data_9IHU
# 
_entry.id   9IHU 
# 
_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   9IHU         pdb_00009ihu 10.2210/pdb9ihu/pdb 
WWPDB D_1300048761 ?            ?                   
# 
_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                        9IHU 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-18 
_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 ? 
'Li, M.J.'    3 ? 
'Xu, Q.'      4 ? 
'Zhou, H.'    5 ? 
'Huang, L.Q.' 6 ? 
'Wang, Q.S.'  7 ? 
'Yu, F.'      8 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            8 
_citation.language                  ? 
_citation.page_first                806 
_citation.page_last                 806 
_citation.title                     
'The crystal structure of GH57 family amylopullulanase reveals its dual binding pockets sharing the same catalytic dyad.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-025-08192-8 
_citation.pdbx_database_id_PubMed   40419759 
_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 0009-0004-3840-9685 
primary 'Wang, W.'  2 0009-0007-7332-8217 
primary 'Li, M.'    3 ?                   
primary 'Xu, Q.'    4 ?                   
primary 'Zhou, H.'  5 ?                   
primary 'Huang, L.' 6 ?                   
primary 'Wang, Q.'  7 0000-0002-0614-6903 
primary 'Yu, F.'    8 0000-0002-9502-3277 
# 
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' 57253.234 2   ? ? ? ? 
2 water   nat water                                                                18.015    560 ? ? ? ? 
# 
_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
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKLFLVFWWHMHQPLYREPYTGEYLLPWTFFHAVKDYYDMPAYLKDFEIKLNFNLTPVLIDQIQEYAQGKAKDVFLEAI
RKDPDDLEKEEVEKLIEFTKLNYEKPIYRFERIRELMNKEKLNREELLDLQTLNLLAWCGRTLRKDLKDLLNKGRNYTQE
EKEYVLNKYFEIIKKTLSIYREIKEEGKGSVSTSPYYHPLIPILLNPNCVYETTPNVKIPDFAVSFREDASKHVELAKEK
YFEIFGEHPVYMWPPEASVSNEALELYYEKGINMLATDEVILKNSVERASPYLRYYFRELISVFFRDKTLSDLIGFSYHA
WNAEDAVRDFIGRLKKIHESVDFQPVVFVVLDGENCWEYYEENGIPFLEKLYSTLEKEEWIETLTLEEAMRKEDVKTEVI
ESVKAGTWFDGNFLKWIGNKEKNEYWKILIEAKKKAKNDYILVAEGSDWFWWQGEEKAPFVEVFDKLFRSFVRRAQE
;
_entity_poly.pdbx_strand_id                 A,B 
_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 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   477 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 aq_720 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Aquifex aeolicus (strain 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 
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 
# 
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 
C 2 HOH 1   501 436 HOH HOH A . 
C 2 HOH 2   502 328 HOH HOH A . 
C 2 HOH 3   503 365 HOH HOH A . 
C 2 HOH 4   504 200 HOH HOH A . 
C 2 HOH 5   505 471 HOH HOH A . 
C 2 HOH 6   506 535 HOH HOH A . 
C 2 HOH 7   507 205 HOH HOH A . 
C 2 HOH 8   508 429 HOH HOH A . 
C 2 HOH 9   509 211 HOH HOH A . 
C 2 HOH 10  510 290 HOH HOH A . 
C 2 HOH 11  511 103 HOH HOH A . 
C 2 HOH 12  512 167 HOH HOH A . 
C 2 HOH 13  513 217 HOH HOH A . 
C 2 HOH 14  514 363 HOH HOH A . 
C 2 HOH 15  515 267 HOH HOH A . 
C 2 HOH 16  516 314 HOH HOH A . 
C 2 HOH 17  517 47  HOH HOH A . 
C 2 HOH 18  518 170 HOH HOH A . 
C 2 HOH 19  519 84  HOH HOH A . 
C 2 HOH 20  520 254 HOH HOH A . 
C 2 HOH 21  521 401 HOH HOH A . 
C 2 HOH 22  522 180 HOH HOH A . 
C 2 HOH 23  523 244 HOH HOH A . 
C 2 HOH 24  524 282 HOH HOH A . 
C 2 HOH 25  525 507 HOH HOH A . 
C 2 HOH 26  526 543 HOH HOH A . 
C 2 HOH 27  527 367 HOH HOH A . 
C 2 HOH 28  528 53  HOH HOH A . 
C 2 HOH 29  529 215 HOH HOH A . 
C 2 HOH 30  530 49  HOH HOH A . 
C 2 HOH 31  531 140 HOH HOH A . 
C 2 HOH 32  532 356 HOH HOH A . 
C 2 HOH 33  533 264 HOH HOH A . 
C 2 HOH 34  534 275 HOH HOH A . 
C 2 HOH 35  535 329 HOH HOH A . 
C 2 HOH 36  536 224 HOH HOH A . 
C 2 HOH 37  537 52  HOH HOH A . 
C 2 HOH 38  538 226 HOH HOH A . 
C 2 HOH 39  539 497 HOH HOH A . 
C 2 HOH 40  540 294 HOH HOH A . 
C 2 HOH 41  541 345 HOH HOH A . 
C 2 HOH 42  542 304 HOH HOH A . 
C 2 HOH 43  543 353 HOH HOH A . 
C 2 HOH 44  544 90  HOH HOH A . 
C 2 HOH 45  545 86  HOH HOH A . 
C 2 HOH 46  546 136 HOH HOH A . 
C 2 HOH 47  547 241 HOH HOH A . 
C 2 HOH 48  548 377 HOH HOH A . 
C 2 HOH 49  549 107 HOH HOH A . 
C 2 HOH 50  550 547 HOH HOH A . 
C 2 HOH 51  551 135 HOH HOH A . 
C 2 HOH 52  552 42  HOH HOH A . 
C 2 HOH 53  553 120 HOH HOH A . 
C 2 HOH 54  554 116 HOH HOH A . 
C 2 HOH 55  555 362 HOH HOH A . 
C 2 HOH 56  556 485 HOH HOH A . 
C 2 HOH 57  557 56  HOH HOH A . 
C 2 HOH 58  558 157 HOH HOH A . 
C 2 HOH 59  559 182 HOH HOH A . 
C 2 HOH 60  560 225 HOH HOH A . 
C 2 HOH 61  561 337 HOH HOH A . 
C 2 HOH 62  562 36  HOH HOH A . 
C 2 HOH 63  563 19  HOH HOH A . 
C 2 HOH 64  564 374 HOH HOH A . 
C 2 HOH 65  565 544 HOH HOH A . 
C 2 HOH 66  566 82  HOH HOH A . 
C 2 HOH 67  567 81  HOH HOH A . 
C 2 HOH 68  568 221 HOH HOH A . 
C 2 HOH 69  569 197 HOH HOH A . 
C 2 HOH 70  570 149 HOH HOH A . 
C 2 HOH 71  571 20  HOH HOH A . 
C 2 HOH 72  572 332 HOH HOH A . 
C 2 HOH 73  573 171 HOH HOH A . 
C 2 HOH 74  574 122 HOH HOH A . 
C 2 HOH 75  575 516 HOH HOH A . 
C 2 HOH 76  576 446 HOH HOH A . 
C 2 HOH 77  577 159 HOH HOH A . 
C 2 HOH 78  578 556 HOH HOH A . 
C 2 HOH 79  579 62  HOH HOH A . 
C 2 HOH 80  580 400 HOH HOH A . 
C 2 HOH 81  581 61  HOH HOH A . 
C 2 HOH 82  582 76  HOH HOH A . 
C 2 HOH 83  583 137 HOH HOH A . 
C 2 HOH 84  584 29  HOH HOH A . 
C 2 HOH 85  585 179 HOH HOH A . 
C 2 HOH 86  586 440 HOH HOH A . 
C 2 HOH 87  587 41  HOH HOH A . 
C 2 HOH 88  588 468 HOH HOH A . 
C 2 HOH 89  589 368 HOH HOH A . 
C 2 HOH 90  590 93  HOH HOH A . 
C 2 HOH 91  591 256 HOH HOH A . 
C 2 HOH 92  592 26  HOH HOH A . 
C 2 HOH 93  593 118 HOH HOH A . 
C 2 HOH 94  594 162 HOH HOH A . 
C 2 HOH 95  595 67  HOH HOH A . 
C 2 HOH 96  596 70  HOH HOH A . 
C 2 HOH 97  597 127 HOH HOH A . 
C 2 HOH 98  598 209 HOH HOH A . 
C 2 HOH 99  599 557 HOH HOH A . 
C 2 HOH 100 600 502 HOH HOH A . 
C 2 HOH 101 601 432 HOH HOH A . 
C 2 HOH 102 602 51  HOH HOH A . 
C 2 HOH 103 603 258 HOH HOH A . 
C 2 HOH 104 604 100 HOH HOH A . 
C 2 HOH 105 605 27  HOH HOH A . 
C 2 HOH 106 606 240 HOH HOH A . 
C 2 HOH 107 607 176 HOH HOH A . 
C 2 HOH 108 608 214 HOH HOH A . 
C 2 HOH 109 609 330 HOH HOH A . 
C 2 HOH 110 610 342 HOH HOH A . 
C 2 HOH 111 611 234 HOH HOH A . 
C 2 HOH 112 612 404 HOH HOH A . 
C 2 HOH 113 613 223 HOH HOH A . 
C 2 HOH 114 614 33  HOH HOH A . 
C 2 HOH 115 615 95  HOH HOH A . 
C 2 HOH 116 616 283 HOH HOH A . 
C 2 HOH 117 617 473 HOH HOH A . 
C 2 HOH 118 618 69  HOH HOH A . 
C 2 HOH 119 619 257 HOH HOH A . 
C 2 HOH 120 620 388 HOH HOH A . 
C 2 HOH 121 621 75  HOH HOH A . 
C 2 HOH 122 622 421 HOH HOH A . 
C 2 HOH 123 623 191 HOH HOH A . 
C 2 HOH 124 624 40  HOH HOH A . 
C 2 HOH 125 625 306 HOH HOH A . 
C 2 HOH 126 626 101 HOH HOH A . 
C 2 HOH 127 627 259 HOH HOH A . 
C 2 HOH 128 628 325 HOH HOH A . 
C 2 HOH 129 629 504 HOH HOH A . 
C 2 HOH 130 630 352 HOH HOH A . 
C 2 HOH 131 631 514 HOH HOH A . 
C 2 HOH 132 632 102 HOH HOH A . 
C 2 HOH 133 633 418 HOH HOH A . 
C 2 HOH 134 634 190 HOH HOH A . 
C 2 HOH 135 635 166 HOH HOH A . 
C 2 HOH 136 636 111 HOH HOH A . 
C 2 HOH 137 637 398 HOH HOH A . 
C 2 HOH 138 638 466 HOH HOH A . 
C 2 HOH 139 639 519 HOH HOH A . 
C 2 HOH 140 640 272 HOH HOH A . 
C 2 HOH 141 641 189 HOH HOH A . 
C 2 HOH 142 642 395 HOH HOH A . 
C 2 HOH 143 643 493 HOH HOH A . 
C 2 HOH 144 644 465 HOH HOH A . 
C 2 HOH 145 645 409 HOH HOH A . 
C 2 HOH 146 646 153 HOH HOH A . 
C 2 HOH 147 647 147 HOH HOH A . 
C 2 HOH 148 648 508 HOH HOH A . 
C 2 HOH 149 649 461 HOH HOH A . 
C 2 HOH 150 650 517 HOH HOH A . 
C 2 HOH 151 651 165 HOH HOH A . 
C 2 HOH 152 652 552 HOH HOH A . 
C 2 HOH 153 653 433 HOH HOH A . 
C 2 HOH 154 654 343 HOH HOH A . 
C 2 HOH 155 655 89  HOH HOH A . 
C 2 HOH 156 656 505 HOH HOH A . 
C 2 HOH 157 657 85  HOH HOH A . 
C 2 HOH 158 658 499 HOH HOH A . 
C 2 HOH 159 659 308 HOH HOH A . 
C 2 HOH 160 660 186 HOH HOH A . 
C 2 HOH 161 661 235 HOH HOH A . 
C 2 HOH 162 662 487 HOH HOH A . 
C 2 HOH 163 663 73  HOH HOH A . 
C 2 HOH 164 664 309 HOH HOH A . 
C 2 HOH 165 665 266 HOH HOH A . 
C 2 HOH 166 666 389 HOH HOH A . 
C 2 HOH 167 667 236 HOH HOH A . 
C 2 HOH 168 668 286 HOH HOH A . 
C 2 HOH 169 669 469 HOH HOH A . 
C 2 HOH 170 670 555 HOH HOH A . 
C 2 HOH 171 671 281 HOH HOH A . 
C 2 HOH 172 672 79  HOH HOH A . 
C 2 HOH 173 673 128 HOH HOH A . 
C 2 HOH 174 674 435 HOH HOH A . 
C 2 HOH 175 675 553 HOH HOH A . 
C 2 HOH 176 676 488 HOH HOH A . 
C 2 HOH 177 677 207 HOH HOH A . 
C 2 HOH 178 678 530 HOH HOH A . 
C 2 HOH 179 679 371 HOH HOH A . 
C 2 HOH 180 680 399 HOH HOH A . 
C 2 HOH 181 681 536 HOH HOH A . 
C 2 HOH 182 682 518 HOH HOH A . 
C 2 HOH 183 683 521 HOH HOH A . 
C 2 HOH 184 684 477 HOH HOH A . 
C 2 HOH 185 685 482 HOH HOH A . 
C 2 HOH 186 686 501 HOH HOH A . 
C 2 HOH 187 687 250 HOH HOH A . 
C 2 HOH 188 688 348 HOH HOH A . 
C 2 HOH 189 689 357 HOH HOH A . 
C 2 HOH 190 690 453 HOH HOH A . 
C 2 HOH 191 691 252 HOH HOH A . 
C 2 HOH 192 692 417 HOH HOH A . 
C 2 HOH 193 693 230 HOH HOH A . 
C 2 HOH 194 694 381 HOH HOH A . 
C 2 HOH 195 695 390 HOH HOH A . 
C 2 HOH 196 696 394 HOH HOH A . 
C 2 HOH 197 697 532 HOH HOH A . 
C 2 HOH 198 698 449 HOH HOH A . 
C 2 HOH 199 699 462 HOH HOH A . 
C 2 HOH 200 700 478 HOH HOH A . 
C 2 HOH 201 701 316 HOH HOH A . 
C 2 HOH 202 702 321 HOH HOH A . 
C 2 HOH 203 703 347 HOH HOH A . 
C 2 HOH 204 704 237 HOH HOH A . 
C 2 HOH 205 705 68  HOH HOH A . 
C 2 HOH 206 706 355 HOH HOH A . 
C 2 HOH 207 707 444 HOH HOH A . 
C 2 HOH 208 708 405 HOH HOH A . 
C 2 HOH 209 709 335 HOH HOH A . 
C 2 HOH 210 710 359 HOH HOH A . 
C 2 HOH 211 711 483 HOH HOH A . 
C 2 HOH 212 712 494 HOH HOH A . 
C 2 HOH 213 713 430 HOH HOH A . 
C 2 HOH 214 714 410 HOH HOH A . 
C 2 HOH 215 715 175 HOH HOH A . 
C 2 HOH 216 716 312 HOH HOH A . 
C 2 HOH 217 717 548 HOH HOH A . 
C 2 HOH 218 718 396 HOH HOH A . 
C 2 HOH 219 719 452 HOH HOH A . 
C 2 HOH 220 720 496 HOH HOH A . 
C 2 HOH 221 721 423 HOH HOH A . 
C 2 HOH 222 722 210 HOH HOH A . 
C 2 HOH 223 723 537 HOH HOH A . 
C 2 HOH 224 724 364 HOH HOH A . 
C 2 HOH 225 725 416 HOH HOH A . 
C 2 HOH 226 726 479 HOH HOH A . 
C 2 HOH 227 727 463 HOH HOH A . 
D 2 HOH 1   501 322 HOH HOH B . 
D 2 HOH 2   502 380 HOH HOH B . 
D 2 HOH 3   503 77  HOH HOH B . 
D 2 HOH 4   504 424 HOH HOH B . 
D 2 HOH 5   505 402 HOH HOH B . 
D 2 HOH 6   506 133 HOH HOH B . 
D 2 HOH 7   507 392 HOH HOH B . 
D 2 HOH 8   508 558 HOH HOH B . 
D 2 HOH 9   509 156 HOH HOH B . 
D 2 HOH 10  510 334 HOH HOH B . 
D 2 HOH 11  511 154 HOH HOH B . 
D 2 HOH 12  512 542 HOH HOH B . 
D 2 HOH 13  513 99  HOH HOH B . 
D 2 HOH 14  514 331 HOH HOH B . 
D 2 HOH 15  515 454 HOH HOH B . 
D 2 HOH 16  516 344 HOH HOH B . 
D 2 HOH 17  517 550 HOH HOH B . 
D 2 HOH 18  518 17  HOH HOH B . 
D 2 HOH 19  519 238 HOH HOH B . 
D 2 HOH 20  520 385 HOH HOH B . 
D 2 HOH 21  521 541 HOH HOH B . 
D 2 HOH 22  522 495 HOH HOH B . 
D 2 HOH 23  523 319 HOH HOH B . 
D 2 HOH 24  524 361 HOH HOH B . 
D 2 HOH 25  525 35  HOH HOH B . 
D 2 HOH 26  526 300 HOH HOH B . 
D 2 HOH 27  527 491 HOH HOH B . 
D 2 HOH 28  528 360 HOH HOH B . 
D 2 HOH 29  529 538 HOH HOH B . 
D 2 HOH 30  530 158 HOH HOH B . 
D 2 HOH 31  531 63  HOH HOH B . 
D 2 HOH 32  532 9   HOH HOH B . 
D 2 HOH 33  533 115 HOH HOH B . 
D 2 HOH 34  534 271 HOH HOH B . 
D 2 HOH 35  535 13  HOH HOH B . 
D 2 HOH 36  536 142 HOH HOH B . 
D 2 HOH 37  537 24  HOH HOH B . 
D 2 HOH 38  538 232 HOH HOH B . 
D 2 HOH 39  539 185 HOH HOH B . 
D 2 HOH 40  540 132 HOH HOH B . 
D 2 HOH 41  541 16  HOH HOH B . 
D 2 HOH 42  542 65  HOH HOH B . 
D 2 HOH 43  543 78  HOH HOH B . 
D 2 HOH 44  544 379 HOH HOH B . 
D 2 HOH 45  545 327 HOH HOH B . 
D 2 HOH 46  546 57  HOH HOH B . 
D 2 HOH 47  547 247 HOH HOH B . 
D 2 HOH 48  548 320 HOH HOH B . 
D 2 HOH 49  549 7   HOH HOH B . 
D 2 HOH 50  550 88  HOH HOH B . 
D 2 HOH 51  551 151 HOH HOH B . 
D 2 HOH 52  552 198 HOH HOH B . 
D 2 HOH 53  553 60  HOH HOH B . 
D 2 HOH 54  554 97  HOH HOH B . 
D 2 HOH 55  555 108 HOH HOH B . 
D 2 HOH 56  556 484 HOH HOH B . 
D 2 HOH 57  557 311 HOH HOH B . 
D 2 HOH 58  558 428 HOH HOH B . 
D 2 HOH 59  559 382 HOH HOH B . 
D 2 HOH 60  560 5   HOH HOH B . 
D 2 HOH 61  561 243 HOH HOH B . 
D 2 HOH 62  562 11  HOH HOH B . 
D 2 HOH 63  563 174 HOH HOH B . 
D 2 HOH 64  564 4   HOH HOH B . 
D 2 HOH 65  565 123 HOH HOH B . 
D 2 HOH 66  566 439 HOH HOH B . 
D 2 HOH 67  567 160 HOH HOH B . 
D 2 HOH 68  568 522 HOH HOH B . 
D 2 HOH 69  569 183 HOH HOH B . 
D 2 HOH 70  570 124 HOH HOH B . 
D 2 HOH 71  571 92  HOH HOH B . 
D 2 HOH 72  572 12  HOH HOH B . 
D 2 HOH 73  573 30  HOH HOH B . 
D 2 HOH 74  574 50  HOH HOH B . 
D 2 HOH 75  575 129 HOH HOH B . 
D 2 HOH 76  576 192 HOH HOH B . 
D 2 HOH 77  577 161 HOH HOH B . 
D 2 HOH 78  578 71  HOH HOH B . 
D 2 HOH 79  579 249 HOH HOH B . 
D 2 HOH 80  580 459 HOH HOH B . 
D 2 HOH 81  581 164 HOH HOH B . 
D 2 HOH 82  582 437 HOH HOH B . 
D 2 HOH 83  583 18  HOH HOH B . 
D 2 HOH 84  584 510 HOH HOH B . 
D 2 HOH 85  585 391 HOH HOH B . 
D 2 HOH 86  586 305 HOH HOH B . 
D 2 HOH 87  587 83  HOH HOH B . 
D 2 HOH 88  588 201 HOH HOH B . 
D 2 HOH 89  589 297 HOH HOH B . 
D 2 HOH 90  590 340 HOH HOH B . 
D 2 HOH 91  591 23  HOH HOH B . 
D 2 HOH 92  592 199 HOH HOH B . 
D 2 HOH 93  593 227 HOH HOH B . 
D 2 HOH 94  594 58  HOH HOH B . 
D 2 HOH 95  595 168 HOH HOH B . 
D 2 HOH 96  596 152 HOH HOH B . 
D 2 HOH 97  597 25  HOH HOH B . 
D 2 HOH 98  598 406 HOH HOH B . 
D 2 HOH 99  599 59  HOH HOH B . 
D 2 HOH 100 600 506 HOH HOH B . 
D 2 HOH 101 601 456 HOH HOH B . 
D 2 HOH 102 602 195 HOH HOH B . 
D 2 HOH 103 603 253 HOH HOH B . 
D 2 HOH 104 604 415 HOH HOH B . 
D 2 HOH 105 605 6   HOH HOH B . 
D 2 HOH 106 606 155 HOH HOH B . 
D 2 HOH 107 607 38  HOH HOH B . 
D 2 HOH 108 608 299 HOH HOH B . 
D 2 HOH 109 609 460 HOH HOH B . 
D 2 HOH 110 610 106 HOH HOH B . 
D 2 HOH 111 611 228 HOH HOH B . 
D 2 HOH 112 612 34  HOH HOH B . 
D 2 HOH 113 613 193 HOH HOH B . 
D 2 HOH 114 614 2   HOH HOH B . 
D 2 HOH 115 615 292 HOH HOH B . 
D 2 HOH 116 616 202 HOH HOH B . 
D 2 HOH 117 617 231 HOH HOH B . 
D 2 HOH 118 618 31  HOH HOH B . 
D 2 HOH 119 619 39  HOH HOH B . 
D 2 HOH 120 620 48  HOH HOH B . 
D 2 HOH 121 621 397 HOH HOH B . 
D 2 HOH 122 622 113 HOH HOH B . 
D 2 HOH 123 623 295 HOH HOH B . 
D 2 HOH 124 624 293 HOH HOH B . 
D 2 HOH 125 625 534 HOH HOH B . 
D 2 HOH 126 626 407 HOH HOH B . 
D 2 HOH 127 627 169 HOH HOH B . 
D 2 HOH 128 628 22  HOH HOH B . 
D 2 HOH 129 629 220 HOH HOH B . 
D 2 HOH 130 630 112 HOH HOH B . 
D 2 HOH 131 631 104 HOH HOH B . 
D 2 HOH 132 632 208 HOH HOH B . 
D 2 HOH 133 633 239 HOH HOH B . 
D 2 HOH 134 634 138 HOH HOH B . 
D 2 HOH 135 635 28  HOH HOH B . 
D 2 HOH 136 636 64  HOH HOH B . 
D 2 HOH 137 637 480 HOH HOH B . 
D 2 HOH 138 638 187 HOH HOH B . 
D 2 HOH 139 639 196 HOH HOH B . 
D 2 HOH 140 640 141 HOH HOH B . 
D 2 HOH 141 641 139 HOH HOH B . 
D 2 HOH 142 642 194 HOH HOH B . 
D 2 HOH 143 643 336 HOH HOH B . 
D 2 HOH 144 644 387 HOH HOH B . 
D 2 HOH 145 645 520 HOH HOH B . 
D 2 HOH 146 646 105 HOH HOH B . 
D 2 HOH 147 647 125 HOH HOH B . 
D 2 HOH 148 648 276 HOH HOH B . 
D 2 HOH 149 649 323 HOH HOH B . 
D 2 HOH 150 650 434 HOH HOH B . 
D 2 HOH 151 651 354 HOH HOH B . 
D 2 HOH 152 652 216 HOH HOH B . 
D 2 HOH 153 653 3   HOH HOH B . 
D 2 HOH 154 654 44  HOH HOH B . 
D 2 HOH 155 655 422 HOH HOH B . 
D 2 HOH 156 656 172 HOH HOH B . 
D 2 HOH 157 657 91  HOH HOH B . 
D 2 HOH 158 658 14  HOH HOH B . 
D 2 HOH 159 659 8   HOH HOH B . 
D 2 HOH 160 660 1   HOH HOH B . 
D 2 HOH 161 661 130 HOH HOH B . 
D 2 HOH 162 662 21  HOH HOH B . 
D 2 HOH 163 663 15  HOH HOH B . 
D 2 HOH 164 664 315 HOH HOH B . 
D 2 HOH 165 665 296 HOH HOH B . 
D 2 HOH 166 666 412 HOH HOH B . 
D 2 HOH 167 667 310 HOH HOH B . 
D 2 HOH 168 668 233 HOH HOH B . 
D 2 HOH 169 669 540 HOH HOH B . 
D 2 HOH 170 670 206 HOH HOH B . 
D 2 HOH 171 671 554 HOH HOH B . 
D 2 HOH 172 672 126 HOH HOH B . 
D 2 HOH 173 673 184 HOH HOH B . 
D 2 HOH 174 674 229 HOH HOH B . 
D 2 HOH 175 675 265 HOH HOH B . 
D 2 HOH 176 676 261 HOH HOH B . 
D 2 HOH 177 677 117 HOH HOH B . 
D 2 HOH 178 678 148 HOH HOH B . 
D 2 HOH 179 679 317 HOH HOH B . 
D 2 HOH 180 680 280 HOH HOH B . 
D 2 HOH 181 681 546 HOH HOH B . 
D 2 HOH 182 682 218 HOH HOH B . 
D 2 HOH 183 683 74  HOH HOH B . 
D 2 HOH 184 684 242 HOH HOH B . 
D 2 HOH 185 685 94  HOH HOH B . 
D 2 HOH 186 686 55  HOH HOH B . 
D 2 HOH 187 687 324 HOH HOH B . 
D 2 HOH 188 688 143 HOH HOH B . 
D 2 HOH 189 689 376 HOH HOH B . 
D 2 HOH 190 690 98  HOH HOH B . 
D 2 HOH 191 691 350 HOH HOH B . 
D 2 HOH 192 692 287 HOH HOH B . 
D 2 HOH 193 693 269 HOH HOH B . 
D 2 HOH 194 694 54  HOH HOH B . 
D 2 HOH 195 695 525 HOH HOH B . 
D 2 HOH 196 696 213 HOH HOH B . 
D 2 HOH 197 697 531 HOH HOH B . 
D 2 HOH 198 698 43  HOH HOH B . 
D 2 HOH 199 699 72  HOH HOH B . 
D 2 HOH 200 700 66  HOH HOH B . 
D 2 HOH 201 701 10  HOH HOH B . 
D 2 HOH 202 702 386 HOH HOH B . 
D 2 HOH 203 703 339 HOH HOH B . 
D 2 HOH 204 704 204 HOH HOH B . 
D 2 HOH 205 705 375 HOH HOH B . 
D 2 HOH 206 706 302 HOH HOH B . 
D 2 HOH 207 707 246 HOH HOH B . 
D 2 HOH 208 708 177 HOH HOH B . 
D 2 HOH 209 709 32  HOH HOH B . 
D 2 HOH 210 710 274 HOH HOH B . 
D 2 HOH 211 711 46  HOH HOH B . 
D 2 HOH 212 712 134 HOH HOH B . 
D 2 HOH 213 713 425 HOH HOH B . 
D 2 HOH 214 714 163 HOH HOH B . 
D 2 HOH 215 715 509 HOH HOH B . 
D 2 HOH 216 716 181 HOH HOH B . 
D 2 HOH 217 717 150 HOH HOH B . 
D 2 HOH 218 718 288 HOH HOH B . 
D 2 HOH 219 719 145 HOH HOH B . 
D 2 HOH 220 720 131 HOH HOH B . 
D 2 HOH 221 721 289 HOH HOH B . 
D 2 HOH 222 722 438 HOH HOH B . 
D 2 HOH 223 723 219 HOH HOH B . 
D 2 HOH 224 724 291 HOH HOH B . 
D 2 HOH 225 725 222 HOH HOH B . 
D 2 HOH 226 726 458 HOH HOH B . 
D 2 HOH 227 727 341 HOH HOH B . 
D 2 HOH 228 728 349 HOH HOH B . 
D 2 HOH 229 729 188 HOH HOH B . 
D 2 HOH 230 730 351 HOH HOH B . 
D 2 HOH 231 731 87  HOH HOH B . 
D 2 HOH 232 732 414 HOH HOH B . 
D 2 HOH 233 733 119 HOH HOH B . 
D 2 HOH 234 734 333 HOH HOH B . 
D 2 HOH 235 735 472 HOH HOH B . 
D 2 HOH 236 736 301 HOH HOH B . 
D 2 HOH 237 737 529 HOH HOH B . 
D 2 HOH 238 738 284 HOH HOH B . 
D 2 HOH 239 739 109 HOH HOH B . 
D 2 HOH 240 740 378 HOH HOH B . 
D 2 HOH 241 741 298 HOH HOH B . 
D 2 HOH 242 742 80  HOH HOH B . 
D 2 HOH 243 743 263 HOH HOH B . 
D 2 HOH 244 744 545 HOH HOH B . 
D 2 HOH 245 745 373 HOH HOH B . 
D 2 HOH 246 746 178 HOH HOH B . 
D 2 HOH 247 747 307 HOH HOH B . 
D 2 HOH 248 748 498 HOH HOH B . 
D 2 HOH 249 749 45  HOH HOH B . 
D 2 HOH 250 750 426 HOH HOH B . 
D 2 HOH 251 751 366 HOH HOH B . 
D 2 HOH 252 752 443 HOH HOH B . 
D 2 HOH 253 753 37  HOH HOH B . 
D 2 HOH 254 754 511 HOH HOH B . 
D 2 HOH 255 755 251 HOH HOH B . 
D 2 HOH 256 756 173 HOH HOH B . 
D 2 HOH 257 757 451 HOH HOH B . 
D 2 HOH 258 758 411 HOH HOH B . 
D 2 HOH 259 759 393 HOH HOH B . 
D 2 HOH 260 760 146 HOH HOH B . 
D 2 HOH 261 761 273 HOH HOH B . 
D 2 HOH 262 762 413 HOH HOH B . 
D 2 HOH 263 763 441 HOH HOH B . 
D 2 HOH 264 764 524 HOH HOH B . 
D 2 HOH 265 765 549 HOH HOH B . 
D 2 HOH 266 766 526 HOH HOH B . 
D 2 HOH 267 767 279 HOH HOH B . 
D 2 HOH 268 768 551 HOH HOH B . 
D 2 HOH 269 769 303 HOH HOH B . 
D 2 HOH 270 770 369 HOH HOH B . 
D 2 HOH 271 771 144 HOH HOH B . 
D 2 HOH 272 772 513 HOH HOH B . 
D 2 HOH 273 773 383 HOH HOH B . 
D 2 HOH 274 774 467 HOH HOH B . 
D 2 HOH 275 775 372 HOH HOH B . 
D 2 HOH 276 776 370 HOH HOH B . 
D 2 HOH 277 777 528 HOH HOH B . 
D 2 HOH 278 778 403 HOH HOH B . 
D 2 HOH 279 779 464 HOH HOH B . 
D 2 HOH 280 780 260 HOH HOH B . 
D 2 HOH 281 781 346 HOH HOH B . 
D 2 HOH 282 782 110 HOH HOH B . 
D 2 HOH 283 783 489 HOH HOH B . 
D 2 HOH 284 784 326 HOH HOH B . 
D 2 HOH 285 785 515 HOH HOH B . 
D 2 HOH 286 786 490 HOH HOH B . 
D 2 HOH 287 787 114 HOH HOH B . 
D 2 HOH 288 788 268 HOH HOH B . 
D 2 HOH 289 789 431 HOH HOH B . 
D 2 HOH 290 790 559 HOH HOH B . 
D 2 HOH 291 791 248 HOH HOH B . 
D 2 HOH 292 792 457 HOH HOH B . 
D 2 HOH 293 793 445 HOH HOH B . 
D 2 HOH 294 794 338 HOH HOH B . 
D 2 HOH 295 795 262 HOH HOH B . 
D 2 HOH 296 796 212 HOH HOH B . 
D 2 HOH 297 797 96  HOH HOH B . 
D 2 HOH 298 798 419 HOH HOH B . 
D 2 HOH 299 799 475 HOH HOH B . 
D 2 HOH 300 800 278 HOH HOH B . 
D 2 HOH 301 801 313 HOH HOH B . 
D 2 HOH 302 802 358 HOH HOH B . 
D 2 HOH 303 803 408 HOH HOH B . 
D 2 HOH 304 804 384 HOH HOH B . 
D 2 HOH 305 805 285 HOH HOH B . 
D 2 HOH 306 806 527 HOH HOH B . 
D 2 HOH 307 807 474 HOH HOH B . 
D 2 HOH 308 808 500 HOH HOH B . 
D 2 HOH 309 809 503 HOH HOH B . 
D 2 HOH 310 810 523 HOH HOH B . 
D 2 HOH 311 811 481 HOH HOH B . 
D 2 HOH 312 812 492 HOH HOH B . 
D 2 HOH 313 813 450 HOH HOH B . 
D 2 HOH 314 814 277 HOH HOH B . 
D 2 HOH 315 815 470 HOH HOH B . 
D 2 HOH 316 816 455 HOH HOH B . 
D 2 HOH 317 817 560 HOH HOH B . 
D 2 HOH 318 818 447 HOH HOH B . 
D 2 HOH 319 819 533 HOH HOH B . 
D 2 HOH 320 820 203 HOH HOH B . 
D 2 HOH 321 821 442 HOH HOH B . 
D 2 HOH 322 822 476 HOH HOH B . 
D 2 HOH 323 823 486 HOH HOH B . 
D 2 HOH 324 824 420 HOH HOH B . 
D 2 HOH 325 825 255 HOH HOH B . 
D 2 HOH 326 826 245 HOH HOH B . 
D 2 HOH 327 827 270 HOH HOH B . 
D 2 HOH 328 828 427 HOH HOH B . 
D 2 HOH 329 829 121 HOH HOH B . 
D 2 HOH 330 830 539 HOH HOH B . 
D 2 HOH 331 831 318 HOH HOH B . 
D 2 HOH 332 832 448 HOH HOH B . 
D 2 HOH 333 833 512 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.13_2998: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                  2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? xia2    ? ? ? .                  3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                  4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.91 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9IHU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     61.441 
_cell.length_a_esd                 ? 
_cell.length_b                     40.918 
_cell.length_b_esd                 ? 
_cell.length_c                     194.064 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9IHU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                3 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9IHU 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.96 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M sodium citrate, pH 4.6, 20% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            338 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-09 
_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   0.9792 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9IHU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.79 
_reflns.d_resolution_low                               193.03 
_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                                     91529 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.73 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.168 
_reflns.pdbx_Rpim_I_all                                0.067 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       565908 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.983 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.153 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.79 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           35343 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6696 
_reflns_shell.percent_possible_obs                          100.0 
_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                               5.3 
_reflns_shell.pdbx_chi_squared                              0.44 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.5 
_reflns_shell.pdbx_Rrim_I_all                               0.795 
_reflns_shell.pdbx_Rpim_I_all                               0.344 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.687 
_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                                  0.713 
_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                                 9IHU 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.790 
_refine.ls_d_res_low                             38.606 
_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                     91171 
_refine.ls_number_reflns_R_free                  4538 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.60 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1923 
_refine.ls_R_factor_R_free                       0.2249 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1906 
_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                          0.84 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.09 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.23 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.790 
_refine_hist.d_res_low                        38.606 
_refine_hist.number_atoms_solvent             560 
_refine_hist.number_atoms_total               8664 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8104 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 8330  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.821 ? 11266 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 2.900 ? 4968  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.051 ? 1170  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 1426  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.7900 1.8103 . . 128 2911 100.00 . . . . 0.2610 . . . . . . . . . . . 0.3083 
'X-RAY DIFFRACTION' 1.8103 1.8316 . . 151 2864 100.00 . . . . 0.2523 . . . . . . . . . . . 0.3007 
'X-RAY DIFFRACTION' 1.8316 1.8540 . . 152 2918 100.00 . . . . 0.2562 . . . . . . . . . . . 0.3198 
'X-RAY DIFFRACTION' 1.8540 1.8775 . . 135 2833 100.00 . . . . 0.2755 . . . . . . . . . . . 0.3223 
'X-RAY DIFFRACTION' 1.8775 1.9022 . . 137 2863 99.00  . . . . 0.3384 . . . . . . . . . . . 0.3776 
'X-RAY DIFFRACTION' 1.9022 1.9282 . . 151 2859 99.00  . . . . 0.2954 . . . . . . . . . . . 0.3506 
'X-RAY DIFFRACTION' 1.9282 1.9558 . . 136 2676 93.00  . . . . 0.3717 . . . . . . . . . . . 0.3858 
'X-RAY DIFFRACTION' 1.9558 1.9849 . . 133 2870 100.00 . . . . 0.2583 . . . . . . . . . . . 0.3382 
'X-RAY DIFFRACTION' 1.9849 2.0160 . . 154 2858 100.00 . . . . 0.2045 . . . . . . . . . . . 0.2749 
'X-RAY DIFFRACTION' 2.0160 2.0490 . . 183 2943 100.00 . . . . 0.1932 . . . . . . . . . . . 0.2580 
'X-RAY DIFFRACTION' 2.0490 2.0843 . . 165 2748 100.00 . . . . 0.1894 . . . . . . . . . . . 0.2388 
'X-RAY DIFFRACTION' 2.0843 2.1222 . . 139 2952 100.00 . . . . 0.1787 . . . . . . . . . . . 0.2272 
'X-RAY DIFFRACTION' 2.1222 2.1631 . . 140 2862 100.00 . . . . 0.1775 . . . . . . . . . . . 0.2240 
'X-RAY DIFFRACTION' 2.1631 2.2072 . . 149 2842 100.00 . . . . 0.1725 . . . . . . . . . . . 0.2248 
'X-RAY DIFFRACTION' 2.2072 2.2552 . . 156 2897 100.00 . . . . 0.1745 . . . . . . . . . . . 0.2280 
'X-RAY DIFFRACTION' 2.2552 2.3076 . . 141 2905 100.00 . . . . 0.1826 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 2.3076 2.3653 . . 150 2887 100.00 . . . . 0.1910 . . . . . . . . . . . 0.2438 
'X-RAY DIFFRACTION' 2.3653 2.4293 . . 138 2887 100.00 . . . . 0.1922 . . . . . . . . . . . 0.1988 
'X-RAY DIFFRACTION' 2.4293 2.5008 . . 156 2853 100.00 . . . . 0.1804 . . . . . . . . . . . 0.2455 
'X-RAY DIFFRACTION' 2.5008 2.5815 . . 139 2936 100.00 . . . . 0.1777 . . . . . . . . . . . 0.2407 
'X-RAY DIFFRACTION' 2.5815 2.6737 . . 175 2863 100.00 . . . . 0.1748 . . . . . . . . . . . 0.2260 
'X-RAY DIFFRACTION' 2.6737 2.7807 . . 157 2868 100.00 . . . . 0.1749 . . . . . . . . . . . 0.1989 
'X-RAY DIFFRACTION' 2.7807 2.9072 . . 160 2923 100.00 . . . . 0.1760 . . . . . . . . . . . 0.1943 
'X-RAY DIFFRACTION' 2.9072 3.0605 . . 135 2920 100.00 . . . . 0.1752 . . . . . . . . . . . 0.1882 
'X-RAY DIFFRACTION' 3.0605 3.2521 . . 140 2915 100.00 . . . . 0.1802 . . . . . . . . . . . 0.1921 
'X-RAY DIFFRACTION' 3.2521 3.5031 . . 158 2925 100.00 . . . . 0.1650 . . . . . . . . . . . 0.2063 
'X-RAY DIFFRACTION' 3.5031 3.8553 . . 169 2908 100.00 . . . . 0.1577 . . . . . . . . . . . 0.1764 
'X-RAY DIFFRACTION' 3.8553 4.4125 . . 162 2943 100.00 . . . . 0.1484 . . . . . . . . . . . 0.1877 
'X-RAY DIFFRACTION' 4.4125 5.5566 . . 163 2954 100.00 . . . . 0.1592 . . . . . . . . . . . 0.1826 
'X-RAY DIFFRACTION' 5.5566 38.606 . . 186 3050 99.00  . . . . 0.1955 . . . . . . . . . . . 0.2117 
# 
_struct.entry_id                     9IHU 
_struct.title                        'GH57 family Amylopullulanase from Aquifex aeolicus' 
_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        9IHU 
_struct_keywords.text            'Amylopullulanase, Aquifex aeolicus, GH57 family, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 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 9IHU A 1 ? 477 ? O66934 1 ? 477 ? 1 477 
2 1 9IHU B 1 ? 477 ? O66934 1 ? 477 ? 1 477 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 28  ? ASP A 37  ? PRO A 28  ASP A 37  1 ? 10 
HELX_P HELX_P2  AA2 TYR A 39  ? TYR A 44  ? TYR A 39  TYR A 44  1 ? 6  
HELX_P HELX_P3  AA3 LEU A 45  ? ASP A 47  ? LEU A 45  ASP A 47  5 ? 3  
HELX_P HELX_P4  AA4 THR A 57  ? GLN A 69  ? THR A 57  GLN A 69  1 ? 13 
HELX_P HELX_P5  AA5 VAL A 75  ? LYS A 82  ? VAL A 75  LYS A 82  1 ? 8  
HELX_P HELX_P6  AA6 ASP A 83  ? LEU A 87  ? ASP A 83  LEU A 87  5 ? 5  
HELX_P HELX_P7  AA7 GLU A 88  ? TYR A 103 ? GLU A 88  TYR A 103 1 ? 16 
HELX_P HELX_P8  AA8 LYS A 105 ? ARG A 109 ? LYS A 105 ARG A 109 5 ? 5  
HELX_P HELX_P9  AA9 PHE A 110 ? ASN A 118 ? PHE A 110 ASN A 118 1 ? 9  
HELX_P HELX_P10 AB1 ASN A 123 ? TRP A 138 ? ASN A 123 TRP A 138 1 ? 16 
HELX_P HELX_P11 AB2 THR A 142 ? LEU A 147 ? THR A 142 LEU A 147 1 ? 6  
HELX_P HELX_P12 AB3 LEU A 147 ? GLY A 154 ? LEU A 147 GLY A 154 1 ? 8  
HELX_P HELX_P13 AB4 THR A 158 ? LYS A 175 ? THR A 158 LYS A 175 1 ? 18 
HELX_P HELX_P14 AB5 LYS A 175 ? GLU A 186 ? LYS A 175 GLU A 186 1 ? 12 
HELX_P HELX_P15 AB6 LEU A 200 ? ASN A 206 ? LEU A 200 ASN A 206 1 ? 7  
HELX_P HELX_P16 AB7 PRO A 207 ? THR A 213 ? PRO A 207 THR A 213 5 ? 7  
HELX_P HELX_P17 AB8 PHE A 226 ? GLY A 246 ? PHE A 226 GLY A 246 1 ? 21 
HELX_P HELX_P18 AB9 PRO A 254 ? SER A 258 ? PRO A 254 SER A 258 5 ? 5  
HELX_P HELX_P19 AC1 SER A 260 ? LYS A 270 ? SER A 260 LYS A 270 1 ? 11 
HELX_P HELX_P20 AC2 GLU A 279 ? VAL A 286 ? GLU A 279 VAL A 286 1 ? 8  
HELX_P HELX_P21 AC3 ASP A 307 ? SER A 317 ? ASP A 307 SER A 317 1 ? 11 
HELX_P HELX_P22 AC4 TYR A 318 ? TRP A 321 ? TYR A 318 TRP A 321 5 ? 4  
HELX_P HELX_P23 AC5 ASN A 322 ? VAL A 341 ? ASN A 322 VAL A 341 1 ? 20 
HELX_P HELX_P24 AC6 CYS A 356 ? ASN A 363 ? CYS A 356 ASN A 363 5 ? 8  
HELX_P HELX_P25 AC7 GLY A 364 ? GLU A 378 ? GLY A 364 GLU A 378 1 ? 15 
HELX_P HELX_P26 AC8 THR A 385 ? LYS A 392 ? THR A 385 LYS A 392 1 ? 8  
HELX_P HELX_P27 AC9 ASN A 419 ? LYS A 435 ? ASN A 419 LYS A 435 1 ? 17 
HELX_P HELX_P28 AD1 ASP A 439 ? GLU A 445 ? ASP A 439 GLU A 445 1 ? 7  
HELX_P HELX_P29 AD2 GLY A 446 ? GLN A 453 ? GLY A 446 GLN A 453 1 ? 8  
HELX_P HELX_P30 AD3 PHE A 460 ? ALA A 475 ? PHE A 460 ALA A 475 1 ? 16 
HELX_P HELX_P31 AD4 PRO B 28  ? ASP B 37  ? PRO B 28  ASP B 37  1 ? 10 
HELX_P HELX_P32 AD5 TYR B 39  ? TYR B 44  ? TYR B 39  TYR B 44  1 ? 6  
HELX_P HELX_P33 AD6 LEU B 45  ? ASP B 47  ? LEU B 45  ASP B 47  5 ? 3  
HELX_P HELX_P34 AD7 THR B 57  ? GLN B 69  ? THR B 57  GLN B 69  1 ? 13 
HELX_P HELX_P35 AD8 VAL B 75  ? LYS B 82  ? VAL B 75  LYS B 82  1 ? 8  
HELX_P HELX_P36 AD9 ASP B 83  ? LEU B 87  ? ASP B 83  LEU B 87  5 ? 5  
HELX_P HELX_P37 AE1 GLU B 88  ? TYR B 103 ? GLU B 88  TYR B 103 1 ? 16 
HELX_P HELX_P38 AE2 LYS B 105 ? ARG B 109 ? LYS B 105 ARG B 109 5 ? 5  
HELX_P HELX_P39 AE3 PHE B 110 ? MET B 117 ? PHE B 110 MET B 117 1 ? 8  
HELX_P HELX_P40 AE4 ASN B 123 ? TRP B 138 ? ASN B 123 TRP B 138 1 ? 16 
HELX_P HELX_P41 AE5 GLY B 140 ? LEU B 147 ? GLY B 140 LEU B 147 1 ? 8  
HELX_P HELX_P42 AE6 LEU B 147 ? GLY B 154 ? LEU B 147 GLY B 154 1 ? 8  
HELX_P HELX_P43 AE7 THR B 158 ? LYS B 175 ? THR B 158 LYS B 175 1 ? 18 
HELX_P HELX_P44 AE8 LYS B 175 ? GLU B 186 ? LYS B 175 GLU B 186 1 ? 12 
HELX_P HELX_P45 AE9 LEU B 200 ? ASN B 206 ? LEU B 200 ASN B 206 1 ? 7  
HELX_P HELX_P46 AF1 PRO B 207 ? THR B 213 ? PRO B 207 THR B 213 5 ? 7  
HELX_P HELX_P47 AF2 PHE B 226 ? GLY B 246 ? PHE B 226 GLY B 246 1 ? 21 
HELX_P HELX_P48 AF3 PRO B 254 ? SER B 258 ? PRO B 254 SER B 258 5 ? 5  
HELX_P HELX_P49 AF4 SER B 260 ? LYS B 270 ? SER B 260 LYS B 270 1 ? 11 
HELX_P HELX_P50 AF5 GLU B 279 ? VAL B 286 ? GLU B 279 VAL B 286 1 ? 8  
HELX_P HELX_P51 AF6 ASP B 307 ? SER B 317 ? ASP B 307 SER B 317 1 ? 11 
HELX_P HELX_P52 AF7 TYR B 318 ? TRP B 321 ? TYR B 318 TRP B 321 5 ? 4  
HELX_P HELX_P53 AF8 ASN B 322 ? VAL B 341 ? ASN B 322 VAL B 341 1 ? 20 
HELX_P HELX_P54 AF9 CYS B 356 ? ASN B 363 ? CYS B 356 ASN B 363 5 ? 8  
HELX_P HELX_P55 AG1 GLY B 364 ? GLU B 378 ? GLY B 364 GLU B 378 1 ? 15 
HELX_P HELX_P56 AG2 THR B 385 ? LYS B 392 ? THR B 385 LYS B 392 1 ? 8  
HELX_P HELX_P57 AG3 ASN B 419 ? LYS B 435 ? ASN B 419 LYS B 435 1 ? 17 
HELX_P HELX_P58 AG4 ASP B 439 ? GLU B 445 ? ASP B 439 GLU B 445 1 ? 7  
HELX_P HELX_P59 AG5 GLY B 446 ? GLN B 453 ? GLY B 446 GLN B 453 1 ? 8  
HELX_P HELX_P60 AG6 PHE B 460 ? ALA B 475 ? PHE B 460 ALA B 475 1 ? 16 
# 
_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 ? 5 ? 
AA5 ? 4 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 5 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA7 1 2 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? anti-parallel 
AA8 4 5 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 191 ? 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 TYR A 251 ? MET A 252 ? TYR A 251 MET A 252 
AA4 2 MET A 274 ? ASP A 278 ? MET A 274 ASP A 278 
AA4 3 ILE A 301 ? ARG A 306 ? ILE A 301 ARG A 306 
AA4 4 ARG A 294 ? PHE A 297 ? ARG A 294 PHE A 297 
AA4 5 THR A 397 ? ILE A 400 ? THR A 397 ILE A 400 
AA5 1 VAL B 191 ? SER B 192 ? VAL B 191 SER B 192 
AA5 2 ASN B 53  ? LEU B 56  ? ASN B 53  LEU B 56  
AA5 3 LEU B 4   ? MET B 12  ? LEU B 4   MET B 12  
AA5 4 VAL B 346 ? 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 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA1 2 3 O ASN A 53  ? O ASN A 53  N TRP A 10  ? N TRP A 10  
AA1 3 4 N VAL A 7   ? N VAL A 7   O VAL A 349 ? O VAL A 349 
AA2 1 2 O SER A 192 ? O SER A 192 N PHE A 54  ? N PHE A 54  
AA2 2 3 O ASN A 53  ? O ASN A 53  N TRP A 10  ? N TRP A 10  
AA2 3 4 N LEU A 4   ? N LEU A 4   O GLU A 382 ? O GLU A 382 
AA3 1 2 N TYR A 25  ? N TYR A 25  O LYS A 73  ? O LYS A 73  
AA4 1 2 N MET A 252 ? N MET A 252 O MET A 274 ? O MET A 274 
AA4 2 3 N THR A 277 ? N THR A 277 O ARG A 306 ? O ARG A 306 
AA4 3 4 O ILE A 301 ? O ILE A 301 N PHE A 297 ? N PHE A 297 
AA4 4 5 N TYR A 296 ? N TYR A 296 O ILE A 400 ? O ILE A 400 
AA5 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA5 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA5 3 4 N PHE B 5   ? N PHE B 5   O VAL B 347 ? O VAL B 347 
AA6 1 2 O SER B 192 ? O SER B 192 N PHE B 54  ? N PHE B 54  
AA6 2 3 O ASN B 53  ? O ASN B 53  N TRP B 10  ? N TRP B 10  
AA6 3 4 N LEU B 4   ? N LEU B 4   O GLU B 382 ? O GLU B 382 
AA7 1 2 N TYR B 25  ? N TYR B 25  O LYS B 73  ? O LYS B 73  
AA8 1 2 N MET B 252 ? N MET B 252 O MET B 274 ? O MET B 274 
AA8 2 3 N THR B 277 ? N THR B 277 O ARG B 306 ? O ARG B 306 
AA8 3 4 O VAL B 303 ? O VAL B 303 N TYR B 295 ? N TYR B 295 
AA8 4 5 N TYR B 296 ? N TYR B 296 O ILE B 400 ? O ILE B 400 
# 
_pdbx_entry_details.entry_id                   9IHU 
_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   B HOH 761 ? ? O B HOH 772 ? ? 1.81 
2  1 O   B HOH 695 ? ? O B HOH 751 ? ? 1.84 
3  1 O   B HOH 799 ? ? O B HOH 831 ? ? 1.85 
4  1 O   B HOH 702 ? ? O B HOH 778 ? ? 1.86 
5  1 OE2 B GLU 431 ? ? O B HOH 501 ? ? 1.89 
6  1 OD1 B ASN 152 ? ? O B HOH 502 ? ? 1.89 
7  1 O   B HOH 627 ? ? O B HOH 804 ? ? 1.89 
8  1 O   B HOH 767 ? ? O B HOH 827 ? ? 1.90 
9  1 O   B HOH 716 ? ? O B HOH 821 ? ? 1.90 
10 1 O   A HOH 506 ? ? O A HOH 697 ? ? 1.96 
11 1 O   B HOH 715 ? ? O B HOH 777 ? ? 1.96 
12 1 O   B HOH 808 ? ? O B HOH 833 ? ? 1.96 
13 1 O   A HOH 701 ? ? O A HOH 716 ? ? 1.98 
14 1 O   B HOH 705 ? ? O B HOH 786 ? ? 1.99 
15 1 OD1 A ASP 394 ? ? O A HOH 501 ? ? 2.00 
16 1 O   A HOH 691 ? ? O B HOH 774 ? ? 2.00 
17 1 OE2 A GLU 66  ? ? O A HOH 502 ? ? 2.07 
18 1 O   B HOH 742 ? ? O B HOH 804 ? ? 2.09 
19 1 OD1 A ASP 410 ? ? O A HOH 503 ? ? 2.10 
20 1 O   A HOH 665 ? ? O A HOH 695 ? ? 2.12 
21 1 O   B HOH 581 ? ? O B HOH 804 ? ? 2.12 
22 1 O   B HOH 675 ? ? O B HOH 803 ? ? 2.12 
23 1 O   A HOH 613 ? ? O A HOH 708 ? ? 2.13 
24 1 O   B HOH 601 ? ? O B HOH 762 ? ? 2.14 
25 1 O   B HOH 637 ? ? O B HOH 732 ? ? 2.15 
26 1 O   A HOH 694 ? ? O A HOH 709 ? ? 2.16 
27 1 O   B HOH 689 ? ? O B HOH 811 ? ? 2.17 
28 1 O   A HOH 676 ? ? O A HOH 685 ? ? 2.17 
29 1 OE2 B GLU 279 ? ? O B HOH 503 ? ? 2.17 
30 1 O   A HOH 660 ? ? O A HOH 700 ? ? 2.17 
31 1 O   B HOH 530 ? ? O B HOH 640 ? ? 2.19 
32 1 OD1 A ASN 273 ? ? O A HOH 504 ? ? 2.19 
33 1 O   B HOH 589 ? ? O B HOH 828 ? ? 2.19 
34 1 O   A HOH 709 ? ? O A HOH 715 ? ? 2.19 
35 1 O   B HOH 764 ? ? O B HOH 785 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 545 ? ? 1_555 O B HOH 644 ? ? 2_656 2.07 
2 1 O A HOH 707 ? ? 1_555 O B HOH 623 ? ? 1_565 2.11 
3 1 O A HOH 680 ? ? 1_555 O B HOH 809 ? ? 1_455 2.15 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD A GLU 256 ? ? OE1 A GLU 256 ? ? 1.168 1.252 -0.084 0.011 N 
2 1 CD B GLU 256 ? ? OE1 B GLU 256 ? ? 1.179 1.252 -0.073 0.011 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 206 ? ? -167.58 86.67   
2 1 THR A 277 ? ? -148.95 -157.94 
3 1 ASP A 394 ? ? -91.07  53.27   
4 1 ASN B 206 ? ? -162.44 87.10   
5 1 THR B 277 ? ? -146.70 -159.59 
6 1 ASP B 410 ? ? 59.08   19.53   
7 1 GLU B 456 ? ? -55.56  93.00   
8 1 LYS B 457 ? ? 9.58    53.85   
9 1 ALA B 458 ? ? -49.19  158.27  
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    195 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   TYR 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    196 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -146.88 
# 
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 4.7226   -3.5688  26.9880 0.1416 ? 0.0924  ? 0.0055  ? 0.0984  ? -0.0940 ? -0.0857 ? 0.0279 ? 
0.0145  ? -0.0180 ? 0.0145 ? 0.0058  ? 0.0203 ? 0.0197  ? -0.0260 ? -0.0480 ? -0.0411 ? -0.0385 ? -0.0325 ? 0.0746  ? 0.0534  ? 
-0.0154 ? 
2  'X-RAY DIFFRACTION' ? refined 11.1361  2.4049   5.5403  0.2454 ? 0.0521  ? -0.0263 ? 0.3435  ? -0.0096 ? 0.1195  ? 0.0015 ? 
0.0035  ? 0.0007  ? 0.0019 ? 0.0011  ? 0.0051 ? 0.0035  ? 0.0376  ? 0.0291  ? -0.0085 ? 0.0130  ? 0.0084  ? 0.0334  ? 0.0070  ? 
0.0000  ? 
3  'X-RAY DIFFRACTION' ? refined 17.9166  2.7336   18.2784 0.1407 ? 0.0867  ? -0.0001 ? 0.2248  ? -0.0061 ? 0.0747  ? 0.0770 ? 
0.0042  ? 0.0572  ? 0.0149 ? 0.0364  ? 0.1087 ? -0.0515 ? 0.0994  ? -0.0351 ? 0.0322  ? 0.0638  ? -0.0097 ? 0.0030  ? 0.2388  ? 
-0.0315 ? 
4  'X-RAY DIFFRACTION' ? refined -15.3414 -7.0098  28.7995 0.1884 ? 0.0134  ? -0.0383 ? 0.1225  ? -0.0091 ? 0.1179  ? 0.0144 ? 
0.0094  ? -0.0228 ? 0.0461 ? -0.0389 ? 0.0478 ? 0.0163  ? 0.0737  ? -0.0165 ? 0.0068  ? 0.0917  ? 0.0211  ? 0.1791  ? -0.1161 ? 
0.0059  ? 
5  'X-RAY DIFFRACTION' ? refined -8.4710  5.4074   41.5348 0.1608 ? 0.0255  ? 0.0018  ? 0.1120  ? -0.0084 ? 0.1218  ? 0.0035 ? 
0.0024  ? 0.0100  ? 0.0142 ? -0.0259 ? 0.0411 ? 0.0389  ? -0.0339 ? -0.0125 ? -0.0362 ? -0.0042 ? 0.0456  ? -0.0691 ? -0.1008 ? 
0.0016  ? 
6  'X-RAY DIFFRACTION' ? refined 3.2470   9.6772   42.4003 0.1792 ? 0.0140  ? 0.0005  ? 0.1064  ? -0.0279 ? 0.0822  ? 0.0052 ? 
-0.0046 ? 0.0031  ? 0.0033 ? 0.0013  ? 0.0067 ? 0.0342  ? -0.0276 ? 0.0510  ? 0.0059  ? -0.0465 ? 0.0269  ? -0.0613 ? 0.0079  ? 
-0.0056 ? 
7  'X-RAY DIFFRACTION' ? refined 7.1837   1.7154   45.0219 0.1346 ? -0.0031 ? -0.0188 ? 0.1672  ? -0.0184 ? 0.0884  ? 0.0077 ? 
-0.0114 ? 0.0027  ? 0.0100 ? -0.0052 ? 0.0048 ? 0.0059  ? -0.0315 ? 0.0002  ? 0.0252  ? 0.0135  ? 0.0070  ? -0.0259 ? 0.0326  ? 
-0.0000 ? 
8  'X-RAY DIFFRACTION' ? refined -18.4675 3.0235   24.2263 0.1433 ? 0.0251  ? -0.0302 ? 0.1936  ? 0.0291  ? 0.1329  ? 0.0091 ? 
0.0052  ? 0.0026  ? 0.0045 ? -0.0048 ? 0.0051 ? 0.0183  ? 0.0523  ? 0.0449  ? -0.0405 ? 0.0009  ? 0.0548  ? -0.0114 ? -0.0364 ? 
0.0000  ? 
9  'X-RAY DIFFRACTION' ? refined -10.1117 -1.0782  12.1192 0.1744 ? 0.0141  ? -0.0364 ? 0.1899  ? -0.0039 ? 0.0789  ? 0.0318 ? 
-0.0192 ? -0.0046 ? 0.0116 ? 0.0002  ? 0.0021 ? -0.0172 ? 0.0697  ? 0.0443  ? -0.0001 ? -0.0096 ? -0.0187 ? 0.0202  ? -0.0327 ? 
0.0013  ? 
10 'X-RAY DIFFRACTION' ? refined 17.6500  -21.0402 75.6978 0.0296 ? -0.0179 ? -0.0037 ? 0.0498  ? 0.0016  ? 0.0671  ? 0.0719 ? 
-0.0109 ? 0.0192  ? 0.0351 ? 0.0044  ? 0.0549 ? -0.0302 ? -0.0128 ? -0.0445 ? -0.0046 ? -0.0003 ? 0.0180  ? 0.0152  ? -0.0098 ? 
-0.0412 ? 
11 'X-RAY DIFFRACTION' ? refined 6.6806   -16.2697 75.4020 0.0200 ? -0.0287 ? 0.0139  ? 0.0296  ? -0.0086 ? 0.1141  ? 0.0253 ? 
0.0294  ? -0.0245 ? 0.0216 ? -0.0096 ? 0.0308 ? -0.0144 ? 0.0480  ? 0.0303  ? -0.0531 ? 0.0451  ? 0.0178  ? -0.0322 ? -0.0956 ? 
0.0044  ? 
12 'X-RAY DIFFRACTION' ? refined 38.9901  -22.0891 65.5361 0.0004 ? -0.1206 ? 0.0070  ? -0.1895 ? -0.0187 ? 0.0939  ? 0.0356 ? 
-0.0016 ? -0.0057 ? 0.0066 ? -0.0161 ? 0.0196 ? -0.0020 ? 0.0960  ? -0.0613 ? -0.0429 ? -0.0189 ? -0.0234 ? 0.0938  ? 0.1639  ? 
-0.0031 ? 
13 'X-RAY DIFFRACTION' ? refined 23.1252  -14.4727 52.5724 0.0839 ? -0.0178 ? 0.0014  ? 0.0967  ? 0.0067  ? 0.0660  ? 0.0475 ? 
0.0205  ? -0.0189 ? 0.0226 ? 0.0018  ? 0.0497 ? 0.0075  ? 0.1079  ? 0.0238  ? -0.0647 ? 0.0228  ? 0.0517  ? -0.0262 ? -0.0209 ? 
0.0221  ? 
14 'X-RAY DIFFRACTION' ? refined 43.1567  -16.6658 75.7249 0.0370 ? 0.0008  ? 0.0048  ? 0.0744  ? -0.0077 ? 0.1113  ? 0.0363 ? 
0.0120  ? 0.0070  ? 0.0058 ? -0.0013 ? 0.0066 ? -0.0003 ? -0.0184 ? 0.0491  ? -0.0017 ? -0.0088 ? -0.0063 ? -0.0341 ? 0.0187  ? 
0.0006  ? 
15 'X-RAY DIFFRACTION' ? refined 32.9392  -20.2274 86.4310 0.0014 ? 0.0123  ? -0.0135 ? 0.0420  ? 0.0204  ? 0.0822  ? 0.0172 ? 
0.0056  ? 0.0082  ? 0.0043 ? 0.0044  ? 0.0146 ? -0.0191 ? -0.0674 ? -0.0047 ? -0.0053 ? -0.0186 ? 0.0200  ? -0.0216 ? -0.0093 ? 
-0.0075 ? 
# 
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 68 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 69 through 102 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 103 through 194 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 195 through 273 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 274 through 322 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 323 through 360 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 361 through 396 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 397 through 435 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 436 through 477 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 1 through 102 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 103 through 194 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 195 through 322 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 323 through 396 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 397 through 435 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 436 through 477 )
;
# 
loop_
_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 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Basic Research Program of China (973 Program)' China 2021YFC2301405 1 
'National Science Foundation (NSF, China)'               China 21ZR1471800    2 
# 
_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                    9IHU 
_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]   0.016276 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001685 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024439 
_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]   0.005180 
_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   ? 5.384   1.815   62.959  1.00 56.47 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 5.310   2.790   61.878  1.00 54.60 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 4.165   2.471   60.916  1.00 51.95 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 3.941   1.319   60.544  1.00 53.51 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 6.634   2.851   61.117  1.00 57.49 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 6.594   3.710   59.862  1.00 59.89 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 8.114   3.610   58.907  1.00 64.25 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 9.333   3.858   60.198  1.00 64.35 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 3.446   3.517   60.518  1.00 41.48 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 2.298   3.420   59.628  1.00 32.91 ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 2.748   3.720   58.199  1.00 23.69 ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 3.370   4.752   57.946  1.00 29.54 ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 1.211   4.396   60.078  1.00 44.04 ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 0.097   4.659   59.110  1.00 49.40 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? -1.149  3.906   59.521  1.00 58.45 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? -1.630  4.251   60.916  1.00 56.96 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? -2.940  3.591   61.197  1.00 55.23 ? 2   LYS A NZ  1 
ATOM   18   N N   . LYS A 1 3   ? 2.435   2.824   57.273  1.00 16.15 ? 3   LYS A N   1 
ATOM   19   C CA  . LYS A 1 3   ? 3.015   2.898   55.944  1.00 18.17 ? 3   LYS A CA  1 
ATOM   20   C C   . LYS A 1 3   ? 1.988   3.331   54.915  1.00 19.66 ? 3   LYS A C   1 
ATOM   21   O O   . LYS A 1 3   ? 0.775   3.247   55.127  1.00 21.67 ? 3   LYS A O   1 
ATOM   22   C CB  . LYS A 1 3   ? 3.625   1.554   55.551  1.00 26.66 ? 3   LYS A CB  1 
ATOM   23   C CG  . LYS A 1 3   ? 4.824   1.215   56.403  1.00 35.79 ? 3   LYS A CG  1 
ATOM   24   C CD  . LYS A 1 3   ? 5.284   -0.200  56.201  1.00 39.52 ? 3   LYS A CD  1 
ATOM   25   C CE  . LYS A 1 3   ? 6.463   -0.497  57.116  1.00 42.26 ? 3   LYS A CE  1 
ATOM   26   N NZ  . LYS A 1 3   ? 7.303   0.713   57.336  1.00 36.00 ? 3   LYS A NZ  1 
ATOM   27   N N   . LEU A 1 4   ? 2.505   3.847   53.807  1.00 13.77 ? 4   LEU A N   1 
ATOM   28   C CA  . LEU A 1 4   ? 1.724   4.066   52.603  1.00 10.76 ? 4   LEU A CA  1 
ATOM   29   C C   . LEU A 1 4   ? 2.058   2.934   51.640  1.00 15.07 ? 4   LEU A C   1 
ATOM   30   O O   . LEU A 1 4   ? 3.238   2.635   51.410  1.00 16.25 ? 4   LEU A O   1 
ATOM   31   C CB  . LEU A 1 4   ? 2.038   5.434   51.980  1.00 12.25 ? 4   LEU A CB  1 
ATOM   32   C CG  . LEU A 1 4   ? 1.330   5.846   50.694  1.00 17.11 ? 4   LEU A CG  1 
ATOM   33   C CD1 . LEU A 1 4   ? 1.011   7.330   50.711  1.00 20.09 ? 4   LEU A CD1 1 
ATOM   34   C CD2 . LEU A 1 4   ? 2.192   5.479   49.447  1.00 11.48 ? 4   LEU A CD2 1 
ATOM   35   N N   . PHE A 1 5   ? 1.033   2.262   51.138  1.00 13.62 ? 5   PHE A N   1 
ATOM   36   C CA  . PHE A 1 5   ? 1.231   1.184   50.177  1.00 12.39 ? 5   PHE A CA  1 
ATOM   37   C C   . PHE A 1 5   ? 1.105   1.758   48.778  1.00 15.65 ? 5   PHE A C   1 
ATOM   38   O O   . PHE A 1 5   ? 0.086   2.374   48.444  1.00 18.95 ? 5   PHE A O   1 
ATOM   39   C CB  . PHE A 1 5   ? 0.226   0.054   50.402  1.00 13.43 ? 5   PHE A CB  1 
ATOM   40   C CG  . PHE A 1 5   ? 0.363   -0.604  51.737  1.00 12.11 ? 5   PHE A CG  1 
ATOM   41   C CD1 . PHE A 1 5   ? 1.552   -1.229  52.091  1.00 17.76 ? 5   PHE A CD1 1 
ATOM   42   C CD2 . PHE A 1 5   ? -0.680  -0.559  52.662  1.00 15.80 ? 5   PHE A CD2 1 
ATOM   43   C CE1 . PHE A 1 5   ? 1.698   -1.823  53.328  1.00 19.00 ? 5   PHE A CE1 1 
ATOM   44   C CE2 . PHE A 1 5   ? -0.548  -1.153  53.895  1.00 16.95 ? 5   PHE A CE2 1 
ATOM   45   C CZ  . PHE A 1 5   ? 0.643   -1.781  54.242  1.00 20.31 ? 5   PHE A CZ  1 
ATOM   46   N N   . LEU A 1 6   ? 2.134   1.543   47.958  1.00 12.66 ? 6   LEU A N   1 
ATOM   47   C CA  . LEU A 1 6   ? 2.210   2.125   46.627  1.00 14.84 ? 6   LEU A CA  1 
ATOM   48   C C   . LEU A 1 6   ? 2.224   0.993   45.613  1.00 12.18 ? 6   LEU A C   1 
ATOM   49   O O   . LEU A 1 6   ? 2.984   0.031   45.758  1.00 12.35 ? 6   LEU A O   1 
ATOM   50   C CB  . LEU A 1 6   ? 3.459   3.018   46.496  1.00 11.56 ? 6   LEU A CB  1 
ATOM   51   C CG  . LEU A 1 6   ? 3.712   3.780   45.193  1.00 10.21 ? 6   LEU A CG  1 
ATOM   52   C CD1 . LEU A 1 6   ? 2.606   4.781   44.888  1.00 12.52 ? 6   LEU A CD1 1 
ATOM   53   C CD2 . LEU A 1 6   ? 5.050   4.487   45.263  1.00 14.42 ? 6   LEU A CD2 1 
ATOM   54   N N   . VAL A 1 7   ? 1.359   1.080   44.614  1.00 11.82 ? 7   VAL A N   1 
ATOM   55   C CA  . VAL A 1 7   ? 1.184   -0.007  43.647  1.00 9.62  ? 7   VAL A CA  1 
ATOM   56   C C   . VAL A 1 7   ? 1.286   0.583   42.241  1.00 14.12 ? 7   VAL A C   1 
ATOM   57   O O   . VAL A 1 7   ? 0.379   1.300   41.798  1.00 14.56 ? 7   VAL A O   1 
ATOM   58   C CB  . VAL A 1 7   ? -0.157  -0.735  43.843  1.00 12.82 ? 7   VAL A CB  1 
ATOM   59   C CG1 . VAL A 1 7   ? -0.220  -2.013  42.997  1.00 11.60 ? 7   VAL A CG1 1 
ATOM   60   C CG2 . VAL A 1 7   ? -0.369  -1.059  45.334  1.00 13.24 ? 7   VAL A CG2 1 
ATOM   61   N N   . PHE A 1 8   ? 2.387   0.296   41.545  1.00 12.87 ? 8   PHE A N   1 
ATOM   62   C CA  . PHE A 1 8   ? 2.528   0.675   40.142  1.00 9.34  ? 8   PHE A CA  1 
ATOM   63   C C   . PHE A 1 8   ? 1.971   -0.437  39.266  1.00 12.34 ? 8   PHE A C   1 
ATOM   64   O O   . PHE A 1 8   ? 2.281   -1.610  39.474  1.00 13.07 ? 8   PHE A O   1 
ATOM   65   C CB  . PHE A 1 8   ? 3.997   0.897   39.762  1.00 9.39  ? 8   PHE A CB  1 
ATOM   66   C CG  . PHE A 1 8   ? 4.586   2.145   40.328  1.00 12.22 ? 8   PHE A CG  1 
ATOM   67   C CD1 . PHE A 1 8   ? 4.491   3.338   39.642  1.00 13.09 ? 8   PHE A CD1 1 
ATOM   68   C CD2 . PHE A 1 8   ? 5.239   2.117   41.551  1.00 12.55 ? 8   PHE A CD2 1 
ATOM   69   C CE1 . PHE A 1 8   ? 5.033   4.495   40.170  1.00 19.04 ? 8   PHE A CE1 1 
ATOM   70   C CE2 . PHE A 1 8   ? 5.777   3.266   42.097  1.00 12.75 ? 8   PHE A CE2 1 
ATOM   71   C CZ  . PHE A 1 8   ? 5.675   4.462   41.401  1.00 21.94 ? 8   PHE A CZ  1 
ATOM   72   N N   . TRP A 1 9   ? 1.195   -0.057  38.258  1.00 11.79 ? 9   TRP A N   1 
ATOM   73   C CA  . TRP A 1 9   ? 0.609   -1.014  37.316  1.00 13.05 ? 9   TRP A CA  1 
ATOM   74   C C   . TRP A 1 9   ? 0.768   -0.386  35.937  1.00 11.13 ? 9   TRP A C   1 
ATOM   75   O O   . TRP A 1 9   ? 0.014   0.523   35.576  1.00 12.54 ? 9   TRP A O   1 
ATOM   76   C CB  . TRP A 1 9   ? -0.851  -1.296  37.664  1.00 12.76 ? 9   TRP A CB  1 
ATOM   77   C CG  . TRP A 1 9   ? -1.449  -2.548  37.065  1.00 12.50 ? 9   TRP A CG  1 
ATOM   78   C CD1 . TRP A 1 9   ? -0.894  -3.363  36.121  1.00 13.13 ? 9   TRP A CD1 1 
ATOM   79   C CD2 . TRP A 1 9   ? -2.727  -3.109  37.384  1.00 11.07 ? 9   TRP A CD2 1 
ATOM   80   N NE1 . TRP A 1 9   ? -1.760  -4.395  35.821  1.00 10.35 ? 9   TRP A NE1 1 
ATOM   81   C CE2 . TRP A 1 9   ? -2.891  -4.259  36.587  1.00 14.14 ? 9   TRP A CE2 1 
ATOM   82   C CE3 . TRP A 1 9   ? -3.756  -2.739  38.265  1.00 8.66  ? 9   TRP A CE3 1 
ATOM   83   C CZ2 . TRP A 1 9   ? -4.045  -5.046  36.639  1.00 12.13 ? 9   TRP A CZ2 1 
ATOM   84   C CZ3 . TRP A 1 9   ? -4.883  -3.522  38.329  1.00 9.80  ? 9   TRP A CZ3 1 
ATOM   85   C CH2 . TRP A 1 9   ? -5.027  -4.664  37.516  1.00 12.94 ? 9   TRP A CH2 1 
ATOM   86   N N   . TRP A 1 10  ? 1.781   -0.846  35.198  1.00 6.93  ? 10  TRP A N   1 
ATOM   87   C CA  . TRP A 1 10  ? 2.155   -0.283  33.905  1.00 7.34  ? 10  TRP A CA  1 
ATOM   88   C C   . TRP A 1 10  ? 1.436   -1.063  32.806  1.00 9.63  ? 10  TRP A C   1 
ATOM   89   O O   . TRP A 1 10  ? 1.644   -2.272  32.660  1.00 10.57 ? 10  TRP A O   1 
ATOM   90   C CB  . TRP A 1 10  ? 3.676   -0.358  33.707  1.00 7.02  ? 10  TRP A CB  1 
ATOM   91   C CG  . TRP A 1 10  ? 4.518   0.426   34.707  1.00 9.71  ? 10  TRP A CG  1 
ATOM   92   C CD1 . TRP A 1 10  ? 5.351   -0.096  35.657  1.00 8.42  ? 10  TRP A CD1 1 
ATOM   93   C CD2 . TRP A 1 10  ? 4.652   1.855   34.808  1.00 9.62  ? 10  TRP A CD2 1 
ATOM   94   N NE1 . TRP A 1 10  ? 5.967   0.909   36.358  1.00 10.78 ? 10  TRP A NE1 1 
ATOM   95   C CE2 . TRP A 1 10  ? 5.557   2.116   35.860  1.00 10.24 ? 10  TRP A CE2 1 
ATOM   96   C CE3 . TRP A 1 10  ? 4.088   2.937   34.116  1.00 14.77 ? 10  TRP A CE3 1 
ATOM   97   C CZ2 . TRP A 1 10  ? 5.922   3.414   36.236  1.00 11.04 ? 10  TRP A CZ2 1 
ATOM   98   C CZ3 . TRP A 1 10  ? 4.447   4.225   34.494  1.00 18.30 ? 10  TRP A CZ3 1 
ATOM   99   C CH2 . TRP A 1 10  ? 5.355   4.451   35.550  1.00 12.78 ? 10  TRP A CH2 1 
ATOM   100  N N   . HIS A 1 11  ? 0.608   -0.380  32.029  1.00 8.18  ? 11  HIS A N   1 
ATOM   101  C CA  . HIS A 1 11  ? -0.241  -1.035  31.034  1.00 13.03 ? 11  HIS A CA  1 
ATOM   102  C C   . HIS A 1 11  ? 0.416   -0.990  29.656  1.00 9.51  ? 11  HIS A C   1 
ATOM   103  O O   . HIS A 1 11  ? 0.702   0.094   29.141  1.00 13.56 ? 11  HIS A O   1 
ATOM   104  C CB  . HIS A 1 11  ? -1.614  -0.363  31.006  1.00 11.82 ? 11  HIS A CB  1 
ATOM   105  C CG  . HIS A 1 11  ? -2.396  -0.669  29.774  1.00 14.75 ? 11  HIS A CG  1 
ATOM   106  N ND1 . HIS A 1 11  ? -2.801  -1.945  29.460  1.00 12.61 ? 11  HIS A ND1 1 
ATOM   107  C CD2 . HIS A 1 11  ? -2.836  0.129   28.772  1.00 15.91 ? 11  HIS A CD2 1 
ATOM   108  C CE1 . HIS A 1 11  ? -3.466  -1.922  28.317  1.00 13.01 ? 11  HIS A CE1 1 
ATOM   109  N NE2 . HIS A 1 11  ? -3.511  -0.674  27.884  1.00 12.86 ? 11  HIS A NE2 1 
ATOM   110  N N   . MET A 1 12  ? 0.644   -2.165  29.049  1.00 9.07  ? 12  MET A N   1 
ATOM   111  C CA  . MET A 1 12  ? 1.302   -2.287  27.750  1.00 9.48  ? 12  MET A CA  1 
ATOM   112  C C   . MET A 1 12  ? 0.318   -2.844  26.727  1.00 12.09 ? 12  MET A C   1 
ATOM   113  O O   . MET A 1 12  ? -0.272  -3.908  26.950  1.00 10.31 ? 12  MET A O   1 
ATOM   114  C CB  . MET A 1 12  ? 2.538   -3.208  27.810  1.00 8.94  ? 12  MET A CB  1 
ATOM   115  C CG  . MET A 1 12  ? 3.474   -2.954  28.973  1.00 14.20 ? 12  MET A CG  1 
ATOM   116  S SD  . MET A 1 12  ? 4.124   -1.281  28.878  1.00 11.99 ? 12  MET A SD  1 
ATOM   117  C CE  . MET A 1 12  ? 5.502   -1.423  30.022  1.00 12.52 ? 12  MET A CE  1 
ATOM   118  N N   . HIS A 1 13  ? 0.150   -2.134  25.612  1.00 12.91 ? 13  HIS A N   1 
ATOM   119  C CA  . HIS A 1 13  ? -0.816  -2.538  24.593  1.00 14.18 ? 13  HIS A CA  1 
ATOM   120  C C   . HIS A 1 13  ? -0.446  -1.950  23.232  1.00 17.06 ? 13  HIS A C   1 
ATOM   121  O O   . HIS A 1 13  ? 0.014   -0.810  23.147  1.00 11.00 ? 13  HIS A O   1 
ATOM   122  C CB  . HIS A 1 13  ? -2.240  -2.092  24.986  1.00 7.35  ? 13  HIS A CB  1 
ATOM   123  C CG  . HIS A 1 13  ? -3.259  -2.315  23.907  1.00 12.39 ? 13  HIS A CG  1 
ATOM   124  N ND1 . HIS A 1 13  ? -3.579  -3.569  23.424  1.00 11.46 ? 13  HIS A ND1 1 
ATOM   125  C CD2 . HIS A 1 13  ? -4.023  -1.439  23.208  1.00 15.06 ? 13  HIS A CD2 1 
ATOM   126  C CE1 . HIS A 1 13  ? -4.492  -3.456  22.473  1.00 12.08 ? 13  HIS A CE1 1 
ATOM   127  N NE2 . HIS A 1 13  ? -4.774  -2.173  22.316  1.00 11.20 ? 13  HIS A NE2 1 
ATOM   128  N N   . GLN A 1 14  ? -0.678  -2.727  22.167  1.00 11.64 ? 14  GLN A N   1 
ATOM   129  C CA  . GLN A 1 14  ? -0.765  -2.197  20.798  1.00 11.11 ? 14  GLN A CA  1 
ATOM   130  C C   . GLN A 1 14  ? -1.900  -2.919  20.082  1.00 9.27  ? 14  GLN A C   1 
ATOM   131  O O   . GLN A 1 14  ? -2.017  -4.149  20.199  1.00 15.91 ? 14  GLN A O   1 
ATOM   132  C CB  . GLN A 1 14  ? 0.537   -2.378  19.991  1.00 11.27 ? 14  GLN A CB  1 
ATOM   133  C CG  . GLN A 1 14  ? 1.757   -1.643  20.563  1.00 14.96 ? 14  GLN A CG  1 
ATOM   134  C CD  . GLN A 1 14  ? 1.630   -0.127  20.473  1.00 15.43 ? 14  GLN A CD  1 
ATOM   135  O OE1 . GLN A 1 14  ? 0.830   0.409   19.695  1.00 16.65 ? 14  GLN A OE1 1 
ATOM   136  N NE2 . GLN A 1 14  ? 2.432   0.573   21.263  1.00 13.32 ? 14  GLN A NE2 1 
ATOM   137  N N   . PRO A 1 15  ? -2.738  -2.198  19.335  1.00 10.68 ? 15  PRO A N   1 
ATOM   138  C CA  . PRO A 1 15  ? -3.717  -2.864  18.461  1.00 11.95 ? 15  PRO A CA  1 
ATOM   139  C C   . PRO A 1 15  ? -3.008  -3.631  17.351  1.00 14.55 ? 15  PRO A C   1 
ATOM   140  O O   . PRO A 1 15  ? -1.810  -3.476  17.115  1.00 16.35 ? 15  PRO A O   1 
ATOM   141  C CB  . PRO A 1 15  ? -4.555  -1.705  17.905  1.00 18.47 ? 15  PRO A CB  1 
ATOM   142  C CG  . PRO A 1 15  ? -3.598  -0.543  17.873  1.00 10.34 ? 15  PRO A CG  1 
ATOM   143  C CD  . PRO A 1 15  ? -2.742  -0.731  19.147  1.00 7.44  ? 15  PRO A CD  1 
ATOM   144  N N   . LEU A 1 16  ? -3.759  -4.499  16.665  1.00 15.58 ? 16  LEU A N   1 
ATOM   145  C CA  . LEU A 1 16  ? -3.117  -5.375  15.683  1.00 17.17 ? 16  LEU A CA  1 
ATOM   146  C C   . LEU A 1 16  ? -2.791  -4.572  14.434  1.00 17.47 ? 16  LEU A C   1 
ATOM   147  O O   . LEU A 1 16  ? -3.695  -4.151  13.709  1.00 18.26 ? 16  LEU A O   1 
ATOM   148  C CB  . LEU A 1 16  ? -3.995  -6.578  15.343  1.00 14.00 ? 16  LEU A CB  1 
ATOM   149  C CG  . LEU A 1 16  ? -3.386  -7.661  14.433  1.00 19.18 ? 16  LEU A CG  1 
ATOM   150  C CD1 . LEU A 1 16  ? -2.005  -8.160  14.924  1.00 16.54 ? 16  LEU A CD1 1 
ATOM   151  C CD2 . LEU A 1 16  ? -4.345  -8.838  14.266  1.00 21.81 ? 16  LEU A CD2 1 
ATOM   152  N N   . TYR A 1 17  ? -1.503  -4.354  14.176  1.00 17.70 ? 17  TYR A N   1 
ATOM   153  C CA  . TYR A 1 17  ? -1.087  -3.595  13.002  1.00 14.87 ? 17  TYR A CA  1 
ATOM   154  C C   . TYR A 1 17  ? -0.959  -4.463  11.754  1.00 17.72 ? 17  TYR A C   1 
ATOM   155  O O   . TYR A 1 17  ? -0.673  -3.939  10.672  1.00 14.81 ? 17  TYR A O   1 
ATOM   156  C CB  . TYR A 1 17  ? 0.236   -2.877  13.284  1.00 14.98 ? 17  TYR A CB  1 
ATOM   157  C CG  . TYR A 1 17  ? 0.129   -1.818  14.354  1.00 16.77 ? 17  TYR A CG  1 
ATOM   158  C CD1 . TYR A 1 17  ? -0.636  -0.678  14.159  1.00 18.25 ? 17  TYR A CD1 1 
ATOM   159  C CD2 . TYR A 1 17  ? 0.792   -1.961  15.566  1.00 21.02 ? 17  TYR A CD2 1 
ATOM   160  C CE1 . TYR A 1 17  ? -0.735  0.300   15.147  1.00 17.29 ? 17  TYR A CE1 1 
ATOM   161  C CE2 . TYR A 1 17  ? 0.691   -1.006  16.550  1.00 13.59 ? 17  TYR A CE2 1 
ATOM   162  C CZ  . TYR A 1 17  ? -0.066  0.126   16.340  1.00 13.91 ? 17  TYR A CZ  1 
ATOM   163  O OH  . TYR A 1 17  ? -0.149  1.072   17.325  1.00 17.10 ? 17  TYR A OH  1 
ATOM   164  N N   . ARG A 1 18  ? -1.192  -5.763  11.883  1.00 18.49 ? 18  ARG A N   1 
ATOM   165  C CA  . ARG A 1 18  ? -0.936  -6.735  10.830  1.00 17.98 ? 18  ARG A CA  1 
ATOM   166  C C   . ARG A 1 18  ? -2.143  -6.817  9.899   1.00 20.73 ? 18  ARG A C   1 
ATOM   167  O O   . ARG A 1 18  ? -3.176  -7.383  10.264  1.00 20.96 ? 18  ARG A O   1 
ATOM   168  C CB  . ARG A 1 18  ? -0.633  -8.093  11.461  1.00 15.73 ? 18  ARG A CB  1 
ATOM   169  C CG  . ARG A 1 18  ? -0.052  -9.137  10.494  1.00 25.26 ? 18  ARG A CG  1 
ATOM   170  C CD  . ARG A 1 18  ? 0.034   -10.518 11.161  1.00 21.52 ? 18  ARG A CD  1 
ATOM   171  N NE  . ARG A 1 18  ? 0.514   -11.567 10.257  1.00 26.62 ? 18  ARG A NE  1 
ATOM   172  C CZ  . ARG A 1 18  ? -0.212  -12.157 9.310   1.00 28.54 ? 18  ARG A CZ  1 
ATOM   173  N NH1 . ARG A 1 18  ? -1.481  -11.827 9.112   1.00 23.67 ? 18  ARG A NH1 1 
ATOM   174  N NH2 . ARG A 1 18  ? 0.335   -13.102 8.557   1.00 40.03 ? 18  ARG A NH2 1 
ATOM   175  N N   . GLU A 1 19  ? -2.005  -6.273  8.692   1.00 23.20 ? 19  GLU A N   1 
ATOM   176  C CA  . GLU A 1 19  ? -3.078  -6.334  7.705   1.00 23.38 ? 19  GLU A CA  1 
ATOM   177  C C   . GLU A 1 19  ? -3.378  -7.788  7.345   1.00 20.18 ? 19  GLU A C   1 
ATOM   178  O O   . GLU A 1 19  ? -2.452  -8.550  7.050   1.00 18.69 ? 19  GLU A O   1 
ATOM   179  C CB  . GLU A 1 19  ? -2.690  -5.552  6.454   1.00 20.13 ? 19  GLU A CB  1 
ATOM   180  C CG  . GLU A 1 19  ? -3.858  -4.873  5.749   1.00 27.37 ? 19  GLU A CG  1 
ATOM   181  C CD  . GLU A 1 19  ? -4.457  -5.731  4.647   1.00 28.41 ? 19  GLU A CD  1 
ATOM   182  O OE1 . GLU A 1 19  ? -3.966  -6.858  4.431   1.00 32.05 ? 19  GLU A OE1 1 
ATOM   183  O OE2 . GLU A 1 19  ? -5.415  -5.269  3.991   1.00 35.68 ? 19  GLU A OE2 1 
ATOM   184  N N   . PRO A 1 20  ? -4.649  -8.203  7.344   1.00 22.71 ? 20  PRO A N   1 
ATOM   185  C CA  . PRO A 1 20  ? -4.955  -9.643  7.282   1.00 25.23 ? 20  PRO A CA  1 
ATOM   186  C C   . PRO A 1 20  ? -4.773  -10.286 5.911   1.00 34.03 ? 20  PRO A C   1 
ATOM   187  O O   . PRO A 1 20  ? -4.583  -11.508 5.852   1.00 31.71 ? 20  PRO A O   1 
ATOM   188  C CB  . PRO A 1 20  ? -6.426  -9.718  7.734   1.00 20.89 ? 20  PRO A CB  1 
ATOM   189  C CG  . PRO A 1 20  ? -6.985  -8.333  7.495   1.00 26.17 ? 20  PRO A CG  1 
ATOM   190  C CD  . PRO A 1 20  ? -5.834  -7.372  7.639   1.00 20.75 ? 20  PRO A CD  1 
ATOM   191  N N   . TYR A 1 21  ? -4.818  -9.525  4.818   1.00 31.51 ? 21  TYR A N   1 
ATOM   192  C CA  . TYR A 1 21  ? -4.644  -10.107 3.489   1.00 30.01 ? 21  TYR A CA  1 
ATOM   193  C C   . TYR A 1 21  ? -3.182  -10.143 3.053   1.00 28.29 ? 21  TYR A C   1 
ATOM   194  O O   . TYR A 1 21  ? -2.725  -11.142 2.492   1.00 35.97 ? 21  TYR A O   1 
ATOM   195  C CB  . TYR A 1 21  ? -5.478  -9.329  2.471   1.00 30.57 ? 21  TYR A CB  1 
ATOM   196  C CG  . TYR A 1 21  ? -6.952  -9.391  2.761   1.00 33.92 ? 21  TYR A CG  1 
ATOM   197  C CD1 . TYR A 1 21  ? -7.729  -10.418 2.250   1.00 28.16 ? 21  TYR A CD1 1 
ATOM   198  C CD2 . TYR A 1 21  ? -7.567  -8.434  3.570   1.00 39.01 ? 21  TYR A CD2 1 
ATOM   199  C CE1 . TYR A 1 21  ? -9.072  -10.488 2.515   1.00 31.74 ? 21  TYR A CE1 1 
ATOM   200  C CE2 . TYR A 1 21  ? -8.926  -8.497  3.845   1.00 39.33 ? 21  TYR A CE2 1 
ATOM   201  C CZ  . TYR A 1 21  ? -9.674  -9.531  3.315   1.00 41.46 ? 21  TYR A CZ  1 
ATOM   202  O OH  . TYR A 1 21  ? -11.025 -9.609  3.578   1.00 40.30 ? 21  TYR A OH  1 
ATOM   203  N N   . THR A 1 22  ? -2.435  -9.073  3.303   1.00 22.43 ? 22  THR A N   1 
ATOM   204  C CA  . THR A 1 22  ? -1.027  -9.021  2.953   1.00 23.82 ? 22  THR A CA  1 
ATOM   205  C C   . THR A 1 22  ? -0.121  -9.567  4.046   1.00 28.86 ? 22  THR A C   1 
ATOM   206  O O   . THR A 1 22  ? 1.038   -9.888  3.764   1.00 27.52 ? 22  THR A O   1 
ATOM   207  C CB  . THR A 1 22  ? -0.626  -7.578  2.646   1.00 30.55 ? 22  THR A CB  1 
ATOM   208  O OG1 . THR A 1 22  ? -0.802  -6.778  3.826   1.00 29.77 ? 22  THR A OG1 1 
ATOM   209  C CG2 . THR A 1 22  ? -1.500  -7.021  1.530   1.00 28.09 ? 22  THR A CG2 1 
ATOM   210  N N   . GLY A 1 23  ? -0.621  -9.700  5.275   1.00 25.67 ? 23  GLY A N   1 
ATOM   211  C CA  . GLY A 1 23  ? 0.218   -10.087 6.392   1.00 20.69 ? 23  GLY A CA  1 
ATOM   212  C C   . GLY A 1 23  ? 1.194   -9.022  6.849   1.00 23.17 ? 23  GLY A C   1 
ATOM   213  O O   . GLY A 1 23  ? 2.030   -9.297  7.715   1.00 33.68 ? 23  GLY A O   1 
ATOM   214  N N   . GLU A 1 24  ? 1.114   -7.813  6.300   1.00 17.94 ? 24  GLU A N   1 
ATOM   215  C CA  . GLU A 1 24  ? 2.105   -6.777  6.556   1.00 21.69 ? 24  GLU A CA  1 
ATOM   216  C C   . GLU A 1 24  ? 1.739   -5.917  7.761   1.00 25.30 ? 24  GLU A C   1 
ATOM   217  O O   . GLU A 1 24  ? 0.576   -5.541  7.947   1.00 18.62 ? 24  GLU A O   1 
ATOM   218  C CB  . GLU A 1 24  ? 2.265   -5.896  5.323   1.00 25.30 ? 24  GLU A CB  1 
ATOM   219  C CG  . GLU A 1 24  ? 3.028   -6.609  4.217   1.00 35.85 ? 24  GLU A CG  1 
ATOM   220  C CD  . GLU A 1 24  ? 2.905   -5.926  2.879   1.00 48.90 ? 24  GLU A CD  1 
ATOM   221  O OE1 . GLU A 1 24  ? 2.211   -4.893  2.795   1.00 49.86 ? 24  GLU A OE1 1 
ATOM   222  O OE2 . GLU A 1 24  ? 3.502   -6.434  1.907   1.00 55.82 ? 24  GLU A OE2 1 
ATOM   223  N N   . TYR A 1 25  ? 2.750   -5.601  8.571   1.00 21.28 ? 25  TYR A N   1 
ATOM   224  C CA  . TYR A 1 25  ? 2.580   -4.699  9.705   1.00 17.53 ? 25  TYR A CA  1 
ATOM   225  C C   . TYR A 1 25  ? 2.653   -3.276  9.181   1.00 18.38 ? 25  TYR A C   1 
ATOM   226  O O   . TYR A 1 25  ? 3.714   -2.825  8.740   1.00 20.60 ? 25  TYR A O   1 
ATOM   227  C CB  . TYR A 1 25  ? 3.648   -4.967  10.762  1.00 17.39 ? 25  TYR A CB  1 
ATOM   228  C CG  . TYR A 1 25  ? 3.283   -6.087  11.700  1.00 18.47 ? 25  TYR A CG  1 
ATOM   229  C CD1 . TYR A 1 25  ? 3.311   -7.416  11.282  1.00 22.64 ? 25  TYR A CD1 1 
ATOM   230  C CD2 . TYR A 1 25  ? 2.902   -5.816  13.008  1.00 18.77 ? 25  TYR A CD2 1 
ATOM   231  C CE1 . TYR A 1 25  ? 2.974   -8.447  12.155  1.00 18.78 ? 25  TYR A CE1 1 
ATOM   232  C CE2 . TYR A 1 25  ? 2.561   -6.831  13.878  1.00 14.10 ? 25  TYR A CE2 1 
ATOM   233  C CZ  . TYR A 1 25  ? 2.595   -8.135  13.455  1.00 19.47 ? 25  TYR A CZ  1 
ATOM   234  O OH  . TYR A 1 25  ? 2.262   -9.135  14.335  1.00 20.82 ? 25  TYR A OH  1 
ATOM   235  N N   . LEU A 1 26  ? 1.518   -2.577  9.202   1.00 16.64 ? 26  LEU A N   1 
ATOM   236  C CA  . LEU A 1 26  ? 1.384   -1.319  8.479   1.00 18.13 ? 26  LEU A CA  1 
ATOM   237  C C   . LEU A 1 26  ? 1.940   -0.118  9.231   1.00 18.27 ? 26  LEU A C   1 
ATOM   238  O O   . LEU A 1 26  ? 2.130   0.937   8.616   1.00 18.59 ? 26  LEU A O   1 
ATOM   239  C CB  . LEU A 1 26  ? -0.084  -1.064  8.135   1.00 20.56 ? 26  LEU A CB  1 
ATOM   240  C CG  . LEU A 1 26  ? -0.764  -2.021  7.153   1.00 24.74 ? 26  LEU A CG  1 
ATOM   241  C CD1 . LEU A 1 26  ? -2.124  -1.455  6.752   1.00 22.70 ? 26  LEU A CD1 1 
ATOM   242  C CD2 . LEU A 1 26  ? 0.113   -2.263  5.920   1.00 18.38 ? 26  LEU A CD2 1 
ATOM   243  N N   . LEU A 1 27  ? 2.173   -0.237  10.537  1.00 16.12 ? 27  LEU A N   1 
ATOM   244  C CA  . LEU A 1 27  ? 2.861   0.758   11.342  1.00 16.37 ? 27  LEU A CA  1 
ATOM   245  C C   . LEU A 1 27  ? 3.873   0.050   12.225  1.00 13.35 ? 27  LEU A C   1 
ATOM   246  O O   . LEU A 1 27  ? 3.672   -1.115  12.590  1.00 18.41 ? 27  LEU A O   1 
ATOM   247  C CB  . LEU A 1 27  ? 1.893   1.557   12.231  1.00 13.78 ? 27  LEU A CB  1 
ATOM   248  C CG  . LEU A 1 27  ? 0.916   2.486   11.509  1.00 19.07 ? 27  LEU A CG  1 
ATOM   249  C CD1 . LEU A 1 27  ? -0.192  2.910   12.449  1.00 17.13 ? 27  LEU A CD1 1 
ATOM   250  C CD2 . LEU A 1 27  ? 1.644   3.678   10.949  1.00 18.12 ? 27  LEU A CD2 1 
ATOM   251  N N   . PRO A 1 28  ? 4.958   0.728   12.601  1.00 12.34 ? 28  PRO A N   1 
ATOM   252  C CA  . PRO A 1 28  ? 6.034   0.041   13.326  1.00 11.07 ? 28  PRO A CA  1 
ATOM   253  C C   . PRO A 1 28  ? 5.997   0.222   14.842  1.00 17.47 ? 28  PRO A C   1 
ATOM   254  O O   . PRO A 1 28  ? 7.004   -0.023  15.517  1.00 15.72 ? 28  PRO A O   1 
ATOM   255  C CB  . PRO A 1 28  ? 7.286   0.691   12.737  1.00 10.43 ? 28  PRO A CB  1 
ATOM   256  C CG  . PRO A 1 28  ? 6.832   2.166   12.580  1.00 15.72 ? 28  PRO A CG  1 
ATOM   257  C CD  . PRO A 1 28  ? 5.333   2.116   12.262  1.00 16.09 ? 28  PRO A CD  1 
ATOM   258  N N   . TRP A 1 29  ? 4.862   0.652   15.400  1.00 19.47 ? 29  TRP A N   1 
ATOM   259  C CA  . TRP A 1 29  ? 4.850   1.059   16.806  1.00 13.55 ? 29  TRP A CA  1 
ATOM   260  C C   . TRP A 1 29  ? 5.123   -0.105  17.756  1.00 18.04 ? 29  TRP A C   1 
ATOM   261  O O   . TRP A 1 29  ? 5.711   0.091   18.830  1.00 14.43 ? 29  TRP A O   1 
ATOM   262  C CB  . TRP A 1 29  ? 3.512   1.704   17.149  1.00 16.53 ? 29  TRP A CB  1 
ATOM   263  C CG  . TRP A 1 29  ? 3.263   2.998   16.459  1.00 21.21 ? 29  TRP A CG  1 
ATOM   264  C CD1 . TRP A 1 29  ? 2.186   3.313   15.690  1.00 20.53 ? 29  TRP A CD1 1 
ATOM   265  C CD2 . TRP A 1 29  ? 4.096   4.168   16.487  1.00 19.63 ? 29  TRP A CD2 1 
ATOM   266  N NE1 . TRP A 1 29  ? 2.295   4.604   15.236  1.00 22.88 ? 29  TRP A NE1 1 
ATOM   267  C CE2 . TRP A 1 29  ? 3.459   5.150   15.709  1.00 21.79 ? 29  TRP A CE2 1 
ATOM   268  C CE3 . TRP A 1 29  ? 5.319   4.478   17.094  1.00 22.48 ? 29  TRP A CE3 1 
ATOM   269  C CZ2 . TRP A 1 29  ? 3.998   6.425   15.523  1.00 22.45 ? 29  TRP A CZ2 1 
ATOM   270  C CZ3 . TRP A 1 29  ? 5.846   5.748   16.916  1.00 21.78 ? 29  TRP A CZ3 1 
ATOM   271  C CH2 . TRP A 1 29  ? 5.191   6.701   16.135  1.00 23.57 ? 29  TRP A CH2 1 
ATOM   272  N N   . THR A 1 30  ? 4.687   -1.313  17.402  1.00 13.07 ? 30  THR A N   1 
ATOM   273  C CA  . THR A 1 30  ? 4.966   -2.455  18.265  1.00 16.60 ? 30  THR A CA  1 
ATOM   274  C C   . THR A 1 30  ? 6.458   -2.754  18.303  1.00 19.58 ? 30  THR A C   1 
ATOM   275  O O   . THR A 1 30  ? 7.025   -2.988  19.381  1.00 15.37 ? 30  THR A O   1 
ATOM   276  C CB  . THR A 1 30  ? 4.164   -3.673  17.803  1.00 17.32 ? 30  THR A CB  1 
ATOM   277  O OG1 . THR A 1 30  ? 2.759   -3.398  17.946  1.00 18.28 ? 30  THR A OG1 1 
ATOM   278  C CG2 . THR A 1 30  ? 4.537   -4.912  18.628  1.00 17.73 ? 30  THR A CG2 1 
ATOM   279  N N   . PHE A 1 31  ? 7.118   -2.709  17.142  1.00 15.07 ? 31  PHE A N   1 
ATOM   280  C CA  . PHE A 1 31  ? 8.569   -2.904  17.093  1.00 12.15 ? 31  PHE A CA  1 
ATOM   281  C C   . PHE A 1 31  ? 9.292   -1.861  17.941  1.00 16.86 ? 31  PHE A C   1 
ATOM   282  O O   . PHE A 1 31  ? 10.115  -2.199  18.799  1.00 16.14 ? 31  PHE A O   1 
ATOM   283  C CB  . PHE A 1 31  ? 9.059   -2.842  15.641  1.00 12.08 ? 31  PHE A CB  1 
ATOM   284  C CG  . PHE A 1 31  ? 10.566  -2.889  15.515  1.00 15.23 ? 31  PHE A CG  1 
ATOM   285  C CD1 . PHE A 1 31  ? 11.239  -4.097  15.601  1.00 17.12 ? 31  PHE A CD1 1 
ATOM   286  C CD2 . PHE A 1 31  ? 11.305  -1.720  15.361  1.00 16.35 ? 31  PHE A CD2 1 
ATOM   287  C CE1 . PHE A 1 31  ? 12.622  -4.139  15.502  1.00 14.51 ? 31  PHE A CE1 1 
ATOM   288  C CE2 . PHE A 1 31  ? 12.684  -1.752  15.257  1.00 17.19 ? 31  PHE A CE2 1 
ATOM   289  C CZ  . PHE A 1 31  ? 13.342  -2.971  15.334  1.00 18.81 ? 31  PHE A CZ  1 
ATOM   290  N N   . PHE A 1 32  ? 8.964   -0.581  17.738  1.00 10.98 ? 32  PHE A N   1 
ATOM   291  C CA  . PHE A 1 32  ? 9.681   0.487   18.427  1.00 10.25 ? 32  PHE A CA  1 
ATOM   292  C C   . PHE A 1 32  ? 9.414   0.484   19.932  1.00 10.75 ? 32  PHE A C   1 
ATOM   293  O O   . PHE A 1 32  ? 10.337  0.673   20.731  1.00 9.62  ? 32  PHE A O   1 
ATOM   294  C CB  . PHE A 1 32  ? 9.311   1.827   17.794  1.00 12.91 ? 32  PHE A CB  1 
ATOM   295  C CG  . PHE A 1 32  ? 10.077  2.117   16.519  1.00 15.77 ? 32  PHE A CG  1 
ATOM   296  C CD1 . PHE A 1 32  ? 11.454  1.958   16.475  1.00 21.29 ? 32  PHE A CD1 1 
ATOM   297  C CD2 . PHE A 1 32  ? 9.423   2.531   15.372  1.00 18.33 ? 32  PHE A CD2 1 
ATOM   298  C CE1 . PHE A 1 32  ? 12.171  2.216   15.311  1.00 22.99 ? 32  PHE A CE1 1 
ATOM   299  C CE2 . PHE A 1 32  ? 10.127  2.781   14.201  1.00 23.78 ? 32  PHE A CE2 1 
ATOM   300  C CZ  . PHE A 1 32  ? 11.508  2.630   14.174  1.00 19.49 ? 32  PHE A CZ  1 
ATOM   301  N N   . HIS A 1 33  ? 8.171   0.275   20.354  1.00 8.78  ? 33  HIS A N   1 
ATOM   302  C CA  . HIS A 1 33  ? 7.966   0.192   21.798  1.00 13.74 ? 33  HIS A CA  1 
ATOM   303  C C   . HIS A 1 33  ? 8.503   -1.106  22.390  1.00 15.76 ? 33  HIS A C   1 
ATOM   304  O O   . HIS A 1 33  ? 8.874   -1.126  23.572  1.00 13.05 ? 33  HIS A O   1 
ATOM   305  C CB  . HIS A 1 33  ? 6.491   0.393   22.118  1.00 12.89 ? 33  HIS A CB  1 
ATOM   306  C CG  . HIS A 1 33  ? 6.073   1.817   21.970  1.00 10.58 ? 33  HIS A CG  1 
ATOM   307  N ND1 . HIS A 1 33  ? 6.608   2.820   22.751  1.00 12.01 ? 33  HIS A ND1 1 
ATOM   308  C CD2 . HIS A 1 33  ? 5.248   2.424   21.087  1.00 9.75  ? 33  HIS A CD2 1 
ATOM   309  C CE1 . HIS A 1 33  ? 6.088   3.982   22.387  1.00 13.16 ? 33  HIS A CE1 1 
ATOM   310  N NE2 . HIS A 1 33  ? 5.267   3.770   21.374  1.00 13.00 ? 33  HIS A NE2 1 
ATOM   311  N N   . ALA A 1 34  ? 8.598   -2.174  21.598  1.00 17.64 ? 34  ALA A N   1 
ATOM   312  C CA  . ALA A 1 34  ? 9.252   -3.384  22.095  1.00 16.39 ? 34  ALA A CA  1 
ATOM   313  C C   . ALA A 1 34  ? 10.729  -3.128  22.360  1.00 13.26 ? 34  ALA A C   1 
ATOM   314  O O   . ALA A 1 34  ? 11.232  -3.415  23.450  1.00 14.30 ? 34  ALA A O   1 
ATOM   315  C CB  . ALA A 1 34  ? 9.074   -4.545  21.109  1.00 15.38 ? 34  ALA A CB  1 
ATOM   316  N N   . VAL A 1 35  ? 11.447  -2.581  21.376  1.00 12.78 ? 35  VAL A N   1 
ATOM   317  C CA  . VAL A 1 35  ? 12.874  -2.362  21.592  1.00 19.92 ? 35  VAL A CA  1 
ATOM   318  C C   . VAL A 1 35  ? 13.124  -1.273  22.634  1.00 17.08 ? 35  VAL A C   1 
ATOM   319  O O   . VAL A 1 35  ? 14.153  -1.293  23.314  1.00 14.04 ? 35  VAL A O   1 
ATOM   320  C CB  . VAL A 1 35  ? 13.591  -2.052  20.262  1.00 23.24 ? 35  VAL A CB  1 
ATOM   321  C CG1 . VAL A 1 35  ? 13.195  -3.069  19.197  1.00 14.31 ? 35  VAL A CG1 1 
ATOM   322  C CG2 . VAL A 1 35  ? 13.278  -0.647  19.786  1.00 23.29 ? 35  VAL A CG2 1 
ATOM   323  N N   . LYS A 1 36  ? 12.208  -0.321  22.803  1.00 18.55 ? 36  LYS A N   1 
ATOM   324  C CA  . LYS A 1 36  ? 12.475  0.779   23.732  1.00 11.15 ? 36  LYS A CA  1 
ATOM   325  C C   . LYS A 1 36  ? 11.893  0.576   25.129  1.00 13.44 ? 36  LYS A C   1 
ATOM   326  O O   . LYS A 1 36  ? 12.533  0.967   26.120  1.00 13.52 ? 36  LYS A O   1 
ATOM   327  C CB  . LYS A 1 36  ? 11.954  2.100   23.152  1.00 9.26  ? 36  LYS A CB  1 
ATOM   328  C CG  . LYS A 1 36  ? 12.376  3.335   23.971  1.00 13.21 ? 36  LYS A CG  1 
ATOM   329  C CD  . LYS A 1 36  ? 12.017  4.668   23.279  1.00 13.93 ? 36  LYS A CD  1 
ATOM   330  C CE  . LYS A 1 36  ? 10.534  5.042   23.457  1.00 16.34 ? 36  LYS A CE  1 
ATOM   331  N NZ  . LYS A 1 36  ? 10.101  5.156   24.903  1.00 16.05 ? 36  LYS A NZ  1 
ATOM   332  N N   . ASP A 1 37  ? 10.713  -0.043  25.243  1.00 13.42 ? 37  ASP A N   1 
ATOM   333  C CA  . ASP A 1 37  ? 9.982   -0.032  26.511  1.00 14.83 ? 37  ASP A CA  1 
ATOM   334  C C   . ASP A 1 37  ? 9.580   -1.402  27.048  1.00 11.20 ? 37  ASP A C   1 
ATOM   335  O O   . ASP A 1 37  ? 9.663   -1.614  28.258  1.00 12.69 ? 37  ASP A O   1 
ATOM   336  C CB  . ASP A 1 37  ? 8.730   0.826   26.357  1.00 18.51 ? 37  ASP A CB  1 
ATOM   337  C CG  . ASP A 1 37  ? 9.031   2.183   25.794  1.00 16.15 ? 37  ASP A CG  1 
ATOM   338  O OD1 . ASP A 1 37  ? 9.707   2.969   26.488  1.00 10.69 ? 37  ASP A OD1 1 
ATOM   339  O OD2 . ASP A 1 37  ? 8.587   2.455   24.662  1.00 14.96 ? 37  ASP A OD2 1 
ATOM   340  N N   . TYR A 1 38  ? 9.122   -2.331  26.197  1.00 7.65  ? 38  TYR A N   1 
ATOM   341  C CA  . TYR A 1 38  ? 8.462   -3.528  26.727  1.00 11.18 ? 38  TYR A CA  1 
ATOM   342  C C   . TYR A 1 38  ? 9.439   -4.450  27.449  1.00 13.86 ? 38  TYR A C   1 
ATOM   343  O O   . TYR A 1 38  ? 9.056   -5.134  28.408  1.00 13.86 ? 38  TYR A O   1 
ATOM   344  C CB  . TYR A 1 38  ? 7.741   -4.281  25.609  1.00 10.85 ? 38  TYR A CB  1 
ATOM   345  C CG  . TYR A 1 38  ? 6.573   -3.503  25.059  1.00 13.44 ? 38  TYR A CG  1 
ATOM   346  C CD1 . TYR A 1 38  ? 5.832   -2.645  25.881  1.00 14.48 ? 38  TYR A CD1 1 
ATOM   347  C CD2 . TYR A 1 38  ? 6.212   -3.603  23.719  1.00 15.85 ? 38  TYR A CD2 1 
ATOM   348  C CE1 . TYR A 1 38  ? 4.758   -1.911  25.366  1.00 11.94 ? 38  TYR A CE1 1 
ATOM   349  C CE2 . TYR A 1 38  ? 5.150   -2.859  23.200  1.00 17.26 ? 38  TYR A CE2 1 
ATOM   350  C CZ  . TYR A 1 38  ? 4.429   -2.028  24.030  1.00 14.94 ? 38  TYR A CZ  1 
ATOM   351  O OH  . TYR A 1 38  ? 3.379   -1.295  23.532  1.00 13.01 ? 38  TYR A OH  1 
ATOM   352  N N   . TYR A 1 39  ? 10.698  -4.475  27.024  1.00 11.78 ? 39  TYR A N   1 
ATOM   353  C CA  . TYR A 1 39  ? 11.701  -5.205  27.795  1.00 11.08 ? 39  TYR A CA  1 
ATOM   354  C C   . TYR A 1 39  ? 12.272  -4.343  28.909  1.00 15.70 ? 39  TYR A C   1 
ATOM   355  O O   . TYR A 1 39  ? 12.482  -4.823  30.028  1.00 14.07 ? 39  TYR A O   1 
ATOM   356  C CB  . TYR A 1 39  ? 12.832  -5.683  26.885  1.00 10.08 ? 39  TYR A CB  1 
ATOM   357  C CG  . TYR A 1 39  ? 14.017  -6.264  27.656  1.00 20.93 ? 39  TYR A CG  1 
ATOM   358  C CD1 . TYR A 1 39  ? 14.030  -7.597  28.042  1.00 17.30 ? 39  TYR A CD1 1 
ATOM   359  C CD2 . TYR A 1 39  ? 15.106  -5.468  28.005  1.00 16.38 ? 39  TYR A CD2 1 
ATOM   360  C CE1 . TYR A 1 39  ? 15.099  -8.122  28.745  1.00 22.39 ? 39  TYR A CE1 1 
ATOM   361  C CE2 . TYR A 1 39  ? 16.175  -5.984  28.704  1.00 20.57 ? 39  TYR A CE2 1 
ATOM   362  C CZ  . TYR A 1 39  ? 16.164  -7.311  29.073  1.00 20.73 ? 39  TYR A CZ  1 
ATOM   363  O OH  . TYR A 1 39  ? 17.224  -7.826  29.777  1.00 25.12 ? 39  TYR A OH  1 
ATOM   364  N N   . ASP A 1 40  ? 12.482  -3.056  28.639  1.00 14.26 ? 40  ASP A N   1 
ATOM   365  C CA  . ASP A 1 40  ? 13.265  -2.234  29.554  1.00 14.22 ? 40  ASP A CA  1 
ATOM   366  C C   . ASP A 1 40  ? 12.475  -1.782  30.775  1.00 16.25 ? 40  ASP A C   1 
ATOM   367  O O   . ASP A 1 40  ? 13.071  -1.558  31.831  1.00 14.39 ? 40  ASP A O   1 
ATOM   368  C CB  . ASP A 1 40  ? 13.830  -1.028  28.811  1.00 15.91 ? 40  ASP A CB  1 
ATOM   369  C CG  . ASP A 1 40  ? 15.164  -1.337  28.148  1.00 21.41 ? 40  ASP A CG  1 
ATOM   370  O OD1 . ASP A 1 40  ? 16.166  -1.440  28.889  1.00 16.02 ? 40  ASP A OD1 1 
ATOM   371  O OD2 . ASP A 1 40  ? 15.196  -1.520  26.910  1.00 17.41 ? 40  ASP A OD2 1 
ATOM   372  N N   . MET A 1 41  ? 11.146  -1.645  30.676  1.00 13.90 ? 41  MET A N   1 
ATOM   373  C CA  . MET A 1 41  ? 10.392  -1.235  31.860  1.00 11.68 ? 41  MET A CA  1 
ATOM   374  C C   . MET A 1 41  ? 10.435  -2.294  32.957  1.00 13.32 ? 41  MET A C   1 
ATOM   375  O O   . MET A 1 41  ? 10.731  -1.943  34.113  1.00 15.00 ? 41  MET A O   1 
ATOM   376  C CB  . MET A 1 41  ? 8.956   -0.860  31.467  1.00 9.64  ? 41  MET A CB  1 
ATOM   377  C CG  . MET A 1 41  ? 8.807   0.542   30.834  1.00 7.26  ? 41  MET A CG  1 
ATOM   378  S SD  . MET A 1 41  ? 9.110   1.877   32.043  1.00 13.41 ? 41  MET A SD  1 
ATOM   379  C CE  . MET A 1 41  ? 7.549   1.909   32.932  1.00 13.87 ? 41  MET A CE  1 
ATOM   380  N N   . PRO A 1 42  ? 10.162  -3.580  32.694  1.00 15.16 ? 42  PRO A N   1 
ATOM   381  C CA  . PRO A 1 42  ? 10.363  -4.588  33.752  1.00 15.28 ? 42  PRO A CA  1 
ATOM   382  C C   . PRO A 1 42  ? 11.831  -4.812  34.093  1.00 15.67 ? 42  PRO A C   1 
ATOM   383  O O   . PRO A 1 42  ? 12.135  -5.239  35.218  1.00 13.89 ? 42  PRO A O   1 
ATOM   384  C CB  . PRO A 1 42  ? 9.718   -5.854  33.174  1.00 13.51 ? 42  PRO A CB  1 
ATOM   385  C CG  . PRO A 1 42  ? 9.681   -5.635  31.686  1.00 12.61 ? 42  PRO A CG  1 
ATOM   386  C CD  . PRO A 1 42  ? 9.522   -4.156  31.490  1.00 11.77 ? 42  PRO A CD  1 
ATOM   387  N N   . ALA A 1 43  ? 12.750  -4.506  33.174  1.00 17.59 ? 43  ALA A N   1 
ATOM   388  C CA  . ALA A 1 43  ? 14.170  -4.708  33.450  1.00 20.29 ? 43  ALA A CA  1 
ATOM   389  C C   . ALA A 1 43  ? 14.700  -3.761  34.522  1.00 18.70 ? 43  ALA A C   1 
ATOM   390  O O   . ALA A 1 43  ? 15.761  -4.036  35.094  1.00 21.25 ? 43  ALA A O   1 
ATOM   391  C CB  . ALA A 1 43  ? 14.990  -4.563  32.162  1.00 18.71 ? 43  ALA A CB  1 
ATOM   392  N N   . TYR A 1 44  ? 13.997  -2.659  34.812  1.00 14.45 ? 44  TYR A N   1 
ATOM   393  C CA  . TYR A 1 44  ? 14.370  -1.832  35.963  1.00 13.73 ? 44  TYR A CA  1 
ATOM   394  C C   . TYR A 1 44  ? 14.453  -2.657  37.243  1.00 16.78 ? 44  TYR A C   1 
ATOM   395  O O   . TYR A 1 44  ? 15.221  -2.321  38.151  1.00 18.55 ? 44  TYR A O   1 
ATOM   396  C CB  . TYR A 1 44  ? 13.370  -0.687  36.167  1.00 16.45 ? 44  TYR A CB  1 
ATOM   397  C CG  . TYR A 1 44  ? 13.630  0.538   35.318  1.00 16.51 ? 44  TYR A CG  1 
ATOM   398  C CD1 . TYR A 1 44  ? 14.450  1.571   35.771  1.00 15.22 ? 44  TYR A CD1 1 
ATOM   399  C CD2 . TYR A 1 44  ? 13.052  0.664   34.056  1.00 19.22 ? 44  TYR A CD2 1 
ATOM   400  C CE1 . TYR A 1 44  ? 14.685  2.701   34.987  1.00 12.91 ? 44  TYR A CE1 1 
ATOM   401  C CE2 . TYR A 1 44  ? 13.271  1.792   33.268  1.00 18.48 ? 44  TYR A CE2 1 
ATOM   402  C CZ  . TYR A 1 44  ? 14.080  2.802   33.733  1.00 17.61 ? 44  TYR A CZ  1 
ATOM   403  O OH  . TYR A 1 44  ? 14.293  3.908   32.939  1.00 20.91 ? 44  TYR A OH  1 
ATOM   404  N N   . LEU A 1 45  ? 13.667  -3.732  37.339  1.00 17.12 ? 45  LEU A N   1 
ATOM   405  C CA  . LEU A 1 45  ? 13.647  -4.540  38.551  1.00 18.78 ? 45  LEU A CA  1 
ATOM   406  C C   . LEU A 1 45  ? 14.962  -5.273  38.781  1.00 22.80 ? 45  LEU A C   1 
ATOM   407  O O   . LEU A 1 45  ? 15.196  -5.764  39.891  1.00 20.68 ? 45  LEU A O   1 
ATOM   408  C CB  . LEU A 1 45  ? 12.484  -5.533  38.491  1.00 22.31 ? 45  LEU A CB  1 
ATOM   409  C CG  . LEU A 1 45  ? 11.100  -4.875  38.562  1.00 18.38 ? 45  LEU A CG  1 
ATOM   410  C CD1 . LEU A 1 45  ? 10.027  -5.875  38.202  1.00 18.56 ? 45  LEU A CD1 1 
ATOM   411  C CD2 . LEU A 1 45  ? 10.857  -4.294  39.956  1.00 16.65 ? 45  LEU A CD2 1 
ATOM   412  N N   . LYS A 1 46  ? 15.826  -5.342  37.767  1.00 20.77 ? 46  LYS A N   1 
ATOM   413  C CA  . LYS A 1 46  ? 17.164  -5.888  37.971  1.00 20.28 ? 46  LYS A CA  1 
ATOM   414  C C   . LYS A 1 46  ? 18.011  -4.994  38.863  1.00 23.17 ? 46  LYS A C   1 
ATOM   415  O O   . LYS A 1 46  ? 18.887  -5.491  39.580  1.00 32.17 ? 46  LYS A O   1 
ATOM   416  C CB  . LYS A 1 46  ? 17.867  -6.085  36.626  1.00 23.03 ? 46  LYS A CB  1 
ATOM   417  C CG  . LYS A 1 46  ? 17.450  -7.341  35.884  1.00 27.44 ? 46  LYS A CG  1 
ATOM   418  C CD  . LYS A 1 46  ? 17.361  -7.070  34.397  1.00 39.80 ? 46  LYS A CD  1 
ATOM   419  C CE  . LYS A 1 46  ? 18.531  -7.689  33.645  1.00 45.53 ? 46  LYS A CE  1 
ATOM   420  N NZ  . LYS A 1 46  ? 18.485  -7.369  32.175  1.00 43.87 ? 46  LYS A NZ  1 
ATOM   421  N N   . ASP A 1 47  ? 17.791  -3.684  38.822  1.00 24.90 ? 47  ASP A N   1 
ATOM   422  C CA  . ASP A 1 47  ? 18.633  -2.752  39.551  1.00 24.03 ? 47  ASP A CA  1 
ATOM   423  C C   . ASP A 1 47  ? 17.955  -2.131  40.756  1.00 27.13 ? 47  ASP A C   1 
ATOM   424  O O   . ASP A 1 47  ? 18.641  -1.510  41.578  1.00 25.72 ? 47  ASP A O   1 
ATOM   425  C CB  . ASP A 1 47  ? 19.112  -1.638  38.618  1.00 24.24 ? 47  ASP A CB  1 
ATOM   426  C CG  . ASP A 1 47  ? 19.895  -2.177  37.437  1.00 29.54 ? 47  ASP A CG  1 
ATOM   427  O OD1 . ASP A 1 47  ? 20.563  -3.220  37.586  1.00 25.67 ? 47  ASP A OD1 1 
ATOM   428  O OD2 . ASP A 1 47  ? 19.811  -1.577  36.351  1.00 33.90 ? 47  ASP A OD2 1 
ATOM   429  N N   . PHE A 1 48  ? 16.640  -2.272  40.884  1.00 22.23 ? 48  PHE A N   1 
ATOM   430  C CA  . PHE A 1 48  ? 15.910  -1.664  41.983  1.00 26.63 ? 48  PHE A CA  1 
ATOM   431  C C   . PHE A 1 48  ? 15.077  -2.718  42.693  1.00 25.41 ? 48  PHE A C   1 
ATOM   432  O O   . PHE A 1 48  ? 14.302  -3.442  42.060  1.00 19.05 ? 48  PHE A O   1 
ATOM   433  C CB  . PHE A 1 48  ? 15.036  -0.517  41.485  1.00 21.09 ? 48  PHE A CB  1 
ATOM   434  C CG  . PHE A 1 48  ? 15.811  0.583   40.845  1.00 24.12 ? 48  PHE A CG  1 
ATOM   435  C CD1 . PHE A 1 48  ? 16.327  1.612   41.608  1.00 29.78 ? 48  PHE A CD1 1 
ATOM   436  C CD2 . PHE A 1 48  ? 16.037  0.587   39.480  1.00 23.02 ? 48  PHE A CD2 1 
ATOM   437  C CE1 . PHE A 1 48  ? 17.052  2.633   41.016  1.00 29.21 ? 48  PHE A CE1 1 
ATOM   438  C CE2 . PHE A 1 48  ? 16.761  1.603   38.882  1.00 20.90 ? 48  PHE A CE2 1 
ATOM   439  C CZ  . PHE A 1 48  ? 17.272  2.622   39.645  1.00 27.54 ? 48  PHE A CZ  1 
ATOM   440  N N   . GLU A 1 49  ? 15.240  -2.795  44.013  1.00 18.92 ? 49  GLU A N   1 
ATOM   441  C CA  . GLU A 1 49  ? 14.569  -3.811  44.820  1.00 21.67 ? 49  GLU A CA  1 
ATOM   442  C C   . GLU A 1 49  ? 13.229  -3.255  45.293  1.00 18.36 ? 49  GLU A C   1 
ATOM   443  O O   . GLU A 1 49  ? 13.003  -2.977  46.474  1.00 20.48 ? 49  GLU A O   1 
ATOM   444  C CB  . GLU A 1 49  ? 15.451  -4.237  45.991  1.00 21.35 ? 49  GLU A CB  1 
ATOM   445  C CG  . GLU A 1 49  ? 16.395  -5.385  45.689  1.00 35.35 ? 49  GLU A CG  1 
ATOM   446  C CD  . GLU A 1 49  ? 16.596  -6.311  46.888  1.00 48.96 ? 49  GLU A CD  1 
ATOM   447  O OE1 . GLU A 1 49  ? 17.372  -7.280  46.768  1.00 53.31 ? 49  GLU A OE1 1 
ATOM   448  O OE2 . GLU A 1 49  ? 15.975  -6.081  47.947  1.00 54.45 ? 49  GLU A OE2 1 
ATOM   449  N N   . ILE A 1 50  ? 12.336  -3.080  44.322  1.00 18.09 ? 50  ILE A N   1 
ATOM   450  C CA  . ILE A 1 50  ? 10.969  -2.645  44.562  1.00 16.82 ? 50  ILE A CA  1 
ATOM   451  C C   . ILE A 1 50  ? 10.039  -3.595  43.813  1.00 13.77 ? 50  ILE A C   1 
ATOM   452  O O   . ILE A 1 50  ? 10.478  -4.479  43.078  1.00 19.75 ? 50  ILE A O   1 
ATOM   453  C CB  . ILE A 1 50  ? 10.730  -1.181  44.126  1.00 18.44 ? 50  ILE A CB  1 
ATOM   454  C CG1 . ILE A 1 50  ? 11.051  -0.987  42.633  1.00 18.20 ? 50  ILE A CG1 1 
ATOM   455  C CG2 . ILE A 1 50  ? 11.547  -0.225  44.982  1.00 26.62 ? 50  ILE A CG2 1 
ATOM   456  C CD1 . ILE A 1 50  ? 10.534  0.341   42.056  1.00 20.05 ? 50  ILE A CD1 1 
ATOM   457  N N   . LYS A 1 51  ? 8.744   -3.429  44.041  1.00 13.94 ? 51  LYS A N   1 
ATOM   458  C CA  . LYS A 1 51  ? 7.728   -4.169  43.313  1.00 13.27 ? 51  LYS A CA  1 
ATOM   459  C C   . LYS A 1 51  ? 7.152   -3.264  42.233  1.00 15.93 ? 51  LYS A C   1 
ATOM   460  O O   . LYS A 1 51  ? 6.934   -2.072  42.465  1.00 12.88 ? 51  LYS A O   1 
ATOM   461  C CB  . LYS A 1 51  ? 6.621   -4.669  44.248  1.00 13.40 ? 51  LYS A CB  1 
ATOM   462  C CG  . LYS A 1 51  ? 7.135   -5.512  45.442  1.00 13.41 ? 51  LYS A CG  1 
ATOM   463  C CD  . LYS A 1 51  ? 7.826   -6.802  44.980  1.00 17.48 ? 51  LYS A CD  1 
ATOM   464  C CE  . LYS A 1 51  ? 8.047   -7.763  46.157  1.00 22.19 ? 51  LYS A CE  1 
ATOM   465  N NZ  . LYS A 1 51  ? 8.863   -7.123  47.207  1.00 30.70 ? 51  LYS A NZ  1 
ATOM   466  N N   . LEU A 1 52  ? 6.962   -3.828  41.041  1.00 14.58 ? 52  LEU A N   1 
ATOM   467  C CA  . LEU A 1 52  ? 6.383   -3.123  39.898  1.00 15.65 ? 52  LEU A CA  1 
ATOM   468  C C   . LEU A 1 52  ? 5.522   -4.117  39.141  1.00 19.84 ? 52  LEU A C   1 
ATOM   469  O O   . LEU A 1 52  ? 5.971   -5.235  38.885  1.00 13.01 ? 52  LEU A O   1 
ATOM   470  C CB  . LEU A 1 52  ? 7.466   -2.563  38.963  1.00 12.84 ? 52  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 52  ? 8.374   -1.415  39.412  1.00 14.03 ? 52  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 52  ? 9.445   -1.103  38.341  1.00 10.87 ? 52  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 52  ? 7.550   -0.166  39.698  1.00 12.57 ? 52  LEU A CD2 1 
ATOM   474  N N   . ASN A 1 53  ? 4.302   -3.722  38.771  1.00 13.92 ? 53  ASN A N   1 
ATOM   475  C CA  . ASN A 1 53  ? 3.379   -4.640  38.117  1.00 10.90 ? 53  ASN A CA  1 
ATOM   476  C C   . ASN A 1 53  ? 3.088   -4.205  36.689  1.00 13.12 ? 53  ASN A C   1 
ATOM   477  O O   . ASN A 1 53  ? 3.219   -3.033  36.334  1.00 10.50 ? 53  ASN A O   1 
ATOM   478  C CB  . ASN A 1 53  ? 2.073   -4.740  38.902  1.00 12.52 ? 53  ASN A CB  1 
ATOM   479  C CG  . ASN A 1 53  ? 2.321   -4.972  40.372  1.00 15.06 ? 53  ASN A CG  1 
ATOM   480  O OD1 . ASN A 1 53  ? 2.626   -6.087  40.780  1.00 14.46 ? 53  ASN A OD1 1 
ATOM   481  N ND2 . ASN A 1 53  ? 2.236   -3.911  41.167  1.00 10.60 ? 53  ASN A ND2 1 
ATOM   482  N N   . PHE A 1 54  ? 2.670   -5.171  35.877  1.00 9.04  ? 54  PHE A N   1 
ATOM   483  C CA  . PHE A 1 54  ? 2.550   -4.956  34.441  1.00 14.04 ? 54  PHE A CA  1 
ATOM   484  C C   . PHE A 1 54  ? 1.301   -5.622  33.907  1.00 12.13 ? 54  PHE A C   1 
ATOM   485  O O   . PHE A 1 54  ? 0.947   -6.725  34.332  1.00 14.43 ? 54  PHE A O   1 
ATOM   486  C CB  . PHE A 1 54  ? 3.795   -5.499  33.702  1.00 9.64  ? 54  PHE A CB  1 
ATOM   487  C CG  . PHE A 1 54  ? 5.056   -4.801  34.105  1.00 15.60 ? 54  PHE A CG  1 
ATOM   488  C CD1 . PHE A 1 54  ? 5.802   -5.257  35.178  1.00 10.84 ? 54  PHE A CD1 1 
ATOM   489  C CD2 . PHE A 1 54  ? 5.467   -3.647  33.446  1.00 14.49 ? 54  PHE A CD2 1 
ATOM   490  C CE1 . PHE A 1 54  ? 6.951   -4.584  35.568  1.00 14.33 ? 54  PHE A CE1 1 
ATOM   491  C CE2 . PHE A 1 54  ? 6.610   -2.971  33.838  1.00 12.94 ? 54  PHE A CE2 1 
ATOM   492  C CZ  . PHE A 1 54  ? 7.343   -3.433  34.905  1.00 13.47 ? 54  PHE A CZ  1 
ATOM   493  N N   . ASN A 1 55  ? 0.647   -4.948  32.960  1.00 8.48  ? 55  ASN A N   1 
ATOM   494  C CA  . ASN A 1 55  ? -0.427  -5.524  32.169  1.00 8.25  ? 55  ASN A CA  1 
ATOM   495  C C   . ASN A 1 55  ? 0.049   -5.697  30.738  1.00 13.80 ? 55  ASN A C   1 
ATOM   496  O O   . ASN A 1 55  ? 0.603   -4.759  30.154  1.00 10.47 ? 55  ASN A O   1 
ATOM   497  C CB  . ASN A 1 55  ? -1.674  -4.636  32.167  1.00 11.06 ? 55  ASN A CB  1 
ATOM   498  C CG  . ASN A 1 55  ? -2.848  -5.315  31.515  1.00 12.41 ? 55  ASN A CG  1 
ATOM   499  O OD1 . ASN A 1 55  ? -3.341  -6.326  32.020  1.00 14.34 ? 55  ASN A OD1 1 
ATOM   500  N ND2 . ASN A 1 55  ? -3.306  -4.774  30.387  1.00 12.10 ? 55  ASN A ND2 1 
ATOM   501  N N   . LEU A 1 56  ? -0.193  -6.881  30.173  1.00 12.44 ? 56  LEU A N   1 
ATOM   502  C CA  . LEU A 1 56  ? 0.131   -7.179  28.781  1.00 17.48 ? 56  LEU A CA  1 
ATOM   503  C C   . LEU A 1 56  ? -1.148  -7.611  28.082  1.00 14.33 ? 56  LEU A C   1 
ATOM   504  O O   . LEU A 1 56  ? -1.757  -8.612  28.470  1.00 15.74 ? 56  LEU A O   1 
ATOM   505  C CB  . LEU A 1 56  ? 1.200   -8.280  28.680  1.00 15.17 ? 56  LEU A CB  1 
ATOM   506  C CG  . LEU A 1 56  ? 2.572   -7.988  29.304  1.00 15.63 ? 56  LEU A CG  1 
ATOM   507  C CD1 . LEU A 1 56  ? 3.461   -9.223  29.249  1.00 20.15 ? 56  LEU A CD1 1 
ATOM   508  C CD2 . LEU A 1 56  ? 3.247   -6.834  28.600  1.00 18.69 ? 56  LEU A CD2 1 
ATOM   509  N N   . THR A 1 57  ? -1.570  -6.854  27.052  1.00 14.03 ? 57  THR A N   1 
ATOM   510  C CA  . THR A 1 57  ? -2.746  -7.355  26.350  1.00 11.79 ? 57  THR A CA  1 
ATOM   511  C C   . THR A 1 57  ? -2.368  -8.527  25.438  1.00 12.06 ? 57  THR A C   1 
ATOM   512  O O   . THR A 1 57  ? -1.265  -8.566  24.885  1.00 14.34 ? 57  THR A O   1 
ATOM   513  C CB  . THR A 1 57  ? -3.410  -6.258  25.515  1.00 12.93 ? 57  THR A CB  1 
ATOM   514  O OG1 . THR A 1 57  ? -2.557  -5.879  24.424  1.00 11.84 ? 57  THR A OG1 1 
ATOM   515  C CG2 . THR A 1 57  ? -3.725  -5.026  26.402  1.00 13.39 ? 57  THR A CG2 1 
ATOM   516  N N   . PRO A 1 58  ? -3.273  -9.495  25.269  1.00 15.88 ? 58  PRO A N   1 
ATOM   517  C CA  . PRO A 1 58  ? -2.929  -10.668 24.445  1.00 15.67 ? 58  PRO A CA  1 
ATOM   518  C C   . PRO A 1 58  ? -2.594  -10.308 23.010  1.00 12.61 ? 58  PRO A C   1 
ATOM   519  O O   . PRO A 1 58  ? -1.717  -10.936 22.405  1.00 16.80 ? 58  PRO A O   1 
ATOM   520  C CB  . PRO A 1 58  ? -4.193  -11.537 24.526  1.00 11.95 ? 58  PRO A CB  1 
ATOM   521  C CG  . PRO A 1 58  ? -4.911  -11.085 25.769  1.00 15.23 ? 58  PRO A CG  1 
ATOM   522  C CD  . PRO A 1 58  ? -4.618  -9.600  25.864  1.00 16.09 ? 58  PRO A CD  1 
ATOM   523  N N   . VAL A 1 59  ? -3.266  -9.299  22.448  1.00 13.59 ? 59  VAL A N   1 
ATOM   524  C CA  . VAL A 1 59  ? -2.957  -8.904  21.076  1.00 15.16 ? 59  VAL A CA  1 
ATOM   525  C C   . VAL A 1 59  ? -1.549  -8.317  20.992  1.00 18.21 ? 59  VAL A C   1 
ATOM   526  O O   . VAL A 1 59  ? -0.870  -8.472  19.971  1.00 16.77 ? 59  VAL A O   1 
ATOM   527  C CB  . VAL A 1 59  ? -4.019  -7.928  20.520  1.00 13.31 ? 59  VAL A CB  1 
ATOM   528  C CG1 . VAL A 1 59  ? -4.045  -6.634  21.309  1.00 15.28 ? 59  VAL A CG1 1 
ATOM   529  C CG2 . VAL A 1 59  ? -3.756  -7.660  19.036  1.00 14.27 ? 59  VAL A CG2 1 
ATOM   530  N N   . LEU A 1 60  ? -1.081  -7.642  22.047  1.00 15.22 ? 60  LEU A N   1 
ATOM   531  C CA  . LEU A 1 60  ? 0.319   -7.228  22.081  1.00 11.47 ? 60  LEU A CA  1 
ATOM   532  C C   . LEU A 1 60  ? 1.237   -8.441  22.140  1.00 13.01 ? 60  LEU A C   1 
ATOM   533  O O   . LEU A 1 60  ? 2.214   -8.529  21.389  1.00 17.12 ? 60  LEU A O   1 
ATOM   534  C CB  . LEU A 1 60  ? 0.583   -6.309  23.275  1.00 16.30 ? 60  LEU A CB  1 
ATOM   535  C CG  . LEU A 1 60  ? 2.049   -5.927  23.471  1.00 12.06 ? 60  LEU A CG  1 
ATOM   536  C CD1 . LEU A 1 60  ? 2.619   -5.245  22.205  1.00 10.05 ? 60  LEU A CD1 1 
ATOM   537  C CD2 . LEU A 1 60  ? 2.217   -5.027  24.707  1.00 11.78 ? 60  LEU A CD2 1 
ATOM   538  N N   . ILE A 1 61  ? 0.938   -9.385  23.035  1.00 15.81 ? 61  ILE A N   1 
ATOM   539  C CA  . ILE A 1 61  ? 1.757   -10.592 23.148  1.00 15.69 ? 61  ILE A CA  1 
ATOM   540  C C   . ILE A 1 61  ? 1.895   -11.266 21.788  1.00 15.18 ? 61  ILE A C   1 
ATOM   541  O O   . ILE A 1 61  ? 3.000   -11.633 21.375  1.00 15.70 ? 61  ILE A O   1 
ATOM   542  C CB  . ILE A 1 61  ? 1.163   -11.549 24.196  1.00 18.35 ? 61  ILE A CB  1 
ATOM   543  C CG1 . ILE A 1 61  ? 1.247   -10.919 25.591  1.00 15.16 ? 61  ILE A CG1 1 
ATOM   544  C CG2 . ILE A 1 61  ? 1.909   -12.885 24.186  1.00 20.42 ? 61  ILE A CG2 1 
ATOM   545  C CD1 . ILE A 1 61  ? 0.397   -11.608 26.615  1.00 15.98 ? 61  ILE A CD1 1 
ATOM   546  N N   . ASP A 1 62  ? 0.777   -11.407 21.062  1.00 19.21 ? 62  ASP A N   1 
ATOM   547  C CA  . ASP A 1 62  ? 0.805   -12.045 19.742  1.00 22.50 ? 62  ASP A CA  1 
ATOM   548  C C   . ASP A 1 62  ? 1.812   -11.376 18.819  1.00 16.35 ? 62  ASP A C   1 
ATOM   549  O O   . ASP A 1 62  ? 2.571   -12.052 18.117  1.00 16.75 ? 62  ASP A O   1 
ATOM   550  C CB  . ASP A 1 62  ? -0.585  -12.013 19.091  1.00 16.86 ? 62  ASP A CB  1 
ATOM   551  C CG  . ASP A 1 62  ? -1.528  -13.058 19.655  1.00 19.82 ? 62  ASP A CG  1 
ATOM   552  O OD1 . ASP A 1 62  ? -1.058  -14.010 20.306  1.00 26.08 ? 62  ASP A OD1 1 
ATOM   553  O OD2 . ASP A 1 62  ? -2.751  -12.920 19.448  1.00 21.80 ? 62  ASP A OD2 1 
ATOM   554  N N   . GLN A 1 63  ? 1.841   -10.041 18.813  1.00 16.35 ? 63  GLN A N   1 
ATOM   555  C CA  . GLN A 1 63  ? 2.744   -9.331  17.915  1.00 11.81 ? 63  GLN A CA  1 
ATOM   556  C C   . GLN A 1 63  ? 4.191   -9.440  18.375  1.00 17.01 ? 63  GLN A C   1 
ATOM   557  O O   . GLN A 1 63  ? 5.105   -9.579  17.550  1.00 14.10 ? 63  GLN A O   1 
ATOM   558  C CB  . GLN A 1 63  ? 2.330   -7.865  17.816  1.00 13.31 ? 63  GLN A CB  1 
ATOM   559  C CG  . GLN A 1 63  ? 0.953   -7.683  17.254  1.00 13.90 ? 63  GLN A CG  1 
ATOM   560  C CD  . GLN A 1 63  ? 0.516   -6.245  17.343  1.00 20.22 ? 63  GLN A CD  1 
ATOM   561  O OE1 . GLN A 1 63  ? 1.020   -5.384  16.614  1.00 17.78 ? 63  GLN A OE1 1 
ATOM   562  N NE2 . GLN A 1 63  ? -0.396  -5.964  18.266  1.00 13.55 ? 63  GLN A NE2 1 
ATOM   563  N N   . ILE A 1 64  ? 4.428   -9.345  19.683  1.00 15.57 ? 64  ILE A N   1 
ATOM   564  C CA  . ILE A 1 64  ? 5.787   -9.518  20.188  1.00 16.75 ? 64  ILE A CA  1 
ATOM   565  C C   . ILE A 1 64  ? 6.346   -10.867 19.745  1.00 16.11 ? 64  ILE A C   1 
ATOM   566  O O   . ILE A 1 64  ? 7.500   -10.963 19.307  1.00 15.91 ? 64  ILE A O   1 
ATOM   567  C CB  . ILE A 1 64  ? 5.810   -9.358  21.719  1.00 15.20 ? 64  ILE A CB  1 
ATOM   568  C CG1 . ILE A 1 64  ? 5.515   -7.894  22.107  1.00 13.49 ? 64  ILE A CG1 1 
ATOM   569  C CG2 . ILE A 1 64  ? 7.150   -9.830  22.265  1.00 20.17 ? 64  ILE A CG2 1 
ATOM   570  C CD1 . ILE A 1 64  ? 5.404   -7.664  23.604  1.00 13.19 ? 64  ILE A CD1 1 
ATOM   571  N N   . GLN A 1 65  ? 5.528   -11.923 19.823  1.00 16.87 ? 65  GLN A N   1 
ATOM   572  C CA  . GLN A 1 65  ? 5.992   -13.256 19.435  1.00 17.51 ? 65  GLN A CA  1 
ATOM   573  C C   . GLN A 1 65  ? 6.341   -13.311 17.956  1.00 20.44 ? 65  GLN A C   1 
ATOM   574  O O   . GLN A 1 65  ? 7.317   -13.957 17.569  1.00 19.59 ? 65  GLN A O   1 
ATOM   575  C CB  . GLN A 1 65  ? 4.932   -14.309 19.765  1.00 19.63 ? 65  GLN A CB  1 
ATOM   576  C CG  . GLN A 1 65  ? 4.700   -14.508 21.262  1.00 23.68 ? 65  GLN A CG  1 
ATOM   577  C CD  . GLN A 1 65  ? 3.582   -15.493 21.569  1.00 24.49 ? 65  GLN A CD  1 
ATOM   578  O OE1 . GLN A 1 65  ? 2.428   -15.288 21.187  1.00 32.98 ? 65  GLN A OE1 1 
ATOM   579  N NE2 . GLN A 1 65  ? 3.923   -16.569 22.272  1.00 35.11 ? 65  GLN A NE2 1 
ATOM   580  N N   . GLU A 1 66  ? 5.562   -12.633 17.115  1.00 22.90 ? 66  GLU A N   1 
ATOM   581  C CA  . GLU A 1 66  ? 5.834   -12.678 15.682  1.00 25.32 ? 66  GLU A CA  1 
ATOM   582  C C   . GLU A 1 66  ? 7.116   -11.935 15.330  1.00 21.66 ? 66  GLU A C   1 
ATOM   583  O O   . GLU A 1 66  ? 7.862   -12.375 14.452  1.00 18.04 ? 66  GLU A O   1 
ATOM   584  C CB  . GLU A 1 66  ? 4.654   -12.113 14.901  1.00 19.22 ? 66  GLU A CB  1 
ATOM   585  C CG  . GLU A 1 66  ? 3.516   -13.096 14.746  1.00 29.22 ? 66  GLU A CG  1 
ATOM   586  C CD  . GLU A 1 66  ? 2.281   -12.457 14.148  1.00 42.77 ? 66  GLU A CD  1 
ATOM   587  O OE1 . GLU A 1 66  ? 1.162   -12.779 14.609  1.00 52.49 ? 66  GLU A OE1 1 
ATOM   588  O OE2 . GLU A 1 66  ? 2.435   -11.622 13.227  1.00 30.72 ? 66  GLU A OE2 1 
ATOM   589  N N   . TYR A 1 67  ? 7.379   -10.798 15.980  1.00 16.57 ? 67  TYR A N   1 
ATOM   590  C CA  . TYR A 1 67  ? 8.658   -10.116 15.788  1.00 17.54 ? 67  TYR A CA  1 
ATOM   591  C C   . TYR A 1 67  ? 9.814   -10.972 16.295  1.00 20.97 ? 67  TYR A C   1 
ATOM   592  O O   . TYR A 1 67  ? 10.831  -11.129 15.609  1.00 27.00 ? 67  TYR A O   1 
ATOM   593  C CB  . TYR A 1 67  ? 8.660   -8.763  16.499  1.00 20.57 ? 67  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 67  ? 8.009   -7.649  15.713  1.00 15.01 ? 67  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 67  ? 8.704   -6.982  14.711  1.00 15.74 ? 67  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 67  ? 6.696   -7.264  15.973  1.00 18.10 ? 67  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 67  ? 8.115   -5.961  13.993  1.00 20.79 ? 67  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 67  ? 6.087   -6.246  15.250  1.00 19.90 ? 67  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 67  ? 6.805   -5.597  14.264  1.00 19.29 ? 67  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 67  ? 6.225   -4.582  13.552  1.00 17.45 ? 67  TYR A OH  1 
ATOM   601  N N   . ALA A 1 68  ? 9.675   -11.530 17.504  1.00 20.49 ? 68  ALA A N   1 
ATOM   602  C CA  . ALA A 1 68  ? 10.737  -12.356 18.075  1.00 18.90 ? 68  ALA A CA  1 
ATOM   603  C C   . ALA A 1 68  ? 11.083  -13.537 17.177  1.00 22.79 ? 68  ALA A C   1 
ATOM   604  O O   . ALA A 1 68  ? 12.252  -13.923 17.081  1.00 27.11 ? 68  ALA A O   1 
ATOM   605  C CB  . ALA A 1 68  ? 10.330  -12.858 19.462  1.00 22.39 ? 68  ALA A CB  1 
ATOM   606  N N   . GLN A 1 69  ? 10.094  -14.110 16.508  1.00 22.04 ? 69  GLN A N   1 
ATOM   607  C CA  . GLN A 1 69  ? 10.323  -15.220 15.593  1.00 30.95 ? 69  GLN A CA  1 
ATOM   608  C C   . GLN A 1 69  ? 10.734  -14.772 14.199  1.00 32.57 ? 69  GLN A C   1 
ATOM   609  O O   . GLN A 1 69  ? 10.842  -15.613 13.303  1.00 40.91 ? 69  GLN A O   1 
ATOM   610  C CB  . GLN A 1 69  ? 9.071   -16.090 15.511  1.00 27.40 ? 69  GLN A CB  1 
ATOM   611  C CG  . GLN A 1 69  ? 8.767   -16.758 16.826  1.00 36.53 ? 69  GLN A CG  1 
ATOM   612  C CD  . GLN A 1 69  ? 7.469   -17.515 16.809  1.00 41.77 ? 69  GLN A CD  1 
ATOM   613  O OE1 . GLN A 1 69  ? 6.652   -17.347 15.908  1.00 47.29 ? 69  GLN A OE1 1 
ATOM   614  N NE2 . GLN A 1 69  ? 7.262   -18.348 17.818  1.00 48.01 ? 69  GLN A NE2 1 
ATOM   615  N N   . GLY A 1 70  ? 10.970  -13.478 13.995  1.00 31.45 ? 70  GLY A N   1 
ATOM   616  C CA  . GLY A 1 70  ? 11.402  -12.995 12.699  1.00 27.75 ? 70  GLY A CA  1 
ATOM   617  C C   . GLY A 1 70  ? 10.387  -13.146 11.590  1.00 32.38 ? 70  GLY A C   1 
ATOM   618  O O   . GLY A 1 70  ? 10.760  -13.084 10.417  1.00 31.82 ? 70  GLY A O   1 
ATOM   619  N N   . LYS A 1 71  ? 9.106   -13.337 11.923  1.00 32.95 ? 71  LYS A N   1 
ATOM   620  C CA  . LYS A 1 71  ? 8.056   -13.495 10.924  1.00 28.71 ? 71  LYS A CA  1 
ATOM   621  C C   . LYS A 1 71  ? 7.313   -12.201 10.597  1.00 34.46 ? 71  LYS A C   1 
ATOM   622  O O   . LYS A 1 71  ? 6.575   -12.168 9.608   1.00 37.97 ? 71  LYS A O   1 
ATOM   623  C CB  . LYS A 1 71  ? 7.028   -14.538 11.383  1.00 33.50 ? 71  LYS A CB  1 
ATOM   624  C CG  . LYS A 1 71  ? 7.600   -15.881 11.814  1.00 41.26 ? 71  LYS A CG  1 
ATOM   625  C CD  . LYS A 1 71  ? 6.467   -16.848 12.151  1.00 50.71 ? 71  LYS A CD  1 
ATOM   626  C CE  . LYS A 1 71  ? 6.998   -18.193 12.632  1.00 57.02 ? 71  LYS A CE  1 
ATOM   627  N NZ  . LYS A 1 71  ? 5.907   -19.204 12.741  1.00 60.14 ? 71  LYS A NZ  1 
ATOM   628  N N   . ALA A 1 72  ? 7.457   -11.151 11.401  1.00 28.07 ? 72  ALA A N   1 
ATOM   629  C CA  . ALA A 1 72  ? 6.670   -9.940  11.191  1.00 27.35 ? 72  ALA A CA  1 
ATOM   630  C C   . ALA A 1 72  ? 7.210   -9.166  9.993   1.00 28.41 ? 72  ALA A C   1 
ATOM   631  O O   . ALA A 1 72  ? 8.363   -8.719  9.999   1.00 38.14 ? 72  ALA A O   1 
ATOM   632  C CB  . ALA A 1 72  ? 6.689   -9.071  12.450  1.00 25.00 ? 72  ALA A CB  1 
ATOM   633  N N   . LYS A 1 73  ? 6.384   -9.006  8.962   1.00 22.60 ? 73  LYS A N   1 
ATOM   634  C CA  . LYS A 1 73  ? 6.749   -8.191  7.803   1.00 26.83 ? 73  LYS A CA  1 
ATOM   635  C C   . LYS A 1 73  ? 6.326   -6.754  8.085   1.00 25.18 ? 73  LYS A C   1 
ATOM   636  O O   . LYS A 1 73  ? 5.169   -6.380  7.882   1.00 31.23 ? 73  LYS A O   1 
ATOM   637  C CB  . LYS A 1 73  ? 6.104   -8.724  6.529   1.00 25.90 ? 73  LYS A CB  1 
ATOM   638  C CG  . LYS A 1 73  ? 6.758   -8.169  5.265   1.00 35.63 ? 73  LYS A CG  1 
ATOM   639  C CD  . LYS A 1 73  ? 6.113   -8.695  3.989   1.00 39.68 ? 73  LYS A CD  1 
ATOM   640  C CE  . LYS A 1 73  ? 6.437   -7.781  2.811   1.00 44.87 ? 73  LYS A CE  1 
ATOM   641  N NZ  . LYS A 1 73  ? 6.730   -8.528  1.560   1.00 45.74 ? 73  LYS A NZ  1 
ATOM   642  N N   . ASP A 1 74  ? 7.274   -5.946  8.548   1.00 20.53 ? 74  ASP A N   1 
ATOM   643  C CA  . ASP A 1 74  ? 7.019   -4.580  8.996   1.00 18.53 ? 74  ASP A CA  1 
ATOM   644  C C   . ASP A 1 74  ? 7.460   -3.647  7.872   1.00 20.43 ? 74  ASP A C   1 
ATOM   645  O O   . ASP A 1 74  ? 8.653   -3.558  7.566   1.00 20.61 ? 74  ASP A O   1 
ATOM   646  C CB  . ASP A 1 74  ? 7.771   -4.308  10.299  1.00 18.47 ? 74  ASP A CB  1 
ATOM   647  C CG  . ASP A 1 74  ? 7.527   -2.905  10.851  1.00 19.22 ? 74  ASP A CG  1 
ATOM   648  O OD1 . ASP A 1 74  ? 7.536   -1.924  10.074  1.00 20.54 ? 74  ASP A OD1 1 
ATOM   649  O OD2 . ASP A 1 74  ? 7.350   -2.789  12.085  1.00 23.10 ? 74  ASP A OD2 1 
ATOM   650  N N   . VAL A 1 75  ? 6.499   -2.944  7.265   1.00 22.04 ? 75  VAL A N   1 
ATOM   651  C CA  . VAL A 1 75  ? 6.797   -2.212  6.037   1.00 26.18 ? 75  VAL A CA  1 
ATOM   652  C C   . VAL A 1 75  ? 7.737   -1.048  6.320   1.00 21.42 ? 75  VAL A C   1 
ATOM   653  O O   . VAL A 1 75  ? 8.676   -0.792  5.548   1.00 22.19 ? 75  VAL A O   1 
ATOM   654  C CB  . VAL A 1 75  ? 5.497   -1.759  5.334   1.00 34.63 ? 75  VAL A CB  1 
ATOM   655  C CG1 . VAL A 1 75  ? 4.655   -2.970  4.952   1.00 34.65 ? 75  VAL A CG1 1 
ATOM   656  C CG2 . VAL A 1 75  ? 4.687   -0.796  6.180   1.00 34.01 ? 75  VAL A CG2 1 
ATOM   657  N N   . PHE A 1 76  ? 7.517   -0.335  7.430   1.00 20.52 ? 76  PHE A N   1 
ATOM   658  C CA  . PHE A 1 76  ? 8.417   0.758   7.779   1.00 26.15 ? 76  PHE A CA  1 
ATOM   659  C C   . PHE A 1 76  ? 9.808   0.246   8.116   1.00 24.91 ? 76  PHE A C   1 
ATOM   660  O O   . PHE A 1 76  ? 10.815  0.823   7.677   1.00 24.18 ? 76  PHE A O   1 
ATOM   661  C CB  . PHE A 1 76  ? 7.892   1.569   8.960   1.00 22.99 ? 76  PHE A CB  1 
ATOM   662  C CG  . PHE A 1 76  ? 8.673   2.814   9.184   1.00 30.40 ? 76  PHE A CG  1 
ATOM   663  C CD1 . PHE A 1 76  ? 8.454   3.915   8.373   1.00 38.89 ? 76  PHE A CD1 1 
ATOM   664  C CD2 . PHE A 1 76  ? 9.665   2.877   10.150  1.00 29.53 ? 76  PHE A CD2 1 
ATOM   665  C CE1 . PHE A 1 76  ? 9.192   5.074   8.537   1.00 41.43 ? 76  PHE A CE1 1 
ATOM   666  C CE2 . PHE A 1 76  ? 10.404  4.034   10.321  1.00 37.29 ? 76  PHE A CE2 1 
ATOM   667  C CZ  . PHE A 1 76  ? 10.174  5.129   9.517   1.00 40.34 ? 76  PHE A CZ  1 
ATOM   668  N N   . LEU A 1 77  ? 9.887   -0.800  8.941   1.00 20.98 ? 77  LEU A N   1 
ATOM   669  C CA  . LEU A 1 77  ? 11.187  -1.368  9.271   1.00 23.63 ? 77  LEU A CA  1 
ATOM   670  C C   . LEU A 1 77  ? 11.938  -1.813  8.021   1.00 24.91 ? 77  LEU A C   1 
ATOM   671  O O   . LEU A 1 77  ? 13.170  -1.787  8.003   1.00 29.47 ? 77  LEU A O   1 
ATOM   672  C CB  . LEU A 1 77  ? 11.023  -2.539  10.230  1.00 29.02 ? 77  LEU A CB  1 
ATOM   673  C CG  . LEU A 1 77  ? 12.289  -3.037  10.930  1.00 29.72 ? 77  LEU A CG  1 
ATOM   674  C CD1 . LEU A 1 77  ? 13.169  -1.874  11.383  1.00 27.75 ? 77  LEU A CD1 1 
ATOM   675  C CD2 . LEU A 1 77  ? 11.872  -3.896  12.100  1.00 24.25 ? 77  LEU A CD2 1 
ATOM   676  N N   . GLU A 1 78  ? 11.221  -2.243  6.982   1.00 26.30 ? 78  GLU A N   1 
ATOM   677  C CA  . GLU A 1 78  ? 11.885  -2.570  5.725   1.00 26.52 ? 78  GLU A CA  1 
ATOM   678  C C   . GLU A 1 78  ? 12.523  -1.339  5.102   1.00 27.05 ? 78  GLU A C   1 
ATOM   679  O O   . GLU A 1 78  ? 13.635  -1.414  4.569   1.00 33.32 ? 78  GLU A O   1 
ATOM   680  C CB  . GLU A 1 78  ? 10.898  -3.195  4.754   1.00 33.60 ? 78  GLU A CB  1 
ATOM   681  C CG  . GLU A 1 78  ? 11.594  -3.826  3.563   1.00 49.06 ? 78  GLU A CG  1 
ATOM   682  C CD  . GLU A 1 78  ? 12.702  -4.785  3.987   1.00 59.26 ? 78  GLU A CD  1 
ATOM   683  O OE1 . GLU A 1 78  ? 12.490  -5.521  4.978   1.00 62.46 ? 78  GLU A OE1 1 
ATOM   684  O OE2 . GLU A 1 78  ? 13.761  -4.832  3.320   1.00 60.24 ? 78  GLU A OE2 1 
ATOM   685  N N   . ALA A 1 79  ? 11.839  -0.191  5.180   1.00 24.74 ? 79  ALA A N   1 
ATOM   686  C CA  . ALA A 1 79  ? 12.412  1.058   4.690   1.00 26.39 ? 79  ALA A CA  1 
ATOM   687  C C   . ALA A 1 79  ? 13.670  1.446   5.459   1.00 25.76 ? 79  ALA A C   1 
ATOM   688  O O   . ALA A 1 79  ? 14.546  2.125   4.915   1.00 25.79 ? 79  ALA A O   1 
ATOM   689  C CB  . ALA A 1 79  ? 11.380  2.184   4.776   1.00 19.62 ? 79  ALA A CB  1 
ATOM   690  N N   . ILE A 1 80  ? 13.769  1.048   6.727   1.00 18.59 ? 80  ILE A N   1 
ATOM   691  C CA  . ILE A 1 80  ? 14.961  1.366   7.503   1.00 18.56 ? 80  ILE A CA  1 
ATOM   692  C C   . ILE A 1 80  ? 16.085  0.400   7.168   1.00 23.85 ? 80  ILE A C   1 
ATOM   693  O O   . ILE A 1 80  ? 17.256  0.785   7.086   1.00 23.39 ? 80  ILE A O   1 
ATOM   694  C CB  . ILE A 1 80  ? 14.625  1.330   9.004   1.00 23.42 ? 80  ILE A CB  1 
ATOM   695  C CG1 . ILE A 1 80  ? 13.686  2.477   9.371   1.00 32.00 ? 80  ILE A CG1 1 
ATOM   696  C CG2 . ILE A 1 80  ? 15.910  1.358   9.839   1.00 24.74 ? 80  ILE A CG2 1 
ATOM   697  C CD1 . ILE A 1 80  ? 14.375  3.791   9.509   1.00 31.33 ? 80  ILE A CD1 1 
ATOM   698  N N   . ARG A 1 81  ? 15.742  -0.869  6.969   1.00 20.17 ? 81  ARG A N   1 
ATOM   699  C CA  . ARG A 1 81  ? 16.755  -1.901  6.796   1.00 23.96 ? 81  ARG A CA  1 
ATOM   700  C C   . ARG A 1 81  ? 17.476  -1.770  5.458   1.00 29.12 ? 81  ARG A C   1 
ATOM   701  O O   . ARG A 1 81  ? 18.689  -2.000  5.382   1.00 32.22 ? 81  ARG A O   1 
ATOM   702  C CB  . ARG A 1 81  ? 16.108  -3.278  6.928   1.00 24.13 ? 81  ARG A CB  1 
ATOM   703  C CG  . ARG A 1 81  ? 17.087  -4.448  6.850   1.00 35.62 ? 81  ARG A CG  1 
ATOM   704  C CD  . ARG A 1 81  ? 16.344  -5.772  6.798   1.00 44.87 ? 81  ARG A CD  1 
ATOM   705  N NE  . ARG A 1 81  ? 15.697  -6.079  8.071   1.00 52.69 ? 81  ARG A NE  1 
ATOM   706  C CZ  . ARG A 1 81  ? 16.308  -6.667  9.097   1.00 60.81 ? 81  ARG A CZ  1 
ATOM   707  N NH1 . ARG A 1 81  ? 17.584  -7.013  8.997   1.00 59.38 ? 81  ARG A NH1 1 
ATOM   708  N NH2 . ARG A 1 81  ? 15.649  -6.910  10.226  1.00 61.87 ? 81  ARG A NH2 1 
ATOM   709  N N   . LYS A 1 82  ? 16.754  -1.393  4.399   1.00 24.93 ? 82  LYS A N   1 
ATOM   710  C CA  . LYS A 1 82  ? 17.311  -1.425  3.049   1.00 27.09 ? 82  LYS A CA  1 
ATOM   711  C C   . LYS A 1 82  ? 18.489  -0.471  2.894   1.00 29.33 ? 82  LYS A C   1 
ATOM   712  O O   . LYS A 1 82  ? 18.505  0.629   3.454   1.00 22.46 ? 82  LYS A O   1 
ATOM   713  C CB  . LYS A 1 82  ? 16.251  -1.032  2.023   1.00 23.77 ? 82  LYS A CB  1 
ATOM   714  C CG  . LYS A 1 82  ? 15.339  -2.122  1.563   1.00 33.61 ? 82  LYS A CG  1 
ATOM   715  C CD  . LYS A 1 82  ? 14.395  -1.542  0.527   1.00 33.34 ? 82  LYS A CD  1 
ATOM   716  C CE  . LYS A 1 82  ? 13.199  -2.431  0.310   1.00 34.47 ? 82  LYS A CE  1 
ATOM   717  N NZ  . LYS A 1 82  ? 12.199  -1.762  -0.576  1.00 34.72 ? 82  LYS A NZ  1 
ATOM   718  N N   . ASP A 1 83  ? 19.462  -0.888  2.082   1.00 34.35 ? 83  ASP A N   1 
ATOM   719  C CA  . ASP A 1 83  ? 20.444  0.050   1.559   1.00 27.47 ? 83  ASP A CA  1 
ATOM   720  C C   . ASP A 1 83  ? 19.711  1.200   0.872   1.00 26.39 ? 83  ASP A C   1 
ATOM   721  O O   . ASP A 1 83  ? 18.763  0.963   0.109   1.00 22.94 ? 83  ASP A O   1 
ATOM   722  C CB  . ASP A 1 83  ? 21.385  -0.653  0.568   1.00 27.40 ? 83  ASP A CB  1 
ATOM   723  C CG  . ASP A 1 83  ? 22.624  0.176   0.221   1.00 30.97 ? 83  ASP A CG  1 
ATOM   724  O OD1 . ASP A 1 83  ? 22.502  1.258   -0.405  1.00 26.39 ? 83  ASP A OD1 1 
ATOM   725  O OD2 . ASP A 1 83  ? 23.737  -0.268  0.574   1.00 31.66 ? 83  ASP A OD2 1 
ATOM   726  N N   . PRO A 1 84  ? 20.107  2.451   1.125   1.00 23.07 ? 84  PRO A N   1 
ATOM   727  C CA  . PRO A 1 84  ? 19.413  3.592   0.500   1.00 18.99 ? 84  PRO A CA  1 
ATOM   728  C C   . PRO A 1 84  ? 19.331  3.521   -1.012  1.00 24.69 ? 84  PRO A C   1 
ATOM   729  O O   . PRO A 1 84  ? 18.378  4.067   -1.598  1.00 19.86 ? 84  PRO A O   1 
ATOM   730  C CB  . PRO A 1 84  ? 20.252  4.793   0.953   1.00 24.12 ? 84  PRO A CB  1 
ATOM   731  C CG  . PRO A 1 84  ? 20.844  4.353   2.257   1.00 19.19 ? 84  PRO A CG  1 
ATOM   732  C CD  . PRO A 1 84  ? 21.109  2.883   2.114   1.00 29.72 ? 84  PRO A CD  1 
ATOM   733  N N   . ASP A 1 85  ? 20.311  2.872   -1.663  1.00 25.09 ? 85  ASP A N   1 
ATOM   734  C CA  . ASP A 1 85  ? 20.261  2.657   -3.104  1.00 27.39 ? 85  ASP A CA  1 
ATOM   735  C C   . ASP A 1 85  ? 19.043  1.855   -3.531  1.00 21.85 ? 85  ASP A C   1 
ATOM   736  O O   . ASP A 1 85  ? 18.621  1.952   -4.690  1.00 25.55 ? 85  ASP A O   1 
ATOM   737  C CB  . ASP A 1 85  ? 21.516  1.928   -3.595  1.00 30.23 ? 85  ASP A CB  1 
ATOM   738  C CG  . ASP A 1 85  ? 22.739  2.812   -3.587  1.00 32.68 ? 85  ASP A CG  1 
ATOM   739  O OD1 . ASP A 1 85  ? 22.580  4.041   -3.404  1.00 33.29 ? 85  ASP A OD1 1 
ATOM   740  O OD2 . ASP A 1 85  ? 23.854  2.283   -3.762  1.00 38.21 ? 85  ASP A OD2 1 
ATOM   741  N N   . ASP A 1 86  ? 18.472  1.057   -2.639  1.00 18.99 ? 86  ASP A N   1 
ATOM   742  C CA  . ASP A 1 86  ? 17.310  0.261   -2.993  1.00 31.37 ? 86  ASP A CA  1 
ATOM   743  C C   . ASP A 1 86  ? 16.002  0.839   -2.469  1.00 29.73 ? 86  ASP A C   1 
ATOM   744  O O   . ASP A 1 86  ? 14.961  0.194   -2.614  1.00 27.33 ? 86  ASP A O   1 
ATOM   745  C CB  . ASP A 1 86  ? 17.503  -1.169  -2.504  1.00 33.71 ? 86  ASP A CB  1 
ATOM   746  C CG  . ASP A 1 86  ? 18.635  -1.871  -3.231  1.00 38.77 ? 86  ASP A CG  1 
ATOM   747  O OD1 . ASP A 1 86  ? 18.719  -1.722  -4.471  1.00 47.31 ? 86  ASP A OD1 1 
ATOM   748  O OD2 . ASP A 1 86  ? 19.433  -2.562  -2.575  1.00 41.55 ? 86  ASP A OD2 1 
ATOM   749  N N   . LEU A 1 87  ? 16.020  2.053   -1.906  1.00 21.51 ? 87  LEU A N   1 
ATOM   750  C CA  . LEU A 1 87  ? 14.794  2.649   -1.379  1.00 18.93 ? 87  LEU A CA  1 
ATOM   751  C C   . LEU A 1 87  ? 13.859  3.106   -2.496  1.00 25.09 ? 87  LEU A C   1 
ATOM   752  O O   . LEU A 1 87  ? 14.273  3.821   -3.416  1.00 20.63 ? 87  LEU A O   1 
ATOM   753  C CB  . LEU A 1 87  ? 15.124  3.840   -0.472  1.00 18.89 ? 87  LEU A CB  1 
ATOM   754  C CG  . LEU A 1 87  ? 15.643  3.503   0.937   1.00 22.78 ? 87  LEU A CG  1 
ATOM   755  C CD1 . LEU A 1 87  ? 16.149  4.752   1.654   1.00 18.83 ? 87  LEU A CD1 1 
ATOM   756  C CD2 . LEU A 1 87  ? 14.547  2.842   1.760   1.00 24.51 ? 87  LEU A CD2 1 
ATOM   757  N N   . GLU A 1 88  ? 12.583  2.727   -2.387  1.00 18.98 ? 88  GLU A N   1 
ATOM   758  C CA  . GLU A 1 88  ? 11.549  3.294   -3.241  1.00 24.55 ? 88  GLU A CA  1 
ATOM   759  C C   . GLU A 1 88  ? 11.338  4.756   -2.887  1.00 21.73 ? 88  GLU A C   1 
ATOM   760  O O   . GLU A 1 88  ? 11.602  5.183   -1.758  1.00 24.91 ? 88  GLU A O   1 
ATOM   761  C CB  . GLU A 1 88  ? 10.233  2.527   -3.079  1.00 19.53 ? 88  GLU A CB  1 
ATOM   762  C CG  . GLU A 1 88  ? 10.343  1.048   -3.433  1.00 23.37 ? 88  GLU A CG  1 
ATOM   763  C CD  . GLU A 1 88  ? 9.206   0.211   -2.869  1.00 32.32 ? 88  GLU A CD  1 
ATOM   764  O OE1 . GLU A 1 88  ? 9.265   -1.034  -2.990  1.00 34.43 ? 88  GLU A OE1 1 
ATOM   765  O OE2 . GLU A 1 88  ? 8.254   0.794   -2.311  1.00 32.82 ? 88  GLU A OE2 1 
ATOM   766  N N   . LYS A 1 89  ? 10.858  5.536   -3.861  1.00 19.03 ? 89  LYS A N   1 
ATOM   767  C CA  . LYS A 1 89  ? 10.554  6.929   -3.555  1.00 27.12 ? 89  LYS A CA  1 
ATOM   768  C C   . LYS A 1 89  ? 9.494   7.022   -2.466  1.00 30.95 ? 89  LYS A C   1 
ATOM   769  O O   . LYS A 1 89  ? 9.544   7.930   -1.622  1.00 25.87 ? 89  LYS A O   1 
ATOM   770  C CB  . LYS A 1 89  ? 10.109  7.681   -4.815  1.00 30.93 ? 89  LYS A CB  1 
ATOM   771  C CG  . LYS A 1 89  ? 9.847   9.158   -4.566  1.00 37.49 ? 89  LYS A CG  1 
ATOM   772  C CD  . LYS A 1 89  ? 9.198   9.841   -5.758  1.00 53.23 ? 89  LYS A CD  1 
ATOM   773  C CE  . LYS A 1 89  ? 9.479   11.336  -5.745  1.00 58.45 ? 89  LYS A CE  1 
ATOM   774  N NZ  . LYS A 1 89  ? 9.442   11.886  -4.362  1.00 59.48 ? 89  LYS A NZ  1 
ATOM   775  N N   . GLU A 1 90  ? 8.558   6.067   -2.446  1.00 23.92 ? 90  GLU A N   1 
ATOM   776  C CA  . GLU A 1 90  ? 7.551   6.017   -1.390  1.00 27.68 ? 90  GLU A CA  1 
ATOM   777  C C   . GLU A 1 90  ? 8.178   5.704   -0.034  1.00 26.89 ? 90  GLU A C   1 
ATOM   778  O O   . GLU A 1 90  ? 7.736   6.220   0.998   1.00 24.69 ? 90  GLU A O   1 
ATOM   779  C CB  . GLU A 1 90  ? 6.494   4.978   -1.756  1.00 31.40 ? 90  GLU A CB  1 
ATOM   780  C CG  . GLU A 1 90  ? 5.615   4.531   -0.613  1.00 46.08 ? 90  GLU A CG  1 
ATOM   781  C CD  . GLU A 1 90  ? 4.365   3.839   -1.105  1.00 54.33 ? 90  GLU A CD  1 
ATOM   782  O OE1 . GLU A 1 90  ? 4.385   3.344   -2.256  1.00 52.18 ? 90  GLU A OE1 1 
ATOM   783  O OE2 . GLU A 1 90  ? 3.368   3.803   -0.350  1.00 54.24 ? 90  GLU A OE2 1 
ATOM   784  N N   . GLU A 1 91  ? 9.207   4.858   -0.008  1.00 21.67 ? 91  GLU A N   1 
ATOM   785  C CA  . GLU A 1 91  ? 9.832   4.542   1.272   1.00 21.89 ? 91  GLU A CA  1 
ATOM   786  C C   . GLU A 1 91  ? 10.652  5.716   1.790   1.00 23.86 ? 91  GLU A C   1 
ATOM   787  O O   . GLU A 1 91  ? 10.696  5.957   3.000   1.00 22.05 ? 91  GLU A O   1 
ATOM   788  C CB  . GLU A 1 91  ? 10.700  3.296   1.149   1.00 25.33 ? 91  GLU A CB  1 
ATOM   789  C CG  . GLU A 1 91  ? 9.922   2.017   0.903   1.00 24.27 ? 91  GLU A CG  1 
ATOM   790  C CD  . GLU A 1 91  ? 10.845  0.847   0.614   1.00 29.17 ? 91  GLU A CD  1 
ATOM   791  O OE1 . GLU A 1 91  ? 10.660  -0.215  1.249   1.00 32.76 ? 91  GLU A OE1 1 
ATOM   792  O OE2 . GLU A 1 91  ? 11.756  0.996   -0.243  1.00 27.72 ? 91  GLU A OE2 1 
ATOM   793  N N   . VAL A 1 92  ? 11.304  6.462   0.891   1.00 21.88 ? 92  VAL A N   1 
ATOM   794  C CA  . VAL A 1 92  ? 11.999  7.681   1.304   1.00 23.89 ? 92  VAL A CA  1 
ATOM   795  C C   . VAL A 1 92  ? 11.019  8.669   1.929   1.00 28.43 ? 92  VAL A C   1 
ATOM   796  O O   . VAL A 1 92  ? 11.298  9.262   2.978   1.00 25.65 ? 92  VAL A O   1 
ATOM   797  C CB  . VAL A 1 92  ? 12.747  8.308   0.110   1.00 25.75 ? 92  VAL A CB  1 
ATOM   798  C CG1 . VAL A 1 92  ? 13.149  9.742   0.433   1.00 27.55 ? 92  VAL A CG1 1 
ATOM   799  C CG2 . VAL A 1 92  ? 13.978  7.482   -0.258  1.00 20.26 ? 92  VAL A CG2 1 
ATOM   800  N N   . GLU A 1 93  ? 9.856   8.861   1.291   1.00 23.34 ? 93  GLU A N   1 
ATOM   801  C CA  . GLU A 1 93  ? 8.839   9.774   1.811   1.00 25.34 ? 93  GLU A CA  1 
ATOM   802  C C   . GLU A 1 93  ? 8.339   9.343   3.185   1.00 24.78 ? 93  GLU A C   1 
ATOM   803  O O   . GLU A 1 93  ? 8.122   10.188  4.066   1.00 25.70 ? 93  GLU A O   1 
ATOM   804  C CB  . GLU A 1 93  ? 7.661   9.861   0.838   1.00 24.61 ? 93  GLU A CB  1 
ATOM   805  C CG  . GLU A 1 93  ? 7.921   10.688  -0.403  1.00 40.01 ? 93  GLU A CG  1 
ATOM   806  C CD  . GLU A 1 93  ? 6.751   10.648  -1.380  1.00 53.66 ? 93  GLU A CD  1 
ATOM   807  O OE1 . GLU A 1 93  ? 5.978   9.663   -1.353  1.00 57.24 ? 93  GLU A OE1 1 
ATOM   808  O OE2 . GLU A 1 93  ? 6.600   11.608  -2.168  1.00 56.80 ? 93  GLU A OE2 1 
ATOM   809  N N   . LYS A 1 94  ? 8.116   8.038   3.381   1.00 23.88 ? 94  LYS A N   1 
ATOM   810  C CA  . LYS A 1 94  ? 7.646   7.564   4.684   1.00 25.85 ? 94  LYS A CA  1 
ATOM   811  C C   . LYS A 1 94  ? 8.702   7.791   5.765   1.00 25.21 ? 94  LYS A C   1 
ATOM   812  O O   . LYS A 1 94  ? 8.373   8.146   6.905   1.00 27.13 ? 94  LYS A O   1 
ATOM   813  C CB  . LYS A 1 94  ? 7.271   6.077   4.621   1.00 28.90 ? 94  LYS A CB  1 
ATOM   814  C CG  . LYS A 1 94  ? 6.145   5.688   3.634   1.00 38.31 ? 94  LYS A CG  1 
ATOM   815  C CD  . LYS A 1 94  ? 5.145   6.810   3.365   1.00 44.89 ? 94  LYS A CD  1 
ATOM   816  C CE  . LYS A 1 94  ? 4.246   6.493   2.167   1.00 48.70 ? 94  LYS A CE  1 
ATOM   817  N NZ  . LYS A 1 94  ? 4.598   7.294   0.952   1.00 47.27 ? 94  LYS A NZ  1 
ATOM   818  N N   . LEU A 1 95  ? 9.973   7.572   5.427   1.00 21.24 ? 95  LEU A N   1 
ATOM   819  C CA  . LEU A 1 95  ? 11.056  7.825   6.372   1.00 21.08 ? 95  LEU A CA  1 
ATOM   820  C C   . LEU A 1 95  ? 11.102  9.294   6.762   1.00 22.53 ? 95  LEU A C   1 
ATOM   821  O O   . LEU A 1 95  ? 11.229  9.634   7.944   1.00 19.30 ? 95  LEU A O   1 
ATOM   822  C CB  . LEU A 1 95  ? 12.386  7.398   5.759   1.00 24.04 ? 95  LEU A CB  1 
ATOM   823  C CG  . LEU A 1 95  ? 13.592  7.534   6.689   1.00 37.34 ? 95  LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 95  ? 13.314  6.807   7.994   1.00 41.55 ? 95  LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 95  ? 14.847  6.996   6.020   1.00 42.51 ? 95  LEU A CD2 1 
ATOM   826  N N   . ILE A 1 96  ? 11.021  10.181  5.767   1.00 21.61 ? 96  ILE A N   1 
ATOM   827  C CA  . ILE A 1 96  ? 11.041  11.615  6.035   1.00 26.51 ? 96  ILE A CA  1 
ATOM   828  C C   . ILE A 1 96  ? 9.867   12.000  6.927   1.00 24.52 ? 96  ILE A C   1 
ATOM   829  O O   . ILE A 1 96  ? 10.017  12.763  7.890   1.00 27.40 ? 96  ILE A O   1 
ATOM   830  C CB  . ILE A 1 96  ? 11.032  12.399  4.706   1.00 22.03 ? 96  ILE A CB  1 
ATOM   831  C CG1 . ILE A 1 96  ? 12.392  12.285  3.999   1.00 37.36 ? 96  ILE A CG1 1 
ATOM   832  C CG2 . ILE A 1 96  ? 10.664  13.856  4.931   1.00 25.09 ? 96  ILE A CG2 1 
ATOM   833  C CD1 . ILE A 1 96  ? 13.534  12.945  4.748   1.00 40.09 ? 96  ILE A CD1 1 
ATOM   834  N N   . GLU A 1 97  ? 8.686   11.455  6.640   1.00 26.06 ? 97  GLU A N   1 
ATOM   835  C CA  . GLU A 1 97  ? 7.506   11.857  7.390   1.00 27.81 ? 97  GLU A CA  1 
ATOM   836  C C   . GLU A 1 97  ? 7.516   11.284  8.801   1.00 25.37 ? 97  GLU A C   1 
ATOM   837  O O   . GLU A 1 97  ? 7.052   11.941  9.741   1.00 23.28 ? 97  GLU A O   1 
ATOM   838  C CB  . GLU A 1 97  ? 6.242   11.450  6.639   1.00 31.51 ? 97  GLU A CB  1 
ATOM   839  C CG  . GLU A 1 97  ? 5.895   12.400  5.486   1.00 48.38 ? 97  GLU A CG  1 
ATOM   840  C CD  . GLU A 1 97  ? 5.402   13.777  5.948   1.00 61.44 ? 97  GLU A CD  1 
ATOM   841  O OE1 . GLU A 1 97  ? 5.069   14.605  5.070   1.00 64.07 ? 97  GLU A OE1 1 
ATOM   842  O OE2 . GLU A 1 97  ? 5.336   14.035  7.174   1.00 63.13 ? 97  GLU A OE2 1 
ATOM   843  N N   . PHE A 1 98  ? 8.032   10.064  8.978   1.00 20.26 ? 98  PHE A N   1 
ATOM   844  C CA  . PHE A 1 98  ? 8.187   9.541   10.338  1.00 22.26 ? 98  PHE A CA  1 
ATOM   845  C C   . PHE A 1 98  ? 9.116   10.421  11.166  1.00 26.04 ? 98  PHE A C   1 
ATOM   846  O O   . PHE A 1 98  ? 8.875   10.649  12.363  1.00 22.30 ? 98  PHE A O   1 
ATOM   847  C CB  . PHE A 1 98  ? 8.718   8.110   10.293  1.00 24.30 ? 98  PHE A CB  1 
ATOM   848  C CG  . PHE A 1 98  ? 8.577   7.377   11.591  1.00 18.37 ? 98  PHE A CG  1 
ATOM   849  C CD1 . PHE A 1 98  ? 7.332   6.929   12.011  1.00 28.40 ? 98  PHE A CD1 1 
ATOM   850  C CD2 . PHE A 1 98  ? 9.677   7.135   12.394  1.00 18.34 ? 98  PHE A CD2 1 
ATOM   851  C CE1 . PHE A 1 98  ? 7.188   6.257   13.212  1.00 26.32 ? 98  PHE A CE1 1 
ATOM   852  C CE2 . PHE A 1 98  ? 9.536   6.457   13.607  1.00 25.60 ? 98  PHE A CE2 1 
ATOM   853  C CZ  . PHE A 1 98  ? 8.294   6.019   14.008  1.00 25.48 ? 98  PHE A CZ  1 
ATOM   854  N N   . THR A 1 99  ? 10.196  10.908  10.551  1.00 23.09 ? 99  THR A N   1 
ATOM   855  C CA  . THR A 1 99  ? 11.132  11.773  11.258  1.00 22.48 ? 99  THR A CA  1 
ATOM   856  C C   . THR A 1 99  ? 10.452  13.075  11.666  1.00 20.31 ? 99  THR A C   1 
ATOM   857  O O   . THR A 1 99  ? 10.558  13.514  12.817  1.00 24.97 ? 99  THR A O   1 
ATOM   858  C CB  . THR A 1 99  ? 12.360  12.056  10.374  1.00 21.93 ? 99  THR A CB  1 
ATOM   859  O OG1 . THR A 1 99  ? 12.948  10.822  9.926   1.00 19.77 ? 99  THR A OG1 1 
ATOM   860  C CG2 . THR A 1 99  ? 13.391  12.844  11.150  1.00 18.36 ? 99  THR A CG2 1 
ATOM   861  N N   . LYS A 1 100 ? 9.731   13.696  10.729  1.00 21.35 ? 100 LYS A N   1 
ATOM   862  C CA  . LYS A 1 100 ? 9.042   14.952  11.017  1.00 25.68 ? 100 LYS A CA  1 
ATOM   863  C C   . LYS A 1 100 ? 8.047   14.796  12.159  1.00 24.93 ? 100 LYS A C   1 
ATOM   864  O O   . LYS A 1 100 ? 7.926   15.684  13.008  1.00 24.80 ? 100 LYS A O   1 
ATOM   865  C CB  . LYS A 1 100 ? 8.330   15.456  9.761   1.00 27.06 ? 100 LYS A CB  1 
ATOM   866  C CG  . LYS A 1 100 ? 9.241   15.984  8.659   1.00 33.86 ? 100 LYS A CG  1 
ATOM   867  C CD  . LYS A 1 100 ? 8.428   16.829  7.684   1.00 38.95 ? 100 LYS A CD  1 
ATOM   868  C CE  . LYS A 1 100 ? 9.102   16.966  6.328   1.00 46.56 ? 100 LYS A CE  1 
ATOM   869  N NZ  . LYS A 1 100 ? 10.307  17.835  6.385   1.00 51.01 ? 100 LYS A NZ  1 
ATOM   870  N N   . LEU A 1 101 ? 7.318   13.680  12.191  1.00 21.67 ? 101 LEU A N   1 
ATOM   871  C CA  . LEU A 1 101 ? 6.348   13.457  13.265  1.00 21.39 ? 101 LEU A CA  1 
ATOM   872  C C   . LEU A 1 101 ? 7.016   13.379  14.633  1.00 19.13 ? 101 LEU A C   1 
ATOM   873  O O   . LEU A 1 101 ? 6.435   13.824  15.634  1.00 18.19 ? 101 LEU A O   1 
ATOM   874  C CB  . LEU A 1 101 ? 5.553   12.176  12.991  1.00 24.20 ? 101 LEU A CB  1 
ATOM   875  C CG  . LEU A 1 101 ? 4.813   11.513  14.156  1.00 35.00 ? 101 LEU A CG  1 
ATOM   876  C CD1 . LEU A 1 101 ? 3.523   12.260  14.484  1.00 40.76 ? 101 LEU A CD1 1 
ATOM   877  C CD2 . LEU A 1 101 ? 4.526   10.034  13.870  1.00 37.43 ? 101 LEU A CD2 1 
ATOM   878  N N   . ASN A 1 102 ? 8.226   12.827  14.705  1.00 24.94 ? 102 ASN A N   1 
ATOM   879  C CA  . ASN A 1 102 ? 8.904   12.592  15.977  1.00 28.47 ? 102 ASN A CA  1 
ATOM   880  C C   . ASN A 1 102 ? 9.987   13.620  16.288  1.00 28.22 ? 102 ASN A C   1 
ATOM   881  O O   . ASN A 1 102 ? 10.673  13.491  17.311  1.00 25.07 ? 102 ASN A O   1 
ATOM   882  C CB  . ASN A 1 102 ? 9.511   11.190  15.992  1.00 19.36 ? 102 ASN A CB  1 
ATOM   883  C CG  . ASN A 1 102 ? 8.459   10.103  16.002  1.00 25.22 ? 102 ASN A CG  1 
ATOM   884  O OD1 . ASN A 1 102 ? 7.727   9.940   16.981  1.00 26.76 ? 102 ASN A OD1 1 
ATOM   885  N ND2 . ASN A 1 102 ? 8.392   9.335   14.923  1.00 22.02 ? 102 ASN A ND2 1 
ATOM   886  N N   . TYR A 1 103 ? 10.105  14.659  15.456  1.00 23.66 ? 103 TYR A N   1 
ATOM   887  C CA  . TYR A 1 103 ? 11.281  15.527  15.435  1.00 25.43 ? 103 TYR A CA  1 
ATOM   888  C C   . TYR A 1 103 ? 11.469  16.294  16.740  1.00 24.41 ? 103 TYR A C   1 
ATOM   889  O O   . TYR A 1 103 ? 12.608  16.544  17.156  1.00 21.75 ? 103 TYR A O   1 
ATOM   890  C CB  . TYR A 1 103 ? 11.146  16.492  14.250  1.00 28.62 ? 103 TYR A CB  1 
ATOM   891  C CG  . TYR A 1 103 ? 12.266  17.478  14.048  1.00 31.97 ? 103 TYR A CG  1 
ATOM   892  C CD1 . TYR A 1 103 ? 12.256  18.709  14.690  1.00 36.42 ? 103 TYR A CD1 1 
ATOM   893  C CD2 . TYR A 1 103 ? 13.315  17.197  13.181  1.00 38.55 ? 103 TYR A CD2 1 
ATOM   894  C CE1 . TYR A 1 103 ? 13.269  19.623  14.494  1.00 43.45 ? 103 TYR A CE1 1 
ATOM   895  C CE2 . TYR A 1 103 ? 14.333  18.106  12.978  1.00 45.12 ? 103 TYR A CE2 1 
ATOM   896  C CZ  . TYR A 1 103 ? 14.305  19.319  13.638  1.00 46.41 ? 103 TYR A CZ  1 
ATOM   897  O OH  . TYR A 1 103 ? 15.318  20.227  13.442  1.00 45.78 ? 103 TYR A OH  1 
ATOM   898  N N   . GLU A 1 104 ? 10.376  16.707  17.382  1.00 27.06 ? 104 GLU A N   1 
ATOM   899  C CA  . GLU A 1 104 ? 10.456  17.532  18.582  1.00 26.42 ? 104 GLU A CA  1 
ATOM   900  C C   . GLU A 1 104 ? 10.636  16.728  19.863  1.00 30.22 ? 104 GLU A C   1 
ATOM   901  O O   . GLU A 1 104 ? 10.860  17.326  20.922  1.00 28.71 ? 104 GLU A O   1 
ATOM   902  C CB  . GLU A 1 104 ? 9.199   18.404  18.709  1.00 24.28 ? 104 GLU A CB  1 
ATOM   903  C CG  . GLU A 1 104 ? 9.021   19.420  17.581  1.00 35.16 ? 104 GLU A CG  1 
ATOM   904  C CD  . GLU A 1 104 ? 10.132  20.454  17.530  1.00 43.05 ? 104 GLU A CD  1 
ATOM   905  O OE1 . GLU A 1 104 ? 10.459  20.917  16.418  1.00 45.34 ? 104 GLU A OE1 1 
ATOM   906  O OE2 . GLU A 1 104 ? 10.677  20.809  18.597  1.00 47.25 ? 104 GLU A OE2 1 
ATOM   907  N N   . LYS A 1 105 ? 10.544  15.402  19.795  1.00 18.83 ? 105 LYS A N   1 
ATOM   908  C CA  . LYS A 1 105 ? 10.684  14.582  20.988  1.00 21.14 ? 105 LYS A CA  1 
ATOM   909  C C   . LYS A 1 105 ? 12.147  14.532  21.432  1.00 21.83 ? 105 LYS A C   1 
ATOM   910  O O   . LYS A 1 105 ? 13.048  14.416  20.593  1.00 23.02 ? 105 LYS A O   1 
ATOM   911  C CB  . LYS A 1 105 ? 10.154  13.169  20.716  1.00 18.09 ? 105 LYS A CB  1 
ATOM   912  C CG  . LYS A 1 105 ? 8.676   13.159  20.352  1.00 15.53 ? 105 LYS A CG  1 
ATOM   913  C CD  . LYS A 1 105 ? 8.202   11.794  19.871  1.00 19.02 ? 105 LYS A CD  1 
ATOM   914  C CE  . LYS A 1 105 ? 6.719   11.827  19.533  1.00 22.61 ? 105 LYS A CE  1 
ATOM   915  N NZ  . LYS A 1 105 ? 6.214   10.491  19.110  1.00 19.94 ? 105 LYS A NZ  1 
ATOM   916  N N   . PRO A 1 106 ? 12.418  14.623  22.739  1.00 23.03 ? 106 PRO A N   1 
ATOM   917  C CA  . PRO A 1 106 ? 13.819  14.599  23.198  1.00 18.37 ? 106 PRO A CA  1 
ATOM   918  C C   . PRO A 1 106 ? 14.593  13.369  22.750  1.00 25.67 ? 106 PRO A C   1 
ATOM   919  O O   . PRO A 1 106 ? 15.818  13.451  22.596  1.00 27.02 ? 106 PRO A O   1 
ATOM   920  C CB  . PRO A 1 106 ? 13.693  14.658  24.732  1.00 21.20 ? 106 PRO A CB  1 
ATOM   921  C CG  . PRO A 1 106 ? 12.353  15.283  24.986  1.00 24.82 ? 106 PRO A CG  1 
ATOM   922  C CD  . PRO A 1 106 ? 11.466  14.834  23.845  1.00 27.16 ? 106 PRO A CD  1 
ATOM   923  N N   . ILE A 1 107 ? 13.931  12.230  22.526  1.00 19.64 ? 107 ILE A N   1 
ATOM   924  C CA  . ILE A 1 107 ? 14.677  11.058  22.081  1.00 22.20 ? 107 ILE A CA  1 
ATOM   925  C C   . ILE A 1 107 ? 15.190  11.229  20.658  1.00 25.87 ? 107 ILE A C   1 
ATOM   926  O O   . ILE A 1 107 ? 16.089  10.491  20.240  1.00 23.94 ? 107 ILE A O   1 
ATOM   927  C CB  . ILE A 1 107 ? 13.836  9.768   22.213  1.00 20.15 ? 107 ILE A CB  1 
ATOM   928  C CG1 . ILE A 1 107 ? 12.616  9.785   21.290  1.00 17.25 ? 107 ILE A CG1 1 
ATOM   929  C CG2 . ILE A 1 107 ? 13.402  9.559   23.648  1.00 17.71 ? 107 ILE A CG2 1 
ATOM   930  C CD1 . ILE A 1 107 ? 11.922  8.443   21.194  1.00 24.03 ? 107 ILE A CD1 1 
ATOM   931  N N   . TYR A 1 108 ? 14.654  12.194  19.901  1.00 19.53 ? 108 TYR A N   1 
ATOM   932  C CA  . TYR A 1 108 ? 15.147  12.500  18.562  1.00 20.74 ? 108 TYR A CA  1 
ATOM   933  C C   . TYR A 1 108 ? 16.129  13.676  18.534  1.00 24.13 ? 108 TYR A C   1 
ATOM   934  O O   . TYR A 1 108 ? 16.411  14.205  17.452  1.00 26.37 ? 108 TYR A O   1 
ATOM   935  C CB  . TYR A 1 108 ? 13.970  12.767  17.615  1.00 16.19 ? 108 TYR A CB  1 
ATOM   936  C CG  . TYR A 1 108 ? 13.466  11.527  16.913  1.00 23.83 ? 108 TYR A CG  1 
ATOM   937  C CD1 . TYR A 1 108 ? 12.737  10.559  17.597  1.00 25.80 ? 108 TYR A CD1 1 
ATOM   938  C CD2 . TYR A 1 108 ? 13.719  11.322  15.561  1.00 21.97 ? 108 TYR A CD2 1 
ATOM   939  C CE1 . TYR A 1 108 ? 12.284  9.412   16.947  1.00 21.61 ? 108 TYR A CE1 1 
ATOM   940  C CE2 . TYR A 1 108 ? 13.274  10.178  14.912  1.00 23.55 ? 108 TYR A CE2 1 
ATOM   941  C CZ  . TYR A 1 108 ? 12.554  9.233   15.606  1.00 21.29 ? 108 TYR A CZ  1 
ATOM   942  O OH  . TYR A 1 108 ? 12.113  8.106   14.948  1.00 17.43 ? 108 TYR A OH  1 
ATOM   943  N N   . ARG A 1 109 ? 16.664  14.096  19.686  1.00 28.35 ? 109 ARG A N   1 
ATOM   944  C CA  . ARG A 1 109 ? 17.604  15.223  19.727  1.00 31.68 ? 109 ARG A CA  1 
ATOM   945  C C   . ARG A 1 109 ? 18.992  14.744  19.302  1.00 24.88 ? 109 ARG A C   1 
ATOM   946  O O   . ARG A 1 109 ? 19.876  14.476  20.119  1.00 30.26 ? 109 ARG A O   1 
ATOM   947  C CB  . ARG A 1 109 ? 17.638  15.874  21.113  1.00 37.55 ? 109 ARG A CB  1 
ATOM   948  C CG  . ARG A 1 109 ? 16.768  17.172  21.244  1.00 46.81 ? 109 ARG A CG  1 
ATOM   949  C CD  . ARG A 1 109 ? 15.243  16.807  21.171  1.00 57.11 ? 109 ARG A CD  1 
ATOM   950  N NE  . ARG A 1 109 ? 14.375  17.974  21.278  1.00 64.63 ? 109 ARG A NE  1 
ATOM   951  C CZ  . ARG A 1 109 ? 13.210  17.985  21.922  1.00 70.59 ? 109 ARG A CZ  1 
ATOM   952  N NH1 . ARG A 1 109 ? 12.772  16.902  22.556  1.00 74.05 ? 109 ARG A NH1 1 
