  0.0415  0.1005  456 GLU D OE2 
16094 N N   . LYS D 457 ? 1.4869 1.0908 1.4459 0.3376  -0.0074 0.1281  457 LYS D N   
16095 C CA  . LYS D 457 ? 1.3788 1.0400 1.4192 0.3474  0.0002  0.1272  457 LYS D CA  
16096 C C   . LYS D 457 ? 1.3501 1.0210 1.4160 0.3536  0.0438  0.1199  457 LYS D C   
16097 O O   . LYS D 457 ? 1.2145 0.9007 1.3340 0.3734  0.0510  0.1140  457 LYS D O   
16098 C CB  . LYS D 457 ? 1.3339 1.0272 1.4435 0.3677  -0.0343 0.1276  457 LYS D CB  
16099 C CG  . LYS D 457 ? 1.1589 0.8390 1.2349 0.3583  -0.0769 0.1346  457 LYS D CG  
16100 C CD  . LYS D 457 ? 1.1753 0.8710 1.2991 0.3788  -0.1099 0.1368  457 LYS D CD  
16101 C CE  . LYS D 457 ? 1.2901 0.9626 1.4232 0.3994  -0.1006 0.1345  457 LYS D CE  
16102 N NZ  . LYS D 457 ? 0.9544 0.6568 1.1518 0.4241  -0.1251 0.1370  457 LYS D NZ  
16103 N N   . ALA D 458 ? 1.4269 1.0930 1.4517 0.3303  0.0710  0.1168  458 ALA D N   
16104 C CA  . ALA D 458 ? 1.2600 0.9220 1.2780 0.3292  0.1137  0.1096  458 ALA D CA  
16105 C C   . ALA D 458 ? 1.0856 0.7960 1.1475 0.3162  0.1339  0.1080  458 ALA D C   
16106 O O   . ALA D 458 ? 0.9857 0.7315 1.0859 0.3088  0.1134  0.1118  458 ALA D O   
16107 C CB  . ALA D 458 ? 1.2113 0.8228 1.1378 0.3137  0.1237  0.1067  458 ALA D CB  
16108 N N   . PRO D 459 ? 1.0411 0.7528 1.0995 0.3136  0.1738  0.1024  459 PRO D N   
16109 C CA  . PRO D 459 ? 0.8674 0.6230 0.9792 0.3066  0.1952  0.1018  459 PRO D CA  
16110 C C   . PRO D 459 ? 0.8451 0.6149 0.9344 0.2818  0.1856  0.1069  459 PRO D C   
16111 O O   . PRO D 459 ? 0.9385 0.6813 0.9576 0.2670  0.1765  0.1081  459 PRO D O   
16112 C CB  . PRO D 459 ? 0.9548 0.6944 1.0472 0.3095  0.2408  0.0952  459 PRO D CB  
16113 C CG  . PRO D 459 ? 1.0251 0.7155 1.0570 0.3176  0.2412  0.0911  459 PRO D CG  
16114 C CD  . PRO D 459 ? 1.0745 0.7452 1.0685 0.3115  0.2014  0.0963  459 PRO D CD  
16115 N N   . PHE D 460 ? 0.8876 0.7015 1.0423 0.2774  0.1886  0.1083  460 PHE D N   
16116 C CA  . PHE D 460 ? 0.8355 0.6666 0.9816 0.2553  0.1887  0.1127  460 PHE D CA  
16117 C C   . PHE D 460 ? 0.7116 0.5264 0.8029 0.2406  0.1541  0.1168  460 PHE D C   
16118 O O   . PHE D 460 ? 0.6620 0.4566 0.6912 0.2257  0.1595  0.1173  460 PHE D O   
16119 C CB  . PHE D 460 ? 0.7903 0.6080 0.8998 0.2470  0.2293  0.1120  460 PHE D CB  
16120 C CG  . PHE D 460 ? 0.8106 0.6439 0.9730 0.2577  0.2686  0.1077  460 PHE D CG  
16121 C CD1 . PHE D 460 ? 0.7748 0.6510 1.0205 0.2565  0.2759  0.1069  460 PHE D CD1 
16122 C CD2 . PHE D 460 ? 0.7644 0.5695 0.8951 0.2677  0.2997  0.1025  460 PHE D CD2 
16123 C CE1 . PHE D 460 ? 0.7075 0.5983 1.0057 0.2646  0.3156  0.1008  460 PHE D CE1 