ATOM   953  N NH2 . ARG A 1 109 ? 12.500  19.099  21.987  1.00 71.45 ? 109 ARG A NH2 1 
ATOM   954  N N   . PHE A 1 110 ? 19.182  14.611  17.989  1.00 23.76 ? 110 PHE A N   1 
ATOM   955  C CA  . PHE A 1 110 ? 20.503  14.472  17.388  1.00 29.13 ? 110 PHE A CA  1 
ATOM   956  C C   . PHE A 1 110 ? 20.689  15.616  16.405  1.00 29.31 ? 110 PHE A C   1 
ATOM   957  O O   . PHE A 1 110 ? 19.832  15.825  15.543  1.00 28.57 ? 110 PHE A O   1 
ATOM   958  C CB  . PHE A 1 110 ? 20.664  13.139  16.654  1.00 27.30 ? 110 PHE A CB  1 
ATOM   959  C CG  . PHE A 1 110 ? 20.340  11.928  17.486  1.00 21.90 ? 110 PHE A CG  1 
ATOM   960  C CD1 . PHE A 1 110 ? 19.039  11.467  17.601  1.00 26.31 ? 110 PHE A CD1 1 
ATOM   961  C CD2 . PHE A 1 110 ? 21.352  11.217  18.107  1.00 22.16 ? 110 PHE A CD2 1 
ATOM   962  C CE1 . PHE A 1 110 ? 18.751  10.333  18.338  1.00 32.26 ? 110 PHE A CE1 1 
ATOM   963  C CE2 . PHE A 1 110 ? 21.069  10.077  18.848  1.00 29.77 ? 110 PHE A CE2 1 
ATOM   964  C CZ  . PHE A 1 110 ? 19.766  9.641   18.965  1.00 31.01 ? 110 PHE A CZ  1 
ATOM   965  N N   . GLU A 1 111 ? 21.800  16.353  16.518  1.00 32.07 ? 111 GLU A N   1 
ATOM   966  C CA  . GLU A 1 111 ? 21.979  17.500  15.631  1.00 28.28 ? 111 GLU A CA  1 
ATOM   967  C C   . GLU A 1 111 ? 22.062  17.063  14.174  1.00 25.29 ? 111 GLU A C   1 
ATOM   968  O O   . GLU A 1 111 ? 21.669  17.817  13.275  1.00 26.48 ? 111 GLU A O   1 
ATOM   969  C CB  . GLU A 1 111 ? 23.223  18.299  16.023  1.00 28.43 ? 111 GLU A CB  1 
ATOM   970  C CG  . GLU A 1 111 ? 24.519  17.797  15.419  1.00 46.68 ? 111 GLU A CG  1 
ATOM   971  C CD  . GLU A 1 111 ? 25.438  17.193  16.463  1.00 59.46 ? 111 GLU A CD  1 
ATOM   972  O OE1 . GLU A 1 111 ? 24.936  16.436  17.323  1.00 66.82 ? 111 GLU A OE1 1 
ATOM   973  O OE2 . GLU A 1 111 ? 26.657  17.476  16.426  1.00 63.49 ? 111 GLU A OE2 1 
ATOM   974  N N   . ARG A 1 112 ? 22.544  15.844  13.923  1.00 23.18 ? 112 ARG A N   1 
ATOM   975  C CA  . ARG A 1 112 ? 22.584  15.334  12.556  1.00 25.46 ? 112 ARG A CA  1 
ATOM   976  C C   . ARG A 1 112 ? 21.183  15.238  11.962  1.00 34.60 ? 112 ARG A C   1 
ATOM   977  O O   . ARG A 1 112 ? 20.992  15.487  10.767  1.00 31.04 ? 112 ARG A O   1 
ATOM   978  C CB  . ARG A 1 112 ? 23.282  13.973  12.524  1.00 23.70 ? 112 ARG A CB  1 
ATOM   979  C CG  . ARG A 1 112 ? 23.428  13.352  11.135  1.00 18.42 ? 112 ARG A CG  1 
ATOM   980  C CD  . ARG A 1 112 ? 24.255  14.238  10.210  1.00 27.82 ? 112 ARG A CD  1 
ATOM   981  N NE  . ARG A 1 112 ? 24.560  13.549  8.959   1.00 29.41 ? 112 ARG A NE  1 
ATOM   982  C CZ  . ARG A 1 112 ? 24.889  14.156  7.822   1.00 32.73 ? 112 ARG A CZ  1 
ATOM   983  N NH1 . ARG A 1 112 ? 24.961  15.479  7.758   1.00 32.03 ? 112 ARG A NH1 1 
ATOM   984  N NH2 . ARG A 1 112 ? 25.141  13.434  6.741   1.00 31.28 ? 112 ARG A NH2 1 
ATOM   985  N N   . ILE A 1 113 ? 20.186  14.883  12.781  1.00 24.46 ? 113 ILE A N   1 
ATOM   986  C CA  . ILE A 1 113 ? 18.812  14.832  12.285  1.00 26.54 ? 113 ILE A CA  1 
ATOM   987  C C   . ILE A 1 113 ? 18.355  16.225  11.873  1.00 28.46 ? 113 ILE A C   1 
ATOM   988  O O   . ILE A 1 113 ? 17.732  16.410  10.818  1.00 26.17 ? 113 ILE A O   1 
ATOM   989  C CB  . ILE A 1 113 ? 17.874  14.215  13.343  1.00 27.72 ? 113 ILE A CB  1 
ATOM   990  C CG1 . ILE A 1 113 ? 18.027  12.695  13.388  1.00 26.76 ? 113 ILE A CG1 1 
ATOM   991  C CG2 . ILE A 1 113 ? 16.413  14.567  13.055  1.00 30.74 ? 113 ILE A CG2 1 
ATOM   992  C CD1 . ILE A 1 113 ? 16.912  12.001  14.139  1.00 34.81 ? 113 ILE A CD1 1 
ATOM   993  N N   . ARG A 1 114 ? 18.676  17.232  12.687  1.00 29.07 ? 114 ARG A N   1 
ATOM   994  C CA  . ARG A 1 114 ? 18.339  18.599  12.317  1.00 32.87 ? 114 ARG A CA  1 
ATOM   995  C C   . ARG A 1 114 ? 19.032  19.010  11.022  1.00 32.39 ? 114 ARG A C   1 
ATOM   996  O O   . ARG A 1 114 ? 18.443  19.727  10.204  1.00 36.43 ? 114 ARG A O   1 
ATOM   997  C CB  . ARG A 1 114 ? 18.694  19.543  13.468  1.00 42.51 ? 114 ARG A CB  1 
ATOM   998  C CG  . ARG A 1 114 ? 17.992  19.165  14.772  1.00 54.05 ? 114 ARG A CG  1 
ATOM   999  C CD  . ARG A 1 114 ? 17.941  20.316  15.760  1.00 59.53 ? 114 ARG A CD  1 
ATOM   1000 N NE  . ARG A 1 114 ? 19.217  20.490  16.447  1.00 67.88 ? 114 ARG A NE  1 
ATOM   1001 C CZ  . ARG A 1 114 ? 19.599  19.782  17.507  1.00 71.38 ? 114 ARG A CZ  1 
ATOM   1002 N NH1 . ARG A 1 114 ? 18.802  18.846  18.009  1.00 70.14 ? 114 ARG A NH1 1 
ATOM   1003 N NH2 . ARG A 1 114 ? 20.779  20.012  18.068  1.00 71.63 ? 114 ARG A NH2 1 
ATOM   1004 N N   . GLU A 1 115 ? 20.264  18.544  10.799  1.00 33.81 ? 115 GLU A N   1 
ATOM   1005 C CA  . GLU A 1 115 ? 20.926  18.809  9.522   1.00 31.82 ? 115 GLU A CA  1 
ATOM   1006 C C   . GLU A 1 115 ? 20.188  18.140  8.366   1.00 37.46 ? 115 GLU A C   1 
ATOM   1007 O O   . GLU A 1 115 ? 20.010  18.744  7.300   1.00 45.45 ? 115 GLU A O   1 
ATOM   1008 C CB  . GLU A 1 115 ? 22.379  18.328  9.563   1.00 33.26 ? 115 GLU A CB  1 
ATOM   1009 C CG  . GLU A 1 115 ? 23.335  19.239  10.313  1.00 39.22 ? 115 GLU A CG  1 
ATOM   1010 C CD  . GLU A 1 115 ? 24.644  18.549  10.664  1.00 42.65 ? 115 GLU A CD  1 
ATOM   1011 O OE1 . GLU A 1 115 ? 25.114  17.703  9.869   1.00 40.94 ? 115 GLU A OE1 1 
ATOM   1012 O OE2 . GLU A 1 115 ? 25.198  18.848  11.745  1.00 50.60 ? 115 GLU A OE2 1 
ATOM   1013 N N   . LEU A 1 116 ? 19.744  16.893  8.559   1.00 33.43 ? 116 LEU A N   1 
ATOM   1014 C CA  . LEU A 1 116 ? 19.165  16.133  7.454   1.00 30.62 ? 116 LEU A CA  1 
ATOM   1015 C C   . LEU A 1 116 ? 17.789  16.658  7.069   1.00 26.60 ? 116 LEU A C   1 
ATOM   1016 O O   . LEU A 1 116 ? 17.420  16.625  5.891   1.00 29.88 ? 116 LEU A O   1 
ATOM   1017 C CB  . LEU A 1 116 ? 19.081  14.650  7.813   1.00 30.22 ? 116 LEU A CB  1 
ATOM   1018 C CG  . LEU A 1 116 ? 20.425  13.970  8.068   1.00 27.82 ? 116 LEU A CG  1 
ATOM   1019 C CD1 . LEU A 1 116 ? 20.235  12.605  8.720   1.00 26.73 ? 116 LEU A CD1 1 
ATOM   1020 C CD2 . LEU A 1 116 ? 21.205  13.865  6.778   1.00 28.43 ? 116 LEU A CD2 1 
ATOM   1021 N N   . MET A 1 117 ? 17.006  17.125  8.050   1.00 31.65 ? 117 MET A N   1 
ATOM   1022 C CA  . MET A 1 117 ? 15.687  17.682  7.760   1.00 32.79 ? 117 MET A CA  1 
ATOM   1023 C C   . MET A 1 117 ? 15.761  19.018  7.036   1.00 40.61 ? 117 MET A C   1 
ATOM   1024 O O   . MET A 1 117 ? 14.737  19.480  6.524   1.00 43.40 ? 117 MET A O   1 
ATOM   1025 C CB  . MET A 1 117 ? 14.870  17.854  9.051   1.00 31.89 ? 117 MET A CB  1 
ATOM   1026 C CG  . MET A 1 117 ? 14.494  16.547  9.725   1.00 36.63 ? 117 MET A CG  1 
ATOM   1027 S SD  . MET A 1 117 ? 14.390  15.197  8.531   1.00 42.60 ? 117 MET A SD  1 
ATOM   1028 C CE  . MET A 1 117 ? 12.660  15.125  8.201   1.00 37.53 ? 117 MET A CE  1 
ATOM   1029 N N   . ASN A 1 118 ? 16.937  19.645  6.985   1.00 47.77 ? 118 ASN A N   1 
ATOM   1030 C CA  . ASN A 1 118 ? 17.106  20.946  6.355   1.00 53.58 ? 118 ASN A CA  1 
ATOM   1031 C C   . ASN A 1 118 ? 17.773  20.867  4.989   1.00 57.66 ? 118 ASN A C   1 
ATOM   1032 O O   . ASN A 1 118 ? 18.035  21.909  4.381   1.00 58.21 ? 118 ASN A O   1 
ATOM   1033 C CB  . ASN A 1 118 ? 17.913  21.871  7.267   1.00 54.43 ? 118 ASN A CB  1 
ATOM   1034 C CG  . ASN A 1 118 ? 17.071  22.475  8.375   1.00 55.57 ? 118 ASN A CG  1 
ATOM   1035 O OD1 . ASN A 1 118 ? 15.989  23.008  8.128   1.00 58.57 ? 118 ASN A OD1 1 
ATOM   1036 N ND2 . ASN A 1 118 ? 17.563  22.391  9.605   1.00 55.89 ? 118 ASN A ND2 1 
ATOM   1037 N N   . LYS A 1 119 ? 18.050  19.668  4.491   1.00 55.52 ? 119 LYS A N   1 
ATOM   1038 C CA  . LYS A 1 119 ? 18.639  19.496  3.174   1.00 51.65 ? 119 LYS A CA  1 
ATOM   1039 C C   . LYS A 1 119 ? 17.551  19.187  2.152   1.00 51.60 ? 119 LYS A C   1 
ATOM   1040 O O   . LYS A 1 119 ? 16.550  18.533  2.457   1.00 48.18 ? 119 LYS A O   1 
ATOM   1041 C CB  . LYS A 1 119 ? 19.691  18.387  3.189   1.00 51.32 ? 119 LYS A CB  1 
ATOM   1042 C CG  . LYS A 1 119 ? 20.955  18.752  3.965   1.00 55.60 ? 119 LYS A CG  1 
ATOM   1043 C CD  . LYS A 1 119 ? 22.022  17.677  3.825   1.00 55.46 ? 119 LYS A CD  1 
ATOM   1044 C CE  . LYS A 1 119 ? 23.301  18.044  4.565   1.00 54.13 ? 119 LYS A CE  1 
ATOM   1045 N NZ  . LYS A 1 119 ? 23.853  19.356  4.138   1.00 52.95 ? 119 LYS A NZ  1 
ATOM   1046 N N   . GLU A 1 120 ? 17.758  19.677  0.928   1.00 52.61 ? 120 GLU A N   1 
ATOM   1047 C CA  . GLU A 1 120 ? 16.743  19.557  -0.113  1.00 50.58 ? 120 GLU A CA  1 
ATOM   1048 C C   . GLU A 1 120 ? 16.607  18.122  -0.592  1.00 46.37 ? 120 GLU A C   1 
ATOM   1049 O O   . GLU A 1 120 ? 15.497  17.584  -0.674  1.00 49.18 ? 120 GLU A O   1 
ATOM   1050 C CB  . GLU A 1 120 ? 17.093  20.474  -1.278  1.00 52.17 ? 120 GLU A CB  1 
ATOM   1051 C CG  . GLU A 1 120 ? 17.353  21.903  -0.873  1.00 56.30 ? 120 GLU A CG  1 
ATOM   1052 C CD  . GLU A 1 120 ? 17.171  22.848  -2.032  1.00 64.00 ? 120 GLU A CD  1 
ATOM   1053 O OE1 . GLU A 1 120 ? 16.020  22.996  -2.481  1.00 65.82 ? 120 GLU A OE1 1 
ATOM   1054 O OE2 . GLU A 1 120 ? 18.168  23.431  -2.503  1.00 66.55 ? 120 GLU A OE2 1 
ATOM   1055 N N   . LYS A 1 121 ? 17.724  17.500  -0.939  1.00 43.63 ? 121 LYS A N   1 
ATOM   1056 C CA  . LYS A 1 121 ? 17.772  16.102  -1.321  1.00 42.38 ? 121 LYS A CA  1 
ATOM   1057 C C   . LYS A 1 121 ? 18.776  15.394  -0.427  1.00 36.15 ? 121 LYS A C   1 
ATOM   1058 O O   . LYS A 1 121 ? 19.688  16.012  0.127   1.00 38.91 ? 121 LYS A O   1 
ATOM   1059 C CB  . LYS A 1 121 ? 18.164  15.924  -2.801  1.00 43.86 ? 121 LYS A CB  1 
ATOM   1060 C CG  . LYS A 1 121 ? 17.087  16.352  -3.790  1.00 50.67 ? 121 LYS A CG  1 
ATOM   1061 C CD  . LYS A 1 121 ? 16.996  15.405  -4.981  1.00 55.24 ? 121 LYS A CD  1 
ATOM   1062 C CE  . LYS A 1 121 ? 15.630  15.505  -5.665  1.00 57.95 ? 121 LYS A CE  1 
ATOM   1063 N NZ  . LYS A 1 121 ? 15.492  14.545  -6.803  1.00 59.24 ? 121 LYS A NZ  1 
ATOM   1064 N N   . LEU A 1 122 ? 18.598  14.089  -0.284  1.00 34.38 ? 122 LEU A N   1 
ATOM   1065 C CA  . LEU A 1 122 ? 19.479  13.269  0.532   1.00 31.34 ? 122 LEU A CA  1 
ATOM   1066 C C   . LEU A 1 122 ? 20.189  12.268  -0.365  1.00 30.31 ? 122 LEU A C   1 
ATOM   1067 O O   . LEU A 1 122 ? 19.535  11.546  -1.124  1.00 29.16 ? 122 LEU A O   1 
ATOM   1068 C CB  . LEU A 1 122 ? 18.694  12.540  1.626   1.00 24.85 ? 122 LEU A CB  1 
ATOM   1069 C CG  . LEU A 1 122 ? 17.806  13.399  2.524   1.00 31.19 ? 122 LEU A CG  1 
ATOM   1070 C CD1 . LEU A 1 122 ? 16.985  12.515  3.439   1.00 33.35 ? 122 LEU A CD1 1 
ATOM   1071 C CD2 . LEU A 1 122 ? 18.637  14.382  3.330   1.00 24.23 ? 122 LEU A CD2 1 
ATOM   1072 N N   . ASN A 1 123 ? 21.517  12.228  -0.276  1.00 31.92 ? 123 ASN A N   1 
ATOM   1073 C CA  . ASN A 1 123 ? 22.287  11.202  -0.963  1.00 31.70 ? 123 ASN A CA  1 
ATOM   1074 C C   . ASN A 1 123 ? 22.308  9.926   -0.119  1.00 29.09 ? 123 ASN A C   1 
ATOM   1075 O O   . ASN A 1 123 ? 21.658  9.832   0.926   1.00 28.75 ? 123 ASN A O   1 
ATOM   1076 C CB  . ASN A 1 123 ? 23.696  11.707  -1.283  1.00 31.80 ? 123 ASN A CB  1 
ATOM   1077 C CG  . ASN A 1 123 ? 24.428  12.247  -0.064  1.00 41.64 ? 123 ASN A CG  1 
ATOM   1078 O OD1 . ASN A 1 123 ? 24.372  11.670  1.028   1.00 37.49 ? 123 ASN A OD1 1 
ATOM   1079 N ND2 . ASN A 1 123 ? 25.138  13.352  -0.253  1.00 42.66 ? 123 ASN A ND2 1 
ATOM   1080 N N   . ARG A 1 124 ? 23.056  8.916   -0.577  1.00 27.06 ? 124 ARG A N   1 
ATOM   1081 C CA  . ARG A 1 124 ? 23.020  7.623   0.102   1.00 22.22 ? 124 ARG A CA  1 
ATOM   1082 C C   . ARG A 1 124 ? 23.559  7.721   1.527   1.00 25.78 ? 124 ARG A C   1 
ATOM   1083 O O   . ARG A 1 124 ? 23.009  7.109   2.455   1.00 23.86 ? 124 ARG A O   1 
ATOM   1084 C CB  . ARG A 1 124 ? 23.799  6.580   -0.697  1.00 25.56 ? 124 ARG A CB  1 
ATOM   1085 C CG  . ARG A 1 124 ? 23.938  5.247   0.045   1.00 21.66 ? 124 ARG A CG  1 
ATOM   1086 C CD  . ARG A 1 124 ? 24.707  4.216   -0.765  1.00 26.11 ? 124 ARG A CD  1 
ATOM   1087 N NE  . ARG A 1 124 ? 24.849  2.961   -0.029  1.00 29.85 ? 124 ARG A NE  1 
ATOM   1088 C CZ  . ARG A 1 124 ? 25.771  2.747   0.908   1.00 26.68 ? 124 ARG A CZ  1 
ATOM   1089 N NH1 . ARG A 1 124 ? 26.640  3.700   1.217   1.00 24.54 ? 124 ARG A NH1 1 
ATOM   1090 N NH2 . ARG A 1 124 ? 25.830  1.579   1.532   1.00 26.50 ? 124 ARG A NH2 1 
ATOM   1091 N N   . GLU A 1 125 ? 24.623  8.495   1.730   1.00 23.84 ? 125 GLU A N   1 
ATOM   1092 C CA  . GLU A 1 125 ? 25.206  8.582   3.066   1.00 28.29 ? 125 GLU A CA  1 
ATOM   1093 C C   . GLU A 1 125 ? 24.262  9.294   4.026   1.00 31.09 ? 125 GLU A C   1 
ATOM   1094 O O   . GLU A 1 125 ? 24.160  8.919   5.201   1.00 30.54 ? 125 GLU A O   1 
ATOM   1095 C CB  . GLU A 1 125 ? 26.561  9.288   2.999   1.00 33.99 ? 125 GLU A CB  1 
ATOM   1096 C CG  . GLU A 1 125 ? 27.691  8.434   2.405   1.00 47.36 ? 125 GLU A CG  1 
ATOM   1097 C CD  . GLU A 1 125 ? 27.359  7.849   1.030   1.00 54.35 ? 125 GLU A CD  1 
ATOM   1098 O OE1 . GLU A 1 125 ? 26.845  8.593   0.157   1.00 48.27 ? 125 GLU A OE1 1 
ATOM   1099 O OE2 . GLU A 1 125 ? 27.609  6.637   0.831   1.00 57.22 ? 125 GLU A OE2 1 
ATOM   1100 N N   . GLU A 1 126 ? 23.545  10.307  3.533   1.00 25.16 ? 126 GLU A N   1 
ATOM   1101 C CA  . GLU A 1 126 ? 22.600  11.034  4.376   1.00 27.33 ? 126 GLU A CA  1 
ATOM   1102 C C   . GLU A 1 126 ? 21.395  10.172  4.733   1.00 26.95 ? 126 GLU A C   1 
ATOM   1103 O O   . GLU A 1 126 ? 20.926  10.197  5.880   1.00 24.24 ? 126 GLU A O   1 
ATOM   1104 C CB  . GLU A 1 126 ? 22.168  12.325  3.674   1.00 29.22 ? 126 GLU A CB  1 
ATOM   1105 C CG  . GLU A 1 126 ? 23.240  13.409  3.712   1.00 32.05 ? 126 GLU A CG  1 
ATOM   1106 C CD  . GLU A 1 126 ? 23.165  14.365  2.537   1.00 35.71 ? 126 GLU A CD  1 
ATOM   1107 O OE1 . GLU A 1 126 ? 22.437  14.066  1.563   1.00 32.31 ? 126 GLU A OE1 1 
ATOM   1108 O OE2 . GLU A 1 126 ? 23.849  15.413  2.582   1.00 38.05 ? 126 GLU A OE2 1 
ATOM   1109 N N   . LEU A 1 127 ? 20.884  9.399   3.769   1.00 23.72 ? 127 LEU A N   1 
ATOM   1110 C CA  . LEU A 1 127 ? 19.780  8.486   4.064   1.00 20.57 ? 127 LEU A CA  1 
ATOM   1111 C C   . LEU A 1 127 ? 20.204  7.404   5.049   1.00 27.34 ? 127 LEU A C   1 
ATOM   1112 O O   . LEU A 1 127 ? 19.416  7.006   5.918   1.00 22.19 ? 127 LEU A O   1 
ATOM   1113 C CB  . LEU A 1 127 ? 19.254  7.851   2.782   1.00 21.28 ? 127 LEU A CB  1 
ATOM   1114 C CG  . LEU A 1 127 ? 18.384  8.745   1.901   1.00 32.32 ? 127 LEU A CG  1 
ATOM   1115 C CD1 . LEU A 1 127 ? 18.280  8.157   0.495   1.00 24.54 ? 127 LEU A CD1 1 
ATOM   1116 C CD2 . LEU A 1 127 ? 17.000  8.945   2.534   1.00 34.95 ? 127 LEU A CD2 1 
ATOM   1117 N N   . LEU A 1 128 ? 21.439  6.904   4.921   1.00 19.84 ? 128 LEU A N   1 
ATOM   1118 C CA  . LEU A 1 128 ? 21.948  5.959   5.915   1.00 22.19 ? 128 LEU A CA  1 
ATOM   1119 C C   . LEU A 1 128 ? 21.896  6.554   7.315   1.00 17.93 ? 128 LEU A C   1 
ATOM   1120 O O   . LEU A 1 128 ? 21.510  5.876   8.278   1.00 20.64 ? 128 LEU A O   1 
ATOM   1121 C CB  . LEU A 1 128 ? 23.378  5.547   5.571   1.00 21.28 ? 128 LEU A CB  1 
ATOM   1122 C CG  . LEU A 1 128 ? 23.519  4.226   4.826   1.00 21.86 ? 128 LEU A CG  1 
ATOM   1123 C CD1 . LEU A 1 128 ? 24.980  3.959   4.470   1.00 23.88 ? 128 LEU A CD1 1 
ATOM   1124 C CD2 . LEU A 1 128 ? 22.944  3.108   5.662   1.00 21.45 ? 128 LEU A CD2 1 
ATOM   1125 N N   . ASP A 1 129 ? 22.273  7.826   7.446   1.00 24.97 ? 129 ASP A N   1 
ATOM   1126 C CA  . ASP A 1 129 ? 22.210  8.485   8.747   1.00 26.75 ? 129 ASP A CA  1 
ATOM   1127 C C   . ASP A 1 129 ? 20.770  8.637   9.212   1.00 27.30 ? 129 ASP A C   1 
ATOM   1128 O O   . ASP A 1 129 ? 20.466  8.433   10.396  1.00 24.18 ? 129 ASP A O   1 
ATOM   1129 C CB  . ASP A 1 129 ? 22.904  9.846   8.681   1.00 22.98 ? 129 ASP A CB  1 
ATOM   1130 C CG  . ASP A 1 129 ? 24.418  9.726   8.723   1.00 30.62 ? 129 ASP A CG  1 
ATOM   1131 O OD1 . ASP A 1 129 ? 24.917  8.584   8.656   1.00 28.03 ? 129 ASP A OD1 1 
ATOM   1132 O OD2 . ASP A 1 129 ? 25.105  10.765  8.832   1.00 30.74 ? 129 ASP A OD2 1 
ATOM   1133 N N   . LEU A 1 130 ? 19.865  8.986   8.292   1.00 22.37 ? 130 LEU A N   1 
ATOM   1134 C CA  . LEU A 1 130 ? 18.462  9.122   8.666   1.00 21.62 ? 130 LEU A CA  1 
ATOM   1135 C C   . LEU A 1 130 ? 17.889  7.791   9.126   1.00 17.11 ? 130 LEU A C   1 
ATOM   1136 O O   . LEU A 1 130 ? 17.127  7.737   10.102  1.00 19.28 ? 130 LEU A O   1 
ATOM   1137 C CB  . LEU A 1 130 ? 17.655  9.686   7.495   1.00 23.94 ? 130 LEU A CB  1 
ATOM   1138 C CG  . LEU A 1 130 ? 16.256  10.176  7.851   1.00 27.76 ? 130 LEU A CG  1 
ATOM   1139 C CD1 . LEU A 1 130 ? 16.310  11.239  8.944   1.00 30.22 ? 130 LEU A CD1 1 
ATOM   1140 C CD2 . LEU A 1 130 ? 15.559  10.712  6.599   1.00 22.93 ? 130 LEU A CD2 1 
ATOM   1141 N N   . GLN A 1 131 ? 18.242  6.707   8.431   1.00 18.22 ? 131 GLN A N   1 
ATOM   1142 C CA  . GLN A 1 131 ? 17.745  5.383   8.795   1.00 16.34 ? 131 GLN A CA  1 
ATOM   1143 C C   . GLN A 1 131 ? 18.265  4.955   10.163  1.00 20.29 ? 131 GLN A C   1 
ATOM   1144 O O   . GLN A 1 131 ? 17.506  4.469   11.013  1.00 19.10 ? 131 GLN A O   1 
ATOM   1145 C CB  . GLN A 1 131 ? 18.169  4.362   7.746   1.00 13.47 ? 131 GLN A CB  1 
ATOM   1146 C CG  . GLN A 1 131 ? 17.508  4.482   6.373   1.00 14.86 ? 131 GLN A CG  1 
ATOM   1147 C CD  . GLN A 1 131 ? 18.189  3.548   5.407   1.00 21.78 ? 131 GLN A CD  1 
ATOM   1148 O OE1 . GLN A 1 131 ? 19.411  3.421   5.437   1.00 17.63 ? 131 GLN A OE1 1 
ATOM   1149 N NE2 . GLN A 1 131 ? 17.409  2.843   4.589   1.00 17.28 ? 131 GLN A NE2 1 
ATOM   1150 N N   . THR A 1 132 ? 19.567  5.115   10.382  1.00 21.20 ? 132 THR A N   1 
ATOM   1151 C CA  . THR A 1 132 ? 20.175  4.649   11.622  1.00 17.10 ? 132 THR A CA  1 
ATOM   1152 C C   . THR A 1 132 ? 19.782  5.529   12.805  1.00 17.76 ? 132 THR A C   1 
ATOM   1153 O O   . THR A 1 132 ? 19.573  5.025   13.912  1.00 21.54 ? 132 THR A O   1 
ATOM   1154 C CB  . THR A 1 132 ? 21.693  4.603   11.469  1.00 15.73 ? 132 THR A CB  1 
ATOM   1155 O OG1 . THR A 1 132 ? 22.024  3.953   10.238  1.00 20.27 ? 132 THR A OG1 1 
ATOM   1156 C CG2 . THR A 1 132 ? 22.328  3.836   12.631  1.00 16.20 ? 132 THR A CG2 1 
ATOM   1157 N N   . LEU A 1 133 ? 19.697  6.845   12.600  1.00 18.31 ? 133 LEU A N   1 
ATOM   1158 C CA  . LEU A 1 133 ? 19.320  7.718   13.709  1.00 18.98 ? 133 LEU A CA  1 
ATOM   1159 C C   . LEU A 1 133 ? 17.870  7.499   14.124  1.00 21.26 ? 133 LEU A C   1 
ATOM   1160 O O   . LEU A 1 133 ? 17.556  7.588   15.316  1.00 20.63 ? 133 LEU A O   1 
ATOM   1161 C CB  . LEU A 1 133 ? 19.568  9.184   13.349  1.00 22.33 ? 133 LEU A CB  1 
ATOM   1162 C CG  . LEU A 1 133 ? 21.058  9.577   13.342  1.00 28.60 ? 133 LEU A CG  1 
ATOM   1163 C CD1 . LEU A 1 133 ? 21.265  11.018  12.886  1.00 30.61 ? 133 LEU A CD1 1 
ATOM   1164 C CD2 . LEU A 1 133 ? 21.697  9.351   14.707  1.00 19.38 ? 133 LEU A CD2 1 
ATOM   1165 N N   . ASN A 1 134 ? 16.973  7.209   13.171  1.00 19.43 ? 134 ASN A N   1 
ATOM   1166 C CA  . ASN A 1 134 ? 15.618  6.822   13.558  1.00 19.35 ? 134 ASN A CA  1 
ATOM   1167 C C   . ASN A 1 134 ? 15.646  5.578   14.438  1.00 16.47 ? 134 ASN A C   1 
ATOM   1168 O O   . ASN A 1 134 ? 14.951  5.517   15.461  1.00 21.18 ? 134 ASN A O   1 
ATOM   1169 C CB  . ASN A 1 134 ? 14.746  6.601   12.321  1.00 15.38 ? 134 ASN A CB  1 
ATOM   1170 C CG  . ASN A 1 134 ? 14.033  7.858   11.889  1.00 20.04 ? 134 ASN A CG  1 
ATOM   1171 O OD1 . ASN A 1 134 ? 12.949  8.180   12.387  1.00 20.12 ? 134 ASN A OD1 1 
ATOM   1172 N ND2 . ASN A 1 134 ? 14.636  8.586   10.957  1.00 18.34 ? 134 ASN A ND2 1 
ATOM   1173 N N   . LEU A 1 135 ? 16.486  4.600   14.085  1.00 13.84 ? 135 LEU A N   1 
ATOM   1174 C CA  . LEU A 1 135 ? 16.656  3.406   14.909  1.00 20.61 ? 135 LEU A CA  1 
ATOM   1175 C C   . LEU A 1 135 ? 17.196  3.744   16.295  1.00 20.34 ? 135 LEU A C   1 
ATOM   1176 O O   . LEU A 1 135 ? 16.693  3.249   17.312  1.00 19.94 ? 135 LEU A O   1 
ATOM   1177 C CB  . LEU A 1 135 ? 17.606  2.431   14.215  1.00 26.84 ? 135 LEU A CB  1 
ATOM   1178 C CG  . LEU A 1 135 ? 17.068  1.338   13.303  1.00 25.38 ? 135 LEU A CG  1 
ATOM   1179 C CD1 . LEU A 1 135 ? 18.229  0.430   12.877  1.00 23.24 ? 135 LEU A CD1 1 
ATOM   1180 C CD2 . LEU A 1 135 ? 15.939  0.546   13.977  1.00 23.60 ? 135 LEU A CD2 1 
ATOM   1181 N N   . LEU A 1 136 ? 18.256  4.554   16.353  1.00 24.47 ? 136 LEU A N   1 
ATOM   1182 C CA  . LEU A 1 136 ? 18.909  4.826   17.630  1.00 21.63 ? 136 LEU A CA  1 
ATOM   1183 C C   . LEU A 1 136 ? 18.058  5.715   18.522  1.00 20.33 ? 136 LEU A C   1 
ATOM   1184 O O   . LEU A 1 136 ? 18.189  5.665   19.753  1.00 22.17 ? 136 LEU A O   1 
ATOM   1185 C CB  . LEU A 1 136 ? 20.271  5.473   17.391  1.00 22.23 ? 136 LEU A CB  1 
ATOM   1186 C CG  . LEU A 1 136 ? 21.351  4.532   16.871  1.00 24.01 ? 136 LEU A CG  1 
ATOM   1187 C CD1 . LEU A 1 136 ? 22.632  5.308   16.547  1.00 22.33 ? 136 LEU A CD1 1 
ATOM   1188 C CD2 . LEU A 1 136 ? 21.610  3.410   17.872  1.00 20.60 ? 136 LEU A CD2 1 
ATOM   1189 N N   . ALA A 1 137 ? 17.197  6.542   17.927  1.00 19.07 ? 137 ALA A N   1 
ATOM   1190 C CA  . ALA A 1 137 ? 16.312  7.380   18.730  1.00 21.57 ? 137 ALA A CA  1 
ATOM   1191 C C   . ALA A 1 137 ? 15.450  6.549   19.667  1.00 20.63 ? 137 ALA A C   1 
ATOM   1192 O O   . ALA A 1 137 ? 15.037  7.044   20.720  1.00 14.81 ? 137 ALA A O   1 
ATOM   1193 C CB  . ALA A 1 137 ? 15.430  8.236   17.826  1.00 22.60 ? 137 ALA A CB  1 
ATOM   1194 N N   . TRP A 1 138 ? 15.190  5.283   19.318  1.00 15.15 ? 138 TRP A N   1 
ATOM   1195 C CA  . TRP A 1 138 ? 14.334  4.396   20.096  1.00 17.90 ? 138 TRP A CA  1 
ATOM   1196 C C   . TRP A 1 138 ? 15.126  3.409   20.956  1.00 18.99 ? 138 TRP A C   1 
ATOM   1197 O O   . TRP A 1 138 ? 14.553  2.433   21.447  1.00 20.26 ? 138 TRP A O   1 
ATOM   1198 C CB  . TRP A 1 138 ? 13.362  3.655   19.167  1.00 18.72 ? 138 TRP A CB  1 
ATOM   1199 C CG  . TRP A 1 138 ? 12.404  4.601   18.473  1.00 18.11 ? 138 TRP A CG  1 
ATOM   1200 C CD1 . TRP A 1 138 ? 12.598  5.226   17.276  1.00 17.83 ? 138 TRP A CD1 1 
ATOM   1201 C CD2 . TRP A 1 138 ? 11.129  5.052   18.954  1.00 17.24 ? 138 TRP A CD2 1 
ATOM   1202 N NE1 . TRP A 1 138 ? 11.531  6.033   16.979  1.00 16.87 ? 138 TRP A NE1 1 
ATOM   1203 C CE2 . TRP A 1 138 ? 10.613  5.947   17.993  1.00 16.88 ? 138 TRP A CE2 1 
ATOM   1204 C CE3 . TRP A 1 138 ? 10.374  4.790   20.099  1.00 16.44 ? 138 TRP A CE3 1 
ATOM   1205 C CZ2 . TRP A 1 138 ? 9.374   6.571   18.138  1.00 19.40 ? 138 TRP A CZ2 1 
ATOM   1206 C CZ3 . TRP A 1 138 ? 9.143   5.429   20.249  1.00 20.72 ? 138 TRP A CZ3 1 
ATOM   1207 C CH2 . TRP A 1 138 ? 8.657   6.302   19.274  1.00 14.93 ? 138 TRP A CH2 1 
ATOM   1208 N N   . CYS A 1 139 ? 16.427  3.648   21.147  1.00 17.51 ? 139 CYS A N   1 
ATOM   1209 C CA  . CYS A 1 139 ? 17.253  2.773   21.971  1.00 15.81 ? 139 CYS A CA  1 
ATOM   1210 C C   . CYS A 1 139 ? 16.720  2.711   23.397  1.00 17.84 ? 139 CYS A C   1 
ATOM   1211 O O   . CYS A 1 139 ? 16.422  3.743   24.004  1.00 16.93 ? 139 CYS A O   1 
ATOM   1212 C CB  . CYS A 1 139 ? 18.702  3.271   21.982  1.00 18.95 ? 139 CYS A CB  1 
ATOM   1213 S SG  . CYS A 1 139 ? 19.867  2.080   22.697  1.00 23.69 ? 139 CYS A SG  1 
ATOM   1214 N N   . GLY A 1 140 ? 16.563  1.492   23.912  1.00 18.00 ? 140 GLY A N   1 
ATOM   1215 C CA  . GLY A 1 140 ? 16.113  1.314   25.276  1.00 15.01 ? 140 GLY A CA  1 
ATOM   1216 C C   . GLY A 1 140 ? 17.251  1.465   26.267  1.00 17.45 ? 140 GLY A C   1 
ATOM   1217 O O   . GLY A 1 140 ? 18.420  1.510   25.893  1.00 15.97 ? 140 GLY A O   1 
ATOM   1218 N N   . ARG A 1 141 ? 16.877  1.524   27.550  1.00 17.90 ? 141 ARG A N   1 
ATOM   1219 C CA  . ARG A 1 141 ? 17.849  1.773   28.613  1.00 16.75 ? 141 ARG A CA  1 
ATOM   1220 C C   . ARG A 1 141 ? 18.981  0.749   28.595  1.00 18.32 ? 141 ARG A C   1 
ATOM   1221 O O   . ARG A 1 141 ? 20.156  1.120   28.693  1.00 17.25 ? 141 ARG A O   1 
ATOM   1222 C CB  . ARG A 1 141 ? 17.128  1.771   29.965  1.00 16.73 ? 141 ARG A CB  1 
ATOM   1223 C CG  . ARG A 1 141 ? 18.036  1.808   31.200  1.00 15.03 ? 141 ARG A CG  1 
ATOM   1224 C CD  . ARG A 1 141 ? 17.180  2.014   32.445  1.00 21.30 ? 141 ARG A CD  1 
ATOM   1225 N NE  . ARG A 1 141 ? 17.922  1.848   33.692  1.00 20.50 ? 141 ARG A NE  1 
ATOM   1226 C CZ  . ARG A 1 141 ? 18.026  0.697   34.344  1.00 20.91 ? 141 ARG A CZ  1 
ATOM   1227 N NH1 . ARG A 1 141 ? 17.449  -0.403  33.878  1.00 17.79 ? 141 ARG A NH1 1 
ATOM   1228 N NH2 . ARG A 1 141 ? 18.717  0.645   35.462  1.00 22.91 ? 141 ARG A NH2 1 
ATOM   1229 N N   . THR A 1 142 ? 18.644  -0.538  28.455  1.00 20.70 ? 142 THR A N   1 
ATOM   1230 C CA  . THR A 1 142 ? 19.644  -1.608  28.513  1.00 21.11 ? 142 THR A CA  1 
ATOM   1231 C C   . THR A 1 142 ? 20.705  -1.447  27.430  1.00 22.06 ? 142 THR A C   1 
ATOM   1232 O O   . THR A 1 142 ? 21.902  -1.611  27.683  1.00 19.61 ? 142 THR A O   1 
ATOM   1233 C CB  . THR A 1 142 ? 18.967  -2.972  28.360  1.00 23.32 ? 142 THR A CB  1 
ATOM   1234 O OG1 . THR A 1 142 ? 18.168  -3.256  29.510  1.00 26.83 ? 142 THR A OG1 1 
ATOM   1235 C CG2 . THR A 1 142 ? 20.007  -4.085  28.170  1.00 26.68 ? 142 THR A CG2 1 
ATOM   1236 N N   . LEU A 1 143 ? 20.280  -1.140  26.205  1.00 18.58 ? 143 LEU A N   1 
ATOM   1237 C CA  . LEU A 1 143 ? 21.203  -1.110  25.078  1.00 21.88 ? 143 LEU A CA  1 
ATOM   1238 C C   . LEU A 1 143 ? 22.005  0.182   24.996  1.00 26.43 ? 143 LEU A C   1 
ATOM   1239 O O   . LEU A 1 143 ? 22.963  0.245   24.214  1.00 21.02 ? 143 LEU A O   1 
ATOM   1240 C CB  . LEU A 1 143 ? 20.434  -1.335  23.772  1.00 17.09 ? 143 LEU A CB  1 
ATOM   1241 C CG  . LEU A 1 143 ? 20.086  -2.796  23.492  1.00 18.60 ? 143 LEU A CG  1 
ATOM   1242 C CD1 . LEU A 1 143 ? 19.478  -2.943  22.108  1.00 15.07 ? 143 LEU A CD1 1 
ATOM   1243 C CD2 . LEU A 1 143 ? 21.327  -3.684  23.629  1.00 18.77 ? 143 LEU A CD2 1 
ATOM   1244 N N   . ARG A 1 144 ? 21.654  1.198   25.793  1.00 31.41 ? 144 ARG A N   1 
ATOM   1245 C CA  . ARG A 1 144 ? 22.364  2.471   25.745  1.00 31.40 ? 144 ARG A CA  1 
ATOM   1246 C C   . ARG A 1 144 ? 23.832  2.319   26.148  1.00 37.98 ? 144 ARG A C   1 
ATOM   1247 O O   . ARG A 1 144 ? 24.648  3.184   25.812  1.00 43.35 ? 144 ARG A O   1 
ATOM   1248 C CB  . ARG A 1 144 ? 21.634  3.504   26.616  1.00 33.48 ? 144 ARG A CB  1 
ATOM   1249 C CG  . ARG A 1 144 ? 20.265  3.879   26.042  1.00 42.67 ? 144 ARG A CG  1 
ATOM   1250 C CD  . ARG A 1 144 ? 19.764  5.270   26.453  1.00 52.42 ? 144 ARG A CD  1 
ATOM   1251 N NE  . ARG A 1 144 ? 18.839  5.800   25.439  1.00 53.11 ? 144 ARG A NE  1 
ATOM   1252 C CZ  . ARG A 1 144 ? 18.084  6.891   25.587  1.00 51.91 ? 144 ARG A CZ  1 
ATOM   1253 N NH1 . ARG A 1 144 ? 18.149  7.600   26.707  1.00 52.39 ? 144 ARG A NH1 1 
ATOM   1254 N NH2 . ARG A 1 144 ? 17.294  7.313   24.602  1.00 46.37 ? 144 ARG A NH2 1 
ATOM   1255 N N   . LYS A 1 145 ? 24.195  1.222   26.817  1.00 35.60 ? 145 LYS A N   1 
ATOM   1256 C CA  . LYS A 1 145 ? 25.594  0.955   27.140  1.00 38.76 ? 145 LYS A CA  1 
ATOM   1257 C C   . LYS A 1 145 ? 26.312  0.260   25.985  1.00 42.07 ? 145 LYS A C   1 
ATOM   1258 O O   . LYS A 1 145 ? 27.346  0.741   25.508  1.00 38.32 ? 145 LYS A O   1 
ATOM   1259 C CB  . LYS A 1 145 ? 25.689  0.113   28.418  1.00 46.24 ? 145 LYS A CB  1 
ATOM   1260 C CG  . LYS A 1 145 ? 27.108  -0.052  28.956  1.00 53.30 ? 145 LYS A CG  1 
ATOM   1261 C CD  . LYS A 1 145 ? 27.130  -0.743  30.323  1.00 57.79 ? 145 LYS A CD  1 
ATOM   1262 C CE  . LYS A 1 145 ? 26.914  0.243   31.468  1.00 59.19 ? 145 LYS A CE  1 
ATOM   1263 N NZ  . LYS A 1 145 ? 27.239  -0.358  32.798  1.00 58.83 ? 145 LYS A NZ  1 
ATOM   1264 N N   . ASP A 1 146 ? 25.760  -0.860  25.511  1.00 43.20 ? 146 ASP A N   1 
ATOM   1265 C CA  . ASP A 1 146 ? 26.387  -1.598  24.419  1.00 36.00 ? 146 ASP A CA  1 
ATOM   1266 C C   . ASP A 1 146 ? 26.472  -0.769  23.143  1.00 33.44 ? 146 ASP A C   1 
ATOM   1267 O O   . ASP A 1 146 ? 27.345  -1.015  22.304  1.00 30.80 ? 146 ASP A O   1 
ATOM   1268 C CB  . ASP A 1 146 ? 25.619  -2.896  24.159  1.00 41.52 ? 146 ASP A CB  1 
ATOM   1269 C CG  . ASP A 1 146 ? 25.387  -3.703  25.434  1.00 55.13 ? 146 ASP A CG  1 
ATOM   1270 O OD1 . ASP A 1 146 ? 24.448  -3.368  26.199  1.00 52.46 ? 146 ASP A OD1 1 
ATOM   1271 O OD2 . ASP A 1 146 ? 26.148  -4.667  25.672  1.00 57.02 ? 146 ASP A OD2 1 
ATOM   1272 N N   . LEU A 1 147 ? 25.585  0.211   22.975  1.00 24.00 ? 147 LEU A N   1 
ATOM   1273 C CA  . LEU A 1 147 ? 25.524  1.012   21.757  1.00 20.82 ? 147 LEU A CA  1 
ATOM   1274 C C   . LEU A 1 147 ? 26.056  2.424   21.953  1.00 22.79 ? 147 LEU A C   1 
ATOM   1275 O O   . LEU A 1 147 ? 25.908  3.258   21.055  1.00 21.74 ? 147 LEU A O   1 
ATOM   1276 C CB  . LEU A 1 147 ? 24.086  1.071   21.228  1.00 20.27 ? 147 LEU A CB  1 
ATOM   1277 C CG  . LEU A 1 147 ? 23.465  -0.255  20.778  1.00 19.68 ? 147 LEU A CG  1 
ATOM   1278 C CD1 . LEU A 1 147 ? 22.058  -0.050  20.181  1.00 20.91 ? 147 LEU A CD1 1 
ATOM   1279 C CD2 . LEU A 1 147 ? 24.374  -0.953  19.775  1.00 24.67 ? 147 LEU A CD2 1 
ATOM   1280 N N   . LYS A 1 148 ? 26.691  2.708   23.096  1.00 24.49 ? 148 LYS A N   1 
ATOM   1281 C CA  . LYS A 1 148 ? 27.172  4.060   23.364  1.00 22.04 ? 148 LYS A CA  1 
ATOM   1282 C C   . LYS A 1 148 ? 28.101  4.554   22.260  1.00 18.73 ? 148 LYS A C   1 
ATOM   1283 O O   . LYS A 1 148 ? 28.066  5.736   21.893  1.00 28.64 ? 148 LYS A O   1 
ATOM   1284 C CB  . LYS A 1 148 ? 27.887  4.106   24.717  1.00 16.02 ? 148 LYS A CB  1 
ATOM   1285 C CG  . LYS A 1 148 ? 28.309  5.510   25.141  1.00 28.71 ? 148 LYS A CG  1 
ATOM   1286 C CD  . LYS A 1 148 ? 28.772  5.525   26.595  1.00 32.74 ? 148 LYS A CD  1 
ATOM   1287 C CE  . LYS A 1 148 ? 29.476  6.828   26.961  1.00 39.27 ? 148 LYS A CE  1 
ATOM   1288 N NZ  . LYS A 1 148 ? 28.617  8.029   26.744  1.00 43.19 ? 148 LYS A NZ  1 
ATOM   1289 N N   . ASP A 1 149 ? 28.939  3.668   21.723  1.00 20.44 ? 149 ASP A N   1 
ATOM   1290 C CA  . ASP A 1 149 ? 29.853  4.059   20.653  1.00 20.89 ? 149 ASP A CA  1 
ATOM   1291 C C   . ASP A 1 149 ? 29.085  4.660   19.480  1.00 23.68 ? 149 ASP A C   1 
ATOM   1292 O O   . ASP A 1 149 ? 29.429  5.737   18.976  1.00 27.51 ? 149 ASP A O   1 
ATOM   1293 C CB  . ASP A 1 149 ? 30.675  2.853   20.184  1.00 29.69 ? 149 ASP A CB  1 
ATOM   1294 C CG  . ASP A 1 149 ? 31.598  2.298   21.261  1.00 38.95 ? 149 ASP A CG  1 
ATOM   1295 O OD1 . ASP A 1 149 ? 31.888  3.013   22.252  1.00 36.77 ? 149 ASP A OD1 1 
ATOM   1296 O OD2 . ASP A 1 149 ? 32.050  1.140   21.098  1.00 43.32 ? 149 ASP A OD2 1 
ATOM   1297 N N   . LEU A 1 150 ? 28.028  3.976   19.042  1.00 24.71 ? 150 LEU A N   1 
ATOM   1298 C CA  . LEU A 1 150 ? 27.258  4.439   17.889  1.00 26.89 ? 150 LEU A CA  1 
ATOM   1299 C C   . LEU A 1 150 ? 26.435  5.680   18.218  1.00 29.00 ? 150 LEU A C   1 
ATOM   1300 O O   . LEU A 1 150 ? 26.263  6.551   17.360  1.00 30.66 ? 150 LEU A O   1 
ATOM   1301 C CB  . LEU A 1 150 ? 26.366  3.308   17.392  1.00 24.22 ? 150 LEU A CB  1 
ATOM   1302 C CG  . LEU A 1 150 ? 27.129  2.173   16.704  1.00 27.39 ? 150 LEU A CG  1 
ATOM   1303 C CD1 . LEU A 1 150 ? 26.227  0.979   16.446  1.00 20.83 ? 150 LEU A CD1 1 
ATOM   1304 C CD2 . LEU A 1 150 ? 27.734  2.679   15.398  1.00 21.45 ? 150 LEU A CD2 1 
ATOM   1305 N N   . LEU A 1 151 ? 25.932  5.783   19.451  1.00 25.04 ? 151 LEU A N   1 
ATOM   1306 C CA  . LEU A 1 151 ? 25.141  6.944   19.844  1.00 20.96 ? 151 LEU A CA  1 
ATOM   1307 C C   . LEU A 1 151 ? 25.998  8.196   19.949  1.00 31.86 ? 151 LEU A C   1 
ATOM   1308 O O   . LEU A 1 151 ? 25.546  9.296   19.603  1.00 34.50 ? 151 LEU A O   1 
ATOM   1309 C CB  . LEU A 1 151 ? 24.453  6.684   21.185  1.00 21.15 ? 151 LEU A CB  1 
ATOM   1310 C CG  . LEU A 1 151 ? 23.338  5.652   21.148  1.00 24.97 ? 151 LEU A CG  1 
ATOM   1311 C CD1 . LEU A 1 151 ? 23.074  5.125   22.557  1.00 26.60 ? 151 LEU A CD1 1 
ATOM   1312 C CD2 . LEU A 1 151 ? 22.090  6.279   20.529  1.00 21.58 ? 151 LEU A CD2 1 
ATOM   1313 N N   . ASN A 1 152 ? 27.226  8.056   20.458  1.00 31.30 ? 152 ASN A N   1 
ATOM   1314 C CA  . ASN A 1 152 ? 28.119  9.205   20.538  1.00 36.05 ? 152 ASN A CA  1 
ATOM   1315 C C   . ASN A 1 152 ? 28.670  9.590   19.172  1.00 29.70 ? 152 ASN A C   1 
ATOM   1316 O O   . ASN A 1 152 ? 29.007  10.758  18.961  1.00 31.94 ? 152 ASN A O   1 
ATOM   1317 C CB  . ASN A 1 152 ? 29.267  8.924   21.506  1.00 42.62 ? 152 ASN A CB  1 
ATOM   1318 C CG  . ASN A 1 152 ? 28.830  8.955   22.960  1.00 49.31 ? 152 ASN A CG  1 
ATOM   1319 O OD1 . ASN A 1 152 ? 27.638  8.900   23.267  1.00 51.16 ? 152 ASN A OD1 1 
ATOM   1320 N ND2 . ASN A 1 152 ? 29.797  9.048   23.861  1.00 51.77 ? 152 ASN A ND2 1 
ATOM   1321 N N   . LYS A 1 153 ? 28.765  8.634   18.241  1.00 29.39 ? 153 LYS A N   1 
ATOM   1322 C CA  . LYS A 1 153 ? 29.239  8.940   16.891  1.00 32.81 ? 153 LYS A CA  1 
ATOM   1323 C C   . LYS A 1 153 ? 28.358  9.990   16.221  1.00 35.74 ? 153 LYS A C   1 
ATOM   1324 O O   . LYS A 1 153 ? 28.858  10.963  15.643  1.00 38.49 ? 153 LYS A O   1 
ATOM   1325 C CB  . LYS A 1 153 ? 29.291  7.662   16.054  1.00 33.26 ? 153 LYS A CB  1 
ATOM   1326 C CG  . LYS A 1 153 ? 29.794  7.860   14.610  1.00 33.89 ? 153 LYS A CG  1 
ATOM   1327 C CD  . LYS A 1 153 ? 29.682  6.560   13.820  1.00 31.44 ? 153 LYS A CD  1 
ATOM   1328 C CE  . LYS A 1 153 ? 30.519  6.581   12.550  1.00 34.33 ? 153 LYS A CE  1 
ATOM   1329 N NZ  . LYS A 1 153 ? 30.487  5.262   11.877  1.00 30.76 ? 153 LYS A NZ  1 
ATOM   1330 N N   . GLY A 1 154 ? 27.038  9.797   16.267  1.00 31.90 ? 154 GLY A N   1 
ATOM   1331 C CA  . GLY A 1 154 ? 26.092  10.816  15.854  1.00 31.02 ? 154 GLY A CA  1 
ATOM   1332 C C   . GLY A 1 154 ? 25.916  11.027  14.365  1.00 32.29 ? 154 GLY A C   1 
ATOM   1333 O O   . GLY A 1 154 ? 24.949  11.692  13.971  1.00 29.83 ? 154 GLY A O   1 
ATOM   1334 N N   . ARG A 1 155 ? 26.798  10.490  13.524  1.00 35.40 ? 155 ARG A N   1 
ATOM   1335 C CA  . ARG A 1 155 ? 26.768  10.762  12.092  1.00 39.46 ? 155 ARG A CA  1 
ATOM   1336 C C   . ARG A 1 155 ? 27.627  9.732   11.370  1.00 36.46 ? 155 ARG A C   1 
ATOM   1337 O O   . ARG A 1 155 ? 28.381  8.978   11.989  1.00 33.52 ? 155 ARG A O   1 
ATOM   1338 C CB  . ARG A 1 155 ? 27.271  12.176  11.793  1.00 44.53 ? 155 ARG A CB  1 
ATOM   1339 C CG  . ARG A 1 155 ? 28.706  12.394  12.251  1.00 47.08 ? 155 ARG A CG  1 
ATOM   1340 C CD  . ARG A 1 155 ? 29.010  13.862  12.472  1.00 49.56 ? 155 ARG A CD  1 
ATOM   1341 N NE  . ARG A 1 155 ? 28.543  14.669  11.354  1.00 52.53 ? 155 ARG A NE  1 
ATOM   1342 C CZ  . ARG A 1 155 ? 27.657  15.655  11.455  1.00 56.89 ? 155 ARG A CZ  1 
ATOM   1343 N NH1 . ARG A 1 155 ? 27.128  15.968  12.633  1.00 54.91 ? 155 ARG A NH1 1 
ATOM   1344 N NH2 . ARG A 1 155 ? 27.293  16.326  10.371  1.00 57.68 ? 155 ARG A NH2 1 
ATOM   1345 N N   . ASN A 1 156 ? 27.505  9.725   10.037  1.00 30.00 ? 156 ASN A N   1 
ATOM   1346 C CA  . ASN A 1 156 ? 28.342  8.905   9.153   1.00 32.38 ? 156 ASN A CA  1 
ATOM   1347 C C   . ASN A 1 156 ? 28.181  7.416   9.436   1.00 31.48 ? 156 ASN A C   1 
ATOM   1348 O O   . ASN A 1 156 ? 29.159  6.669   9.517   1.00 31.67 ? 156 ASN A O   1 
ATOM   1349 C CB  . ASN A 1 156 ? 29.816  9.310   9.243   1.00 42.31 ? 156 ASN A CB  1 
ATOM   1350 C CG  . ASN A 1 156 ? 30.050  10.744  8.825   1.00 51.11 ? 156 ASN A CG  1 
ATOM   1351 O OD1 . ASN A 1 156 ? 30.724  11.509  9.519   1.00 52.89 ? 156 ASN A OD1 1 
ATOM   1352 N ND2 . ASN A 1 156 ? 29.483  11.123  7.687   1.00 55.18 ? 156 ASN A ND2 1 
ATOM   1353 N N   . TYR A 1 157 ? 26.941  6.973   9.577   1.00 29.64 ? 157 TYR A N   1 
ATOM   1354 C CA  . TYR A 1 157 ? 26.700  5.562   9.814   1.00 20.07 ? 157 TYR A CA  1 
ATOM   1355 C C   . TYR A 1 157 ? 26.785  4.769   8.515   1.00 28.03 ? 157 TYR A C   1 
ATOM   1356 O O   . TYR A 1 157 ? 26.479  5.267   7.428   1.00 29.06 ? 157 TYR A O   1 
ATOM   1357 C CB  . TYR A 1 157 ? 25.342  5.353   10.473  1.00 25.27 ? 157 TYR A CB  1 
ATOM   1358 C CG  . TYR A 1 157 ? 25.231  6.016   11.828  1.00 23.48 ? 157 TYR A CG  1 
ATOM   1359 C CD1 . TYR A 1 157 ? 25.742  5.405   12.967  1.00 23.21 ? 157 TYR A CD1 1 
ATOM   1360 C CD2 . TYR A 1 157 ? 24.609  7.247   11.967  1.00 17.70 ? 157 TYR A CD2 1 
ATOM   1361 C CE1 . TYR A 1 157 ? 25.632  6.009   14.215  1.00 24.28 ? 157 TYR A CE1 1 
ATOM   1362 C CE2 . TYR A 1 157 ? 24.497  7.856   13.205  1.00 18.95 ? 157 TYR A CE2 1 
ATOM   1363 C CZ  . TYR A 1 157 ? 25.011  7.232   14.320  1.00 23.26 ? 157 TYR A CZ  1 
ATOM   1364 O OH  . TYR A 1 157 ? 24.896  7.846   15.543  1.00 24.50 ? 157 TYR A OH  1 
ATOM   1365 N N   . THR A 1 158 ? 27.204  3.520   8.649   1.00 25.84 ? 158 THR A N   1 
ATOM   1366 C CA  . THR A 1 158 ? 27.345  2.571   7.556   1.00 30.67 ? 158 THR A CA  1 
ATOM   1367 C C   . THR A 1 158 ? 26.232  1.534   7.616   1.00 27.09 ? 158 THR A C   1 
ATOM   1368 O O   . THR A 1 158 ? 25.578  1.353   8.645   1.00 25.69 ? 158 THR A O   1 
ATOM   1369 C CB  . THR A 1 158 ? 28.696  1.876   7.653   1.00 34.06 ? 158 THR A CB  1 
ATOM   1370 O OG1 . THR A 1 158 ? 28.838  1.410   8.993   1.00 37.26 ? 158 THR A OG1 1 
ATOM   1371 C CG2 . THR A 1 158 ? 29.839  2.828   7.343   1.00 26.60 ? 158 THR A CG2 1 
ATOM   1372 N N   . GLN A 1 159 ? 26.010  0.858   6.485   1.00 24.15 ? 159 GLN A N   1 
ATOM   1373 C CA  . GLN A 1 159 ? 25.006  -0.202  6.450   1.00 26.33 ? 159 GLN A CA  1 
ATOM   1374 C C   . GLN A 1 159 ? 25.342  -1.318  7.437   1.00 30.70 ? 159 GLN A C   1 
ATOM   1375 O O   . GLN A 1 159 ? 24.442  -1.887  8.059   1.00 20.44 ? 159 GLN A O   1 
ATOM   1376 C CB  . GLN A 1 159 ? 24.868  -0.748  5.023   1.00 27.19 ? 159 GLN A CB  1 
ATOM   1377 C CG  . GLN A 1 159 ? 23.877  -1.905  4.870   1.00 23.23 ? 159 GLN A CG  1 
ATOM   1378 C CD  . GLN A 1 159 ? 22.410  -1.465  4.855   1.00 27.80 ? 159 GLN A CD  1 
ATOM   1379 O OE1 . GLN A 1 159 ? 22.092  -0.302  4.594   1.00 26.65 ? 159 GLN A OE1 1 
ATOM   1380 N NE2 . GLN A 1 159 ? 21.514  -2.404  5.127   1.00 28.39 ? 159 GLN A NE2 1 
ATOM   1381 N N   . GLU A 1 160 ? 26.637  -1.629  7.587   1.00 24.07 ? 160 GLU A N   1 
ATOM   1382 C CA  . GLU A 1 160 ? 27.095  -2.627  8.552   1.00 25.61 ? 160 GLU A CA  1 
ATOM   1383 C C   . GLU A 1 160 ? 26.609  -2.297  9.958   1.00 23.28 ? 160 GLU A C   1 
ATOM   1384 O O   . GLU A 1 160 ? 26.106  -3.171  10.677  1.00 21.65 ? 160 GLU A O   1 
ATOM   1385 C CB  . GLU A 1 160 ? 28.636  -2.687  8.524   1.00 36.64 ? 160 GLU A CB  1 
ATOM   1386 C CG  . GLU A 1 160 ? 29.225  -1.352  8.956   1.00 48.96 ? 160 GLU A CG  1 
ATOM   1387 C CD  . GLU A 1 160 ? 30.721  -1.134  8.849   1.00 52.54 ? 160 GLU A CD  1 
ATOM   1388 O OE1 . GLU A 1 160 ? 31.404  -1.139  9.894   1.00 54.63 ? 160 GLU A OE1 1 
ATOM   1389 O OE2 . GLU A 1 160 ? 31.201  -0.850  7.731   1.00 60.46 ? 160 GLU A OE2 1 
ATOM   1390 N N   . GLU A 1 161 ? 26.780  -1.045  10.392  1.00 25.28 ? 161 GLU A N   1 
ATOM   1391 C CA  . GLU A 1 161 ? 26.463  -0.659  11.758  1.00 24.19 ? 161 GLU A CA  1 
ATOM   1392 C C   . GLU A 1 161 ? 24.961  -0.662  11.991  1.00 24.12 ? 161 GLU A C   1 
ATOM   1393 O O   . GLU A 1 161 ? 24.490  -1.125  13.037  1.00 22.20 ? 161 GLU A O   1 
ATOM   1394 C CB  . GLU A 1 161 ? 27.067  0.719   12.052  1.00 26.93 ? 161 GLU A CB  1 
ATOM   1395 C CG  . GLU A 1 161 ? 28.601  0.718   12.136  1.00 25.89 ? 161 GLU A CG  1 
ATOM   1396 C CD  . GLU A 1 161 ? 29.221  2.094   11.923  1.00 32.62 ? 161 GLU A CD  1 
ATOM   1397 O OE1 . GLU A 1 161 ? 28.491  3.049   11.592  1.00 30.51 ? 161 GLU A OE1 1 
ATOM   1398 O OE2 . GLU A 1 161 ? 30.457  2.218   12.070  1.00 43.22 ? 161 GLU A OE2 1 
ATOM   1399 N N   . LYS A 1 162 ? 24.195  -0.164  11.015  1.00 19.85 ? 162 LYS A N   1 
ATOM   1400 C CA  . LYS A 1 162 ? 22.740  -0.232  11.097  1.00 24.16 ? 162 LYS A CA  1 
ATOM   1401 C C   . LYS A 1 162 ? 22.264  -1.668  11.296  1.00 23.31 ? 162 LYS A C   1 
ATOM   1402 O O   . LYS A 1 162 ? 21.351  -1.922  12.093  1.00 20.95 ? 162 LYS A O   1 
ATOM   1403 C CB  . LYS A 1 162 ? 22.119  0.377   9.835   1.00 20.54 ? 162 LYS A CB  1 
ATOM   1404 C CG  . LYS A 1 162 ? 20.605  0.313   9.789   1.00 18.16 ? 162 LYS A CG  1 
ATOM   1405 C CD  . LYS A 1 162 ? 20.066  0.988   8.532   1.00 21.84 ? 162 LYS A CD  1 
ATOM   1406 C CE  . LYS A 1 162 ? 20.390  0.180   7.282   1.00 21.47 ? 162 LYS A CE  1 
ATOM   1407 N NZ  . LYS A 1 162 ? 19.855  0.828   6.035   1.00 22.33 ? 162 LYS A NZ  1 
ATOM   1408 N N   . GLU A 1 163 ? 22.863  -2.621  10.571  1.00 22.48 ? 163 GLU A N   1 
ATOM   1409 C CA  . GLU A 1 163 ? 22.478  -4.022  10.719  1.00 17.92 ? 163 GLU A CA  1 
ATOM   1410 C C   . GLU A 1 163 ? 22.871  -4.562  12.086  1.00 21.56 ? 163 GLU A C   1 
ATOM   1411 O O   . GLU A 1 163 ? 22.188  -5.434  12.634  1.00 21.59 ? 163 GLU A O   1 
ATOM   1412 C CB  . GLU A 1 163 ? 23.112  -4.868  9.607   1.00 21.16 ? 163 GLU A CB  1 
ATOM   1413 C CG  . GLU A 1 163 ? 22.379  -4.747  8.268   1.00 28.21 ? 163 GLU A CG  1 
ATOM   1414 C CD  . GLU A 1 163 ? 23.230  -5.162  7.076   1.00 35.55 ? 163 GLU A CD  1 
ATOM   1415 O OE1 . GLU A 1 163 ? 24.379  -5.607  7.285   1.00 39.91 ? 163 GLU A OE1 1 
ATOM   1416 O OE2 . GLU A 1 163 ? 22.748  -5.034  5.930   1.00 35.83 ? 163 GLU A OE2 1 
ATOM   1417 N N   . TYR A 1 164 ? 23.967  -4.060  12.643  1.00 21.94 ? 164 TYR A N   1 
ATOM   1418 C CA  . TYR A 1 164 ? 24.332  -4.428  14.005  1.00 23.64 ? 164 TYR A CA  1 
ATOM   1419 C C   . TYR A 1 164 ? 23.271  -3.956  14.998  1.00 22.72 ? 164 TYR A C   1 
ATOM   1420 O O   . TYR A 1 164 ? 22.815  -4.727  15.849  1.00 23.60 ? 164 TYR A O   1 
ATOM   1421 C CB  . TYR A 1 164 ? 25.707  -3.844  14.338  1.00 26.37 ? 164 TYR A CB  1 
ATOM   1422 C CG  . TYR A 1 164 ? 26.123  -4.041  15.769  1.00 29.08 ? 164 TYR A CG  1 
ATOM   1423 C CD1 . TYR A 1 164 ? 26.539  -5.288  16.223  1.00 38.96 ? 164 TYR A CD1 1 
ATOM   1424 C CD2 . TYR A 1 164 ? 26.105  -2.986  16.669  1.00 30.18 ? 164 TYR A CD2 1 
ATOM   1425 C CE1 . TYR A 1 164 ? 26.921  -5.478  17.540  1.00 37.30 ? 164 TYR A CE1 1 
ATOM   1426 C CE2 . TYR A 1 164 ? 26.487  -3.165  17.986  1.00 34.56 ? 164 TYR A CE2 1 
ATOM   1427 C CZ  . TYR A 1 164 ? 26.893  -4.413  18.414  1.00 40.91 ? 164 TYR A CZ  1 
ATOM   1428 O OH  . TYR A 1 164 ? 27.271  -4.596  19.723  1.00 52.20 ? 164 TYR A OH  1 
ATOM   1429 N N   . VAL A 1 165 ? 22.846  -2.696  14.887  1.00 19.45 ? 165 VAL A N   1 
ATOM   1430 C CA  . VAL A 1 165 ? 21.806  -2.200  15.786  1.00 16.82 ? 165 VAL A CA  1 
ATOM   1431 C C   . VAL A 1 165 ? 20.541  -3.040  15.662  1.00 21.91 ? 165 VAL A C   1 
ATOM   1432 O O   . VAL A 1 165 ? 19.933  -3.413  16.672  1.00 19.21 ? 165 VAL A O   1 
ATOM   1433 C CB  . VAL A 1 165 ? 21.527  -0.707  15.525  1.00 16.52 ? 165 VAL A CB  1 
ATOM   1434 C CG1 . VAL A 1 165 ? 20.302  -0.245  16.350  1.00 16.39 ? 165 VAL A CG1 1 
ATOM   1435 C CG2 . VAL A 1 165 ? 22.753  0.109   15.860  1.00 22.12 ? 165 VAL A CG2 1 
ATOM   1436 N N   . LEU A 1 166 ? 20.138  -3.372  14.426  1.00 19.25 ? 166 LEU A N   1 
ATOM   1437 C CA  . LEU A 1 166 ? 18.932  -4.175  14.225  1.00 21.69 ? 166 LEU A CA  1 
ATOM   1438 C C   . LEU A 1 166 ? 19.060  -5.543  14.871  1.00 27.28 ? 166 LEU A C   1 
ATOM   1439 O O   . LEU A 1 166 ? 18.095  -6.057  15.453  1.00 24.87 ? 166 LEU A O   1 
ATOM   1440 C CB  . LEU A 1 166 ? 18.641  -4.340  12.733  1.00 22.26 ? 166 LEU A CB  1 
ATOM   1441 C CG  . LEU A 1 166 ? 18.007  -3.145  12.039  1.00 22.41 ? 166 LEU A CG  1 
ATOM   1442 C CD1 . LEU A 1 166 ? 18.089  -3.331  10.525  1.00 27.20 ? 166 LEU A CD1 1 
ATOM   1443 C CD2 . LEU A 1 166 ? 16.575  -2.968  12.499  1.00 22.69 ? 166 LEU A CD2 1 
ATOM   1444 N N   . ASN A 1 167 ? 20.238  -6.161  14.742  1.00 19.66 ? 167 ASN A N   1 
ATOM   1445 C CA  . ASN A 1 167 ? 20.504  -7.438  15.396  1.00 27.01 ? 167 ASN A CA  1 
ATOM   1446 C C   . ASN A 1 167 ? 20.288  -7.347  16.902  1.00 20.74 ? 167 ASN A C   1 
ATOM   1447 O O   . ASN A 1 167 ? 19.599  -8.190  17.495  1.00 23.57 ? 167 ASN A O   1 
ATOM   1448 C CB  . ASN A 1 167 ? 21.936  -7.881  15.086  1.00 30.77 ? 167 ASN A CB  1 
ATOM   1449 C CG  . ASN A 1 167 ? 22.235  -9.292  15.567  1.00 49.89 ? 167 ASN A CG  1 
ATOM   1450 O OD1 . ASN A 1 167 ? 21.326  -10.075 15.852  1.00 58.97 ? 167 ASN A OD1 1 
ATOM   1451 N ND2 . ASN A 1 167 ? 23.519  -9.626  15.654  1.00 55.89 ? 167 ASN A ND2 1 
ATOM   1452 N N   . LYS A 1 168 ? 20.896  -6.346  17.543  1.00 20.02 ? 168 LYS A N   1 
ATOM   1453 C CA  . LYS A 1 168 ? 20.754  -6.205  18.990  1.00 20.86 ? 168 LYS A CA  1 
ATOM   1454 C C   . LYS A 1 168 ? 19.305  -5.931  19.376  1.00 24.48 ? 168 LYS A C   1 
ATOM   1455 O O   . LYS A 1 168 ? 18.819  -6.439  20.393  1.00 21.33 ? 168 LYS A O   1 
ATOM   1456 C CB  . LYS A 1 168 ? 21.661  -5.086  19.500  1.00 18.19 ? 168 LYS A CB  1 
ATOM   1457 C CG  . LYS A 1 168 ? 23.133  -5.255  19.120  1.00 27.17 ? 168 LYS A CG  1 
ATOM   1458 C CD  . LYS A 1 168 ? 23.798  -6.306  19.994  1.00 33.24 ? 168 LYS A CD  1 
ATOM   1459 C CE  . LYS A 1 168 ? 23.888  -5.819  21.430  1.00 42.52 ? 168 LYS A CE  1 
ATOM   1460 N NZ  . LYS A 1 168 ? 24.443  -6.851  22.350  1.00 48.32 ? 168 LYS A NZ  1 
ATOM   1461 N N   . TYR A 1 169 ? 18.596  -5.135  18.567  1.00 18.86 ? 169 TYR A N   1 
ATOM   1462 C CA  . TYR A 1 169 ? 17.199  -4.813  18.863  1.00 20.16 ? 169 TYR A CA  1 
ATOM   1463 C C   . TYR A 1 169 ? 16.344  -6.070  18.878  1.00 20.81 ? 169 TYR A C   1 
ATOM   1464 O O   . TYR A 1 169 ? 15.562  -6.295  19.810  1.00 20.03 ? 169 TYR A O   1 
ATOM   1465 C CB  . TYR A 1 169 ? 16.655  -3.810  17.842  1.00 13.65 ? 169 TYR A CB  1 
ATOM   1466 C CG  . TYR A 1 169 ? 16.981  -2.371  18.149  1.00 17.56 ? 169 TYR A CG  1 
ATOM   1467 C CD1 . TYR A 1 169 ? 17.955  -2.036  19.085  1.00 14.70 ? 169 TYR A CD1 1 
ATOM   1468 C CD2 . TYR A 1 169 ? 16.313  -1.340  17.494  1.00 17.93 ? 169 TYR A CD2 1 
ATOM   1469 C CE1 . TYR A 1 169 ? 18.256  -0.702  19.358  1.00 16.64 ? 169 TYR A CE1 1 
ATOM   1470 C CE2 . TYR A 1 169 ? 16.602  -0.021  17.753  1.00 20.57 ? 169 TYR A CE2 1 
ATOM   1471 C CZ  . TYR A 1 169 ? 17.569  0.295   18.689  1.00 22.36 ? 169 TYR A CZ  1 
ATOM   1472 O OH  . TYR A 1 169 ? 17.840  1.619   18.945  1.00 19.15 ? 169 TYR A OH  1 
ATOM   1473 N N   . PHE A 1 170 ? 16.502  -6.921  17.866  1.00 22.68 ? 170 PHE A N   1 
ATOM   1474 C CA  . PHE A 1 170 ? 15.745  -8.164  17.853  1.00 24.01 ? 170 PHE A CA  1 
ATOM   1475 C C   . PHE A 1 170 ? 16.151  -9.081  19.000  1.00 18.96 ? 170 PHE A C   1 
ATOM   1476 O O   . PHE A 1 170 ? 15.314  -9.855  19.486  1.00 19.94 ? 170 PHE A O   1 
ATOM   1477 C CB  . PHE A 1 170 ? 15.900  -8.862  16.501  1.00 23.41 ? 170 PHE A CB  1 
ATOM   1478 C CG  . PHE A 1 170 ? 14.927  -8.363  15.452  1.00 26.55 ? 170 PHE A CG  1 
ATOM   1479 C CD1 . PHE A 1 170 ? 13.609  -8.813  15.434  1.00 25.14 ? 170 PHE A CD1 1 
ATOM   1480 C CD2 . PHE A 1 170 ? 15.325  -7.444  14.495  1.00 29.82 ? 170 PHE A CD2 1 
ATOM   1481 C CE1 . PHE A 1 170 ? 12.700  -8.356  14.471  1.00 25.20 ? 170 PHE A CE1 1 
ATOM   1482 C CE2 . PHE A 1 170 ? 14.429  -6.990  13.525  1.00 33.10 ? 170 PHE A CE2 1 
ATOM   1483 C CZ  . PHE A 1 170 ? 13.112  -7.446  13.517  1.00 28.25 ? 170 PHE A CZ  1 
ATOM   1484 N N   . GLU A 1 171 ? 17.408  -8.996  19.463  1.00 14.75 ? 171 GLU A N   1 
ATOM   1485 C CA  . GLU A 1 171 ? 17.806  -9.753  20.647  1.00 21.21 ? 171 GLU A CA  1 
ATOM   1486 C C   . GLU A 1 171 ? 16.981  -9.330  21.854  1.00 23.78 ? 171 GLU A C   1 
ATOM   1487 O O   . GLU A 1 171 ? 16.584  -10.171 22.670  1.00 17.20 ? 171 GLU A O   1 
ATOM   1488 C CB  . GLU A 1 171 ? 19.299  -9.561  20.923  1.00 27.79 ? 171 GLU A CB  1 
ATOM   1489 C CG  . GLU A 1 171 ? 20.216  -10.397 20.021  1.00 42.01 ? 171 GLU A CG  1 
ATOM   1490 C CD  . GLU A 1 171 ? 21.700  -10.131 20.254  1.00 48.43 ? 171 GLU A CD  1 
ATOM   1491 O OE1 . GLU A 1 171 ? 22.039  -9.400  21.210  1.00 46.69 ? 171 GLU A OE1 1 
ATOM   1492 O OE2 . GLU A 1 171 ? 22.527  -10.647 19.466  1.00 47.59 ? 171 GLU A OE2 1 
ATOM   1493 N N   . ILE A 1 172 ? 16.715  -8.024  21.973  1.00 15.09 ? 172 ILE A N   1 
ATOM   1494 C CA  . ILE A 1 172 ? 15.894  -7.501  23.065  1.00 18.56 ? 172 ILE A CA  1 
ATOM   1495 C C   . ILE A 1 172 ? 14.466  -8.026  22.957  1.00 20.03 ? 172 ILE A C   1 
ATOM   1496 O O   . ILE A 1 172 ? 13.868  -8.465  23.949  1.00 18.14 ? 172 ILE A O   1 
ATOM   1497 C CB  . ILE A 1 172 ? 15.946  -5.960  23.066  1.00 24.03 ? 172 ILE A CB  1 
ATOM   1498 C CG1 . ILE A 1 172 ? 17.297  -5.475  23.599  1.00 28.06 ? 172 ILE A CG1 1 
ATOM   1499 C CG2 . ILE A 1 172 ? 14.821  -5.368  23.908  1.00 23.86 ? 172 ILE A CG2 1 
ATOM   1500 C CD1 . ILE A 1 172 ? 17.599  -5.917  25.020  1.00 27.32 ? 172 ILE A CD1 1 
ATOM   1501 N N   . ILE A 1 173 ? 13.901  -8.010  21.747  1.00 19.18 ? 173 ILE A N   1 
ATOM   1502 C CA  . ILE A 1 173 ? 12.546  -8.516  21.558  1.00 18.60 ? 173 ILE A CA  1 
ATOM   1503 C C   . ILE A 1 173 ? 12.475  -10.002 21.895  1.00 19.60 ? 173 ILE A C   1 
ATOM   1504 O O   . ILE A 1 173 ? 11.508  -10.474 22.511  1.00 15.89 ? 173 ILE A O   1 
ATOM   1505 C CB  . ILE A 1 173 ? 12.078  -8.244  20.118  1.00 21.84 ? 173 ILE A CB  1 
ATOM   1506 C CG1 . ILE A 1 173 ? 12.043  -6.739  19.831  1.00 24.49 ? 173 ILE A CG1 1 
ATOM   1507 C CG2 . ILE A 1 173 ? 10.715  -8.865  19.877  1.00 22.60 ? 173 ILE A CG2 1 
ATOM   1508 C CD1 . ILE A 1 173 ? 11.733  -6.403  18.367  1.00 19.73 ? 173 ILE A CD1 1 
ATOM   1509 N N   . LYS A 1 174 ? 13.500  -10.764 21.501  1.00 20.26 ? 174 LYS A N   1 
ATOM   1510 C CA  . LYS A 1 174 ? 13.503  -12.195 21.786  1.00 17.81 ? 174 LYS A CA  1 
ATOM   1511 C C   . LYS A 1 174 ? 13.537  -12.479 23.285  1.00 21.01 ? 174 LYS A C   1 
ATOM   1512 O O   . LYS A 1 174 ? 13.080  -13.544 23.718  1.00 25.26 ? 174 LYS A O   1 
ATOM   1513 C CB  . LYS A 1 174 ? 14.693  -12.868 21.107  1.00 17.65 ? 174 LYS A CB  1 
ATOM   1514 C CG  . LYS A 1 174 ? 14.606  -12.942 19.571  1.00 24.40 ? 174 LYS A CG  1 
ATOM   1515 C CD  . LYS A 1 174 ? 15.931  -13.467 19.007  1.00 38.67 ? 174 LYS A CD  1 
ATOM   1516 C CE  . LYS A 1 174 ? 16.091  -13.199 17.517  1.00 48.71 ? 174 LYS A CE  1 
ATOM   1517 N NZ  . LYS A 1 174 ? 14.973  -13.764 16.715  1.00 52.58 ? 174 LYS A NZ  1 
ATOM   1518 N N   . LYS A 1 175 ? 14.075  -11.555 24.085  1.00 17.26 ? 175 LYS A N   1 
ATOM   1519 C CA  . LYS A 1 175 ? 14.174  -11.715 25.537  1.00 22.41 ? 175 LYS A CA  1 
ATOM   1520 C C   . LYS A 1 175 ? 12.997  -11.116 26.309  1.00 18.13 ? 175 LYS A C   1 
ATOM   1521 O O   . LYS A 1 175 ? 12.987  -11.177 27.546  1.00 14.09 ? 175 LYS A O   1 
ATOM   1522 C CB  . LYS A 1 175 ? 15.483  -11.091 26.028  1.00 25.25 ? 175 LYS A CB  1 
ATOM   1523 C CG  . LYS A 1 175 ? 16.676  -11.960 25.728  1.00 35.59 ? 175 LYS A CG  1 
ATOM   1524 C CD  . LYS A 1 175 ? 17.989  -11.172 25.547  1.00 45.76 ? 175 LYS A CD  1 
ATOM   1525 C CE  . LYS A 1 175 ? 18.244  -10.126 26.637  1.00 51.79 ? 175 LYS A CE  1 
ATOM   1526 N NZ  . LYS A 1 175 ? 19.675  -9.883  26.828  1.00 57.85 ? 175 LYS A NZ  1 
ATOM   1527 N N   . THR A 1 176 ? 11.994  -10.578 25.622  1.00 21.45 ? 176 THR A N   1 
ATOM   1528 C CA  . THR A 1 176 ? 11.001  -9.745  26.297  1.00 18.49 ? 176 THR A CA  1 
ATOM   1529 C C   . THR A 1 176 ? 10.015  -10.573 27.123  1.00 26.11 ? 176 THR A C   1 
ATOM   1530 O O   . THR A 1 176 ? 9.872   -10.350 28.329  1.00 19.25 ? 176 THR A O   1 
ATOM   1531 C CB  . THR A 1 176 ? 10.271  -8.876  25.273  1.00 15.30 ? 176 THR A CB  1 
ATOM   1532 O OG1 . THR A 1 176 ? 11.185  -7.905  24.758  1.00 16.18 ? 176 THR A OG1 1 
ATOM   1533 C CG2 . THR A 1 176 ? 9.098   -8.128  25.935  1.00 15.74 ? 176 THR A CG2 1 
ATOM   1534 N N   . LEU A 1 177 ? 9.327   -11.540 26.507  1.00 19.99 ? 177 LEU A N   1 
ATOM   1535 C CA  . LEU A 1 177 ? 8.388   -12.336 27.291  1.00 18.66 ? 177 LEU A CA  1 
ATOM   1536 C C   . LEU A 1 177 ? 9.096   -13.079 28.421  1.00 20.29 ? 177 LEU A C   1 
ATOM   1537 O O   . LEU A 1 177 ? 8.510   -13.286 29.495  1.00 18.13 ? 177 LEU A O   1 
ATOM   1538 C CB  . LEU A 1 177 ? 7.640   -13.311 26.389  1.00 20.14 ? 177 LEU A CB  1 
ATOM   1539 C CG  . LEU A 1 177 ? 6.770   -12.671 25.301  1.00 21.40 ? 177 LEU A CG  1 
ATOM   1540 C CD1 . LEU A 1 177 ? 6.065   -13.760 24.531  1.00 23.81 ? 177 LEU A CD1 1 
ATOM   1541 C CD2 . LEU A 1 177 ? 5.763   -11.692 25.896  1.00 24.70 ? 177 LEU A CD2 1 
ATOM   1542 N N   . SER A 1 178 ? 10.370  -13.431 28.223  1.00 20.55 ? 178 SER A N   1 
ATOM   1543 C CA  . SER A 1 178 ? 11.121  -14.109 29.276  1.00 21.61 ? 178 SER A CA  1 
ATOM   1544 C C   . SER A 1 178 ? 11.308  -13.231 30.507  1.00 22.25 ? 178 SER A C   1 
ATOM   1545 O O   . SER A 1 178 ? 11.295  -13.741 31.629  1.00 21.48 ? 178 SER A O   1 
ATOM   1546 C CB  . SER A 1 178 ? 12.478  -14.567 28.752  1.00 29.86 ? 178 SER A CB  1 
ATOM   1547 O OG  . SER A 1 178 ? 12.340  -15.825 28.120  1.00 37.10 ? 178 SER A OG  1 
ATOM   1548 N N   . ILE A 1 179 ? 11.512  -11.920 30.333  1.00 18.56 ? 179 ILE A N   1 
ATOM   1549 C CA  . ILE A 1 179 ? 11.705  -11.099 31.520  1.00 18.86 ? 179 ILE A CA  1 
ATOM   1550 C C   . ILE A 1 179 ? 10.403  -10.970 32.300  1.00 21.60 ? 179 ILE A C   1 
ATOM   1551 O O   . ILE A 1 179 ? 10.430  -10.841 33.527  1.00 20.77 ? 179 ILE A O   1 
ATOM   1552 C CB  . ILE A 1 179 ? 12.308  -9.720  31.188  1.00 19.83 ? 179 ILE A CB  1 
ATOM   1553 C CG1 . ILE A 1 179 ? 12.845  -9.077  32.471  1.00 28.03 ? 179 ILE A CG1 1 
ATOM   1554 C CG2 . ILE A 1 179 ? 11.296  -8.800  30.571  1.00 18.08 ? 179 ILE A CG2 1 
ATOM   1555 C CD1 . ILE A 1 179 ? 14.032  -8.184  32.257  1.00 29.35 ? 179 ILE A CD1 1 
ATOM   1556 N N   . TYR A 1 180 ? 9.246   -11.027 31.626  1.00 18.44 ? 180 TYR A N   1 
ATOM   1557 C CA  . TYR A 1 180 ? 7.983   -10.981 32.363  1.00 15.72 ? 180 TYR A CA  1 
ATOM   1558 C C   . TYR A 1 180 ? 7.746   -12.284 33.123  1.00 22.75 ? 180 TYR A C   1 
ATOM   1559 O O   . TYR A 1 180 ? 7.247   -12.263 34.254  1.00 17.87 ? 180 TYR A O   1 
ATOM   1560 C CB  . TYR A 1 180 ? 6.813   -10.674 31.414  1.00 17.56 ? 180 TYR A CB  1 
ATOM   1561 C CG  . TYR A 1 180 ? 6.757   -9.227  30.947  1.00 17.50 ? 180 TYR A CG  1 
ATOM   1562 C CD1 . TYR A 1 180 ? 6.273   -8.215  31.782  1.00 15.81 ? 180 TYR A CD1 1 
ATOM   1563 C CD2 . TYR A 1 180 ? 7.216   -8.872  29.688  1.00 15.87 ? 180 TYR A CD2 1 
ATOM   1564 C CE1 . TYR A 1 180 ? 6.236   -6.873  31.350  1.00 11.75 ? 180 TYR A CE1 1 
ATOM   1565 C CE2 . TYR A 1 180 ? 7.182   -7.557  29.254  1.00 9.92  ? 180 TYR A CE2 1 
ATOM   1566 C CZ  . TYR A 1 180 ? 6.696   -6.565  30.091  1.00 9.50  ? 180 TYR A CZ  1 
ATOM   1567 O OH  . TYR A 1 180 ? 6.672   -5.264  29.639  1.00 16.01 ? 180 TYR A OH  1 
ATOM   1568 N N   . ARG A 1 181 ? 8.096   -13.430 32.523  1.00 19.31 ? 181 ARG A N   1 
ATOM   1569 C CA  . ARG A 1 181 ? 8.014   -14.694 33.258  1.00 20.85 ? 181 ARG A CA  1 
ATOM   1570 C C   . ARG A 1 181 ? 8.911   -14.671 34.485  1.00 20.00 ? 181 ARG A C   1 
ATOM   1571 O O   . ARG A 1 181 ? 8.548   -15.194 35.547  1.00 22.77 ? 181 ARG A O   1 
ATOM   1572 C CB  . ARG A 1 181 ? 8.413   -15.873 32.365  1.00 24.51 ? 181 ARG A CB  1 
ATOM   1573 C CG  . ARG A 1 181 ? 7.467   -16.191 31.228  1.00 27.18 ? 181 ARG A CG  1 
ATOM   1574 C CD  . ARG A 1 181 ? 7.982   -17.395 30.442  1.00 20.91 ? 181 ARG A CD  1 
ATOM   1575 N NE  . ARG A 1 181 ? 7.321   -17.500 29.147  1.00 28.61 ? 181 ARG A NE  1 
ATOM   1576 C CZ  . ARG A 1 181 ? 7.898   -17.197 27.987  1.00 31.91 ? 181 ARG A CZ  1 
ATOM   1577 N NH1 . ARG A 1 181 ? 9.161   -16.793 27.959  1.00 39.28 ? 181 ARG A NH1 1 
ATOM   1578 N NH2 . ARG A 1 181 ? 7.217   -17.314 26.853  1.00 37.37 ? 181 ARG A NH2 1 
ATOM   1579 N N   . GLU A 1 182 ? 10.089  -14.064 34.353  1.00 15.23 ? 182 GLU A N   1 
ATOM   1580 C CA  . GLU A 1 182 ? 11.060  -14.060 35.439  1.00 18.50 ? 182 GLU A CA  1 
ATOM   1581 C C   . GLU A 1 182 ? 10.588  -13.214 36.615  1.00 26.57 ? 182 GLU A C   1 
ATOM   1582 O O   . GLU A 1 182 ? 10.628  -13.670 37.763  1.00 26.74 ? 182 GLU A O   1 
ATOM   1583 C CB  . GLU A 1 182 ? 12.408  -13.560 34.930  1.00 19.84 ? 182 GLU A CB  1 
ATOM   1584 C CG  . GLU A 1 182 ? 13.418  -13.299 36.027  1.00 31.52 ? 182 GLU A CG  1 
ATOM   1585 C CD  . GLU A 1 182 ? 14.725  -12.750 35.500  1.00 42.57 ? 182 GLU A CD  1 
ATOM   1586 O OE1 . GLU A 1 182 ? 15.656  -12.565 36.309  1.00 47.35 ? 182 GLU A OE1 1 
ATOM   1587 O OE2 . GLU A 1 182 ? 14.827  -12.508 34.278  1.00 40.27 ? 182 GLU A OE2 1 
ATOM   1588 N N   . ILE A 1 183 ? 10.161  -11.966 36.358  1.00 25.70 ? 183 ILE A N   1 
ATOM   1589 C CA  . ILE A 1 183 ? 9.730   -11.108 37.464  1.00 17.18 ? 183 ILE A CA  1 
ATOM   1590 C C   . ILE A 1 183 ? 8.516   -11.703 38.166  1.00 21.00 ? 183 ILE A C   1 
ATOM   1591 O O   . ILE A 1 183 ? 8.345   -11.539 39.383  1.00 23.65 ? 183 ILE A O   1 
ATOM   1592 C CB  . ILE A 1 183 ? 9.454   -9.665  36.977  1.00 24.43 ? 183 ILE A CB  1 
ATOM   1593 C CG1 . ILE A 1 183 ? 8.194   -9.597  36.104  1.00 25.34 ? 183 ILE A CG1 1 
ATOM   1594 C CG2 . ILE A 1 183 ? 10.657  -9.087  36.238  1.00 20.59 ? 183 ILE A CG2 1 
ATOM   1595 C CD1 . ILE A 1 183 ? 7.423   -8.296  36.265  1.00 31.15 ? 183 ILE A CD1 1 
ATOM   1596 N N   . LYS A 1 184 ? 7.652   -12.394 37.419  1.00 17.66 ? 184 LYS A N   1 
ATOM   1597 C CA  . LYS A 1 184 ? 6.523   -13.084 38.034  1.00 18.25 ? 184 LYS A CA  1 
ATOM   1598 C C   . LYS A 1 184 ? 7.003   -14.247 38.896  1.00 27.19 ? 184 LYS A C   1 
ATOM   1599 O O   . LYS A 1 184 ? 6.471   -14.483 39.991  1.00 22.59 ? 184 LYS A O   1 
ATOM   1600 C CB  . LYS A 1 184 ? 5.584   -13.564 36.936  1.00 18.68 ? 184 LYS A CB  1 
ATOM   1601 C CG  . LYS A 1 184 ? 4.240   -14.110 37.381  1.00 34.77 ? 184 LYS A CG  1 
ATOM   1602 C CD  . LYS A 1 184 ? 3.685   -14.977 36.266  1.00 36.50 ? 184 LYS A CD  1 
ATOM   1603 C CE  . LYS A 1 184 ? 2.220   -15.310 36.448  1.00 34.66 ? 184 LYS A CE  1 
ATOM   1604 N NZ  . LYS A 1 184 ? 1.818   -15.542 37.860  1.00 42.43 ? 184 LYS A NZ  1 
ATOM   1605 N N   . GLU A 1 185 ? 8.023   -14.963 38.413  1.00 24.52 ? 185 GLU A N   1 
ATOM   1606 C CA  . GLU A 1 185 ? 8.597   -16.112 39.110  1.00 29.36 ? 185 GLU A CA  1 
ATOM   1607 C C   . GLU A 1 185 ? 9.312   -15.686 40.385  1.00 28.24 ? 185 GLU A C   1 
ATOM   1608 O O   . GLU A 1 185 ? 9.149   -16.304 41.442  1.00 33.86 ? 185 GLU A O   1 
ATOM   1609 C CB  . GLU A 1 185 ? 9.580   -16.818 38.166  1.00 31.50 ? 185 GLU A CB  1 
ATOM   1610 C CG  . GLU A 1 185 ? 9.579   -18.331 38.155  1.00 42.54 ? 185 GLU A CG  1 
ATOM   1611 C CD  . GLU A 1 185 ? 10.085  -18.884 36.821  1.00 49.59 ? 185 GLU A CD  1 
ATOM   1612 O OE1 . GLU A 1 185 ? 9.345   -18.771 35.815  1.00 51.38 ? 185 GLU A OE1 1 
ATOM   1613 O OE2 . GLU A 1 185 ? 11.224  -19.413 36.778  1.00 47.56 ? 185 GLU A OE2 1 
ATOM   1614 N N   . GLU A 1 186 ? 10.131  -14.641 40.294  1.00 29.50 ? 186 GLU A N   1 
ATOM   1615 C CA  . GLU A 1 186 ? 10.892  -14.127 41.421  1.00 27.96 ? 186 GLU A CA  1 
ATOM   1616 C C   . GLU A 1 186 ? 10.052  -13.329 42.413  1.00 28.13 ? 186 GLU A C   1 
ATOM   1617 O O   . GLU A 1 186 ? 10.609  -12.828 43.395  1.00 28.64 ? 186 GLU A O   1 
ATOM   1618 C CB  . GLU A 1 186 ? 12.044  -13.253 40.913  1.00 34.32 ? 186 GLU A CB  1 
ATOM   1619 C CG  . GLU A 1 186 ? 13.055  -13.994 40.030  1.00 34.08 ? 186 GLU A CG  1 
ATOM   1620 C CD  . GLU A 1 186 ? 14.075  -13.060 39.382  1.00 45.92 ? 186 GLU A CD  1 
ATOM   1621 O OE1 . GLU A 1 186 ? 13.863  -11.826 39.394  1.00 45.75 ? 186 GLU A OE1 1 
ATOM   1622 O OE2 . GLU A 1 186 ? 15.094  -13.562 38.859  1.00 48.17 ? 186 GLU A OE2 1 
ATOM   1623 N N   . GLY A 1 187 ? 8.748   -13.180 42.179  1.00 31.81 ? 187 GLY A N   1 
ATOM   1624 C CA  . GLY A 1 187 ? 7.907   -12.389 43.064  1.00 25.04 ? 187 GLY A CA  1 
ATOM   1625 C C   . GLY A 1 187 ? 8.180   -10.904 43.059  1.00 23.78 ? 187 GLY A C   1 
ATOM   1626 O O   . GLY A 1 187 ? 7.815   -10.217 44.012  1.00 23.50 ? 187 GLY A O   1 
ATOM   1627 N N   . LYS A 1 188 ? 8.812   -10.378 42.009  1.00 19.26 ? 188 LYS A N   1 
ATOM   1628 C CA  . LYS A 1 188 ? 9.116   -8.956  41.971  1.00 19.35 ? 188 LYS A CA  1 
ATOM   1629 C C   . LYS A 1 188 ? 7.987   -8.136  41.374  1.00 18.44 ? 188 LYS A C   1 
ATOM   1630 O O   . LYS A 1 188 ? 8.020   -6.909  41.470  1.00 18.82 ? 188 LYS A O   1 
ATOM   1631 C CB  . LYS A 1 188 ? 10.393  -8.687  41.171  1.00 22.20 ? 188 LYS A CB  1 
ATOM   1632 C CG  . LYS A 1 188 ? 11.633  -9.370  41.714  1.00 28.06 ? 188 LYS A CG  1 
ATOM   1633 C CD  . LYS A 1 188 ? 12.861  -8.922  40.932  1.00 34.80 ? 188 LYS A CD  1 
ATOM   1634 C CE  . LYS A 1 188 ? 14.145  -9.399  41.595  1.00 42.92 ? 188 LYS A CE  1 
ATOM   1635 N NZ  . LYS A 1 188 ? 15.316  -8.586  41.163  1.00 45.97 ? 188 LYS A NZ  1 
ATOM   1636 N N   . GLY A 1 189 ? 7.013   -8.777  40.744  1.00 18.10 ? 189 GLY A N   1 
ATOM   1637 C CA  . GLY A 1 189 ? 5.875   -8.058  40.213  1.00 15.47 ? 189 GLY A CA  1 
ATOM   1638 C C   . GLY A 1 189 ? 4.798   -9.015  39.777  1.00 20.51 ? 189 GLY A C   1 
ATOM   1639 O O   . GLY A 1 189 ? 5.089   -10.171 39.450  1.00 15.35 ? 189 GLY A O   1 
ATOM   1640 N N   . SER A 1 190 ? 3.550   -8.570  39.790  1.00 13.68 ? 190 SER A N   1 
ATOM   1641 C CA  . SER A 1 190 ? 2.490   -9.364  39.188  1.00 12.77 ? 190 SER A CA  1 
ATOM   1642 C C   . SER A 1 190 ? 2.374   -8.988  37.714  1.00 13.28 ? 190 SER A C   1 
ATOM   1643 O O   . SER A 1 190 ? 2.731   -7.875  37.310  1.00 14.99 ? 190 SER A O   1 
ATOM   1644 C CB  . SER A 1 190 ? 1.164   -9.129  39.914  1.00 17.37 ? 190 SER A CB  1 
ATOM   1645 O OG  . SER A 1 190 ? 1.223   -9.567  41.264  1.00 15.62 ? 190 SER A OG  1 
ATOM   1646 N N   . VAL A 1 191 ? 1.911   -9.932  36.897  1.00 14.79 ? 191 VAL A N   1 
ATOM   1647 C CA  . VAL A 1 191 ? 1.598   -9.648  35.494  1.00 13.12 ? 191 VAL A CA  1 
ATOM   1648 C C   . VAL A 1 191 ? 0.130   -9.970  35.266  1.00 17.74 ? 191 VAL A C   1 
ATOM   1649 O O   . VAL A 1 191 ? -0.319  -11.088 35.545  1.00 20.01 ? 191 VAL A O   1 
ATOM   1650 C CB  . VAL A 1 191 ? 2.490   -10.431 34.514  1.00 16.14 ? 191 VAL A CB  1 
ATOM   1651 C CG1 . VAL A 1 191 ? 2.182   -10.017 33.029  1.00 9.75  ? 191 VAL A CG1 1 
ATOM   1652 C CG2 . VAL A 1 191 ? 3.951   -10.200 34.831  1.00 15.38 ? 191 VAL A CG2 1 
ATOM   1653 N N   . SER A 1 192 ? -0.608  -8.998  34.755  1.00 10.38 ? 192 SER A N   1 
ATOM   1654 C CA  . SER A 1 192 ? -2.019  -9.158  34.444  1.00 15.13 ? 192 SER A CA  1 
ATOM   1655 C C   . SER A 1 192 ? -2.206  -9.159  32.929  1.00 15.91 ? 192 SER A C   1 
ATOM   1656 O O   . SER A 1 192 ? -1.263  -8.951  32.168  1.00 15.44 ? 192 SER A O   1 
ATOM   1657 C CB  . SER A 1 192 ? -2.838  -8.041  35.085  1.00 13.73 ? 192 SER A CB  1 
ATOM   1658 O OG  . SER A 1 192 ? -2.644  -6.811  34.392  1.00 16.07 ? 192 SER A OG  1 
ATOM   1659 N N   . THR A 1 193 ? -3.447  -9.366  32.500  1.00 17.51 ? 193 THR A N   1 
ATOM   1660 C CA  . THR A 1 193 ? -3.802  -9.236  31.093  1.00 15.20 ? 193 THR A CA  1 
ATOM   1661 C C   . THR A 1 193 ? -5.150  -8.526  30.990  1.00 13.63 ? 193 THR A C   1 
ATOM   1662 O O   . THR A 1 193 ? -5.792  -8.213  31.998  1.00 12.99 ? 193 THR A O   1 
ATOM   1663 C CB  . THR A 1 193 ? -3.819  -10.602 30.390  1.00 13.52 ? 193 THR A CB  1 
ATOM   1664 O OG1 . THR A 1 193 ? -3.927  -10.408 28.969  1.00 16.63 ? 193 THR A OG1 1 
ATOM   1665 C CG2 . THR A 1 193 ? -4.983  -11.466 30.866  1.00 20.84 ? 193 THR A CG2 1 
ATOM   1666 N N   . SER A 1 194 ? -5.569  -8.250  29.761  1.00 14.21 ? 194 SER A N   1 
ATOM   1667 C CA  . SER A 1 194 ? -6.858  -7.647  29.464  1.00 16.45 ? 194 SER A CA  1 
ATOM   1668 C C   . SER A 1 194 ? -7.655  -8.559  28.536  1.00 15.75 ? 194 SER A C   1 
ATOM   1669 O O   . SER A 1 194 ? -7.088  -9.456  27.897  1.00 15.00 ? 194 SER A O   1 
ATOM   1670 C CB  . SER A 1 194 ? -6.685  -6.275  28.795  1.00 13.23 ? 194 SER A CB  1 
ATOM   1671 O OG  . SER A 1 194 ? -6.065  -5.336  29.658  1.00 17.16 ? 194 SER A OG  1 
ATOM   1672 N N   . PRO A 1 195 ? -8.972  -8.366  28.455  1.00 17.66 ? 195 PRO A N   1 
ATOM   1673 C CA  . PRO A 1 195 ? -9.753  -8.984  27.373  1.00 17.39 ? 195 PRO A CA  1 
ATOM   1674 C C   . PRO A 1 195 ? -9.040  -8.803  26.038  1.00 18.43 ? 195 PRO A C   1 
ATOM   1675 O O   . PRO A 1 195 ? -8.464  -7.753  25.771  1.00 13.08 ? 195 PRO A O   1 
ATOM   1676 C CB  . PRO A 1 195 ? -11.078 -8.218  27.414  1.00 19.18 ? 195 PRO A CB  1 
ATOM   1677 C CG  . PRO A 1 195 ? -11.186 -7.693  28.815  1.00 23.65 ? 195 PRO A CG  1 
ATOM   1678 C CD  . PRO A 1 195 ? -9.821  -7.689  29.454  1.00 14.92 ? 195 PRO A CD  1 
ATOM   1679 N N   . TYR A 1 196 ? -9.134  -9.831  25.181  1.00 21.70 ? 196 TYR A N   1 
ATOM   1680 C CA  . TYR A 1 196 ? -8.082  -10.144 24.206  1.00 18.44 ? 196 TYR A CA  1 
ATOM   1681 C C   . TYR A 1 196 ? -7.672  -8.963  23.335  1.00 16.87 ? 196 TYR A C   1 
ATOM   1682 O O   . TYR A 1 196 ? -6.478  -8.678  23.195  1.00 16.11 ? 196 TYR A O   1 
ATOM   1683 C CB  . TYR A 1 196 ? -8.523  -11.306 23.308  1.00 16.82 ? 196 TYR A CB  1 
ATOM   1684 C CG  . TYR A 1 196 ? -7.357  -12.051 22.683  1.00 23.39 ? 196 TYR A CG  1 
ATOM   1685 C CD1 . TYR A 1 196 ? -6.639  -11.511 21.618  1.00 19.39 ? 196 TYR A CD1 1 
ATOM   1686 C CD2 . TYR A 1 196 ? -6.975  -13.295 23.164  1.00 20.41 ? 196 TYR A CD2 1 
ATOM   1687 C CE1 . TYR A 1 196 ? -5.571  -12.211 21.048  1.00 21.99 ? 196 TYR A CE1 1 
ATOM   1688 C CE2 . TYR A 1 196 ? -5.923  -13.988 22.615  1.00 24.01 ? 196 TYR A CE2 1 
ATOM   1689 C CZ  . TYR A 1 196 ? -5.221  -13.452 21.562  1.00 18.22 ? 196 TYR A CZ  1 
ATOM   1690 O OH  . TYR A 1 196 ? -4.167  -14.177 21.040  1.00 19.85 ? 196 TYR A OH  1 
ATOM   1691 N N   . TYR A 1 197 ? -8.630  -8.313  22.673  1.00 15.08 ? 197 TYR A N   1 
ATOM   1692 C CA  . TYR A 1 197 ? -8.304  -7.238  21.739  1.00 17.64 ? 197 TYR A CA  1 
ATOM   1693 C C   . TYR A 1 197 ? -8.547  -5.844  22.318  1.00 12.80 ? 197 TYR A C   1 
ATOM   1694 O O   . TYR A 1 197 ? -8.674  -4.882  21.556  1.00 15.51 ? 197 TYR A O   1 
ATOM   1695 C CB  . TYR A 1 197 ? -9.069  -7.433  20.425  1.00 18.87 ? 197 TYR A CB  1 
ATOM   1696 C CG  . TYR A 1 197 ? -8.540  -8.633  19.674  1.00 15.87 ? 197 TYR A CG  1 
ATOM   1697 C CD1 . TYR A 1 197 ? -7.287  -8.591  19.059  1.00 14.58 ? 197 TYR A CD1 1 
ATOM   1698 C CD2 . TYR A 1 197 ? -9.246  -9.829  19.645  1.00 16.99 ? 197 TYR A CD2 1 
ATOM   1699 C CE1 . TYR A 1 197 ? -6.770  -9.695  18.408  1.00 20.03 ? 197 TYR A CE1 1 
ATOM   1700 C CE2 . TYR A 1 197 ? -8.738  -10.942 18.983  1.00 22.43 ? 197 TYR A CE2 1 
ATOM   1701 C CZ  . TYR A 1 197 ? -7.502  -10.865 18.371  1.00 21.74 ? 197 TYR A CZ  1 
ATOM   1702 O OH  . TYR A 1 197 ? -6.991  -11.962 17.724  1.00 25.56 ? 197 TYR A OH  1 
ATOM   1703 N N   . HIS A 1 198 ? -8.551  -5.707  23.643  1.00 12.41 ? 198 HIS A N   1 
ATOM   1704 C CA  . HIS A 1 198 ? -8.701  -4.410  24.306  1.00 11.61 ? 198 HIS A CA  1 
ATOM   1705 C C   . HIS A 1 198 ? -9.993  -3.705  23.881  1.00 16.54 ? 198 HIS A C   1 
ATOM   1706 O O   . HIS A 1 198 ? -9.947  -2.535  23.476  1.00 13.00 ? 198 HIS A O   1 
ATOM   1707 C CB  . HIS A 1 198 ? -7.460  -3.561  24.008  1.00 11.47 ? 198 HIS A CB  1 
ATOM   1708 C CG  . HIS A 1 198 ? -7.270  -2.373  24.907  1.00 17.74 ? 198 HIS A CG  1 
ATOM   1709 N ND1 . HIS A 1 198 ? -7.698  -1.112  24.561  1.00 15.26 ? 198 HIS A ND1 1 
ATOM   1710 C CD2 . HIS A 1 198 ? -6.639  -2.240  26.102  1.00 13.46 ? 198 HIS A CD2 1 
ATOM   1711 C CE1 . HIS A 1 198 ? -7.365  -0.255  25.514  1.00 14.55 ? 198 HIS A CE1 1 
ATOM   1712 N NE2 . HIS A 1 198 ? -6.722  -0.915  26.461  1.00 15.66 ? 198 HIS A NE2 1 
ATOM   1713 N N   . PRO A 1 199 ? -11.156 -4.361  23.964  1.00 15.21 ? 199 PRO A N   1 
ATOM   1714 C CA  . PRO A 1 199 ? -12.422 -3.704  23.635  1.00 19.55 ? 199 PRO A CA  1 
ATOM   1715 C C   . PRO A 1 199 ? -13.042 -3.000  24.838  1.00 17.77 ? 199 PRO A C   1 
ATOM   1716 O O   . PRO A 1 199 ? -12.569 -3.113  25.970  1.00 23.61 ? 199 PRO A O   1 
ATOM   1717 C CB  . PRO A 1 199 ? -13.301 -4.882  23.207  1.00 18.41 ? 199 PRO A CB  1 
ATOM   1718 C CG  . PRO A 1 199 ? -12.890 -5.950  24.168  1.00 23.47 ? 199 PRO A CG  1 
ATOM   1719 C CD  . PRO A 1 199 ? -11.384 -5.769  24.352  1.00 19.87 ? 199 PRO A CD  1 
ATOM   1720 N N   . LEU A 1 200 ? -14.148 -2.293  24.570  1.00 19.31 ? 200 LEU A N   1 
ATOM   1721 C CA  . LEU A 1 200 ? -14.946 -1.658  25.620  1.00 16.82 ? 200 LEU A CA  1 
ATOM   1722 C C   . LEU A 1 200 ? -15.992 -2.667  26.074  1.00 22.79 ? 200 LEU A C   1 
ATOM   1723 O O   . LEU A 1 200 ? -17.103 -2.739  25.537  1.00 20.23 ? 200 LEU A O   1 
ATOM   1724 C CB  . LEU A 1 200 ? -15.578 -0.362  25.122  1.00 17.20 ? 200 LEU A CB  1 
ATOM   1725 C CG  . LEU A 1 200 ? -14.578 0.754   24.838  1.00 17.79 ? 200 LEU A CG  1 
ATOM   1726 C CD1 . LEU A 1 200 ? -15.270 1.896   24.122  1.00 24.36 ? 200 LEU A CD1 1 
ATOM   1727 C CD2 . LEU A 1 200 ? -13.899 1.251   26.108  1.00 22.56 ? 200 LEU A CD2 1 
ATOM   1728 N N   . ILE A 1 201 ? -15.617 -3.481  27.062  1.00 18.03 ? 201 ILE A N   1 
ATOM   1729 C CA  . ILE A 1 201 ? -16.510 -4.539  27.536  1.00 20.12 ? 201 ILE A CA  1 
ATOM   1730 C C   . ILE A 1 201 ? -17.885 -3.999  27.921  1.00 15.33 ? 201 ILE A C   1 
ATOM   1731 O O   . ILE A 1 201 ? -18.894 -4.604  27.520  1.00 18.05 ? 201 ILE A O   1 
ATOM   1732 C CB  . ILE A 1 201 ? -15.841 -5.335  28.662  1.00 18.56 ? 201 ILE A CB  1 
ATOM   1733 C CG1 . ILE A 1 201 ? -14.635 -6.118  28.131  1.00 17.83 ? 201 ILE A CG1 1 
ATOM   1734 C CG2 . ILE A 1 201 ? -16.821 -6.296  29.289  1.00 12.47 ? 201 ILE A CG2 1 
ATOM   1735 C CD1 . ILE A 1 201 ? -15.026 -7.372  27.339  1.00 17.24 ? 201 ILE A CD1 1 
ATOM   1736 N N   . PRO A 1 202 ? -18.017 -2.874  28.646  1.00 17.16 ? 202 PRO A N   1 
ATOM   1737 C CA  . PRO A 1 202 ? -19.370 -2.422  29.032  1.00 14.78 ? 202 PRO A CA  1 
ATOM   1738 C C   . PRO A 1 202 ? -20.303 -2.160  27.856  1.00 17.90 ? 202 PRO A C   1 
ATOM   1739 O O   . PRO A 1 202 ? -21.511 -2.411  27.966  1.00 16.15 ? 202 PRO A O   1 
ATOM   1740 C CB  . PRO A 1 202 ? -19.090 -1.143  29.833  1.00 20.42 ? 202 PRO A CB  1 
ATOM   1741 C CG  . PRO A 1 202 ? -17.745 -1.372  30.432  1.00 18.48 ? 202 PRO A CG  1 
ATOM   1742 C CD  . PRO A 1 202 ? -16.967 -2.133  29.381  1.00 18.06 ? 202 PRO A CD  1 
ATOM   1743 N N   . ILE A 1 203 ? -19.780 -1.651  26.737  1.00 18.09 ? 203 ILE A N   1 
ATOM   1744 C CA  . ILE A 1 203 ? -20.629 -1.389  25.578  1.00 16.53 ? 203 ILE A CA  1 
ATOM   1745 C C   . ILE A 1 203 ? -21.006 -2.696  24.893  1.00 15.98 ? 203 ILE A C   1 
ATOM   1746 O O   . ILE A 1 203 ? -22.163 -2.887  24.499  1.00 17.96 ? 203 ILE A O   1 
ATOM   1747 C CB  . ILE A 1 203 ? -19.937 -0.400  24.614  1.00 17.97 ? 203 ILE A CB  1 
ATOM   1748 C CG1 . ILE A 1 203 ? -19.901 0.998   25.240  1.00 19.15 ? 203 ILE A CG1 1 
ATOM   1749 C CG2 . ILE A 1 203 ? -20.649 -0.333  23.230  1.00 15.60 ? 203 ILE A CG2 1 
ATOM   1750 C CD1 . ILE A 1 203 ? -19.224 2.046   24.362  1.00 17.84 ? 203 ILE A CD1 1 
ATOM   1751 N N   . LEU A 1 204 ? -20.052 -3.623  24.749  1.00 12.07 ? 204 LEU A N   1 
ATOM   1752 C CA  . LEU A 1 204 ? -20.398 -4.921  24.172  1.00 19.12 ? 204 LEU A CA  1 
ATOM   1753 C C   . LEU A 1 204 ? -21.487 -5.609  24.986  1.00 19.20 ? 204 LEU A C   1 
ATOM   1754 O O   . LEU A 1 204 ? -22.351 -6.293  24.425  1.00 18.06 ? 204 LEU A O   1 
ATOM   1755 C CB  . LEU A 1 204 ? -19.158 -5.814  24.080  1.00 17.90 ? 204 LEU A CB  1 
ATOM   1756 C CG  . LEU A 1 204 ? -17.970 -5.295  23.257  1.00 11.71 ? 204 LEU A CG  1 
ATOM   1757 C CD1 . LEU A 1 204 ? -16.890 -6.377  23.142  1.00 17.92 ? 204 LEU A CD1 1 
ATOM   1758 C CD2 . LEU A 1 204 ? -18.428 -4.795  21.874  1.00 14.86 ? 204 LEU A CD2 1 
ATOM   1759 N N   . LEU A 1 205 ? -21.477 -5.423  26.305  1.00 22.13 ? 205 LEU A N   1 
ATOM   1760 C CA  . LEU A 1 205 ? -22.467 -6.085  27.145  1.00 22.18 ? 205 LEU A CA  1 
ATOM   1761 C C   . LEU A 1 205 ? -23.815 -5.372  27.122  1.00 18.31 ? 205 LEU A C   1 
ATOM   1762 O O   . LEU A 1 205 ? -24.853 -6.032  27.190  1.00 23.77 ? 205 LEU A O   1 
ATOM   1763 C CB  . LEU A 1 205 ? -21.953 -6.186  28.581  1.00 17.09 ? 205 LEU A CB  1 
ATOM   1764 C CG  . LEU A 1 205 ? -20.868 -7.232  28.845  1.00 15.71 ? 205 LEU A CG  1 
ATOM   1765 C CD1 . LEU A 1 205 ? -20.404 -7.137  30.300  1.00 16.82 ? 205 LEU A CD1 1 
ATOM   1766 C CD2 . LEU A 1 205 ? -21.388 -8.628  28.548  1.00 14.24 ? 205 LEU A CD2 1 
ATOM   1767 N N   . ASN A 1 206 ? -23.823 -4.043  27.021  1.00 18.34 ? 206 ASN A N   1 
ATOM   1768 C CA  . ASN A 1 206 ? -25.045 -3.275  27.204  1.00 19.21 ? 206 ASN A CA  1 
ATOM   1769 C C   . ASN A 1 206 ? -24.813 -1.848  26.732  1.00 17.00 ? 206 ASN A C   1 
ATOM   1770 O O   . ASN A 1 206 ? -24.466 -0.974  27.535  1.00 16.22 ? 206 ASN A O   1 
ATOM   1771 C CB  . ASN A 1 206 ? -25.488 -3.291  28.668  1.00 19.01 ? 206 ASN A CB  1 
ATOM   1772 C CG  . ASN A 1 206 ? -26.678 -2.386  28.923  1.00 27.72 ? 206 ASN A CG  1 
ATOM   1773 O OD1 . ASN A 1 206 ? -27.498 -2.158  28.035  1.00 32.83 ? 206 ASN A OD1 1 
ATOM   1774 N ND2 . ASN A 1 206 ? -26.770 -1.855  30.137  1.00 29.27 ? 206 ASN A ND2 1 
ATOM   1775 N N   . PRO A 1 207 ? -25.004 -1.577  25.439  1.00 20.21 ? 207 PRO A N   1 
ATOM   1776 C CA  . PRO A 1 207 ? -24.693 -0.240  24.910  1.00 20.36 ? 207 PRO A CA  1 
ATOM   1777 C C   . PRO A 1 207 ? -25.483 0.877   25.564  1.00 15.92 ? 207 PRO A C   1 
ATOM   1778 O O   . PRO A 1 207 ? -25.023 2.026   25.569  1.00 15.36 ? 207 PRO A O   1 
ATOM   1779 C CB  . PRO A 1 207 ? -25.037 -0.372  23.419  1.00 25.25 ? 207 PRO A CB  1 
ATOM   1780 C CG  . PRO A 1 207 ? -24.969 -1.832  23.141  1.00 23.55 ? 207 PRO A CG  1 
ATOM   1781 C CD  . PRO A 1 207 ? -25.483 -2.488  24.388  1.00 21.84 ? 207 PRO A CD  1 
ATOM   1782 N N   . ASN A 1 208 ? -26.662 0.579   26.117  1.00 15.24 ? 208 ASN A N   1 
ATOM   1783 C CA  . ASN A 1 208 ? -27.436 1.591   26.820  1.00 18.34 ? 208 ASN A CA  1 
ATOM   1784 C C   . ASN A 1 208 ? -26.708 2.157   28.035  1.00 24.38 ? 208 ASN A C   1 
ATOM   1785 O O   . ASN A 1 208 ? -27.115 3.206   28.547  1.00 19.79 ? 208 ASN A O   1 
ATOM   1786 C CB  . ASN A 1 208 ? -28.785 1.002   27.249  1.00 20.67 ? 208 ASN A CB  1 
ATOM   1787 C CG  . ASN A 1 208 ? -29.777 0.909   26.099  1.00 25.87 ? 208 ASN A CG  1 
ATOM   1788 O OD1 . ASN A 1 208 ? -29.610 1.545   25.063  1.00 24.12 ? 208 ASN A OD1 1 
ATOM   1789 N ND2 . ASN A 1 208 ? -30.823 0.116   26.288  1.00 33.64 ? 208 ASN A ND2 1 
ATOM   1790 N N   . CYS A 1 209 ? -25.644 1.505   28.511  1.00 24.54 ? 209 CYS A N   1 
ATOM   1791 C CA  . CYS A 1 209 ? -24.951 2.034   29.680  1.00 22.81 ? 209 CYS A CA  1 
ATOM   1792 C C   . CYS A 1 209 ? -24.283 3.375   29.401  1.00 18.83 ? 209 CYS A C   1 
ATOM   1793 O O   . CYS A 1 209 ? -23.951 4.092   30.353  1.00 19.30 ? 209 CYS A O   1 
ATOM   1794 C CB  . CYS A 1 209 ? -23.927 1.019   30.209  1.00 23.14 ? 209 CYS A CB  1 
ATOM   1795 S SG  . CYS A 1 209 ? -22.381 0.892   29.276  1.00 23.71 ? 209 CYS A SG  1 
ATOM   1796 N N   . VAL A 1 210 ? -24.106 3.749   28.126  1.00 18.97 ? 210 VAL A N   1 
ATOM   1797 C CA  . VAL A 1 210 ? -23.537 5.060   27.810  1.00 16.37 ? 210 VAL A CA  1 
ATOM   1798 C C   . VAL A 1 210 ? -24.445 6.183   28.297  1.00 18.90 ? 210 VAL A C   1 
ATOM   1799 O O   . VAL A 1 210 ? -23.983 7.303   28.546  1.00 26.13 ? 210 VAL A O   1 
ATOM   1800 C CB  . VAL A 1 210 ? -23.276 5.191   26.294  1.00 22.09 ? 210 VAL A CB  1 
ATOM   1801 C CG1 . VAL A 1 210 ? -22.232 4.186   25.828  1.00 15.49 ? 210 VAL A CG1 1 
ATOM   1802 C CG2 . VAL A 1 210 ? -24.576 5.034   25.517  1.00 27.17 ? 210 VAL A CG2 1 
ATOM   1803 N N   . TYR A 1 211 ? -25.747 5.914   28.425  1.00 17.95 ? 211 TYR A N   1 
ATOM   1804 C CA  . TYR A 1 211 ? -26.678 6.940   28.877  1.00 24.08 ? 211 TYR A CA  1 
ATOM   1805 C C   . TYR A 1 211 ? -26.528 7.265   30.361  1.00 27.05 ? 211 TYR A C   1 
ATOM   1806 O O   . TYR A 1 211 ? -27.018 8.311   30.792  1.00 23.79 ? 211 TYR A O   1 
ATOM   1807 C CB  . TYR A 1 211 ? -28.119 6.511   28.595  1.00 25.01 ? 211 TYR A CB  1 
ATOM   1808 C CG  . TYR A 1 211 ? -28.431 6.305   27.133  1.00 26.07 ? 211 TYR A CG  1 
ATOM   1809 C CD1 . TYR A 1 211 ? -28.392 7.364   26.238  1.00 23.03 ? 211 TYR A CD1 1 
ATOM   1810 C CD2 . TYR A 1 211 ? -28.791 5.055   26.653  1.00 27.22 ? 211 TYR A CD2 1 
ATOM   1811 C CE1 . TYR A 1 211 ? -28.686 7.175   24.898  1.00 25.62 ? 211 TYR A CE1 1 
ATOM   1812 C CE2 . TYR A 1 211 ? -29.090 4.859   25.314  1.00 25.42 ? 211 TYR A CE2 1 
ATOM   1813 C CZ  . TYR A 1 211 ? -29.036 5.923   24.446  1.00 20.21 ? 211 TYR A CZ  1 
ATOM   1814 O OH  . TYR A 1 211 ? -29.337 5.735   23.108  1.00 27.29 ? 211 TYR A OH  1 
ATOM   1815 N N   . GLU A 1 212 ? -25.873 6.400   31.148  1.00 22.74 ? 212 GLU A N   1 
ATOM   1816 C CA  . GLU A 1 212 ? -25.711 6.676   32.574  1.00 23.37 ? 212 GLU A CA  1 
ATOM   1817 C C   . GLU A 1 212 ? -24.878 7.929   32.827  1.00 29.86 ? 212 GLU A C   1 
ATOM   1818 O O   . GLU A 1 212 ? -25.080 8.609   33.837  1.00 25.02 ? 212 GLU A O   1 
ATOM   1819 C CB  . GLU A 1 212 ? -25.080 5.472   33.281  1.00 25.49 ? 212 GLU A CB  1 
ATOM   1820 C CG  . GLU A 1 212 ? -25.844 4.189   33.072  1.00 18.61 ? 212 GLU A CG  1 
ATOM   1821 C CD  . GLU A 1 212 ? -25.167 2.970   33.664  1.00 25.89 ? 212 GLU A CD  1 
ATOM   1822 O OE1 . GLU A 1 212 ? -24.158 3.126   34.384  1.00 25.72 ? 212 GLU A OE1 1 
ATOM   1823 O OE2 . GLU A 1 212 ? -25.647 1.848   33.401  1.00 29.00 ? 212 GLU A OE2 1 
ATOM   1824 N N   . THR A 1 213 ? -23.942 8.255   31.935  1.00 25.89 ? 213 THR A N   1 
ATOM   1825 C CA  . THR A 1 213 ? -23.113 9.444   32.098  1.00 23.15 ? 213 THR A CA  1 
ATOM   1826 C C   . THR A 1 213 ? -23.358 10.519  31.053  1.00 28.04 ? 213 THR A C   1 
ATOM   1827 O O   . THR A 1 213 ? -23.153 11.699  31.345  1.00 29.05 ? 213 THR A O   1 
ATOM   1828 C CB  . THR A 1 213 ? -21.622 9.074   32.059  1.00 31.38 ? 213 THR A CB  1 
ATOM   1829 O OG1 . THR A 1 213 ? -21.360 8.248   30.913  1.00 39.42 ? 213 THR A OG1 1 
ATOM   1830 C CG2 . THR A 1 213 ? -21.229 8.342   33.319  1.00 26.57 ? 213 THR A CG2 1 
ATOM   1831 N N   . THR A 1 214 ? -23.752 10.138  29.839  1.00 27.61 ? 214 THR A N   1 
ATOM   1832 C CA  . THR A 1 214 ? -24.066 11.073  28.758  1.00 32.33 ? 214 THR A CA  1 
ATOM   1833 C C   . THR A 1 214 ? -25.482 10.777  28.290  1.00 30.45 ? 214 THR A C   1 
ATOM   1834 O O   . THR A 1 214 ? -25.686 10.175  27.226  1.00 28.41 ? 214 THR A O   1 
ATOM   1835 C CB  . THR A 1 214 ? -23.079 10.948  27.595  1.00 33.97 ? 214 THR A CB  1 
ATOM   1836 O OG1 . THR A 1 214 ? -23.058 9.590   27.133  1.00 25.66 ? 214 THR A OG1 1 
ATOM   1837 C CG2 . THR A 1 214 ? -21.680 11.371  28.019  1.00 36.15 ? 214 THR A CG2 1 
ATOM   1838 N N   . PRO A 1 215 ? -26.490 11.195  29.060  1.00 31.48 ? 215 PRO A N   1 
ATOM   1839 C CA  . PRO A 1 215 ? -27.877 10.829  28.713  1.00 29.89 ? 215 PRO A CA  1 
ATOM   1840 C C   . PRO A 1 215 ? -28.351 11.375  27.371  1.00 33.06 ? 215 PRO A C   1 
ATOM   1841 O O   . PRO A 1 215 ? -29.236 10.775  26.747  1.00 32.29 ? 215 PRO A O   1 
ATOM   1842 C CB  . PRO A 1 215 ? -28.693 11.408  29.880  1.00 26.20 ? 215 PRO A CB  1 
ATOM   1843 C CG  . PRO A 1 215 ? -27.820 12.486  30.467  1.00 29.75 ? 215 PRO A CG  1 
ATOM   1844 C CD  . PRO A 1 215 ? -26.410 12.017  30.281  1.00 30.44 ? 215 PRO A CD  1 
ATOM   1845 N N   . ASN A 1 216 ? -27.791 12.480  26.892  1.00 35.73 ? 216 ASN A N   1 
ATOM   1846 C CA  . ASN A 1 216 ? -28.263 13.091  25.656  1.00 39.85 ? 216 ASN A CA  1 
ATOM   1847 C C   . ASN A 1 216 ? -27.510 12.613  24.418  1.00 38.53 ? 216 ASN A C   1 
ATOM   1848 O O   . ASN A 1 216 ? -27.736 13.147  23.328  1.00 30.69 ? 216 ASN A O   1 
ATOM   1849 C CB  . ASN A 1 216 ? -28.172 14.610  25.763  1.00 41.80 ? 216 ASN A CB  1 
ATOM   1850 C CG  . ASN A 1 216 ? -29.066 15.159  26.850  1.00 46.44 ? 216 ASN A CG  1 
ATOM   1851 O OD1 . ASN A 1 216 ? -30.127 14.598  27.137  1.00 43.26 ? 216 ASN A OD1 1 
ATOM   1852 N ND2 . ASN A 1 216 ? -28.641 16.253  27.471  1.00 52.08 ? 216 ASN A ND2 1 
ATOM   1853 N N   . VAL A 1 217 ? -26.640 11.613  24.557  1.00 33.40 ? 217 VAL A N   1 
ATOM   1854 C CA  . VAL A 1 217 ? -25.844 11.148  23.431  1.00 30.77 ? 217 VAL A CA  1 
ATOM   1855 C C   . VAL A 1 217 ? -26.719 10.394  22.436  1.00 30.24 ? 217 VAL A C   1 
ATOM   1856 O O   . VAL A 1 217 ? -27.747 9.797   22.792  1.00 31.91 ? 217 VAL A O   1 
ATOM   1857 C CB  . VAL A 1 217 ? -24.684 10.267  23.936  1.00 30.94 ? 217 VAL A CB  1 
ATOM   1858 C CG1 . VAL A 1 217 ? -25.174 8.851   24.245  1.00 29.89 ? 217 VAL A CG1 1 
ATOM   1859 C CG2 . VAL A 1 217 ? -23.552 10.247  22.925  1.00 31.90 ? 217 VAL A CG2 1 
ATOM   1860 N N   . LYS A 1 218 ? -26.309 10.426  21.170  1.00 24.99 ? 218 LYS A N   1 
ATOM   1861 C CA  . LYS A 1 218 ? -26.934 9.660   20.100  1.00 22.09 ? 218 LYS A CA  1 
ATOM   1862 C C   . LYS A 1 218 ? -25.996 8.531   19.704  1.00 28.02 ? 218 LYS A C   1 
ATOM   1863 O O   . LYS A 1 218 ? -24.859 8.787   19.301  1.00 28.79 ? 218 LYS A O   1 
ATOM   1864 C CB  . LYS A 1 218 ? -27.222 10.546  18.886  1.00 33.86 ? 218 LYS A CB  1 
ATOM   1865 C CG  . LYS A 1 218 ? -28.287 11.609  19.102  1.00 43.85 ? 218 LYS A CG  1 
ATOM   1866 C CD  . LYS A 1 218 ? -29.385 11.502  18.055  1.00 54.15 ? 218 LYS A CD  1 
ATOM   1867 C CE  . LYS A 1 218 ? -30.166 12.802  17.928  1.00 55.84 ? 218 LYS A CE  1 
ATOM   1868 N NZ  . LYS A 1 218 ? -29.913 13.473  16.627  1.00 58.88 ? 218 LYS A NZ  1 
ATOM   1869 N N   . ILE A 1 219 ? -26.471 7.297   19.796  1.00 28.60 ? 219 ILE A N   1 
ATOM   1870 C CA  . ILE A 1 219 ? -25.667 6.145   19.395  1.00 31.15 ? 219 ILE A CA  1 
ATOM   1871 C C   . ILE A 1 219 ? -26.455 5.364   18.363  1.00 31.88 ? 219 ILE A C   1 
ATOM   1872 O O   . ILE A 1 219 ? -27.677 5.542   18.225  1.00 29.83 ? 219 ILE A O   1 
ATOM   1873 C CB  . ILE A 1 219 ? -25.277 5.265   20.608  1.00 31.48 ? 219 ILE A CB  1 
ATOM   1874 C CG1 . ILE A 1 219 ? -26.518 4.664   21.268  1.00 32.25 ? 219 ILE A CG1 1 
ATOM   1875 C CG2 . ILE A 1 219 ? -24.444 6.064   21.594  1.00 28.41 ? 219 ILE A CG2 1 
ATOM   1876 C CD1 . ILE A 1 219 ? -26.213 3.457   22.148  1.00 26.13 ? 219 ILE A CD1 1 
ATOM   1877 N N   . PRO A 1 220 ? -25.792 4.511   17.589  1.00 28.97 ? 220 PRO A N   1 
ATOM   1878 C CA  . PRO A 1 220 ? -26.513 3.706   16.601  1.00 33.14 ? 220 PRO A CA  1 
ATOM   1879 C C   . PRO A 1 220 ? -27.432 2.696   17.272  1.00 32.78 ? 220 PRO A C   1 
ATOM   1880 O O   . PRO A 1 220 ? -27.437 2.494   18.489  1.00 32.42 ? 220 PRO A O   1 
ATOM   1881 C CB  . PRO A 1 220 ? -25.410 3.004   15.799  1.00 29.62 ? 220 PRO A CB  1 
ATOM   1882 C CG  . PRO A 1 220 ? -24.133 3.310   16.486  1.00 25.39 ? 220 PRO A CG  1 
ATOM   1883 C CD  . PRO A 1 220 ? -24.338 4.505   17.354  1.00 34.02 ? 220 PRO A CD  1 
ATOM   1884 N N   . ASP A 1 221 ? -28.220 2.049   16.427  1.00 33.10 ? 221 ASP A N   1 
ATOM   1885 C CA  . ASP A 1 221 ? -29.150 1.017   16.849  1.00 32.51 ? 221 ASP A CA  1 
ATOM   1886 C C   . ASP A 1 221 ? -28.405 -0.312  16.876  1.00 32.52 ? 221 ASP A C   1 
ATOM   1887 O O   . ASP A 1 221 ? -28.087 -0.878  15.823  1.00 30.72 ? 221 ASP A O   1 
ATOM   1888 C CB  . ASP A 1 221 ? -30.343 0.991   15.899  1.00 34.94 ? 221 ASP A CB  1 
ATOM   1889 C CG  . ASP A 1 221 ? -31.229 -0.203  16.109  1.00 41.01 ? 221 ASP A CG  1 
ATOM   1890 O OD1 . ASP A 1 221 ? -31.476 -0.568  17.283  1.00 49.12 ? 221 ASP A OD1 1 
ATOM   1891 O OD2 . ASP A 1 221 ? -31.705 -0.763  15.100  1.00 41.90 ? 221 ASP A OD2 1 
ATOM   1892 N N   . PHE A 1 222 ? -28.112 -0.802  18.081  1.00 24.02 ? 222 PHE A N   1 
ATOM   1893 C CA  . PHE A 1 222 ? -27.375 -2.054  18.256  1.00 21.23 ? 222 PHE A CA  1 
ATOM   1894 C C   . PHE A 1 222 ? -28.342 -3.214  18.047  1.00 29.41 ? 222 PHE A C   1 
ATOM   1895 O O   . PHE A 1 222 ? -28.861 -3.817  18.987  1.00 26.22 ? 222 PHE A O   1 
ATOM   1896 C CB  . PHE A 1 222 ? -26.719 -2.107  19.631  1.00 23.80 ? 222 PHE A CB  1 
ATOM   1897 C CG  . PHE A 1 222 ? -25.395 -1.405  19.693  1.00 23.04 ? 222 PHE A CG  1 
ATOM   1898 C CD1 . PHE A 1 222 ? -25.334 -0.026  19.826  1.00 24.31 ? 222 PHE A CD1 1 
ATOM   1899 C CD2 . PHE A 1 222 ? -24.217 -2.119  19.591  1.00 23.10 ? 222 PHE A CD2 1 
ATOM   1900 C CE1 . PHE A 1 222 ? -24.121 0.620   19.875  1.00 24.70 ? 222 PHE A CE1 1 
ATOM   1901 C CE2 . PHE A 1 222 ? -23.004 -1.479  19.640  1.00 22.20 ? 222 PHE A CE2 1 
ATOM   1902 C CZ  . PHE A 1 222 ? -22.957 -0.105  19.776  1.00 20.37 ? 222 PHE A CZ  1 
ATOM   1903 N N   . ALA A 1 223 ? -28.575 -3.536  16.777  1.00 39.97 ? 223 ALA A N   1 
ATOM   1904 C CA  . ALA A 1 223 ? -29.559 -4.544  16.400  1.00 43.23 ? 223 ALA A CA  1 
ATOM   1905 C C   . ALA A 1 223 ? -29.032 -5.967  16.512  1.00 41.25 ? 223 ALA A C   1 
ATOM   1906 O O   . ALA A 1 223 ? -29.767 -6.909  16.198  1.00 45.28 ? 223 ALA A O   1 
ATOM   1907 C CB  . ALA A 1 223 ? -30.046 -4.290  14.971  1.00 45.53 ? 223 ALA A CB  1 
ATOM   1908 N N   . VAL A 1 224 ? -27.784 -6.145  16.933  1.00 31.13 ? 224 VAL A N   1 
ATOM   1909 C CA  . VAL A 1 224 ? -27.179 -7.454  17.112  1.00 29.29 ? 224 VAL A CA  1 
ATOM   1910 C C   . VAL A 1 224 ? -26.530 -7.475  18.491  1.00 31.19 ? 224 VAL A C   1 
ATOM   1911 O O   . VAL A 1 224 ? -26.103 -6.439  19.009  1.00 37.04 ? 224 VAL A O   1 
ATOM   1912 C CB  . VAL A 1 224 ? -26.158 -7.760  15.994  1.00 35.85 ? 224 VAL A CB  1 
ATOM   1913 C CG1 . VAL A 1 224 ? -24.914 -6.895  16.143  1.00 37.92 ? 224 VAL A CG1 1 
ATOM   1914 C CG2 . VAL A 1 224 ? -25.806 -9.243  15.968  1.00 43.05 ? 224 VAL A CG2 1 
ATOM   1915 N N   . SER A 1 225 ? -26.491 -8.653  19.104  1.00 21.08 ? 225 SER A N   1 
ATOM   1916 C CA  . SER A 1 225 ? -25.942 -8.791  20.449  1.00 21.92 ? 225 SER A CA  1 
ATOM   1917 C C   . SER A 1 225 ? -24.440 -9.058  20.388  1.00 23.57 ? 225 SER A C   1 
ATOM   1918 O O   . SER A 1 225 ? -23.978 -9.874  19.582  1.00 21.54 ? 225 SER A O   1 
ATOM   1919 C CB  . SER A 1 225 ? -26.640 -9.919  21.207  1.00 25.17 ? 225 SER A CB  1 
ATOM   1920 O OG  . SER A 1 225 ? -25.966 -10.186 22.433  1.00 29.37 ? 225 SER A OG  1 
ATOM   1921 N N   . PHE A 1 226 ? -23.684 -8.367  21.247  1.00 23.07 ? 226 PHE A N   1 
ATOM   1922 C CA  . PHE A 1 226 ? -22.252 -8.590  21.403  1.00 15.97 ? 226 PHE A CA  1 
ATOM   1923 C C   . PHE A 1 226 ? -21.910 -9.233  22.741  1.00 22.45 ? 226 PHE A C   1 
ATOM   1924 O O   . PHE A 1 226 ? -20.727 -9.378  23.053  1.00 21.36 ? 226 PHE A O   1 
ATOM   1925 C CB  . PHE A 1 226 ? -21.477 -7.267  21.283  1.00 16.82 ? 226 PHE A CB  1 
ATOM   1926 C CG  . PHE A 1 226 ? -21.461 -6.678  19.898  1.00 20.28 ? 226 PHE A CG  1 
ATOM   1927 C CD1 . PHE A 1 226 ? -20.550 -7.119  18.953  1.00 20.56 ? 226 PHE A CD1 1 
ATOM   1928 C CD2 . PHE A 1 226 ? -22.339 -5.662  19.553  1.00 24.78 ? 226 PHE A CD2 1 
ATOM   1929 C CE1 . PHE A 1 226 ? -20.524 -6.571  17.685  1.00 26.45 ? 226 PHE A CE1 1 
ATOM   1930 C CE2 . PHE A 1 226 ? -22.316 -5.109  18.280  1.00 31.36 ? 226 PHE A CE2 1 
ATOM   1931 C CZ  . PHE A 1 226 ? -21.410 -5.568  17.348  1.00 28.26 ? 226 PHE A CZ  1 
ATOM   1932 N N   . ARG A 1 227 ? -22.915 -9.608  23.539  1.00 26.00 ? 227 ARG A N   1 
ATOM   1933 C CA  . ARG A 1 227 ? -22.658 -10.098 24.891  1.00 24.34 ? 227 ARG A CA  1 
ATOM   1934 C C   . ARG A 1 227 ? -21.782 -11.340 24.871  1.00 22.92 ? 227 ARG A C   1 
ATOM   1935 O O   . ARG A 1 227 ? -20.945 -11.541 25.756  1.00 26.07 ? 227 ARG A O   1 
ATOM   1936 C CB  . ARG A 1 227 ? -23.986 -10.394 25.591  1.00 20.35 ? 227 ARG A CB  1 
ATOM   1937 C CG  . ARG A 1 227 ? -24.888 -9.185  25.740  1.00 25.37 ? 227 ARG A CG  1 
ATOM   1938 C CD  . ARG A 1 227 ? -26.121 -9.537  26.553  1.00 27.62 ? 227 ARG A CD  1 
ATOM   1939 N NE  . ARG A 1 227 ? -25.754 -10.147 27.826  1.00 38.37 ? 227 ARG A NE  1 
ATOM   1940 C CZ  . ARG A 1 227 ? -25.461 -9.458  28.924  1.00 37.63 ? 227 ARG A CZ  1 
ATOM   1941 N NH1 . ARG A 1 227 ? -25.499 -8.135  28.907  1.00 33.98 ? 227 ARG A NH1 1 
ATOM   1942 N NH2 . ARG A 1 227 ? -25.133 -10.091 30.039  1.00 40.37 ? 227 ARG A NH2 1 
ATOM   1943 N N   . GLU A 1 228 ? -21.956 -12.180 23.856  1.00 25.79 ? 228 GLU A N   1 
ATOM   1944 C CA  . GLU A 1 228 ? -21.166 -13.397 23.750  1.00 20.54 ? 228 GLU A CA  1 
ATOM   1945 C C   . GLU A 1 228 ? -19.723 -13.075 23.379  1.00 22.62 ? 228 GLU A C   1 
ATOM   1946 O O   . GLU A 1 228 ? -18.785 -13.668 23.930  1.00 20.63 ? 228 GLU A O   1 
ATOM   1947 C CB  . GLU A 1 228 ? -21.811 -14.341 22.729  1.00 34.43 ? 228 GLU A CB  1 
ATOM   1948 C CG  . GLU A 1 228 ? -23.363 -14.387 22.760  1.00 46.56 ? 228 GLU A CG  1 
ATOM   1949 C CD  . GLU A 1 228 ? -24.042 -13.086 22.291  1.00 54.99 ? 228 GLU A CD  1 
ATOM   1950 O OE1 . GLU A 1 228 ? -25.083 -12.700 22.871  1.00 56.75 ? 228 GLU A OE1 1 
ATOM   1951 O OE2 . GLU A 1 228 ? -23.514 -12.432 21.370  1.00 61.22 ? 228 GLU A OE2 1 
ATOM   1952 N N   . ASP A 1 229 ? -19.527 -12.121 22.462  1.00 19.80 ? 229 ASP A N   1 
ATOM   1953 C CA  . ASP A 1 229 ? -18.176 -11.687 22.113  1.00 22.00 ? 229 ASP A CA  1 
ATOM   1954 C C   . ASP A 1 229 ? -17.421 -11.166 23.337  1.00 19.39 ? 229 ASP A C   1 
ATOM   1955 O O   . ASP A 1 229 ? -16.227 -11.445 23.498  1.00 18.40 ? 229 ASP A O   1 
ATOM   1956 C CB  . ASP A 1 229 ? -18.244 -10.624 21.017  1.00 15.33 ? 229 ASP A CB  1 
ATOM   1957 C CG  . ASP A 1 229 ? -18.392 -11.231 19.622  1.00 24.65 ? 229 ASP A CG  1 
ATOM   1958 O OD1 . ASP A 1 229 ? -18.328 -12.476 19.499  1.00 25.39 ? 229 ASP A OD1 1 
ATOM   1959 O OD2 . ASP A 1 229 ? -18.576 -10.469 18.654  1.00 23.43 ? 229 ASP A OD2 1 
ATOM   1960 N N   . ALA A 1 230 ? -18.095 -10.402 24.205  1.00 20.05 ? 230 ALA A N   1 
ATOM   1961 C CA  . ALA A 1 230 ? -17.444 -9.912  25.423  1.00 20.33 ? 230 ALA A CA  1 
ATOM   1962 C C   . ALA A 1 230 ? -16.927 -11.067 26.266  1.00 16.88 ? 230 ALA A C   1 
ATOM   1963 O O   . ALA A 1 230 ? -15.791 -11.037 26.751  1.00 19.26 ? 230 ALA A O   1 
ATOM   1964 C CB  . ALA A 1 230 ? -18.407 -9.048  26.240  1.00 13.95 ? 230 ALA A CB  1 
ATOM   1965 N N   . SER A 1 231 ? -17.753 -12.101 26.450  1.00 17.43 ? 231 SER A N   1 
ATOM   1966 C CA  . SER A 1 231 ? -17.284 -13.313 27.118  1.00 21.26 ? 231 SER A CA  1 
ATOM   1967 C C   . SER A 1 231 ? -16.033 -13.871 26.449  1.00 18.21 ? 231 SER A C   1 
ATOM   1968 O O   . SER A 1 231 ? -15.084 -14.275 27.128  1.00 22.58 ? 231 SER A O   1 
ATOM   1969 C CB  . SER A 1 231 ? -18.389 -14.376 27.125  1.00 29.26 ? 231 SER A CB  1 
ATOM   1970 O OG  . SER A 1 231 ? -19.221 -14.246 28.259  1.00 37.82 ? 231 SER A OG  1 
ATOM   1971 N N   . LYS A 1 232 ? -16.016 -13.903 25.113  1.00 22.05 ? 232 LYS A N   1 
ATOM   1972 C CA  . LYS A 1 232 ? -14.916 -14.534 24.385  1.00 16.47 ? 232 LYS A CA  1 
ATOM   1973 C C   . LYS A 1 232 ? -13.610 -13.759 24.552  1.00 14.93 ? 232 LYS A C   1 
ATOM   1974 O O   . LYS A 1 232 ? -12.546 -14.365 24.736  1.00 20.17 ? 232 LYS A O   1 
ATOM   1975 C CB  . LYS A 1 232 ? -15.275 -14.669 22.899  1.00 24.69 ? 232 LYS A CB  1 
ATOM   1976 C CG  . LYS A 1 232 ? -15.897 -16.010 22.526  1.00 30.51 ? 232 LYS A CG  1 
ATOM   1977 C CD  . LYS A 1 232 ? -16.702 -15.950 21.222  1.00 38.78 ? 232 LYS A CD  1 
ATOM   1978 C CE  . LYS A 1 232 ? -17.934 -15.077 21.410  1.00 46.28 ? 232 LYS A CE  1 
ATOM   1979 N NZ  . LYS A 1 232 ? -18.922 -15.074 20.300  1.00 47.35 ? 232 LYS A NZ  1 
ATOM   1980 N N   . HIS A 1 233 ? -13.663 -12.427 24.472  1.00 13.68 ? 233 HIS A N   1 
ATOM   1981 C CA  . HIS A 1 233 ? -12.475 -11.622 24.759  1.00 20.79 ? 233 HIS A CA  1 
ATOM   1982 C C   . HIS A 1 233 ? -11.853 -12.026 26.093  1.00 19.30 ? 233 HIS A C   1 
ATOM   1983 O O   . HIS A 1 233 ? -10.633 -12.201 26.199  1.00 18.19 ? 233 HIS A O   1 
ATOM   1984 C CB  . HIS A 1 233 ? -12.826 -10.133 24.775  1.00 19.61 ? 233 HIS A CB  1 
ATOM   1985 C CG  . HIS A 1 233 ? -13.063 -9.539  23.415  1.00 20.17 ? 233 HIS A CG  1 
ATOM   1986 N ND1 . HIS A 1 233 ? -12.041 -9.068  22.616  1.00 19.24 ? 233 HIS A ND1 1 
ATOM   1987 C CD2 . HIS A 1 233 ? -14.210 -9.318  22.728  1.00 15.20 ? 233 HIS A CD2 1 
ATOM   1988 C CE1 . HIS A 1 233 ? -12.549 -8.589  21.493  1.00 19.36 ? 233 HIS A CE1 1 
ATOM   1989 N NE2 . HIS A 1 233 ? -13.863 -8.726  21.537  1.00 18.49 ? 233 HIS A NE2 1 
ATOM   1990 N N   . VAL A 1 234 ? -12.684 -12.171 27.127  1.00 17.46 ? 234 VAL A N   1 
ATOM   1991 C CA  . VAL A 1 234 ? -12.155 -12.510 28.443  1.00 16.19 ? 234 VAL A CA  1 
ATOM   1992 C C   . VAL A 1 234 ? -11.624 -13.935 28.440  1.00 15.05 ? 234 VAL A C   1 
ATOM   1993 O O   . VAL A 1 234 ? -10.518 -14.205 28.925  1.00 17.17 ? 234 VAL A O   1 
ATOM   1994 C CB  . VAL A 1 234 ? -13.233 -12.313 29.528  1.00 20.67 ? 234 VAL A CB  1 
ATOM   1995 C CG1 . VAL A 1 234 ? -12.711 -12.789 30.879  1.00 16.48 ? 234 VAL A CG1 1 
ATOM   1996 C CG2 . VAL A 1 234 ? -13.678 -10.856 29.613  1.00 17.77 ? 234 VAL A CG2 1 
ATOM   1997 N N   . GLU A 1 235 ? -12.393 -14.863 27.868  1.00 16.41 ? 235 GLU A N   1 
ATOM   1998 C CA  . GLU A 1 235 ? -12.001 -16.268 27.885  1.00 17.81 ? 235 GLU A CA  1 
ATOM   1999 C C   . GLU A 1 235 ? -10.730 -16.499 27.072  1.00 21.96 ? 235 GLU A C   1 
ATOM   2000 O O   . GLU A 1 235 ? -9.821  -17.203 27.527  1.00 22.71 ? 235 GLU A O   1 
ATOM   2001 C CB  . GLU A 1 235 ? -13.153 -17.134 27.365  1.00 19.72 ? 235 GLU A CB  1 
ATOM   2002 C CG  . GLU A 1 235 ? -12.997 -18.619 27.612  1.00 36.76 ? 235 GLU A CG  1 
ATOM   2003 C CD  . GLU A 1 235 ? -12.415 -18.927 28.976  1.00 46.74 ? 235 GLU A CD  1 
ATOM   2004 O OE1 . GLU A 1 235 ? -11.397 -19.652 29.033  1.00 55.87 ? 235 GLU A OE1 1 
ATOM   2005 O OE2 . GLU A 1 235 ? -12.972 -18.445 29.989  1.00 42.57 ? 235 GLU A OE2 1 
ATOM   2006 N N   . LEU A 1 236 ? -10.636 -15.912 25.870  1.00 18.10 ? 236 LEU A N   1 
ATOM   2007 C CA  . LEU A 1 236 ? -9.420  -16.095 25.081  1.00 21.35 ? 236 LEU A CA  1 
ATOM   2008 C C   . LEU A 1 236 ? -8.202  -15.458 25.749  1.00 17.63 ? 236 LEU A C   1 
ATOM   2009 O O   . LEU A 1 236 ? -7.084  -15.960 25.587  1.00 20.15 ? 236 LEU A O   1 
ATOM   2010 C CB  . LEU A 1 236 ? -9.588  -15.540 23.667  1.00 15.89 ? 236 LEU A CB  1 
ATOM   2011 C CG  . LEU A 1 236 ? -10.593 -16.318 22.803  1.00 17.38 ? 236 LEU A CG  1 
ATOM   2012 C CD1 . LEU A 1 236 ? -11.046 -15.473 21.623  1.00 25.04 ? 236 LEU A CD1 1 
ATOM   2013 C CD2 . LEU A 1 236 ? -10.005 -17.661 22.341  1.00 20.73 ? 236 LEU A CD2 1 
ATOM   2014 N N   . ALA A 1 237 ? -8.392  -14.351 26.482  1.00 17.38 ? 237 ALA A N   1 
ATOM   2015 C CA  . ALA A 1 237 ? -7.273  -13.743 27.192  1.00 15.22 ? 237 ALA A CA  1 
ATOM   2016 C C   . ALA A 1 237 ? -6.749  -14.663 28.287  1.00 22.62 ? 237 ALA A C   1 
ATOM   2017 O O   . ALA A 1 237 ? -5.532  -14.749 28.514  1.00 22.07 ? 237 ALA A O   1 
ATOM   2018 C CB  . ALA A 1 237 ? -7.693  -12.403 27.798  1.00 15.12 ? 237 ALA A CB  1 
ATOM   2019 N N   . LYS A 1 238 ? -7.663  -15.317 29.009  1.00 15.56 ? 238 LYS A N   1 
ATOM   2020 C CA  . LYS A 1 238 ? -7.265  -16.264 30.044  1.00 22.80 ? 238 LYS A CA  1 
ATOM   2021 C C   . LYS A 1 238 ? -6.497  -17.433 29.442  1.00 22.48 ? 238 LYS A C   1 
ATOM   2022 O O   . LYS A 1 238 ? -5.502  -17.888 30.015  1.00 25.66 ? 238 LYS A O   1 
ATOM   2023 C CB  . LYS A 1 238 ? -8.491  -16.777 30.793  1.00 21.46 ? 238 LYS A CB  1 
ATOM   2024 C CG  . LYS A 1 238 ? -9.279  -15.720 31.550  1.00 28.13 ? 238 LYS A CG  1 
ATOM   2025 C CD  . LYS A 1 238 ? -10.495 -16.349 32.236  1.00 28.34 ? 238 LYS A CD  1 
ATOM   2026 C CE  . LYS A 1 238 ? -10.083 -17.506 33.142  1.00 29.94 ? 238 LYS A CE  1 
ATOM   2027 N NZ  . LYS A 1 238 ? -11.269 -18.217 33.704  1.00 37.17 ? 238 LYS A NZ  1 
ATOM   2028 N N   . GLU A 1 239 ? -6.941  -17.922 28.280  1.00 23.36 ? 239 GLU A N   1 
ATOM   2029 C CA  . GLU A 1 239 ? -6.220  -19.002 27.607  1.00 28.67 ? 239 GLU A CA  1 
ATOM   2030 C C   . GLU A 1 239 ? -4.859  -18.529 27.109  1.00 27.28 ? 239 GLU A C   1 
ATOM   2031 O O   . GLU A 1 239 ? -3.866  -19.257 27.221  1.00 27.37 ? 239 GLU A O   1 
ATOM   2032 C CB  . GLU A 1 239 ? -7.056  -19.559 26.453  1.00 32.52 ? 239 GLU A CB  1 
ATOM   2033 C CG  . GLU A 1 239 ? -8.403  -20.115 26.884  1.00 37.32 ? 239 GLU A CG  1 
ATOM   2034 C CD  . GLU A 1 239 ? -9.294  -20.482 25.710  1.00 49.48 ? 239 GLU A CD  1 
ATOM   2035 O OE1 . GLU A 1 239 ? -8.865  -20.295 24.547  1.00 50.11 ? 239 GLU A OE1 1 
ATOM   2036 O OE2 . GLU A 1 239 ? -10.427 -20.955 25.952  1.00 52.88 ? 239 GLU A OE2 1 
ATOM   2037 N N   . LYS A 1 240 ? -4.792  -17.306 26.575  1.00 18.86 ? 240 LYS A N   1 
ATOM   2038 C CA  . LYS A 1 240 ? -3.516  -16.748 26.135  1.00 17.99 ? 240 LYS A CA  1 
ATOM   2039 C C   . LYS A 1 240 ? -2.558  -16.563 27.300  1.00 23.44 ? 240 LYS A C   1 
ATOM   2040 O O   . LYS A 1 240 ? -1.357  -16.846 27.181  1.00 23.60 ? 240 LYS A O   1 
ATOM   2041 C CB  . LYS A 1 240 ? -3.734  -15.409 25.435  1.00 18.77 ? 240 LYS A CB  1 
ATOM   2042 C CG  . LYS A 1 240 ? -2.461  -14.844 24.823  1.00 21.27 ? 240 LYS A CG  1 
ATOM   2043 C CD  . LYS A 1 240 ? -2.043  -15.686 23.623  1.00 32.10 ? 240 LYS A CD  1 
ATOM   2044 C CE  . LYS A 1 240 ? -0.594  -15.438 23.232  1.00 32.15 ? 240 LYS A CE  1 
ATOM   2045 N NZ  . LYS A 1 240 ? -0.272  -16.059 21.911  1.00 35.97 ? 240 LYS A NZ  1 
ATOM   2046 N N   . TYR A 1 241 ? -3.068  -16.055 28.427  1.00 24.95 ? 241 TYR A N   1 
ATOM   2047 C CA  . TYR A 1 241 ? -2.236  -15.907 29.613  1.00 30.10 ? 241 TYR A CA  1 
ATOM   2048 C C   . TYR A 1 241 ? -1.751  -17.265 30.099  1.00 30.92 ? 241 TYR A C   1 
ATOM   2049 O O   . TYR A 1 241 ? -0.595  -17.407 30.513  1.00 31.19 ? 241 TYR A O   1 
ATOM   2050 C CB  . TYR A 1 241 ? -3.019  -15.187 30.712  1.00 30.98 ? 241 TYR A CB  1 
ATOM   2051 C CG  . TYR A 1 241 ? -2.197  -14.772 31.923  1.00 29.57 ? 241 TYR A CG  1 
ATOM   2052 C CD1 . TYR A 1 241 ? -2.029  -15.636 33.002  1.00 26.87 ? 241 TYR A CD1 1 
ATOM   2053 C CD2 . TYR A 1 241 ? -1.599  -13.519 31.988  1.00 31.48 ? 241 TYR A CD2 1 
ATOM   2054 C CE1 . TYR A 1 241 ? -1.286  -15.263 34.112  1.00 22.55 ? 241 TYR A CE1 1 
ATOM   2055 C CE2 . TYR A 1 241 ? -0.855  -13.135 33.097  1.00 31.91 ? 241 TYR A CE2 1 
ATOM   2056 C CZ  . TYR A 1 241 ? -0.699  -14.017 34.154  1.00 24.33 ? 241 TYR A CZ  1 
ATOM   2057 O OH  . TYR A 1 241 ? 0.043   -13.647 35.265  1.00 20.96 ? 241 TYR A OH  1 
ATOM   2058 N N   . PHE A 1 242 ? -2.626  -18.276 30.045  1.00 28.55 ? 242 PHE A N   1 
ATOM   2059 C CA  . PHE A 1 242 ? -2.245  -19.627 30.450  1.00 26.86 ? 242 PHE A CA  1 
ATOM   2060 C C   . PHE A 1 242 ? -1.161  -20.208 29.548  1.00 30.29 ? 242 PHE A C   1 
ATOM   2061 O O   . PHE A 1 242 ? -0.389  -21.072 29.985  1.00 25.21 ? 242 PHE A O   1 
ATOM   2062 C CB  . PHE A 1 242 ? -3.473  -20.542 30.454  1.00 22.49 ? 242 PHE A CB  1 
ATOM   2063 C CG  . PHE A 1 242 ? -3.184  -21.952 30.930  1.00 32.29 ? 242 PHE A CG  1 
ATOM   2064 C CD1 . PHE A 1 242 ? -3.041  -22.231 32.283  1.00 38.15 ? 242 PHE A CD1 1 
ATOM   2065 C CD2 . PHE A 1 242 ? -3.056  -22.991 30.023  1.00 32.57 ? 242 PHE A CD2 1 
ATOM   2066 C CE1 . PHE A 1 242 ? -2.777  -23.524 32.723  1.00 36.79 ? 242 PHE A CE1 1 
ATOM   2067 C CE2 . PHE A 1 242 ? -2.794  -24.282 30.452  1.00 31.48 ? 242 PHE A CE2 1 
ATOM   2068 C CZ  . PHE A 1 242 ? -2.655  -24.549 31.806  1.00 34.52 ? 242 PHE A CZ  1 
ATOM   2069 N N   . GLU A 1 243 ? -1.097  -19.769 28.287  1.00 27.97 ? 243 GLU A N   1 
ATOM   2070 C CA  . GLU A 1 243 ? -0.062  -20.273 27.389  1.00 30.99 ? 243 GLU A CA  1 
ATOM   2071 C C   . GLU A 1 243 ? 1.298   -19.685 27.726  1.00 31.36 ? 243 GLU A C   1 
ATOM   2072 O O   . GLU A 1 243 ? 2.311   -20.393 27.681  1.00 20.87 ? 243 GLU A O   1 
ATOM   2073 C CB  . GLU A 1 243 ? -0.406  -19.960 25.936  1.00 27.80 ? 243 GLU A CB  1 
ATOM   2074 C CG  . GLU A 1 243 ? -1.596  -20.702 25.390  1.00 42.03 ? 243 GLU A CG  1 
ATOM   2075 C CD  . GLU A 1 243 ? -1.837  -20.368 23.935  1.00 52.45 ? 243 GLU A CD  1 
ATOM   2076 O OE1 . GLU A 1 243 ? -1.106  -19.503 23.396  1.00 56.62 ? 243 GLU A OE1 1 
ATOM   2077 O OE2 . GLU A 1 243 ? -2.763  -20.953 23.333  1.00 55.74 ? 243 GLU A OE2 1 
ATOM   2078 N N   . ILE A 1 244 ? 1.339   -18.390 28.054  1.00 24.93 ? 244 ILE A N   1 
ATOM   2079 C CA  . ILE A 1 244 ? 2.603   -17.698 28.292  1.00 23.13 ? 244 ILE A CA  1 
ATOM   2080 C C   . ILE A 1 244 ? 3.146   -18.005 29.682  1.00 28.57 ? 244 ILE A C   1 
ATOM   2081 O O   . ILE A 1 244 ? 4.344   -18.258 29.854  1.00 27.71 ? 244 ILE A O   1 
ATOM   2082 C CB  . ILE A 1 244 ? 2.410   -16.181 28.097  1.00 25.05 ? 244 ILE A CB  1 
ATOM   2083 C CG1 . ILE A 1 244 ? 1.837   -15.900 26.712  1.00 27.22 ? 244 ILE A CG1 1 
ATOM   2084 C CG2 . ILE A 1 244 ? 3.718   -15.426 28.291  1.00 16.14 ? 244 ILE A CG2 1 
ATOM   2085 C CD1 . ILE A 1 244 ? 2.715   -16.388 25.597  1.00 32.59 ? 244 ILE A CD1 1 
ATOM   2086 N N   . PHE A 1 245 ? 2.289   -17.951 30.700  1.00 24.94 ? 245 PHE A N   1 
ATOM   2087 C CA  . PHE A 1 245 ? 2.746   -18.068 32.081  1.00 34.77 ? 245 PHE A CA  1 
ATOM   2088 C C   . PHE A 1 245 ? 2.327   -19.362 32.770  1.00 36.06 ? 245 PHE A C   1 
ATOM   2089 O O   . PHE A 1 245 ? 2.747   -19.598 33.909  1.00 37.32 ? 245 PHE A O   1 
ATOM   2090 C CB  . PHE A 1 245 ? 2.250   -16.863 32.900  1.00 24.67 ? 245 PHE A CB  1 
ATOM   2091 C CG  . PHE A 1 245 ? 2.742   -15.535 32.381  1.00 31.09 ? 245 PHE A CG  1 
ATOM   2092 C CD1 . PHE A 1 245 ? 4.058   -15.138 32.586  1.00 27.59 ? 245 PHE A CD1 1 
ATOM   2093 C CD2 . PHE A 1 245 ? 1.892   -14.687 31.688  1.00 22.25 ? 245 PHE A CD2 1 
ATOM   2094 C CE1 . PHE A 1 245 ? 4.520   -13.932 32.099  1.00 22.68 ? 245 PHE A CE1 1 
ATOM   2095 C CE2 . PHE A 1 245 ? 2.345   -13.470 31.201  1.00 24.08 ? 245 PHE A CE2 1 
ATOM   2096 C CZ  . PHE A 1 245 ? 3.660   -13.090 31.403  1.00 25.92 ? 245 PHE A CZ  1 
ATOM   2097 N N   . GLY A 1 246 ? 1.524   -20.204 32.122  1.00 37.33 ? 246 GLY A N   1 
ATOM   2098 C CA  . GLY A 1 246 ? 1.126   -21.479 32.683  1.00 42.49 ? 246 GLY A CA  1 
ATOM   2099 C C   . GLY A 1 246 ? 0.080   -21.419 33.776  1.00 49.68 ? 246 GLY A C   1 
ATOM   2100 O O   . GLY A 1 246 ? -0.291  -22.471 34.307  1.00 53.80 ? 246 GLY A O   1 
ATOM   2101 N N   . GLU A 1 247 ? -0.404  -20.233 34.133  1.00 42.09 ? 247 GLU A N   1 
ATOM   2102 C CA  . GLU A 1 247 ? -1.399  -20.062 35.179  1.00 40.92 ? 247 GLU A CA  1 
ATOM   2103 C C   . GLU A 1 247 ? -2.611  -19.334 34.614  1.00 35.40 ? 247 GLU A C   1 
ATOM   2104 O O   . GLU A 1 247 ? -2.533  -18.690 33.569  1.00 30.05 ? 247 GLU A O   1 
ATOM   2105 C CB  . GLU A 1 247 ? -0.827  -19.273 36.361  1.00 42.96 ? 247 GLU A CB  1 
ATOM   2106 C CG  . GLU A 1 247 ? -0.121  -20.126 37.398  1.00 55.51 ? 247 GLU A CG  1 
ATOM   2107 C CD  . GLU A 1 247 ? 1.292   -19.648 37.696  1.00 62.35 ? 247 GLU A CD  1 
ATOM   2108 O OE1 . GLU A 1 247 ? 2.085   -20.454 38.232  1.00 64.12 ? 247 GLU A OE1 1 
ATOM   2109 O OE2 . GLU A 1 247 ? 1.608   -18.474 37.399  1.00 62.06 ? 247 GLU A OE2 1 
ATOM   2110 N N   . HIS A 1 248 ? -3.741  -19.458 35.305  1.00 37.78 ? 248 HIS A N   1 
ATOM   2111 C CA  . HIS A 1 248 ? -4.887  -18.632 34.945  1.00 38.96 ? 248 HIS A CA  1 
ATOM   2112 C C   . HIS A 1 248 ? -4.733  -17.251 35.576  1.00 33.67 ? 248 HIS A C   1 
ATOM   2113 O O   . HIS A 1 248 ? -4.291  -17.147 36.720  1.00 27.68 ? 248 HIS A O   1 
ATOM   2114 C CB  . HIS A 1 248 ? -6.190  -19.274 35.415  1.00 46.74 ? 248 HIS A CB  1 
ATOM   2115 C CG  . HIS A 1 248 ? -6.657  -20.400 34.546  1.00 59.47 ? 248 HIS A CG  1 
ATOM   2116 N ND1 . HIS A 1 248 ? -5.798  -21.144 33.765  1.00 62.33 ? 248 HIS A ND1 1 
ATOM   2117 C CD2 . HIS A 1 248 ? -7.894  -20.910 34.334  1.00 63.04 ? 248 HIS A CD2 1 
ATOM   2118 C CE1 . HIS A 1 248 ? -6.484  -22.063 33.109  1.00 62.45 ? 248 HIS A CE1 1 
ATOM   2119 N NE2 . HIS A 1 248 ? -7.759  -21.943 33.437  1.00 63.07 ? 248 HIS A NE2 1 
ATOM   2120 N N   . PRO A 1 249 ? -5.061  -16.177 34.855  1.00 30.78 ? 249 PRO A N   1 
ATOM   2121 C CA  . PRO A 1 249 ? -4.943  -14.839 35.448  1.00 25.68 ? 249 PRO A CA  1 
ATOM   2122 C C   . PRO A 1 249 ? -6.002  -14.626 36.517  1.00 26.51 ? 249 PRO A C   1 
ATOM   2123 O O   . PRO A 1 249 ? -7.177  -14.941 36.322  1.00 35.20 ? 249 PRO A O   1 
ATOM   2124 C CB  . PRO A 1 249 ? -5.143  -13.896 34.256  1.00 24.54 ? 249 PRO A CB  1 
ATOM   2125 C CG  . PRO A 1 249 ? -5.982  -14.679 33.294  1.00 26.53 ? 249 PRO A CG  1 
ATOM   2126 C CD  . PRO A 1 249 ? -5.524  -16.122 33.455  1.00 25.99 ? 249 PRO A CD  1 
ATOM   2127 N N   . VAL A 1 250 ? -5.570  -14.095 37.661  1.00 23.04 ? 250 VAL A N   1 
ATOM   2128 C CA  . VAL A 1 250 ? -6.491  -13.693 38.717  1.00 18.65 ? 250 VAL A CA  1 
ATOM   2129 C C   . VAL A 1 250 ? -6.749  -12.185 38.693  1.00 18.74 ? 250 VAL A C   1 
ATOM   2130 O O   . VAL A 1 250 ? -7.715  -11.717 39.323  1.00 16.82 ? 250 VAL A O   1 
ATOM   2131 C CB  . VAL A 1 250 ? -5.947  -14.174 40.086  1.00 34.67 ? 250 VAL A CB  1 
ATOM   2132 C CG1 . VAL A 1 250 ? -4.484  -13.851 40.212  1.00 37.24 ? 250 VAL A CG1 1 
ATOM   2133 C CG2 . VAL A 1 250 ? -6.724  -13.623 41.271  1.00 45.47 ? 250 VAL A CG2 1 
ATOM   2134 N N   . TYR A 1 251 ? -5.928  -11.419 37.972  1.00 24.98 ? 251 TYR A N   1 
ATOM   2135 C CA  . TYR A 1 251 ? -6.043  -9.972  37.840  1.00 25.67 ? 251 TYR A CA  1 
ATOM   2136 C C   . TYR A 1 251 ? -6.223  -9.608  36.378  1.00 26.23 ? 251 TYR A C   1 
ATOM   2137 O O   . TYR A 1 251 ? -5.599  -10.211 35.504  1.00 25.12 ? 251 TYR A O   1 
ATOM   2138 C CB  . TYR A 1 251 ? -4.789  -9.261  38.351  1.00 25.71 ? 251 TYR A CB  1 
ATOM   2139 C CG  . TYR A 1 251 ? -4.235  -9.918  39.564  1.00 24.25 ? 251 TYR A CG  1 
ATOM   2140 C CD1 . TYR A 1 251 ? -4.982  -9.968  40.716  1.00 30.83 ? 251 TYR A CD1 1 
ATOM   2141 C CD2 . TYR A 1 251 ? -2.987  -10.526 39.550  1.00 32.93 ? 251 TYR A CD2 1 
ATOM   2142 C CE1 . TYR A 1 251 ? -4.513  -10.580 41.828  1.00 41.79 ? 251 TYR A CE1 1 
ATOM   2143 C CE2 . TYR A 1 251 ? -2.501  -11.147 40.677  1.00 30.19 ? 251 TYR A CE2 1 
ATOM   2144 C CZ  . TYR A 1 251 ? -3.281  -11.166 41.816  1.00 37.80 ? 251 TYR A CZ  1 
ATOM   2145 O OH  . TYR A 1 251 ? -2.861  -11.781 42.967  1.00 44.79 ? 251 TYR A OH  1 
ATOM   2146 N N   . MET A 1 252 ? -7.040  -8.589  36.119  1.00 18.65 ? 252 MET A N   1 
ATOM   2147 C CA  . MET A 1 252 ? -7.173  -8.053  34.780  1.00 16.16 ? 252 MET A CA  1 
ATOM   2148 C C   . MET A 1 252 ? -7.256  -6.541  34.860  1.00 15.77 ? 252 MET A C   1 
ATOM   2149 O O   . MET A 1 252 ? -7.864  -5.994  35.783  1.00 15.02 ? 252 MET A O   1 
ATOM   2150 C CB  . MET A 1 252 ? -8.427  -8.593  34.060  1.00 21.04 ? 252 MET A CB  1 
ATOM   2151 C CG  . MET A 1 252 ? -8.316  -10.052 33.612  1.00 21.86 ? 252 MET A CG  1 
ATOM   2152 S SD  . MET A 1 252 ? -9.307  -10.408 32.134  1.00 20.37 ? 252 MET A SD  1 
ATOM   2153 C CE  . MET A 1 252 ? -8.791  -12.089 31.759  1.00 19.47 ? 252 MET A CE  1 
ATOM   2154 N N   . TRP A 1 253 ? -6.651  -5.885  33.878  1.00 11.90 ? 253 TRP A N   1 
ATOM   2155 C CA  . TRP A 1 253 ? -6.856  -4.463  33.654  1.00 16.74 ? 253 TRP A CA  1 
ATOM   2156 C C   . TRP A 1 253 ? -7.979  -4.280  32.642  1.00 18.17 ? 253 TRP A C   1 
ATOM   2157 O O   . TRP A 1 253 ? -7.857  -4.757  31.503  1.00 12.54 ? 253 TRP A O   1 
ATOM   2158 C CB  . TRP A 1 253 ? -5.585  -3.809  33.144  1.00 13.30 ? 253 TRP A CB  1 
ATOM   2159 C CG  . TRP A 1 253 ? -5.813  -2.407  32.676  1.00 9.28  ? 253 TRP A CG  1 
ATOM   2160 C CD1 . TRP A 1 253 ? -5.726  -1.949  31.390  1.00 11.43 ? 253 TRP A CD1 1 
ATOM   2161 C CD2 . TRP A 1 253 ? -6.185  -1.279  33.480  1.00 14.11 ? 253 TRP A CD2 1 
ATOM   2162 N NE1 . TRP A 1 253 ? -6.017  -0.609  31.345  1.00 10.12 ? 253 TRP A NE1 1 
ATOM   2163 C CE2 . TRP A 1 253 ? -6.306  -0.174  32.614  1.00 12.06 ? 253 TRP A CE2 1 
ATOM   2164 C CE3 . TRP A 1 253 ? -6.431  -1.098  34.844  1.00 15.03 ? 253 TRP A CE3 1 
ATOM   2165 C CZ2 . TRP A 1 253 ? -6.658  1.099   33.068  1.00 14.73 ? 253 TRP A CZ2 1 
ATOM   2166 C CZ3 . TRP A 1 253 ? -6.788  0.171   35.296  1.00 20.92 ? 253 TRP A CZ3 1 
ATOM   2167 C CH2 . TRP A 1 253 ? -6.890  1.251   34.411  1.00 17.24 ? 253 TRP A CH2 1 
ATOM   2168 N N   . PRO A 1 254 ? -9.089  -3.655  33.014  1.00 15.42 ? 254 PRO A N   1 
ATOM   2169 C CA  . PRO A 1 254 ? -10.149 -3.394  32.055  1.00 12.22 ? 254 PRO A CA  1 
ATOM   2170 C C   . PRO A 1 254 ? -9.715  -2.317  31.087  1.00 11.16 ? 254 PRO A C   1 
ATOM   2171 O O   . PRO A 1 254 ? -9.258  -1.246  31.514  1.00 12.39 ? 254 PRO A O   1 
ATOM   2172 C CB  . PRO A 1 254 ? -11.322 -2.914  32.931  1.00 10.53 ? 254 PRO A CB  1 
ATOM   2173 C CG  . PRO A 1 254 ? -10.677 -2.388  34.163  1.00 16.03 ? 254 PRO A CG  1 
ATOM   2174 C CD  . PRO A 1 254 ? -9.431  -3.210  34.373  1.00 12.34 ? 254 PRO A CD  1 
ATOM   2175 N N   . PRO A 1 255 ? -9.818  -2.570  29.785  1.00 13.31 ? 255 PRO A N   1 
ATOM   2176 C CA  . PRO A 1 255 ? -9.377  -1.576  28.795  1.00 12.45 ? 255 PRO A CA  1 
ATOM   2177 C C   . PRO A 1 255 ? -10.004 -0.201  29.031  1.00 11.20 ? 255 PRO A C   1 
ATOM   2178 O O   . PRO A 1 255 ? -11.201 -0.076  29.301  1.00 13.39 ? 255 PRO A O   1 
ATOM   2179 C CB  . PRO A 1 255 ? -9.830  -2.191  27.465  1.00 14.10 ? 255 PRO A CB  1 
ATOM   2180 C CG  . PRO A 1 255 ? -9.764  -3.683  27.715  1.00 11.56 ? 255 PRO A CG  1 
ATOM   2181 C CD  . PRO A 1 255 ? -10.193 -3.855  29.166  1.00 14.99 ? 255 PRO A CD  1 
ATOM   2182 N N   . GLU A 1 256 ? -9.194  0.815   28.952  1.00 13.93 ? 256 GLU A N   1 
ATOM   2183 C CA  . GLU A 1 256 ? -9.626  2.203   29.199  1.00 14.18 ? 256 GLU A CA  1 
ATOM   2184 C C   . GLU A 1 256 ? -10.239 2.389   30.613  1.00 15.10 ? 256 GLU A C   1 
ATOM   2185 O O   . GLU A 1 256 ? -11.025 3.315   30.863  1.00 13.56 ? 256 GLU A O   1 
ATOM   2186 C CB  . GLU A 1 256 ? -10.592 2.665   28.110  1.00 17.82 ? 256 GLU A CB  1 
ATOM   2187 C CG  . GLU A 1 256 ? -10.066 2.599   26.693  1.00 16.98 ? 256 GLU A CG  1 
ATOM   2188 C CD  . GLU A 1 256 ? -8.748  3.342   26.442  1.00 17.83 ? 256 GLU A CD  1 
ATOM   2189 O OE1 . GLU A 1 256 ? -8.444  4.233   27.134  1.00 23.39 ? 256 GLU A OE1 1 
ATOM   2190 O OE2 . GLU A 1 256 ? -8.028  3.015   25.552  1.00 19.61 ? 256 GLU A OE2 1 
ATOM   2191 N N   . ALA A 1 257 ? -9.825  1.515   31.503  1.00 8.97  ? 257 ALA A N   1 
ATOM   2192 C CA  . ALA A 1 257 ? -10.371 1.455   32.859  1.00 9.51  ? 257 ALA A CA  1 
ATOM   2193 C C   . ALA A 1 257 ? -11.885 1.246   32.868  1.00 16.34 ? 257 ALA A C   1 
ATOM   2194 O O   . ALA A 1 257 ? -12.549 1.523   33.874  1.00 16.62 ? 257 ALA A O   1 
ATOM   2195 C CB  . ALA A 1 257 ? -10.006 2.715   33.657  1.00 9.78  ? 257 ALA A CB  1 
ATOM   2196 N N   . SER A 1 258 ? -12.449 0.734   31.780  1.00 14.06 ? 258 SER A N   1 
ATOM   2197 C CA  . SER A 1 258 ? -13.895 0.749   31.616  1.00 9.80  ? 258 SER A CA  1 
ATOM   2198 C C   . SER A 1 258 ? -14.564 -0.355  32.418  1.00 9.81  ? 258 SER A C   1 
ATOM   2199 O O   . SER A 1 258 ? -14.217 -1.540  32.299  1.00 14.66 ? 258 SER A O   1 
ATOM   2200 C CB  . SER A 1 258 ? -14.279 0.623   30.142  1.00 10.52 ? 258 SER A CB  1 
ATOM   2201 O OG  . SER A 1 258 ? -15.654 0.931   30.020  1.00 17.59 ? 258 SER A OG  1 
ATOM   2202 N N   . VAL A 1 259 ? -15.530 0.040   33.246  1.00 13.28 ? 259 VAL A N   1 
ATOM   2203 C CA  . VAL A 1 259 ? -16.299 -0.902  34.039  1.00 15.26 ? 259 VAL A CA  1 
ATOM   2204 C C   . VAL A 1 259 ? -17.764 -0.496  34.006  1.00 14.36 ? 259 VAL A C   1 
ATOM   2205 O O   . VAL A 1 259 ? -18.128 0.615   33.621  1.00 13.11 ? 259 VAL A O   1 
ATOM   2206 C CB  . VAL A 1 259 ? -15.808 -0.993  35.503  1.00 15.09 ? 259 VAL A CB  1 
ATOM   2207 C CG1 . VAL A 1 259 ? -14.321 -1.453  35.572  1.00 12.07 ? 259 VAL A CG1 1 
ATOM   2208 C CG2 . VAL A 1 259 ? -16.022 0.330   36.213  1.00 11.19 ? 259 VAL A CG2 1 
ATOM   2209 N N   . SER A 1 260 ? -18.601 -1.435  34.408  1.00 17.02 ? 260 SER A N   1 
ATOM   2210 C CA  . SER A 1 260 ? -20.032 -1.236  34.545  1.00 14.25 ? 260 SER A CA  1 
ATOM   2211 C C   . SER A 1 260 ? -20.496 -2.353  35.452  1.00 18.50 ? 260 SER A C   1 
ATOM   2212 O O   . SER A 1 260 ? -19.747 -3.289  35.720  1.00 13.45 ? 260 SER A O   1 
ATOM   2213 C CB  . SER A 1 260 ? -20.752 -1.303  33.197  1.00 13.47 ? 260 SER A CB  1 
ATOM   2214 O OG  . SER A 1 260 ? -20.636 -2.609  32.661  1.00 18.09 ? 260 SER A OG  1 
ATOM   2215 N N   . ASN A 1 261 ? -21.739 -2.255  35.918  1.00 15.85 ? 261 ASN A N   1 
ATOM   2216 C CA  . ASN A 1 261 ? -22.274 -3.327  36.749  1.00 15.11 ? 261 ASN A CA  1 
ATOM   2217 C C   . ASN A 1 261 ? -22.192 -4.672  36.033  1.00 16.08 ? 261 ASN A C   1 
ATOM   2218 O O   . ASN A 1 261 ? -21.783 -5.674  36.630  1.00 17.53 ? 261 ASN A O   1 
ATOM   2219 C CB  . ASN A 1 261 ? -23.711 -3.009  37.146  1.00 14.00 ? 261 ASN A CB  1 
ATOM   2220 C CG  . ASN A 1 261 ? -23.798 -1.911  38.172  1.00 21.42 ? 261 ASN A CG  1 
ATOM   2221 O OD1 . ASN A 1 261 ? -22.844 -1.662  38.914  1.00 19.32 ? 261 ASN A OD1 1 
ATOM   2222 N ND2 . ASN A 1 261 ? -24.945 -1.230  38.216  1.00 18.02 ? 261 ASN A ND2 1 
ATOM   2223 N N   . GLU A 1 262 ? -22.541 -4.708  34.739  1.00 17.73 ? 262 GLU A N   1 
ATOM   2224 C CA  . GLU A 1 262 ? -22.538 -5.977  34.017  1.00 18.88 ? 262 GLU A CA  1 
ATOM   2225 C C   . GLU A 1 262 ? -21.124 -6.463  33.727  1.00 16.39 ? 262 GLU A C   1 
ATOM   2226 O O   . GLU A 1 262 ? -20.873 -7.671  33.738  1.00 19.82 ? 262 GLU A O   1 
ATOM   2227 C CB  . GLU A 1 262 ? -23.354 -5.861  32.721  1.00 16.02 ? 262 GLU A CB  1 
ATOM   2228 C CG  . GLU A 1 262 ? -24.839 -5.675  32.995  1.00 22.93 ? 262 GLU A CG  1 
ATOM   2229 C CD  . GLU A 1 262 ? -25.691 -5.672  31.741  1.00 29.60 ? 262 GLU A CD  1 
ATOM   2230 O OE1 . GLU A 1 262 ? -26.646 -4.866  31.689  1.00 36.35 ? 262 GLU A OE1 1 
ATOM   2231 O OE2 . GLU A 1 262 ? -25.410 -6.470  30.816  1.00 29.05 ? 262 GLU A OE2 1 
ATOM   2232 N N   . ALA A 1 263 ? -20.187 -5.548  33.450  1.00 14.67 ? 263 ALA A N   1 
ATOM   2233 C CA  . ALA A 1 263 ? -18.810 -5.967  33.178  1.00 14.40 ? 263 ALA A CA  1 
ATOM   2234 C C   . ALA A 1 263 ? -18.153 -6.547  34.425  1.00 12.24 ? 263 ALA A C   1 
ATOM   2235 O O   . ALA A 1 263 ? -17.474 -7.577  34.357  1.00 17.90 ? 263 ALA A O   1 
ATOM   2236 C CB  . ALA A 1 263 ? -17.996 -4.784  32.643  1.00 11.28 ? 263 ALA A CB  1 
ATOM   2237 N N   . LEU A 1 264 ? -18.342 -5.900  35.577  1.00 17.70 ? 264 LEU A N   1 
ATOM   2238 C CA  . LEU A 1 264 ? -17.814 -6.464  36.818  1.00 12.44 ? 264 LEU A CA  1 
ATOM   2239 C C   . LEU A 1 264 ? -18.388 -7.854  37.068  1.00 19.16 ? 264 LEU A C   1 
ATOM   2240 O O   . LEU A 1 264 ? -17.666 -8.761  37.493  1.00 16.96 ? 264 LEU A O   1 
ATOM   2241 C CB  . LEU A 1 264 ? -18.116 -5.530  37.995  1.00 10.85 ? 264 LEU A CB  1 
ATOM   2242 C CG  . LEU A 1 264 ? -17.450 -4.150  37.882  1.00 14.11 ? 264 LEU A CG  1 
ATOM   2243 C CD1 . LEU A 1 264 ? -17.967 -3.189  38.950  1.00 14.38 ? 264 LEU A CD1 1 
ATOM   2244 C CD2 . LEU A 1 264 ? -15.922 -4.264  37.965  1.00 24.45 ? 264 LEU A CD2 1 
ATOM   2245 N N   . GLU A 1 265 ? -19.677 -8.054  36.773  1.00 16.61 ? 265 GLU A N   1 
ATOM   2246 C CA  . GLU A 1 265 ? -20.259 -9.389  36.894  1.00 18.00 ? 265 GLU A CA  1 
ATOM   2247 C C   . GLU A 1 265 ? -19.596 -10.375 35.938  1.00 24.70 ? 265 GLU A C   1 
ATOM   2248 O O   . GLU A 1 265 ? -19.340 -11.521 36.310  1.00 18.38 ? 265 GLU A O   1 
ATOM   2249 C CB  . GLU A 1 265 ? -21.770 -9.347  36.643  1.00 23.76 ? 265 GLU A CB  1 
ATOM   2250 C CG  . GLU A 1 265 ? -22.572 -8.818  37.813  1.00 33.75 ? 265 GLU A CG  1 
ATOM   2251 C CD  . GLU A 1 265 ? -24.051 -8.712  37.500  1.00 42.80 ? 265 GLU A CD  1 
ATOM   2252 O OE1 . GLU A 1 265 ? -24.486 -9.284  36.480  1.00 50.12 ? 265 GLU A OE1 1 
ATOM   2253 O OE2 . GLU A 1 265 ? -24.774 -8.043  38.265  1.00 52.91 ? 265 GLU A OE2 1 
ATOM   2254 N N   . LEU A 1 266 ? -19.311 -9.955  34.704  1.00 20.37 ? 266 LEU A N   1 
ATOM   2255 C CA  . LEU A 1 266 ? -18.632 -10.859 33.778  1.00 14.14 ? 266 LEU A CA  1 
ATOM   2256 C C   . LEU A 1 266 ? -17.236 -11.216 34.285  1.00 20.31 ? 266 LEU A C   1 
ATOM   2257 O O   . LEU A 1 266 ? -16.873 -12.399 34.351  1.00 20.31 ? 266 LEU A O   1 
ATOM   2258 C CB  . LEU A 1 266 ? -18.568 -10.232 32.381  1.00 14.50 ? 266 LEU A CB  1 
ATOM   2259 C CG  . LEU A 1 266 ? -17.735 -10.931 31.308  1.00 18.04 ? 266 LEU A CG  1 
ATOM   2260 C CD1 . LEU A 1 266 ? -18.173 -12.376 31.116  1.00 17.62 ? 266 LEU A CD1 1 
ATOM   2261 C CD2 . LEU A 1 266 ? -17.842 -10.155 29.989  1.00 16.71 ? 266 LEU A CD2 1 
ATOM   2262 N N   . TYR A 1 267 ? -16.437 -10.207 34.650  1.00 14.27 ? 267 TYR A N   1 
ATOM   2263 C CA  . TYR A 1 267 ? -15.117 -10.477 35.208  1.00 12.00 ? 267 TYR A CA  1 
ATOM   2264 C C   . TYR A 1 267 ? -15.191 -11.446 36.390  1.00 15.11 ? 267 TYR A C   1 
ATOM   2265 O O   . TYR A 1 267 ? -14.408 -12.400 36.465  1.00 16.57 ? 267 TYR A O   1 
ATOM   2266 C CB  . TYR A 1 267 ? -14.442 -9.173  35.634  1.00 15.77 ? 267 TYR A CB  1 
ATOM   2267 C CG  . TYR A 1 267 ? -13.922 -8.349  34.481  1.00 18.32 ? 267 TYR A CG  1 
ATOM   2268 C CD1 . TYR A 1 267 ? -12.912 -8.832  33.651  1.00 15.12 ? 267 TYR A CD1 1 
ATOM   2269 C CD2 . TYR A 1 267 ? -14.434 -7.086  34.229  1.00 12.82 ? 267 TYR A CD2 1 
ATOM   2270 C CE1 . TYR A 1 267 ? -12.424 -8.088  32.598  1.00 17.13 ? 267 TYR A CE1 1 
ATOM   2271 C CE2 . TYR A 1 267 ? -13.962 -6.327  33.168  1.00 18.58 ? 267 TYR A CE2 1 
ATOM   2272 C CZ  . TYR A 1 267 ? -12.953 -6.827  32.361  1.00 18.77 ? 267 TYR A CZ  1 
ATOM   2273 O OH  . TYR A 1 267 ? -12.488 -6.066  31.312  1.00 12.14 ? 267 TYR A OH  1 
ATOM   2274 N N   . TYR A 1 268 ? -16.147 -11.236 37.302  1.00 14.50 ? 268 TYR A N   1 
ATOM   2275 C CA  . TYR A 1 268 ? -16.308 -12.146 38.433  1.00 18.01 ? 268 TYR A CA  1 
ATOM   2276 C C   . TYR A 1 268 ? -16.627 -13.561 37.958  1.00 17.66 ? 268 TYR A C   1 
ATOM   2277 O O   . TYR A 1 268 ? -16.056 -14.536 38.457  1.00 18.79 ? 268 TYR A O   1 
ATOM   2278 C CB  . TYR A 1 268 ? -17.404 -11.640 39.375  1.00 22.71 ? 268 TYR A CB  1 
ATOM   2279 C CG  . TYR A 1 268 ? -17.908 -12.720 40.299  1.00 19.62 ? 268 TYR A CG  1 
ATOM   2280 C CD1 . TYR A 1 268 ? -17.188 -13.077 41.430  1.00 25.06 ? 268 TYR A CD1 1 
ATOM   2281 C CD2 . TYR A 1 268 ? -19.089 -13.397 40.035  1.00 24.92 ? 268 TYR A CD2 1 
ATOM   2282 C CE1 . TYR A 1 268 ? -17.632 -14.073 42.277  1.00 30.88 ? 268 TYR A CE1 1 
ATOM   2283 C CE2 . TYR A 1 268 ? -19.537 -14.396 40.876  1.00 22.28 ? 268 TYR A CE2 1 
ATOM   2284 C CZ  . TYR A 1 268 ? -18.806 -14.733 41.987  1.00 26.74 ? 268 TYR A CZ  1 
ATOM   2285 O OH  . TYR A 1 268 ? -19.264 -15.726 42.823  1.00 37.97 ? 268 TYR A OH  1 
ATOM   2286 N N   . GLU A 1 269 ? -17.542 -13.697 36.996  1.00 19.31 ? 269 GLU A N   1 
ATOM   2287 C CA  . GLU A 1 269 ? -17.950 -15.032 36.556  1.00 27.57 ? 269 GLU A CA  1 
ATOM   2288 C C   . GLU A 1 269 ? -16.848 -15.769 35.810  1.00 27.12 ? 269 GLU A C   1 
ATOM   2289 O O   . GLU A 1 269 ? -16.881 -17.002 35.745  1.00 30.00 ? 269 GLU A O   1 
ATOM   2290 C CB  . GLU A 1 269 ? -19.194 -14.956 35.663  1.00 28.91 ? 269 GLU A CB  1 
ATOM   2291 C CG  . GLU A 1 269 ? -20.490 -14.694 36.411  1.00 36.20 ? 269 GLU A CG  1 
ATOM   2292 C CD  . GLU A 1 269 ? -20.933 -15.864 37.286  1.00 44.80 ? 269 GLU A CD  1 
ATOM   2293 O OE1 . GLU A 1 269 ? -21.873 -15.675 38.088  1.00 44.23 ? 269 GLU A OE1 1 
ATOM   2294 O OE2 . GLU A 1 269 ? -20.351 -16.967 37.175  1.00 44.65 ? 269 GLU A OE2 1 
ATOM   2295 N N   . LYS A 1 270 ? -15.889 -15.051 35.233  1.00 22.06 ? 270 LYS A N   1 
ATOM   2296 C CA  . LYS A 1 270 ? -14.730 -15.660 34.599  1.00 22.59 ? 270 LYS A CA  1 
ATOM   2297 C C   . LYS A 1 270 ? -13.574 -15.890 35.571  1.00 25.04 ? 270 LYS A C   1 
ATOM   2298 O O   . LYS A 1 270 ? -12.469 -16.243 35.140  1.00 18.10 ? 270 LYS A O   1 
ATOM   2299 C CB  . LYS A 1 270 ? -14.275 -14.794 33.420  1.00 20.66 ? 270 LYS A CB  1 
ATOM   2300 C CG  . LYS A 1 270 ? -15.283 -14.771 32.276  1.00 23.28 ? 270 LYS A CG  1 
ATOM   2301 C CD  . LYS A 1 270 ? -15.440 -16.170 31.702  1.00 32.79 ? 270 LYS A CD  1 
ATOM   2302 C CE  . LYS A 1 270 ? -16.514 -16.242 30.628  1.00 40.41 ? 270 LYS A CE  1 
ATOM   2303 N NZ  . LYS A 1 270 ? -16.932 -17.660 30.394  1.00 46.57 ? 270 LYS A NZ  1 
ATOM   2304 N N   . GLY A 1 271 ? -13.796 -15.703 36.868  1.00 22.69 ? 271 GLY A N   1 
ATOM   2305 C CA  . GLY A 1 271 ? -12.783 -16.023 37.849  1.00 25.44 ? 271 GLY A CA  1 
ATOM   2306 C C   . GLY A 1 271 ? -11.794 -14.923 38.158  1.00 21.09 ? 271 GLY A C   1 
ATOM   2307 O O   . GLY A 1 271 ? -10.772 -15.192 38.805  1.00 21.91 ? 271 GLY A O   1 
ATOM   2308 N N   . ILE A 1 272 ? -12.040 -13.700 37.708  1.00 13.77 ? 272 ILE A N   1 
ATOM   2309 C CA  . ILE A 1 272 ? -11.165 -12.589 38.055  1.00 15.93 ? 272 ILE A CA  1 
ATOM   2310 C C   . ILE A 1 272 ? -11.502 -12.163 39.475  1.00 17.52 ? 272 ILE A C   1 
ATOM   2311 O O   . ILE A 1 272 ? -12.677 -11.987 39.811  1.00 25.11 ? 272 ILE A O   1 
ATOM   2312 C CB  . ILE A 1 272 ? -11.344 -11.430 37.058  1.00 22.52 ? 272 ILE A CB  1 
ATOM   2313 C CG1 . ILE A 1 272 ? -11.181 -11.938 35.620  1.00 21.26 ? 272 ILE A CG1 1 
ATOM   2314 C CG2 . ILE A 1 272 ? -10.388 -10.287 37.381  1.00 20.51 ? 272 ILE A CG2 1 
ATOM   2315 C CD1 . ILE A 1 272 ? -9.947  -12.796 35.382  1.00 25.39 ? 272 ILE A CD1 1 
ATOM   2316 N N   . ASN A 1 273 ? -10.476 -12.024 40.327  1.00 20.89 ? 273 ASN A N   1 
ATOM   2317 C CA  . ASN A 1 273 ? -10.703 -11.692 41.730  1.00 24.76 ? 273 ASN A CA  1 
ATOM   2318 C C   . ASN A 1 273 ? -10.466 -10.227 42.055  1.00 17.57 ? 273 ASN A C   1 
ATOM   2319 O O   . ASN A 1 273 ? -10.969 -9.755  43.078  1.00 21.88 ? 273 ASN A O   1 
ATOM   2320 C CB  . ASN A 1 273 ? -9.801  -12.533 42.644  1.00 31.80 ? 273 ASN A CB  1 
ATOM   2321 C CG  . ASN A 1 273 ? -10.262 -13.976 42.759  1.00 49.47 ? 273 ASN A CG  1 
ATOM   2322 O OD1 . ASN A 1 273 ? -11.431 -14.293 42.527  1.00 53.35 ? 273 ASN A OD1 1 
ATOM   2323 N ND2 . ASN A 1 273 ? -9.335  -14.863 43.112  1.00 53.69 ? 273 ASN A ND2 1 
ATOM   2324 N N   . MET A 1 274 ? -9.697  -9.513  41.239  1.00 23.95 ? 274 MET A N   1 
ATOM   2325 C CA  . MET A 1 274 ? -9.404  -8.110  41.500  1.00 13.06 ? 274 MET A CA  1 
ATOM   2326 C C   . MET A 1 274 ? -9.135  -7.401  40.183  1.00 17.63 ? 274 MET A C   1 
ATOM   2327 O O   . MET A 1 274 ? -8.473  -7.949  39.299  1.00 19.39 ? 274 MET A O   1 
ATOM   2328 C CB  . MET A 1 274 ? -8.192  -7.954  42.427  1.00 14.30 ? 274 MET A CB  1 
ATOM   2329 C CG  . MET A 1 274 ? -7.870  -6.510  42.783  1.00 28.52 ? 274 MET A CG  1 
ATOM   2330 S SD  . MET A 1 274 ? -6.783  -5.701  41.585  1.00 36.30 ? 274 MET A SD  1 
ATOM   2331 C CE  . MET A 1 274 ? -5.185  -6.293  42.167  1.00 30.49 ? 274 MET A CE  1 
ATOM   2332 N N   . LEU A 1 275 ? -9.633  -6.173  40.062  1.00 11.56 ? 275 LEU A N   1 
ATOM   2333 C CA  . LEU A 1 275 ? -9.235  -5.308  38.964  1.00 15.48 ? 275 LEU A CA  1 
ATOM   2334 C C   . LEU A 1 275 ? -9.085  -3.901  39.512  1.00 17.65 ? 275 LEU A C   1 
ATOM   2335 O O   . LEU A 1 275 ? -9.341  -3.641  40.688  1.00 14.31 ? 275 LEU A O   1 
ATOM   2336 C CB  . LEU A 1 275 ? -10.238 -5.344  37.805  1.00 20.04 ? 275 LEU A CB  1 
ATOM   2337 C CG  . LEU A 1 275 ? -11.725 -5.134  38.085  1.00 26.74 ? 275 LEU A CG  1 
ATOM   2338 C CD1 . LEU A 1 275 ? -12.072 -3.662  38.253  1.00 30.17 ? 275 LEU A CD1 1 
ATOM   2339 C CD2 . LEU A 1 275 ? -12.539 -5.749  36.950  1.00 27.49 ? 275 LEU A CD2 1 
ATOM   2340 N N   . ALA A 1 276 ? -8.674  -2.988  38.647  1.00 14.85 ? 276 ALA A N   1 
ATOM   2341 C CA  . ALA A 1 276 ? -8.615  -1.585  39.008  1.00 14.18 ? 276 ALA A CA  1 
ATOM   2342 C C   . ALA A 1 276 ? -9.355  -0.782  37.953  1.00 11.32 ? 276 ALA A C   1 
ATOM   2343 O O   . ALA A 1 276 ? -9.547  -1.231  36.815  1.00 14.21 ? 276 ALA A O   1 
ATOM   2344 C CB  . ALA A 1 276 ? -7.175  -1.078  39.153  1.00 15.26 ? 276 ALA A CB  1 
ATOM   2345 N N   . THR A 1 277 ? -9.761  0.416   38.346  1.00 10.77 ? 277 THR A N   1 
ATOM   2346 C CA  . THR A 1 277 ? -10.394 1.348   37.427  1.00 12.63 ? 277 THR A CA  1 
ATOM   2347 C C   . THR A 1 277 ? -10.028 2.753   37.895  1.00 16.26 ? 277 THR A C   1 
ATOM   2348 O O   . THR A 1 277 ? -9.013  2.940   38.574  1.00 19.18 ? 277 THR A O   1 
ATOM   2349 C CB  . THR A 1 277 ? -11.905 1.052   37.322  1.00 18.65 ? 277 THR A CB  1 
ATOM   2350 O OG1 . THR A 1 277 ? -12.545 2.061   36.535  1.00 14.77 ? 277 THR A OG1 1 
ATOM   2351 C CG2 . THR A 1 277 ? -12.563 0.974   38.699  1.00 17.75 ? 277 THR A CG2 1 
ATOM   2352 N N   . ASP A 1 278 ? -10.822 3.748   37.513  1.00 12.22 ? 278 ASP A N   1 
ATOM   2353 C CA  . ASP A 1 278 ? -10.407 5.136   37.654  1.00 13.30 ? 278 ASP A CA  1 
ATOM   2354 C C   . ASP A 1 278 ? -11.238 5.856   38.711  1.00 16.03 ? 278 ASP A C   1 
ATOM   2355 O O   . ASP A 1 278 ? -12.427 5.580   38.893  1.00 13.22 ? 278 ASP A O   1 
ATOM   2356 C CB  . ASP A 1 278 ? -10.512 5.874   36.320  1.00 14.44 ? 278 ASP A CB  1 
ATOM   2357 C CG  . ASP A 1 278 ? -10.012 7.301   36.403  1.00 19.95 ? 278 ASP A CG  1 
ATOM   2358 O OD1 . ASP A 1 278 ? -8.810  7.496   36.664  1.00 18.63 ? 278 ASP A OD1 1 
ATOM   2359 O OD2 . ASP A 1 278 ? -10.821 8.230   36.212  1.00 22.30 ? 278 ASP A OD2 1 
ATOM   2360 N N   . GLU A 1 279 ? -10.607 6.811   39.395  1.00 14.72 ? 279 GLU A N   1 
ATOM   2361 C CA  . GLU A 1 279 ? -11.338 7.475   40.466  1.00 22.91 ? 279 GLU A CA  1 
ATOM   2362 C C   . GLU A 1 279 ? -12.411 8.448   39.969  1.00 16.25 ? 279 GLU A C   1 
ATOM   2363 O O   . GLU A 1 279 ? -13.255 8.847   40.773  1.00 24.91 ? 279 GLU A O   1 
ATOM   2364 C CB  . GLU A 1 279 ? -10.366 8.169   41.431  1.00 26.53 ? 279 GLU A CB  1 
ATOM   2365 C CG  . GLU A 1 279 ? -9.928  9.569   41.104  1.00 30.51 ? 279 GLU A CG  1 
ATOM   2366 C CD  . GLU A 1 279 ? -9.095  10.176  42.241  1.00 32.46 ? 279 GLU A CD  1 
ATOM   2367 O OE1 . GLU A 1 279 ? -9.673  10.641  43.257  1.00 31.06 ? 279 GLU A OE1 1 
ATOM   2368 O OE2 . GLU A 1 279 ? -7.852  10.156  42.130  1.00 25.78 ? 279 GLU A OE2 1 
ATOM   2369 N N   . VAL A 1 280 ? -12.439 8.823   38.684  1.00 13.98 ? 280 VAL A N   1 
ATOM   2370 C CA  . VAL A 1 280 ? -13.622 9.542   38.195  1.00 13.33 ? 280 VAL A CA  1 
ATOM   2371 C C   . VAL A 1 280 ? -14.851 8.645   38.290  1.00 20.58 ? 280 VAL A C   1 
ATOM   2372 O O   . VAL A 1 280 ? -15.935 9.077   38.702  1.00 21.52 ? 280 VAL A O   1 
ATOM   2373 C CB  . VAL A 1 280 ? -13.413 10.051  36.757  1.00 19.45 ? 280 VAL A CB  1 
ATOM   2374 C CG1 . VAL A 1 280 ? -14.731 10.573  36.196  1.00 24.45 ? 280 VAL A CG1 1 
ATOM   2375 C CG2 . VAL A 1 280 ? -12.368 11.154  36.721  1.00 27.47 ? 280 VAL A CG2 1 
ATOM   2376 N N   . ILE A 1 281 ? -14.699 7.377   37.912  1.00 15.11 ? 281 ILE A N   1 
ATOM   2377 C CA  . ILE A 1 281 ? -15.795 6.425   38.033  1.00 15.54 ? 281 ILE A CA  1 
ATOM   2378 C C   . ILE A 1 281 ? -16.186 6.261   39.493  1.00 18.26 ? 281 ILE A C   1 
ATOM   2379 O O   . ILE A 1 281 ? -17.377 6.176   39.834  1.00 17.86 ? 281 ILE A O   1 
ATOM   2380 C CB  . ILE A 1 281 ? -15.388 5.088   37.383  1.00 24.27 ? 281 ILE A CB  1 
ATOM   2381 C CG1 . ILE A 1 281 ? -15.159 5.300   35.878  1.00 19.77 ? 281 ILE A CG1 1 
ATOM   2382 C CG2 . ILE A 1 281 ? -16.426 4.018   37.641  1.00 20.97 ? 281 ILE A CG2 1 
ATOM   2383 C CD1 . ILE A 1 281 ? -14.630 4.082   35.138  1.00 19.28 ? 281 ILE A CD1 1 
ATOM   2384 N N   . LEU A 1 282 ? -15.193 6.247   40.386  1.00 21.29 ? 282 LEU A N   1 
ATOM   2385 C CA  . LEU A 1 282 ? -15.495 6.163   41.811  1.00 23.04 ? 282 LEU A CA  1 
ATOM   2386 C C   . LEU A 1 282 ? -16.283 7.386   42.275  1.00 19.32 ? 282 LEU A C   1 
ATOM   2387 O O   . LEU A 1 282 ? -17.307 7.255   42.957  1.00 21.39 ? 282 LEU A O   1 
ATOM   2388 C CB  . LEU A 1 282 ? -14.202 6.009   42.612  1.00 19.16 ? 282 LEU A CB  1 
ATOM   2389 C CG  . LEU A 1 282 ? -14.328 6.092   44.134  1.00 23.34 ? 282 LEU A CG  1 
ATOM   2390 C CD1 . LEU A 1 282 ? -14.978 4.852   44.723  1.00 24.86 ? 282 LEU A CD1 1 
ATOM   2391 C CD2 . LEU A 1 282 ? -12.973 6.368   44.792  1.00 24.80 ? 282 LEU A CD2 1 
ATOM   2392 N N   . LYS A 1 283 ? -15.826 8.589   41.909  1.00 16.12 ? 283 LYS A N   1 
ATOM   2393 C CA  . LYS A 1 283 ? -16.552 9.799   42.299  1.00 17.42 ? 283 LYS A CA  1 
ATOM   2394 C C   . LYS A 1 283 ? -17.964 9.824   41.713  1.00 22.58 ? 283 LYS A C   1 
ATOM   2395 O O   . LYS A 1 283 ? -18.897 10.308  42.361  1.00 23.22 ? 283 LYS A O   1 
ATOM   2396 C CB  . LYS A 1 283 ? -15.790 11.061  41.886  1.00 26.50 ? 283 LYS A CB  1 
ATOM   2397 C CG  . LYS A 1 283 ? -14.386 11.185  42.466  1.00 36.92 ? 283 LYS A CG  1 
ATOM   2398 C CD  . LYS A 1 283 ? -14.383 10.774  43.910  1.00 48.50 ? 283 LYS A CD  1 
ATOM   2399 C CE  . LYS A 1 283 ? -13.618 11.704  44.853  1.00 51.94 ? 283 LYS A CE  1 
ATOM   2400 N NZ  . LYS A 1 283 ? -12.179 11.818  44.514  1.00 48.83 ? 283 LYS A NZ  1 
ATOM   2401 N N   . ASN A 1 284 ? -18.144 9.271   40.511  1.00 17.37 ? 284 ASN A N   1 
ATOM   2402 C CA  . ASN A 1 284 ? -19.477 9.196   39.920  1.00 19.42 ? 284 ASN A CA  1 
ATOM   2403 C C   . ASN A 1 284 ? -20.367 8.167   40.607  1.00 20.15 ? 284 ASN A C   1 
ATOM   2404 O O   . ASN A 1 284 ? -21.594 8.223   40.448  1.00 23.18 ? 284 ASN A O   1 
ATOM   2405 C CB  . ASN A 1 284 ? -19.383 8.847   38.428  1.00 14.23 ? 284 ASN A CB  1 
ATOM   2406 C CG  . ASN A 1 284 ? -18.952 10.032  37.567  1.00 25.38 ? 284 ASN A CG  1 
ATOM   2407 O OD1 . ASN A 1 284 ? -18.886 11.169  38.039  1.00 24.54 ? 284 ASN A OD1 1 
ATOM   2408 N ND2 . ASN A 1 284 ? -18.635 9.762   36.305  1.00 24.15 ? 284 ASN A ND2 1 
ATOM   2409 N N   . SER A 1 285 ? -19.783 7.221   41.336  1.00 17.68 ? 285 SER A N   1 
ATOM   2410 C CA  . SER A 1 285 ? -20.504 6.045   41.803  1.00 18.27 ? 285 SER A CA  1 
ATOM   2411 C C   . SER A 1 285 ? -20.774 6.040   43.302  1.00 20.82 ? 285 SER A C   1 
ATOM   2412 O O   . SER A 1 285 ? -21.847 5.609   43.725  1.00 24.09 ? 285 SER A O   1 
ATOM   2413 C CB  . SER A 1 285 ? -19.733 4.781   41.407  1.00 20.93 ? 285 SER A CB  1 
ATOM   2414 O OG  . SER A 1 285 ? -19.533 4.750   39.999  1.00 25.02 ? 285 SER A OG  1 
ATOM   2415 N N   . VAL A 1 286 ? -19.841 6.496   44.131  1.00 24.13 ? 286 VAL A N   1 
ATOM   2416 C CA  . VAL A 1 286 ? -20.083 6.555   45.565  1.00 21.36 ? 286 VAL A CA  1 
ATOM   2417 C C   . VAL A 1 286 ? -19.831 7.972   46.066  1.00 24.52 ? 286 VAL A C   1 
ATOM   2418 O O   . VAL A 1 286 ? -18.972 8.703   45.559  1.00 28.60 ? 286 VAL A O   1 
ATOM   2419 C CB  . VAL A 1 286 ? -19.236 5.529   46.352  1.00 26.99 ? 286 VAL A CB  1 
ATOM   2420 C CG1 . VAL A 1 286 ? -19.250 4.171   45.657  1.00 21.72 ? 286 VAL A CG1 1 
ATOM   2421 C CG2 . VAL A 1 286 ? -17.842 6.011   46.515  1.00 27.79 ? 286 VAL A CG2 1 
ATOM   2422 N N   . GLU A 1 287 ? -20.602 8.353   47.075  1.00 27.98 ? 287 GLU A N   1 
ATOM   2423 C CA  . GLU A 1 287 ? -20.564 9.683   47.667  1.00 30.33 ? 287 GLU A CA  1 
ATOM   2424 C C   . GLU A 1 287 ? -19.215 10.034  48.276  1.00 28.81 ? 287 GLU A C   1 
ATOM   2425 O O   . GLU A 1 287 ? -18.545 10.970  47.835  1.00 33.69 ? 287 GLU A O   1 
ATOM   2426 C CB  . GLU A 1 287 ? -21.617 9.774   48.753  1.00 35.72 ? 287 GLU A CB  1 
ATOM   2427 C CG  . GLU A 1 287 ? -22.984 9.842   48.206  1.00 46.39 ? 287 GLU A CG  1 
ATOM   2428 C CD  . GLU A 1 287 ? -23.725 10.980  48.790  1.00 52.25 ? 287 GLU A CD  1 
ATOM   2429 O OE1 . GLU A 1 287 ? -24.461 11.614  48.015  1.00 56.15 ? 287 GLU A OE1 1 
ATOM   2430 O OE2 . GLU A 1 287 ? -23.568 11.243  50.007  1.00 54.71 ? 287 GLU A OE2 1 
ATOM   2431 N N   . ARG A 1 288 ? -18.836 9.313   49.320  1.00 24.20 ? 288 ARG A N   1 
ATOM   2432 C CA  . ARG A 1 288 ? -17.589 9.568   50.038  1.00 37.12 ? 288 ARG A CA  1 
ATOM   2433 C C   . ARG A 1 288 ? -16.560 8.641   49.425  1.00 42.36 ? 288 ARG A C   1 
ATOM   2434 O O   . ARG A 1 288 ? -16.400 7.490   49.828  1.00 49.68 ? 288 ARG A O   1 
ATOM   2435 C CB  . ARG A 1 288 ? -17.757 9.315   51.527  1.00 35.93 ? 288 ARG A CB  1 
ATOM   2436 C CG  . ARG A 1 288 ? -18.474 10.412  52.227  1.00 38.84 ? 288 ARG A CG  1 
ATOM   2437 C CD  . ARG A 1 288 ? -18.550 10.097  53.688  1.00 48.22 ? 288 ARG A CD  1 
ATOM   2438 N NE  . ARG A 1 288 ? -19.114 8.778   53.934  1.00 56.41 ? 288 ARG A NE  1 
ATOM   2439 C CZ  . ARG A 1 288 ? -20.405 8.494   53.789  1.00 59.01 ? 288 ARG A CZ  1 
ATOM   2440 N NH1 . ARG A 1 288 ? -21.276 9.427   53.413  1.00 59.46 ? 288 ARG A NH1 1 
ATOM   2441 N NH2 . ARG A 1 288 ? -20.829 7.267   54.042  1.00 57.01 ? 288 ARG A NH2 1 
ATOM   2442 N N   . ALA A 1 289 ? -15.879 9.143   48.408  1.00 38.21 ? 289 ALA A N   1 
ATOM   2443 C CA  . ALA A 1 289 ? -15.144 8.300   47.487  1.00 40.13 ? 289 ALA A CA  1 
ATOM   2444 C C   . ALA A 1 289 ? -13.651 8.511   47.713  1.00 34.26 ? 289 ALA A C   1 
ATOM   2445 O O   . ALA A 1 289 ? -12.991 9.297   47.029  1.00 39.84 ? 289 ALA A O   1 
ATOM   2446 C CB  . ALA A 1 289 ? -15.568 8.613   46.101  1.00 38.18 ? 289 ALA A CB  1 
ATOM   2447 N N   . SER A 1 290 ? -13.135 7.814   48.695  1.00 22.22 ? 290 SER A N   1 
ATOM   2448 C CA  . SER A 1 290 ? -11.693 7.785   48.891  1.00 18.88 ? 290 SER A CA  1 
ATOM   2449 C C   . SER A 1 290 ? -11.072 6.731   47.987  1.00 15.30 ? 290 SER A C   1 
ATOM   2450 O O   . SER A 1 290 ? -11.466 5.561   48.049  1.00 13.08 ? 290 SER A O   1 
ATOM   2451 C CB  . SER A 1 290 ? -11.337 7.470   50.334  1.00 18.26 ? 290 SER A CB  1 
ATOM   2452 O OG  . SER A 1 290 ? -9.930  7.348   50.473  1.00 18.02 ? 290 SER A OG  1 
ATOM   2453 N N   . PRO A 1 291 ? -10.080 7.100   47.183  1.00 12.70 ? 291 PRO A N   1 
ATOM   2454 C CA  . PRO A 1 291 ? -9.371  6.123   46.354  1.00 13.37 ? 291 PRO A CA  1 
ATOM   2455 C C   . PRO A 1 291 ? -8.305  5.321   47.085  1.00 17.52 ? 291 PRO A C   1 
ATOM   2456 O O   . PRO A 1 291 ? -7.544  4.603   46.429  1.00 13.58 ? 291 PRO A O   1 
ATOM   2457 C CB  . PRO A 1 291 ? -8.741  7.019   45.272  1.00 21.30 ? 291 PRO A CB  1 
ATOM   2458 C CG  . PRO A 1 291 ? -8.444  8.295   45.977  1.00 15.97 ? 291 PRO A CG  1 
ATOM   2459 C CD  . PRO A 1 291 ? -9.522  8.462   47.052  1.00 16.15 ? 291 PRO A CD  1 
ATOM   2460 N N   . TYR A 1 292 ? -8.244  5.378   48.419  1.00 13.31 ? 292 TYR A N   1 
ATOM   2461 C CA  . TYR A 1 292 ? -7.156  4.756   49.160  1.00 14.61 ? 292 TYR A CA  1 
ATOM   2462 C C   . TYR A 1 292 ? -7.572  3.472   49.851  1.00 10.15 ? 292 TYR A C   1 
ATOM   2463 O O   . TYR A 1 292 ? -6.793  2.919   50.631  1.00 15.27 ? 292 TYR A O   1 
ATOM   2464 C CB  . TYR A 1 292 ? -6.581  5.751   50.167  1.00 10.14 ? 292 TYR A CB  1 
ATOM   2465 C CG  . TYR A 1 292 ? -6.118  7.009   49.488  1.00 15.21 ? 292 TYR A CG  1 
ATOM   2466 C CD1 . TYR A 1 292 ? -5.418  6.948   48.288  1.00 20.60 ? 292 TYR A CD1 1 
ATOM   2467 C CD2 . TYR A 1 292 ? -6.406  8.259   50.022  1.00 17.72 ? 292 TYR A CD2 1 
ATOM   2468 C CE1 . TYR A 1 292 ? -5.004  8.101   47.633  1.00 24.62 ? 292 TYR A CE1 1 
ATOM   2469 C CE2 . TYR A 1 292 ? -5.992  9.430   49.372  1.00 28.98 ? 292 TYR A CE2 1 
ATOM   2470 C CZ  . TYR A 1 292 ? -5.288  9.335   48.177  1.00 31.32 ? 292 TYR A CZ  1 
ATOM   2471 O OH  . TYR A 1 292 ? -4.865  10.468  47.520  1.00 32.56 ? 292 TYR A OH  1 
ATOM   2472 N N   . LEU A 1 293 ? -8.768  2.971   49.557  1.00 13.83 ? 293 LEU A N   1 
ATOM   2473 C CA  . LEU A 1 293 ? -9.342  1.779   50.162  1.00 10.30 ? 293 LEU A CA  1 
ATOM   2474 C C   . LEU A 1 293 ? -9.333  0.626   49.168  1.00 13.05 ? 293 LEU A C   1 
ATOM   2475 O O   . LEU A 1 293 ? -9.348  0.833   47.953  1.00 10.25 ? 293 LEU A O   1 
ATOM   2476 C CB  . LEU A 1 293 ? -10.795 2.030   50.585  1.00 18.33 ? 293 LEU A CB  1 
ATOM   2477 C CG  . LEU A 1 293 ? -11.138 2.693   51.920  1.00 26.21 ? 293 LEU A CG  1 
ATOM   2478 C CD1 . LEU A 1 293 ? -10.275 3.904   52.197  1.00 27.71 ? 293 LEU A CD1 1 
ATOM   2479 C CD2 . LEU A 1 293 ? -12.619 3.067   51.923  1.00 19.34 ? 293 LEU A CD2 1 
ATOM   2480 N N   . ARG A 1 294 ? -9.358  -0.598  49.692  1.00 16.64 ? 294 ARG A N   1 
ATOM   2481 C CA  . ARG A 1 294 ? -9.705  -1.754  48.874  1.00 13.94 ? 294 ARG A CA  1 
ATOM   2482 C C   . ARG A 1 294 ? -11.225 -1.913  48.885  1.00 17.25 ? 294 ARG A C   1 
ATOM   2483 O O   . ARG A 1 294 ? -11.824 -2.111  49.946  1.00 18.32 ? 294 ARG A O   1 
ATOM   2484 C CB  . ARG A 1 294 ? -9.041  -3.042  49.367  1.00 12.73 ? 294 ARG A CB  1 
ATOM   2485 C CG  . ARG A 1 294 ? -9.445  -4.278  48.545  1.00 15.22 ? 294 ARG A CG  1 
ATOM   2486 C CD  . ARG A 1 294 ? -8.556  -5.521  48.837  1.00 10.11 ? 294 ARG A CD  1 
ATOM   2487 N NE  . ARG A 1 294 ? -8.695  -5.972  50.219  1.00 17.47 ? 294 ARG A NE  1 
ATOM   2488 C CZ  . ARG A 1 294 ? -7.694  -6.111  51.083  1.00 18.75 ? 294 ARG A CZ  1 
ATOM   2489 N NH1 . ARG A 1 294 ? -6.441  -5.855  50.721  1.00 21.05 ? 294 ARG A NH1 1 
ATOM   2490 N NH2 . ARG A 1 294 ? -7.949  -6.524  52.313  1.00 18.63 ? 294 ARG A NH2 1 
ATOM   2491 N N   . TYR A 1 295 ? -11.845 -1.846  47.712  1.00 11.19 ? 295 TYR A N   1 
ATOM   2492 C CA  . TYR A 1 295 ? -13.296 -1.962  47.618  1.00 11.61 ? 295 TYR A CA  1 
ATOM   2493 C C   . TYR A 1 295 ? -13.699 -3.382  47.229  1.00 17.63 ? 295 TYR A C   1 
ATOM   2494 O O   . TYR A 1 295 ? -12.967 -4.087  46.533  1.00 18.51 ? 295 TYR A O   1 
ATOM   2495 C CB  . TYR A 1 295 ? -13.863 -0.972  46.605  1.00 13.98 ? 295 TYR A CB  1 
ATOM   2496 C CG  . TYR A 1 295 ? -13.819 0.468   47.063  1.00 11.73 ? 295 TYR A CG  1 
ATOM   2497 C CD1 . TYR A 1 295 ? -12.707 1.263   46.813  1.00 13.07 ? 295 TYR A CD1 1 
ATOM   2498 C CD2 . TYR A 1 295 ? -14.898 1.037   47.739  1.00 15.20 ? 295 TYR A CD2 1 
ATOM   2499 C CE1 . TYR A 1 295 ? -12.658 2.596   47.232  1.00 10.85 ? 295 TYR A CE1 1 
ATOM   2500 C CE2 . TYR A 1 295 ? -14.863 2.364   48.161  1.00 15.34 ? 295 TYR A CE2 1 
ATOM   2501 C CZ  . TYR A 1 295 ? -13.746 3.140   47.906  1.00 16.02 ? 295 TYR A CZ  1 
ATOM   2502 O OH  . TYR A 1 295 ? -13.730 4.463   48.330  1.00 16.95 ? 295 TYR A OH  1 
ATOM   2503 N N   . TYR A 1 296 ? -14.877 -3.796  47.695  1.00 17.06 ? 296 TYR A N   1 
ATOM   2504 C CA  . TYR A 1 296 ? -15.473 -5.073  47.314  1.00 17.34 ? 296 TYR A CA  1 
ATOM   2505 C C   . TYR A 1 296 ? -16.783 -4.780  46.587  1.00 17.47 ? 296 TYR A C   1 
ATOM   2506 O O   . TYR A 1 296 ? -17.765 -4.337  47.203  1.00 17.17 ? 296 TYR A O   1 
ATOM   2507 C CB  . TYR A 1 296 ? -15.702 -5.958  48.535  1.00 16.96 ? 296 TYR A CB  1 
ATOM   2508 C CG  . TYR A 1 296 ? -14.453 -6.231  49.353  1.00 13.44 ? 296 TYR A CG  1 
ATOM   2509 C CD1 . TYR A 1 296 ? -13.330 -6.806  48.769  1.00 16.48 ? 296 TYR A CD1 1 
ATOM   2510 C CD2 . TYR A 1 296 ? -14.407 -5.930  50.714  1.00 12.91 ? 296 TYR A CD2 1 
ATOM   2511 C CE1 . TYR A 1 296 ? -12.182 -7.062  49.513  1.00 20.85 ? 296 TYR A CE1 1 
ATOM   2512 C CE2 . TYR A 1 296 ? -13.258 -6.188  51.475  1.00 15.91 ? 296 TYR A CE2 1 
ATOM   2513 C CZ  . TYR A 1 296 ? -12.155 -6.749  50.858  1.00 15.41 ? 296 TYR A CZ  1 
ATOM   2514 O OH  . TYR A 1 296 ? -11.026 -7.017  51.577  1.00 18.17 ? 296 TYR A OH  1 
ATOM   2515 N N   . PHE A 1 297 ? -16.794 -5.004  45.277  1.00 16.30 ? 297 PHE A N   1 
ATOM   2516 C CA  . PHE A 1 297 ? -18.019 -4.826  44.505  1.00 15.20 ? 297 PHE A CA  1 
ATOM   2517 C C   . PHE A 1 297 ? -18.967 -5.976  44.818  1.00 12.90 ? 297 PHE A C   1 
ATOM   2518 O O   . PHE A 1 297 ? -18.683 -7.127  44.472  1.00 14.52 ? 297 PHE A O   1 
ATOM   2519 C CB  . PHE A 1 297 ? -17.725 -4.764  43.011  1.00 13.62 ? 297 PHE A CB  1 
ATOM   2520 C CG  . PHE A 1 297 ? -18.960 -4.573  42.173  1.00 13.24 ? 297 PHE A CG  1 
ATOM   2521 C CD1 . PHE A 1 297 ? -19.575 -3.332  42.097  1.00 18.28 ? 297 PHE A CD1 1 
ATOM   2522 C CD2 . PHE A 1 297 ? -19.514 -5.640  41.479  1.00 16.00 ? 297 PHE A CD2 1 
ATOM   2523 C CE1 . PHE A 1 297 ? -20.720 -3.158  41.320  1.00 14.37 ? 297 PHE A CE1 1 
ATOM   2524 C CE2 . PHE A 1 297 ? -20.665 -5.474  40.713  1.00 17.24 ? 297 PHE A CE2 1 
ATOM   2525 C CZ  . PHE A 1 297 ? -21.266 -4.239  40.641  1.00 12.05 ? 297 PHE A CZ  1 
ATOM   2526 N N   . ARG A 1 298 ? -20.071 -5.668  45.503  1.00 15.81 ? 298 ARG A N   1 
ATOM   2527 C CA  . ARG A 1 298 ? -21.098 -6.658  45.873  1.00 13.00 ? 298 ARG A CA  1 
ATOM   2528 C C   . ARG A 1 298 ? -20.504 -7.861  46.607  1.00 20.46 ? 298 ARG A C   1 
ATOM   2529 O O   . ARG A 1 298 ? -21.016 -8.982  46.520  1.00 18.65 ? 298 ARG A O   1 
ATOM   2530 C CB  . ARG A 1 298 ? -21.904 -7.089  44.643  1.00 13.40 ? 298 ARG A CB  1 
ATOM   2531 C CG  . ARG A 1 298 ? -22.714 -5.923  44.088  1.00 12.43 ? 298 ARG A CG  1 
ATOM   2532 C CD  . ARG A 1 298 ? -23.550 -6.278  42.853  1.00 14.19 ? 298 ARG A CD  1 
ATOM   2533 N NE  . ARG A 1 298 ? -24.124 -5.064  42.285  1.00 17.20 ? 298 ARG A NE  1 
ATOM   2534 C CZ  . ARG A 1 298 ? -24.672 -4.967  41.075  1.00 18.19 ? 298 ARG A CZ  1 
ATOM   2535 N NH1 . ARG A 1 298 ? -24.754 -6.022  40.276  1.00 17.74 ? 298 ARG A NH1 1 
ATOM   2536 N NH2 . ARG A 1 298 ? -25.147 -3.803  40.671  1.00 15.08 ? 298 ARG A NH2 1 
ATOM   2537 N N   . GLU A 1 299 ? -19.433 -7.610  47.365  1.00 20.33 ? 299 GLU A N   1 
ATOM   2538 C CA  . GLU A 1 299 ? -18.723 -8.612  48.160  1.00 22.50 ? 299 GLU A CA  1 
ATOM   2539 C C   . GLU A 1 299 ? -18.253 -9.788  47.318  1.00 25.51 ? 299 GLU A C   1 
ATOM   2540 O O   . GLU A 1 299 ? -18.011 -10.882 47.849  1.00 23.42 ? 299 GLU A O   1 
ATOM   2541 C CB  . GLU A 1 299 ? -19.574 -9.104  49.340  1.00 24.12 ? 299 GLU A CB  1 
ATOM   2542 C CG  . GLU A 1 299 ? -19.780 -8.053  50.419  1.00 19.47 ? 299 GLU A CG  1 
ATOM   2543 C CD  . GLU A 1 299 ? -18.626 -7.992  51.406  1.00 28.22 ? 299 GLU A CD  1 
ATOM   2544 O OE1 . GLU A 1 299 ? -18.868 -7.573  52.555  1.00 34.73 ? 299 GLU A OE1 1 
ATOM   2545 O OE2 . GLU A 1 299 ? -17.481 -8.358  51.038  1.00 27.58 ? 299 GLU A OE2 1 
ATOM   2546 N N   . LEU A 1 300 ? -18.083 -9.578  46.009  1.00 15.31 ? 300 LEU A N   1 
ATOM   2547 C CA  . LEU A 1 300 ? -17.718 -10.662 45.116  1.00 20.33 ? 300 LEU A CA  1 
ATOM   2548 C C   . LEU A 1 300 ? -16.403 -10.448 44.371  1.00 17.04 ? 300 LEU A C   1 
ATOM   2549 O O   . LEU A 1 300 ? -15.718 -11.428 44.089  1.00 18.98 ? 300 LEU A O   1 
ATOM   2550 C CB  . LEU A 1 300 ? -18.860 -10.923 44.111  1.00 22.77 ? 300 LEU A CB  1 
ATOM   2551 C CG  . LEU A 1 300 ? -20.100 -11.591 44.743  1.00 27.20 ? 300 LEU A CG  1 
ATOM   2552 C CD1 . LEU A 1 300 ? -21.312 -11.571 43.818  1.00 28.07 ? 300 LEU A CD1 1 
ATOM   2553 C CD2 . LEU A 1 300 ? -19.797 -13.036 45.218  1.00 22.97 ? 300 LEU A CD2 1 
ATOM   2554 N N   . ILE A 1 301 ? -16.000 -9.210  44.079  1.00 14.78 ? 301 ILE A N   1 
ATOM   2555 C CA  . ILE A 1 301 ? -14.732 -8.974  43.386  1.00 10.56 ? 301 ILE A CA  1 
ATOM   2556 C C   . ILE A 1 301 ? -14.104 -7.699  43.934  1.00 10.52 ? 301 ILE A C   1 
ATOM   2557 O O   . ILE A 1 301 ? -14.804 -6.716  44.206  1.00 18.25 ? 301 ILE A O   1 
ATOM   2558 C CB  . ILE A 1 301 ? -14.930 -8.909  41.848  1.00 19.16 ? 301 ILE A CB  1 
ATOM   2559 C CG1 . ILE A 1 301 ? -13.588 -8.826  41.109  1.00 17.29 ? 301 ILE A CG1 1 
ATOM   2560 C CG2 . ILE A 1 301 ? -15.828 -7.742  41.459  1.00 21.22 ? 301 ILE A CG2 1 
ATOM   2561 C CD1 . ILE A 1 301 ? -13.735 -8.674  39.578  1.00 16.50 ? 301 ILE A CD1 1 
ATOM   2562 N N   . SER A 1 302 ? -12.783 -7.730  44.135  1.00 14.51 ? 302 SER A N   1 
ATOM   2563 C CA  . SER A 1 302 ? -12.071 -6.589  44.697  1.00 13.55 ? 302 SER A CA  1 
ATOM   2564 C C   . SER A 1 302 ? -11.769 -5.568  43.611  1.00 16.10 ? 302 SER A C   1 
ATOM   2565 O O   . SER A 1 302 ? -11.478 -5.925  42.462  1.00 13.48 ? 302 SER A O   1 
ATOM   2566 C CB  . SER A 1 302 ? -10.776 -7.041  45.377  1.00 19.56 ? 302 SER A CB  1 
ATOM   2567 O OG  . SER A 1 302 ? -11.054 -7.884  46.487  1.00 18.27 ? 302 SER A OG  1 
ATOM   2568 N N   . VAL A 1 303 ? -11.861 -4.293  43.974  1.00 10.61 ? 303 VAL A N   1 
ATOM   2569 C CA  . VAL A 1 303 ? -11.691 -3.187  43.034  1.00 10.39 ? 303 VAL A CA  1 
ATOM   2570 C C   . VAL A 1 303 ? -10.863 -2.114  43.718  1.00 15.02 ? 303 VAL A C   1 
ATOM   2571 O O   . VAL A 1 303 ? -11.217 -1.656  44.812  1.00 14.95 ? 303 VAL A O   1 
ATOM   2572 C CB  . VAL A 1 303 ? -13.026 -2.565  42.574  1.00 14.92 ? 303 VAL A CB  1 
ATOM   2573 C CG1 . VAL A 1 303 ? -12.746 -1.403  41.626  1.00 16.14 ? 303 VAL A CG1 1 
ATOM   2574 C CG2 . VAL A 1 303 ? -13.943 -3.594  41.913  1.00 11.70 ? 303 VAL A CG2 1 
ATOM   2575 N N   . PHE A 1 304 ? -9.774  -1.707  43.078  1.00 13.10 ? 304 PHE A N   1 
ATOM   2576 C CA  . PHE A 1 304 ? -9.048  -0.514  43.489  1.00 13.65 ? 304 PHE A CA  1 
ATOM   2577 C C   . PHE A 1 304 ? -9.283  0.581   42.461  1.00 14.18 ? 304 PHE A C   1 
ATOM   2578 O O   . PHE A 1 304 ? -9.458  0.313   41.269  1.00 11.53 ? 304 PHE A O   1 
ATOM   2579 C CB  . PHE A 1 304 ? -7.540  -0.777  43.621  1.00 9.94  ? 304 PHE A CB  1 
ATOM   2580 C CG  . PHE A 1 304 ? -7.167  -1.662  44.781  1.00 14.23 ? 304 PHE A CG  1 
ATOM   2581 C CD1 . PHE A 1 304 ? -6.952  -1.116  46.044  1.00 19.81 ? 304 PHE A CD1 1 
ATOM   2582 C CD2 . PHE A 1 304 ? -7.001  -3.025  44.610  1.00 14.40 ? 304 PHE A CD2 1 
ATOM   2583 C CE1 . PHE A 1 304 ? -6.583  -1.922  47.116  1.00 18.25 ? 304 PHE A CE1 1 
ATOM   2584 C CE2 . PHE A 1 304 ? -6.632  -3.840  45.684  1.00 14.15 ? 304 PHE A CE2 1 
ATOM   2585 C CZ  . PHE A 1 304 ? -6.420  -3.285  46.933  1.00 17.12 ? 304 PHE A CZ  1 
ATOM   2586 N N   . PHE A 1 305 ? -9.296  1.820   42.931  1.00 13.36 ? 305 PHE A N   1 
ATOM   2587 C CA  . PHE A 1 305 ? -9.435  2.982   42.066  1.00 12.69 ? 305 PHE A CA  1 
ATOM   2588 C C   . PHE A 1 305 ? -8.100  3.704   42.028  1.00 12.96 ? 305 PHE A C   1 
ATOM   2589 O O   . PHE A 1 305 ? -7.565  4.069   43.081  1.00 14.48 ? 305 PHE A O   1 
ATOM   2590 C CB  . PHE A 1 305 ? -10.563 3.888   42.565  1.00 10.59 ? 305 PHE A CB  1 
ATOM   2591 C CG  . PHE A 1 305 ? -11.902 3.217   42.520  1.00 13.87 ? 305 PHE A CG  1 
ATOM   2592 C CD1 . PHE A 1 305 ? -12.694 3.304   41.385  1.00 17.24 ? 305 PHE A CD1 1 
ATOM   2593 C CD2 . PHE A 1 305 ? -12.333 2.420   43.574  1.00 10.90 ? 305 PHE A CD2 1 
ATOM   2594 C CE1 . PHE A 1 305 ? -13.922 2.660   41.334  1.00 19.18 ? 305 PHE A CE1 1 
ATOM   2595 C CE2 . PHE A 1 305 ? -13.566 1.781   43.524  1.00 14.47 ? 305 PHE A CE2 1 
ATOM   2596 C CZ  . PHE A 1 305 ? -14.351 1.896   42.403  1.00 18.87 ? 305 PHE A CZ  1 
ATOM   2597 N N   . ARG A 1 306 ? -7.559  3.887   40.818  1.00 10.19 ? 306 ARG A N   1 
ATOM   2598 C CA  . ARG A 1 306 ? -6.271  4.546   40.676  1.00 17.14 ? 306 ARG A CA  1 
ATOM   2599 C C   . ARG A 1 306 ? -6.353  5.992   41.153  1.00 20.23 ? 306 ARG A C   1 
ATOM   2600 O O   . ARG A 1 306 ? -7.398  6.652   41.067  1.00 15.56 ? 306 ARG A O   1 
ATOM   2601 C CB  . ARG A 1 306 ? -5.797  4.494   39.218  1.00 23.06 ? 306 ARG A CB  1 
ATOM   2602 C CG  . ARG A 1 306 ? -6.470  5.502   38.311  1.00 18.76 ? 306 ARG A CG  1 
ATOM   2603 C CD  . ARG A 1 306 ? -5.749  5.681   36.971  1.00 21.80 ? 306 ARG A CD  1 
ATOM   2604 N NE  . ARG A 1 306 ? -6.352  6.779   36.216  1.00 21.00 ? 306 ARG A NE  1 
ATOM   2605 C CZ  . ARG A 1 306 ? -5.789  7.398   35.185  1.00 23.02 ? 306 ARG A CZ  1 
ATOM   2606 N NH1 . ARG A 1 306 ? -4.588  7.031   34.742  1.00 17.93 ? 306 ARG A NH1 1 
ATOM   2607 N NH2 . ARG A 1 306 ? -6.438  8.387   34.590  1.00 16.87 ? 306 ARG A NH2 1 
ATOM   2608 N N   . ASP A 1 307 ? -5.238  6.467   41.695  1.00 15.50 ? 307 ASP A N   1 
ATOM   2609 C CA  . ASP A 1 307 ? -5.071  7.880   42.026  1.00 18.71 ? 307 ASP A CA  1 
ATOM   2610 C C   . ASP A 1 307 ? -4.825  8.629   40.725  1.00 19.20 ? 307 ASP A C   1 
ATOM   2611 O O   . ASP A 1 307 ? -3.727  8.583   40.168  1.00 18.07 ? 307 ASP A O   1 
ATOM   2612 C CB  . ASP A 1 307 ? -3.918  8.061   43.007  1.00 18.86 ? 307 ASP A CB  1 
ATOM   2613 C CG  . ASP A 1 307 ? -3.790  9.485   43.495  1.00 17.61 ? 307 ASP A CG  1 
ATOM   2614 O OD1 . ASP A 1 307 ? -3.735  10.401  42.650  1.00 17.29 ? 307 ASP A OD1 1 
ATOM   2615 O OD2 . ASP A 1 307 ? -3.746  9.678   44.729  1.00 23.62 ? 307 ASP A OD2 1 
ATOM   2616 N N   . LYS A 1 308 ? -5.852  9.341   40.252  1.00 17.12 ? 308 LYS A N   1 
ATOM   2617 C CA  . LYS A 1 308 ? -5.802  9.953   38.929  1.00 19.92 ? 308 LYS A CA  1 
ATOM   2618 C C   . LYS A 1 308 ? -4.710  11.013  38.830  1.00 14.60 ? 308 LYS A C   1 
ATOM   2619 O O   . LYS A 1 308 ? -4.010  11.092  37.813  1.00 13.50 ? 308 LYS A O   1 
ATOM   2620 C CB  . LYS A 1 308 ? -7.168  10.561  38.576  1.00 18.53 ? 308 LYS A CB  1 
ATOM   2621 C CG  . LYS A 1 308 ? -7.205  11.306  37.233  1.00 23.30 ? 308 LYS A CG  1 
ATOM   2622 C CD  . LYS A 1 308 ? -8.597  11.906  36.973  1.00 22.12 ? 308 LYS A CD  1 
ATOM   2623 C CE  . LYS A 1 308 ? -8.863  12.222  35.506  1.00 31.03 ? 308 LYS A CE  1 
ATOM   2624 N NZ  . LYS A 1 308 ? -7.667  12.631  34.727  1.00 26.41 ? 308 LYS A NZ  1 
ATOM   2625 N N   . THR A 1 309 ? -4.561  11.872  39.845  1.00 17.81 ? 309 THR A N   1 
ATOM   2626 C CA  . THR A 1 309 ? -3.605  12.957  39.647  1.00 18.30 ? 309 THR A CA  1 
ATOM   2627 C C   . THR A 1 309 ? -2.171  12.434  39.669  1.00 15.39 ? 309 THR A C   1 
ATOM   2628 O O   . THR A 1 309 ? -1.330  12.898  38.891  1.00 18.52 ? 309 THR A O   1 
ATOM   2629 C CB  . THR A 1 309 ? -3.790  14.087  40.671  1.00 24.07 ? 309 THR A CB  1 
ATOM   2630 O OG1 . THR A 1 309 ? -3.007  13.824  41.834  1.00 41.41 ? 309 THR A OG1 1 
ATOM   2631 C CG2 . THR A 1 309 ? -5.242  14.247  41.056  1.00 12.53 ? 309 THR A CG2 1 
ATOM   2632 N N   . LEU A 1 310 ? -1.872  11.451  40.524  1.00 15.07 ? 310 LEU A N   1 
ATOM   2633 C CA  . LEU A 1 310 ? -0.517  10.907  40.526  1.00 12.81 ? 310 LEU A CA  1 
ATOM   2634 C C   . LEU A 1 310 ? -0.224  10.166  39.221  1.00 17.16 ? 310 LEU A C   1 
ATOM   2635 O O   . LEU A 1 310 ? 0.862   10.312  38.651  1.00 16.50 ? 310 LEU A O   1 
ATOM   2636 C CB  . LEU A 1 310 ? -0.304  9.977   41.717  1.00 14.14 ? 310 LEU A CB  1 
ATOM   2637 C CG  . LEU A 1 310 ? -0.150  10.645  43.087  1.00 17.03 ? 310 LEU A CG  1 
ATOM   2638 C CD1 . LEU A 1 310 ? -0.061  9.580   44.165  1.00 21.53 ? 310 LEU A CD1 1 
ATOM   2639 C CD2 . LEU A 1 310 ? 1.061   11.585  43.139  1.00 18.17 ? 310 LEU A CD2 1 
ATOM   2640 N N   . SER A 1 311 ? -1.188  9.382   38.734  1.00 12.50 ? 311 SER A N   1 
ATOM   2641 C CA  . SER A 1 311 ? -1.025  8.703   37.449  1.00 17.80 ? 311 SER A CA  1 
ATOM   2642 C C   . SER A 1 311 ? -0.829  9.694   36.306  1.00 20.99 ? 311 SER A C   1 
ATOM   2643 O O   . SER A 1 311 ? 0.008   9.471   35.426  1.00 14.65 ? 311 SER A O   1 
ATOM   2644 C CB  . SER A 1 311 ? -2.234  7.813   37.172  1.00 14.82 ? 311 SER A CB  1 
ATOM   2645 O OG  . SER A 1 311 ? -2.389  6.827   38.178  1.00 11.29 ? 311 SER A OG  1 
ATOM   2646 N N   . ASP A 1 312 ? -1.602  10.793  36.299  1.00 15.71 ? 312 ASP A N   1 
ATOM   2647 C CA  . ASP A 1 312 ? -1.534  11.769  35.212  1.00 18.62 ? 312 ASP A CA  1 
ATOM   2648 C C   . ASP A 1 312 ? -0.261  12.595  35.276  1.00 17.47 ? 312 ASP A C   1 
ATOM   2649 O O   . ASP A 1 312 ? 0.247   13.026  34.237  1.00 17.86 ? 312 ASP A O   1 
ATOM   2650 C CB  . ASP A 1 312 ? -2.742  12.718  35.251  1.00 18.72 ? 312 ASP A CB  1 
ATOM   2651 C CG  . ASP A 1 312 ? -3.997  12.114  34.636  1.00 21.19 ? 312 ASP A CG  1 
ATOM   2652 O OD1 . ASP A 1 312 ? -3.913  11.055  33.972  1.00 19.21 ? 312 ASP A OD1 1 
ATOM   2653 O OD2 . ASP A 1 312 ? -5.077  12.719  34.807  1.00 24.87 ? 312 ASP A OD2 1 
ATOM   2654 N N   . LEU A 1 313 ? 0.254   12.847  36.479  1.00 15.50 ? 313 LEU A N   1 
ATOM   2655 C CA  . LEU A 1 313 ? 1.508   13.582  36.596  1.00 15.39 ? 313 LEU A CA  1 
ATOM   2656 C C   . LEU A 1 313 ? 2.633   12.858  35.855  1.00 14.14 ? 313 LEU A C   1 
ATOM   2657 O O   . LEU A 1 313 ? 3.403   13.475  35.108  1.00 18.17 ? 313 LEU A O   1 
ATOM   2658 C CB  . LEU A 1 313 ? 1.849   13.794  38.075  1.00 17.48 ? 313 LEU A CB  1 
ATOM   2659 C CG  . LEU A 1 313 ? 1.022   14.917  38.740  1.00 17.96 ? 313 LEU A CG  1 
ATOM   2660 C CD1 . LEU A 1 313 ? 1.146   14.896  40.248  1.00 24.67 ? 313 LEU A CD1 1 
ATOM   2661 C CD2 . LEU A 1 313 ? 1.395   16.290  38.202  1.00 20.59 ? 313 LEU A CD2 1 
ATOM   2662 N N   . ILE A 1 314 ? 2.743   11.546  36.046  1.00 15.95 ? 314 ILE A N   1 
ATOM   2663 C CA  . ILE A 1 314 ? 3.762   10.789  35.326  1.00 10.87 ? 314 ILE A CA  1 
ATOM   2664 C C   . ILE A 1 314 ? 3.426   10.730  33.841  1.00 16.46 ? 314 ILE A C   1 
ATOM   2665 O O   . ILE A 1 314 ? 4.291   10.922  32.981  1.00 18.59 ? 314 ILE A O   1 
ATOM   2666 C CB  . ILE A 1 314 ? 3.906   9.382   35.925  1.00 14.25 ? 314 ILE A CB  1 
ATOM   2667 C CG1 . ILE A 1 314 ? 4.383   9.482   37.382  1.00 14.85 ? 314 ILE A CG1 1 
ATOM   2668 C CG2 . ILE A 1 314 ? 4.841   8.524   35.065  1.00 11.93 ? 314 ILE A CG2 1 
ATOM   2669 C CD1 . ILE A 1 314 ? 4.437   8.150   38.084  1.00 11.86 ? 314 ILE A CD1 1 
ATOM   2670 N N   . GLY A 1 315 ? 2.160   10.476  33.520  1.00 19.83 ? 315 GLY A N   1 
ATOM   2671 C CA  . GLY A 1 315 ? 1.799   10.203  32.144  1.00 18.50 ? 315 GLY A CA  1 
ATOM   2672 C C   . GLY A 1 315 ? 1.808   11.426  31.257  1.00 22.07 ? 315 GLY A C   1 
ATOM   2673 O O   . GLY A 1 315 ? 2.052   11.314  30.055  1.00 24.99 ? 315 GLY A O   1 
ATOM   2674 N N   . PHE A 1 316 ? 1.562   12.609  31.829  1.00 22.53 ? 316 PHE A N   1 
ATOM   2675 C CA  . PHE A 1 316 ? 1.391   13.813  31.025  1.00 24.39 ? 316 PHE A CA  1 
ATOM   2676 C C   . PHE A 1 316 ? 2.184   15.021  31.493  1.00 23.68 ? 316 PHE A C   1 
ATOM   2677 O O   . PHE A 1 316 ? 2.416   15.917  30.682  1.00 26.91 ? 316 PHE A O   1 
ATOM   2678 C CB  . PHE A 1 316 ? -0.093  14.212  30.965  1.00 22.50 ? 316 PHE A CB  1 
ATOM   2679 C CG  . PHE A 1 316 ? -0.980  13.161  30.372  1.00 25.14 ? 316 PHE A CG  1 
ATOM   2680 C CD1 . PHE A 1 316 ? -1.068  13.003  28.999  1.00 29.03 ? 316 PHE A CD1 1 
ATOM   2681 C CD2 . PHE A 1 316 ? -1.739  12.339  31.185  1.00 22.37 ? 316 PHE A CD2 1 
ATOM   2682 C CE1 . PHE A 1 316 ? -1.888  12.034  28.454  1.00 33.10 ? 316 PHE A CE1 1 
ATOM   2683 C CE2 . PHE A 1 316 ? -2.561  11.374  30.646  1.00 23.29 ? 316 PHE A CE2 1 
ATOM   2684 C CZ  . PHE A 1 316 ? -2.634  11.220  29.274  1.00 29.47 ? 316 PHE A CZ  1 
ATOM   2685 N N   . SER A 1 317 ? 2.618   15.086  32.751  1.00 20.79 ? 317 SER A N   1 
ATOM   2686 C CA  . SER A 1 317 ? 3.152   16.332  33.284  1.00 20.69 ? 317 SER A CA  1 
ATOM   2687 C C   . SER A 1 317 ? 4.671   16.345  33.408  1.00 22.03 ? 317 SER A C   1 
ATOM   2688 O O   . SER A 1 317 ? 5.321   17.274  32.917  1.00 24.90 ? 317 SER A O   1 
ATOM   2689 C CB  . SER A 1 317 ? 2.510   16.622  34.649  1.00 27.10 ? 317 SER A CB  1 
ATOM   2690 O OG  . SER A 1 317 ? 3.225   17.641  35.326  1.00 40.41 ? 317 SER A OG  1 
ATOM   2691 N N   . TYR A 1 318 ? 5.254   15.311  34.022  1.00 19.83 ? 318 TYR A N   1 
ATOM   2692 C CA  . TYR A 1 318 ? 6.648   15.356  34.440  1.00 15.37 ? 318 TYR A CA  1 
ATOM   2693 C C   . TYR A 1 318 ? 7.633   15.373  33.277  1.00 15.74 ? 318 TYR A C   1 
ATOM   2694 O O   . TYR A 1 318 ? 8.799   15.728  33.488  1.00 16.76 ? 318 TYR A O   1 
ATOM   2695 C CB  . TYR A 1 318 ? 6.956   14.172  35.352  1.00 16.96 ? 318 TYR A CB  1 
ATOM   2696 C CG  . TYR A 1 318 ? 6.386   14.312  36.748  1.00 19.78 ? 318 TYR A CG  1 
ATOM   2697 C CD1 . TYR A 1 318 ? 6.142   15.564  37.301  1.00 21.33 ? 318 TYR A CD1 1 
ATOM   2698 C CD2 . TYR A 1 318 ? 6.078   13.189  37.505  1.00 22.54 ? 318 TYR A CD2 1 
ATOM   2699 C CE1 . TYR A 1 318 ? 5.613   15.694  38.591  1.00 22.29 ? 318 TYR A CE1 1 
ATOM   2700 C CE2 . TYR A 1 318 ? 5.560   13.302  38.781  1.00 22.25 ? 318 TYR A CE2 1 
ATOM   2701 C CZ  . TYR A 1 318 ? 5.327   14.555  39.321  1.00 24.40 ? 318 TYR A CZ  1 
ATOM   2702 O OH  . TYR A 1 318 ? 4.810   14.652  40.596  1.00 19.85 ? 318 TYR A OH  1 
ATOM   2703 N N   . HIS A 1 319 ? 7.211   14.988  32.067  1.00 16.71 ? 319 HIS A N   1 
ATOM   2704 C CA  . HIS A 1 319 ? 8.122   15.075  30.924  1.00 23.83 ? 319 HIS A CA  1 
ATOM   2705 C C   . HIS A 1 319 ? 8.743   16.461  30.814  1.00 28.11 ? 319 HIS A C   1 
ATOM   2706 O O   . HIS A 1 319 ? 9.900   16.599  30.388  1.00 26.44 ? 319 HIS A O   1 
ATOM   2707 C CB  . HIS A 1 319 ? 7.383   14.736  29.627  1.00 22.67 ? 319 HIS A CB  1 
ATOM   2708 C CG  . HIS A 1 319 ? 6.544   15.860  29.111  1.00 21.04 ? 319 HIS A CG  1 
ATOM   2709 N ND1 . HIS A 1 319 ? 5.242   16.062  29.514  1.00 23.97 ? 319 HIS A ND1 1 
ATOM   2710 C CD2 . HIS A 1 319 ? 6.827   16.858  28.240  1.00 21.78 ? 319 HIS A CD2 1 
ATOM   2711 C CE1 . HIS A 1 319 ? 4.754   17.129  28.905  1.00 27.45 ? 319 HIS A CE1 1 
ATOM   2712 N NE2 . HIS A 1 319 ? 5.697   17.630  28.128  1.00 24.80 ? 319 HIS A NE2 1 
ATOM   2713 N N   . ALA A 1 320 ? 7.996   17.483  31.222  1.00 25.39 ? 320 ALA A N   1 
ATOM   2714 C CA  . ALA A 1 320 ? 8.362   18.888  31.135  1.00 41.75 ? 320 ALA A CA  1 
ATOM   2715 C C   . ALA A 1 320 ? 9.080   19.405  32.376  1.00 47.21 ? 320 ALA A C   1 
ATOM   2716 O O   . ALA A 1 320 ? 9.353   20.609  32.456  1.00 46.21 ? 320 ALA A O   1 
ATOM   2717 C CB  . ALA A 1 320 ? 7.105   19.735  30.889  1.00 35.43 ? 320 ALA A CB  1 
ATOM   2718 N N   . TRP A 1 321 ? 9.374   18.547  33.349  1.00 36.70 ? 321 TRP A N   1 
ATOM   2719 C CA  . TRP A 1 321 ? 10.105  18.949  34.541  1.00 33.78 ? 321 TRP A CA  1 
ATOM   2720 C C   . TRP A 1 321 ? 11.516  18.380  34.509  1.00 33.50 ? 321 TRP A C   1 
ATOM   2721 O O   . TRP A 1 321 ? 11.811  17.415  33.803  1.00 35.13 ? 321 TRP A O   1 
ATOM   2722 C CB  . TRP A 1 321 ? 9.430   18.464  35.832  1.00 29.36 ? 321 TRP A CB  1 
ATOM   2723 C CG  . TRP A 1 321 ? 7.994   18.842  36.068  1.00 24.64 ? 321 TRP A CG  1 
ATOM   2724 C CD1 . TRP A 1 321 ? 6.982   18.890  35.157  1.00 21.59 ? 321 TRP A CD1 1 
ATOM   2725 C CD2 . TRP A 1 321 ? 7.408   19.175  37.332  1.00 29.81 ? 321 TRP A CD2 1 
ATOM   2726 N NE1 . TRP A 1 321 ? 5.808   19.249  35.771  1.00 23.86 ? 321 TRP A NE1 1 
ATOM   2727 C CE2 . TRP A 1 321 ? 6.044   19.427  37.109  1.00 26.60 ? 321 TRP A CE2 1 
ATOM   2728 C CE3 . TRP A 1 321 ? 7.912   19.291  38.632  1.00 32.10 ? 321 TRP A CE3 1 
ATOM   2729 C CZ2 . TRP A 1 321 ? 5.173   19.798  38.138  1.00 32.30 ? 321 TRP A CZ2 1 
ATOM   2730 C CZ3 . TRP A 1 321 ? 7.044   19.654  39.655  1.00 29.08 ? 321 TRP A CZ3 1 
ATOM   2731 C CH2 . TRP A 1 321 ? 5.694   19.902  39.401  1.00 29.15 ? 321 TRP A CH2 1 
ATOM   2732 N N   . ASN A 1 322 ? 12.386  18.996  35.300  1.00 30.30 ? 322 ASN A N   1 
ATOM   2733 C CA  . ASN A 1 322 ? 13.636  18.360  35.680  1.00 29.29 ? 322 ASN A CA  1 
ATOM   2734 C C   . ASN A 1 322 ? 13.337  17.152  36.565  1.00 30.32 ? 322 ASN A C   1 
ATOM   2735 O O   . ASN A 1 322 ? 12.402  17.174  37.369  1.00 27.89 ? 322 ASN A O   1 
ATOM   2736 C CB  . ASN A 1 322 ? 14.519  19.366  36.417  1.00 41.89 ? 322 ASN A CB  1 
ATOM   2737 C CG  . ASN A 1 322 ? 15.863  18.800  36.787  1.00 53.89 ? 322 ASN A CG  1 
ATOM   2738 O OD1 . ASN A 1 322 ? 16.090  18.420  37.937  1.00 61.14 ? 322 ASN A OD1 1 
ATOM   2739 N ND2 . ASN A 1 322 ? 16.770  18.738  35.817  1.00 54.83 ? 322 ASN A ND2 1 
ATOM   2740 N N   . ALA A 1 323 ? 14.134  16.092  36.408  1.00 26.85 ? 323 ALA A N   1 
ATOM   2741 C CA  . ALA A 1 323 ? 13.859  14.840  37.111  1.00 28.83 ? 323 ALA A CA  1 
ATOM   2742 C C   . ALA A 1 323 ? 13.836  15.047  38.620  1.00 32.58 ? 323 ALA A C   1 
ATOM   2743 O O   . ALA A 1 323 ? 12.934  14.563  39.315  1.00 27.41 ? 323 ALA A O   1 
ATOM   2744 C CB  . ALA A 1 323 ? 14.897  13.786  36.724  1.00 24.23 ? 323 ALA A CB  1 
ATOM   2745 N N   . GLU A 1 324 ? 14.817  15.783  39.142  1.00 27.41 ? 324 GLU A N   1 
ATOM   2746 C CA  . GLU A 1 324 ? 14.900  16.004  40.581  1.00 28.35 ? 324 GLU A CA  1 
ATOM   2747 C C   . GLU A 1 324 ? 13.657  16.710  41.106  1.00 28.68 ? 324 GLU A C   1 
ATOM   2748 O O   . GLU A 1 324 ? 13.111  16.326  42.146  1.00 26.81 ? 324 GLU A O   1 
ATOM   2749 C CB  . GLU A 1 324 ? 16.161  16.808  40.910  1.00 37.45 ? 324 GLU A CB  1 
ATOM   2750 C CG  . GLU A 1 324 ? 16.322  17.161  42.382  1.00 46.54 ? 324 GLU A CG  1 
ATOM   2751 C CD  . GLU A 1 324 ? 16.746  15.975  43.237  1.00 56.94 ? 324 GLU A CD  1 
ATOM   2752 O OE1 . GLU A 1 324 ? 17.123  14.921  42.674  1.00 57.40 ? 324 GLU A OE1 1 
ATOM   2753 O OE2 . GLU A 1 324 ? 16.706  16.104  44.482  1.00 62.86 ? 324 GLU A OE2 1 
ATOM   2754 N N   . ASP A 1 325 ? 13.189  17.738  40.396  1.00 28.80 ? 325 ASP A N   1 
ATOM   2755 C CA  . ASP A 1 325 ? 11.993  18.447  40.834  1.00 29.33 ? 325 ASP A CA  1 
ATOM   2756 C C   . ASP A 1 325 ? 10.758  17.563  40.743  1.00 21.39 ? 325 ASP A C   1 
ATOM   2757 O O   . ASP A 1 325 ? 9.904   17.590  41.635  1.00 21.43 ? 325 ASP A O   1 
ATOM   2758 C CB  . ASP A 1 325 ? 11.792  19.713  40.003  1.00 29.80 ? 325 ASP A CB  1 
ATOM   2759 C CG  . ASP A 1 325 ? 12.758  20.816  40.381  1.00 44.37 ? 325 ASP A CG  1 
ATOM   2760 O OD1 . ASP A 1 325 ? 13.544  20.624  41.333  1.00 49.48 ? 325 ASP A OD1 1 
ATOM   2761 O OD2 . ASP A 1 325 ? 12.726  21.878  39.725  1.00 44.15 ? 325 ASP A OD2 1 
ATOM   2762 N N   . ALA A 1 326 ? 10.645  16.778  39.669  1.00 22.80 ? 326 ALA A N   1 
ATOM   2763 C CA  . ALA A 1 326 ? 9.486   15.906  39.502  1.00 20.62 ? 326 ALA A CA  1 
ATOM   2764 C C   . ALA A 1 326 ? 9.400   14.873  40.620  1.00 21.24 ? 326 ALA A C   1 
ATOM   2765 O O   . ALA A 1 326 ? 8.318   14.627  41.166  1.00 21.16 ? 326 ALA A O   1 
ATOM   2766 C CB  . ALA A 1 326 ? 9.547   15.215  38.136  1.00 16.57 ? 326 ALA A CB  1 
ATOM   2767 N N   . VAL A 1 327 ? 10.526  14.250  40.967  1.00 24.22 ? 327 VAL A N   1 
ATOM   2768 C CA  . VAL A 1 327 ? 10.506  13.226  42.009  1.00 22.32 ? 327 VAL A CA  1 
ATOM   2769 C C   . VAL A 1 327 ? 10.156  13.846  43.357  1.00 20.57 ? 327 VAL A C   1 
ATOM   2770 O O   . VAL A 1 327 ? 9.369   13.286  44.134  1.00 17.59 ? 327 VAL A O   1 
ATOM   2771 C CB  . VAL A 1 327 ? 11.856  12.496  42.050  1.00 24.97 ? 327 VAL A CB  1 
ATOM   2772 C CG1 . VAL A 1 327 ? 11.967  11.652  43.333  1.00 23.84 ? 327 VAL A CG1 1 
ATOM   2773 C CG2 . VAL A 1 327 ? 12.027  11.633  40.790  1.00 26.06 ? 327 VAL A CG2 1 
ATOM   2774 N N   . ARG A 1 328 ? 10.733  15.015  43.648  1.00 15.75 ? 328 ARG A N   1 
ATOM   2775 C CA  . ARG A 1 328 ? 10.413  15.735  44.879  1.00 19.81 ? 328 ARG A CA  1 
ATOM   2776 C C   . ARG A 1 328 ? 8.929   16.074  44.944  1.00 24.78 ? 328 ARG A C   1 
ATOM   2777 O O   . ARG A 1 328 ? 8.295   15.922  45.995  1.00 22.08 ? 328 ARG A O   1 
ATOM   2778 C CB  . ARG A 1 328 ? 11.284  16.994  44.977  1.00 31.23 ? 328 ARG A CB  1 
ATOM   2779 C CG  . ARG A 1 328 ? 10.696  18.156  45.767  1.00 41.77 ? 328 ARG A CG  1 
ATOM   2780 C CD  . ARG A 1 328 ? 11.548  19.426  45.583  1.00 49.46 ? 328 ARG A CD  1 
ATOM   2781 N NE  . ARG A 1 328 ? 11.204  20.155  44.363  1.00 52.74 ? 328 ARG A NE  1 
ATOM   2782 C CZ  . ARG A 1 328 ? 10.207  21.031  44.273  1.00 57.75 ? 328 ARG A CZ  1 
ATOM   2783 N NH1 . ARG A 1 328 ? 9.461   21.297  45.339  1.00 63.41 ? 328 ARG A NH1 1 
ATOM   2784 N NH2 . ARG A 1 328 ? 9.959   21.647  43.123  1.00 55.95 ? 328 ARG A NH2 1 
ATOM   2785 N N   . ASP A 1 329 ? 8.353   16.518  43.823  1.00 24.36 ? 329 ASP A N   1 
ATOM   2786 C CA  . ASP A 1 329 ? 6.918   16.781  43.781  1.00 26.38 ? 329 ASP A CA  1 
ATOM   2787 C C   . ASP A 1 329 ? 6.113   15.516  44.060  1.00 24.70 ? 329 ASP A C   1 
ATOM   2788 O O   . ASP A 1 329 ? 5.142   15.541  44.832  1.00 25.14 ? 329 ASP A O   1 
ATOM   2789 C CB  . ASP A 1 329 ? 6.531   17.362  42.420  1.00 17.43 ? 329 ASP A CB  1 
ATOM   2790 C CG  . ASP A 1 329 ? 5.063   17.708  42.338  1.00 24.94 ? 329 ASP A CG  1 
ATOM   2791 O OD1 . ASP A 1 329 ? 4.655   18.757  42.884  1.00 29.54 ? 329 ASP A OD1 1 
ATOM   2792 O OD2 . ASP A 1 329 ? 4.304   16.925  41.745  1.00 27.24 ? 329 ASP A OD2 1 
ATOM   2793 N N   . PHE A 1 330 ? 6.506   14.401  43.434  1.00 17.13 ? 330 PHE A N   1 
ATOM   2794 C CA  . PHE A 1 330 ? 5.776   13.142  43.580  1.00 16.90 ? 330 PHE A CA  1 
ATOM   2795 C C   . PHE A 1 330 ? 5.826   12.640  45.022  1.00 18.79 ? 330 PHE A C   1 
ATOM   2796 O O   . PHE A 1 330 ? 4.785   12.322  45.615  1.00 18.82 ? 330 PHE A O   1 
ATOM   2797 C CB  . PHE A 1 330 ? 6.356   12.103  42.608  1.00 15.37 ? 330 PHE A CB  1 
ATOM   2798 C CG  . PHE A 1 330 ? 5.520   10.851  42.450  1.00 18.78 ? 330 PHE A CG  1 
ATOM   2799 C CD1 . PHE A 1 330 ? 4.475   10.800  41.535  1.00 23.93 ? 330 PHE A CD1 1 
ATOM   2800 C CD2 . PHE A 1 330 ? 5.807   9.714   43.188  1.00 18.45 ? 330 PHE A CD2 1 
ATOM   2801 C CE1 . PHE A 1 330 ? 3.720   9.645   41.375  1.00 21.24 ? 330 PHE A CE1 1 
ATOM   2802 C CE2 . PHE A 1 330 ? 5.057   8.548   43.039  1.00 19.68 ? 330 PHE A CE2 1 
ATOM   2803 C CZ  . PHE A 1 330 ? 4.013   8.509   42.133  1.00 16.79 ? 330 PHE A CZ  1 
ATOM   2804 N N   . ILE A 1 331 ? 7.027   12.570  45.604  1.00 17.50 ? 331 ILE A N   1 
ATOM   2805 C CA  . ILE A 1 331 ? 7.172   12.086  46.973  1.00 20.28 ? 331 ILE A CA  1 
ATOM   2806 C C   . ILE A 1 331 ? 6.459   13.023  47.940  1.00 23.25 ? 331 ILE A C   1 
ATOM   2807 O O   . ILE A 1 331 ? 5.900   12.578  48.948  1.00 24.43 ? 331 ILE A O   1 
ATOM   2808 C CB  . ILE A 1 331 ? 8.665   11.933  47.333  1.00 22.29 ? 331 ILE A CB  1 
ATOM   2809 C CG1 . ILE A 1 331 ? 9.367   10.967  46.380  1.00 24.52 ? 331 ILE A CG1 1 
ATOM   2810 C CG2 . ILE A 1 331 ? 8.846   11.475  48.789  1.00 30.76 ? 331 ILE A CG2 1 
ATOM   2811 C CD1 . ILE A 1 331 ? 9.113   9.498   46.664  1.00 25.16 ? 331 ILE A CD1 1 
ATOM   2812 N N   . GLY A 1 332 ? 6.453   14.325  47.647  1.00 25.91 ? 332 GLY A N   1 
ATOM   2813 C CA  . GLY A 1 332 ? 5.754   15.262  48.508  1.00 19.76 ? 332 GLY A CA  1 
ATOM   2814 C C   . GLY A 1 332 ? 4.259   15.012  48.548  1.00 22.89 ? 332 GLY A C   1 
ATOM   2815 O O   . GLY A 1 332 ? 3.640   15.066  49.611  1.00 25.41 ? 332 GLY A O   1 
ATOM   2816 N N   . ARG A 1 333 ? 3.660   14.714  47.392  1.00 19.45 ? 333 ARG A N   1 
ATOM   2817 C CA  . ARG A 1 333 ? 2.234   14.415  47.366  1.00 24.10 ? 333 ARG A CA  1 
ATOM   2818 C C   . ARG A 1 333 ? 1.922   13.120  48.103  1.00 23.88 ? 333 ARG A C   1 
ATOM   2819 O O   . ARG A 1 333 ? 0.878   13.015  48.757  1.00 19.28 ? 333 ARG A O   1 
ATOM   2820 C CB  . ARG A 1 333 ? 1.735   14.340  45.926  1.00 22.95 ? 333 ARG A CB  1 
ATOM   2821 C CG  . ARG A 1 333 ? 1.873   15.646  45.172  1.00 21.80 ? 333 ARG A CG  1 
ATOM   2822 C CD  . ARG A 1 333 ? 1.549   15.456  43.708  1.00 23.94 ? 333 ARG A CD  1 
ATOM   2823 N NE  . ARG A 1 333 ? 1.679   16.697  42.955  1.00 22.35 ? 333 ARG A NE  1 
ATOM   2824 C CZ  . ARG A 1 333 ? 0.671   17.514  42.667  1.00 22.99 ? 333 ARG A CZ  1 
ATOM   2825 N NH1 . ARG A 1 333 ? -0.562  17.226  43.070  1.00 19.97 ? 333 ARG A NH1 1 
ATOM   2826 N NH2 . ARG A 1 333 ? 0.899   18.624  41.979  1.00 27.27 ? 333 ARG A NH2 1 
ATOM   2827 N N   . LEU A 1 334 ? 2.805   12.117  48.001  1.00 19.26 ? 334 LEU A N   1 
ATOM   2828 C CA  . LEU A 1 334 ? 2.613   10.883  48.758  1.00 15.99 ? 334 LEU A CA  1 
ATOM   2829 C C   . LEU A 1 334 ? 2.663   11.154  50.252  1.00 18.38 ? 334 LEU A C   1 
ATOM   2830 O O   . LEU A 1 334 ? 1.891   10.576  51.026  1.00 21.34 ? 334 LEU A O   1 
ATOM   2831 C CB  . LEU A 1 334 ? 3.682   9.859   48.383  1.00 12.88 ? 334 LEU A CB  1 
ATOM   2832 C CG  . LEU A 1 334 ? 3.574   9.276   46.978  1.00 13.47 ? 334 LEU A CG  1 
ATOM   2833 C CD1 . LEU A 1 334 ? 4.696   8.279   46.729  1.00 12.96 ? 334 LEU A CD1 1 
ATOM   2834 C CD2 . LEU A 1 334 ? 2.185   8.650   46.769  1.00 14.89 ? 334 LEU A CD2 1 
ATOM   2835 N N   . LYS A 1 335 ? 3.593   12.010  50.676  1.00 17.10 ? 335 LYS A N   1 
ATOM   2836 C CA  . LYS A 1 335 ? 3.660   12.402  52.079  1.00 27.52 ? 335 LYS A CA  1 
ATOM   2837 C C   . LYS A 1 335 ? 2.351   13.024  52.545  1.00 26.62 ? 335 LYS A C   1 
ATOM   2838 O O   . LYS A 1 335 ? 1.876   12.727  53.647  1.00 24.24 ? 335 LYS A O   1 
ATOM   2839 C CB  . LYS A 1 335 ? 4.811   13.376  52.288  1.00 20.55 ? 335 LYS A CB  1 
ATOM   2840 C CG  . LYS A 1 335 ? 4.969   13.812  53.731  1.00 35.99 ? 335 LYS A CG  1 
ATOM   2841 C CD  . LYS A 1 335 ? 6.179   14.696  53.883  1.00 38.33 ? 335 LYS A CD  1 
ATOM   2842 C CE  . LYS A 1 335 ? 5.825   16.163  53.708  1.00 41.82 ? 335 LYS A CE  1 
ATOM   2843 N NZ  . LYS A 1 335 ? 5.418   16.769  55.007  1.00 41.24 ? 335 LYS A NZ  1 
ATOM   2844 N N   . LYS A 1 336 ? 1.763   13.902  51.725  1.00 26.01 ? 336 LYS A N   1 
ATOM   2845 C CA  . LYS A 1 336 ? 0.499   14.537  52.086  1.00 31.04 ? 336 LYS A CA  1 
ATOM   2846 C C   . LYS A 1 336 ? -0.609  13.501  52.250  1.00 31.25 ? 336 LYS A C   1 
ATOM   2847 O O   . LYS A 1 336 ? -1.331  13.503  53.251  1.00 32.98 ? 336 LYS A O   1 
ATOM   2848 C CB  . LYS A 1 336 ? 0.119   15.587  51.038  1.00 33.78 ? 336 LYS A CB  1 
ATOM   2849 C CG  . LYS A 1 336 ? 0.524   17.016  51.408  1.00 43.63 ? 336 LYS A CG  1 
ATOM   2850 C CD  . LYS A 1 336 ? 1.622   17.561  50.501  1.00 48.43 ? 336 LYS A CD  1 
ATOM   2851 C CE  . LYS A 1 336 ? 1.083   17.909  49.119  1.00 56.91 ? 336 LYS A CE  1 
ATOM   2852 N NZ  . LYS A 1 336 ? 2.160   18.350  48.181  1.00 59.21 ? 336 LYS A NZ  1 
ATOM   2853 N N   . ILE A 1 337 ? -0.757  12.601  51.274  1.00 29.65 ? 337 ILE A N   1 
ATOM   2854 C CA  . ILE A 1 337 ? -1.666  11.467  51.438  1.00 21.74 ? 337 ILE A CA  1 
ATOM   2855 C C   . ILE A 1 337 ? -1.387  10.760  52.759  1.00 26.41 ? 337 ILE A C   1 
ATOM   2856 O O   . ILE A 1 337 ? -2.291  10.529  53.572  1.00 26.17 ? 337 ILE A O   1 
ATOM   2857 C CB  . ILE A 1 337 ? -1.530  10.488  50.256  1.00 19.97 ? 337 ILE A CB  1 
ATOM   2858 C CG1 . ILE A 1 337 ? -1.772  11.186  48.920  1.00 22.03 ? 337 ILE A CG1 1 
ATOM   2859 C CG2 . ILE A 1 337 ? -2.489  9.341   50.434  1.00 19.86 ? 337 ILE A CG2 1 
ATOM   2860 C CD1 . ILE A 1 337 ? -1.508  10.286  47.714  1.00 26.53 ? 337 ILE A CD1 1 
ATOM   2861 N N   . HIS A 1 338 ? -0.116  10.424  52.992  1.00 20.36 ? 338 HIS A N   1 
ATOM   2862 C CA  . HIS A 1 338 ? 0.264   9.633   54.160  1.00 19.95 ? 338 HIS A CA  1 
ATOM   2863 C C   . HIS A 1 338 ? -0.165  10.316  55.453  1.00 26.49 ? 338 HIS A C   1 
ATOM   2864 O O   . HIS A 1 338 ? -0.682  9.665   56.367  1.00 22.22 ? 338 HIS A O   1 
ATOM   2865 C CB  . HIS A 1 338 ? 1.777   9.390   54.131  1.00 22.81 ? 338 HIS A CB  1 
ATOM   2866 C CG  . HIS A 1 338 ? 2.299   8.606   55.292  1.00 29.55 ? 338 HIS A CG  1 
ATOM   2867 N ND1 . HIS A 1 338 ? 2.963   9.195   56.346  1.00 34.73 ? 338 HIS A ND1 1 
ATOM   2868 C CD2 . HIS A 1 338 ? 2.287   7.276   55.551  1.00 32.85 ? 338 HIS A CD2 1 
ATOM   2869 C CE1 . HIS A 1 338 ? 3.323   8.265   57.212  1.00 29.47 ? 338 HIS A CE1 1 
ATOM   2870 N NE2 . HIS A 1 338 ? 2.927   7.092   56.753  1.00 35.10 ? 338 HIS A NE2 1 
ATOM   2871 N N   . GLU A 1 339 ? -0.006  11.634  55.532  1.00 27.65 ? 339 GLU A N   1 
ATOM   2872 C CA  . GLU A 1 339 ? -0.379  12.348  56.746  1.00 33.24 ? 339 GLU A CA  1 
ATOM   2873 C C   . GLU A 1 339 ? -1.859  12.693  56.811  1.00 33.99 ? 339 GLU A C   1 
ATOM   2874 O O   . GLU A 1 339 ? -2.317  13.162  57.856  1.00 30.42 ? 339 GLU A O   1 
ATOM   2875 C CB  . GLU A 1 339 ? 0.437   13.629  56.870  1.00 31.37 ? 339 GLU A CB  1 
ATOM   2876 C CG  . GLU A 1 339 ? 1.845   13.404  57.360  1.00 42.02 ? 339 GLU A CG  1 
ATOM   2877 C CD  . GLU A 1 339 ? 2.791   14.496  56.924  1.00 51.09 ? 339 GLU A CD  1 
ATOM   2878 O OE1 . GLU A 1 339 ? 2.312   15.518  56.379  1.00 47.25 ? 339 GLU A OE1 1 
ATOM   2879 O OE2 . GLU A 1 339 ? 4.016   14.328  57.133  1.00 58.28 ? 339 GLU A OE2 1 
ATOM   2880 N N   . SER A 1 340 ? -2.611  12.476  55.737  1.00 36.49 ? 340 SER A N   1 
ATOM   2881 C CA  . SER A 1 340 ? -3.997  12.915  55.666  1.00 31.20 ? 340 SER A CA  1 
ATOM   2882 C C   . SER A 1 340 ? -4.985  11.888  56.202  1.00 31.22 ? 340 SER A C   1 
ATOM   2883 O O   . SER A 1 340 ? -6.157  12.226  56.394  1.00 31.72 ? 340 SER A O   1 
ATOM   2884 C CB  . SER A 1 340 ? -4.364  13.259  54.219  1.00 33.77 ? 340 SER A CB  1 
ATOM   2885 O OG  . SER A 1 340 ? -4.613  12.081  53.463  1.00 37.11 ? 340 SER A OG  1 
ATOM   2886 N N   . VAL A 1 341 ? -4.555  10.652  56.440  1.00 26.27 ? 341 VAL A N   1 
ATOM   2887 C CA  . VAL A 1 341 ? -5.457  9.576   56.827  1.00 22.61 ? 341 VAL A CA  1 
ATOM   2888 C C   . VAL A 1 341 ? -4.873  8.877   58.042  1.00 27.62 ? 341 VAL A C   1 
ATOM   2889 O O   . VAL A 1 341 ? -3.662  8.920   58.284  1.00 27.33 ? 341 VAL A O   1 
ATOM   2890 C CB  . VAL A 1 341 ? -5.687  8.572   55.667  1.00 26.86 ? 341 VAL A CB  1 
ATOM   2891 C CG1 . VAL A 1 341 ? -6.294  9.272   54.465  1.00 27.21 ? 341 VAL A CG1 1 
ATOM   2892 C CG2 . VAL A 1 341 ? -4.378  7.885   55.275  1.00 26.97 ? 341 VAL A CG2 1 
ATOM   2893 N N   . ASP A 1 342 ? -5.743  8.230   58.815  1.00 30.96 ? 342 ASP A N   1 
ATOM   2894 C CA  . ASP A 1 342 ? -5.314  7.532   60.018  1.00 34.95 ? 342 ASP A CA  1 
ATOM   2895 C C   . ASP A 1 342 ? -5.082  6.047   59.792  1.00 29.78 ? 342 ASP A C   1 
ATOM   2896 O O   . ASP A 1 342 ? -4.675  5.347   60.723  1.00 36.09 ? 342 ASP A O   1 
ATOM   2897 C CB  . ASP A 1 342 ? -6.330  7.737   61.140  1.00 46.69 ? 342 ASP A CB  1 
ATOM   2898 C CG  . ASP A 1 342 ? -6.209  9.102   61.779  1.00 64.13 ? 342 ASP A CG  1 
ATOM   2899 O OD1 . ASP A 1 342 ? -5.085  9.453   62.203  1.00 69.18 ? 342 ASP A OD1 1 
ATOM   2900 O OD2 . ASP A 1 342 ? -7.228  9.817   61.865  1.00 70.24 ? 342 ASP A OD2 1 
ATOM   2901 N N   . PHE A 1 343 ? -5.305  5.561   58.581  1.00 16.87 ? 343 PHE A N   1 
ATOM   2902 C CA  . PHE A 1 343 ? -5.086  4.174   58.217  1.00 18.31 ? 343 PHE A CA  1 
ATOM   2903 C C   . PHE A 1 343 ? -3.919  4.112   57.233  1.00 13.69 ? 343 PHE A C   1 
ATOM   2904 O O   . PHE A 1 343 ? -3.309  5.129   56.895  1.00 19.81 ? 343 PHE A O   1 
ATOM   2905 C CB  . PHE A 1 343 ? -6.371  3.574   57.629  1.00 20.21 ? 343 PHE A CB  1 
ATOM   2906 C CG  . PHE A 1 343 ? -6.931  4.354   56.458  1.00 23.25 ? 343 PHE A CG  1 
ATOM   2907 C CD1 . PHE A 1 343 ? -7.762  5.453   56.663  1.00 21.94 ? 343 PHE A CD1 1 
ATOM   2908 C CD2 . PHE A 1 343 ? -6.629  3.982   55.151  1.00 16.99 ? 343 PHE A CD2 1 
ATOM   2909 C CE1 . PHE A 1 343 ? -8.274  6.171   55.591  1.00 22.38 ? 343 PHE A CE1 1 
ATOM   2910 C CE2 . PHE A 1 343 ? -7.137  4.697   54.076  1.00 18.17 ? 343 PHE A CE2 1 
ATOM   2911 C CZ  . PHE A 1 343 ? -7.961  5.793   54.295  1.00 23.77 ? 343 PHE A CZ  1 
ATOM   2912 N N   . GLN A 1 344 ? -3.603  2.912   56.789  1.00 14.05 ? 344 GLN A N   1 
ATOM   2913 C CA  . GLN A 1 344 ? -2.553  2.765   55.788  1.00 13.07 ? 344 GLN A CA  1 
ATOM   2914 C C   . GLN A 1 344 ? -3.178  2.814   54.396  1.00 13.76 ? 344 GLN A C   1 
ATOM   2915 O O   . GLN A 1 344 ? -3.800  1.841   53.970  1.00 12.98 ? 344 GLN A O   1 
ATOM   2916 C CB  . GLN A 1 344 ? -1.790  1.460   56.005  1.00 14.38 ? 344 GLN A CB  1 
ATOM   2917 C CG  . GLN A 1 344 ? -1.229  1.321   57.417  1.00 20.52 ? 344 GLN A CG  1 
ATOM   2918 C CD  . GLN A 1 344 ? -0.328  0.118   57.580  1.00 20.47 ? 344 GLN A CD  1 
ATOM   2919 O OE1 . GLN A 1 344 ? 0.865   0.256   57.823  1.00 20.94 ? 344 GLN A OE1 1 
ATOM   2920 N NE2 . GLN A 1 344 ? -0.898  -1.073  57.442  1.00 15.94 ? 344 GLN A NE2 1 
ATOM   2921 N N   . PRO A 1 345 ? -3.036  3.922   53.667  1.00 13.27 ? 345 PRO A N   1 
ATOM   2922 C CA  . PRO A 1 345 ? -3.683  4.036   52.353  1.00 15.68 ? 345 PRO A CA  1 
ATOM   2923 C C   . PRO A 1 345 ? -3.013  3.179   51.291  1.00 16.93 ? 345 PRO A C   1 
ATOM   2924 O O   . PRO A 1 345 ? -1.801  2.953   51.308  1.00 15.53 ? 345 PRO A O   1 
ATOM   2925 C CB  . PRO A 1 345 ? -3.515  5.517   52.015  1.00 20.01 ? 345 PRO A CB  1 
ATOM   2926 C CG  . PRO A 1 345 ? -2.197  5.875   52.678  1.00 18.92 ? 345 PRO A CG  1 
ATOM   2927 C CD  . PRO A 1 345 ? -2.146  5.064   53.954  1.00 14.41 ? 345 PRO A CD  1 
ATOM   2928 N N   . VAL A 1 346 ? -3.816  2.744   50.325  1.00 17.54 ? 346 VAL A N   1 
ATOM   2929 C CA  . VAL A 1 346 ? -3.319  2.045   49.148  1.00 12.42 ? 346 VAL A CA  1 
ATOM   2930 C C   . VAL A 1 346 ? -3.442  3.004   47.979  1.00 18.49 ? 346 VAL A C   1 
ATOM   2931 O O   . VAL A 1 346 ? -4.536  3.499   47.688  1.00 15.42 ? 346 VAL A O   1 
ATOM   2932 C CB  . VAL A 1 346 ? -4.085  0.739   48.891  1.00 14.44 ? 346 VAL A CB  1 
ATOM   2933 C CG1 . VAL A 1 346 ? -3.495  -0.005  47.693  1.00 15.41 ? 346 VAL A CG1 1 
ATOM   2934 C CG2 . VAL A 1 346 ? -4.046  -0.124  50.146  1.00 17.95 ? 346 VAL A CG2 1 
ATOM   2935 N N   . VAL A 1 347 ? -2.317  3.283   47.324  1.00 9.28  ? 347 VAL A N   1 
ATOM   2936 C CA  . VAL A 1 347 ? -2.241  4.260   46.256  1.00 11.29 ? 347 VAL A CA  1 
ATOM   2937 C C   . VAL A 1 347 ? -1.886  3.515   44.979  1.00 18.13 ? 347 VAL A C   1 
ATOM   2938 O O   . VAL A 1 347 ? -0.754  3.041   44.827  1.00 13.08 ? 347 VAL A O   1 
ATOM   2939 C CB  . VAL A 1 347 ? -1.212  5.350   46.558  1.00 12.90 ? 347 VAL A CB  1 
ATOM   2940 C CG1 . VAL A 1 347 ? -1.224  6.394   45.449  1.00 20.51 ? 347 VAL A CG1 1 
ATOM   2941 C CG2 . VAL A 1 347 ? -1.512  5.965   47.922  1.00 13.42 ? 347 VAL A CG2 1 
ATOM   2942 N N   . PHE A 1 348 ? -2.846  3.425   44.063  1.00 13.84 ? 348 PHE A N   1 
ATOM   2943 C CA  . PHE A 1 348 ? -2.653  2.782   42.771  1.00 10.88 ? 348 PHE A CA  1 
ATOM   2944 C C   . PHE A 1 348 ? -2.241  3.826   41.740  1.00 18.91 ? 348 PHE A C   1 
ATOM   2945 O O   . PHE A 1 348 ? -2.933  4.833   41.547  1.00 15.09 ? 348 PHE A O   1 
ATOM   2946 C CB  . PHE A 1 348 ? -3.925  2.056   42.314  1.00 9.03  ? 348 PHE A CB  1 
ATOM   2947 C CG  . PHE A 1 348 ? -3.905  0.574   42.602  1.00 15.75 ? 348 PHE A CG  1 
ATOM   2948 C CD1 . PHE A 1 348 ? -3.947  0.113   43.917  1.00 10.53 ? 348 PHE A CD1 1 
ATOM   2949 C CD2 . PHE A 1 348 ? -3.830  -0.351  41.567  1.00 15.70 ? 348 PHE A CD2 1 
ATOM   2950 C CE1 . PHE A 1 348 ? -3.931  -1.252  44.189  1.00 12.25 ? 348 PHE A CE1 1 
ATOM   2951 C CE2 . PHE A 1 348 ? -3.816  -1.724  41.832  1.00 13.05 ? 348 PHE A CE2 1 
ATOM   2952 C CZ  . PHE A 1 348 ? -3.872  -2.167  43.140  1.00 10.01 ? 348 PHE A CZ  1 
ATOM   2953 N N   . VAL A 1 349 ? -1.107  3.587   41.096  1.00 12.54 ? 349 VAL A N   1 
ATOM   2954 C CA  . VAL A 1 349 ? -0.582  4.440   40.039  1.00 9.14  ? 349 VAL A CA  1 
ATOM   2955 C C   . VAL A 1 349 ? -0.648  3.597   38.775  1.00 12.16 ? 349 VAL A C   1 
ATOM   2956 O O   . VAL A 1 349 ? 0.129   2.647   38.620  1.00 14.18 ? 349 VAL A O   1 
ATOM   2957 C CB  . VAL A 1 349 ? 0.851   4.908   40.344  1.00 10.39 ? 349 VAL A CB  1 
ATOM   2958 C CG1 . VAL A 1 349 ? 1.447   5.691   39.153  1.00 11.30 ? 349 VAL A CG1 1 
ATOM   2959 C CG2 . VAL A 1 349 ? 0.882   5.729   41.639  1.00 15.50 ? 349 VAL A CG2 1 
ATOM   2960 N N   . VAL A 1 350 ? -1.607  3.905   37.891  1.00 12.30 ? 350 VAL A N   1 
ATOM   2961 C CA  . VAL A 1 350 ? -1.905  3.080   36.721  1.00 14.17 ? 350 VAL A CA  1 
ATOM   2962 C C   . VAL A 1 350 ? -1.941  3.981   35.494  1.00 14.18 ? 350 VAL A C   1 
ATOM   2963 O O   . VAL A 1 350 ? -2.661  4.984   35.480  1.00 13.53 ? 350 VAL A O   1 
ATOM   2964 C CB  . VAL A 1 350 ? -3.247  2.329   36.878  1.00 14.88 ? 350 VAL A CB  1 
ATOM   2965 C CG1 . VAL A 1 350 ? -3.460  1.345   35.720  1.00 12.03 ? 350 VAL A CG1 1 
ATOM   2966 C CG2 . VAL A 1 350 ? -3.317  1.609   38.240  1.00 8.91  ? 350 VAL A CG2 1 
ATOM   2967 N N   . LEU A 1 351 ? -1.158  3.632   34.474  1.00 12.89 ? 351 LEU A N   1 
ATOM   2968 C CA  . LEU A 1 351 ? -1.143  4.394   33.233  1.00 12.25 ? 351 LEU A CA  1 
ATOM   2969 C C   . LEU A 1 351 ? -0.499  3.535   32.156  1.00 9.08  ? 351 LEU A C   1 
ATOM   2970 O O   . LEU A 1 351 ? 0.048   2.463   32.437  1.00 11.91 ? 351 LEU A O   1 
ATOM   2971 C CB  . LEU A 1 351 ? -0.403  5.729   33.396  1.00 10.88 ? 351 LEU A CB  1 
ATOM   2972 C CG  . LEU A 1 351 ? 1.070   5.678   33.845  1.00 11.29 ? 351 LEU A CG  1 
ATOM   2973 C CD1 . LEU A 1 351 ? 1.836   6.849   33.233  1.00 11.11 ? 351 LEU A CD1 1 
ATOM   2974 C CD2 . LEU A 1 351 ? 1.195   5.717   35.362  1.00 9.64  ? 351 LEU A CD2 1 
ATOM   2975 N N   . ASP A 1 352 ? -0.596  4.005   30.911  1.00 11.07 ? 352 ASP A N   1 
ATOM   2976 C CA  . ASP A 1 352 ? 0.150   3.374   29.826  1.00 10.94 ? 352 ASP A CA  1 
ATOM   2977 C C   . ASP A 1 352 ? 1.620   3.318   30.207  1.00 14.93 ? 352 ASP A C   1 
ATOM   2978 O O   . ASP A 1 352 ? 2.165   4.281   30.751  1.00 16.04 ? 352 ASP A O   1 
ATOM   2979 C CB  . ASP A 1 352 ? 0.002   4.163   28.520  1.00 10.41 ? 352 ASP A CB  1 
ATOM   2980 C CG  . ASP A 1 352 ? -1.382  4.115   27.959  1.00 23.31 ? 352 ASP A CG  1 
ATOM   2981 O OD1 . ASP A 1 352 ? -2.246  3.407   28.534  1.00 14.62 ? 352 ASP A OD1 1 
ATOM   2982 O OD2 . ASP A 1 352 ? -1.587  4.787   26.924  1.00 19.47 ? 352 ASP A OD2 1 
ATOM   2983 N N   . GLY A 1 353 ? 2.259   2.183   29.931  1.00 9.98  ? 353 GLY A N   1 
ATOM   2984 C CA  . GLY A 1 353 ? 3.620   1.962   30.393  1.00 11.88 ? 353 GLY A CA  1 
ATOM   2985 C C   . GLY A 1 353 ? 4.713   2.287   29.393  1.00 14.72 ? 353 GLY A C   1 
ATOM   2986 O O   . GLY A 1 353 ? 5.899   2.243   29.733  1.00 13.83 ? 353 GLY A O   1 
ATOM   2987 N N   . GLU A 1 354 ? 4.341   2.627   28.158  1.00 10.90 ? 354 GLU A N   1 
ATOM   2988 C CA  . GLU A 1 354 ? 5.325   2.806   27.095  1.00 10.77 ? 354 GLU A CA  1 
ATOM   2989 C C   . GLU A 1 354 ? 5.211   4.123   26.325  1.00 15.13 ? 354 GLU A C   1 
ATOM   2990 O O   . GLU A 1 354 ? 6.114   4.434   25.539  1.00 14.21 ? 354 GLU A O   1 
ATOM   2991 C CB  . GLU A 1 354 ? 5.241   1.633   26.096  1.00 11.35 ? 354 GLU A CB  1 
ATOM   2992 C CG  . GLU A 1 354 ? 4.084   1.675   25.086  1.00 11.63 ? 354 GLU A CG  1 
ATOM   2993 C CD  . GLU A 1 354 ? 2.721   1.232   25.656  1.00 17.43 ? 354 GLU A CD  1 
ATOM   2994 O OE1 . GLU A 1 354 ? 2.221   0.160   25.257  1.00 13.68 ? 354 GLU A OE1 1 
ATOM   2995 O OE2 . GLU A 1 354 ? 2.140   1.950   26.487  1.00 12.69 ? 354 GLU A OE2 1 
ATOM   2996 N N   . ASN A 1 355 ? 4.168   4.920   26.541  1.00 12.68 ? 355 ASN A N   1 
ATOM   2997 C CA  . ASN A 1 355 ? 3.891   6.034   25.640  1.00 17.28 ? 355 ASN A CA  1 
ATOM   2998 C C   . ASN A 1 355 ? 4.421   7.383   26.116  1.00 14.31 ? 355 ASN A C   1 
ATOM   2999 O O   . ASN A 1 355 ? 4.675   8.258   25.280  1.00 17.54 ? 355 ASN A O   1 
ATOM   3000 C CB  . ASN A 1 355 ? 2.378   6.112   25.385  1.00 18.91 ? 355 ASN A CB  1 
ATOM   3001 C CG  . ASN A 1 355 ? 1.891   4.964   24.515  1.00 18.59 ? 355 ASN A CG  1 
ATOM   3002 O OD1 . ASN A 1 355 ? 2.606   4.528   23.618  1.00 13.79 ? 355 ASN A OD1 1 
ATOM   3003 N ND2 . ASN A 1 355 ? 0.701   4.437   24.808  1.00 17.13 ? 355 ASN A ND2 1 
ATOM   3004 N N   . CYS A 1 356 ? 4.646   7.571   27.416  1.00 13.61 ? 356 CYS A N   1 
ATOM   3005 C CA  . CYS A 1 356 ? 5.058   8.882   27.903  1.00 11.69 ? 356 CYS A CA  1 
ATOM   3006 C C   . CYS A 1 356 ? 6.564   9.122   27.826  1.00 11.90 ? 356 CYS A C   1 
ATOM   3007 O O   . CYS A 1 356 ? 6.980   10.284  27.750  1.00 17.56 ? 356 CYS A O   1 
ATOM   3008 C CB  . CYS A 1 356 ? 4.570   9.091   29.346  1.00 11.21 ? 356 CYS A CB  1 
ATOM   3009 S SG  . CYS A 1 356 ? 5.101   7.843   30.556  1.00 14.73 ? 356 CYS A SG  1 
ATOM   3010 N N   . TRP A 1 357 ? 7.388   8.068   27.817  1.00 12.84 ? 357 TRP A N   1 
ATOM   3011 C CA  . TRP A 1 357 ? 8.827   8.250   28.023  1.00 14.71 ? 357 TRP A CA  1 
ATOM   3012 C C   . TRP A 1 357 ? 9.504   8.980   26.867  1.00 16.71 ? 357 TRP A C   1 
ATOM   3013 O O   . TRP A 1 357 ? 10.494  9.695   27.085  1.00 18.38 ? 357 TRP A O   1 
ATOM   3014 C CB  . TRP A 1 357 ? 9.490   6.893   28.267  1.00 15.77 ? 357 TRP A CB  1 
ATOM   3015 C CG  . TRP A 1 357 ? 8.733   6.097   29.286  1.00 14.32 ? 357 TRP A CG  1 
ATOM   3016 C CD1 . TRP A 1 357 ? 8.153   4.873   29.105  1.00 13.63 ? 357 TRP A CD1 1 
ATOM   3017 C CD2 . TRP A 1 357 ? 8.450   6.483   30.637  1.00 13.83 ? 357 TRP A CD2 1 
ATOM   3018 N NE1 . TRP A 1 357 ? 7.525   4.472   30.259  1.00 13.08 ? 357 TRP A NE1 1 
ATOM   3019 C CE2 . TRP A 1 357 ? 7.689   5.446   31.215  1.00 14.08 ? 357 TRP A CE2 1 
ATOM   3020 C CE3 . TRP A 1 357 ? 8.763   7.610   31.415  1.00 13.73 ? 357 TRP A CE3 1 
ATOM   3021 C CZ2 . TRP A 1 357 ? 7.232   5.503   32.533  1.00 17.30 ? 357 TRP A CZ2 1 
ATOM   3022 C CZ3 . TRP A 1 357 ? 8.310   7.659   32.730  1.00 10.28 ? 357 TRP A CZ3 1 
ATOM   3023 C CH2 . TRP A 1 357 ? 7.556   6.612   33.272  1.00 15.27 ? 357 TRP A CH2 1 
ATOM   3024 N N   . GLU A 1 358 ? 9.000   8.824   25.641  1.00 16.72 ? 358 GLU A N   1 
ATOM   3025 C CA  . GLU A 1 358 ? 9.635   9.466   24.496  1.00 19.04 ? 358 GLU A CA  1 
ATOM   3026 C C   . GLU A 1 358 ? 9.611   10.987  24.582  1.00 13.07 ? 358 GLU A C   1 
ATOM   3027 O O   . GLU A 1 358 ? 10.360  11.641  23.844  1.00 17.32 ? 358 GLU A O   1 
ATOM   3028 C CB  . GLU A 1 358 ? 8.960   9.007   23.198  1.00 21.85 ? 358 GLU A CB  1 
ATOM   3029 C CG  . GLU A 1 358 ? 7.489   9.360   23.118  1.00 14.47 ? 358 GLU A CG  1 
ATOM   3030 C CD  . GLU A 1 358 ? 6.731   8.419   22.202  1.00 19.52 ? 358 GLU A CD  1 
ATOM   3031 O OE1 . GLU A 1 358 ? 6.179   8.887   21.186  1.00 21.80 ? 358 GLU A OE1 1 
ATOM   3032 O OE2 . GLU A 1 358 ? 6.708   7.206   22.500  1.00 22.10 ? 358 GLU A OE2 1 
ATOM   3033 N N   . TYR A 1 359 ? 8.797   11.564  25.468  1.00 13.16 ? 359 TYR A N   1 
ATOM   3034 C CA  . TYR A 1 359 ? 8.734   13.012  25.669  1.00 17.26 ? 359 TYR A CA  1 
ATOM   3035 C C   . TYR A 1 359 ? 9.605   13.501  26.815  1.00 19.30 ? 359 TYR A C   1 
ATOM   3036 O O   . TYR A 1 359 ? 9.698   14.713  27.022  1.00 22.10 ? 359 TYR A O   1 
ATOM   3037 C CB  . TYR A 1 359 ? 7.289   13.447  25.936  1.00 18.78 ? 359 TYR A CB  1 
ATOM   3038 C CG  . TYR A 1 359 ? 6.368   13.172  24.775  1.00 18.56 ? 359 TYR A CG  1 
ATOM   3039 C CD1 . TYR A 1 359 ? 6.355   14.012  23.663  1.00 20.97 ? 359 TYR A CD1 1 
ATOM   3040 C CD2 . TYR A 1 359 ? 5.524   12.070  24.777  1.00 17.71 ? 359 TYR A CD2 1 
ATOM   3041 C CE1 . TYR A 1 359 ? 5.519   13.764  22.587  1.00 25.58 ? 359 TYR A CE1 1 
ATOM   3042 C CE2 . TYR A 1 359 ? 4.681   11.811  23.694  1.00 22.03 ? 359 TYR A CE2 1 
ATOM   3043 C CZ  . TYR A 1 359 ? 4.689   12.664  22.609  1.00 20.88 ? 359 TYR A CZ  1 
ATOM   3044 O OH  . TYR A 1 359 ? 3.860   12.426  21.543  1.00 23.29 ? 359 TYR A OH  1 
ATOM   3045 N N   . TYR A 1 360 ? 10.187  12.591  27.587  1.00 17.56 ? 360 TYR A N   1 
ATOM   3046 C CA  . TYR A 1 360 ? 11.067  12.924  28.694  1.00 17.19 ? 360 TYR A CA  1 
ATOM   3047 C C   . TYR A 1 360 ? 12.494  13.057  28.193  1.00 17.42 ? 360 TYR A C   1 
ATOM   3048 O O   . TYR A 1 360 ? 12.920  12.321  27.300  1.00 22.42 ? 360 TYR A O   1 
ATOM   3049 C CB  . TYR A 1 360 ? 11.057  11.822  29.745  1.00 18.21 ? 360 TYR A CB  1 
ATOM   3050 C CG  . TYR A 1 360 ? 9.908   11.749  30.715  1.00 17.56 ? 360 TYR A CG  1 
ATOM   3051 C CD1 . TYR A 1 360 ? 8.626   11.385  30.305  1.00 16.57 ? 360 TYR A CD1 1 
ATOM   3052 C CD2 . TYR A 1 360 ? 10.130  11.961  32.069  1.00 14.60 ? 360 TYR A CD2 1 
ATOM   3053 C CE1 . TYR A 1 360 ? 7.585   11.275  31.229  1.00 13.37 ? 360 TYR A CE1 1 
ATOM   3054 C CE2 . TYR A 1 360 ? 9.105   11.857  32.993  1.00 15.34 ? 360 TYR A CE2 1 
ATOM   3055 C CZ  . TYR A 1 360 ? 7.846   11.507  32.576  1.00 13.17 ? 360 TYR A CZ  1 
ATOM   3056 O OH  . TYR A 1 360 ? 6.856   11.405  33.519  1.00 13.24 ? 360 TYR A OH  1 
ATOM   3057 N N   . GLU A 1 361 ? 13.254  13.964  28.808  1.00 18.64 ? 361 GLU A N   1 
ATOM   3058 C CA  . GLU A 1 361 ? 14.696  13.958  28.578  1.00 20.57 ? 361 GLU A CA  1 
ATOM   3059 C C   . GLU A 1 361 ? 15.258  12.558  28.820  1.00 20.19 ? 361 GLU A C   1 
ATOM   3060 O O   . GLU A 1 361 ? 14.874  11.878  29.776  1.00 20.83 ? 361 GLU A O   1 
ATOM   3061 C CB  . GLU A 1 361 ? 15.401  14.967  29.488  1.00 29.37 ? 361 GLU A CB  1 
ATOM   3062 C CG  . GLU A 1 361 ? 14.871  16.372  29.354  1.00 44.15 ? 361 GLU A CG  1 
ATOM   3063 C CD  . GLU A 1 361 ? 15.245  17.019  28.038  1.00 56.49 ? 361 GLU A CD  1 
ATOM   3064 O OE1 . GLU A 1 361 ? 16.299  16.648  27.480  1.00 66.12 ? 361 GLU A OE1 1 
ATOM   3065 O OE2 . GLU A 1 361 ? 14.492  17.904  27.569  1.00 54.55 ? 361 GLU A OE2 1 
ATOM   3066 N N   . GLU A 1 362 ? 16.151  12.120  27.923  1.00 17.78 ? 362 GLU A N   1 
ATOM   3067 C CA  . GLU A 1 362 ? 16.785  10.801  27.925  1.00 26.12 ? 362 GLU A CA  1 
ATOM   3068 C C   . GLU A 1 362 ? 15.750  9.682   28.151  1.00 28.05 ? 362 GLU A C   1 
ATOM   3069 O O   . GLU A 1 362 ? 15.982  8.743   28.929  1.00 19.00 ? 362 GLU A O   1 
ATOM   3070 C CB  . GLU A 1 362 ? 17.938  10.775  28.959  1.00 33.72 ? 362 GLU A CB  1 
ATOM   3071 C CG  . GLU A 1 362 ? 18.591  9.370   29.184  1.00 48.69 ? 362 GLU A CG  1 
ATOM   3072 C CD  . GLU A 1 362 ? 19.890  9.373   29.953  1.00 57.57 ? 362 GLU A CD  1 
ATOM   3073 O OE1 . GLU A 1 362 ? 20.795  10.156  29.601  1.00 58.00 ? 362 GLU A OE1 1 
ATOM   3074 O OE2 . GLU A 1 362 ? 20.019  8.565   30.898  1.00 58.53 ? 362 GLU A OE2 1 
ATOM   3075 N N   . ASN A 1 363 ? 14.596  9.763   27.474  1.00 20.92 ? 363 ASN A N   1 
ATOM   3076 C CA  . ASN A 1 363 ? 13.661  8.641   27.441  1.00 19.84 ? 363 ASN A CA  1 
ATOM   3077 C C   . ASN A 1 363 ? 13.199  8.241   28.845  1.00 14.47 ? 363 ASN A C   1 
ATOM   3078 O O   . ASN A 1 363 ? 12.880  7.075   29.106  1.00 16.30 ? 363 ASN A O   1 
ATOM   3079 C CB  . ASN A 1 363 ? 14.291  7.448   26.722  1.00 24.10 ? 363 ASN A CB  1 
ATOM   3080 C CG  . ASN A 1 363 ? 13.285  6.356   26.399  1.00 14.84 ? 363 ASN A CG  1 
ATOM   3081 O OD1 . ASN A 1 363 ? 12.142  6.628   26.018  1.00 14.40 ? 363 ASN A OD1 1 
ATOM   3082 N ND2 . ASN A 1 363 ? 13.708  5.102   26.553  1.00 17.92 ? 363 ASN A ND2 1 
ATOM   3083 N N   . GLY A 1 364 ? 13.137  9.209   29.755  1.00 15.67 ? 364 GLY A N   1 
ATOM   3084 C CA  . GLY A 1 364 ? 12.626  8.980   31.098  1.00 15.56 ? 364 GLY A CA  1 
ATOM   3085 C C   . GLY A 1 364 ? 13.562  8.256   32.031  1.00 17.21 ? 364 GLY A C   1 
ATOM   3086 O O   . GLY A 1 364 ? 13.169  7.940   33.161  1.00 14.58 ? 364 GLY A O   1 
ATOM   3087 N N   . ILE A 1 365 ? 14.793  7.996   31.612  1.00 18.15 ? 365 ILE A N   1 
ATOM   3088 C CA  . ILE A 1 365 ? 15.693  7.182   32.421  1.00 17.63 ? 365 ILE A CA  1 
ATOM   3089 C C   . ILE A 1 365 ? 16.150  7.972   33.646  1.00 18.50 ? 365 ILE A C   1 
ATOM   3090 O O   . ILE A 1 365 ? 16.153  7.404   34.748  1.00 21.95 ? 365 ILE A O   1 
ATOM   3091 C CB  . ILE A 1 365 ? 16.862  6.634   31.581  1.00 21.63 ? 365 ILE A CB  1 
ATOM   3092 C CG1 . ILE A 1 365 ? 16.344  5.584   30.589  1.00 20.89 ? 365 ILE A CG1 1 
ATOM   3093 C CG2 . ILE A 1 365 ? 17.927  6.008   32.478  1.00 15.38 ? 365 ILE A CG2 1 
ATOM   3094 C CD1 . ILE A 1 365 ? 17.299  5.282   29.441  1.00 21.39 ? 365 ILE A CD1 1 
ATOM   3095 N N   . PRO A 1 366 ? 16.527  9.260   33.536  1.00 17.08 ? 366 PRO A N   1 
ATOM   3096 C CA  . PRO A 1 366 ? 16.823  10.023  34.762  1.00 26.01 ? 366 PRO A CA  1 
ATOM   3097 C C   . PRO A 1 366 ? 15.671  10.062  35.744  1.00 20.81 ? 366 PRO A C   1 
ATOM   3098 O O   . PRO A 1 366 ? 15.883  9.896   36.955  1.00 19.11 ? 366 PRO A O   1 
ATOM   3099 C CB  . PRO A 1 366 ? 17.146  11.422  34.222  1.00 22.55 ? 366 PRO A CB  1 
ATOM   3100 C CG  . PRO A 1 366 ? 17.764  11.151  32.901  1.00 18.95 ? 366 PRO A CG  1 
ATOM   3101 C CD  . PRO A 1 366 ? 16.989  9.989   32.338  1.00 15.29 ? 366 PRO A CD  1 
ATOM   3102 N N   . PHE A 1 367 ? 14.453  10.280  35.250  1.00 17.79 ? 367 PHE A N   1 
ATOM   3103 C CA  . PHE A 1 367 ? 13.297  10.338  36.133  1.00 19.44 ? 367 PHE A CA  1 
ATOM   3104 C C   . PHE A 1 367 ? 13.091  9.010   36.853  1.00 17.41 ? 367 PHE A C   1 
ATOM   3105 O O   . PHE A 1 367 ? 13.054  8.961   38.088  1.00 15.86 ? 367 PHE A O   1 
ATOM   3106 C CB  . PHE A 1 367 ? 12.046  10.733  35.341  1.00 19.16 ? 367 PHE A CB  1 
ATOM   3107 C CG  . PHE A 1 367 ? 10.783  10.663  36.143  1.00 16.88 ? 367 PHE A CG  1 
ATOM   3108 C CD1 . PHE A 1 367 ? 10.512  11.616  37.120  1.00 21.93 ? 367 PHE A CD1 1 
ATOM   3109 C CD2 . PHE A 1 367 ? 9.872   9.638   35.944  1.00 14.75 ? 367 PHE A CD2 1 
ATOM   3110 C CE1 . PHE A 1 367 ? 9.343   11.549  37.885  1.00 16.78 ? 367 PHE A CE1 1 
ATOM   3111 C CE2 . PHE A 1 367 ? 8.696   9.568   36.700  1.00 16.19 ? 367 PHE A CE2 1 
ATOM   3112 C CZ  . PHE A 1 367 ? 8.442   10.519  37.677  1.00 18.43 ? 367 PHE A CZ  1 
ATOM   3113 N N   . LEU A 1 368 ? 12.969  7.912   36.092  1.00 14.43 ? 368 LEU A N   1 
ATOM   3114 C CA  . LEU A 1 368 ? 12.627  6.630   36.704  1.00 16.36 ? 368 LEU A CA  1 
ATOM   3115 C C   . LEU A 1 368 ? 13.726  6.143   37.645  1.00 14.50 ? 368 LEU A C   1 
ATOM   3116 O O   . LEU A 1 368 ? 13.431  5.623   38.726  1.00 18.79 ? 368 LEU A O   1 
ATOM   3117 C CB  . LEU A 1 368 ? 12.332  5.588   35.623  1.00 11.79 ? 368 LEU A CB  1 
ATOM   3118 C CG  . LEU A 1 368 ? 10.962  5.746   34.953  1.00 11.42 ? 368 LEU A CG  1 
ATOM   3119 C CD1 . LEU A 1 368 ? 10.747  4.644   33.895  1.00 12.46 ? 368 LEU A CD1 1 
ATOM   3120 C CD2 . LEU A 1 368 ? 9.826   5.750   35.989  1.00 16.00 ? 368 LEU A CD2 1 
ATOM   3121 N N   . GLU A 1 369 ? 14.998  6.281   37.260  1.00 16.82 ? 369 GLU A N   1 
ATOM   3122 C CA  . GLU A 1 369 ? 16.060  5.868   38.179  1.00 10.97 ? 369 GLU A CA  1 
ATOM   3123 C C   . GLU A 1 369 ? 16.024  6.701   39.459  1.00 18.56 ? 369 GLU A C   1 
ATOM   3124 O O   . GLU A 1 369 ? 16.166  6.161   40.563  1.00 20.28 ? 369 GLU A O   1 
ATOM   3125 C CB  . GLU A 1 369 ? 17.428  5.969   37.498  1.00 17.58 ? 369 GLU A CB  1 
ATOM   3126 C CG  . GLU A 1 369 ? 17.667  4.852   36.483  1.00 15.11 ? 369 GLU A CG  1 
ATOM   3127 C CD  . GLU A 1 369 ? 19.039  4.888   35.842  1.00 21.26 ? 369 GLU A CD  1 
ATOM   3128 O OE1 . GLU A 1 369 ? 19.810  5.848   36.083  1.00 23.84 ? 369 GLU A OE1 1 
ATOM   3129 O OE2 . GLU A 1 369 ? 19.345  3.947   35.089  1.00 21.51 ? 369 GLU A OE2 1 
ATOM   3130 N N   . LYS A 1 370 ? 15.804  8.011   39.333  1.00 16.78 ? 370 LYS A N   1 
ATOM   3131 C CA  . LYS A 1 370 ? 15.688  8.852   40.522  1.00 14.74 ? 370 LYS A CA  1 
ATOM   3132 C C   . LYS A 1 370 ? 14.441  8.505   41.330  1.00 20.99 ? 370 LYS A C   1 
ATOM   3133 O O   . LYS A 1 370 ? 14.502  8.413   42.561  1.00 20.92 ? 370 LYS A O   1 
ATOM   3134 C CB  . LYS A 1 370 ? 15.680  10.332  40.128  1.00 21.15 ? 370 LYS A CB  1 
ATOM   3135 C CG  . LYS A 1 370 ? 17.062  10.881  39.747  1.00 38.57 ? 370 LYS A CG  1 
ATOM   3136 C CD  . LYS A 1 370 ? 17.195  12.374  40.065  1.00 47.37 ? 370 LYS A CD  1 
ATOM   3137 C CE  . LYS A 1 370 ? 18.170  13.065  39.104  1.00 52.22 ? 370 LYS A CE  1 
ATOM   3138 N NZ  . LYS A 1 370 ? 19.613  12.770  39.384  1.00 55.98 ? 370 LYS A NZ  1 
ATOM   3139 N N   . LEU A 1 371 ? 13.306  8.293   40.656  1.00 19.96 ? 371 LEU A N   1 
ATOM   3140 C CA  . LEU A 1 371 ? 12.072  7.929   41.351  1.00 17.36 ? 371 LEU A CA  1 
ATOM   3141 C C   . LEU A 1 371 ? 12.232  6.618   42.109  1.00 19.94 ? 371 LEU A C   1 
ATOM   3142 O O   . LEU A 1 371 ? 11.957  6.543   43.313  1.00 21.27 ? 371 LEU A O   1 
ATOM   3143 C CB  . LEU A 1 371 ? 10.918  7.811   40.346  1.00 17.64 ? 371 LEU A CB  1 
ATOM   3144 C CG  . LEU A 1 371 ? 9.589   7.283   40.894  1.00 13.61 ? 371 LEU A CG  1 
ATOM   3145 C CD1 . LEU A 1 371 ? 9.037   8.274   41.916  1.00 14.40 ? 371 LEU A CD1 1 
ATOM   3146 C CD2 . LEU A 1 371 ? 8.566   7.024   39.778  1.00 14.19 ? 371 LEU A CD2 1 
ATOM   3147 N N   . TYR A 1 372 ? 12.688  5.572   41.414  1.00 16.85 ? 372 TYR A N   1 
ATOM   3148 C CA  . TYR A 1 372 ? 12.762  4.241   42.012  1.00 12.83 ? 372 TYR A CA  1 
ATOM   3149 C C   . TYR A 1 372 ? 13.764  4.203   43.161  1.00 18.67 ? 372 TYR A C   1 
ATOM   3150 O O   . TYR A 1 372 ? 13.489  3.616   44.216  1.00 11.33 ? 372 TYR A O   1 
ATOM   3151 C CB  . TYR A 1 372 ? 13.137  3.213   40.943  1.00 17.87 ? 372 TYR A CB  1 
ATOM   3152 C CG  . TYR A 1 372 ? 12.043  2.912   39.930  1.00 19.83 ? 372 TYR A CG  1 
ATOM   3153 C CD1 . TYR A 1 372 ? 10.706  3.262   40.175  1.00 10.14 ? 372 TYR A CD1 1 
ATOM   3154 C CD2 . TYR A 1 372 ? 12.346  2.265   38.730  1.00 17.23 ? 372 TYR A CD2 1 
ATOM   3155 C CE1 . TYR A 1 372 ? 9.698   2.982   39.232  1.00 10.56 ? 372 TYR A CE1 1 
ATOM   3156 C CE2 . TYR A 1 372 ? 11.358  1.983   37.796  1.00 14.98 ? 372 TYR A CE2 1 
ATOM   3157 C CZ  . TYR A 1 372 ? 10.038  2.336   38.057  1.00 18.62 ? 372 TYR A CZ  1 
ATOM   3158 O OH  . TYR A 1 372 ? 9.066   2.041   37.126  1.00 10.92 ? 372 TYR A OH  1 
ATOM   3159 N N   . SER A 1 373 ? 14.931  4.829   42.983  1.00 18.79 ? 373 SER A N   1 
ATOM   3160 C CA  . SER A 1 373 ? 15.919  4.814   44.054  1.00 20.59 ? 373 SER A CA  1 
ATOM   3161 C C   . SER A 1 373 ? 15.440  5.616   45.259  1.00 22.82 ? 373 SER A C   1 
ATOM   3162 O O   . SER A 1 373 ? 15.730  5.239   46.398  1.00 19.84 ? 373 SER A O   1 
ATOM   3163 C CB  . SER A 1 373 ? 17.265  5.334   43.549  1.00 25.52 ? 373 SER A CB  1 
ATOM   3164 O OG  . SER A 1 373 ? 17.197  6.703   43.222  1.00 28.89 ? 373 SER A OG  1 
ATOM   3165 N N   . THR A 1 374 ? 14.674  6.691   45.027  1.00 14.83 ? 374 THR A N   1 
ATOM   3166 C CA  . THR A 1 374 ? 14.125  7.479   46.126  1.00 16.66 ? 374 THR A CA  1 
ATOM   3167 C C   . THR A 1 374 ? 13.002  6.739   46.845  1.00 23.22 ? 374 THR A C   1 
ATOM   3168 O O   . THR A 1 374 ? 12.905  6.802   48.078  1.00 24.62 ? 374 THR A O   1 
ATOM   3169 C CB  . THR A 1 374 ? 13.632  8.830   45.602  1.00 17.69 ? 374 THR A CB  1 
ATOM   3170 O OG1 . THR A 1 374 ? 14.734  9.535   45.013  1.00 18.09 ? 374 THR A OG1 1 
ATOM   3171 C CG2 . THR A 1 374 ? 13.022  9.673   46.732  1.00 24.49 ? 374 THR A CG2 1 
ATOM   3172 N N   . LEU A 1 375 ? 12.135  6.044   46.100  1.00 20.84 ? 375 LEU A N   1 
ATOM   3173 C CA  . LEU A 1 375 ? 11.101  5.241   46.750  1.00 20.66 ? 375 LEU A CA  1 
ATOM   3174 C C   . LEU A 1 375 ? 11.722  4.160   47.616  1.00 20.27 ? 375 LEU A C   1 
ATOM   3175 O O   . LEU A 1 375 ? 11.204  3.845   48.696  1.00 25.00 ? 375 LEU A O   1 
ATOM   3176 C CB  . LEU A 1 375 ? 10.177  4.607   45.704  1.00 17.72 ? 375 LEU A CB  1 
ATOM   3177 C CG  . LEU A 1 375 ? 9.193   5.542   45.007  1.00 21.15 ? 375 LEU A CG  1 
ATOM   3178 C CD1 . LEU A 1 375 ? 8.524   4.861   43.790  1.00 16.92 ? 375 LEU A CD1 1 
ATOM   3179 C CD2 . LEU A 1 375 ? 8.148   6.046   45.997  1.00 20.98 ? 375 LEU A CD2 1 
ATOM   3180 N N   . GLU A 1 376 ? 12.841  3.597   47.157  1.00 23.31 ? 376 GLU A N   1 
ATOM   3181 C CA  . GLU A 1 376 ? 13.534  2.543   47.879  1.00 25.84 ? 376 GLU A CA  1 
ATOM   3182 C C   . GLU A 1 376 ? 13.971  3.001   49.261  1.00 28.12 ? 376 GLU A C   1 
ATOM   3183 O O   . GLU A 1 376 ? 14.001  2.202   50.205  1.00 27.01 ? 376 GLU A O   1 
ATOM   3184 C CB  . GLU A 1 376 ? 14.753  2.105   47.071  1.00 30.51 ? 376 GLU A CB  1 
ATOM   3185 C CG  . GLU A 1 376 ? 14.904  0.625   46.892  1.00 35.81 ? 376 GLU A CG  1 
ATOM   3186 C CD  . GLU A 1 376 ? 15.695  0.287   45.647  1.00 31.98 ? 376 GLU A CD  1 
ATOM   3187 O OE1 . GLU A 1 376 ? 15.233  -0.569  44.874  1.00 43.24 ? 376 GLU A OE1 1 
ATOM   3188 O OE2 . GLU A 1 376 ? 16.767  0.891   45.428  1.00 39.58 ? 376 GLU A OE2 1 
ATOM   3189 N N   . LYS A 1 377 ? 14.318  4.278   49.399  1.00 21.21 ? 377 LYS A N   1 
ATOM   3190 C CA  . LYS A 1 377 ? 14.859  4.770   50.651  1.00 20.49 ? 377 LYS A CA  1 
ATOM   3191 C C   . LYS A 1 377 ? 13.793  5.236   51.631  1.00 23.38 ? 377 LYS A C   1 
ATOM   3192 O O   . LYS A 1 377 ? 14.091  5.351   52.823  1.00 28.40 ? 377 LYS A O   1 
ATOM   3193 C CB  . LYS A 1 377 ? 15.852  5.907   50.378  1.00 25.22 ? 377 LYS A CB  1 
ATOM   3194 C CG  . LYS A 1 377 ? 16.946  5.519   49.395  1.00 24.24 ? 377 LYS A CG  1 
ATOM   3195 C CD  . LYS A 1 377 ? 18.027  6.598   49.308  1.00 35.94 ? 377 LYS A CD  1 
ATOM   3196 C CE  . LYS A 1 377 ? 18.933  6.384   48.105  1.00 48.08 ? 377 LYS A CE  1 
ATOM   3197 N NZ  . LYS A 1 377 ? 19.328  4.958   47.928  1.00 55.15 ? 377 LYS A NZ  1 
ATOM   3198 N N   . GLU A 1 378 ? 12.560  5.490   51.187  1.00 19.46 ? 378 GLU A N   1 
ATOM   3199 C CA  . GLU A 1 378 ? 11.540  5.947   52.128  1.00 21.00 ? 378 GLU A CA  1 
ATOM   3200 C C   . GLU A 1 378 ? 11.054  4.772   52.971  1.00 26.36 ? 378 GLU A C   1 
ATOM   3201 O O   . GLU A 1 378 ? 10.457  3.827   52.447  1.00 27.12 ? 378 GLU A O   1 
ATOM   3202 C CB  . GLU A 1 378 ? 10.370  6.605   51.400  1.00 23.15 ? 378 GLU A CB  1 
ATOM   3203 C CG  . GLU A 1 378 ? 10.744  7.701   50.443  1.00 22.70 ? 378 GLU A CG  1 
ATOM   3204 C CD  . GLU A 1 378 ? 11.387  8.916   51.107  1.00 32.83 ? 378 GLU A CD  1 
ATOM   3205 O OE1 . GLU A 1 378 ? 11.203  9.128   52.322  1.00 33.78 ? 378 GLU A OE1 1 
ATOM   3206 O OE2 . GLU A 1 378 ? 12.084  9.673   50.398  1.00 42.51 ? 378 GLU A OE2 1 
ATOM   3207 N N   . GLU A 1 379 ? 11.313  4.834   54.282  1.00 23.67 ? 379 GLU A N   1 
ATOM   3208 C CA  . GLU A 1 379 ? 10.875  3.770   55.179  1.00 17.03 ? 379 GLU A CA  1 
ATOM   3209 C C   . GLU A 1 379 ? 9.359   3.658   55.240  1.00 20.47 ? 379 GLU A C   1 
ATOM   3210 O O   . GLU A 1 379 ? 8.835   2.575   55.514  1.00 21.83 ? 379 GLU A O   1 
ATOM   3211 C CB  . GLU A 1 379 ? 11.419  4.003   56.590  1.00 20.21 ? 379 GLU A CB  1 
ATOM   3212 C CG  . GLU A 1 379 ? 12.883  3.660   56.777  1.00 25.85 ? 379 GLU A CG  1 
ATOM   3213 C CD  . GLU A 1 379 ? 13.337  3.890   58.214  1.00 34.10 ? 379 GLU A CD  1 
ATOM   3214 O OE1 . GLU A 1 379 ? 12.495  4.289   59.047  1.00 39.88 ? 379 GLU A OE1 1 
ATOM   3215 O OE2 . GLU A 1 379 ? 14.532  3.679   58.510  1.00 31.58 ? 379 GLU A OE2 1 
ATOM   3216 N N   . TRP A 1 380 ? 8.645   4.758   55.026  1.00 18.36 ? 380 TRP A N   1 
ATOM   3217 C CA  . TRP A 1 380 ? 7.204   4.789   55.229  1.00 15.95 ? 380 TRP A CA  1 
ATOM   3218 C C   . TRP A 1 380 ? 6.424   4.455   53.961  1.00 18.28 ? 380 TRP A C   1 
ATOM   3219 O O   . TRP A 1 380 ? 5.188   4.497   53.980  1.00 21.00 ? 380 TRP A O   1 
ATOM   3220 C CB  . TRP A 1 380 ? 6.786   6.175   55.763  1.00 14.57 ? 380 TRP A CB  1 
ATOM   3221 C CG  . TRP A 1 380 ? 7.316   7.298   54.922  1.00 18.85 ? 380 TRP A CG  1 
ATOM   3222 C CD1 . TRP A 1 380 ? 8.563   7.855   54.988  1.00 22.57 ? 380 TRP A CD1 1 
ATOM   3223 C CD2 . TRP A 1 380 ? 6.633   7.975   53.861  1.00 21.05 ? 380 TRP A CD2 1 
ATOM   3224 N NE1 . TRP A 1 380 ? 8.687   8.846   54.048  1.00 24.23 ? 380 TRP A NE1 1 
ATOM   3225 C CE2 . TRP A 1 380 ? 7.516   8.941   53.344  1.00 24.10 ? 380 TRP A CE2 1 
ATOM   3226 C CE3 . TRP A 1 380 ? 5.351   7.873   53.311  1.00 24.48 ? 380 TRP A CE3 1 
ATOM   3227 C CZ2 . TRP A 1 380 ? 7.167   9.786   52.291  1.00 28.25 ? 380 TRP A CZ2 1 
ATOM   3228 C CZ3 . TRP A 1 380 ? 5.003   8.718   52.273  1.00 22.57 ? 380 TRP A CZ3 1 
ATOM   3229 C CH2 . TRP A 1 380 ? 5.909   9.660   51.774  1.00 27.83 ? 380 TRP A CH2 1 
ATOM   3230 N N   . ILE A 1 381 ? 7.112   4.150   52.866  1.00 15.55 ? 381 ILE A N   1 
ATOM   3231 C CA  . ILE A 1 381 ? 6.494   3.685   51.626  1.00 19.12 ? 381 ILE A CA  1 
ATOM   3232 C C   . ILE A 1 381 ? 6.861   2.224   51.434  1.00 22.32 ? 381 ILE A C   1 
ATOM   3233 O O   . ILE A 1 381 ? 8.037   1.853   51.556  1.00 23.65 ? 381 ILE A O   1 
ATOM   3234 C CB  . ILE A 1 381 ? 6.956   4.499   50.407  1.00 16.12 ? 381 ILE A CB  1 
ATOM   3235 C CG1 . ILE A 1 381 ? 6.592   5.966   50.564  1.00 17.19 ? 381 ILE A CG1 1 
ATOM   3236 C CG2 . ILE A 1 381 ? 6.342   3.922   49.121  1.00 19.13 ? 381 ILE A CG2 1 
ATOM   3237 C CD1 . ILE A 1 381 ? 6.958   6.815   49.387  1.00 21.67 ? 381 ILE A CD1 1 
ATOM   3238 N N   . GLU A 1 382 ? 5.864   1.401   51.115  1.00 14.96 ? 382 GLU A N   1 
ATOM   3239 C CA  . GLU A 1 382 ? 6.091   0.019   50.713  1.00 10.51 ? 382 GLU A CA  1 
ATOM   3240 C C   . GLU A 1 382 ? 5.410   -0.221  49.374  1.00 10.44 ? 382 GLU A C   1 
ATOM   3241 O O   . GLU A 1 382 ? 4.184   -0.112  49.284  1.00 12.84 ? 382 GLU A O   1 
ATOM   3242 C CB  . GLU A 1 382 ? 5.544   -0.948  51.755  1.00 13.79 ? 382 GLU A CB  1 
ATOM   3243 C CG  . GLU A 1 382 ? 5.721   -2.399  51.389  1.00 23.44 ? 382 GLU A CG  1 
ATOM   3244 C CD  . GLU A 1 382 ? 5.412   -3.332  52.550  1.00 33.41 ? 382 GLU A CD  1 
ATOM   3245 O OE1 . GLU A 1 382 ? 5.282   -4.552  52.316  1.00 40.43 ? 382 GLU A OE1 1 
ATOM   3246 O OE2 . GLU A 1 382 ? 5.298   -2.837  53.697  1.00 35.31 ? 382 GLU A OE2 1 
ATOM   3247 N N   . THR A 1 383 ? 6.189   -0.562  48.341  1.00 14.19 ? 383 THR A N   1 
ATOM   3248 C CA  . THR A 1 383 ? 5.589   -0.947  47.069  1.00 12.95 ? 383 THR A CA  1 
ATOM   3249 C C   . THR A 1 383 ? 5.116   -2.396  47.135  1.00 14.44 ? 383 THR A C   1 
ATOM   3250 O O   . THR A 1 383 ? 5.726   -3.233  47.804  1.00 20.27 ? 383 THR A O   1 
ATOM   3251 C CB  . THR A 1 383 ? 6.568   -0.742  45.906  1.00 14.98 ? 383 THR A CB  1 
ATOM   3252 O OG1 . THR A 1 383 ? 7.791   -1.452  46.146  1.00 13.22 ? 383 THR A OG1 1 
ATOM   3253 C CG2 . THR A 1 383 ? 6.879   0.735   45.736  1.00 15.02 ? 383 THR A CG2 1 
ATOM   3254 N N   . LEU A 1 384 ? 4.015   -2.689  46.442  1.00 11.70 ? 384 LEU A N   1 
ATOM   3255 C CA  . LEU A 1 384 ? 3.360   -3.988  46.524  1.00 13.93 ? 384 LEU A CA  1 
ATOM   3256 C C   . LEU A 1 384 ? 3.136   -4.576  45.138  1.00 13.08 ? 384 LEU A C   1 
ATOM   3257 O O   . LEU A 1 384 ? 2.900   -3.855  44.168  1.00 14.35 ? 384 LEU A O   1 
ATOM   3258 C CB  . LEU A 1 384 ? 1.999   -3.883  47.225  1.00 14.23 ? 384 LEU A CB  1 
ATOM   3259 C CG  . LEU A 1 384 ? 1.926   -3.353  48.655  1.00 12.40 ? 384 LEU A CG  1 
ATOM   3260 C CD1 . LEU A 1 384 ? 0.491   -3.393  49.109  1.00 10.22 ? 384 LEU A CD1 1 
ATOM   3261 C CD2 . LEU A 1 384 ? 2.828   -4.191  49.587  1.00 10.28 ? 384 LEU A CD2 1 
ATOM   3262 N N   . THR A 1 385 ? 3.189   -5.901  45.048  1.00 14.74 ? 385 THR A N   1 
ATOM   3263 C CA  . THR A 1 385 ? 2.624   -6.535  43.867  1.00 17.86 ? 385 THR A CA  1 
ATOM   3264 C C   . THR A 1 385 ? 1.101   -6.490  43.937  1.00 9.90  ? 385 THR A C   1 
ATOM   3265 O O   . THR A 1 385 ? 0.509   -6.231  44.995  1.00 10.94 ? 385 THR A O   1 
ATOM   3266 C CB  . THR A 1 385 ? 3.052   -7.991  43.761  1.00 13.51 ? 385 THR A CB  1 
ATOM   3267 O OG1 . THR A 1 385 ? 2.462   -8.704  44.852  1.00 15.77 ? 385 THR A OG1 1 
ATOM   3268 C CG2 . THR A 1 385 ? 4.578   -8.130  43.820  1.00 18.62 ? 385 THR A CG2 1 
ATOM   3269 N N   . LEU A 1 386 ? 0.461   -6.779  42.795  1.00 9.82  ? 386 LEU A N   1 
ATOM   3270 C CA  . LEU A 1 386 ? -1.001  -6.853  42.775  1.00 13.02 ? 386 LEU A CA  1 
ATOM   3271 C C   . LEU A 1 386 ? -1.495  -7.941  43.713  1.00 17.01 ? 386 LEU A C   1 
ATOM   3272 O O   . LEU A 1 386 ? -2.529  -7.781  44.372  1.00 19.22 ? 386 LEU A O   1 
ATOM   3273 C CB  . LEU A 1 386 ? -1.522  -7.113  41.358  1.00 10.16 ? 386 LEU A CB  1 
ATOM   3274 C CG  . LEU A 1 386 ? -1.100  -6.140  40.253  1.00 13.65 ? 386 LEU A CG  1 
ATOM   3275 C CD1 . LEU A 1 386 ? -1.733  -6.530  38.902  1.00 11.91 ? 386 LEU A CD1 1 
ATOM   3276 C CD2 . LEU A 1 386 ? -1.464  -4.704  40.630  1.00 12.00 ? 386 LEU A CD2 1 
ATOM   3277 N N   . GLU A 1 387 ? -0.776  -9.067  43.780  1.00 15.04 ? 387 GLU A N   1 
ATOM   3278 C CA  . GLU A 1 387 ? -1.160  -10.110 44.724  1.00 15.90 ? 387 GLU A CA  1 
ATOM   3279 C C   . GLU A 1 387 ? -1.118  -9.591  46.162  1.00 16.13 ? 387 GLU A C   1 
ATOM   3280 O O   . GLU A 1 387 ? -2.042  -9.840  46.946  1.00 18.26 ? 387 GLU A O   1 
ATOM   3281 C CB  . GLU A 1 387 ? -0.265  -11.342 44.563  1.00 26.83 ? 387 GLU A CB  1 
ATOM   3282 C CG  . GLU A 1 387 ? -0.559  -12.412 45.614  1.00 34.64 ? 387 GLU A CG  1 
ATOM   3283 C CD  . GLU A 1 387 ? 0.381   -13.608 45.547  1.00 51.03 ? 387 GLU A CD  1 
ATOM   3284 O OE1 . GLU A 1 387 ? 0.269   -14.507 46.412  1.00 55.62 ? 387 GLU A OE1 1 
ATOM   3285 O OE2 . GLU A 1 387 ? 1.223   -13.657 44.628  1.00 56.54 ? 387 GLU A OE2 1 
ATOM   3286 N N   . GLU A 1 388 ? -0.079  -8.823  46.507  1.00 17.52 ? 388 GLU A N   1 
ATOM   3287 C CA  . GLU A 1 388 ? 0.035   -8.328  47.877  1.00 17.83 ? 388 GLU A CA  1 
ATOM   3288 C C   . GLU A 1 388 ? -1.029  -7.284  48.178  1.00 17.79 ? 388 GLU A C   1 
ATOM   3289 O O   . GLU A 1 388 ? -1.579  -7.252  49.288  1.00 18.93 ? 388 GLU A O   1 
ATOM   3290 C CB  . GLU A 1 388 ? 1.428   -7.753  48.124  1.00 15.10 ? 388 GLU A CB  1 
ATOM   3291 C CG  . GLU A 1 388 ? 2.536   -8.806  48.094  1.00 20.46 ? 388 GLU A CG  1 
ATOM   3292 C CD  . GLU A 1 388 ? 3.927   -8.196  48.051  1.00 23.41 ? 388 GLU A CD  1 
ATOM   3293 O OE1 . GLU A 1 388 ? 4.068   -7.046  47.576  1.00 18.27 ? 388 GLU A OE1 1 
ATOM   3294 O OE2 . GLU A 1 388 ? 4.885   -8.868  48.492  1.00 31.63 ? 388 GLU A OE2 1 
ATOM   3295 N N   . ALA A 1 389 ? -1.314  -6.404  47.215  1.00 15.22 ? 389 ALA A N   1 
ATOM   3296 C CA  . ALA A 1 389 ? -2.396  -5.443  47.392  1.00 12.32 ? 389 ALA A CA  1 
ATOM   3297 C C   . ALA A 1 389 ? -3.729  -6.151  47.569  1.00 16.79 ? 389 ALA A C   1 
ATOM   3298 O O   . ALA A 1 389 ? -4.535  -5.774  48.426  1.00 18.52 ? 389 ALA A O   1 
ATOM   3299 C CB  . ALA A 1 389 ? -2.459  -4.492  46.195  1.00 13.07 ? 389 ALA A CB  1 
ATOM   3300 N N   . MET A 1 390 ? -3.965  -7.199  46.785  1.00 14.11 ? 390 MET A N   1 
ATOM   3301 C CA  . MET A 1 390 ? -5.245  -7.892  46.862  1.00 23.15 ? 390 MET A CA  1 
ATOM   3302 C C   . MET A 1 390 ? -5.462  -8.532  48.224  1.00 22.42 ? 390 MET A C   1 
ATOM   3303 O O   . MET A 1 390 ? -6.597  -8.576  48.707  1.00 20.73 ? 390 MET A O   1 
ATOM   3304 C CB  . MET A 1 390 ? -5.327  -8.939  45.757  1.00 25.33 ? 390 MET A CB  1 
ATOM   3305 C CG  . MET A 1 390 ? -6.586  -9.772  45.750  1.00 28.92 ? 390 MET A CG  1 
ATOM   3306 S SD  . MET A 1 390 ? -6.524  -10.907 44.343  1.00 33.63 ? 390 MET A SD  1 
ATOM   3307 C CE  . MET A 1 390 ? -5.448  -12.200 44.978  1.00 33.68 ? 390 MET A CE  1 
ATOM   3308 N N   . ARG A 1 391 ? -4.397  -9.015  48.866  1.00 17.93 ? 391 ARG A N   1 
ATOM   3309 C CA  . ARG A 1 391 ? -4.538  -9.795  50.086  1.00 23.78 ? 391 ARG A CA  1 
ATOM   3310 C C   . ARG A 1 391 ? -4.115  -9.056  51.344  1.00 23.39 ? 391 ARG A C   1 
ATOM   3311 O O   . ARG A 1 391 ? -4.219  -9.627  52.433  1.00 22.25 ? 391 ARG A O   1 
ATOM   3312 C CB  . ARG A 1 391 ? -3.723  -11.087 49.987  1.00 32.40 ? 391 ARG A CB  1 
ATOM   3313 C CG  . ARG A 1 391 ? -2.225  -10.862 49.968  1.00 49.88 ? 391 ARG A CG  1 
ATOM   3314 C CD  . ARG A 1 391 ? -1.489  -11.998 50.639  1.00 61.54 ? 391 ARG A CD  1 
ATOM   3315 N NE  . ARG A 1 391 ? -0.172  -11.572 51.149  1.00 64.36 ? 391 ARG A NE  1 
ATOM   3316 C CZ  . ARG A 1 391 ? 0.073   -11.155 52.407  1.00 61.53 ? 391 ARG A CZ  1 
ATOM   3317 N NH1 . ARG A 1 391 ? -0.905  -11.122 53.338  1.00 58.10 ? 391 ARG A NH1 1 
ATOM   3318 N NH2 . ARG A 1 391 ? 1.309   -10.782 52.764  1.00 57.05 ? 391 ARG A NH2 1 
ATOM   3319 N N   . LYS A 1 392 ? -3.646  -7.815  51.238  1.00 16.51 ? 392 LYS A N   1 
ATOM   3320 C CA  . LYS A 1 392 ? -3.111  -7.148  52.417  1.00 21.27 ? 392 LYS A CA  1 
ATOM   3321 C C   . LYS A 1 392 ? -4.203  -6.973  53.469  1.00 14.29 ? 392 LYS A C   1 
ATOM   3322 O O   . LYS A 1 392 ? -5.312  -6.526  53.165  1.00 22.09 ? 392 LYS A O   1 
ATOM   3323 C CB  . LYS A 1 392 ? -2.508  -5.794  52.045  1.00 26.64 ? 392 LYS A CB  1 
ATOM   3324 C CG  . LYS A 1 392 ? -1.775  -5.130  53.191  1.00 32.18 ? 392 LYS A CG  1 
ATOM   3325 C CD  . LYS A 1 392 ? -0.428  -4.613  52.747  1.00 41.74 ? 392 LYS A CD  1 
ATOM   3326 C CE  . LYS A 1 392 ? 0.676   -5.608  53.053  1.00 39.95 ? 392 LYS A CE  1 
ATOM   3327 N NZ  . LYS A 1 392 ? 0.813   -5.819  54.517  1.00 38.12 ? 392 LYS A NZ  1 
ATOM   3328 N N   . GLU A 1 393 ? -3.882  -7.330  54.713  1.00 21.30 ? 393 GLU A N   1 
ATOM   3329 C CA  . GLU A 1 393 ? -4.883  -7.335  55.777  1.00 29.93 ? 393 GLU A CA  1 
ATOM   3330 C C   . GLU A 1 393 ? -5.039  -5.991  56.481  1.00 25.59 ? 393 GLU A C   1 
ATOM   3331 O O   . GLU A 1 393 ? -6.155  -5.638  56.876  1.00 33.72 ? 393 GLU A O   1 
ATOM   3332 C CB  . GLU A 1 393 ? -4.546  -8.413  56.814  1.00 29.80 ? 393 GLU A CB  1 
ATOM   3333 C CG  . GLU A 1 393 ? -5.383  -9.676  56.670  1.00 46.48 ? 393 GLU A CG  1 
ATOM   3334 C CD  . GLU A 1 393 ? -4.710  -10.902 57.265  1.00 60.50 ? 393 GLU A CD  1 
ATOM   3335 O OE1 . GLU A 1 393 ? -4.757  -11.974 56.623  1.00 63.43 ? 393 GLU A OE1 1 
ATOM   3336 O OE2 . GLU A 1 393 ? -4.141  -10.795 58.374  1.00 64.40 ? 393 GLU A OE2 1 
ATOM   3337 N N   . ASP A 1 394 ? -3.963  -5.236  56.664  1.00 20.10 ? 394 ASP A N   1 
ATOM   3338 C CA  . ASP A 1 394 ? -4.035  -3.987  57.423  1.00 21.33 ? 394 ASP A CA  1 
ATOM   3339 C C   . ASP A 1 394 ? -4.331  -2.786  56.525  1.00 23.22 ? 394 ASP A C   1 
ATOM   3340 O O   . ASP A 1 394 ? -3.608  -1.792  56.538  1.00 25.73 ? 394 ASP A O   1 
ATOM   3341 C CB  . ASP A 1 394 ? -2.739  -3.784  58.197  1.00 27.25 ? 394 ASP A CB  1 
ATOM   3342 C CG  . ASP A 1 394 ? -1.511  -4.030  57.338  1.00 44.41 ? 394 ASP A CG  1 
ATOM   3343 O OD1 . ASP A 1 394 ? -1.668  -4.622  56.255  1.00 43.99 ? 394 ASP A OD1 1 
ATOM   3344 O OD2 . ASP A 1 394 ? -0.393  -3.644  57.743  1.00 47.04 ? 394 ASP A OD2 1 
ATOM   3345 N N   . VAL A 1 395 ? -5.402  -2.869  55.730  1.00 14.37 ? 395 VAL A N   1 
ATOM   3346 C CA  . VAL A 1 395 ? -5.856  -1.755  54.911  1.00 15.81 ? 395 VAL A CA  1 
ATOM   3347 C C   . VAL A 1 395 ? -7.330  -1.514  55.231  1.00 19.67 ? 395 VAL A C   1 
ATOM   3348 O O   . VAL A 1 395 ? -7.995  -2.332  55.861  1.00 21.49 ? 395 VAL A O   1 
ATOM   3349 C CB  . VAL A 1 395 ? -5.656  -1.996  53.398  1.00 18.37 ? 395 VAL A CB  1 
ATOM   3350 C CG1 . VAL A 1 395 ? -4.173  -2.173  53.078  1.00 25.90 ? 395 VAL A CG1 1 
ATOM   3351 C CG2 . VAL A 1 395 ? -6.451  -3.209  52.940  1.00 21.42 ? 395 VAL A CG2 1 
ATOM   3352 N N   . LYS A 1 396 ? -7.830  -0.364  54.804  1.00 20.15 ? 396 LYS A N   1 
ATOM   3353 C CA  . LYS A 1 396 ? -9.231  -0.034  54.995  1.00 15.04 ? 396 LYS A CA  1 
ATOM   3354 C C   . LYS A 1 396 ? -10.024 -0.500  53.778  1.00 18.52 ? 396 LYS A C   1 
ATOM   3355 O O   . LYS A 1 396 ? -9.539  -0.422  52.646  1.00 14.76 ? 396 LYS A O   1 
ATOM   3356 C CB  . LYS A 1 396 ? -9.393  1.471   55.218  1.00 13.81 ? 396 LYS A CB  1 
ATOM   3357 C CG  . LYS A 1 396 ? -10.794 1.886   55.577  1.00 12.56 ? 396 LYS A CG  1 
ATOM   3358 C CD  . LYS A 1 396 ? -10.834 3.363   55.971  1.00 22.87 ? 396 LYS A CD  1 
ATOM   3359 C CE  . LYS A 1 396 ? -12.262 3.865   56.088  1.00 28.79 ? 396 LYS A CE  1 
ATOM   3360 N NZ  . LYS A 1 396 ? -12.284 5.231   56.675  1.00 20.49 ? 396 LYS A NZ  1 
ATOM   3361 N N   . THR A 1 397 ? -11.234 -1.014  54.019  1.00 16.06 ? 397 THR A N   1 
ATOM   3362 C CA  . THR A 1 397 ? -12.060 -1.583  52.964  1.00 13.87 ? 397 THR A CA  1 
ATOM   3363 C C   . THR A 1 397 ? -13.471 -1.022  53.037  1.00 13.82 ? 397 THR A C   1 
ATOM   3364 O O   . THR A 1 397 ? -13.904 -0.489  54.063  1.00 19.03 ? 397 THR A O   1 
ATOM   3365 C CB  . THR A 1 397 ? -12.128 -3.120  53.037  1.00 16.65 ? 397 THR A CB  1 
ATOM   3366 O OG1 . THR A 1 397 ? -12.845 -3.520  54.220  1.00 16.38 ? 397 THR A OG1 1 
ATOM   3367 C CG2 . THR A 1 397 ? -10.723 -3.723  53.068  1.00 15.54 ? 397 THR A CG2 1 
ATOM   3368 N N   . GLU A 1 398 ? -14.196 -1.165  51.928  1.00 16.51 ? 398 GLU A N   1 
ATOM   3369 C CA  . GLU A 1 398 ? -15.572 -0.704  51.838  1.00 19.22 ? 398 GLU A CA  1 
ATOM   3370 C C   . GLU A 1 398 ? -16.292 -1.540  50.790  1.00 22.83 ? 398 GLU A C   1 
ATOM   3371 O O   . GLU A 1 398 ? -15.694 -1.917  49.780  1.00 16.27 ? 398 GLU A O   1 
ATOM   3372 C CB  . GLU A 1 398 ? -15.632 0.786   51.474  1.00 24.69 ? 398 GLU A CB  1 
ATOM   3373 C CG  . GLU A 1 398 ? -17.030 1.302   51.138  1.00 25.07 ? 398 GLU A CG  1 
ATOM   3374 C CD  . GLU A 1 398 ? -17.066 2.812   50.940  1.00 33.28 ? 398 GLU A CD  1 
ATOM   3375 O OE1 . GLU A 1 398 ? -16.042 3.454   51.231  1.00 31.11 ? 398 GLU A OE1 1 
ATOM   3376 O OE2 . GLU A 1 398 ? -18.111 3.357   50.502  1.00 33.84 ? 398 GLU A OE2 1 
ATOM   3377 N N   . VAL A 1 399 ? -17.577 -1.829  51.026  1.00 18.84 ? 399 VAL A N   1 
ATOM   3378 C CA  . VAL A 1 399 ? -18.384 -2.536  50.035  1.00 18.49 ? 399 VAL A CA  1 
ATOM   3379 C C   . VAL A 1 399 ? -19.052 -1.513  49.138  1.00 18.11 ? 399 VAL A C   1 
ATOM   3380 O O   . VAL A 1 399 ? -19.530 -0.480  49.613  1.00 18.67 ? 399 VAL A O   1 
ATOM   3381 C CB  . VAL A 1 399 ? -19.433 -3.440  50.712  1.00 23.34 ? 399 VAL A CB  1 
ATOM   3382 C CG1 . VAL A 1 399 ? -20.335 -4.079  49.667  1.00 24.85 ? 399 VAL A CG1 1 
ATOM   3383 C CG2 . VAL A 1 399 ? -18.762 -4.499  51.562  1.00 28.64 ? 399 VAL A CG2 1 
ATOM   3384 N N   . ILE A 1 400 ? -19.102 -1.795  47.837  1.00 14.06 ? 400 ILE A N   1 
ATOM   3385 C CA  . ILE A 1 400 ? -19.785 -0.935  46.879  1.00 21.30 ? 400 ILE A CA  1 
ATOM   3386 C C   . ILE A 1 400 ? -20.810 -1.772  46.122  1.00 19.59 ? 400 ILE A C   1 
ATOM   3387 O O   . ILE A 1 400 ? -20.536 -2.920  45.758  1.00 20.25 ? 400 ILE A O   1 
ATOM   3388 C CB  . ILE A 1 400 ? -18.765 -0.262  45.933  1.00 22.78 ? 400 ILE A CB  1 
ATOM   3389 C CG1 . ILE A 1 400 ? -19.448 0.550   44.838  1.00 34.04 ? 400 ILE A CG1 1 
ATOM   3390 C CG2 . ILE A 1 400 ? -17.838 -1.286  45.322  1.00 27.55 ? 400 ILE A CG2 1 
ATOM   3391 C CD1 . ILE A 1 400 ? -18.445 1.187   43.891  1.00 36.51 ? 400 ILE A CD1 1 
ATOM   3392 N N   . GLU A 1 401 ? -22.001 -1.205  45.906  1.00 16.78 ? 401 GLU A N   1 
ATOM   3393 C CA  . GLU A 1 401 ? -23.117 -1.948  45.323  1.00 22.53 ? 401 GLU A CA  1 
ATOM   3394 C C   . GLU A 1 401 ? -23.347 -1.686  43.839  1.00 22.25 ? 401 GLU A C   1 
ATOM   3395 O O   . GLU A 1 401 ? -23.971 -2.524  43.176  1.00 22.18 ? 401 GLU A O   1 
ATOM   3396 C CB  . GLU A 1 401 ? -24.416 -1.636  46.082  1.00 23.07 ? 401 GLU A CB  1 
ATOM   3397 C CG  . GLU A 1 401 ? -24.467 -2.268  47.457  1.00 27.30 ? 401 GLU A CG  1 
ATOM   3398 C CD  . GLU A 1 401 ? -24.245 -3.764  47.395  1.00 41.43 ? 401 GLU A CD  1 
ATOM   3399 O OE1 . GLU A 1 401 ? -24.797 -4.407  46.474  1.00 47.25 ? 401 GLU A OE1 1 
ATOM   3400 O OE2 . GLU A 1 401 ? -23.514 -4.298  48.255  1.00 47.87 ? 401 GLU A OE2 1 
ATOM   3401 N N   . SER A 1 402 ? -22.888 -0.559  43.302  1.00 21.32 ? 402 SER A N   1 
ATOM   3402 C CA  . SER A 1 402 ? -23.106 -0.272  41.892  1.00 27.16 ? 402 SER A CA  1 
ATOM   3403 C C   . SER A 1 402 ? -22.138 0.813   41.447  1.00 26.97 ? 402 SER A C   1 
ATOM   3404 O O   . SER A 1 402 ? -21.653 1.612   42.253  1.00 24.67 ? 402 SER A O   1 
ATOM   3405 C CB  . SER A 1 402 ? -24.555 0.148   41.613  1.00 30.28 ? 402 SER A CB  1 
ATOM   3406 O OG  . SER A 1 402 ? -24.676 1.552   41.520  1.00 42.72 ? 402 SER A OG  1 
ATOM   3407 N N   . VAL A 1 403 ? -21.861 0.832   40.147  1.00 20.06 ? 403 VAL A N   1 
ATOM   3408 C CA  . VAL A 1 403 ? -21.029 1.878   39.574  1.00 23.08 ? 403 VAL A CA  1 
ATOM   3409 C C   . VAL A 1 403 ? -21.777 2.504   38.409  1.00 14.44 ? 403 VAL A C   1 
ATOM   3410 O O   . VAL A 1 403 ? -22.629 1.869   37.782  1.00 17.71 ? 403 VAL A O   1 
ATOM   3411 C CB  . VAL A 1 403 ? -19.639 1.353   39.119  1.00 20.39 ? 403 VAL A CB  1 
ATOM   3412 C CG1 . VAL A 1 403 ? -18.860 0.775   40.304  1.00 19.90 ? 403 VAL A CG1 1 
ATOM   3413 C CG2 . VAL A 1 403 ? -19.783 0.310   38.008  1.00 21.10 ? 403 VAL A CG2 1 
ATOM   3414 N N   . LYS A 1 404 ? -21.473 3.771   38.144  1.00 19.35 ? 404 LYS A N   1 
ATOM   3415 C CA  . LYS A 1 404 ? -21.859 4.409   36.895  1.00 20.30 ? 404 LYS A CA  1 
ATOM   3416 C C   . LYS A 1 404 ? -20.887 3.975   35.806  1.00 15.80 ? 404 LYS A C   1 
ATOM   3417 O O   . LYS A 1 404 ? -19.674 4.136   35.959  1.00 18.36 ? 404 LYS A O   1 
ATOM   3418 C CB  . LYS A 1 404 ? -21.824 5.930   37.034  1.00 28.32 ? 404 LYS A CB  1 
ATOM   3419 C CG  . LYS A 1 404 ? -22.858 6.508   37.960  1.00 39.47 ? 404 LYS A CG  1 
ATOM   3420 C CD  . LYS A 1 404 ? -23.606 7.640   37.279  1.00 42.54 ? 404 LYS A CD  1 
ATOM   3421 C CE  . LYS A 1 404 ? -24.898 7.927   38.002  1.00 47.21 ? 404 LYS A CE  1 
ATOM   3422 N NZ  . LYS A 1 404 ? -25.716 6.693   38.148  1.00 47.10 ? 404 LYS A NZ  1 
ATOM   3423 N N   . ALA A 1 405 ? -21.408 3.418   34.718  1.00 18.64 ? 405 ALA A N   1 
ATOM   3424 C CA  . ALA A 1 405 ? -20.527 2.935   33.661  1.00 14.27 ? 405 ALA A CA  1 
ATOM   3425 C C   . ALA A 1 405 ? -19.690 4.080   33.109  1.00 11.96 ? 405 ALA A C   1 
ATOM   3426 O O   . ALA A 1 405 ? -20.186 5.192   32.937  1.00 17.63 ? 405 ALA A O   1 
ATOM   3427 C CB  . ALA A 1 405 ? -21.344 2.300   32.536  1.00 12.41 ? 405 ALA A CB  1 
ATOM   3428 N N   . GLY A 1 406 ? -18.417 3.810   32.834  1.00 16.18 ? 406 GLY A N   1 
ATOM   3429 C CA  . GLY A 1 406 ? -17.565 4.846   32.275  1.00 14.56 ? 406 GLY A CA  1 
ATOM   3430 C C   . GLY A 1 406 ? -16.191 4.314   31.921  1.00 16.76 ? 406 GLY A C   1 
ATOM   3431 O O   . GLY A 1 406 ? -15.954 3.106   31.911  1.00 17.27 ? 406 GLY A O   1 
ATOM   3432 N N   . THR A 1 407 ? -15.291 5.247   31.606  1.00 12.20 ? 407 THR A N   1 
ATOM   3433 C CA  . THR A 1 407 ? -13.877 4.985   31.325  1.00 15.64 ? 407 THR A CA  1 
ATOM   3434 C C   . THR A 1 407 ? -13.040 6.024   32.051  1.00 16.23 ? 407 THR A C   1 
ATOM   3435 O O   . THR A 1 407 ? -13.575 6.960   32.650  1.00 20.92 ? 407 THR A O   1 
ATOM   3436 C CB  . THR A 1 407 ? -13.545 5.068   29.830  1.00 11.59 ? 407 THR A CB  1 
ATOM   3437 O OG1 . THR A 1 407 ? -13.453 6.449   29.456  1.00 16.36 ? 407 THR A OG1 1 
ATOM   3438 C CG2 . THR A 1 407 ? -14.587 4.344   28.959  1.00 12.42 ? 407 THR A CG2 1 
ATOM   3439 N N   . TRP A 1 408 ? -11.711 5.914   31.946  1.00 14.74 ? 408 TRP A N   1 
ATOM   3440 C CA  . TRP A 1 408 ? -10.891 6.941   32.587  1.00 16.87 ? 408 TRP A CA  1 
ATOM   3441 C C   . TRP A 1 408 ? -10.776 8.229   31.774  1.00 22.48 ? 408 TRP A C   1 
ATOM   3442 O O   . TRP A 1 408 ? -10.035 9.133   32.179  1.00 21.35 ? 408 TRP A O   1 
ATOM   3443 C CB  . TRP A 1 408 ? -9.489  6.407   32.920  1.00 19.16 ? 408 TRP A CB  1 
ATOM   3444 C CG  . TRP A 1 408 ? -8.682  5.855   31.775  1.00 19.63 ? 408 TRP A CG  1 
ATOM   3445 C CD1 . TRP A 1 408 ? -8.996  5.880   30.448  1.00 22.23 ? 408 TRP A CD1 1 
ATOM   3446 C CD2 . TRP A 1 408 ? -7.412  5.194   31.875  1.00 14.95 ? 408 TRP A CD2 1 
ATOM   3447 N NE1 . TRP A 1 408 ? -8.002  5.270   29.716  1.00 22.05 ? 408 TRP A NE1 1 
ATOM   3448 C CE2 . TRP A 1 408 ? -7.021  4.838   30.571  1.00 18.33 ? 408 TRP A CE2 1 
ATOM   3449 C CE3 . TRP A 1 408 ? -6.572  4.863   32.945  1.00 20.16 ? 408 TRP A CE3 1 
ATOM   3450 C CZ2 . TRP A 1 408 ? -5.823  4.172   30.305  1.00 22.79 ? 408 TRP A CZ2 1 
ATOM   3451 C CZ3 . TRP A 1 408 ? -5.388  4.200   32.684  1.00 21.42 ? 408 TRP A CZ3 1 
ATOM   3452 C CH2 . TRP A 1 408 ? -5.019  3.865   31.372  1.00 20.19 ? 408 TRP A CH2 1 
ATOM   3453 N N   . PHE A 1 409 ? -11.477 8.357   30.653  1.00 17.08 ? 409 PHE A N   1 
ATOM   3454 C CA  . PHE A 1 409 ? -11.586 9.647   29.971  1.00 18.63 ? 409 PHE A CA  1 
ATOM   3455 C C   . PHE A 1 409 ? -12.918 10.261  30.400  1.00 20.59 ? 409 PHE A C   1 
ATOM   3456 O O   . PHE A 1 409 ? -13.981 9.852   29.930  1.00 19.14 ? 409 PHE A O   1 
ATOM   3457 C CB  . PHE A 1 409 ? -11.460 9.485   28.459  1.00 24.73 ? 409 PHE A CB  1 
ATOM   3458 C CG  . PHE A 1 409 ? -10.032 9.368   27.995  1.00 33.18 ? 409 PHE A CG  1 
ATOM   3459 C CD1 . PHE A 1 409 ? -9.226  10.491  27.901  1.00 32.00 ? 409 PHE A CD1 1 
ATOM   3460 C CD2 . PHE A 1 409 ? -9.483  8.130   27.691  1.00 35.26 ? 409 PHE A CD2 1 
ATOM   3461 C CE1 . PHE A 1 409 ? -7.903  10.385  27.501  1.00 34.84 ? 409 PHE A CE1 1 
ATOM   3462 C CE2 . PHE A 1 409 ? -8.162  8.021   27.292  1.00 38.26 ? 409 PHE A CE2 1 
ATOM   3463 C CZ  . PHE A 1 409 ? -7.373  9.149   27.198  1.00 39.17 ? 409 PHE A CZ  1 
ATOM   3464 N N   . ASP A 1 410 ? -12.850 11.196  31.354  1.00 23.25 ? 410 ASP A N   1 
ATOM   3465 C CA  . ASP A 1 410 ? -14.003 11.952  31.865  1.00 20.31 ? 410 ASP A CA  1 
ATOM   3466 C C   . ASP A 1 410 ? -15.119 11.055  32.388  1.00 27.14 ? 410 ASP A C   1 
ATOM   3467 O O   . ASP A 1 410 ? -16.267 11.498  32.504  1.00 31.86 ? 410 ASP A O   1 
ATOM   3468 C CB  . ASP A 1 410 ? -14.550 12.910  30.800  1.00 28.03 ? 410 ASP A CB  1 
ATOM   3469 C CG  . ASP A 1 410 ? -13.463 13.776  30.191  1.00 43.39 ? 410 ASP A CG  1 
ATOM   3470 O OD1 . ASP A 1 410 ? -12.656 14.341  30.959  1.00 44.39 ? 410 ASP A OD1 1 
ATOM   3471 O OD2 . ASP A 1 410 ? -13.414 13.893  28.949  1.00 49.30 ? 410 ASP A OD2 1 
ATOM   3472 N N   . GLY A 1 411 ? -14.812 9.799   32.714  1.00 21.69 ? 411 GLY A N   1 
ATOM   3473 C CA  . GLY A 1 411 ? -15.831 8.890   33.202  1.00 18.23 ? 411 GLY A CA  1 
ATOM   3474 C C   . GLY A 1 411 ? -16.938 8.569   32.222  1.00 19.95 ? 411 GLY A C   1 
ATOM   3475 O O   . GLY A 1 411 ? -18.019 8.155   32.643  1.00 24.97 ? 411 GLY A O   1 
ATOM   3476 N N   . ASN A 1 412 ? -16.713 8.732   30.923  1.00 18.53 ? 412 ASN A N   1 
ATOM   3477 C CA  . ASN A 1 412 ? -17.766 8.443   29.963  1.00 18.17 ? 412 ASN A CA  1 
ATOM   3478 C C   . ASN A 1 412 ? -17.146 7.837   28.716  1.00 12.77 ? 412 ASN A C   1 
ATOM   3479 O O   . ASN A 1 412 ? -15.933 7.612   28.647  1.00 18.33 ? 412 ASN A O   1 
ATOM   3480 C CB  . ASN A 1 412 ? -18.611 9.692   29.654  1.00 24.35 ? 412 ASN A CB  1 
ATOM   3481 C CG  . ASN A 1 412 ? -17.813 10.814  29.020  1.00 30.53 ? 412 ASN A CG  1 
ATOM   3482 O OD1 . ASN A 1 412 ? -17.067 10.604  28.067  1.00 22.58 ? 412 ASN A OD1 1 
ATOM   3483 N ND2 . ASN A 1 412 ? -17.998 12.026  29.530  1.00 29.37 ? 412 ASN A ND2 1 
ATOM   3484 N N   . PHE A 1 413 ? -17.993 7.574   27.720  1.00 12.75 ? 413 PHE A N   1 
ATOM   3485 C CA  . PHE A 1 413 ? -17.584 6.842   26.527  1.00 15.29 ? 413 PHE A CA  1 
ATOM   3486 C C   . PHE A 1 413 ? -17.431 7.724   25.291  1.00 18.04 ? 413 PHE A C   1 
ATOM   3487 O O   . PHE A 1 413 ? -17.324 7.191   24.181  1.00 15.82 ? 413 PHE A O   1 
ATOM   3488 C CB  . PHE A 1 413 ? -18.583 5.711   26.245  1.00 17.78 ? 413 PHE A CB  1 
ATOM   3489 C CG  . PHE A 1 413 ? -18.601 4.658   27.310  1.00 16.28 ? 413 PHE A CG  1 
ATOM   3490 C CD1 . PHE A 1 413 ? -17.706 3.608   27.268  1.00 15.72 ? 413 PHE A CD1 1 
ATOM   3491 C CD2 . PHE A 1 413 ? -19.496 4.736   28.371  1.00 16.41 ? 413 PHE A CD2 1 
ATOM   3492 C CE1 . PHE A 1 413 ? -17.696 2.650   28.256  1.00 16.22 ? 413 PHE A CE1 1 
ATOM   3493 C CE2 . PHE A 1 413 ? -19.500 3.771   29.361  1.00 17.43 ? 413 PHE A CE2 1 
ATOM   3494 C CZ  . PHE A 1 413 ? -18.592 2.734   29.311  1.00 17.96 ? 413 PHE A CZ  1 
ATOM   3495 N N   . LEU A 1 414 ? -17.383 9.051   25.450  1.00 21.07 ? 414 LEU A N   1 
ATOM   3496 C CA  . LEU A 1 414 ? -17.457 9.938   24.288  1.00 22.93 ? 414 LEU A CA  1 
ATOM   3497 C C   . LEU A 1 414 ? -16.219 9.881   23.393  1.00 21.58 ? 414 LEU A C   1 
ATOM   3498 O O   . LEU A 1 414 ? -16.291 10.329  22.243  1.00 20.49 ? 414 LEU A O   1 
ATOM   3499 C CB  . LEU A 1 414 ? -17.699 11.381  24.731  1.00 21.48 ? 414 LEU A CB  1 
ATOM   3500 C CG  . LEU A 1 414 ? -19.076 11.608  25.364  1.00 24.24 ? 414 LEU A CG  1 
ATOM   3501 C CD1 . LEU A 1 414 ? -19.333 13.090  25.651  1.00 21.48 ? 414 LEU A CD1 1 
ATOM   3502 C CD2 . LEU A 1 414 ? -20.170 11.012  24.477  1.00 19.55 ? 414 LEU A CD2 1 
ATOM   3503 N N   . LYS A 1 415 ? -15.093 9.346   23.874  1.00 15.57 ? 415 LYS A N   1 
ATOM   3504 C CA  . LYS A 1 415 ? -13.931 9.192   22.999  1.00 18.86 ? 415 LYS A CA  1 
ATOM   3505 C C   . LYS A 1 415 ? -14.094 8.076   21.968  1.00 18.14 ? 415 LYS A C   1 
ATOM   3506 O O   . LYS A 1 415 ? -13.300 8.018   21.024  1.00 18.34 ? 415 LYS A O   1 
ATOM   3507 C CB  . LYS A 1 415 ? -12.665 8.935   23.827  1.00 24.18 ? 415 LYS A CB  1 
ATOM   3508 C CG  . LYS A 1 415 ? -12.201 10.138  24.640  1.00 31.74 ? 415 LYS A CG  1 
ATOM   3509 C CD  . LYS A 1 415 ? -12.192 11.418  23.812  1.00 39.47 ? 415 LYS A CD  1 
ATOM   3510 C CE  . LYS A 1 415 ? -10.992 11.489  22.871  1.00 44.08 ? 415 LYS A CE  1 
ATOM   3511 N NZ  . LYS A 1 415 ? -10.857 12.846  22.259  1.00 49.06 ? 415 LYS A NZ  1 
ATOM   3512 N N   . TRP A 1 416 ? -15.095 7.202   22.116  1.00 14.69 ? 416 TRP A N   1 
ATOM   3513 C CA  . TRP A 1 416 ? -15.275 6.059   21.225  1.00 16.37 ? 416 TRP A CA  1 
ATOM   3514 C C   . TRP A 1 416 ? -16.662 5.961   20.602  1.00 14.53 ? 416 TRP A C   1 
ATOM   3515 O O   . TRP A 1 416 ? -16.867 5.106   19.734  1.00 16.62 ? 416 TRP A O   1 
ATOM   3516 C CB  . TRP A 1 416 ? -14.973 4.744   21.976  1.00 12.35 ? 416 TRP A CB  1 
ATOM   3517 C CG  . TRP A 1 416 ? -13.619 4.755   22.667  1.00 17.95 ? 416 TRP A CG  1 
ATOM   3518 C CD1 . TRP A 1 416 ? -12.435 4.307   22.152  1.00 18.16 ? 416 TRP A CD1 1 
ATOM   3519 C CD2 . TRP A 1 416 ? -13.318 5.260   23.981  1.00 17.23 ? 416 TRP A CD2 1 
ATOM   3520 N NE1 . TRP A 1 416 ? -11.419 4.489   23.060  1.00 18.74 ? 416 TRP A NE1 1 
ATOM   3521 C CE2 . TRP A 1 416 ? -11.934 5.061   24.197  1.00 17.04 ? 416 TRP A CE2 1 
ATOM   3522 C CE3 . TRP A 1 416 ? -14.088 5.847   25.001  1.00 12.61 ? 416 TRP A CE3 1 
ATOM   3523 C CZ2 . TRP A 1 416 ? -11.292 5.450   25.376  1.00 14.72 ? 416 TRP A CZ2 1 
ATOM   3524 C CZ3 . TRP A 1 416 ? -13.449 6.222   26.190  1.00 13.05 ? 416 TRP A CZ3 1 
ATOM   3525 C CH2 . TRP A 1 416 ? -12.065 6.021   26.361  1.00 17.82 ? 416 TRP A CH2 1 
ATOM   3526 N N   . ILE A 1 417 ? -17.619 6.792   21.008  1.00 14.38 ? 417 ILE A N   1 
ATOM   3527 C CA  . ILE A 1 417 ? -18.980 6.701   20.486  1.00 16.56 ? 417 ILE A CA  1 
ATOM   3528 C C   . ILE A 1 417 ? -19.635 8.056   20.706  1.00 19.34 ? 417 ILE A C   1 
ATOM   3529 O O   . ILE A 1 417 ? -19.179 8.855   21.526  1.00 17.34 ? 417 ILE A O   1 
ATOM   3530 C CB  . ILE A 1 417 ? -19.758 5.553   21.183  1.00 20.16 ? 417 ILE A CB  1 
ATOM   3531 C CG1 . ILE A 1 417 ? -21.011 5.146   20.389  1.00 15.49 ? 417 ILE A CG1 1 
ATOM   3532 C CG2 . ILE A 1 417 ? -20.088 5.928   22.624  1.00 17.61 ? 417 ILE A CG2 1 
ATOM   3533 C CD1 . ILE A 1 417 ? -21.482 3.737   20.707  1.00 20.98 ? 417 ILE A CD1 1 
ATOM   3534 N N   . GLY A 1 418 ? -20.686 8.339   19.945  1.00 25.83 ? 418 GLY A N   1 
ATOM   3535 C CA  . GLY A 1 418 ? -21.512 9.501   20.190  1.00 27.75 ? 418 GLY A CA  1 
ATOM   3536 C C   . GLY A 1 418 ? -21.483 10.573  19.116  1.00 38.11 ? 418 GLY A C   1 
ATOM   3537 O O   . GLY A 1 418 ? -22.380 11.423  19.099  1.00 45.58 ? 418 GLY A O   1 
ATOM   3538 N N   . ASN A 1 419 ? -20.485 10.589  18.238  1.00 38.18 ? 419 ASN A N   1 
ATOM   3539 C CA  . ASN A 1 419 ? -20.505 11.529  17.123  1.00 34.54 ? 419 ASN A CA  1 
ATOM   3540 C C   . ASN A 1 419 ? -20.642 10.756  15.816  1.00 34.74 ? 419 ASN A C   1 
ATOM   3541 O O   . ASN A 1 419 ? -20.652 9.522   15.798  1.00 32.22 ? 419 ASN A O   1 
ATOM   3542 C CB  . ASN A 1 419 ? -19.275 12.455  17.146  1.00 26.81 ? 419 ASN A CB  1 
ATOM   3543 C CG  . ASN A 1 419 ? -17.964 11.761  16.767  1.00 31.43 ? 419 ASN A CG  1 
ATOM   3544 O OD1 . ASN A 1 419 ? -17.937 10.716  16.121  1.00 30.82 ? 419 ASN A OD1 1 
ATOM   3545 N ND2 . ASN A 1 419 ? -16.859 12.377  17.158  1.00 32.09 ? 419 ASN A ND2 1 
ATOM   3546 N N   . LYS A 1 420 ? -20.727 11.496  14.709  1.00 28.75 ? 420 LYS A N   1 
ATOM   3547 C CA  . LYS A 1 420 ? -21.152 10.882  13.458  1.00 23.27 ? 420 LYS A CA  1 
ATOM   3548 C C   . LYS A 1 420 ? -20.118 9.883   12.954  1.00 21.62 ? 420 LYS A C   1 
ATOM   3549 O O   . LYS A 1 420 ? -20.461 8.761   12.561  1.00 25.20 ? 420 LYS A O   1 
ATOM   3550 C CB  . LYS A 1 420 ? -21.418 11.967  12.405  1.00 24.74 ? 420 LYS A CB  1 
ATOM   3551 C CG  . LYS A 1 420 ? -21.724 11.406  11.031  1.00 28.64 ? 420 LYS A CG  1 
ATOM   3552 C CD  . LYS A 1 420 ? -23.160 11.654  10.623  1.00 45.04 ? 420 LYS A CD  1 
ATOM   3553 C CE  . LYS A 1 420 ? -23.253 12.000  9.144   1.00 49.33 ? 420 LYS A CE  1 
ATOM   3554 N NZ  . LYS A 1 420 ? -24.668 12.067  8.684   1.00 55.12 ? 420 LYS A NZ  1 
ATOM   3555 N N   . GLU A 1 421 ? -18.842 10.276  12.953  1.00 26.11 ? 421 GLU A N   1 
ATOM   3556 C CA  . GLU A 1 421 ? -17.789 9.403   12.439  1.00 31.62 ? 421 GLU A CA  1 
ATOM   3557 C C   . GLU A 1 421 ? -17.603 8.175   13.323  1.00 30.21 ? 421 GLU A C   1 
ATOM   3558 O O   . GLU A 1 421 ? -17.542 7.046   12.826  1.00 24.88 ? 421 GLU A O   1 
ATOM   3559 C CB  . GLU A 1 421 ? -16.478 10.182  12.308  1.00 37.62 ? 421 GLU A CB  1 
ATOM   3560 C CG  . GLU A 1 421 ? -16.565 11.383  11.362  1.00 53.35 ? 421 GLU A CG  1 
ATOM   3561 C CD  . GLU A 1 421 ? -17.069 12.651  12.050  1.00 66.50 ? 421 GLU A CD  1 
ATOM   3562 O OE1 . GLU A 1 421 ? -16.719 13.754  11.579  1.00 71.18 ? 421 GLU A OE1 1 
ATOM   3563 O OE2 . GLU A 1 421 ? -17.798 12.548  13.065  1.00 68.21 ? 421 GLU A OE2 1 
ATOM   3564 N N   . LYS A 1 422 ? -17.528 8.378   14.638  1.00 25.66 ? 422 LYS A N   1 
ATOM   3565 C CA  . LYS A 1 422 ? -17.389 7.228   15.526  1.00 24.42 ? 422 LYS A CA  1 
ATOM   3566 C C   . LYS A 1 422 ? -18.610 6.316   15.447  1.00 29.75 ? 422 LYS A C   1 
ATOM   3567 O O   . LYS A 1 422 ? -18.472 5.085   15.435  1.00 26.92 ? 422 LYS A O   1 
ATOM   3568 C CB  . LYS A 1 422 ? -17.144 7.693   16.961  1.00 25.29 ? 422 LYS A CB  1 
ATOM   3569 C CG  . LYS A 1 422 ? -15.718 8.192   17.195  1.00 23.22 ? 422 LYS A CG  1 
ATOM   3570 C CD  . LYS A 1 422 ? -15.596 8.921   18.518  1.00 22.85 ? 422 LYS A CD  1 
ATOM   3571 C CE  . LYS A 1 422 ? -14.332 9.756   18.572  1.00 24.98 ? 422 LYS A CE  1 
ATOM   3572 N NZ  . LYS A 1 422 ? -13.120 8.959   18.221  1.00 25.13 ? 422 LYS A NZ  1 
ATOM   3573 N N   . ASN A 1 423 ? -19.818 6.897   15.377  1.00 21.82 ? 423 ASN A N   1 
ATOM   3574 C CA  . ASN A 1 423 ? -21.007 6.062   15.255  1.00 21.78 ? 423 ASN A CA  1 
ATOM   3575 C C   . ASN A 1 423 ? -20.978 5.239   13.977  1.00 22.03 ? 423 ASN A C   1 
ATOM   3576 O O   . ASN A 1 423 ? -21.449 4.097   13.964  1.00 23.35 ? 423 ASN A O   1 
ATOM   3577 C CB  . ASN A 1 423 ? -22.275 6.917   15.310  1.00 23.20 ? 423 ASN A CB  1 
ATOM   3578 C CG  . ASN A 1 423 ? -22.617 7.349   16.720  1.00 29.24 ? 423 ASN A CG  1 
ATOM   3579 O OD1 . ASN A 1 423 ? -22.015 6.874   17.687  1.00 23.34 ? 423 ASN A OD1 1 
ATOM   3580 N ND2 . ASN A 1 423 ? -23.587 8.248   16.850  1.00 26.07 ? 423 ASN A ND2 1 
ATOM   3581 N N   . GLU A 1 424 ? -20.400 5.780   12.904  1.00 27.80 ? 424 GLU A N   1 
ATOM   3582 C CA  . GLU A 1 424 ? -20.347 5.031   11.654  1.00 27.86 ? 424 GLU A CA  1 
ATOM   3583 C C   . GLU A 1 424 ? -19.489 3.777   11.781  1.00 26.34 ? 424 GLU A C   1 
ATOM   3584 O O   . GLU A 1 424 ? -19.809 2.740   11.186  1.00 22.96 ? 424 GLU A O   1 
ATOM   3585 C CB  . GLU A 1 424 ? -19.831 5.916   10.520  1.00 39.85 ? 424 GLU A CB  1 
ATOM   3586 C CG  . GLU A 1 424 ? -19.382 5.156   9.291   1.00 48.78 ? 424 GLU A CG  1 
ATOM   3587 C CD  . GLU A 1 424 ? -20.549 4.561   8.525   1.00 61.20 ? 424 GLU A CD  1 
ATOM   3588 O OE1 . GLU A 1 424 ? -21.368 3.810   9.078   1.00 63.40 ? 424 GLU A OE1 1 
ATOM   3589 O OE2 . GLU A 1 424 ? -20.698 4.891   7.346   1.00 67.53 ? 424 GLU A OE2 1 
ATOM   3590 N N   . TYR A 1 425 ? -18.393 3.849   12.545  1.00 26.59 ? 425 TYR A N   1 
ATOM   3591 C CA  . TYR A 1 425 ? -17.622 2.634   12.808  1.00 22.20 ? 425 TYR A CA  1 
ATOM   3592 C C   . TYR A 1 425 ? -18.476 1.590   13.507  1.00 20.04 ? 425 TYR A C   1 
ATOM   3593 O O   . TYR A 1 425 ? -18.461 0.409   13.143  1.00 22.86 ? 425 TYR A O   1 
ATOM   3594 C CB  . TYR A 1 425 ? -16.393 2.933   13.657  1.00 22.52 ? 425 TYR A CB  1 
ATOM   3595 C CG  . TYR A 1 425 ? -15.131 3.100   12.861  1.00 21.58 ? 425 TYR A CG  1 
ATOM   3596 C CD1 . TYR A 1 425 ? -15.181 3.486   11.532  1.00 19.35 ? 425 TYR A CD1 1 
ATOM   3597 C CD2 . TYR A 1 425 ? -13.877 2.866   13.435  1.00 22.37 ? 425 TYR A CD2 1 
ATOM   3598 C CE1 . TYR A 1 425 ? -14.021 3.646   10.792  1.00 17.40 ? 425 TYR A CE1 1 
ATOM   3599 C CE2 . TYR A 1 425 ? -12.706 3.028   12.694  1.00 24.21 ? 425 TYR A CE2 1 
ATOM   3600 C CZ  . TYR A 1 425 ? -12.796 3.421   11.366  1.00 24.41 ? 425 TYR A CZ  1 
ATOM   3601 O OH  . TYR A 1 425 ? -11.672 3.603   10.593  1.00 25.50 ? 425 TYR A OH  1 
ATOM   3602 N N   . TRP A 1 426 ? -19.227 2.016   14.523  1.00 19.00 ? 426 TRP A N   1 
ATOM   3603 C CA  . TRP A 1 426 ? -20.106 1.097   15.234  1.00 20.50 ? 426 TRP A CA  1 
ATOM   3604 C C   . TRP A 1 426 ? -21.181 0.546   14.311  1.00 17.70 ? 426 TRP A C   1 
ATOM   3605 O O   . TRP A 1 426 ? -21.480 -0.656  14.345  1.00 23.02 ? 426 TRP A O   1 
ATOM   3606 C CB  . TRP A 1 426 ? -20.728 1.798   16.446  1.00 21.97 ? 426 TRP A CB  1 
ATOM   3607 C CG  . TRP A 1 426 ? -19.734 2.015   17.569  1.00 19.43 ? 426 TRP A CG  1 
ATOM   3608 C CD1 . TRP A 1 426 ? -19.098 3.176   17.884  1.00 15.74 ? 426 TRP A CD1 1 
ATOM   3609 C CD2 . TRP A 1 426 ? -19.264 1.029   18.510  1.00 21.46 ? 426 TRP A CD2 1 
ATOM   3610 N NE1 . TRP A 1 426 ? -18.264 2.982   18.968  1.00 21.42 ? 426 TRP A NE1 1 
ATOM   3611 C CE2 . TRP A 1 426 ? -18.350 1.673   19.368  1.00 13.87 ? 426 TRP A CE2 1 
ATOM   3612 C CE3 . TRP A 1 426 ? -19.536 -0.330  18.713  1.00 12.76 ? 426 TRP A CE3 1 
ATOM   3613 C CZ2 . TRP A 1 426 ? -17.699 1.003   20.410  1.00 22.88 ? 426 TRP A CZ2 1 
ATOM   3614 C CZ3 . TRP A 1 426 ? -18.888 -0.996  19.741  1.00 21.04 ? 426 TRP A CZ3 1 
ATOM   3615 C CH2 . TRP A 1 426 ? -17.976 -0.329  20.578  1.00 17.09 ? 426 TRP A CH2 1 
ATOM   3616 N N   . LYS A 1 427 ? -21.750 1.398   13.452  1.00 18.23 ? 427 LYS A N   1 
ATOM   3617 C CA  . LYS A 1 427 ? -22.712 0.914   12.462  1.00 20.81 ? 427 LYS A CA  1 
ATOM   3618 C C   . LYS A 1 427 ? -22.092 -0.162  11.578  1.00 21.64 ? 427 LYS A C   1 
ATOM   3619 O O   . LYS A 1 427 ? -22.689 -1.224  11.365  1.00 20.50 ? 427 LYS A O   1 
ATOM   3620 C CB  . LYS A 1 427 ? -23.229 2.075   11.615  1.00 27.56 ? 427 LYS A CB  1 
ATOM   3621 C CG  . LYS A 1 427 ? -24.284 2.923   12.302  1.00 41.98 ? 427 LYS A CG  1 
ATOM   3622 C CD  . LYS A 1 427 ? -24.532 4.212   11.526  1.00 46.62 ? 427 LYS A CD  1 
ATOM   3623 C CE  . LYS A 1 427 ? -25.407 5.170   12.303  1.00 50.88 ? 427 LYS A CE  1 
ATOM   3624 N NZ  . LYS A 1 427 ? -25.331 6.553   11.749  1.00 57.70 ? 427 LYS A NZ  1 
ATOM   3625 N N   . ILE A 1 428 ? -20.885 0.096   11.063  1.00 23.84 ? 428 ILE A N   1 
ATOM   3626 C CA  . ILE A 1 428 ? -20.153 -0.912  10.290  1.00 25.39 ? 428 ILE A CA  1 
ATOM   3627 C C   . ILE A 1 428 ? -19.969 -2.185  11.110  1.00 25.07 ? 428 ILE A C   1 
ATOM   3628 O O   . ILE A 1 428 ? -20.244 -3.298  10.642  1.00 22.10 ? 428 ILE A O   1 
ATOM   3629 C CB  . ILE A 1 428 ? -18.799 -0.344  9.823   1.00 25.34 ? 428 ILE A CB  1 
ATOM   3630 C CG1 . ILE A 1 428 ? -19.007 0.642   8.673   1.00 24.89 ? 428 ILE A CG1 1 
ATOM   3631 C CG2 . ILE A 1 428 ? -17.849 -1.456  9.411   1.00 24.45 ? 428 ILE A CG2 1 
ATOM   3632 C CD1 . ILE A 1 428 ? -17.934 1.696   8.569   1.00 25.99 ? 428 ILE A CD1 1 
ATOM   3633 N N   . LEU A 1 429 ? -19.497 -2.038  12.350  1.00 22.42 ? 429 LEU A N   1 
ATOM   3634 C CA  . LEU A 1 429 ? -19.305 -3.193  13.218  1.00 19.68 ? 429 LEU A CA  1 
ATOM   3635 C C   . LEU A 1 429 ? -20.596 -3.987  13.381  1.00 20.32 ? 429 LEU A C   1 
ATOM   3636 O O   . LEU A 1 429 ? -20.599 -5.216  13.262  1.00 20.49 ? 429 LEU A O   1 
ATOM   3637 C CB  . LEU A 1 429 ? -18.781 -2.739  14.583  1.00 19.09 ? 429 LEU A CB  1 
ATOM   3638 C CG  . LEU A 1 429 ? -18.433 -3.856  15.567  1.00 26.02 ? 429 LEU A CG  1 
ATOM   3639 C CD1 . LEU A 1 429 ? -17.317 -4.738  15.024  1.00 28.98 ? 429 LEU A CD1 1 
ATOM   3640 C CD2 . LEU A 1 429 ? -18.042 -3.269  16.918  1.00 23.66 ? 429 LEU A CD2 1 
ATOM   3641 N N   . ILE A 1 430 ? -21.708 -3.294  13.648  1.00 21.70 ? 430 ILE A N   1 
ATOM   3642 C CA  . ILE A 1 430 ? -22.983 -3.977  13.876  1.00 28.29 ? 430 ILE A CA  1 
ATOM   3643 C C   . ILE A 1 430 ? -23.398 -4.766  12.638  1.00 26.59 ? 430 ILE A C   1 
ATOM   3644 O O   . ILE A 1 430 ? -23.787 -5.938  12.728  1.00 23.17 ? 430 ILE A O   1 
ATOM   3645 C CB  . ILE A 1 430 ? -24.067 -2.964  14.287  1.00 23.99 ? 430 ILE A CB  1 
ATOM   3646 C CG1 . ILE A 1 430 ? -23.808 -2.466  15.706  1.00 23.41 ? 430 ILE A CG1 1 
ATOM   3647 C CG2 . ILE A 1 430 ? -25.465 -3.574  14.161  1.00 17.55 ? 430 ILE A CG2 1 
ATOM   3648 C CD1 . ILE A 1 430 ? -24.317 -1.077  15.956  1.00 23.60 ? 430 ILE A CD1 1 
ATOM   3649 N N   . GLU A 1 431 ? -23.312 -4.139  11.462  1.00 26.89 ? 431 GLU A N   1 
ATOM   3650 C CA  . GLU A 1 431 ? -23.680 -4.843  10.238  1.00 26.93 ? 431 GLU A CA  1 
ATOM   3651 C C   . GLU A 1 431 ? -22.738 -6.010  9.969   1.00 23.44 ? 431 GLU A C   1 
ATOM   3652 O O   . GLU A 1 431 ? -23.173 -7.078  9.521   1.00 27.87 ? 431 GLU A O   1 
ATOM   3653 C CB  . GLU A 1 431 ? -23.700 -3.870  9.057   1.00 30.59 ? 431 GLU A CB  1 
ATOM   3654 C CG  . GLU A 1 431 ? -24.740 -2.765  9.186   1.00 38.66 ? 431 GLU A CG  1 
ATOM   3655 C CD  . GLU A 1 431 ? -26.169 -3.294  9.199   1.00 48.12 ? 431 GLU A CD  1 
ATOM   3656 O OE1 . GLU A 1 431 ? -26.420 -4.369  8.612   1.00 47.47 ? 431 GLU A OE1 1 
ATOM   3657 O OE2 . GLU A 1 431 ? -27.045 -2.632  9.796   1.00 52.27 ? 431 GLU A OE2 1 
ATOM   3658 N N   . ALA A 1 432 ? -21.447 -5.840  10.259  1.00 25.76 ? 432 ALA A N   1 
ATOM   3659 C CA  . ALA A 1 432 ? -20.494 -6.924  10.034  1.00 23.29 ? 432 ALA A CA  1 
ATOM   3660 C C   . ALA A 1 432 ? -20.749 -8.099  10.970  1.00 30.66 ? 432 ALA A C   1 
ATOM   3661 O O   . ALA A 1 432 ? -20.567 -9.259  10.584  1.00 32.22 ? 432 ALA A O   1 
ATOM   3662 C CB  . ALA A 1 432 ? -19.074 -6.407  10.216  1.00 25.37 ? 432 ALA A CB  1 
ATOM   3663 N N   . LYS A 1 433 ? -21.147 -7.810  12.213  1.00 28.92 ? 433 LYS A N   1 
ATOM   3664 C CA  . LYS A 1 433 ? -21.429 -8.862  13.184  1.00 23.16 ? 433 LYS A CA  1 
ATOM   3665 C C   . LYS A 1 433 ? -22.540 -9.785  12.695  1.00 28.83 ? 433 LYS A C   1 
ATOM   3666 O O   . LYS A 1 433 ? -22.507 -10.994 12.953  1.00 35.52 ? 433 LYS A O   1 
ATOM   3667 C CB  . LYS A 1 433 ? -21.800 -8.225  14.527  1.00 25.40 ? 433 LYS A CB  1 
ATOM   3668 C CG  . LYS A 1 433 ? -22.205 -9.211  15.624  1.00 26.51 ? 433 LYS A CG  1 
ATOM   3669 C CD  . LYS A 1 433 ? -21.060 -10.126 16.002  1.00 30.05 ? 433 LYS A CD  1 
ATOM   3670 C CE  . LYS A 1 433 ? -21.471 -11.104 17.101  1.00 26.25 ? 433 LYS A CE  1 
ATOM   3671 N NZ  . LYS A 1 433 ? -20.464 -12.201 17.235  1.00 28.81 ? 433 LYS A NZ  1 
ATOM   3672 N N   . LYS A 1 434 ? -23.520 -9.234  11.967  1.00 32.31 ? 434 LYS A N   1 
ATOM   3673 C CA  . LYS A 1 434 ? -24.664 -10.028 11.521  1.00 37.64 ? 434 LYS A CA  1 
ATOM   3674 C C   . LYS A 1 434 ? -24.246 -11.180 10.618  1.00 34.42 ? 434 LYS A C   1 
ATOM   3675 O O   . LYS A 1 434 ? -24.889 -12.233 10.629  1.00 38.82 ? 434 LYS A O   1 
ATOM   3676 C CB  . LYS A 1 434 ? -25.677 -9.144  10.793  1.00 36.76 ? 434 LYS A CB  1 
ATOM   3677 C CG  . LYS A 1 434 ? -26.542 -8.294  11.698  1.00 35.85 ? 434 LYS A CG  1 
ATOM   3678 C CD  . LYS A 1 434 ? -27.349 -7.300  10.879  1.00 37.79 ? 434 LYS A CD  1 
ATOM   3679 C CE  . LYS A 1 434 ? -28.021 -6.259  11.754  1.00 40.13 ? 434 LYS A CE  1 
ATOM   3680 N NZ  . LYS A 1 434 ? -28.546 -5.118  10.932  1.00 41.43 ? 434 LYS A NZ  1 
ATOM   3681 N N   . LYS A 1 435 ? -23.183 -11.007 9.828   1.00 34.36 ? 435 LYS A N   1 
ATOM   3682 C CA  . LYS A 1 435 ? -22.682 -12.075 8.967   1.00 34.77 ? 435 LYS A CA  1 
ATOM   3683 C C   . LYS A 1 435 ? -21.228 -12.426 9.271   1.00 33.59 ? 435 LYS A C   1 
ATOM   3684 O O   . LYS A 1 435 ? -20.505 -12.920 8.401   1.00 34.10 ? 435 LYS A O   1 
ATOM   3685 C CB  . LYS A 1 435 ? -22.851 -11.714 7.492   1.00 39.79 ? 435 LYS A CB  1 
ATOM   3686 C CG  . LYS A 1 435 ? -22.147 -10.449 7.058   1.00 44.39 ? 435 LYS A CG  1 
ATOM   3687 C CD  . LYS A 1 435 ? -22.466 -10.122 5.600   1.00 47.87 ? 435 LYS A CD  1 
ATOM   3688 C CE  . LYS A 1 435 ? -23.852 -9.513  5.458   1.00 49.59 ? 435 LYS A CE  1 
ATOM   3689 N NZ  . LYS A 1 435 ? -23.960 -8.224  6.197   1.00 50.21 ? 435 LYS A NZ  1 
ATOM   3690 N N   . ALA A 1 436 ? -20.794 -12.199 10.508  1.00 30.23 ? 436 ALA A N   1 
ATOM   3691 C CA  . ALA A 1 436 ? -19.438 -12.555 10.895  1.00 27.97 ? 436 ALA A CA  1 
ATOM   3692 C C   . ALA A 1 436 ? -19.248 -14.068 10.855  1.00 32.42 ? 436 ALA A C   1 
ATOM   3693 O O   . ALA A 1 436 ? -20.136 -14.835 11.235  1.00 38.90 ? 436 ALA A O   1 
ATOM   3694 C CB  . ALA A 1 436 ? -19.127 -12.018 12.294  1.00 22.73 ? 436 ALA A CB  1 
ATOM   3695 N N   . LYS A 1 437 ? -18.071 -14.496 10.404  1.00 32.29 ? 437 LYS A N   1 
ATOM   3696 C CA  . LYS A 1 437 ? -17.751 -15.909 10.268  1.00 36.93 ? 437 LYS A CA  1 
ATOM   3697 C C   . LYS A 1 437 ? -16.597 -16.380 11.142  1.00 36.20 ? 437 LYS A C   1 
ATOM   3698 O O   . LYS A 1 437 ? -16.430 -17.594 11.304  1.00 40.44 ? 437 LYS A O   1 
ATOM   3699 C CB  . LYS A 1 437 ? -17.381 -16.235 8.817   1.00 43.69 ? 437 LYS A CB  1 
ATOM   3700 C CG  . LYS A 1 437 ? -15.892 -16.094 8.635   1.00 56.84 ? 437 LYS A CG  1 
ATOM   3701 C CD  . LYS A 1 437 ? -15.451 -16.026 7.221   1.00 65.00 ? 437 LYS A CD  1 
ATOM   3702 C CE  . LYS A 1 437 ? -13.952 -15.833 7.155   1.00 70.65 ? 437 LYS A CE  1 
ATOM   3703 N NZ  . LYS A 1 437 ? -13.285 -16.710 6.177   1.00 74.41 ? 437 LYS A NZ  1 
ATOM   3704 N N   . ASN A 1 438 ? -15.783 -15.475 11.676  1.00 32.68 ? 438 ASN A N   1 
ATOM   3705 C CA  . ASN A 1 438 ? -14.543 -15.863 12.330  1.00 29.59 ? 438 ASN A CA  1 
ATOM   3706 C C   . ASN A 1 438 ? -14.166 -14.786 13.338  1.00 26.44 ? 438 ASN A C   1 
ATOM   3707 O O   . ASN A 1 438 ? -14.832 -13.753 13.449  1.00 26.35 ? 438 ASN A O   1 
ATOM   3708 C CB  . ASN A 1 438 ? -13.426 -16.071 11.302  1.00 29.48 ? 438 ASN A CB  1 
ATOM   3709 C CG  . ASN A 1 438 ? -12.837 -14.757 10.813  1.00 37.47 ? 438 ASN A CG  1 
ATOM   3710 O OD1 . ASN A 1 438 ? -11.951 -14.186 11.444  1.00 51.44 ? 438 ASN A OD1 1 
ATOM   3711 N ND2 . ASN A 1 438 ? -13.327 -14.275 9.686   1.00 42.02 ? 438 ASN A ND2 1 
ATOM   3712 N N   . ASP A 1 439 ? -13.064 -15.020 14.049  1.00 33.17 ? 439 ASP A N   1 
ATOM   3713 C CA  . ASP A 1 439 ? -12.682 -14.166 15.166  1.00 28.78 ? 439 ASP A CA  1 
ATOM   3714 C C   . ASP A 1 439 ? -12.088 -12.827 14.739  1.00 28.18 ? 439 ASP A C   1 
ATOM   3715 O O   . ASP A 1 439 ? -11.703 -12.044 15.611  1.00 28.46 ? 439 ASP A O   1 
ATOM   3716 C CB  . ASP A 1 439 ? -11.703 -14.907 16.081  1.00 28.61 ? 439 ASP A CB  1 
ATOM   3717 C CG  . ASP A 1 439 ? -12.388 -15.976 16.923  1.00 38.15 ? 439 ASP A CG  1 
ATOM   3718 O OD1 . ASP A 1 439 ? -13.637 -15.978 16.988  1.00 36.02 ? 439 ASP A OD1 1 
ATOM   3719 O OD2 . ASP A 1 439 ? -11.678 -16.809 17.528  1.00 41.49 ? 439 ASP A OD2 1 
ATOM   3720 N N   . TYR A 1 440 ? -12.004 -12.522 13.438  1.00 26.19 ? 440 TYR A N   1 
ATOM   3721 C CA  . TYR A 1 440 ? -11.613 -11.166 13.066  1.00 25.05 ? 440 TYR A CA  1 
ATOM   3722 C C   . TYR A 1 440 ? -12.671 -10.146 13.464  1.00 23.94 ? 440 TYR A C   1 
ATOM   3723 O O   . TYR A 1 440 ? -12.366 -8.951  13.540  1.00 20.00 ? 440 TYR A O   1 
ATOM   3724 C CB  . TYR A 1 440 ? -11.306 -11.079 11.565  1.00 21.21 ? 440 TYR A CB  1 
ATOM   3725 C CG  . TYR A 1 440 ? -9.846  -11.355 11.272  1.00 25.73 ? 440 TYR A CG  1 
ATOM   3726 C CD1 . TYR A 1 440 ? -8.869  -10.417 11.579  1.00 32.39 ? 440 TYR A CD1 1 
ATOM   3727 C CD2 . TYR A 1 440 ? -9.440  -12.563 10.718  1.00 31.44 ? 440 TYR A CD2 1 
ATOM   3728 C CE1 . TYR A 1 440 ? -7.531  -10.668 11.324  1.00 37.22 ? 440 TYR A CE1 1 
ATOM   3729 C CE2 . TYR A 1 440 ? -8.101  -12.828 10.462  1.00 31.30 ? 440 TYR A CE2 1 
ATOM   3730 C CZ  . TYR A 1 440 ? -7.151  -11.874 10.766  1.00 38.84 ? 440 TYR A CZ  1 
ATOM   3731 O OH  . TYR A 1 440 ? -5.818  -12.122 10.514  1.00 43.23 ? 440 TYR A OH  1 
ATOM   3732 N N   . ILE A 1 441 ? -13.904 -10.586 13.733  1.00 17.98 ? 441 ILE A N   1 
ATOM   3733 C CA  . ILE A 1 441 ? -14.880 -9.674  14.309  1.00 19.42 ? 441 ILE A CA  1 
ATOM   3734 C C   . ILE A 1 441 ? -14.434 -9.247  15.700  1.00 25.02 ? 441 ILE A C   1 
ATOM   3735 O O   . ILE A 1 441 ? -14.701 -8.118  16.121  1.00 20.53 ? 441 ILE A O   1 
ATOM   3736 C CB  . ILE A 1 441 ? -16.286 -10.309 14.323  1.00 19.88 ? 441 ILE A CB  1 
ATOM   3737 C CG1 . ILE A 1 441 ? -17.358 -9.238  14.552  1.00 17.21 ? 441 ILE A CG1 1 
ATOM   3738 C CG2 . ILE A 1 441 ? -16.396 -11.420 15.372  1.00 20.25 ? 441 ILE A CG2 1 
ATOM   3739 C CD1 . ILE A 1 441 ? -17.556 -8.318  13.330  1.00 18.93 ? 441 ILE A CD1 1 
ATOM   3740 N N   . LEU A 1 442 ? -13.731 -10.121 16.427  1.00 22.95 ? 442 LEU A N   1 
ATOM   3741 C CA  . LEU A 1 442 ? -13.221 -9.727  17.736  1.00 21.83 ? 442 LEU A CA  1 
ATOM   3742 C C   . LEU A 1 442 ? -12.114 -8.680  17.603  1.00 18.76 ? 442 LEU A C   1 
ATOM   3743 O O   . LEU A 1 442 ? -12.039 -7.745  18.409  1.00 17.93 ? 442 LEU A O   1 
ATOM   3744 C CB  . LEU A 1 442 ? -12.723 -10.956 18.502  1.00 18.83 ? 442 LEU A CB  1 
ATOM   3745 C CG  . LEU A 1 442 ? -13.720 -12.101 18.722  1.00 19.55 ? 442 LEU A CG  1 
ATOM   3746 C CD1 . LEU A 1 442 ? -13.077 -13.248 19.493  1.00 21.51 ? 442 LEU A CD1 1 
ATOM   3747 C CD2 . LEU A 1 442 ? -14.958 -11.605 19.438  1.00 16.31 ? 442 LEU A CD2 1 
ATOM   3748 N N   . VAL A 1 443 ? -11.255 -8.820  16.589  1.00 19.36 ? 443 VAL A N   1 
ATOM   3749 C CA  . VAL A 1 443 ? -10.189 -7.844  16.355  1.00 19.70 ? 443 VAL A CA  1 
ATOM   3750 C C   . VAL A 1 443 ? -10.776 -6.455  16.131  1.00 21.68 ? 443 VAL A C   1 
ATOM   3751 O O   . VAL A 1 443 ? -10.264 -5.456  16.654  1.00 19.69 ? 443 VAL A O   1 
ATOM   3752 C CB  . VAL A 1 443 ? -9.317  -8.273  15.155  1.00 24.95 ? 443 VAL A CB  1 
ATOM   3753 C CG1 . VAL A 1 443 ? -8.256  -7.234  14.868  1.00 17.56 ? 443 VAL A CG1 1 
ATOM   3754 C CG2 . VAL A 1 443 ? -8.684  -9.639  15.392  1.00 24.51 ? 443 VAL A CG2 1 
ATOM   3755 N N   . ALA A 1 444 ? -11.861 -6.374  15.350  1.00 19.20 ? 444 ALA A N   1 
ATOM   3756 C CA  . ALA A 1 444 ? -12.485 -5.097  15.012  1.00 17.59 ? 444 ALA A CA  1 
ATOM   3757 C C   . ALA A 1 444 ? -13.223 -4.466  16.188  1.00 18.09 ? 444 ALA A C   1 
ATOM   3758 O O   . ALA A 1 444 ? -13.577 -3.285  16.117  1.00 13.36 ? 444 ALA A O   1 
ATOM   3759 C CB  . ALA A 1 444 ? -13.462 -5.279  13.853  1.00 18.97 ? 444 ALA A CB  1 
ATOM   3760 N N   . GLU A 1 445 ? -13.505 -5.224  17.241  1.00 15.32 ? 445 GLU A N   1 
ATOM   3761 C CA  . GLU A 1 445 ? -14.113 -4.639  18.431  1.00 16.37 ? 445 GLU A CA  1 
ATOM   3762 C C   . GLU A 1 445 ? -13.101 -3.961  19.351  1.00 20.96 ? 445 GLU A C   1 
ATOM   3763 O O   . GLU A 1 445 ? -13.504 -3.389  20.373  1.00 16.52 ? 445 GLU A O   1 
ATOM   3764 C CB  . GLU A 1 445 ? -14.900 -5.711  19.191  1.00 21.06 ? 445 GLU A CB  1 
ATOM   3765 C CG  . GLU A 1 445 ? -16.088 -6.241  18.381  1.00 20.48 ? 445 GLU A CG  1 
ATOM   3766 C CD  . GLU A 1 445 ? -16.548 -7.616  18.810  1.00 26.43 ? 445 GLU A CD  1 
ATOM   3767 O OE1 . GLU A 1 445 ? -15.995 -8.141  19.798  1.00 24.76 ? 445 GLU A OE1 1 
ATOM   3768 O OE2 . GLU A 1 445 ? -17.462 -8.172  18.150  1.00 24.52 ? 445 GLU A OE2 1 
ATOM   3769 N N   . GLY A 1 446 ? -11.813 -3.979  19.006  1.00 14.96 ? 446 GLY A N   1 
ATOM   3770 C CA  . GLY A 1 446 ? -10.829 -3.308  19.837  1.00 14.36 ? 446 GLY A CA  1 
ATOM   3771 C C   . GLY A 1 446 ? -11.098 -1.819  19.947  1.00 18.07 ? 446 GLY A C   1 
ATOM   3772 O O   . GLY A 1 446 ? -11.598 -1.180  19.016  1.00 19.18 ? 446 GLY A O   1 
ATOM   3773 N N   . SER A 1 447 ? -10.762 -1.260  21.113  1.00 15.15 ? 447 SER A N   1 
ATOM   3774 C CA  . SER A 1 447 ? -11.087 0.138   21.389  1.00 11.37 ? 447 SER A CA  1 
ATOM   3775 C C   . SER A 1 447 ? -10.335 1.099   20.467  1.00 17.89 ? 447 SER A C   1 
ATOM   3776 O O   . SER A 1 447 ? -10.859 2.169   20.120  1.00 14.58 ? 447 SER A O   1 
ATOM   3777 C CB  . SER A 1 447 ? -10.795 0.456   22.863  1.00 12.93 ? 447 SER A CB  1 
ATOM   3778 O OG  . SER A 1 447 ? -9.399  0.431   23.178  1.00 16.02 ? 447 SER A OG  1 
ATOM   3779 N N   . ASP A 1 448 ? -9.126  0.727   20.037  1.00 15.94 ? 448 ASP A N   1 
ATOM   3780 C CA  . ASP A 1 448 ? -8.256  1.664   19.328  1.00 14.80 ? 448 ASP A CA  1 
ATOM   3781 C C   . ASP A 1 448 ? -8.900  2.197   18.051  1.00 14.68 ? 448 ASP A C   1 
ATOM   3782 O O   . ASP A 1 448 ? -8.711  3.366   17.692  1.00 17.56 ? 448 ASP A O   1 
ATOM   3783 C CB  . ASP A 1 448 ? -6.924  0.988   18.998  1.00 13.88 ? 448 ASP A CB  1 
ATOM   3784 C CG  . ASP A 1 448 ? -6.313  0.306   20.212  1.00 18.22 ? 448 ASP A CG  1 
ATOM   3785 O OD1 . ASP A 1 448 ? -6.749  -0.817  20.551  1.00 14.66 ? 448 ASP A OD1 1 
ATOM   3786 O OD2 . ASP A 1 448 ? -5.405  0.893   20.827  1.00 16.11 ? 448 ASP A OD2 1 
ATOM   3787 N N   . TRP A 1 449 ? -9.636  1.354   17.336  1.00 11.39 ? 449 TRP A N   1 
ATOM   3788 C CA  . TRP A 1 449 ? -10.201 1.791   16.063  1.00 14.04 ? 449 TRP A CA  1 
ATOM   3789 C C   . TRP A 1 449 ? -11.172 2.949   16.256  1.00 18.49 ? 449 TRP A C   1 
ATOM   3790 O O   . TRP A 1 449 ? -11.228 3.873   15.432  1.00 16.38 ? 449 TRP A O   1 
ATOM   3791 C CB  . TRP A 1 449 ? -10.892 0.621   15.360  1.00 18.49 ? 449 TRP A CB  1 
ATOM   3792 C CG  . TRP A 1 449 ? -10.113 -0.633  15.444  1.00 19.15 ? 449 TRP A CG  1 
ATOM   3793 C CD1 . TRP A 1 449 ? -10.514 -1.817  15.999  1.00 14.96 ? 449 TRP A CD1 1 
ATOM   3794 C CD2 . TRP A 1 449 ? -8.777  -0.836  14.972  1.00 11.47 ? 449 TRP A CD2 1 
ATOM   3795 N NE1 . TRP A 1 449 ? -9.512  -2.755  15.886  1.00 14.31 ? 449 TRP A NE1 1 
ATOM   3796 C CE2 . TRP A 1 449 ? -8.432  -2.176  15.266  1.00 12.21 ? 449 TRP A CE2 1 
ATOM   3797 C CE3 . TRP A 1 449 ? -7.840  -0.019  14.319  1.00 13.39 ? 449 TRP A CE3 1 
ATOM   3798 C CZ2 . TRP A 1 449 ? -7.190  -2.715  14.941  1.00 11.41 ? 449 TRP A CZ2 1 
ATOM   3799 C CZ3 . TRP A 1 449 ? -6.605  -0.560  13.987  1.00 15.96 ? 449 TRP A CZ3 1 
ATOM   3800 C CH2 . TRP A 1 449 ? -6.290  -1.895  14.306  1.00 12.54 ? 449 TRP A CH2 1 
ATOM   3801 N N   . PHE A 1 450 ? -11.931 2.926   17.346  1.00 17.49 ? 450 PHE A N   1 
ATOM   3802 C CA  . PHE A 1 450 ? -12.935 3.947   17.585  1.00 19.36 ? 450 PHE A CA  1 
ATOM   3803 C C   . PHE A 1 450 ? -12.326 5.208   18.178  1.00 21.69 ? 450 PHE A C   1 
ATOM   3804 O O   . PHE A 1 450 ? -12.901 6.290   18.018  1.00 21.72 ? 450 PHE A O   1 
ATOM   3805 C CB  . PHE A 1 450 ? -14.031 3.379   18.493  1.00 17.02 ? 450 PHE A CB  1 
ATOM   3806 C CG  . PHE A 1 450 ? -14.670 2.124   17.949  1.00 20.11 ? 450 PHE A CG  1 
ATOM   3807 C CD1 . PHE A 1 450 ? -15.734 2.200   17.072  1.00 14.30 ? 450 PHE A CD1 1 
ATOM   3808 C CD2 . PHE A 1 450 ? -14.179 0.872   18.292  1.00 23.31 ? 450 PHE A CD2 1 
ATOM   3809 C CE1 . PHE A 1 450 ? -16.317 1.043   16.550  1.00 12.81 ? 450 PHE A CE1 1 
ATOM   3810 C CE2 . PHE A 1 450 ? -14.755 -0.287  17.782  1.00 20.42 ? 450 PHE A CE2 1 
ATOM   3811 C CZ  . PHE A 1 450 ? -15.828 -0.199  16.910  1.00 17.86 ? 450 PHE A CZ  1 
ATOM   3812 N N   . TRP A 1 451 ? -11.175 5.080   18.846  1.00 17.55 ? 451 TRP A N   1 
ATOM   3813 C CA  . TRP A 1 451 ? -10.431 6.244   19.320  1.00 20.77 ? 451 TRP A CA  1 
ATOM   3814 C C   . TRP A 1 451 ? -9.973  7.118   18.151  1.00 26.92 ? 451 TRP A C   1 
ATOM   3815 O O   . TRP A 1 451 ? -10.131 8.344   18.176  1.00 20.95 ? 451 TRP A O   1 
ATOM   3816 C CB  . TRP A 1 451 ? -9.228  5.781   20.154  1.00 16.50 ? 451 TRP A CB  1 
ATOM   3817 C CG  . TRP A 1 451 ? -8.330  6.896   20.608  1.00 28.77 ? 451 TRP A CG  1 
ATOM   3818 C CD1 . TRP A 1 451 ? -7.271  7.434   19.925  1.00 30.87 ? 451 TRP A CD1 1 
ATOM   3819 C CD2 . TRP A 1 451 ? -8.414  7.613   21.846  1.00 31.92 ? 451 TRP A CD2 1 
ATOM   3820 N NE1 . TRP A 1 451 ? -6.700  8.443   20.658  1.00 30.27 ? 451 TRP A NE1 1 
ATOM   3821 C CE2 . TRP A 1 451 ? -7.379  8.573   21.843  1.00 35.80 ? 451 TRP A CE2 1 
ATOM   3822 C CE3 . TRP A 1 451 ? -9.266  7.542   22.951  1.00 25.32 ? 451 TRP A CE3 1 
ATOM   3823 C CZ2 . TRP A 1 451 ? -7.172  9.452   22.906  1.00 34.97 ? 451 TRP A CZ2 1 
ATOM   3824 C CZ3 . TRP A 1 451 ? -9.063  8.417   24.005  1.00 30.13 ? 451 TRP A CZ3 1 
ATOM   3825 C CH2 . TRP A 1 451 ? -8.022  9.359   23.976  1.00 35.08 ? 451 TRP A CH2 1 
ATOM   3826 N N   . TRP A 1 452 ? -9.405  6.500   17.114  1.00 21.07 ? 452 TRP A N   1 
ATOM   3827 C CA  . TRP A 1 452 ? -8.784  7.270   16.041  1.00 20.61 ? 452 TRP A CA  1 
ATOM   3828 C C   . TRP A 1 452 ? -9.803  7.761   15.031  1.00 25.10 ? 452 TRP A C   1 
ATOM   3829 O O   . TRP A 1 452 ? -9.578  8.792   14.393  1.00 26.47 ? 452 TRP A O   1 
ATOM   3830 C CB  . TRP A 1 452 ? -7.711  6.434   15.331  1.00 22.79 ? 452 TRP A CB  1 
ATOM   3831 C CG  . TRP A 1 452 ? -6.570  6.066   16.236  1.00 25.59 ? 452 TRP A CG  1 
ATOM   3832 C CD1 . TRP A 1 452 ? -6.246  4.817   16.674  1.00 25.97 ? 452 TRP A CD1 1 
ATOM   3833 C CD2 . TRP A 1 452 ? -5.619  6.958   16.826  1.00 32.57 ? 452 TRP A CD2 1 
ATOM   3834 N NE1 . TRP A 1 452 ? -5.152  4.872   17.502  1.00 30.06 ? 452 TRP A NE1 1 
ATOM   3835 C CE2 . TRP A 1 452 ? -4.744  6.176   17.610  1.00 31.62 ? 452 TRP A CE2 1 
ATOM   3836 C CE3 . TRP A 1 452 ? -5.422  8.344   16.773  1.00 38.62 ? 452 TRP A CE3 1 
ATOM   3837 C CZ2 . TRP A 1 452 ? -3.689  6.731   18.332  1.00 39.75 ? 452 TRP A CZ2 1 
ATOM   3838 C CZ3 . TRP A 1 452 ? -4.375  8.894   17.493  1.00 39.89 ? 452 TRP A CZ3 1 
ATOM   3839 C CH2 . TRP A 1 452 ? -3.520  8.088   18.261  1.00 42.90 ? 452 TRP A CH2 1 
ATOM   3840 N N   . GLN A 1 453 ? -10.917 7.049   14.875  1.00 25.70 ? 453 GLN A N   1 
ATOM   3841 C CA  . GLN A 1 453 ? -11.933 7.460   13.915  1.00 32.31 ? 453 GLN A CA  1 
ATOM   3842 C C   . GLN A 1 453 ? -12.403 8.879   14.218  1.00 34.66 ? 453 GLN A C   1 
ATOM   3843 O O   . GLN A 1 453 ? -12.760 9.198   15.354  1.00 31.86 ? 453 GLN A O   1 
ATOM   3844 C CB  . GLN A 1 453 ? -13.112 6.483   13.941  1.00 29.29 ? 453 GLN A CB  1 
ATOM   3845 C CG  . GLN A 1 453 ? -14.333 6.944   13.133  1.00 33.58 ? 453 GLN A CG  1 
ATOM   3846 C CD  . GLN A 1 453 ? -14.137 6.852   11.613  1.00 36.41 ? 453 GLN A CD  1 