16124 C CE2 . PHE D 460 ? 0.7638 0.5818 0.9430 0.2765  0.3390  0.0973  460 PHE D CE2 
16125 C CZ  . PHE D 460 ? 0.7451 0.6061 1.0090 0.2747  0.3479  0.0963  460 PHE D CZ  
16126 N N   . VAL D 461 ? 0.6851 0.5094 0.8014 0.2455  0.1179  0.1185  461 VAL D N   
16127 C CA  . VAL D 461 ? 0.6439 0.4545 0.7140 0.2304  0.0861  0.1216  461 VAL D CA  
16128 C C   . VAL D 461 ? 0.6110 0.4556 0.7100 0.2130  0.0759  0.1240  461 VAL D C   
16129 O O   . VAL D 461 ? 0.6923 0.5260 0.7479 0.1963  0.0583  0.1253  461 VAL D O   
16130 C CB  . VAL D 461 ? 0.6626 0.4572 0.7297 0.2430  0.0512  0.1232  461 VAL D CB  
16131 C CG1 . VAL D 461 ? 0.7407 0.5047 0.7951 0.2641  0.0626  0.1210  461 VAL D CG1 
16132 C CG2 . VAL D 461 ? 0.6767 0.5130 0.8200 0.2509  0.0265  0.1238  461 VAL D CG2 
16133 N N   . GLU D 462 ? 0.5922 0.4771 0.7652 0.2157  0.0881  0.1230  462 GLU D N   
16134 C CA  . GLU D 462 ? 0.5609 0.4751 0.7606 0.1979  0.0837  0.1245  462 GLU D CA  
16135 C C   . GLU D 462 ? 0.5938 0.4932 0.7455 0.1824  0.1099  0.1273  462 GLU D C   
16136 O O   . GLU D 462 ? 0.6895 0.5906 0.8192 0.1654  0.0980  0.1293  462 GLU D O   
16137 C CB  . GLU D 462 ? 0.5495 0.5099 0.8449 0.2038  0.0925  0.1204  462 GLU D CB  
16138 C CG  . GLU D 462 ? 0.5480 0.5424 0.8861 0.1891  0.0715  0.1193  462 GLU D CG  
16139 C CD  . GLU D 462 ? 0.7733 0.7683 1.0937 0.1682  0.0939  0.1230  462 GLU D CD  
16140 O OE1 . GLU D 462 ? 0.6595 0.6715 1.0221 0.1661  0.1277  0.1219  462 GLU D OE1 
16141 O OE2 . GLU D 462 ? 0.6224 0.5992 0.8871 0.1542  0.0784  0.1266  462 GLU D OE2 
16142 N N   . VAL D 463 ? 0.5792 0.4623 0.7118 0.1892  0.1448  0.1268  463 VAL D N   
16143 C CA  . VAL D 463 ? 0.5846 0.4494 0.6648 0.1780  0.1681  0.1294  463 VAL D CA  
16144 C C   . VAL D 463 ? 0.5851 0.4199 0.5879 0.1692  0.1483  0.1282  463 VAL D C   
16145 O O   . VAL D 463 ? 0.5740 0.4054 0.5450 0.1554  0.1460  0.1298  463 VAL D O   
16146 C CB  . VAL D 463 ? 0.7605 0.6107 0.8319 0.1888  0.2090  0.1281  463 VAL D CB  
16147 C CG1 . VAL D 463 ? 0.7778 0.6139 0.8067 0.1787  0.2341  0.1324  463 VAL D CG1 
16148 C CG2 . VAL D 463 ? 0.8500 0.7300 1.0053 0.1999  0.2270  0.1256  463 VAL D CG2 
16149 N N   . PHE D 464 ? 0.6007 0.4125 0.5735 0.1770  0.1350  0.1241  464 PHE D N   
16150 C CA  . PHE D 464 ? 0.6061 0.3897 0.5101 0.1667  0.1184  0.1200  464 PHE D CA  
16151 C C   . PHE D 464 ? 0.6108 0.4067 0.5174 0.1514  0.0880  0.1211  464 PHE D C   
16152 O O   . PHE D 464 ? 0.6569 0.4411 0.5178 0.1375  0.0810  0.1174  464 PHE D O   