ATOM   3847 O OE1 . GLN A 1 453 ? -13.014 6.851   11.114  1.00 31.51 ? 453 GLN A OE1 1 
ATOM   3848 N NE2 . GLN A 1 453 ? -15.244 6.769   10.879  1.00 33.05 ? 453 GLN A NE2 1 
ATOM   3849 N N   . GLY A 1 454 ? -12.359 9.745   13.204  1.00 41.21 ? 454 GLY A N   1 
ATOM   3850 C CA  . GLY A 1 454 ? -12.796 11.116  13.318  1.00 52.55 ? 454 GLY A CA  1 
ATOM   3851 C C   . GLY A 1 454 ? -11.680 12.132  13.494  1.00 62.84 ? 454 GLY A C   1 
ATOM   3852 O O   . GLY A 1 454 ? -11.845 13.288  13.090  1.00 67.99 ? 454 GLY A O   1 
ATOM   3853 N N   . GLU A 1 455 ? -10.555 11.735  14.085  1.00 63.91 ? 455 GLU A N   1 
ATOM   3854 C CA  . GLU A 1 455 ? -9.456  12.661  14.366  1.00 64.75 ? 455 GLU A CA  1 
ATOM   3855 C C   . GLU A 1 455 ? -8.659  12.883  13.086  1.00 65.02 ? 455 GLU A C   1 
ATOM   3856 O O   . GLU A 1 455 ? -7.808  12.074  12.725  1.00 64.99 ? 455 GLU A O   1 
ATOM   3857 C CB  . GLU A 1 455 ? -8.571  12.116  15.480  1.00 60.72 ? 455 GLU A CB  1 
ATOM   3858 C CG  . GLU A 1 455 ? -9.344  11.626  16.692  1.00 60.79 ? 455 GLU A CG  1 
ATOM   3859 C CD  . GLU A 1 455 ? -10.134 12.728  17.367  1.00 63.11 ? 455 GLU A CD  1 
ATOM   3860 O OE1 . GLU A 1 455 ? -9.707  13.901  17.300  1.00 66.19 ? 455 GLU A OE1 1 
ATOM   3861 O OE2 . GLU A 1 455 ? -11.187 12.419  17.960  1.00 63.64 ? 455 GLU A OE2 1 
ATOM   3862 N N   . GLU A 1 456 ? -8.905  14.005  12.408  1.00 68.38 ? 456 GLU A N   1 
ATOM   3863 C CA  . GLU A 1 456 ? -8.379  14.185  11.058  1.00 68.07 ? 456 GLU A CA  1 
ATOM   3864 C C   . GLU A 1 456 ? -6.904  14.583  11.011  1.00 66.33 ? 456 GLU A C   1 
ATOM   3865 O O   . GLU A 1 456 ? -6.275  14.417  9.957   1.00 61.36 ? 456 GLU A O   1 
ATOM   3866 C CB  . GLU A 1 456 ? -9.221  15.220  10.306  1.00 68.78 ? 456 GLU A CB  1 
ATOM   3867 C CG  . GLU A 1 456 ? -10.719 14.904  10.263  1.00 72.24 ? 456 GLU A CG  1 
ATOM   3868 C CD  . GLU A 1 456 ? -11.076 13.797  9.275   1.00 74.34 ? 456 GLU A CD  1 
ATOM   3869 O OE1 . GLU A 1 456 ? -10.155 13.160  8.720   1.00 74.98 ? 456 GLU A OE1 1 
ATOM   3870 O OE2 . GLU A 1 456 ? -12.285 13.567  9.052   1.00 73.23 ? 456 GLU A OE2 1 
ATOM   3871 N N   . LYS A 1 457 ? -6.334  15.096  12.104  1.00 67.58 ? 457 LYS A N   1 
ATOM   3872 C CA  . LYS A 1 457 ? -4.911  15.410  12.136  1.00 68.09 ? 457 LYS A CA  1 
ATOM   3873 C C   . LYS A 1 457 ? -4.111  14.418  12.972  1.00 69.58 ? 457 LYS A C   1 
ATOM   3874 O O   . LYS A 1 457 ? -2.877  14.507  13.011  1.00 72.91 ? 457 LYS A O   1 
ATOM   3875 C CB  . LYS A 1 457 ? -4.686  16.840  12.654  1.00 67.98 ? 457 LYS A CB  1 
ATOM   3876 C CG  . LYS A 1 457 ? -3.275  17.403  12.419  1.00 65.48 ? 457 LYS A CG  1 
ATOM   3877 C CD  . LYS A 1 457 ? -2.867  18.381  13.525  1.00 60.29 ? 457 LYS A CD  1 
ATOM   3878 C CE  . LYS A 1 457 ? -1.452  18.118  14.030  1.00 51.96 ? 457 LYS A CE  1 
ATOM   3879 N NZ  . LYS A 1 457 ? -1.049  19.130  15.056  1.00 50.76 ? 457 LYS A NZ  1 
ATOM   3880 N N   . ALA A 1 458 ? -4.769  13.458  13.620  1.00 66.26 ? 458 ALA A N   1 
ATOM   3881 C CA  . ALA A 1 458 ? -4.040  12.433  14.349  1.00 63.46 ? 458 ALA A CA  1 
ATOM   3882 C C   . ALA A 1 458 ? -3.147  11.649  13.384  1.00 62.90 ? 458 ALA A C   1 
ATOM   3883 O O   . ALA A 1 458 ? -3.475  11.499  12.200  1.00 61.20 ? 458 ALA A O   1 
ATOM   3884 C CB  . ALA A 1 458 ? -5.009  11.499  15.069  1.00 60.77 ? 458 ALA A CB  1 
ATOM   3885 N N   . PRO A 1 459 ? -2.004  11.149  13.860  1.00 59.04 ? 459 PRO A N   1 
ATOM   3886 C CA  . PRO A 1 459 ? -1.005  10.586  12.939  1.00 53.31 ? 459 PRO A CA  1 
ATOM   3887 C C   . PRO A 1 459 ? -1.452  9.255   12.354  1.00 40.12 ? 459 PRO A C   1 
ATOM   3888 O O   . PRO A 1 459 ? -1.843  8.341   13.085  1.00 38.26 ? 459 PRO A O   1 
ATOM   3889 C CB  . PRO A 1 459 ? 0.235   10.418  13.826  1.00 55.73 ? 459 PRO A CB  1 
ATOM   3890 C CG  . PRO A 1 459 ? -0.322  10.248  15.207  1.00 56.92 ? 459 PRO A CG  1 
ATOM   3891 C CD  . PRO A 1 459 ? -1.530  11.145  15.256  1.00 60.18 ? 459 PRO A CD  1 
ATOM   3892 N N   . PHE A 1 460 ? -1.375  9.150   11.020  1.00 23.00 ? 460 PHE A N   1 
ATOM   3893 C CA  . PHE A 1 460 ? -1.612  7.891   10.303  1.00 17.74 ? 460 PHE A CA  1 
ATOM   3894 C C   . PHE A 1 460 ? -3.043  7.383   10.465  1.00 24.13 ? 460 PHE A C   1 
ATOM   3895 O O   . PHE A 1 460 ? -3.287  6.173   10.419  1.00 24.01 ? 460 PHE A O   1 
ATOM   3896 C CB  . PHE A 1 460 ? -0.615  6.810   10.745  1.00 23.24 ? 460 PHE A CB  1 
ATOM   3897 C CG  . PHE A 1 460 ? 0.822   7.223   10.613  1.00 30.34 ? 460 PHE A CG  1 
ATOM   3898 C CD1 . PHE A 1 460 ? 1.371   7.461   9.369   1.00 31.05 ? 460 PHE A CD1 1 
ATOM   3899 C CD2 . PHE A 1 460 ? 1.621   7.372   11.734  1.00 40.58 ? 460 PHE A CD2 1 
ATOM   3900 C CE1 . PHE A 1 460 ? 2.688   7.845   9.236   1.00 38.18 ? 460 PHE A CE1 1 
ATOM   3901 C CE2 . PHE A 1 460 ? 2.941   7.755   11.610  1.00 42.13 ? 460 PHE A CE2 1 
ATOM   3902 C CZ  . PHE A 1 460 ? 3.475   7.993   10.358  1.00 40.62 ? 460 PHE A CZ  1 
ATOM   3903 N N   . VAL A 1 461 ? -4.007  8.295   10.644  1.00 27.27 ? 461 VAL A N   1 
ATOM   3904 C CA  . VAL A 1 461 ? -5.395  7.869   10.813  1.00 32.14 ? 461 VAL A CA  1 
ATOM   3905 C C   . VAL A 1 461 ? -5.862  7.019   9.642   1.00 30.86 ? 461 VAL A C   1 
ATOM   3906 O O   . VAL A 1 461 ? -6.675  6.101   9.819   1.00 29.56 ? 461 VAL A O   1 
ATOM   3907 C CB  . VAL A 1 461 ? -6.329  9.079   11.011  1.00 32.98 ? 461 VAL A CB  1 
ATOM   3908 C CG1 . VAL A 1 461 ? -6.147  9.634   12.389  1.00 38.86 ? 461 VAL A CG1 1 
ATOM   3909 C CG2 . VAL A 1 461 ? -6.079  10.147  9.942   1.00 35.71 ? 461 VAL A CG2 1 
ATOM   3910 N N   . GLU A 1 462 ? -5.377  7.303   8.428   1.00 21.17 ? 462 GLU A N   1 
ATOM   3911 C CA  . GLU A 1 462 ? -5.814  6.497   7.292   1.00 29.57 ? 462 GLU A CA  1 
ATOM   3912 C C   . GLU A 1 462 ? -5.390  5.045   7.450   1.00 20.28 ? 462 GLU A C   1 
ATOM   3913 O O   . GLU A 1 462 ? -6.079  4.143   6.958   1.00 22.58 ? 462 GLU A O   1 
ATOM   3914 C CB  . GLU A 1 462 ? -5.266  7.061   5.982   1.00 36.91 ? 462 GLU A CB  1 
ATOM   3915 C CG  . GLU A 1 462 ? -5.356  8.556   5.888   1.00 44.81 ? 462 GLU A CG  1 
ATOM   3916 C CD  . GLU A 1 462 ? -5.503  9.028   4.466   1.00 55.00 ? 462 GLU A CD  1 
ATOM   3917 O OE1 . GLU A 1 462 ? -4.766  8.527   3.586   1.00 58.40 ? 462 GLU A OE1 1 
ATOM   3918 O OE2 . GLU A 1 462 ? -6.363  9.899   4.234   1.00 55.62 ? 462 GLU A OE2 1 
ATOM   3919 N N   . VAL A 1 463 ? -4.263  4.801   8.128   1.00 17.97 ? 463 VAL A N   1 
ATOM   3920 C CA  . VAL A 1 463 ? -3.798  3.429   8.331   1.00 16.23 ? 463 VAL A CA  1 
ATOM   3921 C C   . VAL A 1 463 ? -4.717  2.695   9.304   1.00 21.82 ? 463 VAL A C   1 
ATOM   3922 O O   . VAL A 1 463 ? -5.105  1.544   9.074   1.00 19.56 ? 463 VAL A O   1 
ATOM   3923 C CB  . VAL A 1 463 ? -2.338  3.424   8.827   1.00 20.29 ? 463 VAL A CB  1 
ATOM   3924 C CG1 . VAL A 1 463 ? -1.880  2.003   9.144   1.00 22.18 ? 463 VAL A CG1 1 
ATOM   3925 C CG2 . VAL A 1 463 ? -1.408  4.061   7.804   1.00 18.26 ? 463 VAL A CG2 1 
ATOM   3926 N N   . PHE A 1 464 ? -5.046  3.337   10.426  1.00 14.56 ? 464 PHE A N   1 
ATOM   3927 C CA  . PHE A 1 464 ? -6.005  2.757   11.358  1.00 19.34 ? 464 PHE A CA  1 
ATOM   3928 C C   . PHE A 1 464 ? -7.347  2.500   10.682  1.00 16.75 ? 464 PHE A C   1 
ATOM   3929 O O   . PHE A 1 464 ? -7.974  1.457   10.902  1.00 20.46 ? 464 PHE A O   1 
ATOM   3930 C CB  . PHE A 1 464 ? -6.173  3.681   12.563  1.00 18.00 ? 464 PHE A CB  1 
ATOM   3931 C CG  . PHE A 1 464 ? -5.020  3.637   13.513  1.00 15.41 ? 464 PHE A CG  1 
ATOM   3932 C CD1 . PHE A 1 464 ? -4.971  2.680   14.509  1.00 24.23 ? 464 PHE A CD1 1 
ATOM   3933 C CD2 . PHE A 1 464 ? -3.974  4.533   13.400  1.00 20.91 ? 464 PHE A CD2 1 
ATOM   3934 C CE1 . PHE A 1 464 ? -3.895  2.628   15.394  1.00 25.66 ? 464 PHE A CE1 1 
ATOM   3935 C CE2 . PHE A 1 464 ? -2.895  4.491   14.291  1.00 24.19 ? 464 PHE A CE2 1 
ATOM   3936 C CZ  . PHE A 1 464 ? -2.860  3.538   15.283  1.00 24.18 ? 464 PHE A CZ  1 
ATOM   3937 N N   . ASP A 1 465 ? -7.802  3.435   9.846   1.00 19.71 ? 465 ASP A N   1 
ATOM   3938 C CA  . ASP A 1 465 ? -9.045  3.221   9.109   1.00 19.42 ? 465 ASP A CA  1 
ATOM   3939 C C   . ASP A 1 465 ? -8.936  2.008   8.189   1.00 17.80 ? 465 ASP A C   1 
ATOM   3940 O O   . ASP A 1 465 ? -9.840  1.161   8.149   1.00 20.63 ? 465 ASP A O   1 
ATOM   3941 C CB  . ASP A 1 465 ? -9.407  4.483   8.319   1.00 18.62 ? 465 ASP A CB  1 
ATOM   3942 C CG  . ASP A 1 465 ? -10.651 4.301   7.460   1.00 23.53 ? 465 ASP A CG  1 
ATOM   3943 O OD1 . ASP A 1 465 ? -11.760 4.155   8.019   1.00 19.66 ? 465 ASP A OD1 1 
ATOM   3944 O OD2 . ASP A 1 465 ? -10.508 4.302   6.221   1.00 18.81 ? 465 ASP A OD2 1 
ATOM   3945 N N   . LYS A 1 466 ? -7.820  1.901   7.454   1.00 16.30 ? 466 LYS A N   1 
ATOM   3946 C CA  . LYS A 1 466 ? -7.596  0.749   6.583   1.00 19.63 ? 466 LYS A CA  1 
ATOM   3947 C C   . LYS A 1 466 ? -7.579  -0.552  7.368   1.00 21.01 ? 466 LYS A C   1 
ATOM   3948 O O   . LYS A 1 466 ? -8.192  -1.545  6.958   1.00 20.20 ? 466 LYS A O   1 
ATOM   3949 C CB  . LYS A 1 466 ? -6.280  0.908   5.818   1.00 20.09 ? 466 LYS A CB  1 
ATOM   3950 C CG  . LYS A 1 466 ? -5.848  -0.372  5.102   1.00 17.93 ? 466 LYS A CG  1 
ATOM   3951 C CD  . LYS A 1 466 ? -4.759  -0.092  4.082   1.00 28.97 ? 466 LYS A CD  1 
ATOM   3952 C CE  . LYS A 1 466 ? -4.277  -1.382  3.437   1.00 41.21 ? 466 LYS A CE  1 
ATOM   3953 N NZ  . LYS A 1 466 ? -3.681  -1.124  2.098   1.00 46.10 ? 466 LYS A NZ  1 
ATOM   3954 N N   . LEU A 1 467 ? -6.871  -0.573  8.498   1.00 17.26 ? 467 LEU A N   1 
ATOM   3955 C CA  . LEU A 1 467 ? -6.797  -1.793  9.288   1.00 13.47 ? 467 LEU A CA  1 
ATOM   3956 C C   . LEU A 1 467 ? -8.178  -2.211  9.782   1.00 16.47 ? 467 LEU A C   1 
ATOM   3957 O O   . LEU A 1 467 ? -8.575  -3.370  9.640   1.00 19.29 ? 467 LEU A O   1 
ATOM   3958 C CB  . LEU A 1 467 ? -5.836  -1.588  10.465  1.00 13.80 ? 467 LEU A CB  1 
ATOM   3959 C CG  . LEU A 1 467 ? -4.344  -1.558  10.102  1.00 14.29 ? 467 LEU A CG  1 
ATOM   3960 C CD1 . LEU A 1 467 ? -3.496  -0.927  11.232  1.00 14.51 ? 467 LEU A CD1 1 
ATOM   3961 C CD2 . LEU A 1 467 ? -3.857  -2.966  9.766   1.00 18.19 ? 467 LEU A CD2 1 
ATOM   3962 N N   . PHE A 1 468 ? -8.931  -1.270  10.359  1.00 15.59 ? 468 PHE A N   1 
ATOM   3963 C CA  . PHE A 1 468 ? -10.242 -1.609  10.900  1.00 18.06 ? 468 PHE A CA  1 
ATOM   3964 C C   . PHE A 1 468 ? -11.129 -2.213  9.819   1.00 21.41 ? 468 PHE A C   1 
ATOM   3965 O O   . PHE A 1 468 ? -11.759 -3.256  10.023  1.00 17.50 ? 468 PHE A O   1 
ATOM   3966 C CB  . PHE A 1 468 ? -10.904 -0.369  11.509  1.00 16.35 ? 468 PHE A CB  1 
ATOM   3967 C CG  . PHE A 1 468 ? -12.362 -0.561  11.839  1.00 20.88 ? 468 PHE A CG  1 
ATOM   3968 C CD1 . PHE A 1 468 ? -12.744 -1.268  12.971  1.00 21.46 ? 468 PHE A CD1 1 
ATOM   3969 C CD2 . PHE A 1 468 ? -13.349 -0.042  11.016  1.00 20.86 ? 468 PHE A CD2 1 
ATOM   3970 C CE1 . PHE A 1 468 ? -14.080 -1.449  13.282  1.00 22.27 ? 468 PHE A CE1 1 
ATOM   3971 C CE2 . PHE A 1 468 ? -14.690 -0.230  11.311  1.00 25.17 ? 468 PHE A CE2 1 
ATOM   3972 C CZ  . PHE A 1 468 ? -15.059 -0.934  12.446  1.00 21.19 ? 468 PHE A CZ  1 
ATOM   3973 N N   . ARG A 1 469 ? -11.175 -1.571  8.653   1.00 15.27 ? 469 ARG A N   1 
ATOM   3974 C CA  . ARG A 1 469 ? -12.075 -2.024  7.597   1.00 18.48 ? 469 ARG A CA  1 
ATOM   3975 C C   . ARG A 1 469 ? -11.623 -3.355  7.015   1.00 25.01 ? 469 ARG A C   1 
ATOM   3976 O O   . ARG A 1 469 ? -12.466 -4.185  6.649   1.00 21.81 ? 469 ARG A O   1 
ATOM   3977 C CB  . ARG A 1 469 ? -12.184 -0.950  6.513   1.00 23.66 ? 469 ARG A CB  1 
ATOM   3978 C CG  . ARG A 1 469 ? -12.918 0.298   6.997   1.00 22.30 ? 469 ARG A CG  1 
ATOM   3979 C CD  . ARG A 1 469 ? -12.965 1.395   5.953   1.00 23.32 ? 469 ARG A CD  1 
ATOM   3980 N NE  . ARG A 1 469 ? -13.667 2.596   6.418   1.00 22.73 ? 469 ARG A NE  1 
ATOM   3981 C CZ  . ARG A 1 469 ? -14.980 2.770   6.322   1.00 23.61 ? 469 ARG A CZ  1 
ATOM   3982 N NH1 . ARG A 1 469 ? -15.733 1.813   5.805   1.00 19.11 ? 469 ARG A NH1 1 
ATOM   3983 N NH2 . ARG A 1 469 ? -15.545 3.892   6.738   1.00 26.62 ? 469 ARG A NH2 1 
ATOM   3984 N N   . SER A 1 470 ? -10.309 -3.582  6.953   1.00 20.19 ? 470 SER A N   1 
ATOM   3985 C CA  . SER A 1 470 ? -9.787  -4.873  6.513   1.00 17.98 ? 470 SER A CA  1 
ATOM   3986 C C   . SER A 1 470 ? -10.214 -5.993  7.449   1.00 22.64 ? 470 SER A C   1 
ATOM   3987 O O   . SER A 1 470 ? -10.591 -7.081  6.998   1.00 18.60 ? 470 SER A O   1 
ATOM   3988 C CB  . SER A 1 470 ? -8.264  -4.822  6.425   1.00 23.11 ? 470 SER A CB  1 
ATOM   3989 O OG  . SER A 1 470 ? -7.827  -3.817  5.533   1.00 27.71 ? 470 SER A OG  1 
ATOM   3990 N N   . PHE A 1 471 ? -10.118 -5.762  8.764   1.00 22.02 ? 471 PHE A N   1 
ATOM   3991 C CA  . PHE A 1 471 ? -10.551 -6.781  9.714   1.00 21.29 ? 471 PHE A CA  1 
ATOM   3992 C C   . PHE A 1 471 ? -12.056 -7.029  9.603   1.00 22.37 ? 471 PHE A C   1 
ATOM   3993 O O   . PHE A 1 471 ? -12.505 -8.181  9.635   1.00 23.29 ? 471 PHE A O   1 
ATOM   3994 C CB  . PHE A 1 471 ? -10.163 -6.374  11.141  1.00 15.18 ? 471 PHE A CB  1 
ATOM   3995 C CG  . PHE A 1 471 ? -8.662  -6.236  11.358  1.00 15.39 ? 471 PHE A CG  1 
ATOM   3996 C CD1 . PHE A 1 471 ? -7.785  -7.199  10.892  1.00 17.00 ? 471 PHE A CD1 1 
ATOM   3997 C CD2 . PHE A 1 471 ? -8.140  -5.134  12.027  1.00 21.61 ? 471 PHE A CD2 1 
ATOM   3998 C CE1 . PHE A 1 471 ? -6.413  -7.078  11.096  1.00 19.41 ? 471 PHE A CE1 1 
ATOM   3999 C CE2 . PHE A 1 471 ? -6.772  -4.995  12.228  1.00 16.96 ? 471 PHE A CE2 1 
ATOM   4000 C CZ  . PHE A 1 471 ? -5.905  -5.971  11.763  1.00 22.26 ? 471 PHE A CZ  1 
ATOM   4001 N N   . VAL A 1 472 ? -12.843 -5.958  9.453   1.00 18.43 ? 472 VAL A N   1 
ATOM   4002 C CA  . VAL A 1 472 ? -14.293 -6.087  9.283   1.00 18.81 ? 472 VAL A CA  1 
ATOM   4003 C C   . VAL A 1 472 ? -14.617 -6.915  8.042   1.00 20.02 ? 472 VAL A C   1 
ATOM   4004 O O   . VAL A 1 472 ? -15.479 -7.806  8.067   1.00 21.22 ? 472 VAL A O   1 
ATOM   4005 C CB  . VAL A 1 472 ? -14.943 -4.695  9.213   1.00 21.35 ? 472 VAL A CB  1 
ATOM   4006 C CG1 . VAL A 1 472 ? -16.358 -4.793  8.667   1.00 27.05 ? 472 VAL A CG1 1 
ATOM   4007 C CG2 . VAL A 1 472 ? -14.929 -4.026  10.608  1.00 18.66 ? 472 VAL A CG2 1 
ATOM   4008 N N   . ARG A 1 473 ? -13.933 -6.624  6.935   1.00 26.87 ? 473 ARG A N   1 
ATOM   4009 C CA  . ARG A 1 473 ? -14.152 -7.382  5.706   1.00 27.35 ? 473 ARG A CA  1 
ATOM   4010 C C   . ARG A 1 473 ? -13.692 -8.828  5.868   1.00 27.72 ? 473 ARG A C   1 
ATOM   4011 O O   . ARG A 1 473 ? -14.428 -9.766  5.539   1.00 27.08 ? 473 ARG A O   1 
ATOM   4012 C CB  . ARG A 1 473 ? -13.424 -6.698  4.548   1.00 22.34 ? 473 ARG A CB  1 
ATOM   4013 C CG  . ARG A 1 473 ? -13.450 -7.476  3.234   1.00 32.44 ? 473 ARG A CG  1 
ATOM   4014 C CD  . ARG A 1 473 ? -12.963 -6.621  2.078   1.00 41.24 ? 473 ARG A CD  1 
ATOM   4015 N NE  . ARG A 1 473 ? -13.444 -7.125  0.789   1.00 51.85 ? 473 ARG A NE  1 
ATOM   4016 C CZ  . ARG A 1 473 ? -14.488 -6.626  0.128   1.00 61.29 ? 473 ARG A CZ  1 
ATOM   4017 N NH1 . ARG A 1 473 ? -15.168 -5.604  0.629   1.00 63.72 ? 473 ARG A NH1 1 
ATOM   4018 N NH2 . ARG A 1 473 ? -14.854 -7.150  -1.036  1.00 64.66 ? 473 ARG A NH2 1 
ATOM   4019 N N   . ARG A 1 474 ? -12.482 -9.025  6.402   1.00 25.52 ? 474 ARG A N   1 
ATOM   4020 C CA  . ARG A 1 474 ? -11.960 -10.374 6.609   1.00 23.86 ? 474 ARG A CA  1 
ATOM   4021 C C   . ARG A 1 474 ? -12.883 -11.210 7.489   1.00 31.88 ? 474 ARG A C   1 
ATOM   4022 O O   . ARG A 1 474 ? -13.015 -12.422 7.276   1.00 31.48 ? 474 ARG A O   1 
ATOM   4023 C CB  . ARG A 1 474 ? -10.559 -10.294 7.222   1.00 30.67 ? 474 ARG A CB  1 
ATOM   4024 C CG  . ARG A 1 474 ? -9.835  -11.625 7.343   1.00 36.67 ? 474 ARG A CG  1 
ATOM   4025 C CD  . ARG A 1 474 ? -9.665  -12.292 5.984   1.00 49.08 ? 474 ARG A CD  1 
ATOM   4026 N NE  . ARG A 1 474 ? -9.276  -13.695 6.117   1.00 59.67 ? 474 ARG A NE  1 
ATOM   4027 C CZ  . ARG A 1 474 ? -8.157  -14.214 5.623   1.00 65.66 ? 474 ARG A CZ  1 
ATOM   4028 N NH1 . ARG A 1 474 ? -7.307  -13.448 4.952   1.00 62.76 ? 474 ARG A NH1 1 
ATOM   4029 N NH2 . ARG A 1 474 ? -7.890  -15.503 5.796   1.00 71.11 ? 474 ARG A NH2 1 
ATOM   4030 N N   . ALA A 1 475 ? -13.544 -10.583 8.466   1.00 27.07 ? 475 ALA A N   1 
ATOM   4031 C CA  . ALA A 1 475 ? -14.396 -11.301 9.410   1.00 22.67 ? 475 ALA A CA  1 
ATOM   4032 C C   . ALA A 1 475 ? -15.606 -11.967 8.760   1.00 33.26 ? 475 ALA A C   1 
ATOM   4033 O O   . ALA A 1 475 ? -16.281 -12.755 9.431   1.00 31.72 ? 475 ALA A O   1 
ATOM   4034 C CB  . ALA A 1 475 ? -14.885 -10.356 10.507  1.00 21.36 ? 475 ALA A CB  1 
ATOM   4035 N N   . GLN A 1 476 ? -15.904 -11.680 7.490   1.00 31.61 ? 476 GLN A N   1 
ATOM   4036 C CA  . GLN A 1 476 ? -17.136 -12.160 6.868   1.00 34.61 ? 476 GLN A CA  1 
ATOM   4037 C C   . GLN A 1 476 ? -16.919 -13.105 5.692   1.00 39.02 ? 476 GLN A C   1 
ATOM   4038 O O   . GLN A 1 476 ? -17.896 -13.469 5.031   1.00 45.02 ? 476 GLN A O   1 
ATOM   4039 C CB  . GLN A 1 476 ? -17.985 -10.981 6.384   1.00 33.21 ? 476 GLN A CB  1 
ATOM   4040 C CG  . GLN A 1 476 ? -18.486 -10.049 7.464   1.00 35.99 ? 476 GLN A CG  1 
ATOM   4041 C CD  . GLN A 1 476 ? -18.791 -8.672  6.917   1.00 39.30 ? 476 GLN A CD  1 
ATOM   4042 O OE1 . GLN A 1 476 ? -19.869 -8.430  6.372   1.00 37.85 ? 476 GLN A OE1 1 
ATOM   4043 N NE2 . GLN A 1 476 ? -17.840 -7.760  7.049   1.00 36.05 ? 476 GLN A NE2 1 
ATOM   4044 N N   . GLU A 1 477 ? -15.692 -13.515 5.397   1.00 41.06 ? 477 GLU A N   1 
ATOM   4045 C CA  . GLU A 1 477 ? -15.444 -14.078 4.068   1.00 52.83 ? 477 GLU A CA  1 
ATOM   4046 C C   . GLU A 1 477 ? -14.738 -15.427 4.016   1.00 60.37 ? 477 GLU A C   1 
ATOM   4047 O O   . GLU A 1 477 ? -15.278 -16.451 4.420   1.00 63.35 ? 477 GLU A O   1 
ATOM   4048 C CB  . GLU A 1 477 ? -14.621 -13.098 3.255   1.00 52.12 ? 477 GLU A CB  1 
ATOM   4049 C CG  . GLU A 1 477 ? -13.161 -13.255 3.533   1.00 52.29 ? 477 GLU A CG  1 
ATOM   4050 C CD  . GLU A 1 477 ? -12.342 -12.299 2.736   1.00 49.54 ? 477 GLU A CD  1 
ATOM   4051 O OE1 . GLU A 1 477 ? -12.932 -11.415 2.080   1.00 45.57 ? 477 GLU A OE1 1 
ATOM   4052 O OE2 . GLU A 1 477 ? -11.109 -12.443 2.768   1.00 58.77 ? 477 GLU A OE2 1 
ATOM   4053 N N   . MET B 1 1   ? 27.121  -19.371 33.582  1.00 65.23 ? 1   MET B N   1 
ATOM   4054 C CA  . MET B 1 1   ? 26.289  -19.008 34.722  1.00 62.24 ? 1   MET B CA  1 
ATOM   4055 C C   . MET B 1 1   ? 27.150  -18.863 35.974  1.00 52.52 ? 1   MET B C   1 
ATOM   4056 O O   . MET B 1 1   ? 27.342  -19.827 36.716  1.00 48.75 ? 1   MET B O   1 
ATOM   4057 C CB  . MET B 1 1   ? 25.192  -20.059 34.934  1.00 69.88 ? 1   MET B CB  1 
ATOM   4058 C CG  . MET B 1 1   ? 24.230  -19.790 36.099  1.00 78.63 ? 1   MET B CG  1 
ATOM   4059 S SD  . MET B 1 1   ? 23.426  -18.169 36.069  1.00 87.82 ? 1   MET B SD  1 
ATOM   4060 C CE  . MET B 1 1   ? 21.774  -18.578 36.637  1.00 84.77 ? 1   MET B CE  1 
ATOM   4061 N N   . LYS B 1 2   ? 27.679  -17.659 36.199  1.00 41.99 ? 2   LYS B N   1 
ATOM   4062 C CA  . LYS B 1 2   ? 28.555  -17.413 37.340  1.00 33.01 ? 2   LYS B CA  1 
ATOM   4063 C C   . LYS B 1 2   ? 27.718  -17.145 38.583  1.00 27.04 ? 2   LYS B C   1 
ATOM   4064 O O   . LYS B 1 2   ? 27.021  -16.129 38.667  1.00 29.56 ? 2   LYS B O   1 
ATOM   4065 C CB  . LYS B 1 2   ? 29.496  -16.243 37.065  1.00 34.41 ? 2   LYS B CB  1 
ATOM   4066 C CG  . LYS B 1 2   ? 30.486  -15.982 38.202  1.00 38.41 ? 2   LYS B CG  1 
ATOM   4067 C CD  . LYS B 1 2   ? 31.224  -14.647 38.042  1.00 41.43 ? 2   LYS B CD  1 
ATOM   4068 C CE  . LYS B 1 2   ? 30.253  -13.476 37.877  1.00 38.97 ? 2   LYS B CE  1 
ATOM   4069 N NZ  . LYS B 1 2   ? 30.977  -12.187 37.699  1.00 35.75 ? 2   LYS B NZ  1 
ATOM   4070 N N   . LYS B 1 3   ? 27.812  -18.036 39.558  1.00 22.26 ? 3   LYS B N   1 
ATOM   4071 C CA  . LYS B 1 3   ? 27.075  -17.913 40.805  1.00 14.80 ? 3   LYS B CA  1 
ATOM   4072 C C   . LYS B 1 3   ? 27.947  -17.314 41.906  1.00 14.93 ? 3   LYS B C   1 
ATOM   4073 O O   . LYS B 1 3   ? 29.182  -17.366 41.868  1.00 13.04 ? 3   LYS B O   1 
ATOM   4074 C CB  . LYS B 1 3   ? 26.562  -19.281 41.259  1.00 17.84 ? 3   LYS B CB  1 
ATOM   4075 C CG  . LYS B 1 3   ? 25.704  -19.978 40.235  1.00 23.44 ? 3   LYS B CG  1 
ATOM   4076 C CD  . LYS B 1 3   ? 24.626  -19.050 39.737  1.00 32.30 ? 3   LYS B CD  1 
ATOM   4077 C CE  . LYS B 1 3   ? 23.339  -19.818 39.564  1.00 39.86 ? 3   LYS B CE  1 
ATOM   4078 N NZ  . LYS B 1 3   ? 23.572  -21.274 39.543  1.00 40.32 ? 3   LYS B NZ  1 
ATOM   4079 N N   . LEU B 1 4   ? 27.276  -16.739 42.895  1.00 14.39 ? 4   LEU B N   1 
ATOM   4080 C CA  . LEU B 1 4   ? 27.867  -16.470 44.201  1.00 8.00  ? 4   LEU B CA  1 
ATOM   4081 C C   . LEU B 1 4   ? 27.381  -17.547 45.167  1.00 10.97 ? 4   LEU B C   1 
ATOM   4082 O O   . LEU B 1 4   ? 26.177  -17.812 45.253  1.00 16.85 ? 4   LEU B O   1 
ATOM   4083 C CB  . LEU B 1 4   ? 27.482  -15.072 44.683  1.00 12.30 ? 4   LEU B CB  1 
ATOM   4084 C CG  . LEU B 1 4   ? 27.991  -14.607 46.050  1.00 12.38 ? 4   LEU B CG  1 
ATOM   4085 C CD1 . LEU B 1 4   ? 28.140  -13.110 46.048  1.00 14.98 ? 4   LEU B CD1 1 
ATOM   4086 C CD2 . LEU B 1 4   ? 27.037  -15.029 47.161  1.00 15.01 ? 4   LEU B CD2 1 
ATOM   4087 N N   . PHE B 1 5   ? 28.315  -18.193 45.858  1.00 11.60 ? 5   PHE B N   1 
ATOM   4088 C CA  . PHE B 1 5   ? 27.976  -19.236 46.818  1.00 13.56 ? 5   PHE B CA  1 
ATOM   4089 C C   . PHE B 1 5   ? 27.886  -18.623 48.206  1.00 16.02 ? 5   PHE B C   1 
ATOM   4090 O O   . PHE B 1 5   ? 28.843  -18.006 48.670  1.00 13.22 ? 5   PHE B O   1 
ATOM   4091 C CB  . PHE B 1 5   ? 29.025  -20.339 46.780  1.00 12.84 ? 5   PHE B CB  1 
ATOM   4092 C CG  . PHE B 1 5   ? 29.050  -21.084 45.486  1.00 14.81 ? 5   PHE B CG  1 
ATOM   4093 C CD1 . PHE B 1 5   ? 27.891  -21.654 44.983  1.00 21.40 ? 5   PHE B CD1 1 
ATOM   4094 C CD2 . PHE B 1 5   ? 30.226  -21.195 44.756  1.00 12.93 ? 5   PHE B CD2 1 
ATOM   4095 C CE1 . PHE B 1 5   ? 27.904  -22.347 43.774  1.00 18.73 ? 5   PHE B CE1 1 
ATOM   4096 C CE2 . PHE B 1 5   ? 30.243  -21.884 43.551  1.00 15.21 ? 5   PHE B CE2 1 
ATOM   4097 C CZ  . PHE B 1 5   ? 29.086  -22.461 43.063  1.00 14.15 ? 5   PHE B CZ  1 
ATOM   4098 N N   . LEU B 1 6   ? 26.742  -18.789 48.869  1.00 13.33 ? 6   LEU B N   1 
ATOM   4099 C CA  . LEU B 1 6   ? 26.504  -18.157 50.160  1.00 11.41 ? 6   LEU B CA  1 
ATOM   4100 C C   . LEU B 1 6   ? 26.309  -19.243 51.211  1.00 15.48 ? 6   LEU B C   1 
ATOM   4101 O O   . LEU B 1 6   ? 25.565  -20.204 50.984  1.00 13.47 ? 6   LEU B O   1 
ATOM   4102 C CB  . LEU B 1 6   ? 25.285  -17.211 50.089  1.00 11.69 ? 6   LEU B CB  1 
ATOM   4103 C CG  . LEU B 1 6   ? 24.846  -16.436 51.339  1.00 10.79 ? 6   LEU B CG  1 
ATOM   4104 C CD1 . LEU B 1 6   ? 25.906  -15.432 51.818  1.00 8.79  ? 6   LEU B CD1 1 
ATOM   4105 C CD2 . LEU B 1 6   ? 23.522  -15.716 51.098  1.00 13.15 ? 6   LEU B CD2 1 
ATOM   4106 N N   . VAL B 1 7   ? 26.985  -19.107 52.350  1.00 10.92 ? 7   VAL B N   1 
ATOM   4107 C CA  . VAL B 1 7   ? 27.009  -20.166 53.364  1.00 11.82 ? 7   VAL B CA  1 
ATOM   4108 C C   . VAL B 1 7   ? 26.710  -19.521 54.713  1.00 13.65 ? 7   VAL B C   1 
ATOM   4109 O O   . VAL B 1 7   ? 27.579  -18.851 55.284  1.00 12.54 ? 7   VAL B O   1 
ATOM   4110 C CB  . VAL B 1 7   ? 28.353  -20.913 53.406  1.00 12.75 ? 7   VAL B CB  1 
ATOM   4111 C CG1 . VAL B 1 7   ? 28.246  -22.175 54.261  1.00 11.48 ? 7   VAL B CG1 1 
ATOM   4112 C CG2 . VAL B 1 7   ? 28.827  -21.277 51.988  1.00 14.33 ? 7   VAL B CG2 1 
ATOM   4113 N N   . PHE B 1 8   ? 25.490  -19.724 55.225  1.00 9.47  ? 8   PHE B N   1 
ATOM   4114 C CA  . PHE B 1 8   ? 25.143  -19.285 56.580  1.00 4.33  ? 8   PHE B CA  1 
ATOM   4115 C C   . PHE B 1 8   ? 25.568  -20.355 57.581  1.00 8.87  ? 8   PHE B C   1 
ATOM   4116 O O   . PHE B 1 8   ? 25.278  -21.536 57.383  1.00 10.35 ? 8   PHE B O   1 
ATOM   4117 C CB  . PHE B 1 8   ? 23.627  -19.044 56.711  1.00 8.45  ? 8   PHE B CB  1 
ATOM   4118 C CG  . PHE B 1 8   ? 23.139  -17.806 56.024  1.00 8.27  ? 8   PHE B CG  1 
ATOM   4119 C CD1 . PHE B 1 8   ? 23.174  -16.583 56.661  1.00 10.83 ? 8   PHE B CD1 1 
ATOM   4120 C CD2 . PHE B 1 8   ? 22.642  -17.869 54.723  1.00 10.50 ? 8   PHE B CD2 1 
ATOM   4121 C CE1 . PHE B 1 8   ? 22.715  -15.429 56.023  1.00 7.88  ? 8   PHE B CE1 1 
ATOM   4122 C CE2 . PHE B 1 8   ? 22.191  -16.726 54.076  1.00 12.50 ? 8   PHE B CE2 1 
ATOM   4123 C CZ  . PHE B 1 8   ? 22.240  -15.496 54.726  1.00 7.51  ? 8   PHE B CZ  1 
ATOM   4124 N N   . TRP B 1 9   ? 26.242  -19.950 58.658  1.00 7.93  ? 9   TRP B N   1 
ATOM   4125 C CA  . TRP B 1 9   ? 26.618  -20.873 59.735  1.00 14.69 ? 9   TRP B CA  1 
ATOM   4126 C C   . TRP B 1 9   ? 26.264  -20.209 61.065  1.00 8.33  ? 9   TRP B C   1 
ATOM   4127 O O   . TRP B 1 9   ? 26.976  -19.312 61.522  1.00 7.31  ? 9   TRP B O   1 
ATOM   4128 C CB  . TRP B 1 9   ? 28.106  -21.223 59.634  1.00 12.20 ? 9   TRP B CB  1 
ATOM   4129 C CG  . TRP B 1 9   ? 28.561  -22.440 60.370  1.00 9.54  ? 9   TRP B CG  1 
ATOM   4130 C CD1 . TRP B 1 9   ? 27.851  -23.202 61.259  1.00 12.43 ? 9   TRP B CD1 1 
ATOM   4131 C CD2 . TRP B 1 9   ? 29.861  -23.026 60.291  1.00 9.65  ? 9   TRP B CD2 1 
ATOM   4132 N NE1 . TRP B 1 9   ? 28.632  -24.224 61.733  1.00 9.12  ? 9   TRP B NE1 1 
ATOM   4133 C CE2 . TRP B 1 9   ? 29.875  -24.137 61.158  1.00 6.46  ? 9   TRP B CE2 1 
ATOM   4134 C CE3 . TRP B 1 9   ? 31.022  -22.712 59.572  1.00 13.44 ? 9   TRP B CE3 1 
ATOM   4135 C CZ2 . TRP B 1 9   ? 30.996  -24.944 61.318  1.00 12.68 ? 9   TRP B CZ2 1 
ATOM   4136 C CZ3 . TRP B 1 9   ? 32.134  -23.520 59.726  1.00 7.64  ? 9   TRP B CZ3 1 
ATOM   4137 C CH2 . TRP B 1 9   ? 32.116  -24.618 60.601  1.00 9.08  ? 9   TRP B CH2 1 
ATOM   4138 N N   . TRP B 1 10  ? 25.141  -20.632 61.658  1.00 5.94  ? 10  TRP B N   1 
ATOM   4139 C CA  . TRP B 1 10  ? 24.592  -20.076 62.886  1.00 4.88  ? 10  TRP B CA  1 
ATOM   4140 C C   . TRP B 1 10  ? 25.127  -20.861 64.077  1.00 5.48  ? 10  TRP B C   1 
ATOM   4141 O O   . TRP B 1 10  ? 24.865  -22.068 64.189  1.00 11.31 ? 10  TRP B O   1 
ATOM   4142 C CB  . TRP B 1 10  ? 23.060  -20.165 62.870  1.00 3.76  ? 10  TRP B CB  1 
ATOM   4143 C CG  . TRP B 1 10  ? 22.384  -19.455 61.728  1.00 9.25  ? 10  TRP B CG  1 
ATOM   4144 C CD1 . TRP B 1 10  ? 21.685  -20.029 60.692  1.00 12.13 ? 10  TRP B CD1 1 
ATOM   4145 C CD2 . TRP B 1 10  ? 22.324  -18.038 61.514  1.00 6.02  ? 10  TRP B CD2 1 
ATOM   4146 N NE1 . TRP B 1 10  ? 21.187  -19.045 59.856  1.00 9.38  ? 10  TRP B NE1 1 
ATOM   4147 C CE2 . TRP B 1 10  ? 21.565  -17.820 60.339  1.00 6.38  ? 10  TRP B CE2 1 
ATOM   4148 C CE3 . TRP B 1 10  ? 22.824  -16.928 62.209  1.00 8.01  ? 10  TRP B CE3 1 
ATOM   4149 C CZ2 . TRP B 1 10  ? 21.304  -16.542 59.846  1.00 5.80  ? 10  TRP B CZ2 1 
ATOM   4150 C CZ3 . TRP B 1 10  ? 22.570  -15.662 61.711  1.00 12.49 ? 10  TRP B CZ3 1 
ATOM   4151 C CH2 . TRP B 1 10  ? 21.820  -15.478 60.537  1.00 9.56  ? 10  TRP B CH2 1 
ATOM   4152 N N   . HIS B 1 11  ? 25.832  -20.177 64.982  1.00 8.25  ? 11  HIS B N   1 
ATOM   4153 C CA  . HIS B 1 11  ? 26.518  -20.823 66.103  1.00 6.81  ? 11  HIS B CA  1 
ATOM   4154 C C   . HIS B 1 11  ? 25.654  -20.712 67.357  1.00 6.95  ? 11  HIS B C   1 
ATOM   4155 O O   . HIS B 1 11  ? 25.303  -19.604 67.762  1.00 6.34  ? 11  HIS B O   1 
ATOM   4156 C CB  . HIS B 1 11  ? 27.884  -20.172 66.334  1.00 9.87  ? 11  HIS B CB  1 
ATOM   4157 C CG  . HIS B 1 11  ? 28.444  -20.436 67.691  1.00 8.06  ? 11  HIS B CG  1 
ATOM   4158 N ND1 . HIS B 1 11  ? 28.767  -21.706 68.120  1.00 6.63  ? 11  HIS B ND1 1 
ATOM   4159 C CD2 . HIS B 1 11  ? 28.686  -19.609 68.736  1.00 4.09  ? 11  HIS B CD2 1 
ATOM   4160 C CE1 . HIS B 1 11  ? 29.227  -21.644 69.361  1.00 8.96  ? 11  HIS B CE1 1 
ATOM   4161 N NE2 . HIS B 1 11  ? 29.188  -20.383 69.759  1.00 4.41  ? 11  HIS B NE2 1 
ATOM   4162 N N   . MET B 1 12  ? 25.322  -21.853 67.973  1.00 6.69  ? 12  MET B N   1 
ATOM   4163 C CA  . MET B 1 12  ? 24.429  -21.909 69.130  1.00 7.59  ? 12  MET B CA  1 
ATOM   4164 C C   . MET B 1 12  ? 25.179  -22.409 70.352  1.00 6.42  ? 12  MET B C   1 
ATOM   4165 O O   . MET B 1 12  ? 25.750  -23.503 70.329  1.00 8.19  ? 12  MET B O   1 
ATOM   4166 C CB  . MET B 1 12  ? 23.231  -22.837 68.900  1.00 7.24  ? 12  MET B CB  1 
ATOM   4167 C CG  . MET B 1 12  ? 22.465  -22.603 67.613  1.00 5.35  ? 12  MET B CG  1 
ATOM   4168 S SD  . MET B 1 12  ? 21.852  -20.920 67.477  1.00 8.42  ? 12  MET B SD  1 
ATOM   4169 C CE  . MET B 1 12  ? 20.671  -21.152 66.150  1.00 11.50 ? 12  MET B CE  1 
ATOM   4170 N N   . HIS B 1 13  ? 25.121  -21.649 71.441  1.00 6.04  ? 13  HIS B N   1 
ATOM   4171 C CA  . HIS B 1 13  ? 25.896  -22.068 72.597  1.00 7.46  ? 13  HIS B CA  1 
ATOM   4172 C C   . HIS B 1 13  ? 25.367  -21.392 73.849  1.00 7.60  ? 13  HIS B C   1 
ATOM   4173 O O   . HIS B 1 13  ? 24.954  -20.233 73.801  1.00 7.63  ? 13  HIS B O   1 
ATOM   4174 C CB  . HIS B 1 13  ? 27.386  -21.730 72.398  1.00 6.51  ? 13  HIS B CB  1 
ATOM   4175 C CG  . HIS B 1 13  ? 28.198  -21.859 73.649  1.00 8.49  ? 13  HIS B CG  1 
ATOM   4176 N ND1 . HIS B 1 13  ? 28.329  -23.053 74.326  1.00 6.96  ? 13  HIS B ND1 1 
ATOM   4177 C CD2 . HIS B 1 13  ? 28.896  -20.941 74.364  1.00 7.80  ? 13  HIS B CD2 1 
ATOM   4178 C CE1 . HIS B 1 13  ? 29.079  -22.871 75.397  1.00 5.75  ? 13  HIS B CE1 1 
ATOM   4179 N NE2 . HIS B 1 13  ? 29.447  -21.600 75.440  1.00 9.51  ? 13  HIS B NE2 1 
ATOM   4180 N N   . GLN B 1 14  ? 25.390  -22.123 74.966  1.00 6.56  ? 14  GLN B N   1 
ATOM   4181 C CA  . GLN B 1 14  ? 25.287  -21.534 76.295  1.00 7.86  ? 14  GLN B CA  1 
ATOM   4182 C C   . GLN B 1 14  ? 26.233  -22.275 77.225  1.00 11.77 ? 14  GLN B C   1 
ATOM   4183 O O   . GLN B 1 14  ? 26.313  -23.513 77.160  1.00 6.55  ? 14  GLN B O   1 
ATOM   4184 C CB  . GLN B 1 14  ? 23.874  -21.619 76.883  1.00 4.81  ? 14  GLN B CB  1 
ATOM   4185 C CG  . GLN B 1 14  ? 22.821  -20.915 76.087  1.00 6.34  ? 14  GLN B CG  1 
ATOM   4186 C CD  . GLN B 1 14  ? 22.919  -19.404 76.225  1.00 9.69  ? 14  GLN B CD  1 
ATOM   4187 O OE1 . GLN B 1 14  ? 23.475  -18.877 77.200  1.00 15.11 ? 14  GLN B OE1 1 
ATOM   4188 N NE2 . GLN B 1 14  ? 22.379  -18.702 75.247  1.00 12.90 ? 14  GLN B NE2 1 
ATOM   4189 N N   . PRO B 1 15  ? 26.917  -21.565 78.121  1.00 10.36 ? 15  PRO B N   1 
ATOM   4190 C CA  . PRO B 1 15  ? 27.700  -22.242 79.157  1.00 6.90  ? 15  PRO B CA  1 
ATOM   4191 C C   . PRO B 1 15  ? 26.780  -22.956 80.131  1.00 12.73 ? 15  PRO B C   1 
ATOM   4192 O O   . PRO B 1 15  ? 25.571  -22.750 80.155  1.00 10.85 ? 15  PRO B O   1 
ATOM   4193 C CB  . PRO B 1 15  ? 28.445  -21.094 79.842  1.00 9.07  ? 15  PRO B CB  1 
ATOM   4194 C CG  . PRO B 1 15  ? 27.469  -19.976 79.794  1.00 7.86  ? 15  PRO B CG  1 
ATOM   4195 C CD  . PRO B 1 15  ? 26.796  -20.109 78.399  1.00 4.88  ? 15  PRO B CD  1 
ATOM   4196 N N   . LEU B 1 16  ? 27.375  -23.790 80.973  1.00 10.44 ? 16  LEU B N   1 
ATOM   4197 C CA  . LEU B 1 16  ? 26.583  -24.638 81.856  1.00 10.20 ? 16  LEU B CA  1 
ATOM   4198 C C   . LEU B 1 16  ? 26.049  -23.809 83.021  1.00 10.55 ? 16  LEU B C   1 
ATOM   4199 O O   . LEU B 1 16  ? 26.813  -23.407 83.898  1.00 9.57  ? 16  LEU B O   1 
ATOM   4200 C CB  . LEU B 1 16  ? 27.423  -25.811 82.357  1.00 7.06  ? 16  LEU B CB  1 
ATOM   4201 C CG  . LEU B 1 16  ? 26.601  -26.789 83.211  1.00 7.55  ? 16  LEU B CG  1 
ATOM   4202 C CD1 . LEU B 1 16  ? 25.419  -27.363 82.406  1.00 7.87  ? 16  LEU B CD1 1 
ATOM   4203 C CD2 . LEU B 1 16  ? 27.494  -27.885 83.773  1.00 12.49 ? 16  LEU B CD2 1 
ATOM   4204 N N   . TYR B 1 17  ? 24.726  -23.584 83.053  1.00 8.32  ? 17  TYR B N   1 
ATOM   4205 C CA  . TYR B 1 17  ? 24.108  -22.780 84.107  1.00 7.93  ? 17  TYR B CA  1 
ATOM   4206 C C   . TYR B 1 17  ? 23.761  -23.612 85.328  1.00 12.54 ? 17  TYR B C   1 
ATOM   4207 O O   . TYR B 1 17  ? 23.287  -23.058 86.326  1.00 10.17 ? 17  TYR B O   1 
ATOM   4208 C CB  . TYR B 1 17  ? 22.842  -22.073 83.580  1.00 7.27  ? 17  TYR B CB  1 
ATOM   4209 C CG  . TYR B 1 17  ? 23.136  -21.028 82.524  1.00 8.20  ? 17  TYR B CG  1 
ATOM   4210 C CD1 . TYR B 1 17  ? 23.988  -19.962 82.799  1.00 6.36  ? 17  TYR B CD1 1 
ATOM   4211 C CD2 . TYR B 1 17  ? 22.595  -21.127 81.241  1.00 10.58 ? 17  TYR B CD2 1 
ATOM   4212 C CE1 . TYR B 1 17  ? 24.277  -18.995 81.834  1.00 7.03  ? 17  TYR B CE1 1 
ATOM   4213 C CE2 . TYR B 1 17  ? 22.891  -20.173 80.256  1.00 8.26  ? 17  TYR B CE2 1 
ATOM   4214 C CZ  . TYR B 1 17  ? 23.727  -19.118 80.563  1.00 9.14  ? 17  TYR B CZ  1 
ATOM   4215 O OH  . TYR B 1 17  ? 24.010  -18.191 79.591  1.00 10.18 ? 17  TYR B OH  1 
ATOM   4216 N N   . ARG B 1 18  ? 23.991  -24.920 85.258  1.00 4.08  ? 18  ARG B N   1 
ATOM   4217 C CA  . ARG B 1 18  ? 23.576  -25.860 86.291  1.00 5.62  ? 18  ARG B CA  1 
ATOM   4218 C C   . ARG B 1 18  ? 24.630  -25.907 87.398  1.00 8.14  ? 18  ARG B C   1 
ATOM   4219 O O   . ARG B 1 18  ? 25.737  -26.425 87.201  1.00 11.97 ? 18  ARG B O   1 
ATOM   4220 C CB  . ARG B 1 18  ? 23.356  -27.238 85.671  1.00 8.39  ? 18  ARG B CB  1 
ATOM   4221 C CG  . ARG B 1 18  ? 22.711  -28.252 86.627  1.00 14.04 ? 18  ARG B CG  1 
ATOM   4222 C CD  . ARG B 1 18  ? 22.744  -29.654 86.000  1.00 18.14 ? 18  ARG B CD  1 
ATOM   4223 N NE  . ARG B 1 18  ? 22.050  -30.657 86.803  1.00 22.52 ? 18  ARG B NE  1 
ATOM   4224 C CZ  . ARG B 1 18  ? 22.588  -31.317 87.825  1.00 27.24 ? 18  ARG B CZ  1 
ATOM   4225 N NH1 . ARG B 1 18  ? 23.848  -31.101 88.184  1.00 25.73 ? 18  ARG B NH1 1 
ATOM   4226 N NH2 . ARG B 1 18  ? 21.866  -32.209 88.489  1.00 32.36 ? 18  ARG B NH2 1 
ATOM   4227 N N   . GLU B 1 19  ? 24.283  -25.379 88.560  1.00 7.41  ? 19  GLU B N   1 
ATOM   4228 C CA  . GLU B 1 19  ? 25.189  -25.379 89.703  1.00 7.68  ? 19  GLU B CA  1 
ATOM   4229 C C   . GLU B 1 19  ? 25.422  -26.821 90.164  1.00 12.84 ? 19  GLU B C   1 
ATOM   4230 O O   . GLU B 1 19  ? 24.457  -27.569 90.328  1.00 14.38 ? 19  GLU B O   1 
ATOM   4231 C CB  . GLU B 1 19  ? 24.564  -24.550 90.822  1.00 13.22 ? 19  GLU B CB  1 
ATOM   4232 C CG  . GLU B 1 19  ? 25.536  -23.806 91.704  1.00 24.91 ? 19  GLU B CG  1 
ATOM   4233 C CD  . GLU B 1 19  ? 25.937  -24.609 92.922  1.00 28.88 ? 19  GLU B CD  1 
ATOM   4234 O OE1 . GLU B 1 19  ? 25.288  -25.637 93.203  1.00 26.19 ? 19  GLU B OE1 1 
ATOM   4235 O OE2 . GLU B 1 19  ? 26.908  -24.214 93.593  1.00 36.57 ? 19  GLU B OE2 1 
ATOM   4236 N N   . PRO B 1 20  ? 26.677  -27.264 90.334  1.00 11.79 ? 20  PRO B N   1 
ATOM   4237 C CA  . PRO B 1 20  ? 26.924  -28.707 90.450  1.00 14.85 ? 20  PRO B CA  1 
ATOM   4238 C C   . PRO B 1 20  ? 26.527  -29.304 91.785  1.00 21.35 ? 20  PRO B C   1 
ATOM   4239 O O   . PRO B 1 20  ? 26.384  -30.529 91.870  1.00 27.23 ? 20  PRO B O   1 
ATOM   4240 C CB  . PRO B 1 20  ? 28.448  -28.827 90.250  1.00 12.29 ? 20  PRO B CB  1 
ATOM   4241 C CG  . PRO B 1 20  ? 28.979  -27.526 90.749  1.00 16.32 ? 20  PRO B CG  1 
ATOM   4242 C CD  . PRO B 1 20  ? 27.930  -26.485 90.388  1.00 11.68 ? 20  PRO B CD  1 
ATOM   4243 N N   . TYR B 1 21  ? 26.368  -28.496 92.825  1.00 12.89 ? 21  TYR B N   1 
ATOM   4244 C CA  . TYR B 1 21  ? 25.996  -29.037 94.126  1.00 16.44 ? 21  TYR B CA  1 
ATOM   4245 C C   . TYR B 1 21  ? 24.484  -29.123 94.309  1.00 17.99 ? 21  TYR B C   1 
ATOM   4246 O O   . TYR B 1 21  ? 23.984  -30.138 94.808  1.00 22.84 ? 21  TYR B O   1 
ATOM   4247 C CB  . TYR B 1 21  ? 26.625  -28.194 95.232  1.00 15.54 ? 21  TYR B CB  1 
ATOM   4248 C CG  . TYR B 1 21  ? 28.131  -28.334 95.272  1.00 24.11 ? 21  TYR B CG  1 
ATOM   4249 C CD1 . TYR B 1 21  ? 28.733  -29.353 96.008  1.00 25.44 ? 21  TYR B CD1 1 
ATOM   4250 C CD2 . TYR B 1 21  ? 28.953  -27.474 94.544  1.00 20.07 ? 21  TYR B CD2 1 
ATOM   4251 C CE1 . TYR B 1 21  ? 30.108  -29.503 96.041  1.00 21.51 ? 21  TYR B CE1 1 
ATOM   4252 C CE2 . TYR B 1 21  ? 30.337  -27.615 94.577  1.00 20.57 ? 21  TYR B CE2 1 
ATOM   4253 C CZ  . TYR B 1 21  ? 30.905  -28.630 95.327  1.00 22.23 ? 21  TYR B CZ  1 
ATOM   4254 O OH  . TYR B 1 21  ? 32.278  -28.776 95.359  1.00 20.41 ? 21  TYR B OH  1 
ATOM   4255 N N   . THR B 1 22  ? 23.734  -28.097 93.896  1.00 15.61 ? 22  THR B N   1 
ATOM   4256 C CA  . THR B 1 22  ? 22.280  -28.134 94.028  1.00 18.17 ? 22  THR B CA  1 
ATOM   4257 C C   . THR B 1 22  ? 21.581  -28.677 92.791  1.00 21.91 ? 22  THR B C   1 
ATOM   4258 O O   . THR B 1 22  ? 20.424  -29.101 92.886  1.00 17.32 ? 22  THR B O   1 
ATOM   4259 C CB  . THR B 1 22  ? 21.720  -26.734 94.318  1.00 20.31 ? 22  THR B CB  1 
ATOM   4260 O OG1 . THR B 1 22  ? 21.992  -25.867 93.205  1.00 16.17 ? 22  THR B OG1 1 
ATOM   4261 C CG2 . THR B 1 22  ? 22.342  -26.139 95.589  1.00 20.02 ? 22  THR B CG2 1 
ATOM   4262 N N   . GLY B 1 23  ? 22.242  -28.673 91.641  1.00 18.40 ? 23  GLY B N   1 
ATOM   4263 C CA  . GLY B 1 23  ? 21.569  -29.008 90.402  1.00 15.05 ? 23  GLY B CA  1 
ATOM   4264 C C   . GLY B 1 23  ? 20.693  -27.908 89.840  1.00 18.25 ? 23  GLY B C   1 
ATOM   4265 O O   . GLY B 1 23  ? 19.974  -28.145 88.862  1.00 23.26 ? 23  GLY B O   1 
ATOM   4266 N N   . GLU B 1 24  ? 20.715  -26.711 90.419  1.00 11.06 ? 24  GLU B N   1 
ATOM   4267 C CA  . GLU B 1 24  ? 19.801  -25.650 90.002  1.00 8.22  ? 24  GLU B CA  1 
ATOM   4268 C C   . GLU B 1 24  ? 20.389  -24.862 88.838  1.00 11.77 ? 24  GLU B C   1 
ATOM   4269 O O   . GLU B 1 24  ? 21.562  -24.485 88.871  1.00 9.99  ? 24  GLU B O   1 
ATOM   4270 C CB  . GLU B 1 24  ? 19.509  -24.711 91.165  1.00 12.06 ? 24  GLU B CB  1 
ATOM   4271 C CG  . GLU B 1 24  ? 18.682  -25.392 92.253  1.00 15.54 ? 24  GLU B CG  1 
ATOM   4272 C CD  . GLU B 1 24  ? 18.516  -24.540 93.477  1.00 25.47 ? 24  GLU B CD  1 
ATOM   4273 O OE1 . GLU B 1 24  ? 17.708  -24.916 94.354  1.00 37.67 ? 24  GLU B OE1 1 
ATOM   4274 O OE2 . GLU B 1 24  ? 19.197  -23.497 93.568  1.00 27.05 ? 24  GLU B OE2 1 
ATOM   4275 N N   . TYR B 1 25  ? 19.575  -24.617 87.814  1.00 7.52  ? 25  TYR B N   1 
ATOM   4276 C CA  . TYR B 1 25  ? 19.967  -23.701 86.749  1.00 7.94  ? 25  TYR B CA  1 
ATOM   4277 C C   . TYR B 1 25  ? 19.812  -22.277 87.277  1.00 11.13 ? 25  TYR B C   1 
ATOM   4278 O O   . TYR B 1 25  ? 18.699  -21.821 87.544  1.00 10.41 ? 25  TYR B O   1 
ATOM   4279 C CB  . TYR B 1 25  ? 19.127  -23.927 85.496  1.00 11.99 ? 25  TYR B CB  1 
ATOM   4280 C CG  . TYR B 1 25  ? 19.585  -25.107 84.675  1.00 10.41 ? 25  TYR B CG  1 
ATOM   4281 C CD1 . TYR B 1 25  ? 19.397  -26.414 85.120  1.00 10.31 ? 25  TYR B CD1 1 
ATOM   4282 C CD2 . TYR B 1 25  ? 20.217  -24.915 83.453  1.00 7.22  ? 25  TYR B CD2 1 
ATOM   4283 C CE1 . TYR B 1 25  ? 19.834  -27.497 84.358  1.00 13.36 ? 25  TYR B CE1 1 
ATOM   4284 C CE2 . TYR B 1 25  ? 20.630  -25.969 82.697  1.00 10.15 ? 25  TYR B CE2 1 
ATOM   4285 C CZ  . TYR B 1 25  ? 20.447  -27.259 83.142  1.00 13.10 ? 25  TYR B CZ  1 
ATOM   4286 O OH  . TYR B 1 25  ? 20.886  -28.299 82.346  1.00 11.64 ? 25  TYR B OH  1 
ATOM   4287 N N   . LEU B 1 26  ? 20.932  -21.577 87.443  1.00 10.27 ? 26  LEU B N   1 
ATOM   4288 C CA  . LEU B 1 26  ? 20.905  -20.305 88.149  1.00 13.52 ? 26  LEU B CA  1 
ATOM   4289 C C   . LEU B 1 26  ? 20.517  -19.130 87.267  1.00 15.83 ? 26  LEU B C   1 
ATOM   4290 O O   . LEU B 1 26  ? 20.220  -18.063 87.807  1.00 10.58 ? 26  LEU B O   1 
ATOM   4291 C CB  . LEU B 1 26  ? 22.259  -20.029 88.801  1.00 11.08 ? 26  LEU B CB  1 
ATOM   4292 C CG  . LEU B 1 26  ? 22.634  -21.033 89.903  1.00 16.28 ? 26  LEU B CG  1 
ATOM   4293 C CD1 . LEU B 1 26  ? 24.027  -20.728 90.490  1.00 19.22 ? 26  LEU B CD1 1 
ATOM   4294 C CD2 . LEU B 1 26  ? 21.563  -21.101 90.991  1.00 14.36 ? 26  LEU B CD2 1 
ATOM   4295 N N   . LEU B 1 27  ? 20.546  -19.288 85.946  1.00 8.01  ? 27  LEU B N   1 
ATOM   4296 C CA  . LEU B 1 27  ? 20.038  -18.309 85.002  1.00 9.44  ? 27  LEU B CA  1 
ATOM   4297 C C   . LEU B 1 27  ? 19.174  -19.033 83.984  1.00 14.40 ? 27  LEU B C   1 
ATOM   4298 O O   . LEU B 1 27  ? 19.371  -20.229 83.736  1.00 13.39 ? 27  LEU B O   1 
ATOM   4299 C CB  . LEU B 1 27  ? 21.176  -17.562 84.282  1.00 8.57  ? 27  LEU B CB  1 
ATOM   4300 C CG  . LEU B 1 27  ? 22.069  -16.696 85.179  1.00 18.02 ? 27  LEU B CG  1 
ATOM   4301 C CD1 . LEU B 1 27  ? 23.293  -16.231 84.410  1.00 16.89 ? 27  LEU B CD1 1 
ATOM   4302 C CD2 . LEU B 1 27  ? 21.314  -15.511 85.734  1.00 19.21 ? 27  LEU B CD2 1 
ATOM   4303 N N   . PRO B 1 28  ? 18.178  -18.346 83.412  1.00 11.91 ? 28  PRO B N   1 
ATOM   4304 C CA  . PRO B 1 28  ? 17.244  -19.003 82.488  1.00 10.24 ? 28  PRO B CA  1 
ATOM   4305 C C   . PRO B 1 28  ? 17.608  -18.883 81.011  1.00 4.08  ? 28  PRO B C   1 
ATOM   4306 O O   . PRO B 1 28  ? 16.753  -19.164 80.172  1.00 5.81  ? 28  PRO B O   1 
ATOM   4307 C CB  . PRO B 1 28  ? 15.938  -18.246 82.767  1.00 12.65 ? 28  PRO B CB  1 
ATOM   4308 C CG  . PRO B 1 28  ? 16.422  -16.856 83.024  1.00 8.56  ? 28  PRO B CG  1 
ATOM   4309 C CD  . PRO B 1 28  ? 17.724  -16.990 83.792  1.00 10.44 ? 28  PRO B CD  1 
ATOM   4310 N N   . TRP B 1 29  ? 18.836  -18.490 80.682  1.00 9.74  ? 29  TRP B N   1 
ATOM   4311 C CA  . TRP B 1 29  ? 19.147  -18.125 79.304  1.00 9.22  ? 29  TRP B CA  1 
ATOM   4312 C C   . TRP B 1 29  ? 19.083  -19.310 78.356  1.00 11.84 ? 29  TRP B C   1 
ATOM   4313 O O   . TRP B 1 29  ? 18.776  -19.126 77.173  1.00 9.55  ? 29  TRP B O   1 
ATOM   4314 C CB  . TRP B 1 29  ? 20.527  -17.480 79.232  1.00 9.77  ? 29  TRP B CB  1 
ATOM   4315 C CG  . TRP B 1 29  ? 20.654  -16.167 79.942  1.00 10.06 ? 29  TRP B CG  1 
ATOM   4316 C CD1 . TRP B 1 29  ? 21.592  -15.845 80.879  1.00 16.01 ? 29  TRP B CD1 1 
ATOM   4317 C CD2 . TRP B 1 29  ? 19.853  -14.986 79.756  1.00 14.75 ? 29  TRP B CD2 1 
ATOM   4318 N NE1 . TRP B 1 29  ? 21.431  -14.541 81.288  1.00 17.09 ? 29  TRP B NE1 1 
ATOM   4319 C CE2 . TRP B 1 29  ? 20.368  -13.993 80.621  1.00 15.46 ? 29  TRP B CE2 1 
ATOM   4320 C CE3 . TRP B 1 29  ? 18.760  -14.669 78.941  1.00 16.00 ? 29  TRP B CE3 1 
ATOM   4321 C CZ2 . TRP B 1 29  ? 19.823  -12.719 80.702  1.00 15.84 ? 29  TRP B CZ2 1 
ATOM   4322 C CZ3 . TRP B 1 29  ? 18.219  -13.397 79.022  1.00 20.70 ? 29  TRP B CZ3 1 
ATOM   4323 C CH2 . TRP B 1 29  ? 18.755  -12.436 79.892  1.00 16.43 ? 29  TRP B CH2 1 
ATOM   4324 N N   . THR B 1 30  ? 19.374  -20.525 78.839  1.00 9.01  ? 30  THR B N   1 
ATOM   4325 C CA  . THR B 1 30  ? 19.216  -21.689 77.974  1.00 4.80  ? 30  THR B CA  1 
ATOM   4326 C C   . THR B 1 30  ? 17.745  -21.957 77.689  1.00 8.88  ? 30  THR B C   1 
ATOM   4327 O O   . THR B 1 30  ? 17.359  -22.168 76.534  1.00 7.53  ? 30  THR B O   1 
ATOM   4328 C CB  . THR B 1 30  ? 19.888  -22.910 78.586  1.00 10.20 ? 30  THR B CB  1 
ATOM   4329 O OG1 . THR B 1 30  ? 21.302  -22.674 78.646  1.00 10.59 ? 30  THR B OG1 1 
ATOM   4330 C CG2 . THR B 1 30  ? 19.616  -24.147 77.707  1.00 7.88  ? 30  THR B CG2 1 
ATOM   4331 N N   . PHE B 1 31  ? 16.898  -21.927 78.726  1.00 6.79  ? 31  PHE B N   1 
ATOM   4332 C CA  . PHE B 1 31  ? 15.463  -22.081 78.484  1.00 4.00  ? 31  PHE B CA  1 
ATOM   4333 C C   . PHE B 1 31  ? 14.965  -21.030 77.502  1.00 5.42  ? 31  PHE B C   1 
ATOM   4334 O O   . PHE B 1 31  ? 14.259  -21.339 76.531  1.00 5.78  ? 31  PHE B O   1 
ATOM   4335 C CB  . PHE B 1 31  ? 14.699  -21.983 79.805  1.00 5.89  ? 31  PHE B CB  1 
ATOM   4336 C CG  . PHE B 1 31  ? 13.219  -21.963 79.624  1.00 10.88 ? 31  PHE B CG  1 
ATOM   4337 C CD1 . PHE B 1 31  ? 12.538  -23.147 79.381  1.00 10.48 ? 31  PHE B CD1 1 
ATOM   4338 C CD2 . PHE B 1 31  ? 12.510  -20.765 79.661  1.00 10.18 ? 31  PHE B CD2 1 
ATOM   4339 C CE1 . PHE B 1 31  ? 11.165  -23.152 79.206  1.00 10.66 ? 31  PHE B CE1 1 
ATOM   4340 C CE2 . PHE B 1 31  ? 11.125  -20.762 79.475  1.00 11.97 ? 31  PHE B CE2 1 
ATOM   4341 C CZ  . PHE B 1 31  ? 10.460  -21.957 79.243  1.00 10.19 ? 31  PHE B CZ  1 
ATOM   4342 N N   . PHE B 1 32  ? 15.301  -19.763 77.751  1.00 4.06  ? 32  PHE B N   1 
ATOM   4343 C CA  . PHE B 1 32  ? 14.716  -18.707 76.937  1.00 7.55  ? 32  PHE B CA  1 
ATOM   4344 C C   . PHE B 1 32  ? 15.205  -18.774 75.497  1.00 8.92  ? 32  PHE B C   1 
ATOM   4345 O O   . PHE B 1 32  ? 14.429  -18.526 74.568  1.00 7.58  ? 32  PHE B O   1 
ATOM   4346 C CB  . PHE B 1 32  ? 15.008  -17.342 77.569  1.00 6.91  ? 32  PHE B CB  1 
ATOM   4347 C CG  . PHE B 1 32  ? 14.066  -16.991 78.681  1.00 7.58  ? 32  PHE B CG  1 
ATOM   4348 C CD1 . PHE B 1 32  ? 12.708  -17.262 78.560  1.00 9.33  ? 32  PHE B CD1 1 
ATOM   4349 C CD2 . PHE B 1 32  ? 14.530  -16.396 79.857  1.00 10.94 ? 32  PHE B CD2 1 
ATOM   4350 C CE1 . PHE B 1 32  ? 11.827  -16.947 79.588  1.00 6.42  ? 32  PHE B CE1 1 
ATOM   4351 C CE2 . PHE B 1 32  ? 13.659  -16.076 80.885  1.00 11.06 ? 32  PHE B CE2 1 
ATOM   4352 C CZ  . PHE B 1 32  ? 12.307  -16.350 80.758  1.00 7.13  ? 32  PHE B CZ  1 
ATOM   4353 N N   . HIS B 1 33  ? 16.491  -19.093 75.281  1.00 4.41  ? 33  HIS B N   1 
ATOM   4354 C CA  . HIS B 1 33  ? 16.956  -19.196 73.907  1.00 5.49  ? 33  HIS B CA  1 
ATOM   4355 C C   . HIS B 1 33  ? 16.505  -20.489 73.250  1.00 6.93  ? 33  HIS B C   1 
ATOM   4356 O O   . HIS B 1 33  ? 16.395  -20.539 72.019  1.00 6.46  ? 33  HIS B O   1 
ATOM   4357 C CB  . HIS B 1 33  ? 18.484  -19.027 73.852  1.00 3.72  ? 33  HIS B CB  1 
ATOM   4358 C CG  . HIS B 1 33  ? 18.911  -17.592 74.008  1.00 6.40  ? 33  HIS B CG  1 
ATOM   4359 N ND1 . HIS B 1 33  ? 18.589  -16.626 73.081  1.00 7.74  ? 33  HIS B ND1 1 
ATOM   4360 C CD2 . HIS B 1 33  ? 19.571  -16.950 75.004  1.00 8.60  ? 33  HIS B CD2 1 
ATOM   4361 C CE1 . HIS B 1 33  ? 19.059  -15.455 73.480  1.00 8.42  ? 33  HIS B CE1 1 
ATOM   4362 N NE2 . HIS B 1 33  ? 19.662  -15.625 74.644  1.00 10.29 ? 33  HIS B NE2 1 
ATOM   4363 N N   . ALA B 1 34  ? 16.215  -21.526 74.042  1.00 6.65  ? 34  ALA B N   1 
ATOM   4364 C CA  . ALA B 1 34  ? 15.623  -22.726 73.467  1.00 9.48  ? 34  ALA B CA  1 
ATOM   4365 C C   . ALA B 1 34  ? 14.231  -22.421 72.920  1.00 9.64  ? 34  ALA B C   1 
ATOM   4366 O O   . ALA B 1 34  ? 13.920  -22.737 71.763  1.00 12.52 ? 34  ALA B O   1 
ATOM   4367 C CB  . ALA B 1 34  ? 15.571  -23.843 74.512  1.00 6.22  ? 34  ALA B CB  1 
ATOM   4368 N N   . VAL B 1 35  ? 13.388  -21.766 73.722  1.00 8.22  ? 35  VAL B N   1 
ATOM   4369 C CA  . VAL B 1 35  ? 12.022  -21.555 73.250  1.00 5.60  ? 35  VAL B CA  1 
ATOM   4370 C C   . VAL B 1 35  ? 11.954  -20.482 72.181  1.00 12.18 ? 35  VAL B C   1 
ATOM   4371 O O   . VAL B 1 35  ? 11.025  -20.494 71.365  1.00 9.32  ? 35  VAL B O   1 
ATOM   4372 C CB  . VAL B 1 35  ? 11.059  -21.233 74.413  1.00 6.05  ? 35  VAL B CB  1 
ATOM   4373 C CG1 . VAL B 1 35  ? 11.143  -22.355 75.505  1.00 4.13  ? 35  VAL B CG1 1 
ATOM   4374 C CG2 . VAL B 1 35  ? 11.369  -19.849 75.025  1.00 8.95  ? 35  VAL B CG2 1 
ATOM   4375 N N   . LYS B 1 36  ? 12.928  -19.572 72.138  1.00 6.52  ? 36  LYS B N   1 
ATOM   4376 C CA  . LYS B 1 36  ? 12.883  -18.472 71.181  1.00 8.98  ? 36  LYS B CA  1 
ATOM   4377 C C   . LYS B 1 36  ? 13.662  -18.759 69.903  1.00 12.87 ? 36  LYS B C   1 
ATOM   4378 O O   . LYS B 1 36  ? 13.219  -18.367 68.817  1.00 10.32 ? 36  LYS B O   1 
ATOM   4379 C CB  . LYS B 1 36  ? 13.432  -17.199 71.830  1.00 7.18  ? 36  LYS B CB  1 
ATOM   4380 C CG  . LYS B 1 36  ? 13.206  -15.913 70.988  1.00 8.41  ? 36  LYS B CG  1 
ATOM   4381 C CD  . LYS B 1 36  ? 13.604  -14.654 71.751  1.00 11.06 ? 36  LYS B CD  1 
ATOM   4382 C CE  . LYS B 1 36  ? 15.101  -14.354 71.682  1.00 12.84 ? 36  LYS B CE  1 
ATOM   4383 N NZ  . LYS B 1 36  ? 15.617  -14.158 70.275  1.00 7.05  ? 36  LYS B NZ  1 
ATOM   4384 N N   . ASP B 1 37  ? 14.835  -19.397 70.005  1.00 8.08  ? 37  ASP B N   1 
ATOM   4385 C CA  . ASP B 1 37  ? 15.742  -19.471 68.853  1.00 9.78  ? 37  ASP B CA  1 
ATOM   4386 C C   . ASP B 1 37  ? 16.179  -20.880 68.458  1.00 13.50 ? 37  ASP B C   1 
ATOM   4387 O O   . ASP B 1 37  ? 16.362  -21.144 67.262  1.00 8.56  ? 37  ASP B O   1 
ATOM   4388 C CB  . ASP B 1 37  ? 17.017  -18.631 69.130  1.00 10.31 ? 37  ASP B CB  1 
ATOM   4389 C CG  . ASP B 1 37  ? 16.704  -17.251 69.669  1.00 12.05 ? 37  ASP B CG  1 
ATOM   4390 O OD1 . ASP B 1 37  ? 16.161  -16.424 68.900  1.00 9.45  ? 37  ASP B OD1 1 
ATOM   4391 O OD2 . ASP B 1 37  ? 16.982  -16.999 70.864  1.00 7.52  ? 37  ASP B OD2 1 
ATOM   4392 N N   . TYR B 1 38  ? 16.414  -21.779 69.417  1.00 8.69  ? 38  TYR B N   1 
ATOM   4393 C CA  . TYR B 1 38  ? 17.122  -23.013 69.047  1.00 8.36  ? 38  TYR B CA  1 
ATOM   4394 C C   . TYR B 1 38  ? 16.256  -23.954 68.208  1.00 6.20  ? 38  TYR B C   1 
ATOM   4395 O O   . TYR B 1 38  ? 16.790  -24.711 67.383  1.00 9.60  ? 38  TYR B O   1 
ATOM   4396 C CB  . TYR B 1 38  ? 17.671  -23.722 70.293  1.00 8.79  ? 38  TYR B CB  1 
ATOM   4397 C CG  . TYR B 1 38  ? 18.750  -22.926 70.993  1.00 12.16 ? 38  TYR B CG  1 
ATOM   4398 C CD1 . TYR B 1 38  ? 19.619  -22.094 70.268  1.00 10.38 ? 38  TYR B CD1 1 
ATOM   4399 C CD2 . TYR B 1 38  ? 18.892  -22.972 72.376  1.00 5.80  ? 38  TYR B CD2 1 
ATOM   4400 C CE1 . TYR B 1 38  ? 20.613  -21.356 70.911  1.00 11.19 ? 38  TYR B CE1 1 
ATOM   4401 C CE2 . TYR B 1 38  ? 19.879  -22.228 73.028  1.00 10.94 ? 38  TYR B CE2 1 
ATOM   4402 C CZ  . TYR B 1 38  ? 20.732  -21.424 72.294  1.00 8.04  ? 38  TYR B CZ  1 
ATOM   4403 O OH  . TYR B 1 38  ? 21.728  -20.688 72.928  1.00 9.65  ? 38  TYR B OH  1 
ATOM   4404 N N   . TYR B 1 39  ? 14.931  -23.929 68.389  1.00 6.93  ? 39  TYR B N   1 
ATOM   4405 C CA  . TYR B 1 39  ? 14.050  -24.620 67.448  1.00 10.50 ? 39  TYR B CA  1 
ATOM   4406 C C   . TYR B 1 39  ? 13.736  -23.754 66.237  1.00 9.27  ? 39  TYR B C   1 
ATOM   4407 O O   . TYR B 1 39  ? 13.739  -24.239 65.101  1.00 7.15  ? 39  TYR B O   1 
ATOM   4408 C CB  . TYR B 1 39  ? 12.739  -25.038 68.136  1.00 4.53  ? 39  TYR B CB  1 
ATOM   4409 C CG  . TYR B 1 39  ? 11.699  -25.638 67.194  1.00 7.09  ? 39  TYR B CG  1 
ATOM   4410 C CD1 . TYR B 1 39  ? 11.751  -26.985 66.846  1.00 10.84 ? 39  TYR B CD1 1 
ATOM   4411 C CD2 . TYR B 1 39  ? 10.669  -24.865 66.661  1.00 12.39 ? 39  TYR B CD2 1 
ATOM   4412 C CE1 . TYR B 1 39  ? 10.825  -27.539 65.991  1.00 12.14 ? 39  TYR B CE1 1 
ATOM   4413 C CE2 . TYR B 1 39  ? 9.732   -25.422 65.782  1.00 11.00 ? 39  TYR B CE2 1 
ATOM   4414 C CZ  . TYR B 1 39  ? 9.821   -26.764 65.474  1.00 11.50 ? 39  TYR B CZ  1 
ATOM   4415 O OH  . TYR B 1 39  ? 8.916   -27.341 64.629  1.00 14.32 ? 39  TYR B OH  1 
ATOM   4416 N N   . ASP B 1 40  ? 13.491  -22.466 66.450  1.00 7.09  ? 40  ASP B N   1 
ATOM   4417 C CA  . ASP B 1 40  ? 12.922  -21.678 65.371  1.00 5.80  ? 40  ASP B CA  1 
ATOM   4418 C C   . ASP B 1 40  ? 13.933  -21.331 64.291  1.00 9.93  ? 40  ASP B C   1 
ATOM   4419 O O   . ASP B 1 40  ? 13.540  -21.188 63.131  1.00 9.91  ? 40  ASP B O   1 
ATOM   4420 C CB  . ASP B 1 40  ? 12.275  -20.420 65.937  1.00 9.54  ? 40  ASP B CB  1 
ATOM   4421 C CG  . ASP B 1 40  ? 10.871  -20.701 66.461  1.00 11.64 ? 40  ASP B CG  1 
ATOM   4422 O OD1 . ASP B 1 40  ? 9.970   -20.960 65.635  1.00 13.09 ? 40  ASP B OD1 1 
ATOM   4423 O OD2 . ASP B 1 40  ? 10.694  -20.718 67.688  1.00 13.36 ? 40  ASP B OD2 1 
ATOM   4424 N N   . MET B 1 41  ? 15.225  -21.216 64.627  1.00 5.96  ? 41  MET B N   1 
ATOM   4425 C CA  . MET B 1 41  ? 16.192  -20.892 63.581  1.00 7.68  ? 41  MET B CA  1 
ATOM   4426 C C   . MET B 1 41  ? 16.248  -21.991 62.528  1.00 8.83  ? 41  MET B C   1 
ATOM   4427 O O   . MET B 1 41  ? 16.033  -21.689 61.345  1.00 8.92  ? 41  MET B O   1 
ATOM   4428 C CB  . MET B 1 41  ? 17.563  -20.589 64.204  1.00 5.22  ? 41  MET B CB  1 
ATOM   4429 C CG  . MET B 1 41  ? 17.640  -19.178 64.835  1.00 3.78  ? 41  MET B CG  1 
ATOM   4430 S SD  . MET B 1 41  ? 17.570  -17.853 63.592  1.00 7.97  ? 41  MET B SD  1 
ATOM   4431 C CE  . MET B 1 41  ? 19.267  -17.889 63.017  1.00 5.51  ? 41  MET B CE  1 
ATOM   4432 N N   . PRO B 1 42  ? 16.475  -23.264 62.867  1.00 11.97 ? 42  PRO B N   1 
ATOM   4433 C CA  . PRO B 1 42  ? 16.345  -24.305 61.833  1.00 9.92  ? 42  PRO B CA  1 
ATOM   4434 C C   . PRO B 1 42  ? 14.935  -24.413 61.255  1.00 10.19 ? 42  PRO B C   1 
ATOM   4435 O O   . PRO B 1 42  ? 14.793  -24.706 60.060  1.00 11.24 ? 42  PRO B O   1 
ATOM   4436 C CB  . PRO B 1 42  ? 16.772  -25.590 62.561  1.00 9.41  ? 42  PRO B CB  1 
ATOM   4437 C CG  . PRO B 1 42  ? 16.609  -25.287 64.029  1.00 10.12 ? 42  PRO B CG  1 
ATOM   4438 C CD  . PRO B 1 42  ? 16.952  -23.816 64.151  1.00 11.62 ? 42  PRO B CD  1 
ATOM   4439 N N   . ALA B 1 43  ? 13.888  -24.133 62.038  1.00 10.10 ? 43  ALA B N   1 
ATOM   4440 C CA  . ALA B 1 43  ? 12.530  -24.295 61.512  1.00 11.51 ? 43  ALA B CA  1 
ATOM   4441 C C   . ALA B 1 43  ? 12.209  -23.353 60.347  1.00 14.40 ? 43  ALA B C   1 
ATOM   4442 O O   . ALA B 1 43  ? 11.219  -23.595 59.642  1.00 9.53  ? 43  ALA B O   1 
ATOM   4443 C CB  . ALA B 1 43  ? 11.484  -24.100 62.623  1.00 10.67 ? 43  ALA B CB  1 
ATOM   4444 N N   . TYR B 1 44  ? 12.999  -22.288 60.122  1.00 9.52  ? 44  TYR B N   1 
ATOM   4445 C CA  . TYR B 1 44  ? 12.820  -21.506 58.894  1.00 6.45  ? 44  TYR B CA  1 
ATOM   4446 C C   . TYR B 1 44  ? 12.957  -22.371 57.646  1.00 11.11 ? 44  TYR B C   1 
ATOM   4447 O O   . TYR B 1 44  ? 12.366  -22.048 56.607  1.00 11.70 ? 44  TYR B O   1 
ATOM   4448 C CB  . TYR B 1 44  ? 13.831  -20.354 58.812  1.00 10.02 ? 44  TYR B CB  1 
ATOM   4449 C CG  . TYR B 1 44  ? 13.475  -19.117 59.610  1.00 8.32  ? 44  TYR B CG  1 
ATOM   4450 C CD1 . TYR B 1 44  ? 13.886  -18.986 60.938  1.00 6.42  ? 44  TYR B CD1 1 
ATOM   4451 C CD2 . TYR B 1 44  ? 12.760  -18.072 59.036  1.00 9.78  ? 44  TYR B CD2 1 
ATOM   4452 C CE1 . TYR B 1 44  ? 13.577  -17.851 61.665  1.00 6.65  ? 44  TYR B CE1 1 
ATOM   4453 C CE2 . TYR B 1 44  ? 12.450  -16.929 59.758  1.00 11.08 ? 44  TYR B CE2 1 
ATOM   4454 C CZ  . TYR B 1 44  ? 12.876  -16.827 61.072  1.00 8.73  ? 44  TYR B CZ  1 
ATOM   4455 O OH  . TYR B 1 44  ? 12.581  -15.711 61.800  1.00 13.05 ? 44  TYR B OH  1 
ATOM   4456 N N   . LEU B 1 45  ? 13.749  -23.455 57.715  1.00 9.28  ? 45  LEU B N   1 
ATOM   4457 C CA  . LEU B 1 45  ? 13.923  -24.348 56.573  1.00 13.74 ? 45  LEU B CA  1 
ATOM   4458 C C   . LEU B 1 45  ? 12.638  -25.092 56.218  1.00 13.26 ? 45  LEU B C   1 
ATOM   4459 O O   . LEU B 1 45  ? 12.558  -25.684 55.136  1.00 13.52 ? 45  LEU B O   1 
ATOM   4460 C CB  . LEU B 1 45  ? 15.040  -25.365 56.855  1.00 9.90  ? 45  LEU B CB  1 
ATOM   4461 C CG  . LEU B 1 45  ? 16.432  -24.730 56.995  1.00 14.73 ? 45  LEU B CG  1 
ATOM   4462 C CD1 . LEU B 1 45  ? 17.462  -25.697 57.530  1.00 10.12 ? 45  LEU B CD1 1 
ATOM   4463 C CD2 . LEU B 1 45  ? 16.889  -24.150 55.648  1.00 13.87 ? 45  LEU B CD2 1 
ATOM   4464 N N   . LYS B 1 46  ? 11.647  -25.107 57.108  1.00 11.66 ? 46  LYS B N   1 
ATOM   4465 C CA  . LYS B 1 46  ? 10.349  -25.673 56.734  1.00 15.25 ? 46  LYS B CA  1 
ATOM   4466 C C   . LYS B 1 46  ? 9.652   -24.827 55.682  1.00 19.45 ? 46  LYS B C   1 
ATOM   4467 O O   . LYS B 1 46  ? 8.872   -25.354 54.882  1.00 20.21 ? 46  LYS B O   1 
ATOM   4468 C CB  . LYS B 1 46  ? 9.446   -25.799 57.956  1.00 18.89 ? 46  LYS B CB  1 
ATOM   4469 C CG  . LYS B 1 46  ? 9.849   -26.903 58.881  1.00 26.81 ? 46  LYS B CG  1 
ATOM   4470 C CD  . LYS B 1 46  ? 8.628   -27.472 59.542  1.00 36.28 ? 46  LYS B CD  1 
ATOM   4471 C CE  . LYS B 1 46  ? 8.851   -27.661 61.015  1.00 34.59 ? 46  LYS B CE  1 
ATOM   4472 N NZ  . LYS B 1 46  ? 7.819   -28.577 61.567  1.00 42.83 ? 46  LYS B NZ  1 
ATOM   4473 N N   . ASP B 1 47  ? 9.931   -23.521 55.662  1.00 16.01 ? 47  ASP B N   1 
ATOM   4474 C CA  . ASP B 1 47  ? 9.195   -22.563 54.857  1.00 19.45 ? 47  ASP B CA  1 
ATOM   4475 C C   . ASP B 1 47  ? 9.983   -21.968 53.706  1.00 19.88 ? 47  ASP B C   1 
ATOM   4476 O O   . ASP B 1 47  ? 9.376   -21.401 52.795  1.00 17.09 ? 47  ASP B O   1 
ATOM   4477 C CB  . ASP B 1 47  ? 8.698   -21.412 55.743  1.00 19.98 ? 47  ASP B CB  1 
ATOM   4478 C CG  . ASP B 1 47  ? 7.730   -21.885 56.811  1.00 32.25 ? 47  ASP B CG  1 
ATOM   4479 O OD1 . ASP B 1 47  ? 6.981   -22.849 56.541  1.00 19.64 ? 47  ASP B OD1 1 
ATOM   4480 O OD2 . ASP B 1 47  ? 7.724   -21.296 57.914  1.00 40.29 ? 47  ASP B OD2 1 
ATOM   4481 N N   . PHE B 1 48  ? 11.307  -22.040 53.736  1.00 15.80 ? 48  PHE B N   1 
ATOM   4482 C CA  . PHE B 1 48  ? 12.128  -21.398 52.720  1.00 13.70 ? 48  PHE B CA  1 
ATOM   4483 C C   . PHE B 1 48  ? 13.067  -22.432 52.128  1.00 17.66 ? 48  PHE B C   1 
ATOM   4484 O O   . PHE B 1 48  ? 13.728  -23.169 52.863  1.00 17.44 ? 48  PHE B O   1 
ATOM   4485 C CB  . PHE B 1 48  ? 12.898  -20.208 53.318  1.00 11.81 ? 48  PHE B CB  1 
ATOM   4486 C CG  . PHE B 1 48  ? 12.004  -19.145 53.851  1.00 18.58 ? 48  PHE B CG  1 
ATOM   4487 C CD1 . PHE B 1 48  ? 11.408  -18.237 52.990  1.00 16.78 ? 48  PHE B CD1 1 
ATOM   4488 C CD2 . PHE B 1 48  ? 11.724  -19.067 55.203  1.00 14.31 ? 48  PHE B CD2 1 
ATOM   4489 C CE1 . PHE B 1 48  ? 10.559  -17.275 53.464  1.00 18.91 ? 48  PHE B CE1 1 
ATOM   4490 C CE2 . PHE B 1 48  ? 10.877  -18.096 55.686  1.00 14.99 ? 48  PHE B CE2 1 
ATOM   4491 C CZ  . PHE B 1 48  ? 10.293  -17.194 54.808  1.00 18.41 ? 48  PHE B CZ  1 
ATOM   4492 N N   . GLU B 1 49  ? 13.107  -22.504 50.797  1.00 15.64 ? 49  GLU B N   1 
ATOM   4493 C CA  . GLU B 1 49  ? 13.924  -23.507 50.114  1.00 22.42 ? 49  GLU B CA  1 
ATOM   4494 C C   . GLU B 1 49  ? 15.341  -22.964 49.934  1.00 21.32 ? 49  GLU B C   1 
ATOM   4495 O O   . GLU B 1 49  ? 15.782  -22.614 48.841  1.00 19.82 ? 49  GLU B O   1 
ATOM   4496 C CB  . GLU B 1 49  ? 13.294  -23.890 48.778  1.00 27.00 ? 49  GLU B CB  1 
ATOM   4497 C CG  . GLU B 1 49  ? 13.375  -25.378 48.441  1.00 41.03 ? 49  GLU B CG  1 
ATOM   4498 C CD  . GLU B 1 49  ? 12.716  -26.269 49.485  1.00 51.66 ? 49  GLU B CD  1 
ATOM   4499 O OE1 . GLU B 1 49  ? 11.648  -25.886 50.009  1.00 54.32 ? 49  GLU B OE1 1 
ATOM   4500 O OE2 . GLU B 1 49  ? 13.263  -27.356 49.782  1.00 54.09 ? 49  GLU B OE2 1 
ATOM   4501 N N   . ILE B 1 50  ? 16.050  -22.865 51.063  1.00 12.49 ? 50  ILE B N   1 
ATOM   4502 C CA  . ILE B 1 50  ? 17.444  -22.443 51.075  1.00 11.67 ? 50  ILE B CA  1 
ATOM   4503 C C   . ILE B 1 50  ? 18.191  -23.411 51.984  1.00 12.07 ? 50  ILE B C   1 
ATOM   4504 O O   . ILE B 1 50  ? 17.585  -24.249 52.652  1.00 13.69 ? 50  ILE B O   1 
ATOM   4505 C CB  . ILE B 1 50  ? 17.605  -20.994 51.558  1.00 21.53 ? 50  ILE B CB  1 
ATOM   4506 C CG1 . ILE B 1 50  ? 16.979  -20.851 52.947  1.00 21.98 ? 50  ILE B CG1 1 
ATOM   4507 C CG2 . ILE B 1 50  ? 16.941  -20.029 50.586  1.00 19.98 ? 50  ILE B CG2 1 
ATOM   4508 C CD1 . ILE B 1 50  ? 17.398  -19.634 53.659  1.00 21.67 ? 50  ILE B CD1 1 
ATOM   4509 N N   . LYS B 1 51  ? 19.522  -23.326 51.954  1.00 10.88 ? 51  LYS B N   1 
ATOM   4510 C CA  . LYS B 1 51  ? 20.382  -24.100 52.842  1.00 11.18 ? 51  LYS B CA  1 
ATOM   4511 C C   . LYS B 1 51  ? 20.832  -23.213 53.997  1.00 9.99  ? 51  LYS B C   1 
ATOM   4512 O O   . LYS B 1 51  ? 21.211  -22.053 53.791  1.00 12.30 ? 51  LYS B O   1 
ATOM   4513 C CB  . LYS B 1 51  ? 21.625  -24.653 52.116  1.00 12.19 ? 51  LYS B CB  1 
ATOM   4514 C CG  . LYS B 1 51  ? 21.344  -25.495 50.860  1.00 18.44 ? 51  LYS B CG  1 
ATOM   4515 C CD  . LYS B 1 51  ? 20.503  -26.722 51.195  1.00 16.51 ? 51  LYS B CD  1 
ATOM   4516 C CE  . LYS B 1 51  ? 20.426  -27.696 50.016  1.00 25.97 ? 51  LYS B CE  1 
ATOM   4517 N NZ  . LYS B 1 51  ? 19.956  -27.021 48.798  1.00 34.69 ? 51  LYS B NZ  1 
ATOM   4518 N N   . LEU B 1 52  ? 20.797  -23.766 55.210  1.00 6.58  ? 52  LEU B N   1 
ATOM   4519 C CA  . LEU B 1 52  ? 21.261  -23.078 56.413  1.00 7.05  ? 52  LEU B CA  1 
ATOM   4520 C C   . LEU B 1 52  ? 21.986  -24.078 57.298  1.00 11.52 ? 52  LEU B C   1 
ATOM   4521 O O   . LEU B 1 52  ? 21.464  -25.171 57.546  1.00 9.66  ? 52  LEU B O   1 
ATOM   4522 C CB  . LEU B 1 52  ? 20.101  -22.455 57.196  1.00 13.37 ? 52  LEU B CB  1 
ATOM   4523 C CG  . LEU B 1 52  ? 19.244  -21.375 56.532  1.00 9.46  ? 52  LEU B CG  1 
ATOM   4524 C CD1 . LEU B 1 52  ? 18.062  -20.977 57.454  1.00 11.46 ? 52  LEU B CD1 1 
ATOM   4525 C CD2 . LEU B 1 52  ? 20.067  -20.153 56.112  1.00 10.60 ? 52  LEU B CD2 1 
ATOM   4526 N N   . ASN B 1 53  ? 23.166  -23.703 57.786  1.00 9.51  ? 53  ASN B N   1 
ATOM   4527 C CA  . ASN B 1 53  ? 23.976  -24.572 58.628  1.00 6.77  ? 53  ASN B CA  1 
ATOM   4528 C C   . ASN B 1 53  ? 24.022  -24.076 60.072  1.00 6.85  ? 53  ASN B C   1 
ATOM   4529 O O   . ASN B 1 53  ? 23.826  -22.889 60.365  1.00 9.37  ? 53  ASN B O   1 
ATOM   4530 C CB  . ASN B 1 53  ? 25.385  -24.686 58.050  1.00 7.99  ? 53  ASN B CB  1 
ATOM   4531 C CG  . ASN B 1 53  ? 25.346  -24.999 56.573  1.00 9.04  ? 53  ASN B CG  1 
ATOM   4532 O OD1 . ASN B 1 53  ? 25.083  -26.140 56.191  1.00 12.17 ? 53  ASN B OD1 1 
ATOM   4533 N ND2 . ASN B 1 53  ? 25.508  -23.973 55.738  1.00 6.61  ? 53  ASN B ND2 1 
ATOM   4534 N N   . PHE B 1 54  ? 24.299  -25.014 60.971  1.00 5.45  ? 54  PHE B N   1 
ATOM   4535 C CA  . PHE B 1 54  ? 24.204  -24.774 62.409  1.00 5.42  ? 54  PHE B CA  1 
ATOM   4536 C C   . PHE B 1 54  ? 25.357  -25.424 63.147  1.00 11.33 ? 54  PHE B C   1 
ATOM   4537 O O   . PHE B 1 54  ? 25.810  -26.507 62.786  1.00 9.48  ? 54  PHE B O   1 
ATOM   4538 C CB  . PHE B 1 54  ? 22.872  -25.303 62.956  1.00 8.32  ? 54  PHE B CB  1 
ATOM   4539 C CG  . PHE B 1 54  ? 21.697  -24.622 62.340  1.00 9.33  ? 54  PHE B CG  1 
ATOM   4540 C CD1 . PHE B 1 54  ? 21.161  -25.083 61.133  1.00 6.85  ? 54  PHE B CD1 1 
ATOM   4541 C CD2 . PHE B 1 54  ? 21.177  -23.474 62.911  1.00 9.95  ? 54  PHE B CD2 1 
ATOM   4542 C CE1 . PHE B 1 54  ? 20.098  -24.436 60.531  1.00 8.14  ? 54  PHE B CE1 1 
ATOM   4543 C CE2 . PHE B 1 54  ? 20.098  -22.831 62.320  1.00 11.00 ? 54  PHE B CE2 1 
ATOM   4544 C CZ  . PHE B 1 54  ? 19.569  -23.310 61.115  1.00 11.54 ? 54  PHE B CZ  1 
ATOM   4545 N N   . ASN B 1 55  ? 25.814  -24.746 64.193  1.00 8.02  ? 55  ASN B N   1 
ATOM   4546 C CA  . ASN B 1 55  ? 26.737  -25.294 65.165  1.00 8.44  ? 55  ASN B CA  1 
ATOM   4547 C C   . ASN B 1 55  ? 26.021  -25.420 66.496  1.00 10.63 ? 55  ASN B C   1 
ATOM   4548 O O   . ASN B 1 55  ? 25.384  -24.467 66.943  1.00 10.82 ? 55  ASN B O   1 
ATOM   4549 C CB  . ASN B 1 55  ? 27.960  -24.392 65.353  1.00 6.05  ? 55  ASN B CB  1 
ATOM   4550 C CG  . ASN B 1 55  ? 29.002  -25.046 66.225  1.00 8.85  ? 55  ASN B CG  1 
ATOM   4551 O OD1 . ASN B 1 55  ? 29.543  -26.077 65.853  1.00 8.06  ? 55  ASN B OD1 1 
ATOM   4552 N ND2 . ASN B 1 55  ? 29.262  -24.477 67.397  1.00 5.65  ? 55  ASN B ND2 1 
ATOM   4553 N N   . LEU B 1 56  ? 26.138  -26.587 67.125  1.00 9.12  ? 56  LEU B N   1 
ATOM   4554 C CA  . LEU B 1 56  ? 25.577  -26.833 68.452  1.00 9.10  ? 56  LEU B CA  1 
ATOM   4555 C C   . LEU B 1 56  ? 26.707  -27.268 69.373  1.00 6.33  ? 56  LEU B C   1 
ATOM   4556 O O   . LEU B 1 56  ? 27.326  -28.308 69.138  1.00 11.47 ? 56  LEU B O   1 
ATOM   4557 C CB  . LEU B 1 56  ? 24.508  -27.925 68.402  1.00 9.93  ? 56  LEU B CB  1 
ATOM   4558 C CG  . LEU B 1 56  ? 23.313  -27.663 67.487  1.00 11.11 ? 56  LEU B CG  1 
ATOM   4559 C CD1 . LEU B 1 56  ? 22.475  -28.937 67.350  1.00 15.27 ? 56  LEU B CD1 1 
ATOM   4560 C CD2 . LEU B 1 56  ? 22.457  -26.530 68.025  1.00 13.79 ? 56  LEU B CD2 1 
ATOM   4561 N N   . THR B 1 57  ? 26.959  -26.496 70.439  1.00 6.14  ? 57  THR B N   1 
ATOM   4562 C CA  . THR B 1 57  ? 27.999  -26.992 71.339  1.00 7.40  ? 57  THR B CA  1 
ATOM   4563 C C   . THR B 1 57  ? 27.459  -28.150 72.179  1.00 4.85  ? 57  THR B C   1 
ATOM   4564 O O   . THR B 1 57  ? 26.250  -28.230 72.449  1.00 7.38  ? 57  THR B O   1 
ATOM   4565 C CB  . THR B 1 57  ? 28.515  -25.875 72.257  1.00 9.65  ? 57  THR B CB  1 
ATOM   4566 O OG1 . THR B 1 57  ? 27.459  -25.439 73.135  1.00 10.12 ? 57  THR B OG1 1 
ATOM   4567 C CG2 . THR B 1 57  ? 28.998  -24.688 71.398  1.00 6.91  ? 57  THR B CG2 1 
ATOM   4568 N N   . PRO B 1 58  ? 28.329  -29.080 72.585  1.00 4.71  ? 58  PRO B N   1 
ATOM   4569 C CA  . PRO B 1 58  ? 27.827  -30.224 73.363  1.00 5.09  ? 58  PRO B CA  1 
ATOM   4570 C C   . PRO B 1 58  ? 27.245  -29.814 74.699  1.00 10.25 ? 58  PRO B C   1 
ATOM   4571 O O   . PRO B 1 58  ? 26.258  -30.411 75.142  1.00 10.36 ? 58  PRO B O   1 
ATOM   4572 C CB  . PRO B 1 58  ? 29.070  -31.109 73.520  1.00 7.07  ? 58  PRO B CB  1 
ATOM   4573 C CG  . PRO B 1 58  ? 29.868  -30.832 72.286  1.00 8.79  ? 58  PRO B CG  1 
ATOM   4574 C CD  . PRO B 1 58  ? 29.695  -29.323 72.078  1.00 4.15  ? 58  PRO B CD  1 
ATOM   4575 N N   . VAL B 1 59  ? 27.820  -28.800 75.347  1.00 7.77  ? 59  VAL B N   1 
ATOM   4576 C CA  . VAL B 1 59  ? 27.282  -28.361 76.635  1.00 6.73  ? 59  VAL B CA  1 
ATOM   4577 C C   . VAL B 1 59  ? 25.922  -27.707 76.449  1.00 8.82  ? 59  VAL B C   1 
ATOM   4578 O O   . VAL B 1 59  ? 25.067  -27.777 77.343  1.00 7.79  ? 59  VAL B O   1 
ATOM   4579 C CB  . VAL B 1 59  ? 28.287  -27.435 77.363  1.00 8.26  ? 59  VAL B CB  1 
ATOM   4580 C CG1 . VAL B 1 59  ? 28.631  -26.221 76.516  1.00 8.78  ? 59  VAL B CG1 1 
ATOM   4581 C CG2 . VAL B 1 59  ? 27.751  -27.013 78.750  1.00 9.43  ? 59  VAL B CG2 1 
ATOM   4582 N N   . LEU B 1 60  ? 25.666  -27.079 75.292  1.00 5.40  ? 60  LEU B N   1 
ATOM   4583 C CA  . LEU B 1 60  ? 24.293  -26.633 75.051  1.00 5.48  ? 60  LEU B CA  1 
ATOM   4584 C C   . LEU B 1 60  ? 23.364  -27.830 74.877  1.00 9.32  ? 60  LEU B C   1 
ATOM   4585 O O   . LEU B 1 60  ? 22.261  -27.868 75.446  1.00 8.60  ? 60  LEU B O   1 
ATOM   4586 C CB  . LEU B 1 60  ? 24.223  -25.716 73.824  1.00 10.55 ? 60  LEU B CB  1 
ATOM   4587 C CG  . LEU B 1 60  ? 22.797  -25.365 73.365  1.00 8.09  ? 60  LEU B CG  1 
ATOM   4588 C CD1 . LEU B 1 60  ? 22.050  -24.681 74.515  1.00 7.01  ? 60  LEU B CD1 1 
ATOM   4589 C CD2 . LEU B 1 60  ? 22.800  -24.493 72.099  1.00 8.44  ? 60  LEU B CD2 1 
ATOM   4590 N N   . ILE B 1 61  ? 23.793  -28.819 74.095  1.00 7.45  ? 61  ILE B N   1 
ATOM   4591 C CA  . ILE B 1 61  ? 22.961  -29.993 73.849  1.00 8.53  ? 61  ILE B CA  1 
ATOM   4592 C C   . ILE B 1 61  ? 22.562  -30.659 75.162  1.00 5.46  ? 61  ILE B C   1 
ATOM   4593 O O   . ILE B 1 61  ? 21.393  -31.009 75.357  1.00 9.02  ? 61  ILE B O   1 
ATOM   4594 C CB  . ILE B 1 61  ? 23.683  -30.976 72.910  1.00 9.13  ? 61  ILE B CB  1 
ATOM   4595 C CG1 . ILE B 1 61  ? 23.872  -30.332 71.520  1.00 7.97  ? 61  ILE B CG1 1 
ATOM   4596 C CG2 . ILE B 1 61  ? 22.897  -32.288 72.812  1.00 13.73 ? 61  ILE B CG2 1 
ATOM   4597 C CD1 . ILE B 1 61  ? 24.689  -31.238 70.542  1.00 11.07 ? 61  ILE B CD1 1 
ATOM   4598 N N   . ASP B 1 62  ? 23.513  -30.818 76.090  1.00 9.02  ? 62  ASP B N   1 
ATOM   4599 C CA  . ASP B 1 62  ? 23.196  -31.407 77.392  1.00 8.38  ? 62  ASP B CA  1 
ATOM   4600 C C   . ASP B 1 62  ? 22.063  -30.654 78.082  1.00 11.71 ? 62  ASP B C   1 
ATOM   4601 O O   . ASP B 1 62  ? 21.153  -31.268 78.645  1.00 9.43  ? 62  ASP B O   1 
ATOM   4602 C CB  . ASP B 1 62  ? 24.423  -31.405 78.310  1.00 10.03 ? 62  ASP B CB  1 
ATOM   4603 C CG  . ASP B 1 62  ? 25.481  -32.412 77.909  1.00 17.41 ? 62  ASP B CG  1 
ATOM   4604 O OD1 . ASP B 1 62  ? 25.155  -33.418 77.258  1.00 14.99 ? 62  ASP B OD1 1 
ATOM   4605 O OD2 . ASP B 1 62  ? 26.662  -32.189 78.258  1.00 13.25 ? 62  ASP B OD2 1 
ATOM   4606 N N   . GLN B 1 63  ? 22.115  -29.320 78.074  1.00 9.96  ? 63  GLN B N   1 
ATOM   4607 C CA  . GLN B 1 63  ? 21.090  -28.550 78.772  1.00 9.09  ? 63  GLN B CA  1 
ATOM   4608 C C   . GLN B 1 63  ? 19.736  -28.659 78.072  1.00 8.14  ? 63  GLN B C   1 
ATOM   4609 O O   . GLN B 1 63  ? 18.705  -28.827 78.726  1.00 9.81  ? 63  GLN B O   1 
ATOM   4610 C CB  . GLN B 1 63  ? 21.536  -27.094 78.884  1.00 6.96  ? 63  GLN B CB  1 
ATOM   4611 C CG  . GLN B 1 63  ? 22.868  -26.944 79.594  1.00 5.02  ? 63  GLN B CG  1 
ATOM   4612 C CD  . GLN B 1 63  ? 23.291  -25.501 79.600  1.00 13.37 ? 63  GLN B CD  1 
ATOM   4613 O OE1 . GLN B 1 63  ? 22.656  -24.670 80.240  1.00 11.35 ? 63  GLN B OE1 1 
ATOM   4614 N NE2 . GLN B 1 63  ? 24.342  -25.187 78.869  1.00 8.81  ? 63  GLN B NE2 1 
ATOM   4615 N N   . ILE B 1 64  ? 19.722  -28.598 76.744  1.00 7.09  ? 64  ILE B N   1 
ATOM   4616 C CA  . ILE B 1 64  ? 18.471  -28.799 76.019  1.00 6.93  ? 64  ILE B CA  1 
ATOM   4617 C C   . ILE B 1 64  ? 17.857  -30.143 76.392  1.00 9.89  ? 64  ILE B C   1 
ATOM   4618 O O   . ILE B 1 64  ? 16.648  -30.239 76.653  1.00 10.22 ? 64  ILE B O   1 
ATOM   4619 C CB  . ILE B 1 64  ? 18.709  -28.683 74.504  1.00 12.02 ? 64  ILE B CB  1 
ATOM   4620 C CG1 . ILE B 1 64  ? 19.100  -27.246 74.139  1.00 6.21  ? 64  ILE B CG1 1 
ATOM   4621 C CG2 . ILE B 1 64  ? 17.449  -29.092 73.736  1.00 15.55 ? 64  ILE B CG2 1 
ATOM   4622 C CD1 . ILE B 1 64  ? 19.562  -27.125 72.700  1.00 7.97  ? 64  ILE B CD1 1 
ATOM   4623 N N   . GLN B 1 65  ? 18.680  -31.190 76.460  1.00 12.57 ? 65  GLN B N   1 
ATOM   4624 C CA  . GLN B 1 65  ? 18.158  -32.513 76.808  1.00 11.39 ? 65  GLN B CA  1 
ATOM   4625 C C   . GLN B 1 65  ? 17.552  -32.519 78.210  1.00 13.16 ? 65  GLN B C   1 
ATOM   4626 O O   . GLN B 1 65  ? 16.475  -33.089 78.427  1.00 13.09 ? 65  GLN B O   1 
ATOM   4627 C CB  . GLN B 1 65  ? 19.270  -33.549 76.701  1.00 14.78 ? 65  GLN B CB  1 
ATOM   4628 C CG  . GLN B 1 65  ? 19.717  -33.829 75.275  1.00 12.03 ? 65  GLN B CG  1 
ATOM   4629 C CD  . GLN B 1 65  ? 20.776  -34.910 75.215  1.00 18.29 ? 65  GLN B CD  1 
ATOM   4630 O OE1 . GLN B 1 65  ? 21.874  -34.757 75.763  1.00 16.75 ? 65  GLN B OE1 1 
ATOM   4631 N NE2 . GLN B 1 65  ? 20.442  -36.022 74.573  1.00 24.25 ? 65  GLN B NE2 1 
ATOM   4632 N N   . GLU B 1 66  ? 18.214  -31.864 79.170  1.00 9.33  ? 66  GLU B N   1 
ATOM   4633 C CA  . GLU B 1 66  ? 17.684  -31.809 80.529  1.00 9.75  ? 66  GLU B CA  1 
ATOM   4634 C C   . GLU B 1 66  ? 16.348  -31.073 80.592  1.00 8.56  ? 66  GLU B C   1 
ATOM   4635 O O   . GLU B 1 66  ? 15.419  -31.520 81.277  1.00 12.89 ? 66  GLU B O   1 
ATOM   4636 C CB  . GLU B 1 66  ? 18.690  -31.155 81.475  1.00 9.68  ? 66  GLU B CB  1 
ATOM   4637 C CG  . GLU B 1 66  ? 18.413  -31.476 82.949  1.00 24.44 ? 66  GLU B CG  1 
ATOM   4638 C CD  . GLU B 1 66  ? 19.577  -31.135 83.875  1.00 27.19 ? 66  GLU B CD  1 
ATOM   4639 O OE1 . GLU B 1 66  ? 20.661  -30.757 83.373  1.00 15.10 ? 66  GLU B OE1 1 
ATOM   4640 O OE2 . GLU B 1 66  ? 19.403  -31.254 85.109  1.00 31.89 ? 66  GLU B OE2 1 
ATOM   4641 N N   . TYR B 1 67  ? 16.233  -29.930 79.911  1.00 8.46  ? 67  TYR B N   1 
ATOM   4642 C CA  . TYR B 1 67  ? 14.936  -29.253 79.871  1.00 11.93 ? 67  TYR B CA  1 
ATOM   4643 C C   . TYR B 1 67  ? 13.886  -30.120 79.176  1.00 15.55 ? 67  TYR B C   1 
ATOM   4644 O O   . TYR B 1 67  ? 12.742  -30.219 79.642  1.00 13.45 ? 67  TYR B O   1 
ATOM   4645 C CB  . TYR B 1 67  ? 15.049  -27.892 79.168  1.00 10.55 ? 67  TYR B CB  1 
ATOM   4646 C CG  . TYR B 1 67  ? 15.564  -26.755 80.040  1.00 8.17  ? 67  TYR B CG  1 
ATOM   4647 C CD1 . TYR B 1 67  ? 14.704  -26.027 80.860  1.00 8.48  ? 67  TYR B CD1 1 
ATOM   4648 C CD2 . TYR B 1 67  ? 16.911  -26.413 80.030  1.00 14.42 ? 67  TYR B CD2 1 
ATOM   4649 C CE1 . TYR B 1 67  ? 15.181  -24.958 81.655  1.00 9.64  ? 67  TYR B CE1 1 
ATOM   4650 C CE2 . TYR B 1 67  ? 17.399  -25.377 80.820  1.00 11.80 ? 67  TYR B CE2 1 
ATOM   4651 C CZ  . TYR B 1 67  ? 16.539  -24.652 81.628  1.00 9.15  ? 67  TYR B CZ  1 
ATOM   4652 O OH  . TYR B 1 67  ? 17.041  -23.608 82.391  1.00 8.49  ? 67  TYR B OH  1 
ATOM   4653 N N   . ALA B 1 68  ? 14.250  -30.762 78.058  1.00 12.41 ? 68  ALA B N   1 
ATOM   4654 C CA  . ALA B 1 68  ? 13.263  -31.537 77.309  1.00 14.15 ? 68  ALA B CA  1 
ATOM   4655 C C   . ALA B 1 68  ? 12.780  -32.756 78.090  1.00 12.79 ? 68  ALA B C   1 
ATOM   4656 O O   . ALA B 1 68  ? 11.640  -33.205 77.896  1.00 15.90 ? 68  ALA B O   1 
ATOM   4657 C CB  . ALA B 1 68  ? 13.834  -31.964 75.959  1.00 14.48 ? 68  ALA B CB  1 
ATOM   4658 N N   . GLN B 1 69  ? 13.616  -33.288 78.981  1.00 11.09 ? 69  GLN B N   1 
ATOM   4659 C CA  . GLN B 1 69  ? 13.263  -34.406 79.843  1.00 15.52 ? 69  GLN B CA  1 
ATOM   4660 C C   . GLN B 1 69  ? 12.543  -33.964 81.109  1.00 20.80 ? 69  GLN B C   1 
ATOM   4661 O O   . GLN B 1 69  ? 12.192  -34.812 81.937  1.00 30.66 ? 69  GLN B O   1 
ATOM   4662 C CB  . GLN B 1 69  ? 14.530  -35.200 80.198  1.00 17.17 ? 69  GLN B CB  1 
ATOM   4663 C CG  . GLN B 1 69  ? 15.177  -35.848 78.983  1.00 17.99 ? 69  GLN B CG  1 
ATOM   4664 C CD  . GLN B 1 69  ? 16.577  -36.391 79.242  1.00 31.57 ? 69  GLN B CD  1 
ATOM   4665 O OE1 . GLN B 1 69  ? 17.059  -36.390 80.371  1.00 44.25 ? 69  GLN B OE1 1 
ATOM   4666 N NE2 . GLN B 1 69  ? 17.238  -36.855 78.180  1.00 31.13 ? 69  GLN B NE2 1 
ATOM   4667 N N   . GLY B 1 70  ? 12.320  -32.664 81.288  1.00 19.71 ? 70  GLY B N   1 
ATOM   4668 C CA  . GLY B 1 70  ? 11.662  -32.176 82.483  1.00 19.17 ? 70  GLY B CA  1 
ATOM   4669 C C   . GLY B 1 70  ? 12.516  -32.214 83.726  1.00 22.56 ? 70  GLY B C   1 
ATOM   4670 O O   . GLY B 1 70  ? 11.987  -32.072 84.831  1.00 23.28 ? 70  GLY B O   1 
ATOM   4671 N N   . LYS B 1 71  ? 13.832  -32.393 83.579  1.00 19.18 ? 71  LYS B N   1 
ATOM   4672 C CA  . LYS B 1 71  ? 14.730  -32.532 84.719  1.00 22.45 ? 71  LYS B CA  1 
ATOM   4673 C C   . LYS B 1 71  ? 15.419  -31.234 85.134  1.00 31.72 ? 71  LYS B C   1 
ATOM   4674 O O   . LYS B 1 71  ? 16.095  -31.216 86.169  1.00 33.10 ? 71  LYS B O   1 
ATOM   4675 C CB  . LYS B 1 71  ? 15.815  -33.571 84.422  1.00 29.50 ? 71  LYS B CB  1 
ATOM   4676 C CG  . LYS B 1 71  ? 15.314  -34.991 84.155  1.00 36.64 ? 71  LYS B CG  1 
ATOM   4677 C CD  . LYS B 1 71  ? 16.506  -35.909 83.853  1.00 38.83 ? 71  LYS B CD  1 
ATOM   4678 C CE  . LYS B 1 71  ? 16.066  -37.267 83.313  1.00 42.79 ? 71  LYS B CE  1 
ATOM   4679 N NZ  . LYS B 1 71  ? 17.230  -38.096 82.872  1.00 46.60 ? 71  LYS B NZ  1 
ATOM   4680 N N   . ALA B 1 72  ? 15.292  -30.165 84.357  1.00 15.93 ? 72  ALA B N   1 
ATOM   4681 C CA  . ALA B 1 72  ? 15.980  -28.917 84.672  1.00 10.61 ? 72  ALA B CA  1 
ATOM   4682 C C   . ALA B 1 72  ? 15.246  -28.192 85.790  1.00 21.33 ? 72  ALA B C   1 
ATOM   4683 O O   . ALA B 1 72  ? 14.050  -27.902 85.667  1.00 25.03 ? 72  ALA B O   1 
ATOM   4684 C CB  . ALA B 1 72  ? 16.072  -28.036 83.427  1.00 13.06 ? 72  ALA B CB  1 
ATOM   4685 N N   . LYS B 1 73  ? 15.959  -27.907 86.881  1.00 11.12 ? 73  LYS B N   1 
ATOM   4686 C CA  . LYS B 1 73  ? 15.430  -27.104 87.990  1.00 11.67 ? 73  LYS B CA  1 
ATOM   4687 C C   . LYS B 1 73  ? 15.904  -25.669 87.784  1.00 17.69 ? 73  LYS B C   1 
ATOM   4688 O O   . LYS B 1 73  ? 16.962  -25.261 88.266  1.00 19.58 ? 73  LYS B O   1 
ATOM   4689 C CB  . LYS B 1 73  ? 15.886  -27.649 89.343  1.00 19.11 ? 73  LYS B CB  1 
ATOM   4690 C CG  . LYS B 1 73  ? 15.711  -29.161 89.505  1.00 29.21 ? 73  LYS B CG  1 
ATOM   4691 C CD  . LYS B 1 73  ? 16.775  -29.746 90.438  1.00 44.34 ? 73  LYS B CD  1 
ATOM   4692 C CE  . LYS B 1 73  ? 16.999  -31.238 90.196  1.00 48.39 ? 73  LYS B CE  1 
ATOM   4693 N NZ  . LYS B 1 73  ? 17.454  -31.532 88.809  1.00 47.48 ? 73  LYS B NZ  1 
ATOM   4694 N N   . ASP B 1 74  ? 15.092  -24.894 87.092  1.00 10.96 ? 74  ASP B N   1 
ATOM   4695 C CA  . ASP B 1 74  ? 15.446  -23.550 86.664  1.00 6.74  ? 74  ASP B CA  1 
ATOM   4696 C C   . ASP B 1 74  ? 14.799  -22.584 87.648  1.00 12.02 ? 74  ASP B C   1 
ATOM   4697 O O   . ASP B 1 74  ? 13.564  -22.515 87.728  1.00 12.62 ? 74  ASP B O   1 
ATOM   4698 C CB  . ASP B 1 74  ? 14.969  -23.355 85.222  1.00 7.98  ? 74  ASP B CB  1 
ATOM   4699 C CG  . ASP B 1 74  ? 15.257  -21.991 84.670  1.00 10.50 ? 74  ASP B CG  1 
ATOM   4700 O OD1 . ASP B 1 74  ? 15.116  -20.960 85.378  1.00 13.63 ? 74  ASP B OD1 1 
ATOM   4701 O OD2 . ASP B 1 74  ? 15.597  -21.942 83.464  1.00 13.17 ? 74  ASP B OD2 1 
ATOM   4702 N N   . VAL B 1 75  ? 15.631  -21.856 88.411  1.00 14.57 ? 75  VAL B N   1 
ATOM   4703 C CA  . VAL B 1 75  ? 15.129  -21.058 89.529  1.00 13.33 ? 75  VAL B CA  1 
ATOM   4704 C C   . VAL B 1 75  ? 14.295  -19.884 89.030  1.00 10.54 ? 75  VAL B C   1 
ATOM   4705 O O   . VAL B 1 75  ? 13.256  -19.551 89.621  1.00 12.94 ? 75  VAL B O   1 
ATOM   4706 C CB  . VAL B 1 75  ? 16.282  -20.582 90.444  1.00 18.67 ? 75  VAL B CB  1 
ATOM   4707 C CG1 . VAL B 1 75  ? 16.988  -21.768 91.102  1.00 22.23 ? 75  VAL B CG1 1 
ATOM   4708 C CG2 . VAL B 1 75  ? 17.280  -19.714 89.697  1.00 20.13 ? 75  VAL B CG2 1 
ATOM   4709 N N   . PHE B 1 76  ? 14.730  -19.228 87.954  1.00 14.53 ? 76  PHE B N   1 
ATOM   4710 C CA  . PHE B 1 76  ? 13.925  -18.136 87.419  1.00 14.33 ? 76  PHE B CA  1 
ATOM   4711 C C   . PHE B 1 76  ? 12.601  -18.648 86.857  1.00 15.47 ? 76  PHE B C   1 
ATOM   4712 O O   . PHE B 1 76  ? 11.547  -18.037 87.080  1.00 14.88 ? 76  PHE B O   1 
ATOM   4713 C CB  . PHE B 1 76  ? 14.692  -17.361 86.344  1.00 13.60 ? 76  PHE B CB  1 
ATOM   4714 C CG  . PHE B 1 76  ? 13.974  -16.125 85.917  1.00 26.31 ? 76  PHE B CG  1 
ATOM   4715 C CD1 . PHE B 1 76  ? 13.965  -15.006 86.741  1.00 30.31 ? 76  PHE B CD1 1 
ATOM   4716 C CD2 . PHE B 1 76  ? 13.231  -16.100 84.743  1.00 24.25 ? 76  PHE B CD2 1 
ATOM   4717 C CE1 . PHE B 1 76  ? 13.264  -13.871 86.382  1.00 29.29 ? 76  PHE B CE1 1 
ATOM   4718 C CE2 . PHE B 1 76  ? 12.530  -14.962 84.374  1.00 28.53 ? 76  PHE B CE2 1 
ATOM   4719 C CZ  . PHE B 1 76  ? 12.543  -13.849 85.200  1.00 29.79 ? 76  PHE B CZ  1 
ATOM   4720 N N   . LEU B 1 77  ? 12.633  -19.760 86.117  1.00 11.77 ? 77  LEU B N   1 
ATOM   4721 C CA  . LEU B 1 77  ? 11.395  -20.310 85.564  1.00 15.85 ? 77  LEU B CA  1 
ATOM   4722 C C   . LEU B 1 77  ? 10.412  -20.695 86.663  1.00 15.36 ? 77  LEU B C   1 
ATOM   4723 O O   . LEU B 1 77  ? 9.194   -20.563 86.485  1.00 11.44 ? 77  LEU B O   1 
ATOM   4724 C CB  . LEU B 1 77  ? 11.699  -21.519 84.676  1.00 15.36 ? 77  LEU B CB  1 
ATOM   4725 C CG  . LEU B 1 77  ? 10.563  -21.991 83.757  1.00 18.70 ? 77  LEU B CG  1 
ATOM   4726 C CD1 . LEU B 1 77  ? 10.054  -20.822 82.903  1.00 16.39 ? 77  LEU B CD1 1 
ATOM   4727 C CD2 . LEU B 1 77  ? 11.048  -23.141 82.871  1.00 14.97 ? 77  LEU B CD2 1 
ATOM   4728 N N   . GLU B 1 78  ? 10.918  -21.162 87.806  1.00 14.81 ? 78  GLU B N   1 
ATOM   4729 C CA  . GLU B 1 78  ? 10.044  -21.461 88.940  1.00 16.47 ? 78  GLU B CA  1 
ATOM   4730 C C   . GLU B 1 78  ? 9.317   -20.206 89.420  1.00 14.79 ? 78  GLU B C   1 
ATOM   4731 O O   . GLU B 1 78  ? 8.132   -20.261 89.771  1.00 20.01 ? 78  GLU B O   1 
ATOM   4732 C CB  . GLU B 1 78  ? 10.869  -22.093 90.073  1.00 20.41 ? 78  GLU B CB  1 
ATOM   4733 C CG  . GLU B 1 78  ? 10.061  -22.798 91.153  1.00 40.54 ? 78  GLU B CG  1 
ATOM   4734 C CD  . GLU B 1 78  ? 9.038   -23.777 90.596  1.00 51.15 ? 78  GLU B CD  1 
ATOM   4735 O OE1 . GLU B 1 78  ? 9.316   -24.417 89.559  1.00 56.15 ? 78  GLU B OE1 1 
ATOM   4736 O OE2 . GLU B 1 78  ? 7.949   -23.903 91.200  1.00 53.35 ? 78  GLU B OE2 1 
ATOM   4737 N N   . ALA B 1 79  ? 10.006  -19.063 89.424  1.00 11.92 ? 79  ALA B N   1 
ATOM   4738 C CA  . ALA B 1 79  ? 9.367   -17.799 89.791  1.00 13.17 ? 79  ALA B CA  1 
ATOM   4739 C C   . ALA B 1 79  ? 8.282   -17.398 88.794  1.00 21.57 ? 79  ALA B C   1 
ATOM   4740 O O   . ALA B 1 79  ? 7.284   -16.775 89.178  1.00 18.13 ? 79  ALA B O   1 
ATOM   4741 C CB  . ALA B 1 79  ? 10.413  -16.690 89.894  1.00 16.59 ? 79  ALA B CB  1 
ATOM   4742 N N   . ILE B 1 80  ? 8.466   -17.724 87.513  1.00 12.37 ? 80  ILE B N   1 
ATOM   4743 C CA  . ILE B 1 80  ? 7.422   -17.454 86.525  1.00 13.51 ? 80  ILE B CA  1 
ATOM   4744 C C   . ILE B 1 80  ? 6.234   -18.401 86.710  1.00 13.91 ? 80  ILE B C   1 
ATOM   4745 O O   . ILE B 1 80  ? 5.069   -17.992 86.599  1.00 16.23 ? 80  ILE B O   1 
ATOM   4746 C CB  . ILE B 1 80  ? 8.013   -17.564 85.104  1.00 9.49  ? 80  ILE B CB  1 
ATOM   4747 C CG1 . ILE B 1 80  ? 8.903   -16.349 84.822  1.00 13.78 ? 80  ILE B CG1 1 
ATOM   4748 C CG2 . ILE B 1 80  ? 6.887   -17.716 84.058  1.00 8.43  ? 80  ILE B CG2 1 
ATOM   4749 C CD1 . ILE B 1 80  ? 9.556   -16.379 83.468  1.00 14.65 ? 80  ILE B CD1 1 
ATOM   4750 N N   . ARG B 1 81  ? 6.503   -19.676 86.989  1.00 8.69  ? 81  ARG B N   1 
ATOM   4751 C CA  . ARG B 1 81  ? 5.446   -20.689 86.940  1.00 14.96 ? 81  ARG B CA  1 
ATOM   4752 C C   . ARG B 1 81  ? 4.476   -20.578 88.113  1.00 13.25 ? 81  ARG B C   1 
ATOM   4753 O O   . ARG B 1 81  ? 3.281   -20.831 87.946  1.00 14.67 ? 81  ARG B O   1 
ATOM   4754 C CB  . ARG B 1 81  ? 6.060   -22.084 86.916  1.00 14.37 ? 81  ARG B CB  1 
ATOM   4755 C CG  . ARG B 1 81  ? 5.049   -23.207 86.723  1.00 28.45 ? 81  ARG B CG  1 
ATOM   4756 C CD  . ARG B 1 81  ? 5.691   -24.575 86.962  1.00 36.13 ? 81  ARG B CD  1 
ATOM   4757 N NE  . ARG B 1 81  ? 6.594   -24.961 85.878  1.00 39.75 ? 81  ARG B NE  1 
ATOM   4758 C CZ  . ARG B 1 81  ? 6.200   -25.535 84.741  1.00 50.48 ? 81  ARG B CZ  1 
ATOM   4759 N NH1 . ARG B 1 81  ? 4.913   -25.788 84.532  1.00 47.02 ? 81  ARG B NH1 1 
ATOM   4760 N NH2 . ARG B 1 81  ? 7.092   -25.856 83.809  1.00 53.49 ? 81  ARG B NH2 1 
ATOM   4761 N N   . LYS B 1 82  ? 4.974   -20.240 89.309  1.00 10.95 ? 82  LYS B N   1 
ATOM   4762 C CA  . LYS B 1 82  ? 4.147   -20.260 90.518  1.00 15.00 ? 82  LYS B CA  1 
ATOM   4763 C C   . LYS B 1 82  ? 2.963   -19.316 90.401  1.00 14.55 ? 82  LYS B C   1 
ATOM   4764 O O   . LYS B 1 82  ? 3.041   -18.280 89.743  1.00 11.56 ? 82  LYS B O   1 
ATOM   4765 C CB  . LYS B 1 82  ? 4.957   -19.821 91.742  1.00 17.70 ? 82  LYS B CB  1 
ATOM   4766 C CG  . LYS B 1 82  ? 5.908   -20.839 92.326  1.00 29.29 ? 82  LYS B CG  1 
ATOM   4767 C CD  . LYS B 1 82  ? 6.728   -20.147 93.420  1.00 29.12 ? 82  LYS B CD  1 
ATOM   4768 C CE  . LYS B 1 82  ? 7.874   -20.998 93.914  1.00 27.40 ? 82  LYS B CE  1 
ATOM   4769 N NZ  . LYS B 1 82  ? 8.402   -20.441 95.187  1.00 29.19 ? 82  LYS B NZ  1 
ATOM   4770 N N   . ASP B 1 83  ? 1.876   -19.655 91.101  1.00 15.02 ? 83  ASP B N   1 
ATOM   4771 C CA  . ASP B 1 83  ? 0.850   -18.661 91.389  1.00 16.72 ? 83  ASP B CA  1 
ATOM   4772 C C   . ASP B 1 83  ? 1.482   -17.502 92.158  1.00 13.99 ? 83  ASP B C   1 
ATOM   4773 O O   . ASP B 1 83  ? 2.312   -17.726 93.051  1.00 11.83 ? 83  ASP B O   1 
ATOM   4774 C CB  . ASP B 1 83  ? -0.298  -19.278 92.207  1.00 16.67 ? 83  ASP B CB  1 
ATOM   4775 C CG  . ASP B 1 83  ? -1.527  -18.362 92.300  1.00 21.09 ? 83  ASP B CG  1 
ATOM   4776 O OD1 . ASP B 1 83  ? -1.477  -17.344 93.024  1.00 17.84 ? 83  ASP B OD1 1 
ATOM   4777 O OD2 . ASP B 1 83  ? -2.555  -18.670 91.651  1.00 23.95 ? 83  ASP B OD2 1 
ATOM   4778 N N   . PRO B 1 84  ? 1.149   -16.252 91.828  1.00 13.30 ? 84  PRO B N   1 
ATOM   4779 C CA  . PRO B 1 84  ? 1.786   -15.135 92.537  1.00 11.47 ? 84  PRO B CA  1 
ATOM   4780 C C   . PRO B 1 84  ? 1.574   -15.165 94.040  1.00 15.65 ? 84  PRO B C   1 
ATOM   4781 O O   . PRO B 1 84  ? 2.437   -14.672 94.772  1.00 10.41 ? 84  PRO B O   1 
ATOM   4782 C CB  . PRO B 1 84  ? 1.149   -13.900 91.887  1.00 15.56 ? 84  PRO B CB  1 
ATOM   4783 C CG  . PRO B 1 84  ? 0.815   -14.359 90.506  1.00 13.49 ? 84  PRO B CG  1 
ATOM   4784 C CD  . PRO B 1 84  ? 0.370   -15.791 90.664  1.00 19.53 ? 84  PRO B CD  1 
ATOM   4785 N N   . ASP B 1 85  ? 0.469   -15.737 94.524  1.00 13.92 ? 85  ASP B N   1 
ATOM   4786 C CA  . ASP B 1 85  ? 0.279   -15.874 95.970  1.00 13.12 ? 85  ASP B CA  1 
ATOM   4787 C C   . ASP B 1 85  ? 1.380   -16.703 96.626  1.00 14.00 ? 85  ASP B C   1 
ATOM   4788 O O   . ASP B 1 85  ? 1.620   -16.555 97.832  1.00 15.76 ? 85  ASP B O   1 
ATOM   4789 C CB  . ASP B 1 85  ? -1.076  -16.520 96.272  1.00 18.26 ? 85  ASP B CB  1 
ATOM   4790 C CG  . ASP B 1 85  ? -2.245  -15.607 95.957  1.00 28.43 ? 85  ASP B CG  1 
ATOM   4791 O OD1 . ASP B 1 85  ? -2.033  -14.378 95.829  1.00 26.77 ? 85  ASP B OD1 1 
ATOM   4792 O OD2 . ASP B 1 85  ? -3.381  -16.126 95.853  1.00 32.13 ? 85  ASP B OD2 1 
ATOM   4793 N N   . ASP B 1 86  ? 2.055   -17.561 95.864  1.00 12.56 ? 86  ASP B N   1 
ATOM   4794 C CA  . ASP B 1 86  ? 3.102   -18.435 96.384  1.00 9.94  ? 86  ASP B CA  1 
ATOM   4795 C C   . ASP B 1 86  ? 4.505   -17.905 96.138  1.00 14.42 ? 86  ASP B C   1 
ATOM   4796 O O   . ASP B 1 86  ? 5.478   -18.566 96.515  1.00 15.46 ? 86  ASP B O   1 
ATOM   4797 C CB  . ASP B 1 86  ? 2.966   -19.835 95.770  1.00 10.67 ? 86  ASP B CB  1 
ATOM   4798 C CG  . ASP B 1 86  ? 1.711   -20.547 96.236  1.00 26.15 ? 86  ASP B CG  1 
ATOM   4799 O OD1 . ASP B 1 86  ? 1.231   -20.220 97.337  1.00 30.23 ? 86  ASP B OD1 1 
ATOM   4800 O OD2 . ASP B 1 86  ? 1.223   -21.429 95.511  1.00 30.54 ? 86  ASP B OD2 1 
ATOM   4801 N N   . LEU B 1 87  ? 4.634   -16.734 95.527  1.00 10.88 ? 87  LEU B N   1 
ATOM   4802 C CA  . LEU B 1 87  ? 5.951   -16.154 95.289  1.00 11.12 ? 87  LEU B CA  1 
ATOM   4803 C C   . LEU B 1 87  ? 6.648   -15.758 96.584  1.00 15.36 ? 87  LEU B C   1 
ATOM   4804 O O   . LEU B 1 87  ? 6.050   -15.151 97.477  1.00 10.93 ? 87  LEU B O   1 
ATOM   4805 C CB  . LEU B 1 87  ? 5.835   -14.922 94.398  1.00 9.58  ? 87  LEU B CB  1 
ATOM   4806 C CG  . LEU B 1 87  ? 5.635   -15.239 92.911  1.00 13.33 ? 87  LEU B CG  1 
ATOM   4807 C CD1 . LEU B 1 87  ? 5.301   -13.947 92.163  1.00 12.18 ? 87  LEU B CD1 1 
ATOM   4808 C CD2 . LEU B 1 87  ? 6.875   -15.918 92.354  1.00 9.15  ? 87  LEU B CD2 1 
ATOM   4809 N N   . GLU B 1 88  ? 7.931   -16.095 96.673  1.00 9.74  ? 88  GLU B N   1 
ATOM   4810 C CA  . GLU B 1 88  ? 8.783   -15.555 97.719  1.00 13.72 ? 88  GLU B CA  1 
ATOM   4811 C C   . GLU B 1 88  ? 9.129   -14.107 97.406  1.00 15.46 ? 88  GLU B C   1 
ATOM   4812 O O   . GLU B 1 88  ? 9.181   -13.692 96.240  1.00 14.07 ? 88  GLU B O   1 
ATOM   4813 C CB  . GLU B 1 88  ? 10.056  -16.400 97.858  1.00 12.92 ? 88  GLU B CB  1 
ATOM   4814 C CG  . GLU B 1 88  ? 9.750   -17.874 98.086  1.00 14.31 ? 88  GLU B CG  1 
ATOM   4815 C CD  . GLU B 1 88  ? 10.916  -18.800 97.740  1.00 22.86 ? 88  GLU B CD  1 
ATOM   4816 O OE1 . GLU B 1 88  ? 10.755  -20.028 97.898  1.00 27.39 ? 88  GLU B OE1 1 
ATOM   4817 O OE2 . GLU B 1 88  ? 11.986  -18.303 97.332  1.00 23.28 ? 88  GLU B OE2 1 
ATOM   4818 N N   . LYS B 1 89  ? 9.348   -13.329 98.467  1.00 11.33 ? 89  LYS B N   1 
ATOM   4819 C CA  . LYS B 1 89  ? 9.821   -11.958 98.291  1.00 16.18 ? 89  LYS B CA  1 
ATOM   4820 C C   . LYS B 1 89  ? 11.058  -11.913 97.400  1.00 20.94 ? 89  LYS B C   1 
ATOM   4821 O O   . LYS B 1 89  ? 11.188  -11.029 96.543  1.00 18.78 ? 89  LYS B O   1 
ATOM   4822 C CB  . LYS B 1 89  ? 10.117  -11.339 99.659  1.00 19.60 ? 89  LYS B CB  1 
ATOM   4823 C CG  . LYS B 1 89  ? 10.555  -9.886  99.611  1.00 31.77 ? 89  LYS B CG  1 
ATOM   4824 C CD  . LYS B 1 89  ? 9.346   -8.960  99.577  1.00 42.72 ? 89  LYS B CD  1 
ATOM   4825 C CE  . LYS B 1 89  ? 9.574   -7.713  100.417 1.00 49.13 ? 89  LYS B CE  1 
ATOM   4826 N NZ  . LYS B 1 89  ? 9.421   -7.988  101.873 1.00 51.11 ? 89  LYS B NZ  1 
ATOM   4827 N N   . GLU B 1 90  ? 11.972  -12.872 97.578  1.00 13.65 ? 90  GLU B N   1 
ATOM   4828 C CA  . GLU B 1 90  ? 13.155  -12.944 96.720  1.00 20.95 ? 90  GLU B CA  1 
ATOM   4829 C C   . GLU B 1 90  ? 12.774  -13.208 95.267  1.00 19.99 ? 90  GLU B C   1 
ATOM   4830 O O   . GLU B 1 90  ? 13.478  -12.778 94.344  1.00 17.57 ? 90  GLU B O   1 
ATOM   4831 C CB  . GLU B 1 90  ? 14.099  -14.051 97.192  1.00 21.69 ? 90  GLU B CB  1 
ATOM   4832 C CG  . GLU B 1 90  ? 14.852  -13.791 98.491  1.00 33.87 ? 90  GLU B CG  1 
ATOM   4833 C CD  . GLU B 1 90  ? 15.796  -14.940 98.844  1.00 40.28 ? 90  GLU B CD  1 
ATOM   4834 O OE1 . GLU B 1 90  ? 16.046  -15.792 97.961  1.00 40.99 ? 90  GLU B OE1 1 
ATOM   4835 O OE2 . GLU B 1 90  ? 16.280  -14.996 100.003 1.00 38.68 ? 90  GLU B OE2 1 
ATOM   4836 N N   . GLU B 1 91  ? 11.700  -13.971 95.041  1.00 13.65 ? 91  GLU B N   1 
ATOM   4837 C CA  . GLU B 1 91  ? 11.328  -14.279 93.665  1.00 13.58 ? 91  GLU B CA  1 
ATOM   4838 C C   . GLU B 1 91  ? 10.687  -13.077 92.991  1.00 7.36  ? 91  GLU B C   1 
ATOM   4839 O O   . GLU B 1 91  ? 10.896  -12.845 91.794  1.00 13.89 ? 91  GLU B O   1 
ATOM   4840 C CB  . GLU B 1 91  ? 10.399  -15.487 93.625  1.00 9.86  ? 91  GLU B CB  1 
ATOM   4841 C CG  . GLU B 1 91  ? 11.102  -16.796 94.024  1.00 8.76  ? 91  GLU B CG  1 
ATOM   4842 C CD  . GLU B 1 91  ? 10.142  -17.968 94.126  1.00 21.06 ? 91  GLU B CD  1 
ATOM   4843 O OE1 . GLU B 1 91  ? 9.122   -17.838 94.833  1.00 14.94 ? 91  GLU B OE1 1 
ATOM   4844 O OE2 . GLU B 1 91  ? 10.416  -19.021 93.508  1.00 17.13 ? 91  GLU B OE2 1 
ATOM   4845 N N   . VAL B 1 92  ? 9.912   -12.290 93.739  1.00 13.74 ? 92  VAL B N   1 
ATOM   4846 C CA  . VAL B 1 92  ? 9.377   -11.062 93.165  1.00 11.84 ? 92  VAL B CA  1 
ATOM   4847 C C   . VAL B 1 92  ? 10.516  -10.112 92.800  1.00 16.70 ? 92  VAL B C   1 
ATOM   4848 O O   . VAL B 1 92  ? 10.489  -9.457  91.748  1.00 14.93 ? 92  VAL B O   1 
ATOM   4849 C CB  . VAL B 1 92  ? 8.362   -10.415 94.127  1.00 9.94  ? 92  VAL B CB  1 
ATOM   4850 C CG1 . VAL B 1 92  ? 7.787   -9.138  93.506  1.00 12.52 ? 92  VAL B CG1 1 
ATOM   4851 C CG2 . VAL B 1 92  ? 7.243   -11.399 94.457  1.00 12.18 ? 92  VAL B CG2 1 
ATOM   4852 N N   . GLU B 1 93  ? 11.538  -10.025 93.654  1.00 15.21 ? 93  GLU B N   1 
ATOM   4853 C CA  . GLU B 1 93  ? 12.686  -9.172  93.340  1.00 19.06 ? 93  GLU B CA  1 
ATOM   4854 C C   . GLU B 1 93  ? 13.384  -9.626  92.064  1.00 18.89 ? 93  GLU B C   1 
ATOM   4855 O O   . GLU B 1 93  ? 13.737  -8.800  91.213  1.00 20.16 ? 93  GLU B O   1 
ATOM   4856 C CB  . GLU B 1 93  ? 13.682  -9.174  94.500  1.00 19.74 ? 93  GLU B CB  1 
ATOM   4857 C CG  . GLU B 1 93  ? 13.258  -8.323  95.659  1.00 27.72 ? 93  GLU B CG  1 
ATOM   4858 C CD  . GLU B 1 93  ? 14.040  -8.634  96.917  1.00 33.93 ? 93  GLU B CD  1 
ATOM   4859 O OE1 . GLU B 1 93  ? 14.890  -9.554  96.895  1.00 38.68 ? 93  GLU B OE1 1 
ATOM   4860 O OE2 . GLU B 1 93  ? 13.795  -7.951  97.928  1.00 34.43 ? 93  GLU B OE2 1 
ATOM   4861 N N   . LYS B 1 94  ? 13.598  -10.936 91.919  1.00 15.54 ? 94  LYS B N   1 
ATOM   4862 C CA  . LYS B 1 94  ? 14.255  -11.449 90.719  1.00 16.88 ? 94  LYS B CA  1 
ATOM   4863 C C   . LYS B 1 94  ? 13.432  -11.170 89.466  1.00 17.53 ? 94  LYS B C   1 
ATOM   4864 O O   . LYS B 1 94  ? 13.990  -10.789 88.428  1.00 14.94 ? 94  LYS B O   1 
ATOM   4865 C CB  . LYS B 1 94  ? 14.529  -12.946 90.861  1.00 20.32 ? 94  LYS B CB  1 
ATOM   4866 C CG  . LYS B 1 94  ? 15.531  -13.294 91.950  1.00 37.98 ? 94  LYS B CG  1 
ATOM   4867 C CD  . LYS B 1 94  ? 16.702  -12.321 91.967  1.00 47.35 ? 94  LYS B CD  1 
ATOM   4868 C CE  . LYS B 1 94  ? 17.414  -12.318 93.309  1.00 49.78 ? 94  LYS B CE  1 
ATOM   4869 N NZ  . LYS B 1 94  ? 18.314  -11.134 93.443  1.00 49.35 ? 94  LYS B NZ  1 
ATOM   4870 N N   . LEU B 1 95  ? 12.106  -11.362 89.540  1.00 14.39 ? 95  LEU B N   1 
ATOM   4871 C CA  . LEU B 1 95  ? 11.248  -11.083 88.391  1.00 10.29 ? 95  LEU B CA  1 
ATOM   4872 C C   . LEU B 1 95  ? 11.360  -9.631  87.989  1.00 10.55 ? 95  LEU B C   1 
ATOM   4873 O O   . LEU B 1 95  ? 11.447  -9.306  86.799  1.00 12.68 ? 95  LEU B O   1 
ATOM   4874 C CB  . LEU B 1 95  ? 9.791   -11.406 88.714  1.00 12.12 ? 95  LEU B CB  1 
ATOM   4875 C CG  . LEU B 1 95  ? 9.391   -12.882 88.770  1.00 22.93 ? 95  LEU B CG  1 
ATOM   4876 C CD1 . LEU B 1 95  ? 8.047   -13.000 89.474  1.00 26.26 ? 95  LEU B CD1 1 
ATOM   4877 C CD2 . LEU B 1 95  ? 9.318   -13.487 87.374  1.00 25.88 ? 95  LEU B CD2 1 
ATOM   4878 N N   . ILE B 1 96  ? 11.363  -8.735  88.979  1.00 12.31 ? 96  ILE B N   1 
ATOM   4879 C CA  . ILE B 1 96  ? 11.431  -7.314  88.673  1.00 17.47 ? 96  ILE B CA  1 
ATOM   4880 C C   . ILE B 1 96  ? 12.796  -6.963  88.084  1.00 14.13 ? 96  ILE B C   1 
ATOM   4881 O O   . ILE B 1 96  ? 12.885  -6.267  87.066  1.00 15.89 ? 96  ILE B O   1 
ATOM   4882 C CB  . ILE B 1 96  ? 11.105  -6.481  89.928  1.00 16.99 ? 96  ILE B CB  1 
ATOM   4883 C CG1 . ILE B 1 96  ? 9.612   -6.580  90.263  1.00 16.00 ? 96  ILE B CG1 1 
ATOM   4884 C CG2 . ILE B 1 96  ? 11.486  -5.031  89.712  1.00 17.89 ? 96  ILE B CG2 1 
ATOM   4885 C CD1 . ILE B 1 96  ? 9.285   -6.126  91.662  1.00 25.23 ? 96  ILE B CD1 1 
ATOM   4886 N N   . GLU B 1 97  ? 13.876  -7.460  88.694  1.00 15.42 ? 97  GLU B N   1 
ATOM   4887 C CA  . GLU B 1 97  ? 15.207  -7.156  88.177  1.00 22.75 ? 97  GLU B CA  1 
ATOM   4888 C C   . GLU B 1 97  ? 15.400  -7.725  86.773  1.00 21.07 ? 97  GLU B C   1 
ATOM   4889 O O   . GLU B 1 97  ? 15.947  -7.049  85.895  1.00 17.33 ? 97  GLU B O   1 
ATOM   4890 C CB  . GLU B 1 97  ? 16.296  -7.678  89.124  1.00 19.29 ? 97  GLU B CB  1 
ATOM   4891 C CG  . GLU B 1 97  ? 16.202  -7.178  90.586  1.00 35.13 ? 97  GLU B CG  1 
ATOM   4892 C CD  . GLU B 1 97  ? 16.476  -5.679  90.781  1.00 52.60 ? 97  GLU B CD  1 
ATOM   4893 O OE1 . GLU B 1 97  ? 15.530  -4.870  90.659  1.00 52.93 ? 97  GLU B OE1 1 
ATOM   4894 O OE2 . GLU B 1 97  ? 17.630  -5.310  91.097  1.00 58.66 ? 97  GLU B OE2 1 
ATOM   4895 N N   . PHE B 1 98  ? 14.958  -8.965  86.535  1.00 16.70 ? 98  PHE B N   1 
ATOM   4896 C CA  . PHE B 1 98  ? 15.018  -9.510  85.177  1.00 11.94 ? 98  PHE B CA  1 
ATOM   4897 C C   . PHE B 1 98  ? 14.306  -8.617  84.172  1.00 15.52 ? 98  PHE B C   1 
ATOM   4898 O O   . PHE B 1 98  ? 14.788  -8.417  83.049  1.00 14.59 ? 98  PHE B O   1 
ATOM   4899 C CB  . PHE B 1 98  ? 14.420  -10.910 85.135  1.00 11.00 ? 98  PHE B CB  1 
ATOM   4900 C CG  . PHE B 1 98  ? 14.795  -11.682 83.899  1.00 18.72 ? 98  PHE B CG  1 
ATOM   4901 C CD1 . PHE B 1 98  ? 16.091  -12.163 83.733  1.00 19.05 ? 98  PHE B CD1 1 
ATOM   4902 C CD2 . PHE B 1 98  ? 13.865  -11.922 82.905  1.00 16.30 ? 98  PHE B CD2 1 
ATOM   4903 C CE1 . PHE B 1 98  ? 16.442  -12.877 82.590  1.00 17.16 ? 98  PHE B CE1 1 
ATOM   4904 C CE2 . PHE B 1 98  ? 14.207  -12.637 81.755  1.00 14.49 ? 98  PHE B CE2 1 
ATOM   4905 C CZ  . PHE B 1 98  ? 15.497  -13.116 81.601  1.00 16.33 ? 98  PHE B CZ  1 
ATOM   4906 N N   . THR B 1 99  ? 13.146  -8.087  84.546  1.00 17.79 ? 99  THR B N   1 
ATOM   4907 C CA  . THR B 1 99  ? 12.384  -7.244  83.636  1.00 11.03 ? 99  THR B CA  1 
ATOM   4908 C C   . THR B 1 99  ? 13.129  -5.946  83.323  1.00 15.74 ? 99  THR B C   1 
ATOM   4909 O O   . THR B 1 99  ? 13.187  -5.515  82.161  1.00 12.87 ? 99  THR B O   1 
ATOM   4910 C CB  . THR B 1 99  ? 11.010  -6.958  84.257  1.00 14.82 ? 99  THR B CB  1 
ATOM   4911 O OG1 . THR B 1 99  ? 10.322  -8.203  84.518  1.00 15.44 ? 99  THR B OG1 1 
ATOM   4912 C CG2 . THR B 1 99  ? 10.171  -6.106  83.349  1.00 9.88  ? 99  THR B CG2 1 
ATOM   4913 N N   . LYS B 1 100 ? 13.717  -5.320  84.347  1.00 14.52 ? 100 LYS B N   1 
ATOM   4914 C CA  . LYS B 1 100 ? 14.449  -4.071  84.142  1.00 16.82 ? 100 LYS B CA  1 
ATOM   4915 C C   . LYS B 1 100 ? 15.682  -4.288  83.275  1.00 16.75 ? 100 LYS B C   1 
ATOM   4916 O O   . LYS B 1 100 ? 16.064  -3.413  82.489  1.00 22.24 ? 100 LYS B O   1 
ATOM   4917 C CB  . LYS B 1 100 ? 14.852  -3.477  85.492  1.00 23.29 ? 100 LYS B CB  1 
ATOM   4918 C CG  . LYS B 1 100 ? 13.683  -3.062  86.374  1.00 30.94 ? 100 LYS B CG  1 
ATOM   4919 C CD  . LYS B 1 100 ? 14.105  -2.076  87.465  1.00 39.35 ? 100 LYS B CD  1 
ATOM   4920 C CE  . LYS B 1 100 ? 14.912  -2.742  88.572  1.00 48.77 ? 100 LYS B CE  1 
ATOM   4921 N NZ  . LYS B 1 100 ? 16.354  -2.978  88.238  1.00 52.79 ? 100 LYS B NZ  1 
ATOM   4922 N N   . LEU B 1 101 ? 16.321  -5.447  83.403  1.00 11.26 ? 101 LEU B N   1 
ATOM   4923 C CA  . LEU B 1 101 ? 17.482  -5.733  82.569  1.00 15.18 ? 101 LEU B CA  1 
ATOM   4924 C C   . LEU B 1 101 ? 17.103  -5.779  81.094  1.00 22.66 ? 101 LEU B C   1 
ATOM   4925 O O   . LEU B 1 101 ? 17.866  -5.325  80.231  1.00 20.08 ? 101 LEU B O   1 
ATOM   4926 C CB  . LEU B 1 101 ? 18.122  -7.056  82.991  1.00 22.53 ? 101 LEU B CB  1 
ATOM   4927 C CG  . LEU B 1 101 ? 19.120  -7.564  81.947  1.00 30.44 ? 101 LEU B CG  1 
ATOM   4928 C CD1 . LEU B 1 101 ? 20.408  -6.748  82.056  1.00 29.56 ? 101 LEU B CD1 1 
ATOM   4929 C CD2 . LEU B 1 101 ? 19.396  -9.066  82.058  1.00 33.70 ? 101 LEU B CD2 1 
ATOM   4930 N N   . ASN B 1 102 ? 15.919  -6.305  80.786  1.00 14.56 ? 102 ASN B N   1 
ATOM   4931 C CA  . ASN B 1 102 ? 15.497  -6.566  79.417  1.00 12.83 ? 102 ASN B CA  1 
ATOM   4932 C C   . ASN B 1 102 ? 14.543  -5.508  78.873  1.00 13.83 ? 102 ASN B C   1 
ATOM   4933 O O   . ASN B 1 102 ? 14.158  -5.578  77.695  1.00 13.22 ? 102 ASN B O   1 
ATOM   4934 C CB  . ASN B 1 102 ? 14.829  -7.947  79.347  1.00 12.78 ? 102 ASN B CB  1 
ATOM   4935 C CG  . ASN B 1 102 ? 15.825  -9.080  79.477  1.00 25.35 ? 102 ASN B CG  1 
ATOM   4936 O OD1 . ASN B 1 102 ? 16.655  -9.289  78.593  1.00 18.31 ? 102 ASN B OD1 1 
ATOM   4937 N ND2 . ASN B 1 102 ? 15.751  -9.817  80.581  1.00 20.63 ? 102 ASN B ND2 1 
ATOM   4938 N N   . TYR B 1 103 ? 14.193  -4.524  79.706  1.00 16.01 ? 103 TYR B N   1 
ATOM   4939 C CA  . TYR B 1 103 ? 13.084  -3.599  79.478  1.00 21.23 ? 103 TYR B CA  1 
ATOM   4940 C C   . TYR B 1 103 ? 13.159  -2.878  78.131  1.00 24.85 ? 103 TYR B C   1 
ATOM   4941 O O   . TYR B 1 103 ? 12.126  -2.607  77.497  1.00 16.53 ? 103 TYR B O   1 
ATOM   4942 C CB  . TYR B 1 103 ? 13.091  -2.582  80.625  1.00 27.51 ? 103 TYR B CB  1 
ATOM   4943 C CG  . TYR B 1 103 ? 11.962  -1.601  80.640  1.00 28.48 ? 103 TYR B CG  1 
ATOM   4944 C CD1 . TYR B 1 103 ? 10.766  -1.905  81.268  1.00 34.52 ? 103 TYR B CD1 1 
ATOM   4945 C CD2 . TYR B 1 103 ? 12.097  -0.353  80.050  1.00 29.35 ? 103 TYR B CD2 1 
ATOM   4946 C CE1 . TYR B 1 103 ? 9.725   -0.996  81.295  1.00 32.59 ? 103 TYR B CE1 1 
ATOM   4947 C CE2 . TYR B 1 103 ? 11.062  0.562   80.070  1.00 30.33 ? 103 TYR B CE2 1 
ATOM   4948 C CZ  . TYR B 1 103 ? 9.880   0.234   80.692  1.00 34.87 ? 103 TYR B CZ  1 
ATOM   4949 O OH  . TYR B 1 103 ? 8.855   1.148   80.722  1.00 38.64 ? 103 TYR B OH  1 
ATOM   4950 N N   . GLU B 1 104 ? 14.362  -2.516  77.701  1.00 20.37 ? 104 GLU B N   1 
ATOM   4951 C CA  . GLU B 1 104 ? 14.512  -1.692  76.510  1.00 22.18 ? 104 GLU B CA  1 
ATOM   4952 C C   . GLU B 1 104 ? 14.571  -2.513  75.232  1.00 21.29 ? 104 GLU B C   1 
ATOM   4953 O O   . GLU B 1 104 ? 14.579  -1.935  74.141  1.00 21.28 ? 104 GLU B O   1 
ATOM   4954 C CB  . GLU B 1 104 ? 15.770  -0.824  76.629  1.00 24.61 ? 104 GLU B CB  1 
ATOM   4955 C CG  . GLU B 1 104 ? 15.687  0.230   77.728  1.00 31.14 ? 104 GLU B CG  1 
ATOM   4956 C CD  . GLU B 1 104 ? 14.540  1.207   77.520  1.00 35.25 ? 104 GLU B CD  1 
ATOM   4957 O OE1 . GLU B 1 104 ? 14.090  1.827   78.511  1.00 46.47 ? 104 GLU B OE1 1 
ATOM   4958 O OE2 . GLU B 1 104 ? 14.082  1.361   76.369  1.00 40.19 ? 104 GLU B OE2 1 
ATOM   4959 N N   . LYS B 1 105 ? 14.604  -3.832  75.338  1.00 17.09 ? 105 LYS B N   1 
ATOM   4960 C CA  . LYS B 1 105 ? 14.712  -4.660  74.145  1.00 15.95 ? 105 LYS B CA  1 
ATOM   4961 C C   . LYS B 1 105 ? 13.383  -4.680  73.395  1.00 17.80 ? 105 LYS B C   1 
ATOM   4962 O O   . LYS B 1 105 ? 12.312  -4.712  74.012  1.00 15.36 ? 105 LYS B O   1 
ATOM   4963 C CB  . LYS B 1 105 ? 15.147  -6.082  74.516  1.00 10.65 ? 105 LYS B CB  1 
ATOM   4964 C CG  . LYS B 1 105 ? 16.581  -6.145  75.056  1.00 16.78 ? 105 LYS B CG  1 
ATOM   4965 C CD  . LYS B 1 105 ? 16.950  -7.526  75.609  1.00 13.61 ? 105 LYS B CD  1 
ATOM   4966 C CE  . LYS B 1 105 ? 18.275  -7.483  76.371  1.00 17.31 ? 105 LYS B CE  1 
ATOM   4967 N NZ  . LYS B 1 105 ? 18.681  -8.835  76.823  1.00 16.90 ? 105 LYS B NZ  1 
ATOM   4968 N N   . PRO B 1 106 ? 13.418  -4.654  72.063  1.00 17.34 ? 106 PRO B N   1 
ATOM   4969 C CA  . PRO B 1 106 ? 12.166  -4.662  71.292  1.00 15.01 ? 106 PRO B CA  1 
ATOM   4970 C C   . PRO B 1 106 ? 11.245  -5.833  71.585  1.00 12.70 ? 106 PRO B C   1 
ATOM   4971 O O   . PRO B 1 106 ? 10.018  -5.679  71.479  1.00 13.91 ? 106 PRO B O   1 
ATOM   4972 C CB  . PRO B 1 106 ? 12.668  -4.672  69.837  1.00 17.42 ? 106 PRO B CB  1 
ATOM   4973 C CG  . PRO B 1 106 ? 13.969  -3.951  69.914  1.00 16.96 ? 106 PRO B CG  1 
ATOM   4974 C CD  . PRO B 1 106 ? 14.589  -4.361  71.219  1.00 14.20 ? 106 PRO B CD  1 
ATOM   4975 N N   . ILE B 1 107 ? 11.769  -7.003  71.961  1.00 13.06 ? 107 ILE B N   1 
ATOM   4976 C CA  . ILE B 1 107 ? 10.867  -8.104  72.281  1.00 12.65 ? 107 ILE B CA  1 
ATOM   4977 C C   . ILE B 1 107 ? 10.134  -7.891  73.593  1.00 11.35 ? 107 ILE B C   1 
ATOM   4978 O O   . ILE B 1 107 ? 9.201   -8.649  73.900  1.00 14.26 ? 107 ILE B O   1 
ATOM   4979 C CB  . ILE B 1 107 ? 11.599  -9.463  72.311  1.00 5.25  ? 107 ILE B CB  1 
ATOM   4980 C CG1 . ILE B 1 107 ? 12.739  -9.486  73.326  1.00 5.95  ? 107 ILE B CG1 1 
ATOM   4981 C CG2 . ILE B 1 107 ? 12.134  -9.826  70.908  1.00 10.70 ? 107 ILE B CG2 1 
ATOM   4982 C CD1 . ILE B 1 107 ? 13.276  -10.939 73.600  1.00 8.03  ? 107 ILE B CD1 1 
ATOM   4983 N N   . TYR B 1 108 ? 10.515  -6.871  74.372  1.00 11.28 ? 108 TYR B N   1 
ATOM   4984 C CA  . TYR B 1 108 ? 9.812   -6.535  75.598  1.00 13.83 ? 108 TYR B CA  1 
ATOM   4985 C C   . TYR B 1 108 ? 8.877   -5.335  75.440  1.00 16.69 ? 108 TYR B C   1 
ATOM   4986 O O   . TYR B 1 108 ? 8.410   -4.800  76.449  1.00 16.01 ? 108 TYR B O   1 
ATOM   4987 C CB  . TYR B 1 108 ? 10.815  -6.274  76.722  1.00 12.60 ? 108 TYR B CB  1 
ATOM   4988 C CG  . TYR B 1 108 ? 11.142  -7.499  77.535  1.00 15.17 ? 108 TYR B CG  1 
ATOM   4989 C CD1 . TYR B 1 108 ? 12.036  -8.452  77.065  1.00 10.66 ? 108 TYR B CD1 1 
ATOM   4990 C CD2 . TYR B 1 108 ? 10.562  -7.701  78.776  1.00 15.92 ? 108 TYR B CD2 1 
ATOM   4991 C CE1 . TYR B 1 108 ? 12.333  -9.594  77.815  1.00 14.24 ? 108 TYR B CE1 1 
ATOM   4992 C CE2 . TYR B 1 108 ? 10.850  -8.830  79.527  1.00 11.91 ? 108 TYR B CE2 1 
ATOM   4993 C CZ  . TYR B 1 108 ? 11.750  -9.767  79.046  1.00 14.81 ? 108 TYR B CZ  1 
ATOM   4994 O OH  . TYR B 1 108 ? 12.037  -10.884 79.803  1.00 14.17 ? 108 TYR B OH  1 
ATOM   4995 N N   . ARG B 1 109 ? 8.560   -4.920  74.210  1.00 10.90 ? 109 ARG B N   1 
ATOM   4996 C CA  . ARG B 1 109 ? 7.766   -3.699  74.012  1.00 19.87 ? 109 ARG B CA  1 
ATOM   4997 C C   . ARG B 1 109 ? 6.287   -4.040  74.146  1.00 16.80 ? 109 ARG B C   1 
ATOM   4998 O O   . ARG B 1 109 ? 5.554   -4.207  73.168  1.00 20.94 ? 109 ARG B O   1 
ATOM   4999 C CB  . ARG B 1 109 ? 8.062   -3.046  72.666  1.00 33.34 ? 109 ARG B CB  1 
ATOM   5000 C CG  . ARG B 1 109 ? 9.521   -2.846  72.372  1.00 48.94 ? 109 ARG B CG  1 
ATOM   5001 C CD  . ARG B 1 109 ? 9.911   -1.379  72.194  1.00 56.23 ? 109 ARG B CD  1 
ATOM   5002 N NE  . ARG B 1 109 ? 9.787   -0.951  70.804  1.00 52.44 ? 109 ARG B NE  1 
ATOM   5003 C CZ  . ARG B 1 109 ? 10.808  -0.861  69.958  1.00 48.62 ? 109 ARG B CZ  1 
ATOM   5004 N NH1 . ARG B 1 109 ? 12.032  -1.182  70.353  1.00 44.25 ? 109 ARG B NH1 1 
ATOM   5005 N NH2 . ARG B 1 109 ? 10.602  -0.451  68.713  1.00 50.69 ? 109 ARG B NH2 1 
ATOM   5006 N N   . PHE B 1 110 ? 5.859   -4.185  75.395  1.00 11.21 ? 110 PHE B N   1 
ATOM   5007 C CA  . PHE B 1 110 ? 4.459   -4.336  75.752  1.00 12.54 ? 110 PHE B CA  1 
ATOM   5008 C C   . PHE B 1 110 ? 4.077   -3.137  76.594  1.00 14.49 ? 110 PHE B C   1 
ATOM   5009 O O   . PHE B 1 110 ? 4.776   -2.818  77.562  1.00 16.78 ? 110 PHE B O   1 
ATOM   5010 C CB  . PHE B 1 110 ? 4.204   -5.621  76.549  1.00 14.74 ? 110 PHE B CB  1 
ATOM   5011 C CG  . PHE B 1 110 ? 4.511   -6.884  75.798  1.00 13.90 ? 110 PHE B CG  1 
ATOM   5012 C CD1 . PHE B 1 110 ? 3.556   -7.486  74.990  1.00 10.24 ? 110 PHE B CD1 1 
ATOM   5013 C CD2 . PHE B 1 110 ? 5.747   -7.498  75.936  1.00 20.81 ? 110 PHE B CD2 1 
ATOM   5014 C CE1 . PHE B 1 110 ? 3.840   -8.667  74.323  1.00 13.76 ? 110 PHE B CE1 1 
ATOM   5015 C CE2 . PHE B 1 110 ? 6.035   -8.673  75.270  1.00 23.23 ? 110 PHE B CE2 1 
ATOM   5016 C CZ  . PHE B 1 110 ? 5.080   -9.264  74.466  1.00 18.78 ? 110 PHE B CZ  1 
ATOM   5017 N N   . GLU B 1 111 ? 2.980   -2.467  76.217  1.00 19.29 ? 111 GLU B N   1 
ATOM   5018 C CA  . GLU B 1 111 ? 2.486   -1.342  77.007  1.00 24.13 ? 111 GLU B CA  1 
ATOM   5019 C C   . GLU B 1 111 ? 2.301   -1.742  78.462  1.00 17.23 ? 111 GLU B C   1 
ATOM   5020 O O   . GLU B 1 111 ? 2.609   -0.968  79.376  1.00 20.27 ? 111 GLU B O   1 
ATOM   5021 C CB  . GLU B 1 111 ? 1.166   -0.830  76.429  1.00 31.63 ? 111 GLU B CB  1 
ATOM   5022 C CG  . GLU B 1 111 ? 0.915   0.625   76.731  1.00 42.16 ? 111 GLU B CG  1 
ATOM   5023 C CD  . GLU B 1 111 ? 2.124   1.494   76.424  1.00 62.74 ? 111 GLU B CD  1 
ATOM   5024 O OE1 . GLU B 1 111 ? 2.720   1.328   75.334  1.00 69.81 ? 111 GLU B OE1 1 
ATOM   5025 O OE2 . GLU B 1 111 ? 2.486   2.335   77.276  1.00 65.02 ? 111 GLU B OE2 1 
ATOM   5026 N N   . ARG B 1 112 ? 1.842   -2.973  78.690  1.00 17.36 ? 112 ARG B N   1 
ATOM   5027 C CA  . ARG B 1 112 ? 1.575   -3.432  80.046  1.00 17.50 ? 112 ARG B CA  1 
ATOM   5028 C C   . ARG B 1 112 ? 2.850   -3.542  80.871  1.00 14.84 ? 112 ARG B C   1 
ATOM   5029 O O   . ARG B 1 112 ? 2.814   -3.355  82.089  1.00 19.00 ? 112 ARG B O   1 
ATOM   5030 C CB  . ARG B 1 112 ? 0.847   -4.770  79.995  1.00 15.72 ? 112 ARG B CB  1 
ATOM   5031 C CG  . ARG B 1 112 ? 0.494   -5.377  81.351  1.00 20.11 ? 112 ARG B CG  1 
ATOM   5032 C CD  . ARG B 1 112 ? -0.289  -4.437  82.234  1.00 18.53 ? 112 ARG B CD  1 
ATOM   5033 N NE  . ARG B 1 112 ? -0.992  -5.181  83.285  1.00 17.97 ? 112 ARG B NE  1 
ATOM   5034 C CZ  . ARG B 1 112 ? -1.646  -4.608  84.286  1.00 24.74 ? 112 ARG B CZ  1 
ATOM   5035 N NH1 . ARG B 1 112 ? -1.684  -3.281  84.375  1.00 17.60 ? 112 ARG B NH1 1 
ATOM   5036 N NH2 . ARG B 1 112 ? -2.260  -5.360  85.193  1.00 17.98 ? 112 ARG B NH2 1 
ATOM   5037 N N   . ILE B 1 113 ? 3.986   -3.852  80.240  1.00 15.57 ? 113 ILE B N   1 
ATOM   5038 C CA  . ILE B 1 113 ? 5.234   -3.881  80.999  1.00 16.56 ? 113 ILE B CA  1 
ATOM   5039 C C   . ILE B 1 113 ? 5.594   -2.482  81.481  1.00 21.50 ? 113 ILE B C   1 
ATOM   5040 O O   . ILE B 1 113 ? 6.048   -2.304  82.619  1.00 19.73 ? 113 ILE B O   1 
ATOM   5041 C CB  . ILE B 1 113 ? 6.361   -4.505  80.164  1.00 18.78 ? 113 ILE B CB  1 
ATOM   5042 C CG1 . ILE B 1 113 ? 6.125   -6.002  80.038  1.00 16.29 ? 113 ILE B CG1 1 
ATOM   5043 C CG2 . ILE B 1 113 ? 7.718   -4.264  80.823  1.00 22.12 ? 113 ILE B CG2 1 
ATOM   5044 C CD1 . ILE B 1 113 ? 7.201   -6.730  79.303  1.00 19.54 ? 113 ILE B CD1 1 
ATOM   5045 N N   . ARG B 1 114 ? 5.372   -1.467  80.635  1.00 19.23 ? 114 ARG B N   1 
ATOM   5046 C CA  . ARG B 1 114 ? 5.613   -0.081  81.037  1.00 19.54 ? 114 ARG B CA  1 
ATOM   5047 C C   . ARG B 1 114 ? 4.746   0.314   82.232  1.00 19.91 ? 114 ARG B C   1 
ATOM   5048 O O   . ARG B 1 114 ? 5.223   0.984   83.155  1.00 23.47 ? 114 ARG B O   1 
ATOM   5049 C CB  . ARG B 1 114 ? 5.356   0.861   79.852  1.00 21.64 ? 114 ARG B CB  1 
ATOM   5050 C CG  . ARG B 1 114 ? 6.429   0.795   78.772  1.00 43.92 ? 114 ARG B CG  1 
ATOM   5051 C CD  . ARG B 1 114 ? 6.205   1.825   77.666  1.00 53.37 ? 114 ARG B CD  1 
ATOM   5052 N NE  . ARG B 1 114 ? 5.370   1.315   76.577  1.00 55.66 ? 114 ARG B NE  1 
ATOM   5053 C CZ  . ARG B 1 114 ? 5.792   0.474   75.635  1.00 52.17 ? 114 ARG B CZ  1 
ATOM   5054 N NH1 . ARG B 1 114 ? 7.045   0.034   75.642  1.00 48.22 ? 114 ARG B NH1 1 
ATOM   5055 N NH2 . ARG B 1 114 ? 4.959   0.070   74.685  1.00 49.64 ? 114 ARG B NH2 1 
ATOM   5056 N N   . GLU B 1 115 ? 3.470   -0.088  82.234  1.00 21.70 ? 115 GLU B N   1 
ATOM   5057 C CA  . GLU B 1 115 ? 2.597   0.199   83.374  1.00 18.25 ? 115 GLU B CA  1 
ATOM   5058 C C   . GLU B 1 115 ? 3.079   -0.499  84.641  1.00 25.66 ? 115 GLU B C   1 
ATOM   5059 O O   . GLU B 1 115 ? 3.108   0.096   85.723  1.00 26.87 ? 115 GLU B O   1 
ATOM   5060 C CB  . GLU B 1 115 ? 1.165   -0.241  83.077  1.00 20.53 ? 115 GLU B CB  1 
ATOM   5061 C CG  . GLU B 1 115 ? 0.527   0.333   81.848  1.00 22.47 ? 115 GLU B CG  1 
ATOM   5062 C CD  . GLU B 1 115 ? -0.788  -0.353  81.528  1.00 35.63 ? 115 GLU B CD  1 
ATOM   5063 O OE1 . GLU B 1 115 ? -1.252  -1.192  82.339  1.00 31.63 ? 115 GLU B OE1 1 
ATOM   5064 O OE2 . GLU B 1 115 ? -1.361  -0.057  80.463  1.00 37.15 ? 115 GLU B OE2 1 
ATOM   5065 N N   . LEU B 1 116 ? 3.417   -1.786  84.529  1.00 17.92 ? 116 LEU B N   1 
ATOM   5066 C CA  . LEU B 1 116 ? 3.821   -2.571  85.693  1.00 19.24 ? 116 LEU B CA  1 
ATOM   5067 C C   . LEU B 1 116 ? 5.076   -2.006  86.352  1.00 29.07 ? 116 LEU B C   1 
ATOM   5068 O O   . LEU B 1 116 ? 5.159   -1.934  87.585  1.00 24.69 ? 116 LEU B O   1 
ATOM   5069 C CB  . LEU B 1 116 ? 4.056   -4.026  85.277  1.00 19.42 ? 116 LEU B CB  1 
ATOM   5070 C CG  . LEU B 1 116 ? 2.954   -5.090  85.395  1.00 28.22 ? 116 LEU B CG  1 
ATOM   5071 C CD1 . LEU B 1 116 ? 1.573   -4.498  85.661  1.00 26.34 ? 116 LEU B CD1 1 
ATOM   5072 C CD2 . LEU B 1 116 ? 2.942   -6.030  84.174  1.00 20.17 ? 116 LEU B CD2 1 
ATOM   5073 N N   . MET B 1 117 ? 6.073   -1.621  85.555  1.00 29.21 ? 117 MET B N   1 
ATOM   5074 C CA  . MET B 1 117 ? 7.319   -1.102  86.107  1.00 24.44 ? 117 MET B CA  1 
ATOM   5075 C C   . MET B 1 117 ? 7.189   0.327   86.609  1.00 30.87 ? 117 MET B C   1 
ATOM   5076 O O   . MET B 1 117 ? 8.156   0.866   87.157  1.00 35.56 ? 117 MET B O   1 
ATOM   5077 C CB  . MET B 1 117 ? 8.447   -1.196  85.071  1.00 23.93 ? 117 MET B CB  1 
ATOM   5078 C CG  . MET B 1 117 ? 8.774   -2.632  84.683  1.00 24.30 ? 117 MET B CG  1 
ATOM   5079 S SD  . MET B 1 117 ? 9.618   -3.489  86.034  1.00 34.26 ? 117 MET B SD  1 
ATOM   5080 C CE  . MET B 1 117 ? 8.296   -4.342  86.857  1.00 34.89 ? 117 MET B CE  1 
ATOM   5081 N N   . ASN B 1 118 ? 6.021   0.937   86.437  1.00 30.65 ? 118 ASN B N   1 
ATOM   5082 C CA  . ASN B 1 118 ? 5.727   2.260   86.951  1.00 38.30 ? 118 ASN B CA  1 
ATOM   5083 C C   . ASN B 1 118 ? 4.790   2.219   88.146  1.00 39.64 ? 118 ASN B C   1 
ATOM   5084 O O   . ASN B 1 118 ? 4.475   3.272   88.706  1.00 42.85 ? 118 ASN B O   1 
ATOM   5085 C CB  . ASN B 1 118 ? 5.118   3.127   85.845  1.00 41.93 ? 118 ASN B CB  1 
ATOM   5086 C CG  . ASN B 1 118 ? 6.166   3.724   84.939  1.00 44.15 ? 118 ASN B CG  1 
ATOM   5087 O OD1 . ASN B 1 118 ? 7.141   4.308   85.407  1.00 48.54 ? 118 ASN B OD1 1 
ATOM   5088 N ND2 . ASN B 1 118 ? 5.981   3.570   83.632  1.00 49.36 ? 118 ASN B ND2 1 
ATOM   5089 N N   . LYS B 1 119 ? 4.330   1.037   88.541  1.00 38.10 ? 119 LYS B N   1 
ATOM   5090 C CA  . LYS B 1 119 ? 3.439   0.896   89.679  1.00 35.72 ? 119 LYS B CA  1 
ATOM   5091 C C   . LYS B 1 119 ? 4.267   0.688   90.938  1.00 37.75 ? 119 LYS B C   1 
ATOM   5092 O O   . LYS B 1 119 ? 5.332   0.065   90.897  1.00 34.89 ? 119 LYS B O   1 
ATOM   5093 C CB  . LYS B 1 119 ? 2.469   -0.266  89.462  1.00 35.48 ? 119 LYS B CB  1 
ATOM   5094 C CG  . LYS B 1 119 ? 1.087   -0.023  90.021  1.00 45.73 ? 119 LYS B CG  1 
ATOM   5095 C CD  . LYS B 1 119 ? 0.621   -1.229  90.804  1.00 49.26 ? 119 LYS B CD  1 
ATOM   5096 C CE  . LYS B 1 119 ? -0.745  -1.029  91.439  1.00 50.87 ? 119 LYS B CE  1 
ATOM   5097 N NZ  . LYS B 1 119 ? -1.135  -2.211  92.265  1.00 49.73 ? 119 LYS B NZ  1 
ATOM   5098 N N   . GLU B 1 120 ? 3.790   1.249   92.052  1.00 42.68 ? 120 GLU B N   1 
ATOM   5099 C CA  . GLU B 1 120 ? 4.571   1.222   93.284  1.00 45.16 ? 120 GLU B CA  1 
ATOM   5100 C C   . GLU B 1 120 ? 4.787   -0.207  93.764  1.00 42.91 ? 120 GLU B C   1 
ATOM   5101 O O   . GLU B 1 120 ? 5.925   -0.666  93.887  1.00 45.66 ? 120 GLU B O   1 
ATOM   5102 C CB  . GLU B 1 120 ? 3.888   2.076   94.352  1.00 46.34 ? 120 GLU B CB  1 
ATOM   5103 C CG  . GLU B 1 120 ? 3.986   3.570   94.052  1.00 53.17 ? 120 GLU B CG  1 
ATOM   5104 C CD  . GLU B 1 120 ? 3.149   4.429   94.984  1.00 58.60 ? 120 GLU B CD  1 
ATOM   5105 O OE1 . GLU B 1 120 ? 1.949   4.625   94.692  1.00 60.07 ? 120 GLU B OE1 1 
ATOM   5106 O OE2 . GLU B 1 120 ? 3.697   4.923   95.994  1.00 55.10 ? 120 GLU B OE2 1 
ATOM   5107 N N   . LYS B 1 121 ? 3.702   -0.934  94.015  1.00 44.27 ? 121 LYS B N   1 
ATOM   5108 C CA  . LYS B 1 121 ? 3.771   -2.342  94.383  1.00 43.89 ? 121 LYS B CA  1 
ATOM   5109 C C   . LYS B 1 121 ? 2.694   -3.098  93.613  1.00 36.55 ? 121 LYS B C   1 
ATOM   5110 O O   . LYS B 1 121 ? 1.670   -2.533  93.225  1.00 38.29 ? 121 LYS B O   1 
ATOM   5111 C CB  . LYS B 1 121 ? 3.607   -2.544  95.898  1.00 49.06 ? 121 LYS B CB  1 
ATOM   5112 C CG  . LYS B 1 121 ? 4.620   -1.781  96.762  1.00 55.84 ? 121 LYS B CG  1 
ATOM   5113 C CD  . LYS B 1 121 ? 5.903   -2.574  97.076  1.00 59.60 ? 121 LYS B CD  1 
ATOM   5114 C CE  . LYS B 1 121 ? 6.890   -2.591  95.905  1.00 61.38 ? 121 LYS B CE  1 
ATOM   5115 N NZ  . LYS B 1 121 ? 8.314   -2.535  96.341  1.00 60.33 ? 121 LYS B NZ  1 
ATOM   5116 N N   . LEU B 1 122 ? 2.927   -4.390  93.399  1.00 27.18 ? 122 LEU B N   1 
ATOM   5117 C CA  . LEU B 1 122 ? 2.130   -5.180  92.469  1.00 21.79 ? 122 LEU B CA  1 
ATOM   5118 C C   . LEU B 1 122 ? 1.217   -6.141  93.218  1.00 17.87 ? 122 LEU B C   1 
ATOM   5119 O O   . LEU B 1 122 ? 1.660   -6.832  94.142  1.00 21.11 ? 122 LEU B O   1 
ATOM   5120 C CB  . LEU B 1 122 ? 3.039   -5.965  91.518  1.00 27.29 ? 122 LEU B CB  1 
ATOM   5121 C CG  . LEU B 1 122 ? 4.021   -5.128  90.698  1.00 24.52 ? 122 LEU B CG  1 
ATOM   5122 C CD1 . LEU B 1 122 ? 5.085   -6.019  90.053  1.00 19.98 ? 122 LEU B CD1 1 
ATOM   5123 C CD2 . LEU B 1 122 ? 3.287   -4.305  89.653  1.00 21.37 ? 122 LEU B CD2 1 
ATOM   5124 N N   . ASN B 1 123 ? -0.053  -6.199  92.803  1.00 22.88 ? 123 ASN B N   1 
ATOM   5125 C CA  . ASN B 1 123 ? -0.990  -7.161  93.361  1.00 21.95 ? 123 ASN B CA  1 
ATOM   5126 C C   . ASN B 1 123 ? -0.881  -8.469  92.573  1.00 22.39 ? 123 ASN B C   1 
ATOM   5127 O O   . ASN B 1 123 ? 0.015   -8.639  91.741  1.00 15.34 ? 123 ASN B O   1 
ATOM   5128 C CB  . ASN B 1 123 ? -2.405  -6.577  93.385  1.00 17.59 ? 123 ASN B CB  1 
ATOM   5129 C CG  . ASN B 1 123 ? -2.879  -6.110  92.019  1.00 23.22 ? 123 ASN B CG  1 
ATOM   5130 O OD1 . ASN B 1 123 ? -2.695  -6.792  91.008  1.00 16.90 ? 123 ASN B OD1 1 
ATOM   5131 N ND2 . ASN B 1 123 ? -3.495  -4.935  91.985  1.00 27.42 ? 123 ASN B ND2 1 
ATOM   5132 N N   . ARG B 1 124 ? -1.790  -9.415  92.834  1.00 17.28 ? 124 ARG B N   1 
ATOM   5133 C CA  . ARG B 1 124 ? -1.688  -10.732 92.202  1.00 14.62 ? 124 ARG B CA  1 
ATOM   5134 C C   . ARG B 1 124 ? -1.917  -10.662 90.691  1.00 12.62 ? 124 ARG B C   1 
ATOM   5135 O O   . ARG B 1 124 ? -1.198  -11.307 89.925  1.00 14.56 ? 124 ARG B O   1 
ATOM   5136 C CB  . ARG B 1 124 ? -2.684  -11.707 92.838  1.00 16.43 ? 124 ARG B CB  1 
ATOM   5137 C CG  . ARG B 1 124 ? -2.624  -13.112 92.235  1.00 20.91 ? 124 ARG B CG  1 
ATOM   5138 C CD  . ARG B 1 124 ? -3.640  -14.076 92.854  1.00 23.13 ? 124 ARG B CD  1 
ATOM   5139 N NE  . ARG B 1 124 ? -3.598  -15.371 92.171  1.00 23.32 ? 124 ARG B NE  1 
ATOM   5140 C CZ  . ARG B 1 124 ? -4.263  -15.642 91.052  1.00 17.93 ? 124 ARG B CZ  1 
ATOM   5141 N NH1 . ARG B 1 124 ? -5.044  -14.721 90.500  1.00 21.82 ? 124 ARG B NH1 1 
ATOM   5142 N NH2 . ARG B 1 124 ? -4.151  -16.828 90.487  1.00 21.77 ? 124 ARG B NH2 1 
ATOM   5143 N N   . GLU B 1 125 ? -2.936  -9.925  90.245  1.00 10.58 ? 125 GLU B N   1 
ATOM   5144 C CA  . GLU B 1 125 ? -3.200  -9.828  88.807  1.00 16.03 ? 125 GLU B CA  1 
ATOM   5145 C C   . GLU B 1 125 ? -2.047  -9.142  88.081  1.00 15.22 ? 125 GLU B C   1 
ATOM   5146 O O   . GLU B 1 125 ? -1.698  -9.509  86.949  1.00 12.96 ? 125 GLU B O   1 
ATOM   5147 C CB  . GLU B 1 125 ? -4.515  -9.076  88.557  1.00 24.82 ? 125 GLU B CB  1 
ATOM   5148 C CG  . GLU B 1 125 ? -5.746  -9.949  88.680  1.00 36.64 ? 125 GLU B CG  1 
ATOM   5149 C CD  . GLU B 1 125 ? -7.057  -9.188  88.481  1.00 48.70 ? 125 GLU B CD  1 
ATOM   5150 O OE1 . GLU B 1 125 ? -7.048  -8.109  87.847  1.00 49.86 ? 125 GLU B OE1 1 
ATOM   5151 O OE2 . GLU B 1 125 ? -8.101  -9.680  88.963  1.00 52.92 ? 125 GLU B OE2 1 
ATOM   5152 N N   . GLU B 1 126 ? -1.434  -8.153  88.720  1.00 14.39 ? 126 GLU B N   1 
ATOM   5153 C CA  . GLU B 1 126 ? -0.302  -7.486  88.093  1.00 13.41 ? 126 GLU B CA  1 
ATOM   5154 C C   . GLU B 1 126 ? 0.926   -8.396  88.039  1.00 13.13 ? 126 GLU B C   1 
ATOM   5155 O O   . GLU B 1 126 ? 1.663   -8.386  87.048  1.00 13.07 ? 126 GLU B O   1 
ATOM   5156 C CB  . GLU B 1 126 ? -0.024  -6.177  88.828  1.00 14.53 ? 126 GLU B CB  1 
ATOM   5157 C CG  . GLU B 1 126 ? -1.063  -5.102  88.500  1.00 13.16 ? 126 GLU B CG  1 
ATOM   5158 C CD  . GLU B 1 126 ? -1.172  -4.022  89.573  1.00 18.31 ? 126 GLU B CD  1 
ATOM   5159 O OE1 . GLU B 1 126 ? -0.495  -4.140  90.612  1.00 25.47 ? 126 GLU B OE1 1 
ATOM   5160 O OE2 . GLU B 1 126 ? -1.958  -3.069  89.379  1.00 25.87 ? 126 GLU B OE2 1 
ATOM   5161 N N   . LEU B 1 127 ? 1.148   -9.222  89.064  1.00 13.42 ? 127 LEU B N   1 
ATOM   5162 C CA  . LEU B 1 127 ? 2.289   -10.145 89.007  1.00 13.50 ? 127 LEU B CA  1 
ATOM   5163 C C   . LEU B 1 127 ? 2.074   -11.238 87.967  1.00 9.67  ? 127 LEU B C   1 
ATOM   5164 O O   . LEU B 1 127 ? 3.020   -11.646 87.279  1.00 11.63 ? 127 LEU B O   1 
ATOM   5165 C CB  . LEU B 1 127 ? 2.544   -10.754 90.381  1.00 14.28 ? 127 LEU B CB  1 
ATOM   5166 C CG  . LEU B 1 127 ? 3.175   -9.805  91.401  1.00 22.88 ? 127 LEU B CG  1 
ATOM   5167 C CD1 . LEU B 1 127 ? 2.910   -10.309 92.806  1.00 20.54 ? 127 LEU B CD1 1 
ATOM   5168 C CD2 . LEU B 1 127 ? 4.672   -9.706  91.152  1.00 25.14 ? 127 LEU B CD2 1 
ATOM   5169 N N   . LEU B 1 128 ? 0.845   -11.741 87.845  1.00 6.43  ? 128 LEU B N   1 
ATOM   5170 C CA  . LEU B 1 128 ? 0.539   -12.690 86.772  1.00 12.13 ? 128 LEU B CA  1 
ATOM   5171 C C   . LEU B 1 128 ? 0.890   -12.116 85.404  1.00 12.93 ? 128 LEU B C   1 
ATOM   5172 O O   . LEU B 1 128 ? 1.434   -12.822 84.543  1.00 14.84 ? 128 LEU B O   1 
ATOM   5173 C CB  . LEU B 1 128 ? -0.938  -13.077 86.808  1.00 8.33  ? 128 LEU B CB  1 
ATOM   5174 C CG  . LEU B 1 128 ? -1.205  -14.456 87.409  1.00 13.30 ? 128 LEU B CG  1 
ATOM   5175 C CD1 . LEU B 1 128 ? -2.706  -14.660 87.576  1.00 25.56 ? 128 LEU B CD1 1 
ATOM   5176 C CD2 . LEU B 1 128 ? -0.604  -15.528 86.533  1.00 14.13 ? 128 LEU B CD2 1 
ATOM   5177 N N   . ASP B 1 129 ? 0.581   -10.837 85.182  1.00 5.92  ? 129 ASP B N   1 
ATOM   5178 C CA  . ASP B 1 129 ? 0.943   -10.218 83.916  1.00 10.71 ? 129 ASP B CA  1 
ATOM   5179 C C   . ASP B 1 129 ? 2.457   -10.109 83.789  1.00 12.24 ? 129 ASP B C   1 
ATOM   5180 O O   . ASP B 1 129 ? 3.009   -10.357 82.717  1.00 10.49 ? 129 ASP B O   1 
ATOM   5181 C CB  . ASP B 1 129 ? 0.299   -8.842  83.781  1.00 9.97  ? 129 ASP B CB  1 
ATOM   5182 C CG  . ASP B 1 129 ? -1.184  -8.923  83.424  1.00 19.30 ? 129 ASP B CG  1 
ATOM   5183 O OD1 . ASP B 1 129 ? -1.689  -10.047 83.242  1.00 21.09 ? 129 ASP B OD1 1 
ATOM   5184 O OD2 . ASP B 1 129 ? -1.839  -7.867  83.306  1.00 20.90 ? 129 ASP B OD2 1 
ATOM   5185 N N   . LEU B 1 130 ? 3.140   -9.766  84.885  1.00 11.00 ? 130 LEU B N   1 
ATOM   5186 C CA  . LEU B 1 130 ? 4.595   -9.636  84.826  1.00 10.31 ? 130 LEU B CA  1 
ATOM   5187 C C   . LEU B 1 130 ? 5.252   -10.975 84.511  1.00 10.72 ? 130 LEU B C   1 
ATOM   5188 O O   . LEU B 1 130 ? 6.167   -11.042 83.681  1.00 10.84 ? 130 LEU B O   1 
ATOM   5189 C CB  . LEU B 1 130 ? 5.137   -9.062  86.146  1.00 9.06  ? 130 LEU B CB  1 
ATOM   5190 C CG  . LEU B 1 130 ? 6.644   -8.729  86.126  1.00 11.71 ? 130 LEU B CG  1 
ATOM   5191 C CD1 . LEU B 1 130 ? 6.933   -7.610  85.143  1.00 13.62 ? 130 LEU B CD1 1 
ATOM   5192 C CD2 . LEU B 1 130 ? 7.151   -8.353  87.515  1.00 16.52 ? 130 LEU B CD2 1 
ATOM   5193 N N   . GLN B 1 131 ? 4.794   -12.051 85.154  1.00 12.63 ? 131 GLN B N   1 
ATOM   5194 C CA  . GLN B 1 131 ? 5.306   -13.384 84.839  1.00 7.21  ? 131 GLN B CA  1 
ATOM   5195 C C   . GLN B 1 131 ? 5.016   -13.754 83.395  1.00 9.31  ? 131 GLN B C   1 
ATOM   5196 O O   . GLN B 1 131 ? 5.899   -14.216 82.667  1.00 9.61  ? 131 GLN B O   1 
ATOM   5197 C CB  . GLN B 1 131 ? 4.679   -14.441 85.751  1.00 8.21  ? 131 GLN B CB  1 
ATOM   5198 C CG  . GLN B 1 131 ? 4.902   -14.251 87.230  1.00 10.44 ? 131 GLN B CG  1 
ATOM   5199 C CD  . GLN B 1 131 ? 4.032   -15.175 88.063  1.00 10.09 ? 131 GLN B CD  1 
ATOM   5200 O OE1 . GLN B 1 131 ? 2.821   -15.298 87.833  1.00 13.54 ? 131 GLN B OE1 1 
ATOM   5201 N NE2 . GLN B 1 131 ? 4.652   -15.864 89.008  1.00 10.11 ? 131 GLN B NE2 1 
ATOM   5202 N N   . THR B 1 132 ? 3.764   -13.608 82.978  1.00 6.72  ? 132 THR B N   1 
ATOM   5203 C CA  . THR B 1 132 ? 3.376   -14.129 81.675  1.00 7.06  ? 132 THR B CA  1 
ATOM   5204 C C   . THR B 1 132 ? 3.995   -13.319 80.545  1.00 9.50  ? 132 THR B C   1 
ATOM   5205 O O   . THR B 1 132 ? 4.351   -13.881 79.495  1.00 12.77 ? 132 THR B O   1 
ATOM   5206 C CB  . THR B 1 132 ? 1.848   -14.140 81.546  1.00 10.23 ? 132 THR B CB  1 
ATOM   5207 O OG1 . THR B 1 132 ? 1.278   -14.791 82.694  1.00 8.99  ? 132 THR B OG1 1 
ATOM   5208 C CG2 . THR B 1 132 ? 1.433   -14.865 80.294  1.00 13.45 ? 132 THR B CG2 1 
ATOM   5209 N N   . LEU B 1 133 ? 4.120   -12.001 80.736  1.00 11.84 ? 133 LEU B N   1 
ATOM   5210 C CA  . LEU B 1 133 ? 4.727   -11.171 79.707  1.00 9.82  ? 133 LEU B CA  1 
ATOM   5211 C C   . LEU B 1 133 ? 6.226   -11.416 79.613  1.00 11.73 ? 133 LEU B C   1 
ATOM   5212 O O   . LEU B 1 133 ? 6.785   -11.348 78.516  1.00 7.87  ? 133 LEU B O   1 
ATOM   5213 C CB  . LEU B 1 133 ? 4.428   -9.689  79.963  1.00 11.74 ? 133 LEU B CB  1 
ATOM   5214 C CG  . LEU B 1 133 ? 2.996   -9.249  79.620  1.00 10.08 ? 133 LEU B CG  1 
ATOM   5215 C CD1 . LEU B 1 133 ? 2.636   -7.901  80.238  1.00 8.56  ? 133 LEU B CD1 1 
ATOM   5216 C CD2 . LEU B 1 133 ? 2.726   -9.271  78.110  1.00 13.95 ? 133 LEU B CD2 1 
ATOM   5217 N N   . ASN B 1 134 ? 6.901   -11.705 80.736  1.00 11.93 ? 134 ASN B N   1 
ATOM   5218 C CA  . ASN B 1 134 ? 8.294   -12.149 80.629  1.00 12.61 ? 134 ASN B CA  1 
ATOM   5219 C C   . ASN B 1 134 ? 8.402   -13.432 79.819  1.00 17.26 ? 134 ASN B C   1 
ATOM   5220 O O   . ASN B 1 134 ? 9.310   -13.584 78.989  1.00 12.07 ? 134 ASN B O   1 
ATOM   5221 C CB  . ASN B 1 134 ? 8.916   -12.329 82.017  1.00 4.46  ? 134 ASN B CB  1 
ATOM   5222 C CG  . ASN B 1 134 ? 9.596   -11.070 82.474  1.00 13.51 ? 134 ASN B CG  1 
ATOM   5223 O OD1 . ASN B 1 134 ? 10.727  -10.788 82.079  1.00 12.23 ? 134 ASN B OD1 1 
ATOM   5224 N ND2 . ASN B 1 134 ? 8.882   -10.267 83.249  1.00 10.64 ? 134 ASN B ND2 1 
ATOM   5225 N N   . LEU B 1 135 ? 7.480   -14.364 80.040  1.00 8.73  ? 135 LEU B N   1 
ATOM   5226 C CA  . LEU B 1 135 ? 7.432   -15.569 79.221  1.00 12.09 ? 135 LEU B CA  1 
ATOM   5227 C C   . LEU B 1 135 ? 7.214   -15.233 77.749  1.00 10.91 ? 135 LEU B C   1 
ATOM   5228 O O   . LEU B 1 135 ? 7.944   -15.716 76.879  1.00 10.17 ? 135 LEU B O   1 
ATOM   5229 C CB  . LEU B 1 135 ? 6.309   -16.472 79.709  1.00 15.01 ? 135 LEU B CB  1 
ATOM   5230 C CG  . LEU B 1 135 ? 6.522   -17.768 80.477  1.00 24.68 ? 135 LEU B CG  1 
ATOM   5231 C CD1 . LEU B 1 135 ? 5.284   -18.691 80.269  1.00 18.37 ? 135 LEU B CD1 1 
ATOM   5232 C CD2 . LEU B 1 135 ? 7.857   -18.475 80.165  1.00 10.06 ? 135 LEU B CD2 1 
ATOM   5233 N N   . LEU B 1 136 ? 6.187   -14.425 77.449  1.00 7.91  ? 136 LEU B N   1 
ATOM   5234 C CA  . LEU B 1 136 ? 5.802   -14.186 76.058  1.00 4.74  ? 136 LEU B CA  1 
ATOM   5235 C C   . LEU B 1 136 ? 6.828   -13.356 75.306  1.00 11.35 ? 136 LEU B C   1 
ATOM   5236 O O   . LEU B 1 136 ? 6.892   -13.437 74.077  1.00 10.56 ? 136 LEU B O   1 
ATOM   5237 C CB  . LEU B 1 136 ? 4.437   -13.500 76.006  1.00 5.76  ? 136 LEU B CB  1 
ATOM   5238 C CG  . LEU B 1 136 ? 3.312   -14.485 76.367  1.00 8.21  ? 136 LEU B CG  1 
ATOM   5239 C CD1 . LEU B 1 136 ? 2.005   -13.717 76.644  1.00 12.81 ? 136 LEU B CD1 1 
ATOM   5240 C CD2 . LEU B 1 136 ? 3.119   -15.535 75.287  1.00 11.66 ? 136 LEU B CD2 1 
ATOM   5241 N N   . ALA B 1 137 ? 7.622   -12.554 76.018  1.00 9.95  ? 137 ALA B N   1 
ATOM   5242 C CA  . ALA B 1 137 ? 8.655   -11.758 75.362  1.00 13.65 ? 137 ALA B CA  1 
ATOM   5243 C C   . ALA B 1 137 ? 9.650   -12.639 74.611  1.00 8.28  ? 137 ALA B C   1 
ATOM   5244 O O   . ALA B 1 137 ? 10.218  -12.216 73.596  1.00 9.63  ? 137 ALA B O   1 
ATOM   5245 C CB  . ALA B 1 137 ? 9.378   -10.889 76.398  1.00 8.66  ? 137 ALA B CB  1 
ATOM   5246 N N   . TRP B 1 138 ? 9.867   -13.862 75.080  1.00 10.59 ? 138 TRP B N   1 
ATOM   5247 C CA  . TRP B 1 138 ? 10.807  -14.781 74.450  1.00 14.88 ? 138 TRP B CA  1 
ATOM   5248 C C   . TRP B 1 138 ? 10.116  -15.754 73.501  1.00 8.67  ? 138 TRP B C   1 
ATOM   5249 O O   . TRP B 1 138 ? 10.691  -16.788 73.147  1.00 9.63  ? 138 TRP B O   1 
ATOM   5250 C CB  . TRP B 1 138 ? 11.609  -15.522 75.526  1.00 12.94 ? 138 TRP B CB  1 
ATOM   5251 C CG  . TRP B 1 138 ? 12.379  -14.536 76.344  1.00 9.19  ? 138 TRP B CG  1 
ATOM   5252 C CD1 . TRP B 1 138 ? 11.945  -13.883 77.458  1.00 10.73 ? 138 TRP B CD1 1 
ATOM   5253 C CD2 . TRP B 1 138 ? 13.704  -14.042 76.083  1.00 10.77 ? 138 TRP B CD2 1 
ATOM   5254 N NE1 . TRP B 1 138 ? 12.913  -13.017 77.916  1.00 12.60 ? 138 TRP B NE1 1 
ATOM   5255 C CE2 . TRP B 1 138 ? 14.007  -13.100 77.094  1.00 12.34 ? 138 TRP B CE2 1 
ATOM   5256 C CE3 . TRP B 1 138 ? 14.668  -14.316 75.110  1.00 9.83  ? 138 TRP B CE3 1 
ATOM   5257 C CZ2 . TRP B 1 138 ? 15.234  -12.429 77.157  1.00 14.15 ? 138 TRP B CZ2 1 
ATOM   5258 C CZ3 . TRP B 1 138 ? 15.895  -13.638 75.174  1.00 9.97  ? 138 TRP B CZ3 1 
ATOM   5259 C CH2 . TRP B 1 138 ? 16.158  -12.707 76.187  1.00 14.18 ? 138 TRP B CH2 1 
ATOM   5260 N N   . CYS B 1 139 ? 8.896   -15.445 73.075  1.00 7.09  ? 139 CYS B N   1 
ATOM   5261 C CA  . CYS B 1 139 ? 8.174   -16.353 72.189  1.00 9.05  ? 139 CYS B CA  1 
ATOM   5262 C C   . CYS B 1 139 ? 8.857   -16.444 70.829  1.00 9.52  ? 139 CYS B C   1 
ATOM   5263 O O   . CYS B 1 139 ? 9.206   -15.425 70.231  1.00 8.65  ? 139 CYS B O   1 
ATOM   5264 C CB  . CYS B 1 139 ? 6.737   -15.885 72.010  1.00 9.58  ? 139 CYS B CB  1 
ATOM   5265 S SG  . CYS B 1 139 ? 5.646   -17.111 71.258  1.00 10.67 ? 139 CYS B SG  1 
ATOM   5266 N N   . GLY B 1 140 ? 9.033   -17.664 70.337  1.00 8.97  ? 140 GLY B N   1 
ATOM   5267 C CA  . GLY B 1 140 ? 9.641   -17.858 69.037  1.00 8.16  ? 140 GLY B CA  1 
ATOM   5268 C C   . GLY B 1 140 ? 8.652   -17.691 67.903  1.00 10.80 ? 140 GLY B C   1 
ATOM   5269 O O   . GLY B 1 140 ? 7.440   -17.562 68.102  1.00 9.74  ? 140 GLY B O   1 
ATOM   5270 N N   . ARG B 1 141 ? 9.208   -17.711 66.691  1.00 8.89  ? 141 ARG B N   1 
ATOM   5271 C CA  . ARG B 1 141 ? 8.426   -17.471 65.482  1.00 12.79 ? 141 ARG B CA  1 
ATOM   5272 C C   . ARG B 1 141 ? 7.247   -18.435 65.358  1.00 12.46 ? 141 ARG B C   1 
ATOM   5273 O O   . ARG B 1 141 ? 6.142   -18.024 64.996  1.00 8.86  ? 141 ARG B O   1 
ATOM   5274 C CB  . ARG B 1 141 ? 9.347   -17.572 64.263  1.00 11.68 ? 141 ARG B CB  1 
ATOM   5275 C CG  . ARG B 1 141 ? 8.635   -17.506 62.911  1.00 12.56 ? 141 ARG B CG  1 
ATOM   5276 C CD  . ARG B 1 141 ? 9.672   -17.563 61.774  1.00 13.71 ? 141 ARG B CD  1 
ATOM   5277 N NE  . ARG B 1 141 ? 9.041   -17.639 60.459  1.00 16.45 ? 141 ARG B NE  1 
ATOM   5278 C CZ  . ARG B 1 141 ? 8.888   -18.759 59.767  1.00 17.48 ? 141 ARG B CZ  1 
ATOM   5279 N NH1 . ARG B 1 141 ? 9.325   -19.910 60.257  1.00 10.28 ? 141 ARG B NH1 1 
ATOM   5280 N NH2 . ARG B 1 141 ? 8.300   -18.722 58.580  1.00 20.14 ? 141 ARG B NH2 1 
ATOM   5281 N N   . THR B 1 142 ? 7.465   -19.726 65.642  1.00 8.32  ? 142 THR B N   1 
ATOM   5282 C CA  . THR B 1 142 ? 6.402   -20.709 65.448  1.00 11.32 ? 142 THR B CA  1 
ATOM   5283 C C   . THR B 1 142 ? 5.216   -20.399 66.346  1.00 12.82 ? 142 THR B C   1 
ATOM   5284 O O   . THR B 1 142 ? 4.074   -20.302 65.887  1.00 14.01 ? 142 THR B O   1 
ATOM   5285 C CB  . THR B 1 142 ? 6.934   -22.114 65.745  1.00 10.91 ? 142 THR B CB  1 
ATOM   5286 O OG1 . THR B 1 142 ? 8.006   -22.418 64.849  1.00 10.23 ? 142 THR B OG1 1 
ATOM   5287 C CG2 . THR B 1 142 ? 5.836   -23.174 65.614  1.00 12.03 ? 142 THR B CG2 1 
ATOM   5288 N N   . LEU B 1 143 ? 5.477   -20.219 67.634  1.00 12.64 ? 143 LEU B N   1 
ATOM   5289 C CA  . LEU B 1 143 ? 4.392   -19.979 68.570  1.00 11.77 ? 143 LEU B CA  1 
ATOM   5290 C C   . LEU B 1 143 ? 3.858   -18.563 68.496  1.00 14.18 ? 143 LEU B C   1 
ATOM   5291 O O   . LEU B 1 143 ? 2.720   -18.326 68.921  1.00 16.00 ? 143 LEU B O   1 
ATOM   5292 C CB  . LEU B 1 143 ? 4.862   -20.288 69.978  1.00 8.05  ? 143 LEU B CB  1 
ATOM   5293 C CG  . LEU B 1 143 ? 5.032   -21.796 70.160  1.00 9.12  ? 143 LEU B CG  1 
ATOM   5294 C CD1 . LEU B 1 143 ? 5.412   -22.094 71.598  1.00 9.93  ? 143 LEU B CD1 1 
ATOM   5295 C CD2 . LEU B 1 143 ? 3.743   -22.529 69.774  1.00 15.64 ? 143 LEU B CD2 1 
ATOM   5296 N N   . ARG B 1 144 ? 4.652   -17.615 67.987  1.00 13.17 ? 144 ARG B N   1 
ATOM   5297 C CA  . ARG B 1 144 ? 4.115   -16.276 67.761  1.00 8.40  ? 144 ARG B CA  1 
ATOM   5298 C C   . ARG B 1 144 ? 2.927   -16.348 66.813  1.00 15.49 ? 144 ARG B C   1 
ATOM   5299 O O   . ARG B 1 144 ? 1.936   -15.623 66.975  1.00 16.04 ? 144 ARG B O   1 
ATOM   5300 C CB  . ARG B 1 144 ? 5.201   -15.356 67.211  1.00 11.03 ? 144 ARG B CB  1 
ATOM   5301 C CG  . ARG B 1 144 ? 6.041   -14.673 68.302  1.00 14.01 ? 144 ARG B CG  1 
ATOM   5302 C CD  . ARG B 1 144 ? 7.183   -13.913 67.669  1.00 16.54 ? 144 ARG B CD  1 
ATOM   5303 N NE  . ARG B 1 144 ? 8.016   -13.244 68.656  1.00 19.42 ? 144 ARG B NE  1 
ATOM   5304 C CZ  . ARG B 1 144 ? 7.817   -11.995 69.062  1.00 16.63 ? 144 ARG B CZ  1 
ATOM   5305 N NH1 . ARG B 1 144 ? 6.794   -11.299 68.577  1.00 23.89 ? 144 ARG B NH1 1 
ATOM   5306 N NH2 . ARG B 1 144 ? 8.621   -11.452 69.960  1.00 21.05 ? 144 ARG B NH2 1 
ATOM   5307 N N   . LYS B 1 145 ? 2.996   -17.260 65.845  1.00 12.42 ? 145 LYS B N   1 
ATOM   5308 C CA  . LYS B 1 145 ? 1.861   -17.502 64.963  1.00 19.46 ? 145 LYS B CA  1 
ATOM   5309 C C   . LYS B 1 145 ? 0.762   -18.283 65.678  1.00 18.37 ? 145 LYS B C   1 
ATOM   5310 O O   . LYS B 1 145 ? -0.410  -17.891 65.641  1.00 18.08 ? 145 LYS B O   1 
ATOM   5311 C CB  . LYS B 1 145 ? 2.338   -18.227 63.700  1.00 19.00 ? 145 LYS B CB  1 
ATOM   5312 C CG  . LYS B 1 145 ? 3.257   -17.337 62.830  1.00 33.56 ? 145 LYS B CG  1 
ATOM   5313 C CD  . LYS B 1 145 ? 4.129   -18.122 61.839  1.00 41.21 ? 145 LYS B CD  1 
ATOM   5314 C CE  . LYS B 1 145 ? 4.600   -17.261 60.642  1.00 37.07 ? 145 LYS B CE  1 
ATOM   5315 N NZ  . LYS B 1 145 ? 5.586   -16.190 60.984  1.00 26.74 ? 145 LYS B NZ  1 
ATOM   5316 N N   . ASP B 1 146 ? 1.120   -19.370 66.371  1.00 19.86 ? 146 ASP B N   1 
ATOM   5317 C CA  . ASP B 1 146 ? 0.094   -20.235 66.954  1.00 18.29 ? 146 ASP B CA  1 
ATOM   5318 C C   . ASP B 1 146 ? -0.623  -19.565 68.126  1.00 22.36 ? 146 ASP B C   1 
ATOM   5319 O O   . ASP B 1 146 ? -1.834  -19.747 68.301  1.00 24.92 ? 146 ASP B O   1 
ATOM   5320 C CB  . ASP B 1 146 ? 0.711   -21.562 67.407  1.00 20.24 ? 146 ASP B CB  1 
ATOM   5321 C CG  . ASP B 1 146 ? 1.263   -22.399 66.254  1.00 23.85 ? 146 ASP B CG  1 
ATOM   5322 O OD1 . ASP B 1 146 ? 0.978   -22.100 65.081  1.00 29.26 ? 146 ASP B OD1 1 
ATOM   5323 O OD2 . ASP B 1 146 ? 1.992   -23.375 66.529  1.00 31.97 ? 146 ASP B OD2 1 
ATOM   5324 N N   . LEU B 1 147 ? 0.106   -18.809 68.951  1.00 15.75 ? 147 LEU B N   1 
ATOM   5325 C CA  . LEU B 1 147 ? -0.427  -18.132 70.132  1.00 13.94 ? 147 LEU B CA  1 
ATOM   5326 C C   . LEU B 1 147 ? -0.735  -16.657 69.883  1.00 13.87 ? 147 LEU B C   1 
ATOM   5327 O O   . LEU B 1 147 ? -0.696  -15.849 70.819  1.00 16.76 ? 147 LEU B O   1 
ATOM   5328 C CB  . LEU B 1 147 ? 0.561   -18.251 71.295  1.00 15.59 ? 147 LEU B CB  1 
ATOM   5329 C CG  . LEU B 1 147 ? 1.149   -19.628 71.606  1.00 19.19 ? 147 LEU B CG  1 
ATOM   5330 C CD1 . LEU B 1 147 ? 2.232   -19.536 72.682  1.00 16.62 ? 147 LEU B CD1 1 
ATOM   5331 C CD2 . LEU B 1 147 ? 0.046   -20.595 72.021  1.00 30.71 ? 147 LEU B CD2 1 
ATOM   5332 N N   . LYS B 1 148 ? -1.041  -16.284 68.638  1.00 10.97 ? 148 LYS B N   1 
ATOM   5333 C CA  . LYS B 1 148 ? -1.071  -14.867 68.268  1.00 15.24 ? 148 LYS B CA  1 
ATOM   5334 C C   . LYS B 1 148 ? -2.085  -14.074 69.089  1.00 20.01 ? 148 LYS B C   1 
ATOM   5335 O O   . LYS B 1 148 ? -1.830  -12.923 69.461  1.00 22.26 ? 148 LYS B O   1 
ATOM   5336 C CB  . LYS B 1 148 ? -1.383  -14.734 66.780  1.00 22.32 ? 148 LYS B CB  1 
ATOM   5337 C CG  . LYS B 1 148 ? -1.103  -13.365 66.200  1.00 36.74 ? 148 LYS B CG  1 
ATOM   5338 C CD  . LYS B 1 148 ? -0.958  -13.441 64.681  1.00 48.38 ? 148 LYS B CD  1 
ATOM   5339 C CE  . LYS B 1 148 ? -2.132  -14.168 64.049  1.00 50.76 ? 148 LYS B CE  1 
ATOM   5340 N NZ  . LYS B 1 148 ? -3.437  -13.611 64.512  1.00 51.95 ? 148 LYS B NZ  1 
ATOM   5341 N N   . ASP B 1 149 ? -3.245  -14.656 69.357  1.00 19.95 ? 149 ASP B N   1 
ATOM   5342 C CA  . ASP B 1 149 ? -4.298  -13.910 70.041  1.00 26.46 ? 149 ASP B CA  1 
ATOM   5343 C C   . ASP B 1 149 ? -3.972  -13.722 71.517  1.00 20.84 ? 149 ASP B C   1 
ATOM   5344 O O   . ASP B 1 149 ? -4.303  -12.687 72.111  1.00 22.23 ? 149 ASP B O   1 
ATOM   5345 C CB  . ASP B 1 149 ? -5.628  -14.637 69.866  1.00 31.70 ? 149 ASP B CB  1 
ATOM   5346 C CG  . ASP B 1 149 ? -5.993  -14.808 68.411  1.00 39.95 ? 149 ASP B CG  1 
ATOM   5347 O OD1 . ASP B 1 149 ? -5.872  -13.813 67.661  1.00 32.31 ? 149 ASP B OD1 1 
ATOM   5348 O OD2 . ASP B 1 149 ? -6.371  -15.933 68.014  1.00 49.15 ? 149 ASP B OD2 1 
ATOM   5349 N N   . LEU B 1 150 ? -3.327  -14.719 72.117  1.00 19.54 ? 150 LEU B N   1 
ATOM   5350 C CA  . LEU B 1 150 ? -2.847  -14.595 73.486  1.00 18.78 ? 150 LEU B CA  1 
ATOM   5351 C C   . LEU B 1 150 ? -1.777  -13.523 73.586  1.00 19.96 ? 150 LEU B C   1 
ATOM   5352 O O   . LEU B 1 150 ? -1.782  -12.715 74.516  1.00 17.54 ? 150 LEU B O   1 
ATOM   5353 C CB  . LEU B 1 150 ? -2.303  -15.946 73.947  1.00 23.98 ? 150 LEU B CB  1 
ATOM   5354 C CG  . LEU B 1 150 ? -2.672  -16.509 75.306  1.00 29.78 ? 150 LEU B CG  1 
ATOM   5355 C CD1 . LEU B 1 150 ? -4.115  -16.181 75.670  1.00 27.86 ? 150 LEU B CD1 1 
ATOM   5356 C CD2 . LEU B 1 150 ? -2.442  -18.016 75.283  1.00 23.99 ? 150 LEU B CD2 1 
ATOM   5357 N N   . LEU B 1 151 ? -0.856  -13.494 72.621  1.00 17.73 ? 151 LEU B N   1 
ATOM   5358 C CA  . LEU B 1 151 ? 0.180   -12.469 72.594  1.00 20.02 ? 151 LEU B CA  1 
ATOM   5359 C C   . LEU B 1 151 ? -0.410  -11.075 72.380  1.00 24.26 ? 151 LEU B C   1 
ATOM   5360 O O   . LEU B 1 151 ? 0.051   -10.104 72.987  1.00 25.49 ? 151 LEU B O   1 
ATOM   5361 C CB  . LEU B 1 151 ? 1.196   -12.807 71.503  1.00 23.67 ? 151 LEU B CB  1 
ATOM   5362 C CG  . LEU B 1 151 ? 2.626   -12.320 71.727  1.00 38.87 ? 151 LEU B CG  1 
ATOM   5363 C CD1 . LEU B 1 151 ? 3.579   -13.226 70.984  1.00 42.64 ? 151 LEU B CD1 1 
ATOM   5364 C CD2 . LEU B 1 151 ? 2.774   -10.872 71.261  1.00 37.05 ? 151 LEU B CD2 1 
ATOM   5365 N N   . ASN B 1 152 ? -1.443  -10.961 71.536  1.00 31.05 ? 152 ASN B N   1 
ATOM   5366 C CA  . ASN B 1 152 ? -2.101  -9.676  71.287  1.00 33.35 ? 152 ASN B CA  1 
ATOM   5367 C C   . ASN B 1 152 ? -2.862  -9.137  72.493  1.00 29.21 ? 152 ASN B C   1 
ATOM   5368 O O   . ASN B 1 152 ? -3.116  -7.929  72.555  1.00 33.45 ? 152 ASN B O   1 
ATOM   5369 C CB  . ASN B 1 152 ? -3.079  -9.795  70.118  1.00 43.12 ? 152 ASN B CB  1 
ATOM   5370 C CG  . ASN B 1 152 ? -2.387  -10.015 68.804  1.00 51.11 ? 152 ASN B CG  1 
ATOM   5371 O OD1 . ASN B 1 152 ? -1.182  -9.796  68.684  1.00 50.57 ? 152 ASN B OD1 1 
ATOM   5372 N ND2 . ASN B 1 152 ? -3.142  -10.450 67.801  1.00 55.63 ? 152 ASN B ND2 1 
ATOM   5373 N N   . LYS B 1 153 ? -3.284  -9.998  73.418  1.00 26.74 ? 153 LYS B N   1 
ATOM   5374 C CA  . LYS B 1 153 ? -3.891  -9.517  74.655  1.00 27.50 ? 153 LYS B CA  1 
ATOM   5375 C C   . LYS B 1 153 ? -3.006  -8.475  75.316  1.00 29.02 ? 153 LYS B C   1 
ATOM   5376 O O   . LYS B 1 153 ? -3.467  -7.397  75.713  1.00 26.59 ? 153 LYS B O   1 
ATOM   5377 C CB  . LYS B 1 153 ? -4.099  -10.673 75.628  1.00 28.74 ? 153 LYS B CB  1 
ATOM   5378 C CG  . LYS B 1 153 ? -5.250  -11.565 75.342  1.00 28.90 ? 153 LYS B CG  1 
ATOM   5379 C CD  . LYS B 1 153 ? -5.185  -12.766 76.268  1.00 25.34 ? 153 LYS B CD  1 
ATOM   5380 C CE  . LYS B 1 153 ? -4.943  -12.357 77.715  1.00 18.31 ? 153 LYS B CE  1 
ATOM   5381 N NZ  . LYS B 1 153 ? -6.135  -11.736 78.389  1.00 22.45 ? 153 LYS B NZ  1 
ATOM   5382 N N   . GLY B 1 154 ? -1.726  -8.807  75.472  1.00 24.55 ? 154 GLY B N   1 
ATOM   5383 C CA  . GLY B 1 154 ? -0.765  -7.953  76.131  1.00 26.68 ? 154 GLY B CA  1 
ATOM   5384 C C   . GLY B 1 154 ? -1.038  -7.684  77.592  1.00 21.33 ? 154 GLY B C   1 
ATOM   5385 O O   . GLY B 1 154 ? -0.273  -6.945  78.212  1.00 18.19 ? 154 GLY B O   1 
ATOM   5386 N N   . ARG B 1 155 ? -2.079  -8.271  78.178  1.00 16.51 ? 155 ARG B N   1 
ATOM   5387 C CA  . ARG B 1 155 ? -2.459  -7.936  79.547  1.00 18.36 ? 155 ARG B CA  1 
ATOM   5388 C C   . ARG B 1 155 ? -3.527  -8.916  80.023  1.00 15.47 ? 155 ARG B C   1 
ATOM   5389 O O   . ARG B 1 155 ? -4.078  -9.691  79.237  1.00 23.28 ? 155 ARG B O   1 
ATOM   5390 C CB  . ARG B 1 155 ? -2.975  -6.497  79.630  1.00 26.97 ? 155 ARG B CB  1 
ATOM   5391 C CG  . ARG B 1 155 ? -4.089  -6.200  78.619  1.00 26.99 ? 155 ARG B CG  1 
ATOM   5392 C CD  . ARG B 1 155 ? -4.188  -4.709  78.344  1.00 34.15 ? 155 ARG B CD  1 
ATOM   5393 N NE  . ARG B 1 155 ? -3.929  -3.958  79.566  1.00 30.20 ? 155 ARG B NE  1 
ATOM   5394 C CZ  . ARG B 1 155 ? -3.121  -2.911  79.652  1.00 29.24 ? 155 ARG B CZ  1 
ATOM   5395 N NH1 . ARG B 1 155 ? -2.476  -2.460  78.581  1.00 31.95 ? 155 ARG B NH1 1 
ATOM   5396 N NH2 . ARG B 1 155 ? -2.959  -2.319  80.823  1.00 41.53 ? 155 ARG B NH2 1 
ATOM   5397 N N   . ASN B 1 156 ? -3.805  -8.868  81.325  1.00 14.23 ? 156 ASN B N   1 
ATOM   5398 C CA  . ASN B 1 156 ? -4.917  -9.609  81.932  1.00 18.62 ? 156 ASN B CA  1 
ATOM   5399 C C   . ASN B 1 156 ? -4.782  -11.116 81.721  1.00 20.67 ? 156 ASN B C   1 
ATOM   5400 O O   . ASN B 1 156 ? -5.713  -11.795 81.280  1.00 18.01 ? 156 ASN B O   1 
ATOM   5401 C CB  . ASN B 1 156 ? -6.259  -9.111  81.391  1.00 24.13 ? 156 ASN B CB  1 
ATOM   5402 C CG  . ASN B 1 156 ? -6.399  -7.605  81.458  1.00 31.08 ? 156 ASN B CG  1 
ATOM   5403 O OD1 . ASN B 1 156 ? -6.845  -6.967  80.499  1.00 37.10 ? 156 ASN B OD1 1 
ATOM   5404 N ND2 . ASN B 1 156 ? -6.019  -7.027  82.586  1.00 25.99 ? 156 ASN B ND2 1 
ATOM   5405 N N   . TYR B 1 157 ? -3.615  -11.646 82.053  1.00 11.73 ? 157 TYR B N   1 
ATOM   5406 C CA  . TYR B 1 157 ? -3.361  -13.065 81.885  1.00 8.09  ? 157 TYR B CA  1 
ATOM   5407 C C   . TYR B 1 157 ? -3.805  -13.840 83.123  1.00 10.77 ? 157 TYR B C   1 
ATOM   5408 O O   . TYR B 1 157 ? -3.683  -13.362 84.254  1.00 14.07 ? 157 TYR B O   1 
ATOM   5409 C CB  . TYR B 1 157 ? -1.877  -13.295 81.625  1.00 10.37 ? 157 TYR B CB  1 
ATOM   5410 C CG  . TYR B 1 157 ? -1.467  -12.800 80.267  1.00 8.45  ? 157 TYR B CG  1 
ATOM   5411 C CD1 . TYR B 1 157 ? -1.779  -13.532 79.126  1.00 12.84 ? 157 TYR B CD1 1 
ATOM   5412 C CD2 . TYR B 1 157 ? -0.791  -11.589 80.115  1.00 9.97  ? 157 TYR B CD2 1 
ATOM   5413 C CE1 . TYR B 1 157 ? -1.419  -13.067 77.859  1.00 16.36 ? 157 TYR B CE1 1 
ATOM   5414 C CE2 . TYR B 1 157 ? -0.416  -11.129 78.872  1.00 12.91 ? 157 TYR B CE2 1 
ATOM   5415 C CZ  . TYR B 1 157 ? -0.736  -11.870 77.745  1.00 19.85 ? 157 TYR B CZ  1 
ATOM   5416 O OH  . TYR B 1 157 ? -0.379  -11.407 76.501  1.00 16.51 ? 157 TYR B OH  1 
ATOM   5417 N N   . THR B 1 158 ? -4.289  -15.062 82.900  1.00 10.24 ? 158 THR B N   1 
ATOM   5418 C CA  . THR B 1 158 ? -4.650  -15.964 83.980  1.00 9.81  ? 158 THR B CA  1 
ATOM   5419 C C   . THR B 1 158 ? -3.586  -17.043 84.146  1.00 12.79 ? 158 THR B C   1 
ATOM   5420 O O   . THR B 1 158 ? -2.797  -17.316 83.241  1.00 7.81  ? 158 THR B O   1 
ATOM   5421 C CB  . THR B 1 158 ? -6.011  -16.612 83.701  1.00 9.99  ? 158 THR B CB  1 
ATOM   5422 O OG1 . THR B 1 158 ? -5.890  -17.426 82.533  1.00 8.66  ? 158 THR B OG1 1 
ATOM   5423 C CG2 . THR B 1 158 ? -7.073  -15.538 83.442  1.00 11.60 ? 158 THR B CG2 1 
ATOM   5424 N N   . GLN B 1 159 ? -3.570  -17.643 85.337  1.00 9.22  ? 159 GLN B N   1 
ATOM   5425 C CA  . GLN B 1 159 ? -2.660  -18.750 85.608  1.00 17.48 ? 159 GLN B CA  1 
ATOM   5426 C C   . GLN B 1 159 ? -2.824  -19.850 84.570  1.00 15.95 ? 159 GLN B C   1 
ATOM   5427 O O   . GLN B 1 159 ? -1.841  -20.463 84.127  1.00 12.06 ? 159 GLN B O   1 
ATOM   5428 C CB  . GLN B 1 159 ? -2.917  -19.291 87.019  1.00 11.74 ? 159 GLN B CB  1 
ATOM   5429 C CG  . GLN B 1 159 ? -2.074  -20.509 87.395  1.00 13.04 ? 159 GLN B CG  1 
ATOM   5430 C CD  . GLN B 1 159 ? -0.620  -20.152 87.646  1.00 13.47 ? 159 GLN B CD  1 
ATOM   5431 O OE1 . GLN B 1 159 ? -0.289  -19.009 87.951  1.00 12.91 ? 159 GLN B OE1 1 
ATOM   5432 N NE2 . GLN B 1 159 ? 0.253   -21.138 87.527  1.00 15.24 ? 159 GLN B NE2 1 
ATOM   5433 N N   . GLU B 1 160 ? -4.063  -20.101 84.152  1.00 6.73  ? 160 GLU B N   1 
ATOM   5434 C CA  . GLU B 1 160 ? -4.294  -21.133 83.144  1.00 10.76 ? 160 GLU B CA  1 
ATOM   5435 C C   . GLU B 1 160 ? -3.654  -20.764 81.813  1.00 9.12  ? 160 GLU B C   1 
ATOM   5436 O O   . GLU B 1 160 ? -3.036  -21.611 81.161  1.00 10.97 ? 160 GLU B O   1 
ATOM   5437 C CB  . GLU B 1 160 ? -5.790  -21.365 82.953  1.00 12.67 ? 160 GLU B CB  1 
ATOM   5438 C CG  . GLU B 1 160 ? -6.078  -22.503 81.985  1.00 19.55 ? 160 GLU B CG  1 
ATOM   5439 C CD  . GLU B 1 160 ? -5.668  -23.852 82.550  1.00 29.05 ? 160 GLU B CD  1 
ATOM   5440 O OE1 . GLU B 1 160 ? -5.450  -24.781 81.750  1.00 39.72 ? 160 GLU B OE1 1 
ATOM   5441 O OE2 . GLU B 1 160 ? -5.562  -23.988 83.792  1.00 35.39 ? 160 GLU B OE2 1 
ATOM   5442 N N   . GLU B 1 161 ? -3.800  -19.508 81.387  1.00 8.93  ? 161 GLU B N   1 
ATOM   5443 C CA  . GLU B 1 161 ? -3.129  -19.068 80.162  1.00 6.92  ? 161 GLU B CA  1 
ATOM   5444 C C   . GLU B 1 161 ? -1.611  -19.177 80.282  1.00 8.09  ? 161 GLU B C   1 
ATOM   5445 O O   . GLU B 1 161 ? -0.937  -19.600 79.337  1.00 7.93  ? 161 GLU B O   1 
ATOM   5446 C CB  . GLU B 1 161 ? -3.551  -17.638 79.822  1.00 5.86  ? 161 GLU B CB  1 
ATOM   5447 C CG  . GLU B 1 161 ? -4.997  -17.598 79.302  1.00 8.70  ? 161 GLU B CG  1 
ATOM   5448 C CD  . GLU B 1 161 ? -5.617  -16.219 79.327  1.00 16.16 ? 161 GLU B CD  1 
ATOM   5449 O OE1 . GLU B 1 161 ? -4.978  -15.270 79.811  1.00 10.76 ? 161 GLU B OE1 1 
ATOM   5450 O OE2 . GLU B 1 161 ? -6.782  -16.101 78.892  1.00 25.60 ? 161 GLU B OE2 1 
ATOM   5451 N N   . LYS B 1 162 ? -1.052  -18.801 81.432  1.00 8.45  ? 162 LYS B N   1 
ATOM   5452 C CA  . LYS B 1 162 ? 0.402   -18.900 81.600  1.00 5.29  ? 162 LYS B CA  1 
ATOM   5453 C C   . LYS B 1 162 ? 0.866   -20.351 81.514  1.00 11.88 ? 162 LYS B C   1 
ATOM   5454 O O   . LYS B 1 162 ? 1.878   -20.656 80.868  1.00 9.51  ? 162 LYS B O   1 
ATOM   5455 C CB  . LYS B 1 162 ? 0.799   -18.294 82.944  1.00 4.29  ? 162 LYS B CB  1 
ATOM   5456 C CG  . LYS B 1 162 ? 2.303   -18.302 83.228  1.00 8.28  ? 162 LYS B CG  1 
ATOM   5457 C CD  . LYS B 1 162 ? 2.576   -17.638 84.589  1.00 10.90 ? 162 LYS B CD  1 
ATOM   5458 C CE  . LYS B 1 162 ? 1.845   -18.380 85.701  1.00 13.73 ? 162 LYS B CE  1 
ATOM   5459 N NZ  . LYS B 1 162 ? 2.300   -17.958 87.080  1.00 10.74 ? 162 LYS B NZ  1 
ATOM   5460 N N   . GLU B 1 163 ? 0.141   -21.260 82.176  1.00 8.74  ? 163 GLU B N   1 
ATOM   5461 C CA  . GLU B 1 163 ? 0.505   -22.672 82.124  1.00 11.31 ? 163 GLU B CA  1 
ATOM   5462 C C   . GLU B 1 163 ? 0.359   -23.228 80.714  1.00 10.43 ? 163 GLU B C   1 
ATOM   5463 O O   . GLU B 1 163 ? 1.137   -24.091 80.299  1.00 12.29 ? 163 GLU B O   1 
ATOM   5464 C CB  . GLU B 1 163 ? -0.358  -23.463 83.111  1.00 15.15 ? 163 GLU B CB  1 
ATOM   5465 C CG  . GLU B 1 163 ? -0.004  -23.170 84.574  1.00 14.41 ? 163 GLU B CG  1 
ATOM   5466 C CD  . GLU B 1 163 ? -0.886  -23.899 85.569  1.00 25.80 ? 163 GLU B CD  1 
ATOM   5467 O OE1 . GLU B 1 163 ? -1.662  -24.782 85.141  1.00 31.03 ? 163 GLU B OE1 1 
ATOM   5468 O OE2 . GLU B 1 163 ? -0.797  -23.589 86.784  1.00 19.97 ? 163 GLU B OE2 1 
ATOM   5469 N N   . TYR B 1 164 ? -0.635  -22.755 79.965  1.00 12.48 ? 164 TYR B N   1 
ATOM   5470 C CA  . TYR B 1 164 ? -0.783  -23.190 78.578  1.00 14.76 ? 164 TYR B CA  1 
ATOM   5471 C C   . TYR B 1 164 ? 0.433   -22.796 77.748  1.00 16.57 ? 164 TYR B C   1 
ATOM   5472 O O   . TYR B 1 164 ? 0.971   -23.607 76.982  1.00 10.15 ? 164 TYR B O   1 
ATOM   5473 C CB  . TYR B 1 164 ? -2.054  -22.579 77.993  1.00 19.22 ? 164 TYR B CB  1 
ATOM   5474 C CG  . TYR B 1 164 ? -2.335  -22.976 76.566  1.00 15.01 ? 164 TYR B CG  1 
ATOM   5475 C CD1 . TYR B 1 164 ? -2.822  -24.245 76.264  1.00 25.12 ? 164 TYR B CD1 1 
ATOM   5476 C CD2 . TYR B 1 164 ? -2.144  -22.080 75.525  1.00 18.68 ? 164 TYR B CD2 1 
ATOM   5477 C CE1 . TYR B 1 164 ? -3.099  -24.613 74.956  1.00 30.67 ? 164 TYR B CE1 1 
ATOM   5478 C CE2 . TYR B 1 164 ? -2.424  -22.443 74.203  1.00 18.89 ? 164 TYR B CE2 1 
ATOM   5479 C CZ  . TYR B 1 164 ? -2.899  -23.708 73.934  1.00 30.25 ? 164 TYR B CZ  1 
ATOM   5480 O OH  . TYR B 1 164 ? -3.178  -24.080 72.639  1.00 30.20 ? 164 TYR B OH  1 
ATOM   5481 N N   . VAL B 1 165 ? 0.863   -21.538 77.875  1.00 9.87  ? 165 VAL B N   1 
ATOM   5482 C CA  . VAL B 1 165 ? 2.064   -21.068 77.181  1.00 9.18  ? 165 VAL B CA  1 
ATOM   5483 C C   . VAL B 1 165 ? 3.268   -21.922 77.560  1.00 8.91  ? 165 VAL B C   1 
ATOM   5484 O O   . VAL B 1 165 ? 4.034   -22.353 76.697  1.00 9.67  ? 165 VAL B O   1 
ATOM   5485 C CB  . VAL B 1 165 ? 2.326   -19.582 77.491  1.00 8.53  ? 165 VAL B CB  1 
ATOM   5486 C CG1 . VAL B 1 165 ? 3.685   -19.161 76.935  1.00 4.50  ? 165 VAL B CG1 1 
ATOM   5487 C CG2 . VAL B 1 165 ? 1.226   -18.698 76.923  1.00 7.96  ? 165 VAL B CG2 1 
ATOM   5488 N N   . LEU B 1 166 ? 3.466   -22.151 78.863  1.00 9.30  ? 166 LEU B N   1 
ATOM   5489 C CA  . LEU B 1 166 ? 4.587   -22.977 79.322  1.00 4.90  ? 166 LEU B CA  1 
ATOM   5490 C C   . LEU B 1 166 ? 4.567   -24.354 78.687  1.00 12.23 ? 166 LEU B C   1 
ATOM   5491 O O   . LEU B 1 166 ? 5.616   -24.877 78.282  1.00 9.34  ? 166 LEU B O   1 
ATOM   5492 C CB  . LEU B 1 166 ? 4.539   -23.129 80.846  1.00 5.43  ? 166 LEU B CB  1 
ATOM   5493 C CG  . LEU B 1 166 ? 5.137   -21.987 81.643  1.00 12.45 ? 166 LEU B CG  1 
ATOM   5494 C CD1 . LEU B 1 166 ? 4.769   -22.154 83.132  1.00 21.23 ? 166 LEU B CD1 1 
ATOM   5495 C CD2 . LEU B 1 166 ? 6.650   -21.962 81.438  1.00 15.79 ? 166 LEU B CD2 1 
ATOM   5496 N N   . ASN B 1 167 ? 3.385   -24.972 78.618  1.00 7.87  ? 167 ASN B N   1 
ATOM   5497 C CA  . ASN B 1 167 ? 3.283   -26.296 78.011  1.00 8.46  ? 167 ASN B CA  1 
ATOM   5498 C C   . ASN B 1 167 ? 3.671   -26.257 76.539  1.00 11.01 ? 167 ASN B C   1 
ATOM   5499 O O   . ASN B 1 167 ? 4.395   -27.137 76.057  1.00 12.44 ? 167 ASN B O   1 
ATOM   5500 C CB  . ASN B 1 167 ? 1.861   -26.839 78.177  1.00 15.73 ? 167 ASN B CB  1 
ATOM   5501 C CG  . ASN B 1 167 ? 1.637   -27.469 79.531  1.00 35.43 ? 167 ASN B CG  1 
ATOM   5502 O OD1 . ASN B 1 167 ? 2.589   -27.817 80.232  1.00 39.74 ? 167 ASN B OD1 1 
ATOM   5503 N ND2 . ASN B 1 167 ? 0.369   -27.623 79.908  1.00 35.52 ? 167 ASN B ND2 1 
ATOM   5504 N N   . LYS B 1 168 ? 3.196   -25.246 75.802  1.00 9.71  ? 168 LYS B N   1 
ATOM   5505 C CA  . LYS B 1 168 ? 3.602   -25.103 74.401  1.00 9.09  ? 168 LYS B CA  1 
ATOM   5506 C C   . LYS B 1 168 ? 5.107   -24.910 74.286  1.00 11.68 ? 168 LYS B C   1 
ATOM   5507 O O   . LYS B 1 168 ? 5.744   -25.477 73.389  1.00 9.12  ? 168 LYS B O   1 
ATOM   5508 C CB  . LYS B 1 168 ? 2.882   -23.928 73.736  1.00 12.10 ? 168 LYS B CB  1 
ATOM   5509 C CG  . LYS B 1 168 ? 1.366   -24.088 73.586  1.00 15.35 ? 168 LYS B CG  1 
ATOM   5510 C CD  . LYS B 1 168 ? 0.994   -25.313 72.776  1.00 21.61 ? 168 LYS B CD  1 
ATOM   5511 C CE  . LYS B 1 168 ? 1.314   -25.149 71.305  1.00 39.55 ? 168 LYS B CE  1 
ATOM   5512 N NZ  . LYS B 1 168 ? 1.072   -26.414 70.531  1.00 45.06 ? 168 LYS B NZ  1 
ATOM   5513 N N   . TYR B 1 169 ? 5.688   -24.096 75.171  1.00 7.85  ? 169 TYR B N   1 
ATOM   5514 C CA  . TYR B 1 169 ? 7.132   -23.871 75.143  1.00 6.94  ? 169 TYR B CA  1 
ATOM   5515 C C   . TYR B 1 169 ? 7.891   -25.166 75.328  1.00 8.54  ? 169 TYR B C   1 
ATOM   5516 O O   . TYR B 1 169 ? 8.867   -25.430 74.620  1.00 8.72  ? 169 TYR B O   1 
ATOM   5517 C CB  . TYR B 1 169 ? 7.551   -22.893 76.229  1.00 6.67  ? 169 TYR B CB  1 
ATOM   5518 C CG  . TYR B 1 169 ? 7.379   -21.443 75.868  1.00 4.37  ? 169 TYR B CG  1 
ATOM   5519 C CD1 . TYR B 1 169 ? 6.545   -21.062 74.823  1.00 9.24  ? 169 TYR B CD1 1 
ATOM   5520 C CD2 . TYR B 1 169 ? 8.044   -20.454 76.590  1.00 6.78  ? 169 TYR B CD2 1 
ATOM   5521 C CE1 . TYR B 1 169 ? 6.375   -19.733 74.506  1.00 8.06  ? 169 TYR B CE1 1 
ATOM   5522 C CE2 . TYR B 1 169 ? 7.899   -19.120 76.277  1.00 7.25  ? 169 TYR B CE2 1 
ATOM   5523 C CZ  . TYR B 1 169 ? 7.060   -18.762 75.240  1.00 11.35 ? 169 TYR B CZ  1 
ATOM   5524 O OH  . TYR B 1 169 ? 6.899   -17.441 74.933  1.00 9.70  ? 169 TYR B OH  1 
ATOM   5525 N N   . PHE B 1 170 ? 7.482   -25.984 76.305  1.00 9.26  ? 170 PHE B N   1 
ATOM   5526 C CA  . PHE B 1 170 ? 8.232   -27.221 76.497  1.00 9.81  ? 170 PHE B CA  1 
ATOM   5527 C C   . PHE B 1 170 ? 8.047   -28.174 75.327  1.00 10.54 ? 170 PHE B C   1 
ATOM   5528 O O   . PHE B 1 170 ? 8.965   -28.942 75.018  1.00 9.40  ? 170 PHE B O   1 
ATOM   5529 C CB  . PHE B 1 170 ? 7.863   -27.876 77.831  1.00 7.62  ? 170 PHE B CB  1 
ATOM   5530 C CG  . PHE B 1 170 ? 8.681   -27.339 78.988  1.00 17.01 ? 170 PHE B CG  1 
ATOM   5531 C CD1 . PHE B 1 170 ? 9.950   -27.848 79.252  1.00 15.07 ? 170 PHE B CD1 1 
ATOM   5532 C CD2 . PHE B 1 170 ? 8.202   -26.303 79.775  1.00 16.36 ? 170 PHE B CD2 1 
ATOM   5533 C CE1 . PHE B 1 170 ? 10.724  -27.345 80.299  1.00 16.07 ? 170 PHE B CE1 1 
ATOM   5534 C CE2 . PHE B 1 170 ? 8.960   -25.796 80.829  1.00 14.16 ? 170 PHE B CE2 1 
ATOM   5535 C CZ  . PHE B 1 170 ? 10.225  -26.320 81.092  1.00 21.62 ? 170 PHE B CZ  1 
ATOM   5536 N N   . GLU B 1 171 ? 6.896   -28.135 74.653  1.00 9.59  ? 171 GLU B N   1 
ATOM   5537 C CA  . GLU B 1 171 ? 6.751   -28.942 73.442  1.00 10.09 ? 171 GLU B CA  1 
ATOM   5538 C C   . GLU B 1 171 ? 7.792   -28.537 72.407  1.00 16.34 ? 171 GLU B C   1 
ATOM   5539 O O   . GLU B 1 171 ? 8.370   -29.387 71.731  1.00 9.14  ? 171 GLU B O   1 
ATOM   5540 C CB  . GLU B 1 171 ? 5.337   -28.798 72.862  1.00 20.93 ? 171 GLU B CB  1 
ATOM   5541 C CG  . GLU B 1 171 ? 4.211   -29.310 73.762  1.00 30.25 ? 171 GLU B CG  1 
ATOM   5542 C CD  . GLU B 1 171 ? 2.810   -29.146 73.145  1.00 38.15 ? 171 GLU B CD  1 
ATOM   5543 O OE1 . GLU B 1 171 ? 2.670   -28.484 72.089  1.00 32.15 ? 171 GLU B OE1 1 
ATOM   5544 O OE2 . GLU B 1 171 ? 1.844   -29.687 73.729  1.00 38.75 ? 171 GLU B OE2 1 
ATOM   5545 N N   . ILE B 1 172 ? 8.061   -27.233 72.294  1.00 9.88  ? 172 ILE B N   1 
ATOM   5546 C CA  . ILE B 1 172 ? 9.058   -26.739 71.348  1.00 6.85  ? 172 ILE B CA  1 
ATOM   5547 C C   . ILE B 1 172 ? 10.440  -27.277 71.703  1.00 6.57  ? 172 ILE B C   1 
ATOM   5548 O O   . ILE B 1 172 ? 11.209  -27.687 70.828  1.00 8.81  ? 172 ILE B O   1 
ATOM   5549 C CB  . ILE B 1 172 ? 9.027   -25.198 71.333  1.00 10.21 ? 172 ILE B CB  1 
ATOM   5550 C CG1 . ILE B 1 172 ? 7.765   -24.702 70.628  1.00 9.24  ? 172 ILE B CG1 1 
ATOM   5551 C CG2 . ILE B 1 172 ? 10.275  -24.630 70.644  1.00 12.90 ? 172 ILE B CG2 1 
ATOM   5552 C CD1 . ILE B 1 172 ? 7.740   -24.993 69.145  1.00 16.04 ? 172 ILE B CD1 1 
ATOM   5553 N N   . ILE B 1 173 ? 10.773  -27.299 72.993  1.00 7.21  ? 173 ILE B N   1 
ATOM   5554 C CA  . ILE B 1 173 ? 12.076  -27.804 73.401  1.00 8.15  ? 173 ILE B CA  1 
ATOM   5555 C C   . ILE B 1 173 ? 12.193  -29.288 73.077  1.00 13.17 ? 173 ILE B C   1 
ATOM   5556 O O   . ILE B 1 173 ? 13.215  -29.739 72.557  1.00 10.11 ? 173 ILE B O   1 
ATOM   5557 C CB  . ILE B 1 173 ? 12.319  -27.524 74.895  1.00 7.79  ? 173 ILE B CB  1 
ATOM   5558 C CG1 . ILE B 1 173 ? 12.327  -26.003 75.154  1.00 10.04 ? 173 ILE B CG1 1 
ATOM   5559 C CG2 . ILE B 1 173 ? 13.618  -28.168 75.346  1.00 11.09 ? 173 ILE B CG2 1 
ATOM   5560 C CD1 . ILE B 1 173 ? 12.520  -25.639 76.626  1.00 14.41 ? 173 ILE B CD1 1 
ATOM   5561 N N   . LYS B 1 174 ? 11.138  -30.063 73.351  1.00 7.15  ? 174 LYS B N   1 
ATOM   5562 C CA  . LYS B 1 174 ? 11.157  -31.501 73.086  1.00 6.31  ? 174 LYS B CA  1 
ATOM   5563 C C   . LYS B 1 174 ? 11.300  -31.818 71.605  1.00 10.41 ? 174 LYS B C   1 
ATOM   5564 O O   . LYS B 1 174 ? 11.752  -32.914 71.263  1.00 11.99 ? 174 LYS B O   1 
ATOM   5565 C CB  . LYS B 1 174 ? 9.877   -32.159 73.631  1.00 15.19 ? 174 LYS B CB  1 
ATOM   5566 C CG  . LYS B 1 174 ? 9.760   -32.094 75.146  1.00 16.96 ? 174 LYS B CG  1 
ATOM   5567 C CD  . LYS B 1 174 ? 8.454   -32.748 75.607  1.00 26.32 ? 174 LYS B CD  1 
ATOM   5568 C CE  . LYS B 1 174 ? 8.414   -32.918 77.115  1.00 37.84 ? 174 LYS B CE  1 
ATOM   5569 N NZ  . LYS B 1 174 ? 7.014   -33.050 77.603  1.00 41.99 ? 174 LYS B NZ  1 
ATOM   5570 N N   . LYS B 1 175 ? 10.937  -30.890 70.716  1.00 6.09  ? 175 LYS B N   1 
ATOM   5571 C CA  . LYS B 1 175 ? 11.053  -31.125 69.279  1.00 10.68 ? 175 LYS B CA  1 
ATOM   5572 C C   . LYS B 1 175 ? 12.386  -30.661 68.708  1.00 18.24 ? 175 LYS B C   1 
ATOM   5573 O O   . LYS B 1 175 ? 12.624  -30.840 67.501  1.00 9.91  ? 175 LYS B O   1 
ATOM   5574 C CB  . LYS B 1 175 ? 9.927   -30.402 68.535  1.00 15.14 ? 175 LYS B CB  1 
ATOM   5575 C CG  . LYS B 1 175 ? 8.544   -30.971 68.717  1.00 24.88 ? 175 LYS B CG  1 
ATOM   5576 C CD  . LYS B 1 175 ? 7.587   -30.228 67.793  1.00 26.29 ? 175 LYS B CD  1 
ATOM   5577 C CE  . LYS B 1 175 ? 6.143   -30.415 68.219  1.00 40.20 ? 175 LYS B CE  1 
ATOM   5578 N NZ  . LYS B 1 175 ? 5.738   -31.841 68.135  1.00 49.12 ? 175 LYS B NZ  1 
ATOM   5579 N N   . THR B 1 176 ? 13.242  -30.054 69.536  1.00 12.74 ? 176 THR B N   1 
ATOM   5580 C CA  . THR B 1 176 ? 14.377  -29.292 69.013  1.00 10.81 ? 176 THR B CA  1 
ATOM   5581 C C   . THR B 1 176 ? 15.454  -30.194 68.416  1.00 15.99 ? 176 THR B C   1 
ATOM   5582 O O   . THR B 1 176 ? 15.857  -30.002 67.262  1.00 13.68 ? 176 THR B O   1 
ATOM   5583 C CB  . THR B 1 176 ? 14.961  -28.391 70.104  1.00 10.92 ? 176 THR B CB  1 
ATOM   5584 O OG1 . THR B 1 176 ? 14.013  -27.366 70.405  1.00 9.91  ? 176 THR B OG1 1 
ATOM   5585 C CG2 . THR B 1 176 ? 16.248  -27.701 69.610  1.00 10.83 ? 176 THR B CG2 1 
ATOM   5586 N N   . LEU B 1 177 ? 15.967  -31.164 69.175  1.00 14.41 ? 177 LEU B N   1 
ATOM   5587 C CA  . LEU B 1 177 ? 17.028  -31.986 68.587  1.00 12.56 ? 177 LEU B CA  1 
ATOM   5588 C C   . LEU B 1 177 ? 16.523  -32.732 67.357  1.00 12.03 ? 177 LEU B C   1 
ATOM   5589 O O   . LEU B 1 177 ? 17.288  -32.965 66.415  1.00 15.84 ? 177 LEU B O   1 
ATOM   5590 C CB  . LEU B 1 177 ? 17.603  -32.964 69.617  1.00 12.36 ? 177 LEU B CB  1 
ATOM   5591 C CG  . LEU B 1 177 ? 18.334  -32.277 70.779  1.00 13.09 ? 177 LEU B CG  1 
ATOM   5592 C CD1 . LEU B 1 177 ? 18.957  -33.298 71.702  1.00 16.61 ? 177 LEU B CD1 1 
ATOM   5593 C CD2 . LEU B 1 177 ? 19.398  -31.293 70.254  1.00 15.59 ? 177 LEU B CD2 1 
ATOM   5594 N N   . SER B 1 178 ? 15.232  -33.080 67.342  1.00 10.89 ? 178 SER B N   1 
ATOM   5595 C CA  . SER B 1 178 ? 14.629  -33.736 66.184  1.00 13.49 ? 178 SER B CA  1 
ATOM   5596 C C   . SER B 1 178 ? 14.702  -32.865 64.936  1.00 11.31 ? 178 SER B C   1 
ATOM   5597 O O   . SER B 1 178 ? 14.897  -33.379 63.830  1.00 11.26 ? 178 SER B O   1 
ATOM   5598 C CB  . SER B 1 178 ? 13.168  -34.087 66.475  1.00 16.25 ? 178 SER B CB  1 
ATOM   5599 O OG  . SER B 1 178 ? 13.076  -35.228 67.295  1.00 22.86 ? 178 SER B OG  1 
ATOM   5600 N N   . ILE B 1 179 ? 14.516  -31.546 65.071  1.00 12.70 ? 179 ILE B N   1 
ATOM   5601 C CA  . ILE B 1 179 ? 14.512  -30.771 63.837  1.00 8.78  ? 179 ILE B CA  1 
ATOM   5602 C C   . ILE B 1 179 ? 15.926  -30.683 63.284  1.00 16.56 ? 179 ILE B C   1 
ATOM   5603 O O   . ILE B 1 179 ? 16.115  -30.651 62.060  1.00 12.51 ? 179 ILE B O   1 
ATOM   5604 C CB  . ILE B 1 179 ? 13.852  -29.382 64.017  1.00 14.90 ? 179 ILE B CB  1 
ATOM   5605 C CG1 . ILE B 1 179 ? 13.580  -28.739 62.650  1.00 18.83 ? 179 ILE B CG1 1 
ATOM   5606 C CG2 . ILE B 1 179 ? 14.698  -28.419 64.850  1.00 11.62 ? 179 ILE B CG2 1 
ATOM   5607 C CD1 . ILE B 1 179 ? 12.477  -27.727 62.674  1.00 16.17 ? 179 ILE B CD1 1 
ATOM   5608 N N   . TYR B 1 180 ? 16.943  -30.696 64.154  1.00 10.79 ? 180 TYR B N   1 
ATOM   5609 C CA  . TYR B 1 180 ? 18.316  -30.703 63.651  1.00 14.30 ? 180 TYR B CA  1 
ATOM   5610 C C   . TYR B 1 180 ? 18.621  -32.001 62.920  1.00 13.53 ? 180 TYR B C   1 
ATOM   5611 O O   . TYR B 1 180 ? 19.305  -31.992 61.886  1.00 14.71 ? 180 TYR B O   1 
ATOM   5612 C CB  . TYR B 1 180 ? 19.312  -30.478 64.792  1.00 14.48 ? 180 TYR B CB  1 
ATOM   5613 C CG  . TYR B 1 180 ? 19.339  -29.029 65.229  1.00 10.96 ? 180 TYR B CG  1 
ATOM   5614 C CD1 . TYR B 1 180 ? 19.972  -28.056 64.459  1.00 14.23 ? 180 TYR B CD1 1 
ATOM   5615 C CD2 . TYR B 1 180 ? 18.692  -28.629 66.393  1.00 11.34 ? 180 TYR B CD2 1 
ATOM   5616 C CE1 . TYR B 1 180 ? 19.967  -26.712 64.848  1.00 13.84 ? 180 TYR B CE1 1 
ATOM   5617 C CE2 . TYR B 1 180 ? 18.695  -27.311 66.789  1.00 7.31  ? 180 TYR B CE2 1 
ATOM   5618 C CZ  . TYR B 1 180 ? 19.327  -26.354 66.013  1.00 9.37  ? 180 TYR B CZ  1 
ATOM   5619 O OH  . TYR B 1 180 ? 19.300  -25.040 66.410  1.00 4.94  ? 180 TYR B OH  1 
ATOM   5620 N N   . ARG B 1 181 ? 18.125  -33.132 63.436  1.00 10.00 ? 181 ARG B N   1 
ATOM   5621 C CA  . ARG B 1 181 ? 18.334  -34.386 62.717  1.00 12.89 ? 181 ARG B CA  1 
ATOM   5622 C C   . ARG B 1 181 ? 17.612  -34.360 61.377  1.00 13.38 ? 181 ARG B C   1 
ATOM   5623 O O   . ARG B 1 181 ? 18.141  -34.847 60.373  1.00 13.23 ? 181 ARG B O   1 
ATOM   5624 C CB  . ARG B 1 181 ? 17.879  -35.582 63.560  1.00 12.63 ? 181 ARG B CB  1 
ATOM   5625 C CG  . ARG B 1 181 ? 18.807  -35.894 64.742  1.00 14.17 ? 181 ARG B CG  1 
ATOM   5626 C CD  . ARG B 1 181 ? 18.408  -37.182 65.461  1.00 16.56 ? 181 ARG B CD  1 
ATOM   5627 N NE  . ARG B 1 181 ? 17.241  -36.969 66.303  1.00 21.92 ? 181 ARG B NE  1 
ATOM   5628 C CZ  . ARG B 1 181 ? 17.284  -36.820 67.624  1.00 24.04 ? 181 ARG B CZ  1 
ATOM   5629 N NH1 . ARG B 1 181 ? 18.439  -36.869 68.280  1.00 23.82 ? 181 ARG B NH1 1 
ATOM   5630 N NH2 . ARG B 1 181 ? 16.167  -36.631 68.293  1.00 29.47 ? 181 ARG B NH2 1 
ATOM   5631 N N   . GLU B 1 182 ? 16.428  -33.739 61.332  1.00 13.75 ? 182 GLU B N   1 
ATOM   5632 C CA  . GLU B 1 182 ? 15.628  -33.756 60.115  1.00 10.47 ? 182 GLU B CA  1 
ATOM   5633 C C   . GLU B 1 182 ? 16.249  -32.898 59.020  1.00 18.02 ? 182 GLU B C   1 
ATOM   5634 O O   . GLU B 1 182 ? 16.340  -33.332 57.866  1.00 17.23 ? 182 GLU B O   1 
ATOM   5635 C CB  . GLU B 1 182 ? 14.200  -33.299 60.396  1.00 20.34 ? 182 GLU B CB  1 
ATOM   5636 C CG  . GLU B 1 182 ? 13.319  -33.424 59.160  1.00 32.67 ? 182 GLU B CG  1 
ATOM   5637 C CD  . GLU B 1 182 ? 11.876  -33.033 59.397  1.00 38.85 ? 182 GLU B CD  1 
ATOM   5638 O OE1 . GLU B 1 182 ? 11.594  -32.352 60.407  1.00 32.76 ? 182 GLU B OE1 1 
ATOM   5639 O OE2 . GLU B 1 182 ? 11.023  -33.404 58.559  1.00 40.31 ? 182 GLU B OE2 1 
ATOM   5640 N N   . ILE B 1 183 ? 16.656  -31.663 59.345  1.00 11.31 ? 183 ILE B N   1 
ATOM   5641 C CA  . ILE B 1 183 ? 17.226  -30.819 58.297  1.00 11.07 ? 183 ILE B CA  1 
ATOM   5642 C C   . ILE B 1 183 ? 18.560  -31.376 57.828  1.00 10.66 ? 183 ILE B C   1 
ATOM   5643 O O   . ILE B 1 183 ? 18.924  -31.240 56.650  1.00 16.62 ? 183 ILE B O   1 
ATOM   5644 C CB  . ILE B 1 183 ? 17.336  -29.354 58.771  1.00 12.07 ? 183 ILE B CB  1 
ATOM   5645 C CG1 . ILE B 1 183 ? 18.292  -29.221 59.965  1.00 20.13 ? 183 ILE B CG1 1 
ATOM   5646 C CG2 . ILE B 1 183 ? 15.966  -28.838 59.141  1.00 18.51 ? 183 ILE B CG2 1 
ATOM   5647 C CD1 . ILE B 1 183 ? 19.647  -28.628 59.605  1.00 21.27 ? 183 ILE B CD1 1 
ATOM   5648 N N   . LYS B 1 184 ? 19.294  -32.037 58.718  1.00 16.45 ? 184 LYS B N   1 
ATOM   5649 C CA  . LYS B 1 184 ? 20.542  -32.686 58.333  1.00 15.11 ? 184 LYS B CA  1 
ATOM   5650 C C   . LYS B 1 184 ? 20.286  -33.845 57.372  1.00 22.80 ? 184 LYS B C   1 
ATOM   5651 O O   . LYS B 1 184 ? 20.910  -33.938 56.306  1.00 19.25 ? 184 LYS B O   1 
ATOM   5652 C CB  . LYS B 1 184 ? 21.259  -33.156 59.599  1.00 15.33 ? 184 LYS B CB  1 
ATOM   5653 C CG  . LYS B 1 184 ? 22.627  -33.746 59.413  1.00 17.78 ? 184 LYS B CG  1 
ATOM   5654 C CD  . LYS B 1 184 ? 23.112  -34.281 60.740  1.00 17.64 ? 184 LYS B CD  1 
ATOM   5655 C CE  . LYS B 1 184 ? 24.504  -34.865 60.631  1.00 15.56 ? 184 LYS B CE  1 
ATOM   5656 N NZ  . LYS B 1 184 ? 24.621  -35.681 59.406  1.00 29.30 ? 184 LYS B NZ  1 
ATOM   5657 N N   . GLU B 1 185 ? 19.348  -34.724 57.730  1.00 16.05 ? 185 GLU B N   1 
ATOM   5658 C CA  . GLU B 1 185 ? 19.013  -35.880 56.901  1.00 20.09 ? 185 GLU B CA  1 
ATOM   5659 C C   . GLU B 1 185 ? 18.453  -35.463 55.547  1.00 17.97 ? 185 GLU B C   1 
ATOM   5660 O O   . GLU B 1 185 ? 18.701  -36.126 54.534  1.00 19.42 ? 185 GLU B O   1 
ATOM   5661 C CB  . GLU B 1 185 ? 17.990  -36.738 57.638  1.00 20.48 ? 185 GLU B CB  1 
ATOM   5662 C CG  . GLU B 1 185 ? 17.842  -38.153 57.150  1.00 27.09 ? 185 GLU B CG  1 
ATOM   5663 C CD  . GLU B 1 185 ? 16.906  -38.935 58.047  1.00 29.30 ? 185 GLU B CD  1 
ATOM   5664 O OE1 . GLU B 1 185 ? 17.016  -38.807 59.285  1.00 32.74 ? 185 GLU B OE1 1 
ATOM   5665 O OE2 . GLU B 1 185 ? 16.042  -39.655 57.522  1.00 32.72 ? 185 GLU B OE2 1 
ATOM   5666 N N   . GLU B 1 186 ? 17.629  -34.420 55.524  1.00 12.70 ? 186 GLU B N   1 
ATOM   5667 C CA  . GLU B 1 186 ? 17.030  -33.927 54.288  1.00 17.91 ? 186 GLU B CA  1 
ATOM   5668 C C   . GLU B 1 186 ? 17.998  -33.119 53.433  1.00 22.23 ? 186 GLU B C   1 
ATOM   5669 O O   . GLU B 1 186 ? 17.619  -32.694 52.335  1.00 18.99 ? 186 GLU B O   1 
ATOM   5670 C CB  . GLU B 1 186 ? 15.797  -33.079 54.607  1.00 16.01 ? 186 GLU B CB  1 
ATOM   5671 C CG  . GLU B 1 186 ? 14.646  -33.876 55.246  1.00 13.39 ? 186 GLU B CG  1 
ATOM   5672 C CD  . GLU B 1 186 ? 13.426  -33.028 55.546  1.00 21.62 ? 186 GLU B CD  1 
ATOM   5673 O OE1 . GLU B 1 186 ? 13.581  -31.808 55.743  1.00 25.37 ? 186 GLU B OE1 1 
ATOM   5674 O OE2 . GLU B 1 186 ? 12.314  -33.587 55.603  1.00 24.68 ? 186 GLU B OE2 1 
ATOM   5675 N N   . GLY B 1 187 ? 19.217  -32.879 53.908  1.00 20.41 ? 187 GLY B N   1 
ATOM   5676 C CA  . GLY B 1 187 ? 20.181  -32.137 53.115  1.00 15.33 ? 187 GLY B CA  1 
ATOM   5677 C C   . GLY B 1 187 ? 19.917  -30.651 53.075  1.00 18.37 ? 187 GLY B C   1 
ATOM   5678 O O   . GLY B 1 187 ? 20.466  -29.952 52.220  1.00 16.01 ? 187 GLY B O   1 
ATOM   5679 N N   . LYS B 1 188 ? 19.086  -30.141 53.977  1.00 9.00  ? 188 LYS B N   1 
ATOM   5680 C CA  . LYS B 1 188 ? 18.820  -28.714 54.017  1.00 10.27 ? 188 LYS B CA  1 
ATOM   5681 C C   . LYS B 1 188 ? 19.887  -27.953 54.781  1.00 13.03 ? 188 LYS B C   1 
ATOM   5682 O O   . LYS B 1 188 ? 19.920  -26.727 54.702  1.00 13.26 ? 188 LYS B O   1 
ATOM   5683 C CB  . LYS B 1 188 ? 17.444  -28.451 54.627  1.00 15.83 ? 188 LYS B CB  1 
ATOM   5684 C CG  . LYS B 1 188 ? 16.298  -29.029 53.805  1.00 18.54 ? 188 LYS B CG  1 
ATOM   5685 C CD  . LYS B 1 188 ? 15.013  -29.077 54.614  1.00 22.61 ? 188 LYS B CD  1 
ATOM   5686 C CE  . LYS B 1 188 ? 13.806  -29.332 53.712  1.00 22.88 ? 188 LYS B CE  1 
ATOM   5687 N NZ  . LYS B 1 188 ? 13.277  -28.025 53.250  1.00 35.81 ? 188 LYS B NZ  1 
ATOM   5688 N N   . GLY B 1 189 ? 20.751  -28.647 55.511  1.00 13.58 ? 189 GLY B N   1 
ATOM   5689 C CA  . GLY B 1 189 ? 21.804  -27.981 56.258  1.00 17.81 ? 189 GLY B CA  1 
ATOM   5690 C C   . GLY B 1 189 ? 22.764  -28.977 56.866  1.00 18.80 ? 189 GLY B C   1 
ATOM   5691 O O   . GLY B 1 189 ? 22.376  -30.117 57.145  1.00 15.85 ? 189 GLY B O   1 
ATOM   5692 N N   . SER B 1 190 ? 24.016  -28.575 57.062  1.00 10.18 ? 190 SER B N   1 
ATOM   5693 C CA  . SER B 1 190 ? 24.943  -29.375 57.843  1.00 10.36 ? 190 SER B CA  1 
ATOM   5694 C C   . SER B 1 190 ? 24.883  -28.937 59.301  1.00 11.56 ? 190 SER B C   1 
ATOM   5695 O O   . SER B 1 190 ? 24.533  -27.794 59.611  1.00 11.77 ? 190 SER B O   1 
ATOM   5696 C CB  . SER B 1 190 ? 26.375  -29.244 57.314  1.00 9.95  ? 190 SER B CB  1 
ATOM   5697 O OG  . SER B 1 190 ? 26.443  -29.617 55.946  1.00 12.95 ? 190 SER B OG  1 
ATOM   5698 N N   . VAL B 1 191 ? 25.207  -29.858 60.204  1.00 11.98 ? 191 VAL B N   1 
ATOM   5699 C CA  . VAL B 1 191 ? 25.310  -29.542 61.623  1.00 13.75 ? 191 VAL B CA  1 
ATOM   5700 C C   . VAL B 1 191 ? 26.729  -29.852 62.072  1.00 15.65 ? 191 VAL B C   1 
ATOM   5701 O O   . VAL B 1 191 ? 27.243  -30.950 61.819  1.00 15.12 ? 191 VAL B O   1 
ATOM   5702 C CB  . VAL B 1 191 ? 24.282  -30.307 62.476  1.00 11.18 ? 191 VAL B CB  1 
ATOM   5703 C CG1 . VAL B 1 191 ? 24.306  -29.794 63.935  1.00 4.82  ? 191 VAL B CG1 1 
ATOM   5704 C CG2 . VAL B 1 191 ? 22.886  -30.173 61.882  1.00 9.22  ? 191 VAL B CG2 1 
ATOM   5705 N N   . SER B 1 192 ? 27.356  -28.881 62.724  1.00 13.01 ? 192 SER B N   1 
ATOM   5706 C CA  . SER B 1 192 ? 28.693  -29.013 63.286  1.00 10.33 ? 192 SER B CA  1 
ATOM   5707 C C   . SER B 1 192 ? 28.600  -29.021 64.802  1.00 10.74 ? 192 SER B C   1 
ATOM   5708 O O   . SER B 1 192 ? 27.525  -28.826 65.386  1.00 8.53  ? 192 SER B O   1 
ATOM   5709 C CB  . SER B 1 192 ? 29.592  -27.871 62.818  1.00 4.82  ? 192 SER B CB  1 
ATOM   5710 O OG  . SER B 1 192 ? 29.193  -26.629 63.407  1.00 11.22 ? 192 SER B OG  1 
ATOM   5711 N N   . THR B 1 193 ? 29.739  -29.234 65.450  1.00 9.50  ? 193 THR B N   1 
ATOM   5712 C CA  . THR B 1 193 ? 29.835  -28.981 66.888  1.00 10.46 ? 193 THR B CA  1 
ATOM   5713 C C   . THR B 1 193 ? 31.154  -28.268 67.194  1.00 9.22  ? 193 THR B C   1 
ATOM   5714 O O   . THR B 1 193 ? 31.949  -27.975 66.297  1.00 6.83  ? 193 THR B O   1 
ATOM   5715 C CB  . THR B 1 193 ? 29.680  -30.279 67.689  1.00 10.50 ? 193 THR B CB  1 
ATOM   5716 O OG1 . THR B 1 193 ? 29.492  -29.952 69.072  1.00 12.31 ? 193 THR B OG1 1 
ATOM   5717 C CG2 . THR B 1 193 ? 30.895  -31.192 67.543  1.00 9.61  ? 193 THR B CG2 1 
ATOM   5718 N N   . SER B 1 194 ? 31.367  -27.963 68.473  1.00 9.93  ? 194 SER B N   1 
ATOM   5719 C CA  . SER B 1 194 ? 32.555  -27.301 68.995  1.00 11.07 ? 194 SER B CA  1 
ATOM   5720 C C   . SER B 1 194 ? 33.193  -28.187 70.047  1.00 11.96 ? 194 SER B C   1 
ATOM   5721 O O   . SER B 1 194 ? 32.510  -29.034 70.636  1.00 7.43  ? 194 SER B O   1 
ATOM   5722 C CB  . SER B 1 194 ? 32.198  -25.954 69.644  1.00 8.84  ? 194 SER B CB  1 
ATOM   5723 O OG  . SER B 1 194 ? 31.872  -24.996 68.641  1.00 9.10  ? 194 SER B OG  1 
ATOM   5724 N N   . PRO B 1 195 ? 34.487  -28.011 70.336  1.00 7.50  ? 195 PRO B N   1 
ATOM   5725 C CA  . PRO B 1 195 ? 35.049  -28.638 71.540  1.00 12.18 ? 195 PRO B CA  1 
ATOM   5726 C C   . PRO B 1 195 ? 34.151  -28.377 72.748  1.00 12.82 ? 195 PRO B C   1 
ATOM   5727 O O   . PRO B 1 195 ? 33.552  -27.308 72.879  1.00 10.04 ? 195 PRO B O   1 
ATOM   5728 C CB  . PRO B 1 195 ? 36.420  -27.975 71.687  1.00 17.14 ? 195 PRO B CB  1 
ATOM   5729 C CG  . PRO B 1 195 ? 36.755  -27.469 70.326  1.00 21.94 ? 195 PRO B CG  1 
ATOM   5730 C CD  . PRO B 1 195 ? 35.456  -27.150 69.641  1.00 10.84 ? 195 PRO B CD  1 
ATOM   5731 N N   . TYR B 1 196 ? 34.080  -29.366 73.646  1.00 5.75  ? 196 TYR B N   1 
ATOM   5732 C CA  . TYR B 1 196 ? 32.859  -29.646 74.417  1.00 8.14  ? 196 TYR B CA  1 
ATOM   5733 C C   . TYR B 1 196 ? 32.299  -28.434 75.178  1.00 10.87 ? 196 TYR B C   1 
ATOM   5734 O O   . TYR B 1 196 ? 31.108  -28.116 75.062  1.00 9.57  ? 196 TYR B O   1 
ATOM   5735 C CB  . TYR B 1 196 ? 33.125  -30.803 75.388  1.00 7.18  ? 196 TYR B CB  1 
ATOM   5736 C CG  . TYR B 1 196 ? 31.867  -31.523 75.872  1.00 7.82  ? 196 TYR B CG  1 
ATOM   5737 C CD1 . TYR B 1 196 ? 31.001  -30.927 76.788  1.00 8.64  ? 196 TYR B CD1 1 
ATOM   5738 C CD2 . TYR B 1 196 ? 31.538  -32.785 75.381  1.00 7.60  ? 196 TYR B CD2 1 
ATOM   5739 C CE1 . TYR B 1 196 ? 29.861  -31.585 77.223  1.00 11.61 ? 196 TYR B CE1 1 
ATOM   5740 C CE2 . TYR B 1 196 ? 30.398  -33.449 75.808  1.00 6.97  ? 196 TYR B CE2 1 
ATOM   5741 C CZ  . TYR B 1 196 ? 29.567  -32.842 76.737  1.00 10.79 ? 196 TYR B CZ  1 
ATOM   5742 O OH  . TYR B 1 196 ? 28.427  -33.488 77.170  1.00 13.77 ? 196 TYR B OH  1 
ATOM   5743 N N   . TYR B 1 197 ? 33.112  -27.796 76.030  1.00 8.15  ? 197 TYR B N   1 
ATOM   5744 C CA  . TYR B 1 197 ? 32.655  -26.659 76.830  1.00 12.08 ? 197 TYR B CA  1 
ATOM   5745 C C   . TYR B 1 197 ? 33.060  -25.314 76.240  1.00 9.97  ? 197 TYR B C   1 
ATOM   5746 O O   . TYR B 1 197 ? 33.164  -24.327 76.978  1.00 6.43  ? 197 TYR B O   1 
ATOM   5747 C CB  . TYR B 1 197 ? 33.150  -26.780 78.272  1.00 11.22 ? 197 TYR B CB  1 
ATOM   5748 C CG  . TYR B 1 197 ? 32.559  -27.999 78.919  1.00 9.17  ? 197 TYR B CG  1 
ATOM   5749 C CD1 . TYR B 1 197 ? 31.238  -28.003 79.327  1.00 9.41  ? 197 TYR B CD1 1 
ATOM   5750 C CD2 . TYR B 1 197 ? 33.300  -29.177 79.051  1.00 11.34 ? 197 TYR B CD2 1 
ATOM   5751 C CE1 . TYR B 1 197 ? 30.659  -29.133 79.895  1.00 8.35  ? 197 TYR B CE1 1 
ATOM   5752 C CE2 . TYR B 1 197 ? 32.723  -30.319 79.628  1.00 12.71 ? 197 TYR B CE2 1 
ATOM   5753 C CZ  . TYR B 1 197 ? 31.404  -30.278 80.041  1.00 13.02 ? 197 TYR B CZ  1 
ATOM   5754 O OH  . TYR B 1 197 ? 30.809  -31.383 80.599  1.00 13.80 ? 197 TYR B OH  1 
ATOM   5755 N N   . HIS B 1 198 ? 33.253  -25.245 74.929  1.00 7.05  ? 198 HIS B N   1 
ATOM   5756 C CA  . HIS B 1 198 ? 33.563  -23.981 74.259  1.00 10.60 ? 198 HIS B CA  1 
ATOM   5757 C C   . HIS B 1 198 ? 34.801  -23.305 74.863  1.00 11.90 ? 198 HIS B C   1 
ATOM   5758 O O   . HIS B 1 198 ? 34.738  -22.128 75.219  1.00 8.67  ? 198 HIS B O   1 
ATOM   5759 C CB  . HIS B 1 198 ? 32.321  -23.078 74.341  1.00 9.82  ? 198 HIS B CB  1 
ATOM   5760 C CG  . HIS B 1 198 ? 32.268  -21.953 73.341  1.00 4.79  ? 198 HIS B CG  1 
ATOM   5761 N ND1 . HIS B 1 198 ? 32.633  -20.662 73.659  1.00 6.92  ? 198 HIS B ND1 1 
ATOM   5762 C CD2 . HIS B 1 198 ? 31.810  -21.908 72.064  1.00 6.21  ? 198 HIS B CD2 1 
ATOM   5763 C CE1 . HIS B 1 198 ? 32.432  -19.877 72.613  1.00 7.57  ? 198 HIS B CE1 1 
ATOM   5764 N NE2 . HIS B 1 198 ? 31.937  -20.607 71.627  1.00 9.00  ? 198 HIS B NE2 1 
ATOM   5765 N N   . PRO B 1 199 ? 35.935  -23.993 75.003  1.00 12.74 ? 199 PRO B N   1 
ATOM   5766 C CA  . PRO B 1 199 ? 37.150  -23.340 75.515  1.00 10.37 ? 199 PRO B CA  1 
ATOM   5767 C C   . PRO B 1 199 ? 37.902  -22.589 74.417  1.00 11.58 ? 199 PRO B C   1 
ATOM   5768 O O   . PRO B 1 199 ? 37.638  -22.747 73.225  1.00 13.30 ? 199 PRO B O   1 
ATOM   5769 C CB  . PRO B 1 199 ? 37.981  -24.530 75.986  1.00 10.76 ? 199 PRO B CB  1 
ATOM   5770 C CG  . PRO B 1 199 ? 37.685  -25.549 74.959  1.00 6.76  ? 199 PRO B CG  1 
ATOM   5771 C CD  . PRO B 1 199 ? 36.184  -25.420 74.731  1.00 8.00  ? 199 PRO B CD  1 
ATOM   5772 N N   . LEU B 1 200 ? 38.904  -21.800 74.839  1.00 15.45 ? 200 LEU B N   1 
ATOM   5773 C CA  . LEU B 1 200 ? 39.896  -21.245 73.910  1.00 9.10  ? 200 LEU B CA  1 
ATOM   5774 C C   . LEU B 1 200 ? 41.009  -22.271 73.705  1.00 10.67 ? 200 LEU B C   1 
ATOM   5775 O O   . LEU B 1 200 ? 42.016  -22.285 74.420  1.00 9.37  ? 200 LEU B O   1 
ATOM   5776 C CB  . LEU B 1 200 ? 40.456  -19.929 74.435  1.00 10.06 ? 200 LEU B CB  1 
ATOM   5777 C CG  . LEU B 1 200 ? 39.408  -18.820 74.637  1.00 9.91  ? 200 LEU B CG  1 
ATOM   5778 C CD1 . LEU B 1 200 ? 40.014  -17.674 75.387  1.00 12.93 ? 200 LEU B CD1 1 
ATOM   5779 C CD2 . LEU B 1 200 ? 38.857  -18.353 73.282  1.00 15.48 ? 200 LEU B CD2 1 
ATOM   5780 N N   . ILE B 1 201 ? 40.833  -23.130 72.702  1.00 13.47 ? 201 ILE B N   1 
ATOM   5781 C CA  . ILE B 1 201 ? 41.765  -24.222 72.405  1.00 8.35  ? 201 ILE B CA  1 
ATOM   5782 C C   . ILE B 1 201 ? 43.200  -23.726 72.215  1.00 6.76  ? 201 ILE B C   1 
ATOM   5783 O O   . ILE B 1 201 ? 44.126  -24.350 72.761  1.00 9.00  ? 201 ILE B O   1 
ATOM   5784 C CB  . ILE B 1 201 ? 41.289  -25.033 71.180  1.00 7.38  ? 201 ILE B CB  1 
ATOM   5785 C CG1 . ILE B 1 201 ? 39.966  -25.756 71.493  1.00 7.76  ? 201 ILE B CG1 1 
ATOM   5786 C CG2 . ILE B 1 201 ? 42.357  -26.008 70.721  1.00 4.86  ? 201 ILE B CG2 1 
ATOM   5787 C CD1 . ILE B 1 201 ? 40.119  -26.873 72.513  1.00 7.87  ? 201 ILE B CD1 1 
ATOM   5788 N N   . PRO B 1 202 ? 43.466  -22.625 71.488  1.00 11.28 ? 202 PRO B N   1 
ATOM   5789 C CA  . PRO B 1 202 ? 44.874  -22.216 71.326  1.00 9.98  ? 202 PRO B CA  1 
ATOM   5790 C C   . PRO B 1 202 ? 45.550  -21.880 72.630  1.00 13.39 ? 202 PRO B C   1 
ATOM   5791 O O   . PRO B 1 202 ? 46.755  -22.127 72.772  1.00 7.91  ? 202 PRO B O   1 
ATOM   5792 C CB  . PRO B 1 202 ? 44.787  -20.983 70.417  1.00 8.47  ? 202 PRO B CB  1 
ATOM   5793 C CG  . PRO B 1 202 ? 43.518  -21.248 69.616  1.00 10.56 ? 202 PRO B CG  1 
ATOM   5794 C CD  . PRO B 1 202 ? 42.577  -21.827 70.617  1.00 9.13  ? 202 PRO B CD  1 
ATOM   5795 N N   . ILE B 1 203 ? 44.814  -21.311 73.586  1.00 6.83  ? 203 ILE B N   1 
ATOM   5796 C CA  . ILE B 1 203 ? 45.425  -20.990 74.871  1.00 7.98  ? 203 ILE B CA  1 
ATOM   5797 C C   . ILE B 1 203 ? 45.699  -22.261 75.656  1.00 10.65 ? 203 ILE B C   1 
ATOM   5798 O O   . ILE B 1 203 ? 46.765  -22.407 76.265  1.00 9.24  ? 203 ILE B O   1 
ATOM   5799 C CB  . ILE B 1 203 ? 44.539  -20.015 75.661  1.00 9.86  ? 203 ILE B CB  1 
ATOM   5800 C CG1 . ILE B 1 203 ? 44.530  -18.649 74.964  1.00 12.51 ? 203 ILE B CG1 1 
ATOM   5801 C CG2 . ILE B 1 203 ? 45.018  -19.927 77.126  1.00 7.97  ? 203 ILE B CG2 1 
ATOM   5802 C CD1 . ILE B 1 203 ? 43.851  -17.525 75.806  1.00 19.79 ? 203 ILE B CD1 1 
ATOM   5803 N N   . LEU B 1 204 ? 44.749  -23.201 75.656  1.00 9.83  ? 204 LEU B N   1 
ATOM   5804 C CA  . LEU B 1 204 ? 44.962  -24.468 76.341  1.00 6.46  ? 204 LEU B CA  1 
ATOM   5805 C C   . LEU B 1 204 ? 46.187  -25.191 75.791  1.00 15.15 ? 204 LEU B C   1 
ATOM   5806 O O   . LEU B 1 204 ? 46.947  -25.805 76.549  1.00 12.08 ? 204 LEU B O   1 
ATOM   5807 C CB  . LEU B 1 204 ? 43.720  -25.361 76.207  1.00 4.91  ? 204 LEU B CB  1 
ATOM   5808 C CG  . LEU B 1 204 ? 42.396  -24.901 76.858  1.00 9.53  ? 204 LEU B CG  1 
ATOM   5809 C CD1 . LEU B 1 204 ? 41.367  -26.048 76.816  1.00 7.82  ? 204 LEU B CD1 1 
ATOM   5810 C CD2 . LEU B 1 204 ? 42.604  -24.370 78.283  1.00 16.06 ? 204 LEU B CD2 1 
ATOM   5811 N N   . LEU B 1 205 ? 46.391  -25.140 74.474  1.00 6.55  ? 205 LEU B N   1 
ATOM   5812 C CA  . LEU B 1 205 ? 47.544  -25.820 73.877  1.00 8.44  ? 205 LEU B CA  1 
ATOM   5813 C C   . LEU B 1 205 ? 48.849  -25.085 74.166  1.00 12.81 ? 205 LEU B C   1 
ATOM   5814 O O   . LEU B 1 205 ? 49.897  -25.712 74.367  1.00 8.73  ? 205 LEU B O   1 
ATOM   5815 C CB  . LEU B 1 205 ? 47.341  -25.949 72.363  1.00 5.99  ? 205 LEU B CB  1 
ATOM   5816 C CG  . LEU B 1 205 ? 46.259  -26.934 71.953  1.00 9.40  ? 205 LEU B CG  1 
ATOM   5817 C CD1 . LEU B 1 205 ? 46.073  -26.938 70.441  1.00 10.72 ? 205 LEU B CD1 1 
ATOM   5818 C CD2 . LEU B 1 205 ? 46.631  -28.318 72.449  1.00 16.50 ? 205 LEU B CD2 1 
ATOM   5819 N N   . ASN B 1 206 ? 48.819  -23.756 74.162  1.00 7.97  ? 206 ASN B N   1 
ATOM   5820 C CA  . ASN B 1 206 ? 50.053  -22.987 74.192  1.00 9.20  ? 206 ASN B CA  1 
ATOM   5821 C C   . ASN B 1 206 ? 49.740  -21.557 74.615  1.00 6.59  ? 206 ASN B C   1 
ATOM   5822 O O   . ASN B 1 206 ? 49.487  -20.702 73.756  1.00 11.70 ? 206 ASN B O   1 
ATOM   5823 C CB  . ASN B 1 206 ? 50.739  -22.999 72.823  1.00 16.58 ? 206 ASN B CB  1 
ATOM   5824 C CG  . ASN B 1 206 ? 51.958  -22.068 72.774  1.00 16.45 ? 206 ASN B CG  1 
ATOM   5825 O OD1 . ASN B 1 206 ? 52.563  -21.795 73.806  1.00 16.00 ? 206 ASN B OD1 1 
ATOM   5826 N ND2 . ASN B 1 206 ? 52.311  -21.576 71.573  1.00 14.40 ? 206 ASN B ND2 1 
ATOM   5827 N N   . PRO B 1 207 ? 49.709  -21.268 75.917  1.00 10.49 ? 207 PRO B N   1 
ATOM   5828 C CA  . PRO B 1 207 ? 49.354  -19.905 76.361  1.00 5.77  ? 207 PRO B CA  1 
ATOM   5829 C C   . PRO B 1 207 ? 50.187  -18.800 75.743  1.00 13.76 ? 207 PRO B C   1 
ATOM   5830 O O   . PRO B 1 207 ? 49.694  -17.668 75.603  1.00 8.48  ? 207 PRO B O   1 
ATOM   5831 C CB  . PRO B 1 207 ? 49.563  -19.969 77.880  1.00 9.95  ? 207 PRO B CB  1 
ATOM   5832 C CG  . PRO B 1 207 ? 49.338  -21.445 78.216  1.00 7.97  ? 207 PRO B CG  1 
ATOM   5833 C CD  . PRO B 1 207 ? 49.858  -22.208 77.040  1.00 8.75  ? 207 PRO B CD  1 
ATOM   5834 N N   . ASN B 1 208 ? 51.436  -19.081 75.379  1.00 9.83  ? 208 ASN B N   1 
ATOM   5835 C CA  . ASN B 1 208 ? 52.300  -18.076 74.778  1.00 8.29  ? 208 ASN B CA  1 
ATOM   5836 C C   . ASN B 1 208 ? 51.794  -17.582 73.431  1.00 7.44  ? 208 ASN B C   1 
ATOM   5837 O O   . ASN B 1 208 ? 52.313  -16.584 72.918  1.00 11.16 ? 208 ASN B O   1 
ATOM   5838 C CB  . ASN B 1 208 ? 53.711  -18.647 74.597  1.00 13.48 ? 208 ASN B CB  1 
ATOM   5839 C CG  . ASN B 1 208 ? 54.379  -18.967 75.920  1.00 13.49 ? 208 ASN B CG  1 
ATOM   5840 O OD1 . ASN B 1 208 ? 53.982  -18.449 76.965  1.00 16.40 ? 208 ASN B OD1 1 
ATOM   5841 N ND2 . ASN B 1 208 ? 55.422  -19.800 75.877  1.00 22.43 ? 208 ASN B ND2 1 
ATOM   5842 N N   . CYS B 1 209 ? 50.809  -18.245 72.840  1.00 9.98  ? 209 CYS B N   1 
ATOM   5843 C CA  . CYS B 1 209 ? 50.357  -17.815 71.532  1.00 7.46  ? 209 CYS B CA  1 
ATOM   5844 C C   . CYS B 1 209 ? 49.683  -16.449 71.592  1.00 8.81  ? 209 CYS B C   1 
ATOM   5845 O O   . CYS B 1 209 ? 49.543  -15.803 70.551  1.00 8.05  ? 209 CYS B O   1 
ATOM   5846 C CB  . CYS B 1 209 ? 49.427  -18.866 70.927  1.00 13.80 ? 209 CYS B CB  1 
ATOM   5847 S SG  . CYS B 1 209 ? 47.734  -18.863 71.589  1.00 14.46 ? 209 CYS B SG  1 
ATOM   5848 N N   . VAL B 1 210 ? 49.328  -15.971 72.788  1.00 7.06  ? 210 VAL B N   1 
ATOM   5849 C CA  . VAL B 1 210 ? 48.729  -14.638 72.889  1.00 7.63  ? 210 VAL B CA  1 
ATOM   5850 C C   . VAL B 1 210 ? 49.732  -13.574 72.469  1.00 6.99  ? 210 VAL B C   1 
ATOM   5851 O O   . VAL B 1 210 ? 49.347  -12.502 71.987  1.00 11.90 ? 210 VAL B O   1 
ATOM   5852 C CB  . VAL B 1 210 ? 48.185  -14.371 74.307  1.00 16.36 ? 210 VAL B CB  1 
ATOM   5853 C CG1 . VAL B 1 210 ? 47.140  -15.428 74.688  1.00 13.59 ? 210 VAL B CG1 1 
ATOM   5854 C CG2 . VAL B 1 210 ? 49.321  -14.327 75.329  1.00 14.44 ? 210 VAL B CG2 1 
ATOM   5855 N N   . TYR B 1 211 ? 51.026  -13.863 72.598  1.00 11.84 ? 211 TYR B N   1 
ATOM   5856 C CA  . TYR B 1 211 ? 52.064  -12.904 72.245  1.00 11.61 ? 211 TYR B CA  1 
ATOM   5857 C C   . TYR B 1 211 ? 52.233  -12.736 70.742  1.00 19.33 ? 211 TYR B C   1 
ATOM   5858 O O   . TYR B 1 211 ? 52.962  -11.833 70.322  1.00 16.80 ? 211 TYR B O   1 
ATOM   5859 C CB  . TYR B 1 211 ? 53.391  -13.333 72.902  1.00 8.20  ? 211 TYR B CB  1 
ATOM   5860 C CG  . TYR B 1 211 ? 53.271  -13.377 74.404  1.00 11.64 ? 211 TYR B CG  1 
ATOM   5861 C CD1 . TYR B 1 211 ? 52.873  -12.244 75.112  1.00 12.64 ? 211 TYR B CD1 1 
ATOM   5862 C CD2 . TYR B 1 211 ? 53.508  -14.550 75.118  1.00 13.77 ? 211 TYR B CD2 1 
ATOM   5863 C CE1 . TYR B 1 211 ? 52.725  -12.267 76.478  1.00 15.51 ? 211 TYR B CE1 1 
ATOM   5864 C CE2 . TYR B 1 211 ? 53.359  -14.579 76.496  1.00 18.99 ? 211 TYR B CE2 1 
ATOM   5865 C CZ  . TYR B 1 211 ? 52.973  -13.429 77.167  1.00 25.96 ? 211 TYR B CZ  1 
ATOM   5866 O OH  . TYR B 1 211 ? 52.833  -13.426 78.534  1.00 46.09 ? 211 TYR B OH  1 
ATOM   5867 N N   . GLU B 1 212 ? 51.584  -13.568 69.919  1.00 15.05 ? 212 GLU B N   1 
ATOM   5868 C CA  . GLU B 1 212 ? 51.651  -13.339 68.479  1.00 21.82 ? 212 GLU B CA  1 
ATOM   5869 C C   . GLU B 1 212 ? 50.936  -12.056 68.068  1.00 21.69 ? 212 GLU B C   1 
ATOM   5870 O O   . GLU B 1 212 ? 51.306  -11.457 67.052  1.00 22.36 ? 212 GLU B O   1 
ATOM   5871 C CB  . GLU B 1 212 ? 51.078  -14.536 67.723  1.00 15.35 ? 212 GLU B CB  1 
ATOM   5872 C CG  . GLU B 1 212 ? 51.797  -15.855 68.054  1.00 11.27 ? 212 GLU B CG  1 
ATOM   5873 C CD  . GLU B 1 212 ? 51.254  -17.029 67.295  1.00 14.79 ? 212 GLU B CD  1 
ATOM   5874 O OE1 . GLU B 1 212 ? 50.608  -16.823 66.260  1.00 20.25 ? 212 GLU B OE1 1 
ATOM   5875 O OE2 . GLU B 1 212 ? 51.474  -18.163 67.745  1.00 25.23 ? 212 GLU B OE2 1 
ATOM   5876 N N   . THR B 1 213 ? 49.937  -11.614 68.837  1.00 18.08 ? 213 THR B N   1 
ATOM   5877 C CA  . THR B 1 213 ? 49.174  -10.413 68.515  1.00 15.24 ? 213 THR B CA  1 
ATOM   5878 C C   . THR B 1 213 ? 49.258  -9.316  69.559  1.00 17.36 ? 213 THR B C   1 
ATOM   5879 O O   . THR B 1 213 ? 49.102  -8.152  69.204  1.00 19.17 ? 213 THR B O   1 
ATOM   5880 C CB  . THR B 1 213 ? 47.684  -10.744 68.314  1.00 17.93 ? 213 THR B CB  1 
ATOM   5881 O OG1 . THR B 1 213 ? 47.214  -11.440 69.475  1.00 16.33 ? 213 THR B OG1 1 
ATOM   5882 C CG2 . THR B 1 213 ? 47.500  -11.602 67.083  1.00 13.71 ? 213 THR B CG2 1 
ATOM   5883 N N   . THR B 1 214 ? 49.452  -9.644  70.834  1.00 17.16 ? 214 THR B N   1 
ATOM   5884 C CA  . THR B 1 214 ? 49.491  -8.647  71.899  1.00 12.61 ? 214 THR B CA  1 
ATOM   5885 C C   . THR B 1 214 ? 50.751  -8.862  72.723  1.00 14.59 ? 214 THR B C   1 
ATOM   5886 O O   . THR B 1 214 ? 50.721  -9.530  73.764  1.00 15.34 ? 214 THR B O   1 
ATOM   5887 C CB  . THR B 1 214 ? 48.232  -8.702  72.765  1.00 9.76  ? 214 THR B CB  1 
ATOM   5888 O OG1 . THR B 1 214 ? 48.077  -10.013 73.330  1.00 12.76 ? 214 THR B OG1 1 
ATOM   5889 C CG2 . THR B 1 214 ? 46.999  -8.354  71.921  1.00 10.51 ? 214 THR B CG2 1 
ATOM   5890 N N   . PRO B 1 215 ? 51.885  -8.304  72.280  1.00 14.79 ? 215 PRO B N   1 
ATOM   5891 C CA  . PRO B 1 215 ? 53.169  -8.587  72.953  1.00 17.50 ? 215 PRO B CA  1 
ATOM   5892 C C   . PRO B 1 215 ? 53.283  -8.052  74.370  1.00 16.30 ? 215 PRO B C   1 
ATOM   5893 O O   . PRO B 1 215 ? 54.123  -8.553  75.131  1.00 19.53 ? 215 PRO B O   1 
ATOM   5894 C CB  . PRO B 1 215 ? 54.204  -7.907  72.043  1.00 20.91 ? 215 PRO B CB  1 
ATOM   5895 C CG  . PRO B 1 215 ? 53.550  -7.761  70.726  1.00 22.83 ? 215 PRO B CG  1 
ATOM   5896 C CD  . PRO B 1 215 ? 52.065  -7.696  70.951  1.00 16.58 ? 215 PRO B CD  1 
ATOM   5897 N N   . ASN B 1 216 ? 52.520  -7.033  74.744  1.00 20.30 ? 216 ASN B N   1 
ATOM   5898 C CA  . ASN B 1 216 ? 52.697  -6.410  76.051  1.00 23.58 ? 216 ASN B CA  1 
ATOM   5899 C C   . ASN B 1 216 ? 51.763  -6.984  77.107  1.00 27.12 ? 216 ASN B C   1 
ATOM   5900 O O   . ASN B 1 216 ? 51.846  -6.585  78.273  1.00 24.74 ? 216 ASN B O   1 
ATOM   5901 C CB  . ASN B 1 216 ? 52.496  -4.897  75.940  1.00 32.65 ? 216 ASN B CB  1 
ATOM   5902 C CG  . ASN B 1 216 ? 53.555  -4.234  75.073  1.00 36.43 ? 216 ASN B CG  1 
ATOM   5903 O OD1 . ASN B 1 216 ? 54.717  -4.658  75.048  1.00 39.53 ? 216 ASN B OD1 1 
ATOM   5904 N ND2 . ASN B 1 216 ? 53.152  -3.204  74.341  1.00 37.43 ? 216 ASN B ND2 1 
ATOM   5905 N N   . VAL B 1 217 ? 50.902  -7.929  76.734  1.00 22.17 ? 217 VAL B N   1 
ATOM   5906 C CA  . VAL B 1 217 ? 49.922  -8.465  77.667  1.00 16.09 ? 217 VAL B CA  1 
ATOM   5907 C C   . VAL B 1 217 ? 50.642  -9.216  78.779  1.00 17.15 ? 217 VAL B C   1 
ATOM   5908 O O   . VAL B 1 217 ? 51.681  -9.854  78.557  1.00 19.13 ? 217 VAL B O   1 
ATOM   5909 C CB  . VAL B 1 217 ? 48.917  -9.359  76.909  1.00 17.80 ? 217 VAL B CB  1 
ATOM   5910 C CG1 . VAL B 1 217 ? 49.540  -10.656 76.475  1.00 20.12 ? 217 VAL B CG1 1 
ATOM   5911 C CG2 . VAL B 1 217 ? 47.665  -9.619  77.719  1.00 20.31 ? 217 VAL B CG2 1 
ATOM   5912 N N   . LYS B 1 218 ? 50.114  -9.113  79.993  1.00 17.63 ? 218 LYS B N   1 
ATOM   5913 C CA  . LYS B 1 218 ? 50.585  -9.903  81.121  1.00 12.39 ? 218 LYS B CA  1 
ATOM   5914 C C   . LYS B 1 218 ? 49.662  -11.095 81.286  1.00 10.08 ? 218 LYS B C   1 
ATOM   5915 O O   . LYS B 1 218 ? 48.442  -10.931 81.288  1.00 12.72 ? 218 LYS B O   1 
ATOM   5916 C CB  . LYS B 1 218 ? 50.602  -9.076  82.406  1.00 17.74 ? 218 LYS B CB  1 
ATOM   5917 C CG  . LYS B 1 218 ? 51.410  -7.799  82.296  1.00 25.53 ? 218 LYS B CG  1 
ATOM   5918 C CD  . LYS B 1 218 ? 51.394  -7.021  83.606  1.00 38.57 ? 218 LYS B CD  1 
ATOM   5919 C CE  . LYS B 1 218 ? 51.752  -5.559  83.383  1.00 47.98 ? 218 LYS B CE  1 
ATOM   5920 N NZ  . LYS B 1 218 ? 51.670  -4.771  84.648  1.00 52.79 ? 218 LYS B NZ  1 
ATOM   5921 N N   . ILE B 1 219 ? 50.233  -12.289 81.410  1.00 11.97 ? 219 ILE B N   1 
ATOM   5922 C CA  . ILE B 1 219 ? 49.426  -13.471 81.705  1.00 12.70 ? 219 ILE B CA  1 
ATOM   5923 C C   . ILE B 1 219 ? 50.012  -14.145 82.946  1.00 11.58 ? 219 ILE B C   1 
ATOM   5924 O O   . ILE B 1 219 ? 51.181  -13.926 83.290  1.00 12.22 ? 219 ILE B O   1 
ATOM   5925 C CB  . ILE B 1 219 ? 49.374  -14.449 80.508  1.00 14.51 ? 219 ILE B CB  1 
ATOM   5926 C CG1 . ILE B 1 219 ? 50.735  -15.118 80.294  1.00 17.67 ? 219 ILE B CG1 1 
ATOM   5927 C CG2 . ILE B 1 219 ? 48.891  -13.716 79.237  1.00 14.13 ? 219 ILE B CG2 1 
ATOM   5928 C CD1 . ILE B 1 219 ? 50.751  -16.200 79.200  1.00 18.39 ? 219 ILE B CD1 1 
ATOM   5929 N N   . PRO B 1 220 ? 49.209  -14.972 83.639  1.00 16.14 ? 220 PRO B N   1 
ATOM   5930 C CA  . PRO B 1 220 ? 49.746  -15.684 84.810  1.00 14.93 ? 220 PRO B CA  1 
ATOM   5931 C C   . PRO B 1 220 ? 50.768  -16.757 84.451  1.00 10.28 ? 220 PRO B C   1 
ATOM   5932 O O   . PRO B 1 220 ? 51.017  -17.039 83.276  1.00 11.31 ? 220 PRO B O   1 
ATOM   5933 C CB  . PRO B 1 220 ? 48.504  -16.307 85.464  1.00 17.61 ? 220 PRO B CB  1 
ATOM   5934 C CG  . PRO B 1 220 ? 47.417  -16.187 84.476  1.00 16.68 ? 220 PRO B CG  1 
ATOM   5935 C CD  . PRO B 1 220 ? 47.744  -15.083 83.530  1.00 21.80 ? 220 PRO B CD  1 
ATOM   5936 N N   . ASP B 1 221 ? 51.353  -17.363 85.485  1.00 10.15 ? 221 ASP B N   1 
ATOM   5937 C CA  . ASP B 1 221 ? 52.325  -18.451 85.350  1.00 11.42 ? 221 ASP B CA  1 
ATOM   5938 C C   . ASP B 1 221 ? 51.575  -19.746 85.062  1.00 11.11 ? 221 ASP B C   1 
ATOM   5939 O O   . ASP B 1 221 ? 50.991  -20.338 85.967  1.00 11.92 ? 221 ASP B O   1 
ATOM   5940 C CB  . ASP B 1 221 ? 53.144  -18.572 86.634  1.00 10.12 ? 221 ASP B CB  1 
ATOM   5941 C CG  . ASP B 1 221 ? 54.298  -19.544 86.504  1.00 15.99 ? 221 ASP B CG  1 
ATOM   5942 O OD1 . ASP B 1 221 ? 54.877  -19.615 85.413  1.00 16.05 ? 221 ASP B OD1 1 
ATOM   5943 O OD2 . ASP B 1 221 ? 54.626  -20.230 87.493  1.00 19.65 ? 221 ASP B OD2 1 
ATOM   5944 N N   . PHE B 1 222 ? 51.589  -20.210 83.802  1.00 8.73  ? 222 PHE B N   1 
ATOM   5945 C CA  . PHE B 1 222 ? 50.891  -21.452 83.448  1.00 13.97 ? 222 PHE B CA  1 
ATOM   5946 C C   . PHE B 1 222 ? 51.754  -22.642 83.870  1.00 14.35 ? 222 PHE B C   1 
ATOM   5947 O O   . PHE B 1 222 ? 52.428  -23.296 83.068  1.00 13.91 ? 222 PHE B O   1 
ATOM   5948 C CB  . PHE B 1 222 ? 50.541  -21.479 81.960  1.00 10.04 ? 222 PHE B CB  1 
ATOM   5949 C CG  . PHE B 1 222 ? 49.289  -20.695 81.637  1.00 13.80 ? 222 PHE B CG  1 
ATOM   5950 C CD1 . PHE B 1 222 ? 49.325  -19.317 81.580  1.00 11.32 ? 222 PHE B CD1 1 
ATOM   5951 C CD2 . PHE B 1 222 ? 48.079  -21.341 81.442  1.00 11.02 ? 222 PHE B CD2 1 
ATOM   5952 C CE1 . PHE B 1 222 ? 48.194  -18.588 81.296  1.00 9.80  ? 222 PHE B CE1 1 
ATOM   5953 C CE2 . PHE B 1 222 ? 46.925  -20.620 81.151  1.00 13.13 ? 222 PHE B CE2 1 
ATOM   5954 C CZ  . PHE B 1 222 ? 46.979  -19.249 81.083  1.00 9.29  ? 222 PHE B CZ  1 
ATOM   5955 N N   . ALA B 1 223 ? 51.719  -22.932 85.174  1.00 13.99 ? 223 ALA B N   1 
ATOM   5956 C CA  . ALA B 1 223 ? 52.578  -23.958 85.755  1.00 17.96 ? 223 ALA B CA  1 
ATOM   5957 C C   . ALA B 1 223 ? 52.044  -25.369 85.564  1.00 17.65 ? 223 ALA B C   1 
ATOM   5958 O O   . ALA B 1 223 ? 52.642  -26.312 86.089  1.00 22.82 ? 223 ALA B O   1 
ATOM   5959 C CB  . ALA B 1 223 ? 52.786  -23.681 87.248  1.00 15.11 ? 223 ALA B CB  1 
ATOM   5960 N N   . VAL B 1 224 ? 50.926  -25.533 84.858  1.00 9.81  ? 224 VAL B N   1 
ATOM   5961 C CA  . VAL B 1 224 ? 50.356  -26.840 84.539  1.00 14.66 ? 224 VAL B CA  1 
ATOM   5962 C C   . VAL B 1 224 ? 50.090  -26.872 83.043  1.00 12.74 ? 224 VAL B C   1 
ATOM   5963 O O   . VAL B 1 224 ? 49.849  -25.834 82.420  1.00 13.92 ? 224 VAL B O   1 
ATOM   5964 C CB  . VAL B 1 224 ? 49.041  -27.101 85.311  1.00 16.12 ? 224 VAL B CB  1 
ATOM   5965 C CG1 . VAL B 1 224 ? 48.745  -28.601 85.413  1.00 20.64 ? 224 VAL B CG1 1 
ATOM   5966 C CG2 . VAL B 1 224 ? 49.094  -26.461 86.669  1.00 32.32 ? 224 VAL B CG2 1 
ATOM   5967 N N   . SER B 1 225 ? 50.091  -28.074 82.474  1.00 10.70 ? 225 SER B N   1 
ATOM   5968 C CA  . SER B 1 225 ? 49.766  -28.254 81.066  1.00 14.39 ? 225 SER B CA  1 
ATOM   5969 C C   . SER B 1 225 ? 48.265  -28.487 80.904  1.00 13.33 ? 225 SER B C   1 
ATOM   5970 O O   . SER B 1 225 ? 47.693  -29.323 81.602  1.00 9.64  ? 225 SER B O   1 
ATOM   5971 C CB  . SER B 1 225 ? 50.528  -29.443 80.482  1.00 14.15 ? 225 SER B CB  1 
ATOM   5972 O OG  . SER B 1 225 ? 50.130  -29.659 79.141  1.00 15.06 ? 225 SER B OG  1 
ATOM   5973 N N   . PHE B 1 226 ? 47.645  -27.757 79.968  1.00 10.87 ? 226 PHE B N   1 
ATOM   5974 C CA  . PHE B 1 226 ? 46.261  -27.968 79.545  1.00 11.45 ? 226 PHE B CA  1 
ATOM   5975 C C   . PHE B 1 226 ? 46.153  -28.666 78.199  1.00 10.81 ? 226 PHE B C   1 
ATOM   5976 O O   . PHE B 1 226 ? 45.074  -28.664 77.596  1.00 10.04 ? 226 PHE B O   1 
ATOM   5977 C CB  . PHE B 1 226 ? 45.517  -26.627 79.466  1.00 6.80  ? 226 PHE B CB  1 
ATOM   5978 C CG  . PHE B 1 226 ? 45.215  -26.022 80.817  1.00 10.88 ? 226 PHE B CG  1 
ATOM   5979 C CD1 . PHE B 1 226 ? 44.172  -26.504 81.595  1.00 5.88  ? 226 PHE B CD1 1 
ATOM   5980 C CD2 . PHE B 1 226 ? 45.982  -24.983 81.309  1.00 11.77 ? 226 PHE B CD2 1 
ATOM   5981 C CE1 . PHE B 1 226 ? 43.902  -25.960 82.845  1.00 10.69 ? 226 PHE B CE1 1 
ATOM   5982 C CE2 . PHE B 1 226 ? 45.711  -24.427 82.560  1.00 15.38 ? 226 PHE B CE2 1 
ATOM   5983 C CZ  . PHE B 1 226 ? 44.671  -24.916 83.322  1.00 15.06 ? 226 PHE B CZ  1 
ATOM   5984 N N   . ARG B 1 227 ? 47.248  -29.236 77.686  1.00 12.52 ? 227 ARG B N   1 
ATOM   5985 C CA  . ARG B 1 227 ? 47.210  -29.763 76.326  1.00 6.80  ? 227 ARG B CA  1 
ATOM   5986 C C   . ARG B 1 227 ? 46.336  -31.013 76.233  1.00 12.61 ? 227 ARG B C   1 
ATOM   5987 O O   . ARG B 1 227 ? 45.598  -31.184 75.260  1.00 10.40 ? 227 ARG B O   1 
ATOM   5988 C CB  . ARG B 1 227 ? 48.631  -30.062 75.821  1.00 12.15 ? 227 ARG B CB  1 
ATOM   5989 C CG  . ARG B 1 227 ? 49.563  -28.865 75.788  1.00 20.24 ? 227 ARG B CG  1 
ATOM   5990 C CD  . ARG B 1 227 ? 50.965  -29.244 75.291  1.00 15.15 ? 227 ARG B CD  1 
ATOM   5991 N NE  . ARG B 1 227 ? 50.953  -29.938 74.006  1.00 14.90 ? 227 ARG B NE  1 
ATOM   5992 C CZ  . ARG B 1 227 ? 50.896  -29.328 72.823  1.00 23.79 ? 227 ARG B CZ  1 
ATOM   5993 N NH1 . ARG B 1 227 ? 50.828  -28.003 72.753  1.00 14.69 ? 227 ARG B NH1 1 
ATOM   5994 N NH2 . ARG B 1 227 ? 50.896  -30.038 71.705  1.00 27.40 ? 227 ARG B NH2 1 
ATOM   5995 N N   . GLU B 1 228 ? 46.403  -31.907 77.226  1.00 12.73 ? 228 GLU B N   1 
ATOM   5996 C CA  . GLU B 1 228 ? 45.536  -33.079 77.143  1.00 11.48 ? 228 GLU B CA  1 
ATOM   5997 C C   . GLU B 1 228 ? 44.067  -32.700 77.308  1.00 11.37 ? 228 GLU B C   1 
ATOM   5998 O O   . GLU B 1 228 ? 43.194  -33.336 76.706  1.00 10.13 ? 228 GLU B O   1 
ATOM   5999 C CB  . GLU B 1 228 ? 45.933  -34.134 78.178  1.00 16.11 ? 228 GLU B CB  1 
ATOM   6000 C CG  . GLU B 1 228 ? 44.915  -35.269 78.259  1.00 30.30 ? 228 GLU B CG  1 
ATOM   6001 C CD  . GLU B 1 228 ? 45.472  -36.569 78.801  1.00 49.99 ? 228 GLU B CD  1 
ATOM   6002 O OE1 . GLU B 1 228 ? 46.296  -36.525 79.741  1.00 52.93 ? 228 GLU B OE1 1 
ATOM   6003 O OE2 . GLU B 1 228 ? 45.070  -37.638 78.284  1.00 54.90 ? 228 GLU B OE2 1 
ATOM   6004 N N   . ASP B 1 229 ? 43.775  -31.683 78.122  1.00 8.00  ? 229 ASP B N   1 
ATOM   6005 C CA  . ASP B 1 229 ? 42.400  -31.194 78.236  1.00 7.47  ? 229 ASP B CA  1 
ATOM   6006 C C   . ASP B 1 229 ? 41.884  -30.655 76.905  1.00 11.98 ? 229 ASP B C   1 
ATOM   6007 O O   . ASP B 1 229 ? 40.725  -30.885 76.545  1.00 14.54 ? 229 ASP B O   1 
ATOM   6008 C CB  . ASP B 1 229 ? 42.303  -30.124 79.312  1.00 8.65  ? 229 ASP B CB  1 
ATOM   6009 C CG  . ASP B 1 229 ? 42.231  -30.708 80.705  1.00 12.09 ? 229 ASP B CG  1 
ATOM   6010 O OD1 . ASP B 1 229 ? 42.201  -31.942 80.832  1.00 13.93 ? 229 ASP B OD1 1 
ATOM   6011 O OD2 . ASP B 1 229 ? 42.182  -29.933 81.679  1.00 12.02 ? 229 ASP B OD2 1 
ATOM   6012 N N   . ALA B 1 230 ? 42.720  -29.926 76.165  1.00 7.40  ? 230 ALA B N   1 
ATOM   6013 C CA  . ALA B 1 230 ? 42.330  -29.487 74.830  1.00 4.25  ? 230 ALA B CA  1 
ATOM   6014 C C   . ALA B 1 230 ? 41.889  -30.662 73.957  1.00 9.64  ? 230 ALA B C   1 
ATOM   6015 O O   . ALA B 1 230 ? 40.833  -30.614 73.314  1.00 12.58 ? 230 ALA B O   1 
ATOM   6016 C CB  . ALA B 1 230 ? 43.486  -28.746 74.169  1.00 4.23  ? 230 ALA B CB  1 
ATOM   6017 N N   . SER B 1 231 ? 42.690  -31.733 73.935  1.00 11.04 ? 231 SER B N   1 
ATOM   6018 C CA  . SER B 1 231 ? 42.313  -32.946 73.210  1.00 9.40  ? 231 SER B CA  1 
ATOM   6019 C C   . SER B 1 231 ? 40.977  -33.499 73.695  1.00 9.63  ? 231 SER B C   1 
ATOM   6020 O O   . SER B 1 231 ? 40.138  -33.929 72.886  1.00 10.90 ? 231 SER B O   1 
ATOM   6021 C CB  . SER B 1 231 ? 43.389  -34.024 73.392  1.00 16.49 ? 231 SER B CB  1 
ATOM   6022 O OG  . SER B 1 231 ? 44.332  -34.018 72.345  1.00 32.49 ? 231 SER B OG  1 
ATOM   6023 N N   . LYS B 1 232 ? 40.784  -33.535 75.017  1.00 9.89  ? 232 LYS B N   1 
ATOM   6024 C CA  . LYS B 1 232 ? 39.582  -34.133 75.589  1.00 10.37 ? 232 LYS B CA  1 
ATOM   6025 C C   . LYS B 1 232 ? 38.342  -33.358 75.197  1.00 13.39 ? 232 LYS B C   1 
ATOM   6026 O O   . LYS B 1 232 ? 37.333  -33.957 74.835  1.00 7.67  ? 232 LYS B O   1 
ATOM   6027 C CB  . LYS B 1 232 ? 39.688  -34.212 77.113  1.00 18.29 ? 232 LYS B CB  1 
ATOM   6028 C CG  . LYS B 1 232 ? 40.145  -35.541 77.638  1.00 33.49 ? 232 LYS B CG  1 
ATOM   6029 C CD  . LYS B 1 232 ? 40.219  -35.508 79.157  1.00 37.06 ? 232 LYS B CD  1 
ATOM   6030 C CE  . LYS B 1 232 ? 38.839  -35.622 79.783  1.00 38.95 ? 232 LYS B CE  1 
ATOM   6031 N NZ  . LYS B 1 232 ? 38.220  -36.970 79.602  1.00 45.49 ? 232 LYS B NZ  1 
ATOM   6032 N N   . HIS B 1 233 ? 38.400  -32.021 75.230  1.00 10.29 ? 233 HIS B N   1 
ATOM   6033 C CA  . HIS B 1 233 ? 37.266  -31.243 74.742  1.00 9.46  ? 233 HIS B CA  1 
ATOM   6034 C C   . HIS B 1 233 ? 36.850  -31.690 73.347  1.00 10.72 ? 233 HIS B C   1 
ATOM   6035 O O   . HIS B 1 233 ? 35.661  -31.872 73.071  1.00 8.75  ? 233 HIS B O   1 
ATOM   6036 C CB  . HIS B 1 233 ? 37.600  -29.753 74.720  1.00 9.61  ? 233 HIS B CB  1 
ATOM   6037 C CG  . HIS B 1 233 ? 37.598  -29.108 76.069  1.00 6.51  ? 233 HIS B CG  1 
ATOM   6038 N ND1 . HIS B 1 233 ? 36.456  -28.599 76.648  1.00 10.37 ? 233 HIS B ND1 1 
ATOM   6039 C CD2 . HIS B 1 233 ? 38.608  -28.838 76.926  1.00 7.31  ? 233 HIS B CD2 1 
ATOM   6040 C CE1 . HIS B 1 233 ? 36.762  -28.072 77.822  1.00 8.91  ? 233 HIS B CE1 1 
ATOM   6041 N NE2 . HIS B 1 233 ? 38.063  -28.190 78.005  1.00 6.59  ? 233 HIS B NE2 1 
ATOM   6042 N N   . VAL B 1 234 ? 37.817  -31.841 72.443  1.00 9.57  ? 234 VAL B N   1 
ATOM   6043 C CA  . VAL B 1 234 ? 37.492  -32.203 71.067  1.00 8.39  ? 234 VAL B CA  1 
ATOM   6044 C C   . VAL B 1 234 ? 36.934  -33.622 71.007  1.00 12.93 ? 234 VAL B C   1 
ATOM   6045 O O   . VAL B 1 234 ? 35.900  -33.879 70.369  1.00 11.18 ? 234 VAL B O   1 
ATOM   6046 C CB  . VAL B 1 234 ? 38.726  -32.040 70.164  1.00 10.75 ? 234 VAL B CB  1 
ATOM   6047 C CG1 . VAL B 1 234 ? 38.385  -32.501 68.748  1.00 12.64 ? 234 VAL B CG1 1 
ATOM   6048 C CG2 . VAL B 1 234 ? 39.184  -30.566 70.157  1.00 11.06 ? 234 VAL B CG2 1 
ATOM   6049 N N   . GLU B 1 235 ? 37.604  -34.562 71.683  1.00 6.85  ? 235 GLU B N   1 
ATOM   6050 C CA  . GLU B 1 235 ? 37.185  -35.965 71.635  1.00 15.29 ? 235 GLU B CA  1 
ATOM   6051 C C   . GLU B 1 235 ? 35.785  -36.157 72.220  1.00 14.55 ? 235 GLU B C   1 
ATOM   6052 O O   . GLU B 1 235 ? 34.946  -36.866 71.640  1.00 12.37 ? 235 GLU B O   1 
ATOM   6053 C CB  . GLU B 1 235 ? 38.217  -36.822 72.379  1.00 22.68 ? 235 GLU B CB  1 
ATOM   6054 C CG  . GLU B 1 235 ? 38.106  -38.325 72.146  1.00 33.80 ? 235 GLU B CG  1 
ATOM   6055 C CD  . GLU B 1 235 ? 37.850  -38.675 70.691  1.00 39.99 ? 235 GLU B CD  1 
ATOM   6056 O OE1 . GLU B 1 235 ? 38.707  -38.360 69.833  1.00 32.91 ? 235 GLU B OE1 1 
ATOM   6057 O OE2 . GLU B 1 235 ? 36.781  -39.257 70.408  1.00 48.73 ? 235 GLU B OE2 1 
ATOM   6058 N N   . LEU B 1 236 ? 35.528  -35.572 73.396  1.00 8.58  ? 236 LEU B N   1 
ATOM   6059 C CA  . LEU B 1 236 ? 34.203  -35.704 74.004  1.00 8.52  ? 236 LEU B CA  1 
ATOM   6060 C C   . LEU B 1 236 ? 33.136  -35.063 73.133  1.00 8.64  ? 236 LEU B C   1 
ATOM   6061 O O   . LEU B 1 236 ? 32.002  -35.554 73.067  1.00 10.22 ? 236 LEU B O   1 
ATOM   6062 C CB  . LEU B 1 236 ? 34.193  -35.079 75.397  1.00 9.80  ? 236 LEU B CB  1 
ATOM   6063 C CG  . LEU B 1 236 ? 35.048  -35.807 76.444  1.00 14.35 ? 236 LEU B CG  1 
ATOM   6064 C CD1 . LEU B 1 236 ? 35.277  -34.923 77.657  1.00 18.95 ? 236 LEU B CD1 1 
ATOM   6065 C CD2 . LEU B 1 236 ? 34.400  -37.120 76.856  1.00 16.09 ? 236 LEU B CD2 1 
ATOM   6066 N N   . ALA B 1 237 ? 33.473  -33.957 72.463  1.00 7.46  ? 237 ALA B N   1 
ATOM   6067 C CA  . ALA B 1 237 ? 32.506  -33.350 71.554  1.00 10.64 ? 237 ALA B CA  1 
ATOM   6068 C C   . ALA B 1 237 ? 32.165  -34.297 70.407  1.00 14.07 ? 237 ALA B C   1 
ATOM   6069 O O   . ALA B 1 237 ? 30.990  -34.441 70.038  1.00 10.18 ? 237 ALA B O   1 
ATOM   6070 C CB  . ALA B 1 237 ? 33.042  -32.016 71.023  1.00 10.56 ? 237 ALA B CB  1 
ATOM   6071 N N   . LYS B 1 238 ? 33.178  -34.956 69.829  1.00 10.82 ? 238 LYS B N   1 
ATOM   6072 C CA  . LYS B 1 238 ? 32.902  -35.950 68.793  1.00 11.56 ? 238 LYS B CA  1 
ATOM   6073 C C   . LYS B 1 238 ? 31.972  -37.051 69.307  1.00 13.45 ? 238 LYS B C   1 
ATOM   6074 O O   . LYS B 1 238 ? 31.086  -37.524 68.579  1.00 13.33 ? 238 LYS B O   1 
ATOM   6075 C CB  . LYS B 1 238 ? 34.214  -36.549 68.279  1.00 12.24 ? 238 LYS B CB  1 
ATOM   6076 C CG  . LYS B 1 238 ? 35.083  -35.572 67.482  1.00 16.42 ? 238 LYS B CG  1 
ATOM   6077 C CD  . LYS B 1 238 ? 36.406  -36.209 67.111  1.00 19.31 ? 238 LYS B CD  1 
ATOM   6078 C CE  . LYS B 1 238 ? 36.220  -37.306 66.086  1.00 29.44 ? 238 LYS B CE  1 
ATOM   6079 N NZ  . LYS B 1 238 ? 37.504  -38.041 65.904  1.00 23.79 ? 238 LYS B NZ  1 
ATOM   6080 N N   . GLU B 1 239 ? 32.130  -37.443 70.571  1.00 11.72 ? 239 GLU B N   1 
ATOM   6081 C CA  . GLU B 1 239 ? 31.279  -38.488 71.131  1.00 13.69 ? 239 GLU B CA  1 
ATOM   6082 C C   . GLU B 1 239 ? 29.856  -37.994 71.336  1.00 15.67 ? 239 GLU B C   1 
ATOM   6083 O O   . GLU B 1 239 ? 28.900  -38.717 71.036  1.00 16.31 ? 239 GLU B O   1 
ATOM   6084 C CB  . GLU B 1 239 ? 31.870  -38.998 72.444  1.00 19.70 ? 239 GLU B CB  1 
ATOM   6085 C CG  . GLU B 1 239 ? 33.067  -39.887 72.226  1.00 35.52 ? 239 GLU B CG  1 
ATOM   6086 C CD  . GLU B 1 239 ? 32.791  -40.954 71.171  1.00 55.85 ? 239 GLU B CD  1 
ATOM   6087 O OE1 . GLU B 1 239 ? 31.962  -41.857 71.431  1.00 60.23 ? 239 GLU B OE1 1 
ATOM   6088 O OE2 . GLU B 1 239 ? 33.397  -40.889 70.080  1.00 59.91 ? 239 GLU B OE2 1 
ATOM   6089 N N   . LYS B 1 240 ? 29.687  -36.759 71.829  1.00 11.57 ? 240 LYS B N   1 
ATOM   6090 C CA  . LYS B 1 240 ? 28.332  -36.272 72.072  1.00 8.45  ? 240 LYS B CA  1 
ATOM   6091 C C   . LYS B 1 240 ? 27.570  -36.108 70.763  1.00 12.51 ? 240 LYS B C   1 
ATOM   6092 O O   . LYS B 1 240 ? 26.394  -36.487 70.667  1.00 12.89 ? 240 LYS B O   1 
ATOM   6093 C CB  . LYS B 1 240 ? 28.363  -34.955 72.850  1.00 8.22  ? 240 LYS B CB  1 
ATOM   6094 C CG  . LYS B 1 240 ? 26.957  -34.403 73.209  1.00 7.15  ? 240 LYS B CG  1 
ATOM   6095 C CD  . LYS B 1 240 ? 26.337  -35.154 74.404  1.00 7.74  ? 240 LYS B CD  1 
ATOM   6096 C CE  . LYS B 1 240 ? 24.815  -34.995 74.450  1.00 15.32 ? 240 LYS B CE  1 
ATOM   6097 N NZ  . LYS B 1 240 ? 24.236  -35.565 75.703  1.00 18.70 ? 240 LYS B NZ  1 
ATOM   6098 N N   . TYR B 1 241 ? 28.231  -35.555 69.743  1.00 8.49  ? 241 TYR B N   1 
ATOM   6099 C CA  . TYR B 1 241 ? 27.619  -35.410 68.427  1.00 12.14 ? 241 TYR B CA  1 
ATOM   6100 C C   . TYR B 1 241 ? 27.214  -36.766 67.868  1.00 14.96 ? 241 TYR B C   1 
ATOM   6101 O O   . TYR B 1 241 ? 26.141  -36.914 67.268  1.00 14.00 ? 241 TYR B O   1 
ATOM   6102 C CB  . TYR B 1 241 ? 28.614  -34.720 67.493  1.00 13.35 ? 241 TYR B CB  1 
ATOM   6103 C CG  . TYR B 1 241 ? 28.098  -34.385 66.124  1.00 12.27 ? 241 TYR B CG  1 
ATOM   6104 C CD1 . TYR B 1 241 ? 28.089  -35.341 65.109  1.00 12.85 ? 241 TYR B CD1 1 
ATOM   6105 C CD2 . TYR B 1 241 ? 27.651  -33.102 65.829  1.00 11.02 ? 241 TYR B CD2 1 
ATOM   6106 C CE1 . TYR B 1 241 ? 27.642  -35.033 63.844  1.00 11.89 ? 241 TYR B CE1 1 
ATOM   6107 C CE2 . TYR B 1 241 ? 27.192  -32.782 64.553  1.00 12.49 ? 241 TYR B CE2 1 
ATOM   6108 C CZ  . TYR B 1 241 ? 27.197  -33.753 63.572  1.00 8.64  ? 241 TYR B CZ  1 
ATOM   6109 O OH  . TYR B 1 241 ? 26.751  -33.473 62.317  1.00 11.71 ? 241 TYR B OH  1 
ATOM   6110 N N   . PHE B 1 242 ? 28.080  -37.760 68.048  1.00 15.08 ? 242 PHE B N   1 
ATOM   6111 C CA  . PHE B 1 242 ? 27.808  -39.107 67.565  1.00 17.72 ? 242 PHE B CA  1 
ATOM   6112 C C   . PHE B 1 242 ? 26.566  -39.687 68.242  1.00 18.58 ? 242 PHE B C   1 
ATOM   6113 O O   . PHE B 1 242 ? 25.730  -40.319 67.585  1.00 17.52 ? 242 PHE B O   1 
ATOM   6114 C CB  . PHE B 1 242 ? 29.069  -39.942 67.805  1.00 19.77 ? 242 PHE B CB  1 
ATOM   6115 C CG  . PHE B 1 242 ? 28.923  -41.407 67.526  1.00 22.75 ? 242 PHE B CG  1 
ATOM   6116 C CD1 . PHE B 1 242 ? 28.944  -41.886 66.233  1.00 26.48 ? 242 PHE B CD1 1 
ATOM   6117 C CD2 . PHE B 1 242 ? 28.818  -42.310 68.573  1.00 25.85 ? 242 PHE B CD2 1 
ATOM   6118 C CE1 . PHE B 1 242 ? 28.826  -43.255 65.983  1.00 29.09 ? 242 PHE B CE1 1 
ATOM   6119 C CE2 . PHE B 1 242 ? 28.704  -43.671 68.332  1.00 36.24 ? 242 PHE B CE2 1 
ATOM   6120 C CZ  . PHE B 1 242 ? 28.716  -44.141 67.034  1.00 28.37 ? 242 PHE B CZ  1 
ATOM   6121 N N   . GLU B 1 243 ? 26.404  -39.417 69.543  1.00 18.90 ? 243 GLU B N   1 
ATOM   6122 C CA  . GLU B 1 243 ? 25.210  -39.814 70.294  1.00 24.09 ? 243 GLU B CA  1 
ATOM   6123 C C   . GLU B 1 243 ? 23.935  -39.226 69.698  1.00 25.78 ? 243 GLU B C   1 
ATOM   6124 O O   . GLU B 1 243 ? 22.919  -39.922 69.578  1.00 27.25 ? 243 GLU B O   1 
ATOM   6125 C CB  . GLU B 1 243 ? 25.357  -39.371 71.757  1.00 28.80 ? 243 GLU B CB  1 
ATOM   6126 C CG  . GLU B 1 243 ? 24.235  -39.795 72.703  1.00 42.13 ? 243 GLU B CG  1 
ATOM   6127 C CD  . GLU B 1 243 ? 24.046  -38.828 73.877  1.00 46.33 ? 243 GLU B CD  1 
ATOM   6128 O OE1 . GLU B 1 243 ? 25.051  -38.440 74.511  1.00 45.05 ? 243 GLU B OE1 1 
ATOM   6129 O OE2 . GLU B 1 243 ? 22.886  -38.469 74.178  1.00 48.82 ? 243 GLU B OE2 1 
ATOM   6130 N N   . ILE B 1 244 ? 23.959  -37.942 69.332  1.00 11.79 ? 244 ILE B N   1 
ATOM   6131 C CA  . ILE B 1 244 ? 22.751  -37.282 68.842  1.00 12.24 ? 244 ILE B CA  1 
ATOM   6132 C C   . ILE B 1 244 ? 22.448  -37.666 67.399  1.00 17.53 ? 244 ILE B C   1 
ATOM   6133 O O   . ILE B 1 244 ? 21.297  -37.973 67.058  1.00 19.23 ? 244 ILE B O   1 
ATOM   6134 C CB  . ILE B 1 244 ? 22.874  -35.753 68.986  1.00 11.35 ? 244 ILE B CB  1 
ATOM   6135 C CG1 . ILE B 1 244 ? 23.172  -35.382 70.438  1.00 14.20 ? 244 ILE B CG1 1 
ATOM   6136 C CG2 . ILE B 1 244 ? 21.602  -35.064 68.478  1.00 15.09 ? 244 ILE B CG2 1 
ATOM   6137 C CD1 . ILE B 1 244 ? 22.193  -35.999 71.445  1.00 16.18 ? 244 ILE B CD1 1 
ATOM   6138 N N   . PHE B 1 245 ? 23.461  -37.633 66.522  1.00 16.14 ? 245 PHE B N   1 
ATOM   6139 C CA  . PHE B 1 245 ? 23.244  -37.718 65.081  1.00 18.24 ? 245 PHE B CA  1 
ATOM   6140 C C   . PHE B 1 245 ? 23.685  -39.039 64.460  1.00 15.21 ? 245 PHE B C   1 
ATOM   6141 O O   . PHE B 1 245 ? 23.391  -39.270 63.282  1.00 19.13 ? 245 PHE B O   1 
ATOM   6142 C CB  . PHE B 1 245 ? 23.952  -36.555 64.357  1.00 15.22 ? 245 PHE B CB  1 
ATOM   6143 C CG  . PHE B 1 245 ? 23.441  -35.195 64.767  1.00 17.61 ? 245 PHE B CG  1 
ATOM   6144 C CD1 . PHE B 1 245 ? 22.213  -34.738 64.304  1.00 16.55 ? 245 PHE B CD1 1 
ATOM   6145 C CD2 . PHE B 1 245 ? 24.180  -34.382 65.620  1.00 15.93 ? 245 PHE B CD2 1 
ATOM   6146 C CE1 . PHE B 1 245 ? 21.723  -33.494 64.682  1.00 21.85 ? 245 PHE B CE1 1 
ATOM   6147 C CE2 . PHE B 1 245 ? 23.697  -33.144 66.005  1.00 16.76 ? 245 PHE B CE2 1 
ATOM   6148 C CZ  . PHE B 1 245 ? 22.463  -32.698 65.539  1.00 15.48 ? 245 PHE B CZ  1 
ATOM   6149 N N   . GLY B 1 246 ? 24.356  -39.912 65.208  1.00 16.29 ? 246 GLY B N   1 
ATOM   6150 C CA  . GLY B 1 246 ? 24.673  -41.238 64.704  1.00 18.58 ? 246 GLY B CA  1 
ATOM   6151 C C   . GLY B 1 246 ? 25.974  -41.343 63.935  1.00 23.72 ? 246 GLY B C   1 
ATOM   6152 O O   . GLY B 1 246 ? 26.359  -42.453 63.544  1.00 17.80 ? 246 GLY B O   1 
ATOM   6153 N N   . GLU B 1 247 ? 26.661  -40.232 63.697  1.00 26.57 ? 247 GLU B N   1 
ATOM   6154 C CA  . GLU B 1 247 ? 27.953  -40.260 63.027  1.00 25.19 ? 247 GLU B CA  1 
ATOM   6155 C C   . GLU B 1 247 ? 28.885  -39.290 63.734  1.00 26.20 ? 247 GLU B C   1 
ATOM   6156 O O   . GLU B 1 247 ? 28.446  -38.442 64.511  1.00 18.30 ? 247 GLU B O   1 
ATOM   6157 C CB  . GLU B 1 247 ? 27.832  -39.898 61.540  1.00 26.89 ? 247 GLU B CB  1 
ATOM   6158 C CG  . GLU B 1 247 ? 26.936  -38.706 61.269  1.00 41.90 ? 247 GLU B CG  1 
ATOM   6159 C CD  . GLU B 1 247 ? 26.997  -38.262 59.823  1.00 54.48 ? 247 GLU B CD  1 
ATOM   6160 O OE1 . GLU B 1 247 ? 27.146  -39.136 58.943  1.00 60.03 ? 247 GLU B OE1 1 
ATOM   6161 O OE2 . GLU B 1 247 ? 26.908  -37.043 59.568  1.00 54.52 ? 247 GLU B OE2 1 
ATOM   6162 N N   . HIS B 1 248 ? 30.180  -39.439 63.479  1.00 16.75 ? 248 HIS B N   1 
ATOM   6163 C CA  . HIS B 1 248 ? 31.123  -38.467 64.010  1.00 18.28 ? 248 HIS B CA  1 
ATOM   6164 C C   . HIS B 1 248 ? 31.090  -37.178 63.190  1.00 17.37 ? 248 HIS B C   1 
ATOM   6165 O O   . HIS B 1 248 ? 30.852  -37.208 61.979  1.00 17.72 ? 248 HIS B O   1 
ATOM   6166 C CB  . HIS B 1 248 ? 32.530  -39.060 64.022  1.00 23.20 ? 248 HIS B CB  1 
ATOM   6167 C CG  . HIS B 1 248 ? 32.692  -40.152 65.030  1.00 35.99 ? 248 HIS B CG  1 
ATOM   6168 N ND1 . HIS B 1 248 ? 32.693  -41.489 64.687  1.00 41.11 ? 248 HIS B ND1 1 
ATOM   6169 C CD2 . HIS B 1 248 ? 32.795  -40.109 66.380  1.00 39.01 ? 248 HIS B CD2 1 
ATOM   6170 C CE1 . HIS B 1 248 ? 32.813  -42.220 65.782  1.00 38.76 ? 248 HIS B CE1 1 
ATOM   6171 N NE2 . HIS B 1 248 ? 32.882  -41.408 66.822  1.00 40.26 ? 248 HIS B NE2 1 
ATOM   6172 N N   . PRO B 1 249 ? 31.297  -36.024 63.835  1.00 9.78  ? 249 PRO B N   1 
ATOM   6173 C CA  . PRO B 1 249 ? 31.293  -34.761 63.088  1.00 11.33 ? 249 PRO B CA  1 
ATOM   6174 C C   . PRO B 1 249 ? 32.556  -34.619 62.267  1.00 17.13 ? 249 PRO B C   1 
ATOM   6175 O O   . PRO B 1 249 ? 33.640  -34.998 62.706  1.00 18.85 ? 249 PRO B O   1 
ATOM   6176 C CB  . PRO B 1 249 ? 31.238  -33.696 64.190  1.00 5.08  ? 249 PRO B CB  1 
ATOM   6177 C CG  . PRO B 1 249 ? 31.937  -34.318 65.350  1.00 12.68 ? 249 PRO B CG  1 
ATOM   6178 C CD  . PRO B 1 249 ? 31.690  -35.837 65.245  1.00 10.07 ? 249 PRO B CD  1 
ATOM   6179 N N   . VAL B 1 250 ? 32.407  -34.069 61.064  1.00 13.95 ? 250 VAL B N   1 
ATOM   6180 C CA  . VAL B 1 250 ? 33.554  -33.742 60.226  1.00 18.40 ? 250 VAL B CA  1 
ATOM   6181 C C   . VAL B 1 250 ? 33.782  -32.247 60.116  1.00 11.83 ? 250 VAL B C   1 
ATOM   6182 O O   . VAL B 1 250 ? 34.821  -31.839 59.577  1.00 12.99 ? 250 VAL B O   1 
ATOM   6183 C CB  . VAL B 1 250 ? 33.434  -34.364 58.817  1.00 26.26 ? 250 VAL B CB  1 
ATOM   6184 C CG1 . VAL B 1 250 ? 33.378  -35.889 58.907  1.00 24.80 ? 250 VAL B CG1 1 
ATOM   6185 C CG2 . VAL B 1 250 ? 32.212  -33.827 58.104  1.00 19.81 ? 250 VAL B CG2 1 
ATOM   6186 N N   . TYR B 1 251 ? 32.845  -31.421 60.588  1.00 13.42 ? 251 TYR B N   1 
ATOM   6187 C CA  . TYR B 1 251 ? 33.000  -29.973 60.655  1.00 13.71 ? 251 TYR B CA  1 
ATOM   6188 C C   . TYR B 1 251 ? 32.955  -29.522 62.106  1.00 12.51 ? 251 TYR B C   1 
ATOM   6189 O O   . TYR B 1 251 ? 32.174  -30.047 62.902  1.00 9.65  ? 251 TYR B O   1 
ATOM   6190 C CB  . TYR B 1 251 ? 31.899  -29.263 59.867  1.00 20.22 ? 251 TYR B CB  1 
ATOM   6191 C CG  . TYR B 1 251 ? 31.640  -29.932 58.550  1.00 19.57 ? 251 TYR B CG  1 
ATOM   6192 C CD1 . TYR B 1 251 ? 32.643  -30.011 57.603  1.00 18.41 ? 251 TYR B CD1 1 
ATOM   6193 C CD2 . TYR B 1 251 ? 30.407  -30.511 58.259  1.00 24.87 ? 251 TYR B CD2 1 
ATOM   6194 C CE1 . TYR B 1 251 ? 32.433  -30.628 56.390  1.00 25.42 ? 251 TYR B CE1 1 
ATOM   6195 C CE2 . TYR B 1 251 ? 30.188  -31.146 57.034  1.00 21.15 ? 251 TYR B CE2 1 
ATOM   6196 C CZ  . TYR B 1 251 ? 31.211  -31.192 56.108  1.00 27.58 ? 251 TYR B CZ  1 
ATOM   6197 O OH  . TYR B 1 251 ? 31.042  -31.816 54.890  1.00 29.98 ? 251 TYR B OH  1 
ATOM   6198 N N   . MET B 1 252 ? 33.792  -28.544 62.453  1.00 12.18 ? 252 MET B N   1 
ATOM   6199 C CA  . MET B 1 252 ? 33.716  -27.937 63.773  1.00 10.95 ? 252 MET B CA  1 
ATOM   6200 C C   . MET B 1 252 ? 33.807  -26.425 63.668  1.00 9.90  ? 252 MET B C   1 
ATOM   6201 O O   . MET B 1 252 ? 34.508  -25.881 62.812  1.00 8.74  ? 252 MET B O   1 
ATOM   6202 C CB  . MET B 1 252 ? 34.813  -28.445 64.696  1.00 12.05 ? 252 MET B CB  1 
ATOM   6203 C CG  . MET B 1 252 ? 34.570  -29.854 65.212  1.00 16.22 ? 252 MET B CG  1 
ATOM   6204 S SD  . MET B 1 252 ? 35.403  -30.136 66.792  1.00 17.43 ? 252 MET B SD  1 
ATOM   6205 C CE  . MET B 1 252 ? 34.750  -31.756 67.217  1.00 15.39 ? 252 MET B CE  1 
ATOM   6206 N N   . TRP B 1 253 ? 33.088  -25.749 64.557  1.00 7.40  ? 253 TRP B N   1 
ATOM   6207 C CA  . TRP B 1 253 ? 33.269  -24.321 64.742  1.00 4.17  ? 253 TRP B CA  1 
ATOM   6208 C C   . TRP B 1 253 ? 34.216  -24.091 65.905  1.00 7.79  ? 253 TRP B C   1 
ATOM   6209 O O   . TRP B 1 253 ? 33.890  -24.493 67.033  1.00 8.43  ? 253 TRP B O   1 
ATOM   6210 C CB  . TRP B 1 253 ? 31.933  -23.637 65.008  1.00 4.53  ? 253 TRP B CB  1 
ATOM   6211 C CG  . TRP B 1 253 ? 32.118  -22.199 65.453  1.00 7.06  ? 253 TRP B CG  1 
ATOM   6212 C CD1 . TRP B 1 253 ? 31.830  -21.680 66.696  1.00 5.13  ? 253 TRP B CD1 1 
ATOM   6213 C CD2 . TRP B 1 253 ? 32.654  -21.111 64.677  1.00 6.98  ? 253 TRP B CD2 1 
ATOM   6214 N NE1 . TRP B 1 253 ? 32.157  -20.351 66.733  1.00 8.93  ? 253 TRP B NE1 1 
ATOM   6215 C CE2 . TRP B 1 253 ? 32.658  -19.972 65.510  1.00 12.23 ? 253 TRP B CE2 1 
ATOM   6216 C CE3 . TRP B 1 253 ? 33.131  -20.989 63.360  1.00 6.97  ? 253 TRP B CE3 1 
ATOM   6217 C CZ2 . TRP B 1 253 ? 33.113  -18.729 65.074  1.00 7.40  ? 253 TRP B CZ2 1 
ATOM   6218 C CZ3 . TRP B 1 253 ? 33.600  -19.748 62.928  1.00 8.19  ? 253 TRP B CZ3 1 
ATOM   6219 C CH2 . TRP B 1 253 ? 33.591  -18.638 63.776  1.00 6.27  ? 253 TRP B CH2 1 
ATOM   6220 N N   . PRO B 1 254 ? 35.388  -23.489 65.702  1.00 9.09  ? 254 PRO B N   1 
ATOM   6221 C CA  . PRO B 1 254 ? 36.280  -23.235 66.830  1.00 5.11  ? 254 PRO B CA  1 
ATOM   6222 C C   . PRO B 1 254 ? 35.726  -22.114 67.686  1.00 6.45  ? 254 PRO B C   1 
ATOM   6223 O O   . PRO B 1 254 ? 35.385  -21.042 67.167  1.00 6.72  ? 254 PRO B O   1 
ATOM   6224 C CB  . PRO B 1 254 ? 37.606  -22.824 66.161  1.00 7.21  ? 254 PRO B CB  1 
ATOM   6225 C CG  . PRO B 1 254 ? 37.217  -22.249 64.854  1.00 12.14 ? 254 PRO B CG  1 
ATOM   6226 C CD  . PRO B 1 254 ? 35.927  -22.971 64.432  1.00 6.28  ? 254 PRO B CD  1 
ATOM   6227 N N   . PRO B 1 255 ? 35.620  -22.319 68.997  1.00 7.74  ? 255 PRO B N   1 
ATOM   6228 C CA  . PRO B 1 255 ? 35.033  -21.282 69.849  1.00 5.53  ? 255 PRO B CA  1 
ATOM   6229 C C   . PRO B 1 255 ? 35.701  -19.926 69.649  1.00 8.68  ? 255 PRO B C   1 
ATOM   6230 O O   . PRO B 1 255 ? 36.932  -19.816 69.651  1.00 8.08  ? 255 PRO B O   1 
ATOM   6231 C CB  . PRO B 1 255 ? 35.265  -21.823 71.261  1.00 4.93  ? 255 PRO B CB  1 
ATOM   6232 C CG  . PRO B 1 255 ? 35.172  -23.331 71.079  1.00 8.33  ? 255 PRO B CG  1 
ATOM   6233 C CD  . PRO B 1 255 ? 35.779  -23.603 69.704  1.00 8.04  ? 255 PRO B CD  1 
ATOM   6234 N N   . GLU B 1 256 ? 34.878  -18.920 69.486  1.00 6.11  ? 256 GLU B N   1 
ATOM   6235 C CA  . GLU B 1 256 ? 35.298  -17.550 69.251  1.00 8.34  ? 256 GLU B CA  1 
ATOM   6236 C C   . GLU B 1 256 ? 36.184  -17.404 67.959  1.00 8.16  ? 256 GLU B C   1 
ATOM   6237 O O   . GLU B 1 256 ? 36.999  -16.530 67.861  1.00 9.29  ? 256 GLU B O   1 
ATOM   6238 C CB  . GLU B 1 256 ? 36.005  -16.988 70.456  1.00 9.00  ? 256 GLU B CB  1 
ATOM   6239 C CG  . GLU B 1 256 ? 35.228  -17.037 71.768  1.00 12.41 ? 256 GLU B CG  1 
ATOM   6240 C CD  . GLU B 1 256 ? 33.907  -16.269 71.777  1.00 14.62 ? 256 GLU B CD  1 
ATOM   6241 O OE1 . GLU B 1 256 ? 33.742  -15.359 71.045  1.00 14.98 ? 256 GLU B OE1 1 
ATOM   6242 O OE2 . GLU B 1 256 ? 33.058  -16.597 72.566  1.00 15.04 ? 256 GLU B OE2 1 
ATOM   6243 N N   . ALA B 1 257 ? 35.917  -18.255 67.004  1.00 5.00  ? 257 ALA B N   1 
ATOM   6244 C CA  . ALA B 1 257 ? 36.701  -18.349 65.776  1.00 12.28 ? 257 ALA B CA  1 
ATOM   6245 C C   . ALA B 1 257 ? 38.191  -18.555 66.057  1.00 12.13 ? 257 ALA B C   1 
ATOM   6246 O O   . ALA B 1 257 ? 39.036  -18.249 65.211  1.00 9.53  ? 257 ALA B O   1 
ATOM   6247 C CB  . ALA B 1 257 ? 36.508  -17.111 64.893  1.00 7.76  ? 257 ALA B CB  1 
ATOM   6248 N N   . SER B 1 258 ? 38.538  -19.052 67.241  1.00 11.53 ? 258 SER B N   1 
ATOM   6249 C CA  . SER B 1 258 ? 39.925  -18.998 67.696  1.00 9.62  ? 258 SER B CA  1 
ATOM   6250 C C   . SER B 1 258 ? 40.720  -20.133 67.072  1.00 5.09  ? 258 SER B C   1 
ATOM   6251 O O   . SER B 1 258 ? 40.330  -21.299 67.173  1.00 9.42  ? 258 SER B O   1 
ATOM   6252 C CB  . SER B 1 258 ? 40.013  -19.076 69.219  1.00 13.89 ? 258 SER B CB  1 
ATOM   6253 O OG  . SER B 1 258 ? 41.357  -18.820 69.614  1.00 17.91 ? 258 SER B OG  1 
ATOM   6254 N N   . VAL B 1 259 ? 41.815  -19.786 66.390  1.00 8.42  ? 259 VAL B N   1 
ATOM   6255 C CA  . VAL B 1 259 ? 42.719  -20.762 65.800  1.00 5.99  ? 259 VAL B CA  1 
ATOM   6256 C C   . VAL B 1 259 ? 44.166  -20.378 66.096  1.00 9.34  ? 259 VAL B C   1 
ATOM   6257 O O   . VAL B 1 259 ? 44.478  -19.260 66.504  1.00 5.85  ? 259 VAL B O   1 
ATOM   6258 C CB  . VAL B 1 259 ? 42.528  -20.902 64.264  1.00 11.90 ? 259 VAL B CB  1 
ATOM   6259 C CG1 . VAL B 1 259 ? 41.123  -21.420 63.922  1.00 13.71 ? 259 VAL B CG1 1 
ATOM   6260 C CG2 . VAL B 1 259 ? 42.796  -19.573 63.571  1.00 11.43 ? 259 VAL B CG2 1 
ATOM   6261 N N   . SER B 1 260 ? 45.046  -21.343 65.873  1.00 8.28  ? 260 SER B N   1 
ATOM   6262 C CA  . SER B 1 260 ? 46.492  -21.199 65.949  1.00 7.55  ? 260 SER B CA  1 
ATOM   6263 C C   . SER B 1 260 ? 47.051  -22.353 65.143  1.00 7.17  ? 260 SER B C   1 
ATOM   6264 O O   . SER B 1 260 ? 46.324  -23.292 64.820  1.00 8.72  ? 260 SER B O   1 
ATOM   6265 C CB  . SER B 1 260 ? 46.992  -21.232 67.400  1.00 7.77  ? 260 SER B CB  1 
ATOM   6266 O OG  . SER B 1 260 ? 46.699  -22.486 68.012  1.00 9.80  ? 260 SER B OG  1 
ATOM   6267 N N   . ASN B 1 261 ? 48.357  -22.296 64.834  1.00 6.91  ? 261 ASN B N   1 
ATOM   6268 C CA  . ASN B 1 261 ? 48.968  -23.436 64.165  1.00 13.39 ? 261 ASN B CA  1 
ATOM   6269 C C   . ASN B 1 261 ? 48.738  -24.710 64.956  1.00 12.64 ? 261 ASN B C   1 
ATOM   6270 O O   . ASN B 1 261 ? 48.398  -25.753 64.385  1.00 10.96 ? 261 ASN B O   1 
ATOM   6271 C CB  . ASN B 1 261 ? 50.470  -23.204 63.958  1.00 14.86 ? 261 ASN B CB  1 
ATOM   6272 C CG  . ASN B 1 261 ? 50.735  -22.138 62.934  1.00 16.55 ? 261 ASN B CG  1 
ATOM   6273 O OD1 . ASN B 1 261 ? 49.908  -21.912 62.049  1.00 13.49 ? 261 ASN B OD1 1 
ATOM   6274 N ND2 . ASN B 1 261 ? 51.883  -21.466 63.043  1.00 11.06 ? 261 ASN B ND2 1 
ATOM   6275 N N   . GLU B 1 262 ? 48.897  -24.645 66.279  1.00 11.74 ? 262 GLU B N   1 
ATOM   6276 C CA  . GLU B 1 262 ? 48.766  -25.874 67.056  1.00 11.04 ? 262 GLU B CA  1 
ATOM   6277 C C   . GLU B 1 262 ? 47.323  -26.323 67.147  1.00 12.32 ? 262 GLU B C   1 
ATOM   6278 O O   . GLU B 1 262 ? 47.055  -27.529 67.195  1.00 10.22 ? 262 GLU B O   1 
ATOM   6279 C CB  . GLU B 1 262 ? 49.353  -25.699 68.456  1.00 8.36  ? 262 GLU B CB  1 
ATOM   6280 C CG  . GLU B 1 262 ? 50.868  -25.519 68.426  1.00 13.94 ? 262 GLU B CG  1 
ATOM   6281 C CD  . GLU B 1 262 ? 51.496  -25.476 69.801  1.00 23.92 ? 262 GLU B CD  1 
ATOM   6282 O OE1 . GLU B 1 262 ? 52.639  -24.975 69.925  1.00 25.96 ? 262 GLU B OE1 1 
ATOM   6283 O OE2 . GLU B 1 262 ? 50.852  -25.937 70.761  1.00 20.20 ? 262 GLU B OE2 1 
ATOM   6284 N N   . ALA B 1 263 ? 46.387  -25.379 67.199  1.00 8.50  ? 263 ALA B N   1 
ATOM   6285 C CA  . ALA B 1 263 ? 44.977  -25.756 67.237  1.00 7.53  ? 263 ALA B CA  1 
ATOM   6286 C C   . ALA B 1 263 ? 44.562  -26.426 65.937  1.00 10.62 ? 263 ALA B C   1 
ATOM   6287 O O   . ALA B 1 263 ? 43.850  -27.433 65.943  1.00 8.48  ? 263 ALA B O   1 
ATOM   6288 C CB  . ALA B 1 263 ? 44.107  -24.522 67.505  1.00 6.19  ? 263 ALA B CB  1 
ATOM   6289 N N   . LEU B 1 264 ? 44.958  -25.856 64.804  1.00 11.06 ? 264 LEU B N   1 
ATOM   6290 C CA  . LEU B 1 264 ? 44.574  -26.458 63.529  1.00 10.15 ? 264 LEU B CA  1 
ATOM   6291 C C   . LEU B 1 264 ? 45.145  -27.863 63.396  1.00 11.21 ? 264 LEU B C   1 
ATOM   6292 O O   . LEU B 1 264 ? 44.482  -28.763 62.860  1.00 11.63 ? 264 LEU B O   1 
ATOM   6293 C CB  . LEU B 1 264 ? 45.031  -25.578 62.368  1.00 11.60 ? 264 LEU B CB  1 
ATOM   6294 C CG  . LEU B 1 264 ? 44.302  -24.238 62.267  1.00 12.22 ? 264 LEU B CG  1 
ATOM   6295 C CD1 . LEU B 1 264 ? 45.034  -23.310 61.346  1.00 13.19 ? 264 LEU B CD1 1 
ATOM   6296 C CD2 . LEU B 1 264 ? 42.867  -24.456 61.791  1.00 17.19 ? 264 LEU B CD2 1 
ATOM   6297 N N   . GLU B 1 265 ? 46.358  -28.083 63.915  1.00 13.27 ? 265 GLU B N   1 
ATOM   6298 C CA  . GLU B 1 265 ? 46.912  -29.435 63.926  1.00 13.40 ? 265 GLU B CA  1 
ATOM   6299 C C   . GLU B 1 265 ? 46.077  -30.371 64.792  1.00 15.70 ? 265 GLU B C   1 
ATOM   6300 O O   . GLU B 1 265 ? 45.843  -31.515 64.413  1.00 10.08 ? 265 GLU B O   1 
ATOM   6301 C CB  . GLU B 1 265 ? 48.358  -29.418 64.414  1.00 15.33 ? 265 GLU B CB  1 
ATOM   6302 C CG  . GLU B 1 265 ? 49.295  -28.699 63.476  1.00 17.78 ? 265 GLU B CG  1 
ATOM   6303 C CD  . GLU B 1 265 ? 49.845  -29.603 62.396  1.00 36.34 ? 265 GLU B CD  1 
ATOM   6304 O OE1 . GLU B 1 265 ? 50.581  -29.095 61.515  1.00 36.63 ? 265 GLU B OE1 1 
ATOM   6305 O OE2 . GLU B 1 265 ? 49.536  -30.818 62.426  1.00 39.19 ? 265 GLU B OE2 1 
ATOM   6306 N N   . LEU B 1 266 ? 45.638  -29.924 65.970  1.00 12.43 ? 266 LEU B N   1 
ATOM   6307 C CA  . LEU B 1 266 ? 44.830  -30.816 66.802  1.00 8.52  ? 266 LEU B CA  1 
ATOM   6308 C C   . LEU B 1 266 ? 43.511  -31.172 66.115  1.00 6.57  ? 266 LEU B C   1 
ATOM   6309 O O   . LEU B 1 266 ? 43.100  -32.338 66.112  1.00 10.79 ? 266 LEU B O   1 
ATOM   6310 C CB  . LEU B 1 266 ? 44.580  -30.180 68.176  1.00 9.11  ? 266 LEU B CB  1 
ATOM   6311 C CG  . LEU B 1 266 ? 43.569  -30.901 69.069  1.00 12.70 ? 266 LEU B CG  1 
ATOM   6312 C CD1 . LEU B 1 266 ? 44.126  -32.242 69.495  1.00 9.64  ? 266 LEU B CD1 1 
ATOM   6313 C CD2 . LEU B 1 266 ? 43.190  -30.062 70.295  1.00 11.30 ? 266 LEU B CD2 1 
ATOM   6314 N N   . TYR B 1 267 ? 42.843  -30.187 65.498  1.00 8.96  ? 267 TYR B N   1 
ATOM   6315 C CA  . TYR B 1 267 ? 41.588  -30.475 64.804  1.00 12.52 ? 267 TYR B CA  1 
ATOM   6316 C C   . TYR B 1 267 ? 41.811  -31.495 63.695  1.00 19.32 ? 267 TYR B C   1 
ATOM   6317 O O   . TYR B 1 267 ? 41.022  -32.437 63.531  1.00 9.69  ? 267 TYR B O   1 
ATOM   6318 C CB  . TYR B 1 267 ? 40.993  -29.188 64.238  1.00 12.06 ? 267 TYR B CB  1 
ATOM   6319 C CG  . TYR B 1 267 ? 40.339  -28.298 65.285  1.00 9.88  ? 267 TYR B CG  1 
ATOM   6320 C CD1 . TYR B 1 267 ? 39.207  -28.723 65.974  1.00 9.91  ? 267 TYR B CD1 1 
ATOM   6321 C CD2 . TYR B 1 267 ? 40.834  -27.028 65.559  1.00 13.28 ? 267 TYR B CD2 1 
ATOM   6322 C CE1 . TYR B 1 267 ? 38.592  -27.919 66.923  1.00 12.83 ? 267 TYR B CE1 1 
ATOM   6323 C CE2 . TYR B 1 267 ? 40.224  -26.209 66.513  1.00 12.60 ? 267 TYR B CE2 1 
ATOM   6324 C CZ  . TYR B 1 267 ? 39.100  -26.658 67.179  1.00 12.47 ? 267 TYR B CZ  1 
ATOM   6325 O OH  . TYR B 1 267 ? 38.497  -25.856 68.120  1.00 10.48 ? 267 TYR B OH  1 
ATOM   6326 N N   . TYR B 1 268 ? 42.917  -31.338 62.963  1.00 14.01 ? 268 TYR B N   1 
ATOM   6327 C CA  . TYR B 1 268 ? 43.300  -32.287 61.927  1.00 10.70 ? 268 TYR B CA  1 
ATOM   6328 C C   . TYR B 1 268 ? 43.523  -33.677 62.508  1.00 8.07  ? 268 TYR B C   1 
ATOM   6329 O O   . TYR B 1 268 ? 43.017  -34.671 61.977  1.00 10.63 ? 268 TYR B O   1 
ATOM   6330 C CB  . TYR B 1 268 ? 44.576  -31.804 61.236  1.00 11.49 ? 268 TYR B CB  1 
ATOM   6331 C CG  . TYR B 1 268 ? 45.259  -32.920 60.483  1.00 12.07 ? 268 TYR B CG  1 
ATOM   6332 C CD1 . TYR B 1 268 ? 44.698  -33.431 59.319  1.00 16.56 ? 268 TYR B CD1 1 
ATOM   6333 C CD2 . TYR B 1 268 ? 46.431  -33.493 60.955  1.00 15.02 ? 268 TYR B CD2 1 
ATOM   6334 C CE1 . TYR B 1 268 ? 45.307  -34.474 58.622  1.00 19.56 ? 268 TYR B CE1 1 
ATOM   6335 C CE2 . TYR B 1 268 ? 47.043  -34.530 60.266  1.00 14.88 ? 268 TYR B CE2 1 
ATOM   6336 C CZ  . TYR B 1 268 ? 46.477  -35.012 59.107  1.00 23.83 ? 268 TYR B CZ  1 
ATOM   6337 O OH  . TYR B 1 268 ? 47.094  -36.044 58.440  1.00 32.94 ? 268 TYR B OH  1 
ATOM   6338 N N   . GLU B 1 269 ? 44.299  -33.765 63.598  1.00 11.01 ? 269 GLU B N   1 
ATOM   6339 C CA  . GLU B 1 269 ? 44.601  -35.059 64.203  1.00 13.87 ? 269 GLU B CA  1 
ATOM   6340 C C   . GLU B 1 269 ? 43.347  -35.748 64.724  1.00 17.52 ? 269 GLU B C   1 
ATOM   6341 O O   . GLU B 1 269 ? 43.295  -36.982 64.771  1.00 16.32 ? 269 GLU B O   1 
ATOM   6342 C CB  . GLU B 1 269 ? 45.623  -34.896 65.330  1.00 16.24 ? 269 GLU B CB  1 
ATOM   6343 C CG  . GLU B 1 269 ? 47.057  -34.711 64.827  1.00 27.75 ? 269 GLU B CG  1 
ATOM   6344 C CD  . GLU B 1 269 ? 47.954  -33.970 65.803  1.00 42.00 ? 269 GLU B CD  1 
ATOM   6345 O OE1 . GLU B 1 269 ? 47.601  -33.870 67.000  1.00 46.42 ? 269 GLU B OE1 1 
ATOM   6346 O OE2 . GLU B 1 269 ? 49.026  -33.495 65.370  1.00 47.21 ? 269 GLU B OE2 1 
ATOM   6347 N N   . LYS B 1 270 ? 42.329  -34.984 65.109  1.00 17.37 ? 270 LYS B N   1 
ATOM   6348 C CA  . LYS B 1 270 ? 41.066  -35.560 65.570  1.00 9.94  ? 270 LYS B CA  1 
ATOM   6349 C C   . LYS B 1 270 ? 40.063  -35.772 64.445  1.00 10.32 ? 270 LYS B C   1 
ATOM   6350 O O   . LYS B 1 270 ? 38.887  -36.037 64.724  1.00 15.84 ? 270 LYS B O   1 
ATOM   6351 C CB  . LYS B 1 270 ? 40.447  -34.675 66.654  1.00 10.08 ? 270 LYS B CB  1 
ATOM   6352 C CG  . LYS B 1 270 ? 41.354  -34.472 67.872  1.00 11.88 ? 270 LYS B CG  1 
ATOM   6353 C CD  . LYS B 1 270 ? 41.441  -35.753 68.706  1.00 23.77 ? 270 LYS B CD  1 
ATOM   6354 C CE  . LYS B 1 270 ? 42.628  -35.743 69.657  1.00 31.69 ? 270 LYS B CE  1 
ATOM   6355 N NZ  . LYS B 1 270 ? 43.155  -37.119 69.918  1.00 39.61 ? 270 LYS B NZ  1 
ATOM   6356 N N   . GLY B 1 271 ? 40.489  -35.668 63.187  1.00 12.56 ? 271 GLY B N   1 
ATOM   6357 C CA  . GLY B 1 271 ? 39.630  -36.039 62.077  1.00 15.63 ? 271 GLY B CA  1 
ATOM   6358 C C   . GLY B 1 271 ? 38.659  -34.982 61.609  1.00 15.16 ? 271 GLY B C   1 
ATOM   6359 O O   . GLY B 1 271 ? 37.697  -35.314 60.906  1.00 14.92 ? 271 GLY B O   1 
ATOM   6360 N N   . ILE B 1 272 ? 38.865  -33.722 61.972  1.00 12.89 ? 272 ILE B N   1 
ATOM   6361 C CA  . ILE B 1 272 ? 37.999  -32.661 61.476  1.00 8.17  ? 272 ILE B CA  1 
ATOM   6362 C C   . ILE B 1 272 ? 38.493  -32.281 60.088  1.00 15.70 ? 272 ILE B C   1 
ATOM   6363 O O   . ILE B 1 272 ? 39.699  -32.102 59.880  1.00 14.09 ? 272 ILE B O   1 
ATOM   6364 C CB  . ILE B 1 272 ? 38.004  -31.462 62.441  1.00 11.39 ? 272 ILE B CB  1 
ATOM   6365 C CG1 . ILE B 1 272 ? 37.557  -31.921 63.838  1.00 14.85 ? 272 ILE B CG1 1 
ATOM   6366 C CG2 . ILE B 1 272 ? 37.102  -30.320 61.931  1.00 11.81 ? 272 ILE B CG2 1 
ATOM   6367 C CD1 . ILE B 1 272 ? 36.253  -32.723 63.828  1.00 17.80 ? 272 ILE B CD1 1 
ATOM   6368 N N   . ASN B 1 273 ? 37.573  -32.207 59.120  1.00 10.05 ? 273 ASN B N   1 
ATOM   6369 C CA  . ASN B 1 273 ? 37.977  -31.927 57.747  1.00 16.18 ? 273 ASN B CA  1 
ATOM   6370 C C   . ASN B 1 273 ? 37.891  -30.454 57.376  1.00 13.13 ? 273 ASN B C   1 
ATOM   6371 O O   . ASN B 1 273 ? 38.614  -30.007 56.479  1.00 14.64 ? 273 ASN B O   1 
ATOM   6372 C CB  . ASN B 1 273 ? 37.120  -32.738 56.774  1.00 30.23 ? 273 ASN B CB  1 
ATOM   6373 C CG  . ASN B 1 273 ? 37.546  -34.181 56.705  1.00 37.23 ? 273 ASN B CG  1 
ATOM   6374 O OD1 . ASN B 1 273 ? 38.689  -34.518 57.025  1.00 45.43 ? 273 ASN B OD1 1 
ATOM   6375 N ND2 . ASN B 1 273 ? 36.635  -35.046 56.288  1.00 39.09 ? 273 ASN B ND2 1 
ATOM   6376 N N   . MET B 1 274 ? 36.993  -29.697 58.003  1.00 11.39 ? 274 MET B N   1 
ATOM   6377 C CA  . MET B 1 274 ? 36.866  -28.280 57.688  1.00 8.50  ? 274 MET B CA  1 
ATOM   6378 C C   . MET B 1 274 ? 36.428  -27.516 58.928  1.00 14.79 ? 274 MET B C   1 
ATOM   6379 O O   . MET B 1 274 ? 35.641  -28.017 59.737  1.00 12.22 ? 274 MET B O   1 
ATOM   6380 C CB  . MET B 1 274 ? 35.860  -28.041 56.554  1.00 12.75 ? 274 MET B CB  1 
ATOM   6381 C CG  . MET B 1 274 ? 35.772  -26.589 56.096  1.00 16.32 ? 274 MET B CG  1 
ATOM   6382 S SD  . MET B 1 274 ? 34.476  -25.662 56.966  1.00 30.42 ? 274 MET B SD  1 
ATOM   6383 C CE  . MET B 1 274 ? 33.032  -26.167 55.999  1.00 28.39 ? 274 MET B CE  1 
ATOM   6384 N N   . LEU B 1 275 ? 36.942  -26.298 59.062  1.00 9.03  ? 275 LEU B N   1 
ATOM   6385 C CA  . LEU B 1 275 ? 36.438  -25.337 60.028  1.00 15.97 ? 275 LEU B CA  1 
ATOM   6386 C C   . LEU B 1 275 ? 36.413  -23.964 59.369  1.00 15.51 ? 275 LEU B C   1 
ATOM   6387 O O   . LEU B 1 275 ? 36.827  -23.793 58.224  1.00 14.37 ? 275 LEU B O   1 
ATOM   6388 C CB  . LEU B 1 275 ? 37.287  -25.313 61.307  1.00 15.08 ? 275 LEU B CB  1 
ATOM   6389 C CG  . LEU B 1 275 ? 38.806  -25.275 61.147  1.00 20.26 ? 275 LEU B CG  1 
ATOM   6390 C CD1 . LEU B 1 275 ? 39.298  -23.867 60.915  1.00 26.71 ? 275 LEU B CD1 1 
ATOM   6391 C CD2 . LEU B 1 275 ? 39.517  -25.893 62.360  1.00 19.95 ? 275 LEU B CD2 1 
ATOM   6392 N N   . ALA B 1 276 ? 35.898  -22.984 60.099  1.00 9.51  ? 276 ALA B N   1 
ATOM   6393 C CA  . ALA B 1 276 ? 35.968  -21.598 59.678  1.00 15.83 ? 276 ALA B CA  1 
ATOM   6394 C C   . ALA B 1 276 ? 36.530  -20.756 60.813  1.00 11.15 ? 276 ALA B C   1 
ATOM   6395 O O   . ALA B 1 276 ? 36.497  -21.149 61.981  1.00 11.88 ? 276 ALA B O   1 
ATOM   6396 C CB  . ALA B 1 276 ? 34.595  -21.061 59.256  1.00 9.44  ? 276 ALA B CB  1 
ATOM   6397 N N   . THR B 1 277 ? 37.048  -19.587 60.453  1.00 9.52  ? 277 THR B N   1 
ATOM   6398 C CA  . THR B 1 277 ? 37.507  -18.604 61.420  1.00 9.51  ? 277 THR B CA  1 
ATOM   6399 C C   . THR B 1 277 ? 37.233  -17.224 60.815  1.00 10.89 ? 277 THR B C   1 
ATOM   6400 O O   . THR B 1 277 ? 36.387  -17.089 59.926  1.00 16.33 ? 277 THR B O   1 
ATOM   6401 C CB  . THR B 1 277 ? 38.977  -18.888 61.820  1.00 13.47 ? 277 THR B CB  1 
ATOM   6402 O OG1 . THR B 1 277 ? 39.419  -17.910 62.764  1.00 13.73 ? 277 THR B OG1 1 
ATOM   6403 C CG2 . THR B 1 277 ? 39.928  -18.876 60.604  1.00 12.49 ? 277 THR B CG2 1 
ATOM   6404 N N   . ASP B 1 278 ? 37.923  -16.195 61.302  1.00 8.36  ? 278 ASP B N   1 
ATOM   6405 C CA  . ASP B 1 278 ? 37.580  -14.806 61.004  1.00 10.65 ? 278 ASP B CA  1 
ATOM   6406 C C   . ASP B 1 278 ? 38.557  -14.191 60.010  1.00 13.89 ? 278 ASP B C   1 
ATOM   6407 O O   . ASP B 1 278 ? 39.740  -14.524 59.991  1.00 10.46 ? 278 ASP B O   1 
ATOM   6408 C CB  . ASP B 1 278 ? 37.580  -13.964 62.278  1.00 12.37 ? 278 ASP B CB  1 
ATOM   6409 C CG  . ASP B 1 278 ? 37.055  -12.568 62.054  1.00 11.98 ? 278 ASP B CG  1 
ATOM   6410 O OD1 . ASP B 1 278 ? 35.941  -12.443 61.516  1.00 14.49 ? 278 ASP B OD1 1 
ATOM   6411 O OD2 . ASP B 1 278 ? 37.758  -11.598 62.413  1.00 16.65 ? 278 ASP B OD2 1 
ATOM   6412 N N   . GLU B 1 279 ? 38.073  -13.238 59.215  1.00 15.59 ? 279 GLU B N   1 
ATOM   6413 C CA  . GLU B 1 279 ? 38.985  -12.703 58.212  1.00 18.35 ? 279 GLU B CA  1 
ATOM   6414 C C   . GLU B 1 279 ? 40.036  -11.754 58.788  1.00 13.61 ? 279 GLU B C   1 
ATOM   6415 O O   . GLU B 1 279 ? 41.033  -11.504 58.111  1.00 18.66 ? 279 GLU B O   1 
ATOM   6416 C CB  . GLU B 1 279 ? 38.211  -12.044 57.069  1.00 24.43 ? 279 GLU B CB  1 
ATOM   6417 C CG  . GLU B 1 279 ? 37.727  -10.674 57.290  1.00 25.79 ? 279 GLU B CG  1 
ATOM   6418 C CD  . GLU B 1 279 ? 37.125  -10.090 56.019  1.00 31.36 ? 279 GLU B CD  1 
ATOM   6419 O OE1 . GLU B 1 279 ? 37.865  -9.879  55.029  1.00 33.21 ? 279 GLU B OE1 1 
ATOM   6420 O OE2 . GLU B 1 279 ? 35.900  -9.863  56.004  1.00 21.12 ? 279 GLU B OE2 1 
ATOM   6421 N N   . VAL B 1 280 ? 39.891  -11.277 60.030  1.00 12.65 ? 280 VAL B N   1 
ATOM   6422 C CA  . VAL B 1 280 ? 41.016  -10.589 60.669  1.00 14.32 ? 280 VAL B CA  1 
ATOM   6423 C C   . VAL B 1 280 ? 42.206  -11.534 60.799  1.00 14.17 ? 280 VAL B C   1 
ATOM   6424 O O   . VAL B 1 280 ? 43.363  -11.133 60.603  1.00 14.24 ? 280 VAL B O   1 
ATOM   6425 C CB  . VAL B 1 280 ? 40.605  -10.001 62.032  1.00 19.00 ? 280 VAL B CB  1 
ATOM   6426 C CG1 . VAL B 1 280 ? 41.841  -9.475  62.796  1.00 18.45 ? 280 VAL B CG1 1 
ATOM   6427 C CG2 . VAL B 1 280 ? 39.587  -8.882  61.848  1.00 19.27 ? 280 VAL B CG2 1 
ATOM   6428 N N   . ILE B 1 281 ? 41.943  -12.809 61.118  1.00 11.18 ? 281 ILE B N   1 
ATOM   6429 C CA  . ILE B 1 281 ? 43.017  -13.792 61.226  1.00 11.82 ? 281 ILE B CA  1 
ATOM   6430 C C   . ILE B 1 281 ? 43.713  -13.954 59.883  1.00 10.91 ? 281 ILE B C   1 
ATOM   6431 O O   . ILE B 1 281 ? 44.947  -14.030 59.807  1.00 13.07 ? 281 ILE B O   1 
ATOM   6432 C CB  . ILE B 1 281 ? 42.472  -15.143 61.732  1.00 15.34 ? 281 ILE B CB  1 
ATOM   6433 C CG1 . ILE B 1 281 ? 41.816  -15.027 63.118  1.00 22.39 ? 281 ILE B CG1 1 
ATOM   6434 C CG2 . ILE B 1 281 ? 43.565  -16.225 61.711  1.00 18.16 ? 281 ILE B CG2 1 
ATOM   6435 C CD1 . ILE B 1 281 ? 42.522  -14.140 64.073  1.00 24.85 ? 281 ILE B CD1 1 
ATOM   6436 N N   . LEU B 1 282 ? 42.933  -14.030 58.804  1.00 8.79  ? 282 LEU B N   1 
ATOM   6437 C CA  . LEU B 1 282 ? 43.528  -14.137 57.476  1.00 9.48  ? 282 LEU B CA  1 
ATOM   6438 C C   . LEU B 1 282 ? 44.348  -12.891 57.140  1.00 14.17 ? 282 LEU B C   1 
ATOM   6439 O O   . LEU B 1 282 ? 45.476  -12.994 56.657  1.00 16.83 ? 282 LEU B O   1 
ATOM   6440 C CB  . LEU B 1 282 ? 42.432  -14.364 56.437  1.00 14.86 ? 282 LEU B CB  1 
ATOM   6441 C CG  . LEU B 1 282 ? 42.900  -14.538 54.994  1.00 15.64 ? 282 LEU B CG  1 
ATOM   6442 C CD1 . LEU B 1 282 ? 43.690  -15.823 54.871  1.00 13.59 ? 282 LEU B CD1 1 
ATOM   6443 C CD2 . LEU B 1 282 ? 41.715  -14.572 54.039  1.00 15.69 ? 282 LEU B CD2 1 
ATOM   6444 N N   . LYS B 1 283 ? 43.806  -11.702 57.412  1.00 11.78 ? 283 LYS B N   1 
ATOM   6445 C CA  . LYS B 1 283 ? 44.562  -10.474 57.140  1.00 13.96 ? 283 LYS B CA  1 
ATOM   6446 C C   . LYS B 1 283 ? 45.867  -10.437 57.928  1.00 13.42 ? 283 LYS B C   1 
ATOM   6447 O O   . LYS B 1 283 ? 46.888  -9.934  57.438  1.00 13.00 ? 283 LYS B O   1 
ATOM   6448 C CB  . LYS B 1 283 ? 43.719  -9.244  57.472  1.00 15.30 ? 283 LYS B CB  1 
ATOM   6449 C CG  . LYS B 1 283 ? 42.779  -8.800  56.357  1.00 31.90 ? 283 LYS B CG  1 
ATOM   6450 C CD  . LYS B 1 283 ? 41.781  -7.753  56.850  1.00 33.59 ? 283 LYS B CD  1 
ATOM   6451 C CE  . LYS B 1 283 ? 41.166  -6.978  55.683  1.00 47.26 ? 283 LYS B CE  1 
ATOM   6452 N NZ  . LYS B 1 283 ? 39.753  -6.583  55.950  1.00 49.69 ? 283 LYS B NZ  1 
ATOM   6453 N N   . ASN B 1 284 ? 45.858  -10.969 59.144  1.00 13.82 ? 284 ASN B N   1 
ATOM   6454 C CA  . ASN B 1 284 ? 47.068  -10.995 59.953  1.00 13.25 ? 284 ASN B CA  1 
ATOM   6455 C C   . ASN B 1 284 ? 48.058  -12.046 59.481  1.00 17.27 ? 284 ASN B C   1 
ATOM   6456 O O   . ASN B 1 284 ? 49.233  -11.972 59.856  1.00 16.67 ? 284 ASN B O   1 
ATOM   6457 C CB  . ASN B 1 284 ? 46.721  -11.278 61.414  1.00 10.15 ? 284 ASN B CB  1 
ATOM   6458 C CG  . ASN B 1 284 ? 46.118  -10.094 62.119  1.00 17.88 ? 284 ASN B CG  1 
ATOM   6459 O OD1 . ASN B 1 284 ? 46.157  -8.966  61.622  1.00 20.31 ? 284 ASN B OD1 1 
ATOM   6460 N ND2 . ASN B 1 284 ? 45.558  -10.340 63.303  1.00 16.67 ? 284 ASN B ND2 1 
ATOM   6461 N N   . SER B 1 285 ? 47.612  -13.022 58.683  1.00 15.96 ? 285 SER B N   1 
ATOM   6462 C CA  . SER B 1 285 ? 48.427  -14.181 58.347  1.00 12.78 ? 285 SER B CA  1 
ATOM   6463 C C   . SER B 1 285 ? 48.976  -14.161 56.931  1.00 15.62 ? 285 SER B C   1 
ATOM   6464 O O   . SER B 1 285 ? 50.043  -14.732 56.694  1.00 24.68 ? 285 SER B O   1 
ATOM   6465 C CB  . SER B 1 285 ? 47.622  -15.476 58.523  1.00 13.23 ? 285 SER B CB  1 
ATOM   6466 O OG  . SER B 1 285 ? 47.109  -15.592 59.843  1.00 15.44 ? 285 SER B OG  1 
ATOM   6467 N N   . VAL B 1 286 ? 48.251  -13.585 55.975  1.00 13.12 ? 286 VAL B N   1 
ATOM   6468 C CA  . VAL B 1 286 ? 48.645  -13.609 54.569  1.00 18.37 ? 286 VAL B CA  1 
ATOM   6469 C C   . VAL B 1 286 ? 48.540  -12.193 54.018  1.00 21.32 ? 286 VAL B C   1 
ATOM   6470 O O   . VAL B 1 286 ? 47.856  -11.334 54.578  1.00 17.42 ? 286 VAL B O   1 
ATOM   6471 C CB  . VAL B 1 286 ? 47.785  -14.581 53.718  1.00 22.24 ? 286 VAL B CB  1 
ATOM   6472 C CG1 . VAL B 1 286 ? 47.614  -15.930 54.409  1.00 24.35 ? 286 VAL B CG1 1 
ATOM   6473 C CG2 . VAL B 1 286 ? 46.413  -13.978 53.427  1.00 25.19 ? 286 VAL B CG2 1 
ATOM   6474 N N   . GLU B 1 287 ? 49.225  -11.952 52.898  1.00 24.96 ? 287 GLU B N   1 
ATOM   6475 C CA  . GLU B 1 287 ? 49.188  -10.618 52.297  1.00 18.45 ? 287 GLU B CA  1 
ATOM   6476 C C   . GLU B 1 287 ? 47.878  -10.383 51.554  1.00 18.63 ? 287 GLU B C   1 
ATOM   6477 O O   . GLU B 1 287 ? 47.127  -9.456  51.869  1.00 22.21 ? 287 GLU B O   1 
ATOM   6478 C CB  . GLU B 1 287 ? 50.384  -10.421 51.353  1.00 23.91 ? 287 GLU B CB  1 
ATOM   6479 C CG  . GLU B 1 287 ? 51.736  -10.395 52.057  1.00 17.29 ? 287 GLU B CG  1 
ATOM   6480 C CD  . GLU B 1 287 ? 52.891  -10.163 51.092  1.00 37.68 ? 287 GLU B CD  1 
ATOM   6481 O OE1 . GLU B 1 287 ? 52.636  -9.748  49.941  1.00 42.01 ? 287 GLU B OE1 1 
ATOM   6482 O OE2 . GLU B 1 287 ? 54.053  -10.396 51.481  1.00 43.77 ? 287 GLU B OE2 1 
ATOM   6483 N N   . ARG B 1 288 ? 47.577  -11.227 50.574  1.00 18.13 ? 288 ARG B N   1 
ATOM   6484 C CA  . ARG B 1 288 ? 46.384  -11.052 49.751  1.00 23.09 ? 288 ARG B CA  1 
ATOM   6485 C C   . ARG B 1 288 ? 45.257  -11.864 50.373  1.00 17.50 ? 288 ARG B C   1 
ATOM   6486 O O   . ARG B 1 288 ? 45.024  -13.030 50.050  1.00 27.57 ? 288 ARG B O   1 
ATOM   6487 C CB  . ARG B 1 288 ? 46.681  -11.431 48.307  1.00 24.86 ? 288 ARG B CB  1 
ATOM   6488 C CG  . ARG B 1 288 ? 47.478  -10.334 47.601  1.00 24.49 ? 288 ARG B CG  1 
ATOM   6489 C CD  . ARG B 1 288 ? 47.931  -10.793 46.236  1.00 30.21 ? 288 ARG B CD  1 
ATOM   6490 N NE  . ARG B 1 288 ? 48.955  -11.821 46.327  1.00 36.06 ? 288 ARG B NE  1 
ATOM   6491 C CZ  . ARG B 1 288 ? 48.817  -13.065 45.883  1.00 44.13 ? 288 ARG B CZ  1 
ATOM   6492 N NH1 . ARG B 1 288 ? 47.686  -13.449 45.303  1.00 46.61 ? 288 ARG B NH1 1 
ATOM   6493 N NH2 . ARG B 1 288 ? 49.821  -13.924 46.014  1.00 53.76 ? 288 ARG B NH2 1 
ATOM   6494 N N   . ALA B 1 289 ? 44.529  -11.215 51.269  1.00 24.53 ? 289 ALA B N   1 
ATOM   6495 C CA  . ALA B 1 289 ? 43.653  -11.914 52.197  1.00 23.45 ? 289 ALA B CA  1 
ATOM   6496 C C   . ALA B 1 289 ? 42.214  -11.865 51.697  1.00 16.83 ? 289 ALA B C   1 
ATOM   6497 O O   . ALA B 1 289 ? 41.340  -11.223 52.284  1.00 23.91 ? 289 ALA B O   1 
ATOM   6498 C CB  . ALA B 1 289 ? 43.787  -11.307 53.592  1.00 24.02 ? 289 ALA B CB  1 
ATOM   6499 N N   . SER B 1 290 ? 41.960  -12.577 50.605  1.00 15.46 ? 290 SER B N   1 
ATOM   6500 C CA  . SER B 1 290 ? 40.585  -12.666 50.124  1.00 13.00 ? 290 SER B CA  1 
ATOM   6501 C C   . SER B 1 290 ? 39.814  -13.765 50.853  1.00 9.71  ? 290 SER B C   1 
ATOM   6502 O O   . SER B 1 290 ? 40.212  -14.938 50.776  1.00 12.44 ? 290 SER B O   1 
ATOM   6503 C CB  . SER B 1 290 ? 40.516  -12.929 48.636  1.00 14.56 ? 290 SER B CB  1 
ATOM   6504 O OG  . SER B 1 290 ? 39.140  -12.972 48.274  1.00 13.09 ? 290 SER B OG  1 
ATOM   6505 N N   . PRO B 1 291 ? 38.702  -13.448 51.497  1.00 11.55 ? 291 PRO B N   1 
ATOM   6506 C CA  . PRO B 1 291 ? 37.906  -14.475 52.173  1.00 13.18 ? 291 PRO B CA  1 
ATOM   6507 C C   . PRO B 1 291 ? 37.002  -15.275 51.252  1.00 12.04 ? 291 PRO B C   1 
ATOM   6508 O O   . PRO B 1 291 ? 36.172  -16.038 51.751  1.00 12.31 ? 291 PRO B O   1 
ATOM   6509 C CB  . PRO B 1 291 ? 37.071  -13.652 53.170  1.00 12.39 ? 291 PRO B CB  1 
ATOM   6510 C CG  . PRO B 1 291 ? 36.852  -12.320 52.463  1.00 14.77 ? 291 PRO B CG  1 
ATOM   6511 C CD  . PRO B 1 291 ? 38.123  -12.092 51.645  1.00 15.06 ? 291 PRO B CD  1 
ATOM   6512 N N   . TYR B 1 292 ? 37.105  -15.129 49.931  1.00 14.43 ? 292 TYR B N   1 
ATOM   6513 C CA  . TYR B 1 292 ? 36.156  -15.786 49.043  1.00 14.15 ? 292 TYR B CA  1 
ATOM   6514 C C   . TYR B 1 292 ? 36.711  -17.084 48.465  1.00 11.99 ? 292 TYR B C   1 
ATOM   6515 O O   . TYR B 1 292 ? 36.050  -17.719 47.639  1.00 13.84 ? 292 TYR B O   1 
ATOM   6516 C CB  . TYR B 1 292 ? 35.718  -14.816 47.934  1.00 13.02 ? 292 TYR B CB  1 
ATOM   6517 C CG  . TYR B 1 292 ? 35.132  -13.540 48.505  1.00 12.47 ? 292 TYR B CG  1 
ATOM   6518 C CD1 . TYR B 1 292 ? 34.153  -13.595 49.491  1.00 16.66 ? 292 TYR B CD1 1 
ATOM   6519 C CD2 . TYR B 1 292 ? 35.564  -12.295 48.086  1.00 20.17 ? 292 TYR B CD2 1 
ATOM   6520 C CE1 . TYR B 1 292 ? 33.616  -12.465 50.043  1.00 16.24 ? 292 TYR B CE1 1 
ATOM   6521 C CE2 . TYR B 1 292 ? 35.023  -11.135 48.635  1.00 16.41 ? 292 TYR B CE2 1 
ATOM   6522 C CZ  . TYR B 1 292 ? 34.046  -11.231 49.612  1.00 16.36 ? 292 TYR B CZ  1 
ATOM   6523 O OH  . TYR B 1 292 ? 33.504  -10.096 50.178  1.00 23.14 ? 292 TYR B OH  1 
ATOM   6524 N N   . LEU B 1 293 ? 37.893  -17.502 48.908  1.00 11.89 ? 293 LEU B N   1 
ATOM   6525 C CA  . LEU B 1 293 ? 38.506  -18.766 48.521  1.00 10.96 ? 293 LEU B CA  1 
ATOM   6526 C C   . LEU B 1 293 ? 38.325  -19.821 49.605  1.00 13.35 ? 293 LEU B C   1 
ATOM   6527 O O   . LEU B 1 293 ? 38.162  -19.508 50.788  1.00 13.04 ? 293 LEU B O   1 
ATOM   6528 C CB  . LEU B 1 293 ? 40.015  -18.591 48.282  1.00 13.18 ? 293 LEU B CB  1 
ATOM   6529 C CG  . LEU B 1 293 ? 40.554  -17.928 47.010  1.00 18.69 ? 293 LEU B CG  1 
ATOM   6530 C CD1 . LEU B 1 293 ? 40.034  -16.527 46.868  1.00 18.88 ? 293 LEU B CD1 1 
ATOM   6531 C CD2 . LEU B 1 293 ? 42.076  -17.897 47.082  1.00 19.93 ? 293 LEU B CD2 1 
ATOM   6532 N N   . ARG B 1 294 ? 38.427  -21.091 49.193  1.00 11.98 ? 294 ARG B N   1 
ATOM   6533 C CA  . ARG B 1 294 ? 38.622  -22.186 50.138  1.00 11.26 ? 294 ARG B CA  1 
ATOM   6534 C C   . ARG B 1 294 ? 40.118  -22.337 50.407  1.00 17.16 ? 294 ARG B C   1 
ATOM   6535 O O   . ARG B 1 294 ? 40.915  -22.399 49.466  1.00 15.68 ? 294 ARG B O   1 
ATOM   6536 C CB  . ARG B 1 294 ? 38.026  -23.490 49.597  1.00 10.87 ? 294 ARG B CB  1 
ATOM   6537 C CG  . ARG B 1 294 ? 38.200  -24.695 50.549  1.00 14.94 ? 294 ARG B CG  1 
ATOM   6538 C CD  . ARG B 1 294 ? 37.302  -25.893 50.176  1.00 14.45 ? 294 ARG B CD  1 
ATOM   6539 N NE  . ARG B 1 294 ? 37.688  -26.412 48.873  1.00 16.40 ? 294 ARG B NE  1 
ATOM   6540 C CZ  . ARG B 1 294 ? 36.875  -26.534 47.836  1.00 18.12 ? 294 ARG B CZ  1 
ATOM   6541 N NH1 . ARG B 1 294 ? 35.585  -26.225 47.938  1.00 16.54 ? 294 ARG B NH1 1 
ATOM   6542 N NH2 . ARG B 1 294 ? 37.356  -27.002 46.694  1.00 18.93 ? 294 ARG B NH2 1 
ATOM   6543 N N   . TYR B 1 295 ? 40.513  -22.366 51.680  1.00 12.64 ? 295 TYR B N   1 
ATOM   6544 C CA  . TYR B 1 295 ? 41.931  -22.468 52.013  1.00 9.96  ? 295 TYR B CA  1 
ATOM   6545 C C   . TYR B 1 295 ? 42.259  -23.863 52.529  1.00 13.69 ? 295 TYR B C   1 
ATOM   6546 O O   . TYR B 1 295 ? 41.407  -24.545 53.104  1.00 14.98 ? 295 TYR B O   1 
ATOM   6547 C CB  . TYR B 1 295 ? 42.357  -21.409 53.044  1.00 10.66 ? 295 TYR B CB  1 
ATOM   6548 C CG  . TYR B 1 295 ? 42.410  -20.013 52.452  1.00 12.18 ? 295 TYR B CG  1 
ATOM   6549 C CD1 . TYR B 1 295 ? 41.255  -19.264 52.289  1.00 14.10 ? 295 TYR B CD1 1 
ATOM   6550 C CD2 . TYR B 1 295 ? 43.609  -19.460 52.027  1.00 12.86 ? 295 TYR B CD2 1 
ATOM   6551 C CE1 . TYR B 1 295 ? 41.296  -17.986 51.749  1.00 13.66 ? 295 TYR B CE1 1 
ATOM   6552 C CE2 . TYR B 1 295 ? 43.658  -18.181 51.474  1.00 14.31 ? 295 TYR B CE2 1 
ATOM   6553 C CZ  . TYR B 1 295 ? 42.500  -17.457 51.327  1.00 13.41 ? 295 TYR B CZ  1 
ATOM   6554 O OH  . TYR B 1 295 ? 42.548  -16.194 50.777  1.00 14.08 ? 295 TYR B OH  1 
ATOM   6555 N N   . TYR B 1 296 ? 43.491  -24.303 52.281  1.00 12.22 ? 296 TYR B N   1 
ATOM   6556 C CA  . TYR B 1 296 ? 43.967  -25.596 52.776  1.00 12.13 ? 296 TYR B CA  1 
ATOM   6557 C C   . TYR B 1 296 ? 45.157  -25.324 53.687  1.00 14.85 ? 296 TYR B C   1 
ATOM   6558 O O   . TYR B 1 296 ? 46.228  -24.920 53.215  1.00 15.17 ? 296 TYR B O   1 
ATOM   6559 C CB  . TYR B 1 296 ? 44.356  -26.546 51.638  1.00 12.99 ? 296 TYR B CB  1 
ATOM   6560 C CG  . TYR B 1 296 ? 43.255  -26.827 50.641  1.00 20.06 ? 296 TYR B CG  1 
ATOM   6561 C CD1 . TYR B 1 296 ? 42.057  -27.415 51.039  1.00 19.27 ? 296 TYR B CD1 1 
ATOM   6562 C CD2 . TYR B 1 296 ? 43.414  -26.510 49.295  1.00 23.96 ? 296 TYR B CD2 1 
ATOM   6563 C CE1 . TYR B 1 296 ? 41.039  -27.670 50.119  1.00 18.54 ? 296 TYR B CE1 1 
ATOM   6564 C CE2 . TYR B 1 296 ? 42.404  -26.764 48.363  1.00 14.35 ? 296 TYR B CE2 1 
ATOM   6565 C CZ  . TYR B 1 296 ? 41.226  -27.348 48.784  1.00 19.80 ? 296 TYR B CZ  1 
ATOM   6566 O OH  . TYR B 1 296 ? 40.225  -27.606 47.876  1.00 19.15 ? 296 TYR B OH  1 
ATOM   6567 N N   . PHE B 1 297 ? 44.977  -25.535 54.987  1.00 13.80 ? 297 PHE B N   1 
ATOM   6568 C CA  . PHE B 1 297 ? 46.079  -25.347 55.924  1.00 9.86  ? 297 PHE B CA  1 
ATOM   6569 C C   . PHE B 1 297 ? 47.023  -26.545 55.840  1.00 11.89 ? 297 PHE B C   1 
ATOM   6570 O O   . PHE B 1 297 ? 46.672  -27.657 56.263  1.00 9.70  ? 297 PHE B O   1 
ATOM   6571 C CB  . PHE B 1 297 ? 45.551  -25.156 57.340  1.00 14.61 ? 297 PHE B CB  1 
ATOM   6572 C CG  . PHE B 1 297 ? 46.635  -25.005 58.367  1.00 9.96  ? 297 PHE B CG  1 
ATOM   6573 C CD1 . PHE B 1 297 ? 47.310  -23.809 58.516  1.00 12.85 ? 297 PHE B CD1 1 
ATOM   6574 C CD2 . PHE B 1 297 ? 46.993  -26.076 59.166  1.00 11.99 ? 297 PHE B CD2 1 
ATOM   6575 C CE1 . PHE B 1 297 ? 48.319  -23.672 59.481  1.00 13.51 ? 297 PHE B CE1 1 
ATOM   6576 C CE2 . PHE B 1 297 ? 47.994  -25.950 60.118  1.00 14.45 ? 297 PHE B CE2 1 
ATOM   6577 C CZ  . PHE B 1 297 ? 48.655  -24.749 60.278  1.00 13.28 ? 297 PHE B CZ  1 
ATOM   6578 N N   . ARG B 1 298 ? 48.215  -26.317 55.289  1.00 13.84 ? 298 ARG B N   1 
ATOM   6579 C CA  . ARG B 1 298 ? 49.265  -27.341 55.187  1.00 16.30 ? 298 ARG B CA  1 
ATOM   6580 C C   . ARG B 1 298 ? 48.777  -28.597 54.468  1.00 13.57 ? 298 ARG B C   1 
ATOM   6581 O O   . ARG B 1 298 ? 49.308  -29.686 54.679  1.00 12.81 ? 298 ARG B O   1 
ATOM   6582 C CB  . ARG B 1 298 ? 49.820  -27.706 56.569  1.00 17.30 ? 298 ARG B CB  1 
ATOM   6583 C CG  . ARG B 1 298 ? 50.577  -26.560 57.177  1.00 10.77 ? 298 ARG B CG  1 
ATOM   6584 C CD  . ARG B 1 298 ? 51.260  -26.851 58.524  1.00 21.98 ? 298 ARG B CD  1 
ATOM   6585 N NE  . ARG B 1 298 ? 51.748  -25.588 59.105  1.00 22.60 ? 298 ARG B NE  1 
ATOM   6586 C CZ  . ARG B 1 298 ? 52.137  -25.436 60.373  1.00 22.01 ? 298 ARG B CZ  1 
ATOM   6587 N NH1 . ARG B 1 298 ? 52.104  -26.466 61.205  1.00 26.93 ? 298 ARG B NH1 1 
ATOM   6588 N NH2 . ARG B 1 298 ? 52.558  -24.255 60.810  1.00 22.47 ? 298 ARG B NH2 1 
ATOM   6589 N N   . GLU B 1 299 ? 47.744  -28.458 53.632  1.00 14.07 ? 299 GLU B N   1 
ATOM   6590 C CA  . GLU B 1 299 ? 47.065  -29.590 52.998  1.00 14.35 ? 299 GLU B CA  1 
ATOM   6591 C C   . GLU B 1 299 ? 46.516  -30.583 54.016  1.00 20.72 ? 299 GLU B C   1 
ATOM   6592 O O   . GLU B 1 299 ? 46.266  -31.747 53.687  1.00 17.74 ? 299 GLU B O   1 
ATOM   6593 C CB  . GLU B 1 299 ? 47.984  -30.325 52.009  1.00 23.42 ? 299 GLU B CB  1 
ATOM   6594 C CG  . GLU B 1 299 ? 48.756  -29.415 51.078  1.00 22.86 ? 299 GLU B CG  1 
ATOM   6595 C CD  . GLU B 1 299 ? 47.940  -28.977 49.878  1.00 29.39 ? 299 GLU B CD  1 
ATOM   6596 O OE1 . GLU B 1 299 ? 48.555  -28.644 48.842  1.00 37.17 ? 299 GLU B OE1 1 
ATOM   6597 O OE2 . GLU B 1 299 ? 46.688  -28.973 49.965  1.00 27.12 ? 299 GLU B OE2 1 
ATOM   6598 N N   . LEU B 1 300 ? 46.318  -30.151 55.256  1.00 17.25 ? 300 LEU B N   1 
ATOM   6599 C CA  . LEU B 1 300 ? 45.803  -31.031 56.296  1.00 14.82 ? 300 LEU B CA  1 
ATOM   6600 C C   . LEU B 1 300 ? 44.313  -30.853 56.534  1.00 19.08 ? 300 LEU B C   1 
ATOM   6601 O O   . LEU B 1 300 ? 43.603  -31.832 56.770  1.00 19.11 ? 300 LEU B O   1 
ATOM   6602 C CB  . LEU B 1 300 ? 46.544  -30.778 57.609  1.00 19.25 ? 300 LEU B CB  1 
ATOM   6603 C CG  . LEU B 1 300 ? 48.056  -30.998 57.626  1.00 16.94 ? 300 LEU B CG  1 
ATOM   6604 C CD1 . LEU B 1 300 ? 48.610  -30.682 58.992  1.00 14.51 ? 300 LEU B CD1 1 
ATOM   6605 C CD2 . LEU B 1 300 ? 48.394  -32.429 57.218  1.00 21.13 ? 300 LEU B CD2 1 
ATOM   6606 N N   . ILE B 1 301 ? 43.818  -29.623 56.476  1.00 12.58 ? 301 ILE B N   1 
ATOM   6607 C CA  . ILE B 1 301 ? 42.446  -29.336 56.880  1.00 8.84  ? 301 ILE B CA  1 
ATOM   6608 C C   . ILE B 1 301 ? 41.980  -28.103 56.109  1.00 12.16 ? 301 ILE B C   1 
ATOM   6609 O O   . ILE B 1 301 ? 42.773  -27.194 55.847  1.00 15.22 ? 301 ILE B O   1 
ATOM   6610 C CB  . ILE B 1 301 ? 42.379  -29.144 58.415  1.00 9.45  ? 301 ILE B CB  1 
ATOM   6611 C CG1 . ILE B 1 301 ? 40.952  -28.874 58.894  1.00 11.28 ? 301 ILE B CG1 1 
ATOM   6612 C CG2 . ILE B 1 301 ? 43.281  -28.021 58.874  1.00 16.29 ? 301 ILE B CG2 1 
ATOM   6613 C CD1 . ILE B 1 301 ? 40.865  -28.768 60.420  1.00 15.27 ? 301 ILE B CD1 1 
ATOM   6614 N N   . SER B 1 302 ? 40.695  -28.086 55.722  1.00 11.79 ? 302 SER B N   1 
ATOM   6615 C CA  . SER B 1 302 ? 40.147  -26.961 54.970  1.00 13.07 ? 302 SER B CA  1 
ATOM   6616 C C   . SER B 1 302 ? 39.711  -25.850 55.909  1.00 11.73 ? 302 SER B C   1 
ATOM   6617 O O   . SER B 1 302 ? 39.185  -26.107 56.991  1.00 10.05 ? 302 SER B O   1 
ATOM   6618 C CB  . SER B 1 302 ? 38.956  -27.392 54.115  1.00 21.38 ? 302 SER B CB  1 
ATOM   6619 O OG  . SER B 1 302 ? 39.346  -28.345 53.149  1.00 20.16 ? 302 SER B OG  1 
ATOM   6620 N N   . VAL B 1 303 ? 39.905  -24.610 55.479  1.00 14.79 ? 303 VAL B N   1 
ATOM   6621 C CA  . VAL B 1 303 ? 39.601  -23.448 56.303  1.00 12.82 ? 303 VAL B CA  1 
ATOM   6622 C C   . VAL B 1 303 ? 38.876  -22.421 55.446  1.00 16.32 ? 303 VAL B C   1 
ATOM   6623 O O   . VAL B 1 303 ? 39.373  -22.028 54.387  1.00 13.38 ? 303 VAL B O   1 
ATOM   6624 C CB  . VAL B 1 303 ? 40.870  -22.819 56.911  1.00 11.69 ? 303 VAL B CB  1 
ATOM   6625 C CG1 . VAL B 1 303 ? 40.480  -21.665 57.819  1.00 11.98 ? 303 VAL B CG1 1 
ATOM   6626 C CG2 . VAL B 1 303 ? 41.653  -23.830 57.715  1.00 10.02 ? 303 VAL B CG2 1 
ATOM   6627 N N   . PHE B 1 304 ? 37.704  -21.986 55.896  1.00 8.16  ? 304 PHE B N   1 
ATOM   6628 C CA  . PHE B 1 304 ? 37.069  -20.802 55.335  1.00 7.66  ? 304 PHE B CA  1 
ATOM   6629 C C   . PHE B 1 304 ? 37.182  -19.645 56.313  1.00 10.44 ? 304 PHE B C   1 
ATOM   6630 O O   . PHE B 1 304 ? 37.132  -19.833 57.530  1.00 9.77  ? 304 PHE B O   1 
ATOM   6631 C CB  . PHE B 1 304 ? 35.602  -21.064 54.990  1.00 8.26  ? 304 PHE B CB  1 
ATOM   6632 C CG  . PHE B 1 304 ? 35.417  -21.832 53.705  1.00 10.61 ? 304 PHE B CG  1 
ATOM   6633 C CD1 . PHE B 1 304 ? 35.426  -21.171 52.488  1.00 8.81  ? 304 PHE B CD1 1 
ATOM   6634 C CD2 . PHE B 1 304 ? 35.216  -23.207 53.719  1.00 10.78 ? 304 PHE B CD2 1 
ATOM   6635 C CE1 . PHE B 1 304 ? 35.237  -21.870 51.297  1.00 14.92 ? 304 PHE B CE1 1 
ATOM   6636 C CE2 . PHE B 1 304 ? 35.020  -23.912 52.529  1.00 16.68 ? 304 PHE B CE2 1 
ATOM   6637 C CZ  . PHE B 1 304 ? 35.028  -23.243 51.324  1.00 11.48 ? 304 PHE B CZ  1 
ATOM   6638 N N   . PHE B 1 305 ? 37.382  -18.451 55.781  1.00 6.97  ? 305 PHE B N   1 
ATOM   6639 C CA  . PHE B 1 305 ? 37.427  -17.247 56.591  1.00 10.38 ? 305 PHE B CA  1 
ATOM   6640 C C   . PHE B 1 305 ? 36.114  -16.520 56.350  1.00 7.69  ? 305 PHE B C   1 
ATOM   6641 O O   . PHE B 1 305 ? 35.744  -16.274 55.196  1.00 10.85 ? 305 PHE B O   1 
ATOM   6642 C CB  . PHE B 1 305 ? 38.658  -16.414 56.226  1.00 11.25 ? 305 PHE B CB  1 
ATOM   6643 C CG  . PHE B 1 305 ? 39.961  -17.143 56.491  1.00 12.42 ? 305 PHE B CG  1 
ATOM   6644 C CD1 . PHE B 1 305 ? 40.489  -18.026 55.551  1.00 12.42 ? 305 PHE B CD1 1 
ATOM   6645 C CD2 . PHE B 1 305 ? 40.609  -16.996 57.704  1.00 12.93 ? 305 PHE B CD2 1 
ATOM   6646 C CE1 . PHE B 1 305 ? 41.658  -18.710 55.800  1.00 11.81 ? 305 PHE B CE1 1 
ATOM   6647 C CE2 . PHE B 1 305 ? 41.779  -17.676 57.966  1.00 9.77  ? 305 PHE B CE2 1 
ATOM   6648 C CZ  . PHE B 1 305 ? 42.312  -18.533 57.013  1.00 12.50 ? 305 PHE B CZ  1 
ATOM   6649 N N   . ARG B 1 306 ? 35.371  -16.254 57.424  1.00 7.25  ? 306 ARG B N   1 
ATOM   6650 C CA  . ARG B 1 306 ? 34.056  -15.659 57.246  1.00 5.59  ? 306 ARG B CA  1 
ATOM   6651 C C   . ARG B 1 306 ? 34.195  -14.239 56.699  1.00 11.53 ? 306 ARG B C   1 
ATOM   6652 O O   . ARG B 1 306 ? 35.197  -13.548 56.929  1.00 13.66 ? 306 ARG B O   1 
ATOM   6653 C CB  . ARG B 1 306 ? 33.281  -15.629 58.566  1.00 8.36  ? 306 ARG B CB  1 
ATOM   6654 C CG  . ARG B 1 306 ? 33.839  -14.626 59.548  1.00 10.20 ? 306 ARG B CG  1 
ATOM   6655 C CD  . ARG B 1 306 ? 32.956  -14.422 60.769  1.00 14.89 ? 306 ARG B CD  1 
ATOM   6656 N NE  . ARG B 1 306 ? 33.476  -13.294 61.545  1.00 15.19 ? 306 ARG B NE  1 
ATOM   6657 C CZ  . ARG B 1 306 ? 32.779  -12.587 62.422  1.00 10.67 ? 306 ARG B CZ  1 
ATOM   6658 N NH1 . ARG B 1 306 ? 31.496  -12.880 62.683  1.00 7.90  ? 306 ARG B NH1 1 
ATOM   6659 N NH2 . ARG B 1 306 ? 33.375  -11.594 63.063  1.00 10.44 ? 306 ARG B NH2 1 
ATOM   6660 N N   . ASP B 1 307 ? 33.186  -13.810 55.949  1.00 5.94  ? 307 ASP B N   1 
ATOM   6661 C CA  . ASP B 1 307 ? 33.093  -12.403 55.578  1.00 10.21 ? 307 ASP B CA  1 
ATOM   6662 C C   . ASP B 1 307 ? 32.693  -11.616 56.817  1.00 10.44 ? 307 ASP B C   1 
ATOM   6663 O O   . ASP B 1 307 ? 31.532  -11.668 57.245  1.00 10.54 ? 307 ASP B O   1 
ATOM   6664 C CB  . ASP B 1 307 ? 32.078  -12.208 54.453  1.00 11.29 ? 307 ASP B CB  1 
ATOM   6665 C CG  . ASP B 1 307 ? 32.087  -10.787 53.901  1.00 15.23 ? 307 ASP B CG  1 
ATOM   6666 O OD1 . ASP B 1 307 ? 32.025  -9.829  54.699  1.00 11.42 ? 307 ASP B OD1 1 
ATOM   6667 O OD2 . ASP B 1 307 ? 32.182  -10.626 52.670  1.00 20.24 ? 307 ASP B OD2 1 
ATOM   6668 N N   . LYS B 1 308 ? 33.649  -10.872 57.380  1.00 8.78  ? 308 LYS B N   1 
ATOM   6669 C CA  . LYS B 1 308 ? 33.421  -10.196 58.657  1.00 13.46 ? 308 LYS B CA  1 
ATOM   6670 C C   . LYS B 1 308 ? 32.347  -9.118  58.551  1.00 12.36 ? 308 LYS B C   1 
ATOM   6671 O O   . LYS B 1 308 ? 31.513  -8.973  59.458  1.00 13.19 ? 308 LYS B O   1 
ATOM   6672 C CB  . LYS B 1 308 ? 34.729  -9.586  59.170  1.00 13.25 ? 308 LYS B CB  1 
ATOM   6673 C CG  . LYS B 1 308 ? 34.571  -8.721  60.431  1.00 13.88 ? 308 LYS B CG  1 
ATOM   6674 C CD  . LYS B 1 308 ? 35.916  -8.040  60.747  1.00 23.18 ? 308 LYS B CD  1 
ATOM   6675 C CE  . LYS B 1 308 ? 35.981  -7.357  62.126  1.00 20.58 ? 308 LYS B CE  1 
ATOM   6676 N NZ  . LYS B 1 308 ? 34.833  -7.569  63.036  1.00 13.60 ? 308 LYS B NZ  1 
ATOM   6677 N N   . THR B 1 309 ? 32.363  -8.323  57.477  1.00 12.51 ? 309 THR B N   1 
ATOM   6678 C CA  . THR B 1 309 ? 31.405  -7.221  57.434  1.00 9.16  ? 309 THR B CA  1 
ATOM   6679 C C   . THR B 1 309 ? 29.976  -7.727  57.280  1.00 7.12  ? 309 THR B C   1 
ATOM   6680 O O   . THR B 1 309 ? 29.071  -7.216  57.942  1.00 11.83 ? 309 THR B O   1 
ATOM   6681 C CB  . THR B 1 309 ? 31.720  -6.213  56.322  1.00 22.11 ? 309 THR B CB  1 
ATOM   6682 O OG1 . THR B 1 309 ? 31.091  -6.612  55.105  1.00 41.94 ? 309 THR B OG1 1 
ATOM   6683 C CG2 . THR B 1 309 ? 33.207  -6.047  56.110  1.00 11.67 ? 309 THR B CG2 1 
ATOM   6684 N N   . LEU B 1 310 ? 29.747  -8.700  56.392  1.00 9.90  ? 310 LEU B N   1 
ATOM   6685 C CA  . LEU B 1 310 ? 28.396  -9.240  56.255  1.00 7.08  ? 310 LEU B CA  1 
ATOM   6686 C C   . LEU B 1 310 ? 27.943  -9.888  57.551  1.00 6.39  ? 310 LEU B C   1 
ATOM   6687 O O   . LEU B 1 310 ? 26.776  -9.759  57.945  1.00 10.98 ? 310 LEU B O   1 
ATOM   6688 C CB  . LEU B 1 310 ? 28.341  -10.261 55.124  1.00 10.67 ? 310 LEU B CB  1 
ATOM   6689 C CG  . LEU B 1 310 ? 28.505  -9.670  53.713  1.00 13.07 ? 310 LEU B CG  1 
ATOM   6690 C CD1 . LEU B 1 310 ? 28.432  -10.793 52.693  1.00 13.18 ? 310 LEU B CD1 1 
ATOM   6691 C CD2 . LEU B 1 310 ? 27.425  -8.624  53.455  1.00 15.51 ? 310 LEU B CD2 1 
ATOM   6692 N N   . SER B 1 311 ? 28.850  -10.604 58.218  1.00 6.10  ? 311 SER B N   1 
ATOM   6693 C CA  . SER B 1 311 ? 28.490  -11.281 59.463  1.00 9.25  ? 311 SER B CA  1 
ATOM   6694 C C   . SER B 1 311 ? 28.172  -10.271 60.548  1.00 13.82 ? 311 SER B C   1 
ATOM   6695 O O   . SER B 1 311 ? 27.198  -10.436 61.297  1.00 10.46 ? 311 SER B O   1 
ATOM   6696 C CB  . SER B 1 311 ? 29.632  -12.197 59.910  1.00 7.42  ? 311 SER B CB  1 
ATOM   6697 O OG  . SER B 1 311 ? 29.809  -13.243 58.965  1.00 10.08 ? 311 SER B OG  1 
ATOM   6698 N N   . ASP B 1 312 ? 28.982  -9.206  60.631  1.00 11.97 ? 312 ASP B N   1 
ATOM   6699 C CA  . ASP B 1 312 ? 28.763  -8.169  61.631  1.00 13.66 ? 312 ASP B CA  1 
ATOM   6700 C C   . ASP B 1 312 ? 27.512  -7.367  61.333  1.00 11.35 ? 312 ASP B C   1 
ATOM   6701 O O   . ASP B 1 312 ? 26.871  -6.876  62.267  1.00 11.40 ? 312 ASP B O   1 
ATOM   6702 C CB  . ASP B 1 312 ? 29.966  -7.213  61.709  1.00 14.64 ? 312 ASP B CB  1 
ATOM   6703 C CG  . ASP B 1 312 ? 31.150  -7.789  62.491  1.00 20.03 ? 312 ASP B CG  1 
ATOM   6704 O OD1 . ASP B 1 312 ? 30.995  -8.826  63.172  1.00 16.32 ? 312 ASP B OD1 1 
ATOM   6705 O OD2 . ASP B 1 312 ? 32.246  -7.178  62.427  1.00 22.46 ? 312 ASP B OD2 1 
ATOM   6706 N N   . LEU B 1 313 ? 27.152  -7.200  60.050  1.00 10.55 ? 313 LEU B N   1 
ATOM   6707 C CA  . LEU B 1 313 ? 25.941  -6.444  59.726  1.00 9.39  ? 313 LEU B CA  1 
ATOM   6708 C C   . LEU B 1 313 ? 24.700  -7.098  60.338  1.00 6.55  ? 313 LEU B C   1 
ATOM   6709 O O   . LEU B 1 313 ? 23.858  -6.423  60.950  1.00 8.08  ? 313 LEU B O   1 
ATOM   6710 C CB  . LEU B 1 313 ? 25.784  -6.299  58.203  1.00 9.79  ? 313 LEU B CB  1 
ATOM   6711 C CG  . LEU B 1 313 ? 26.652  -5.206  57.542  1.00 15.71 ? 313 LEU B CG  1 
ATOM   6712 C CD1 . LEU B 1 313 ? 26.650  -5.345  56.028  1.00 11.16 ? 313 LEU B CD1 1 
ATOM   6713 C CD2 . LEU B 1 313 ? 26.240  -3.787  57.961  1.00 12.31 ? 313 LEU B CD2 1 
ATOM   6714 N N   . ILE B 1 314 ? 24.572  -8.416  60.201  1.00 6.98  ? 314 ILE B N   1 
ATOM   6715 C CA  . ILE B 1 314 ? 23.434  -9.097  60.817  1.00 7.36  ? 314 ILE B CA  1 
ATOM   6716 C C   . ILE B 1 314 ? 23.577  -9.101  62.340  1.00 12.45 ? 314 ILE B C   1 
ATOM   6717 O O   . ILE B 1 314 ? 22.627  -8.805  63.082  1.00 10.57 ? 314 ILE B O   1 
ATOM   6718 C CB  . ILE B 1 314 ? 23.314  -10.528 60.258  1.00 8.89  ? 314 ILE B CB  1 
ATOM   6719 C CG1 . ILE B 1 314 ? 23.069  -10.484 58.748  1.00 8.77  ? 314 ILE B CG1 1 
ATOM   6720 C CG2 . ILE B 1 314 ? 22.195  -11.274 60.947  1.00 10.16 ? 314 ILE B CG2 1 
ATOM   6721 C CD1 . ILE B 1 314 ? 23.079  -11.879 58.083  1.00 10.19 ? 314 ILE B CD1 1 
ATOM   6722 N N   . GLY B 1 315 ? 24.770  -9.437  62.829  1.00 9.01  ? 315 GLY B N   1 
ATOM   6723 C CA  . GLY B 1 315 ? 24.959  -9.656  64.255  1.00 10.25 ? 315 GLY B CA  1 
ATOM   6724 C C   . GLY B 1 315 ? 24.894  -8.400  65.096  1.00 17.39 ? 315 GLY B C   1 
ATOM   6725 O O   . GLY B 1 315 ? 24.549  -8.480  66.279  1.00 12.94 ? 315 GLY B O   1 
ATOM   6726 N N   . PHE B 1 316 ? 25.199  -7.243  64.509  1.00 10.51 ? 316 PHE B N   1 
ATOM   6727 C CA  . PHE B 1 316 ? 25.346  -6.013  65.282  1.00 13.98 ? 316 PHE B CA  1 
ATOM   6728 C C   . PHE B 1 316 ? 24.625  -4.825  64.669  1.00 12.72 ? 316 PHE B C   1 
ATOM   6729 O O   . PHE B 1 316 ? 24.239  -3.901  65.391  1.00 19.05 ? 316 PHE B O   1 
ATOM   6730 C CB  . PHE B 1 316 ? 26.828  -5.665  65.434  1.00 12.23 ? 316 PHE B CB  1 
ATOM   6731 C CG  . PHE B 1 316 ? 27.589  -6.653  66.229  1.00 17.69 ? 316 PHE B CG  1 
ATOM   6732 C CD1 . PHE B 1 316 ? 27.285  -6.861  67.560  1.00 23.16 ? 316 PHE B CD1 1 
ATOM   6733 C CD2 . PHE B 1 316 ? 28.597  -7.401  65.647  1.00 22.57 ? 316 PHE B CD2 1 
ATOM   6734 C CE1 . PHE B 1 316 ? 27.981  -7.796  68.298  1.00 19.23 ? 316 PHE B CE1 1 
ATOM   6735 C CE2 . PHE B 1 316 ? 29.297  -8.331  66.380  1.00 25.09 ? 316 PHE B CE2 1 
ATOM   6736 C CZ  . PHE B 1 316 ? 28.984  -8.533  67.710  1.00 21.77 ? 316 PHE B CZ  1 
ATOM   6737 N N   . SER B 1 317 ? 24.461  -4.803  63.344  1.00 14.39 ? 317 SER B N   1 
ATOM   6738 C CA  . SER B 1 317 ? 24.000  -3.574  62.698  1.00 13.47 ? 317 SER B CA  1 
ATOM   6739 C C   . SER B 1 317 ? 22.508  -3.545  62.400  1.00 16.79 ? 317 SER B C   1 
ATOM   6740 O O   . SER B 1 317 ? 21.843  -2.557  62.724  1.00 13.93 ? 317 SER B O   1 