16153 C CB  . PHE D 464 ? 0.6306 0.3840 0.5062 0.1772  0.1125  0.1153  464 PHE D CB  
16154 C CG  . PHE D 464 ? 0.6589 0.3821 0.4804 0.1802  0.1356  0.1084  464 PHE D CG  
16155 C CD1 . PHE D 464 ? 0.7078 0.4088 0.4669 0.1673  0.1295  0.1006  464 PHE D CD1 
16156 C CD2 . PHE D 464 ? 0.7329 0.4511 0.5682 0.1957  0.1636  0.1074  464 PHE D CD2 
16157 C CE1 . PHE D 464 ? 0.8091 0.4843 0.5199 0.1699  0.1486  0.0916  464 PHE D CE1 
16158 C CE2 . PHE D 464 ? 0.7467 0.4360 0.5295 0.1982  0.1843  0.0996  464 PHE D CE2 
16159 C CZ  . PHE D 464 ? 0.7167 0.3850 0.4369 0.1854  0.1756  0.0915  464 PHE D CZ  
16160 N N   . ASP D 465 ? 0.5615 0.3815 0.5219 0.1538  0.0691  0.1245  465 ASP D N   
16161 C CA  . ASP D 465 ? 0.5905 0.4220 0.5534 0.1388  0.0411  0.1247  465 ASP D CA  
16162 C C   . ASP D 465 ? 0.5810 0.4348 0.5611 0.1254  0.0503  0.1268  465 ASP D C   
16163 O O   . ASP D 465 ? 0.5898 0.4393 0.5400 0.1101  0.0379  0.1246  465 ASP D O   
16164 C CB  . ASP D 465 ? 0.6230 0.4729 0.6355 0.1465  0.0158  0.1264  465 ASP D CB  
16165 C CG  . ASP D 465 ? 0.5269 0.3847 0.5358 0.1308  -0.0140 0.1256  465 ASP D CG  
16166 O OD1 . ASP D 465 ? 0.5584 0.3875 0.5108 0.1220  -0.0285 0.1230  465 ASP D OD1 
16167 O OD2 . ASP D 465 ? 0.6326 0.5245 0.6952 0.1262  -0.0209 0.1262  465 ASP D OD2 
16168 N N   . LYS D 466 ? 0.5483 0.4239 0.5767 0.1309  0.0735  0.1304  466 LYS D N   
16169 C CA  . LYS D 466 ? 0.4950 0.3860 0.5381 0.1188  0.0854  0.1336  466 LYS D CA  
16170 C C   . LYS D 466 ? 0.5554 0.4206 0.5320 0.1126  0.0969  0.1335  466 LYS D C   
16171 O O   . LYS D 466 ? 0.6448 0.5128 0.6090 0.0998  0.0897  0.1341  466 LYS D O   
16172 C CB  . LYS D 466 ? 0.4999 0.4123 0.6024 0.1254  0.1147  0.1367  466 LYS D CB  
16173 C CG  . LYS D 466 ? 0.5116 0.4406 0.6408 0.1120  0.1260  0.1403  466 LYS D CG  
16174 C CD  . LYS D 466 ? 0.6974 0.6527 0.9006 0.1156  0.1521  0.1405  466 LYS D CD  
16175 C CE  . LYS D 466 ? 0.7593 0.6938 0.9401 0.1219  0.1954  0.1449  466 LYS D CE  
16176 N NZ  . LYS D 466 ? 0.5322 0.4869 0.7791 0.1318  0.2207  0.1411  466 LYS D NZ  
16177 N N   . LEU D 467 ? 0.5351 0.3752 0.4693 0.1224  0.1135  0.1316  467 LEU D N   
16178 C CA  . LEU D 467 ? 0.5433 0.3599 0.4134 0.1188  0.1211  0.1290  467 LEU D CA  
16179 C C   . LEU D 467 ? 0.5297 0.3378 0.3618 0.1068  0.0929  0.1212  467 LEU D C   
16180 O O   . LEU D 467 ? 0.5900 0.3946 0.3936 0.0985  0.0893  0.1189  467 LEU D O   
16181 C CB  . LEU D 467 ? 0.5772 0.3695 0.4111 0.1318  0.1430  0.1259  467 LEU D CB  
16182 C CG  . LEU D 467 ? 0.6007 0.3910 0.4444 0.1402  0.1789  0.1324  467 LEU D CG  