ATOM   6741 C CB  . SER B 1 317 ? 24.763  -3.334  61.394  1.00 15.32 ? 317 SER B CB  1 
ATOM   6742 O OG  . SER B 1 317 ? 26.141  -3.236  61.660  1.00 18.80 ? 317 SER B OG  1 
ATOM   6743 N N   . TYR B 1 318 ? 21.974  -4.579  61.746  1.00 9.80  ? 318 TYR B N   1 
ATOM   6744 C CA  . TYR B 1 318 ? 20.660  -4.423  61.131  1.00 7.98  ? 318 TYR B CA  1 
ATOM   6745 C C   . TYR B 1 318 ? 19.528  -4.306  62.145  1.00 8.96  ? 318 TYR B C   1 
ATOM   6746 O O   . TYR B 1 318 ? 18.416  -3.929  61.756  1.00 10.84 ? 318 TYR B O   1 
ATOM   6747 C CB  . TYR B 1 318 ? 20.384  -5.583  60.179  1.00 8.38  ? 318 TYR B CB  1 
ATOM   6748 C CG  . TYR B 1 318 ? 21.170  -5.536  58.869  1.00 11.32 ? 318 TYR B CG  1 
ATOM   6749 C CD1 . TYR B 1 318 ? 21.563  -4.317  58.293  1.00 15.52 ? 318 TYR B CD1 1 
ATOM   6750 C CD2 . TYR B 1 318 ? 21.499  -6.704  58.205  1.00 14.07 ? 318 TYR B CD2 1 
ATOM   6751 C CE1 . TYR B 1 318 ? 22.260  -4.290  57.089  1.00 12.47 ? 318 TYR B CE1 1 
ATOM   6752 C CE2 . TYR B 1 318 ? 22.195  -6.692  57.009  1.00 10.91 ? 318 TYR B CE2 1 
ATOM   6753 C CZ  . TYR B 1 318 ? 22.571  -5.496  56.454  1.00 15.61 ? 318 TYR B CZ  1 
ATOM   6754 O OH  . TYR B 1 318 ? 23.260  -5.552  55.258  1.00 12.92 ? 318 TYR B OH  1 
ATOM   6755 N N   . HIS B 1 319 ? 19.759  -4.632  63.422  1.00 14.50 ? 319 HIS B N   1 
ATOM   6756 C CA  . HIS B 1 319 ? 18.706  -4.377  64.404  1.00 15.05 ? 319 HIS B CA  1 
ATOM   6757 C C   . HIS B 1 319 ? 18.267  -2.918  64.372  1.00 17.83 ? 319 HIS B C   1 
ATOM   6758 O O   . HIS B 1 319 ? 17.092  -2.615  64.603  1.00 18.10 ? 319 HIS B O   1 
ATOM   6759 C CB  . HIS B 1 319 ? 19.167  -4.742  65.813  1.00 11.15 ? 319 HIS B CB  1 
ATOM   6760 C CG  . HIS B 1 319 ? 20.097  -3.743  66.422  1.00 10.19 ? 319 HIS B CG  1 
ATOM   6761 N ND1 . HIS B 1 319 ? 19.660  -2.674  67.177  1.00 15.46 ? 319 HIS B ND1 1 
ATOM   6762 C CD2 . HIS B 1 319 ? 21.446  -3.634  66.362  1.00 12.83 ? 319 HIS B CD2 1 
ATOM   6763 C CE1 . HIS B 1 319 ? 20.702  -1.965  67.578  1.00 11.20 ? 319 HIS B CE1 1 
ATOM   6764 N NE2 . HIS B 1 319 ? 21.800  -2.525  67.097  1.00 17.89 ? 319 HIS B NE2 1 
ATOM   6765 N N   . ALA B 1 320 ? 19.188  -2.008  64.060  1.00 16.38 ? 320 ALA B N   1 
ATOM   6766 C CA  . ALA B 1 320 ? 18.893  -0.585  64.032  1.00 15.86 ? 320 ALA B CA  1 
ATOM   6767 C C   . ALA B 1 320 ? 18.323  -0.132  62.696  1.00 15.35 ? 320 ALA B C   1 
ATOM   6768 O O   . ALA B 1 320 ? 18.160  1.071   62.489  1.00 24.15 ? 320 ALA B O   1 
ATOM   6769 C CB  . ALA B 1 320 ? 20.158  0.218   64.361  1.00 17.87 ? 320 ALA B CB  1 
ATOM   6770 N N   . TRP B 1 321 ? 18.046  -1.064  61.787  1.00 15.11 ? 321 TRP B N   1 
ATOM   6771 C CA  . TRP B 1 321 ? 17.483  -0.762  60.479  1.00 19.99 ? 321 TRP B CA  1 
ATOM   6772 C C   . TRP B 1 321 ? 16.050  -1.268  60.377  1.00 20.39 ? 321 TRP B C   1 
ATOM   6773 O O   . TRP B 1 321 ? 15.640  -2.204  61.067  1.00 20.72 ? 321 TRP B O   1 
ATOM   6774 C CB  . TRP B 1 321 ? 18.279  -1.429  59.349  1.00 10.06 ? 321 TRP B CB  1 
ATOM   6775 C CG  . TRP B 1 321 ? 19.697  -1.047  59.216  1.00 12.35 ? 321 TRP B CG  1 
ATOM   6776 C CD1 . TRP B 1 321 ? 20.626  -0.917  60.209  1.00 15.13 ? 321 TRP B CD1 1 
ATOM   6777 C CD2 . TRP B 1 321 ? 20.375  -0.782  57.987  1.00 13.69 ? 321 TRP B CD2 1 
ATOM   6778 N NE1 . TRP B 1 321 ? 21.845  -0.579  59.665  1.00 21.21 ? 321 TRP B NE1 1 
ATOM   6779 C CE2 . TRP B 1 321 ? 21.712  -0.486  58.302  1.00 16.46 ? 321 TRP B CE2 1 
ATOM   6780 C CE3 . TRP B 1 321 ? 19.974  -0.763  56.646  1.00 20.62 ? 321 TRP B CE3 1 
ATOM   6781 C CZ2 . TRP B 1 321 ? 22.657  -0.181  57.324  1.00 24.17 ? 321 TRP B CZ2 1 
ATOM   6782 C CZ3 . TRP B 1 321 ? 20.914  -0.461  55.676  1.00 20.15 ? 321 TRP B CZ3 1 
ATOM   6783 C CH2 . TRP B 1 321 ? 22.237  -0.172  56.023  1.00 17.13 ? 321 TRP B CH2 1 
ATOM   6784 N N   . ASN B 1 322 ? 15.314  -0.667  59.451  1.00 16.96 ? 322 ASN B N   1 
ATOM   6785 C CA  . ASN B 1 322 ? 14.076  -1.249  58.964  1.00 18.54 ? 322 ASN B CA  1 
ATOM   6786 C C   . ASN B 1 322 ? 14.402  -2.525  58.192  1.00 16.83 ? 322 ASN B C   1 
ATOM   6787 O O   . ASN B 1 322 ? 15.438  -2.620  57.525  1.00 15.10 ? 322 ASN B O   1 
ATOM   6788 C CB  . ASN B 1 322 ? 13.340  -0.201  58.111  1.00 24.35 ? 322 ASN B CB  1 
ATOM   6789 C CG  . ASN B 1 322 ? 12.404  -0.789  57.087  1.00 37.18 ? 322 ASN B CG  1 
ATOM   6790 O OD1 . ASN B 1 322 ? 12.838  -1.270  56.039  1.00 38.53 ? 322 ASN B OD1 1 
ATOM   6791 N ND2 . ASN B 1 322 ? 11.103  -0.700  57.355  1.00 42.34 ? 322 ASN B ND2 1 
ATOM   6792 N N   . ALA B 1 323 ? 13.522  -3.524  58.322  1.00 15.22 ? 323 ALA B N   1 
ATOM   6793 C CA  . ALA B 1 323 ? 13.795  -4.850  57.756  1.00 16.97 ? 323 ALA B CA  1 
ATOM   6794 C C   . ALA B 1 323 ? 14.062  -4.808  56.255  1.00 21.90 ? 323 ALA B C   1 
ATOM   6795 O O   . ALA B 1 323 ? 15.030  -5.417  55.773  1.00 15.49 ? 323 ALA B O   1 
ATOM   6796 C CB  . ALA B 1 323 ? 12.650  -5.820  58.078  1.00 18.34 ? 323 ALA B CB  1 
ATOM   6797 N N   . GLU B 1 324 ? 13.213  -4.128  55.498  1.00 15.83 ? 324 GLU B N   1 
ATOM   6798 C CA  . GLU B 1 324 ? 13.358  -4.169  54.057  1.00 14.96 ? 324 GLU B CA  1 
ATOM   6799 C C   . GLU B 1 324 ? 14.668  -3.498  53.620  1.00 18.60 ? 324 GLU B C   1 
ATOM   6800 O O   . GLU B 1 324 ? 15.406  -4.017  52.765  1.00 15.09 ? 324 GLU B O   1 
ATOM   6801 C CB  . GLU B 1 324 ? 12.136  -3.532  53.414  1.00 22.12 ? 324 GLU B CB  1 
ATOM   6802 C CG  . GLU B 1 324 ? 12.274  -3.920  51.929  1.00 39.53 ? 324 GLU B CG  1 
ATOM   6803 C CD  . GLU B 1 324 ? 12.780  -5.309  51.667  1.00 58.55 ? 324 GLU B CD  1 
ATOM   6804 O OE1 . GLU B 1 324 ? 12.043  -6.265  52.102  1.00 64.43 ? 324 GLU B OE1 1 
ATOM   6805 O OE2 . GLU B 1 324 ? 13.954  -5.429  51.172  1.00 65.16 ? 324 GLU B OE2 1 
ATOM   6806 N N   . ASP B 1 325 ? 14.978  -2.351  54.221  1.00 17.49 ? 325 ASP B N   1 
ATOM   6807 C CA  . ASP B 1 325 ? 16.217  -1.648  53.910  1.00 19.75 ? 325 ASP B CA  1 
ATOM   6808 C C   . ASP B 1 325 ? 17.434  -2.518  54.209  1.00 16.80 ? 325 ASP B C   1 
ATOM   6809 O O   . ASP B 1 325 ? 18.390  -2.544  53.433  1.00 13.49 ? 325 ASP B O   1 
ATOM   6810 C CB  . ASP B 1 325 ? 16.286  -0.344  54.707  1.00 26.51 ? 325 ASP B CB  1 
ATOM   6811 C CG  . ASP B 1 325 ? 15.246  0.668   54.266  1.00 35.43 ? 325 ASP B CG  1 
ATOM   6812 O OD1 . ASP B 1 325 ? 14.736  0.551   53.132  1.00 39.40 ? 325 ASP B OD1 1 
ATOM   6813 O OD2 . ASP B 1 325 ? 14.921  1.569   55.068  1.00 38.46 ? 325 ASP B OD2 1 
ATOM   6814 N N   . ALA B 1 326 ? 17.423  -3.229  55.340  1.00 12.70 ? 326 ALA B N   1 
ATOM   6815 C CA  . ALA B 1 326 ? 18.544  -4.094  55.678  1.00 8.96  ? 326 ALA B CA  1 
ATOM   6816 C C   . ALA B 1 326 ? 18.728  -5.204  54.646  1.00 15.03 ? 326 ALA B C   1 
ATOM   6817 O O   . ALA B 1 326 ? 19.857  -5.525  54.263  1.00 12.23 ? 326 ALA B O   1 
ATOM   6818 C CB  . ALA B 1 326 ? 18.335  -4.678  57.080  1.00 12.25 ? 326 ALA B CB  1 
ATOM   6819 N N   . VAL B 1 327 ? 17.635  -5.825  54.203  1.00 13.31 ? 327 VAL B N   1 
ATOM   6820 C CA  . VAL B 1 327 ? 17.752  -6.863  53.177  1.00 16.05 ? 327 VAL B CA  1 
ATOM   6821 C C   . VAL B 1 327 ? 18.311  -6.270  51.882  1.00 11.80 ? 327 VAL B C   1 
ATOM   6822 O O   . VAL B 1 327 ? 19.217  -6.840  51.262  1.00 13.46 ? 327 VAL B O   1 
ATOM   6823 C CB  . VAL B 1 327 ? 16.397  -7.554  52.953  1.00 15.35 ? 327 VAL B CB  1 
ATOM   6824 C CG1 . VAL B 1 327 ? 16.413  -8.390  51.656  1.00 17.39 ? 327 VAL B CG1 1 
ATOM   6825 C CG2 . VAL B 1 327 ? 16.049  -8.430  54.174  1.00 13.52 ? 327 VAL B CG2 1 
ATOM   6826 N N   . ARG B 1 328 ? 17.781  -5.116  51.462  1.00 17.97 ? 328 ARG B N   1 
ATOM   6827 C CA  . ARG B 1 328 ? 18.291  -4.438  50.267  1.00 18.31 ? 328 ARG B CA  1 
ATOM   6828 C C   . ARG B 1 328 ? 19.783  -4.173  50.377  1.00 20.53 ? 328 ARG B C   1 
ATOM   6829 O O   . ARG B 1 328 ? 20.530  -4.323  49.399  1.00 15.26 ? 328 ARG B O   1 
ATOM   6830 C CB  . ARG B 1 328 ? 17.559  -3.108  50.058  1.00 14.58 ? 328 ARG B CB  1 
ATOM   6831 C CG  . ARG B 1 328 ? 16.150  -3.238  49.517  1.00 24.13 ? 328 ARG B CG  1 
ATOM   6832 C CD  . ARG B 1 328 ? 15.388  -1.913  49.578  1.00 34.80 ? 328 ARG B CD  1 
ATOM   6833 N NE  . ARG B 1 328 ? 14.068  -2.037  48.967  1.00 33.64 ? 328 ARG B NE  1 
ATOM   6834 C CZ  . ARG B 1 328 ? 12.983  -1.401  49.394  1.00 40.33 ? 328 ARG B CZ  1 
ATOM   6835 N NH1 . ARG B 1 328 ? 13.055  -0.586  50.442  1.00 38.62 ? 328 ARG B NH1 1 
ATOM   6836 N NH2 . ARG B 1 328 ? 11.823  -1.581  48.773  1.00 34.19 ? 328 ARG B NH2 1 
ATOM   6837 N N   . ASP B 1 329 ? 20.222  -3.715  51.548  1.00 17.94 ? 329 ASP B N   1 
ATOM   6838 C CA  . ASP B 1 329 ? 21.636  -3.455  51.763  1.00 16.00 ? 329 ASP B CA  1 
ATOM   6839 C C   . ASP B 1 329 ? 22.453  -4.734  51.618  1.00 16.77 ? 329 ASP B C   1 
ATOM   6840 O O   . ASP B 1 329 ? 23.473  -4.757  50.919  1.00 20.37 ? 329 ASP B O   1 
ATOM   6841 C CB  . ASP B 1 329 ? 21.832  -2.831  53.146  1.00 10.08 ? 329 ASP B CB  1 
ATOM   6842 C CG  . ASP B 1 329 ? 23.286  -2.507  53.423  1.00 22.21 ? 329 ASP B CG  1 
ATOM   6843 O OD1 . ASP B 1 329 ? 23.751  -1.480  52.892  1.00 27.71 ? 329 ASP B OD1 1 
ATOM   6844 O OD2 . ASP B 1 329 ? 23.962  -3.291  54.126  1.00 19.32 ? 329 ASP B OD2 1 
ATOM   6845 N N   . PHE B 1 330 ? 21.998  -5.817  52.261  1.00 8.75  ? 330 PHE B N   1 
ATOM   6846 C CA  . PHE B 1 330 ? 22.707  -7.096  52.237  1.00 9.44  ? 330 PHE B CA  1 
ATOM   6847 C C   . PHE B 1 330 ? 22.798  -7.660  50.822  1.00 18.03 ? 330 PHE B C   1 
ATOM   6848 O O   . PHE B 1 330 ? 23.872  -8.088  50.371  1.00 17.65 ? 330 PHE B O   1 
ATOM   6849 C CB  . PHE B 1 330 ? 21.979  -8.080  53.166  1.00 9.97  ? 330 PHE B CB  1 
ATOM   6850 C CG  . PHE B 1 330 ? 22.756  -9.331  53.492  1.00 12.09 ? 330 PHE B CG  1 
ATOM   6851 C CD1 . PHE B 1 330 ? 23.693  -9.331  54.516  1.00 16.21 ? 330 PHE B CD1 1 
ATOM   6852 C CD2 . PHE B 1 330 ? 22.500  -10.522 52.819  1.00 12.66 ? 330 PHE B CD2 1 
ATOM   6853 C CE1 . PHE B 1 330 ? 24.393  -10.476 54.845  1.00 17.54 ? 330 PHE B CE1 1 
ATOM   6854 C CE2 . PHE B 1 330 ? 23.206  -11.689 53.146  1.00 16.18 ? 330 PHE B CE2 1 
ATOM   6855 C CZ  . PHE B 1 330 ? 24.148  -11.662 54.157  1.00 20.00 ? 330 PHE B CZ  1 
ATOM   6856 N N   . ILE B 1 331 ? 21.665  -7.702  50.119  1.00 17.54 ? 331 ILE B N   1 
ATOM   6857 C CA  . ILE B 1 331 ? 21.665  -8.193  48.743  1.00 17.99 ? 331 ILE B CA  1 
ATOM   6858 C C   . ILE B 1 331 ? 22.566  -7.331  47.865  1.00 15.55 ? 331 ILE B C   1 
ATOM   6859 O O   . ILE B 1 331 ? 23.292  -7.843  47.003  1.00 19.30 ? 331 ILE B O   1 
ATOM   6860 C CB  . ILE B 1 331 ? 20.226  -8.242  48.206  1.00 18.10 ? 331 ILE B CB  1 
ATOM   6861 C CG1 . ILE B 1 331 ? 19.395  -9.219  49.044  1.00 19.68 ? 331 ILE B CG1 1 
ATOM   6862 C CG2 . ILE B 1 331 ? 20.206  -8.616  46.716  1.00 15.33 ? 331 ILE B CG2 1 
ATOM   6863 C CD1 . ILE B 1 331 ? 19.777  -10.684 48.851  1.00 18.04 ? 331 ILE B CD1 1 
ATOM   6864 N N   . GLY B 1 332 ? 22.533  -6.010  48.067  1.00 15.79 ? 332 GLY B N   1 
ATOM   6865 C CA  . GLY B 1 332 ? 23.342  -5.129  47.243  1.00 13.60 ? 332 GLY B CA  1 
ATOM   6866 C C   . GLY B 1 332 ? 24.821  -5.350  47.451  1.00 16.96 ? 332 GLY B C   1 
ATOM   6867 O O   . GLY B 1 332 ? 25.617  -5.187  46.517  1.00 14.19 ? 332 GLY B O   1 
ATOM   6868 N N   . ARG B 1 333 ? 25.210  -5.740  48.669  1.00 12.44 ? 333 ARG B N   1 
ATOM   6869 C CA  . ARG B 1 333 ? 26.605  -6.055  48.933  1.00 16.39 ? 333 ARG B CA  1 
ATOM   6870 C C   . ARG B 1 333 ? 26.999  -7.369  48.276  1.00 16.60 ? 333 ARG B C   1 
ATOM   6871 O O   . ARG B 1 333 ? 28.108  -7.496  47.749  1.00 14.70 ? 333 ARG B O   1 
ATOM   6872 C CB  . ARG B 1 333 ? 26.850  -6.101  50.443  1.00 15.31 ? 333 ARG B CB  1 
ATOM   6873 C CG  . ARG B 1 333 ? 26.806  -4.726  51.101  1.00 13.72 ? 333 ARG B CG  1 
ATOM   6874 C CD  . ARG B 1 333 ? 26.830  -4.852  52.623  1.00 17.14 ? 333 ARG B CD  1 
ATOM   6875 N NE  . ARG B 1 333 ? 26.732  -3.553  53.299  1.00 15.16 ? 333 ARG B NE  1 
ATOM   6876 C CZ  . ARG B 1 333 ? 27.785  -2.792  53.597  1.00 20.45 ? 333 ARG B CZ  1 
ATOM   6877 N NH1 . ARG B 1 333 ? 29.011  -3.180  53.261  1.00 18.69 ? 333 ARG B NH1 1 
ATOM   6878 N NH2 . ARG B 1 333 ? 27.620  -1.633  54.220  1.00 23.00 ? 333 ARG B NH2 1 
ATOM   6879 N N   . LEU B 1 334 ? 26.104  -8.356  48.297  1.00 13.63 ? 334 LEU B N   1 
ATOM   6880 C CA  . LEU B 1 334 ? 26.366  -9.595  47.578  1.00 13.44 ? 334 LEU B CA  1 
ATOM   6881 C C   . LEU B 1 334 ? 26.502  -9.334  46.082  1.00 14.26 ? 334 LEU B C   1 
ATOM   6882 O O   . LEU B 1 334 ? 27.371  -9.910  45.414  1.00 13.81 ? 334 LEU B O   1 
ATOM   6883 C CB  . LEU B 1 334 ? 25.249  -10.600 47.851  1.00 9.12  ? 334 LEU B CB  1 
ATOM   6884 C CG  . LEU B 1 334 ? 25.131  -11.093 49.310  1.00 10.66 ? 334 LEU B CG  1 
ATOM   6885 C CD1 . LEU B 1 334 ? 23.908  -11.989 49.500  1.00 17.26 ? 334 LEU B CD1 1 
ATOM   6886 C CD2 . LEU B 1 334 ? 26.398  -11.829 49.762  1.00 11.64 ? 334 LEU B CD2 1 
ATOM   6887 N N   . LYS B 1 335 ? 25.643  -8.476  45.534  1.00 11.81 ? 335 LYS B N   1 
ATOM   6888 C CA  . LYS B 1 335 ? 25.758  -8.145  44.115  1.00 20.99 ? 335 LYS B CA  1 
ATOM   6889 C C   . LYS B 1 335 ? 27.131  -7.568  43.795  1.00 21.60 ? 335 LYS B C   1 
ATOM   6890 O O   . LYS B 1 335 ? 27.708  -7.867  42.742  1.00 19.70 ? 335 LYS B O   1 
ATOM   6891 C CB  . LYS B 1 335 ? 24.651  -7.167  43.705  1.00 19.54 ? 335 LYS B CB  1 
ATOM   6892 C CG  . LYS B 1 335 ? 24.461  -7.075  42.189  1.00 36.71 ? 335 LYS B CG  1 
ATOM   6893 C CD  . LYS B 1 335 ? 23.410  -6.038  41.801  1.00 41.81 ? 335 LYS B CD  1 
ATOM   6894 C CE  . LYS B 1 335 ? 23.441  -5.753  40.303  1.00 46.05 ? 335 LYS B CE  1 
ATOM   6895 N NZ  . LYS B 1 335 ? 23.049  -4.351  39.976  1.00 48.76 ? 335 LYS B NZ  1 
ATOM   6896 N N   . LYS B 1 336 ? 27.668  -6.731  44.683  1.00 22.31 ? 336 LYS B N   1 
ATOM   6897 C CA  . LYS B 1 336 ? 28.979  -6.139  44.432  1.00 19.62 ? 336 LYS B CA  1 
ATOM   6898 C C   . LYS B 1 336 ? 30.073  -7.195  44.459  1.00 19.01 ? 336 LYS B C   1 
ATOM   6899 O O   . LYS B 1 336 ? 30.958  -7.203  43.599  1.00 22.75 ? 336 LYS B O   1 
ATOM   6900 C CB  . LYS B 1 336 ? 29.273  -5.047  45.455  1.00 24.42 ? 336 LYS B CB  1 
ATOM   6901 C CG  . LYS B 1 336 ? 28.636  -3.711  45.123  1.00 29.84 ? 336 LYS B CG  1 
ATOM   6902 C CD  . LYS B 1 336 ? 28.918  -2.674  46.204  1.00 42.83 ? 336 LYS B CD  1 
ATOM   6903 C CE  . LYS B 1 336 ? 28.199  -1.359  45.898  1.00 50.69 ? 336 LYS B CE  1 
ATOM   6904 N NZ  . LYS B 1 336 ? 27.962  -0.548  47.127  1.00 50.92 ? 336 LYS B NZ  1 
ATOM   6905 N N   . ILE B 1 337 ? 30.043  -8.082  45.457  1.00 17.63 ? 337 ILE B N   1 
ATOM   6906 C CA  . ILE B 1 337 ? 30.986  -9.198  45.493  1.00 15.35 ? 337 ILE B CA  1 
ATOM   6907 C C   . ILE B 1 337 ? 30.875  -10.020 44.214  1.00 20.44 ? 337 ILE B C   1 
ATOM   6908 O O   . ILE B 1 337 ? 31.880  -10.370 43.579  1.00 21.29 ? 337 ILE B O   1 
ATOM   6909 C CB  . ILE B 1 337 ? 30.735  -10.072 46.736  1.00 15.99 ? 337 ILE B CB  1 
ATOM   6910 C CG1 . ILE B 1 337 ? 30.947  -9.269  48.022  1.00 16.20 ? 337 ILE B CG1 1 
ATOM   6911 C CG2 . ILE B 1 337 ? 31.629  -11.304 46.701  1.00 14.39 ? 337 ILE B CG2 1 
ATOM   6912 C CD1 . ILE B 1 337 ? 30.445  -9.978  49.280  1.00 16.14 ? 337 ILE B CD1 1 
ATOM   6913 N N   . HIS B 1 338 ? 29.641  -10.358 43.836  1.00 15.09 ? 338 HIS B N   1 
ATOM   6914 C CA  . HIS B 1 338 ? 29.378  -11.121 42.621  1.00 17.64 ? 338 HIS B CA  1 
ATOM   6915 C C   . HIS B 1 338 ? 30.030  -10.479 41.394  1.00 17.33 ? 338 HIS B C   1 
ATOM   6916 O O   . HIS B 1 338 ? 30.629  -11.172 40.560  1.00 21.32 ? 338 HIS B O   1 
ATOM   6917 C CB  . HIS B 1 338 ? 27.861  -11.230 42.443  1.00 11.88 ? 338 HIS B CB  1 
ATOM   6918 C CG  . HIS B 1 338 ? 27.438  -11.994 41.232  1.00 18.58 ? 338 HIS B CG  1 
ATOM   6919 N ND1 . HIS B 1 338 ? 26.665  -11.436 40.237  1.00 26.41 ? 338 HIS B ND1 1 
ATOM   6920 C CD2 . HIS B 1 338 ? 27.643  -13.283 40.872  1.00 24.30 ? 338 HIS B CD2 1 
ATOM   6921 C CE1 . HIS B 1 338 ? 26.428  -12.344 39.307  1.00 26.55 ? 338 HIS B CE1 1 
ATOM   6922 N NE2 . HIS B 1 338 ? 27.005  -13.475 39.672  1.00 24.80 ? 338 HIS B NE2 1 
ATOM   6923 N N   . GLU B 1 339 ? 29.935  -9.158  41.274  1.00 19.19 ? 339 GLU B N   1 
ATOM   6924 C CA  . GLU B 1 339 ? 30.496  -8.464  40.118  1.00 24.90 ? 339 GLU B CA  1 
ATOM   6925 C C   . GLU B 1 339 ? 31.989  -8.185  40.240  1.00 25.48 ? 339 GLU B C   1 
ATOM   6926 O O   . GLU B 1 339 ? 32.610  -7.828  39.234  1.00 25.21 ? 339 GLU B O   1 
ATOM   6927 C CB  . GLU B 1 339 ? 29.769  -7.135  39.884  1.00 19.80 ? 339 GLU B CB  1 
ATOM   6928 C CG  . GLU B 1 339 ? 28.273  -7.266  39.646  1.00 27.11 ? 339 GLU B CG  1 
ATOM   6929 C CD  . GLU B 1 339 ? 27.562  -5.945  39.832  1.00 41.32 ? 339 GLU B CD  1 
ATOM   6930 O OE1 . GLU B 1 339 ? 28.174  -5.020  40.411  1.00 44.69 ? 339 GLU B OE1 1 
ATOM   6931 O OE2 . GLU B 1 339 ? 26.399  -5.824  39.397  1.00 48.31 ? 339 GLU B OE2 1 
ATOM   6932 N N   . SER B 1 340 ? 32.572  -8.338  41.431  1.00 19.42 ? 340 SER B N   1 
ATOM   6933 C CA  . SER B 1 340 ? 33.936  -7.893  41.698  1.00 21.37 ? 340 SER B CA  1 
ATOM   6934 C C   . SER B 1 340 ? 34.994  -8.899  41.274  1.00 23.41 ? 340 SER B C   1 
ATOM   6935 O O   . SER B 1 340 ? 36.183  -8.555  41.269  1.00 23.27 ? 340 SER B O   1 
ATOM   6936 C CB  . SER B 1 340 ? 34.121  -7.617  43.192  1.00 28.15 ? 340 SER B CB  1 
ATOM   6937 O OG  . SER B 1 340 ? 34.303  -8.846  43.893  1.00 26.53 ? 340 SER B OG  1 
ATOM   6938 N N   . VAL B 1 341 ? 34.604  -10.134 40.967  1.00 22.76 ? 341 VAL B N   1 
ATOM   6939 C CA  . VAL B 1 341 ? 35.539  -11.193 40.608  1.00 25.56 ? 341 VAL B CA  1 
ATOM   6940 C C   . VAL B 1 341 ? 34.918  -12.010 39.485  1.00 24.47 ? 341 VAL B C   1 
ATOM   6941 O O   . VAL B 1 341 ? 33.698  -12.064 39.329  1.00 22.14 ? 341 VAL B O   1 
ATOM   6942 C CB  . VAL B 1 341 ? 35.889  -12.109 41.804  1.00 26.28 ? 341 VAL B CB  1 
ATOM   6943 C CG1 . VAL B 1 341 ? 36.549  -11.301 42.930  1.00 22.59 ? 341 VAL B CG1 1 
ATOM   6944 C CG2 . VAL B 1 341 ? 34.644  -12.846 42.304  1.00 25.87 ? 341 VAL B CG2 1 
ATOM   6945 N N   . ASP B 1 342 ? 35.776  -12.648 38.693  1.00 21.13 ? 342 ASP B N   1 
ATOM   6946 C CA  . ASP B 1 342 ? 35.306  -13.463 37.583  1.00 27.28 ? 342 ASP B CA  1 
ATOM   6947 C C   . ASP B 1 342 ? 35.278  -14.949 37.914  1.00 27.12 ? 342 ASP B C   1 
ATOM   6948 O O   . ASP B 1 342 ? 34.915  -15.755 37.053  1.00 33.44 ? 342 ASP B O   1 
ATOM   6949 C CB  . ASP B 1 342 ? 36.156  -13.208 36.329  1.00 37.65 ? 342 ASP B CB  1 
ATOM   6950 C CG  . ASP B 1 342 ? 37.642  -13.170 36.619  1.00 50.24 ? 342 ASP B CG  1 
ATOM   6951 O OD1 . ASP B 1 342 ? 38.040  -13.291 37.801  1.00 56.36 ? 342 ASP B OD1 1 
ATOM   6952 O OD2 . ASP B 1 342 ? 38.416  -13.013 35.649  1.00 54.70 ? 342 ASP B OD2 1 
ATOM   6953 N N   . PHE B 1 343 ? 35.645  -15.334 39.131  1.00 23.36 ? 343 PHE B N   1 
ATOM   6954 C CA  . PHE B 1 343 ? 35.406  -16.692 39.583  1.00 15.43 ? 343 PHE B CA  1 
ATOM   6955 C C   . PHE B 1 343 ? 34.158  -16.700 40.461  1.00 19.66 ? 343 PHE B C   1 
ATOM   6956 O O   . PHE B 1 343 ? 33.493  -15.682 40.648  1.00 16.83 ? 343 PHE B O   1 
ATOM   6957 C CB  . PHE B 1 343 ? 36.613  -17.262 40.325  1.00 16.44 ? 343 PHE B CB  1 
ATOM   6958 C CG  . PHE B 1 343 ? 37.059  -16.442 41.504  1.00 15.88 ? 343 PHE B CG  1 
ATOM   6959 C CD1 . PHE B 1 343 ? 37.943  -15.383 41.337  1.00 25.11 ? 343 PHE B CD1 1 
ATOM   6960 C CD2 . PHE B 1 343 ? 36.620  -16.744 42.781  1.00 15.30 ? 343 PHE B CD2 1 
ATOM   6961 C CE1 . PHE B 1 343 ? 38.368  -14.627 42.423  1.00 16.70 ? 343 PHE B CE1 1 
ATOM   6962 C CE2 . PHE B 1 343 ? 37.046  -15.993 43.875  1.00 14.69 ? 343 PHE B CE2 1 
ATOM   6963 C CZ  . PHE B 1 343 ? 37.920  -14.941 43.698  1.00 22.36 ? 343 PHE B CZ  1 
ATOM   6964 N N   . GLN B 1 344 ? 33.842  -17.867 41.010  1.00 12.35 ? 344 GLN B N   1 
ATOM   6965 C CA  . GLN B 1 344 ? 32.656  -18.009 41.840  1.00 11.46 ? 344 GLN B CA  1 
ATOM   6966 C C   . GLN B 1 344 ? 33.048  -17.904 43.310  1.00 11.83 ? 344 GLN B C   1 
ATOM   6967 O O   . GLN B 1 344 ? 33.605  -18.861 43.870  1.00 14.50 ? 344 GLN B O   1 
ATOM   6968 C CB  . GLN B 1 344 ? 31.956  -19.341 41.561  1.00 9.45  ? 344 GLN B CB  1 
ATOM   6969 C CG  . GLN B 1 344 ? 31.436  -19.476 40.114  1.00 15.59 ? 344 GLN B CG  1 
ATOM   6970 C CD  . GLN B 1 344 ? 30.639  -20.749 39.895  1.00 17.87 ? 344 GLN B CD  1 
ATOM   6971 O OE1 . GLN B 1 344 ? 29.478  -20.702 39.485  1.00 26.97 ? 344 GLN B OE1 1 
ATOM   6972 N NE2 . GLN B 1 344 ? 31.251  -21.889 40.169  1.00 23.09 ? 344 GLN B NE2 1 
ATOM   6973 N N   . PRO B 1 345 ? 32.794  -16.771 43.963  1.00 13.07 ? 345 PRO B N   1 
ATOM   6974 C CA  . PRO B 1 345 ? 33.232  -16.598 45.352  1.00 15.28 ? 345 PRO B CA  1 
ATOM   6975 C C   . PRO B 1 345 ? 32.374  -17.401 46.310  1.00 13.59 ? 345 PRO B C   1 
ATOM   6976 O O   . PRO B 1 345 ? 31.179  -17.626 46.075  1.00 11.13 ? 345 PRO B O   1 
ATOM   6977 C CB  . PRO B 1 345 ? 33.040  -15.098 45.592  1.00 12.51 ? 345 PRO B CB  1 
ATOM   6978 C CG  . PRO B 1 345 ? 31.845  -14.758 44.737  1.00 12.13 ? 345 PRO B CG  1 
ATOM   6979 C CD  . PRO B 1 345 ? 31.959  -15.647 43.497  1.00 11.56 ? 345 PRO B CD  1 
ATOM   6980 N N   . VAL B 1 346 ? 33.000  -17.812 47.412  1.00 12.63 ? 346 VAL B N   1 
ATOM   6981 C CA  . VAL B 1 346 ? 32.311  -18.434 48.541  1.00 8.97  ? 346 VAL B CA  1 
ATOM   6982 C C   . VAL B 1 346 ? 32.284  -17.428 49.684  1.00 14.05 ? 346 VAL B C   1 
ATOM   6983 O O   . VAL B 1 346 ? 33.335  -16.987 50.169  1.00 13.50 ? 346 VAL B O   1 
ATOM   6984 C CB  . VAL B 1 346 ? 32.980  -19.742 48.970  1.00 11.80 ? 346 VAL B CB  1 
ATOM   6985 C CG1 . VAL B 1 346 ? 32.097  -20.448 50.009  1.00 15.76 ? 346 VAL B CG1 1 
ATOM   6986 C CG2 . VAL B 1 346 ? 33.197  -20.629 47.742  1.00 9.59  ? 346 VAL B CG2 1 
ATOM   6987 N N   . VAL B 1 347 ? 31.081  -17.087 50.121  1.00 7.31  ? 347 VAL B N   1 
ATOM   6988 C CA  . VAL B 1 347 ? 30.849  -16.042 51.101  1.00 8.01  ? 347 VAL B CA  1 
ATOM   6989 C C   . VAL B 1 347 ? 30.285  -16.700 52.351  1.00 10.69 ? 347 VAL B C   1 
ATOM   6990 O O   . VAL B 1 347 ? 29.107  -17.080 52.368  1.00 12.00 ? 347 VAL B O   1 
ATOM   6991 C CB  . VAL B 1 347 ? 29.882  -14.984 50.564  1.00 12.43 ? 347 VAL B CB  1 
ATOM   6992 C CG1 . VAL B 1 347 ? 29.713  -13.860 51.582  1.00 12.92 ? 347 VAL B CG1 1 
ATOM   6993 C CG2 . VAL B 1 347 ? 30.400  -14.451 49.210  1.00 10.13 ? 347 VAL B CG2 1 
ATOM   6994 N N   . PHE B 1 348 ? 31.101  -16.806 53.401  1.00 9.69  ? 348 PHE B N   1 
ATOM   6995 C CA  . PHE B 1 348 ? 30.672  -17.389 54.670  1.00 14.53 ? 348 PHE B CA  1 
ATOM   6996 C C   . PHE B 1 348 ? 30.156  -16.289 55.585  1.00 8.06  ? 348 PHE B C   1 
ATOM   6997 O O   . PHE B 1 348 ? 30.856  -15.305 55.845  1.00 9.85  ? 348 PHE B O   1 
ATOM   6998 C CB  . PHE B 1 348 ? 31.812  -18.137 55.374  1.00 11.17 ? 348 PHE B CB  1 
ATOM   6999 C CG  . PHE B 1 348 ? 31.847  -19.621 55.098  1.00 14.50 ? 348 PHE B CG  1 
ATOM   7000 C CD1 . PHE B 1 348 ? 32.131  -20.099 53.821  1.00 8.36  ? 348 PHE B CD1 1 
ATOM   7001 C CD2 . PHE B 1 348 ? 31.620  -20.535 56.123  1.00 14.38 ? 348 PHE B CD2 1 
ATOM   7002 C CE1 . PHE B 1 348 ? 32.171  -21.476 53.561  1.00 9.38  ? 348 PHE B CE1 1 
ATOM   7003 C CE2 . PHE B 1 348 ? 31.671  -21.912 55.894  1.00 12.60 ? 348 PHE B CE2 1 
ATOM   7004 C CZ  . PHE B 1 348 ? 31.938  -22.391 54.591  1.00 9.49  ? 348 PHE B CZ  1 
ATOM   7005 N N   . VAL B 1 349 ? 28.940  -16.471 56.077  1.00 10.02 ? 349 VAL B N   1 
ATOM   7006 C CA  . VAL B 1 349 ? 28.315  -15.568 57.031  1.00 9.35  ? 349 VAL B CA  1 
ATOM   7007 C C   . VAL B 1 349 ? 28.178  -16.372 58.317  1.00 11.92 ? 349 VAL B C   1 
ATOM   7008 O O   . VAL B 1 349 ? 27.334  -17.274 58.401  1.00 8.41  ? 349 VAL B O   1 
ATOM   7009 C CB  . VAL B 1 349 ? 26.950  -15.069 56.528  1.00 8.25  ? 349 VAL B CB  1 
ATOM   7010 C CG1 . VAL B 1 349 ? 26.311  -14.124 57.544  1.00 10.26 ? 349 VAL B CG1 1 
ATOM   7011 C CG2 . VAL B 1 349 ? 27.084  -14.387 55.161  1.00 13.32 ? 349 VAL B CG2 1 
ATOM   7012 N N   . VAL B 1 350 ? 29.031  -16.095 59.305  1.00 8.02  ? 350 VAL B N   1 
ATOM   7013 C CA  . VAL B 1 350 ? 29.135  -16.925 60.500  1.00 6.87  ? 350 VAL B CA  1 
ATOM   7014 C C   . VAL B 1 350 ? 29.006  -16.026 61.716  1.00 8.52  ? 350 VAL B C   1 
ATOM   7015 O O   . VAL B 1 350 ? 29.758  -15.055 61.850  1.00 10.86 ? 350 VAL B O   1 
ATOM   7016 C CB  . VAL B 1 350 ? 30.478  -17.684 60.571  1.00 10.04 ? 350 VAL B CB  1 
ATOM   7017 C CG1 . VAL B 1 350 ? 30.484  -18.642 61.786  1.00 5.97  ? 350 VAL B CG1 1 
ATOM   7018 C CG2 . VAL B 1 350 ? 30.807  -18.429 59.258  1.00 8.78  ? 350 VAL B CG2 1 
ATOM   7019 N N   . LEU B 1 351 ? 28.075  -16.352 62.609  1.00 9.68  ? 351 LEU B N   1 
ATOM   7020 C CA  . LEU B 1 351 ? 27.883  -15.534 63.802  1.00 9.20  ? 351 LEU B CA  1 
ATOM   7021 C C   . LEU B 1 351 ? 27.025  -16.318 64.790  1.00 11.27 ? 351 LEU B C   1 
ATOM   7022 O O   . LEU B 1 351 ? 26.487  -17.375 64.453  1.00 6.01  ? 351 LEU B O   1 
ATOM   7023 C CB  . LEU B 1 351 ? 27.240  -14.186 63.444  1.00 8.47  ? 351 LEU B CB  1 
ATOM   7024 C CG  . LEU B 1 351 ? 25.863  -14.211 62.774  1.00 9.69  ? 351 LEU B CG  1 
ATOM   7025 C CD1 . LEU B 1 351 ? 25.060  -12.981 63.182  1.00 11.98 ? 351 LEU B CD1 1 
ATOM   7026 C CD2 . LEU B 1 351 ? 25.962  -14.313 61.246  1.00 11.15 ? 351 LEU B CD2 1 
ATOM   7027 N N   . ASP B 1 352 ? 26.916  -15.801 66.021  1.00 7.58  ? 352 ASP B N   1 
ATOM   7028 C CA  . ASP B 1 352 ? 25.972  -16.369 66.984  1.00 11.77 ? 352 ASP B CA  1 
ATOM   7029 C C   . ASP B 1 352 ? 24.571  -16.422 66.375  1.00 13.00 ? 352 ASP B C   1 
ATOM   7030 O O   . ASP B 1 352 ? 24.117  -15.462 65.757  1.00 8.00  ? 352 ASP B O   1 
ATOM   7031 C CB  . ASP B 1 352 ? 25.935  -15.537 68.268  1.00 11.07 ? 352 ASP B CB  1 
ATOM   7032 C CG  . ASP B 1 352 ? 27.245  -15.544 69.023  1.00 14.53 ? 352 ASP B CG  1 
ATOM   7033 O OD1 . ASP B 1 352 ? 28.198  -16.256 68.618  1.00 13.28 ? 352 ASP B OD1 1 
ATOM   7034 O OD2 . ASP B 1 352 ? 27.289  -14.847 70.057  1.00 16.03 ? 352 ASP B OD2 1 
ATOM   7035 N N   . GLY B 1 353 ? 23.895  -17.556 66.543  1.00 7.09  ? 353 GLY B N   1 
ATOM   7036 C CA  . GLY B 1 353 ? 22.586  -17.799 65.968  1.00 9.79  ? 353 GLY B CA  1 
ATOM   7037 C C   . GLY B 1 353 ? 21.406  -17.404 66.831  1.00 9.56  ? 353 GLY B C   1 
ATOM   7038 O O   . GLY B 1 353 ? 20.260  -17.520 66.383  1.00 11.14 ? 353 GLY B O   1 
ATOM   7039 N N   . GLU B 1 354 ? 21.632  -16.950 68.072  1.00 7.55  ? 354 GLU B N   1 
ATOM   7040 C CA  . GLU B 1 354 ? 20.524  -16.715 68.990  1.00 5.73  ? 354 GLU B CA  1 
ATOM   7041 C C   . GLU B 1 354 ? 20.600  -15.387 69.725  1.00 13.22 ? 354 GLU B C   1 
ATOM   7042 O O   . GLU B 1 354 ? 19.601  -14.985 70.333  1.00 8.30  ? 354 GLU B O   1 
ATOM   7043 C CB  . GLU B 1 354 ? 20.429  -17.855 70.037  1.00 3.91  ? 354 GLU B CB  1 
ATOM   7044 C CG  . GLU B 1 354 ? 21.408  -17.749 71.217  1.00 5.23  ? 354 GLU B CG  1 
ATOM   7045 C CD  . GLU B 1 354 ? 22.819  -18.252 70.867  1.00 7.67  ? 354 GLU B CD  1 
ATOM   7046 O OE1 . GLU B 1 354 ? 23.220  -19.326 71.389  1.00 7.83  ? 354 GLU B OE1 1 
ATOM   7047 O OE2 . GLU B 1 354 ? 23.531  -17.587 70.075  1.00 9.24  ? 354 GLU B OE2 1 
ATOM   7048 N N   . ASN B 1 355 ? 21.720  -14.678 69.678  1.00 8.99  ? 355 ASN B N   1 
ATOM   7049 C CA  . ASN B 1 355 ? 21.865  -13.535 70.569  1.00 14.17 ? 355 ASN B CA  1 
ATOM   7050 C C   . ASN B 1 355 ? 21.436  -12.200 69.971  1.00 11.73 ? 355 ASN B C   1 
ATOM   7051 O O   . ASN B 1 355 ? 21.164  -11.261 70.735  1.00 12.81 ? 355 ASN B O   1 
ATOM   7052 C CB  . ASN B 1 355 ? 23.315  -13.454 71.059  1.00 13.61 ? 355 ASN B CB  1 
ATOM   7053 C CG  . ASN B 1 355 ? 23.632  -14.552 72.059  1.00 12.84 ? 355 ASN B CG  1 
ATOM   7054 O OD1 . ASN B 1 355 ? 22.768  -14.933 72.849  1.00 17.53 ? 355 ASN B OD1 1 
ATOM   7055 N ND2 . ASN B 1 355 ? 24.839  -15.100 71.999  1.00 15.12 ? 355 ASN B ND2 1 
ATOM   7056 N N   . CYS B 1 356 ? 21.392  -12.058 68.641  1.00 12.18 ? 356 CYS B N   1 
ATOM   7057 C CA  . CYS B 1 356 ? 21.103  -10.732 68.096  1.00 11.68 ? 356 CYS B CA  1 
ATOM   7058 C C   . CYS B 1 356 ? 19.613  -10.443 67.973  1.00 14.23 ? 356 CYS B C   1 
ATOM   7059 O O   . CYS B 1 356 ? 19.228  -9.274  67.955  1.00 10.18 ? 356 CYS B O   1 
ATOM   7060 C CB  . CYS B 1 356 ? 21.754  -10.542 66.717  1.00 8.03  ? 356 CYS B CB  1 
ATOM   7061 S SG  . CYS B 1 356 ? 21.342  -11.797 65.486  1.00 11.22 ? 356 CYS B SG  1 
ATOM   7062 N N   . TRP B 1 357 ? 18.768  -11.465 67.887  1.00 11.40 ? 357 TRP B N   1 
ATOM   7063 C CA  . TRP B 1 357 ? 17.387  -11.224 67.461  1.00 9.65  ? 357 TRP B CA  1 
ATOM   7064 C C   . TRP B 1 357 ? 16.572  -10.445 68.489  1.00 7.67  ? 357 TRP B C   1 
ATOM   7065 O O   . TRP B 1 357 ? 15.631  -9.741  68.104  1.00 10.20 ? 357 TRP B O   1 
ATOM   7066 C CB  . TRP B 1 357 ? 16.723  -12.561 67.130  1.00 5.12  ? 357 TRP B CB  1 
ATOM   7067 C CG  . TRP B 1 357 ? 17.607  -13.389 66.247  1.00 9.26  ? 357 TRP B CG  1 
ATOM   7068 C CD1 . TRP B 1 357 ? 18.154  -14.613 66.540  1.00 6.93  ? 357 TRP B CD1 1 
ATOM   7069 C CD2 . TRP B 1 357 ? 18.063  -13.045 64.934  1.00 8.57  ? 357 TRP B CD2 1 
ATOM   7070 N NE1 . TRP B 1 357 ? 18.906  -15.054 65.474  1.00 6.85  ? 357 TRP B NE1 1 
ATOM   7071 C CE2 . TRP B 1 357 ? 18.874  -14.102 64.482  1.00 7.68  ? 357 TRP B CE2 1 
ATOM   7072 C CE3 . TRP B 1 357 ? 17.853  -11.947 64.089  1.00 9.34  ? 357 TRP B CE3 1 
ATOM   7073 C CZ2 . TRP B 1 357 ? 19.503  -14.084 63.220  1.00 11.66 ? 357 TRP B CZ2 1 
ATOM   7074 C CZ3 . TRP B 1 357 ? 18.475  -11.936 62.823  1.00 8.75  ? 357 TRP B CZ3 1 
ATOM   7075 C CH2 . TRP B 1 357 ? 19.284  -13.005 62.412  1.00 11.37 ? 357 TRP B CH2 1 
ATOM   7076 N N   . GLU B 1 358 ? 16.909  -10.548 69.783  1.00 7.90  ? 358 GLU B N   1 
ATOM   7077 C CA  . GLU B 1 358 ? 16.142  -9.835  70.808  1.00 11.58 ? 358 GLU B CA  1 
ATOM   7078 C C   . GLU B 1 358 ? 16.189  -8.324  70.633  1.00 7.37  ? 358 GLU B C   1 
ATOM   7079 O O   . GLU B 1 358 ? 15.327  -7.628  71.194  1.00 12.04 ? 358 GLU B O   1 
ATOM   7080 C CB  . GLU B 1 358 ? 16.628  -10.180 72.219  1.00 8.07  ? 358 GLU B CB  1 
ATOM   7081 C CG  . GLU B 1 358 ? 18.096  -9.856  72.524  1.00 7.91  ? 358 GLU B CG  1 
ATOM   7082 C CD  . GLU B 1 358 ? 18.649  -10.798 73.575  1.00 15.39 ? 358 GLU B CD  1 
ATOM   7083 O OE1 . GLU B 1 358 ? 19.075  -10.322 74.651  1.00 18.18 ? 358 GLU B OE1 1 
ATOM   7084 O OE2 . GLU B 1 358 ? 18.611  -12.027 73.329  1.00 14.04 ? 358 GLU B OE2 1 
ATOM   7085 N N   . TYR B 1 359 ? 17.168  -7.808  69.875  1.00 10.08 ? 359 TYR B N   1 
ATOM   7086 C CA  . TYR B 1 359 ? 17.321  -6.378  69.610  1.00 14.69 ? 359 TYR B CA  1 
ATOM   7087 C C   . TYR B 1 359 ? 16.654  -5.940  68.311  1.00 13.25 ? 359 TYR B C   1 
ATOM   7088 O O   . TYR B 1 359 ? 16.542  -4.733  68.072  1.00 13.30 ? 359 TYR B O   1 
ATOM   7089 C CB  . TYR B 1 359 ? 18.820  -5.987  69.583  1.00 14.23 ? 359 TYR B CB  1 
ATOM   7090 C CG  . TYR B 1 359 ? 19.511  -6.286  70.904  1.00 10.15 ? 359 TYR B CG  1 
ATOM   7091 C CD1 . TYR B 1 359 ? 19.339  -5.450  72.016  1.00 9.50  ? 359 TYR B CD1 1 
ATOM   7092 C CD2 . TYR B 1 359 ? 20.298  -7.426  71.052  1.00 16.73 ? 359 TYR B CD2 1 
ATOM   7093 C CE1 . TYR B 1 359 ? 19.963  -5.751  73.237  1.00 10.69 ? 359 TYR B CE1 1 
ATOM   7094 C CE2 . TYR B 1 359 ? 20.913  -7.726  72.243  1.00 19.01 ? 359 TYR B CE2 1 
ATOM   7095 C CZ  . TYR B 1 359 ? 20.741  -6.892  73.334  1.00 23.31 ? 359 TYR B CZ  1 
ATOM   7096 O OH  . TYR B 1 359 ? 21.363  -7.220  74.514  1.00 22.70 ? 359 TYR B OH  1 
ATOM   7097 N N   . TYR B 1 360 ? 16.194  -6.880  67.487  1.00 11.72 ? 360 TYR B N   1 
ATOM   7098 C CA  . TYR B 1 360 ? 15.434  -6.570  66.284  1.00 13.19 ? 360 TYR B CA  1 
ATOM   7099 C C   . TYR B 1 360 ? 13.951  -6.431  66.617  1.00 12.72 ? 360 TYR B C   1 
ATOM   7100 O O   . TYR B 1 360 ? 13.439  -7.096  67.517  1.00 15.29 ? 360 TYR B O   1 
ATOM   7101 C CB  . TYR B 1 360 ? 15.547  -7.683  65.247  1.00 14.46 ? 360 TYR B CB  1 
ATOM   7102 C CG  . TYR B 1 360 ? 16.815  -7.818  64.429  1.00 13.07 ? 360 TYR B CG  1 
ATOM   7103 C CD1 . TYR B 1 360 ? 18.025  -8.168  65.018  1.00 10.86 ? 360 TYR B CD1 1 
ATOM   7104 C CD2 . TYR B 1 360 ? 16.770  -7.682  63.048  1.00 14.32 ? 360 TYR B CD2 1 
ATOM   7105 C CE1 . TYR B 1 360 ? 19.160  -8.344  64.246  1.00 11.86 ? 360 TYR B CE1 1 
ATOM   7106 C CE2 . TYR B 1 360 ? 17.878  -7.862  62.279  1.00 12.24 ? 360 TYR B CE2 1 
ATOM   7107 C CZ  . TYR B 1 360 ? 19.079  -8.168  62.876  1.00 7.45  ? 360 TYR B CZ  1 
ATOM   7108 O OH  . TYR B 1 360 ? 20.183  -8.359  62.067  1.00 9.16  ? 360 TYR B OH  1 
ATOM   7109 N N   . GLU B 1 361 ? 13.250  -5.624  65.829  1.00 15.46 ? 361 GLU B N   1 
ATOM   7110 C CA  . GLU B 1 361 ? 11.799  -5.580  65.942  1.00 14.81 ? 361 GLU B CA  1 
ATOM   7111 C C   . GLU B 1 361 ? 11.199  -6.958  65.678  1.00 15.81 ? 361 GLU B C   1 
ATOM   7112 O O   . GLU B 1 361 ? 11.620  -7.675  64.765  1.00 14.00 ? 361 GLU B O   1 
ATOM   7113 C CB  . GLU B 1 361 ? 11.218  -4.547  64.977  1.00 20.46 ? 361 GLU B CB  1 
ATOM   7114 C CG  . GLU B 1 361 ? 11.714  -3.125  65.241  1.00 39.25 ? 361 GLU B CG  1 
ATOM   7115 C CD  . GLU B 1 361 ? 11.285  -2.592  66.603  1.00 51.59 ? 361 GLU B CD  1 
ATOM   7116 O OE1 . GLU B 1 361 ? 12.136  -2.043  67.339  1.00 52.85 ? 361 GLU B OE1 1 
ATOM   7117 O OE2 . GLU B 1 361 ? 10.090  -2.725  66.939  1.00 57.60 ? 361 GLU B OE2 1 
ATOM   7118 N N   . GLU B 1 362 ? 10.219  -7.324  66.504  1.00 15.07 ? 362 GLU B N   1 
ATOM   7119 C CA  . GLU B 1 362 ? 9.511   -8.607  66.390  1.00 14.64 ? 362 GLU B CA  1 
ATOM   7120 C C   . GLU B 1 362 ? 10.499  -9.765  66.267  1.00 11.29 ? 362 GLU B C   1 
ATOM   7121 O O   . GLU B 1 362 ? 10.331  -10.684 65.457  1.00 15.57 ? 362 GLU B O   1 
ATOM   7122 C CB  . GLU B 1 362 ? 8.530   -8.574  65.220  1.00 18.17 ? 362 GLU B CB  1 
ATOM   7123 C CG  . GLU B 1 362 ? 7.702   -7.298  65.211  1.00 24.96 ? 362 GLU B CG  1 
ATOM   7124 C CD  . GLU B 1 362 ? 6.423   -7.409  64.407  1.00 41.16 ? 362 GLU B CD  1 
ATOM   7125 O OE1 . GLU B 1 362 ? 6.334   -8.279  63.515  1.00 40.71 ? 362 GLU B OE1 1 
ATOM   7126 O OE2 . GLU B 1 362 ? 5.501   -6.613  64.678  1.00 50.07 ? 362 GLU B OE2 1 
ATOM   7127 N N   . ASN B 1 363 ? 11.574  -9.691  67.052  1.00 6.67  ? 363 ASN B N   1 
ATOM   7128 C CA  . ASN B 1 363 ? 12.495  -10.811 67.228  1.00 7.30  ? 363 ASN B CA  1 
ATOM   7129 C C   . ASN B 1 363 ? 13.196  -11.199 65.924  1.00 16.48 ? 363 ASN B C   1 
ATOM   7130 O O   . ASN B 1 363 ? 13.524  -12.372 65.704  1.00 14.50 ? 363 ASN B O   1 
ATOM   7131 C CB  . ASN B 1 363 ? 11.757  -12.014 67.823  1.00 9.93  ? 363 ASN B CB  1 
ATOM   7132 C CG  . ASN B 1 363 ? 12.696  -13.077 68.328  1.00 15.03 ? 363 ASN B CG  1 
ATOM   7133 O OD1 . ASN B 1 363 ? 13.782  -12.778 68.818  1.00 14.01 ? 363 ASN B OD1 1 
ATOM   7134 N ND2 . ASN B 1 363 ? 12.297  -14.327 68.181  1.00 13.81 ? 363 ASN B ND2 1 
ATOM   7135 N N   . GLY B 1 364 ? 13.434  -10.221 65.047  1.00 12.66 ? 364 GLY B N   1 
ATOM   7136 C CA  . GLY B 1 364 ? 14.106  -10.475 63.784  1.00 9.03  ? 364 GLY B CA  1 
ATOM   7137 C C   . GLY B 1 364 ? 13.308  -11.248 62.759  1.00 12.53 ? 364 GLY B C   1 
ATOM   7138 O O   . GLY B 1 364 ? 13.848  -11.594 61.707  1.00 12.56 ? 364 GLY B O   1 
ATOM   7139 N N   . ILE B 1 365 ? 12.034  -11.526 63.021  1.00 6.68  ? 365 ILE B N   1 
ATOM   7140 C CA  . ILE B 1 365 ? 11.263  -12.375 62.118  1.00 10.79 ? 365 ILE B CA  1 
ATOM   7141 C C   . ILE B 1 365 ? 10.978  -11.641 60.808  1.00 15.11 ? 365 ILE B C   1 
ATOM   7142 O O   . ILE B 1 365 ? 11.188  -12.230 59.735  1.00 11.70 ? 365 ILE B O   1 
ATOM   7143 C CB  . ILE B 1 365 ? 9.984   -12.876 62.801  1.00 14.65 ? 365 ILE B CB  1 
ATOM   7144 C CG1 . ILE B 1 365 ? 10.363  -13.795 63.969  1.00 11.33 ? 365 ILE B CG1 1 
ATOM   7145 C CG2 . ILE B 1 365 ? 9.062   -13.576 61.784  1.00 14.03 ? 365 ILE B CG2 1 
ATOM   7146 C CD1 . ILE B 1 365 ? 9.285   -13.882 65.009  1.00 14.33 ? 365 ILE B CD1 1 
ATOM   7147 N N   . PRO B 1 366 ? 10.515  -10.379 60.812  1.00 16.64 ? 366 PRO B N   1 
ATOM   7148 C CA  . PRO B 1 366 ? 10.401  -9.673  59.518  1.00 15.22 ? 366 PRO B CA  1 
ATOM   7149 C C   . PRO B 1 366 ? 11.706  -9.674  58.739  1.00 12.83 ? 366 PRO B C   1 
ATOM   7150 O O   . PRO B 1 366 ? 11.700  -9.879  57.513  1.00 10.05 ? 366 PRO B O   1 
ATOM   7151 C CB  . PRO B 1 366 ? 9.974   -8.249  59.922  1.00 14.80 ? 366 PRO B CB  1 
ATOM   7152 C CG  . PRO B 1 366 ? 9.269   -8.436  61.240  1.00 12.29 ? 366 PRO B CG  1 
ATOM   7153 C CD  . PRO B 1 366 ? 10.005  -9.556  61.929  1.00 12.20 ? 366 PRO B CD  1 
ATOM   7154 N N   . PHE B 1 367 ? 12.835  -9.486  59.427  1.00 10.85 ? 367 PHE B N   1 
ATOM   7155 C CA  . PHE B 1 367 ? 14.116  -9.460  58.731  1.00 11.63 ? 367 PHE B CA  1 
ATOM   7156 C C   . PHE B 1 367 ? 14.445  -10.814 58.104  1.00 12.43 ? 367 PHE B C   1 
ATOM   7157 O O   . PHE B 1 367 ? 14.749  -10.889 56.910  1.00 11.94 ? 367 PHE B O   1 
ATOM   7158 C CB  . PHE B 1 367 ? 15.242  -9.017  59.664  1.00 15.50 ? 367 PHE B CB  1 
ATOM   7159 C CG  . PHE B 1 367 ? 16.597  -9.103  59.017  1.00 15.46 ? 367 PHE B CG  1 
ATOM   7160 C CD1 . PHE B 1 367 ? 16.971  -8.170  58.052  1.00 10.75 ? 367 PHE B CD1 1 
ATOM   7161 C CD2 . PHE B 1 367 ? 17.474  -10.128 59.332  1.00 10.89 ? 367 PHE B CD2 1 
ATOM   7162 C CE1 . PHE B 1 367 ? 18.222  -8.254  57.427  1.00 13.90 ? 367 PHE B CE1 1 
ATOM   7163 C CE2 . PHE B 1 367 ? 18.723  -10.221 58.710  1.00 11.03 ? 367 PHE B CE2 1 
ATOM   7164 C CZ  . PHE B 1 367 ? 19.090  -9.293  57.755  1.00 13.16 ? 367 PHE B CZ  1 
ATOM   7165 N N   . LEU B 1 368 ? 14.392  -11.902 58.882  1.00 8.18  ? 368 LEU B N   1 
ATOM   7166 C CA  . LEU B 1 368 ? 14.784  -13.193 58.307  1.00 6.24  ? 368 LEU B CA  1 
ATOM   7167 C C   . LEU B 1 368 ? 13.806  -13.660 57.235  1.00 6.46  ? 368 LEU B C   1 
ATOM   7168 O O   . LEU B 1 368 ? 14.219  -14.251 56.230  1.00 7.41  ? 368 LEU B O   1 
ATOM   7169 C CB  . LEU B 1 368 ? 14.918  -14.254 59.408  1.00 6.01  ? 368 LEU B CB  1 
ATOM   7170 C CG  . LEU B 1 368 ? 16.230  -14.086 60.195  1.00 7.76  ? 368 LEU B CG  1 
ATOM   7171 C CD1 . LEU B 1 368 ? 16.384  -15.185 61.230  1.00 12.97 ? 368 LEU B CD1 1 
ATOM   7172 C CD2 . LEU B 1 368 ? 17.453  -14.028 59.266  1.00 11.42 ? 368 LEU B CD2 1 
ATOM   7173 N N   . GLU B 1 369 ? 12.502  -13.457 57.445  1.00 10.53 ? 369 GLU B N   1 
ATOM   7174 C CA  . GLU B 1 369 ? 11.541  -13.878 56.435  1.00 12.09 ? 369 GLU B CA  1 
ATOM   7175 C C   . GLU B 1 369 ? 11.763  -13.139 55.116  1.00 17.21 ? 369 GLU B C   1 
ATOM   7176 O O   . GLU B 1 369 ? 11.727  -13.749 54.044  1.00 10.48 ? 369 GLU B O   1 
ATOM   7177 C CB  . GLU B 1 369 ? 10.114  -13.684 56.959  1.00 7.11  ? 369 GLU B CB  1 
ATOM   7178 C CG  . GLU B 1 369 ? 9.768   -14.759 58.015  1.00 10.19 ? 369 GLU B CG  1 
ATOM   7179 C CD  . GLU B 1 369 ? 8.344   -14.640 58.534  1.00 20.61 ? 369 GLU B CD  1 
ATOM   7180 O OE1 . GLU B 1 369 ? 7.710   -13.594 58.282  1.00 18.03 ? 369 GLU B OE1 1 
ATOM   7181 O OE2 . GLU B 1 369 ? 7.865   -15.583 59.202  1.00 17.13 ? 369 GLU B OE2 1 
ATOM   7182 N N   . LYS B 1 370 ? 12.004  -11.828 55.167  1.00 9.90  ? 370 LYS B N   1 
ATOM   7183 C CA  . LYS B 1 370 ? 12.288  -11.100 53.929  1.00 13.31 ? 370 LYS B CA  1 
ATOM   7184 C C   . LYS B 1 370 ? 13.637  -11.498 53.337  1.00 13.52 ? 370 LYS B C   1 
ATOM   7185 O O   . LYS B 1 370 ? 13.784  -11.588 52.109  1.00 11.19 ? 370 LYS B O   1 
ATOM   7186 C CB  . LYS B 1 370 ? 12.254  -9.588  54.172  1.00 15.89 ? 370 LYS B CB  1 
ATOM   7187 C CG  . LYS B 1 370 ? 10.869  -9.043  54.495  1.00 25.95 ? 370 LYS B CG  1 
ATOM   7188 C CD  . LYS B 1 370 ? 10.931  -7.575  54.908  1.00 30.21 ? 370 LYS B CD  1 
ATOM   7189 C CE  . LYS B 1 370 ? 9.623   -7.122  55.550  1.00 30.82 ? 370 LYS B CE  1 
ATOM   7190 N NZ  . LYS B 1 370 ? 8.439   -7.320  54.652  1.00 28.25 ? 370 LYS B NZ  1 
ATOM   7191 N N   . LEU B 1 371 ? 14.647  -11.695 54.186  1.00 15.20 ? 371 LEU B N   1 
ATOM   7192 C CA  . LEU B 1 371 ? 15.968  -12.080 53.683  1.00 8.29  ? 371 LEU B CA  1 
ATOM   7193 C C   . LEU B 1 371 ? 15.916  -13.441 53.004  1.00 11.81 ? 371 LEU B C   1 
ATOM   7194 O O   . LEU B 1 371 ? 16.415  -13.612 51.885  1.00 14.54 ? 371 LEU B O   1 
ATOM   7195 C CB  . LEU B 1 371 ? 16.987  -12.096 54.830  1.00 6.68  ? 371 LEU B CB  1 
ATOM   7196 C CG  . LEU B 1 371 ? 18.393  -12.561 54.439  1.00 10.59 ? 371 LEU B CG  1 
ATOM   7197 C CD1 . LEU B 1 371 ? 19.024  -11.580 53.470  1.00 12.14 ? 371 LEU B CD1 1 
ATOM   7198 C CD2 . LEU B 1 371 ? 19.284  -12.757 55.686  1.00 9.58  ? 371 LEU B CD2 1 
ATOM   7199 N N   . TYR B 1 372 ? 15.307  -14.425 53.661  1.00 10.32 ? 372 TYR B N   1 
ATOM   7200 C CA  . TYR B 1 372 ? 15.285  -15.775 53.101  1.00 10.69 ? 372 TYR B CA  1 
ATOM   7201 C C   . TYR B 1 372 ? 14.398  -15.852 51.855  1.00 18.37 ? 372 TYR B C   1 
ATOM   7202 O O   . TYR B 1 372 ? 14.733  -16.550 50.888  1.00 16.54 ? 372 TYR B O   1 
ATOM   7203 C CB  . TYR B 1 372 ? 14.806  -16.750 54.170  1.00 8.09  ? 372 TYR B CB  1 
ATOM   7204 C CG  . TYR B 1 372 ? 15.788  -16.955 55.312  1.00 7.47  ? 372 TYR B CG  1 
ATOM   7205 C CD1 . TYR B 1 372 ? 17.148  -16.644 55.179  1.00 15.32 ? 372 TYR B CD1 1 
ATOM   7206 C CD2 . TYR B 1 372 ? 15.360  -17.487 56.510  1.00 7.73  ? 372 TYR B CD2 1 
ATOM   7207 C CE1 . TYR B 1 372 ? 18.042  -16.874 56.238  1.00 13.07 ? 372 TYR B CE1 1 
ATOM   7208 C CE2 . TYR B 1 372 ? 16.226  -17.707 57.568  1.00 10.47 ? 372 TYR B CE2 1 
ATOM   7209 C CZ  . TYR B 1 372 ? 17.563  -17.423 57.429  1.00 11.70 ? 372 TYR B CZ  1 
ATOM   7210 O OH  . TYR B 1 372 ? 18.395  -17.661 58.497  1.00 9.34  ? 372 TYR B OH  1 
ATOM   7211 N N   . SER B 1 373 ? 13.266  -15.137 51.850  1.00 14.50 ? 373 SER B N   1 
ATOM   7212 C CA  . SER B 1 373 ? 12.409  -15.154 50.660  1.00 13.27 ? 373 SER B CA  1 
ATOM   7213 C C   . SER B 1 373 ? 13.075  -14.455 49.490  1.00 16.12 ? 373 SER B C   1 
ATOM   7214 O O   . SER B 1 373 ? 12.863  -14.841 48.336  1.00 18.94 ? 373 SER B O   1 
ATOM   7215 C CB  . SER B 1 373 ? 11.062  -14.501 50.952  1.00 24.49 ? 373 SER B CB  1 
ATOM   7216 O OG  . SER B 1 373 ? 11.253  -13.227 51.527  1.00 35.63 ? 373 SER B OG  1 
ATOM   7217 N N   . THR B 1 374 ? 13.869  -13.420 49.761  1.00 14.43 ? 374 THR B N   1 
ATOM   7218 C CA  . THR B 1 374 ? 14.595  -12.757 48.685  1.00 18.15 ? 374 THR B CA  1 
ATOM   7219 C C   . THR B 1 374 ? 15.712  -13.651 48.153  1.00 24.81 ? 374 THR B C   1 
ATOM   7220 O O   . THR B 1 374 ? 15.814  -13.875 46.941  1.00 22.88 ? 374 THR B O   1 
ATOM   7221 C CB  . THR B 1 374 ? 15.136  -11.414 49.170  1.00 19.20 ? 374 THR B CB  1 
ATOM   7222 O OG1 . THR B 1 374 ? 14.055  -10.629 49.681  1.00 17.82 ? 374 THR B OG1 1 
ATOM   7223 C CG2 . THR B 1 374 ? 15.814  -10.657 48.028  1.00 22.65 ? 374 THR B CG2 1 
ATOM   7224 N N   . LEU B 1 375 ? 16.544  -14.192 49.054  1.00 21.58 ? 375 LEU B N   1 
ATOM   7225 C CA  . LEU B 1 375 ? 17.623  -15.092 48.647  1.00 16.23 ? 375 LEU B CA  1 
ATOM   7226 C C   . LEU B 1 375 ? 17.090  -16.271 47.851  1.00 24.05 ? 375 LEU B C   1 
ATOM   7227 O O   . LEU B 1 375 ? 17.694  -16.689 46.853  1.00 23.58 ? 375 LEU B O   1 
ATOM   7228 C CB  . LEU B 1 375 ? 18.361  -15.603 49.881  1.00 10.70 ? 375 LEU B CB  1 
ATOM   7229 C CG  . LEU B 1 375 ? 19.267  -14.597 50.592  1.00 11.38 ? 375 LEU B CG  1 
ATOM   7230 C CD1 . LEU B 1 375 ? 19.848  -15.225 51.868  1.00 10.90 ? 375 LEU B CD1 1 
ATOM   7231 C CD2 . LEU B 1 375 ? 20.360  -14.171 49.646  1.00 18.12 ? 375 LEU B CD2 1 
ATOM   7232 N N   . GLU B 1 376 ? 15.963  -16.820 48.301  1.00 27.70 ? 376 GLU B N   1 
ATOM   7233 C CA  . GLU B 1 376 ? 15.329  -17.985 47.704  1.00 24.36 ? 376 GLU B CA  1 
ATOM   7234 C C   . GLU B 1 376 ? 15.113  -17.825 46.202  1.00 32.66 ? 376 GLU B C   1 
ATOM   7235 O O   . GLU B 1 376 ? 15.156  -18.811 45.458  1.00 29.03 ? 376 GLU B O   1 
ATOM   7236 C CB  . GLU B 1 376 ? 14.003  -18.204 48.440  1.00 26.01 ? 376 GLU B CB  1 
ATOM   7237 C CG  . GLU B 1 376 ? 13.149  -19.369 48.080  1.00 33.16 ? 376 GLU B CG  1 
ATOM   7238 C CD  . GLU B 1 376 ? 11.931  -19.430 48.982  1.00 32.42 ? 376 GLU B CD  1 
ATOM   7239 O OE1 . GLU B 1 376 ? 11.122  -18.479 48.976  1.00 34.74 ? 376 GLU B OE1 1 
ATOM   7240 O OE2 . GLU B 1 376 ? 11.797  -20.418 49.727  1.00 39.00 ? 376 GLU B OE2 1 
ATOM   7241 N N   . LYS B 1 377 ? 14.901  -16.598 45.735  1.00 29.48 ? 377 LYS B N   1 
ATOM   7242 C CA  . LYS B 1 377 ? 14.520  -16.358 44.353  1.00 29.96 ? 377 LYS B CA  1 
ATOM   7243 C C   . LYS B 1 377 ? 15.613  -15.685 43.535  1.00 33.02 ? 377 LYS B C   1 
ATOM   7244 O O   . LYS B 1 377 ? 15.432  -15.501 42.325  1.00 30.30 ? 377 LYS B O   1 
ATOM   7245 C CB  . LYS B 1 377 ? 13.239  -15.513 44.308  1.00 38.75 ? 377 LYS B CB  1 
ATOM   7246 C CG  . LYS B 1 377 ? 12.037  -16.171 44.991  1.00 37.26 ? 377 LYS B CG  1 
ATOM   7247 C CD  . LYS B 1 377 ? 11.059  -15.126 45.514  1.00 44.85 ? 377 LYS B CD  1 
ATOM   7248 C CE  . LYS B 1 377 ? 10.070  -15.728 46.504  1.00 47.37 ? 377 LYS B CE  1 
ATOM   7249 N NZ  . LYS B 1 377 ? 9.293   -14.666 47.198  1.00 49.44 ? 377 LYS B NZ  1 
ATOM   7250 N N   . GLU B 1 378 ? 16.735  -15.310 44.155  1.00 24.32 ? 378 GLU B N   1 
ATOM   7251 C CA  . GLU B 1 378 ? 17.885  -14.768 43.431  1.00 28.12 ? 378 GLU B CA  1 
ATOM   7252 C C   . GLU B 1 378 ? 18.595  -15.894 42.689  1.00 27.92 ? 378 GLU B C   1 
ATOM   7253 O O   . GLU B 1 378 ? 19.275  -16.720 43.303  1.00 32.99 ? 378 GLU B O   1 
ATOM   7254 C CB  . GLU B 1 378 ? 18.847  -14.079 44.394  1.00 34.63 ? 378 GLU B CB  1 
ATOM   7255 C CG  . GLU B 1 378 ? 18.337  -12.781 44.969  1.00 37.60 ? 378 GLU B CG  1 
ATOM   7256 C CD  . GLU B 1 378 ? 18.501  -11.626 44.011  1.00 50.56 ? 378 GLU B CD  1 
ATOM   7257 O OE1 . GLU B 1 378 ? 18.952  -11.853 42.867  1.00 56.19 ? 378 GLU B OE1 1 
ATOM   7258 O OE2 . GLU B 1 378 ? 18.182  -10.486 44.403  1.00 55.67 ? 378 GLU B OE2 1 
ATOM   7259 N N   . GLU B 1 379 ? 18.460  -15.922 41.362  1.00 30.01 ? 379 GLU B N   1 
ATOM   7260 C CA  . GLU B 1 379 ? 18.985  -17.053 40.610  1.00 28.12 ? 379 GLU B CA  1 
ATOM   7261 C C   . GLU B 1 379 ? 20.507  -17.096 40.606  1.00 27.42 ? 379 GLU B C   1 
ATOM   7262 O O   . GLU B 1 379 ? 21.079  -18.172 40.421  1.00 26.32 ? 379 GLU B O   1 
ATOM   7263 C CB  . GLU B 1 379 ? 18.446  -17.030 39.177  1.00 36.90 ? 379 GLU B CB  1 
ATOM   7264 C CG  . GLU B 1 379 ? 16.985  -17.453 39.077  1.00 49.54 ? 379 GLU B CG  1 
ATOM   7265 C CD  . GLU B 1 379 ? 16.240  -16.764 37.947  1.00 63.01 ? 379 GLU B CD  1 
ATOM   7266 O OE1 . GLU B 1 379 ? 16.801  -16.669 36.835  1.00 66.08 ? 379 GLU B OE1 1 
ATOM   7267 O OE2 . GLU B 1 379 ? 15.091  -16.321 38.173  1.00 65.39 ? 379 GLU B OE2 1 
ATOM   7268 N N   . TRP B 1 380 ? 21.176  -15.972 40.824  1.00 19.38 ? 380 TRP B N   1 
ATOM   7269 C CA  . TRP B 1 380 ? 22.633  -15.958 40.807  1.00 19.77 ? 380 TRP B CA  1 
ATOM   7270 C C   . TRP B 1 380 ? 23.247  -16.244 42.172  1.00 15.74 ? 380 TRP B C   1 
ATOM   7271 O O   . TRP B 1 380 ? 24.477  -16.305 42.274  1.00 18.24 ? 380 TRP B O   1 
ATOM   7272 C CB  . TRP B 1 380 ? 23.142  -14.614 40.284  1.00 22.12 ? 380 TRP B CB  1 
ATOM   7273 C CG  . TRP B 1 380 ? 22.540  -13.456 40.986  1.00 22.69 ? 380 TRP B CG  1 
ATOM   7274 C CD1 . TRP B 1 380 ? 21.342  -12.876 40.718  1.00 26.21 ? 380 TRP B CD1 1 
ATOM   7275 C CD2 . TRP B 1 380 ? 23.103  -12.733 42.088  1.00 24.35 ? 380 TRP B CD2 1 
ATOM   7276 N NE1 . TRP B 1 380 ? 21.117  -11.834 41.581  1.00 19.15 ? 380 TRP B NE1 1 
ATOM   7277 C CE2 . TRP B 1 380 ? 22.185  -11.726 42.435  1.00 19.87 ? 380 TRP B CE2 1 
ATOM   7278 C CE3 . TRP B 1 380 ? 24.299  -12.840 42.811  1.00 16.62 ? 380 TRP B CE3 1 
ATOM   7279 C CZ2 . TRP B 1 380 ? 22.419  -10.827 43.471  1.00 20.21 ? 380 TRP B CZ2 1 
ATOM   7280 C CZ3 . TRP B 1 380 ? 24.531  -11.951 43.843  1.00 17.51 ? 380 TRP B CZ3 1 
ATOM   7281 C CH2 . TRP B 1 380 ? 23.598  -10.957 44.166  1.00 17.38 ? 380 TRP B CH2 1 
ATOM   7282 N N   . ILE B 1 381 ? 22.432  -16.392 43.219  1.00 15.47 ? 381 ILE B N   1 
ATOM   7283 C CA  . ILE B 1 381 ? 22.900  -16.797 44.545  1.00 18.02 ? 381 ILE B CA  1 
ATOM   7284 C C   . ILE B 1 381 ? 22.515  -18.253 44.761  1.00 19.95 ? 381 ILE B C   1 
ATOM   7285 O O   . ILE B 1 381 ? 21.369  -18.646 44.506  1.00 20.48 ? 381 ILE B O   1 
ATOM   7286 C CB  . ILE B 1 381 ? 22.313  -15.917 45.663  1.00 17.96 ? 381 ILE B CB  1 
ATOM   7287 C CG1 . ILE B 1 381 ? 22.703  -14.456 45.471  1.00 16.70 ? 381 ILE B CG1 1 
ATOM   7288 C CG2 . ILE B 1 381 ? 22.822  -16.382 47.035  1.00 16.02 ? 381 ILE B CG2 1 
ATOM   7289 C CD1 . ILE B 1 381 ? 21.991  -13.495 46.415  1.00 19.11 ? 381 ILE B CD1 1 
ATOM   7290 N N   . GLU B 1 382 ? 23.462  -19.052 45.234  1.00 13.18 ? 382 GLU B N   1 
ATOM   7291 C CA  . GLU B 1 382 ? 23.173  -20.423 45.636  1.00 15.05 ? 382 GLU B CA  1 
ATOM   7292 C C   . GLU B 1 382 ? 23.660  -20.617 47.064  1.00 15.16 ? 382 GLU B C   1 
ATOM   7293 O O   . GLU B 1 382 ? 24.866  -20.572 47.323  1.00 14.16 ? 382 GLU B O   1 
ATOM   7294 C CB  . GLU B 1 382 ? 23.833  -21.416 44.689  1.00 16.42 ? 382 GLU B CB  1 
ATOM   7295 C CG  . GLU B 1 382 ? 23.604  -22.878 45.034  1.00 22.28 ? 382 GLU B CG  1 
ATOM   7296 C CD  . GLU B 1 382 ? 24.298  -23.805 44.045  1.00 37.27 ? 382 GLU B CD  1 
ATOM   7297 O OE1 . GLU B 1 382 ? 24.506  -23.381 42.887  1.00 40.68 ? 382 GLU B OE1 1 
ATOM   7298 O OE2 . GLU B 1 382 ? 24.636  -24.950 44.421  1.00 41.62 ? 382 GLU B OE2 1 
ATOM   7299 N N   . THR B 1 383 ? 22.728  -20.817 47.996  1.00 17.30 ? 383 THR B N   1 
ATOM   7300 C CA  . THR B 1 383 ? 23.132  -21.167 49.349  1.00 11.14 ? 383 THR B CA  1 
ATOM   7301 C C   . THR B 1 383 ? 23.598  -22.620 49.392  1.00 18.23 ? 383 THR B C   1 
ATOM   7302 O O   . THR B 1 383 ? 23.095  -23.483 48.659  1.00 17.53 ? 383 THR B O   1 
ATOM   7303 C CB  . THR B 1 383 ? 21.989  -20.942 50.347  1.00 12.61 ? 383 THR B CB  1 
ATOM   7304 O OG1 . THR B 1 383 ? 20.819  -21.654 49.913  1.00 13.58 ? 383 THR B OG1 1 
ATOM   7305 C CG2 . THR B 1 383 ? 21.657  -19.444 50.469  1.00 19.02 ? 383 THR B CG2 1 
ATOM   7306 N N   . LEU B 1 384 ? 24.573  -22.885 50.264  1.00 11.58 ? 384 LEU B N   1 
ATOM   7307 C CA  . LEU B 1 384 ? 25.246  -24.170 50.349  1.00 10.95 ? 384 LEU B CA  1 
ATOM   7308 C C   . LEU B 1 384 ? 25.221  -24.699 51.776  1.00 11.85 ? 384 LEU B C   1 
ATOM   7309 O O   . LEU B 1 384 ? 25.290  -23.936 52.744  1.00 10.24 ? 384 LEU B O   1 
ATOM   7310 C CB  . LEU B 1 384 ? 26.720  -24.070 49.909  1.00 11.62 ? 384 LEU B CB  1 
ATOM   7311 C CG  . LEU B 1 384 ? 27.020  -23.594 48.485  1.00 17.75 ? 384 LEU B CG  1 
ATOM   7312 C CD1 . LEU B 1 384 ? 28.526  -23.588 48.236  1.00 11.98 ? 384 LEU B CD1 1 
ATOM   7313 C CD2 . LEU B 1 384 ? 26.315  -24.479 47.460  1.00 15.34 ? 384 LEU B CD2 1 
ATOM   7314 N N   . THR B 1 385 ? 25.148  -26.017 51.898  1.00 10.75 ? 385 THR B N   1 
ATOM   7315 C CA  . THR B 1 385 ? 25.486  -26.640 53.166  1.00 8.81  ? 385 THR B CA  1 
ATOM   7316 C C   . THR B 1 385 ? 27.006  -26.619 53.341  1.00 10.92 ? 385 THR B C   1 
ATOM   7317 O O   . THR B 1 385 ? 27.762  -26.365 52.397  1.00 14.07 ? 385 THR B O   1 
ATOM   7318 C CB  . THR B 1 385 ? 24.997  -28.091 53.210  1.00 10.39 ? 385 THR B CB  1 
ATOM   7319 O OG1 . THR B 1 385 ? 25.746  -28.840 52.253  1.00 15.25 ? 385 THR B OG1 1 
ATOM   7320 C CG2 . THR B 1 385 ? 23.475  -28.205 52.849  1.00 11.46 ? 385 THR B CG2 1 
ATOM   7321 N N   . LEU B 1 386 ? 27.456  -26.893 54.569  1.00 8.03  ? 386 LEU B N   1 
ATOM   7322 C CA  . LEU B 1 386 ? 28.895  -26.977 54.815  1.00 10.48 ? 386 LEU B CA  1 
ATOM   7323 C C   . LEU B 1 386 ? 29.521  -28.045 53.933  1.00 12.28 ? 386 LEU B C   1 
ATOM   7324 O O   . LEU B 1 386 ? 30.628  -27.869 53.407  1.00 14.87 ? 386 LEU B O   1 
ATOM   7325 C CB  . LEU B 1 386 ? 29.164  -27.292 56.282  1.00 6.61  ? 386 LEU B CB  1 
ATOM   7326 C CG  . LEU B 1 386 ? 28.620  -26.297 57.309  1.00 13.15 ? 386 LEU B CG  1 
ATOM   7327 C CD1 . LEU B 1 386 ? 29.027  -26.709 58.724  1.00 12.59 ? 386 LEU B CD1 1 
ATOM   7328 C CD2 . LEU B 1 386 ? 29.130  -24.910 56.974  1.00 12.99 ? 386 LEU B CD2 1 
ATOM   7329 N N   . GLU B 1 387 ? 28.828  -29.173 53.785  1.00 15.04 ? 387 GLU B N   1 
ATOM   7330 C CA  . GLU B 1 387 ? 29.336  -30.253 52.948  1.00 15.63 ? 387 GLU B CA  1 
ATOM   7331 C C   . GLU B 1 387 ? 29.500  -29.796 51.504  1.00 13.91 ? 387 GLU B C   1 
ATOM   7332 O O   . GLU B 1 387 ? 30.526  -30.071 50.873  1.00 21.96 ? 387 GLU B O   1 
ATOM   7333 C CB  . GLU B 1 387 ? 28.399  -31.460 53.041  1.00 16.66 ? 387 GLU B CB  1 
ATOM   7334 C CG  . GLU B 1 387 ? 29.019  -32.745 52.510  1.00 31.15 ? 387 GLU B CG  1 
ATOM   7335 C CD  . GLU B 1 387 ? 28.033  -33.901 52.454  1.00 37.95 ? 387 GLU B CD  1 
ATOM   7336 O OE1 . GLU B 1 387 ? 26.942  -33.798 53.053  1.00 44.72 ? 387 GLU B OE1 1 
ATOM   7337 O OE2 . GLU B 1 387 ? 28.347  -34.911 51.798  1.00 44.70 ? 387 GLU B OE2 1 
ATOM   7338 N N   . GLU B 1 388 ? 28.503  -29.081 50.967  1.00 15.77 ? 388 GLU B N   1 
ATOM   7339 C CA  . GLU B 1 388 ? 28.607  -28.584 49.594  1.00 15.03 ? 388 GLU B CA  1 
ATOM   7340 C C   . GLU B 1 388 ? 29.735  -27.566 49.448  1.00 19.22 ? 388 GLU B C   1 
ATOM   7341 O O   . GLU B 1 388 ? 30.467  -27.581 48.450  1.00 17.48 ? 388 GLU B O   1 
ATOM   7342 C CB  . GLU B 1 388 ? 27.268  -27.991 49.159  1.00 16.41 ? 388 GLU B CB  1 
ATOM   7343 C CG  . GLU B 1 388 ? 26.188  -29.080 48.972  1.00 14.08 ? 388 GLU B CG  1 
ATOM   7344 C CD  . GLU B 1 388 ? 24.806  -28.517 48.755  1.00 24.32 ? 388 GLU B CD  1 
ATOM   7345 O OE1 . GLU B 1 388 ? 24.503  -27.421 49.287  1.00 15.38 ? 388 GLU B OE1 1 
ATOM   7346 O OE2 . GLU B 1 388 ? 24.009  -29.180 48.054  1.00 36.89 ? 388 GLU B OE2 1 
ATOM   7347 N N   . ALA B 1 389 ? 29.898  -26.682 50.433  1.00 14.13 ? 389 ALA B N   1 
ATOM   7348 C CA  . ALA B 1 389 ? 31.007  -25.731 50.407  1.00 16.32 ? 389 ALA B CA  1 
ATOM   7349 C C   . ALA B 1 389 ? 32.348  -26.449 50.468  1.00 19.83 ? 389 ALA B C   1 
ATOM   7350 O O   . ALA B 1 389 ? 33.317  -26.029 49.824  1.00 19.50 ? 389 ALA B O   1 
ATOM   7351 C CB  . ALA B 1 389 ? 30.880  -24.746 51.569  1.00 14.18 ? 389 ALA B CB  1 
ATOM   7352 N N   . MET B 1 390 ? 32.416  -27.550 51.218  1.00 18.53 ? 390 MET B N   1 
ATOM   7353 C CA  . MET B 1 390 ? 33.680  -28.258 51.377  1.00 23.54 ? 390 MET B CA  1 
ATOM   7354 C C   . MET B 1 390 ? 34.099  -28.964 50.101  1.00 24.61 ? 390 MET B C   1 
ATOM   7355 O O   . MET B 1 390 ? 35.294  -29.041 49.821  1.00 21.45 ? 390 MET B O   1 
ATOM   7356 C CB  . MET B 1 390 ? 33.598  -29.269 52.525  1.00 17.80 ? 390 MET B CB  1 
ATOM   7357 C CG  . MET B 1 390 ? 34.870  -30.081 52.742  1.00 35.62 ? 390 MET B CG  1 
ATOM   7358 S SD  . MET B 1 390 ? 34.779  -31.234 54.139  1.00 38.89 ? 390 MET B SD  1 
ATOM   7359 C CE  . MET B 1 390 ? 33.762  -32.557 53.471  1.00 31.03 ? 390 MET B CE  1 
ATOM   7360 N N   . ARG B 1 391 ? 33.144  -29.456 49.315  1.00 20.72 ? 391 ARG B N   1 
ATOM   7361 C CA  . ARG B 1 391 ? 33.411  -30.321 48.177  1.00 25.70 ? 391 ARG B CA  1 
ATOM   7362 C C   . ARG B 1 391 ? 33.227  -29.613 46.842  1.00 25.76 ? 391 ARG B C   1 
ATOM   7363 O O   . ARG B 1 391 ? 33.513  -30.206 45.794  1.00 22.73 ? 391 ARG B O   1 
ATOM   7364 C CB  . ARG B 1 391 ? 32.504  -31.559 48.227  1.00 29.90 ? 391 ARG B CB  1 
ATOM   7365 C CG  . ARG B 1 391 ? 32.609  -32.405 49.501  1.00 42.27 ? 391 ARG B CG  1 
ATOM   7366 C CD  . ARG B 1 391 ? 32.071  -33.815 49.285  1.00 51.58 ? 391 ARG B CD  1 
ATOM   7367 N NE  . ARG B 1 391 ? 32.069  -34.666 50.478  1.00 62.10 ? 391 ARG B NE  1 
ATOM   7368 C CZ  . ARG B 1 391 ? 33.128  -35.319 50.944  1.00 66.83 ? 391 ARG B CZ  1 
ATOM   7369 N NH1 . ARG B 1 391 ? 34.296  -35.232 50.320  1.00 71.84 ? 391 ARG B NH1 1 
ATOM   7370 N NH2 . ARG B 1 391 ? 33.029  -36.057 52.043  1.00 59.29 ? 391 ARG B NH2 1 
ATOM   7371 N N   . LYS B 1 392 ? 32.747  -28.373 46.852  1.00 17.15 ? 392 LYS B N   1 
ATOM   7372 C CA  . LYS B 1 392 ? 32.496  -27.628 45.625  1.00 29.06 ? 392 LYS B CA  1 
ATOM   7373 C C   . LYS B 1 392 ? 33.743  -27.531 44.765  1.00 28.42 ? 392 LYS B C   1 
ATOM   7374 O O   . LYS B 1 392 ? 34.774  -27.017 45.204  1.00 18.59 ? 392 LYS B O   1 
ATOM   7375 C CB  . LYS B 1 392 ? 31.998  -26.230 45.971  1.00 29.25 ? 392 LYS B CB  1 
ATOM   7376 C CG  . LYS B 1 392 ? 31.520  -25.458 44.775  1.00 35.17 ? 392 LYS B CG  1 
ATOM   7377 C CD  . LYS B 1 392 ? 30.175  -24.878 45.068  1.00 39.31 ? 392 LYS B CD  1 
ATOM   7378 C CE  . LYS B 1 392 ? 29.079  -25.879 44.788  1.00 37.42 ? 392 LYS B CE  1 
ATOM   7379 N NZ  . LYS B 1 392 ? 28.839  -25.996 43.328  1.00 44.31 ? 392 LYS B NZ  1 
ATOM   7380 N N   . GLU B 1 393 ? 33.625  -27.978 43.515  1.00 21.78 ? 393 GLU B N   1 
ATOM   7381 C CA  . GLU B 1 393 ? 34.788  -28.030 42.639  1.00 26.75 ? 393 GLU B CA  1 
ATOM   7382 C C   . GLU B 1 393 ? 35.081  -26.678 41.995  1.00 23.72 ? 393 GLU B C   1 
ATOM   7383 O O   . GLU B 1 393 ? 36.241  -26.256 41.943  1.00 26.33 ? 393 GLU B O   1 
ATOM   7384 C CB  . GLU B 1 393 ? 34.584  -29.106 41.568  1.00 33.12 ? 393 GLU B CB  1 
ATOM   7385 C CG  . GLU B 1 393 ? 34.532  -30.525 42.128  1.00 43.48 ? 393 GLU B CG  1 
ATOM   7386 C CD  . GLU B 1 393 ? 34.608  -31.601 41.050  1.00 53.99 ? 393 GLU B CD  1 
ATOM   7387 O OE1 . GLU B 1 393 ? 34.393  -31.283 39.859  1.00 55.49 ? 393 GLU B OE1 1 
ATOM   7388 O OE2 . GLU B 1 393 ? 34.891  -32.769 41.398  1.00 55.31 ? 393 GLU B OE2 1 
ATOM   7389 N N   . ASP B 1 394 ? 34.053  -25.976 41.522  1.00 20.39 ? 394 ASP B N   1 
ATOM   7390 C CA  . ASP B 1 394 ? 34.248  -24.768 40.729  1.00 19.17 ? 394 ASP B CA  1 
ATOM   7391 C C   . ASP B 1 394 ? 34.463  -23.516 41.582  1.00 27.06 ? 394 ASP B C   1 
ATOM   7392 O O   . ASP B 1 394 ? 33.816  -22.487 41.359  1.00 24.75 ? 394 ASP B O   1 
ATOM   7393 C CB  . ASP B 1 394 ? 33.049  -24.563 39.787  1.00 22.65 ? 394 ASP B CB  1 
ATOM   7394 C CG  . ASP B 1 394 ? 31.720  -24.949 40.435  1.00 33.71 ? 394 ASP B CG  1 
ATOM   7395 O OD1 . ASP B 1 394 ? 31.754  -25.496 41.555  1.00 41.38 ? 394 ASP B OD1 1 
ATOM   7396 O OD2 . ASP B 1 394 ? 30.644  -24.702 39.836  1.00 34.31 ? 394 ASP B OD2 1 
ATOM   7397 N N   . VAL B 1 395 ? 35.380  -23.585 42.546  1.00 19.69 ? 395 VAL B N   1 
ATOM   7398 C CA  . VAL B 1 395 ? 35.737  -22.445 43.378  1.00 20.26 ? 395 VAL B CA  1 
ATOM   7399 C C   . VAL B 1 395 ? 37.250  -22.282 43.341  1.00 18.21 ? 395 VAL B C   1 
ATOM   7400 O O   . VAL B 1 395 ? 37.983  -23.167 42.896  1.00 23.24 ? 395 VAL B O   1 
ATOM   7401 C CB  . VAL B 1 395 ? 35.239  -22.599 44.832  1.00 20.26 ? 395 VAL B CB  1 
ATOM   7402 C CG1 . VAL B 1 395 ? 33.728  -22.713 44.859  1.00 23.38 ? 395 VAL B CG1 1 
ATOM   7403 C CG2 . VAL B 1 395 ? 35.876  -23.809 45.492  1.00 22.70 ? 395 VAL B CG2 1 
ATOM   7404 N N   . LYS B 1 396 ? 37.715  -21.128 43.800  1.00 18.26 ? 396 LYS B N   1 
ATOM   7405 C CA  . LYS B 1 396 ? 39.143  -20.846 43.874  1.00 13.17 ? 396 LYS B CA  1 
ATOM   7406 C C   . LYS B 1 396 ? 39.691  -21.256 45.235  1.00 18.56 ? 396 LYS B C   1 
ATOM   7407 O O   . LYS B 1 396 ? 39.013  -21.109 46.258  1.00 13.15 ? 396 LYS B O   1 
ATOM   7408 C CB  . LYS B 1 396 ? 39.415  -19.366 43.624  1.00 20.74 ? 396 LYS B CB  1 
ATOM   7409 C CG  . LYS B 1 396 ? 39.325  -18.988 42.153  1.00 32.69 ? 396 LYS B CG  1 
ATOM   7410 C CD  . LYS B 1 396 ? 40.620  -18.365 41.645  1.00 37.35 ? 396 LYS B CD  1 
ATOM   7411 C CE  . LYS B 1 396 ? 40.504  -17.955 40.179  1.00 40.30 ? 396 LYS B CE  1 
ATOM   7412 N NZ  . LYS B 1 396 ? 40.796  -19.078 39.236  1.00 38.99 ? 396 LYS B NZ  1 
ATOM   7413 N N   . THR B 1 397 ? 40.924  -21.773 45.240  1.00 15.28 ? 397 THR B N   1 
ATOM   7414 C CA  . THR B 1 397 ? 41.529  -22.352 46.435  1.00 19.26 ? 397 THR B CA  1 
ATOM   7415 C C   . THR B 1 397 ? 42.975  -21.890 46.556  1.00 24.87 ? 397 THR B C   1 
ATOM   7416 O O   . THR B 1 397 ? 43.584  -21.426 45.587  1.00 20.75 ? 397 THR B O   1 
ATOM   7417 C CB  . THR B 1 397 ? 41.478  -23.895 46.439  1.00 20.70 ? 397 THR B CB  1 
ATOM   7418 O OG1 . THR B 1 397 ? 42.452  -24.431 45.526  1.00 20.60 ? 397 THR B OG1 1 
ATOM   7419 C CG2 . THR B 1 397 ? 40.074  -24.421 46.094  1.00 18.68 ? 397 THR B CG2 1 
ATOM   7420 N N   . GLU B 1 398 ? 43.520  -22.021 47.767  1.00 18.02 ? 398 GLU B N   1 
ATOM   7421 C CA  . GLU B 1 398 ? 44.885  -21.591 48.052  1.00 15.50 ? 398 GLU B CA  1 
ATOM   7422 C C   . GLU B 1 398 ? 45.398  -22.344 49.273  1.00 18.88 ? 398 GLU B C   1 
ATOM   7423 O O   . GLU B 1 398 ? 44.638  -22.601 50.207  1.00 16.24 ? 398 GLU B O   1 
ATOM   7424 C CB  . GLU B 1 398 ? 44.949  -20.077 48.299  1.00 16.33 ? 398 GLU B CB  1 
ATOM   7425 C CG  . GLU B 1 398 ? 46.300  -19.590 48.805  1.00 22.92 ? 398 GLU B CG  1 
ATOM   7426 C CD  . GLU B 1 398 ? 46.361  -18.085 49.004  1.00 34.70 ? 398 GLU B CD  1 
ATOM   7427 O OE1 . GLU B 1 398 ? 45.468  -17.375 48.495  1.00 39.65 ? 398 GLU B OE1 1 
ATOM   7428 O OE2 . GLU B 1 398 ? 47.308  -17.610 49.670  1.00 39.16 ? 398 GLU B OE2 1 
ATOM   7429 N N   . VAL B 1 399 ? 46.696  -22.694 49.261  1.00 17.00 ? 399 VAL B N   1 
ATOM   7430 C CA  . VAL B 1 399 ? 47.345  -23.356 50.389  1.00 16.16 ? 399 VAL B CA  1 
ATOM   7431 C C   . VAL B 1 399 ? 47.976  -22.298 51.277  1.00 20.19 ? 399 VAL B C   1 
ATOM   7432 O O   . VAL B 1 399 ? 48.618  -21.366 50.783  1.00 21.41 ? 399 VAL B O   1 
ATOM   7433 C CB  . VAL B 1 399 ? 48.412  -24.361 49.905  1.00 20.39 ? 399 VAL B CB  1 
ATOM   7434 C CG1 . VAL B 1 399 ? 49.171  -24.948 51.091  1.00 22.62 ? 399 VAL B CG1 1 
ATOM   7435 C CG2 . VAL B 1 399 ? 47.775  -25.472 49.057  1.00 17.69 ? 399 VAL B CG2 1 
ATOM   7436 N N   . ILE B 1 400 ? 47.812  -22.442 52.595  1.00 21.71 ? 400 ILE B N   1 
ATOM   7437 C CA  . ILE B 1 400 ? 48.479  -21.565 53.547  1.00 18.93 ? 400 ILE B CA  1 
ATOM   7438 C C   . ILE B 1 400 ? 49.229  -22.414 54.561  1.00 15.14 ? 400 ILE B C   1 
ATOM   7439 O O   . ILE B 1 400 ? 48.785  -23.501 54.946  1.00 14.12 ? 400 ILE B O   1 
ATOM   7440 C CB  . ILE B 1 400 ? 47.491  -20.615 54.248  1.00 23.16 ? 400 ILE B CB  1 
ATOM   7441 C CG1 . ILE B 1 400 ? 46.282  -21.394 54.762  1.00 26.88 ? 400 ILE B CG1 1 
ATOM   7442 C CG2 . ILE B 1 400 ? 47.073  -19.501 53.286  1.00 30.50 ? 400 ILE B CG2 1 
ATOM   7443 C CD1 . ILE B 1 400 ? 45.207  -20.521 55.359  1.00 37.20 ? 400 ILE B CD1 1 
ATOM   7444 N N   . GLU B 1 401 ? 50.379  -21.905 54.999  1.00 15.08 ? 401 GLU B N   1 
ATOM   7445 C CA  . GLU B 1 401 ? 51.271  -22.681 55.845  1.00 15.91 ? 401 GLU B CA  1 
ATOM   7446 C C   . GLU B 1 401 ? 51.245  -22.266 57.311  1.00 15.55 ? 401 GLU B C   1 
ATOM   7447 O O   . GLU B 1 401 ? 51.696  -23.041 58.161  1.00 13.16 ? 401 GLU B O   1 
ATOM   7448 C CB  . GLU B 1 401 ? 52.710  -22.573 55.324  1.00 19.90 ? 401 GLU B CB  1 
ATOM   7449 C CG  . GLU B 1 401 ? 52.890  -23.088 53.891  1.00 29.48 ? 401 GLU B CG  1 
ATOM   7450 C CD  . GLU B 1 401 ? 52.601  -24.572 53.747  1.00 36.51 ? 401 GLU B CD  1 
ATOM   7451 O OE1 . GLU B 1 401 ? 52.139  -24.981 52.661  1.00 39.55 ? 401 GLU B OE1 1 
ATOM   7452 O OE2 . GLU B 1 401 ? 52.836  -25.333 54.707  1.00 36.63 ? 401 GLU B OE2 1 
ATOM   7453 N N   . SER B 1 402 ? 50.738  -21.076 57.633  1.00 12.88 ? 402 SER B N   1 
ATOM   7454 C CA  . SER B 1 402 ? 50.862  -20.570 58.997  1.00 14.00 ? 402 SER B CA  1 
ATOM   7455 C C   . SER B 1 402 ? 49.764  -19.546 59.252  1.00 16.30 ? 402 SER B C   1 
ATOM   7456 O O   . SER B 1 402 ? 49.399  -18.792 58.351  1.00 15.04 ? 402 SER B O   1 
ATOM   7457 C CB  . SER B 1 402 ? 52.245  -19.939 59.227  1.00 18.47 ? 402 SER B CB  1 
ATOM   7458 O OG  . SER B 1 402 ? 52.448  -19.615 60.598  1.00 20.57 ? 402 SER B OG  1 
ATOM   7459 N N   . VAL B 1 403 ? 49.218  -19.545 60.470  1.00 12.59 ? 403 VAL B N   1 
ATOM   7460 C CA  . VAL B 1 403 ? 48.286  -18.498 60.871  1.00 10.77 ? 403 VAL B CA  1 
ATOM   7461 C C   . VAL B 1 403 ? 48.821  -17.807 62.115  1.00 13.08 ? 403 VAL B C   1 
ATOM   7462 O O   . VAL B 1 403 ? 49.581  -18.385 62.895  1.00 12.87 ? 403 VAL B O   1 
ATOM   7463 C CB  . VAL B 1 403 ? 46.855  -19.040 61.114  1.00 12.31 ? 403 VAL B CB  1 
ATOM   7464 C CG1 . VAL B 1 403 ? 46.328  -19.698 59.841  1.00 16.47 ? 403 VAL B CG1 1 
ATOM   7465 C CG2 . VAL B 1 403 ? 46.859  -20.054 62.260  1.00 12.07 ? 403 VAL B CG2 1 
ATOM   7466 N N   . LYS B 1 404 ? 48.436  -16.545 62.282  1.00 14.16 ? 404 LYS B N   1 
ATOM   7467 C CA  . LYS B 1 404 ? 48.714  -15.804 63.500  1.00 12.69 ? 404 LYS B CA  1 
ATOM   7468 C C   . LYS B 1 404 ? 47.554  -16.034 64.464  1.00 11.33 ? 404 LYS B C   1 
ATOM   7469 O O   . LYS B 1 404 ? 46.407  -15.707 64.137  1.00 13.10 ? 404 LYS B O   1 
ATOM   7470 C CB  . LYS B 1 404 ? 48.890  -14.317 63.189  1.00 11.30 ? 404 LYS B CB  1 
ATOM   7471 C CG  . LYS B 1 404 ? 49.250  -13.480 64.392  1.00 24.39 ? 404 LYS B CG  1 
ATOM   7472 C CD  . LYS B 1 404 ? 49.992  -12.225 63.973  1.00 40.74 ? 404 LYS B CD  1 
ATOM   7473 C CE  . LYS B 1 404 ? 51.391  -12.565 63.471  1.00 44.41 ? 404 LYS B CE  1 
ATOM   7474 N NZ  . LYS B 1 404 ? 52.229  -11.347 63.304  1.00 46.12 ? 404 LYS B NZ  1 
ATOM   7475 N N   . ALA B 1 405 ? 47.843  -16.621 65.627  1.00 13.48 ? 405 ALA B N   1 
ATOM   7476 C CA  . ALA B 1 405 ? 46.792  -17.014 66.559  1.00 8.56  ? 405 ALA B CA  1 
ATOM   7477 C C   . ALA B 1 405 ? 45.918  -15.821 66.929  1.00 8.53  ? 405 ALA B C   1 
ATOM   7478 O O   . ALA B 1 405 ? 46.413  -14.707 67.081  1.00 12.21 ? 405 ALA B O   1 
ATOM   7479 C CB  . ALA B 1 405 ? 47.404  -17.611 67.835  1.00 7.68  ? 405 ALA B CB  1 
ATOM   7480 N N   . GLY B 1 406 ? 44.620  -16.064 67.099  1.00 6.94  ? 406 GLY B N   1 
ATOM   7481 C CA  . GLY B 1 406 ? 43.721  -14.992 67.479  1.00 7.64  ? 406 GLY B CA  1 
ATOM   7482 C C   . GLY B 1 406 ? 42.284  -15.466 67.598  1.00 13.80 ? 406 GLY B C   1 
ATOM   7483 O O   . GLY B 1 406 ? 42.001  -16.665 67.594  1.00 9.61  ? 406 GLY B O   1 
ATOM   7484 N N   . THR B 1 407 ? 41.374  -14.491 67.723  1.00 10.12 ? 407 THR B N   1 
ATOM   7485 C CA  . THR B 1 407 ? 39.929  -14.727 67.797  1.00 12.38 ? 407 THR B CA  1 
ATOM   7486 C C   . THR B 1 407 ? 39.224  -13.756 66.867  1.00 12.26 ? 407 THR B C   1 
ATOM   7487 O O   . THR B 1 407 ? 39.841  -12.847 66.303  1.00 10.21 ? 407 THR B O   1 
ATOM   7488 C CB  . THR B 1 407 ? 39.367  -14.533 69.218  1.00 5.86  ? 407 THR B CB  1 
ATOM   7489 O OG1 . THR B 1 407 ? 39.331  -13.131 69.519  1.00 9.12  ? 407 THR B OG1 1 
ATOM   7490 C CG2 . THR B 1 407 ? 40.213  -15.272 70.264  1.00 8.67  ? 407 THR B CG2 1 
ATOM   7491 N N   . TRP B 1 408 ? 37.901  -13.901 66.755  1.00 8.24  ? 408 TRP B N   1 
ATOM   7492 C CA  . TRP B 1 408 ? 37.180  -12.944 65.930  1.00 10.13 ? 408 TRP B CA  1 
ATOM   7493 C C   . TRP B 1 408 ? 36.952  -11.625 66.650  1.00 10.35 ? 408 TRP B C   1 
ATOM   7494 O O   . TRP B 1 408 ? 36.332  -10.718 66.082  1.00 15.24 ? 408 TRP B O   1 
ATOM   7495 C CB  . TRP B 1 408 ? 35.852  -13.542 65.434  1.00 5.82  ? 408 TRP B CB  1 
ATOM   7496 C CG  . TRP B 1 408 ? 34.860  -14.026 66.453  1.00 15.52 ? 408 TRP B CG  1 
ATOM   7497 C CD1 . TRP B 1 408 ? 34.933  -13.930 67.817  1.00 14.87 ? 408 TRP B CD1 1 
ATOM   7498 C CD2 . TRP B 1 408 ? 33.612  -14.665 66.158  1.00 5.68  ? 408 TRP B CD2 1 
ATOM   7499 N NE1 . TRP B 1 408 ? 33.799  -14.492 68.388  1.00 11.55 ? 408 TRP B NE1 1 
ATOM   7500 C CE2 . TRP B 1 408 ? 32.981  -14.950 67.385  1.00 12.42 ? 408 TRP B CE2 1 
ATOM   7501 C CE3 . TRP B 1 408 ? 32.976  -15.042 64.966  1.00 6.87  ? 408 TRP B CE3 1 
ATOM   7502 C CZ2 . TRP B 1 408 ? 31.740  -15.584 67.455  1.00 17.73 ? 408 TRP B CZ2 1 
ATOM   7503 C CZ3 . TRP B 1 408 ? 31.743  -15.672 65.037  1.00 11.93 ? 408 TRP B CZ3 1 
ATOM   7504 C CH2 . TRP B 1 408 ? 31.139  -15.937 66.271  1.00 13.16 ? 408 TRP B CH2 1 
ATOM   7505 N N   . PHE B 1 409 ? 37.434  -11.485 67.879  1.00 9.59  ? 409 PHE B N   1 
ATOM   7506 C CA  . PHE B 1 409 ? 37.416  -10.192 68.564  1.00 11.68 ? 409 PHE B CA  1 
ATOM   7507 C C   . PHE B 1 409 ? 38.793  -9.568  68.387  1.00 17.03 ? 409 PHE B C   1 
ATOM   7508 O O   . PHE B 1 409 ? 39.737  -9.902  69.110  1.00 15.97 ? 409 PHE B O   1 
ATOM   7509 C CB  . PHE B 1 409 ? 37.014  -10.342 70.028  1.00 15.66 ? 409 PHE B CB  1 
ATOM   7510 C CG  . PHE B 1 409 ? 35.530  -10.375 70.208  1.00 28.64 ? 409 PHE B CG  1 
ATOM   7511 C CD1 . PHE B 1 409 ? 34.775  -9.233  70.003  1.00 24.59 ? 409 PHE B CD1 1 
ATOM   7512 C CD2 . PHE B 1 409 ? 34.880  -11.562 70.496  1.00 19.99 ? 409 PHE B CD2 1 
ATOM   7513 C CE1 . PHE B 1 409 ? 33.396  -9.266  70.122  1.00 26.71 ? 409 PHE B CE1 1 
ATOM   7514 C CE2 . PHE B 1 409 ? 33.503  -11.605 70.622  1.00 27.89 ? 409 PHE B CE2 1 
ATOM   7515 C CZ  . PHE B 1 409 ? 32.759  -10.453 70.434  1.00 31.37 ? 409 PHE B CZ  1 
ATOM   7516 N N   . ASP B 1 410 ? 38.902  -8.691  67.379  1.00 18.33 ? 410 ASP B N   1 
ATOM   7517 C CA  . ASP B 1 410 ? 40.109  -7.933  67.045  1.00 19.77 ? 410 ASP B CA  1 
ATOM   7518 C C   . ASP B 1 410 ? 41.301  -8.818  66.724  1.00 17.02 ? 410 ASP B C   1 
ATOM   7519 O O   . ASP B 1 410 ? 42.447  -8.361  66.776  1.00 14.90 ? 410 ASP B O   1 
ATOM   7520 C CB  . ASP B 1 410 ? 40.488  -6.957  68.161  1.00 20.52 ? 410 ASP B CB  1 
ATOM   7521 C CG  . ASP B 1 410 ? 39.350  -6.062  68.541  1.00 35.60 ? 410 ASP B CG  1 
ATOM   7522 O OD1 . ASP B 1 410 ? 38.755  -5.434  67.632  1.00 31.61 ? 410 ASP B OD1 1 
ATOM   7523 O OD2 . ASP B 1 410 ? 39.048  -5.997  69.749  1.00 40.61 ? 410 ASP B OD2 1 
ATOM   7524 N N   . GLY B 1 411 ? 41.077  -10.081 66.388  1.00 10.83 ? 411 GLY B N   1 
ATOM   7525 C CA  . GLY B 1 411 ? 42.212  -10.928 66.087  1.00 10.51 ? 411 GLY B CA  1 
ATOM   7526 C C   . GLY B 1 411 ? 43.085  -11.299 67.269  1.00 12.41 ? 411 GLY B C   1 
ATOM   7527 O O   . GLY B 1 411 ? 44.206  -11.760 67.061  1.00 11.93 ? 411 GLY B O   1 
ATOM   7528 N N   . ASN B 1 412 ? 42.615  -11.130 68.507  1.00 10.63 ? 412 ASN B N   1 
ATOM   7529 C CA  . ASN B 1 412 ? 43.481  -11.374 69.661  1.00 11.57 ? 412 ASN B CA  1 
ATOM   7530 C C   . ASN B 1 412 ? 42.651  -11.916 70.823  1.00 8.05  ? 412 ASN B C   1 
ATOM   7531 O O   . ASN B 1 412 ? 41.460  -12.203 70.685  1.00 12.34 ? 412 ASN B O   1 
ATOM   7532 C CB  . ASN B 1 412 ? 44.285  -10.109 70.032  1.00 17.90 ? 412 ASN B CB  1 
ATOM   7533 C CG  . ASN B 1 412 ? 43.420  -8.972  70.598  1.00 17.59 ? 412 ASN B CG  1 
ATOM   7534 O OD1 . ASN B 1 412 ? 42.533  -9.183  71.427  1.00 16.06 ? 412 ASN B OD1 1 
ATOM   7535 N ND2 . ASN B 1 412 ? 43.730  -7.737  70.182  1.00 16.26 ? 412 ASN B ND2 1 
ATOM   7536 N N   . PHE B 1 413 ? 43.303  -12.101 71.972  1.00 7.75  ? 413 PHE B N   1 
ATOM   7537 C CA  . PHE B 1 413 ? 42.685  -12.795 73.101  1.00 9.73  ? 413 PHE B CA  1 
ATOM   7538 C C   . PHE B 1 413 ? 42.350  -11.879 74.274  1.00 13.83 ? 413 PHE B C   1 
ATOM   7539 O O   . PHE B 1 413 ? 42.050  -12.381 75.358  1.00 9.88  ? 413 PHE B O   1 
ATOM   7540 C CB  . PHE B 1 413 ? 43.600  -13.927 73.588  1.00 10.19 ? 413 PHE B CB  1 
ATOM   7541 C CG  . PHE B 1 413 ? 43.801  -15.027 72.575  1.00 13.14 ? 413 PHE B CG  1 
ATOM   7542 C CD1 . PHE B 1 413 ? 42.913  -16.098 72.509  1.00 11.42 ? 413 PHE B CD1 1 
ATOM   7543 C CD2 . PHE B 1 413 ? 44.874  -14.979 71.680  1.00 11.94 ? 413 PHE B CD2 1 
ATOM   7544 C CE1 . PHE B 1 413 ? 43.101  -17.114 71.568  1.00 10.88 ? 413 PHE B CE1 1 
ATOM   7545 C CE2 . PHE B 1 413 ? 45.072  -15.982 70.748  1.00 7.54  ? 413 PHE B CE2 1 
ATOM   7546 C CZ  . PHE B 1 413 ? 44.177  -17.054 70.688  1.00 9.63  ? 413 PHE B CZ  1 
ATOM   7547 N N   . LEU B 1 414 ? 42.380  -10.553 74.095  1.00 8.51  ? 414 LEU B N   1 
ATOM   7548 C CA  . LEU B 1 414 ? 42.234  -9.659  75.251  1.00 8.13  ? 414 LEU B CA  1 
ATOM   7549 C C   . LEU B 1 414 ? 40.848  -9.705  75.911  1.00 14.20 ? 414 LEU B C   1 
ATOM   7550 O O   . LEU B 1 414 ? 40.706  -9.234  77.053  1.00 10.72 ? 414 LEU B O   1 
ATOM   7551 C CB  . LEU B 1 414 ? 42.571  -8.228  74.829  1.00 13.00 ? 414 LEU B CB  1 
ATOM   7552 C CG  . LEU B 1 414 ? 44.023  -8.002  74.400  1.00 11.92 ? 414 LEU B CG  1 
ATOM   7553 C CD1 . LEU B 1 414 ? 44.255  -6.528  73.989  1.00 14.29 ? 414 LEU B CD1 1 
ATOM   7554 C CD2 . LEU B 1 414 ? 44.977  -8.418  75.523  1.00 14.54 ? 414 LEU B CD2 1 
ATOM   7555 N N   . LYS B 1 415 ? 39.825  -10.263 75.246  1.00 8.91  ? 415 LYS B N   1 
ATOM   7556 C CA  . LYS B 1 415 ? 38.520  -10.385 75.892  1.00 12.39 ? 415 LYS B CA  1 
ATOM   7557 C C   . LYS B 1 415 ? 38.487  -11.457 76.966  1.00 16.50 ? 415 LYS B C   1 
ATOM   7558 O O   . LYS B 1 415 ? 37.522  -11.497 77.741  1.00 9.59  ? 415 LYS B O   1 
ATOM   7559 C CB  . LYS B 1 415 ? 37.429  -10.687 74.864  1.00 12.45 ? 415 LYS B CB  1 
ATOM   7560 C CG  . LYS B 1 415 ? 37.093  -9.481  73.997  1.00 17.02 ? 415 LYS B CG  1 
ATOM   7561 C CD  . LYS B 1 415 ? 36.290  -8.478  74.814  1.00 29.38 ? 415 LYS B CD  1 
ATOM   7562 C CE  . LYS B 1 415 ? 35.717  -7.369  73.947  1.00 38.01 ? 415 LYS B CE  1 
ATOM   7563 N NZ  . LYS B 1 415 ? 35.149  -6.277  74.800  1.00 36.42 ? 415 LYS B NZ  1 
ATOM   7564 N N   . TRP B 1 416 ? 39.500  -12.325 77.032  1.00 6.90  ? 416 TRP B N   1 
ATOM   7565 C CA  . TRP B 1 416 ? 39.489  -13.449 77.969  1.00 9.08  ? 416 TRP B CA  1 
ATOM   7566 C C   . TRP B 1 416 ? 40.716  -13.513 78.868  1.00 8.36  ? 416 TRP B C   1 
ATOM   7567 O O   . TRP B 1 416 ? 40.742  -14.333 79.793  1.00 7.09  ? 416 TRP B O   1 
ATOM   7568 C CB  . TRP B 1 416 ? 39.370  -14.787 77.212  1.00 10.75 ? 416 TRP B CB  1 
ATOM   7569 C CG  . TRP B 1 416 ? 38.175  -14.830 76.316  1.00 8.00  ? 416 TRP B CG  1 
ATOM   7570 C CD1 . TRP B 1 416 ? 36.926  -15.270 76.634  1.00 5.93  ? 416 TRP B CD1 1 
ATOM   7571 C CD2 . TRP B 1 416 ? 38.114  -14.379 74.960  1.00 9.41  ? 416 TRP B CD2 1 
ATOM   7572 N NE1 . TRP B 1 416 ? 36.085  -15.139 75.548  1.00 5.82  ? 416 TRP B NE1 1 
ATOM   7573 C CE2 . TRP B 1 416 ? 36.794  -14.580 74.511  1.00 8.36  ? 416 TRP B CE2 1 
ATOM   7574 C CE3 . TRP B 1 416 ? 39.059  -13.836 74.075  1.00 9.65  ? 416 TRP B CE3 1 
ATOM   7575 C CZ2 . TRP B 1 416 ? 36.379  -14.226 73.220  1.00 7.31  ? 416 TRP B CZ2 1 
ATOM   7576 C CZ3 . TRP B 1 416 ? 38.644  -13.494 72.783  1.00 8.33  ? 416 TRP B CZ3 1 
ATOM   7577 C CH2 . TRP B 1 416 ? 37.326  -13.714 72.366  1.00 7.94  ? 416 TRP B CH2 1 
ATOM   7578 N N   . ILE B 1 417 ? 41.730  -12.684 78.632  1.00 8.32  ? 417 ILE B N   1 
ATOM   7579 C CA  . ILE B 1 417 ? 42.975  -12.744 79.393  1.00 9.21  ? 417 ILE B CA  1 
ATOM   7580 C C   . ILE B 1 417 ? 43.635  -11.383 79.267  1.00 17.12 ? 417 ILE B C   1 
ATOM   7581 O O   . ILE B 1 417 ? 43.393  -10.648 78.310  1.00 11.19 ? 417 ILE B O   1 
ATOM   7582 C CB  . ILE B 1 417 ? 43.902  -13.876 78.877  1.00 11.95 ? 417 ILE B CB  1 
ATOM   7583 C CG1 . ILE B 1 417 ? 45.006  -14.199 79.889  1.00 7.31  ? 417 ILE B CG1 1 
ATOM   7584 C CG2 . ILE B 1 417 ? 44.525  -13.488 77.530  1.00 14.26 ? 417 ILE B CG2 1 
ATOM   7585 C CD1 . ILE B 1 417 ? 45.575  -15.624 79.725  1.00 7.94  ? 417 ILE B CD1 1 
ATOM   7586 N N   . GLY B 1 418 ? 44.476  -11.038 80.241  1.00 15.81 ? 418 GLY B N   1 
ATOM   7587 C CA  . GLY B 1 418 ? 45.369  -9.899  80.125  1.00 13.48 ? 418 GLY B CA  1 
ATOM   7588 C C   . GLY B 1 418 ? 45.156  -8.780  81.124  1.00 21.20 ? 418 GLY B C   1 
ATOM   7589 O O   . GLY B 1 418 ? 46.033  -7.915  81.246  1.00 32.40 ? 418 GLY B O   1 
ATOM   7590 N N   . ASN B 1 419 ? 44.044  -8.748  81.847  1.00 18.25 ? 419 ASN B N   1 
ATOM   7591 C CA  . ASN B 1 419 ? 43.881  -7.748  82.897  1.00 22.19 ? 419 ASN B CA  1 
ATOM   7592 C C   . ASN B 1 419 ? 43.831  -8.465  84.237  1.00 25.39 ? 419 ASN B C   1 
ATOM   7593 O O   . ASN B 1 419 ? 43.783  -9.695  84.290  1.00 19.54 ? 419 ASN B O   1 
ATOM   7594 C CB  . ASN B 1 419 ? 42.647  -6.854  82.649  1.00 27.45 ? 419 ASN B CB  1 
ATOM   7595 C CG  . ASN B 1 419 ? 41.315  -7.577  82.816  1.00 24.84 ? 419 ASN B CG  1 
ATOM   7596 O OD1 . ASN B 1 419 ? 41.217  -8.606  83.476  1.00 23.35 ? 419 ASN B OD1 1 
ATOM   7597 N ND2 . ASN B 1 419 ? 40.264  -6.997  82.245  1.00 29.37 ? 419 ASN B ND2 1 
ATOM   7598 N N   . LYS B 1 420 ? 43.881  -7.695  85.331  1.00 19.43 ? 420 LYS B N   1 
ATOM   7599 C CA  . LYS B 1 420 ? 44.029  -8.327  86.641  1.00 20.50 ? 420 LYS B CA  1 
ATOM   7600 C C   . LYS B 1 420 ? 42.876  -9.269  86.931  1.00 21.21 ? 420 LYS B C   1 
ATOM   7601 O O   . LYS B 1 420 ? 43.086  -10.392 87.409  1.00 20.60 ? 420 LYS B O   1 
ATOM   7602 C CB  . LYS B 1 420 ? 44.148  -7.274  87.749  1.00 26.21 ? 420 LYS B CB  1 
ATOM   7603 C CG  . LYS B 1 420 ? 45.504  -6.583  87.780  1.00 40.10 ? 420 LYS B CG  1 
ATOM   7604 C CD  . LYS B 1 420 ? 45.767  -5.885  89.104  1.00 45.76 ? 420 LYS B CD  1 
ATOM   7605 C CE  . LYS B 1 420 ? 47.120  -5.173  89.082  1.00 52.07 ? 420 LYS B CE  1 
ATOM   7606 N NZ  . LYS B 1 420 ? 47.602  -4.833  90.456  1.00 53.98 ? 420 LYS B NZ  1 
ATOM   7607 N N   . GLU B 1 421 ? 41.649  -8.841  86.620  1.00 15.41 ? 421 GLU B N   1 
ATOM   7608 C CA  . GLU B 1 421 ? 40.490  -9.638  86.984  1.00 14.27 ? 421 GLU B CA  1 
ATOM   7609 C C   . GLU B 1 421 ? 40.430  -10.936 86.182  1.00 13.24 ? 421 GLU B C   1 
ATOM   7610 O O   . GLU B 1 421 ? 40.180  -12.010 86.740  1.00 15.27 ? 421 GLU B O   1 
ATOM   7611 C CB  . GLU B 1 421 ? 39.215  -8.817  86.789  1.00 32.38 ? 421 GLU B CB  1 
ATOM   7612 C CG  . GLU B 1 421 ? 38.262  -8.901  87.962  1.00 51.09 ? 421 GLU B CG  1 
ATOM   7613 C CD  . GLU B 1 421 ? 38.870  -8.376  89.242  1.00 66.80 ? 421 GLU B CD  1 
ATOM   7614 O OE1 . GLU B 1 421 ? 39.274  -7.194  89.265  1.00 73.00 ? 421 GLU B OE1 1 
ATOM   7615 O OE2 . GLU B 1 421 ? 38.953  -9.151  90.223  1.00 73.86 ? 421 GLU B OE2 1 
ATOM   7616 N N   . LYS B 1 422 ? 40.622  -10.856 84.870  1.00 13.76 ? 422 LYS B N   1 
ATOM   7617 C CA  . LYS B 1 422 ? 40.606  -12.081 84.073  1.00 8.50  ? 422 LYS B CA  1 
ATOM   7618 C C   . LYS B 1 422 ? 41.786  -12.984 84.418  1.00 9.84  ? 422 LYS B C   1 
ATOM   7619 O O   . LYS B 1 422 ? 41.628  -14.211 84.482  1.00 14.91 ? 422 LYS B O   1 
ATOM   7620 C CB  . LYS B 1 422 ? 40.586  -11.737 82.584  1.00 10.93 ? 422 LYS B CB  1 
ATOM   7621 C CG  . LYS B 1 422 ? 39.237  -11.178 82.143  1.00 8.49  ? 422 LYS B CG  1 
ATOM   7622 C CD  . LYS B 1 422 ? 39.249  -10.636 80.729  1.00 6.34  ? 422 LYS B CD  1 
ATOM   7623 C CE  . LYS B 1 422 ? 37.852  -10.052 80.399  1.00 16.19 ? 422 LYS B CE  1 
ATOM   7624 N NZ  . LYS B 1 422 ? 38.049  -8.967  79.427  1.00 31.79 ? 422 LYS B NZ  1 
ATOM   7625 N N   . ASN B 1 423 ? 42.977  -12.404 84.643  1.00 10.75 ? 423 ASN B N   1 
ATOM   7626 C CA  . ASN B 1 423 ? 44.133  -13.218 85.013  1.00 12.43 ? 423 ASN B CA  1 
ATOM   7627 C C   . ASN B 1 423 ? 43.918  -13.918 86.344  1.00 12.77 ? 423 ASN B C   1 
ATOM   7628 O O   . ASN B 1 423 ? 44.485  -14.993 86.583  1.00 10.60 ? 423 ASN B O   1 
ATOM   7629 C CB  . ASN B 1 423 ? 45.401  -12.362 85.075  1.00 12.42 ? 423 ASN B CB  1 
ATOM   7630 C CG  . ASN B 1 423 ? 45.942  -12.027 83.704  1.00 12.14 ? 423 ASN B CG  1 
ATOM   7631 O OD1 . ASN B 1 423 ? 45.344  -12.365 82.681  1.00 12.46 ? 423 ASN B OD1 1 
ATOM   7632 N ND2 . ASN B 1 423 ? 47.073  -11.349 83.675  1.00 16.40 ? 423 ASN B ND2 1 
ATOM   7633 N N   . GLU B 1 424 ? 43.091  -13.346 87.219  1.00 11.01 ? 424 GLU B N   1 
ATOM   7634 C CA  . GLU B 1 424 ? 42.810  -14.038 88.472  1.00 16.81 ? 424 GLU B CA  1 
ATOM   7635 C C   . GLU B 1 424 ? 42.059  -15.339 88.221  1.00 15.13 ? 424 GLU B C   1 
ATOM   7636 O O   . GLU B 1 424 ? 42.310  -16.349 88.890  1.00 11.27 ? 424 GLU B O   1 
ATOM   7637 C CB  . GLU B 1 424 ? 42.015  -13.137 89.413  1.00 16.94 ? 424 GLU B CB  1 
ATOM   7638 C CG  . GLU B 1 424 ? 41.529  -13.834 90.677  1.00 27.13 ? 424 GLU B CG  1 
ATOM   7639 C CD  . GLU B 1 424 ? 42.643  -14.254 91.619  1.00 39.17 ? 424 GLU B CD  1 
ATOM   7640 O OE1 . GLU B 1 424 ? 43.774  -13.725 91.500  1.00 43.08 ? 424 GLU B OE1 1 
ATOM   7641 O OE2 . GLU B 1 424 ? 42.372  -15.101 92.498  1.00 35.01 ? 424 GLU B OE2 1 
ATOM   7642 N N   . TYR B 1 425 ? 41.134  -15.335 87.261  1.00 13.75 ? 425 TYR B N   1 
ATOM   7643 C CA  . TYR B 1 425 ? 40.430  -16.568 86.932  1.00 9.59  ? 425 TYR B CA  1 
ATOM   7644 C C   . TYR B 1 425 ? 41.384  -17.608 86.360  1.00 11.82 ? 425 TYR B C   1 
ATOM   7645 O O   . TYR B 1 425 ? 41.297  -18.787 86.707  1.00 7.28  ? 425 TYR B O   1 
ATOM   7646 C CB  . TYR B 1 425 ? 39.309  -16.297 85.935  1.00 12.68 ? 425 TYR B CB  1 
ATOM   7647 C CG  . TYR B 1 425 ? 37.951  -16.064 86.533  1.00 8.11  ? 425 TYR B CG  1 
ATOM   7648 C CD1 . TYR B 1 425 ? 37.798  -15.463 87.776  1.00 15.56 ? 425 TYR B CD1 1 
ATOM   7649 C CD2 . TYR B 1 425 ? 36.804  -16.432 85.833  1.00 9.43  ? 425 TYR B CD2 1 
ATOM   7650 C CE1 . TYR B 1 425 ? 36.529  -15.256 88.313  1.00 10.46 ? 425 TYR B CE1 1 
ATOM   7651 C CE2 . TYR B 1 425 ? 35.540  -16.211 86.348  1.00 14.39 ? 425 TYR B CE2 1 
ATOM   7652 C CZ  . TYR B 1 425 ? 35.411  -15.622 87.582  1.00 17.22 ? 425 TYR B CZ  1 
ATOM   7653 O OH  . TYR B 1 425 ? 34.152  -15.405 88.080  1.00 14.38 ? 425 TYR B OH  1 
ATOM   7654 N N   . TRP B 1 426 ? 42.282  -17.206 85.457  1.00 8.07  ? 426 TRP B N   1 
ATOM   7655 C CA  . TRP B 1 426 ? 43.229  -18.187 84.928  1.00 7.37  ? 426 TRP B CA  1 
ATOM   7656 C C   . TRP B 1 426 ? 44.116  -18.717 86.038  1.00 6.14  ? 426 TRP B C   1 
ATOM   7657 O O   . TRP B 1 426 ? 44.431  -19.910 86.086  1.00 9.59  ? 426 TRP B O   1 
ATOM   7658 C CB  . TRP B 1 426 ? 44.081  -17.584 83.817  1.00 8.94  ? 426 TRP B CB  1 
ATOM   7659 C CG  . TRP B 1 426 ? 43.328  -17.429 82.532  1.00 8.38  ? 426 TRP B CG  1 
ATOM   7660 C CD1 . TRP B 1 426 ? 42.802  -16.279 82.029  1.00 9.43  ? 426 TRP B CD1 1 
ATOM   7661 C CD2 . TRP B 1 426 ? 43.025  -18.462 81.586  1.00 9.08  ? 426 TRP B CD2 1 
ATOM   7662 N NE1 . TRP B 1 426 ? 42.186  -16.532 80.814  1.00 10.89 ? 426 TRP B NE1 1 
ATOM   7663 C CE2 . TRP B 1 426 ? 42.308  -17.867 80.531  1.00 11.03 ? 426 TRP B CE2 1 
ATOM   7664 C CE3 . TRP B 1 426 ? 43.276  -19.835 81.540  1.00 8.98  ? 426 TRP B CE3 1 
ATOM   7665 C CZ2 . TRP B 1 426 ? 41.841  -18.597 79.438  1.00 14.72 ? 426 TRP B CZ2 1 
ATOM   7666 C CZ3 . TRP B 1 426 ? 42.814  -20.558 80.459  1.00 9.05  ? 426 TRP B CZ3 1 
ATOM   7667 C CH2 . TRP B 1 426 ? 42.110  -19.936 79.415  1.00 10.15 ? 426 TRP B CH2 1 
ATOM   7668 N N   . LYS B 1 427 ? 44.510  -17.845 86.956  1.00 7.41  ? 427 LYS B N   1 
ATOM   7669 C CA  . LYS B 1 427 ? 45.274  -18.281 88.119  1.00 11.09 ? 427 LYS B CA  1 
ATOM   7670 C C   . LYS B 1 427 ? 44.536  -19.324 88.933  1.00 11.02 ? 427 LYS B C   1 
ATOM   7671 O O   . LYS B 1 427 ? 45.130  -20.312 89.385  1.00 8.96  ? 427 LYS B O   1 
ATOM   7672 C CB  . LYS B 1 427 ? 45.547  -17.094 89.012  1.00 23.15 ? 427 LYS B CB  1 
ATOM   7673 C CG  . LYS B 1 427 ? 46.506  -17.467 90.049  1.00 41.75 ? 427 LYS B CG  1 
ATOM   7674 C CD  . LYS B 1 427 ? 47.753  -16.575 89.994  1.00 52.67 ? 427 LYS B CD  1 
ATOM   7675 C CE  . LYS B 1 427 ? 48.683  -16.990 88.942  1.00 55.70 ? 427 LYS B CE  1 
ATOM   7676 N NZ  . LYS B 1 427 ? 50.016  -16.335 88.809  1.00 45.27 ? 427 LYS B NZ  1 
ATOM   7677 N N   . ILE B 1 428 ? 43.253  -19.073 89.182  1.00 8.81  ? 428 ILE B N   1 
ATOM   7678 C CA  . ILE B 1 428 ? 42.436  -20.021 89.925  1.00 13.76 ? 428 ILE B CA  1 
ATOM   7679 C C   . ILE B 1 428 ? 42.353  -21.342 89.177  1.00 10.10 ? 428 ILE B C   1 
ATOM   7680 O O   . ILE B 1 428 ? 42.514  -22.421 89.760  1.00 12.07 ? 428 ILE B O   1 
ATOM   7681 C CB  . ILE B 1 428 ? 41.041  -19.427 90.159  1.00 9.56  ? 428 ILE B CB  1 
ATOM   7682 C CG1 . ILE B 1 428 ? 41.102  -18.333 91.214  1.00 17.16 ? 428 ILE B CG1 1 
ATOM   7683 C CG2 . ILE B 1 428 ? 40.045  -20.521 90.536  1.00 12.87 ? 428 ILE B CG2 1 
ATOM   7684 C CD1 . ILE B 1 428 ? 39.800  -17.656 91.366  1.00 19.31 ? 428 ILE B CD1 1 
ATOM   7685 N N   . LEU B 1 429 ? 42.108  -21.266 87.863  1.00 9.01  ? 429 LEU B N   1 
ATOM   7686 C CA  . LEU B 1 429 ? 42.047  -22.466 87.033  1.00 12.12 ? 429 LEU B CA  1 
ATOM   7687 C C   . LEU B 1 429 ? 43.353  -23.249 87.072  1.00 11.24 ? 429 LEU B C   1 
ATOM   7688 O O   . LEU B 1 429 ? 43.351  -24.482 87.167  1.00 11.68 ? 429 LEU B O   1 
ATOM   7689 C CB  . LEU B 1 429 ? 41.722  -22.073 85.590  1.00 9.48  ? 429 LEU B CB  1 
ATOM   7690 C CG  . LEU B 1 429 ? 41.537  -23.260 84.663  1.00 10.26 ? 429 LEU B CG  1 
ATOM   7691 C CD1 . LEU B 1 429 ? 40.228  -23.978 84.994  1.00 15.54 ? 429 LEU B CD1 1 
ATOM   7692 C CD2 . LEU B 1 429 ? 41.564  -22.781 83.192  1.00 12.42 ? 429 LEU B CD2 1 
ATOM   7693 N N   . ILE B 1 430 ? 44.483  -22.551 86.952  1.00 10.16 ? 430 ILE B N   1 
ATOM   7694 C CA  . ILE B 1 430 ? 45.772  -23.239 86.931  1.00 10.37 ? 430 ILE B CA  1 
ATOM   7695 C C   . ILE B 1 430 ? 45.995  -23.988 88.240  1.00 10.73 ? 430 ILE B C   1 
ATOM   7696 O O   . ILE B 1 430 ? 46.394  -25.160 88.246  1.00 9.50  ? 430 ILE B O   1 
ATOM   7697 C CB  . ILE B 1 430 ? 46.901  -22.235 86.640  1.00 14.78 ? 430 ILE B CB  1 
ATOM   7698 C CG1 . ILE B 1 430 ? 46.903  -21.860 85.154  1.00 11.51 ? 430 ILE B CG1 1 
ATOM   7699 C CG2 . ILE B 1 430 ? 48.268  -22.808 87.046  1.00 15.71 ? 430 ILE B CG2 1 
ATOM   7700 C CD1 . ILE B 1 430 ? 47.471  -20.479 84.901  1.00 10.37 ? 430 ILE B CD1 1 
ATOM   7701 N N   . GLU B 1 431 ? 45.680  -23.349 89.366  1.00 13.62 ? 431 GLU B N   1 
ATOM   7702 C CA  . GLU B 1 431 ? 45.902  -24.000 90.652  1.00 13.60 ? 431 GLU B CA  1 
ATOM   7703 C C   . GLU B 1 431 ? 44.946  -25.172 90.844  1.00 20.35 ? 431 GLU B C   1 
ATOM   7704 O O   . GLU B 1 431 ? 45.346  -26.234 91.344  1.00 15.05 ? 431 GLU B O   1 
ATOM   7705 C CB  . GLU B 1 431 ? 45.769  -22.970 91.779  1.00 19.21 ? 431 GLU B CB  1 
ATOM   7706 C CG  . GLU B 1 431 ? 46.028  -23.516 93.173  1.00 29.52 ? 431 GLU B CG  1 
ATOM   7707 C CD  . GLU B 1 431 ? 47.361  -24.255 93.290  1.00 44.92 ? 431 GLU B CD  1 
ATOM   7708 O OE1 . GLU B 1 431 ? 47.368  -25.353 93.885  1.00 45.46 ? 431 GLU B OE1 1 
ATOM   7709 O OE2 . GLU B 1 431 ? 48.397  -23.741 92.801  1.00 39.33 ? 431 GLU B OE2 1 
ATOM   7710 N N   . ALA B 1 432 ? 43.689  -25.020 90.405  1.00 15.81 ? 432 ALA B N   1 
ATOM   7711 C CA  . ALA B 1 432 ? 42.735  -26.119 90.512  1.00 11.98 ? 432 ALA B CA  1 
ATOM   7712 C C   . ALA B 1 432 ? 43.096  -27.281 89.596  1.00 19.12 ? 432 ALA B C   1 
ATOM   7713 O O   . ALA B 1 432 ? 42.820  -28.439 89.929  1.00 11.55 ? 432 ALA B O   1 
ATOM   7714 C CB  . ALA B 1 432 ? 41.319  -25.613 90.212  1.00 14.00 ? 432 ALA B CB  1 
ATOM   7715 N N   . LYS B 1 433 ? 43.720  -27.004 88.446  1.00 10.30 ? 433 LYS B N   1 
ATOM   7716 C CA  . LYS B 1 433 ? 44.093  -28.084 87.542  1.00 13.97 ? 433 LYS B CA  1 
ATOM   7717 C C   . LYS B 1 433 ? 45.132  -28.998 88.180  1.00 15.32 ? 433 LYS B C   1 
ATOM   7718 O O   . LYS B 1 433 ? 45.119  -30.213 87.950  1.00 14.54 ? 433 LYS B O   1 
ATOM   7719 C CB  . LYS B 1 433 ? 44.598  -27.503 86.214  1.00 13.66 ? 433 LYS B CB  1 
ATOM   7720 C CG  . LYS B 1 433 ? 45.209  -28.517 85.250  1.00 11.53 ? 433 LYS B CG  1 
ATOM   7721 C CD  . LYS B 1 433 ? 44.173  -29.505 84.737  1.00 13.69 ? 433 LYS B CD  1 
ATOM   7722 C CE  . LYS B 1 433 ? 44.790  -30.477 83.710  1.00 10.51 ? 433 LYS B CE  1 
ATOM   7723 N NZ  . LYS B 1 433 ? 43.861  -31.603 83.366  1.00 14.84 ? 433 LYS B NZ  1 
ATOM   7724 N N   . LYS B 1 434 ? 46.023  -28.440 89.000  1.00 17.16 ? 434 LYS B N   1 
ATOM   7725 C CA  . LYS B 1 434 ? 47.008  -29.273 89.684  1.00 24.10 ? 434 LYS B CA  1 
ATOM   7726 C C   . LYS B 1 434 ? 46.348  -30.350 90.538  1.00 21.52 ? 434 LYS B C   1 
ATOM   7727 O O   . LYS B 1 434 ? 46.943  -31.404 90.769  1.00 32.11 ? 434 LYS B O   1 
ATOM   7728 C CB  . LYS B 1 434 ? 47.903  -28.413 90.575  1.00 15.82 ? 434 LYS B CB  1 
ATOM   7729 C CG  . LYS B 1 434 ? 48.785  -27.430 89.861  1.00 18.91 ? 434 LYS B CG  1 
ATOM   7730 C CD  . LYS B 1 434 ? 49.617  -26.665 90.887  1.00 28.84 ? 434 LYS B CD  1 
ATOM   7731 C CE  . LYS B 1 434 ? 50.376  -25.505 90.264  1.00 30.04 ? 434 LYS B CE  1 
ATOM   7732 N NZ  . LYS B 1 434 ? 51.036  -24.671 91.322  1.00 36.10 ? 434 LYS B NZ  1 
ATOM   7733 N N   . LYS B 1 435 ? 45.137  -30.088 91.042  1.00 18.58 ? 435 LYS B N   1 
ATOM   7734 C CA  . LYS B 1 435 ? 44.440  -30.991 91.954  1.00 20.42 ? 435 LYS B CA  1 
ATOM   7735 C C   . LYS B 1 435 ? 43.143  -31.549 91.370  1.00 28.16 ? 435 LYS B C   1 
ATOM   7736 O O   . LYS B 1 435 ? 42.353  -32.162 92.107  1.00 19.20 ? 435 LYS B O   1 
ATOM   7737 C CB  . LYS B 1 435 ? 44.134  -30.279 93.277  1.00 29.02 ? 435 LYS B CB  1 
ATOM   7738 C CG  . LYS B 1 435 ? 45.159  -29.234 93.700  1.00 36.79 ? 435 LYS B CG  1 
ATOM   7739 C CD  . LYS B 1 435 ? 45.052  -28.936 95.188  1.00 44.66 ? 435 LYS B CD  1 
ATOM   7740 C CE  . LYS B 1 435 ? 45.953  -27.783 95.602  1.00 50.72 ? 435 LYS B CE  1 
ATOM   7741 N NZ  . LYS B 1 435 ? 46.617  -28.049 96.915  1.00 53.97 ? 435 LYS B NZ  1 
ATOM   7742 N N   . ALA B 1 436 ? 42.903  -31.371 90.075  1.00 16.34 ? 436 ALA B N   1 
ATOM   7743 C CA  . ALA B 1 436 ? 41.632  -31.794 89.502  1.00 18.34 ? 436 ALA B CA  1 
ATOM   7744 C C   . ALA B 1 436 ? 41.488  -33.312 89.541  1.00 21.86 ? 436 ALA B C   1 
ATOM   7745 O O   . ALA B 1 436 ? 42.452  -34.052 89.334  1.00 25.87 ? 436 ALA B O   1 
ATOM   7746 C CB  . ALA B 1 436 ? 41.498  -31.279 88.065  1.00 17.44 ? 436 ALA B CB  1 
ATOM   7747 N N   . LYS B 1 437 ? 40.265  -33.769 89.818  1.00 16.80 ? 437 LYS B N   1 
ATOM   7748 C CA  . LYS B 1 437 ? 39.949  -35.187 89.932  1.00 20.37 ? 437 LYS B CA  1 
ATOM   7749 C C   . LYS B 1 437 ? 38.822  -35.632 89.007  1.00 26.36 ? 437 LYS B C   1 
ATOM   7750 O O   . LYS B 1 437 ? 38.530  -36.832 88.939  1.00 27.01 ? 437 LYS B O   1 
ATOM   7751 C CB  . LYS B 1 437 ? 39.591  -35.533 91.388  1.00 23.59 ? 437 LYS B CB  1 
ATOM   7752 C CG  . LYS B 1 437 ? 40.781  -35.470 92.347  1.00 26.97 ? 437 LYS B CG  1 
ATOM   7753 C CD  . LYS B 1 437 ? 40.467  -34.679 93.601  1.00 39.41 ? 437 LYS B CD  1 
ATOM   7754 C CE  . LYS B 1 437 ? 41.741  -34.312 94.371  1.00 37.75 ? 437 LYS B CE  1 
ATOM   7755 N NZ  . LYS B 1 437 ? 41.825  -32.833 94.667  1.00 30.53 ? 437 LYS B NZ  1 
ATOM   7756 N N   . ASN B 1 438 ? 38.188  -34.714 88.286  1.00 19.44 ? 438 ASN B N   1 
ATOM   7757 C CA  . ASN B 1 438 ? 37.058  -35.068 87.442  1.00 20.60 ? 438 ASN B CA  1 
ATOM   7758 C C   . ASN B 1 438 ? 36.902  -34.000 86.364  1.00 23.60 ? 438 ASN B C   1 
ATOM   7759 O O   . ASN B 1 438 ? 37.599  -32.980 86.371  1.00 17.21 ? 438 ASN B O   1 
ATOM   7760 C CB  . ASN B 1 438 ? 35.784  -35.215 88.278  1.00 22.12 ? 438 ASN B CB  1 
ATOM   7761 C CG  . ASN B 1 438 ? 35.458  -33.959 89.051  1.00 18.92 ? 438 ASN B CG  1 
ATOM   7762 O OD1 . ASN B 1 438 ? 35.195  -32.916 88.460  1.00 17.56 ? 438 ASN B OD1 1 
ATOM   7763 N ND2 . ASN B 1 438 ? 35.473  -34.048 90.375  1.00 16.11 ? 438 ASN B ND2 1 
ATOM   7764 N N   . ASP B 1 439 ? 35.933  -34.221 85.472  1.00 15.76 ? 439 ASP B N   1 
ATOM   7765 C CA  . ASP B 1 439 ? 35.759  -33.420 84.266  1.00 19.62 ? 439 ASP B CA  1 
ATOM   7766 C C   . ASP B 1 439 ? 35.093  -32.072 84.527  1.00 15.97 ? 439 ASP B C   1 
ATOM   7767 O O   . ASP B 1 439 ? 34.838  -31.320 83.577  1.00 12.97 ? 439 ASP B O   1 
ATOM   7768 C CB  . ASP B 1 439 ? 34.958  -34.210 83.226  1.00 21.10 ? 439 ASP B CB  1 
ATOM   7769 C CG  . ASP B 1 439 ? 35.824  -35.194 82.439  1.00 31.24 ? 439 ASP B CG  1 
ATOM   7770 O OD1 . ASP B 1 439 ? 37.055  -35.239 82.652  1.00 28.27 ? 439 ASP B OD1 1 
ATOM   7771 O OD2 . ASP B 1 439 ? 35.269  -35.921 81.594  1.00 31.02 ? 439 ASP B OD2 1 
ATOM   7772 N N   . TYR B 1 440 ? 34.816  -31.726 85.780  1.00 15.05 ? 440 TYR B N   1 
ATOM   7773 C CA  . TYR B 1 440 ? 34.356  -30.369 86.022  1.00 13.20 ? 440 TYR B CA  1 
ATOM   7774 C C   . TYR B 1 440 ? 35.464  -29.354 85.771  1.00 11.98 ? 440 TYR B C   1 
ATOM   7775 O O   . TYR B 1 440 ? 35.164  -28.171 85.570  1.00 10.89 ? 440 TYR B O   1 
ATOM   7776 C CB  . TYR B 1 440 ? 33.782  -30.235 87.438  1.00 12.28 ? 440 TYR B CB  1 
ATOM   7777 C CG  . TYR B 1 440 ? 32.288  -30.489 87.482  1.00 16.54 ? 440 TYR B CG  1 
ATOM   7778 C CD1 . TYR B 1 440 ? 31.389  -29.560 86.979  1.00 18.05 ? 440 TYR B CD1 1 
ATOM   7779 C CD2 . TYR B 1 440 ? 31.774  -31.678 87.992  1.00 18.42 ? 440 TYR B CD2 1 
ATOM   7780 C CE1 . TYR B 1 440 ? 30.007  -29.799 87.007  1.00 22.34 ? 440 TYR B CE1 1 
ATOM   7781 C CE2 . TYR B 1 440 ? 30.392  -31.917 88.023  1.00 14.07 ? 440 TYR B CE2 1 
ATOM   7782 C CZ  . TYR B 1 440 ? 29.527  -30.976 87.534  1.00 28.16 ? 440 TYR B CZ  1 
ATOM   7783 O OH  . TYR B 1 440 ? 28.171  -31.222 87.571  1.00 31.64 ? 440 TYR B OH  1 
ATOM   7784 N N   . ILE B 1 441 ? 36.732  -29.789 85.745  1.00 11.87 ? 441 ILE B N   1 
ATOM   7785 C CA  . ILE B 1 441 ? 37.796  -28.877 85.336  1.00 5.05  ? 441 ILE B CA  1 
ATOM   7786 C C   . ILE B 1 441 ? 37.604  -28.475 83.872  1.00 7.48  ? 441 ILE B C   1 
ATOM   7787 O O   . ILE B 1 441 ? 37.910  -27.342 83.485  1.00 13.01 ? 441 ILE B O   1 
ATOM   7788 C CB  . ILE B 1 441 ? 39.191  -29.510 85.597  1.00 7.28  ? 441 ILE B CB  1 
ATOM   7789 C CG1 . ILE B 1 441 ? 40.280  -28.431 85.559  1.00 8.52  ? 441 ILE B CG1 1 
ATOM   7790 C CG2 . ILE B 1 441 ? 39.546  -30.586 84.573  1.00 14.86 ? 441 ILE B CG2 1 
ATOM   7791 C CD1 . ILE B 1 441 ? 40.217  -27.486 86.744  1.00 17.00 ? 441 ILE B CD1 1 
ATOM   7792 N N   . LEU B 1 442 ? 37.065  -29.377 83.047  1.00 6.90  ? 442 LEU B N   1 
ATOM   7793 C CA  . LEU B 1 442 ? 36.777  -29.030 81.654  1.00 9.54  ? 442 LEU B CA  1 
ATOM   7794 C C   . LEU B 1 442 ? 35.653  -28.001 81.557  1.00 11.79 ? 442 LEU B C   1 
ATOM   7795 O O   . LEU B 1 442 ? 35.686  -27.116 80.697  1.00 8.80  ? 442 LEU B O   1 
ATOM   7796 C CB  . LEU B 1 442 ? 36.395  -30.285 80.868  1.00 8.57  ? 442 LEU B CB  1 
ATOM   7797 C CG  . LEU B 1 442 ? 37.426  -31.427 80.908  1.00 10.68 ? 442 LEU B CG  1 
ATOM   7798 C CD1 . LEU B 1 442 ? 36.945  -32.572 80.038  1.00 16.27 ? 442 LEU B CD1 1 
ATOM   7799 C CD2 . LEU B 1 442 ? 38.784  -30.922 80.425  1.00 3.94  ? 442 LEU B CD2 1 
ATOM   7800 N N   . VAL B 1 443 ? 34.640  -28.115 82.418  1.00 9.29  ? 443 VAL B N   1 
ATOM   7801 C CA  . VAL B 1 443 ? 33.559  -27.127 82.421  1.00 7.29  ? 443 VAL B CA  1 
ATOM   7802 C C   . VAL B 1 443 ? 34.123  -25.740 82.702  1.00 9.07  ? 443 VAL B C   1 
ATOM   7803 O O   . VAL B 1 443 ? 33.738  -24.751 82.063  1.00 6.77  ? 443 VAL B O   1 
ATOM   7804 C CB  . VAL B 1 443 ? 32.496  -27.517 83.468  1.00 9.62  ? 443 VAL B CB  1 
ATOM   7805 C CG1 . VAL B 1 443 ? 31.351  -26.491 83.493  1.00 5.60  ? 443 VAL B CG1 1 
ATOM   7806 C CG2 . VAL B 1 443 ? 31.967  -28.938 83.203  1.00 8.08  ? 443 VAL B CG2 1 
ATOM   7807 N N   . ALA B 1 444 ? 35.051  -25.651 83.664  1.00 11.05 ? 444 ALA B N   1 
ATOM   7808 C CA  . ALA B 1 444 ? 35.616  -24.376 84.080  1.00 8.61  ? 444 ALA B CA  1 
ATOM   7809 C C   . ALA B 1 444 ? 36.570  -23.792 83.049  1.00 12.95 ? 444 ALA B C   1 
ATOM   7810 O O   . ALA B 1 444 ? 36.894  -22.605 83.134  1.00 10.74 ? 444 ALA B O   1 
ATOM   7811 C CB  . ALA B 1 444 ? 36.341  -24.527 85.428  1.00 6.53  ? 444 ALA B CB  1 
ATOM   7812 N N   . GLU B 1 445 ? 37.014  -24.587 82.070  1.00 9.81  ? 445 GLU B N   1 
ATOM   7813 C CA  . GLU B 1 445 ? 37.824  -24.064 80.974  1.00 8.60  ? 445 GLU B CA  1 
ATOM   7814 C C   . GLU B 1 445 ? 36.983  -23.402 79.886  1.00 5.96  ? 445 GLU B C   1 
ATOM   7815 O O   . GLU B 1 445 ? 37.543  -22.839 78.935  1.00 7.66  ? 445 GLU B O   1 
ATOM   7816 C CB  . GLU B 1 445 ? 38.694  -25.204 80.392  1.00 11.27 ? 445 GLU B CB  1 
ATOM   7817 C CG  . GLU B 1 445 ? 39.728  -25.723 81.387  1.00 11.34 ? 445 GLU B CG  1 
ATOM   7818 C CD  . GLU B 1 445 ? 40.271  -27.115 81.065  1.00 13.76 ? 445 GLU B CD  1 
ATOM   7819 O OE1 . GLU B 1 445 ? 39.934  -27.672 79.997  1.00 7.92  ? 445 GLU B OE1 1 
ATOM   7820 O OE2 . GLU B 1 445 ? 41.066  -27.640 81.887  1.00 14.06 ? 445 GLU B OE2 1 
ATOM   7821 N N   . GLY B 1 446 ? 35.659  -23.392 80.016  1.00 7.89  ? 446 GLY B N   1 
ATOM   7822 C CA  . GLY B 1 446 ? 34.847  -22.724 79.006  1.00 7.64  ? 446 GLY B CA  1 
ATOM   7823 C C   . GLY B 1 446 ? 35.188  -21.244 78.905  1.00 8.04  ? 446 GLY B C   1 
ATOM   7824 O O   . GLY B 1 446 ? 35.532  -20.599 79.900  1.00 8.95  ? 446 GLY B O   1 
ATOM   7825 N N   . SER B 1 447 ? 35.074  -20.701 77.684  1.00 5.22  ? 447 SER B N   1 
ATOM   7826 C CA  . SER B 1 447 ? 35.443  -19.301 77.461  1.00 6.21  ? 447 SER B CA  1 
ATOM   7827 C C   . SER B 1 447 ? 34.536  -18.333 78.212  1.00 10.54 ? 447 SER B C   1 
ATOM   7828 O O   . SER B 1 447 ? 34.965  -17.226 78.573  1.00 5.97  ? 447 SER B O   1 
ATOM   7829 C CB  . SER B 1 447 ? 35.434  -18.965 75.961  1.00 7.62  ? 447 SER B CB  1 
ATOM   7830 O OG  . SER B 1 447 ? 34.127  -18.907 75.430  1.00 12.83 ? 447 SER B OG  1 
ATOM   7831 N N   . ASP B 1 448 ? 33.283  -18.714 78.443  1.00 9.80  ? 448 ASP B N   1 
ATOM   7832 C CA  . ASP B 1 448 ? 32.317  -17.754 78.957  1.00 9.44  ? 448 ASP B CA  1 
ATOM   7833 C C   . ASP B 1 448 ? 32.739  -17.174 80.309  1.00 8.65  ? 448 ASP B C   1 
ATOM   7834 O O   . ASP B 1 448 ? 32.498  -15.992 80.582  1.00 6.93  ? 448 ASP B O   1 
ATOM   7835 C CB  . ASP B 1 448 ? 30.944  -18.419 79.042  1.00 12.02 ? 448 ASP B CB  1 
ATOM   7836 C CG  . ASP B 1 448 ? 30.538  -19.061 77.728  1.00 10.30 ? 448 ASP B CG  1 
ATOM   7837 O OD1 . ASP B 1 448 ? 31.017  -20.180 77.439  1.00 6.56  ? 448 ASP B OD1 1 
ATOM   7838 O OD2 . ASP B 1 448 ? 29.739  -18.438 76.988  1.00 11.48 ? 448 ASP B OD2 1 
ATOM   7839 N N   . TRP B 1 449 ? 33.357  -17.982 81.170  1.00 10.60 ? 449 TRP B N   1 
ATOM   7840 C CA  . TRP B 1 449 ? 33.697  -17.486 82.504  1.00 11.16 ? 449 TRP B CA  1 
ATOM   7841 C C   . TRP B 1 449 ? 34.668  -16.320 82.418  1.00 13.04 ? 449 TRP B C   1 
ATOM   7842 O O   . TRP B 1 449 ? 34.538  -15.329 83.152  1.00 10.28 ? 449 TRP B O   1 
ATOM   7843 C CB  . TRP B 1 449 ? 34.274  -18.622 83.359  1.00 7.68  ? 449 TRP B CB  1 
ATOM   7844 C CG  . TRP B 1 449 ? 33.494  -19.884 83.182  1.00 11.50 ? 449 TRP B CG  1 
ATOM   7845 C CD1 . TRP B 1 449 ? 33.969  -21.090 82.738  1.00 10.07 ? 449 TRP B CD1 1 
ATOM   7846 C CD2 . TRP B 1 449 ? 32.090  -20.066 83.417  1.00 9.32  ? 449 TRP B CD2 1 
ATOM   7847 N NE1 . TRP B 1 449 ? 32.946  -22.015 82.699  1.00 10.90 ? 449 TRP B NE1 1 
ATOM   7848 C CE2 . TRP B 1 449 ? 31.783  -21.405 83.096  1.00 5.91  ? 449 TRP B CE2 1 
ATOM   7849 C CE3 . TRP B 1 449 ? 31.059  -19.226 83.869  1.00 10.83 ? 449 TRP B CE3 1 
ATOM   7850 C CZ2 . TRP B 1 449 ? 30.490  -21.923 83.209  1.00 7.68  ? 449 TRP B CZ2 1 
ATOM   7851 C CZ3 . TRP B 1 449 ? 29.778  -19.740 83.980  1.00 8.60  ? 449 TRP B CZ3 1 
ATOM   7852 C CH2 . TRP B 1 449 ? 29.506  -21.084 83.655  1.00 10.51 ? 449 TRP B CH2 1 
ATOM   7853 N N   . PHE B 1 450 ? 35.609  -16.400 81.483  1.00 7.80  ? 450 PHE B N   1 
ATOM   7854 C CA  . PHE B 1 450 ? 36.654  -15.390 81.359  1.00 9.39  ? 450 PHE B CA  1 
ATOM   7855 C C   . PHE B 1 450 ? 36.160  -14.163 80.612  1.00 10.15 ? 450 PHE B C   1 
ATOM   7856 O O   . PHE B 1 450 ? 36.707  -13.072 80.800  1.00 12.13 ? 450 PHE B O   1 
ATOM   7857 C CB  . PHE B 1 450 ? 37.867  -15.998 80.666  1.00 9.00  ? 450 PHE B CB  1 
ATOM   7858 C CG  . PHE B 1 450 ? 38.347  -17.247 81.325  1.00 8.63  ? 450 PHE B CG  1 
ATOM   7859 C CD1 . PHE B 1 450 ? 39.296  -17.189 82.337  1.00 10.25 ? 450 PHE B CD1 1 
ATOM   7860 C CD2 . PHE B 1 450 ? 37.818  -18.482 80.974  1.00 12.50 ? 450 PHE B CD2 1 
ATOM   7861 C CE1 . PHE B 1 450 ? 39.722  -18.341 82.980  1.00 9.96  ? 450 PHE B CE1 1 
ATOM   7862 C CE2 . PHE B 1 450 ? 38.248  -19.638 81.607  1.00 8.84  ? 450 PHE B CE2 1 
ATOM   7863 C CZ  . PHE B 1 450 ? 39.205  -19.569 82.610  1.00 9.94  ? 450 PHE B CZ  1 
ATOM   7864 N N   . TRP B 1 451 ? 35.137  -14.336 79.770  1.00 10.70 ? 451 TRP B N   1 
ATOM   7865 C CA  . TRP B 1 451 ? 34.527  -13.207 79.073  1.00 13.09 ? 451 TRP B CA  1 
ATOM   7866 C C   . TRP B 1 451 ? 33.858  -12.252 80.059  1.00 13.17 ? 451 TRP B C   1 
ATOM   7867 O O   . TRP B 1 451 ? 34.042  -11.033 79.982  1.00 14.21 ? 451 TRP B O   1 
ATOM   7868 C CB  . TRP B 1 451 ? 33.514  -13.742 78.058  1.00 10.93 ? 451 TRP B CB  1 
ATOM   7869 C CG  . TRP B 1 451 ? 32.645  -12.699 77.413  1.00 19.61 ? 451 TRP B CG  1 
ATOM   7870 C CD1 . TRP B 1 451 ? 31.456  -12.204 77.887  1.00 17.35 ? 451 TRP B CD1 1 
ATOM   7871 C CD2 . TRP B 1 451 ? 32.884  -12.043 76.158  1.00 14.50 ? 451 TRP B CD2 1 
ATOM   7872 N NE1 . TRP B 1 451 ? 30.950  -11.267 77.008  1.00 24.02 ? 451 TRP B NE1 1 
ATOM   7873 C CE2 . TRP B 1 451 ? 31.805  -11.150 75.941  1.00 22.74 ? 451 TRP B CE2 1 
ATOM   7874 C CE3 . TRP B 1 451 ? 33.906  -12.113 75.204  1.00 8.09  ? 451 TRP B CE3 1 
ATOM   7875 C CZ2 . TRP B 1 451 ? 31.722  -10.339 74.807  1.00 24.33 ? 451 TRP B CZ2 1 
ATOM   7876 C CZ3 . TRP B 1 451 ? 33.825  -11.305 74.078  1.00 19.72 ? 451 TRP B CZ3 1 
ATOM   7877 C CH2 . TRP B 1 451 ? 32.737  -10.429 73.892  1.00 27.53 ? 451 TRP B CH2 1 
ATOM   7878 N N   . TRP B 1 452 ? 33.078  -12.797 80.996  1.00 10.62 ? 452 TRP B N   1 
ATOM   7879 C CA  . TRP B 1 452 ? 32.307  -11.970 81.923  1.00 18.47 ? 452 TRP B CA  1 
ATOM   7880 C C   . TRP B 1 452 ? 33.137  -11.480 83.100  1.00 24.09 ? 452 TRP B C   1 
ATOM   7881 O O   . TRP B 1 452 ? 32.761  -10.487 83.734  1.00 20.01 ? 452 TRP B O   1 
ATOM   7882 C CB  . TRP B 1 452 ? 31.085  -12.744 82.442  1.00 14.63 ? 452 TRP B CB  1 
ATOM   7883 C CG  . TRP B 1 452 ? 30.115  -13.136 81.358  1.00 18.90 ? 452 TRP B CG  1 
ATOM   7884 C CD1 . TRP B 1 452 ? 29.838  -14.397 80.923  1.00 24.07 ? 452 TRP B CD1 1 
ATOM   7885 C CD2 . TRP B 1 452 ? 29.296  -12.254 80.578  1.00 23.78 ? 452 TRP B CD2 1 
ATOM   7886 N NE1 . TRP B 1 452 ? 28.904  -14.357 79.915  1.00 21.40 ? 452 TRP B NE1 1 
ATOM   7887 C CE2 . TRP B 1 452 ? 28.557  -13.053 79.682  1.00 22.19 ? 452 TRP B CE2 1 
ATOM   7888 C CE3 . TRP B 1 452 ? 29.136  -10.865 80.532  1.00 23.67 ? 452 TRP B CE3 1 
ATOM   7889 C CZ2 . TRP B 1 452 ? 27.660  -12.512 78.764  1.00 30.91 ? 452 TRP B CZ2 1 
ATOM   7890 C CZ3 . TRP B 1 452 ? 28.245  -10.328 79.616  1.00 28.75 ? 452 TRP B CZ3 1 
ATOM   7891 C CH2 . TRP B 1 452 ? 27.521  -11.149 78.745  1.00 36.52 ? 452 TRP B CH2 1 
ATOM   7892 N N   . GLN B 1 453 ? 34.261  -12.131 83.395  1.00 21.67 ? 453 GLN B N   1 
ATOM   7893 C CA  . GLN B 1 453 ? 35.036  -11.760 84.571  1.00 21.44 ? 453 GLN B CA  1 
ATOM   7894 C C   . GLN B 1 453 ? 35.575  -10.345 84.435  1.00 23.89 ? 453 GLN B C   1 
ATOM   7895 O O   . GLN B 1 453 ? 36.058  -9.944  83.374  1.00 20.28 ? 453 GLN B O   1 
ATOM   7896 C CB  . GLN B 1 453 ? 36.191  -12.738 84.797  1.00 10.40 ? 453 GLN B CB  1 
ATOM   7897 C CG  . GLN B 1 453 ? 37.247  -12.276 85.811  1.00 19.66 ? 453 GLN B CG  1 
ATOM   7898 C CD  . GLN B 1 453 ? 36.734  -12.159 87.253  1.00 23.51 ? 453 GLN B CD  1 
ATOM   7899 O OE1 . GLN B 1 453 ? 35.527  -12.087 87.502  1.00 25.01 ? 453 GLN B OE1 1 
ATOM   7900 N NE2 . GLN B 1 453 ? 37.666  -12.148 88.210  1.00 18.76 ? 453 GLN B NE2 1 
ATOM   7901 N N   . GLY B 1 454 ? 35.484  -9.592  85.526  1.00 39.16 ? 454 GLY B N   1 
ATOM   7902 C CA  . GLY B 1 454 ? 35.947  -8.226  85.560  1.00 50.47 ? 454 GLY B CA  1 
ATOM   7903 C C   . GLY B 1 454 ? 35.002  -7.212  84.965  1.00 61.49 ? 454 GLY B C   1 
ATOM   7904 O O   . GLY B 1 454 ? 35.318  -6.016  84.976  1.00 69.37 ? 454 GLY B O   1 
ATOM   7905 N N   . GLU B 1 455 ? 33.852  -7.635  84.456  1.00 59.26 ? 455 GLU B N   1 
ATOM   7906 C CA  . GLU B 1 455 ? 33.004  -6.715  83.718  1.00 61.07 ? 455 GLU B CA  1 
ATOM   7907 C C   . GLU B 1 455 ? 32.188  -5.862  84.673  1.00 59.46 ? 455 GLU B C   1 
ATOM   7908 O O   . GLU B 1 455 ? 31.605  -6.369  85.635  1.00 55.52 ? 455 GLU B O   1 
ATOM   7909 C CB  . GLU B 1 455 ? 32.108  -7.471  82.739  1.00 64.25 ? 455 GLU B CB  1 
ATOM   7910 C CG  . GLU B 1 455 ? 32.889  -8.285  81.704  1.00 65.52 ? 455 GLU B CG  1 
ATOM   7911 C CD  . GLU B 1 455 ? 33.965  -7.493  80.958  1.00 64.69 ? 455 GLU B CD  1 
ATOM   7912 O OE1 . GLU B 1 455 ? 33.978  -6.243  81.012  1.00 64.84 ? 455 GLU B OE1 1 
ATOM   7913 O OE2 . GLU B 1 455 ? 34.822  -8.135  80.312  1.00 64.44 ? 455 GLU B OE2 1 
ATOM   7914 N N   . GLU B 1 456 ? 32.169  -4.558  84.402  1.00 69.09 ? 456 GLU B N   1 
ATOM   7915 C CA  . GLU B 1 456 ? 31.560  -3.569  85.278  1.00 72.86 ? 456 GLU B CA  1 
ATOM   7916 C C   . GLU B 1 456 ? 30.104  -3.933  85.545  1.00 66.97 ? 456 GLU B C   1 
ATOM   7917 O O   . GLU B 1 456 ? 29.198  -3.558  84.791  1.00 64.17 ? 456 GLU B O   1 
ATOM   7918 C CB  . GLU B 1 456 ? 31.739  -2.178  84.665  1.00 76.31 ? 456 GLU B CB  1 
ATOM   7919 C CG  . GLU B 1 456 ? 33.225  -1.875  84.430  1.00 77.75 ? 456 GLU B CG  1 
ATOM   7920 C CD  . GLU B 1 456 ? 33.570  -0.400  84.492  1.00 78.69 ? 456 GLU B CD  1 
ATOM   7921 O OE1 . GLU B 1 456 ? 34.182  0.028   85.495  1.00 77.93 ? 456 GLU B OE1 1 
ATOM   7922 O OE2 . GLU B 1 456 ? 33.255  0.324   83.524  1.00 79.04 ? 456 GLU B OE2 1 
ATOM   7923 N N   . LYS B 1 457 ? 29.914  -4.664  86.651  1.00 64.80 ? 457 LYS B N   1 
ATOM   7924 C CA  . LYS B 1 457 ? 28.771  -5.502  87.014  1.00 63.67 ? 457 LYS B CA  1 
ATOM   7925 C C   . LYS B 1 457 ? 27.752  -5.727  85.895  1.00 62.85 ? 457 LYS B C   1 
ATOM   7926 O O   . LYS B 1 457 ? 26.554  -5.491  86.076  1.00 61.16 ? 457 LYS B O   1 
ATOM   7927 C CB  . LYS B 1 457 ? 28.118  -4.932  88.273  1.00 60.95 ? 457 LYS B CB  1 
ATOM   7928 C CG  . LYS B 1 457 ? 29.049  -5.063  89.483  1.00 62.73 ? 457 LYS B CG  1 
ATOM   7929 C CD  . LYS B 1 457 ? 28.359  -4.773  90.797  1.00 63.73 ? 457 LYS B CD  1 
ATOM   7930 C CE  . LYS B 1 457 ? 27.212  -5.734  91.020  1.00 64.18 ? 457 LYS B CE  1 
ATOM   7931 N NZ  . LYS B 1 457 ? 25.956  -4.994  91.286  1.00 65.52 ? 457 LYS B NZ  1 
ATOM   7932 N N   . ALA B 1 458 ? 28.239  -6.205  84.737  1.00 60.41 ? 458 ALA B N   1 
ATOM   7933 C CA  . ALA B 1 458 ? 27.483  -6.689  83.586  1.00 54.38 ? 458 ALA B CA  1 
ATOM   7934 C C   . ALA B 1 458 ? 26.416  -7.683  84.030  1.00 51.81 ? 458 ALA B C   1 
ATOM   7935 O O   . ALA B 1 458 ? 26.561  -8.284  85.099  1.00 52.42 ? 458 ALA B O   1 
ATOM   7936 C CB  . ALA B 1 458 ? 28.441  -7.330  82.568  1.00 47.87 ? 458 ALA B CB  1 
ATOM   7937 N N   . PRO B 1 459 ? 25.358  -7.907  83.239  1.00 49.04 ? 459 PRO B N   1 
ATOM   7938 C CA  . PRO B 1 459 ? 24.151  -8.561  83.782  1.00 42.35 ? 459 PRO B CA  1 
ATOM   7939 C C   . PRO B 1 459 ? 24.436  -9.896  84.452  1.00 28.68 ? 459 PRO B C   1 
ATOM   7940 O O   . PRO B 1 459 ? 24.926  -10.845 83.825  1.00 27.19 ? 459 PRO B O   1 
ATOM   7941 C CB  . PRO B 1 459 ? 23.250  -8.734  82.551  1.00 44.63 ? 459 PRO B CB  1 
ATOM   7942 C CG  . PRO B 1 459 ? 24.153  -8.612  81.370  1.00 49.68 ? 459 PRO B CG  1 
ATOM   7943 C CD  . PRO B 1 459 ? 25.221  -7.649  81.793  1.00 48.31 ? 459 PRO B CD  1 
ATOM   7944 N N   . PHE B 1 460 ? 24.131  -9.953  85.750  1.00 24.94 ? 460 PHE B N   1 
ATOM   7945 C CA  . PHE B 1 460 ? 24.224  -11.180 86.545  1.00 24.23 ? 460 PHE B CA  1 
ATOM   7946 C C   . PHE B 1 460 ? 25.653  -11.714 86.619  1.00 25.57 ? 460 PHE B C   1 
ATOM   7947 O O   . PHE B 1 460 ? 25.871  -12.919 86.773  1.00 17.37 ? 460 PHE B O   1 
ATOM   7948 C CB  . PHE B 1 460 ? 23.269  -12.252 86.010  1.00 24.15 ? 460 PHE B CB  1 
ATOM   7949 C CG  . PHE B 1 460 ? 21.827  -11.837 86.039  1.00 22.33 ? 460 PHE B CG  1 
ATOM   7950 C CD1 . PHE B 1 460 ? 21.165  -11.672 87.246  1.00 26.27 ? 460 PHE B CD1 1 
ATOM   7951 C CD2 . PHE B 1 460 ? 21.138  -11.594 84.863  1.00 26.75 ? 460 PHE B CD2 1 
ATOM   7952 C CE1 . PHE B 1 460 ? 19.828  -11.286 87.283  1.00 30.63 ? 460 PHE B CE1 1 
ATOM   7953 C CE2 . PHE B 1 460 ? 19.804  -11.206 84.891  1.00 27.96 ? 460 PHE B CE2 1 
ATOM   7954 C CZ  . PHE B 1 460 ? 19.151  -11.052 86.105  1.00 30.08 ? 460 PHE B CZ  1 
ATOM   7955 N N   . VAL B 1 461 ? 26.642  -10.821 86.537  1.00 18.73 ? 461 VAL B N   1 
ATOM   7956 C CA  . VAL B 1 461 ? 28.032  -11.260 86.556  1.00 22.64 ? 461 VAL B CA  1 
ATOM   7957 C C   . VAL B 1 461 ? 28.353  -12.016 87.842  1.00 22.06 ? 461 VAL B C   1 
ATOM   7958 O O   . VAL B 1 461 ? 29.229  -12.891 87.860  1.00 14.93 ? 461 VAL B O   1 
ATOM   7959 C CB  . VAL B 1 461 ? 28.965  -10.049 86.334  1.00 30.53 ? 461 VAL B CB  1 
ATOM   7960 C CG1 . VAL B 1 461 ? 28.745  -8.993  87.402  1.00 29.86 ? 461 VAL B CG1 1 
ATOM   7961 C CG2 . VAL B 1 461 ? 30.418  -10.481 86.293  1.00 24.76 ? 461 VAL B CG2 1 
ATOM   7962 N N   . GLU B 1 462 ? 27.640  -11.737 88.930  1.00 11.77 ? 462 GLU B N   1 
ATOM   7963 C CA  . GLU B 1 462 ? 27.932  -12.498 90.137  1.00 16.51 ? 462 GLU B CA  1 
ATOM   7964 C C   . GLU B 1 462 ? 27.453  -13.942 90.025  1.00 16.83 ? 462 GLU B C   1 
ATOM   7965 O O   . GLU B 1 462 ? 27.983  -14.814 90.723  1.00 14.56 ? 462 GLU B O   1 
ATOM   7966 C CB  . GLU B 1 462 ? 27.315  -11.807 91.345  1.00 26.13 ? 462 GLU B CB  1 
ATOM   7967 C CG  . GLU B 1 462 ? 27.525  -10.317 91.281  1.00 40.15 ? 462 GLU B CG  1 
ATOM   7968 C CD  . GLU B 1 462 ? 27.331  -9.636  92.600  1.00 49.83 ? 462 GLU B CD  1 
ATOM   7969 O OE1 . GLU B 1 462 ? 27.104  -10.337 93.606  1.00 52.20 ? 462 GLU B OE1 1 
ATOM   7970 O OE2 . GLU B 1 462 ? 27.387  -8.390  92.614  1.00 56.39 ? 462 GLU B OE2 1 
ATOM   7971 N N   . VAL B 1 463 ? 26.473  -14.215 89.160  1.00 13.48 ? 463 VAL B N   1 
ATOM   7972 C CA  . VAL B 1 463 ? 26.015  -15.590 88.983  1.00 7.39  ? 463 VAL B CA  1 
ATOM   7973 C C   . VAL B 1 463 ? 27.043  -16.387 88.187  1.00 10.02 ? 463 VAL B C   1 
ATOM   7974 O O   . VAL B 1 463 ? 27.367  -17.525 88.537  1.00 13.64 ? 463 VAL B O   1 
ATOM   7975 C CB  . VAL B 1 463 ? 24.629  -15.619 88.319  1.00 16.00 ? 463 VAL B CB  1 
ATOM   7976 C CG1 . VAL B 1 463 ? 24.208  -17.066 88.055  1.00 12.17 ? 463 VAL B CG1 1 
ATOM   7977 C CG2 . VAL B 1 463 ? 23.603  -14.912 89.216  1.00 11.68 ? 463 VAL B CG2 1 
ATOM   7978 N N   . PHE B 1 464 ? 27.560  -15.804 87.094  1.00 8.94  ? 464 PHE B N   1 
ATOM   7979 C CA  . PHE B 1 464 ? 28.657  -16.432 86.363  1.00 9.52  ? 464 PHE B CA  1 
ATOM   7980 C C   . PHE B 1 464 ? 29.843  -16.690 87.280  1.00 10.29 ? 464 PHE B C   1 
ATOM   7981 O O   . PHE B 1 464 ? 30.500  -17.730 87.183  1.00 11.65 ? 464 PHE B O   1 
ATOM   7982 C CB  . PHE B 1 464 ? 29.082  -15.553 85.178  1.00 10.95 ? 464 PHE B CB  1 
ATOM   7983 C CG  . PHE B 1 464 ? 28.090  -15.560 84.039  1.00 10.94 ? 464 PHE B CG  1 
ATOM   7984 C CD1 . PHE B 1 464 ? 27.039  -14.659 84.009  1.00 12.94 ? 464 PHE B CD1 1 
ATOM   7985 C CD2 . PHE B 1 464 ? 28.188  -16.502 83.019  1.00 17.06 ? 464 PHE B CD2 1 
ATOM   7986 C CE1 . PHE B 1 464 ? 26.109  -14.675 82.963  1.00 14.53 ? 464 PHE B CE1 1 
ATOM   7987 C CE2 . PHE B 1 464 ? 27.262  -16.532 81.985  1.00 20.27 ? 464 PHE B CE2 1 
ATOM   7988 C CZ  . PHE B 1 464 ? 26.224  -15.614 81.956  1.00 14.28 ? 464 PHE B CZ  1 
ATOM   7989 N N   . ASP B 1 465 ? 30.126  -15.748 88.180  1.00 12.71 ? 465 ASP B N   1 
ATOM   7990 C CA  . ASP B 1 465 ? 31.253  -15.906 89.093  1.00 12.97 ? 465 ASP B CA  1 
ATOM   7991 C C   . ASP B 1 465 ? 30.997  -17.040 90.075  1.00 9.26  ? 465 ASP B C   1 
ATOM   7992 O O   . ASP B 1 465 ? 31.882  -17.867 90.326  1.00 11.88 ? 465 ASP B O   1 
ATOM   7993 C CB  . ASP B 1 465 ? 31.518  -14.591 89.836  1.00 9.74  ? 465 ASP B CB  1 
ATOM   7994 C CG  . ASP B 1 465 ? 32.574  -14.741 90.918  1.00 17.31 ? 465 ASP B CG  1 
ATOM   7995 O OD1 . ASP B 1 465 ? 33.762  -14.833 90.563  1.00 14.33 ? 465 ASP B OD1 1 
ATOM   7996 O OD2 . ASP B 1 465 ? 32.222  -14.784 92.115  1.00 18.15 ? 465 ASP B OD2 1 
ATOM   7997 N N   . LYS B 1 466 ? 29.773  -17.126 90.602  1.00 7.33  ? 466 LYS B N   1 
ATOM   7998 C CA  . LYS B 1 466 ? 29.422  -18.253 91.465  1.00 8.25  ? 466 LYS B CA  1 
ATOM   7999 C C   . LYS B 1 466 ? 29.520  -19.586 90.723  1.00 8.33  ? 466 LYS B C   1 
ATOM   8000 O O   . LYS B 1 466 ? 30.025  -20.574 91.272  1.00 13.78 ? 466 LYS B O   1 
ATOM   8001 C CB  . LYS B 1 466 ? 28.008  -18.065 92.023  1.00 12.99 ? 466 LYS B CB  1 
ATOM   8002 C CG  . LYS B 1 466 ? 27.440  -19.328 92.689  1.00 12.19 ? 466 LYS B CG  1 
ATOM   8003 C CD  . LYS B 1 466 ? 26.050  -19.057 93.270  1.00 22.31 ? 466 LYS B CD  1 
ATOM   8004 C CE  . LYS B 1 466 ? 25.798  -19.846 94.555  1.00 28.38 ? 466 LYS B CE  1 
ATOM   8005 N NZ  . LYS B 1 466 ? 25.245  -21.201 94.302  1.00 41.95 ? 466 LYS B NZ  1 
ATOM   8006 N N   . LEU B 1 467 ? 29.036  -19.634 89.471  1.00 10.91 ? 467 LEU B N   1 
ATOM   8007 C CA  . LEU B 1 467 ? 29.118  -20.856 88.672  1.00 5.32  ? 467 LEU B CA  1 
ATOM   8008 C C   . LEU B 1 467 ? 30.566  -21.289 88.459  1.00 8.10  ? 467 LEU B C   1 
ATOM   8009 O O   . LEU B 1 467 ? 30.931  -22.438 88.727  1.00 6.23  ? 467 LEU B O   1 
ATOM   8010 C CB  . LEU B 1 467 ? 28.413  -20.651 87.315  1.00 3.64  ? 467 LEU B CB  1 
ATOM   8011 C CG  . LEU B 1 467 ? 26.872  -20.684 87.376  1.00 8.60  ? 467 LEU B CG  1 
ATOM   8012 C CD1 . LEU B 1 467 ? 26.254  -20.189 86.071  1.00 5.64  ? 467 LEU B CD1 1 
ATOM   8013 C CD2 . LEU B 1 467 ? 26.423  -22.106 87.676  1.00 4.54  ? 467 LEU B CD2 1 
ATOM   8014 N N   . PHE B 1 468 ? 31.394  -20.391 87.925  1.00 10.65 ? 468 PHE B N   1 
ATOM   8015 C CA  . PHE B 1 468 ? 32.789  -20.741 87.663  1.00 7.93  ? 468 PHE B CA  1 
ATOM   8016 C C   . PHE B 1 468 ? 33.465  -21.256 88.923  1.00 8.56  ? 468 PHE B C   1 
ATOM   8017 O O   . PHE B 1 468 ? 34.135  -22.290 88.898  1.00 10.52 ? 468 PHE B O   1 
ATOM   8018 C CB  . PHE B 1 468 ? 33.534  -19.530 87.130  1.00 3.49  ? 468 PHE B CB  1 
ATOM   8019 C CG  . PHE B 1 468 ? 35.030  -19.719 87.052  1.00 8.84  ? 468 PHE B CG  1 
ATOM   8020 C CD1 . PHE B 1 468 ? 35.588  -20.446 86.016  1.00 7.14  ? 468 PHE B CD1 1 
ATOM   8021 C CD2 . PHE B 1 468 ? 35.868  -19.186 88.031  1.00 9.32  ? 468 PHE B CD2 1 
ATOM   8022 C CE1 . PHE B 1 468 ? 36.977  -20.644 85.945  1.00 7.34  ? 468 PHE B CE1 1 
ATOM   8023 C CE2 . PHE B 1 468 ? 37.264  -19.366 87.962  1.00 8.71  ? 468 PHE B CE2 1 
ATOM   8024 C CZ  . PHE B 1 468 ? 37.806  -20.087 86.908  1.00 12.30 ? 468 PHE B CZ  1 
ATOM   8025 N N   . ARG B 1 469 ? 33.266  -20.564 90.050  1.00 6.38  ? 469 ARG B N   1 
ATOM   8026 C CA  . ARG B 1 469 ? 33.982  -20.960 91.258  1.00 13.31 ? 469 ARG B CA  1 
ATOM   8027 C C   . ARG B 1 469 ? 33.431  -22.263 91.819  1.00 11.08 ? 469 ARG B C   1 
ATOM   8028 O O   . ARG B 1 469 ? 34.182  -23.049 92.416  1.00 12.87 ? 469 ARG B O   1 
ATOM   8029 C CB  . ARG B 1 469 ? 33.936  -19.831 92.291  1.00 11.25 ? 469 ARG B CB  1 
ATOM   8030 C CG  . ARG B 1 469 ? 34.887  -18.664 91.949  1.00 6.44  ? 469 ARG B CG  1 
ATOM   8031 C CD  . ARG B 1 469 ? 34.766  -17.504 92.927  1.00 11.39 ? 469 ARG B CD  1 
ATOM   8032 N NE  . ARG B 1 469 ? 35.499  -16.309 92.503  1.00 13.90 ? 469 ARG B NE  1 
ATOM   8033 C CZ  . ARG B 1 469 ? 36.748  -16.011 92.865  1.00 13.02 ? 469 ARG B CZ  1 
ATOM   8034 N NH1 . ARG B 1 469 ? 37.445  -16.825 93.659  1.00 11.11 ? 469 ARG B NH1 1 
ATOM   8035 N NH2 . ARG B 1 469 ? 37.297  -14.873 92.456  1.00 17.38 ? 469 ARG B NH2 1 
ATOM   8036 N N   . SER B 1 470 ? 32.135  -22.519 91.621  1.00 7.88  ? 470 SER B N   1 
ATOM   8037 C CA  . SER B 1 470 ? 31.555  -23.798 92.030  1.00 10.04 ? 470 SER B CA  1 
ATOM   8038 C C   . SER B 1 470 ? 32.104  -24.952 91.205  1.00 9.80  ? 470 SER B C   1 
ATOM   8039 O O   . SER B 1 470 ? 32.343  -26.045 91.734  1.00 9.12  ? 470 SER B O   1 
ATOM   8040 C CB  . SER B 1 470 ? 30.030  -23.753 91.892  1.00 16.41 ? 470 SER B CB  1 
ATOM   8041 O OG  . SER B 1 470 ? 29.471  -22.777 92.741  1.00 24.12 ? 470 SER B OG  1 
ATOM   8042 N N   . PHE B 1 471 ? 32.243  -24.760 89.891  1.00 10.04 ? 471 PHE B N   1 
ATOM   8043 C CA  . PHE B 1 471 ? 32.827  -25.819 89.070  1.00 10.01 ? 471 PHE B CA  1 
ATOM   8044 C C   . PHE B 1 471 ? 34.278  -26.068 89.465  1.00 10.13 ? 471 PHE B C   1 
ATOM   8045 O O   . PHE B 1 471 ? 34.738  -27.214 89.479  1.00 12.91 ? 471 PHE B O   1 
ATOM   8046 C CB  . PHE B 1 471 ? 32.736  -25.463 87.580  1.00 4.64  ? 471 PHE B CB  1 
ATOM   8047 C CG  . PHE B 1 471 ? 31.314  -25.314 87.063  1.00 14.65 ? 471 PHE B CG  1 
ATOM   8048 C CD1 . PHE B 1 471 ? 30.349  -26.270 87.342  1.00 11.86 ? 471 PHE B CD1 1 
ATOM   8049 C CD2 . PHE B 1 471 ? 30.955  -24.222 86.294  1.00 10.51 ? 471 PHE B CD2 1 
ATOM   8050 C CE1 . PHE B 1 471 ? 29.041  -26.137 86.866  1.00 12.00 ? 471 PHE B CE1 1 
ATOM   8051 C CE2 . PHE B 1 471 ? 29.656  -24.086 85.804  1.00 10.33 ? 471 PHE B CE2 1 
ATOM   8052 C CZ  . PHE B 1 471 ? 28.701  -25.035 86.101  1.00 14.97 ? 471 PHE B CZ  1 
ATOM   8053 N N   . VAL B 1 472 ? 35.014  -24.999 89.786  1.00 8.89  ? 472 VAL B N   1 
ATOM   8054 C CA  . VAL B 1 472 ? 36.411  -25.141 90.185  1.00 11.65 ? 472 VAL B CA  1 
ATOM   8055 C C   . VAL B 1 472 ? 36.513  -25.921 91.493  1.00 10.16 ? 472 VAL B C   1 
ATOM   8056 O O   . VAL B 1 472 ? 37.383  -26.790 91.657  1.00 13.26 ? 472 VAL B O   1 
ATOM   8057 C CB  . VAL B 1 472 ? 37.064  -23.750 90.291  1.00 11.21 ? 472 VAL B CB  1 
ATOM   8058 C CG1 . VAL B 1 472 ? 38.339  -23.800 91.128  1.00 17.76 ? 472 VAL B CG1 1 
ATOM   8059 C CG2 . VAL B 1 472 ? 37.356  -23.186 88.880  1.00 14.87 ? 472 VAL B CG2 1 
ATOM   8060 N N   . ARG B 1 473 ? 35.608  -25.643 92.433  1.00 11.01 ? 473 ARG B N   1 
ATOM   8061 C CA  . ARG B 1 473 ? 35.601  -26.377 93.701  1.00 14.57 ? 473 ARG B CA  1 
ATOM   8062 C C   . ARG B 1 473 ? 35.224  -27.835 93.480  1.00 17.06 ? 473 ARG B C   1 
ATOM   8063 O O   . ARG B 1 473 ? 35.888  -28.752 93.983  1.00 14.65 ? 473 ARG B O   1 
ATOM   8064 C CB  . ARG B 1 473 ? 34.635  -25.694 94.672  1.00 17.12 ? 473 ARG B CB  1 
ATOM   8065 C CG  . ARG B 1 473 ? 34.486  -26.333 96.054  1.00 21.36 ? 473 ARG B CG  1 
ATOM   8066 C CD  . ARG B 1 473 ? 33.098  -26.043 96.668  1.00 35.89 ? 473 ARG B CD  1 
ATOM   8067 N NE  . ARG B 1 473 ? 32.635  -24.672 96.428  1.00 49.84 ? 473 ARG B NE  1 
ATOM   8068 C CZ  . ARG B 1 473 ? 31.355  -24.315 96.289  1.00 57.43 ? 473 ARG B CZ  1 
ATOM   8069 N NH1 . ARG B 1 473 ? 30.391  -25.221 96.369  1.00 64.52 ? 473 ARG B NH1 1 
ATOM   8070 N NH2 . ARG B 1 473 ? 31.032  -23.046 96.072  1.00 56.85 ? 473 ARG B NH2 1 
ATOM   8071 N N   . ARG B 1 474 ? 34.192  -28.066 92.676  1.00 14.06 ? 474 ARG B N   1 
ATOM   8072 C CA  . ARG B 1 474 ? 33.705  -29.415 92.443  1.00 17.53 ? 474 ARG B CA  1 
ATOM   8073 C C   . ARG B 1 474 ? 34.734  -30.268 91.708  1.00 16.45 ? 474 ARG B C   1 
ATOM   8074 O O   . ARG B 1 474 ? 34.822  -31.479 91.947  1.00 13.18 ? 474 ARG B O   1 
ATOM   8075 C CB  . ARG B 1 474 ? 32.388  -29.326 91.667  1.00 17.07 ? 474 ARG B CB  1 
ATOM   8076 C CG  . ARG B 1 474 ? 31.722  -30.640 91.354  1.00 19.76 ? 474 ARG B CG  1 
ATOM   8077 C CD  . ARG B 1 474 ? 31.254  -31.369 92.610  1.00 27.09 ? 474 ARG B CD  1 
ATOM   8078 N NE  . ARG B 1 474 ? 30.658  -32.648 92.243  1.00 36.10 ? 474 ARG B NE  1 
ATOM   8079 C CZ  . ARG B 1 474 ? 31.313  -33.805 92.239  1.00 45.50 ? 474 ARG B CZ  1 
ATOM   8080 N NH1 . ARG B 1 474 ? 32.589  -33.855 92.606  1.00 44.85 ? 474 ARG B NH1 1 
ATOM   8081 N NH2 . ARG B 1 474 ? 30.691  -34.917 91.870  1.00 48.31 ? 474 ARG B NH2 1 
ATOM   8082 N N   . ALA B 1 475 ? 35.526  -29.653 90.822  1.00 13.31 ? 475 ALA B N   1 
ATOM   8083 C CA  . ALA B 1 475 ? 36.527  -30.396 90.057  1.00 13.74 ? 475 ALA B CA  1 
ATOM   8084 C C   . ALA B 1 475 ? 37.623  -30.979 90.939  1.00 16.73 ? 475 ALA B C   1 
ATOM   8085 O O   . ALA B 1 475 ? 38.363  -31.859 90.488  1.00 16.72 ? 475 ALA B O   1 
ATOM   8086 C CB  . ALA B 1 475 ? 37.166  -29.496 89.001  1.00 14.26 ? 475 ALA B CB  1 
ATOM   8087 N N   . GLN B 1 476 ? 37.766  -30.488 92.162  1.00 12.98 ? 476 GLN B N   1 
ATOM   8088 C CA  . GLN B 1 476 ? 38.813  -30.954 93.054  1.00 13.36 ? 476 GLN B CA  1 
ATOM   8089 C C   . GLN B 1 476 ? 38.298  -31.965 94.059  1.00 27.06 ? 476 GLN B C   1 
ATOM   8090 O O   . GLN B 1 476 ? 39.000  -32.267 95.024  1.00 28.42 ? 476 GLN B O   1 
ATOM   8091 C CB  . GLN B 1 476 ? 39.464  -29.764 93.760  1.00 15.49 ? 476 GLN B CB  1 
ATOM   8092 C CG  . GLN B 1 476 ? 40.104  -28.802 92.755  1.00 14.91 ? 476 GLN B CG  1 
ATOM   8093 C CD  . GLN B 1 476 ? 40.565  -27.503 93.381  1.00 24.82 ? 476 GLN B CD  1 
ATOM   8094 O OE1 . GLN B 1 476 ? 41.670  -27.423 93.915  1.00 27.99 ? 476 GLN B OE1 1 
ATOM   8095 N NE2 . GLN B 1 476 ? 39.726  -26.476 93.313  1.00 16.21 ? 476 GLN B NE2 1 
ATOM   8096 N N   . GLU B 1 477 ? 37.092  -32.488 93.847  1.00 24.62 ? 477 GLU B N   1 
ATOM   8097 C CA  . GLU B 1 477 ? 36.512  -33.532 94.686  1.00 22.47 ? 477 GLU B CA  1 
ATOM   8098 C C   . GLU B 1 477 ? 36.222  -34.789 93.859  1.00 36.18 ? 477 GLU B C   1 
ATOM   8099 O O   . GLU B 1 477 ? 36.212  -35.912 94.388  1.00 39.79 ? 477 GLU B O   1 
ATOM   8100 C CB  . GLU B 1 477 ? 35.229  -33.027 95.352  1.00 31.60 ? 477 GLU B CB  1 
ATOM   8101 C CG  . GLU B 1 477 ? 35.437  -31.791 96.209  1.00 39.57 ? 477 GLU B CG  1 
ATOM   8102 C CD  . GLU B 1 477 ? 34.134  -31.095 96.574  1.00 47.98 ? 477 GLU B CD  1 
ATOM   8103 O OE1 . GLU B 1 477 ? 33.065  -31.565 96.132  1.00 47.69 ? 477 GLU B OE1 1 
ATOM   8104 O OE2 . GLU B 1 477 ? 34.185  -30.075 97.300  1.00 45.25 ? 477 GLU B OE2 1 
HETATM 8105 O O   . HOH C 2 .   ? -1.135  -6.495  56.700  1.00 45.84 ? 501 HOH A O   1 
HETATM 8106 O O   . HOH C 2 .   ? 3.468   -12.166 11.523  1.00 43.10 ? 502 HOH A O   1 
HETATM 8107 O O   . HOH C 2 .   ? -10.841 15.221  30.369  1.00 48.84 ? 503 HOH A O   1 
HETATM 8108 O O   . HOH C 2 .   ? -13.466 -13.496 42.464  1.00 34.39 ? 504 HOH A O   1 
HETATM 8109 O O   . HOH C 2 .   ? -8.563  -16.545 36.946  1.00 46.60 ? 505 HOH A O   1 
HETATM 8110 O O   . HOH C 2 .   ? 23.842  21.536  4.558   1.00 46.03 ? 506 HOH A O   1 
HETATM 8111 O O   . HOH C 2 .   ? -21.642 -11.760 20.369  1.00 29.55 ? 507 HOH A O   1 
HETATM 8112 O O   . HOH C 2 .   ? -3.211  8.986   33.441  1.00 37.24 ? 508 HOH A O   1 
HETATM 8113 O O   . HOH C 2 .   ? 13.519  -6.597  9.558   1.00 40.31 ? 509 HOH A O   1 
HETATM 8114 O O   . HOH C 2 .   ? -23.543 -6.515  48.830  1.00 41.88 ? 510 HOH A O   1 
HETATM 8115 O O   . HOH C 2 .   ? -6.403  11.925  42.403  1.00 29.51 ? 511 HOH A O   1 
HETATM 8116 O O   . HOH C 2 .   ? 1.167   -19.171 23.051  1.00 35.96 ? 512 HOH A O   1 
HETATM 8117 O O   . HOH C 2 .   ? 24.250  13.373  15.416  1.00 30.16 ? 513 HOH A O   1 
HETATM 8118 O O   . HOH C 2 .   ? -18.621 5.616   51.079  1.00 38.16 ? 514 HOH A O   1 
HETATM 8119 O O   . HOH C 2 .   ? 12.175  18.364  27.939  1.00 38.35 ? 515 HOH A O   1 
HETATM 8120 O O   . HOH C 2 .   ? -3.926  -18.881 23.031  1.00 42.12 ? 516 HOH A O   1 
HETATM 8121 O O   . HOH C 2 .   ? 15.389  6.437   23.427  1.00 21.28 ? 517 HOH A O   1 
HETATM 8122 O O   . HOH C 2 .   ? 13.744  23.592  41.094  1.00 33.69 ? 518 HOH A O   1 
HETATM 8123 O O   . HOH C 2 .   ? -14.930 5.797   50.770  1.00 17.85 ? 519 HOH A O   1 
HETATM 8124 O O   . HOH C 2 .   ? 18.720  0.362   44.047  1.00 42.79 ? 520 HOH A O   1 
HETATM 8125 O O   . HOH C 2 .   ? -0.947  9.577   58.805  1.00 47.06 ? 521 HOH A O   1 
HETATM 8126 O O   . HOH C 2 .   ? -14.704 -1.688  21.693  1.00 25.95 ? 522 HOH A O   1 
HETATM 8127 O O   . HOH C 2 .   ? -25.419 -0.408  34.426  1.00 43.42 ? 523 HOH A O   1 
HETATM 8128 O O   . HOH C 2 .   ? 12.980  -6.556  7.194   1.00 39.17 ? 524 HOH A O   1 
HETATM 8129 O O   . HOH C 2 .   ? -14.330 -17.635 18.725  1.00 41.94 ? 525 HOH A O   1 
HETATM 8130 O O   . HOH C 2 .   ? -20.314 -13.683 5.628   1.00 41.40 ? 526 HOH A O   1 
HETATM 8131 O O   . HOH C 2 .   ? 26.009  -5.238  5.416   1.00 36.54 ? 527 HOH A O   1 
HETATM 8132 O O   . HOH C 2 .   ? 7.509   6.435   24.932  1.00 17.15 ? 528 HOH A O   1 
HETATM 8133 O O   . HOH C 2 .   ? -24.086 12.600  20.524  1.00 33.87 ? 529 HOH A O   1 
HETATM 8134 O O   . HOH C 2 .   ? -22.252 5.882   30.955  1.00 18.61 ? 530 HOH A O   1 
HETATM 8135 O O   . HOH C 2 .   ? 10.329  1.806   49.941  1.00 28.28 ? 531 HOH A O   1 
HETATM 8136 O O   . HOH C 2 .   ? -19.934 -16.295 29.606  1.00 44.64 ? 532 HOH A O   1 
HETATM 8137 O O   . HOH C 2 .   ? 10.458  -3.269  0.545   1.00 46.38 ? 533 HOH A O   1 
HETATM 8138 O O   . HOH C 2 .   ? 18.890  -4.245  31.761  1.00 27.27 ? 534 HOH A O   1 
HETATM 8139 O O   . HOH C 2 .   ? -23.216 7.966   12.104  1.00 44.14 ? 535 HOH A O   1 
HETATM 8140 O O   . HOH C 2 .   ? -9.213  9.134   52.182  1.00 26.04 ? 536 HOH A O   1 
HETATM 8141 O O   . HOH C 2 .   ? 5.421   -0.513  9.658   1.00 16.66 ? 537 HOH A O   1 
HETATM 8142 O O   . HOH C 2 .   ? 26.374  7.483   6.096   1.00 29.50 ? 538 HOH A O   1 
HETATM 8143 O O   . HOH C 2 .   ? -16.778 -6.909  53.943  1.00 40.54 ? 539 HOH A O   1 
HETATM 8144 O O   . HOH C 2 .   ? -18.638 11.188  20.513  1.00 39.16 ? 540 HOH A O   1 
HETATM 8145 O O   . HOH C 2 .   ? -0.313  14.314  13.454  1.00 43.09 ? 541 HOH A O   1 
HETATM 8146 O O   . HOH C 2 .   ? 2.934   10.032  21.036  1.00 40.56 ? 542 HOH A O   1 
HETATM 8147 O O   . HOH C 2 .   ? -10.560 12.275  32.021  1.00 38.46 ? 543 HOH A O   1 
HETATM 8148 O O   . HOH C 2 .   ? 16.690  -1.108  22.692  1.00 17.69 ? 544 HOH A O   1 
HETATM 8149 O O   . HOH C 2 .   ? 2.013   3.347   21.356  1.00 24.27 ? 545 HOH A O   1 
HETATM 8150 O O   . HOH C 2 .   ? 8.558   -0.342  2.969   1.00 21.46 ? 546 HOH A O   1 
HETATM 8151 O O   . HOH C 2 .   ? 3.972   -10.375 9.107   1.00 26.71 ? 547 HOH A O   1 
HETATM 8152 O O   . HOH C 2 .   ? 9.126   -16.776 25.137  1.00 32.96 ? 548 HOH A O   1 
HETATM 8153 O O   . HOH C 2 .   ? -22.282 -2.782  30.616  1.00 20.97 ? 549 HOH A O   1 
HETATM 8154 O O   . HOH C 2 .   ? -22.993 10.332  39.726  1.00 40.76 ? 550 HOH A O   1 
HETATM 8155 O O   . HOH C 2 .   ? -4.228  3.111   19.235  1.00 25.51 ? 551 HOH A O   1 
HETATM 8156 O O   . HOH C 2 .   ? -0.393  1.243   26.700  1.00 13.69 ? 552 HOH A O   1 
HETATM 8157 O O   . HOH C 2 .   ? -8.845  2.998   22.896  1.00 19.16 ? 553 HOH A O   1 
HETATM 8158 O O   . HOH C 2 .   ? 17.418  -1.815  25.512  1.00 21.42 ? 554 HOH A O   1 
HETATM 8159 O O   . HOH C 2 .   ? -5.631  1.588   23.368  1.00 37.32 ? 555 HOH A O   1 
HETATM 8160 O O   . HOH C 2 .   ? 19.001  -11.148 16.530  1.00 35.61 ? 556 HOH A O   1 
HETATM 8161 O O   . HOH C 2 .   ? 15.961  -1.216  31.527  1.00 18.29 ? 557 HOH A O   1 
HETATM 8162 O O   . HOH C 2 .   ? -25.519 13.767  27.407  1.00 30.44 ? 558 HOH A O   1 
HETATM 8163 O O   . HOH C 2 .   ? 10.946  14.790  34.785  1.00 27.36 ? 559 HOH A O   1 
HETATM 8164 O O   . HOH C 2 .   ? 3.540   -11.109 45.339  1.00 28.60 ? 560 HOH A O   1 
HETATM 8165 O O   . HOH C 2 .   ? -28.907 8.858   32.623  1.00 41.09 ? 561 HOH A O   1 
HETATM 8166 O O   . HOH C 2 .   ? -13.909 -3.841  30.771  1.00 13.69 ? 562 HOH A O   1 
HETATM 8167 O O   . HOH C 2 .   ? -9.134  2.336   45.577  1.00 14.66 ? 563 HOH A O   1 
HETATM 8168 O O   . HOH C 2 .   ? 12.327  15.371  30.924  1.00 35.25 ? 564 HOH A O   1 
HETATM 8169 O O   . HOH C 2 .   ? 2.146   -12.112 41.340  1.00 50.40 ? 565 HOH A O   1 
HETATM 8170 O O   . HOH C 2 .   ? 2.624   6.170   28.864  1.00 21.61 ? 566 HOH A O   1 
HETATM 8171 O O   . HOH C 2 .   ? -7.038  -3.426  19.849  1.00 17.94 ? 567 HOH A O   1 
HETATM 8172 O O   . HOH C 2 .   ? -30.052 11.722  14.553  1.00 38.51 ? 568 HOH A O   1 
HETATM 8173 O O   . HOH C 2 .   ? 2.647   11.681  27.428  1.00 26.79 ? 569 HOH A O   1 
HETATM 8174 O O   . HOH C 2 .   ? -0.213  1.894   23.313  1.00 26.71 ? 570 HOH A O   1 
HETATM 8175 O O   . HOH C 2 .   ? 9.689   0.407   35.008  1.00 12.27 ? 571 HOH A O   1 
HETATM 8176 O O   . HOH C 2 .   ? -13.327 12.759  16.310  1.00 38.72 ? 572 HOH A O   1 
HETATM 8177 O O   . HOH C 2 .   ? -13.000 -2.305  28.535  1.00 23.55 ? 573 HOH A O   1 
HETATM 8178 O O   . HOH C 2 .   ? 7.615   15.669  17.295  1.00 31.41 ? 574 HOH A O   1 
HETATM 8179 O O   . HOH C 2 .   ? 16.751  4.958   -3.768  1.00 38.55 ? 575 HOH A O   1 
HETATM 8180 O O   . HOH C 2 .   ? 2.365   -2.043  57.652  1.00 47.28 ? 576 HOH A O   1 
HETATM 8181 O O   . HOH C 2 .   ? 11.150  -14.343 25.515  1.00 29.79 ? 577 HOH A O   1 
HETATM 8182 O O   . HOH C 2 .   ? -1.748  -4.274  3.154   1.00 44.13 ? 578 HOH A O   1 
HETATM 8183 O O   . HOH C 2 .   ? -20.838 8.250   28.078  1.00 22.14 ? 579 HOH A O   1 
HETATM 8184 O O   . HOH C 2 .   ? 23.888  9.432   -3.158  1.00 40.57 ? 580 HOH A O   1 
HETATM 8185 O O   . HOH C 2 .   ? -22.827 0.248   35.483  1.00 17.20 ? 581 HOH A O   1 
HETATM 8186 O O   . HOH C 2 .   ? -4.828  0.600   57.686  1.00 18.55 ? 582 HOH A O   1 
HETATM 8187 O O   . HOH C 2 .   ? -3.528  -10.110 10.572  1.00 29.42 ? 583 HOH A O   1 