16183 C CD1 . LEU D 467 ? 0.6289 0.4063 0.4713 0.1549  0.1996  0.1293  467 LEU D CD1 
16184 C CD2 . LEU D 467 ? 0.6653 0.4365 0.4531 0.1375  0.1888  0.1336  467 LEU D CD2 
16185 N N   . PHE D 468 ? 0.5276 0.3303 0.3583 0.1061  0.0735  0.1165  468 PHE D N   
16186 C CA  . PHE D 468 ? 0.5458 0.3373 0.3398 0.0927  0.0508  0.1076  468 PHE D CA  
16187 C C   . PHE D 468 ? 0.4980 0.3098 0.3143 0.0784  0.0338  0.1089  468 PHE D C   
16188 O O   . PHE D 468 ? 0.5670 0.3744 0.3538 0.0667  0.0252  0.1015  468 PHE D O   
16189 C CB  . PHE D 468 ? 0.5708 0.3455 0.3550 0.0951  0.0366  0.1042  468 PHE D CB  
16190 C CG  . PHE D 468 ? 0.5288 0.2892 0.2771 0.0791  0.0163  0.0948  468 PHE D CG  
16191 C CD1 . PHE D 468 ? 0.5550 0.2929 0.2520 0.0728  0.0207  0.0823  468 PHE D CD1 
16192 C CD2 . PHE D 468 ? 0.5514 0.3207 0.3176 0.0696  -0.0062 0.0965  468 PHE D CD2 
16193 C CE1 . PHE D 468 ? 0.6139 0.3390 0.2814 0.0563  0.0059  0.0713  468 PHE D CE1 
16194 C CE2 . PHE D 468 ? 0.5802 0.3333 0.3108 0.0536  -0.0211 0.0871  468 PHE D CE2 
16195 C CZ  . PHE D 468 ? 0.6262 0.3574 0.3091 0.0464  -0.0137 0.0742  468 PHE D CZ  
16196 N N   . ARG D 469 ? 0.5043 0.3399 0.3756 0.0792  0.0287  0.1162  469 ARG D N   
16197 C CA  . ARG D 469 ? 0.4774 0.3323 0.3725 0.0651  0.0138  0.1164  469 ARG D CA  
16198 C C   . ARG D 469 ? 0.4762 0.3351 0.3653 0.0607  0.0285  0.1186  469 ARG D C   
16199 O O   . ARG D 469 ? 0.4776 0.3400 0.3580 0.0481  0.0165  0.1145  469 ARG D O   
16200 C CB  . ARG D 469 ? 0.5417 0.4233 0.5009 0.0677  0.0063  0.1216  469 ARG D CB  
16201 C CG  . ARG D 469 ? 0.4573 0.3342 0.4212 0.0732  -0.0154 0.1198  469 ARG D CG  
16202 C CD  . ARG D 469 ? 0.4956 0.3574 0.4209 0.0591  -0.0405 0.1133  469 ARG D CD  
16203 N NE  . ARG D 469 ? 0.6065 0.4845 0.5647 0.0551  -0.0656 0.1134  469 ARG D NE  
16204 C CZ  . ARG D 469 ? 0.6339 0.5085 0.6040 0.0666  -0.0822 0.1153  469 ARG D CZ  
16205 N NH1 . ARG D 469 ? 0.4844 0.3390 0.4385 0.0826  -0.0749 0.1178  469 ARG D NH1 
16206 N NH2 . ARG D 469 ? 0.6012 0.4916 0.5989 0.0629  -0.1077 0.1142  469 ARG D NH2 
16207 N N   . SER D 470 ? 0.4797 0.3351 0.3712 0.0718  0.0551  0.1251  470 SER D N   
16208 C CA  . SER D 470 ? 0.4670 0.3190 0.3463 0.0703  0.0704  0.1295  470 SER D CA  
16209 C C   . SER D 470 ? 0.4773 0.3107 0.2973 0.0675  0.0620  0.1212  470 SER D C   
16210 O O   . SER D 470 ? 0.5998 0.4351 0.4129 0.0607  0.0565  0.1206  470 SER D O   
16211 C CB  . SER D 470 ? 0.4976 0.3427 0.3827 0.0830  0.1030  0.1380  470 SER D CB  
16212 O OG  . SER D 470 ? 0.5071 0.3744 0.4561 0.0817  0.1144  0.1445  470 SER D OG  
16213 N N   . PHE D 471 ? 0.4894 0.3054 0.2690 0.0729  0.0609  0.1131  471 PHE D N   
16214 C CA  . PHE D 471 ? 0.4959 0.2984 0.2251 0.0697  0.0515  0.1011  471 PHE D CA  
16215 C C   . PHE D 471 ? 0.4797 0.2913 0.2126 0.0534  0.0267  0.0910  471 PHE D C   
16216 O O   . PHE D 471 ? 0.5555 0.3668 0.2678 0.0483  0.0183  0.0826  471 PHE D O   
16217 C CB  . PHE D 471 ? 0.5193 0.3021 0.2093 0.0769  0.0566  0.0919  471 PHE D CB  
16218 C CG  . PHE D 471 ? 0.5507 0.3211 0.2283 0.0927  0.0824  0.0991  471 PHE D CG  
16219 C CD1 . PHE D 471 ? 0.5673 0.3324 0.2299 0.0997  0.0967  0.1058  471 PHE D CD1 
16220 C CD2 . PHE D 471 ? 0.5667 0.3272 0.2445 0.1008  0.0932  0.0986  471 PHE D CD2 
16221 C CE1 . PHE D 471 ? 0.5986 0.3511 0.2495 0.1122  0.1213  0.1099  471 PHE D CE1 
16222 C CE2 . PHE D 471 ? 0.5953 0.3435 0.2613 0.1146  0.1192  0.1037  471 PHE D CE2 
16223 C CZ  . PHE D 471 ? 0.6144 0.3565 0.2623 0.1203  0.1349  0.1104  471 PHE D CZ  
16224 N N   . VAL D 472 ? 0.4996 0.3181 0.2573 0.0459  0.0144  0.0910  472 VAL D N   
16225 C CA  . VAL D 472 ? 0.4499 0.2735 0.2078 0.0292  -0.0069 0.0815  472 VAL D CA  
16226 C C   . VAL D 472 ? 0.4766 0.3189 0.2650 0.0216  -0.0117 0.0858  472 VAL D C   
16227 O O   . VAL D 472 ? 0.5696 0.4143 0.3476 0.0105  -0.0230 0.0758  472 VAL D O   
16228 C CB  . VAL D 472 ? 0.4390 0.2584 0.2065 0.0252  -0.0188 0.0816  472 VAL D CB  
16229 C CG1 . VAL D 472 ? 0.4211 0.2500 0.2026 0.0088  -0.0385 0.0774  472 VAL D CG1 
16230 C CG2 . VAL D 472 ? 0.4608 0.2545 0.1849 0.0257  -0.0181 0.0714  472 VAL D CG2 
16231 N N   . ARG D 473 ? 0.4875 0.3432 0.3168 0.0269  -0.0017 0.0991  473 ARG D N   
16232 C CA  . ARG D 473 ? 0.5101 0.3804 0.3688 0.0194  -0.0027 0.1032  473 ARG D CA  
16233 C C   . ARG D 473 ? 0.4822 0.3424 0.3134 0.0242  0.0066  0.1033  473 ARG D C   
16234 O O   . ARG D 473 ? 0.4730 0.3375 0.3059 0.0158  -0.0026 0.0986  473 ARG D O   
16235 C CB  . ARG D 473 ? 0.4722 0.3586 0.3836 0.0230  0.0092  0.1152  473 ARG D CB  
16236 C CG  . ARG D 473 ? 0.4525 0.3559 0.4024 0.0110  0.0041  0.1165  473 ARG D CG  
16237 C CD  . ARG D 473 ? 0.5293 0.4412 0.5202 0.0156  0.0277  0.1280  473 ARG D CD  
16238 N NE  . ARG D 473 ? 0.6122 0.5251 0.6170 0.0281  0.0435  0.1335  473 ARG D NE  
16239 C CZ  . ARG D 473 ? 0.6872 0.6068 0.7287 0.0328  0.0687  0.1416  473 ARG D CZ  
16240 N NH1 . ARG D 473 ? 0.6365 0.5594 0.7024 0.0257  0.0823  0.1464  473 ARG D NH1 
16241 N NH2 . ARG D 473 ? 0.5682 0.4895 0.6231 0.0444  0.0825  0.1441  473 ARG D NH2 
16242 N N   . ARG D 474 ? 0.5120 0.3569 0.3157 0.0388  0.0242  0.1083  474 ARG D N   