HETATM 8188 O O   . HOH C 2 .   ? 4.490   -2.763  14.721  1.00 14.52 ? 584 HOH A O   1 
HETATM 8189 O O   . HOH C 2 .   ? 18.069  9.760   22.042  1.00 28.29 ? 585 HOH A O   1 
HETATM 8190 O O   . HOH C 2 .   ? -18.245 11.822  34.424  1.00 34.83 ? 586 HOH A O   1 
HETATM 8191 O O   . HOH C 2 .   ? -6.361  1.327   53.028  1.00 13.11 ? 587 HOH A O   1 
HETATM 8192 O O   . HOH C 2 .   ? 18.339  -3.644  34.126  1.00 33.33 ? 588 HOH A O   1 
HETATM 8193 O O   . HOH C 2 .   ? -22.905 6.443   6.654   1.00 50.35 ? 589 HOH A O   1 
HETATM 8194 O O   . HOH C 2 .   ? -8.003  4.634   5.004   1.00 20.22 ? 590 HOH A O   1 
HETATM 8195 O O   . HOH C 2 .   ? 18.946  7.058   22.044  1.00 31.47 ? 591 HOH A O   1 
HETATM 8196 O O   . HOH C 2 .   ? -6.335  0.622   28.758  1.00 12.90 ? 592 HOH A O   1 
HETATM 8197 O O   . HOH C 2 .   ? 4.817   6.327   20.350  1.00 24.65 ? 593 HOH A O   1 
HETATM 8198 O O   . HOH C 2 .   ? -6.037  10.007  32.348  1.00 33.89 ? 594 HOH A O   1 
HETATM 8199 O O   . HOH C 2 .   ? -5.323  4.565   44.727  1.00 17.03 ? 595 HOH A O   1 
HETATM 8200 O O   . HOH C 2 .   ? -11.673 6.549   54.277  1.00 17.71 ? 596 HOH A O   1 
HETATM 8201 O O   . HOH C 2 .   ? -15.544 -4.176  53.823  1.00 25.12 ? 597 HOH A O   1 
HETATM 8202 O O   . HOH C 2 .   ? -24.764 -6.411  22.995  1.00 29.62 ? 598 HOH A O   1 
HETATM 8203 O O   . HOH C 2 .   ? -28.408 -6.049  29.848  1.00 52.29 ? 599 HOH A O   1 
HETATM 8204 O O   . HOH C 2 .   ? 4.054   -18.118 36.063  1.00 49.63 ? 600 HOH A O   1 
HETATM 8205 O O   . HOH C 2 .   ? 11.241  -17.869 29.709  1.00 45.37 ? 601 HOH A O   1 
HETATM 8206 O O   . HOH C 2 .   ? 4.982   13.449  31.303  1.00 17.06 ? 602 HOH A O   1 
HETATM 8207 O O   . HOH C 2 .   ? -4.146  -11.666 17.348  1.00 35.20 ? 603 HOH A O   1 
HETATM 8208 O O   . HOH C 2 .   ? -14.038 -14.640 40.425  1.00 25.14 ? 604 HOH A O   1 
HETATM 8209 O O   . HOH C 2 .   ? 11.326  2.721   28.785  1.00 19.12 ? 605 HOH A O   1 
HETATM 8210 O O   . HOH C 2 .   ? 4.582   -11.479 49.519  1.00 37.62 ? 606 HOH A O   1 
HETATM 8211 O O   . HOH C 2 .   ? 4.345   18.240  46.396  1.00 40.90 ? 607 HOH A O   1 
HETATM 8212 O O   . HOH C 2 .   ? 15.590  16.527  16.049  1.00 41.36 ? 608 HOH A O   1 
HETATM 8213 O O   . HOH C 2 .   ? 28.549  -1.381  5.502   1.00 38.17 ? 609 HOH A O   1 
HETATM 8214 O O   . HOH C 2 .   ? 3.465   8.371   22.713  1.00 31.91 ? 610 HOH A O   1 
HETATM 8215 O O   . HOH C 2 .   ? -7.389  -3.693  2.684   1.00 44.90 ? 611 HOH A O   1 
HETATM 8216 O O   . HOH C 2 .   ? 6.046   -10.938 46.123  1.00 35.84 ? 612 HOH A O   1 
HETATM 8217 O O   . HOH C 2 .   ? -22.765 1.215   47.198  1.00 31.05 ? 613 HOH A O   1 
HETATM 8218 O O   . HOH C 2 .   ? 12.646  -2.566  25.838  1.00 14.50 ? 614 HOH A O   1 
HETATM 8219 O O   . HOH C 2 .   ? -18.565 7.077   35.352  1.00 19.50 ? 615 HOH A O   1 
HETATM 8220 O O   . HOH C 2 .   ? 19.101  -3.168  0.198   1.00 46.38 ? 616 HOH A O   1 
HETATM 8221 O O   . HOH C 2 .   ? -21.469 -12.422 28.424  1.00 37.26 ? 617 HOH A O   1 
HETATM 8222 O O   . HOH C 2 .   ? 4.124   -1.617  42.770  1.00 15.98 ? 618 HOH A O   1 
HETATM 8223 O O   . HOH C 2 .   ? 4.875   -12.230 41.424  1.00 33.81 ? 619 HOH A O   1 
HETATM 8224 O O   . HOH C 2 .   ? -18.215 5.026   5.922   1.00 29.25 ? 620 HOH A O   1 
HETATM 8225 O O   . HOH C 2 .   ? 12.409  4.323   30.818  1.00 20.90 ? 621 HOH A O   1 
HETATM 8226 O O   . HOH C 2 .   ? 17.607  -13.016 40.130  1.00 38.76 ? 622 HOH A O   1 
HETATM 8227 O O   . HOH C 2 .   ? -18.471 11.539  44.942  1.00 23.38 ? 623 HOH A O   1 
HETATM 8228 O O   . HOH C 2 .   ? 14.111  2.373   28.095  1.00 16.26 ? 624 HOH A O   1 
HETATM 8229 O O   . HOH C 2 .   ? 1.868   1.827   5.868   1.00 31.80 ? 625 HOH A O   1 
HETATM 8230 O O   . HOH C 2 .   ? 9.644   -12.374 23.666  1.00 21.17 ? 626 HOH A O   1 
HETATM 8231 O O   . HOH C 2 .   ? -14.647 -3.104  5.067   1.00 32.86 ? 627 HOH A O   1 
HETATM 8232 O O   . HOH C 2 .   ? -14.408 9.806   27.055  1.00 33.18 ? 628 HOH A O   1 
HETATM 8233 O O   . HOH C 2 .   ? 31.825  5.557   9.171   1.00 42.73 ? 629 HOH A O   1 
HETATM 8234 O O   . HOH C 2 .   ? 17.941  16.187  37.703  1.00 44.78 ? 630 HOH A O   1 
HETATM 8235 O O   . HOH C 2 .   ? -27.760 -6.071  27.026  1.00 44.58 ? 631 HOH A O   1 
HETATM 8236 O O   . HOH C 2 .   ? -1.745  6.592   30.212  1.00 19.65 ? 632 HOH A O   1 
HETATM 8237 O O   . HOH C 2 .   ? -7.930  11.041  31.513  1.00 48.87 ? 633 HOH A O   1 
HETATM 8238 O O   . HOH C 2 .   ? -26.828 -1.665  36.027  1.00 34.37 ? 634 HOH A O   1 
HETATM 8239 O O   . HOH C 2 .   ? -5.630  4.209   24.376  1.00 32.84 ? 635 HOH A O   1 
HETATM 8240 O O   . HOH C 2 .   ? 13.871  11.736  32.522  1.00 20.26 ? 636 HOH A O   1 
HETATM 8241 O O   . HOH C 2 .   ? 2.472   -13.202 47.830  1.00 35.86 ? 637 HOH A O   1 
HETATM 8242 O O   . HOH C 2 .   ? 8.308   17.048  25.923  1.00 44.56 ? 638 HOH A O   1 
HETATM 8243 O O   . HOH C 2 .   ? 20.314  -9.923  13.103  1.00 47.41 ? 639 HOH A O   1 
HETATM 8244 O O   . HOH C 2 .   ? -19.745 12.811  31.759  1.00 41.51 ? 640 HOH A O   1 
HETATM 8245 O O   . HOH C 2 .   ? 17.062  13.094  25.235  1.00 27.71 ? 641 HOH A O   1 
HETATM 8246 O O   . HOH C 2 .   ? -1.383  -8.777  55.272  1.00 35.98 ? 642 HOH A O   1 
HETATM 8247 O O   . HOH C 2 .   ? 4.000   14.338  19.310  1.00 45.13 ? 643 HOH A O   1 
HETATM 8248 O O   . HOH C 2 .   ? 17.992  -2.615  45.041  1.00 45.38 ? 644 HOH A O   1 
HETATM 8249 O O   . HOH C 2 .   ? 12.067  -11.176 45.364  1.00 33.25 ? 645 HOH A O   1 
HETATM 8250 O O   . HOH C 2 .   ? -21.613 -14.108 19.183  1.00 30.26 ? 646 HOH A O   1 
HETATM 8251 O O   . HOH C 2 .   ? -11.625 -7.316  54.468  1.00 27.18 ? 647 HOH A O   1 
HETATM 8252 O O   . HOH C 2 .   ? 24.417  -3.031  1.425   1.00 43.86 ? 648 HOH A O   1 
HETATM 8253 O O   . HOH C 2 .   ? -18.582 -1.083  53.727  1.00 35.60 ? 649 HOH A O   1 
HETATM 8254 O O   . HOH C 2 .   ? 33.053  0.819   12.512  1.00 45.73 ? 650 HOH A O   1 
HETATM 8255 O O   . HOH C 2 .   ? -15.956 -1.157  6.005   1.00 27.10 ? 651 HOH A O   1 
HETATM 8256 O O   . HOH C 2 .   ? 16.593  -5.792  3.373   1.00 52.08 ? 652 HOH A O   1 
HETATM 8257 O O   . HOH C 2 .   ? 10.407  0.389   52.647  1.00 48.27 ? 653 HOH A O   1 
HETATM 8258 O O   . HOH C 2 .   ? 21.246  -2.936  41.962  1.00 35.80 ? 654 HOH A O   1 
HETATM 8259 O O   . HOH C 2 .   ? -6.564  -4.981  17.680  1.00 14.48 ? 655 HOH A O   1 
HETATM 8260 O O   . HOH C 2 .   ? 16.409  -16.419 16.903  1.00 45.04 ? 656 HOH A O   1 
HETATM 8261 O O   . HOH C 2 .   ? 27.702  1.428   3.911   1.00 23.56 ? 657 HOH A O   1 
HETATM 8262 O O   . HOH C 2 .   ? -24.728 -11.466 32.711  1.00 40.54 ? 658 HOH A O   1 
HETATM 8263 O O   . HOH C 2 .   ? -18.709 -19.398 35.403  1.00 50.63 ? 659 HOH A O   1 
HETATM 8264 O O   . HOH C 2 .   ? 3.435   10.327  17.899  1.00 33.26 ? 660 HOH A O   1 
HETATM 8265 O O   . HOH C 2 .   ? -26.113 -4.798  21.567  1.00 30.77 ? 661 HOH A O   1 
HETATM 8266 O O   . HOH C 2 .   ? 20.663  2.444   37.387  1.00 41.93 ? 662 HOH A O   1 
HETATM 8267 O O   . HOH C 2 .   ? 5.176   12.528  28.748  1.00 19.19 ? 663 HOH A O   1 
HETATM 8268 O O   . HOH C 2 .   ? -0.079  6.504   14.990  1.00 28.33 ? 664 HOH A O   1 
HETATM 8269 O O   . HOH C 2 .   ? -16.682 -18.077 27.377  1.00 41.63 ? 665 HOH A O   1 
HETATM 8270 O O   . HOH C 2 .   ? -22.586 -10.036 32.830  1.00 31.70 ? 666 HOH A O   1 
HETATM 8271 O O   . HOH C 2 .   ? -4.897  15.163  36.657  1.00 36.63 ? 667 HOH A O   1 
HETATM 8272 O O   . HOH C 2 .   ? -15.073 5.547   55.428  1.00 31.05 ? 668 HOH A O   1 
HETATM 8273 O O   . HOH C 2 .   ? 2.028   -14.985 17.383  1.00 43.73 ? 669 HOH A O   1 
HETATM 8274 O O   . HOH C 2 .   ? 24.160  11.478  21.263  1.00 47.83 ? 670 HOH A O   1 
HETATM 8275 O O   . HOH C 2 .   ? -9.701  16.392  15.498  1.00 53.64 ? 671 HOH A O   1 
HETATM 8276 O O   . HOH C 2 .   ? -5.012  2.722   27.379  1.00 23.06 ? 672 HOH A O   1 
HETATM 8277 O O   . HOH C 2 .   ? -3.349  1.034   25.328  1.00 24.92 ? 673 HOH A O   1 
HETATM 8278 O O   . HOH C 2 .   ? -22.244 5.988   48.184  1.00 35.89 ? 674 HOH A O   1 
HETATM 8279 O O   . HOH C 2 .   ? -17.276 -6.482  2.704   1.00 42.46 ? 675 HOH A O   1 
HETATM 8280 O O   . HOH C 2 .   ? 15.132  -11.927 29.643  1.00 37.85 ? 676 HOH A O   1 
HETATM 8281 O O   . HOH C 2 .   ? -11.841 -1.348  57.040  1.00 24.07 ? 677 HOH A O   1 
HETATM 8282 O O   . HOH C 2 .   ? -25.458 -11.996 17.866  1.00 43.30 ? 678 HOH A O   1 
HETATM 8283 O O   . HOH C 2 .   ? 1.012   -12.456 38.469  1.00 16.16 ? 679 HOH A O   1 
HETATM 8284 O O   . HOH C 2 .   ? -23.026 -18.583 37.056  1.00 43.53 ? 680 HOH A O   1 
HETATM 8285 O O   . HOH C 2 .   ? 10.063  -10.908 8.268   1.00 47.82 ? 681 HOH A O   1 
HETATM 8286 O O   . HOH C 2 .   ? -10.466 6.190   59.072  1.00 32.79 ? 682 HOH A O   1 
HETATM 8287 O O   . HOH C 2 .   ? 3.811   15.586  60.051  1.00 41.90 ? 683 HOH A O   1 
HETATM 8288 O O   . HOH C 2 .   ? 5.594   -18.161 34.241  1.00 46.71 ? 684 HOH A O   1 
HETATM 8289 O O   . HOH C 2 .   ? 16.803  -10.911 30.578  1.00 40.58 ? 685 HOH A O   1 
HETATM 8290 O O   . HOH C 2 .   ? 7.607   -17.164 20.791  1.00 41.31 ? 686 HOH A O   1 
HETATM 8291 O O   . HOH C 2 .   ? -25.189 9.068   13.769  1.00 40.08 ? 687 HOH A O   1 
HETATM 8292 O O   . HOH C 2 .   ? -28.273 -4.575  22.082  1.00 38.96 ? 688 HOH A O   1 
HETATM 8293 O O   . HOH C 2 .   ? -0.486  -13.600 41.649  1.00 39.54 ? 689 HOH A O   1 
HETATM 8294 O O   . HOH C 2 .   ? 10.568  -6.275  8.533   1.00 33.00 ? 690 HOH A O   1 
HETATM 8295 O O   . HOH C 2 .   ? 8.774   -9.864  49.079  1.00 35.75 ? 691 HOH A O   1 
HETATM 8296 O O   . HOH C 2 .   ? 0.678   8.562   28.755  1.00 38.68 ? 692 HOH A O   1 
HETATM 8297 O O   . HOH C 2 .   ? -6.287  4.012   21.686  1.00 26.73 ? 693 HOH A O   1 
HETATM 8298 O O   . HOH C 2 .   ? -1.772  3.304   19.231  1.00 43.21 ? 694 HOH A O   1 
HETATM 8299 O O   . HOH C 2 .   ? -16.319 -17.240 25.464  1.00 44.43 ? 695 HOH A O   1 
HETATM 8300 O O   . HOH C 2 .   ? 15.575  15.285  33.469  1.00 40.39 ? 696 HOH A O   1 
HETATM 8301 O O   . HOH C 2 .   ? 22.191  22.289  3.824   1.00 47.06 ? 697 HOH A O   1 
HETATM 8302 O O   . HOH C 2 .   ? -27.398 -3.677  34.811  1.00 42.50 ? 698 HOH A O   1 
HETATM 8303 O O   . HOH C 2 .   ? -2.156  -24.139 36.661  1.00 44.73 ? 699 HOH A O   1 
HETATM 8304 O O   . HOH C 2 .   ? 3.679   12.483  17.774  1.00 44.88 ? 700 HOH A O   1 
HETATM 8305 O O   . HOH C 2 .   ? 7.563   17.096  22.144  1.00 47.46 ? 701 HOH A O   1 
HETATM 8306 O O   . HOH C 2 .   ? 13.249  14.241  33.123  1.00 25.22 ? 702 HOH A O   1 
HETATM 8307 O O   . HOH C 2 .   ? 16.853  -4.749  -4.577  1.00 33.50 ? 703 HOH A O   1 
HETATM 8308 O O   . HOH C 2 .   ? -5.866  -13.533 14.709  1.00 42.47 ? 704 HOH A O   1 
HETATM 8309 O O   . HOH C 2 .   ? -24.482 -2.006  32.915  1.00 24.73 ? 705 HOH A O   1 
HETATM 8310 O O   . HOH C 2 .   ? 19.562  2.800   44.024  1.00 52.17 ? 706 HOH A O   1 
HETATM 8311 O O   . HOH C 2 .   ? 11.862  5.114   62.628  1.00 46.52 ? 707 HOH A O   1 
HETATM 8312 O O   . HOH C 2 .   ? -23.192 2.661   45.696  1.00 52.54 ? 708 HOH A O   1 
HETATM 8313 O O   . HOH C 2 .   ? -0.019  4.545   19.047  1.00 45.21 ? 709 HOH A O   1 
HETATM 8314 O O   . HOH C 2 .   ? -4.007  7.032   28.979  1.00 40.75 ? 710 HOH A O   1 
HETATM 8315 O O   . HOH C 2 .   ? 3.069   7.666   19.158  1.00 40.93 ? 711 HOH A O   1 
HETATM 8316 O O   . HOH C 2 .   ? -19.884 13.763  21.091  1.00 55.05 ? 712 HOH A O   1 
HETATM 8317 O O   . HOH C 2 .   ? -15.323 13.994  45.712  1.00 41.58 ? 713 HOH A O   1 
HETATM 8318 O O   . HOH C 2 .   ? -5.059  7.853   30.848  1.00 43.18 ? 714 HOH A O   1 
HETATM 8319 O O   . HOH C 2 .   ? 2.015   5.208   19.515  1.00 38.96 ? 715 HOH A O   1 
HETATM 8320 O O   . HOH C 2 .   ? 8.075   18.202  23.699  1.00 47.01 ? 716 HOH A O   1 
HETATM 8321 O O   . HOH C 2 .   ? -13.697 0.044   58.082  1.00 45.93 ? 717 HOH A O   1 
HETATM 8322 O O   . HOH C 2 .   ? -23.314 -8.694  49.865  1.00 33.25 ? 718 HOH A O   1 
HETATM 8323 O O   . HOH C 2 .   ? -17.491 -16.881 15.918  1.00 39.50 ? 719 HOH A O   1 
HETATM 8324 O O   . HOH C 2 .   ? 0.836   4.610   -3.985  1.00 48.54 ? 720 HOH A O   1 
HETATM 8325 O O   . HOH C 2 .   ? 6.281   15.593  19.411  1.00 37.03 ? 721 HOH A O   1 
HETATM 8326 O O   . HOH C 2 .   ? -7.988  -14.324 14.416  1.00 37.70 ? 722 HOH A O   1 
HETATM 8327 O O   . HOH C 2 .   ? -28.635 -5.453  47.987  1.00 42.18 ? 723 HOH A O   1 
HETATM 8328 O O   . HOH C 2 .   ? -28.850 -4.536  24.493  1.00 50.68 ? 724 HOH A O   1 
HETATM 8329 O O   . HOH C 2 .   ? 8.900   -14.899 22.138  1.00 34.36 ? 725 HOH A O   1 
HETATM 8330 O O   . HOH C 2 .   ? 2.386   15.769  13.766  1.00 45.48 ? 726 HOH A O   1 
HETATM 8331 O O   . HOH C 2 .   ? 1.615   4.839   5.502   1.00 45.95 ? 727 HOH A O   1 
HETATM 8332 O O   . HOH D 2 .   ? 48.999  -22.625 91.401  1.00 41.81 ? 501 HOH B O   1 
HETATM 8333 O O   . HOH D 2 .   ? 0.209   -10.980 68.200  1.00 34.34 ? 502 HOH B O   1 
HETATM 8334 O O   . HOH D 2 .   ? 34.580  -8.343  55.195  1.00 19.45 ? 503 HOH B O   1 
HETATM 8335 O O   . HOH D 2 .   ? 34.686  -36.439 95.884  1.00 47.59 ? 504 HOH B O   1 
HETATM 8336 O O   . HOH D 2 .   ? 12.548  -26.138 52.372  1.00 42.42 ? 505 HOH B O   1 
HETATM 8337 O O   . HOH D 2 .   ? 52.203  -8.952  47.927  1.00 35.51 ? 506 HOH B O   1 
HETATM 8338 O O   . HOH D 2 .   ? 16.998  -33.378 87.640  1.00 43.62 ? 507 HOH B O   1 
HETATM 8339 O O   . HOH D 2 .   ? 52.944  -12.108 80.344  1.00 40.07 ? 508 HOH B O   1 
HETATM 8340 O O   . HOH D 2 .   ? 45.509  -35.789 71.409  1.00 30.43 ? 509 HOH B O   1 
HETATM 8341 O O   . HOH D 2 .   ? 19.116  -33.179 86.379  1.00 48.18 ? 510 HOH B O   1 
HETATM 8342 O O   . HOH D 2 .   ? 22.405  -23.591 93.668  1.00 27.20 ? 511 HOH B O   1 
HETATM 8343 O O   . HOH D 2 .   ? -5.848  -17.589 66.288  1.00 47.39 ? 512 HOH B O   1 
HETATM 8344 O O   . HOH D 2 .   ? 48.152  -6.949  80.470  1.00 21.87 ? 513 HOH B O   1 
HETATM 8345 O O   . HOH D 2 .   ? 28.395  -32.553 93.193  1.00 30.40 ? 514 HOH B O   1 
HETATM 8346 O O   . HOH D 2 .   ? 9.060   -29.717 64.013  1.00 34.42 ? 515 HOH B O   1 
HETATM 8347 O O   . HOH D 2 .   ? 47.354  -15.151 49.474  1.00 44.35 ? 516 HOH B O   1 
HETATM 8348 O O   . HOH D 2 .   ? 38.694  -7.220  58.089  1.00 50.78 ? 517 HOH B O   1 
HETATM 8349 O O   . HOH D 2 .   ? 47.637  -13.892 69.374  1.00 14.10 ? 518 HOH B O   1 
HETATM 8350 O O   . HOH D 2 .   ? 32.258  -33.389 80.887  1.00 30.37 ? 519 HOH B O   1 
HETATM 8351 O O   . HOH D 2 .   ? 40.236  -9.729  54.278  1.00 29.32 ? 520 HOH B O   1 
HETATM 8352 O O   . HOH D 2 .   ? -0.202  4.693   93.429  1.00 39.36 ? 521 HOH B O   1 
HETATM 8353 O O   . HOH D 2 .   ? 3.027   -22.009 63.643  1.00 45.93 ? 522 HOH B O   1 
HETATM 8354 O O   . HOH D 2 .   ? 52.360  -30.087 60.053  1.00 30.80 ? 523 HOH B O   1 
HETATM 8355 O O   . HOH D 2 .   ? -2.374  -24.990 88.171  1.00 45.12 ? 524 HOH B O   1 
HETATM 8356 O O   . HOH D 2 .   ? 18.446  -29.333 87.234  1.00 13.90 ? 525 HOH B O   1 
HETATM 8357 O O   . HOH D 2 .   ? -4.862  -7.494  84.788  1.00 38.76 ? 526 HOH B O   1 
HETATM 8358 O O   . HOH D 2 .   ? 4.266   -0.859  72.424  1.00 48.87 ? 527 HOH B O   1 
HETATM 8359 O O   . HOH D 2 .   ? 12.694  1.995   52.644  1.00 41.09 ? 528 HOH B O   1 
HETATM 8360 O O   . HOH D 2 .   ? 26.810  -2.203  48.687  1.00 40.80 ? 529 HOH B O   1 
HETATM 8361 O O   . HOH D 2 .   ? 23.177  -15.968 75.157  1.00 21.51 ? 530 HOH B O   1 
HETATM 8362 O O   . HOH D 2 .   ? 38.450  -10.650 47.432  1.00 18.67 ? 531 HOH B O   1 
HETATM 8363 O O   . HOH D 2 .   ? 18.190  -12.930 70.944  1.00 11.71 ? 532 HOH B O   1 
HETATM 8364 O O   . HOH D 2 .   ? 39.230  -21.249 77.832  1.00 20.92 ? 533 HOH B O   1 
HETATM 8365 O O   . HOH D 2 .   ? 22.043  -9.622  75.162  1.00 36.72 ? 534 HOH B O   1 
HETATM 8366 O O   . HOH D 2 .   ? 10.439  -12.977 71.136  1.00 11.33 ? 535 HOH B O   1 
HETATM 8367 O O   . HOH D 2 .   ? -7.192  -9.453  77.797  1.00 26.43 ? 536 HOH B O   1 
HETATM 8368 O O   . HOH D 2 .   ? 49.756  -24.529 80.183  1.00 16.38 ? 537 HOH B O   1 
HETATM 8369 O O   . HOH D 2 .   ? 29.620  -10.910 63.872  1.00 36.04 ? 538 HOH B O   1 
HETATM 8370 O O   . HOH D 2 .   ? 40.725  -27.849 45.342  1.00 25.61 ? 539 HOH B O   1 
HETATM 8371 O O   . HOH D 2 .   ? 54.001  -25.100 72.134  1.00 27.28 ? 540 HOH B O   1 
HETATM 8372 O O   . HOH D 2 .   ? 30.139  -16.893 70.226  1.00 13.13 ? 541 HOH B O   1 
HETATM 8373 O O   . HOH D 2 .   ? 14.830  -3.790  64.057  1.00 22.78 ? 542 HOH B O   1 
HETATM 8374 O O   . HOH D 2 .   ? 23.557  -13.551 67.449  1.00 18.84 ? 543 HOH B O   1 
HETATM 8375 O O   . HOH D 2 .   ? 28.066  -25.526 97.526  1.00 36.28 ? 544 HOH B O   1 
HETATM 8376 O O   . HOH D 2 .   ? 6.653   -21.237 96.966  1.00 45.36 ? 545 HOH B O   1 
HETATM 8377 O O   . HOH D 2 .   ? 35.995  -9.951  63.593  1.00 21.78 ? 546 HOH B O   1 
HETATM 8378 O O   . HOH D 2 .   ? -3.435  -21.003 90.816  1.00 36.63 ? 547 HOH B O   1 
HETATM 8379 O O   . HOH D 2 .   ? 19.299  -18.700 46.276  1.00 36.35 ? 548 HOH B O   1 
HETATM 8380 O O   . HOH D 2 .   ? 48.027  -22.653 70.290  1.00 6.21  ? 549 HOH B O   1 
HETATM 8381 O O   . HOH D 2 .   ? 14.845  -25.343 71.892  1.00 17.26 ? 550 HOH B O   1 
HETATM 8382 O O   . HOH D 2 .   ? 7.636   -23.748 62.586  1.00 22.25 ? 551 HOH B O   1 
HETATM 8383 O O   . HOH D 2 .   ? 45.616  -28.499 47.587  1.00 30.22 ? 552 HOH B O   1 
HETATM 8384 O O   . HOH D 2 .   ? 13.748  -33.837 69.780  1.00 15.73 ? 553 HOH B O   1 
HETATM 8385 O O   . HOH D 2 .   ? 5.851   -15.756 63.645  1.00 19.67 ? 554 HOH B O   1 
HETATM 8386 O O   . HOH D 2 .   ? 7.631   -9.342  71.871  1.00 23.20 ? 555 HOH B O   1 
HETATM 8387 O O   . HOH D 2 .   ? 35.298  -9.607  78.122  1.00 36.38 ? 556 HOH B O   1 
HETATM 8388 O O   . HOH D 2 .   ? 13.006  -21.319 97.293  1.00 39.07 ? 557 HOH B O   1 
HETATM 8389 O O   . HOH D 2 .   ? 4.825   -27.383 81.620  1.00 41.09 ? 558 HOH B O   1 
HETATM 8390 O O   . HOH D 2 .   ? 24.116  -22.704 96.195  1.00 34.22 ? 559 HOH B O   1 
HETATM 8391 O O   . HOH D 2 .   ? -8.277  -18.458 81.934  1.00 10.32 ? 560 HOH B O   1 
HETATM 8392 O O   . HOH D 2 .   ? 25.028  -3.518  44.516  1.00 27.12 ? 561 HOH B O   1 
HETATM 8393 O O   . HOH D 2 .   ? 26.098  -18.284 70.328  1.00 10.13 ? 562 HOH B O   1 
HETATM 8394 O O   . HOH D 2 .   ? 24.756  -31.221 51.548  1.00 22.32 ? 563 HOH B O   1 
HETATM 8395 O O   . HOH D 2 .   ? 39.677  -23.529 68.708  1.00 9.73  ? 564 HOH B O   1 
HETATM 8396 O O   . HOH D 2 .   ? 19.856  -20.829 47.558  1.00 23.15 ? 565 HOH B O   1 
HETATM 8397 O O   . HOH D 2 .   ? 24.923  -32.316 90.514  1.00 40.77 ? 566 HOH B O   1 
HETATM 8398 O O   . HOH D 2 .   ? 53.217  -19.409 79.345  1.00 20.96 ? 567 HOH B O   1 
HETATM 8399 O O   . HOH D 2 .   ? 24.792  -31.647 47.359  1.00 39.83 ? 568 HOH B O   1 
HETATM 8400 O O   . HOH D 2 .   ? 42.923  -32.928 85.499  1.00 29.67 ? 569 HOH B O   1 
HETATM 8401 O O   . HOH D 2 .   ? 20.199  -13.092 75.340  1.00 24.59 ? 570 HOH B O   1 
HETATM 8402 O O   . HOH D 2 .   ? 12.745  -19.499 92.265  1.00 18.86 ? 571 HOH B O   1 
HETATM 8403 O O   . HOH D 2 .   ? 23.875  -21.732 53.815  1.00 12.28 ? 572 HOH B O   1 
HETATM 8404 O O   . HOH D 2 .   ? 33.277  -16.364 75.320  1.00 10.19 ? 573 HOH B O   1 
HETATM 8405 O O   . HOH D 2 .   ? 8.365   -20.165 71.600  1.00 15.79 ? 574 HOH B O   1 
HETATM 8406 O O   . HOH D 2 .   ? 15.349  -35.872 70.744  1.00 27.48 ? 575 HOH B O   1 
HETATM 8407 O O   . HOH D 2 .   ? 51.356  -31.405 55.004  1.00 29.04 ? 576 HOH B O   1 
HETATM 8408 O O   . HOH D 2 .   ? 22.761  -32.070 55.329  1.00 25.22 ? 577 HOH B O   1 
HETATM 8409 O O   . HOH D 2 .   ? 28.242  -16.362 78.239  1.00 17.90 ? 578 HOH B O   1 
HETATM 8410 O O   . HOH D 2 .   ? 24.150  -40.373 60.941  1.00 30.11 ? 579 HOH B O   1 
HETATM 8411 O O   . HOH D 2 .   ? 2.016   -26.701 68.020  1.00 44.55 ? 580 HOH B O   1 
HETATM 8412 O O   . HOH D 2 .   ? 53.535  -22.854 76.094  1.00 27.32 ? 581 HOH B O   1 
HETATM 8413 O O   . HOH D 2 .   ? 2.176   -12.930 66.873  1.00 41.84 ? 582 HOH B O   1 
HETATM 8414 O O   . HOH D 2 .   ? 37.726  -18.161 53.094  1.00 11.65 ? 583 HOH B O   1 
HETATM 8415 O O   . HOH D 2 .   ? 41.146  -33.216 57.883  1.00 40.53 ? 584 HOH B O   1 
HETATM 8416 O O   . HOH D 2 .   ? 51.924  -22.167 90.803  1.00 38.40 ? 585 HOH B O   1 
HETATM 8417 O O   . HOH D 2 .   ? 46.376  -31.831 72.739  1.00 29.51 ? 586 HOH B O   1 
HETATM 8418 O O   . HOH D 2 .   ? 38.549  -21.998 70.776  1.00 15.38 ? 587 HOH B O   1 
HETATM 8419 O O   . HOH D 2 .   ? 47.343  -34.180 53.122  1.00 26.65 ? 588 HOH B O   1 
HETATM 8420 O O   . HOH D 2 .   ? 6.245   -10.974 63.126  1.00 36.91 ? 589 HOH B O   1 
HETATM 8421 O O   . HOH D 2 .   ? 8.596   -22.933 59.998  1.00 43.11 ? 590 HOH B O   1 
HETATM 8422 O O   . HOH D 2 .   ? 49.170  -26.038 78.114  1.00 16.07 ? 591 HOH B O   1 
HETATM 8423 O O   . HOH D 2 .   ? 45.519  -11.086 88.439  1.00 25.61 ? 592 HOH B O   1 
HETATM 8424 O O   . HOH D 2 .   ? 35.731  -36.766 62.514  1.00 36.12 ? 593 HOH B O   1 
HETATM 8425 O O   . HOH D 2 .   ? 29.599  -14.585 92.931  1.00 15.82 ? 594 HOH B O   1 
HETATM 8426 O O   . HOH D 2 .   ? 17.056  -3.680  78.182  1.00 25.61 ? 595 HOH B O   1 
HETATM 8427 O O   . HOH D 2 .   ? 42.408  -8.080  78.883  1.00 22.04 ? 596 HOH B O   1 
HETATM 8428 O O   . HOH D 2 .   ? 49.514  -19.762 65.281  1.00 12.99 ? 597 HOH B O   1 
HETATM 8429 O O   . HOH D 2 .   ? 1.073   -7.596  72.478  1.00 35.60 ? 598 HOH B O   1 
HETATM 8430 O O   . HOH D 2 .   ? 16.401  -4.921  60.156  1.00 19.08 ? 599 HOH B O   1 
HETATM 8431 O O   . HOH D 2 .   ? 31.031  -1.671  54.379  1.00 43.05 ? 600 HOH B O   1 
HETATM 8432 O O   . HOH D 2 .   ? 52.469  -20.935 65.687  1.00 43.91 ? 601 HOH B O   1 
HETATM 8433 O O   . HOH D 2 .   ? 56.489  -22.251 87.229  1.00 30.59 ? 602 HOH B O   1 
HETATM 8434 O O   . HOH D 2 .   ? 44.233  -5.001  84.832  1.00 35.91 ? 603 HOH B O   1 
HETATM 8435 O O   . HOH D 2 .   ? 7.118   -25.858 63.146  1.00 35.93 ? 604 HOH B O   1 
HETATM 8436 O O   . HOH D 2 .   ? 18.948  -21.755 81.472  1.00 9.90  ? 605 HOH B O   1 
HETATM 8437 O O   . HOH D 2 .   ? 14.649  -37.417 65.457  1.00 33.58 ? 606 HOH B O   1 
HETATM 8438 O O   . HOH D 2 .   ? 31.204  -22.793 78.335  1.00 12.30 ? 607 HOH B O   1 
HETATM 8439 O O   . HOH D 2 .   ? 15.496  -24.496 95.966  1.00 48.10 ? 608 HOH B O   1 
HETATM 8440 O O   . HOH D 2 .   ? 25.319  0.569   53.898  1.00 44.68 ? 609 HOH B O   1 
HETATM 8441 O O   . HOH D 2 .   ? 8.995   -5.934  68.563  1.00 23.49 ? 610 HOH B O   1 
HETATM 8442 O O   . HOH D 2 .   ? 32.641  -5.147  60.579  1.00 29.32 ? 611 HOH B O   1 
HETATM 8443 O O   . HOH D 2 .   ? 15.082  -16.796 66.371  1.00 17.37 ? 612 HOH B O   1 
HETATM 8444 O O   . HOH D 2 .   ? 48.332  -31.221 83.525  1.00 31.37 ? 613 HOH B O   1 
HETATM 8445 O O   . HOH D 2 .   ? 12.096  -17.044 66.645  1.00 11.39 ? 614 HOH B O   1 
HETATM 8446 O O   . HOH D 2 .   ? 2.238   -25.876 82.195  1.00 35.49 ? 615 HOH B O   1 
HETATM 8447 O O   . HOH D 2 .   ? 22.703  -25.957 47.446  1.00 33.55 ? 616 HOH B O   1 
HETATM 8448 O O   . HOH D 2 .   ? 9.025   -19.690 50.349  1.00 33.97 ? 617 HOH B O   1 
HETATM 8449 O O   . HOH D 2 .   ? 33.727  -15.905 53.197  1.00 13.00 ? 618 HOH B O   1 
HETATM 8450 O O   . HOH D 2 .   ? 0.903   -4.946  76.671  1.00 18.31 ? 619 HOH B O   1 
HETATM 8451 O O   . HOH D 2 .   ? -3.815  -10.702 85.589  1.00 16.78 ? 620 HOH B O   1 
HETATM 8452 O O   . HOH D 2 .   ? 15.501  -12.719 42.180  1.00 33.30 ? 621 HOH B O   1 
HETATM 8453 O O   . HOH D 2 .   ? 9.288   -0.484  48.389  1.00 25.08 ? 622 HOH B O   1 
HETATM 8454 O O   . HOH D 2 .   ? 13.895  -35.900 63.180  1.00 30.13 ? 623 HOH B O   1 
HETATM 8455 O O   . HOH D 2 .   ? 21.920  -11.410 73.418  1.00 32.69 ? 624 HOH B O   1 
HETATM 8456 O O   . HOH D 2 .   ? 21.934  0.398   51.892  1.00 46.25 ? 625 HOH B O   1 
HETATM 8457 O O   . HOH D 2 .   ? -4.229  -24.261 86.239  1.00 42.40 ? 626 HOH B O   1 
HETATM 8458 O O   . HOH D 2 .   ? 52.620  -25.197 74.782  1.00 29.51 ? 627 HOH B O   1 
HETATM 8459 O O   . HOH D 2 .   ? 17.369  -19.542 86.255  1.00 16.80 ? 628 HOH B O   1 
HETATM 8460 O O   . HOH D 2 .   ? 45.483  -38.737 64.847  1.00 41.00 ? 629 HOH B O   1 
HETATM 8461 O O   . HOH D 2 .   ? 23.257  -12.477 81.820  1.00 20.54 ? 630 HOH B O   1 
HETATM 8462 O O   . HOH D 2 .   ? 46.993  -8.666  54.741  1.00 24.21 ? 631 HOH B O   1 
HETATM 8463 O O   . HOH D 2 .   ? 23.444  -7.411  68.630  1.00 24.22 ? 632 HOH B O   1 
HETATM 8464 O O   . HOH D 2 .   ? 25.978  -32.379 56.163  1.00 33.91 ? 633 HOH B O   1 
HETATM 8465 O O   . HOH D 2 .   ? -5.960  -10.659 71.087  1.00 25.50 ? 634 HOH B O   1 
HETATM 8466 O O   . HOH D 2 .   ? 46.202  -11.714 72.087  1.00 14.30 ? 635 HOH B O   1 
HETATM 8467 O O   . HOH D 2 .   ? 36.063  -19.191 45.203  1.00 14.92 ? 636 HOH B O   1 
HETATM 8468 O O   . HOH D 2 .   ? 29.076  -28.794 43.074  1.00 41.69 ? 637 HOH B O   1 
HETATM 8469 O O   . HOH D 2 .   ? 1.493   -14.194 99.370  1.00 27.76 ? 638 HOH B O   1 
HETATM 8470 O O   . HOH D 2 .   ? 48.577  -29.542 68.460  1.00 26.25 ? 639 HOH B O   1 
HETATM 8471 O O   . HOH D 2 .   ? 21.706  -15.099 76.520  1.00 25.82 ? 640 HOH B O   1 
HETATM 8472 O O   . HOH D 2 .   ? 44.892  -8.233  65.366  1.00 23.60 ? 641 HOH B O   1 
HETATM 8473 O O   . HOH D 2 .   ? 9.277   -2.598  77.994  1.00 29.52 ? 642 HOH B O   1 
HETATM 8474 O O   . HOH D 2 .   ? 3.556   -13.835 97.284  1.00 29.38 ? 643 HOH B O   1 
HETATM 8475 O O   . HOH D 2 .   ? 33.248  -21.810 94.826  1.00 53.62 ? 644 HOH B O   1 
HETATM 8476 O O   . HOH D 2 .   ? 39.858  -7.389  72.078  1.00 48.66 ? 645 HOH B O   1 
HETATM 8477 O O   . HOH D 2 .   ? 48.516  -31.990 79.129  1.00 22.24 ? 646 HOH B O   1 
HETATM 8478 O O   . HOH D 2 .   ? 35.207  -20.204 40.164  1.00 22.52 ? 647 HOH B O   1 
HETATM 8479 O O   . HOH D 2 .   ? 45.125  -24.838 46.384  1.00 31.12 ? 648 HOH B O   1 
HETATM 8480 O O   . HOH D 2 .   ? 43.749  -14.923 48.364  1.00 35.29 ? 649 HOH B O   1 
HETATM 8481 O O   . HOH D 2 .   ? 36.530  -3.479  85.365  1.00 49.45 ? 650 HOH B O   1 
HETATM 8482 O O   . HOH D 2 .   ? 29.131  -17.765 74.298  1.00 31.28 ? 651 HOH B O   1 
HETATM 8483 O O   . HOH D 2 .   ? 36.606  -7.345  66.389  1.00 35.13 ? 652 HOH B O   1 
HETATM 8484 O O   . HOH D 2 .   ? 8.093   -20.989 68.800  1.00 7.76  ? 653 HOH B O   1 
HETATM 8485 O O   . HOH D 2 .   ? 25.942  -29.258 87.109  1.00 15.98 ? 654 HOH B O   1 
HETATM 8486 O O   . HOH D 2 .   ? 39.391  -11.843 91.029  1.00 38.81 ? 655 HOH B O   1 
HETATM 8487 O O   . HOH D 2 .   ? 41.166  -34.685 59.816  1.00 27.72 ? 656 HOH B O   1 
HETATM 8488 O O   . HOH D 2 .   ? 41.086  -33.517 82.926  1.00 25.95 ? 657 HOH B O   1 
HETATM 8489 O O   . HOH D 2 .   ? 15.094  -31.799 71.960  1.00 10.00 ? 658 HOH B O   1 
HETATM 8490 O O   . HOH D 2 .   ? 17.465  -19.309 60.631  1.00 8.64  ? 659 HOH B O   1 
HETATM 8491 O O   . HOH D 2 .   ? 12.826  -21.825 69.226  1.00 8.32  ? 660 HOH B O   1 
HETATM 8492 O O   . HOH D 2 .   ? 36.283  -22.053 94.073  1.00 26.08 ? 661 HOH B O   1 
HETATM 8493 O O   . HOH D 2 .   ? 10.784  -20.505 62.811  1.00 13.57 ? 662 HOH B O   1 
HETATM 8494 O O   . HOH D 2 .   ? 31.997  -18.992 69.251  1.00 8.31  ? 663 HOH B O   1 
HETATM 8495 O O   . HOH D 2 .   ? 50.720  -18.243 55.863  1.00 40.48 ? 664 HOH B O   1 
HETATM 8496 O O   . HOH D 2 .   ? 22.199  -30.839 50.110  1.00 32.43 ? 665 HOH B O   1 
HETATM 8497 O O   . HOH D 2 .   ? 24.303  -2.457  49.413  1.00 31.64 ? 666 HOH B O   1 
HETATM 8498 O O   . HOH D 2 .   ? 27.521  -30.974 80.715  1.00 30.41 ? 667 HOH B O   1 
HETATM 8499 O O   . HOH D 2 .   ? 31.819  -7.579  52.497  1.00 27.64 ? 668 HOH B O   1 
HETATM 8500 O O   . HOH D 2 .   ? 53.285  -9.388  66.784  1.00 48.28 ? 669 HOH B O   1 
HETATM 8501 O O   . HOH D 2 .   ? 32.831  -9.946  65.356  1.00 36.23 ? 670 HOH B O   1 
HETATM 8502 O O   . HOH D 2 .   ? 19.399  -20.398 43.344  1.00 40.46 ? 671 HOH B O   1 
HETATM 8503 O O   . HOH D 2 .   ? 1.824   -22.089 92.645  1.00 24.72 ? 672 HOH B O   1 
HETATM 8504 O O   . HOH D 2 .   ? 21.052  -9.028  78.461  1.00 31.66 ? 673 HOH B O   1 
HETATM 8505 O O   . HOH D 2 .   ? 50.622  -9.696  60.984  1.00 30.60 ? 674 HOH B O   1 
HETATM 8506 O O   . HOH D 2 .   ? 5.364   -21.531 59.585  1.00 34.26 ? 675 HOH B O   1 
HETATM 8507 O O   . HOH D 2 .   ? 15.249  -37.980 61.433  1.00 39.64 ? 676 HOH B O   1 
HETATM 8508 O O   . HOH D 2 .   ? 47.989  -20.246 89.914  1.00 22.55 ? 677 HOH B O   1 
HETATM 8509 O O   . HOH D 2 .   ? 31.074  -14.195 71.013  1.00 27.98 ? 678 HOH B O   1 
HETATM 8510 O O   . HOH D 2 .   ? 34.001  -9.103  37.015  1.00 39.64 ? 679 HOH B O   1 
HETATM 8511 O O   . HOH D 2 .   ? 50.971  -14.105 51.992  1.00 36.78 ? 680 HOH B O   1 
HETATM 8512 O O   . HOH D 2 .   ? 20.257  -39.727 70.756  1.00 39.06 ? 681 HOH B O   1 
HETATM 8513 O O   . HOH D 2 .   ? 31.308  -41.464 61.703  1.00 30.83 ? 682 HOH B O   1 
HETATM 8514 O O   . HOH D 2 .   ? 27.821  -13.143 66.842  1.00 17.41 ? 683 HOH B O   1 
HETATM 8515 O O   . HOH D 2 .   ? 45.376  -33.550 81.793  1.00 37.81 ? 684 HOH B O   1 
HETATM 8516 O O   . HOH D 2 .   ? 52.480  -24.056 80.241  1.00 16.99 ? 685 HOH B O   1 
HETATM 8517 O O   . HOH D 2 .   ? 45.319  -13.015 64.518  1.00 15.31 ? 686 HOH B O   1 
HETATM 8518 O O   . HOH D 2 .   ? 51.441  -29.141 48.981  1.00 48.17 ? 687 HOH B O   1 
HETATM 8519 O O   . HOH D 2 .   ? 4.584   -11.615 66.675  1.00 25.64 ? 688 HOH B O   1 
HETATM 8520 O O   . HOH D 2 .   ? 25.347  -9.972  89.441  1.00 29.59 ? 689 HOH B O   1 
HETATM 8521 O O   . HOH D 2 .   ? 30.584  -15.221 73.361  1.00 21.32 ? 690 HOH B O   1 
HETATM 8522 O O   . HOH D 2 .   ? 32.760  -12.699 86.676  1.00 45.27 ? 691 HOH B O   1 
HETATM 8523 O O   . HOH D 2 .   ? 35.655  -12.680 91.357  1.00 33.25 ? 692 HOH B O   1 
HETATM 8524 O O   . HOH D 2 .   ? 19.671  -4.017  46.589  1.00 33.88 ? 693 HOH B O   1 
HETATM 8525 O O   . HOH D 2 .   ? 26.075  -32.349 58.872  1.00 14.45 ? 694 HOH B O   1 
HETATM 8526 O O   . HOH D 2 .   ? 32.874  -7.649  65.276  1.00 53.73 ? 695 HOH B O   1 
HETATM 8527 O O   . HOH D 2 .   ? 24.802  -43.092 68.012  1.00 35.92 ? 696 HOH B O   1 
HETATM 8528 O O   . HOH D 2 .   ? -6.067  -14.857 95.811  1.00 40.03 ? 697 HOH B O   1 
HETATM 8529 O O   . HOH D 2 .   ? 45.676  -31.117 80.360  1.00 14.66 ? 698 HOH B O   1 
HETATM 8530 O O   . HOH D 2 .   ? 14.150  -14.888 64.252  1.00 18.00 ? 699 HOH B O   1 
HETATM 8531 O O   . HOH D 2 .   ? 39.831  -10.234 72.204  1.00 16.33 ? 700 HOH B O   1 
HETATM 8532 O O   . HOH D 2 .   ? 21.919  -6.337  64.589  1.00 10.94 ? 701 HOH B O   1 
HETATM 8533 O O   . HOH D 2 .   ? 22.202  -37.667 61.057  1.00 34.19 ? 702 HOH B O   1 
HETATM 8534 O O   . HOH D 2 .   ? 45.513  -33.013 86.979  1.00 41.08 ? 703 HOH B O   1 
HETATM 8535 O O   . HOH D 2 .   ? 32.772  -14.695 85.482  1.00 22.69 ? 704 HOH B O   1 
HETATM 8536 O O   . HOH D 2 .   ? -4.071  -17.838 68.852  1.00 26.70 ? 705 HOH B O   1 
HETATM 8537 O O   . HOH D 2 .   ? 14.665  -12.131 44.797  1.00 32.08 ? 706 HOH B O   1 
HETATM 8538 O O   . HOH D 2 .   ? 56.049  -21.207 78.447  1.00 23.92 ? 707 HOH B O   1 
HETATM 8539 O O   . HOH D 2 .   ? 20.674  -17.059 90.598  1.00 32.33 ? 708 HOH B O   1 
HETATM 8540 O O   . HOH D 2 .   ? 21.227  -7.186  67.148  1.00 11.23 ? 709 HOH B O   1 
HETATM 8541 O O   . HOH D 2 .   ? -4.386  -2.453  93.418  1.00 36.68 ? 710 HOH B O   1 
HETATM 8542 O O   . HOH D 2 .   ? 13.052  -7.815  62.126  1.00 11.85 ? 711 HOH B O   1 
HETATM 8543 O O   . HOH D 2 .   ? 11.928  -24.909 86.914  1.00 28.10 ? 712 HOH B O   1 
HETATM 8544 O O   . HOH D 2 .   ? -0.651  -27.649 72.672  1.00 43.02 ? 713 HOH B O   1 
HETATM 8545 O O   . HOH D 2 .   ? 1.628   -3.128  73.606  1.00 23.02 ? 714 HOH B O   1 
HETATM 8546 O O   . HOH D 2 .   ? 28.497  -1.339  49.986  1.00 44.25 ? 715 HOH B O   1 
HETATM 8547 O O   . HOH D 2 .   ? 51.522  -30.322 83.885  1.00 25.32 ? 716 HOH B O   1 
HETATM 8548 O O   . HOH D 2 .   ? -4.202  -3.737  86.833  1.00 37.44 ? 717 HOH B O   1 
HETATM 8549 O O   . HOH D 2 .   ? 10.940  -30.524 56.443  1.00 39.00 ? 718 HOH B O   1 
HETATM 8550 O O   . HOH D 2 .   ? -5.373  -9.120  91.835  1.00 28.43 ? 719 HOH B O   1 
HETATM 8551 O O   . HOH D 2 .   ? 44.933  -15.704 46.034  1.00 31.21 ? 720 HOH B O   1 
HETATM 8552 O O   . HOH D 2 .   ? 37.231  -28.772 96.696  1.00 39.25 ? 721 HOH B O   1 
HETATM 8553 O O   . HOH D 2 .   ? 11.661  3.417   77.632  1.00 39.40 ? 722 HOH B O   1 
HETATM 8554 O O   . HOH D 2 .   ? 30.255  -5.822  49.098  1.00 33.08 ? 723 HOH B O   1 
HETATM 8555 O O   . HOH D 2 .   ? 11.777  -3.561  60.816  1.00 29.18 ? 724 HOH B O   1 
HETATM 8556 O O   . HOH D 2 .   ? 37.251  -7.172  82.718  1.00 35.68 ? 725 HOH B O   1 
HETATM 8557 O O   . HOH D 2 .   ? 52.524  -31.320 78.221  1.00 40.59 ? 726 HOH B O   1 
HETATM 8558 O O   . HOH D 2 .   ? 4.647   -32.294 75.824  1.00 33.57 ? 727 HOH B O   1 
HETATM 8559 O O   . HOH D 2 .   ? 42.155  -22.541 42.548  1.00 35.59 ? 728 HOH B O   1 
HETATM 8560 O O   . HOH D 2 .   ? 29.899  -32.279 61.081  1.00 23.52 ? 729 HOH B O   1 
HETATM 8561 O O   . HOH D 2 .   ? 51.506  -19.382 53.671  1.00 30.15 ? 730 HOH B O   1 
HETATM 8562 O O   . HOH D 2 .   ? 28.606  -18.307 71.948  1.00 18.56 ? 731 HOH B O   1 
HETATM 8563 O O   . HOH D 2 .   ? 31.065  -29.283 42.406  1.00 39.40 ? 732 HOH B O   1 
HETATM 8564 O O   . HOH D 2 .   ? 30.085  -5.653  51.761  1.00 27.14 ? 733 HOH B O   1 
HETATM 8565 O O   . HOH D 2 .   ? -6.011  -11.870 91.186  1.00 38.54 ? 734 HOH B O   1 
HETATM 8566 O O   . HOH D 2 .   ? 21.053  -29.866 47.445  1.00 40.22 ? 735 HOH B O   1 
HETATM 8567 O O   . HOH D 2 .   ? -4.796  -17.883 97.975  1.00 41.17 ? 736 HOH B O   1 
HETATM 8568 O O   . HOH D 2 .   ? 17.581  -36.451 73.448  1.00 39.29 ? 737 HOH B O   1 
HETATM 8569 O O   . HOH D 2 .   ? 49.536  -13.541 49.869  1.00 27.62 ? 738 HOH B O   1 
HETATM 8570 O O   . HOH D 2 .   ? 37.613  -19.962 93.579  1.00 17.78 ? 739 HOH B O   1 
HETATM 8571 O O   . HOH D 2 .   ? 10.621  -31.563 65.172  1.00 31.16 ? 740 HOH B O   1 
HETATM 8572 O O   . HOH D 2 .   ? 34.731  -37.129 85.230  1.00 36.50 ? 741 HOH B O   1 
HETATM 8573 O O   . HOH D 2 .   ? 51.618  -26.283 76.951  1.00 21.44 ? 742 HOH B O   1 
HETATM 8574 O O   . HOH D 2 .   ? 42.259  -5.012  70.796  1.00 32.21 ? 743 HOH B O   1 
HETATM 8575 O O   . HOH D 2 .   ? -3.177  -27.220 72.310  1.00 42.28 ? 744 HOH B O   1 
HETATM 8576 O O   . HOH D 2 .   ? 50.248  -5.546  73.129  1.00 26.25 ? 745 HOH B O   1 
HETATM 8577 O O   . HOH D 2 .   ? 6.561   -8.419  69.856  1.00 36.33 ? 746 HOH B O   1 
HETATM 8578 O O   . HOH D 2 .   ? 18.423  -17.163 100.849 1.00 36.75 ? 747 HOH B O   1 
HETATM 8579 O O   . HOH D 2 .   ? -5.265  -26.438 72.325  1.00 36.89 ? 748 HOH B O   1 
HETATM 8580 O O   . HOH D 2 .   ? 30.926  -15.580 76.292  1.00 15.70 ? 749 HOH B O   1 
HETATM 8581 O O   . HOH D 2 .   ? 30.089  -4.648  59.512  1.00 38.05 ? 750 HOH B O   1 
HETATM 8582 O O   . HOH D 2 .   ? 34.296  -8.284  66.253  1.00 44.19 ? 751 HOH B O   1 
HETATM 8583 O O   . HOH D 2 .   ? 25.131  -27.974 45.274  1.00 48.50 ? 752 HOH B O   1 
HETATM 8584 O O   . HOH D 2 .   ? 30.440  -24.468 80.414  1.00 11.45 ? 753 HOH B O   1 
HETATM 8585 O O   . HOH D 2 .   ? 20.346  -6.500  92.285  1.00 40.38 ? 754 HOH B O   1 
HETATM 8586 O O   . HOH D 2 .   ? 54.406  -19.187 71.008  1.00 27.31 ? 755 HOH B O   1 
HETATM 8587 O O   . HOH D 2 .   ? 4.908   -30.031 77.401  1.00 26.18 ? 756 HOH B O   1 
HETATM 8588 O O   . HOH D 2 .   ? 21.565  -34.239 79.850  1.00 33.65 ? 757 HOH B O   1 
HETATM 8589 O O   . HOH D 2 .   ? 23.902  -32.716 53.366  1.00 40.29 ? 758 HOH B O   1 
HETATM 8590 O O   . HOH D 2 .   ? 19.951  -23.149 47.169  1.00 36.74 ? 759 HOH B O   1 
HETATM 8591 O O   . HOH D 2 .   ? 45.972  -7.080  67.914  1.00 30.07 ? 760 HOH B O   1 
HETATM 8592 O O   . HOH D 2 .   ? 51.921  -16.386 60.703  1.00 36.60 ? 761 HOH B O   1 
HETATM 8593 O O   . HOH D 2 .   ? 53.295  -22.912 65.619  1.00 43.63 ? 762 HOH B O   1 
HETATM 8594 O O   . HOH D 2 .   ? 31.756  -4.937  64.775  1.00 34.70 ? 763 HOH B O   1 
HETATM 8595 O O   . HOH D 2 .   ? -3.426  -0.168  89.849  1.00 46.93 ? 764 HOH B O   1 
HETATM 8596 O O   . HOH D 2 .   ? 48.229  -31.827 70.931  1.00 42.27 ? 765 HOH B O   1 
HETATM 8597 O O   . HOH D 2 .   ? 53.121  -28.717 78.071  1.00 40.85 ? 766 HOH B O   1 
HETATM 8598 O O   . HOH D 2 .   ? 17.336  -16.394 87.586  1.00 37.30 ? 767 HOH B O   1 
HETATM 8599 O O   . HOH D 2 .   ? 53.123  -22.100 68.263  1.00 35.61 ? 768 HOH B O   1 
HETATM 8600 O O   . HOH D 2 .   ? 40.333  -23.372 94.459  1.00 28.99 ? 769 HOH B O   1 
HETATM 8601 O O   . HOH D 2 .   ? 39.507  -30.324 97.742  1.00 32.63 ? 770 HOH B O   1 
HETATM 8602 O O   . HOH D 2 .   ? 38.157  -23.951 94.932  1.00 23.40 ? 771 HOH B O   1 
HETATM 8603 O O   . HOH D 2 .   ? 52.148  -15.235 59.320  1.00 38.88 ? 772 HOH B O   1 
HETATM 8604 O O   . HOH D 2 .   ? 53.071  -25.574 64.344  1.00 37.33 ? 773 HOH B O   1 
HETATM 8605 O O   . HOH D 2 .   ? 9.713   -10.265 50.801  1.00 44.60 ? 774 HOH B O   1 
HETATM 8606 O O   . HOH D 2 .   ? 43.345  -37.795 60.592  1.00 38.62 ? 775 HOH B O   1 
HETATM 8607 O O   . HOH D 2 .   ? 50.541  -22.079 67.866  1.00 19.32 ? 776 HOH B O   1 
HETATM 8608 O O   . HOH D 2 .   ? 30.087  -2.253  49.298  1.00 44.85 ? 777 HOH B O   1 
HETATM 8609 O O   . HOH D 2 .   ? 20.365  -37.417 61.162  1.00 34.96 ? 778 HOH B O   1 
HETATM 8610 O O   . HOH D 2 .   ? 32.982  -37.242 94.475  1.00 43.30 ? 779 HOH B O   1 
HETATM 8611 O O   . HOH D 2 .   ? 37.251  -37.984 84.825  1.00 34.32 ? 780 HOH B O   1 
HETATM 8612 O O   . HOH D 2 .   ? 20.957  -4.569  76.784  1.00 50.37 ? 781 HOH B O   1 
HETATM 8613 O O   . HOH D 2 .   ? 25.627  -11.601 67.536  1.00 25.09 ? 782 HOH B O   1 
HETATM 8614 O O   . HOH D 2 .   ? 21.227  -21.319 42.188  1.00 41.51 ? 783 HOH B O   1 
HETATM 8615 O O   . HOH D 2 .   ? 12.642  -35.058 73.931  1.00 31.87 ? 784 HOH B O   1 
HETATM 8616 O O   . HOH D 2 .   ? -4.338  -0.797  91.740  1.00 50.31 ? 785 HOH B O   1 
HETATM 8617 O O   . HOH D 2 .   ? -4.274  -17.908 70.829  1.00 39.38 ? 786 HOH B O   1 
HETATM 8618 O O   . HOH D 2 .   ? 13.971  -5.372  61.696  1.00 20.44 ? 787 HOH B O   1 
HETATM 8619 O O   . HOH D 2 .   ? 11.086  -11.237 47.656  1.00 36.62 ? 788 HOH B O   1 
HETATM 8620 O O   . HOH D 2 .   ? 5.856   -29.532 80.576  1.00 35.98 ? 789 HOH B O   1 
HETATM 8621 O O   . HOH D 2 .   ? 29.632  -12.304 68.723  1.00 44.86 ? 790 HOH B O   1 
HETATM 8622 O O   . HOH D 2 .   ? 28.684  -33.706 59.143  1.00 31.45 ? 791 HOH B O   1 
HETATM 8623 O O   . HOH D 2 .   ? -5.205  -8.857  94.270  1.00 41.28 ? 792 HOH B O   1 
HETATM 8624 O O   . HOH D 2 .   ? 49.545  -8.729  63.451  1.00 50.53 ? 793 HOH B O   1 
HETATM 8625 O O   . HOH D 2 .   ? 49.595  -33.730 76.456  1.00 32.53 ? 794 HOH B O   1 
HETATM 8626 O O   . HOH D 2 .   ? 24.323  -15.118 77.234  1.00 36.31 ? 795 HOH B O   1 
HETATM 8627 O O   . HOH D 2 .   ? 30.713  -11.646 66.263  1.00 33.66 ? 796 HOH B O   1 
HETATM 8628 O O   . HOH D 2 .   ? 53.219  -21.871 78.664  1.00 18.46 ? 797 HOH B O   1 
HETATM 8629 O O   . HOH D 2 .   ? 45.329  -39.064 60.187  1.00 48.10 ? 798 HOH B O   1 
HETATM 8630 O O   . HOH D 2 .   ? 40.808  -39.474 90.722  1.00 46.05 ? 799 HOH B O   1 
HETATM 8631 O O   . HOH D 2 .   ? 44.253  -5.689  78.551  1.00 41.72 ? 800 HOH B O   1 
HETATM 8632 O O   . HOH D 2 .   ? 52.920  -14.302 54.026  1.00 38.50 ? 801 HOH B O   1 
HETATM 8633 O O   . HOH D 2 .   ? 47.309  -35.355 74.597  1.00 55.89 ? 802 HOH B O   1 
HETATM 8634 O O   . HOH D 2 .   ? 5.690   -20.865 61.573  1.00 37.56 ? 803 HOH B O   1 
HETATM 8635 O O   . HOH D 2 .   ? 53.112  -24.875 76.579  1.00 38.17 ? 804 HOH B O   1 
HETATM 8636 O O   . HOH D 2 .   ? 47.807  -19.763 92.745  1.00 51.80 ? 805 HOH B O   1 
HETATM 8637 O O   . HOH D 2 .   ? 21.083  -36.456 80.506  1.00 45.68 ? 806 HOH B O   1 
HETATM 8638 O O   . HOH D 2 .   ? 34.261  -44.193 62.120  1.00 56.79 ? 807 HOH B O   1 
HETATM 8639 O O   . HOH D 2 .   ? 34.581  -6.845  53.036  1.00 43.32 ? 808 HOH B O   1 
HETATM 8640 O O   . HOH D 2 .   ? 37.164  -20.184 37.766  1.00 50.86 ? 809 HOH B O   1 
HETATM 8641 O O   . HOH D 2 .   ? 4.753   -11.241 97.457  1.00 50.90 ? 810 HOH B O   1 
HETATM 8642 O O   . HOH D 2 .   ? 23.765  -11.214 90.248  1.00 37.59 ? 811 HOH B O   1 
HETATM 8643 O O   . HOH D 2 .   ? 34.727  -5.162  58.774  1.00 40.13 ? 812 HOH B O   1 
HETATM 8644 O O   . HOH D 2 .   ? 4.552   -26.409 67.902  1.00 42.21 ? 813 HOH B O   1 
HETATM 8645 O O   . HOH D 2 .   ? 49.123  -4.743  81.307  1.00 34.06 ? 814 HOH B O   1 
HETATM 8646 O O   . HOH D 2 .   ? 25.731  -10.942 70.059  1.00 51.20 ? 815 HOH B O   1 
HETATM 8647 O O   . HOH D 2 .   ? 55.006  -28.211 73.456  1.00 48.98 ? 816 HOH B O   1 
HETATM 8648 O O   . HOH D 2 .   ? 11.583  -1.686  62.201  1.00 41.72 ? 817 HOH B O   1 
HETATM 8649 O O   . HOH D 2 .   ? 48.957  -33.675 73.609  1.00 43.99 ? 818 HOH B O   1 
HETATM 8650 O O   . HOH D 2 .   ? 44.654  -5.556  64.449  1.00 39.93 ? 819 HOH B O   1 
HETATM 8651 O O   . HOH D 2 .   ? 18.738  -3.011  76.095  1.00 31.60 ? 820 HOH B O   1 
HETATM 8652 O O   . HOH D 2 .   ? 50.599  -31.882 84.461  1.00 40.16 ? 821 HOH B O   1 
HETATM 8653 O O   . HOH D 2 .   ? 0.083   -5.007  74.212  1.00 50.97 ? 822 HOH B O   1 
HETATM 8654 O O   . HOH D 2 .   ? 54.271  -31.016 79.937  1.00 42.29 ? 823 HOH B O   1 
HETATM 8655 O O   . HOH D 2 .   ? 39.911  -5.873  74.108  1.00 44.48 ? 824 HOH B O   1 
HETATM 8656 O O   . HOH D 2 .   ? 42.749  -35.748 84.565  1.00 45.81 ? 825 HOH B O   1 
HETATM 8657 O O   . HOH D 2 .   ? 14.753  -17.797 93.765  1.00 31.06 ? 826 HOH B O   1 
HETATM 8658 O O   . HOH D 2 .   ? 17.406  -14.509 87.808  1.00 37.54 ? 827 HOH B O   1 
HETATM 8659 O O   . HOH D 2 .   ? 5.919   -12.801 64.283  1.00 41.25 ? 828 HOH B O   1 
HETATM 8660 O O   . HOH D 2 .   ? 15.577  -34.247 73.629  1.00 25.70 ? 829 HOH B O   1 
HETATM 8661 O O   . HOH D 2 .   ? -7.050  -12.634 94.294  1.00 47.10 ? 830 HOH B O   1 
HETATM 8662 O O   . HOH D 2 .   ? 42.545  -39.075 90.243  1.00 44.38 ? 831 HOH B O   1 
HETATM 8663 O O   . HOH D 2 .   ? 36.759  -39.150 48.910  1.00 36.29 ? 832 HOH B O   1 
HETATM 8664 O O   . HOH D 2 .   ? 36.072  -5.593  52.776  1.00 43.38 ? 833 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . MET A 1   ? 0.7092 0.7593 0.6772 0.0318  -0.0087 -0.0234 1   MET A N   
2    C CA  . MET A 1   ? 0.6850 0.7354 0.6542 0.0320  -0.0087 -0.0236 1   MET A CA  
3    C C   . MET A 1   ? 0.6533 0.6997 0.6209 0.0319  -0.0089 -0.0239 1   MET A C   
4    O O   . MET A 1   ? 0.6750 0.7180 0.6400 0.0328  -0.0092 -0.0238 1   MET A O   
5    C CB  . MET A 1   ? 0.7212 0.7726 0.6905 0.0339  -0.0088 -0.0234 1   MET A CB  
6    C CG  . MET A 1   ? 0.7514 0.8026 0.7216 0.0342  -0.0089 -0.0235 1   MET A CG  
7    S SD  . MET A 1   ? 0.8065 0.8583 0.7763 0.0366  -0.0091 -0.0232 1   MET A SD  
8    C CE  . MET A 1   ? 0.8056 0.8620 0.7773 0.0365  -0.0088 -0.0229 1   MET A CE  
9    N N   . LYS A 2   ? 0.5200 0.5670 0.4892 0.0308  -0.0088 -0.0242 2   LYS A N   
10   C CA  . LYS A 2   ? 0.4128 0.4565 0.3809 0.0305  -0.0090 -0.0244 2   LYS A CA  
11   C C   . LYS A 2   ? 0.2965 0.3393 0.2643 0.0319  -0.0092 -0.0244 2   LYS A C   
12   O O   . LYS A 2   ? 0.3690 0.4146 0.3389 0.0320  -0.0091 -0.0244 2   LYS A O   
13   C CB  . LYS A 2   ? 0.5528 0.5977 0.5228 0.0285  -0.0087 -0.0247 2   LYS A CB  
14   C CG  . LYS A 2   ? 0.6217 0.6641 0.5912 0.0280  -0.0089 -0.0249 2   LYS A CG  
15   C CD  . LYS A 2   ? 0.7378 0.7774 0.7056 0.0270  -0.0089 -0.0250 2   LYS A CD  
16   C CE  . LYS A 2   ? 0.7178 0.7594 0.6870 0.0252  -0.0086 -0.0251 2   LYS A CE  
17   N NZ  . LYS A 2   ? 0.6974 0.7361 0.6650 0.0242  -0.0087 -0.0252 2   LYS A NZ  
18   N N   . LYS A 3   ? 0.2030 0.2422 0.1684 0.0329  -0.0095 -0.0243 3   LYS A N   
19   C CA  . LYS A 3   ? 0.2291 0.2674 0.1940 0.0345  -0.0097 -0.0242 3   LYS A CA  
20   C C   . LYS A 3   ? 0.2487 0.2849 0.2134 0.0340  -0.0098 -0.0245 3   LYS A C   
21   O O   . LYS A 3   ? 0.2748 0.3095 0.2391 0.0327  -0.0098 -0.0247 3   LYS A O   
22   C CB  . LYS A 3   ? 0.3384 0.3741 0.3006 0.0363  -0.0100 -0.0239 3   LYS A CB  
23   C CG  . LYS A 3   ? 0.4532 0.4912 0.4156 0.0370  -0.0098 -0.0236 3   LYS A CG  
24   C CD  . LYS A 3   ? 0.5022 0.5376 0.4620 0.0387  -0.0100 -0.0233 3   LYS A CD  
25   C CE  . LYS A 3   ? 0.5359 0.5738 0.4961 0.0394  -0.0099 -0.0230 3   LYS A CE  
26   N NZ  . LYS A 3   ? 0.4544 0.4964 0.4172 0.0391  -0.0097 -0.0230 3   LYS A NZ  
27   N N   . LEU A 4   ? 0.1739 0.2103 0.1389 0.0350  -0.0099 -0.0244 4   LEU A N   
28   C CA  . LEU A 4   ? 0.1368 0.1708 0.1012 0.0350  -0.0101 -0.0245 4   LEU A CA  
29   C C   . LEU A 4   ? 0.1934 0.2243 0.1551 0.0368  -0.0104 -0.0243 4   LEU A C   
30   O O   . LEU A 4   ? 0.2083 0.2397 0.1696 0.0383  -0.0105 -0.0240 4   LEU A O   
31   C CB  . LEU A 4   ? 0.1541 0.1905 0.1207 0.0348  -0.0100 -0.0246 4   LEU A CB  
32   C CG  . LEU A 4   ? 0.2164 0.2509 0.1827 0.0349  -0.0102 -0.0248 4   LEU A CG  
33   C CD1 . LEU A 4   ? 0.2525 0.2895 0.2213 0.0336  -0.0100 -0.0250 4   LEU A CD1 
34   C CD2 . LEU A 4   ? 0.1461 0.1791 0.1109 0.0368  -0.0105 -0.0245 4   LEU A CD2 
35   N N   . PHE A 5   ? 0.1766 0.2042 0.1366 0.0367  -0.0106 -0.0244 5   PHE A N   
36   C CA  . PHE A 5   ? 0.1630 0.1873 0.1204 0.0383  -0.0109 -0.0242 5   PHE A CA  
37   C C   . PHE A 5   ? 0.2046 0.2280 0.1620 0.0388  -0.0111 -0.0242 5   PHE A C   
38   O O   . PHE A 5   ? 0.2463 0.2692 0.2044 0.0377  -0.0110 -0.0245 5   PHE A O   
39   C CB  . PHE A 5   ? 0.1779 0.1991 0.1333 0.0379  -0.0110 -0.0243 5   PHE A CB  
40   C CG  . PHE A 5   ? 0.1610 0.1828 0.1161 0.0375  -0.0109 -0.0242 5   PHE A CG  
41   C CD1 . PHE A 5   ? 0.2327 0.2552 0.1871 0.0389  -0.0109 -0.0239 5   PHE A CD1 
42   C CD2 . PHE A 5   ? 0.2077 0.2295 0.1632 0.0358  -0.0108 -0.0245 5   PHE A CD2 
43   C CE1 . PHE A 5   ? 0.2482 0.2715 0.2024 0.0385  -0.0108 -0.0238 5   PHE A CE1 
44   C CE2 . PHE A 5   ? 0.2221 0.2446 0.1773 0.0353  -0.0107 -0.0244 5   PHE A CE2 
45   C CZ  . PHE A 5   ? 0.2647 0.2879 0.2192 0.0367  -0.0107 -0.0241 5   PHE A CZ  
46   N N   . LEU A 6   ? 0.1671 0.1901 0.1237 0.0405  -0.0112 -0.0240 6   LEU A N   
47   C CA  . LEU A 6   ? 0.1949 0.2174 0.1516 0.0411  -0.0114 -0.0239 6   LEU A CA  
48   C C   . LEU A 6   ? 0.1633 0.1822 0.1173 0.0426  -0.0117 -0.0237 6   LEU A C   
49   O O   . LEU A 6   ? 0.1662 0.1843 0.1187 0.0439  -0.0117 -0.0234 6   LEU A O   
50   C CB  . LEU A 6   ? 0.1518 0.1773 0.1101 0.0418  -0.0113 -0.0238 6   LEU A CB  
51   C CG  . LEU A 6   ? 0.1346 0.1601 0.0933 0.0424  -0.0114 -0.0238 6   LEU A CG  
52   C CD1 . LEU A 6   ? 0.1633 0.1890 0.1234 0.0409  -0.0114 -0.0241 6   LEU A CD1 
53   C CD2 . LEU A 6   ? 0.1864 0.2149 0.1465 0.0430  -0.0113 -0.0236 6   LEU A CD2 
54   N N   . VAL A 7   ? 0.1597 0.1764 0.1129 0.0424  -0.0118 -0.0238 7   VAL A N   
55   C CA  . VAL A 7   ? 0.1340 0.1471 0.0846 0.0437  -0.0121 -0.0237 7   VAL A CA  
56   C C   . VAL A 7   ? 0.1912 0.2037 0.1417 0.0443  -0.0122 -0.0236 7   VAL A C   
57   O O   . VAL A 7   ? 0.1965 0.2088 0.1478 0.0432  -0.0122 -0.0239 7   VAL A O   
58   C CB  . VAL A 7   ? 0.1757 0.1863 0.1251 0.0428  -0.0122 -0.0239 7   VAL A CB  
59   C CG1 . VAL A 7   ? 0.1625 0.1694 0.1090 0.0441  -0.0124 -0.0236 7   VAL A CG1 
60   C CG2 . VAL A 7   ? 0.1806 0.1922 0.1304 0.0418  -0.0120 -0.0240 7   VAL A CG2 
61   N N   . PHE A 8   ? 0.1757 0.1879 0.1253 0.0459  -0.0123 -0.0233 8   PHE A N   
62   C CA  . PHE A 8   ? 0.1316 0.1428 0.0806 0.0467  -0.0125 -0.0232 8   PHE A CA  
63   C C   . PHE A 8   ? 0.1717 0.1790 0.1181 0.0475  -0.0127 -0.0231 8   PHE A C   
64   O O   . PHE A 8   ? 0.1821 0.1877 0.1266 0.0484  -0.0128 -0.0229 8   PHE A O   
65   C CB  . PHE A 8   ? 0.1316 0.1443 0.0808 0.0481  -0.0125 -0.0229 8   PHE A CB  
66   C CG  . PHE A 8   ? 0.1653 0.1818 0.1172 0.0474  -0.0123 -0.0230 8   PHE A CG  
67   C CD1 . PHE A 8   ? 0.1755 0.1932 0.1287 0.0469  -0.0123 -0.0231 8   PHE A CD1 
68   C CD2 . PHE A 8   ? 0.1683 0.1872 0.1213 0.0473  -0.0121 -0.0229 8   PHE A CD2 
69   C CE1 . PHE A 8   ? 0.2488 0.2701 0.2046 0.0463  -0.0121 -0.0232 8   PHE A CE1 
70   C CE2 . PHE A 8   ? 0.1689 0.1913 0.1243 0.0466  -0.0119 -0.0230 8   PHE A CE2 
71   C CZ  . PHE A 8   ? 0.2844 0.3081 0.2412 0.0461  -0.0119 -0.0232 8   PHE A CZ  
72   N N   . TRP A 9   ? 0.1652 0.1712 0.1114 0.0471  -0.0128 -0.0232 9   TRP A N   
73   C CA  . TRP A 9   ? 0.1832 0.1856 0.1269 0.0478  -0.0131 -0.0231 9   TRP A CA  
74   C C   . TRP A 9   ? 0.1591 0.1611 0.1027 0.0483  -0.0132 -0.0231 9   TRP A C   
75   O O   . TRP A 9   ? 0.1764 0.1789 0.1212 0.0472  -0.0132 -0.0233 9   TRP A O   
76   C CB  . TRP A 9   ? 0.1802 0.1811 0.1237 0.0464  -0.0131 -0.0234 9   TRP A CB  
77   C CG  . TRP A 9   ? 0.1789 0.1761 0.1198 0.0471  -0.0133 -0.0233 9   TRP A CG  
78   C CD1 . TRP A 9   ? 0.1884 0.1834 0.1272 0.0487  -0.0135 -0.0230 9   TRP A CD1 
79   C CD2 . TRP A 9   ? 0.1617 0.1570 0.1018 0.0461  -0.0134 -0.0235 9   TRP A CD2 
80   N NE1 . TRP A 9   ? 0.1549 0.1468 0.0917 0.0487  -0.0136 -0.0230 9   TRP A NE1 
81   C CE2 . TRP A 9   ? 0.2025 0.1945 0.1401 0.0471  -0.0136 -0.0234 9   TRP A CE2 
82   C CE3 . TRP A 9   ? 0.1305 0.1267 0.0720 0.0443  -0.0132 -0.0239 9   TRP A CE3 
83   C CZ2 . TRP A 9   ? 0.1784 0.1680 0.1147 0.0466  -0.0137 -0.0235 9   TRP A CZ2 
84   C CZ3 . TRP A 9   ? 0.1461 0.1399 0.0862 0.0438  -0.0134 -0.0240 9   TRP A CZ3 
85   C CH2 . TRP A 9   ? 0.1878 0.1783 0.1254 0.0449  -0.0136 -0.0238 9   TRP A CH2 
86   N N   . TRP A 10  ? 0.1067 0.1078 0.0489 0.0499  -0.0133 -0.0227 10  TRP A N   
87   C CA  . TRP A 10  ? 0.1120 0.1128 0.0540 0.0506  -0.0134 -0.0226 10  TRP A CA  
88   C C   . TRP A 10  ? 0.1430 0.1403 0.0827 0.0511  -0.0136 -0.0226 10  TRP A C   
89   O O   . TRP A 10  ? 0.1564 0.1514 0.0939 0.0521  -0.0136 -0.0223 10  TRP A O   
90   C CB  . TRP A 10  ? 0.1077 0.1096 0.0494 0.0521  -0.0133 -0.0223 10  TRP A CB  
91   C CG  . TRP A 10  ? 0.1399 0.1454 0.0838 0.0518  -0.0131 -0.0223 10  TRP A CG  
92   C CD1 . TRP A 10  ? 0.1232 0.1298 0.0671 0.0524  -0.0130 -0.0221 10  TRP A CD1 
93   C CD2 . TRP A 10  ? 0.1369 0.1454 0.0834 0.0509  -0.0130 -0.0225 10  TRP A CD2 
94   N NE1 . TRP A 10  ? 0.1510 0.1611 0.0973 0.0519  -0.0129 -0.0222 10  TRP A NE1 
95   C CE2 . TRP A 10  ? 0.1433 0.1546 0.0911 0.0509  -0.0129 -0.0224 10  TRP A CE2 
96   C CE3 . TRP A 10  ? 0.2016 0.2106 0.1491 0.0501  -0.0130 -0.0227 10  TRP A CE3 
97   C CZ2 . TRP A 10  ? 0.1515 0.1662 0.1019 0.0502  -0.0127 -0.0225 10  TRP A CZ2 
98   C CZ3 . TRP A 10  ? 0.2443 0.2566 0.1943 0.0493  -0.0129 -0.0228 10  TRP A CZ3 
99   C CH2 . TRP A 10  ? 0.1730 0.1881 0.1245 0.0493  -0.0127 -0.0228 10  TRP A CH2 
100  N N   . HIS A 11  ? 0.1246 0.1215 0.0647 0.0503  -0.0136 -0.0228 11  HIS A N   
101  C CA  . HIS A 11  ? 0.1877 0.1814 0.1259 0.0505  -0.0138 -0.0228 11  HIS A CA  
102  C C   . HIS A 11  ? 0.1440 0.1365 0.0809 0.0518  -0.0139 -0.0225 11  HIS A C   
103  O O   . HIS A 11  ? 0.1943 0.1885 0.1325 0.0516  -0.0138 -0.0226 11  HIS A O   
104  C CB  . HIS A 11  ? 0.1721 0.1658 0.1114 0.0489  -0.0138 -0.0231 11  HIS A CB  
105  C CG  . HIS A 11  ? 0.2106 0.2016 0.1483 0.0491  -0.0139 -0.0232 11  HIS A CG  
106  N ND1 . HIS A 11  ? 0.1853 0.1732 0.1206 0.0497  -0.0141 -0.0231 11  HIS A ND1 
107  C CD2 . HIS A 11  ? 0.2251 0.2160 0.1632 0.0488  -0.0140 -0.0233 11  HIS A CD2 
108  C CE1 . HIS A 11  ? 0.1912 0.1774 0.1256 0.0497  -0.0142 -0.0231 11  HIS A CE1 
109  N NE2 . HIS A 11  ? 0.1883 0.1761 0.1243 0.0491  -0.0142 -0.0232 11  HIS A NE2 
110  N N   . MET A 12  ? 0.1401 0.1299 0.0745 0.0530  -0.0140 -0.0223 12  MET A N   
111  C CA  . MET A 12  ? 0.1462 0.1347 0.0791 0.0543  -0.0140 -0.0220 12  MET A CA  
112  C C   . MET A 12  ? 0.1809 0.1665 0.1121 0.0543  -0.0142 -0.0221 12  MET A C   
113  O O   . MET A 12  ? 0.1596 0.1429 0.0892 0.0543  -0.0143 -0.0221 12  MET A O   
114  C CB  . MET A 12  ? 0.1402 0.1281 0.0716 0.0559  -0.0140 -0.0216 12  MET A CB  
115  C CG  . MET A 12  ? 0.2053 0.1960 0.1381 0.0560  -0.0139 -0.0215 12  MET A CG  
116  S SD  . MET A 12  ? 0.1753 0.1696 0.1109 0.0556  -0.0138 -0.0216 12  MET A SD  
117  C CE  . MET A 12  ? 0.1809 0.1776 0.1172 0.0563  -0.0136 -0.0214 12  MET A CE  
118  N N   . HIS A 13  ? 0.1914 0.1767 0.1226 0.0542  -0.0142 -0.0221 13  HIS A N   
119  C CA  . HIS A 13  ? 0.2088 0.1915 0.1385 0.0541  -0.0144 -0.0222 13  HIS A CA  
120  C C   . HIS A 13  ? 0.2454 0.2278 0.1748 0.0547  -0.0144 -0.0221 13  HIS A C   
121  O O   . HIS A 13  ? 0.1674 0.1521 0.0985 0.0544  -0.0143 -0.0222 13  HIS A O   
122  C CB  . HIS A 13  ? 0.1219 0.1047 0.0528 0.0525  -0.0144 -0.0226 13  HIS A CB  
123  C CG  . HIS A 13  ? 0.1869 0.1674 0.1166 0.0523  -0.0145 -0.0227 13  HIS A CG  
124  N ND1 . HIS A 13  ? 0.1769 0.1543 0.1041 0.0529  -0.0147 -0.0226 13  HIS A ND1 
125  C CD2 . HIS A 13  ? 0.2204 0.2011 0.1509 0.0515  -0.0146 -0.0229 13  HIS A CD2 
126  C CE1 . HIS A 13  ? 0.1855 0.1614 0.1120 0.0525  -0.0147 -0.0227 13  HIS A CE1 
127  N NE2 . HIS A 13  ? 0.1731 0.1509 0.1016 0.0517  -0.0147 -0.0229 13  HIS A NE2 
128  N N   . GLN A 14  ? 0.1785 0.1581 0.1055 0.0554  -0.0145 -0.0220 14  GLN A N   
129  C CA  . GLN A 14  ? 0.1723 0.1512 0.0989 0.0556  -0.0145 -0.0220 14  GLN A CA  
130  C C   . GLN A 14  ? 0.1505 0.1264 0.0753 0.0554  -0.0146 -0.0222 14  GLN A C   
131  O O   . GLN A 14  ? 0.2360 0.2097 0.1589 0.0560  -0.0147 -0.0221 14  GLN A O   
132  C CB  . GLN A 14  ? 0.1747 0.1533 0.1000 0.0571  -0.0144 -0.0217 14  GLN A CB  
133  C CG  . GLN A 14  ? 0.2200 0.2014 0.1470 0.0575  -0.0143 -0.0216 14  GLN A CG  
134  C CD  . GLN A 14  ? 0.2243 0.2083 0.1537 0.0565  -0.0142 -0.0218 14  GLN A CD  
135  O OE1 . GLN A 14  ? 0.2399 0.2232 0.1694 0.0559  -0.0143 -0.0220 14  GLN A OE1 
136  N NE2 . GLN A 14  ? 0.1961 0.1828 0.1272 0.0564  -0.0141 -0.0218 14  GLN A NE2 
137  N N   . PRO A 15  ? 0.1682 0.1440 0.0935 0.0547  -0.0147 -0.0224 15  PRO A N   
138  C CA  . PRO A 15  ? 0.1858 0.1588 0.1093 0.0546  -0.0148 -0.0225 15  PRO A CA  
139  C C   . PRO A 15  ? 0.2202 0.1911 0.1413 0.0560  -0.0148 -0.0222 15  PRO A C   
140  O O   . PRO A 15  ? 0.2428 0.2145 0.1638 0.0570  -0.0147 -0.0220 15  PRO A O   
141  C CB  . PRO A 15  ? 0.2676 0.2415 0.1926 0.0535  -0.0148 -0.0227 15  PRO A CB  
142  C CG  . PRO A 15  ? 0.1632 0.1398 0.0899 0.0537  -0.0147 -0.0227 15  PRO A CG  
143  C CD  . PRO A 15  ? 0.1257 0.1039 0.0532 0.0539  -0.0146 -0.0225 15  PRO A CD  
144  N N   . LEU A 16  ? 0.2349 0.2030 0.1540 0.0562  -0.0149 -0.0223 16  LEU A N   
145  C CA  . LEU A 16  ? 0.2566 0.2225 0.1733 0.0575  -0.0148 -0.0220 16  LEU A CA  
146  C C   . LEU A 16  ? 0.2604 0.2265 0.1771 0.0578  -0.0147 -0.0220 16  LEU A C   
147  O O   . LEU A 16  ? 0.2706 0.2361 0.1873 0.0572  -0.0148 -0.0222 16  LEU A O   
148  C CB  . LEU A 16  ? 0.2182 0.1810 0.1327 0.0575  -0.0149 -0.0221 16  LEU A CB  
149  C CG  . LEU A 16  ? 0.2855 0.2458 0.1973 0.0589  -0.0148 -0.0218 16  LEU A CG  
150  C CD1 . LEU A 16  ? 0.2522 0.2130 0.1634 0.0601  -0.0146 -0.0215 16  LEU A CD1 
151  C CD2 . LEU A 16  ? 0.3205 0.2779 0.2303 0.0588  -0.0149 -0.0219 16  LEU A CD2 
152  N N   . TYR A 17  ? 0.2630 0.2300 0.1795 0.0588  -0.0146 -0.0218 17  TYR A N   
153  C CA  . TYR A 17  ? 0.2270 0.1943 0.1436 0.0592  -0.0145 -0.0217 17  TYR A CA  
154  C C   . TYR A 17  ? 0.2649 0.2295 0.1788 0.0602  -0.0145 -0.0216 17  TYR A C   
155  O O   . TYR A 17  ? 0.2282 0.1927 0.1418 0.0605  -0.0144 -0.0216 17  TYR A O   
156  C CB  . TYR A 17  ? 0.2272 0.1969 0.1450 0.0597  -0.0144 -0.0215 17  TYR A CB  
157  C CG  . TYR A 17  ? 0.2479 0.2207 0.1685 0.0587  -0.0144 -0.0217 17  TYR A CG  
158  C CD1 . TYR A 17  ? 0.2657 0.2397 0.1880 0.0576  -0.0145 -0.0219 17  TYR A CD1 
159  C CD2 . TYR A 17  ? 0.3009 0.2752 0.2224 0.0589  -0.0144 -0.0216 17  TYR A CD2 
160  C CE1 . TYR A 17  ? 0.2517 0.2285 0.1766 0.0566  -0.0145 -0.0221 17  TYR A CE1 
161  C CE2 . TYR A 17  ? 0.2050 0.1821 0.1291 0.0579  -0.0144 -0.0217 17  TYR A CE2 
162  C CZ  . TYR A 17  ? 0.2082 0.1865 0.1339 0.0567  -0.0144 -0.0220 17  TYR A CZ  
163  O OH  . TYR A 17  ? 0.2468 0.2279 0.1751 0.0557  -0.0144 -0.0221 17  TYR A OH  
164  N N   . ARG A 18  ? 0.2761 0.2383 0.1880 0.0606  -0.0145 -0.0216 18  ARG A N   
165  C CA  . ARG A 18  ? 0.2715 0.2310 0.1807 0.0616  -0.0143 -0.0214 18  ARG A CA  
166  C C   . ARG A 18  ? 0.3071 0.2648 0.2156 0.0610  -0.0144 -0.0217 18  ARG A C   
167  O O   . ARG A 18  ? 0.3106 0.2671 0.2187 0.0604  -0.0146 -0.0219 18  ARG A O   
168  C CB  . ARG A 18  ? 0.2440 0.2020 0.1516 0.0623  -0.0143 -0.0212 18  ARG A CB  
169  C CG  . ARG A 18  ? 0.3665 0.3219 0.2714 0.0636  -0.0141 -0.0210 18  ARG A CG  
170  C CD  . ARG A 18  ? 0.3202 0.2740 0.2235 0.0641  -0.0140 -0.0209 18  ARG A CD  
171  N NE  . ARG A 18  ? 0.3865 0.3377 0.2871 0.0653  -0.0138 -0.0207 18  ARG A NE  
172  C CZ  . ARG A 18  ? 0.4122 0.3610 0.3111 0.0653  -0.0138 -0.0209 18  ARG A CZ  
173  N NH1 . ARG A 18  ? 0.3505 0.2989 0.2500 0.0641  -0.0140 -0.0212 18  ARG A NH1 
174  N NH2 . ARG A 18  ? 0.5593 0.5059 0.4558 0.0663  -0.0135 -0.0207 18  ARG A NH2 
175  N N   . GLU A 19  ? 0.3387 0.2961 0.2468 0.0613  -0.0144 -0.0217 19  GLU A N   
176  C CA  . GLU A 19  ? 0.3419 0.2976 0.2490 0.0608  -0.0144 -0.0220 19  GLU A CA  
177  C C   . GLU A 19  ? 0.3032 0.2559 0.2078 0.0613  -0.0144 -0.0220 19  GLU A C   
178  O O   . GLU A 19  ? 0.2853 0.2368 0.1881 0.0625  -0.0142 -0.0217 19  GLU A O   
179  C CB  . GLU A 19  ? 0.3006 0.2565 0.2077 0.0611  -0.0143 -0.0220 19  GLU A CB  
180  C CG  . GLU A 19  ? 0.3922 0.3479 0.2998 0.0601  -0.0145 -0.0223 19  GLU A CG  
181  C CD  . GLU A 19  ? 0.4071 0.3600 0.3124 0.0604  -0.0144 -0.0224 19  GLU A CD  
182  O OE1 . GLU A 19  ? 0.4545 0.4055 0.3577 0.0613  -0.0143 -0.0223 19  GLU A OE1 
183  O OE2 . GLU A 19  ? 0.4992 0.4517 0.4047 0.0597  -0.0145 -0.0227 19  GLU A OE2 
184  N N   . PRO A 20  ? 0.3359 0.2871 0.2400 0.0605  -0.0145 -0.0222 20  PRO A N   
185  C CA  . PRO A 20  ? 0.3694 0.3179 0.2712 0.0610  -0.0145 -0.0222 20  PRO A CA  
186  C C   . PRO A 20  ? 0.4825 0.4286 0.3819 0.0618  -0.0143 -0.0222 20  PRO A C   
187  O O   . PRO A 20  ? 0.4545 0.3985 0.3518 0.0625  -0.0142 -0.0221 20  PRO A O   
188  C CB  . PRO A 20  ? 0.3144 0.2625 0.2168 0.0597  -0.0147 -0.0225 20  PRO A CB  
189  C CG  . PRO A 20  ? 0.3800 0.3300 0.2845 0.0587  -0.0149 -0.0227 20  PRO A CG  
190  C CD  . PRO A 20  ? 0.3100 0.2624 0.2159 0.0592  -0.0148 -0.0225 20  PRO A CD  
191  N N   . TYR A 21  ? 0.4505 0.3968 0.3500 0.0617  -0.0143 -0.0223 21  TYR A N   
192  C CA  . TYR A 21  ? 0.4329 0.3770 0.3302 0.0625  -0.0141 -0.0223 21  TYR A CA  
193  C C   . TYR A 21  ? 0.4114 0.3557 0.3079 0.0637  -0.0138 -0.0220 21  TYR A C   
194  O O   . TYR A 21  ? 0.5101 0.4524 0.4044 0.0647  -0.0135 -0.0220 21  TYR A O   
195  C CB  . TYR A 21  ? 0.4399 0.3839 0.3376 0.0618  -0.0141 -0.0226 21  TYR A CB  
196  C CG  . TYR A 21  ? 0.4824 0.4259 0.3805 0.0607  -0.0144 -0.0229 21  TYR A CG  
197  C CD1 . TYR A 21  ? 0.4109 0.3518 0.3071 0.0606  -0.0144 -0.0231 21  TYR A CD1 
198  C CD2 . TYR A 21  ? 0.5453 0.4909 0.4458 0.0596  -0.0146 -0.0230 21  TYR A CD2 
199  C CE1 . TYR A 21  ? 0.4563 0.3968 0.3529 0.0596  -0.0146 -0.0233 21  TYR A CE1 
200  C CE2 . TYR A 21  ? 0.5494 0.4946 0.4504 0.0585  -0.0148 -0.0233 21  TYR A CE2 
201  C CZ  . TYR A 21  ? 0.5779 0.5205 0.4769 0.0585  -0.0148 -0.0234 21  TYR A CZ  
202  O OH  . TYR A 21  ? 0.5633 0.5054 0.4627 0.0574  -0.0150 -0.0237 21  TYR A OH  
203  N N   . THR A 22  ? 0.3357 0.2825 0.2340 0.0638  -0.0138 -0.0219 22  THR A N   
204  C CA  . THR A 22  ? 0.3533 0.3005 0.2511 0.0649  -0.0135 -0.0216 22  THR A CA  
205  C C   . THR A 22  ? 0.4169 0.3648 0.3147 0.0656  -0.0134 -0.0213 22  THR A C   
206  O O   . THR A 22  ? 0.4004 0.3481 0.2972 0.0667  -0.0131 -0.0211 22  THR A O   
207  C CB  . THR A 22  ? 0.4372 0.3868 0.3368 0.0647  -0.0135 -0.0216 22  THR A CB  
208  O OG1 . THR A 22  ? 0.4257 0.3778 0.3278 0.0639  -0.0137 -0.0216 22  THR A OG1 
209  C CG2 . THR A 22  ? 0.4062 0.3552 0.3058 0.0641  -0.0136 -0.0219 22  THR A CG2 
210  N N   . GLY A 23  ? 0.3759 0.3246 0.2748 0.0649  -0.0136 -0.0214 23  GLY A N   
211  C CA  . GLY A 23  ? 0.3124 0.2621 0.2117 0.0654  -0.0136 -0.0211 23  GLY A CA  
212  C C   . GLY A 23  ? 0.3422 0.2947 0.2434 0.0656  -0.0136 -0.0209 23  GLY A C   
213  O O   . GLY A 23  ? 0.4749 0.4284 0.3765 0.0661  -0.0135 -0.0207 23  GLY A O   
214  N N   . GLU A 24  ? 0.2751 0.2291 0.1777 0.0651  -0.0136 -0.0210 24  GLU A N   
215  C CA  . GLU A 24  ? 0.3210 0.2777 0.2253 0.0653  -0.0136 -0.0209 24  GLU A CA  
216  C C   . GLU A 24  ? 0.3650 0.3242 0.2720 0.0642  -0.0138 -0.0210 24  GLU A C   
217  O O   . GLU A 24  ? 0.2799 0.2394 0.1880 0.0631  -0.0140 -0.0213 24  GLU A O   
218  C CB  . GLU A 24  ? 0.3666 0.3236 0.2711 0.0653  -0.0135 -0.0210 24  GLU A CB  
219  C CG  . GLU A 24  ? 0.5017 0.4567 0.4038 0.0666  -0.0132 -0.0208 24  GLU A CG  
220  C CD  . GLU A 24  ? 0.6672 0.6219 0.5690 0.0665  -0.0131 -0.0210 24  GLU A CD  
221  O OE1 . GLU A 24  ? 0.6784 0.6343 0.5818 0.0655  -0.0133 -0.0212 24  GLU A OE1 
222  O OE2 . GLU A 24  ? 0.7560 0.7091 0.6559 0.0674  -0.0128 -0.0209 24  GLU A OE2 
223  N N   . TYR A 25  ? 0.3131 0.2744 0.2213 0.0646  -0.0137 -0.0208 25  TYR A N   
224  C CA  . TYR A 25  ? 0.2637 0.2278 0.1745 0.0637  -0.0139 -0.0209 25  TYR A CA  
225  C C   . TYR A 25  ? 0.2733 0.2393 0.1859 0.0632  -0.0139 -0.0210 25  TYR A C   
226  O O   . TYR A 25  ? 0.3011 0.2681 0.2137 0.0639  -0.0137 -0.0208 25  TYR A O   
227  C CB  . TYR A 25  ? 0.2614 0.2268 0.1726 0.0643  -0.0138 -0.0206 25  TYR A CB  
228  C CG  . TYR A 25  ? 0.2757 0.2400 0.1862 0.0643  -0.0139 -0.0206 25  TYR A CG  
229  C CD1 . TYR A 25  ? 0.3303 0.2918 0.2382 0.0652  -0.0137 -0.0204 25  TYR A CD1 
230  C CD2 . TYR A 25  ? 0.2783 0.2443 0.1906 0.0635  -0.0140 -0.0207 25  TYR A CD2 
231  C CE1 . TYR A 25  ? 0.2820 0.2424 0.1892 0.0652  -0.0138 -0.0204 25  TYR A CE1 
232  C CE2 . TYR A 25  ? 0.2197 0.1847 0.1314 0.0635  -0.0141 -0.0206 25  TYR A CE2 
233  C CZ  . TYR A 25  ? 0.2895 0.2516 0.1985 0.0643  -0.0140 -0.0205 25  TYR A CZ  
234  O OH  . TYR A 25  ? 0.3072 0.2682 0.2155 0.0643  -0.0140 -0.0204 25  TYR A OH  
235  N N   . LEU A 26  ? 0.2506 0.2171 0.1644 0.0620  -0.0141 -0.0213 26  LEU A N   
236  C CA  . LEU A 26  ? 0.2686 0.2364 0.1837 0.0615  -0.0141 -0.0214 26  LEU A CA  
237  C C   . LEU A 26  ? 0.2685 0.2395 0.1862 0.0610  -0.0141 -0.0214 26  LEU A C   
238  O O   . LEU A 26  ? 0.2718 0.2440 0.1904 0.0608  -0.0140 -0.0215 26  LEU A O   
239  C CB  . LEU A 26  ? 0.2996 0.2666 0.2150 0.0604  -0.0142 -0.0218 26  LEU A CB  
240  C CG  . LEU A 26  ? 0.3545 0.3183 0.2675 0.0607  -0.0142 -0.0218 26  LEU A CG  
241  C CD1 . LEU A 26  ? 0.3284 0.2919 0.2421 0.0595  -0.0144 -0.0221 26  LEU A CD1 
242  C CD2 . LEU A 26  ? 0.2749 0.2375 0.1861 0.0618  -0.0140 -0.0217 26  LEU A CD2 
243  N N   . LEU A 27  ? 0.2404 0.2128 0.1592 0.0608  -0.0141 -0.0214 27  LEU A N   
244  C CA  . LEU A 27  ? 0.2417 0.2173 0.1629 0.0605  -0.0140 -0.0213 27  LEU A CA  
245  C C   . LEU A 27  ? 0.2035 0.1796 0.1243 0.0614  -0.0140 -0.0211 27  LEU A C   
246  O O   . LEU A 27  ? 0.2686 0.2429 0.1880 0.0617  -0.0140 -0.0210 27  LEU A O   
247  C CB  . LEU A 27  ? 0.2075 0.1849 0.1310 0.0590  -0.0142 -0.0216 27  LEU A CB  
248  C CG  . LEU A 27  ? 0.2743 0.2517 0.1986 0.0581  -0.0142 -0.0219 27  LEU A CG  
249  C CD1 . LEU A 27  ? 0.2487 0.2272 0.1748 0.0567  -0.0144 -0.0222 27  LEU A CD1 
250  C CD2 . LEU A 27  ? 0.2612 0.2405 0.1867 0.0582  -0.0141 -0.0219 27  LEU A CD2 
251  N N   . PRO A 28  ? 0.1895 0.1679 0.1116 0.0617  -0.0139 -0.0209 28  PRO A N   
252  C CA  . PRO A 28  ? 0.1733 0.1522 0.0950 0.0626  -0.0138 -0.0206 28  PRO A CA  
253  C C   . PRO A 28  ? 0.2531 0.2341 0.1766 0.0620  -0.0138 -0.0207 28  PRO A C   
254  O O   . PRO A 28  ? 0.2305 0.2126 0.1542 0.0627  -0.0137 -0.0205 28  PRO A O   
255  C CB  . PRO A 28  ? 0.1647 0.1449 0.0866 0.0634  -0.0136 -0.0204 28  PRO A CB  
256  C CG  . PRO A 28  ? 0.2304 0.2126 0.1544 0.0623  -0.0137 -0.0207 28  PRO A CG  
257  C CD  . PRO A 28  ? 0.2356 0.2163 0.1595 0.0613  -0.0138 -0.0210 28  PRO A CD  
258  N N   . TRP A 29  ? 0.2777 0.2593 0.2026 0.0606  -0.0140 -0.0210 29  TRP A N   
259  C CA  . TRP A 29  ? 0.2012 0.1852 0.1283 0.0599  -0.0140 -0.0211 29  TRP A CA  
260  C C   . TRP A 29  ? 0.2586 0.2420 0.1848 0.0604  -0.0140 -0.0209 29  TRP A C   
261  O O   . TRP A 29  ? 0.2117 0.1972 0.1393 0.0603  -0.0139 -0.0209 29  TRP A O   
262  C CB  . TRP A 29  ? 0.2383 0.2228 0.1669 0.0583  -0.0141 -0.0215 29  TRP A CB  
263  C CG  . TRP A 29  ? 0.2967 0.2825 0.2267 0.0576  -0.0141 -0.0217 29  TRP A CG  
264  C CD1 . TRP A 29  ? 0.2886 0.2732 0.2184 0.0569  -0.0142 -0.0219 29  TRP A CD1 
265  C CD2 . TRP A 29  ? 0.2751 0.2636 0.2069 0.0576  -0.0140 -0.0216 29  TRP A CD2 
266  N NE1 . TRP A 29  ? 0.3171 0.3035 0.2485 0.0565  -0.0141 -0.0220 29  TRP A NE1 
267  C CE2 . TRP A 29  ? 0.3022 0.2910 0.2348 0.0569  -0.0140 -0.0218 29  TRP A CE2 
268  C CE3 . TRP A 29  ? 0.3102 0.3009 0.2430 0.0581  -0.0139 -0.0214 29  TRP A CE3 
269  C CZ2 . TRP A 29  ? 0.3092 0.3003 0.2435 0.0566  -0.0139 -0.0219 29  TRP A CZ2 
270  C CZ3 . TRP A 29  ? 0.3000 0.2931 0.2345 0.0578  -0.0138 -0.0215 29  TRP A CZ3 
271  C CH2 . TRP A 29  ? 0.3223 0.3156 0.2575 0.0571  -0.0138 -0.0217 29  TRP A CH2 
272  N N   . THR A 30  ? 0.1974 0.1778 0.1213 0.0609  -0.0140 -0.0209 30  THR A N   
273  C CA  . THR A 30  ? 0.2428 0.2224 0.1657 0.0615  -0.0140 -0.0207 30  THR A CA  
274  C C   . THR A 30  ? 0.2804 0.2607 0.2027 0.0628  -0.0138 -0.0203 30  THR A C   
275  O O   . THR A 30  ? 0.2265 0.2082 0.1494 0.0630  -0.0138 -0.0202 30  THR A O   
276  C CB  . THR A 30  ? 0.2537 0.2300 0.1743 0.0617  -0.0141 -0.0207 30  THR A CB  
277  O OG1 . THR A 30  ? 0.2658 0.2417 0.1871 0.0603  -0.0142 -0.0210 30  THR A OG1 
278  C CG2 . THR A 30  ? 0.2597 0.2350 0.1790 0.0624  -0.0140 -0.0205 30  THR A CG2 
279  N N   . PHE A 31  ? 0.2241 0.2035 0.1451 0.0638  -0.0137 -0.0201 31  PHE A N   
280  C CA  . PHE A 31  ? 0.1871 0.1672 0.1075 0.0651  -0.0136 -0.0198 31  PHE A CA  
281  C C   . PHE A 31  ? 0.2446 0.2283 0.1676 0.0647  -0.0135 -0.0198 31  PHE A C   
282  O O   . PHE A 31  ? 0.2351 0.2199 0.1582 0.0653  -0.0135 -0.0195 31  PHE A O   
283  C CB  . PHE A 31  ? 0.1870 0.1659 0.1060 0.0659  -0.0134 -0.0196 31  PHE A CB  
284  C CG  . PHE A 31  ? 0.2268 0.2066 0.1453 0.0672  -0.0132 -0.0193 31  PHE A CG  
285  C CD1 . PHE A 31  ? 0.2520 0.2302 0.1684 0.0684  -0.0131 -0.0190 31  PHE A CD1 
286  C CD2 . PHE A 31  ? 0.2396 0.2219 0.1597 0.0671  -0.0132 -0.0193 31  PHE A CD2 
287  C CE1 . PHE A 31  ? 0.2186 0.1978 0.1347 0.0695  -0.0129 -0.0186 31  PHE A CE1 
288  C CE2 . PHE A 31  ? 0.2500 0.2332 0.1698 0.0682  -0.0130 -0.0189 31  PHE A CE2 
289  C CZ  . PHE A 31  ? 0.2718 0.2534 0.1895 0.0695  -0.0128 -0.0186 31  PHE A CZ  
290  N N   . PHE A 32  ? 0.1689 0.1544 0.0938 0.0638  -0.0136 -0.0200 32  PHE A N   
291  C CA  . PHE A 32  ? 0.1578 0.1466 0.0850 0.0634  -0.0135 -0.0200 32  PHE A CA  
292  C C   . PHE A 32  ? 0.1630 0.1536 0.0919 0.0627  -0.0136 -0.0201 32  PHE A C   
293  O O   . PHE A 32  ? 0.1476 0.1403 0.0775 0.0630  -0.0135 -0.0200 32  PHE A O   
294  C CB  . PHE A 32  ? 0.1906 0.1807 0.1194 0.0625  -0.0136 -0.0203 32  PHE A CB  
295  C CG  . PHE A 32  ? 0.2273 0.2168 0.1550 0.0634  -0.0134 -0.0201 32  PHE A CG  
296  C CD1 . PHE A 32  ? 0.2971 0.2875 0.2244 0.0646  -0.0133 -0.0198 32  PHE A CD1 
297  C CD2 . PHE A 32  ? 0.2602 0.2486 0.1875 0.0631  -0.0135 -0.0203 32  PHE A CD2 
298  C CE1 . PHE A 32  ? 0.3191 0.3090 0.2454 0.0654  -0.0132 -0.0196 32  PHE A CE1 
299  C CE2 . PHE A 32  ? 0.3298 0.3176 0.2561 0.0639  -0.0134 -0.0201 32  PHE A CE2 
300  C CZ  . PHE A 32  ? 0.2753 0.2639 0.2011 0.0650  -0.0132 -0.0198 32  PHE A CZ  
301  N N   . HIS A 33  ? 0.1382 0.1279 0.0674 0.0616  -0.0137 -0.0204 33  HIS A N   
302  C CA  . HIS A 33  ? 0.2001 0.1913 0.1306 0.0610  -0.0137 -0.0205 33  HIS A CA  
303  C C   . HIS A 33  ? 0.2266 0.2167 0.1555 0.0620  -0.0137 -0.0202 33  HIS A C   
304  O O   . HIS A 33  ? 0.1913 0.1832 0.1214 0.0618  -0.0136 -0.0202 33  HIS A O   
305  C CB  . HIS A 33  ? 0.1892 0.1799 0.1205 0.0595  -0.0138 -0.0209 33  HIS A CB  
306  C CG  . HIS A 33  ? 0.1585 0.1513 0.0921 0.0583  -0.0138 -0.0212 33  HIS A CG  
307  N ND1 . HIS A 33  ? 0.1747 0.1708 0.1107 0.0578  -0.0137 -0.0213 33  HIS A ND1 
308  C CD2 . HIS A 33  ? 0.1483 0.1403 0.0820 0.0577  -0.0139 -0.0214 33  HIS A CD2 
309  C CE1 . HIS A 33  ? 0.1885 0.1857 0.1259 0.0568  -0.0137 -0.0215 33  HIS A CE1 
310  N NE2 . HIS A 33  ? 0.1876 0.1825 0.1238 0.0567  -0.0138 -0.0216 33  HIS A NE2 
311  N N   . ALA A 34  ? 0.2522 0.2394 0.1785 0.0630  -0.0137 -0.0200 34  ALA A N   
312  C CA  . ALA A 34  ? 0.2373 0.2234 0.1621 0.0642  -0.0136 -0.0197 34  ALA A CA  
313  C C   . ALA A 34  ? 0.1968 0.1850 0.1221 0.0651  -0.0134 -0.0194 34  ALA A C   
314  O O   . ALA A 34  ? 0.2092 0.1988 0.1351 0.0653  -0.0134 -0.0192 34  ALA A O   
315  C CB  . ALA A 34  ? 0.2267 0.2093 0.1485 0.0651  -0.0136 -0.0195 34  ALA A CB  
316  N N   . VAL A 35  ? 0.1906 0.1792 0.1157 0.0657  -0.0134 -0.0192 35  VAL A N   
317  C CA  . VAL A 35  ? 0.2803 0.2708 0.2058 0.0667  -0.0132 -0.0189 35  VAL A CA  
318  C C   . VAL A 35  ? 0.2421 0.2363 0.1705 0.0658  -0.0132 -0.0191 35  VAL A C   
319  O O   . VAL A 35  ? 0.2029 0.1989 0.1318 0.0665  -0.0131 -0.0188 35  VAL A O   
320  C CB  . VAL A 35  ? 0.3228 0.3128 0.2473 0.0676  -0.0131 -0.0188 35  VAL A CB  
321  C CG1 . VAL A 35  ? 0.2119 0.1983 0.1336 0.0682  -0.0131 -0.0187 35  VAL A CG1 
322  C CG2 . VAL A 35  ? 0.3223 0.3139 0.2486 0.0666  -0.0132 -0.0190 35  VAL A CG2 
323  N N   . LYS A 36  ? 0.2598 0.2551 0.1900 0.0644  -0.0133 -0.0195 36  LYS A N   
324  C CA  . LYS A 36  ? 0.1639 0.1628 0.0970 0.0635  -0.0133 -0.0196 36  LYS A CA  
325  C C   . LYS A 36  ? 0.1922 0.1921 0.1265 0.0626  -0.0133 -0.0198 36  LYS A C   
326  O O   . LYS A 36  ? 0.1918 0.1944 0.1277 0.0625  -0.0133 -0.0198 36  LYS A O   
327  C CB  . LYS A 36  ? 0.1391 0.1391 0.0738 0.0624  -0.0133 -0.0200 36  LYS A CB  
328  C CG  . LYS A 36  ? 0.1869 0.1907 0.1244 0.0616  -0.0133 -0.0201 36  LYS A CG  
329  C CD  . LYS A 36  ? 0.1952 0.2000 0.1341 0.0607  -0.0133 -0.0204 36  LYS A CD  
330  C CE  . LYS A 36  ? 0.2255 0.2300 0.1654 0.0592  -0.0134 -0.0208 36  LYS A CE  
331  N NZ  . LYS A 36  ? 0.2206 0.2268 0.1623 0.0582  -0.0134 -0.0210 36  LYS A NZ  
332  N N   . ASP A 37  ? 0.1929 0.1907 0.1264 0.0620  -0.0134 -0.0200 37  ASP A N   
333  C CA  . ASP A 37  ? 0.2100 0.2088 0.1448 0.0609  -0.0135 -0.0203 37  ASP A CA  
334  C C   . ASP A 37  ? 0.1653 0.1619 0.0985 0.0612  -0.0135 -0.0202 37  ASP A C   
335  O O   . ASP A 37  ? 0.1834 0.1814 0.1175 0.0609  -0.0134 -0.0202 37  ASP A O   
336  C CB  . ASP A 37  ? 0.2560 0.2550 0.1922 0.0593  -0.0135 -0.0207 37  ASP A CB  
337  C CG  . ASP A 37  ? 0.2249 0.2260 0.1628 0.0589  -0.0135 -0.0208 37  ASP A CG  
338  O OD1 . ASP A 37  ? 0.1540 0.1581 0.0939 0.0586  -0.0134 -0.0208 37  ASP A OD1 
339  O OD2 . ASP A 37  ? 0.2105 0.2102 0.1477 0.0588  -0.0136 -0.0209 37  ASP A OD2 
340  N N   . TYR A 38  ? 0.1222 0.1155 0.0530 0.0618  -0.0136 -0.0201 38  TYR A N   
341  C CA  . TYR A 38  ? 0.1681 0.1593 0.0975 0.0618  -0.0136 -0.0201 38  TYR A CA  
342  C C   . TYR A 38  ? 0.2023 0.1936 0.1308 0.0629  -0.0135 -0.0197 38  TYR A C   
343  O O   . TYR A 38  ? 0.2024 0.1933 0.1307 0.0627  -0.0135 -0.0198 38  TYR A O   
344  C CB  . TYR A 38  ? 0.1659 0.1535 0.0929 0.0621  -0.0137 -0.0201 38  TYR A CB  
345  C CG  . TYR A 38  ? 0.1984 0.1858 0.1263 0.0608  -0.0138 -0.0205 38  TYR A CG  
346  C CD1 . TYR A 38  ? 0.2101 0.1996 0.1404 0.0593  -0.0138 -0.0208 38  TYR A CD1 
347  C CD2 . TYR A 38  ? 0.2302 0.2155 0.1567 0.0611  -0.0139 -0.0205 38  TYR A CD2 
348  C CE1 . TYR A 38  ? 0.1778 0.1670 0.1088 0.0581  -0.0139 -0.0211 38  TYR A CE1 
349  C CE2 . TYR A 38  ? 0.2478 0.2328 0.1750 0.0599  -0.0140 -0.0208 38  TYR A CE2 
350  C CZ  . TYR A 38  ? 0.2170 0.2040 0.1465 0.0585  -0.0140 -0.0211 38  TYR A CZ  
351  O OH  . TYR A 38  ? 0.1923 0.1792 0.1226 0.0574  -0.0141 -0.0214 38  TYR A OH  
352  N N   . TYR A 39  ? 0.1760 0.1678 0.1038 0.0642  -0.0134 -0.0194 39  TYR A N   
353  C CA  . TYR A 39  ? 0.1671 0.1595 0.0944 0.0653  -0.0133 -0.0190 39  TYR A CA  
354  C C   . TYR A 39  ? 0.2235 0.2197 0.1534 0.0648  -0.0132 -0.0191 39  TYR A C   
355  O O   . TYR A 39  ? 0.2025 0.1995 0.1327 0.0649  -0.0132 -0.0190 39  TYR A O   
356  C CB  . TYR A 39  ? 0.1554 0.1467 0.0808 0.0670  -0.0132 -0.0186 39  TYR A CB  
357  C CG  . TYR A 39  ? 0.2925 0.2850 0.2177 0.0681  -0.0130 -0.0182 39  TYR A CG  
358  C CD1 . TYR A 39  ? 0.2479 0.2384 0.1712 0.0689  -0.0130 -0.0179 39  TYR A CD1 
359  C CD2 . TYR A 39  ? 0.2334 0.2289 0.1602 0.0684  -0.0129 -0.0180 39  TYR A CD2 
360  C CE1 . TYR A 39  ? 0.3121 0.3036 0.2351 0.0700  -0.0128 -0.0175 39  TYR A CE1 
361  C CE2 . TYR A 39  ? 0.2861 0.2828 0.2127 0.0695  -0.0128 -0.0176 39  TYR A CE2 
362  C CZ  . TYR A 39  ? 0.2894 0.2841 0.2141 0.0703  -0.0127 -0.0174 39  TYR A CZ  
363  O OH  . TYR A 39  ? 0.3448 0.3405 0.2692 0.0714  -0.0126 -0.0170 39  TYR A OH  
364  N N   . ASP A 40  ? 0.2039 0.2024 0.1357 0.0642  -0.0132 -0.0192 40  ASP A N   
365  C CA  . ASP A 40  ? 0.2014 0.2035 0.1355 0.0639  -0.0131 -0.0192 40  ASP A CA  
366  C C   . ASP A 40  ? 0.2257 0.2296 0.1619 0.0624  -0.0131 -0.0196 40  ASP A C   
367  O O   . ASP A 40  ? 0.2009 0.2073 0.1385 0.0623  -0.0130 -0.0196 40  ASP A O   
368  C CB  . ASP A 40  ? 0.2218 0.2257 0.1571 0.0639  -0.0131 -0.0193 40  ASP A CB  
369  C CG  . ASP A 40  ? 0.2920 0.2957 0.2259 0.0655  -0.0130 -0.0188 40  ASP A CG  
370  O OD1 . ASP A 40  ? 0.2228 0.2284 0.1573 0.0662  -0.0129 -0.0185 40  ASP A OD1 
371  O OD2 . ASP A 40  ? 0.2425 0.2441 0.1748 0.0662  -0.0130 -0.0187 40  ASP A OD2 
372  N N   . MET A 41  ? 0.1964 0.1991 0.1328 0.0612  -0.0132 -0.0200 41  MET A N   
373  C CA  . MET A 41  ? 0.1671 0.1714 0.1054 0.0597  -0.0132 -0.0204 41  MET A CA  
374  C C   . MET A 41  ? 0.1883 0.1922 0.1259 0.0599  -0.0131 -0.0202 41  MET A C   
375  O O   . MET A 41  ? 0.2080 0.2145 0.1473 0.0594  -0.0130 -0.0203 41  MET A O   
376  C CB  . MET A 41  ? 0.1416 0.1446 0.0801 0.0583  -0.0133 -0.0208 41  MET A CB  
377  C CG  . MET A 41  ? 0.1103 0.1149 0.0506 0.0575  -0.0133 -0.0210 41  MET A CG  
378  S SD  . MET A 41  ? 0.1855 0.1947 0.1293 0.0563  -0.0131 -0.0212 41  MET A SD  
379  C CE  . MET A 41  ? 0.1912 0.2001 0.1359 0.0544  -0.0131 -0.0217 41  MET A CE  
380  N N   . PRO A 42  ? 0.2134 0.2142 0.1486 0.0607  -0.0132 -0.0201 42  PRO A N   
381  C CA  . PRO A 42  ? 0.2152 0.2156 0.1496 0.0611  -0.0131 -0.0199 42  PRO A CA  
382  C C   . PRO A 42  ? 0.2197 0.2217 0.1540 0.0625  -0.0130 -0.0195 42  PRO A C   
383  O O   . PRO A 42  ? 0.1966 0.1998 0.1314 0.0626  -0.0129 -0.0194 42  PRO A O   
384  C CB  . PRO A 42  ? 0.1950 0.1915 0.1267 0.0617  -0.0133 -0.0198 42  PRO A CB  
385  C CG  . PRO A 42  ? 0.1845 0.1794 0.1151 0.0622  -0.0133 -0.0197 42  PRO A CG  
386  C CD  . PRO A 42  ? 0.1723 0.1697 0.1053 0.0611  -0.0133 -0.0200 42  PRO A CD  
387  N N   . ALA A 43  ? 0.2440 0.2463 0.1779 0.0635  -0.0130 -0.0192 43  ALA A N   
388  C CA  . ALA A 43  ? 0.2777 0.2816 0.2115 0.0649  -0.0129 -0.0188 43  ALA A CA  
389  C C   . ALA A 43  ? 0.2553 0.2632 0.1919 0.0642  -0.0127 -0.0189 43  ALA A C   
390  O O   . ALA A 43  ? 0.2871 0.2965 0.2237 0.0651  -0.0126 -0.0185 43  ALA A O   
391  C CB  . ALA A 43  ? 0.2584 0.2615 0.1911 0.0661  -0.0129 -0.0185 43  ALA A CB  
392  N N   . TYR A 44  ? 0.2002 0.2099 0.1389 0.0626  -0.0128 -0.0193 44  TYR A N   
393  C CA  . TYR A 44  ? 0.1890 0.2024 0.1303 0.0618  -0.0126 -0.0195 44  TYR A CA  
394  C C   . TYR A 44  ? 0.2275 0.2414 0.1687 0.0619  -0.0125 -0.0194 44  TYR A C   
395  O O   . TYR A 44  ? 0.2485 0.2652 0.1912 0.0619  -0.0124 -0.0193 44  TYR A O   
396  C CB  . TYR A 44  ? 0.2223 0.2371 0.1657 0.0599  -0.0127 -0.0200 44  TYR A CB  
397  C CG  . TYR A 44  ? 0.2221 0.2383 0.1668 0.0596  -0.0127 -0.0201 44  TYR A CG  
398  C CD1 . TYR A 44  ? 0.2038 0.2236 0.1508 0.0594  -0.0126 -0.0201 44  TYR A CD1 
399  C CD2 . TYR A 44  ? 0.2575 0.2714 0.2012 0.0596  -0.0128 -0.0202 44  TYR A CD2 
400  C CE1 . TYR A 44  ? 0.1739 0.1949 0.1219 0.0591  -0.0126 -0.0202 44  TYR A CE1 
401  C CE2 . TYR A 44  ? 0.2474 0.2625 0.1921 0.0594  -0.0129 -0.0202 44  TYR A CE2 
402  C CZ  . TYR A 44  ? 0.2345 0.2531 0.1814 0.0591  -0.0128 -0.0203 44  TYR A CZ  
403  O OH  . TYR A 44  ? 0.2756 0.2954 0.2236 0.0589  -0.0128 -0.0203 44  TYR A OH  
404  N N   . LEU A 45  ? 0.2334 0.2443 0.1728 0.0619  -0.0126 -0.0194 45  LEU A N   
405  C CA  . LEU A 45  ? 0.2544 0.2655 0.1936 0.0619  -0.0125 -0.0193 45  LEU A CA  
406  C C   . LEU A 45  ? 0.3056 0.3171 0.2437 0.0636  -0.0124 -0.0188 45  LEU A C   
407  O O   . LEU A 45  ? 0.2783 0.2908 0.2167 0.0636  -0.0123 -0.0187 45  LEU A O   
408  C CB  . LEU A 45  ? 0.3009 0.3086 0.2383 0.0615  -0.0126 -0.0195 45  LEU A CB  
409  C CG  . LEU A 45  ? 0.2508 0.2583 0.1893 0.0597  -0.0127 -0.0200 45  LEU A CG  
410  C CD1 . LEU A 45  ? 0.2549 0.2588 0.1914 0.0596  -0.0128 -0.0201 45  LEU A CD1 
411  C CD2 . LEU A 45  ? 0.2271 0.2375 0.1679 0.0583  -0.0125 -0.0203 45  LEU A CD2 
412  N N   . LYS A 46  ? 0.2804 0.2913 0.2175 0.0650  -0.0124 -0.0184 46  LYS A N   
413  C CA  . LYS A 46  ? 0.2741 0.2859 0.2104 0.0666  -0.0123 -0.0179 46  LYS A CA  
414  C C   . LYS A 46  ? 0.3085 0.3244 0.2473 0.0663  -0.0121 -0.0179 46  LYS A C   
415  O O   . LYS A 46  ? 0.4222 0.4393 0.3608 0.0672  -0.0120 -0.0175 46  LYS A O   
416  C CB  . LYS A 46  ? 0.3102 0.3202 0.2447 0.0680  -0.0123 -0.0175 46  LYS A CB  
417  C CG  . LYS A 46  ? 0.3683 0.3743 0.2999 0.0689  -0.0124 -0.0173 46  LYS A CG  
418  C CD  . LYS A 46  ? 0.5258 0.5299 0.4563 0.0692  -0.0125 -0.0173 46  LYS A CD  
419  C CE  . LYS A 46  ? 0.5994 0.6025 0.5280 0.0711  -0.0124 -0.0167 46  LYS A CE  
420  N NZ  . LYS A 46  ? 0.5793 0.5808 0.5069 0.0713  -0.0124 -0.0168 46  LYS A NZ  
421  N N   . ASP A 47  ? 0.3290 0.3472 0.2700 0.0650  -0.0122 -0.0182 47  ASP A N   
422  C CA  . ASP A 47  ? 0.3158 0.3381 0.2592 0.0648  -0.0121 -0.0182 47  ASP A CA  
423  C C   . ASP A 47  ? 0.3535 0.3781 0.2992 0.0630  -0.0120 -0.0186 47  ASP A C   
424  O O   . ASP A 47  ? 0.3338 0.3619 0.2815 0.0627  -0.0118 -0.0186 47  ASP A O   
425  C CB  . ASP A 47  ? 0.3177 0.3413 0.2621 0.0648  -0.0121 -0.0182 47  ASP A CB  
426  C CG  . ASP A 47  ? 0.3861 0.4077 0.3284 0.0665  -0.0122 -0.0178 47  ASP A CG  
427  O OD1 . ASP A 47  ? 0.3381 0.3587 0.2787 0.0679  -0.0121 -0.0173 47  ASP A OD1 
428  O OD2 . ASP A 47  ? 0.4417 0.4626 0.3838 0.0664  -0.0123 -0.0179 47  ASP A OD2 
429  N N   . PHE A 48  ? 0.2921 0.3150 0.2376 0.0618  -0.0120 -0.0190 48  PHE A N   
430  C CA  . PHE A 48  ? 0.3464 0.3713 0.2940 0.0600  -0.0119 -0.0195 48  PHE A CA  
431  C C   . PHE A 48  ? 0.3320 0.3549 0.2784 0.0596  -0.0119 -0.0196 48  PHE A C   
432  O O   . PHE A 48  ? 0.2533 0.2727 0.1977 0.0598  -0.0120 -0.0196 48  PHE A O   
433  C CB  . PHE A 48  ? 0.2757 0.3010 0.2248 0.0585  -0.0120 -0.0199 48  PHE A CB  
434  C CG  . PHE A 48  ? 0.3129 0.3403 0.2633 0.0588  -0.0120 -0.0199 48  PHE A CG  
435  C CD1 . PHE A 48  ? 0.3824 0.4137 0.3354 0.0580  -0.0119 -0.0200 48  PHE A CD1 
436  C CD2 . PHE A 48  ? 0.3000 0.3255 0.2490 0.0597  -0.0122 -0.0197 48  PHE A CD2 
437  C CE1 . PHE A 48  ? 0.3741 0.4074 0.3284 0.0582  -0.0119 -0.0199 48  PHE A CE1 
438  C CE2 . PHE A 48  ? 0.2722 0.2996 0.2224 0.0599  -0.0122 -0.0197 48  PHE A CE2 
439  C CZ  . PHE A 48  ? 0.3541 0.3855 0.3069 0.0591  -0.0121 -0.0198 48  PHE A CZ  
440  N N   . GLU A 49  ? 0.2488 0.2738 0.1963 0.0591  -0.0117 -0.0196 49  GLU A N   
441  C CA  . GLU A 49  ? 0.2846 0.3079 0.2310 0.0588  -0.0117 -0.0197 49  GLU A CA  
442  C C   . GLU A 49  ? 0.2422 0.2656 0.1898 0.0567  -0.0117 -0.0202 49  GLU A C   
443  O O   . GLU A 49  ? 0.2678 0.2934 0.2169 0.0555  -0.0115 -0.0204 49  GLU A O   
444  C CB  . GLU A 49  ? 0.2797 0.3052 0.2264 0.0593  -0.0115 -0.0194 49  GLU A CB  
445  C CG  . GLU A 49  ? 0.4582 0.4822 0.4028 0.0614  -0.0115 -0.0188 49  GLU A CG  
446  C CD  . GLU A 49  ? 0.6307 0.6549 0.5747 0.0616  -0.0113 -0.0186 49  GLU A CD  
447  O OE1 . GLU A 49  ? 0.6867 0.7098 0.6290 0.0633  -0.0112 -0.0181 49  GLU A OE1 
448  O OE2 . GLU A 49  ? 0.6993 0.7249 0.6445 0.0602  -0.0112 -0.0189 49  GLU A OE2 
449  N N   . ILE A 50  ? 0.2398 0.2609 0.1867 0.0563  -0.0118 -0.0205 50  ILE A N   
450  C CA  . ILE A 50  ? 0.2236 0.2442 0.1714 0.0544  -0.0119 -0.0209 50  ILE A CA  
451  C C   . ILE A 50  ? 0.1871 0.2036 0.1325 0.0547  -0.0121 -0.0210 50  ILE A C   
452  O O   . ILE A 50  ? 0.2643 0.2785 0.2075 0.0563  -0.0122 -0.0206 50  ILE A O   
453  C CB  . ILE A 50  ? 0.2427 0.2653 0.1926 0.0534  -0.0119 -0.0212 50  ILE A CB  
454  C CG1 . ILE A 50  ? 0.2405 0.2617 0.1895 0.0544  -0.0120 -0.0211 50  ILE A CG1 
455  C CG2 . ILE A 50  ? 0.3440 0.3709 0.2965 0.0529  -0.0117 -0.0213 50  ILE A CG2 
456  C CD1 . ILE A 50  ? 0.2628 0.2852 0.2136 0.0533  -0.0121 -0.0214 50  ILE A CD1 
457  N N   . LYS A 51  ? 0.1894 0.2050 0.1351 0.0532  -0.0121 -0.0214 51  LYS A N   
458  C CA  . LYS A 51  ? 0.1829 0.1948 0.1266 0.0532  -0.0123 -0.0215 51  LYS A CA  
459  C C   . LYS A 51  ? 0.2165 0.2280 0.1609 0.0526  -0.0124 -0.0217 51  LYS A C   
460  O O   . LYS A 51  ? 0.1763 0.1902 0.1229 0.0514  -0.0123 -0.0220 51  LYS A O   
461  C CB  . LYS A 51  ? 0.1849 0.1958 0.1284 0.0519  -0.0122 -0.0217 51  LYS A CB  
462  C CG  . LYS A 51  ? 0.1850 0.1965 0.1281 0.0522  -0.0121 -0.0216 51  LYS A CG  
463  C CD  . LYS A 51  ? 0.2382 0.2473 0.1787 0.0542  -0.0122 -0.0211 51  LYS A CD  
464  C CE  . LYS A 51  ? 0.2981 0.3072 0.2378 0.0544  -0.0121 -0.0210 51  LYS A CE  
465  N NZ  . LYS A 51  ? 0.4039 0.4168 0.3456 0.0541  -0.0119 -0.0209 51  LYS A NZ  
466  N N   . LEU A 52  ? 0.2011 0.2096 0.1435 0.0535  -0.0126 -0.0215 52  LEU A N   
467  C CA  . LEU A 52  ? 0.2149 0.2225 0.1574 0.0531  -0.0127 -0.0217 52  LEU A CA  
468  C C   . LEU A 52  ? 0.2700 0.2737 0.2101 0.0534  -0.0129 -0.0217 52  LEU A C   
469  O O   . LEU A 52  ? 0.1849 0.1865 0.1229 0.0548  -0.0130 -0.0214 52  LEU A O   
470  C CB  . LEU A 52  ? 0.1788 0.1874 0.1215 0.0543  -0.0127 -0.0215 52  LEU A CB  
471  C CG  . LEU A 52  ? 0.1919 0.2044 0.1370 0.0541  -0.0126 -0.0215 52  LEU A CG  
472  C CD1 . LEU A 52  ? 0.1518 0.1646 0.0966 0.0554  -0.0126 -0.0211 52  LEU A CD1 
473  C CD2 . LEU A 52  ? 0.1719 0.1864 0.1195 0.0522  -0.0125 -0.0219 52  LEU A CD2 
474  N N   . ASN A 53  ? 0.1952 0.1979 0.1357 0.0522  -0.0130 -0.0220 53  ASN A N   
475  C CA  . ASN A 53  ? 0.1588 0.1580 0.0972 0.0524  -0.0132 -0.0220 53  ASN A CA  
476  C C   . ASN A 53  ? 0.1876 0.1854 0.1254 0.0526  -0.0133 -0.0221 53  ASN A C   
477  O O   . ASN A 53  ? 0.1532 0.1529 0.0927 0.0521  -0.0133 -0.0222 53  ASN A O   
478  C CB  . ASN A 53  ? 0.1794 0.1781 0.1182 0.0507  -0.0132 -0.0224 53  ASN A CB  
479  C CG  . ASN A 53  ? 0.2107 0.2111 0.1503 0.0503  -0.0130 -0.0224 53  ASN A CG  
480  O OD1 . ASN A 53  ? 0.2041 0.2032 0.1421 0.0511  -0.0130 -0.0222 53  ASN A OD1 
481  N ND2 . ASN A 53  ? 0.1524 0.1558 0.0944 0.0490  -0.0128 -0.0227 53  ASN A ND2 
482  N N   . PHE A 54  ? 0.1378 0.1324 0.0733 0.0533  -0.0135 -0.0219 54  PHE A N   
483  C CA  . PHE A 54  ? 0.2020 0.1950 0.1366 0.0538  -0.0136 -0.0219 54  PHE A CA  
484  C C   . PHE A 54  ? 0.1794 0.1692 0.1124 0.0534  -0.0138 -0.0220 54  PHE A C   
485  O O   . PHE A 54  ? 0.2096 0.1975 0.1411 0.0535  -0.0138 -0.0220 54  PHE A O   
486  C CB  . PHE A 54  ? 0.1471 0.1392 0.0800 0.0557  -0.0136 -0.0214 54  PHE A CB  
487  C CG  . PHE A 54  ? 0.2210 0.2162 0.1555 0.0562  -0.0135 -0.0213 54  PHE A CG  
488  C CD1 . PHE A 54  ? 0.1602 0.1567 0.0949 0.0566  -0.0134 -0.0211 54  PHE A CD1 
489  C CD2 . PHE A 54  ? 0.2058 0.2028 0.1417 0.0561  -0.0135 -0.0213 54  PHE A CD2 
490  C CE1 . PHE A 54  ? 0.2029 0.2024 0.1391 0.0571  -0.0132 -0.0210 54  PHE A CE1 
491  C CE2 . PHE A 54  ? 0.1847 0.1847 0.1221 0.0565  -0.0133 -0.0212 54  PHE A CE2 
492  C CZ  . PHE A 54  ? 0.1910 0.1922 0.1285 0.0570  -0.0132 -0.0210 54  PHE A CZ  
493  N N   . ASN A 55  ? 0.1332 0.1226 0.0665 0.0528  -0.0139 -0.0222 55  ASN A N   
494  C CA  . ASN A 55  ? 0.1318 0.1183 0.0635 0.0526  -0.0140 -0.0223 55  ASN A CA  
495  C C   . ASN A 55  ? 0.2032 0.1880 0.1333 0.0539  -0.0141 -0.0220 55  ASN A C   
496  O O   . ASN A 55  ? 0.1601 0.1464 0.0912 0.0541  -0.0141 -0.0220 55  ASN A O   
497  C CB  . ASN A 55  ? 0.1666 0.1537 0.0998 0.0509  -0.0140 -0.0227 55  ASN A CB  
498  C CG  . ASN A 55  ? 0.1853 0.1693 0.1168 0.0507  -0.0142 -0.0228 55  ASN A CG  
499  O OD1 . ASN A 55  ? 0.2107 0.1931 0.1411 0.0506  -0.0142 -0.0228 55  ASN A OD1 
500  N ND2 . ASN A 55  ? 0.1816 0.1650 0.1131 0.0505  -0.0143 -0.0229 55  ASN A ND2 
501  N N   . LEU A 56  ? 0.1878 0.1695 0.1154 0.0547  -0.0142 -0.0219 56  LEU A N   
502  C CA  . LEU A 56  ? 0.2529 0.2326 0.1787 0.0558  -0.0143 -0.0217 56  LEU A CA  
503  C C   . LEU A 56  ? 0.2144 0.1914 0.1389 0.0553  -0.0145 -0.0218 56  LEU A C   
504  O O   . LEU A 56  ? 0.2333 0.2084 0.1565 0.0551  -0.0145 -0.0219 56  LEU A O   
505  C CB  . LEU A 56  ? 0.2248 0.2031 0.1485 0.0575  -0.0143 -0.0212 56  LEU A CB  
506  C CG  . LEU A 56  ? 0.2294 0.2102 0.1541 0.0583  -0.0141 -0.0210 56  LEU A CG  
507  C CD1 . LEU A 56  ? 0.2880 0.2671 0.2105 0.0599  -0.0141 -0.0206 56  LEU A CD1 
508  C CD2 . LEU A 56  ? 0.2671 0.2498 0.1931 0.0585  -0.0141 -0.0210 56  LEU A CD2 
509  N N   . THR A 57  ? 0.2104 0.1874 0.1353 0.0549  -0.0145 -0.0220 57  THR A N   
510  C CA  . THR A 57  ? 0.1834 0.1577 0.1069 0.0545  -0.0146 -0.0221 57  THR A CA  
511  C C   . THR A 57  ? 0.1887 0.1601 0.1094 0.0559  -0.0147 -0.0218 57  THR A C   
512  O O   . THR A 57  ? 0.2178 0.1892 0.1378 0.0571  -0.0146 -0.0216 57  THR A O   
513  C CB  . THR A 57  ? 0.1972 0.1722 0.1219 0.0537  -0.0147 -0.0224 57  THR A CB  
514  O OG1 . THR A 57  ? 0.1836 0.1586 0.1077 0.0547  -0.0146 -0.0222 57  THR A OG1 
515  C CG2 . THR A 57  ? 0.2011 0.1791 0.1287 0.0523  -0.0146 -0.0226 57  THR A CG2 
516  N N   . PRO A 58  ? 0.2385 0.2073 0.1575 0.0557  -0.0148 -0.0219 58  PRO A N   
517  C CA  . PRO A 58  ? 0.2377 0.2036 0.1540 0.0571  -0.0148 -0.0216 58  PRO A CA  
518  C C   . PRO A 58  ? 0.1995 0.1647 0.1150 0.0577  -0.0148 -0.0215 58  PRO A C   
519  O O   . PRO A 58  ? 0.2535 0.2174 0.1672 0.0591  -0.0147 -0.0212 58  PRO A O   
520  C CB  . PRO A 58  ? 0.1919 0.1554 0.1069 0.0564  -0.0149 -0.0218 58  PRO A CB  
521  C CG  . PRO A 58  ? 0.2323 0.1974 0.1492 0.0550  -0.0150 -0.0221 58  PRO A CG  
522  C CD  . PRO A 58  ? 0.2412 0.2095 0.1607 0.0544  -0.0149 -0.0222 58  PRO A CD  
523  N N   . VAL A 59  ? 0.2112 0.1772 0.1279 0.0568  -0.0148 -0.0218 59  VAL A N   
524  C CA  . VAL A 59  ? 0.2315 0.1969 0.1475 0.0574  -0.0148 -0.0217 59  VAL A CA  
525  C C   . VAL A 59  ? 0.2693 0.2366 0.1860 0.0583  -0.0147 -0.0215 59  VAL A C   
526  O O   . VAL A 59  ? 0.2518 0.2182 0.1672 0.0594  -0.0146 -0.0213 59  VAL A O   
527  C CB  . VAL A 59  ? 0.2075 0.1734 0.1248 0.0562  -0.0149 -0.0221 59  VAL A CB  
528  C CG1 . VAL A 59  ? 0.2304 0.1995 0.1506 0.0552  -0.0149 -0.0222 59  VAL A CG1 
529  C CG2 . VAL A 59  ? 0.2203 0.1853 0.1366 0.0569  -0.0149 -0.0220 59  VAL A CG2 
530  N N   . LEU A 60  ? 0.2298 0.1999 0.1487 0.0579  -0.0146 -0.0215 60  LEU A N   
531  C CA  . LEU A 60  ? 0.1815 0.1534 0.1009 0.0589  -0.0145 -0.0212 60  LEU A CA  
532  C C   . LEU A 60  ? 0.2023 0.1727 0.1196 0.0603  -0.0144 -0.0209 60  LEU A C   
533  O O   . LEU A 60  ? 0.2547 0.2248 0.1710 0.0615  -0.0143 -0.0206 60  LEU A O   
534  C CB  . LEU A 60  ? 0.2407 0.2159 0.1627 0.0581  -0.0144 -0.0214 60  LEU A CB  
535  C CG  . LEU A 60  ? 0.1861 0.1633 0.1088 0.0591  -0.0143 -0.0211 60  LEU A CG  
536  C CD1 . LEU A 60  ? 0.1607 0.1381 0.0832 0.0596  -0.0143 -0.0210 60  LEU A CD1 
537  C CD2 . LEU A 60  ? 0.1806 0.1611 0.1060 0.0581  -0.0142 -0.0212 60  LEU A CD2 
538  N N   . ILE A 61  ? 0.2382 0.2077 0.1549 0.0603  -0.0144 -0.0209 61  ILE A N   
539  C CA  . ILE A 61  ? 0.2379 0.2059 0.1525 0.0617  -0.0143 -0.0205 61  ILE A CA  
540  C C   . ILE A 61  ? 0.2331 0.1983 0.1452 0.0627  -0.0143 -0.0203 61  ILE A C   
541  O O   . ILE A 61  ? 0.2402 0.2050 0.1511 0.0640  -0.0141 -0.0200 61  ILE A O   
542  C CB  . ILE A 61  ? 0.2721 0.2389 0.1861 0.0613  -0.0144 -0.0205 61  ILE A CB  
543  C CG1 . ILE A 61  ? 0.2300 0.1997 0.1464 0.0604  -0.0144 -0.0207 61  ILE A CG1 
544  C CG2 . ILE A 61  ? 0.2998 0.2647 0.2114 0.0627  -0.0143 -0.0202 61  ILE A CG2 
545  C CD1 . ILE A 61  ? 0.2407 0.2096 0.1570 0.0597  -0.0145 -0.0208 61  ILE A CD1 
546  N N   . ASP A 62  ? 0.2851 0.2484 0.1964 0.0620  -0.0144 -0.0206 62  ASP A N   
547  C CA  . ASP A 62  ? 0.3284 0.2890 0.2373 0.0628  -0.0143 -0.0205 62  ASP A CA  
548  C C   . ASP A 62  ? 0.2502 0.2118 0.1592 0.0637  -0.0142 -0.0203 62  ASP A C   
549  O O   . ASP A 62  ? 0.2564 0.2165 0.1635 0.0649  -0.0140 -0.0200 62  ASP A O   
550  C CB  . ASP A 62  ? 0.2576 0.2167 0.1662 0.0619  -0.0145 -0.0208 62  ASP A CB  
551  C CG  . ASP A 62  ? 0.2962 0.2533 0.2037 0.0614  -0.0146 -0.0209 62  ASP A CG  
552  O OD1 . ASP A 62  ? 0.3761 0.3324 0.2825 0.0621  -0.0145 -0.0207 62  ASP A OD1 
553  O OD2 . ASP A 62  ? 0.3213 0.2777 0.2291 0.0603  -0.0147 -0.0212 62  ASP A OD2 
554  N N   . GLN A 63  ? 0.2486 0.2127 0.1599 0.0630  -0.0143 -0.0204 63  GLN A N   
555  C CA  . GLN A 63  ? 0.1907 0.1558 0.1022 0.0636  -0.0141 -0.0203 63  GLN A CA  
556  C C   . GLN A 63  ? 0.2561 0.2225 0.1676 0.0648  -0.0140 -0.0200 63  GLN A C   
557  O O   . GLN A 63  ? 0.2199 0.1858 0.1302 0.0659  -0.0138 -0.0197 63  GLN A O   
558  C CB  . GLN A 63  ? 0.2082 0.1756 0.1221 0.0625  -0.0142 -0.0206 63  GLN A CB  
559  C CG  . GLN A 63  ? 0.2161 0.1822 0.1299 0.0615  -0.0144 -0.0209 63  GLN A CG  
560  C CD  . GLN A 63  ? 0.2944 0.2629 0.2108 0.0603  -0.0144 -0.0212 63  GLN A CD  
561  O OE1 . GLN A 63  ? 0.2630 0.2326 0.1800 0.0605  -0.0144 -0.0212 63  GLN A OE1 
562  N NE2 . GLN A 63  ? 0.2092 0.1786 0.1271 0.0591  -0.0146 -0.0214 63  GLN A NE2 
563  N N   . ILE A 64  ? 0.2368 0.2051 0.1498 0.0645  -0.0140 -0.0199 64  ILE A N   
564  C CA  . ILE A 64  ? 0.2513 0.2208 0.1643 0.0656  -0.0138 -0.0196 64  ILE A CA  
565  C C   . ILE A 64  ? 0.2449 0.2119 0.1551 0.0670  -0.0137 -0.0192 64  ILE A C   
566  O O   . ILE A 64  ? 0.2427 0.2099 0.1521 0.0682  -0.0135 -0.0189 64  ILE A O   
567  C CB  . ILE A 64  ? 0.2304 0.2021 0.1451 0.0650  -0.0139 -0.0196 64  ILE A CB  
568  C CG1 . ILE A 64  ? 0.2068 0.1815 0.1245 0.0637  -0.0139 -0.0199 64  ILE A CG1 
569  C CG2 . ILE A 64  ? 0.2932 0.2657 0.2075 0.0662  -0.0137 -0.0192 64  ILE A CG2 
570  C CD1 . ILE A 64  ? 0.2016 0.1785 0.1212 0.0629  -0.0140 -0.0200 64  ILE A CD1 
571  N N   . GLN A 65  ? 0.2559 0.2204 0.1645 0.0668  -0.0137 -0.0193 65  GLN A N   
572  C CA  . GLN A 65  ? 0.2659 0.2277 0.1717 0.0681  -0.0135 -0.0190 65  GLN A CA  
573  C C   . GLN A 65  ? 0.3040 0.2643 0.2082 0.0689  -0.0134 -0.0189 65  GLN A C   
574  O O   . GLN A 65  ? 0.2941 0.2534 0.1967 0.0702  -0.0131 -0.0186 65  GLN A O   
575  C CB  . GLN A 65  ? 0.2940 0.2534 0.1985 0.0677  -0.0136 -0.0191 65  GLN A CB  
576  C CG  . GLN A 65  ? 0.3445 0.3051 0.2502 0.0671  -0.0138 -0.0192 65  GLN A CG  
577  C CD  . GLN A 65  ? 0.3560 0.3142 0.2604 0.0666  -0.0139 -0.0193 65  GLN A CD  
578  O OE1 . GLN A 65  ? 0.4637 0.4210 0.3682 0.0656  -0.0140 -0.0196 65  GLN A OE1 
579  N NE2 . GLN A 65  ? 0.4912 0.4484 0.3943 0.0673  -0.0138 -0.0191 65  GLN A NE2 
580  N N   . GLU A 66  ? 0.3351 0.2951 0.2397 0.0681  -0.0135 -0.0192 66  GLU A N   
581  C CA  . GLU A 66  ? 0.3667 0.3253 0.2699 0.0687  -0.0133 -0.0192 66  GLU A CA  
582  C C   . GLU A 66  ? 0.3196 0.2800 0.2234 0.0695  -0.0132 -0.0189 66  GLU A C   
583  O O   . GLU A 66  ? 0.2747 0.2339 0.1768 0.0706  -0.0129 -0.0187 66  GLU A O   
584  C CB  . GLU A 66  ? 0.2896 0.2475 0.1931 0.0677  -0.0135 -0.0195 66  GLU A CB  
585  C CG  . GLU A 66  ? 0.4178 0.3729 0.3197 0.0673  -0.0136 -0.0197 66  GLU A CG  
586  C CD  . GLU A 66  ? 0.5893 0.5441 0.4919 0.0661  -0.0138 -0.0201 66  GLU A CD  
587  O OE1 . GLU A 66  ? 0.7125 0.6665 0.6152 0.0652  -0.0140 -0.0203 66  GLU A OE1 
588  O OE2 . GLU A 66  ? 0.4363 0.3917 0.3393 0.0660  -0.0138 -0.0202 66  GLU A OE2 
589  N N   . TYR A 67  ? 0.2533 0.2168 0.1597 0.0689  -0.0133 -0.0190 67  TYR A N   
590  C CA  . TYR A 67  ? 0.2647 0.2302 0.1718 0.0697  -0.0131 -0.0188 67  TYR A CA  
591  C C   . TYR A 67  ? 0.3085 0.2738 0.2144 0.0710  -0.0129 -0.0183 67  TYR A C   
592  O O   . TYR A 67  ? 0.3853 0.3503 0.2901 0.0721  -0.0126 -0.0181 67  TYR A O   
593  C CB  . TYR A 67  ? 0.3009 0.2698 0.2110 0.0687  -0.0133 -0.0189 67  TYR A CB  
594  C CG  . TYR A 67  ? 0.2299 0.1993 0.1412 0.0678  -0.0134 -0.0193 67  TYR A CG  
595  C CD1 . TYR A 67  ? 0.2390 0.2090 0.1502 0.0683  -0.0132 -0.0192 67  TYR A CD1 
596  C CD2 . TYR A 67  ? 0.2687 0.2381 0.1810 0.0664  -0.0136 -0.0196 67  TYR A CD2 
597  C CE1 . TYR A 67  ? 0.3024 0.2729 0.2146 0.0674  -0.0133 -0.0195 67  TYR A CE1 
598  C CE2 . TYR A 67  ? 0.2909 0.2609 0.2043 0.0656  -0.0137 -0.0199 67  TYR A CE2 
599  C CZ  . TYR A 67  ? 0.2830 0.2535 0.1963 0.0661  -0.0136 -0.0198 67  TYR A CZ  
600  O OH  . TYR A 67  ? 0.2591 0.2302 0.1735 0.0653  -0.0136 -0.0201 67  TYR A OH  
601  N N   . ALA A 68  ? 0.3022 0.2679 0.2085 0.0708  -0.0130 -0.0183 68  ALA A N   
602  C CA  . ALA A 68  ? 0.2824 0.2481 0.1877 0.0721  -0.0128 -0.0179 68  ALA A CA  
603  C C   . ALA A 68  ? 0.3336 0.2963 0.2360 0.0733  -0.0125 -0.0176 68  ALA A C   
604  O O   . ALA A 68  ? 0.3887 0.3514 0.2900 0.0745  -0.0122 -0.0173 68  ALA A O   
605  C CB  . ALA A 68  ? 0.3263 0.2923 0.2321 0.0716  -0.0129 -0.0179 68  ALA A CB  
606  N N   . GLN A 69  ? 0.3099 0.3767 0.1509 0.0551  -0.0309 -0.0254 69  GLN A N   
607  C CA  . GLN A 69  ? 0.4238 0.4903 0.2621 0.0552  -0.0314 -0.0258 69  GLN A CA  
608  C C   . GLN A 69  ? 0.4434 0.5120 0.2822 0.0552  -0.0313 -0.0250 69  GLN A C   
609  O O   . GLN A 69  ? 0.5498 0.6183 0.3864 0.0553  -0.0317 -0.0251 69  GLN A O   
610  C CB  . GLN A 69  ? 0.3798 0.4450 0.2164 0.0546  -0.0319 -0.0257 69  GLN A CB  
611  C CG  . GLN A 69  ? 0.4964 0.5594 0.3320 0.0546  -0.0320 -0.0266 69  GLN A CG  
612  C CD  . GLN A 69  ? 0.5636 0.6254 0.3979 0.0539  -0.0324 -0.0264 69  GLN A CD  
613  O OE1 . GLN A 69  ? 0.6331 0.6958 0.4677 0.0533  -0.0326 -0.0255 69  GLN A OE1 
614  N NE2 . GLN A 69  ? 0.6440 0.7036 0.4767 0.0540  -0.0326 -0.0274 69  GLN A NE2 
615  N N   . GLY A 70  ? 0.4277 0.4981 0.2692 0.0552  -0.0308 -0.0242 70  GLY A N   
616  C CA  . GLY A 70  ? 0.3799 0.4524 0.2221 0.0552  -0.0308 -0.0234 70  GLY A CA  
617  C C   . GLY A 70  ? 0.4384 0.5116 0.2802 0.0544  -0.0311 -0.0224 70  GLY A C   
618  O O   . GLY A 70  ? 0.4310 0.5056 0.2725 0.0545  -0.0312 -0.0220 70  GLY A O   
619  N N   . LYS A 71  ? 0.4460 0.5183 0.2878 0.0537  -0.0313 -0.0221 71  LYS A N   
620  C CA  . LYS A 71  ? 0.3922 0.4650 0.2336 0.0530  -0.0317 -0.0212 71  LYS A CA  
621  C C   . LYS A 71  ? 0.4634 0.5381 0.3079 0.0523  -0.0313 -0.0198 71  LYS A C   
622  O O   . LYS A 71  ? 0.5076 0.5831 0.3520 0.0517  -0.0316 -0.0189 71  LYS A O   
623  C CB  . LYS A 71  ? 0.4541 0.5250 0.2936 0.0525  -0.0321 -0.0215 71  LYS A CB  
624  C CG  . LYS A 71  ? 0.5541 0.6230 0.3906 0.0531  -0.0325 -0.0229 71  LYS A CG  
625  C CD  . LYS A 71  ? 0.6749 0.7421 0.5096 0.0526  -0.0329 -0.0232 71  LYS A CD  
626  C CE  . LYS A 71  ? 0.7566 0.8217 0.5883 0.0531  -0.0333 -0.0245 71  LYS A CE  
627  N NZ  . LYS A 71  ? 0.7972 0.8606 0.6273 0.0525  -0.0337 -0.0247 71  LYS A NZ  
628  N N   . ALA A 72  ? 0.3815 0.4566 0.2284 0.0524  -0.0308 -0.0196 72  ALA A N   
629  C CA  . ALA A 72  ? 0.3709 0.4475 0.2207 0.0518  -0.0305 -0.0183 72  ALA A CA  
630  C C   . ALA A 72  ? 0.3831 0.4620 0.2342 0.0518  -0.0303 -0.0174 72  ALA A C   
631  O O   . ALA A 72  ? 0.5059 0.5856 0.3576 0.0525  -0.0300 -0.0177 72  ALA A O   
632  C CB  . ALA A 72  ? 0.3405 0.4169 0.1926 0.0519  -0.0301 -0.0183 72  ALA A CB  
633  N N   . LYS A 73  ? 0.3091 0.3891 0.1604 0.0511  -0.0305 -0.0164 73  LYS A N   
634  C CA  . LYS A 73  ? 0.3615 0.4437 0.2142 0.0511  -0.0304 -0.0154 73  LYS A CA  
635  C C   . LYS A 73  ? 0.3390 0.4225 0.1951 0.0507  -0.0299 -0.0144 73  LYS A C   
636  O O   . LYS A 73  ? 0.4151 0.4991 0.2723 0.0499  -0.0299 -0.0135 73  LYS A O   
637  C CB  . LYS A 73  ? 0.3500 0.4327 0.2013 0.0506  -0.0308 -0.0148 73  LYS A CB  
638  C CG  . LYS A 73  ? 0.4723 0.5571 0.3243 0.0507  -0.0307 -0.0141 73  LYS A CG  
639  C CD  . LYS A 73  ? 0.5239 0.6093 0.3746 0.0501  -0.0312 -0.0135 73  LYS A CD  
640  C CE  . LYS A 73  ? 0.5883 0.6760 0.4406 0.0500  -0.0310 -0.0125 73  LYS A CE  
641  N NZ  . LYS A 73  ? 0.5999 0.6880 0.4500 0.0501  -0.0313 -0.0125 73  LYS A NZ  
642  N N   . ASP A 74  ? 0.2793 0.3635 0.1370 0.0513  -0.0294 -0.0146 74  ASP A N   
643  C CA  . ASP A 74  ? 0.2526 0.3380 0.1135 0.0510  -0.0289 -0.0138 74  ASP A CA  
644  C C   . ASP A 74  ? 0.2754 0.3631 0.1379 0.0510  -0.0286 -0.0129 74  ASP A C   
645  O O   . ASP A 74  ? 0.2774 0.3658 0.1398 0.0516  -0.0285 -0.0133 74  ASP A O   
646  C CB  . ASP A 74  ? 0.2519 0.3364 0.1136 0.0516  -0.0285 -0.0147 74  ASP A CB  
647  C CG  . ASP A 74  ? 0.2598 0.3454 0.1249 0.0514  -0.0280 -0.0139 74  ASP A CG  
648  O OD1 . ASP A 74  ? 0.2753 0.3629 0.1423 0.0512  -0.0277 -0.0129 74  ASP A OD1 
649  O OD2 . ASP A 74  ? 0.3092 0.3936 0.1749 0.0515  -0.0278 -0.0144 74  ASP A OD2 
650  N N   . VAL A 75  ? 0.2948 0.3837 0.1590 0.0502  -0.0286 -0.0116 75  VAL A N   
651  C CA  . VAL A 75  ? 0.3461 0.4372 0.2114 0.0501  -0.0285 -0.0106 75  VAL A CA  
652  C C   . VAL A 75  ? 0.2846 0.3770 0.1523 0.0506  -0.0279 -0.0105 75  VAL A C   
653  O O   . VAL A 75  ? 0.2939 0.3876 0.1617 0.0510  -0.0278 -0.0104 75  VAL A O   
654  C CB  . VAL A 75  ? 0.4524 0.5445 0.3189 0.0492  -0.0286 -0.0093 75  VAL A CB  
655  C CG1 . VAL A 75  ? 0.4538 0.5447 0.3178 0.0488  -0.0292 -0.0095 75  VAL A CG1 
656  C CG2 . VAL A 75  ? 0.4436 0.5358 0.3127 0.0488  -0.0283 -0.0087 75  VAL A CG2 
657  N N   . PHE A 76  ? 0.2726 0.3647 0.1423 0.0506  -0.0275 -0.0105 76  PHE A N   
658  C CA  . PHE A 76  ? 0.3427 0.4360 0.2147 0.0510  -0.0270 -0.0104 76  PHE A CA  
659  C C   . PHE A 76  ? 0.3278 0.4205 0.1983 0.0520  -0.0269 -0.0116 76  PHE A C   
660  O O   . PHE A 76  ? 0.3178 0.4118 0.1892 0.0524  -0.0266 -0.0115 76  PHE A O   
661  C CB  . PHE A 76  ? 0.3022 0.3950 0.1764 0.0508  -0.0266 -0.0102 76  PHE A CB  
662  C CG  . PHE A 76  ? 0.3946 0.4889 0.2714 0.0512  -0.0260 -0.0099 76  PHE A CG  
663  C CD1 . PHE A 76  ? 0.5007 0.5971 0.3798 0.0508  -0.0258 -0.0087 76  PHE A CD1 
664  C CD2 . PHE A 76  ? 0.3839 0.4775 0.2608 0.0519  -0.0257 -0.0109 76  PHE A CD2 
665  C CE1 . PHE A 76  ? 0.5317 0.6294 0.4131 0.0511  -0.0252 -0.0084 76  PHE A CE1 
666  C CE2 . PHE A 76  ? 0.4808 0.5758 0.3601 0.0522  -0.0252 -0.0106 76  PHE A CE2 
667  C CZ  . PHE A 76  ? 0.5181 0.6151 0.3996 0.0518  -0.0249 -0.0093 76  PHE A CZ  
668  N N   . LEU A 77  ? 0.2793 0.3699 0.1478 0.0523  -0.0271 -0.0128 77  LEU A N   
669  C CA  . LEU A 77  ? 0.3137 0.4036 0.1806 0.0532  -0.0271 -0.0140 77  LEU A CA  
670  C C   . LEU A 77  ? 0.3301 0.4210 0.1955 0.0535  -0.0273 -0.0140 77  LEU A C   
671  O O   . LEU A 77  ? 0.3879 0.4790 0.2529 0.0542  -0.0271 -0.0146 77  LEU A O   
672  C CB  . LEU A 77  ? 0.3835 0.4710 0.2482 0.0533  -0.0274 -0.0152 77  LEU A CB  
673  C CG  . LEU A 77  ? 0.3931 0.4796 0.2565 0.0543  -0.0273 -0.0165 77  LEU A CG  
674  C CD1 . LEU A 77  ? 0.3670 0.4546 0.2328 0.0547  -0.0267 -0.0164 77  LEU A CD1 
675  C CD2 . LEU A 77  ? 0.3251 0.4092 0.1871 0.0543  -0.0275 -0.0174 77  LEU A CD2 
676  N N   . GLU A 78  ? 0.3479 0.4391 0.2122 0.0529  -0.0277 -0.0134 78  GLU A N   
677  C CA  . GLU A 78  ? 0.3508 0.4430 0.2138 0.0531  -0.0279 -0.0133 78  GLU A CA  
678  C C   . GLU A 78  ? 0.3560 0.4505 0.2214 0.0533  -0.0275 -0.0125 78  GLU A C   
679  O O   . GLU A 78  ? 0.4353 0.5305 0.3001 0.0538  -0.0274 -0.0129 78  GLU A O   
680  C CB  . GLU A 78  ? 0.4409 0.5331 0.3025 0.0525  -0.0284 -0.0127 78  GLU A CB  
681  C CG  . GLU A 78  ? 0.6371 0.7300 0.4969 0.0528  -0.0287 -0.0129 78  GLU A CG  
682  C CD  . GLU A 78  ? 0.7676 0.8592 0.6250 0.0536  -0.0288 -0.0143 78  GLU A CD  
683  O OE1 . GLU A 78  ? 0.8092 0.8988 0.6653 0.0537  -0.0290 -0.0152 78  GLU A OE1 
684  O OE2 . GLU A 78  ? 0.7798 0.8723 0.6366 0.0541  -0.0288 -0.0146 78  GLU A OE2 
685  N N   . ALA A 79  ? 0.3255 0.4210 0.1936 0.0527  -0.0272 -0.0115 79  ALA A N   
686  C CA  . ALA A 79  ? 0.3448 0.4425 0.2153 0.0528  -0.0267 -0.0107 79  ALA A CA  
687  C C   . ALA A 79  ? 0.3366 0.4343 0.2078 0.0536  -0.0263 -0.0115 79  ALA A C   
688  O O   . ALA A 79  ? 0.3361 0.4353 0.2084 0.0540  -0.0260 -0.0112 79  ALA A O   
689  C CB  . ALA A 79  ? 0.2579 0.3565 0.1312 0.0521  -0.0265 -0.0095 79  ALA A CB  
690  N N   . ILE A 80  ? 0.2466 0.3426 0.1173 0.0540  -0.0262 -0.0124 80  ILE A N   
691  C CA  . ILE A 80  ? 0.2460 0.3418 0.1173 0.0548  -0.0258 -0.0132 80  ILE A CA  
692  C C   . ILE A 80  ? 0.3140 0.4094 0.1828 0.0555  -0.0261 -0.0143 80  ILE A C   
693  O O   . ILE A 80  ? 0.3078 0.4039 0.1770 0.0561  -0.0258 -0.0146 80  ILE A O   
694  C CB  . ILE A 80  ? 0.3080 0.4022 0.1797 0.0548  -0.0257 -0.0138 80  ILE A CB  
695  C CG1 . ILE A 80  ? 0.4154 0.5103 0.2901 0.0542  -0.0254 -0.0128 80  ILE A CG1 
696  C CG2 . ILE A 80  ? 0.3248 0.4185 0.1965 0.0557  -0.0254 -0.0149 80  ILE A CG2 
697  C CD1 . ILE A 80  ? 0.4055 0.5020 0.2829 0.0544  -0.0248 -0.0124 80  ILE A CD1 
698  N N   . ARG A 81  ? 0.2688 0.3627 0.1348 0.0554  -0.0266 -0.0148 81  ARG A N   
699  C CA  . ARG A 81  ? 0.3179 0.4111 0.1813 0.0561  -0.0268 -0.0160 81  ARG A CA  
700  C C   . ARG A 81  ? 0.3828 0.4777 0.2460 0.0563  -0.0269 -0.0156 81  ARG A C   
701  O O   . ARG A 81  ? 0.4223 0.5173 0.2846 0.0570  -0.0268 -0.0163 81  ARG A O   
702  C CB  . ARG A 81  ? 0.3216 0.4129 0.1823 0.0559  -0.0274 -0.0166 81  ARG A CB  
703  C CG  . ARG A 81  ? 0.4685 0.5587 0.3264 0.0566  -0.0277 -0.0178 81  ARG A CG  
704  C CD  . ARG A 81  ? 0.5871 0.6756 0.4422 0.0564  -0.0283 -0.0183 81  ARG A CD  
705  N NE  . ARG A 81  ? 0.6868 0.7734 0.5418 0.0562  -0.0283 -0.0188 81  ARG A NE  
706  C CZ  . ARG A 81  ? 0.7905 0.8756 0.6444 0.0568  -0.0283 -0.0200 81  ARG A CZ  
707  N NH1 . ARG A 81  ? 0.7728 0.8579 0.6255 0.0576  -0.0282 -0.0208 81  ARG A NH1 
708  N NH2 . ARG A 81  ? 0.8045 0.8879 0.6583 0.0566  -0.0283 -0.0204 81  ARG A NH2 
709  N N   . LYS A 82  ? 0.3290 0.4252 0.1929 0.0556  -0.0270 -0.0144 82  LYS A N   
710  C CA  . LYS A 82  ? 0.3561 0.4539 0.2194 0.0557  -0.0271 -0.0141 82  LYS A CA  
711  C C   . LYS A 82  ? 0.3833 0.4826 0.2483 0.0563  -0.0266 -0.0140 82  LYS A C   
712  O O   . LYS A 82  ? 0.2953 0.3953 0.1628 0.0562  -0.0261 -0.0135 82  LYS A O   
713  C CB  . LYS A 82  ? 0.3133 0.4123 0.1774 0.0549  -0.0273 -0.0127 82  LYS A CB  
714  C CG  . LYS A 82  ? 0.4391 0.5370 0.3009 0.0544  -0.0278 -0.0127 82  LYS A CG  
715  C CD  . LYS A 82  ? 0.4348 0.5341 0.2978 0.0536  -0.0279 -0.0113 82  LYS A CD  
716  C CE  . LYS A 82  ? 0.4501 0.5483 0.3115 0.0530  -0.0284 -0.0112 82  LYS A CE  
717  N NZ  . LYS A 82  ? 0.4522 0.5519 0.3150 0.0521  -0.0285 -0.0098 82  LYS A NZ  
718  N N   . ASP A 83  ? 0.4472 0.5471 0.3108 0.0568  -0.0267 -0.0143 83  ASP A N   
719  C CA  . ASP A 83  ? 0.3590 0.4608 0.2241 0.0571  -0.0263 -0.0140 83  ASP A CA  
720  C C   . ASP A 83  ? 0.3438 0.4475 0.2115 0.0564  -0.0261 -0.0125 83  ASP A C   
721  O O   . ASP A 83  ? 0.3002 0.4041 0.1674 0.0558  -0.0265 -0.0118 83  ASP A O   
722  C CB  . ASP A 83  ? 0.3586 0.4609 0.2217 0.0576  -0.0266 -0.0145 83  ASP A CB  
723  C CG  . ASP A 83  ? 0.4028 0.5067 0.2672 0.0581  -0.0261 -0.0144 83  ASP A CG  
724  O OD1 . ASP A 83  ? 0.3434 0.4492 0.2100 0.0578  -0.0259 -0.0133 83  ASP A OD1 
725  O OD2 . ASP A 83  ? 0.4121 0.5154 0.2753 0.0589  -0.0261 -0.0154 83  ASP A OD2 
726  N N   . PRO A 84  ? 0.3004 0.4054 0.1707 0.0565  -0.0256 -0.0120 84  PRO A N   
727  C CA  . PRO A 84  ? 0.2474 0.3541 0.1202 0.0559  -0.0254 -0.0106 84  PRO A CA  
728  C C   . PRO A 84  ? 0.3193 0.4274 0.1914 0.0555  -0.0256 -0.0098 84  PRO A C   
729  O O   . PRO A 84  ? 0.2573 0.3664 0.1307 0.0548  -0.0257 -0.0087 84  PRO A O   
730  C CB  . PRO A 84  ? 0.3112 0.4190 0.1864 0.0563  -0.0248 -0.0104 84  PRO A CB  
731  C CG  . PRO A 84  ? 0.2494 0.3556 0.1240 0.0569  -0.0247 -0.0117 84  PRO A CG  
732  C CD  . PRO A 84  ? 0.3844 0.4891 0.2556 0.0572  -0.0252 -0.0127 84  PRO A CD  
733  N N   . ASP A 85  ? 0.3249 0.4333 0.1952 0.0561  -0.0258 -0.0104 85  ASP A N   
734  C CA  . ASP A 85  ? 0.3539 0.4634 0.2233 0.0558  -0.0261 -0.0098 85  ASP A CA  
735  C C   . ASP A 85  ? 0.2845 0.3932 0.1524 0.0551  -0.0266 -0.0095 85  ASP A C   
736  O O   . ASP A 85  ? 0.3311 0.4410 0.1989 0.0547  -0.0268 -0.0087 85  ASP A O   
737  C CB  . ASP A 85  ? 0.3906 0.5001 0.2579 0.0565  -0.0262 -0.0107 85  ASP A CB  
738  C CG  . ASP A 85  ? 0.4206 0.5315 0.2895 0.0571  -0.0257 -0.0108 85  ASP A CG  
739  O OD1 . ASP A 85  ? 0.4271 0.5392 0.2987 0.0569  -0.0253 -0.0100 85  ASP A OD1 
740  O OD2 . ASP A 85  ? 0.4912 0.6020 0.3586 0.0578  -0.0258 -0.0117 85  ASP A OD2 
741  N N   . ASP A 86  ? 0.2494 0.3561 0.1160 0.0551  -0.0269 -0.0102 86  ASP A N   
742  C CA  . ASP A 86  ? 0.4070 0.5128 0.2720 0.0544  -0.0274 -0.0099 86  ASP A CA  
743  C C   . ASP A 86  ? 0.3857 0.4913 0.2526 0.0537  -0.0273 -0.0091 86  ASP A C   
744  O O   . ASP A 86  ? 0.3560 0.4607 0.2217 0.0531  -0.0277 -0.0089 86  ASP A O   
745  C CB  . ASP A 86  ? 0.4384 0.5421 0.3004 0.0548  -0.0277 -0.0112 86  ASP A CB  
746  C CG  . ASP A 86  ? 0.5031 0.6070 0.3631 0.0555  -0.0279 -0.0119 86  ASP A CG  
747  O OD1 . ASP A 86  ? 0.6108 0.7162 0.4707 0.0553  -0.0280 -0.0112 86  ASP A OD1 
748  O OD2 . ASP A 86  ? 0.5392 0.6419 0.3977 0.0561  -0.0279 -0.0131 86  ASP A OD2 
749  N N   . LEU A 87  ? 0.2804 0.3869 0.1501 0.0537  -0.0268 -0.0086 87  LEU A N   
750  C CA  . LEU A 87  ? 0.2472 0.3535 0.1187 0.0530  -0.0267 -0.0078 87  LEU A CA  
751  C C   . LEU A 87  ? 0.3244 0.4321 0.1968 0.0522  -0.0268 -0.0065 87  LEU A C   
752  O O   . LEU A 87  ? 0.2670 0.3766 0.1405 0.0521  -0.0267 -0.0058 87  LEU A O   
753  C CB  . LEU A 87  ? 0.2455 0.3524 0.1198 0.0532  -0.0261 -0.0077 87  LEU A CB  
754  C CG  . LEU A 87  ? 0.2955 0.4007 0.1693 0.0538  -0.0259 -0.0089 87  LEU A CG  
755  C CD1 . LEU A 87  ? 0.2442 0.3503 0.1208 0.0540  -0.0253 -0.0087 87  LEU A CD1 
756  C CD2 . LEU A 87  ? 0.3184 0.4217 0.1913 0.0534  -0.0262 -0.0092 87  LEU A CD2 
757  N N   . GLU A 88  ? 0.2474 0.3543 0.1194 0.0515  -0.0272 -0.0061 88  GLU A N   
758  C CA  . GLU A 88  ? 0.3171 0.4252 0.1903 0.0507  -0.0272 -0.0048 88  GLU A CA  
759  C C   . GLU A 88  ? 0.2799 0.3893 0.1564 0.0504  -0.0267 -0.0039 88  GLU A C   
760  O O   . GLU A 88  ? 0.3200 0.4288 0.1978 0.0507  -0.0264 -0.0043 88  GLU A O   
761  C CB  . GLU A 88  ? 0.2545 0.3612 0.1265 0.0500  -0.0277 -0.0047 88  GLU A CB  
762  C CG  . GLU A 88  ? 0.3046 0.4101 0.1733 0.0502  -0.0282 -0.0055 88  GLU A CG  
763  C CD  . GLU A 88  ? 0.4191 0.5227 0.2864 0.0497  -0.0286 -0.0058 88  GLU A CD  
764  O OE1 . GLU A 88  ? 0.4471 0.5494 0.3117 0.0499  -0.0290 -0.0066 88  GLU A OE1 
765  O OE2 . GLU A 88  ? 0.4248 0.5283 0.2938 0.0492  -0.0285 -0.0052 88  GLU A OE2 
766  N N   . LYS A 89  ? 0.2446 0.3558 0.1227 0.0499  -0.0267 -0.0026 89  LYS A N   
767  C CA  . LYS A 89  ? 0.3456 0.4580 0.2269 0.0496  -0.0262 -0.0017 89  LYS A CA  
768  C C   . LYS A 89  ? 0.3942 0.5053 0.2763 0.0492  -0.0262 -0.0016 89  LYS A C   
769  O O   . LYS A 89  ? 0.3291 0.4404 0.2135 0.0492  -0.0257 -0.0015 89  LYS A O   
770  C CB  . LYS A 89  ? 0.3927 0.5071 0.2754 0.0490  -0.0262 -0.0003 89  LYS A CB  
771  C CG  . LYS A 89  ? 0.4742 0.5900 0.3603 0.0487  -0.0257 0.0007  89  LYS A CG  
772  C CD  . LYS A 89  ? 0.6725 0.7901 0.5599 0.0480  -0.0258 0.0021  89  LYS A CD  
773  C CE  . LYS A 89  ? 0.7370 0.8563 0.6275 0.0480  -0.0253 0.0029  89  LYS A CE  
774  N NZ  . LYS A 89  ? 0.7497 0.8683 0.6419 0.0482  -0.0249 0.0026  89  LYS A NZ  
775  N N   . GLU A 90  ? 0.3062 0.4160 0.1866 0.0487  -0.0266 -0.0018 90  GLU A N   
776  C CA  . GLU A 90  ? 0.3542 0.4626 0.2351 0.0484  -0.0267 -0.0018 90  GLU A CA  
777  C C   . GLU A 90  ? 0.3449 0.4517 0.2253 0.0490  -0.0265 -0.0031 90  GLU A C   
778  O O   . GLU A 90  ? 0.3166 0.4229 0.1987 0.0489  -0.0262 -0.0030 90  GLU A O   
779  C CB  . GLU A 90  ? 0.4023 0.5097 0.2812 0.0478  -0.0272 -0.0018 90  GLU A CB  
780  C CG  . GLU A 90  ? 0.5889 0.6944 0.4675 0.0475  -0.0273 -0.0022 90  GLU A CG  
781  C CD  . GLU A 90  ? 0.6941 0.7990 0.5713 0.0468  -0.0278 -0.0018 90  GLU A CD  
782  O OE1 . GLU A 90  ? 0.6671 0.7726 0.5429 0.0467  -0.0282 -0.0015 90  GLU A OE1 
783  O OE2 . GLU A 90  ? 0.6931 0.7970 0.5708 0.0464  -0.0279 -0.0017 90  GLU A OE2 
784  N N   . GLU A 91  ? 0.2796 0.3857 0.1579 0.0497  -0.0266 -0.0042 91  GLU A N   
785  C CA  . GLU A 91  ? 0.2832 0.3877 0.1610 0.0503  -0.0264 -0.0053 91  GLU A CA  
786  C C   . GLU A 91  ? 0.3069 0.4125 0.1872 0.0507  -0.0258 -0.0053 91  GLU A C   
787  O O   . GLU A 91  ? 0.2840 0.3887 0.1652 0.0509  -0.0255 -0.0057 91  GLU A O   
788  C CB  . GLU A 91  ? 0.3280 0.4315 0.2029 0.0510  -0.0267 -0.0066 91  GLU A CB  
789  C CG  . GLU A 91  ? 0.3159 0.4180 0.1881 0.0506  -0.0273 -0.0069 91  GLU A CG  
790  C CD  . GLU A 91  ? 0.3793 0.4805 0.2486 0.0512  -0.0276 -0.0080 91  GLU A CD  
791  O OE1 . GLU A 91  ? 0.4261 0.5254 0.2933 0.0514  -0.0279 -0.0089 91  GLU A OE1 
792  O OE2 . GLU A 91  ? 0.3606 0.4631 0.2297 0.0516  -0.0276 -0.0079 91  GLU A OE2 
793  N N   . VAL A 92  ? 0.2807 0.3883 0.1622 0.0509  -0.0256 -0.0046 92  VAL A N   
794  C CA  . VAL A 92  ? 0.3050 0.4137 0.1890 0.0512  -0.0250 -0.0044 92  VAL A CA  
795  C C   . VAL A 92  ? 0.3616 0.4706 0.2482 0.0506  -0.0247 -0.0036 92  VAL A C   
796  O O   . VAL A 92  ? 0.3260 0.4346 0.2141 0.0509  -0.0243 -0.0039 92  VAL A O   
797  C CB  . VAL A 92  ? 0.3276 0.4384 0.2124 0.0513  -0.0249 -0.0038 92  VAL A CB  
798  C CG1 . VAL A 92  ? 0.3489 0.4611 0.2367 0.0514  -0.0243 -0.0032 92  VAL A CG1 
799  C CG2 . VAL A 92  ? 0.2589 0.3694 0.1414 0.0521  -0.0250 -0.0048 92  VAL A CG2 
800  N N   . GLU A 93  ? 0.2966 0.4062 0.1839 0.0498  -0.0249 -0.0025 93  GLU A N   
801  C CA  . GLU A 93  ? 0.3211 0.4309 0.2107 0.0492  -0.0247 -0.0017 93  GLU A CA  
802  C C   . GLU A 93  ? 0.3148 0.4226 0.2041 0.0492  -0.0247 -0.0024 93  GLU A C   
803  O O   . GLU A 93  ? 0.3257 0.4336 0.2172 0.0491  -0.0243 -0.0022 93  GLU A O   
804  C CB  . GLU A 93  ? 0.3116 0.4222 0.2015 0.0484  -0.0250 -0.0005 93  GLU A CB  
805  C CG  . GLU A 93  ? 0.5054 0.6183 0.3967 0.0482  -0.0249 0.0005  93  GLU A CG  
806  C CD  . GLU A 93  ? 0.6781 0.7916 0.5693 0.0474  -0.0252 0.0016  93  GLU A CD  
807  O OE1 . GLU A 93  ? 0.7245 0.8367 0.6138 0.0470  -0.0257 0.0014  93  GLU A OE1 
808  O OE2 . GLU A 93  ? 0.7166 0.8320 0.6097 0.0470  -0.0251 0.0027  93  GLU A OE2 
809  N N   . LYS A 94  ? 0.3049 0.4110 0.1915 0.0493  -0.0252 -0.0032 94  LYS A N   
810  C CA  . LYS A 94  ? 0.3307 0.4348 0.2168 0.0493  -0.0252 -0.0040 94  LYS A CA  
811  C C   . LYS A 94  ? 0.3226 0.4261 0.2092 0.0500  -0.0248 -0.0049 94  LYS A C   
812  O O   . LYS A 94  ? 0.3468 0.4495 0.2346 0.0500  -0.0245 -0.0051 94  LYS A O   
813  C CB  . LYS A 94  ? 0.3709 0.4733 0.2539 0.0492  -0.0258 -0.0047 94  LYS A CB  
814  C CG  . LYS A 94  ? 0.4903 0.5930 0.3725 0.0485  -0.0262 -0.0039 94  LYS A CG  
815  C CD  . LYS A 94  ? 0.5723 0.6763 0.4571 0.0477  -0.0260 -0.0025 94  LYS A CD  
816  C CE  . LYS A 94  ? 0.6205 0.7251 0.5046 0.0470  -0.0265 -0.0016 94  LYS A CE  
817  N NZ  . LYS A 94  ? 0.6013 0.7081 0.4866 0.0469  -0.0263 -0.0007 94  LYS A NZ  
818  N N   . LEU A 95  ? 0.2725 0.3764 0.1582 0.0507  -0.0247 -0.0055 95  LEU A N   
819  C CA  . LEU A 95  ? 0.2705 0.3740 0.1566 0.0515  -0.0243 -0.0064 95  LEU A CA  
820  C C   . LEU A 95  ? 0.2872 0.3921 0.1767 0.0514  -0.0238 -0.0057 95  LEU A C   
821  O O   . LEU A 95  ? 0.2462 0.3503 0.1367 0.0516  -0.0234 -0.0061 95  LEU A O   
822  C CB  . LEU A 95  ? 0.3083 0.4122 0.1929 0.0522  -0.0244 -0.0071 95  LEU A CB  
823  C CG  . LEU A 95  ? 0.4768 0.5803 0.3617 0.0530  -0.0240 -0.0081 95  LEU A CG  
824  C CD1 . LEU A 95  ? 0.5313 0.6325 0.4150 0.0532  -0.0241 -0.0091 95  LEU A CD1 
825  C CD2 . LEU A 95  ? 0.5427 0.6466 0.4258 0.0537  -0.0241 -0.0087 95  LEU A CD2 
826  N N   . ILE A 96  ? 0.2743 0.3812 0.1654 0.0511  -0.0236 -0.0045 96  ILE A N   
827  C CA  . ILE A 96  ? 0.3349 0.4431 0.2292 0.0510  -0.0231 -0.0038 96  ILE A CA  
828  C C   . ILE A 96  ? 0.3095 0.4169 0.2052 0.0504  -0.0230 -0.0034 96  ILE A C   
829  O O   . ILE A 96  ? 0.3454 0.4528 0.2430 0.0506  -0.0225 -0.0034 96  ILE A O   
830  C CB  . ILE A 96  ? 0.2770 0.3875 0.1726 0.0506  -0.0230 -0.0026 96  ILE A CB  
831  C CG1 . ILE A 96  ? 0.4712 0.5825 0.3659 0.0513  -0.0230 -0.0030 96  ILE A CG1 
832  C CG2 . ILE A 96  ? 0.3142 0.4260 0.2131 0.0503  -0.0225 -0.0015 96  ILE A CG2 
833  C CD1 . ILE A 96  ? 0.5052 0.6168 0.4011 0.0520  -0.0224 -0.0035 96  ILE A CD1 
834  N N   . GLU A 97  ? 0.3295 0.4364 0.2244 0.0497  -0.0234 -0.0030 97  GLU A N   
835  C CA  . GLU A 97  ? 0.3513 0.4576 0.2477 0.0492  -0.0233 -0.0025 97  GLU A CA  
836  C C   . GLU A 97  ? 0.3215 0.4256 0.2170 0.0495  -0.0233 -0.0036 97  GLU A C   
837  O O   . GLU A 97  ? 0.2944 0.3983 0.1918 0.0493  -0.0230 -0.0034 97  GLU A O   
838  C CB  . GLU A 97  ? 0.3984 0.5047 0.2940 0.0484  -0.0238 -0.0017 97  GLU A CB  
839  C CG  . GLU A 97  ? 0.6108 0.7192 0.5083 0.0479  -0.0237 -0.0003 97  GLU A CG  
840  C CD  . GLU A 97  ? 0.7748 0.8842 0.6755 0.0475  -0.0232 0.0006  97  GLU A CD  
841  O OE1 . GLU A 97  ? 0.8070 0.9181 0.7093 0.0471  -0.0231 0.0018  97  GLU A OE1 
842  O OE2 . GLU A 97  ? 0.7962 0.9046 0.6978 0.0476  -0.0229 0.0001  97  GLU A OE2 
843  N N   . PHE A 98  ? 0.2581 0.3609 0.1509 0.0499  -0.0236 -0.0047 98  PHE A N   
844  C CA  . PHE A 98  ? 0.2843 0.3851 0.1763 0.0503  -0.0236 -0.0059 98  PHE A CA  
845  C C   . PHE A 98  ? 0.3315 0.4327 0.2253 0.0508  -0.0230 -0.0062 98  PHE A C   
846  O O   . PHE A 98  ? 0.2842 0.3844 0.1789 0.0509  -0.0227 -0.0065 98  PHE A O   
847  C CB  . PHE A 98  ? 0.3118 0.4111 0.2005 0.0507  -0.0240 -0.0070 98  PHE A CB  
848  C CG  . PHE A 98  ? 0.2378 0.3349 0.1253 0.0510  -0.0241 -0.0081 98  PHE A CG  
849  C CD1 . PHE A 98  ? 0.3653 0.4612 0.2524 0.0503  -0.0243 -0.0080 98  PHE A CD1 
850  C CD2 . PHE A 98  ? 0.2379 0.3341 0.1247 0.0517  -0.0239 -0.0092 98  PHE A CD2 
851  C CE1 . PHE A 98  ? 0.3401 0.4340 0.2261 0.0505  -0.0244 -0.0090 98  PHE A CE1 
852  C CE2 . PHE A 98  ? 0.3308 0.4251 0.2166 0.0519  -0.0239 -0.0102 98  PHE A CE2 
853  C CZ  . PHE A 98  ? 0.3300 0.4230 0.2153 0.0513  -0.0242 -0.0101 98  PHE A CZ  
854  N N   . THR A 99  ? 0.2934 0.3961 0.1878 0.0513  -0.0227 -0.0061 99  THR A N   
855  C CA  . THR A 99  ? 0.2849 0.3880 0.1811 0.0518  -0.0222 -0.0064 99  THR A CA  
856  C C   . THR A 99  ? 0.2561 0.3602 0.1555 0.0514  -0.0218 -0.0054 99  THR A C   
857  O O   . THR A 99  ? 0.3149 0.4183 0.2155 0.0516  -0.0214 -0.0057 99  THR A O   
858  C CB  . THR A 99  ? 0.2775 0.3821 0.1736 0.0524  -0.0220 -0.0064 99  THR A CB  
859  O OG1 . THR A 99  ? 0.2514 0.3552 0.1445 0.0528  -0.0225 -0.0072 99  THR A OG1 
860  C CG2 . THR A 99  ? 0.2317 0.3367 0.1294 0.0530  -0.0215 -0.0068 99  THR A CG2 
861  N N   . LYS A 100 ? 0.2683 0.3738 0.1689 0.0507  -0.0218 -0.0041 100 LYS A N   
862  C CA  . LYS A 100 ? 0.3219 0.4284 0.2255 0.0502  -0.0214 -0.0031 100 LYS A CA  
863  C C   . LYS A 100 ? 0.3128 0.4177 0.2168 0.0499  -0.0214 -0.0033 100 LYS A C   
864  O O   . LYS A 100 ? 0.3104 0.4154 0.2166 0.0498  -0.0210 -0.0031 100 LYS A O   
865  C CB  . LYS A 100 ? 0.3385 0.4466 0.2430 0.0496  -0.0216 -0.0018 100 LYS A CB  
866  C CG  . LYS A 100 ? 0.4239 0.5339 0.3289 0.0499  -0.0214 -0.0013 100 LYS A CG  
867  C CD  . LYS A 100 ? 0.4870 0.5988 0.3939 0.0491  -0.0214 0.0001  100 LYS A CD  
868  C CE  . LYS A 100 ? 0.5830 0.6965 0.4896 0.0493  -0.0215 0.0006  100 LYS A CE  
869  N NZ  . LYS A 100 ? 0.6385 0.7532 0.5465 0.0499  -0.0210 0.0005  100 LYS A NZ  
870  N N   . LEU A 101 ? 0.2727 0.3762 0.1745 0.0496  -0.0219 -0.0037 101 LEU A N   
871  C CA  . LEU A 101 ? 0.2696 0.3715 0.1715 0.0492  -0.0220 -0.0039 101 LEU A CA  
872  C C   . LEU A 101 ? 0.2415 0.3421 0.1434 0.0498  -0.0217 -0.0050 101 LEU A C   
873  O O   . LEU A 101 ? 0.2292 0.3292 0.1326 0.0496  -0.0215 -0.0049 101 LEU A O   
874  C CB  . LEU A 101 ? 0.3065 0.4071 0.2058 0.0489  -0.0226 -0.0042 101 LEU A CB  
875  C CG  . LEU A 101 ? 0.4443 0.5427 0.3427 0.0487  -0.0228 -0.0049 101 LEU A CG  
876  C CD1 . LEU A 101 ? 0.5165 0.6152 0.4171 0.0479  -0.0226 -0.0039 101 LEU A CD1 
877  C CD2 . LEU A 101 ? 0.4767 0.5737 0.3719 0.0487  -0.0234 -0.0055 101 LEU A CD2 
878  N N   . ASN A 102 ? 0.3157 0.4159 0.2161 0.0506  -0.0217 -0.0060 102 ASN A N   
879  C CA  . ASN A 102 ? 0.3610 0.4597 0.2610 0.0512  -0.0215 -0.0071 102 ASN A CA  
880  C C   . ASN A 102 ? 0.3568 0.4566 0.2588 0.0517  -0.0209 -0.0072 102 ASN A C   
881  O O   . ASN A 102 ? 0.3173 0.4161 0.2191 0.0523  -0.0207 -0.0081 102 ASN A O   
882  C CB  . ASN A 102 ? 0.2472 0.3445 0.1440 0.0517  -0.0219 -0.0084 102 ASN A CB  
883  C CG  . ASN A 102 ? 0.3226 0.4184 0.2174 0.0512  -0.0224 -0.0085 102 ASN A CG  
884  O OD1 . ASN A 102 ? 0.3424 0.4369 0.2373 0.0510  -0.0224 -0.0088 102 ASN A OD1 
885  N ND2 . ASN A 102 ? 0.2826 0.3786 0.1754 0.0511  -0.0229 -0.0085 102 ASN A ND2 
886  N N   . TYR A 103 ? 0.3168 0.3459 0.2363 0.0337  -0.0071 0.0217  103 TYR A N   
887  C CA  . TYR A 103 ? 0.3366 0.3745 0.2551 0.0297  -0.0086 0.0220  103 TYR A CA  
888  C C   . TYR A 103 ? 0.3259 0.3593 0.2423 0.0294  -0.0098 0.0235  103 TYR A C   
889  O O   . TYR A 103 ? 0.2900 0.3305 0.2060 0.0288  -0.0106 0.0230  103 TYR A O   
890  C CB  . TYR A 103 ? 0.3761 0.4171 0.2941 0.0233  -0.0096 0.0235  103 TYR A CB  
891  C CG  . TYR A 103 ? 0.4159 0.4659 0.3330 0.0184  -0.0112 0.0241  103 TYR A CG  
892  C CD1 . TYR A 103 ? 0.4744 0.5204 0.3892 0.0148  -0.0129 0.0263  103 TYR A CD1 
893  C CD2 . TYR A 103 ? 0.4946 0.5571 0.4130 0.0171  -0.0111 0.0223  103 TYR A CD2 
894  C CE1 . TYR A 103 ? 0.5611 0.6151 0.4748 0.0101  -0.0144 0.0269  103 TYR A CE1 
895  C CE2 . TYR A 103 ? 0.5754 0.6462 0.4928 0.0124  -0.0126 0.0229  103 TYR A CE2 
896  C CZ  . TYR A 103 ? 0.5940 0.6597 0.5097 0.0088  -0.0142 0.0250  103 TYR A CZ  
897  O OH  . TYR A 103 ? 0.5836 0.6557 0.5001 0.0039  -0.0154 0.0250  103 TYR A OH  
898  N N   . GLU A 104 ? 0.3637 0.3855 0.2788 0.0296  -0.0099 0.0254  104 GLU A N   
899  C CA  . GLU A 104 ? 0.3580 0.3749 0.2710 0.0290  -0.0111 0.0270  104 GLU A CA  
900  C C   . GLU A 104 ? 0.4071 0.4210 0.3203 0.0348  -0.0103 0.0259  104 GLU A C   
901  O O   . GLU A 104 ? 0.3894 0.4004 0.3009 0.0347  -0.0113 0.0269  104 GLU A O   
902  C CB  . GLU A 104 ? 0.3351 0.3409 0.2466 0.0264  -0.0118 0.0295  104 GLU A CB  
903  C CG  . GLU A 104 ? 0.4724 0.4802 0.3832 0.0201  -0.0130 0.0310  104 GLU A CG  
904  C CD  . GLU A 104 ? 0.5702 0.5858 0.4798 0.0153  -0.0148 0.0317  104 GLU A CD  
905  O OE1 . GLU A 104 ? 0.5969 0.6190 0.5067 0.0108  -0.0154 0.0320  104 GLU A OE1 
906  O OE2 . GLU A 104 ? 0.6238 0.6391 0.5322 0.0160  -0.0156 0.0320  104 GLU A OE2 
907  N N   . LYS A 105 ? 0.2620 0.2764 0.1769 0.0399  -0.0087 0.0239  105 LYS A N   
908  C CA  . LYS A 105 ? 0.2924 0.3036 0.2073 0.0456  -0.0079 0.0228  105 LYS A CA  
909  C C   . LYS A 105 ? 0.2978 0.3188 0.2129 0.0463  -0.0085 0.0215  105 LYS A C   
910  O O   . LYS A 105 ? 0.3090 0.3405 0.2252 0.0446  -0.0087 0.0201  105 LYS A O   
911  C CB  . LYS A 105 ? 0.2538 0.2628 0.1706 0.0506  -0.0060 0.0211  105 LYS A CB  
912  C CG  . LYS A 105 ? 0.2246 0.2238 0.1415 0.0503  -0.0053 0.0224  105 LYS A CG  
913  C CD  . LYS A 105 ? 0.2685 0.2666 0.1874 0.0546  -0.0034 0.0205  105 LYS A CD  
914  C CE  . LYS A 105 ? 0.3173 0.3055 0.2362 0.0542  -0.0028 0.0218  105 LYS A CE  
915  N NZ  . LYS A 105 ? 0.2834 0.2700 0.2041 0.0584  -0.0010 0.0201  105 LYS A NZ  
916  N N   . PRO A 106 ? 0.3145 0.3323 0.2283 0.0486  -0.0089 0.0218  106 PRO A N   
917  C CA  . PRO A 106 ? 0.2524 0.2794 0.1662 0.0493  -0.0096 0.0205  106 PRO A CA  
918  C C   . PRO A 106 ? 0.3413 0.3768 0.2572 0.0530  -0.0085 0.0176  106 PRO A C   
919  O O   . PRO A 106 ? 0.3548 0.4008 0.2711 0.0520  -0.0092 0.0164  106 PRO A O   
920  C CB  . PRO A 106 ? 0.2910 0.3108 0.2036 0.0523  -0.0098 0.0211  106 PRO A CB  
921  C CG  . PRO A 106 ? 0.3410 0.3490 0.2531 0.0504  -0.0098 0.0232  106 PRO A CG  
922  C CD  . PRO A 106 ? 0.3712 0.3771 0.2837 0.0504  -0.0089 0.0233  106 PRO A CD  
923  N N   . ILE A 107 ? 0.2657 0.2975 0.1831 0.0572  -0.0070 0.0164  107 ILE A N   
924  C CA  . ILE A 107 ? 0.2948 0.3348 0.2141 0.0608  -0.0060 0.0136  107 ILE A CA  
925  C C   . ILE A 107 ? 0.3374 0.3874 0.2581 0.0570  -0.0063 0.0127  107 ILE A C   
926  O O   . ILE A 107 ? 0.3093 0.3686 0.2315 0.0589  -0.0059 0.0103  107 ILE A O   
927  C CB  . ILE A 107 ? 0.2707 0.3039 0.1912 0.0663  -0.0044 0.0126  107 ILE A CB  
928  C CG1 . ILE A 107 ? 0.2357 0.2630 0.1567 0.0645  -0.0037 0.0135  107 ILE A CG1 
929  C CG2 . ILE A 107 ? 0.2432 0.2671 0.1624 0.0702  -0.0042 0.0134  107 ILE A CG2 
930  C CD1 . ILE A 107 ? 0.3226 0.3453 0.2452 0.0697  -0.0020 0.0121  107 ILE A CD1 
931  N N   . TYR A 108 ? 0.2579 0.3063 0.1779 0.0516  -0.0069 0.0146  108 TYR A N   
932  C CA  . TYR A 108 ? 0.2696 0.3276 0.1906 0.0474  -0.0072 0.0140  108 TYR A CA  
933  C C   . TYR A 108 ? 0.3105 0.3759 0.2303 0.0422  -0.0089 0.0149  108 TYR A C   
934  O O   . TYR A 108 ? 0.3366 0.4087 0.2567 0.0376  -0.0095 0.0152  108 TYR A O   
935  C CB  . TYR A 108 ? 0.2139 0.2661 0.1351 0.0446  -0.0069 0.0154  108 TYR A CB  
936  C CG  . TYR A 108 ? 0.3101 0.3620 0.2334 0.0482  -0.0052 0.0136  108 TYR A CG  
937  C CD1 . TYR A 108 ? 0.3377 0.3812 0.2614 0.0537  -0.0040 0.0130  108 TYR A CD1 
938  C CD2 . TYR A 108 ? 0.2833 0.3432 0.2082 0.0461  -0.0049 0.0124  108 TYR A CD2 
939  C CE1 . TYR A 108 ? 0.2841 0.3273 0.2098 0.0571  -0.0025 0.0113  108 TYR A CE1 
940  C CE2 . TYR A 108 ? 0.3027 0.3624 0.2296 0.0495  -0.0035 0.0107  108 TYR A CE2 
941  C CZ  . TYR A 108 ? 0.2768 0.3280 0.2041 0.0550  -0.0023 0.0101  108 TYR A CZ  
942  O OH  . TYR A 108 ? 0.2274 0.2783 0.1567 0.0582  -0.0009 0.0084  108 TYR A OH  
943  N N   . ARG A 109 ? 0.3648 0.4294 0.2831 0.0428  -0.0098 0.0155  109 ARG A N   
944  C CA  . ARG A 109 ? 0.4051 0.4763 0.3225 0.0379  -0.0114 0.0163  109 ARG A CA  
945  C C   . ARG A 109 ? 0.3137 0.3979 0.2337 0.0381  -0.0113 0.0136  109 ARG A C   
946  O O   . ARG A 109 ? 0.3805 0.4682 0.3010 0.0405  -0.0114 0.0123  109 ARG A O   
947  C CB  . ARG A 109 ? 0.4819 0.5469 0.3977 0.0381  -0.0123 0.0177  109 ARG A CB  
948  C CG  . ARG A 109 ? 0.6028 0.6592 0.5165 0.0334  -0.0135 0.0208  109 ARG A CG  
949  C CD  . ARG A 109 ? 0.7373 0.7823 0.6504 0.0356  -0.0125 0.0219  109 ARG A CD  
950  N NE  . ARG A 109 ? 0.8359 0.8726 0.7471 0.0315  -0.0136 0.0247  109 ARG A NE  
951  C CZ  . ARG A 109 ? 0.9157 0.9405 0.8260 0.0334  -0.0132 0.0260  109 ARG A CZ  
952  N NH1 . ARG A 109 ? 0.9608 0.9806 0.8720 0.0392  -0.0118 0.0249  109 ARG A NH1 
953  N NH2 . ARG A 109 ? 0.9293 0.9473 0.8381 0.0294  -0.0144 0.0284  109 ARG A NH2 
954  N N   . PHE A 110 ? 0.2967 0.3879 0.2182 0.0356  -0.0109 0.0127  110 PHE A N   
955  C CA  . PHE A 110 ? 0.3596 0.4635 0.2838 0.0340  -0.0110 0.0106  110 PHE A CA  
956  C C   . PHE A 110 ? 0.3604 0.4682 0.2849 0.0267  -0.0120 0.0119  110 PHE A C   
957  O O   . PHE A 110 ? 0.3524 0.4570 0.2763 0.0244  -0.0118 0.0131  110 PHE A O   
958  C CB  . PHE A 110 ? 0.3337 0.4434 0.2601 0.0381  -0.0096 0.0078  110 PHE A CB  
959  C CG  . PHE A 110 ? 0.2670 0.3720 0.1932 0.0455  -0.0086 0.0065  110 PHE A CG  
960  C CD1 . PHE A 110 ? 0.3267 0.4216 0.2512 0.0485  -0.0078 0.0074  110 PHE A CD1 
961  C CD2 . PHE A 110 ? 0.2679 0.3785 0.1955 0.0494  -0.0084 0.0042  110 PHE A CD2 
962  C CE1 . PHE A 110 ? 0.4036 0.4933 0.3287 0.0550  -0.0067 0.0061  110 PHE A CE1 
963  C CE2 . PHE A 110 ? 0.3659 0.4721 0.2933 0.0562  -0.0075 0.0029  110 PHE A CE2 
964  C CZ  . PHE A 110 ? 0.3856 0.4814 0.3114 0.0591  -0.0067 0.0039  110 PHE A CZ  
965  N N   . GLU A 111 ? 0.3929 0.5073 0.3183 0.0232  -0.0129 0.0118  111 GLU A N   
966  C CA  . GLU A 111 ? 0.3438 0.4612 0.2694 0.0162  -0.0139 0.0132  111 GLU A CA  
967  C C   . GLU A 111 ? 0.3029 0.4274 0.2307 0.0148  -0.0131 0.0119  111 GLU A C   
968  O O   . GLU A 111 ? 0.3182 0.4420 0.2458 0.0098  -0.0136 0.0134  111 GLU A O   
969  C CB  . GLU A 111 ? 0.3435 0.4671 0.2698 0.0130  -0.0149 0.0131  111 GLU A CB  
970  C CG  . GLU A 111 ? 0.5692 0.7056 0.4987 0.0131  -0.0143 0.0106  111 GLU A CG  
971  C CD  . GLU A 111 ? 0.7297 0.8697 0.6600 0.0175  -0.0141 0.0087  111 GLU A CD  
972  O OE1 . GLU A 111 ? 0.8252 0.9594 0.7544 0.0229  -0.0136 0.0083  111 GLU A OE1 
973  O OE2 . GLU A 111 ? 0.7771 0.9259 0.7093 0.0156  -0.0144 0.0077  111 GLU A OE2 
974  N N   . ARG A 112 ? 0.2732 0.4043 0.2033 0.0191  -0.0119 0.0092  112 ARG A N   
975  C CA  . ARG A 112 ? 0.2991 0.4369 0.2315 0.0183  -0.0111 0.0078  112 ARG A CA  
976  C C   . ARG A 112 ? 0.4178 0.5479 0.3488 0.0181  -0.0107 0.0091  112 ARG A C   
977  O O   . ARG A 112 ? 0.3715 0.5046 0.3034 0.0145  -0.0106 0.0094  112 ARG A O   
978  C CB  . ARG A 112 ? 0.2734 0.4187 0.2084 0.0237  -0.0100 0.0045  112 ARG A CB  
979  C CG  . ARG A 112 ? 0.2030 0.3561 0.1408 0.0233  -0.0091 0.0027  112 ARG A CG  
980  C CD  . ARG A 112 ? 0.3185 0.4802 0.2581 0.0170  -0.0098 0.0030  112 ARG A CD  
981  N NE  . ARG A 112 ? 0.3348 0.5051 0.2774 0.0171  -0.0089 0.0010  112 ARG A NE  
982  C CZ  . ARG A 112 ? 0.3743 0.5509 0.3185 0.0118  -0.0091 0.0013  112 ARG A CZ  
983  N NH1 . ARG A 112 ? 0.3663 0.5413 0.3093 0.0060  -0.0101 0.0037  112 ARG A NH1 
984  N NH2 . ARG A 112 ? 0.3524 0.5366 0.2994 0.0125  -0.0082 -0.0007 112 ARG A NH2 
985  N N   . ILE A 113 ? 0.2936 0.4136 0.2222 0.0220  -0.0104 0.0100  113 ILE A N   
986  C CA  . ILE A 113 ? 0.3230 0.4350 0.2502 0.0220  -0.0099 0.0115  113 ILE A CA  
987  C C   . ILE A 113 ? 0.3491 0.4572 0.2748 0.0153  -0.0112 0.0143  113 ILE A C   
988  O O   . ILE A 113 ? 0.3204 0.4278 0.2463 0.0125  -0.0110 0.0151  113 ILE A O   
989  C CB  . ILE A 113 ? 0.3422 0.4437 0.2673 0.0277  -0.0093 0.0120  113 ILE A CB  
990  C CG1 . ILE A 113 ? 0.3286 0.4329 0.2552 0.0343  -0.0079 0.0091  113 ILE A CG1 
991  C CG2 . ILE A 113 ? 0.3845 0.4757 0.3078 0.0264  -0.0092 0.0143  113 ILE A CG2 
992  C CD1 . ILE A 113 ? 0.4347 0.5269 0.3608 0.0394  -0.0069 0.0095  113 ILE A CD1 
993  N N   . ARG A 114 ? 0.3583 0.4636 0.2826 0.0127  -0.0124 0.0159  114 ARG A N   
994  C CA  . ARG A 114 ? 0.4080 0.5098 0.3311 0.0063  -0.0138 0.0185  114 ARG A CA  
995  C C   . ARG A 114 ? 0.3980 0.5091 0.3234 0.0014  -0.0139 0.0179  114 ARG A C   
996  O O   . ARG A 114 ? 0.4502 0.5587 0.3752 -0.0030 -0.0144 0.0195  114 ARG A O   
997  C CB  . ARG A 114 ? 0.5319 0.6299 0.4533 0.0048  -0.0151 0.0199  114 ARG A CB  
998  C CG  . ARG A 114 ? 0.6820 0.7705 0.6013 0.0097  -0.0149 0.0206  114 ARG A CG  
999  C CD  . ARG A 114 ? 0.7542 0.8363 0.6714 0.0072  -0.0164 0.0227  114 ARG A CD  
1000 N NE  . ARG A 114 ? 0.8576 0.9460 0.7756 0.0072  -0.0169 0.0216  114 ARG A NE  
1001 C CZ  . ARG A 114 ? 0.9019 0.9904 0.8198 0.0123  -0.0164 0.0203  114 ARG A CZ  
1002 N NH1 . ARG A 114 ? 0.8884 0.9708 0.8056 0.0178  -0.0153 0.0200  114 ARG A NH1 
1003 N NH2 . ARG A 114 ? 0.9028 0.9973 0.8215 0.0119  -0.0169 0.0194  114 ARG A NH2 