16243 C CA  . ARG D 474 ? 0.5586 0.3894 0.3280 0.0469  0.0308  0.1089  474 ARG D CA  
16244 C C   . ARG D 474 ? 0.5664 0.3949 0.3034 0.0420  0.0108  0.0915  474 ARG D C   
16245 O O   . ARG D 474 ? 0.4961 0.3211 0.2194 0.0446  0.0063  0.0891  474 ARG D O   
16246 C CB  . ARG D 474 ? 0.5197 0.3317 0.2591 0.0636  0.0526  0.1161  474 ARG D CB  
16247 C CG  . ARG D 474 ? 0.5389 0.3360 0.2409 0.0736  0.0571  0.1145  474 ARG D CG  
16248 C CD  . ARG D 474 ? 0.5904 0.3861 0.3057 0.0716  0.0590  0.1237  474 ARG D CD  
16249 N NE  . ARG D 474 ? 0.7362 0.5159 0.4367 0.0826  0.0786  0.1312  474 ARG D NE  
16250 C CZ  . ARG D 474 ? 0.8633 0.6320 0.5338 0.0905  0.0721  0.1254  474 ARG D CZ  
16251 N NH1 . ARG D 474 ? 0.7568 0.5326 0.4142 0.0891  0.0477  0.1112  474 ARG D NH1 
16252 N NH2 . ARG D 474 ? 0.7246 0.4735 0.3778 0.1006  0.0912  0.1336  474 ARG D NH2 
16253 N N   . ALA D 475 ? 0.4988 0.3283 0.2249 0.0350  -0.0006 0.0782  475 ALA D N   
16254 C CA  . ALA D 475 ? 0.4384 0.2666 0.1371 0.0287  -0.0161 0.0581  475 ALA D CA  
16255 C C   . ALA D 475 ? 0.4417 0.2836 0.1614 0.0136  -0.0317 0.0497  475 ALA D C   
16256 O O   . ALA D 475 ? 0.4866 0.3323 0.1933 0.0081  -0.0428 0.0310  475 ALA D O   
16257 C CB  . ALA D 475 ? 0.4385 0.2628 0.1259 0.0228  -0.0189 0.0452  475 ALA D CB  
16258 N N   . GLN D 476 ? 0.4038 0.2564 0.1613 0.0063  -0.0320 0.0604  476 GLN D N   
16259 C CA  . GLN D 476 ? 0.4385 0.3030 0.2165 -0.0093 -0.0457 0.0518  476 GLN D CA  
16260 C C   . GLN D 476 ? 0.4832 0.3522 0.2825 -0.0061 -0.0415 0.0615  476 GLN D C   
16261 O O   . GLN D 476 ? 0.3759 0.2556 0.2027 -0.0190 -0.0493 0.0588  476 GLN D O   
16262 C CB  . GLN D 476 ? 0.3611 0.2325 0.1622 -0.0234 -0.0533 0.0523  476 GLN D CB  
16263 C CG  . GLN D 476 ? 0.4288 0.2894 0.2034 -0.0298 -0.0593 0.0408  476 GLN D CG  
16264 C CD  . GLN D 476 ? 0.5045 0.3649 0.2947 -0.0365 -0.0657 0.0469  476 GLN D CD  
16265 O OE1 . GLN D 476 ? 0.5478 0.4049 0.3321 -0.0517 -0.0777 0.0372  476 GLN D OE1 
16266 N NE2 . GLN D 476 ? 0.4845 0.3475 0.2939 -0.0244 -0.0580 0.0623  476 GLN D NE2 
16267 N N   . GLU D 477 ? 0.5251 0.3824 0.3088 0.0107  -0.0285 0.0724  477 GLU D N   
16268 C CA  . GLU D 477 ? 0.4656 0.3189 0.2640 0.0151  -0.0205 0.0842  477 GLU D CA  
16269 C C   . GLU D 477 ? 0.6297 0.4752 0.4026 0.0230  -0.0301 0.0752  477 GLU D C   
16270 O O   . GLU D 477 ? 0.6239 0.4648 0.3626 0.0312  -0.0381 0.0631  477 GLU D O   
16271 C CB  . GLU D 477 ? 0.4304 0.2696 0.2257 0.0287  0.0036  0.1041  477 GLU D CB  
16272 C CG  . GLU D 477 ? 0.5272 0.3782 0.3614 0.0223  0.0143  0.1130  477 GLU D CG  
16273 C CD  . GLU D 477 ? 0.6128 0.4551 0.4653 0.0288  0.0404  0.1310  477 GLU D CD  
16274 O OE1 . GLU D 477 ? 0.7864 0.6053 0.6026 0.0437  0.0566  0.1396  477 GLU D OE1 
16275 O OE2 . GLU D 477 ? 0.5071 0.3648 0.4092 0.0184  0.0455  0.1355  477 GLU D OE2 
16276 N N   . LEU D 478 ? 0.6072 0.4518 0.3999 0.0206  -0.0300 0.0799  478 LEU D N   
16277 C CA  . LEU D 478 ? 0.4325 0.2672 0.2068 0.0310  -0.0386 0.0746  478 LEU D CA  
16278 C C   . LEU D 478 ? 0.5598 0.3658 0.3021 0.0526  -0.0225 0.0936  478 LEU D C   
16279 O O   . LEU D 478 ? 0.6173 0.4128 0.3441 0.0595  -0.0061 0.1055  478 LEU D O   
16280 C CB  . LEU D 478 ? 0.4128 0.2571 0.2237 0.0176  -0.0451 0.0703  478 LEU D CB  
16281 C CG  . LEU D 478 ? 0.3748 0.2424 0.2206 -0.0065 -0.0542 0.0579  478 LEU D CG  
16282 C CD1 . LEU D 478 ? 0.3652 0.2385 0.2428 -0.0179 -0.0587 0.0535  478 LEU D CD1 
16283 C CD2 . LEU D 478 ? 0.4578 0.3363 0.2870 -0.0130 -0.0694 0.0358  478 LEU D CD2 
16284 N N   . GLU D 479 ? 0.5681 0.3577 0.2962 0.0645  -0.0265 0.0963  479 GLU D N   
16285 C CA  . GLU D 479 ? 0.5526 0.3066 0.2470 0.0839  -0.0087 0.1175  479 GLU D CA  
16286 C C   . GLU D 479 ? 0.5623 0.3020 0.2800 0.0805  0.0013  0.1298  479 GLU D C   
16287 O O   . GLU D 479 ? 0.5740 0.3054 0.2847 0.0884  -0.0124 0.1244  479 GLU D O   
16288 C CB  . GLU D 479 ? 0.5818 0.3306 0.2372 0.1028  -0.0213 0.1057  479 GLU D CB  
16289 C CG  . GLU D 479 ? 0.6822 0.4406 0.3324 0.1082  -0.0506 0.0854  479 GLU D CG  
16290 C CD  . GLU D 479 ? 0.6662 0.4032 0.3069 0.1230  -0.0547 0.0914  479 GLU D CD  
16291 O OE1 . GLU D 479 ? 0.6513 0.3692 0.2639 0.1386  -0.0470 0.0979  479 GLU D OE1 
16292 O OE2 . GLU D 479 ? 0.5925 0.3315 0.2552 0.1180  -0.0660 0.0877  479 GLU D OE2 
16293 N N   . HIS D 480 ? 0.6163 0.3532 0.3641 0.0693  0.0260  0.1452  480 HIS D N   
16294 C CA  . HIS D 480 ? 0.6187 0.3304 0.3773 0.0693  0.0473  0.1620  480 HIS D CA  
16295 C C   . HIS D 480 ? 0.5728 0.2888 0.3607 0.0606  0.0351  0.1548  480 HIS D C   
16296 O O   . HIS D 480 ? 0.6431 0.3339 0.4043 0.0755  0.0286  0.1571  480 HIS D O   
16297 C CB  . HIS D 480 ? 0.7021 0.3901 0.4197 0.0872  0.0570  0.1673  480 HIS D CB  
16298 C CG  . HIS D 480 ? 0.9174 0.5967 0.6401 0.0841  0.0879  0.1789  480 HIS D CG  
16299 N ND1 . HIS D 480 ? 0.8416 0.5165 0.6028 0.0705  0.1116  0.1888  480 HIS D ND1 
16300 C CD2 . HIS D 480 ? 1.0023 0.6756 0.6983 0.0926  0.1002  0.1801  480 HIS D CD2 
16301 C CE1 . HIS D 480 ? 0.8612 0.5286 0.6195 0.0713  0.1375  0.1953  480 HIS D CE1 
16302 N NE2 . HIS D 480 ? 0.9435 0.6081 0.6610 0.0851  0.1314  0.1910  480 HIS D NE2 
16303 N N   . HIS D 481 ? 0.5246 0.2737 0.3677 0.0369  0.0303  0.1443  481 HIS D N   
16304 C CA  . HIS D 481 ? 0.5019 0.2628 0.3799 0.0237  0.0180  0.1327  481 HIS D CA  
16305 C C   . HIS D 481 ? 0.4875 0.2569 0.4192 0.0028  0.0355  0.1383  481 HIS D C   
16306 O O   . HIS D 481 ? 0.6017 0.3724 0.5485 -0.0016 0.0558  0.1493  481 HIS D O   
16307 C CB  . HIS D 481 ? 0.4574 0.2530 0.3477 0.0126  -0.0094 0.1084  481 HIS D CB  
16308 C CG  . HIS D 481 ? 0.4277 0.2483 0.3327 0.0002  -0.0099 0.1047  481 HIS D CG  
16309 N ND1 . HIS D 481 ? 0.3981 0.2407 0.3495 -0.0210 -0.0081 0.1019  481 HIS D ND1 
16310 C CD2 . HIS D 481 ? 0.4449 0.2689 0.3230 0.0079  -0.0115 0.1043  481 HIS D CD2 
16311 C CE1 . HIS D 481 ? 0.4679 0.3259 0.4195 -0.0245 -0.0105 0.1002  481 HIS D CE1 
16312 N NE2 . HIS D 481 ? 0.4253 0.2718 0.3335 -0.0078 -0.0112 0.1018  481 HIS D NE2 
16313 N N   . HIS D 482 ? 0.4712 0.2485 0.4347 -0.0102 0.0273  0.1281  482 HIS D N   
16314 C CA  . HIS D 482 ? 0.4475 0.2435 0.4681 -0.0340 0.0350  0.1248  482 HIS D CA  
16315 C C   . HIS D 482 ? 0.4225 0.2334 0.4654 -0.0472 0.0151  0.1055  482 HIS D C   
16316 O O   . HIS D 482 ? 0.4305 0.2317 0.4489 -0.0363 0.0015  0.0978  482 HIS D O   
16317 C CB  . HIS D 482 ? 0.4826 0.2512 0.5190 -0.0351 0.0663  0.1424  482 HIS D CB  
16318 C CG  . HIS D 482 ? 0.5090 0.2491 0.5429 -0.0323 0.0703  0.1441  482 HIS D CG  
16319 N ND1 . HIS D 482 ? 0.5676 0.2652 0.5502 -0.0082 0.0752  0.1566  482 HIS D ND1 
16320 C CD2 . HIS D 482 ? 0.4974 0.2431 0.5724 -0.0495 0.0698  0.1347  482 HIS D CD2 
16321 C CE1 . HIS D 482 ? 0.5755 0.2526 0.5685 -0.0098 0.0777  0.1557  482 HIS D CE1 
16322 N NE2 . HIS D 482 ? 0.5381 0.2443 0.5881 -0.0356 0.0756  0.1420  482 HIS D NE2 
16323 N N   . HIS D 483 ? 0.3958 0.2312 0.4866 -0.0705 0.0134  0.0963  483 HIS D N   
16324 C CA  . HIS D 483 ? 0.3730 0.2221 0.4861 -0.0859 -0.0030 0.0769  483 HIS D CA  
16325 C C   . HIS D 483 ? 0.4106 0.2342 0.5356 -0.0852 0.0088  0.0801  483 HIS D C   
16326 O O   . HIS D 483 ? 0.3845 0.2170 0.5359 -0.1003 0.0009  0.0649  483 HIS D O   
16327 C CB  . HIS D 483 ? 0.3779 0.2589 0.5326 -0.1102 -0.0105 0.0656  483 HIS D CB  
16328 C CG  . HIS D 483 ? 0.3436 0.2469 0.4858 -0.1182 -0.0349 0.0478  483 HIS D CG  
16329 N ND1 . HIS D 483 ? 0.3559 0.2682 0.5013 -0.1295 -0.0481 0.0271  483 HIS D ND1 
16330 C CD2 . HIS D 483 ? 0.3623 0.2780 0.4840 -0.1153 -0.0449 0.0466  483 HIS D CD2 
16331 C CE1 . HIS D 483 ? 0.3664 0.2968 0.4880 -0.1294 -0.0602 0.0133  483 HIS D CE1 
16332 N NE2 . HIS D 483 ? 0.3373 0.2653 0.4506 -0.1275 -0.0640 0.0269  483 HIS D NE2 
# 