1004 N N   . GLU A 115 ? 0.4116 0.5335 0.3395 0.0021  -0.0135 0.0156  115 GLU A N   
1005 C CA  . GLU A 115 ? 0.3824 0.5138 0.3129 -0.0021 -0.0135 0.0149  115 GLU A CA  
1006 C C   . GLU A 115 ? 0.4534 0.5853 0.3848 -0.0015 -0.0125 0.0143  115 GLU A C   
1007 O O   . GLU A 115 ? 0.5537 0.6873 0.4858 -0.0061 -0.0127 0.0152  115 GLU A O   
1008 C CB  . GLU A 115 ? 0.3958 0.5387 0.3291 -0.0008 -0.0131 0.0124  115 GLU A CB  
1009 C CG  . GLU A 115 ? 0.4707 0.6159 0.4038 -0.0034 -0.0142 0.0131  115 GLU A CG  
1010 C CD  . GLU A 115 ? 0.5102 0.6650 0.4455 -0.0005 -0.0136 0.0104  115 GLU A CD  
1011 O OE1 . GLU A 115 ? 0.4848 0.6480 0.4229 0.0011  -0.0126 0.0082  115 GLU A OE1 
1012 O OE2 . GLU A 115 ? 0.6114 0.7654 0.5459 0.0004  -0.0142 0.0106  115 GLU A OE2 
1013 N N   . LEU A 116 ? 0.4027 0.5331 0.3343 0.0044  -0.0113 0.0127  116 LEU A N   
1014 C CA  . LEU A 116 ? 0.3662 0.4982 0.2990 0.0054  -0.0102 0.0117  116 LEU A CA  
1015 C C   . LEU A 116 ? 0.3192 0.4417 0.2498 0.0031  -0.0104 0.0141  116 LEU A C   
1016 O O   . LEU A 116 ? 0.3597 0.4843 0.2913 0.0009  -0.0101 0.0141  116 LEU A O   
1017 C CB  . LEU A 116 ? 0.3607 0.4934 0.2942 0.0126  -0.0088 0.0092  116 LEU A CB  
1018 C CG  . LEU A 116 ? 0.3261 0.4687 0.2622 0.0154  -0.0085 0.0064  116 LEU A CG  
1019 C CD1 . LEU A 116 ? 0.3129 0.4535 0.2491 0.0229  -0.0074 0.0043  116 LEU A CD1 
1020 C CD2 . LEU A 116 ? 0.3290 0.4829 0.2683 0.0126  -0.0082 0.0048  116 LEU A CD2 
1021 N N   . MET A 117 ? 0.3876 0.4995 0.3153 0.0038  -0.0110 0.0162  117 MET A N   
1022 C CA  . MET A 117 ? 0.4060 0.5083 0.3316 0.0015  -0.0114 0.0187  117 MET A CA  
1023 C C   . MET A 117 ? 0.5049 0.6077 0.4305 -0.0055 -0.0126 0.0205  117 MET A C   
1024 O O   . MET A 117 ? 0.5427 0.6391 0.4673 -0.0079 -0.0129 0.0223  117 MET A O   
1025 C CB  . MET A 117 ? 0.3994 0.4903 0.3221 0.0042  -0.0117 0.0204  117 MET A CB  
1026 C CG  . MET A 117 ? 0.4604 0.5484 0.3829 0.0115  -0.0103 0.0190  117 MET A CG  
1027 S SD  . MET A 117 ? 0.5331 0.6271 0.4584 0.0146  -0.0085 0.0162  117 MET A SD  
1028 C CE  . MET A 117 ? 0.4732 0.5542 0.3984 0.0150  -0.0077 0.0177  117 MET A CE  
1029 N N   . ASN A 118 ? 0.5925 0.7028 0.5196 -0.0088 -0.0134 0.0202  118 ASN A N   
1030 C CA  . ASN A 118 ? 0.6657 0.7769 0.5931 -0.0154 -0.0146 0.0219  118 ASN A CA  
1031 C C   . ASN A 118 ? 0.7129 0.8346 0.6432 -0.0183 -0.0141 0.0207  118 ASN A C   
1032 O O   . ASN A 118 ? 0.7191 0.8427 0.6500 -0.0238 -0.0150 0.0219  118 ASN A O   
1033 C CB  . ASN A 118 ? 0.6767 0.7881 0.6034 -0.0174 -0.0158 0.0227  118 ASN A CB  
1034 C CG  . ASN A 118 ? 0.6961 0.7956 0.6198 -0.0169 -0.0167 0.0248  118 ASN A CG  
1035 O OD1 . ASN A 118 ? 0.7373 0.8285 0.6596 -0.0188 -0.0172 0.0267  118 ASN A OD1 
1036 N ND2 . ASN A 118 ? 0.7008 0.7993 0.6235 -0.0142 -0.0170 0.0245  118 ASN A ND2 
1037 N N   . LYS A 119 ? 0.6829 0.8113 0.6152 -0.0148 -0.0128 0.0182  119 LYS A N   
1038 C CA  . LYS A 119 ? 0.6296 0.7681 0.5648 -0.0173 -0.0123 0.0169  119 LYS A CA  
1039 C C   . LYS A 119 ? 0.6300 0.7653 0.5652 -0.0176 -0.0117 0.0173  119 LYS A C   
1040 O O   . LYS A 119 ? 0.5897 0.7177 0.5232 -0.0138 -0.0111 0.0173  119 LYS A O   
1041 C CB  . LYS A 119 ? 0.6212 0.7698 0.5589 -0.0133 -0.0112 0.0138  119 LYS A CB  
1042 C CG  . LYS A 119 ? 0.6733 0.8275 0.6118 -0.0138 -0.0118 0.0132  119 LYS A CG  
1043 C CD  . LYS A 119 ? 0.6669 0.8319 0.6084 -0.0103 -0.0108 0.0101  119 LYS A CD  
1044 C CE  . LYS A 119 ? 0.6480 0.8187 0.5902 -0.0108 -0.0113 0.0095  119 LYS A CE  
1045 N NZ  . LYS A 119 ? 0.6318 0.8057 0.5745 -0.0174 -0.0123 0.0112  119 LYS A NZ  
1046 N N   . GLU A 120 ? 0.6404 0.7811 0.5774 -0.0222 -0.0118 0.0176  120 GLU A N   
1047 C CA  . GLU A 120 ? 0.6158 0.7535 0.5527 -0.0234 -0.0114 0.0181  120 GLU A CA  
1048 C C   . GLU A 120 ? 0.5606 0.7025 0.4990 -0.0186 -0.0099 0.0156  120 GLU A C   
1049 O O   . GLU A 120 ? 0.5988 0.7340 0.5359 -0.0161 -0.0092 0.0158  120 GLU A O   
1050 C CB  . GLU A 120 ? 0.6336 0.7766 0.5722 -0.0296 -0.0120 0.0191  120 GLU A CB  
1051 C CG  . GLU A 120 ? 0.6872 0.8272 0.6248 -0.0345 -0.0135 0.0214  120 GLU A CG  
1052 C CD  . GLU A 120 ? 0.7840 0.9252 0.7224 -0.0404 -0.0141 0.0230  120 GLU A CD  
1053 O OE1 . GLU A 120 ? 0.8098 0.9439 0.7471 -0.0412 -0.0142 0.0242  120 GLU A OE1 
1054 O OE2 . GLU A 120 ? 0.8129 0.9623 0.7532 -0.0443 -0.0144 0.0229  120 GLU A OE2 
1055 N N   . LYS A 121 ? 0.5212 0.6742 0.4625 -0.0174 -0.0092 0.0131  121 LYS A N   
1056 C CA  . LYS A 121 ? 0.5031 0.6611 0.4462 -0.0125 -0.0078 0.0103  121 LYS A CA  
1057 C C   . LYS A 121 ? 0.4220 0.5852 0.3662 -0.0082 -0.0075 0.0081  121 LYS A C   
1058 O O   . LYS A 121 ? 0.4558 0.6222 0.4002 -0.0100 -0.0082 0.0085  121 LYS A O   
1059 C CB  . LYS A 121 ? 0.5176 0.6851 0.4639 -0.0151 -0.0073 0.0091  121 LYS A CB  
1060 C CG  . LYS A 121 ? 0.6057 0.7684 0.5512 -0.0184 -0.0074 0.0107  121 LYS A CG  
1061 C CD  . LYS A 121 ? 0.6606 0.8297 0.6087 -0.0169 -0.0062 0.0086  121 LYS A CD  
1062 C CE  . LYS A 121 ? 0.6979 0.8595 0.6445 -0.0180 -0.0061 0.0100  121 LYS A CE  
1063 N NZ  . LYS A 121 ? 0.7114 0.8789 0.6605 -0.0163 -0.0049 0.0079  121 LYS A NZ  
1064 N N   . LEU A 122 ? 0.3992 0.5630 0.3441 -0.0023 -0.0063 0.0058  122 LEU A N   
1065 C CA  . LEU A 122 ? 0.3588 0.5272 0.3049 0.0025  -0.0059 0.0035  122 LEU A CA  
1066 C C   . LEU A 122 ? 0.3408 0.5201 0.2906 0.0046  -0.0050 0.0004  122 LEU A C   
1067 O O   . LEU A 122 ? 0.3261 0.5051 0.2767 0.0064  -0.0042 -0.0007 122 LEU A O   
1068 C CB  . LEU A 122 ? 0.2804 0.4397 0.2242 0.0084  -0.0054 0.0033  122 LEU A CB  
1069 C CG  . LEU A 122 ? 0.3659 0.5133 0.3058 0.0071  -0.0062 0.0064  122 LEU A CG  
1070 C CD1 . LEU A 122 ? 0.3967 0.5357 0.3347 0.0133  -0.0054 0.0060  122 LEU A CD1 
1071 C CD2 . LEU A 122 ? 0.2776 0.4260 0.2169 0.0042  -0.0075 0.0076  122 LEU A CD2 
1072 N N   . ASN A 123 ? 0.3571 0.5462 0.3094 0.0043  -0.0052 -0.0012 123 ASN A N   
1073 C CA  . ASN A 123 ? 0.3496 0.5492 0.3056 0.0070  -0.0044 -0.0044 123 ASN A CA  
1074 C C   . ASN A 123 ? 0.3170 0.5151 0.2732 0.0143  -0.0037 -0.0067 123 ASN A C   
1075 O O   . ASN A 123 ? 0.3168 0.5055 0.2702 0.0173  -0.0037 -0.0058 123 ASN A O   
1076 C CB  . ASN A 123 ? 0.3462 0.5571 0.3049 0.0035  -0.0048 -0.0050 123 ASN A CB  
1077 C CG  . ASN A 123 ? 0.4715 0.6817 0.4290 0.0034  -0.0055 -0.0044 123 ASN A CG  
1078 O OD1 . ASN A 123 ? 0.4207 0.6267 0.3770 0.0082  -0.0054 -0.0051 123 ASN A OD1 
1079 N ND2 . ASN A 123 ? 0.4828 0.6973 0.4408 -0.0021 -0.0062 -0.0030 123 ASN A ND2 
1080 N N   . ARG A 124 ? 0.2871 0.4944 0.2468 0.0175  -0.0031 -0.0098 124 ARG A N   
1081 C CA  . ARG A 124 ? 0.2262 0.4318 0.1863 0.0247  -0.0026 -0.0122 124 ARG A CA  
1082 C C   . ARG A 124 ? 0.2725 0.4758 0.2312 0.0271  -0.0030 -0.0121 124 ARG A C   
1083 O O   . ARG A 124 ? 0.2514 0.4470 0.2083 0.0321  -0.0027 -0.0123 124 ARG A O   
1084 C CB  . ARG A 124 ? 0.2635 0.4800 0.2278 0.0273  -0.0021 -0.0156 124 ARG A CB  
1085 C CG  . ARG A 124 ? 0.2141 0.4296 0.1793 0.0348  -0.0018 -0.0182 124 ARG A CG  
1086 C CD  . ARG A 124 ? 0.2655 0.4915 0.2350 0.0374  -0.0017 -0.0215 124 ARG A CD  
1087 N NE  . ARG A 124 ? 0.3132 0.5377 0.2834 0.0444  -0.0017 -0.0238 124 ARG A NE  
1088 C CZ  . ARG A 124 ? 0.2718 0.4993 0.2426 0.0471  -0.0022 -0.0249 124 ARG A CZ  
1089 N NH1 . ARG A 124 ? 0.2431 0.4755 0.2139 0.0432  -0.0027 -0.0239 124 ARG A NH1 
1090 N NH2 . ARG A 124 ? 0.2701 0.4953 0.2415 0.0535  -0.0024 -0.0268 124 ARG A NH2 
1091 N N   . GLU A 125 ? 0.2456 0.4552 0.2052 0.0236  -0.0037 -0.0116 125 GLU A N   
1092 C CA  . GLU A 125 ? 0.3028 0.5108 0.2613 0.0259  -0.0042 -0.0116 125 GLU A CA  
1093 C C   . GLU A 125 ? 0.3439 0.5395 0.2981 0.0252  -0.0046 -0.0087 125 GLU A C   
1094 O O   . GLU A 125 ? 0.3392 0.5293 0.2918 0.0294  -0.0046 -0.0089 125 GLU A O   
1095 C CB  . GLU A 125 ? 0.3712 0.5889 0.3316 0.0220  -0.0048 -0.0118 125 GLU A CB  
1096 C CG  . GLU A 125 ? 0.5348 0.7651 0.4995 0.0242  -0.0044 -0.0151 125 GLU A CG  
1097 C CD  . GLU A 125 ? 0.6211 0.8559 0.5882 0.0240  -0.0038 -0.0164 125 GLU A CD  
1098 O OE1 . GLU A 125 ? 0.5446 0.7783 0.5111 0.0190  -0.0038 -0.0146 125 GLU A OE1 
1099 O OE2 . GLU A 125 ? 0.6552 0.8943 0.6247 0.0289  -0.0034 -0.0192 125 GLU A OE2 
1100 N N   . GLU A 126 ? 0.2709 0.4618 0.2233 0.0200  -0.0050 -0.0060 126 GLU A N   
1101 C CA  . GLU A 126 ? 0.3037 0.4827 0.2521 0.0190  -0.0056 -0.0032 126 GLU A CA  
1102 C C   . GLU A 126 ? 0.3026 0.4723 0.2492 0.0242  -0.0047 -0.0033 126 GLU A C   
1103 O O   . GLU A 126 ? 0.2720 0.4331 0.2159 0.0268  -0.0049 -0.0023 126 GLU A O   
1104 C CB  . GLU A 126 ? 0.3288 0.5055 0.2760 0.0120  -0.0063 -0.0004 126 GLU A CB  
1105 C CG  . GLU A 126 ? 0.3623 0.5452 0.3104 0.0069  -0.0073 0.0005  126 GLU A CG  
1106 C CD  . GLU A 126 ? 0.4076 0.5931 0.3563 0.0003  -0.0077 0.0021  126 GLU A CD  
1107 O OE1 . GLU A 126 ? 0.3646 0.5493 0.3138 -0.0001 -0.0071 0.0020  126 GLU A OE1 
1108 O OE2 . GLU A 126 ? 0.4362 0.6247 0.3850 -0.0043 -0.0085 0.0034  126 GLU A OE2 
1109 N N   . LEU A 127 ? 0.2608 0.4318 0.2087 0.0257  -0.0038 -0.0047 127 LEU A N   
1110 C CA  . LEU A 127 ? 0.2241 0.3867 0.1706 0.0310  -0.0029 -0.0051 127 LEU A CA  
1111 C C   . LEU A 127 ? 0.3098 0.4723 0.2569 0.0377  -0.0024 -0.0073 127 LEU A C   
1112 O O   . LEU A 127 ? 0.2484 0.4014 0.1932 0.0419  -0.0020 -0.0068 127 LEU A O   
1113 C CB  . LEU A 127 ? 0.2318 0.3968 0.1801 0.0312  -0.0020 -0.0063 127 LEU A CB  
1114 C CG  . LEU A 127 ? 0.3733 0.5346 0.3202 0.0258  -0.0022 -0.0039 127 LEU A CG  
1115 C CD1 . LEU A 127 ? 0.2718 0.4392 0.2213 0.0254  -0.0015 -0.0056 127 LEU A CD1 
1116 C CD2 . LEU A 127 ? 0.4122 0.5602 0.3554 0.0270  -0.0020 -0.0016 127 LEU A CD2 
1117 N N   . LEU A 128 ? 0.2102 0.3831 0.1605 0.0391  -0.0025 -0.0098 128 LEU A N   
1118 C CA  . LEU A 128 ? 0.2397 0.4128 0.1905 0.0452  -0.0023 -0.0119 128 LEU A CA  
1119 C C   . LEU A 128 ? 0.1892 0.3551 0.1370 0.0457  -0.0029 -0.0100 128 LEU A C   
1120 O O   . LEU A 128 ? 0.2262 0.3853 0.1727 0.0510  -0.0025 -0.0104 128 LEU A O   
1121 C CB  . LEU A 128 ? 0.2227 0.4085 0.1774 0.0457  -0.0026 -0.0145 128 LEU A CB  
1122 C CG  . LEU A 128 ? 0.2272 0.4183 0.1851 0.0498  -0.0020 -0.0176 128 LEU A CG  
1123 C CD1 . LEU A 128 ? 0.2472 0.4514 0.2089 0.0497  -0.0025 -0.0200 128 LEU A CD1 
1124 C CD2 . LEU A 128 ? 0.2249 0.4082 0.1819 0.0568  -0.0014 -0.0187 128 LEU A CD2 
1125 N N   . ASP A 129 ? 0.2782 0.4453 0.2251 0.0401  -0.0039 -0.0079 129 ASP A N   
1126 C CA  . ASP A 129 ? 0.3040 0.4643 0.2480 0.0401  -0.0046 -0.0060 129 ASP A CA  
1127 C C   . ASP A 129 ? 0.3165 0.4637 0.2570 0.0412  -0.0043 -0.0037 129 ASP A C   
1128 O O   . ASP A 129 ? 0.2801 0.4200 0.2187 0.0449  -0.0043 -0.0032 129 ASP A O   
1129 C CB  . ASP A 129 ? 0.2550 0.4193 0.1989 0.0335  -0.0057 -0.0042 129 ASP A CB  
1130 C CG  . ASP A 129 ? 0.3469 0.5227 0.2938 0.0334  -0.0060 -0.0063 129 ASP A CG  
1131 O OD1 . ASP A 129 ? 0.3116 0.4927 0.2608 0.0382  -0.0054 -0.0091 129 ASP A OD1 
1132 O OD2 . ASP A 129 ? 0.3473 0.5264 0.2941 0.0287  -0.0069 -0.0050 129 ASP A OD2 
1133 N N   . LEU A 130 ? 0.2553 0.3995 0.1952 0.0381  -0.0041 -0.0023 130 LEU A N   
1134 C CA  . LEU A 130 ? 0.2510 0.3829 0.1877 0.0392  -0.0038 -0.0002 130 LEU A CA  
1135 C C   . LEU A 130 ? 0.1957 0.3218 0.1326 0.0463  -0.0025 -0.0018 130 LEU A C   
1136 O O   . LEU A 130 ? 0.2272 0.3422 0.1631 0.0488  -0.0023 -0.0005 130 LEU A O   
1137 C CB  . LEU A 130 ? 0.2810 0.4113 0.2173 0.0345  -0.0038 0.0014  130 LEU A CB  
1138 C CG  . LEU A 130 ? 0.3346 0.4516 0.2687 0.0337  -0.0038 0.0042  130 LEU A CG  
1139 C CD1 . LEU A 130 ? 0.3684 0.4800 0.3000 0.0315  -0.0050 0.0067  130 LEU A CD1 
1140 C CD2 . LEU A 130 ? 0.2735 0.3900 0.2076 0.0290  -0.0038 0.0055  130 LEU A CD2 
1141 N N   . GLN A 131 ? 0.2067 0.3397 0.1459 0.0495  -0.0016 -0.0048 131 GLN A N   
1142 C CA  . GLN A 131 ? 0.1843 0.3117 0.1249 0.0561  -0.0004 -0.0065 131 GLN A CA  
1143 C C   . GLN A 131 ? 0.2352 0.3605 0.1752 0.0607  -0.0005 -0.0073 131 GLN A C   
1144 O O   . GLN A 131 ? 0.2238 0.3386 0.1634 0.0646  0.0001  -0.0067 131 GLN A O   
1145 C CB  . GLN A 131 ? 0.1441 0.2806 0.0873 0.0583  0.0004  -0.0097 131 GLN A CB  
1146 C CG  . GLN A 131 ? 0.1609 0.2985 0.1051 0.0550  0.0008  -0.0094 131 GLN A CG  
1147 C CD  . GLN A 131 ? 0.2440 0.3916 0.1920 0.0566  0.0012  -0.0125 131 GLN A CD  
1148 O OE1 . GLN A 131 ? 0.1875 0.3444 0.1378 0.0566  0.0005  -0.0142 131 GLN A OE1 
1149 N NE2 . GLN A 131 ? 0.1874 0.3328 0.1364 0.0582  0.0023  -0.0135 131 GLN A NE2 
1150 N N   . THR A 132 ? 0.2433 0.3783 0.1840 0.0601  -0.0014 -0.0085 132 THR A N   
1151 C CA  . THR A 132 ? 0.1917 0.3259 0.1323 0.0646  -0.0016 -0.0095 132 THR A CA  
1152 C C   . THR A 132 ? 0.2040 0.3296 0.1411 0.0635  -0.0022 -0.0067 132 THR A C   
1153 O O   . THR A 132 ? 0.2544 0.3730 0.1910 0.0681  -0.0019 -0.0068 132 THR A O   
1154 C CB  . THR A 132 ? 0.1690 0.3157 0.1127 0.0636  -0.0023 -0.0115 132 THR A CB  
1155 O OG1 . THR A 132 ? 0.2227 0.3777 0.1697 0.0636  -0.0019 -0.0137 132 THR A OG1 
1156 C CG2 . THR A 132 ? 0.1750 0.3215 0.1191 0.0692  -0.0024 -0.0131 132 THR A CG2 
1157 N N   . LEU A 133 ? 0.2116 0.3368 0.1474 0.0574  -0.0032 -0.0042 133 LEU A N   
1158 C CA  . LEU A 133 ? 0.2237 0.3404 0.1569 0.0561  -0.0039 -0.0015 133 LEU A CA  
1159 C C   . LEU A 133 ? 0.2576 0.3600 0.1901 0.0581  -0.0031 0.0001  133 LEU A C   
1160 O O   . LEU A 133 ? 0.2527 0.3470 0.1839 0.0603  -0.0032 0.0013  133 LEU A O   
1161 C CB  . LEU A 133 ? 0.2656 0.3851 0.1979 0.0488  -0.0052 0.0007  133 LEU A CB  
1162 C CG  . LEU A 133 ? 0.3405 0.4710 0.2750 0.0461  -0.0060 -0.0004 133 LEU A CG  
1163 C CD1 . LEU A 133 ? 0.3654 0.4981 0.2995 0.0386  -0.0071 0.0018  133 LEU A CD1 
1164 C CD2 . LEU A 133 ? 0.2243 0.3539 0.1583 0.0498  -0.0063 -0.0011 133 LEU A CD2 
1165 N N   . ASN A 134 ? 0.2351 0.3344 0.1687 0.0575  -0.0022 0.0002  134 ASN A N   
1166 C CA  . ASN A 134 ? 0.2385 0.3248 0.1718 0.0601  -0.0013 0.0014  134 ASN A CA  
1167 C C   . ASN A 134 ? 0.2030 0.2858 0.1370 0.0671  -0.0004 -0.0004 134 ASN A C   
1168 O O   . ASN A 134 ? 0.2666 0.3389 0.1994 0.0695  -0.0002 0.0009  134 ASN A O   
1169 C CB  . ASN A 134 ? 0.1883 0.2731 0.1228 0.0586  -0.0005 0.0014  134 ASN A CB  
1170 C CG  . ASN A 134 ? 0.2493 0.3298 0.1824 0.0526  -0.0012 0.0043  134 ASN A CG  
1171 O OD1 . ASN A 134 ? 0.2545 0.3236 0.1863 0.0525  -0.0010 0.0064  134 ASN A OD1 
1172 N ND2 . ASN A 134 ? 0.2248 0.3142 0.1579 0.0475  -0.0020 0.0045  134 ASN A ND2 
1173 N N   . LEU A 135 ? 0.1662 0.2578 0.1020 0.0704  0.0000  -0.0034 135 LEU A N   
1174 C CA  . LEU A 135 ? 0.2524 0.3416 0.1889 0.0771  0.0007  -0.0053 135 LEU A CA  
1175 C C   . LEU A 135 ? 0.2503 0.3376 0.1850 0.0785  -0.0001 -0.0046 135 LEU A C   
1176 O O   . LEU A 135 ? 0.2484 0.3268 0.1825 0.0826  0.0004  -0.0042 135 LEU A O   
1177 C CB  . LEU A 135 ? 0.3269 0.4274 0.2657 0.0798  0.0009  -0.0087 135 LEU A CB  
1178 C CG  . LEU A 135 ? 0.3077 0.4079 0.2486 0.0826  0.0021  -0.0106 135 LEU A CG  
1179 C CD1 . LEU A 135 ? 0.2760 0.3876 0.2195 0.0853  0.0019  -0.0139 135 LEU A CD1 
1180 C CD2 . LEU A 135 ? 0.2895 0.3769 0.2302 0.0872  0.0031  -0.0101 135 LEU A CD2 
1181 N N   . LEU A 136 ? 0.2999 0.3958 0.2340 0.0752  -0.0013 -0.0045 136 LEU A N   
1182 C CA  . LEU A 136 ? 0.2646 0.3601 0.1972 0.0766  -0.0021 -0.0041 136 LEU A CA  
1183 C C   . LEU A 136 ? 0.2526 0.3368 0.1830 0.0748  -0.0024 -0.0010 136 LEU A C   
1184 O O   . LEU A 136 ? 0.2778 0.3576 0.2069 0.0775  -0.0027 -0.0006 136 LEU A O   
1185 C CB  . LEU A 136 ? 0.2679 0.3760 0.2005 0.0733  -0.0032 -0.0049 136 LEU A CB  
1186 C CG  . LEU A 136 ? 0.2858 0.4053 0.2212 0.0760  -0.0030 -0.0083 136 LEU A CG  
1187 C CD1 . LEU A 136 ? 0.2601 0.3909 0.1974 0.0713  -0.0041 -0.0087 136 LEU A CD1 
1188 C CD2 . LEU A 136 ? 0.2433 0.3603 0.1791 0.0829  -0.0026 -0.0101 136 LEU A CD2 
1189 N N   . ALA A 137 ? 0.2384 0.3181 0.1681 0.0702  -0.0025 0.0012  137 ALA A N   
1190 C CA  . ALA A 137 ? 0.2745 0.3431 0.2020 0.0684  -0.0029 0.0041  137 ALA A CA  
1191 C C   . ALA A 137 ? 0.2664 0.3240 0.1937 0.0738  -0.0019 0.0043  137 ALA A C   
1192 O O   . ALA A 137 ? 0.1958 0.2455 0.1214 0.0740  -0.0023 0.0061  137 ALA A O   
1193 C CB  . ALA A 137 ? 0.2888 0.3539 0.2160 0.0632  -0.0031 0.0062  137 ALA A CB  
1194 N N   . TRP A 138 ? 0.1965 0.2536 0.1256 0.0783  -0.0007 0.0023  138 TRP A N   
1195 C CA  . TRP A 138 ? 0.2348 0.2816 0.1638 0.0834  0.0004  0.0023  138 TRP A CA  
1196 C C   . TRP A 138 ? 0.2476 0.2970 0.1770 0.0891  0.0005  0.0002  138 TRP A C   
1197 O O   . TRP A 138 ? 0.2659 0.3084 0.1956 0.0940  0.0015  -0.0003 138 TRP A O   
1198 C CB  . TRP A 138 ? 0.2459 0.2889 0.1764 0.0845  0.0016  0.0017  138 TRP A CB  
1199 C CG  . TRP A 138 ? 0.2399 0.2783 0.1699 0.0794  0.0015  0.0040  138 TRP A CG  
1200 C CD1 . TRP A 138 ? 0.2339 0.2791 0.1645 0.0745  0.0010  0.0042  138 TRP A CD1 
1201 C CD2 . TRP A 138 ? 0.2334 0.2597 0.1620 0.0785  0.0017  0.0065  138 TRP A CD2 
1202 N NE1 . TRP A 138 ? 0.2245 0.2624 0.1542 0.0707  0.0010  0.0066  138 TRP A NE1 
1203 C CE2 . TRP A 138 ? 0.2289 0.2551 0.1573 0.0731  0.0014  0.0080  138 TRP A CE2 
1204 C CE3 . TRP A 138 ? 0.2272 0.2427 0.1547 0.0818  0.0022  0.0076  138 TRP A CE3 
1205 C CZ2 . TRP A 138 ? 0.2647 0.2806 0.1919 0.0711  0.0014  0.0104  138 TRP A CZ2 
1206 C CZ3 . TRP A 138 ? 0.2853 0.2906 0.2115 0.0797  0.0023  0.0100  138 TRP A CZ3 
1207 C CH2 . TRP A 138 ? 0.2118 0.2174 0.1380 0.0744  0.0019  0.0114  138 TRP A CH2 
1208 N N   . CYS A 139 ? 0.2257 0.2847 0.1549 0.0886  -0.0004 -0.0009 139 CYS A N   
1209 C CA  . CYS A 139 ? 0.2030 0.2651 0.1326 0.0939  -0.0004 -0.0029 139 CYS A CA  
1210 C C   . CYS A 139 ? 0.2329 0.2843 0.1606 0.0969  -0.0003 -0.0014 139 CYS A C   
1211 O O   . CYS A 139 ? 0.2235 0.2701 0.1494 0.0940  -0.0009 0.0009  139 CYS A O   
1212 C CB  . CYS A 139 ? 0.2389 0.3128 0.1684 0.0920  -0.0016 -0.0040 139 CYS A CB  
1213 S SG  . CYS A 139 ? 0.2965 0.3767 0.2268 0.0985  -0.0016 -0.0071 139 CYS A SG  
1214 N N   . GLY A 140 ? 0.2366 0.2828 0.1644 0.0998  0.0001  -0.0024 140 GLY A N   
1215 C CA  . GLY A 140 ? 0.2031 0.2386 0.1286 0.0992  0.0002  -0.0012 140 GLY A CA  
1216 C C   . GLY A 140 ? 0.2327 0.2730 0.1572 0.1010  -0.0007 -0.0019 140 GLY A C   
1217 O O   . GLY A 140 ? 0.2097 0.2616 0.1354 0.1027  -0.0015 -0.0035 140 GLY A O   
1218 N N   . ARG A 141 ? 0.2420 0.2735 0.1645 0.1002  -0.0004 -0.0007 141 ARG A N   
1219 C CA  . ARG A 141 ? 0.2269 0.2615 0.1480 0.1017  -0.0011 -0.0011 141 ARG A CA  
1220 C C   . ARG A 141 ? 0.2441 0.2860 0.1660 0.1039  -0.0020 -0.0034 141 ARG A C   
1221 O O   . ARG A 141 ? 0.2273 0.2788 0.1493 0.1056  -0.0028 -0.0044 141 ARG A O   
1222 C CB  . ARG A 141 ? 0.2311 0.2544 0.1504 0.1001  -0.0004 0.0002  141 ARG A CB  
1223 C CG  . ARG A 141 ? 0.2094 0.2344 0.1273 0.1015  -0.0010 -0.0003 141 ARG A CG  
1224 C CD  . ARG A 141 ? 0.2929 0.3071 0.2094 0.0993  -0.0002 0.0012  141 ARG A CD  
1225 N NE  . ARG A 141 ? 0.2830 0.2976 0.1982 0.1005  -0.0006 0.0007  141 ARG A NE  
1226 C CZ  . ARG A 141 ? 0.2892 0.3012 0.2041 0.1009  -0.0007 0.0000  141 ARG A CZ  
1227 N NH1 . ARG A 141 ? 0.2503 0.2593 0.1665 0.1000  -0.0004 -0.0003 141 ARG A NH1 
1228 N NH2 . ARG A 141 ? 0.3148 0.3273 0.2284 0.1020  -0.0011 -0.0004 141 ARG A NH2 
1229 N N   . THR A 142 ? 0.2754 0.3132 0.1980 0.1036  -0.0018 -0.0041 142 THR A N   
1230 C CA  . THR A 142 ? 0.2786 0.3217 0.2019 0.1054  -0.0027 -0.0060 142 THR A CA  
1231 C C   . THR A 142 ? 0.2854 0.3418 0.2108 0.1069  -0.0036 -0.0079 142 THR A C   
1232 O O   . THR A 142 ? 0.2517 0.3160 0.1774 0.1086  -0.0047 -0.0094 142 THR A O   
1233 C CB  . THR A 142 ? 0.3084 0.3450 0.2328 0.1046  -0.0023 -0.0063 142 THR A CB  
1234 O OG1 . THR A 142 ? 0.3568 0.3830 0.2798 0.1031  -0.0016 -0.0049 142 THR A OG1 
1235 C CG2 . THR A 142 ? 0.3485 0.3914 0.2739 0.1066  -0.0033 -0.0085 142 THR A CG2 
1236 N N   . LEU A 143 ? 0.2397 0.2993 0.1669 0.1058  -0.0032 -0.0079 143 LEU A N   
1237 C CA  . LEU A 143 ? 0.2763 0.3489 0.2062 0.1064  -0.0039 -0.0099 143 LEU A CA  
1238 C C   . LEU A 143 ? 0.3301 0.4134 0.2607 0.1063  -0.0042 -0.0100 143 LEU A C   
1239 O O   . LEU A 143 ? 0.2567 0.3522 0.1899 0.1058  -0.0047 -0.0118 143 LEU A O   
1240 C CB  . LEU A 143 ? 0.2151 0.2873 0.1469 0.1049  -0.0032 -0.0100 143 LEU A CB  
1241 C CG  . LEU A 143 ? 0.2356 0.3028 0.1682 0.1051  -0.0032 -0.0109 143 LEU A CG  
1242 C CD1 . LEU A 143 ? 0.1898 0.2584 0.1245 0.1038  -0.0026 -0.0113 143 LEU A CD1 
1243 C CD2 . LEU A 143 ? 0.2353 0.3093 0.1686 0.1070  -0.0044 -0.0131 143 LEU A CD2 
1244 N N   . ARG A 144 ? 0.3954 0.4744 0.3238 0.1060  -0.0038 -0.0081 144 ARG A N   
1245 C CA  . ARG A 144 ? 0.3927 0.4800 0.3204 0.1032  -0.0039 -0.0080 144 ARG A CA  
1246 C C   . ARG A 144 ? 0.4721 0.5692 0.4018 0.1041  -0.0050 -0.0098 144 ARG A C   
1247 O O   . ARG A 144 ? 0.5370 0.6424 0.4676 0.0996  -0.0056 -0.0099 144 ARG A O   
1248 C CB  . ARG A 144 ? 0.4232 0.5009 0.3481 0.1007  -0.0043 -0.0048 144 ARG A CB  
1249 C CG  . ARG A 144 ? 0.5425 0.6115 0.4672 0.0979  -0.0036 -0.0027 144 ARG A CG  
1250 C CD  . ARG A 144 ? 0.6685 0.7319 0.5912 0.0930  -0.0044 0.0004  144 ARG A CD  
1251 N NE  . ARG A 144 ? 0.6782 0.7384 0.6012 0.0887  -0.0041 0.0019  144 ARG A NE  
1252 C CZ  . ARG A 144 ? 0.6658 0.7193 0.5872 0.0845  -0.0046 0.0047  144 ARG A CZ  
1253 N NH1 . ARG A 144 ? 0.6739 0.7232 0.5934 0.0840  -0.0054 0.0062  144 ARG A NH1 
1254 N NH2 . ARG A 144 ? 0.5963 0.6475 0.5181 0.0808  -0.0043 0.0058  144 ARG A NH2 
1255 N N   . LYS A 145 ? 0.4425 0.5379 0.3723 0.1084  -0.0060 -0.0107 145 LYS A N   
1256 C CA  . LYS A 145 ? 0.4787 0.5837 0.4102 0.1097  -0.0072 -0.0126 145 LYS A CA  
1257 C C   . LYS A 145 ? 0.5164 0.6311 0.4510 0.1093  -0.0078 -0.0149 145 LYS A C   
1258 O O   . LYS A 145 ? 0.4639 0.5905 0.4016 0.1074  -0.0078 -0.0164 145 LYS A O   
1259 C CB  . LYS A 145 ? 0.5776 0.6743 0.5051 0.1121  -0.0079 -0.0125 145 LYS A CB  
1260 C CG  . LYS A 145 ? 0.6638 0.7689 0.5924 0.1134  -0.0091 -0.0142 145 LYS A CG  
1261 C CD  . LYS A 145 ? 0.7250 0.8212 0.6494 0.1151  -0.0093 -0.0139 145 LYS A CD  
1262 C CE  . LYS A 145 ? 0.7451 0.8360 0.6680 0.1145  -0.0085 -0.0123 145 LYS A CE  
1263 N NZ  . LYS A 145 ? 0.7434 0.8288 0.6632 0.1161  -0.0088 -0.0125 145 LYS A NZ  
1264 N N   . ASP A 146 ? 0.5327 0.6419 0.4666 0.1100  -0.0078 -0.0154 146 ASP A N   
1265 C CA  . ASP A 146 ? 0.4378 0.5554 0.3745 0.1099  -0.0084 -0.0177 146 ASP A CA  
1266 C C   . ASP A 146 ? 0.4011 0.5284 0.3412 0.1068  -0.0076 -0.0182 146 ASP A C   
1267 O O   . ASP A 146 ? 0.3631 0.5011 0.3062 0.1060  -0.0081 -0.0202 146 ASP A O   
1268 C CB  . ASP A 146 ? 0.5112 0.6196 0.4468 0.1106  -0.0081 -0.0179 146 ASP A CB  
1269 C CG  . ASP A 146 ? 0.6881 0.7857 0.6207 0.1122  -0.0081 -0.0173 146 ASP A CG  
1270 O OD1 . ASP A 146 ? 0.6586 0.7458 0.5889 0.1116  -0.0072 -0.0152 146 ASP A OD1 
1271 O OD2 . ASP A 146 ? 0.7115 0.8111 0.6440 0.1138  -0.0091 -0.0189 146 ASP A OD2 
1272 N N   . LEU A 147 ? 0.2833 0.4063 0.2224 0.1042  -0.0062 -0.0163 147 LEU A N   
1273 C CA  . LEU A 147 ? 0.2405 0.3699 0.1808 0.0993  -0.0054 -0.0163 147 LEU A CA  
1274 C C   . LEU A 147 ? 0.2644 0.3979 0.2036 0.0941  -0.0056 -0.0150 147 LEU A C   
1275 O O   . LEU A 147 ? 0.2501 0.3867 0.1893 0.0886  -0.0055 -0.0140 147 LEU A O   
1276 C CB  . LEU A 147 ? 0.2372 0.3574 0.1758 0.0984  -0.0042 -0.0148 147 LEU A CB  
1277 C CG  . LEU A 147 ? 0.2309 0.3460 0.1708 0.1014  -0.0042 -0.0156 147 LEU A CG  
1278 C CD1 . LEU A 147 ? 0.2496 0.3565 0.1885 0.0999  -0.0028 -0.0140 147 LEU A CD1 
1279 C CD2 . LEU A 147 ? 0.2894 0.4152 0.2326 0.1013  -0.0050 -0.0181 147 LEU A CD2 
1280 N N   . LYS A 148 ? 0.2862 0.4198 0.2246 0.0951  -0.0062 -0.0148 148 LYS A N   
1281 C CA  . LYS A 148 ? 0.2546 0.3908 0.1921 0.0897  -0.0068 -0.0132 148 LYS A CA  
1282 C C   . LYS A 148 ? 0.2077 0.3561 0.1480 0.0848  -0.0072 -0.0142 148 LYS A C   
1283 O O   . LYS A 148 ? 0.3332 0.4825 0.2727 0.0787  -0.0076 -0.0124 148 LYS A O   
1284 C CB  . LYS A 148 ? 0.1786 0.3145 0.1155 0.0922  -0.0074 -0.0134 148 LYS A CB  
1285 C CG  . LYS A 148 ? 0.3394 0.4764 0.2752 0.0867  -0.0081 -0.0115 148 LYS A CG  
1286 C CD  . LYS A 148 ? 0.3916 0.5259 0.3264 0.0896  -0.0085 -0.0114 148 LYS A CD  
1287 C CE  . LYS A 148 ? 0.4733 0.6111 0.4078 0.0843  -0.0094 -0.0101 148 LYS A CE  
1288 N NZ  . LYS A 148 ? 0.5257 0.6572 0.4580 0.0788  -0.0098 -0.0071 148 LYS A NZ  
1289 N N   . ASP A 149 ? 0.2252 0.3826 0.1687 0.0872  -0.0072 -0.0170 149 ASP A N   
1290 C CA  . ASP A 149 ? 0.2261 0.3954 0.1724 0.0828  -0.0075 -0.0181 149 ASP A CA  
1291 C C   . ASP A 149 ? 0.2619 0.4302 0.2077 0.0778  -0.0071 -0.0167 149 ASP A C   
1292 O O   . ASP A 149 ? 0.3088 0.4816 0.2549 0.0718  -0.0075 -0.0155 149 ASP A O   
1293 C CB  . ASP A 149 ? 0.3333 0.5114 0.2833 0.0868  -0.0077 -0.0213 149 ASP A CB  
1294 C CG  . ASP A 149 ? 0.4495 0.6302 0.4003 0.0913  -0.0083 -0.0228 149 ASP A CG  
1295 O OD1 . ASP A 149 ? 0.4232 0.6017 0.3723 0.0903  -0.0086 -0.0217 149 ASP A OD1 
1296 O OD2 . ASP A 149 ? 0.5027 0.6875 0.4559 0.0958  -0.0090 -0.0251 149 ASP A OD2 
1297 N N   . LEU A 150 ? 0.2771 0.4393 0.2224 0.0803  -0.0064 -0.0167 150 LEU A N   
1298 C CA  . LEU A 150 ? 0.3052 0.4664 0.2501 0.0760  -0.0060 -0.0155 150 LEU A CA  
1299 C C   . LEU A 150 ? 0.3359 0.4887 0.2774 0.0716  -0.0062 -0.0121 150 LEU A C   
1300 O O   . LEU A 150 ? 0.3561 0.5110 0.2976 0.0659  -0.0064 -0.0108 150 LEU A O   
1301 C CB  . LEU A 150 ? 0.2727 0.4293 0.2180 0.0802  -0.0051 -0.0165 150 LEU A CB  
1302 C CG  . LEU A 150 ? 0.3086 0.4743 0.2578 0.0833  -0.0053 -0.0197 150 LEU A CG  
1303 C CD1 . LEU A 150 ? 0.2276 0.3868 0.1770 0.0880  -0.0047 -0.0205 150 LEU A CD1 
1304 C CD2 . LEU A 150 ? 0.2290 0.4054 0.1806 0.0781  -0.0054 -0.0203 150 LEU A CD2 
1305 N N   . LEU A 151 ? 0.2897 0.4332 0.2285 0.0741  -0.0063 -0.0107 151 LEU A N   
1306 C CA  . LEU A 151 ? 0.2418 0.3769 0.1776 0.0701  -0.0068 -0.0074 151 LEU A CA  
1307 C C   . LEU A 151 ? 0.3780 0.5185 0.3139 0.0644  -0.0078 -0.0063 151 LEU A C   
1308 O O   . LEU A 151 ? 0.4128 0.5506 0.3473 0.0589  -0.0084 -0.0040 151 LEU A O   
1309 C CB  . LEU A 151 ? 0.2489 0.3728 0.1820 0.0745  -0.0066 -0.0063 151 LEU A CB  
1310 C CG  . LEU A 151 ? 0.3003 0.4160 0.2324 0.0795  -0.0055 -0.0066 151 LEU A CG  
1311 C CD1 . LEU A 151 ? 0.3243 0.4317 0.2547 0.0849  -0.0053 -0.0064 151 LEU A CD1 
1312 C CD2 . LEU A 151 ? 0.2605 0.3689 0.1907 0.0760  -0.0053 -0.0042 151 LEU A CD2 
1313 N N   . ASN A 152 ? 0.3679 0.5158 0.3055 0.0655  -0.0082 -0.0080 152 ASN A N   
1314 C CA  . ASN A 152 ? 0.4261 0.5796 0.3640 0.0602  -0.0092 -0.0071 152 ASN A CA  
1315 C C   . ASN A 152 ? 0.3417 0.5049 0.2820 0.0552  -0.0093 -0.0077 152 ASN A C   
1316 O O   . ASN A 152 ? 0.3694 0.5349 0.3093 0.0493  -0.0100 -0.0061 152 ASN A O   
1317 C CB  . ASN A 152 ? 0.5074 0.6658 0.4464 0.0631  -0.0095 -0.0087 152 ASN A CB  
1318 C CG  . ASN A 152 ? 0.5961 0.7449 0.5325 0.0663  -0.0097 -0.0075 152 ASN A CG  
1319 O OD1 . ASN A 152 ? 0.6239 0.7622 0.5578 0.0678  -0.0094 -0.0059 152 ASN A OD1 
1320 N ND2 . ASN A 152 ? 0.6260 0.7783 0.5628 0.0675  -0.0102 -0.0082 152 ASN A ND2 
1321 N N   . LYS A 153 ? 0.3351 0.5039 0.2778 0.0574  -0.0085 -0.0099 153 LYS A N   
1322 C CA  . LYS A 153 ? 0.3745 0.5525 0.3196 0.0528  -0.0085 -0.0105 153 LYS A CA  
1323 C C   . LYS A 153 ? 0.4139 0.5870 0.3572 0.0470  -0.0088 -0.0077 153 LYS A C   
1324 O O   . LYS A 153 ? 0.4468 0.6250 0.3907 0.0412  -0.0093 -0.0068 153 LYS A O   
1325 C CB  . LYS A 153 ? 0.3776 0.5608 0.3254 0.0567  -0.0076 -0.0132 153 LYS A CB  
1326 C CG  . LYS A 153 ? 0.3812 0.5744 0.3319 0.0524  -0.0075 -0.0141 153 LYS A CG  
1327 C CD  . LYS A 153 ? 0.3482 0.5451 0.3013 0.0566  -0.0067 -0.0167 153 LYS A CD  
1328 C CE  . LYS A 153 ? 0.3795 0.5886 0.3363 0.0534  -0.0067 -0.0182 153 LYS A CE  
1329 N NZ  . LYS A 153 ? 0.3322 0.5451 0.2915 0.0579  -0.0062 -0.0209 153 LYS A NZ  
1330 N N   . GLY A 154 ? 0.3693 0.5323 0.3103 0.0486  -0.0084 -0.0064 154 GLY A N   
1331 C CA  . GLY A 154 ? 0.3612 0.5177 0.2999 0.0436  -0.0088 -0.0035 154 GLY A CA  
1332 C C   . GLY A 154 ? 0.3752 0.5365 0.3154 0.0394  -0.0085 -0.0035 154 GLY A C   
1333 O O   . GLY A 154 ? 0.3467 0.5016 0.2850 0.0361  -0.0088 -0.0012 154 GLY A O   
1334 N N   . ARG A 155 ? 0.4098 0.5820 0.3534 0.0395  -0.0081 -0.0059 155 ARG A N   
1335 C CA  . ARG A 155 ? 0.4588 0.6366 0.4041 0.0352  -0.0080 -0.0059 155 ARG A CA  
1336 C C   . ARG A 155 ? 0.4159 0.6045 0.3649 0.0378  -0.0073 -0.0091 155 ARG A C   
1337 O O   . ARG A 155 ? 0.3769 0.5695 0.3274 0.0422  -0.0071 -0.0113 155 ARG A O   
1338 C CB  . ARG A 155 ? 0.5220 0.7029 0.4670 0.0280  -0.0089 -0.0039 155 ARG A CB  
1339 C CG  . ARG A 155 ? 0.5509 0.7404 0.4977 0.0274  -0.0093 -0.0051 155 ARG A CG  
1340 C CD  . ARG A 155 ? 0.5830 0.7716 0.5285 0.0213  -0.0104 -0.0027 155 ARG A CD  
1341 N NE  . ARG A 155 ? 0.6207 0.8091 0.5660 0.0156  -0.0107 -0.0010 155 ARG A NE  
1342 C CZ  . ARG A 155 ? 0.6799 0.8595 0.6223 0.0120  -0.0114 0.0019  155 ARG A CZ  
1343 N NH1 . ARG A 155 ? 0.6588 0.8290 0.5983 0.0134  -0.0120 0.0035  155 ARG A NH1 
1344 N NH2 . ARG A 155 ? 0.6897 0.8698 0.6323 0.0069  -0.0116 0.0033  155 ARG A NH2 
1345 N N   . ASN A 156 ? 0.3319 0.5254 0.2827 0.0349  -0.0069 -0.0095 156 ASN A N   
1346 C CA  . ASN A 156 ? 0.3569 0.5617 0.3116 0.0363  -0.0064 -0.0124 156 ASN A CA  
1347 C C   . ASN A 156 ? 0.3454 0.5494 0.3013 0.0437  -0.0057 -0.0150 156 ASN A C   
1348 O O   . ASN A 156 ? 0.3442 0.5561 0.3028 0.0469  -0.0057 -0.0176 156 ASN A O   
1349 C CB  . ASN A 156 ? 0.4785 0.6937 0.4355 0.0341  -0.0068 -0.0134 156 ASN A CB  
1350 C CG  . ASN A 156 ? 0.5896 0.8065 0.5460 0.0267  -0.0075 -0.0111 156 ASN A CG  
1351 O OD1 . ASN A 156 ? 0.6120 0.8300 0.5678 0.0246  -0.0081 -0.0102 156 ASN A OD1 
1352 N ND2 . ASN A 156 ? 0.6410 0.8579 0.5976 0.0228  -0.0073 -0.0100 156 ASN A ND2 
1353 N N   . TYR A 157 ? 0.3261 0.5203 0.2798 0.0465  -0.0052 -0.0143 157 TYR A N   
1354 C CA  . TYR A 157 ? 0.2052 0.3976 0.1597 0.0535  -0.0046 -0.0166 157 TYR A CA  
1355 C C   . TYR A 157 ? 0.3026 0.5020 0.2604 0.0541  -0.0041 -0.0187 157 TYR A C   
1356 O O   . TYR A 157 ? 0.3148 0.5165 0.2731 0.0497  -0.0040 -0.0179 157 TYR A O   
1357 C CB  . TYR A 157 ? 0.2766 0.4557 0.2278 0.0564  -0.0042 -0.0150 157 TYR A CB  
1358 C CG  . TYR A 157 ? 0.2574 0.4292 0.2055 0.0565  -0.0047 -0.0130 157 TYR A CG  
1359 C CD1 . TYR A 157 ? 0.2542 0.4252 0.2023 0.0615  -0.0048 -0.0142 157 TYR A CD1 
1360 C CD2 . TYR A 157 ? 0.1872 0.3527 0.1325 0.0516  -0.0052 -0.0099 157 TYR A CD2 
1361 C CE1 . TYR A 157 ? 0.2710 0.4353 0.2164 0.0616  -0.0053 -0.0124 157 TYR A CE1 
1362 C CE2 . TYR A 157 ? 0.2062 0.3649 0.1489 0.0517  -0.0058 -0.0080 157 TYR A CE2 
1363 C CZ  . TYR A 157 ? 0.2609 0.4191 0.2036 0.0567  -0.0058 -0.0093 157 TYR A CZ  
1364 O OH  . TYR A 157 ? 0.2797 0.4312 0.2198 0.0567  -0.0064 -0.0075 157 TYR A OH  
1365 N N   . THR A 158 ? 0.2731 0.4758 0.2331 0.0598  -0.0041 -0.0215 158 THR A N   
1366 C CA  . THR A 158 ? 0.3309 0.5401 0.2942 0.0616  -0.0039 -0.0239 158 THR A CA  
1367 C C   . THR A 158 ? 0.2889 0.4890 0.2513 0.0666  -0.0033 -0.0244 158 THR A C   
1368 O O   . THR A 158 ? 0.2754 0.4656 0.2351 0.0698  -0.0031 -0.0234 158 THR A O   
1369 C CB  . THR A 158 ? 0.3693 0.5889 0.3361 0.0644  -0.0046 -0.0268 158 THR A CB  
1370 O OG1 . THR A 158 ? 0.4120 0.6264 0.3774 0.0693  -0.0050 -0.0271 158 THR A OG1 
1371 C CG2 . THR A 158 ? 0.2708 0.5007 0.2392 0.0592  -0.0049 -0.0266 158 THR A CG2 
1372 N N   . GLN A 159 ? 0.2498 0.4533 0.2144 0.0671  -0.0031 -0.0259 159 GLN A N   
1373 C CA  . GLN A 159 ? 0.2804 0.4754 0.2445 0.0716  -0.0027 -0.0265 159 GLN A CA  
1374 C C   . GLN A 159 ? 0.3368 0.5286 0.3011 0.0779  -0.0035 -0.0280 159 GLN A C   
1375 O O   . GLN A 159 ? 0.2112 0.3919 0.1736 0.0814  -0.0032 -0.0273 159 GLN A O   
1376 C CB  . GLN A 159 ? 0.2888 0.4889 0.2555 0.0708  -0.0027 -0.0279 159 GLN A CB  
1377 C CG  . GLN A 159 ? 0.2416 0.4330 0.2081 0.0751  -0.0024 -0.0286 159 GLN A CG  
1378 C CD  . GLN A 159 ? 0.3040 0.4844 0.2678 0.0739  -0.0010 -0.0263 159 GLN A CD  
1379 O OE1 . GLN A 159 ? 0.2899 0.4704 0.2521 0.0690  -0.0004 -0.0243 159 GLN A OE1 
1380 N NE2 . GLN A 159 ? 0.3150 0.4854 0.2783 0.0779  -0.0006 -0.0264 159 GLN A NE2 
1381 N N   . GLU A 160 ? 0.2490 0.4501 0.2155 0.0790  -0.0047 -0.0299 160 GLU A N   
1382 C CA  . GLU A 160 ? 0.2695 0.4679 0.2357 0.0844  -0.0059 -0.0312 160 GLU A CA  
1383 C C   . GLU A 160 ? 0.2444 0.4328 0.2075 0.0862  -0.0055 -0.0293 160 GLU A C   
1384 O O   . GLU A 160 ? 0.2275 0.4064 0.1889 0.0903  -0.0058 -0.0292 160 GLU A O   
1385 C CB  . GLU A 160 ? 0.4041 0.6152 0.3729 0.0843  -0.0072 -0.0332 160 GLU A CB  
1386 C CG  . GLU A 160 ? 0.5585 0.7746 0.5273 0.0803  -0.0066 -0.0318 160 GLU A CG  
1387 C CD  . GLU A 160 ? 0.5984 0.8275 0.5702 0.0789  -0.0074 -0.0335 160 GLU A CD  
1388 O OE1 . GLU A 160 ? 0.6249 0.8546 0.5963 0.0810  -0.0080 -0.0337 160 GLU A OE1 
1389 O OE2 . GLU A 160 ? 0.6947 0.9333 0.6692 0.0754  -0.0073 -0.0343 160 GLU A OE2 
1390 N N   . GLU A 161 ? 0.2697 0.4595 0.2315 0.0827  -0.0049 -0.0276 161 GLU A N   
1391 C CA  . GLU A 161 ? 0.2596 0.4409 0.2184 0.0842  -0.0047 -0.0258 161 GLU A CA  
1392 C C   . GLU A 161 ? 0.2641 0.4322 0.2200 0.0851  -0.0036 -0.0239 161 GLU A C   
1393 O O   . GLU A 161 ? 0.2436 0.4023 0.1977 0.0889  -0.0036 -0.0232 161 GLU A O   
1394 C CB  . GLU A 161 ? 0.2931 0.4791 0.2511 0.0793  -0.0046 -0.0244 161 GLU A CB  
1395 C CG  . GLU A 161 ? 0.2750 0.4728 0.2357 0.0790  -0.0056 -0.0263 161 GLU A CG  
1396 C CD  . GLU A 161 ? 0.3583 0.5623 0.3189 0.0725  -0.0055 -0.0249 161 GLU A CD  
1397 O OE1 . GLU A 161 ? 0.3336 0.5333 0.2922 0.0679  -0.0051 -0.0225 161 GLU A OE1 
1398 O OE2 . GLU A 161 ? 0.4887 0.7019 0.4515 0.0719  -0.0061 -0.0262 161 GLU A OE2 
1399 N N   . LYS A 162 ? 0.2105 0.3776 0.1661 0.0814  -0.0027 -0.0228 162 LYS A N   
1400 C CA  . LYS A 162 ? 0.2698 0.4249 0.2231 0.0823  -0.0016 -0.0212 162 LYS A CA  
1401 C C   . LYS A 162 ? 0.2611 0.4091 0.2153 0.0876  -0.0017 -0.0223 162 LYS A C   
1402 O O   . LYS A 162 ? 0.2358 0.3721 0.1881 0.0900  -0.0013 -0.0209 162 LYS A O   
1403 C CB  . LYS A 162 ? 0.2235 0.3801 0.1767 0.0776  -0.0009 -0.0203 162 LYS A CB  
1404 C CG  . LYS A 162 ? 0.1980 0.3428 0.1491 0.0783  0.0003  -0.0187 162 LYS A CG  
1405 C CD  . LYS A 162 ? 0.2440 0.3911 0.1949 0.0732  0.0008  -0.0177 162 LYS A CD  
1406 C CE  . LYS A 162 ? 0.2355 0.3903 0.1901 0.0735  0.0007  -0.0201 162 LYS A CE  
1407 N NZ  . LYS A 162 ? 0.2456 0.4026 0.2001 0.0685  0.0012  -0.0191 162 LYS A NZ  
1408 N N   . GLU A 163 ? 0.2477 0.4020 0.2046 0.0889  -0.0026 -0.0246 163 GLU A N   
1409 C CA  . GLU A 163 ? 0.1924 0.3392 0.1494 0.0927  -0.0032 -0.0255 163 GLU A CA  
1410 C C   . GLU A 163 ? 0.2407 0.3823 0.1960 0.0961  -0.0041 -0.0254 163 GLU A C   
1411 O O   . GLU A 163 ? 0.2454 0.3759 0.1992 0.0984  -0.0040 -0.0248 163 GLU A O   
1412 C CB  . GLU A 163 ? 0.2298 0.3848 0.1894 0.0928  -0.0040 -0.0280 163 GLU A CB  
1413 C CG  . GLU A 163 ? 0.3182 0.4743 0.2792 0.0903  -0.0031 -0.0280 163 GLU A CG  
1414 C CD  . GLU A 163 ? 0.4064 0.5741 0.3703 0.0892  -0.0040 -0.0304 163 GLU A CD  
1415 O OE1 . GLU A 163 ? 0.4589 0.6336 0.4237 0.0907  -0.0054 -0.0321 163 GLU A OE1 
1416 O OE2 . GLU A 163 ? 0.4087 0.5786 0.3739 0.0869  -0.0033 -0.0305 163 GLU A OE2 
1417 N N   . TYR A 164 ? 0.2430 0.3922 0.1984 0.0961  -0.0049 -0.0259 164 TYR A N   
1418 C CA  . TYR A 164 ? 0.2668 0.4110 0.2203 0.0991  -0.0057 -0.0257 164 TYR A CA  
1419 C C   . TYR A 164 ? 0.2602 0.3922 0.2109 0.0995  -0.0047 -0.0230 164 TYR A C   
1420 O O   . TYR A 164 ? 0.2754 0.3970 0.2242 0.1018  -0.0048 -0.0224 164 TYR A O   
1421 C CB  . TYR A 164 ? 0.2972 0.4529 0.2518 0.0986  -0.0066 -0.0267 164 TYR A CB  
1422 C CG  . TYR A 164 ? 0.3337 0.4850 0.2861 0.1014  -0.0074 -0.0263 164 TYR A CG  
1423 C CD1 . TYR A 164 ? 0.4602 0.6085 0.4116 0.1045  -0.0085 -0.0276 164 TYR A CD1 
1424 C CD2 . TYR A 164 ? 0.3485 0.4984 0.2996 0.1007  -0.0069 -0.0246 164 TYR A CD2 
1425 C CE1 . TYR A 164 ? 0.4413 0.5854 0.3905 0.1068  -0.0092 -0.0272 164 TYR A CE1 
1426 C CE2 . TYR A 164 ? 0.4061 0.5520 0.3551 0.1033  -0.0077 -0.0242 164 TYR A CE2 
1427 C CZ  . TYR A 164 ? 0.4877 0.6308 0.4358 0.1062  -0.0088 -0.0255 164 TYR A CZ  
1428 O OH  . TYR A 164 ? 0.6329 0.7719 0.5787 0.1084  -0.0095 -0.0252 164 TYR A OH  
1429 N N   . VAL A 165 ? 0.2187 0.3514 0.1688 0.0968  -0.0035 -0.0215 165 VAL A N   
1430 C CA  . VAL A 165 ? 0.1902 0.3113 0.1375 0.0972  -0.0026 -0.0190 165 VAL A CA  
1431 C C   . VAL A 165 ? 0.2588 0.3679 0.2056 0.0982  -0.0021 -0.0181 165 VAL A C   
1432 O O   . VAL A 165 ? 0.2290 0.3270 0.1738 0.0998  -0.0020 -0.0168 165 VAL A O   
1433 C CB  . VAL A 165 ? 0.1861 0.3097 0.1320 0.0931  -0.0015 -0.0174 165 VAL A CB  
1434 C CG1 . VAL A 165 ? 0.1898 0.3004 0.1325 0.0936  -0.0006 -0.0149 165 VAL A CG1 
1435 C CG2 . VAL A 165 ? 0.2539 0.3871 0.1997 0.0910  -0.0023 -0.0178 165 VAL A CG2 
1436 N N   . LEU A 166 ? 0.2239 0.3350 0.1725 0.0969  -0.0016 -0.0189 166 LEU A N   
1437 C CA  . LEU A 166 ? 0.2586 0.3586 0.2070 0.0974  -0.0010 -0.0181 166 LEU A CA  
1438 C C   . LEU A 166 ? 0.3316 0.4255 0.2795 0.0997  -0.0018 -0.0188 166 LEU A C   
1439 O O   . LEU A 166 ? 0.3055 0.3875 0.2520 0.0999  -0.0013 -0.0174 166 LEU A O   
1440 C CB  . LEU A 166 ? 0.2635 0.3682 0.2142 0.0956  -0.0005 -0.0192 166 LEU A CB  
1441 C CG  . LEU A 166 ? 0.2649 0.3713 0.2153 0.0927  0.0008  -0.0180 166 LEU A CG  
1442 C CD1 . LEU A 166 ? 0.3222 0.4364 0.2751 0.0907  0.0009  -0.0195 166 LEU A CD1 
1443 C CD2 . LEU A 166 ? 0.2735 0.3665 0.2221 0.0927  0.0018  -0.0156 166 LEU A CD2 
1444 N N   . ASN A 167 ? 0.2321 0.3341 0.1810 0.1010  -0.0030 -0.0210 167 ASN A N   
1445 C CA  . ASN A 167 ? 0.3270 0.4242 0.2752 0.1030  -0.0038 -0.0218 167 ASN A CA  
1446 C C   . ASN A 167 ? 0.2514 0.3399 0.1969 0.1040  -0.0037 -0.0201 167 ASN A C   
1447 O O   . ASN A 167 ? 0.2909 0.3692 0.2355 0.1042  -0.0034 -0.0193 167 ASN A O   
1448 C CB  . ASN A 167 ? 0.3704 0.4790 0.3199 0.1043  -0.0052 -0.0244 167 ASN A CB  
1449 C CG  . ASN A 167 ? 0.6141 0.7185 0.5630 0.1064  -0.0059 -0.0255 167 ASN A CG  
1450 O OD1 . ASN A 167 ? 0.7328 0.8267 0.6810 0.1064  -0.0053 -0.0246 167 ASN A OD1 
1451 N ND2 . ASN A 167 ? 0.6872 0.8000 0.6364 0.1079  -0.0073 -0.0275 167 ASN A ND2 
1452 N N   . LYS A 168 ? 0.2411 0.3340 0.1856 0.1042  -0.0041 -0.0196 168 LYS A N   
1453 C CA  . LYS A 168 ? 0.2552 0.3404 0.1971 0.1050  -0.0041 -0.0181 168 LYS A CA  
1454 C C   . LYS A 168 ? 0.3056 0.3785 0.2461 0.1036  -0.0028 -0.0156 168 LYS A C   
1455 O O   . LYS A 168 ? 0.2694 0.3328 0.2082 0.1038  -0.0026 -0.0144 168 LYS A O   
1456 C CB  . LYS A 168 ? 0.2190 0.3119 0.1603 0.1054  -0.0046 -0.0180 168 LYS A CB  
1457 C CG  . LYS A 168 ? 0.3277 0.4338 0.2707 0.1063  -0.0059 -0.0205 168 LYS A CG  
1458 C CD  . LYS A 168 ? 0.4057 0.5096 0.3475 0.1086  -0.0069 -0.0215 168 LYS A CD  
1459 C CE  . LYS A 168 ? 0.5257 0.6247 0.4649 0.1094  -0.0070 -0.0201 168 LYS A CE  
1460 N NZ  . LYS A 168 ? 0.6008 0.6967 0.5386 0.1115  -0.0078 -0.0209 168 LYS A NZ  
1461 N N   . TYR A 169 ? 0.2341 0.3074 0.1753 0.1019  -0.0019 -0.0147 169 TYR A N   
1462 C CA  . TYR A 169 ? 0.2547 0.3166 0.1946 0.1004  -0.0008 -0.0123 169 TYR A CA  
1463 C C   . TYR A 169 ? 0.2659 0.3187 0.2063 0.0999  -0.0004 -0.0122 169 TYR A C   
1464 O O   . TYR A 169 ? 0.2597 0.3025 0.1987 0.0990  0.0001  -0.0106 169 TYR A O   
1465 C CB  . TYR A 169 ? 0.1710 0.2359 0.1118 0.0988  0.0001  -0.0117 169 TYR A CB  
1466 C CG  . TYR A 169 ? 0.2193 0.2888 0.1590 0.0984  0.0002  -0.0107 169 TYR A CG  
1467 C CD1 . TYR A 169 ? 0.1821 0.2557 0.1207 0.0997  -0.0006 -0.0110 169 TYR A CD1 
1468 C CD2 . TYR A 169 ? 0.2240 0.2939 0.1635 0.0966  0.0013  -0.0097 169 TYR A CD2 
1469 C CE1 . TYR A 169 ? 0.2055 0.2836 0.1430 0.0990  -0.0002 -0.0102 169 TYR A CE1 
1470 C CE2 . TYR A 169 ? 0.2566 0.3307 0.1944 0.0956  0.0018  -0.0089 169 TYR A CE2 
1471 C CZ  . TYR A 169 ? 0.2783 0.3565 0.2150 0.0966  0.0010  -0.0091 169 TYR A CZ  
1472 O OH  . TYR A 169 ? 0.2376 0.3179 0.1721 0.0927  0.0005  -0.0075 169 TYR A OH  
1473 N N   . PHE A 170 ? 0.2875 0.3443 0.2301 0.1000  -0.0006 -0.0139 170 PHE A N   
1474 C CA  . PHE A 170 ? 0.3067 0.3556 0.2500 0.0995  -0.0002 -0.0138 170 PHE A CA  
1475 C C   . PHE A 170 ? 0.2443 0.2896 0.1866 0.1007  -0.0007 -0.0141 170 PHE A C   
1476 O O   . PHE A 170 ? 0.2596 0.2961 0.2019 0.0996  -0.0002 -0.0132 170 PHE A O   
1477 C CB  . PHE A 170 ? 0.2965 0.3509 0.2422 0.0996  -0.0004 -0.0157 170 PHE A CB  
1478 C CG  . PHE A 170 ? 0.3362 0.3894 0.2831 0.0977  0.0006  -0.0150 170 PHE A CG  
1479 C CD1 . PHE A 170 ? 0.3215 0.3648 0.2687 0.0960  0.0015  -0.0137 170 PHE A CD1 
1480 C CD2 . PHE A 170 ? 0.3743 0.4365 0.3221 0.0973  0.0006  -0.0156 170 PHE A CD2 
1481 C CE1 . PHE A 170 ? 0.3225 0.3644 0.2706 0.0942  0.0024  -0.0130 170 PHE A CE1 
1482 C CE2 . PHE A 170 ? 0.4159 0.4770 0.3646 0.0956  0.0015  -0.0150 170 PHE A CE2 
1483 C CZ  . PHE A 170 ? 0.3580 0.4086 0.3068 0.0942  0.0024  -0.0136 170 PHE A CZ  
1484 N N   . GLU A 171 ? 0.1890 0.2410 0.1304 0.1026  -0.0018 -0.0153 171 GLU A N   
1485 C CA  . GLU A 171 ? 0.2724 0.3209 0.2127 0.1038  -0.0023 -0.0154 171 GLU A CA  
1486 C C   . GLU A 171 ? 0.3087 0.3477 0.2471 0.1025  -0.0015 -0.0130 171 GLU A C   
1487 O O   . GLU A 171 ? 0.2278 0.2599 0.1658 0.1021  -0.0013 -0.0125 171 GLU A O   
1488 C CB  . GLU A 171 ? 0.3528 0.4107 0.2925 0.1061  -0.0036 -0.0170 171 GLU A CB  
1489 C CG  . GLU A 171 ? 0.5295 0.5958 0.4710 0.1075  -0.0045 -0.0196 171 GLU A CG  
1490 C CD  . GLU A 171 ? 0.6075 0.6839 0.5486 0.1094  -0.0058 -0.0212 171 GLU A CD  
1491 O OE1 . GLU A 171 ? 0.5860 0.6624 0.5254 0.1098  -0.0060 -0.0204 171 GLU A OE1 
1492 O OE2 . GLU A 171 ? 0.5936 0.6782 0.5362 0.1104  -0.0067 -0.0235 171 GLU A OE2 
1493 N N   . ILE A 172 ? 0.1991 0.2379 0.1363 0.1017  -0.0011 -0.0117 172 ILE A N   
1494 C CA  . ILE A 172 ? 0.2465 0.2766 0.1819 0.1001  -0.0004 -0.0094 172 ILE A CA  
1495 C C   . ILE A 172 ? 0.2678 0.2888 0.2043 0.0976  0.0007  -0.0082 172 ILE A C   
1496 O O   . ILE A 172 ? 0.2465 0.2601 0.1825 0.0964  0.0011  -0.0072 172 ILE A O   
1497 C CB  . ILE A 172 ? 0.3155 0.3481 0.2496 0.0999  -0.0003 -0.0084 172 ILE A CB  
1498 C CG1 . ILE A 172 ? 0.3643 0.4047 0.2973 0.1021  -0.0013 -0.0093 172 ILE A CG1 
1499 C CG2 . ILE A 172 ? 0.3171 0.3399 0.2497 0.0978  0.0007  -0.0060 172 ILE A CG2 
1500 C CD1 . ILE A 172 ? 0.3570 0.3930 0.2882 0.1028  -0.0016 -0.0090 172 ILE A CD1 
1501 N N   . ILE A 173 ? 0.2563 0.2781 0.1943 0.0966  0.0011  -0.0084 173 ILE A N   
1502 C CA  . ILE A 173 ? 0.2511 0.2650 0.1905 0.0941  0.0021  -0.0074 173 ILE A CA  
1503 C C   . ILE A 173 ? 0.2643 0.2753 0.2050 0.0942  0.0020  -0.0082 173 ILE A C   
1504 O O   . ILE A 173 ? 0.2196 0.2233 0.1609 0.0921  0.0027  -0.0071 173 ILE A O   
1505 C CB  . ILE A 173 ? 0.2909 0.3073 0.2318 0.0934  0.0025  -0.0077 173 ILE A CB  
1506 C CG1 . ILE A 173 ? 0.3241 0.3428 0.2637 0.0931  0.0027  -0.0067 173 ILE A CG1 
1507 C CG2 . ILE A 173 ? 0.3025 0.3113 0.2451 0.0908  0.0034  -0.0069 173 ILE A CG2 
1508 C CD1 . ILE A 173 ? 0.2620 0.2846 0.2031 0.0926  0.0031  -0.0072 173 ILE A CD1 
1509 N N   . LYS A 174 ? 0.2704 0.2876 0.2118 0.0965  0.0012  -0.0101 174 LYS A N   
1510 C CA  . LYS A 174 ? 0.2397 0.2546 0.1823 0.0968  0.0010  -0.0109 174 LYS A CA  
1511 C C   . LYS A 174 ? 0.2823 0.2924 0.2236 0.0967  0.0010  -0.0101 174 LYS A C   
1512 O O   . LYS A 174 ? 0.3375 0.3431 0.2791 0.0965  0.0012  -0.0100 174 LYS A O   
1513 C CB  . LYS A 174 ? 0.2348 0.2576 0.1780 0.0994  0.0000  -0.0133 174 LYS A CB  
1514 C CG  . LYS A 174 ? 0.3182 0.3457 0.2634 0.0993  0.0000  -0.0145 174 LYS A CG  
1515 C CD  . LYS A 174 ? 0.4957 0.5323 0.4414 0.1019  -0.0012 -0.0169 174 LYS A CD  
1516 C CE  . LYS A 174 ? 0.6200 0.6636 0.5673 0.1019  -0.0013 -0.0182 174 LYS A CE  
1517 N NZ  . LYS A 174 ? 0.6700 0.7087 0.6192 0.1001  -0.0004 -0.0179 174 LYS A NZ  
1518 N N   . LYS A 175 ? 0.2352 0.2465 0.1742 0.0974  0.0007  -0.0095 175 LYS A N   
1519 C CA  . LYS A 175 ? 0.3022 0.3095 0.2398 0.0974  0.0006  -0.0087 175 LYS A CA  
1520 C C   . LYS A 175 ? 0.2507 0.2505 0.1879 0.0945  0.0016  -0.0066 175 LYS A C   
1521 O O   . LYS A 175 ? 0.2012 0.1977 0.1367 0.0947  0.0016  -0.0059 175 LYS A O   
1522 C CB  . LYS A 175 ? 0.3369 0.3502 0.2724 0.0999  -0.0003 -0.0094 175 LYS A CB  
1523 C CG  . LYS A 175 ? 0.4656 0.4854 0.4014 0.1026  -0.0014 -0.0116 175 LYS A CG  
1524 C CD  . LYS A 175 ? 0.5917 0.6206 0.5263 0.1050  -0.0025 -0.0128 175 LYS A CD  
1525 C CE  . LYS A 175 ? 0.6691 0.6972 0.6014 0.1051  -0.0025 -0.0116 175 LYS A CE  
1526 N NZ  . LYS A 175 ? 0.7434 0.7799 0.6747 0.1077  -0.0038 -0.0131 175 LYS A NZ  
1527 N N   . THR A 176 ? 0.2931 0.2904 0.2313 0.0924  0.0024  -0.0057 176 THR A N   
1528 C CA  . THR A 176 ? 0.2579 0.2493 0.1954 0.0898  0.0032  -0.0038 176 THR A CA  
1529 C C   . THR A 176 ? 0.3574 0.3420 0.2924 0.0898  0.0037  -0.0029 176 THR A C   
1530 O O   . THR A 176 ? 0.2725 0.2538 0.2053 0.0897  0.0038  -0.0019 176 THR A O   
1531 C CB  . THR A 176 ? 0.2174 0.2085 0.1554 0.0883  0.0037  -0.0031 176 THR A CB  
1532 O OG1 . THR A 176 ? 0.2271 0.2243 0.1634 0.0904  0.0032  -0.0036 176 THR A OG1 
1533 C CG2 . THR A 176 ? 0.2252 0.2098 0.1630 0.0852  0.0046  -0.0013 176 THR A CG2 
1534 N N   . LEU A 177 ? 0.2805 0.2632 0.2159 0.0899  0.0040  -0.0032 177 LEU A N   
1535 C CA  . LEU A 177 ? 0.2664 0.2430 0.1995 0.0898  0.0045  -0.0023 177 LEU A CA  
1536 C C   . LEU A 177 ? 0.2878 0.2643 0.2188 0.0921  0.0039  -0.0027 177 LEU A C   
1537 O O   . LEU A 177 ? 0.2628 0.2346 0.1915 0.0918  0.0044  -0.0017 177 LEU A O   
1538 C CB  . LEU A 177 ? 0.2853 0.2605 0.2195 0.0897  0.0048  -0.0027 177 LEU A CB  
1539 C CG  . LEU A 177 ? 0.3009 0.2754 0.2369 0.0874  0.0054  -0.0022 177 LEU A CG  
1540 C CD1 . LEU A 177 ? 0.3316 0.3046 0.2684 0.0876  0.0057  -0.0026 177 LEU A CD1 
1541 C CD2 . LEU A 177 ? 0.3446 0.3145 0.2794 0.0849  0.0063  -0.0004 177 LEU A CD2 
1542 N N   . SER A 178 ? 0.2891 0.2710 0.2209 0.0943  0.0030  -0.0042 178 SER A N   
1543 C CA  . SER A 178 ? 0.3030 0.2851 0.2328 0.0965  0.0023  -0.0047 178 SER A CA  
1544 C C   . SER A 178 ? 0.3124 0.2929 0.2402 0.0960  0.0024  -0.0037 178 SER A C   
1545 O O   . SER A 178 ? 0.3044 0.2820 0.2299 0.0970  0.0024  -0.0034 178 SER A O   
1546 C CB  . SER A 178 ? 0.4049 0.3937 0.3360 0.0988  0.0012  -0.0067 178 SER A CB  
1547 O OG  . SER A 178 ? 0.4964 0.4853 0.4280 0.1001  0.0010  -0.0077 178 SER A OG  
1548 N N   . ILE A 179 ? 0.2645 0.2471 0.1935 0.0946  0.0025  -0.0033 179 ILE A N   
1549 C CA  . ILE A 179 ? 0.2695 0.2506 0.1967 0.0942  0.0026  -0.0023 179 ILE A CA  
1550 C C   . ILE A 179 ? 0.3070 0.2812 0.2322 0.0924  0.0036  -0.0007 179 ILE A C   
1551 O O   . ILE A 179 ? 0.2982 0.2699 0.2211 0.0927  0.0037  -0.0001 179 ILE A O   
1552 C CB  . ILE A 179 ? 0.2798 0.2650 0.2087 0.0931  0.0024  -0.0023 179 ILE A CB  
1553 C CG1 . ILE A 179 ? 0.3844 0.3692 0.3115 0.0935  0.0022  -0.0018 179 ILE A CG1 
1554 C CG2 . ILE A 179 ? 0.2580 0.2408 0.1881 0.0904  0.0032  -0.0012 179 ILE A CG2 
1555 C CD1 . ILE A 179 ? 0.3989 0.3899 0.3266 0.0944  0.0014  -0.0025 179 ILE A CD1 
1556 N N   . TYR A 180 ? 0.2678 0.2390 0.1938 0.0906  0.0044  -0.0001 180 TYR A N   
1557 C CA  . TYR A 180 ? 0.2361 0.2011 0.1602 0.0890  0.0053  0.0013  180 TYR A CA  
1558 C C   . TYR A 180 ? 0.3267 0.2888 0.2487 0.0905  0.0054  0.0012  180 TYR A C   
1559 O O   . TYR A 180 ? 0.2670 0.2253 0.1868 0.0901  0.0060  0.0021  180 TYR A O   
1560 C CB  . TYR A 180 ? 0.2596 0.2225 0.1851 0.0867  0.0061  0.0020  180 TYR A CB  
1561 C CG  . TYR A 180 ? 0.2580 0.2221 0.1849 0.0847  0.0063  0.0025  180 TYR A CG  
1562 C CD1 . TYR A 180 ? 0.2380 0.1992 0.1636 0.0830  0.0068  0.0036  180 TYR A CD1 
1563 C CD2 . TYR A 180 ? 0.2351 0.2035 0.1646 0.0845  0.0059  0.0017  180 TYR A CD2 
1564 C CE1 . TYR A 180 ? 0.1857 0.1480 0.1127 0.0812  0.0068  0.0041  180 TYR A CE1 
1565 C CE2 . TYR A 180 ? 0.1588 0.1284 0.0897 0.0827  0.0059  0.0022  180 TYR A CE2 
1566 C CZ  . TYR A 180 ? 0.1550 0.1214 0.0846 0.0811  0.0064  0.0034  180 TYR A CZ  
1567 O OH  . TYR A 180 ? 0.2366 0.2041 0.1676 0.0793  0.0064  0.0039  180 TYR A OH  
1568 N N   . ARG A 181 ? 0.2823 0.2462 0.2051 0.0923  0.0049  0.0001  181 ARG A N   
1569 C CA  . ARG A 181 ? 0.3033 0.2648 0.2242 0.0940  0.0048  -0.0001 181 ARG A CA  
1570 C C   . ARG A 181 ? 0.2930 0.2552 0.2119 0.0957  0.0043  -0.0002 181 ARG A C   
1571 O O   . ARG A 181 ? 0.3301 0.2886 0.2466 0.0962  0.0046  0.0003  181 ARG A O   
1572 C CB  . ARG A 181 ? 0.3484 0.3123 0.2706 0.0959  0.0042  -0.0015 181 ARG A CB  
1573 C CG  . ARG A 181 ? 0.3821 0.3448 0.3060 0.0946  0.0047  -0.0014 181 ARG A CG  
1574 C CD  . ARG A 181 ? 0.3013 0.2667 0.2264 0.0967  0.0040  -0.0030 181 ARG A CD  
1575 N NE  . ARG A 181 ? 0.3980 0.3636 0.3253 0.0955  0.0044  -0.0032 181 ARG A NE  
1576 C CZ  . ARG A 181 ? 0.4375 0.4079 0.3673 0.0956  0.0039  -0.0042 181 ARG A CZ  
1577 N NH1 . ARG A 181 ? 0.5288 0.5043 0.4592 0.0969  0.0031  -0.0052 181 ARG A NH1 
1578 N NH2 . ARG A 181 ? 0.5060 0.4763 0.4377 0.0944  0.0043  -0.0043 181 ARG A NH2 
1579 N N   . GLU A 182 ? 0.2306 0.1976 0.1503 0.0966  0.0035  -0.0010 182 GLU A N   
1580 C CA  . GLU A 182 ? 0.2722 0.2405 0.1902 0.0983  0.0029  -0.0013 182 GLU A CA  
1581 C C   . GLU A 182 ? 0.3762 0.3409 0.2923 0.0969  0.0035  0.0000  182 GLU A C   
1582 O O   . GLU A 182 ? 0.3800 0.3423 0.2937 0.0979  0.0036  0.0003  182 GLU A O   
1583 C CB  . GLU A 182 ? 0.2864 0.2612 0.2061 0.0995  0.0019  -0.0026 182 GLU A CB  
1584 C CG  . GLU A 182 ? 0.4343 0.4109 0.3524 0.1009  0.0013  -0.0028 182 GLU A CG  
1585 C CD  . GLU A 182 ? 0.5714 0.5548 0.4913 0.1019  0.0003  -0.0040 182 GLU A CD  
1586 O OE1 . GLU A 182 ? 0.6315 0.6171 0.5503 0.1032  -0.0003 -0.0044 182 GLU A OE1 
1587 O OE2 . GLU A 182 ? 0.5402 0.5272 0.4627 0.1013  0.0002  -0.0046 182 GLU A OE2 
1588 N N   . ILE A 183 ? 0.3650 0.3294 0.2820 0.0946  0.0040  0.0008  183 ILE A N   
1589 C CA  . ILE A 183 ? 0.2588 0.2201 0.1741 0.0932  0.0047  0.0020  183 ILE A CA  
1590 C C   . ILE A 183 ? 0.3096 0.2652 0.2229 0.0925  0.0056  0.0030  183 ILE A C   
1591 O O   . ILE A 183 ? 0.3448 0.2979 0.2560 0.0924  0.0060  0.0036  183 ILE A O   
1592 C CB  . ILE A 183 ? 0.3498 0.3118 0.2667 0.0909  0.0050  0.0027  183 ILE A CB  
1593 C CG1 . ILE A 183 ? 0.3618 0.3211 0.2798 0.0887  0.0058  0.0033  183 ILE A CG1 
1594 C CG2 . ILE A 183 ? 0.2985 0.2664 0.2175 0.0916  0.0040  0.0017  183 ILE A CG2 
1595 C CD1 . ILE A 183 ? 0.4362 0.3931 0.3543 0.0860  0.0065  0.0044  183 ILE A CD1 
1596 N N   . LYS A 184 ? 0.2677 0.2215 0.1819 0.0919  0.0061  0.0030  184 LYS A N   
1597 C CA  . LYS A 184 ? 0.2774 0.2263 0.1898 0.0913  0.0070  0.0038  184 LYS A CA  
1598 C C   . LYS A 184 ? 0.3915 0.3397 0.3020 0.0938  0.0066  0.0034  184 LYS A C   
1599 O O   . LYS A 184 ? 0.3351 0.2799 0.2435 0.0936  0.0071  0.0041  184 LYS A O   
1600 C CB  . LYS A 184 ? 0.2826 0.2304 0.1966 0.0902  0.0075  0.0039  184 LYS A CB  
1601 C CG  . LYS A 184 ? 0.4884 0.4313 0.4012 0.0891  0.0085  0.0048  184 LYS A CG  
1602 C CD  . LYS A 184 ? 0.5100 0.4527 0.4243 0.0890  0.0086  0.0044  184 LYS A CD  
1603 C CE  . LYS A 184 ? 0.4883 0.4266 0.4019 0.0874  0.0098  0.0053  184 LYS A CE  
1604 N NZ  . LYS A 184 ? 0.5886 0.5237 0.4997 0.0876  0.0104  0.0060  184 LYS A NZ  
1605 N N   . GLU A 185 ? 0.3562 0.3080 0.2675 0.0960  0.0055  0.0021  185 GLU A N   
1606 C CA  . GLU A 185 ? 0.4181 0.3696 0.3277 0.0986  0.0050  0.0015  185 GLU A CA  
1607 C C   . GLU A 185 ? 0.4045 0.3564 0.3121 0.0995  0.0047  0.0016  185 GLU A C   
1608 O O   . GLU A 185 ? 0.4774 0.4264 0.3827 0.1004  0.0048  0.0019  185 GLU A O   
1609 C CB  . GLU A 185 ? 0.4432 0.3991 0.3544 0.1006  0.0038  -0.0001 185 GLU A CB  
1610 C CG  . GLU A 185 ? 0.5836 0.5384 0.4942 0.1026  0.0035  -0.0008 185 GLU A CG  
1611 C CD  . GLU A 185 ? 0.6708 0.6295 0.5838 0.1037  0.0027  -0.0022 185 GLU A CD  
1612 O OE1 . GLU A 185 ? 0.6930 0.6513 0.6078 0.1021  0.0032  -0.0020 185 GLU A OE1 
1613 O OE2 . GLU A 185 ? 0.6439 0.6062 0.5570 0.1061  0.0016  -0.0036 185 GLU A OE2 
1614 N N   . GLU A 186 ? 0.4191 0.3744 0.3275 0.0993  0.0042  0.0014  186 GLU A N   
1615 C CA  . GLU A 186 ? 0.3998 0.3559 0.3066 0.1001  0.0038  0.0014  186 GLU A CA  
1616 C C   . GLU A 186 ? 0.4038 0.3560 0.3091 0.0982  0.0048  0.0028  186 GLU A C   
1617 O O   . GLU A 186 ? 0.4106 0.3632 0.3145 0.0987  0.0046  0.0029  186 GLU A O   
1618 C CB  . GLU A 186 ? 0.4780 0.4395 0.3865 0.1005  0.0030  0.0006  186 GLU A CB  
1619 C CG  . GLU A 186 ? 0.4729 0.4393 0.3829 0.1027  0.0019  -0.0009 186 GLU A CG  
1620 C CD  . GLU A 186 ? 0.6201 0.5923 0.5322 0.1027  0.0012  -0.0017 186 GLU A CD  
1621 O OE1 . GLU A 186 ? 0.6178 0.5900 0.5306 0.1008  0.0016  -0.0009 186 GLU A OE1 
1622 O OE2 . GLU A 186 ? 0.6467 0.6236 0.5598 0.1047  0.0002  -0.0031 186 GLU A OE2 
1623 N N   . GLY A 187 ? 0.4514 0.4001 0.3569 0.0960  0.0059  0.0037  187 GLY A N   
1624 C CA  . GLY A 187 ? 0.3673 0.3126 0.2715 0.0941  0.0068  0.0049  187 GLY A CA  
1625 C C   . GLY A 187 ? 0.3505 0.2974 0.2555 0.0926  0.0068  0.0052  187 GLY A C   
1626 O O   . GLY A 187 ? 0.3481 0.2929 0.2518 0.0916  0.0073  0.0059  187 GLY A O   
1627 N N   . LYS A 188 ? 0.2912 0.2419 0.1985 0.0925  0.0062  0.0046  188 LYS A N   
1628 C CA  . LYS A 188 ? 0.2914 0.2439 0.1997 0.0911  0.0060  0.0048  188 LYS A CA  
1629 C C   . LYS A 188 ? 0.2803 0.2306 0.1898 0.0883  0.0069  0.0056  188 LYS A C   
1630 O O   . LYS A 188 ? 0.2847 0.2355 0.1948 0.0869  0.0069  0.0060  188 LYS A O   
1631 C CB  . LYS A 188 ? 0.3251 0.2832 0.2353 0.0924  0.0050  0.0038  188 LYS A CB  
1632 C CG  . LYS A 188 ? 0.3986 0.3596 0.3079 0.0952  0.0040  0.0028  188 LYS A CG  
1633 C CD  . LYS A 188 ? 0.4813 0.4483 0.3927 0.0961  0.0030  0.0018  188 LYS A CD  
1634 C CE  . LYS A 188 ? 0.5834 0.5536 0.4937 0.0988  0.0020  0.0008  188 LYS A CE  
1635 N NZ  . LYS A 188 ? 0.6194 0.5956 0.5315 0.0993  0.0012  0.0000  188 LYS A NZ  
1636 N N   . GLY A 189 ? 0.2766 0.2247 0.1865 0.0875  0.0075  0.0059  189 GLY A N   
1637 C CA  . GLY A 189 ? 0.2436 0.1896 0.1546 0.0848  0.0083  0.0066  189 GLY A CA  
1638 C C   . GLY A 189 ? 0.3084 0.2517 0.2194 0.0844  0.0090  0.0069  189 GLY A C   
1639 O O   . GLY A 189 ? 0.2428 0.1868 0.1538 0.0861  0.0086  0.0063  189 GLY A O   
1640 N N   . SER A 190 ? 0.2229 0.1631 0.1338 0.0821  0.0100  0.0077  190 SER A N   
1641 C CA  . SER A 190 ? 0.2119 0.1500 0.1233 0.0814  0.0106  0.0079  190 SER A CA  
1642 C C   . SER A 190 ? 0.2169 0.1569 0.1309 0.0803  0.0105  0.0076  190 SER A C   
1643 O O   . SER A 190 ? 0.2375 0.1793 0.1526 0.0793  0.0102  0.0076  190 SER A O   
1644 C CB  . SER A 190 ? 0.2719 0.2061 0.1820 0.0796  0.0118  0.0088  190 SER A CB  
1645 O OG  . SER A 190 ? 0.2512 0.1835 0.1589 0.0807  0.0120  0.0090  190 SER A OG  
1646 N N   . VAL A 191 ? 0.2358 0.1754 0.1506 0.0805  0.0106  0.0074  191 VAL A N   
1647 C CA  . VAL A 191 ? 0.2135 0.1544 0.1307 0.0793  0.0106  0.0072  191 VAL A CA  
1648 C C   . VAL A 191 ? 0.2732 0.2107 0.1903 0.0776  0.0117  0.0079  191 VAL A C   
1649 O O   . VAL A 191 ? 0.3028 0.2384 0.2190 0.0784  0.0120  0.0079  191 VAL A O   
1650 C CB  . VAL A 191 ? 0.2500 0.1944 0.1687 0.0812  0.0098  0.0062  191 VAL A CB  
1651 C CG1 . VAL A 191 ? 0.1677 0.1137 0.0891 0.0798  0.0098  0.0060  191 VAL A CG1 
1652 C CG2 . VAL A 191 ? 0.2392 0.1873 0.1579 0.0830  0.0087  0.0055  191 VAL A CG2 
1653 N N   . SER A 192 ? 0.1798 0.1167 0.0980 0.0753  0.0121  0.0083  192 SER A N   
1654 C CA  . SER A 192 ? 0.2408 0.1749 0.1592 0.0735  0.0131  0.0089  192 SER A CA  
1655 C C   . SER A 192 ? 0.2493 0.1850 0.1701 0.0728  0.0130  0.0086  192 SER A C   
1656 O O   . SER A 192 ? 0.2418 0.1807 0.1641 0.0735  0.0122  0.0080  192 SER A O   
1657 C CB  . SER A 192 ? 0.2240 0.1561 0.1417 0.0713  0.0138  0.0096  192 SER A CB  
1658 O OG  . SER A 192 ? 0.2526 0.1862 0.1718 0.0699  0.0135  0.0096  192 SER A OG  
1659 N N   . THR A 193 ? 0.2701 0.2036 0.1914 0.0712  0.0138  0.0090  193 THR A N   
1660 C CA  . THR A 193 ? 0.2398 0.1744 0.1632 0.0702  0.0138  0.0088  193 THR A CA  
1661 C C   . THR A 193 ? 0.2206 0.1529 0.1442 0.0676  0.0147  0.0095  193 THR A C   
1662 O O   . THR A 193 ? 0.2139 0.1438 0.1359 0.0668  0.0153  0.0100  193 THR A O   
1663 C CB  . THR A 193 ? 0.2182 0.1532 0.1424 0.0716  0.0136  0.0082  193 THR A CB  
1664 O OG1 . THR A 193 ? 0.2562 0.1929 0.1827 0.0708  0.0135  0.0079  193 THR A OG1 
1665 C CG2 . THR A 193 ? 0.3123 0.2440 0.2354 0.0712  0.0145  0.0086  193 THR A CG2 
1666 N N   . SER A 194 ? 0.2272 0.1601 0.1527 0.0664  0.0147  0.0094  194 SER A N   
1667 C CA  . SER A 194 ? 0.2560 0.1871 0.1819 0.0640  0.0155  0.0099  194 SER A CA  
1668 C C   . SER A 194 ? 0.2470 0.1775 0.1740 0.0637  0.0160  0.0098  194 SER A C   
1669 O O   . SER A 194 ? 0.2367 0.1687 0.1646 0.0653  0.0155  0.0092  194 SER A O   
1670 C CB  . SER A 194 ? 0.2143 0.1468 0.1416 0.0624  0.0152  0.0100  194 SER A CB  
1671 O OG  . SER A 194 ? 0.2643 0.1971 0.1907 0.0623  0.0148  0.0101  194 SER A OG  
1672 N N   . PRO A 195 ? 0.2840 0.1853 0.2018 0.0303  -0.0420 -0.0326 195 PRO A N   
1673 C CA  . PRO A 195 ? 0.2809 0.1841 0.1957 0.0253  -0.0435 -0.0311 195 PRO A CA  
1674 C C   . PRO A 195 ? 0.2931 0.1983 0.2088 0.0262  -0.0435 -0.0337 195 PRO A C   
1675 O O   . PRO A 195 ? 0.2217 0.1320 0.1432 0.0297  -0.0415 -0.0344 195 PRO A O   
1676 C CB  . PRO A 195 ? 0.2985 0.2117 0.2185 0.0226  -0.0418 -0.0257 195 PRO A CB  
1677 C CG  . PRO A 195 ? 0.3542 0.2674 0.2771 0.0251  -0.0402 -0.0242 195 PRO A CG  
1678 C CD  . PRO A 195 ? 0.2463 0.1524 0.1682 0.0302  -0.0402 -0.0286 195 PRO A CD  
1679 N N   . TYR A 196 ? 0.3378 0.2389 0.2477 0.0228  -0.0459 -0.0350 196 TYR A N   
1680 C CA  . TYR A 196 ? 0.2985 0.1960 0.2060 0.0243  -0.0468 -0.0392 196 TYR A CA  
1681 C C   . TYR A 196 ? 0.2737 0.1795 0.1879 0.0268  -0.0446 -0.0393 196 TYR A C   
1682 O O   . TYR A 196 ? 0.2645 0.1679 0.1799 0.0310  -0.0441 -0.0429 196 TYR A O   
1683 C CB  . TYR A 196 ? 0.2813 0.1754 0.1824 0.0194  -0.0494 -0.0394 196 TYR A CB  
1684 C CG  . TYR A 196 ? 0.3689 0.2550 0.2649 0.0210  -0.0510 -0.0444 196 TYR A CG  
1685 C CD1 . TYR A 196 ? 0.3159 0.2056 0.2150 0.0230  -0.0501 -0.0464 196 TYR A CD1 
1686 C CD2 . TYR A 196 ? 0.3342 0.2141 0.2270 0.0200  -0.0516 -0.0448 196 TYR A CD2 
1687 C CE1 . TYR A 196 ? 0.3487 0.2377 0.2492 0.0235  -0.0490 -0.0474 196 TYR A CE1 
1688 C CE2 . TYR A 196 ? 0.3795 0.2590 0.2737 0.0206  -0.0505 -0.0459 196 TYR A CE2 
1689 C CZ  . TYR A 196 ? 0.3035 0.1874 0.2014 0.0222  -0.0492 -0.0471 196 TYR A CZ  
1690 O OH  . TYR A 196 ? 0.3240 0.2073 0.2230 0.0227  -0.0482 -0.0480 196 TYR A OH  
1691 N N   . TYR A 197 ? 0.2463 0.1617 0.1648 0.0242  -0.0434 -0.0355 197 TYR A N   
1692 C CA  . TYR A 197 ? 0.2740 0.1975 0.1987 0.0261  -0.0415 -0.0355 197 TYR A CA  
1693 C C   . TYR A 197 ? 0.2072 0.1391 0.1401 0.0288  -0.0384 -0.0328 197 TYR A C   
1694 O O   . TYR A 197 ? 0.2368 0.1772 0.1753 0.0294  -0.0366 -0.0314 197 TYR A O   
1695 C CB  . TYR A 197 ? 0.2881 0.2167 0.2121 0.0216  -0.0422 -0.0336 197 TYR A CB  
1696 C CG  . TYR A 197 ? 0.2552 0.1758 0.1718 0.0199  -0.0449 -0.0372 197 TYR A CG  
1697 C CD1 . TYR A 197 ? 0.2401 0.1575 0.1563 0.0233  -0.0449 -0.0415 197 TYR A CD1 
1698 C CD2 . TYR A 197 ? 0.2733 0.1890 0.1833 0.0152  -0.0474 -0.0363 197 TYR A CD2 
1699 C CE1 . TYR A 197 ? 0.3140 0.2238 0.2234 0.0220  -0.0473 -0.0448 197 TYR A CE1 
1700 C CE2 . TYR A 197 ? 0.3471 0.2551 0.2501 0.0138  -0.0498 -0.0397 197 TYR A CE2 
1701 C CZ  . TYR A 197 ? 0.3394 0.2444 0.2421 0.0172  -0.0497 -0.0439 197 TYR A CZ  
1702 O OH  . TYR A 197 ? 0.3927 0.2899 0.2885 0.0159  -0.0520 -0.0472 197 TYR A OH  
1703 N N   . HIS A 198 ? 0.2029 0.1321 0.1364 0.0308  -0.0378 -0.0322 198 HIS A N   
1704 C CA  . HIS A 198 ? 0.1880 0.1243 0.1289 0.0337  -0.0348 -0.0298 198 HIS A CA  
1705 C C   . HIS A 198 ? 0.2453 0.1922 0.1910 0.0305  -0.0334 -0.0247 198 HIS A C   
1706 O O   . HIS A 198 ? 0.1955 0.1506 0.1479 0.0324  -0.0310 -0.0235 198 HIS A O   
1707 C CB  . HIS A 198 ? 0.1844 0.1219 0.1294 0.0388  -0.0332 -0.0330 198 HIS A CB  
1708 C CG  . HIS A 198 ? 0.2603 0.2020 0.2117 0.0428  -0.0305 -0.0319 198 HIS A CG  
1709 N ND1 . HIS A 198 ? 0.2230 0.1751 0.1819 0.0435  -0.0278 -0.0290 198 HIS A ND1 
1710 C CD2 . HIS A 198 ? 0.2077 0.1445 0.1593 0.0465  -0.0300 -0.0335 198 HIS A CD2 
1711 C CE1 . HIS A 198 ? 0.2120 0.1655 0.1753 0.0474  -0.0258 -0.0288 198 HIS A CE1 
1712 N NE2 . HIS A 198 ? 0.2305 0.1749 0.1895 0.0492  -0.0271 -0.0315 198 HIS A NE2 
1713 N N   . PRO A 199 ? 0.2294 0.1765 0.1720 0.0256  -0.0346 -0.0216 199 PRO A N   
1714 C CA  . PRO A 199 ? 0.2793 0.2366 0.2267 0.0225  -0.0332 -0.0165 199 PRO A CA  
1715 C C   . PRO A 199 ? 0.2543 0.2151 0.2058 0.0236  -0.0312 -0.0131 199 PRO A C   
1716 O O   . PRO A 199 ? 0.3306 0.2857 0.2809 0.0263  -0.0311 -0.0145 199 PRO A O   
1717 C CB  . PRO A 199 ? 0.2679 0.2225 0.2092 0.0168  -0.0358 -0.0151 199 PRO A CB  
1718 C CG  . PRO A 199 ? 0.3378 0.2814 0.2725 0.0172  -0.0378 -0.0176 199 PRO A CG  
1719 C CD  . PRO A 199 ? 0.2940 0.2322 0.2287 0.0226  -0.0375 -0.0225 199 PRO A CD  
1720 N N   . LEU A 200 ? 0.2689 0.2394 0.2253 0.0212  -0.0296 -0.0084 200 LEU A N   
1721 C CA  . LEU A 200 ? 0.2347 0.2094 0.1950 0.0214  -0.0277 -0.0045 200 LEU A CA  
1722 C C   . LEU A 200 ? 0.3131 0.2846 0.2684 0.0167  -0.0297 -0.0020 200 LEU A C   
1723 O O   . LEU A 200 ? 0.2786 0.2557 0.2344 0.0124  -0.0299 0.0018  200 LEU A O   
1724 C CB  . LEU A 200 ? 0.2329 0.2196 0.2011 0.0215  -0.0249 -0.0007 200 LEU A CB  
1725 C CG  . LEU A 200 ? 0.2373 0.2275 0.2111 0.0265  -0.0227 -0.0028 200 LEU A CG  
1726 C CD1 . LEU A 200 ? 0.3141 0.3163 0.2951 0.0258  -0.0202 0.0009  200 LEU A CD1 
1727 C CD2 . LEU A 200 ? 0.2982 0.2850 0.2738 0.0311  -0.0212 -0.0043 200 LEU A CD2 
1728 N N   . ILE A 201 ? 0.2576 0.2197 0.2078 0.0175  -0.0311 -0.0041 201 ILE A N   
1729 C CA  . ILE A 201 ? 0.2874 0.2451 0.2320 0.0132  -0.0332 -0.0022 201 ILE A CA  
1730 C C   . ILE A 201 ? 0.2227 0.1884 0.1715 0.0105  -0.0316 0.0035  201 ILE A C   
1731 O O   . ILE A 201 ? 0.2574 0.2247 0.2037 0.0056  -0.0330 0.0062  201 ILE A O   
1732 C CB  . ILE A 201 ? 0.2730 0.2199 0.2124 0.0151  -0.0346 -0.0052 201 ILE A CB  
1733 C CG1 . ILE A 201 ? 0.2683 0.2069 0.2025 0.0166  -0.0367 -0.0106 201 ILE A CG1 
1734 C CG2 . ILE A 201 ? 0.1987 0.1418 0.1332 0.0109  -0.0363 -0.0029 201 ILE A CG2 
1735 C CD1 . ILE A 201 ? 0.2643 0.1989 0.1918 0.0118  -0.0396 -0.0111 201 ILE A CD1 
1736 N N   . PRO A 202 ? 0.2420 0.2131 0.1970 0.0134  -0.0288 0.0057  202 PRO A N   
1737 C CA  . PRO A 202 ? 0.2082 0.1865 0.1667 0.0107  -0.0274 0.0112  202 PRO A CA  
1738 C C   . PRO A 202 ? 0.2439 0.2312 0.2051 0.0068  -0.0271 0.0147  202 PRO A C   
1739 O O   . PRO A 202 ? 0.2207 0.2112 0.1816 0.0028  -0.0275 0.0188  202 PRO A O   
1740 C CB  . PRO A 202 ? 0.2761 0.2586 0.2412 0.0153  -0.0241 0.0121  202 PRO A CB  
1741 C CG  . PRO A 202 ? 0.2553 0.2290 0.2177 0.0197  -0.0247 0.0071  202 PRO A CG  
1742 C CD  . PRO A 202 ? 0.2530 0.2221 0.2110 0.0191  -0.0270 0.0031  202 PRO A CD  
1743 N N   . ILE A 203 ? 0.2440 0.2355 0.2080 0.0080  -0.0265 0.0131  203 ILE A N   
1744 C CA  . ILE A 203 ? 0.2204 0.2206 0.1870 0.0044  -0.0263 0.0163  203 ILE A CA  
1745 C C   . ILE A 203 ? 0.2173 0.2130 0.1770 -0.0005 -0.0296 0.0158  203 ILE A C   
1746 O O   . ILE A 203 ? 0.2407 0.2413 0.2004 -0.0051 -0.0301 0.0197  203 ILE A O   
1747 C CB  . ILE A 203 ? 0.2350 0.2411 0.2068 0.0073  -0.0246 0.0148  203 ILE A CB  
1748 C CG1 . ILE A 203 ? 0.2451 0.2578 0.2246 0.0112  -0.0211 0.0167  203 ILE A CG1 
1749 C CG2 . ILE A 203 ? 0.2020 0.2157 0.1752 0.0034  -0.0250 0.0172  203 ILE A CG2 
1750 C CD1 . ILE A 203 ? 0.2246 0.2434 0.2096 0.0143  -0.0191 0.0154  203 ILE A CD1 
1751 N N   . LEU A 204 ? 0.1730 0.1592 0.1265 0.0003  -0.0319 0.0110  204 LEU A N   
1752 C CA  . LEU A 204 ? 0.2662 0.2475 0.2127 -0.0043 -0.0350 0.0104  204 LEU A CA  
1753 C C   . LEU A 204 ? 0.2689 0.2482 0.2123 -0.0081 -0.0361 0.0136  204 LEU A C   
1754 O O   . LEU A 204 ? 0.2552 0.2354 0.1954 -0.0131 -0.0379 0.0157  204 LEU A O   
1755 C CB  . LEU A 204 ? 0.2564 0.2271 0.1967 -0.0025 -0.0372 0.0047  204 LEU A CB  
1756 C CG  . LEU A 204 ? 0.1771 0.1483 0.1195 0.0013  -0.0364 0.0009  204 LEU A CG  
1757 C CD1 . LEU A 204 ? 0.2618 0.2219 0.1971 0.0023  -0.0389 -0.0044 204 LEU A CD1 
1758 C CD2 . LEU A 204 ? 0.2129 0.1930 0.1587 -0.0010 -0.0359 0.0028  204 LEU A CD2 
1759 N N   . LEU A 205 ? 0.3067 0.2832 0.2508 -0.0058 -0.0351 0.0142  205 LEU A N   
1760 C CA  . LEU A 205 ? 0.3091 0.2834 0.2502 -0.0092 -0.0361 0.0171  205 LEU A CA  
1761 C C   . LEU A 205 ? 0.2549 0.2395 0.2014 -0.0119 -0.0343 0.0231  205 LEU A C   
1762 O O   . LEU A 205 ? 0.3248 0.3096 0.2686 -0.0165 -0.0357 0.0260  205 LEU A O   
1763 C CB  . LEU A 205 ? 0.2474 0.2146 0.1871 -0.0058 -0.0357 0.0155  205 LEU A CB  
1764 C CG  . LEU A 205 ? 0.2362 0.1916 0.1689 -0.0042 -0.0381 0.0102  205 LEU A CG  
1765 C CD1 . LEU A 205 ? 0.2523 0.2021 0.1848 -0.0006 -0.0373 0.0091  205 LEU A CD1 
1766 C CD2 . LEU A 205 ? 0.2220 0.1716 0.1472 -0.0092 -0.0413 0.0102  205 LEU A CD2 
1767 N N   . ASN A 206 ? 0.2498 0.2430 0.2039 -0.0092 -0.0313 0.0249  206 ASN A N   
1768 C CA  . ASN A 206 ? 0.2559 0.2586 0.2156 -0.0110 -0.0293 0.0305  206 ASN A CA  
1769 C C   . ASN A 206 ? 0.2221 0.2340 0.1898 -0.0079 -0.0262 0.0315  206 ASN A C   
1770 O O   . ASN A 206 ? 0.2103 0.2236 0.1823 -0.0038 -0.0238 0.0315  206 ASN A O   
1771 C CB  . ASN A 206 ? 0.2542 0.2543 0.2139 -0.0104 -0.0285 0.0325  206 ASN A CB  
1772 C CG  . ASN A 206 ? 0.3591 0.3692 0.3250 -0.0117 -0.0260 0.0383  206 ASN A CG  
1773 O OD1 . ASN A 206 ? 0.4203 0.4381 0.3887 -0.0150 -0.0258 0.0415  206 ASN A OD1 
1774 N ND2 . ASN A 206 ? 0.3779 0.3878 0.3464 -0.0091 -0.0241 0.0396  206 ASN A ND2 
1775 N N   . PRO A 207 ? 0.2599 0.2782 0.2297 -0.0097 -0.0262 0.0323  207 PRO A N   
1776 C CA  . PRO A 207 ? 0.2565 0.2833 0.2338 -0.0066 -0.0234 0.0328  207 PRO A CA  
1777 C C   . PRO A 207 ? 0.1952 0.2302 0.1794 -0.0056 -0.0203 0.0374  207 PRO A C   
1778 O O   . PRO A 207 ? 0.1844 0.2245 0.1746 -0.0017 -0.0176 0.0373  207 PRO A O   
1779 C CB  . PRO A 207 ? 0.3167 0.3487 0.2940 -0.0100 -0.0244 0.0336  207 PRO A CB  
1780 C CG  . PRO A 207 ? 0.3008 0.3242 0.2697 -0.0134 -0.0280 0.0312  207 PRO A CG  
1781 C CD  . PRO A 207 ? 0.2823 0.3001 0.2476 -0.0147 -0.0289 0.0326  207 PRO A CD  
1782 N N   . ASN A 208 ? 0.1862 0.2230 0.1698 -0.0091 -0.0205 0.0416  208 ASN A N   
1783 C CA  . ASN A 208 ? 0.2209 0.2650 0.2108 -0.0082 -0.0175 0.0462  208 ASN A CA  
1784 C C   . ASN A 208 ? 0.2981 0.3385 0.2898 -0.0031 -0.0156 0.0444  208 ASN A C   
1785 O O   . ASN A 208 ? 0.2357 0.2826 0.2335 -0.0013 -0.0127 0.0475  208 ASN A O   
1786 C CB  . ASN A 208 ? 0.2507 0.2959 0.2387 -0.0130 -0.0184 0.0506  208 ASN A CB  
1787 C CG  . ASN A 208 ? 0.3137 0.3664 0.3027 -0.0179 -0.0192 0.0541  208 ASN A CG  
1788 O OD1 . ASN A 208 ? 0.2882 0.3473 0.2810 -0.0174 -0.0183 0.0541  208 ASN A OD1 
1789 N ND2 . ASN A 208 ? 0.4134 0.4654 0.3991 -0.0226 -0.0208 0.0571  208 ASN A ND2 
1790 N N   . CYS A 209 ? 0.3051 0.3355 0.2918 -0.0006 -0.0172 0.0396  209 CYS A N   
1791 C CA  . CYS A 209 ? 0.2838 0.3107 0.2722 0.0042  -0.0154 0.0379  209 CYS A CA  
1792 C C   . CYS A 209 ? 0.2291 0.2619 0.2243 0.0087  -0.0125 0.0372  209 CYS A C   
1793 O O   . CYS A 209 ? 0.2341 0.2667 0.2325 0.0125  -0.0103 0.0371  209 CYS A O   
1794 C CB  . CYS A 209 ? 0.2943 0.3090 0.2758 0.0058  -0.0178 0.0328  209 CYS A CB  
1795 S SG  . CYS A 209 ? 0.3036 0.3139 0.2833 0.0089  -0.0189 0.0267  209 CYS A SG  
1796 N N   . VAL A 210 ? 0.2283 0.2666 0.2260 0.0083  -0.0123 0.0367  210 VAL A N   
1797 C CA  . VAL A 210 ? 0.1909 0.2356 0.1954 0.0124  -0.0094 0.0363  210 VAL A CA  
1798 C C   . VAL A 210 ? 0.2176 0.2713 0.2290 0.0128  -0.0062 0.0413  210 VAL A C   
1799 O O   . VAL A 210 ? 0.3061 0.3636 0.3230 0.0169  -0.0034 0.0411  210 VAL A O   
1800 C CB  . VAL A 210 ? 0.2615 0.3107 0.2672 0.0114  -0.0099 0.0351  210 VAL A CB  
1801 C CG1 . VAL A 210 ? 0.1830 0.2231 0.1823 0.0118  -0.0128 0.0298  210 VAL A CG1 
1802 C CG2 . VAL A 210 ? 0.3231 0.3795 0.3297 0.0062  -0.0104 0.0397  210 VAL A CG2 
1803 N N   . TYR A 211 ? 0.2044 0.2618 0.2157 0.0086  -0.0064 0.0459  211 TYR A N   
1804 C CA  . TYR A 211 ? 0.2771 0.3430 0.2948 0.0087  -0.0034 0.0510  211 TYR A CA  
1805 C C   . TYR A 211 ? 0.3158 0.3780 0.3342 0.0118  -0.0017 0.0512  211 TYR A C   
1806 O O   . TYR A 211 ? 0.2702 0.3392 0.2945 0.0133  0.0013  0.0545  211 TYR A O   
1807 C CB  . TYR A 211 ? 0.2874 0.3581 0.3046 0.0031  -0.0042 0.0559  211 TYR A CB  
1808 C CG  . TYR A 211 ? 0.2993 0.3750 0.3164 -0.0003 -0.0055 0.0566  211 TYR A CG  
1809 C CD1 . TYR A 211 ? 0.2557 0.3404 0.2791 0.0010  -0.0034 0.0577  211 TYR A CD1 
1810 C CD2 . TYR A 211 ? 0.3173 0.3888 0.3282 -0.0048 -0.0088 0.0562  211 TYR A CD2 
1811 C CE1 . TYR A 211 ? 0.2869 0.3762 0.3102 -0.0022 -0.0046 0.0584  211 TYR A CE1 
1812 C CE2 . TYR A 211 ? 0.2930 0.3689 0.3037 -0.0080 -0.0100 0.0568  211 TYR A CE2 
1813 C CZ  . TYR A 211 ? 0.2220 0.3068 0.2390 -0.0067 -0.0079 0.0579  211 TYR A CZ  
1814 O OH  . TYR A 211 ? 0.3102 0.3996 0.3270 -0.0099 -0.0091 0.0586  211 TYR A OH  
1815 N N   . GLU A 212 ? 0.2666 0.3184 0.2791 0.0129  -0.0037 0.0476  212 GLU A N   
1816 C CA  . GLU A 212 ? 0.2757 0.3236 0.2886 0.0159  -0.0022 0.0477  212 GLU A CA  
1817 C C   . GLU A 212 ? 0.3552 0.4059 0.3737 0.0213  0.0007  0.0462  212 GLU A C   
1818 O O   . GLU A 212 ? 0.2923 0.3443 0.3139 0.0234  0.0031  0.0481  212 GLU A O   
1819 C CB  . GLU A 212 ? 0.3091 0.3450 0.3143 0.0160  -0.0051 0.0438  212 GLU A CB  
1820 C CG  . GLU A 212 ? 0.2252 0.2576 0.2245 0.0108  -0.0081 0.0449  212 GLU A CG  
1821 C CD  . GLU A 212 ? 0.3238 0.3443 0.3154 0.0109  -0.0110 0.0409  212 GLU A CD  
1822 O OE1 . GLU A 212 ? 0.3239 0.3386 0.3148 0.0152  -0.0105 0.0374  212 GLU A OE1 
1823 O OE2 . GLU A 212 ? 0.3663 0.3831 0.3525 0.0068  -0.0137 0.0411  212 GLU A OE2 
1824 N N   . THR A 213 ? 0.3041 0.3556 0.3239 0.0235  0.0007  0.0429  213 THR A N   
1825 C CA  . THR A 213 ? 0.2668 0.3211 0.2919 0.0286  0.0035  0.0414  213 THR A CA  
1826 C C   . THR A 213 ? 0.3229 0.3879 0.3548 0.0288  0.0057  0.0436  213 THR A C   
1827 O O   . THR A 213 ? 0.3321 0.4019 0.3698 0.0323  0.0088  0.0444  213 THR A O   
1828 C CB  . THR A 213 ? 0.3749 0.4209 0.3965 0.0320  0.0020  0.0353  213 THR A CB  
1829 O OG1 . THR A 213 ? 0.4786 0.5226 0.4964 0.0296  -0.0007 0.0330  213 THR A OG1 
1830 C CG2 . THR A 213 ? 0.3190 0.3550 0.3355 0.0332  0.0007  0.0331  213 THR A CG2 
1831 N N   . THR A 214 ? 0.3165 0.3850 0.3476 0.0253  0.0043  0.0443  214 THR A N   
1832 C CA  . THR A 214 ? 0.3707 0.4496 0.4079 0.0250  0.0062  0.0466  214 THR A CA  
1833 C C   . THR A 214 ? 0.3449 0.4297 0.3823 0.0197  0.0056  0.0515  214 THR A C   
1834 O O   . THR A 214 ? 0.3195 0.4054 0.3546 0.0164  0.0036  0.0513  214 THR A O   
1835 C CB  . THR A 214 ? 0.3922 0.4700 0.4284 0.0261  0.0049  0.0424  214 THR A CB  
1836 O OG1 . THR A 214 ? 0.2914 0.3628 0.3206 0.0227  0.0013  0.0404  214 THR A OG1 
1837 C CG2 . THR A 214 ? 0.4213 0.4942 0.4581 0.0316  0.0057  0.0378  214 THR A CG2 
1838 N N   . PRO A 215 ? 0.3555 0.4446 0.3959 0.0188  0.0075  0.0561  215 PRO A N   
1839 C CA  . PRO A 215 ? 0.3337 0.4280 0.3739 0.0135  0.0068  0.0609  215 PRO A CA  
1840 C C   . PRO A 215 ? 0.3692 0.4732 0.4138 0.0116  0.0075  0.0633  215 PRO A C   
1841 O O   . PRO A 215 ? 0.3591 0.4658 0.4019 0.0068  0.0059  0.0659  215 PRO A O   
1842 C CB  . PRO A 215 ? 0.2849 0.3821 0.3285 0.0141  0.0092  0.0651  215 PRO A CB  
1843 C CG  . PRO A 215 ? 0.3284 0.4258 0.3762 0.0197  0.0121  0.0633  215 PRO A CG  
1844 C CD  . PRO A 215 ? 0.3412 0.4304 0.3849 0.0224  0.0102  0.0571  215 PRO A CD  
1845 N N   . ASN A 216 ? 0.3992 0.5088 0.4495 0.0150  0.0099  0.0626  216 ASN A N   
1846 C CA  . ASN A 216 ? 0.4466 0.5660 0.5015 0.0134  0.0109  0.0651  216 ASN A CA  
1847 C C   . ASN A 216 ? 0.4315 0.5489 0.4836 0.0128  0.0087  0.0612  216 ASN A C   
1848 O O   . ASN A 216 ? 0.3284 0.4536 0.3843 0.0119  0.0095  0.0627  216 ASN A O   
1849 C CB  . ASN A 216 ? 0.4683 0.5917 0.5284 0.0168  0.0143  0.0658  216 ASN A CB  
1850 C CG  . ASN A 216 ? 0.5282 0.6491 0.5874 0.0167  0.0155  0.0686  216 ASN A CG  
1851 O OD1 . ASN A 216 ? 0.4866 0.6109 0.5462 0.0133  0.0148  0.0727  216 ASN A OD1 
1852 N ND2 . ASN A 216 ? 0.6022 0.7167 0.6599 0.0199  0.0170  0.0662  216 ASN A ND2 
1853 N N   . VAL A 217 ? 0.3721 0.4794 0.4176 0.0133  0.0060  0.0565  217 VAL A N   
1854 C CA  . VAL A 217 ? 0.3405 0.4453 0.3833 0.0130  0.0039  0.0525  217 VAL A CA  
1855 C C   . VAL A 217 ? 0.3338 0.4413 0.3738 0.0074  0.0017  0.0547  217 VAL A C   
1856 O O   . VAL A 217 ? 0.3557 0.4631 0.3935 0.0036  0.0006  0.0580  217 VAL A O   
1857 C CB  . VAL A 217 ? 0.3488 0.4416 0.3851 0.0152  0.0017  0.0469  217 VAL A CB  
1858 C CG1 . VAL A 217 ? 0.3403 0.4260 0.3693 0.0110  -0.0016 0.0469  217 VAL A CG1 
1859 C CG2 . VAL A 217 ? 0.3619 0.4529 0.3974 0.0171  0.0008  0.0424  217 VAL A CG2 
1860 N N   . LYS A 218 ? 0.2664 0.3764 0.3067 0.0070  0.0009  0.0529  218 LYS A N   
1861 C CA  . LYS A 218 ? 0.2301 0.3418 0.2673 0.0019  -0.0015 0.0541  218 LYS A CA  
1862 C C   . LYS A 218 ? 0.3109 0.4129 0.3409 0.0017  -0.0047 0.0488  218 LYS A C   
1863 O O   . LYS A 218 ? 0.3214 0.4210 0.3516 0.0051  -0.0045 0.0447  218 LYS A O   
1864 C CB  . LYS A 218 ? 0.3738 0.4960 0.4168 0.0014  0.0001  0.0563  218 LYS A CB  
1865 C CG  . LYS A 218 ? 0.4945 0.6271 0.5446 0.0009  0.0031  0.0620  218 LYS A CG  
1866 C CD  . LYS A 218 ? 0.6219 0.7624 0.6732 -0.0040 0.0024  0.0660  218 LYS A CD  
1867 C CE  . LYS A 218 ? 0.6377 0.7879 0.6960 -0.0034 0.0056  0.0705  218 LYS A CE  
1868 N NZ  . LYS A 218 ? 0.6762 0.8269 0.7342 -0.0025 0.0056  0.0685  218 LYS A NZ  
1869 N N   . ILE A 219 ? 0.3223 0.4186 0.3458 -0.0024 -0.0077 0.0489  219 ILE A N   
1870 C CA  . ILE A 219 ? 0.3602 0.4472 0.3764 -0.0031 -0.0108 0.0441  219 ILE A CA  
1871 C C   . ILE A 219 ? 0.3698 0.4587 0.3826 -0.0087 -0.0132 0.0459  219 ILE A C   
1872 O O   . ILE A 219 ? 0.3407 0.4367 0.3560 -0.0123 -0.0127 0.0508  219 ILE A O   
1873 C CB  . ILE A 219 ? 0.3698 0.4460 0.3802 -0.0022 -0.0124 0.0417  219 ILE A CB  
1874 C CG1 . ILE A 219 ? 0.3805 0.4564 0.3886 -0.0064 -0.0133 0.0457  219 ILE A CG1 
1875 C CG2 . ILE A 219 ? 0.3305 0.4047 0.3442 0.0035  -0.0100 0.0398  219 ILE A CG2 
1876 C CD1 . ILE A 219 ? 0.3092 0.3738 0.3099 -0.0069 -0.0158 0.0431  219 ILE A CD1 
1877 N N   . PRO A 220 ? 0.3368 0.4198 0.3442 -0.0097 -0.0158 0.0420  220 PRO A N   
1878 C CA  . PRO A 220 ? 0.3905 0.4747 0.3941 -0.0152 -0.0182 0.0434  220 PRO A CA  
1879 C C   . PRO A 220 ? 0.3889 0.4690 0.3876 -0.0194 -0.0202 0.0457  220 PRO A C   
1880 O O   . PRO A 220 ? 0.3864 0.4616 0.3838 -0.0181 -0.0200 0.0456  220 PRO A O   
1881 C CB  . PRO A 220 ? 0.3499 0.4272 0.3484 -0.0145 -0.0204 0.0380  220 PRO A CB  
1882 C CG  . PRO A 220 ? 0.2981 0.3695 0.2970 -0.0088 -0.0194 0.0337  220 PRO A CG  
1883 C CD  . PRO A 220 ? 0.4033 0.4804 0.4091 -0.0056 -0.0161 0.0363  220 PRO A CD  
1884 N N   . ASP A 221 ? 0.3932 0.4754 0.3892 -0.0246 -0.0222 0.0476  221 ASP A N   
1885 C CA  . ASP A 221 ? 0.3885 0.4673 0.3794 -0.0293 -0.0244 0.0499  221 ASP A CA  
1886 C C   . ASP A 221 ? 0.3955 0.4624 0.3778 -0.0299 -0.0276 0.0451  221 ASP A C   
1887 O O   . ASP A 221 ? 0.3746 0.4394 0.3532 -0.0318 -0.0296 0.0428  221 ASP A O   
1888 C CB  . ASP A 221 ? 0.4161 0.5031 0.4084 -0.0345 -0.0250 0.0543  221 ASP A CB  
1889 C CG  . ASP A 221 ? 0.4964 0.5793 0.4827 -0.0398 -0.0277 0.0561  221 ASP A CG  
1890 O OD1 . ASP A 221 ? 0.6013 0.6796 0.5857 -0.0396 -0.0279 0.0568  221 ASP A OD1 
1891 O OD2 . ASP A 221 ? 0.5080 0.5925 0.4916 -0.0442 -0.0297 0.0569  221 ASP A OD2 
1892 N N   . PHE A 222 ? 0.2916 0.3505 0.2706 -0.0283 -0.0281 0.0435  222 PHE A N   
1893 C CA  . PHE A 222 ? 0.2629 0.3100 0.2336 -0.0286 -0.0310 0.0389  222 PHE A CA  
1894 C C   . PHE A 222 ? 0.3693 0.4140 0.3343 -0.0346 -0.0338 0.0409  222 PHE A C   
1895 O O   . PHE A 222 ? 0.3312 0.3717 0.2932 -0.0363 -0.0347 0.0423  222 PHE A O   
1896 C CB  . PHE A 222 ? 0.2983 0.3381 0.2680 -0.0246 -0.0304 0.0367  222 PHE A CB  
1897 C CG  . PHE A 222 ? 0.2883 0.3264 0.2606 -0.0188 -0.0288 0.0326  222 PHE A CG  
1898 C CD1 . PHE A 222 ? 0.2991 0.3452 0.2793 -0.0153 -0.0255 0.0343  222 PHE A CD1 
1899 C CD2 . PHE A 222 ? 0.2940 0.3226 0.2610 -0.0168 -0.0306 0.0271  222 PHE A CD2 
1900 C CE1 . PHE A 222 ? 0.3037 0.3483 0.2865 -0.0100 -0.0240 0.0307  222 PHE A CE1 
1901 C CE2 . PHE A 222 ? 0.2823 0.3095 0.2518 -0.0115 -0.0291 0.0235  222 PHE A CE2 
1902 C CZ  . PHE A 222 ? 0.2537 0.2889 0.2311 -0.0081 -0.0259 0.0253  222 PHE A CZ  
1903 N N   . ALA A 223 ? 0.5027 0.5501 0.4661 -0.0380 -0.0353 0.0411  223 ALA A N   
1904 C CA  . ALA A 223 ? 0.5459 0.5923 0.5043 -0.0441 -0.0379 0.0433  223 ALA A CA  
1905 C C   . ALA A 223 ? 0.5279 0.5623 0.4772 -0.0455 -0.0411 0.0393  223 ALA A C   
1906 O O   . ALA A 223 ? 0.5812 0.6138 0.5256 -0.0506 -0.0435 0.0407  223 ALA A O   
1907 C CB  . ALA A 223 ? 0.5716 0.6260 0.5321 -0.0473 -0.0381 0.0453  223 ALA A CB  
1908 N N   . VAL A 224 ? 0.4032 0.4296 0.3501 -0.0412 -0.0412 0.0344  224 VAL A N   
1909 C CA  . VAL A 224 ? 0.3866 0.4012 0.3250 -0.0420 -0.0441 0.0302  224 VAL A CA  
1910 C C   . VAL A 224 ? 0.4132 0.4210 0.3509 -0.0378 -0.0434 0.0281  224 VAL A C   
1911 O O   . VAL A 224 ? 0.4843 0.4954 0.4277 -0.0333 -0.0408 0.0281  224 VAL A O   
1912 C CB  . VAL A 224 ? 0.4720 0.4830 0.4073 -0.0410 -0.0453 0.0256  224 VAL A CB  
1913 C CG1 . VAL A 224 ? 0.4969 0.5076 0.4362 -0.0348 -0.0432 0.0222  224 VAL A CG1 
1914 C CG2 . VAL A 224 ? 0.5700 0.5696 0.4959 -0.0433 -0.0486 0.0222  224 VAL A CG2 
1915 N N   . SER A 225 ? 0.2907 0.2889 0.2213 -0.0394 -0.0457 0.0265  225 SER A N   
1916 C CA  . SER A 225 ? 0.3041 0.2952 0.2334 -0.0359 -0.0453 0.0245  225 SER A CA  
1917 C C   . SER A 225 ? 0.3288 0.3117 0.2550 -0.0317 -0.0459 0.0186  225 SER A C   
1918 O O   . SER A 225 ? 0.3067 0.2844 0.2275 -0.0332 -0.0481 0.0155  225 SER A O   
1919 C CB  . SER A 225 ? 0.3494 0.3343 0.2727 -0.0396 -0.0475 0.0258  225 SER A CB  
1920 O OG  . SER A 225 ? 0.4060 0.3827 0.3271 -0.0361 -0.0475 0.0232  225 SER A OG  
1921 N N   . PHE A 226 ? 0.3218 0.3035 0.2514 -0.0265 -0.0440 0.0169  226 PHE A N   
1922 C CA  . PHE A 226 ? 0.2354 0.2089 0.1623 -0.0221 -0.0444 0.0114  226 PHE A CA  
1923 C C   . PHE A 226 ? 0.3220 0.2862 0.2448 -0.0205 -0.0452 0.0097  226 PHE A C   
1924 O O   . PHE A 226 ? 0.3111 0.2684 0.2319 -0.0165 -0.0454 0.0053  226 PHE A O   
1925 C CB  . PHE A 226 ? 0.2420 0.2211 0.1761 -0.0169 -0.0415 0.0103  226 PHE A CB  
1926 C CG  . PHE A 226 ? 0.2821 0.2687 0.2196 -0.0176 -0.0408 0.0107  226 PHE A CG  
1927 C CD1 . PHE A 226 ? 0.2883 0.2706 0.2223 -0.0169 -0.0422 0.0065  226 PHE A CD1 
1928 C CD2 . PHE A 226 ? 0.3331 0.3310 0.2774 -0.0187 -0.0387 0.0152  226 PHE A CD2 
1929 C CE1 . PHE A 226 ? 0.3595 0.3486 0.2967 -0.0175 -0.0416 0.0068  226 PHE A CE1 
1930 C CE2 . PHE A 226 ? 0.4131 0.4179 0.3607 -0.0192 -0.0381 0.0156  226 PHE A CE2 
1931 C CZ  . PHE A 226 ? 0.3765 0.3769 0.3204 -0.0186 -0.0395 0.0114  226 PHE A CZ  
1932 N N   . ARG A 227 ? 0.3675 0.3315 0.2890 -0.0234 -0.0457 0.0130  227 ARG A N   
1933 C CA  . ARG A 227 ? 0.3502 0.3061 0.2685 -0.0216 -0.0461 0.0118  227 ARG A CA  
1934 C C   . ARG A 227 ? 0.3388 0.2830 0.2490 -0.0215 -0.0489 0.0069  227 ARG A C   
1935 O O   . ARG A 227 ? 0.3818 0.3187 0.2900 -0.0180 -0.0489 0.0039  227 ARG A O   
1936 C CB  . ARG A 227 ? 0.2991 0.2570 0.2169 -0.0255 -0.0464 0.0165  227 ARG A CB  
1937 C CG  . ARG A 227 ? 0.3564 0.3256 0.2821 -0.0256 -0.0436 0.0215  227 ARG A CG  
1938 C CD  . ARG A 227 ? 0.3849 0.3549 0.3097 -0.0291 -0.0439 0.0258  227 ARG A CD  
1939 N NE  . ARG A 227 ? 0.5254 0.4863 0.4462 -0.0274 -0.0447 0.0240  227 ARG A NE  
1940 C CZ  . ARG A 227 ? 0.5150 0.4757 0.4392 -0.0233 -0.0426 0.0241  227 ARG A CZ  
1941 N NH1 . ARG A 227 ? 0.4633 0.4326 0.3952 -0.0206 -0.0396 0.0260  227 ARG A NH1 
1942 N NH2 . ARG A 227 ? 0.5540 0.5061 0.4740 -0.0221 -0.0435 0.0223  227 ARG A NH2 
1943 N N   . GLU A 228 ? 0.3774 0.3196 0.2827 -0.0253 -0.0511 0.0061  228 GLU A N   
1944 C CA  . GLU A 228 ? 0.3173 0.2485 0.2148 -0.0255 -0.0538 0.0016  228 GLU A CA  
1945 C C   . GLU A 228 ? 0.3444 0.2725 0.2425 -0.0207 -0.0532 -0.0032 228 GLU A C   
1946 O O   . GLU A 228 ? 0.3237 0.2425 0.2175 -0.0180 -0.0542 -0.0072 228 GLU A O   
1947 C CB  . GLU A 228 ? 0.4951 0.4256 0.3874 -0.0312 -0.0563 0.0024  228 GLU A CB  
1948 C CG  . GLU A 228 ? 0.6463 0.5831 0.5397 -0.0364 -0.0564 0.0079  228 GLU A CG  
1949 C CD  . GLU A 228 ? 0.7459 0.6956 0.6478 -0.0365 -0.0539 0.0121  228 GLU A CD  
1950 O OE1 . GLU A 228 ? 0.7653 0.7205 0.6705 -0.0382 -0.0528 0.0166  228 GLU A OE1 
1951 O OE2 . GLU A 228 ? 0.8223 0.7763 0.7274 -0.0347 -0.0529 0.0108  228 GLU A OE2 
1952 N N   . ASP A 229 ? 0.3042 0.2401 0.2078 -0.0193 -0.0516 -0.0029 229 ASP A N   
1953 C CA  . ASP A 229 ? 0.3323 0.2663 0.2374 -0.0145 -0.0507 -0.0072 229 ASP A CA  
1954 C C   . ASP A 229 ? 0.2994 0.2304 0.2070 -0.0092 -0.0491 -0.0089 229 ASP A C   
1955 O O   . ASP A 229 ? 0.2901 0.2139 0.1952 -0.0057 -0.0497 -0.0134 229 ASP A O   
1956 C CB  . ASP A 229 ? 0.2423 0.1864 0.1537 -0.0140 -0.0489 -0.0059 229 ASP A CB  
1957 C CG  . ASP A 229 ? 0.3615 0.3058 0.2692 -0.0178 -0.0508 -0.0066 229 ASP A CG  
1958 O OD1 . ASP A 229 ? 0.3762 0.3123 0.2764 -0.0204 -0.0534 -0.0086 229 ASP A OD1 
1959 O OD2 . ASP A 229 ? 0.3417 0.2944 0.2541 -0.0181 -0.0495 -0.0052 229 ASP A OD2 
1960 N N   . ALA A 230 ? 0.3043 0.2407 0.2169 -0.0085 -0.0472 -0.0052 230 ALA A N   
1961 C CA  . ALA A 230 ? 0.3080 0.2416 0.2229 -0.0037 -0.0457 -0.0065 230 ALA A CA  
1962 C C   . ALA A 230 ? 0.2706 0.1923 0.1783 -0.0033 -0.0478 -0.0096 230 ALA A C   
1963 O O   . ALA A 230 ? 0.3029 0.2189 0.2099 0.0011  -0.0476 -0.0134 230 ALA A O   
1964 C CB  . ALA A 230 ? 0.2228 0.1637 0.1435 -0.0039 -0.0434 -0.0017 230 ALA A CB  
1965 N N   . SER A 231 ? 0.2806 0.1987 0.1830 -0.0079 -0.0499 -0.0080 231 SER A N   
1966 C CA  . SER A 231 ? 0.3354 0.2419 0.2303 -0.0079 -0.0522 -0.0110 231 SER A CA  
1967 C C   . SER A 231 ? 0.3006 0.2001 0.1913 -0.0059 -0.0537 -0.0163 231 SER A C   
1968 O O   . SER A 231 ? 0.3597 0.2509 0.2473 -0.0027 -0.0543 -0.0199 231 SER A O   
1969 C CB  . SER A 231 ? 0.4393 0.3435 0.3288 -0.0137 -0.0544 -0.0085 231 SER A CB  
1970 O OG  . SER A 231 ? 0.5469 0.4523 0.4377 -0.0145 -0.0537 -0.0051 231 SER A OG  
1971 N N   . LYS A 232 ? 0.3483 0.2510 0.2387 -0.0078 -0.0542 -0.0168 232 LYS A N   
1972 C CA  . LYS A 232 ? 0.2813 0.1772 0.1673 -0.0065 -0.0557 -0.0217 232 LYS A CA  
1973 C C   . LYS A 232 ? 0.2608 0.1560 0.1505 -0.0004 -0.0541 -0.0251 232 LYS A C   
1974 O O   . LYS A 232 ? 0.3315 0.2180 0.2169 0.0021  -0.0552 -0.0294 232 LYS A O   
1975 C CB  . LYS A 232 ? 0.3842 0.2845 0.2695 -0.0100 -0.0565 -0.0211 232 LYS A CB  
1976 C CG  . LYS A 232 ? 0.4623 0.3571 0.3399 -0.0154 -0.0594 -0.0208 232 LYS A CG  
1977 C CD  . LYS A 232 ? 0.5644 0.4662 0.4427 -0.0198 -0.0598 -0.0184 232 LYS A CD  
1978 C CE  . LYS A 232 ? 0.6538 0.5662 0.5383 -0.0218 -0.0581 -0.0128 232 LYS A CE  
1979 N NZ  . LYS A 232 ? 0.6649 0.5842 0.5500 -0.0267 -0.0586 -0.0097 232 LYS A NZ  
1980 N N   . HIS A 233 ? 0.2394 0.1437 0.1369 0.0020  -0.0513 -0.0232 233 HIS A N   
1981 C CA  . HIS A 233 ? 0.3282 0.2322 0.2297 0.0079  -0.0496 -0.0261 233 HIS A CA  
1982 C C   . HIS A 233 ? 0.3131 0.2085 0.2118 0.0109  -0.0500 -0.0283 233 HIS A C   
1983 O O   . HIS A 233 ? 0.3016 0.1908 0.1986 0.0146  -0.0504 -0.0326 233 HIS A O   
1984 C CB  . HIS A 233 ? 0.3066 0.2216 0.2170 0.0098  -0.0465 -0.0230 233 HIS A CB  
1985 C CG  . HIS A 233 ? 0.3097 0.2330 0.2238 0.0084  -0.0457 -0.0218 233 HIS A CG  
1986 N ND1 . HIS A 233 ? 0.2969 0.2212 0.2131 0.0116  -0.0450 -0.0250 233 HIS A ND1 
1987 C CD2 . HIS A 233 ? 0.2434 0.1747 0.1596 0.0042  -0.0454 -0.0178 233 HIS A CD2 
1988 C CE1 . HIS A 233 ? 0.2947 0.2271 0.2140 0.0094  -0.0443 -0.0230 233 HIS A CE1 
1989 N NE2 . HIS A 233 ? 0.2821 0.2188 0.2015 0.0049  -0.0446 -0.0186 233 HIS A NE2 
1990 N N   . VAL A 234 ? 0.2899 0.1851 0.1883 0.0093  -0.0500 -0.0254 234 VAL A N   
1991 C CA  . VAL A 234 ? 0.2772 0.1646 0.1731 0.0120  -0.0503 -0.0272 234 VAL A CA  
1992 C C   . VAL A 234 ? 0.2695 0.1456 0.1568 0.0109  -0.0532 -0.0308 234 VAL A C   
1993 O O   . VAL A 234 ? 0.2995 0.1683 0.1846 0.0146  -0.0537 -0.0346 234 VAL A O   
1994 C CB  . VAL A 234 ? 0.3325 0.2226 0.2301 0.0104  -0.0495 -0.0229 234 VAL A CB  
1995 C CG1 . VAL A 234 ? 0.2834 0.1648 0.1778 0.0129  -0.0501 -0.0249 234 VAL A CG1 
1996 C CG2 . VAL A 234 ? 0.2893 0.1902 0.1956 0.0120  -0.0464 -0.0195 234 VAL A CG2 
1997 N N   . GLU A 235 ? 0.2888 0.1635 0.1712 0.0058  -0.0553 -0.0295 235 GLU A N   
1998 C CA  . GLU A 235 ? 0.3130 0.1769 0.1870 0.0043  -0.0581 -0.0326 235 GLU A CA  
1999 C C   . GLU A 235 ? 0.3677 0.2271 0.2396 0.0070  -0.0588 -0.0374 235 GLU A C   
2000 O O   . GLU A 235 ? 0.3782 0.2339 0.2506 0.0092  -0.0578 -0.0387 235 GLU A O   
2001 C CB  . GLU A 235 ? 0.3386 0.2026 0.2081 -0.0019 -0.0600 -0.0300 235 GLU A CB  
2002 C CG  . GLU A 235 ? 0.5610 0.4141 0.4217 -0.0040 -0.0629 -0.0324 235 GLU A CG  
2003 C CD  . GLU A 235 ? 0.6903 0.5361 0.5494 -0.0008 -0.0628 -0.0340 235 GLU A CD  
2004 O OE1 . GLU A 235 ? 0.8061 0.6499 0.6668 0.0016  -0.0615 -0.0355 235 GLU A OE1 
2005 O OE2 . GLU A 235 ? 0.6359 0.4840 0.4977 -0.0003 -0.0618 -0.0314 235 GLU A OE2 
2006 N N   . LEU A 236 ? 0.3155 0.1814 0.1907 0.0068  -0.0579 -0.0374 236 LEU A N   
2007 C CA  . LEU A 236 ? 0.3569 0.2214 0.2330 0.0094  -0.0573 -0.0407 236 LEU A CA  
2008 C C   . LEU A 236 ? 0.3069 0.1733 0.1896 0.0152  -0.0544 -0.0418 236 LEU A C   
2009 O O   . LEU A 236 ? 0.3379 0.2043 0.2232 0.0171  -0.0530 -0.0429 236 LEU A O   
2010 C CB  . LEU A 236 ? 0.2859 0.1555 0.1626 0.0081  -0.0577 -0.0412 236 LEU A CB  
2011 C CG  . LEU A 236 ? 0.3057 0.1762 0.1782 0.0020  -0.0596 -0.0391 236 LEU A CG  
2012 C CD1 . LEU A 236 ? 0.3977 0.2785 0.2753 0.0006  -0.0583 -0.0369 236 LEU A CD1 
2013 C CD2 . LEU A 236 ? 0.3513 0.2162 0.2201 0.0009  -0.0602 -0.0409 236 LEU A CD2 
2014 N N   . ALA A 237 ? 0.3020 0.1706 0.1877 0.0178  -0.0536 -0.0413 237 ALA A N   
2015 C CA  . ALA A 237 ? 0.2716 0.1428 0.1641 0.0230  -0.0507 -0.0418 237 ALA A CA  
2016 C C   . ALA A 237 ? 0.3666 0.2343 0.2588 0.0235  -0.0503 -0.0412 237 ALA A C   
2017 O O   . ALA A 237 ? 0.3573 0.2272 0.2539 0.0262  -0.0484 -0.0417 237 ALA A O   
2018 C CB  . ALA A 237 ? 0.2682 0.1425 0.1639 0.0255  -0.0498 -0.0412 237 ALA A CB  
2019 N N   . LYS A 238 ? 0.2806 0.1432 0.1675 0.0208  -0.0521 -0.0401 238 LYS A N   
2020 C CA  . LYS A 238 ? 0.3737 0.2327 0.2598 0.0211  -0.0519 -0.0396 238 LYS A CA  
2021 C C   . LYS A 238 ? 0.3706 0.2282 0.2555 0.0201  -0.0519 -0.0405 238 LYS A C   
2022 O O   . LYS A 238 ? 0.4100 0.2678 0.2973 0.0220  -0.0507 -0.0408 238 LYS A O   
2023 C CB  . LYS A 238 ? 0.3605 0.2143 0.2407 0.0179  -0.0539 -0.0380 238 LYS A CB  
2024 C CG  . LYS A 238 ? 0.4445 0.2989 0.3254 0.0187  -0.0539 -0.0369 238 LYS A CG  
2025 C CD  . LYS A 238 ? 0.4512 0.3001 0.3257 0.0148  -0.0562 -0.0352 238 LYS A CD  
2026 C CE  . LYS A 238 ? 0.4732 0.3180 0.3463 0.0149  -0.0561 -0.0349 238 LYS A CE  
2027 N NZ  . LYS A 238 ? 0.5687 0.4082 0.4354 0.0107  -0.0584 -0.0332 238 LYS A NZ  
2028 N N   . GLU A 239 ? 0.3833 0.2398 0.2645 0.0169  -0.0534 -0.0410 239 GLU A N   
2029 C CA  . GLU A 239 ? 0.4513 0.3064 0.3314 0.0161  -0.0533 -0.0421 239 GLU A CA  
2030 C C   . GLU A 239 ? 0.4301 0.2901 0.3163 0.0195  -0.0511 -0.0433 239 GLU A C   
2031 O O   . GLU A 239 ? 0.4310 0.2905 0.3184 0.0205  -0.0502 -0.0439 239 GLU A O   
2032 C CB  . GLU A 239 ? 0.5024 0.3558 0.3774 0.0117  -0.0553 -0.0421 239 GLU A CB  
2033 C CG  . GLU A 239 ? 0.5667 0.4158 0.4356 0.0076  -0.0577 -0.0405 239 GLU A CG  
2034 C CD  . GLU A 239 ? 0.7222 0.5712 0.5866 0.0028  -0.0596 -0.0401 239 GLU A CD  
2035 O OE1 . GLU A 239 ? 0.7286 0.5807 0.5947 0.0030  -0.0591 -0.0413 239 GLU A OE1 
2036 O OE2 . GLU A 239 ? 0.7677 0.6141 0.6273 -0.0013 -0.0616 -0.0384 239 GLU A OE2 
2037 N N   . LYS A 240 ? 0.3207 0.1854 0.2106 0.0212  -0.0501 -0.0437 240 LYS A N   
2038 C CA  . LYS A 240 ? 0.3060 0.1757 0.2019 0.0243  -0.0479 -0.0446 240 LYS A CA  
2039 C C   . LYS A 240 ? 0.3728 0.2445 0.2732 0.0272  -0.0461 -0.0441 240 LYS A C   
2040 O O   . LYS A 240 ? 0.3733 0.2469 0.2766 0.0285  -0.0447 -0.0446 240 LYS A O   
2041 C CB  . LYS A 240 ? 0.3132 0.1878 0.2123 0.0256  -0.0473 -0.0450 240 LYS A CB  
2042 C CG  . LYS A 240 ? 0.3411 0.2210 0.2461 0.0283  -0.0451 -0.0458 240 LYS A CG  
2043 C CD  . LYS A 240 ? 0.4794 0.3581 0.3823 0.0265  -0.0455 -0.0470 240 LYS A CD  
2044 C CE  . LYS A 240 ? 0.4769 0.3597 0.3851 0.0289  -0.0434 -0.0476 240 LYS A CE  
2045 N NZ  . LYS A 240 ? 0.5260 0.4082 0.4324 0.0273  -0.0437 -0.0488 240 LYS A NZ  
2046 N N   . TYR A 241 ? 0.3919 0.2634 0.2929 0.0281  -0.0460 -0.0429 241 TYR A N   
2047 C CA  . TYR A 241 ? 0.4551 0.3286 0.3600 0.0304  -0.0444 -0.0422 241 TYR A CA  
2048 C C   . TYR A 241 ? 0.4676 0.3373 0.3699 0.0294  -0.0449 -0.0423 241 TYR A C   
2049 O O   . TYR A 241 ? 0.4690 0.3411 0.3748 0.0309  -0.0435 -0.0424 241 TYR A O   
2050 C CB  . TYR A 241 ? 0.4662 0.3396 0.3715 0.0312  -0.0444 -0.0409 241 TYR A CB  
2051 C CG  . TYR A 241 ? 0.4455 0.3223 0.3556 0.0335  -0.0425 -0.0401 241 TYR A CG  
2052 C CD1 . TYR A 241 ? 0.4130 0.2867 0.3212 0.0331  -0.0428 -0.0395 241 TYR A CD1 
2053 C CD2 . TYR A 241 ? 0.4655 0.3488 0.3819 0.0359  -0.0403 -0.0398 241 TYR A CD2 
2054 C CE1 . TYR A 241 ? 0.3557 0.2328 0.2682 0.0348  -0.0411 -0.0388 241 TYR A CE1 
2055 C CE2 . TYR A 241 ? 0.4684 0.3551 0.3890 0.0373  -0.0385 -0.0389 241 TYR A CE2 
2056 C CZ  . TYR A 241 ? 0.3741 0.2576 0.2927 0.0367  -0.0390 -0.0385 241 TYR A CZ  
2057 O OH  . TYR A 241 ? 0.3290 0.2159 0.2515 0.0378  -0.0373 -0.0377 241 TYR A OH  
2058 N N   . PHE A 242 ? 0.4416 0.3055 0.3377 0.0266  -0.0470 -0.0422 242 PHE A N   
2059 C CA  . PHE A 242 ? 0.4225 0.2825 0.3158 0.0255  -0.0476 -0.0423 242 PHE A CA  
2060 C C   . PHE A 242 ? 0.4651 0.3262 0.3596 0.0257  -0.0468 -0.0436 242 PHE A C   
2061 O O   . PHE A 242 ? 0.4012 0.2612 0.2957 0.0260  -0.0465 -0.0437 242 PHE A O   
2062 C CB  . PHE A 242 ? 0.3715 0.2253 0.2578 0.0222  -0.0500 -0.0419 242 PHE A CB  
2063 C CG  . PHE A 242 ? 0.4980 0.3476 0.3812 0.0211  -0.0506 -0.0419 242 PHE A CG  
2064 C CD1 . PHE A 242 ? 0.5727 0.4209 0.4560 0.0220  -0.0504 -0.0410 242 PHE A CD1 
2065 C CD2 . PHE A 242 ? 0.5035 0.3505 0.3835 0.0191  -0.0514 -0.0428 242 PHE A CD2 
2066 C CE1 . PHE A 242 ? 0.5576 0.4021 0.4381 0.0211  -0.0510 -0.0411 242 PHE A CE1 
2067 C CE2 . PHE A 242 ? 0.4919 0.3351 0.3690 0.0182  -0.0520 -0.0428 242 PHE A CE2 
2068 C CZ  . PHE A 242 ? 0.5308 0.3727 0.4081 0.0192  -0.0518 -0.0420 242 PHE A CZ  
2069 N N   . GLU A 243 ? 0.4346 0.2980 0.3300 0.0255  -0.0466 -0.0445 243 GLU A N   
2070 C CA  . GLU A 243 ? 0.4721 0.3367 0.3688 0.0257  -0.0459 -0.0456 243 GLU A CA  
2071 C C   . GLU A 243 ? 0.4729 0.3426 0.3758 0.0284  -0.0436 -0.0456 243 GLU A C   
2072 O O   . GLU A 243 ? 0.3398 0.2095 0.2435 0.0287  -0.0429 -0.0461 243 GLU A O   
2073 C CB  . GLU A 243 ? 0.4317 0.2973 0.3275 0.0245  -0.0463 -0.0465 243 GLU A CB  
2074 C CG  . GLU A 243 ? 0.6155 0.4765 0.5050 0.0210  -0.0485 -0.0466 243 GLU A CG  
2075 C CD  . GLU A 243 ? 0.7471 0.6098 0.6360 0.0197  -0.0489 -0.0475 243 GLU A CD  
2076 O OE1 . GLU A 243 ? 0.7968 0.6642 0.6904 0.0219  -0.0473 -0.0481 243 GLU A OE1 
2077 O OE2 . GLU A 243 ? 0.7915 0.6510 0.6752 0.0164  -0.0507 -0.0476 243 GLU A OE2 
2078 N N   . ILE A 244 ? 0.3886 0.2629 0.2959 0.0303  -0.0424 -0.0450 244 ILE A N   
2079 C CA  . ILE A 244 ? 0.3619 0.2416 0.2752 0.0325  -0.0402 -0.0448 244 ILE A CA  
2080 C C   . ILE A 244 ? 0.4318 0.3095 0.3444 0.0343  -0.0410 -0.0440 244 ILE A C   
2081 O O   . ILE A 244 ? 0.4210 0.2982 0.3335 0.0364  -0.0418 -0.0442 244 ILE A O   
2082 C CB  . ILE A 244 ? 0.3832 0.2680 0.3008 0.0340  -0.0391 -0.0443 244 ILE A CB  
2083 C CG1 . ILE A 244 ? 0.4110 0.2959 0.3271 0.0332  -0.0399 -0.0453 244 ILE A CG1 
2084 C CG2 . ILE A 244 ? 0.2674 0.1565 0.1894 0.0368  -0.0382 -0.0441 244 ILE A CG2 
2085 C CD1 . ILE A 244 ? 0.4787 0.3642 0.3952 0.0328  -0.0394 -0.0464 244 ILE A CD1 
2086 N N   . PHE A 245 ? 0.3862 0.2631 0.2983 0.0334  -0.0409 -0.0430 245 PHE A N   
2087 C CA  . PHE A 245 ? 0.5111 0.3869 0.4230 0.0351  -0.0414 -0.0422 245 PHE A CA  
2088 C C   . PHE A 245 ? 0.5310 0.4010 0.4380 0.0336  -0.0428 -0.0420 245 PHE A C   
2089 O O   . PHE A 245 ? 0.5477 0.4163 0.4539 0.0350  -0.0434 -0.0414 245 PHE A O   
2090 C CB  . PHE A 245 ? 0.3808 0.2604 0.2963 0.0359  -0.0401 -0.0411 245 PHE A CB  
2091 C CG  . PHE A 245 ? 0.4585 0.3439 0.3790 0.0376  -0.0387 -0.0411 245 PHE A CG  
2092 C CD1 . PHE A 245 ? 0.4127 0.3005 0.3352 0.0402  -0.0390 -0.0411 245 PHE A CD1 
2093 C CD2 . PHE A 245 ? 0.3447 0.2332 0.2675 0.0367  -0.0374 -0.0410 245 PHE A CD2 
2094 C CE1 . PHE A 245 ? 0.3473 0.2405 0.2742 0.0417  -0.0379 -0.0411 245 PHE A CE1 
2095 C CE2 . PHE A 245 ? 0.3644 0.2585 0.2919 0.0382  -0.0360 -0.0409 245 PHE A CE2 
2096 C CZ  . PHE A 245 ? 0.3864 0.2827 0.3158 0.0407  -0.0363 -0.0409 245 PHE A CZ  
2097 N N   . GLY A 246 ? 0.5493 0.4161 0.4529 0.0308  -0.0433 -0.0426 246 GLY A N   
2098 C CA  . GLY A 246 ? 0.6181 0.4795 0.5170 0.0292  -0.0447 -0.0424 246 GLY A CA  
2099 C C   . GLY A 246 ? 0.7108 0.5696 0.6074 0.0286  -0.0455 -0.0412 246 GLY A C   
2100 O O   . GLY A 246 ? 0.7659 0.6200 0.6583 0.0272  -0.0468 -0.0410 246 GLY A O   
2101 N N   . GLU A 247 ? 0.6129 0.4745 0.5119 0.0296  -0.0450 -0.0405 247 GLU A N   
2102 C CA  . GLU A 247 ? 0.5995 0.4587 0.4964 0.0292  -0.0458 -0.0393 247 GLU A CA  
2103 C C   . GLU A 247 ? 0.5306 0.3889 0.4256 0.0283  -0.0467 -0.0390 247 GLU A C   
2104 O O   . GLU A 247 ? 0.4613 0.3224 0.3581 0.0286  -0.0463 -0.0397 247 GLU A O   
2105 C CB  . GLU A 247 ? 0.6224 0.4857 0.5241 0.0314  -0.0440 -0.0385 247 GLU A CB  
2106 C CG  . GLU A 247 ? 0.7817 0.6440 0.6834 0.0316  -0.0438 -0.0383 247 GLU A CG  
2107 C CD  . GLU A 247 ? 0.8666 0.7317 0.7709 0.0347  -0.0436 -0.0384 247 GLU A CD  
2108 O OE1 . GLU A 247 ? 0.8908 0.7530 0.7926 0.0358  -0.0449 -0.0386 247 GLU A OE1 
2109 O OE2 . GLU A 247 ? 0.8598 0.7298 0.7684 0.0361  -0.0424 -0.0384 247 GLU A OE2 
2110 N N   . HIS A 248 ? 0.5634 0.4177 0.4545 0.0270  -0.0481 -0.0379 248 HIS A N   
2111 C CA  . HIS A 248 ? 0.5789 0.4327 0.4686 0.0261  -0.0489 -0.0374 248 HIS A CA  
2112 C C   . HIS A 248 ? 0.5085 0.3672 0.4035 0.0289  -0.0471 -0.0368 248 HIS A C   
2113 O O   . HIS A 248 ? 0.4314 0.2916 0.3289 0.0304  -0.0460 -0.0362 248 HIS A O   
2114 C CB  . HIS A 248 ? 0.6818 0.5293 0.5650 0.0232  -0.0511 -0.0364 248 HIS A CB  
2115 C CG  . HIS A 248 ? 0.8462 0.6893 0.7239 0.0198  -0.0530 -0.0368 248 HIS A CG  
2116 N ND1 . HIS A 248 ? 0.8822 0.7258 0.7602 0.0197  -0.0527 -0.0380 248 HIS A ND1 
2117 C CD2 . HIS A 248 ? 0.8951 0.7335 0.7666 0.0160  -0.0553 -0.0360 248 HIS A CD2 
2118 C CE1 . HIS A 248 ? 0.8869 0.7264 0.7595 0.0162  -0.0546 -0.0381 248 HIS A CE1 
2119 N NE2 . HIS A 248 ? 0.8971 0.7336 0.7657 0.0138  -0.0562 -0.0368 248 HIS A NE2 
2120 N N   . PRO A 249 ? 0.4702 0.3320 0.3673 0.0296  -0.0467 -0.0370 249 PRO A N   
2121 C CA  . PRO A 249 ? 0.4022 0.2690 0.3046 0.0323  -0.0448 -0.0363 249 PRO A CA  
2122 C C   . PRO A 249 ? 0.4145 0.2781 0.3145 0.0319  -0.0454 -0.0349 249 PRO A C   
2123 O O   . PRO A 249 ? 0.5281 0.3866 0.4226 0.0294  -0.0475 -0.0345 249 PRO A O   
2124 C CB  . PRO A 249 ? 0.3860 0.2561 0.2904 0.0328  -0.0445 -0.0370 249 PRO A CB  
2125 C CG  . PRO A 249 ? 0.4150 0.2801 0.3130 0.0296  -0.0470 -0.0376 249 PRO A CG  
2126 C CD  . PRO A 249 ? 0.4104 0.2717 0.3053 0.0280  -0.0478 -0.0379 249 PRO A CD  
2127 N N   . VAL A 250 ? 0.3682 0.2350 0.2723 0.0339  -0.0437 -0.0340 250 VAL A N   
2128 C CA  . VAL A 250 ? 0.3137 0.1785 0.2166 0.0340  -0.0438 -0.0326 250 VAL A CA  
2129 C C   . VAL A 250 ? 0.3115 0.1812 0.2192 0.0362  -0.0420 -0.0319 250 VAL A C   
2130 O O   . VAL A 250 ? 0.2883 0.1560 0.1949 0.0364  -0.0421 -0.0306 250 VAL A O   
2131 C CB  . VAL A 250 ? 0.5162 0.3810 0.4201 0.0345  -0.0430 -0.0319 250 VAL A CB  
2132 C CG1 . VAL A 250 ? 0.5445 0.4158 0.4546 0.0363  -0.0407 -0.0325 250 VAL A CG1 
2133 C CG2 . VAL A 250 ? 0.6533 0.5173 0.5573 0.0351  -0.0425 -0.0303 250 VAL A CG2 
2134 N N   . TYR A 251 ? 0.3867 0.2627 0.2998 0.0379  -0.0403 -0.0327 251 TYR A N   
2135 C CA  . TYR A 251 ? 0.3917 0.2735 0.3102 0.0401  -0.0382 -0.0321 251 TYR A CA  
2136 C C   . TYR A 251 ? 0.3984 0.2813 0.3168 0.0401  -0.0388 -0.0331 251 TYR A C   
2137 O O   . TYR A 251 ? 0.3847 0.2675 0.3022 0.0392  -0.0395 -0.0345 251 TYR A O   
2138 C CB  . TYR A 251 ? 0.3873 0.2767 0.3130 0.0417  -0.0353 -0.0318 251 TYR A CB  
2139 C CG  . TYR A 251 ? 0.3692 0.2575 0.2946 0.0412  -0.0350 -0.0315 251 TYR A CG  
2140 C CD1 . TYR A 251 ? 0.4541 0.3396 0.3777 0.0410  -0.0353 -0.0302 251 TYR A CD1 
2141 C CD2 . TYR A 251 ? 0.4782 0.3681 0.4050 0.0408  -0.0346 -0.0323 251 TYR A CD2 
2142 C CE1 . TYR A 251 ? 0.5934 0.4779 0.5166 0.0406  -0.0351 -0.0299 251 TYR A CE1 
2143 C CE2 . TYR A 251 ? 0.4440 0.3328 0.3704 0.0404  -0.0344 -0.0319 251 TYR A CE2 
2144 C CZ  . TYR A 251 ? 0.5417 0.4280 0.4664 0.0403  -0.0347 -0.0308 251 TYR A CZ  
2145 O OH  . TYR A 251 ? 0.6309 0.5160 0.5550 0.0399  -0.0346 -0.0305 251 TYR A OH  
2146 N N   . MET A 252 ? 0.3014 0.1858 0.2213 0.0414  -0.0383 -0.0324 252 MET A N   
2147 C CA  . MET A 252 ? 0.2688 0.1555 0.1896 0.0418  -0.0384 -0.0334 252 MET A CA  
2148 C C   . MET A 252 ? 0.2592 0.1531 0.1870 0.0448  -0.0357 -0.0321 252 MET A C   
2149 O O   . MET A 252 ? 0.2490 0.1433 0.1784 0.0460  -0.0347 -0.0302 252 MET A O   
2150 C CB  . MET A 252 ? 0.3341 0.2165 0.2487 0.0385  -0.0410 -0.0330 252 MET A CB  
2151 C CG  . MET A 252 ? 0.3499 0.2242 0.2566 0.0355  -0.0441 -0.0352 252 MET A CG  
2152 S SD  . MET A 252 ? 0.3295 0.2092 0.2351 0.0299  -0.0451 -0.0329 252 MET A SD  
2153 C CE  . MET A 252 ? 0.3253 0.1935 0.2212 0.0278  -0.0487 -0.0368 252 MET A CE  
2154 N N   . TRP A 253 ? 0.2067 0.1066 0.1388 0.0460  -0.0344 -0.0330 253 TRP A N   
2155 C CA  . TRP A 253 ? 0.2635 0.1706 0.2021 0.0486  -0.0319 -0.0317 253 TRP A CA  
2156 C C   . TRP A 253 ? 0.2801 0.1912 0.2189 0.0463  -0.0324 -0.0296 253 TRP A C   
2157 O O   . TRP A 253 ? 0.2096 0.1206 0.1461 0.0444  -0.0337 -0.0310 253 TRP A O   
2158 C CB  . TRP A 253 ? 0.2151 0.1302 0.1601 0.0491  -0.0296 -0.0322 253 TRP A CB  
2159 C CG  . TRP A 253 ? 0.1594 0.0824 0.1109 0.0512  -0.0272 -0.0310 253 TRP A CG  
2160 C CD1 . TRP A 253 ? 0.1847 0.1115 0.1382 0.0520  -0.0270 -0.0318 253 TRP A CD1 
2161 C CD2 . TRP A 253 ? 0.2168 0.1454 0.1738 0.0525  -0.0245 -0.0284 253 TRP A CD2 
2162 N NE1 . TRP A 253 ? 0.1631 0.0979 0.1234 0.0537  -0.0242 -0.0298 253 TRP A NE1 
2163 C CE2 . TRP A 253 ? 0.1866 0.1227 0.1491 0.0539  -0.0226 -0.0276 253 TRP A CE2 
2164 C CE3 . TRP A 253 ? 0.2281 0.1565 0.1862 0.0524  -0.0233 -0.0265 253 TRP A CE3 
2165 C CZ2 . TRP A 253 ? 0.2156 0.1592 0.1847 0.0549  -0.0195 -0.0247 253 TRP A CZ2 
2166 C CZ3 . TRP A 253 ? 0.2984 0.2338 0.2627 0.0535  -0.0203 -0.0240 253 TRP A CZ3 
2167 C CH2 . TRP A 253 ? 0.2474 0.1904 0.2173 0.0546  -0.0184 -0.0230 253 TRP A CH2 
2168 N N   . PRO A 254 ? 0.2418 0.1598 0.1844 0.0445  -0.0307 -0.0251 254 PRO A N   
2169 C CA  . PRO A 254 ? 0.1976 0.1241 0.1427 0.0407  -0.0302 -0.0214 254 PRO A CA  
2170 C C   . PRO A 254 ? 0.1795 0.1137 0.1307 0.0429  -0.0282 -0.0219 254 PRO A C   
2171 O O   . PRO A 254 ? 0.1922 0.1298 0.1487 0.0469  -0.0259 -0.0220 254 PRO A O   
2172 C CB  . PRO A 254 ? 0.1735 0.1049 0.1217 0.0391  -0.0286 -0.0166 254 PRO A CB  
2173 C CG  . PRO A 254 ? 0.2436 0.1720 0.1936 0.0436  -0.0272 -0.0178 254 PRO A CG  
2174 C CD  . PRO A 254 ? 0.2020 0.1201 0.1466 0.0460  -0.0292 -0.0230 254 PRO A CD  
2175 N N   . PRO A 255 ? 0.2063 0.1430 0.1566 0.0405  -0.0291 -0.0222 255 PRO A N   
2176 C CA  . PRO A 255 ? 0.1911 0.1350 0.1471 0.0426  -0.0274 -0.0227 255 PRO A CA  
2177 C C   . PRO A 255 ? 0.1693 0.1233 0.1331 0.0437  -0.0242 -0.0188 255 PRO A C   
2178 O O   . PRO A 255 ? 0.1950 0.1537 0.1602 0.0406  -0.0236 -0.0145 255 PRO A O   
2179 C CB  . PRO A 255 ? 0.2122 0.1579 0.1655 0.0384  -0.0290 -0.0223 255 PRO A CB  
2180 C CG  . PRO A 255 ? 0.1863 0.1218 0.1311 0.0360  -0.0322 -0.0244 255 PRO A CG  
2181 C CD  . PRO A 255 ? 0.2313 0.1634 0.1749 0.0361  -0.0320 -0.0227 255 PRO A CD  
2182 N N   . GLU A 256 ? 0.2009 0.1583 0.1700 0.0481  -0.0221 -0.0204 256 GLU A N   
2183 C CA  . GLU A 256 ? 0.1985 0.1651 0.1752 0.0498  -0.0188 -0.0171 256 GLU A CA  
2184 C C   . GLU A 256 ? 0.2102 0.1760 0.1876 0.0499  -0.0178 -0.0144 256 GLU A C   
2185 O O   . GLU A 256 ? 0.1863 0.1600 0.1691 0.0496  -0.0155 -0.0105 256 GLU A O   
2186 C CB  . GLU A 256 ? 0.2400 0.2165 0.2206 0.0465  -0.0178 -0.0135 256 GLU A CB  
2187 C CG  . GLU A 256 ? 0.2291 0.2068 0.2091 0.0461  -0.0188 -0.0158 256 GLU A CG  
2188 C CD  . GLU A 256 ? 0.2386 0.2167 0.2222 0.0512  -0.0174 -0.0194 256 GLU A CD  
2189 O OE1 . GLU A 256 ? 0.3103 0.2863 0.2920 0.0516  -0.0186 -0.0225 256 GLU A OE1 
2190 O OE2 . GLU A 256 ? 0.2588 0.2391 0.2470 0.0549  -0.0151 -0.0190 256 GLU A OE2 
2191 N N   . ALA A 257 ? 0.1375 0.0938 0.1094 0.0505  -0.0196 -0.0166 257 ALA A N   
2192 C CA  . ALA A 257 ? 0.1454 0.0994 0.1166 0.0503  -0.0192 -0.0145 257 ALA A CA  
2193 C C   . ALA A 257 ? 0.2304 0.1891 0.2015 0.0455  -0.0192 -0.0095 257 ALA A C   
2194 O O   . ALA A 257 ? 0.2331 0.1929 0.2056 0.0452  -0.0181 -0.0066 257 ALA A O   
2195 C CB  . ALA A 257 ? 0.1456 0.1032 0.1229 0.0547  -0.0162 -0.0140 257 ALA A CB  
2196 N N   . SER A 258 ? 0.2013 0.1624 0.1706 0.0415  -0.0206 -0.0085 258 SER A N   
2197 C CA  . SER A 258 ? 0.1448 0.1122 0.1153 0.0370  -0.0203 -0.0035 258 SER A CA  
2198 C C   . SER A 258 ? 0.1491 0.1101 0.1137 0.0338  -0.0223 -0.0023 258 SER A C   
2199 O O   . SER A 258 ? 0.2154 0.1683 0.1733 0.0323  -0.0251 -0.0051 258 SER A O   
2200 C CB  . SER A 258 ? 0.1521 0.1247 0.1229 0.0338  -0.0210 -0.0027 258 SER A CB  
2201 O OG  . SER A 258 ? 0.2381 0.2184 0.2117 0.0301  -0.0200 0.0025  258 SER A OG  
2202 N N   . VAL A 259 ? 0.1910 0.1557 0.1581 0.0327  -0.0208 0.0018  259 VAL A N   
2203 C CA  . VAL A 259 ? 0.2193 0.1791 0.1815 0.0296  -0.0225 0.0035  259 VAL A CA  
2204 C C   . VAL A 259 ? 0.2039 0.1721 0.1695 0.0260  -0.0212 0.0092  259 VAL A C   
2205 O O   . VAL A 259 ? 0.1829 0.1603 0.1550 0.0267  -0.0187 0.0118  259 VAL A O   
2206 C CB  . VAL A 259 ? 0.2201 0.1728 0.1805 0.0327  -0.0222 0.0020  259 VAL A CB  
2207 C CG1 . VAL A 259 ? 0.1860 0.1299 0.1428 0.0362  -0.0237 -0.0037 259 VAL A CG1 
2208 C CG2 . VAL A 259 ? 0.1662 0.1254 0.1335 0.0355  -0.0189 0.0046  259 VAL A CG2 
2209 N N   . SER A 260 ? 0.2404 0.2051 0.2013 0.0221  -0.0229 0.0111  260 SER A N   
2210 C CA  . SER A 260 ? 0.2023 0.1737 0.1655 0.0184  -0.0220 0.0166  260 SER A CA  
2211 C C   . SER A 260 ? 0.2607 0.2244 0.2177 0.0159  -0.0241 0.0170  260 SER A C   
2212 O O   . SER A 260 ? 0.2019 0.1562 0.1530 0.0166  -0.0263 0.0132  260 SER A O   
2213 C CB  . SER A 260 ? 0.1899 0.1680 0.1541 0.0144  -0.0226 0.0187  260 SER A CB  
2214 O OG  . SER A 260 ? 0.2529 0.2244 0.2101 0.0113  -0.0259 0.0165  260 SER A OG  
2215 N N   . ASN A 261 ? 0.2252 0.1932 0.1837 0.0130  -0.0233 0.0218  261 ASN A N   
2216 C CA  . ASN A 261 ? 0.2201 0.1813 0.1728 0.0103  -0.0253 0.0226  261 ASN A CA  
2217 C C   . ASN A 261 ? 0.2368 0.1919 0.1824 0.0068  -0.0287 0.0203  261 ASN A C   
2218 O O   . ASN A 261 ? 0.2604 0.2059 0.1998 0.0068  -0.0309 0.0177  261 ASN A O   
2219 C CB  . ASN A 261 ? 0.2028 0.1707 0.1584 0.0072  -0.0239 0.0283  261 ASN A CB  
2220 C CG  . ASN A 261 ? 0.2938 0.2652 0.2548 0.0106  -0.0208 0.0303  261 ASN A CG  
2221 O OD1 . ASN A 261 ? 0.2689 0.2354 0.2298 0.0149  -0.0201 0.0273  261 ASN A OD1 
2222 N ND2 . ASN A 261 ? 0.2463 0.2264 0.2121 0.0088  -0.0188 0.0355  261 ASN A ND2 
2223 N N   . GLU A 262 ? 0.2557 0.2160 0.2020 0.0040  -0.0294 0.0212  262 GLU A N   
2224 C CA  . GLU A 262 ? 0.2743 0.2291 0.2139 0.0003  -0.0326 0.0194  262 GLU A CA  
2225 C C   . GLU A 262 ? 0.2467 0.1935 0.1824 0.0032  -0.0341 0.0135  262 GLU A C   
2226 O O   . GLU A 262 ? 0.2954 0.2337 0.2241 0.0015  -0.0369 0.0110  262 GLU A O   
2227 C CB  . GLU A 262 ? 0.2348 0.1977 0.1764 -0.0037 -0.0328 0.0222  262 GLU A CB  
2228 C CG  . GLU A 262 ? 0.3192 0.2887 0.2632 -0.0075 -0.0320 0.0280  262 GLU A CG  
2229 C CD  . GLU A 262 ? 0.4008 0.3778 0.3461 -0.0118 -0.0324 0.0308  262 GLU A CD  
2230 O OE1 . GLU A 262 ? 0.4814 0.4676 0.4322 -0.0131 -0.0304 0.0355  262 GLU A OE1 
2231 O OE2 . GLU A 262 ? 0.3964 0.3701 0.3373 -0.0140 -0.0348 0.0285  262 GLU A OE2 
2232 N N   . ALA A 263 ? 0.2226 0.1720 0.1627 0.0076  -0.0324 0.0112  263 ALA A N   
2233 C CA  . ALA A 263 ? 0.2228 0.1647 0.1595 0.0106  -0.0337 0.0057  263 ALA A CA  
2234 C C   . ALA A 263 ? 0.2002 0.1323 0.1327 0.0131  -0.0346 0.0030  263 ALA A C   
2235 O O   . ALA A 263 ? 0.2769 0.2001 0.2031 0.0130  -0.0371 -0.0008 263 ALA A O   
2236 C CB  . ALA A 263 ? 0.1794 0.1269 0.1223 0.0148  -0.0314 0.0042  263 ALA A CB  
2237 N N   . LEU A 264 ? 0.2678 0.2011 0.2035 0.0153  -0.0327 0.0048  264 LEU A N   
2238 C CA  . LEU A 264 ? 0.2057 0.1297 0.1373 0.0174  -0.0335 0.0025  264 LEU A CA  
2239 C C   . LEU A 264 ? 0.2956 0.2127 0.2198 0.0132  -0.0364 0.0029  264 LEU A C   
2240 O O   . LEU A 264 ? 0.2728 0.1802 0.1913 0.0141  -0.0384 -0.0007 264 LEU A O   
2241 C CB  . LEU A 264 ? 0.1829 0.1102 0.1192 0.0199  -0.0309 0.0051  264 LEU A CB  
2242 C CG  . LEU A 264 ? 0.2198 0.1530 0.1632 0.0245  -0.0280 0.0045  264 LEU A CG  
2243 C CD1 . LEU A 264 ? 0.2202 0.1578 0.1685 0.0262  -0.0252 0.0078  264 LEU A CD1 
2244 C CD2 . LEU A 264 ? 0.3537 0.2799 0.2952 0.0289  -0.0287 -0.0010 264 LEU A CD2 
2245 N N   . GLU A 265 ? 0.2616 0.1836 0.1859 0.0085  -0.0367 0.0071  265 GLU A N   
2246 C CA  . GLU A 265 ? 0.2836 0.1994 0.2010 0.0041  -0.0395 0.0075  265 GLU A CA  
2247 C C   . GLU A 265 ? 0.3722 0.2821 0.2839 0.0029  -0.0422 0.0036  265 GLU A C   
2248 O O   . GLU A 265 ? 0.2976 0.1983 0.2025 0.0018  -0.0446 0.0013  265 GLU A O   
2249 C CB  . GLU A 265 ? 0.3535 0.2766 0.2726 -0.0007 -0.0392 0.0129  265 GLU A CB  
2250 C CG  . GLU A 265 ? 0.4780 0.4041 0.4003 -0.0005 -0.0373 0.0168  265 GLU A CG  
2251 C CD  . GLU A 265 ? 0.5893 0.5232 0.5137 -0.0052 -0.0369 0.0222  265 GLU A CD  
2252 O OE1 . GLU A 265 ? 0.6823 0.6176 0.6043 -0.0092 -0.0386 0.0228  265 GLU A OE1 
2253 O OE2 . GLU A 265 ? 0.7144 0.6530 0.6429 -0.0050 -0.0348 0.0260  265 GLU A OE2 
2254 N N   . LEU A 266 ? 0.3150 0.2299 0.2292 0.0030  -0.0418 0.0028  266 LEU A N   
2255 C CA  . LEU A 266 ? 0.2396 0.1489 0.1486 0.0020  -0.0443 -0.0011 266 LEU A CA  
2256 C C   . LEU A 266 ? 0.3220 0.2219 0.2277 0.0063  -0.0451 -0.0063 266 LEU A C   
2257 O O   . LEU A 266 ? 0.3273 0.2182 0.2260 0.0051  -0.0476 -0.0090 266 LEU A O   
2258 C CB  . LEU A 266 ? 0.2404 0.1572 0.1532 0.0016  -0.0435 -0.0009 266 LEU A CB  
2259 C CG  . LEU A 266 ? 0.2882 0.2004 0.1967 0.0013  -0.0455 -0.0051 266 LEU A CG  
2260 C CD1 . LEU A 266 ? 0.2879 0.1932 0.1884 -0.0033 -0.0487 -0.0054 266 LEU A CD1 
2261 C CD2 . LEU A 266 ? 0.2668 0.1879 0.1800 0.0008  -0.0444 -0.0041 266 LEU A CD2 
2262 N N   . TYR A 267 ? 0.2432 0.1451 0.1538 0.0113  -0.0429 -0.0077 267 TYR A N   
2263 C CA  . TYR A 267 ? 0.2182 0.1116 0.1262 0.0156  -0.0435 -0.0124 267 TYR A CA  
2264 C C   . TYR A 267 ? 0.2626 0.1469 0.1647 0.0150  -0.0451 -0.0130 267 TYR A C   
2265 O O   . TYR A 267 ? 0.2861 0.1612 0.1824 0.0156  -0.0472 -0.0168 267 TYR A O   
2266 C CB  . TYR A 267 ? 0.2624 0.1600 0.1770 0.0208  -0.0406 -0.0130 267 TYR A CB  
2267 C CG  . TYR A 267 ? 0.2910 0.1949 0.2102 0.0225  -0.0394 -0.0141 267 TYR A CG  
2268 C CD1 . TYR A 267 ? 0.2530 0.1524 0.1692 0.0236  -0.0409 -0.0184 267 TYR A CD1 
2269 C CD2 . TYR A 267 ? 0.2153 0.1297 0.1420 0.0231  -0.0366 -0.0108 267 TYR A CD2 
2270 C CE1 . TYR A 267 ? 0.2752 0.1802 0.1955 0.0253  -0.0397 -0.0194 267 TYR A CE1 
2271 C CE2 . TYR A 267 ? 0.2849 0.2052 0.2159 0.0247  -0.0354 -0.0118 267 TYR A CE2 
2272 C CZ  . TYR A 267 ? 0.2899 0.2054 0.2177 0.0258  -0.0370 -0.0161 267 TYR A CZ  
2273 O OH  . TYR A 267 ? 0.2026 0.1240 0.1347 0.0274  -0.0358 -0.0170 267 TYR A OH  
2274 N N   . TYR A 268 ? 0.2534 0.1402 0.1571 0.0136  -0.0442 -0.0092 268 TYR A N   
2275 C CA  . TYR A 268 ? 0.3025 0.1810 0.2008 0.0128  -0.0457 -0.0094 268 TYR A CA  
2276 C C   . TYR A 268 ? 0.3026 0.1750 0.1934 0.0084  -0.0488 -0.0102 268 TYR A C   
2277 O O   . TYR A 268 ? 0.3222 0.1849 0.2070 0.0089  -0.0508 -0.0132 268 TYR A O   
2278 C CB  . TYR A 268 ? 0.3593 0.2426 0.2609 0.0117  -0.0440 -0.0047 268 TYR A CB  
2279 C CG  . TYR A 268 ? 0.3247 0.2006 0.2202 0.0092  -0.0459 -0.0040 268 TYR A CG  
2280 C CD1 . TYR A 268 ? 0.3974 0.2649 0.2900 0.0122  -0.0464 -0.0066 268 TYR A CD1 
2281 C CD2 . TYR A 268 ? 0.3923 0.2695 0.2852 0.0038  -0.0472 -0.0008 268 TYR A CD2 
2282 C CE1 . TYR A 268 ? 0.4751 0.3358 0.3622 0.0100  -0.0481 -0.0060 268 TYR A CE1 
2283 C CE2 . TYR A 268 ? 0.3630 0.2333 0.2503 0.0016  -0.0489 -0.0003 268 TYR A CE2 
2284 C CZ  . TYR A 268 ? 0.4231 0.2852 0.3076 0.0047  -0.0493 -0.0029 268 TYR A CZ  
2285 O OH  . TYR A 268 ? 0.5695 0.4249 0.4484 0.0024  -0.0510 -0.0023 268 TYR A OH  
2286 N N   . GLU A 269 ? 0.3216 0.1995 0.2126 0.0040  -0.0493 -0.0075 269 GLU A N   
2287 C CA  . GLU A 269 ? 0.4303 0.3028 0.3143 -0.0006 -0.0522 -0.0079 269 GLU A CA  
2288 C C   . GLU A 269 ? 0.4287 0.2941 0.3078 0.0004  -0.0542 -0.0129 269 GLU A C   
2289 O O   . GLU A 269 ? 0.4700 0.3279 0.3421 -0.0022 -0.0568 -0.0144 269 GLU A O   
2290 C CB  . GLU A 269 ? 0.4441 0.3246 0.3298 -0.0056 -0.0523 -0.0038 269 GLU A CB  
2291 C CG  . GLU A 269 ? 0.5340 0.4193 0.4220 -0.0081 -0.0512 0.0013  269 GLU A CG  
2292 C CD  . GLU A 269 ? 0.6478 0.5251 0.5293 -0.0107 -0.0533 0.0017  269 GLU A CD  
2293 O OE1 . GLU A 269 ? 0.6391 0.5191 0.5222 -0.0121 -0.0524 0.0055  269 GLU A OE1 
2294 O OE2 . GLU A 269 ? 0.6512 0.5194 0.5259 -0.0112 -0.0558 -0.0018 269 GLU A OE2 
2295 N N   . LYS A 270 ? 0.3626 0.2304 0.2453 0.0041  -0.0530 -0.0155 270 LYS A N   
2296 C CA  . LYS A 270 ? 0.3729 0.2339 0.2515 0.0057  -0.0546 -0.0204 270 LYS A CA  
2297 C C   . LYS A 270 ? 0.4075 0.2599 0.2838 0.0102  -0.0549 -0.0243 270 LYS A C   
2298 O O   . LYS A 270 ? 0.3223 0.1693 0.1960 0.0125  -0.0559 -0.0286 270 LYS A O   
2299 C CB  . LYS A 270 ? 0.3446 0.2125 0.2280 0.0073  -0.0533 -0.0213 270 LYS A CB  
2300 C CG  . LYS A 270 ? 0.3749 0.2501 0.2594 0.0026  -0.0535 -0.0182 270 LYS A CG  
2301 C CD  . LYS A 270 ? 0.5003 0.3686 0.3768 -0.0015 -0.0566 -0.0196 270 LYS A CD  
2302 C CE  . LYS A 270 ? 0.5945 0.4695 0.4714 -0.0066 -0.0571 -0.0164 270 LYS A CE  
2303 N NZ  . LYS A 270 ? 0.6774 0.5456 0.5464 -0.0111 -0.0600 -0.0168 270 LYS A NZ  
2304 N N   . GLY A 271 ? 0.3780 0.2289 0.2552 0.0116  -0.0541 -0.0229 271 GLY A N   
2305 C CA  . GLY A 271 ? 0.4166 0.2588 0.2910 0.0155  -0.0545 -0.0264 271 GLY A CA  
2306 C C   . GLY A 271 ? 0.3589 0.2035 0.2389 0.0211  -0.0524 -0.0282 271 GLY A C   
2307 O O   . GLY A 271 ? 0.3692 0.2125 0.2506 0.0240  -0.0515 -0.0297 271 GLY A O   
2308 N N   . ILE A 272 ? 0.2606 0.1150 0.1477 0.0221  -0.0499 -0.0260 272 ILE A N   
2309 C CA  . ILE A 272 ? 0.2852 0.1421 0.1778 0.0274  -0.0477 -0.0275 272 ILE A CA  
2310 C C   . ILE A 272 ? 0.3048 0.1616 0.1994 0.0289  -0.0463 -0.0254 272 ILE A C   
2311 O O   . ILE A 272 ? 0.3988 0.2603 0.2950 0.0260  -0.0456 -0.0211 272 ILE A O   
2312 C CB  . ILE A 272 ? 0.3628 0.2304 0.2624 0.0278  -0.0455 -0.0258 272 ILE A CB  
2313 C CG1 . ILE A 272 ? 0.3476 0.2154 0.2447 0.0255  -0.0470 -0.0274 272 ILE A CG1 
2314 C CG2 . ILE A 272 ? 0.3346 0.2047 0.2398 0.0333  -0.0432 -0.0275 272 ILE A CG2 
2315 C CD1 . ILE A 272 ? 0.4049 0.2633 0.2965 0.0274  -0.0491 -0.0326 272 ILE A CD1 
2316 N N   . ASN A 273 ? 0.3476 0.2023 0.2437 0.0328  -0.0454 -0.0274 273 ASN A N   
2317 C CA  . ASN A 273 ? 0.3959 0.2510 0.2940 0.0341  -0.0440 -0.0256 273 ASN A CA  
2318 C C   . ASN A 273 ? 0.2998 0.1623 0.2055 0.0376  -0.0409 -0.0245 273 ASN A C   
2319 O O   . ASN A 273 ? 0.3538 0.2165 0.2610 0.0385  -0.0397 -0.0224 273 ASN A O   
2320 C CB  . ASN A 273 ? 0.4847 0.3404 0.3831 0.0341  -0.0436 -0.0262 273 ASN A CB  
2321 C CG  . ASN A 273 ? 0.7134 0.5617 0.6045 0.0308  -0.0464 -0.0263 273 ASN A CG  
2322 O OD1 . ASN A 273 ? 0.7666 0.6086 0.6519 0.0280  -0.0485 -0.0253 273 ASN A OD1 
2323 N ND2 . ASN A 273 ? 0.7667 0.6155 0.6579 0.0308  -0.0463 -0.0272 273 ASN A ND2 
2324 N N   . MET A 274 ? 0.3065 0.2944 0.3089 0.0007  -0.0192 0.0011  274 MET A N   
2325 C CA  . MET A 274 ? 0.1709 0.1555 0.1697 0.0027  -0.0168 0.0002  274 MET A CA  
2326 C C   . MET A 274 ? 0.2321 0.2108 0.2267 0.0047  -0.0167 -0.0007 274 MET A C   
2327 O O   . MET A 274 ? 0.2559 0.2311 0.2496 0.0037  -0.0176 -0.0010 274 MET A O   
2328 C CB  . MET A 274 ? 0.1877 0.1702 0.1855 0.0010  -0.0150 -0.0004 274 MET A CB  
2329 C CG  . MET A 274 ? 0.3701 0.3493 0.3642 0.0029  -0.0125 -0.0014 274 MET A CG  
2330 S SD  . MET A 274 ? 0.4734 0.4439 0.4620 0.0041  -0.0116 -0.0027 274 MET A SD  
2331 C CE  . MET A 274 ? 0.4008 0.3686 0.3893 0.0009  -0.0108 -0.0031 274 MET A CE  
2332 N N   . LEU A 275 ? 0.1565 0.1341 0.1486 0.0075  -0.0155 -0.0012 275 LEU A N   
2333 C CA  . LEU A 275 ? 0.2097 0.1812 0.1974 0.0094  -0.0149 -0.0022 275 LEU A CA  
2334 C C   . LEU A 275 ? 0.2388 0.2082 0.2234 0.0113  -0.0124 -0.0030 275 LEU A C   
2335 O O   . LEU A 275 ? 0.1950 0.1678 0.1810 0.0112  -0.0113 -0.0027 275 LEU A O   
2336 C CB  . LEU A 275 ? 0.2673 0.2393 0.2549 0.0113  -0.0166 -0.0018 275 LEU A CB  
2337 C CG  . LEU A 275 ? 0.3495 0.3271 0.3394 0.0130  -0.0171 -0.0010 275 LEU A CG  
2338 C CD1 . LEU A 275 ? 0.3944 0.3706 0.3813 0.0159  -0.0152 -0.0016 275 LEU A CD1 
2339 C CD2 . LEU A 275 ? 0.3582 0.3370 0.3493 0.0136  -0.0195 -0.0004 275 LEU A CD2 
2340 N N   . ALA A 276 ? 0.2067 0.1704 0.1870 0.0132  -0.0116 -0.0039 276 ALA A N   
2341 C CA  . ALA A 276 ? 0.2001 0.1615 0.1772 0.0153  -0.0094 -0.0047 276 ALA A CA  
2342 C C   . ALA A 276 ? 0.1653 0.1248 0.1399 0.0183  -0.0097 -0.0050 276 ALA A C   
2343 O O   . ALA A 276 ? 0.2024 0.1606 0.1769 0.0186  -0.0113 -0.0049 276 ALA A O   
2344 C CB  . ALA A 276 ? 0.2168 0.1724 0.1905 0.0145  -0.0076 -0.0058 276 ALA A CB  
2345 N N   . THR A 277 ? 0.1592 0.1184 0.1318 0.0206  -0.0081 -0.0054 277 THR A N   
2346 C CA  . THR A 277 ? 0.1843 0.1414 0.1542 0.0236  -0.0080 -0.0058 277 THR A CA  
2347 C C   . THR A 277 ? 0.2326 0.1864 0.1987 0.0253  -0.0055 -0.0067 277 THR A C   
2348 O O   . THR A 277 ? 0.2708 0.2223 0.2357 0.0240  -0.0041 -0.0073 277 THR A O   
2349 C CB  . THR A 277 ? 0.2576 0.2205 0.2306 0.0249  -0.0095 -0.0047 277 THR A CB  
2350 O OG1 . THR A 277 ? 0.2100 0.1709 0.1802 0.0280  -0.0092 -0.0051 277 THR A OG1 
2351 C CG2 . THR A 277 ? 0.2431 0.2120 0.2192 0.0244  -0.0090 -0.0040 277 THR A CG2 
2352 N N   . ASP A 278 ? 0.1822 0.1356 0.1464 0.0283  -0.0051 -0.0069 278 ASP A N   
2353 C CA  . ASP A 278 ? 0.1988 0.1478 0.1587 0.0302  -0.0029 -0.0080 278 ASP A CA  
2354 C C   . ASP A 278 ? 0.2319 0.1848 0.1925 0.0317  -0.0016 -0.0077 278 ASP A C   
2355 O O   . ASP A 278 ? 0.1935 0.1518 0.1571 0.0325  -0.0026 -0.0068 278 ASP A O   
2356 C CB  . ASP A 278 ? 0.2160 0.1604 0.1723 0.0326  -0.0031 -0.0086 278 ASP A CB  
2357 C CG  . ASP A 278 ? 0.2890 0.2284 0.2406 0.0344  -0.0008 -0.0097 278 ASP A CG  
2358 O OD1 . ASP A 278 ? 0.2743 0.2097 0.2237 0.0332  0.0004  -0.0105 278 ASP A OD1 
2359 O OD2 . ASP A 278 ? 0.3192 0.2588 0.2692 0.0372  -0.0003 -0.0099 278 ASP A OD2 
2360 N N   . GLU A 279 ? 0.2171 0.1672 0.1749 0.0321  0.0006  -0.0085 279 GLU A N   
2361 C CA  . GLU A 279 ? 0.3195 0.2732 0.2779 0.0334  0.0018  -0.0082 279 GLU A CA  
2362 C C   . GLU A 279 ? 0.2356 0.1895 0.1923 0.0368  0.0020  -0.0083 279 GLU A C   
2363 O O   . GLU A 279 ? 0.3435 0.3015 0.3014 0.0380  0.0027  -0.0079 279 GLU A O   
2364 C CB  . GLU A 279 ? 0.3671 0.3180 0.3231 0.0328  0.0041  -0.0090 279 GLU A CB  
2365 C CG  . GLU A 279 ? 0.4212 0.3662 0.3720 0.0349  0.0059  -0.0101 279 GLU A CG  
2366 C CD  . GLU A 279 ? 0.4471 0.3903 0.3961 0.0341  0.0081  -0.0107 279 GLU A CD  
2367 O OE1 . GLU A 279 ? 0.4279 0.3744 0.3777 0.0350  0.0091  -0.0105 279 GLU A OE1 
2368 O OE2 . GLU A 279 ? 0.3647 0.3033 0.3116 0.0326  0.0087  -0.0114 279 GLU A OE2 
2369 N N   . VAL A 280 ? 0.2090 0.1590 0.1631 0.0385  0.0014  -0.0088 280 VAL A N   
2370 C CA  . VAL A 280 ? 0.2006 0.1519 0.1539 0.0415  0.0013  -0.0086 280 VAL A CA  
2371 C C   . VAL A 280 ? 0.2886 0.2468 0.2467 0.0414  -0.0006 -0.0073 280 VAL A C   
2372 O O   . VAL A 280 ? 0.2988 0.2609 0.2579 0.0432  -0.0004 -0.0068 280 VAL A O   
2373 C CB  . VAL A 280 ? 0.2812 0.2270 0.2310 0.0432  0.0009  -0.0094 280 VAL A CB  
2374 C CG1 . VAL A 280 ? 0.3437 0.2917 0.2935 0.0462  0.0003  -0.0090 280 VAL A CG1 
2375 C CG2 . VAL A 280 ? 0.3866 0.3258 0.3314 0.0439  0.0029  -0.0106 280 VAL A CG2 
2376 N N   . ILE A 281 ? 0.2178 0.1776 0.1787 0.0391  -0.0025 -0.0067 281 ILE A N   
2377 C CA  . ILE A 281 ? 0.2195 0.1859 0.1851 0.0386  -0.0043 -0.0054 281 ILE A CA  
2378 C C   . ILE A 281 ? 0.2512 0.2231 0.2197 0.0378  -0.0036 -0.0047 281 ILE A C   
2379 O O   . ILE A 281 ? 0.2433 0.2206 0.2145 0.0388  -0.0042 -0.0038 281 ILE A O   
2380 C CB  . ILE A 281 ? 0.3293 0.2957 0.2971 0.0361  -0.0064 -0.0050 281 ILE A CB  
2381 C CG1 . ILE A 281 ? 0.2750 0.2363 0.2399 0.0373  -0.0072 -0.0056 281 ILE A CG1 
2382 C CG2 . ILE A 281 ? 0.2835 0.2569 0.2563 0.0352  -0.0083 -0.0036 281 ILE A CG2 
2383 C CD1 . ILE A 281 ? 0.2686 0.2289 0.2349 0.0350  -0.0091 -0.0054 281 ILE A CD1 
2384 N N   . LEU A 282 ? 0.2901 0.2606 0.2582 0.0359  -0.0023 -0.0052 282 LEU A N   
2385 C CA  . LEU A 282 ? 0.3099 0.2852 0.2805 0.0351  -0.0014 -0.0046 282 LEU A CA  
2386 C C   . LEU A 282 ? 0.2629 0.2393 0.2318 0.0381  0.0002  -0.0048 282 LEU A C   
2387 O O   . LEU A 282 ? 0.2863 0.2685 0.2581 0.0386  -0.0001 -0.0039 282 LEU A O   
2388 C CB  . LEU A 282 ? 0.2617 0.2346 0.2316 0.0327  -0.0001 -0.0052 282 LEU A CB  
2389 C CG  . LEU A 282 ? 0.3128 0.2897 0.2845 0.0319  0.0012  -0.0048 282 LEU A CG  
2390 C CD1 . LEU A 282 ? 0.3278 0.3116 0.3049 0.0300  -0.0004 -0.0036 282 LEU A CD1 
2391 C CD2 . LEU A 282 ? 0.3332 0.3061 0.3028 0.0303  0.0029  -0.0057 282 LEU A CD2 
2392 N N   . LYS A 283 ? 0.2258 0.1966 0.1901 0.0400  0.0017  -0.0059 283 LYS A N   
2393 C CA  . LYS A 283 ? 0.2428 0.2142 0.2051 0.0429  0.0032  -0.0061 283 LYS A CA  
2394 C C   . LYS A 283 ? 0.3062 0.2814 0.2702 0.0451  0.0019  -0.0053 283 LYS A C   
2395 O O   . LYS A 283 ? 0.3127 0.2918 0.2776 0.0468  0.0026  -0.0048 283 LYS A O   
2396 C CB  . LYS A 283 ? 0.3619 0.3262 0.3187 0.0445  0.0050  -0.0074 283 LYS A CB  
2397 C CG  . LYS A 283 ? 0.4958 0.4561 0.4507 0.0426  0.0064  -0.0083 283 LYS A CG  
2398 C CD  . LYS A 283 ? 0.6400 0.6048 0.5978 0.0408  0.0071  -0.0077 283 LYS A CD  
2399 C CE  . LYS A 283 ? 0.6856 0.6474 0.6404 0.0409  0.0095  -0.0085 283 LYS A CE  
2400 N NZ  . LYS A 283 ? 0.6494 0.6048 0.6011 0.0394  0.0102  -0.0095 283 LYS A NZ  
2401 N N   . ASN A 284 ? 0.2405 0.2148 0.2049 0.0451  0.0001  -0.0051 284 ASN A N   
2402 C CA  . ASN A 284 ? 0.2646 0.2427 0.2308 0.0470  -0.0013 -0.0043 284 ASN A CA  
2403 C C   . ASN A 284 ? 0.2695 0.2552 0.2410 0.0457  -0.0027 -0.0028 284 ASN A C   
2404 O O   . ASN A 284 ? 0.3058 0.2957 0.2791 0.0474  -0.0035 -0.0020 284 ASN A O   
2405 C CB  . ASN A 284 ? 0.2002 0.1751 0.1654 0.0472  -0.0030 -0.0044 284 ASN A CB  
2406 C CG  . ASN A 284 ? 0.3453 0.3136 0.3053 0.0494  -0.0019 -0.0056 284 ASN A CG  
2407 O OD1 . ASN A 284 ? 0.3363 0.3026 0.2935 0.0512  0.0001  -0.0063 284 ASN A OD1 
2408 N ND2 . ASN A 284 ? 0.3314 0.2960 0.2901 0.0494  -0.0031 -0.0059 284 ASN A ND2 
2409 N N   . SER A 285 ? 0.2367 0.2243 0.2108 0.0427  -0.0030 -0.0025 285 SER A N   
2410 C CA  . SER A 285 ? 0.2401 0.2345 0.2194 0.0410  -0.0047 -0.0012 285 SER A CA  
2411 C C   . SER A 285 ? 0.2700 0.2692 0.2517 0.0404  -0.0036 -0.0007 285 SER A C   
2412 O O   . SER A 285 ? 0.3082 0.3137 0.2935 0.0406  -0.0045 0.0005  285 SER A O   
2413 C CB  . SER A 285 ? 0.2735 0.2670 0.2546 0.0379  -0.0063 -0.0010 285 SER A CB  
2414 O OG  . SER A 285 ? 0.3275 0.3167 0.3065 0.0386  -0.0074 -0.0014 285 SER A OG  
2415 N N   . VAL A 286 ? 0.3135 0.3100 0.2932 0.0395  -0.0017 -0.0014 286 VAL A N   
2416 C CA  . VAL A 286 ? 0.2763 0.2772 0.2581 0.0390  -0.0005 -0.0010 286 VAL A CA  
2417 C C   . VAL A 286 ? 0.3188 0.3163 0.2965 0.0411  0.0020  -0.0020 286 VAL A C   
2418 O O   . VAL A 286 ? 0.3740 0.3652 0.3476 0.0417  0.0031  -0.0031 286 VAL A O   
2419 C CB  . VAL A 286 ? 0.3464 0.3485 0.3306 0.0354  -0.0008 -0.0008 286 VAL A CB  
2420 C CG1 . VAL A 286 ? 0.2780 0.2819 0.2654 0.0333  -0.0032 -0.0001 286 VAL A CG1 
2421 C CG2 . VAL A 286 ? 0.3597 0.3558 0.3404 0.0345  0.0009  -0.0020 286 VAL A CG2 
2422 N N   . GLU A 287 ? 0.3606 0.3626 0.3397 0.0421  0.0029  -0.0015 287 GLU A N   
2423 C CA  . GLU A 287 ? 0.3923 0.3922 0.3681 0.0442  0.0052  -0.0022 287 GLU A CA  
2424 C C   . GLU A 287 ? 0.3755 0.3707 0.3486 0.0427  0.0070  -0.0032 287 GLU A C   
2425 O O   . GLU A 287 ? 0.4408 0.4299 0.4094 0.0439  0.0083  -0.0044 287 GLU A O   
2426 C CB  . GLU A 287 ? 0.4574 0.4638 0.4359 0.0451  0.0057  -0.0013 287 GLU A CB  
2427 C CG  . GLU A 287 ? 0.5908 0.6010 0.5708 0.0474  0.0045  -0.0005 287 GLU A CG  
2428 C CD  . GLU A 287 ? 0.6651 0.6766 0.6436 0.0502  0.0062  -0.0005 287 GLU A CD  
2429 O OE1 . GLU A 287 ? 0.7152 0.7260 0.6921 0.0529  0.0060  -0.0005 287 GLU A OE1 
2430 O OE2 . GLU A 287 ? 0.6956 0.7087 0.6744 0.0498  0.0077  -0.0006 287 GLU A OE2 
2431 N N   . ARG A 288 ? 0.3152 0.3134 0.2910 0.0402  0.0071  -0.0028 288 ARG A N   
2432 C CA  . ARG A 288 ? 0.4808 0.4752 0.4545 0.0385  0.0088  -0.0037 288 ARG A CA  
2433 C C   . ARG A 288 ? 0.5479 0.5395 0.5221 0.0358  0.0076  -0.0039 288 ARG A C   
2434 O O   . ARG A 288 ? 0.6382 0.6331 0.6161 0.0332  0.0065  -0.0032 288 ARG A O   
2435 C CB  . ARG A 288 ? 0.4632 0.4625 0.4397 0.0372  0.0096  -0.0031 288 ARG A CB  
2436 C CG  . ARG A 288 ? 0.5000 0.5008 0.4750 0.0398  0.0113  -0.0032 288 ARG A CG  
2437 C CD  . ARG A 288 ? 0.6164 0.6217 0.5941 0.0383  0.0120  -0.0026 288 ARG A CD  
2438 N NE  . ARG A 288 ? 0.7162 0.7278 0.6993 0.0364  0.0101  -0.0014 288 ARG A NE  
2439 C CZ  . ARG A 288 ? 0.7463 0.7634 0.7323 0.0377  0.0089  -0.0003 288 ARG A CZ  
2440 N NH1 . ARG A 288 ? 0.7527 0.7698 0.7368 0.0409  0.0094  -0.0004 288 ARG A NH1 
2441 N NH2 . ARG A 288 ? 0.7176 0.7403 0.7084 0.0357  0.0072  0.0008  288 ARG A NH2 
2442 N N   . ALA A 289 ? 0.4988 0.4840 0.4691 0.0366  0.0078  -0.0049 289 ALA A N   
2443 C CA  . ALA A 289 ? 0.5238 0.5063 0.4945 0.0347  0.0064  -0.0050 289 ALA A CA  
2444 C C   . ALA A 289 ? 0.4524 0.4293 0.4201 0.0330  0.0077  -0.0060 289 ALA A C   
2445 O O   . ALA A 289 ? 0.5264 0.4972 0.4899 0.0341  0.0086  -0.0070 289 ALA A O   
2446 C CB  . ALA A 289 ? 0.5007 0.4806 0.4695 0.0368  0.0054  -0.0052 289 ALA A CB  
2447 N N   . SER A 290 ? 0.2983 0.2775 0.2685 0.0304  0.0079  -0.0057 290 SER A N   
2448 C CA  . SER A 290 ? 0.2583 0.2328 0.2264 0.0283  0.0089  -0.0064 290 SER A CA  
2449 C C   . SER A 290 ? 0.2131 0.1859 0.1823 0.0262  0.0071  -0.0063 290 SER A C   
2450 O O   . SER A 290 ? 0.1821 0.1593 0.1554 0.0246  0.0054  -0.0054 290 SER A O   
2451 C CB  . SER A 290 ? 0.2487 0.2261 0.2189 0.0262  0.0098  -0.0061 290 SER A CB  
2452 O OG  . SER A 290 ? 0.2478 0.2207 0.2162 0.0240  0.0106  -0.0068 290 SER A OG  
2453 N N   . PRO A 291 ? 0.1835 0.1498 0.1491 0.0262  0.0075  -0.0073 291 PRO A N   
2454 C CA  . PRO A 291 ? 0.1924 0.1567 0.1588 0.0242  0.0060  -0.0073 291 PRO A CA  
2455 C C   . PRO A 291 ? 0.2445 0.2087 0.2124 0.0209  0.0062  -0.0072 291 PRO A C   
2456 O O   . PRO A 291 ? 0.1955 0.1572 0.1634 0.0192  0.0052  -0.0073 291 PRO A O   
2457 C CB  . PRO A 291 ? 0.2969 0.2540 0.2582 0.0258  0.0067  -0.0084 291 PRO A CB  
2458 C CG  . PRO A 291 ? 0.2315 0.1860 0.1894 0.0272  0.0091  -0.0091 291 PRO A CG  
2459 C CD  . PRO A 291 ? 0.2309 0.1914 0.1913 0.0281  0.0095  -0.0084 291 PRO A CD  
2460 N N   . TYR A 292 ? 0.1898 0.1568 0.1590 0.0199  0.0074  -0.0070 292 TYR A N   
2461 C CA  . TYR A 292 ? 0.2061 0.1727 0.1763 0.0169  0.0078  -0.0070 292 TYR A CA  
2462 C C   . TYR A 292 ? 0.1458 0.1187 0.1213 0.0146  0.0065  -0.0059 292 TYR A C   
2463 O O   . TYR A 292 ? 0.2100 0.1834 0.1869 0.0120  0.0069  -0.0058 292 TYR A O   
2464 C CB  . TYR A 292 ? 0.1511 0.1155 0.1187 0.0171  0.0103  -0.0077 292 TYR A CB  
2465 C CG  . TYR A 292 ? 0.2192 0.1771 0.1814 0.0193  0.0116  -0.0088 292 TYR A CG  
2466 C CD1 . TYR A 292 ? 0.2900 0.2429 0.2500 0.0192  0.0110  -0.0093 292 TYR A CD1 
2467 C CD2 . TYR A 292 ? 0.2522 0.2092 0.2118 0.0214  0.0134  -0.0093 292 TYR A CD2 
2468 C CE1 . TYR A 292 ? 0.3445 0.2914 0.2996 0.0212  0.0121  -0.0103 292 TYR A CE1 
2469 C CE2 . TYR A 292 ? 0.3986 0.3495 0.3531 0.0234  0.0146  -0.0103 292 TYR A CE2 
2470 C CZ  . TYR A 292 ? 0.4306 0.3765 0.3829 0.0233  0.0139  -0.0108 292 TYR A CZ  
2471 O OH  . TYR A 292 ? 0.4499 0.3898 0.3974 0.0252  0.0151  -0.0118 292 TYR A OH  
2472 N N   . LEU A 293 ? 0.1897 0.1674 0.1682 0.0154  0.0049  -0.0050 293 LEU A N   
2473 C CA  . LEU A 293 ? 0.1412 0.1253 0.1248 0.0135  0.0034  -0.0038 293 LEU A CA  
2474 C C   . LEU A 293 ? 0.1753 0.1597 0.1609 0.0122  0.0011  -0.0034 293 LEU A C   
2475 O O   . LEU A 293 ? 0.1417 0.1227 0.1252 0.0135  0.0004  -0.0038 293 LEU A O   
2476 C CB  . LEU A 293 ? 0.2403 0.2301 0.2260 0.0154  0.0032  -0.0031 293 LEU A CB  
2477 C CG  . LEU A 293 ? 0.3391 0.3318 0.3251 0.0160  0.0049  -0.0030 293 LEU A CG  
2478 C CD1 . LEU A 293 ? 0.3615 0.3486 0.3428 0.0170  0.0073  -0.0042 293 LEU A CD1 
2479 C CD2 . LEU A 293 ? 0.2501 0.2473 0.2374 0.0186  0.0045  -0.0024 293 LEU A CD2 
2480 N N   . ARG A 294 ? 0.2179 0.2067 0.2078 0.0096  -0.0001 -0.0025 294 ARG A N   
2481 C CA  . ARG A 294 ? 0.1821 0.1729 0.1748 0.0086  -0.0025 -0.0018 294 ARG A CA  
2482 C C   . ARG A 294 ? 0.2212 0.2178 0.2167 0.0101  -0.0037 -0.0008 294 ARG A C   
2483 O O   . ARG A 294 ? 0.2319 0.2339 0.2303 0.0096  -0.0036 -0.0001 294 ARG A O   
2484 C CB  . ARG A 294 ? 0.1651 0.1577 0.1609 0.0051  -0.0034 -0.0013 294 ARG A CB  
2485 C CG  . ARG A 294 ? 0.1950 0.1898 0.1937 0.0040  -0.0060 -0.0005 294 ARG A CG  
2486 C CD  . ARG A 294 ? 0.1293 0.1245 0.1304 0.0006  -0.0069 -0.0002 294 ARG A CD  
2487 N NE  . ARG A 294 ? 0.2197 0.2199 0.2241 -0.0012 -0.0065 0.0005  294 ARG A NE  
2488 C CZ  . ARG A 294 ? 0.2362 0.2354 0.2406 -0.0033 -0.0053 0.0002  294 ARG A CZ  
2489 N NH1 . ARG A 294 ? 0.2685 0.2618 0.2698 -0.0040 -0.0044 -0.0007 294 ARG A NH1 
2490 N NH2 . ARG A 294 ? 0.2320 0.2362 0.2396 -0.0047 -0.0051 0.0009  294 ARG A NH2 
2491 N N   . TYR A 295 ? 0.1448 0.1406 0.1396 0.0118  -0.0050 -0.0007 295 TYR A N   
2492 C CA  . TYR A 295 ? 0.1476 0.1487 0.1449 0.0134  -0.0062 0.0002  295 TYR A CA  
2493 C C   . TYR A 295 ? 0.2212 0.2261 0.2226 0.0115  -0.0087 0.0012  295 TYR A C   
2494 O O   . TYR A 295 ? 0.2334 0.2354 0.2345 0.0099  -0.0098 0.0010  295 TYR A O   
2495 C CB  . TYR A 295 ? 0.1796 0.1779 0.1738 0.0166  -0.0060 -0.0003 295 TYR A CB  
2496 C CG  . TYR A 295 ? 0.1530 0.1489 0.1437 0.0189  -0.0037 -0.0011 295 TYR A CG  
2497 C CD1 . TYR A 295 ? 0.1737 0.1630 0.1600 0.0192  -0.0021 -0.0023 295 TYR A CD1 
2498 C CD2 . TYR A 295 ? 0.1952 0.1954 0.1869 0.0207  -0.0030 -0.0006 295 TYR A CD2 
2499 C CE1 . TYR A 295 ? 0.1474 0.1344 0.1304 0.0212  0.0001  -0.0031 295 TYR A CE1 
2500 C CE2 . TYR A 295 ? 0.1988 0.1968 0.1872 0.0228  -0.0009 -0.0014 295 TYR A CE2 
2501 C CZ  . TYR A 295 ? 0.2112 0.2025 0.1951 0.0231  0.0007  -0.0026 295 TYR A CZ  
2502 O OH  . TYR A 295 ? 0.2248 0.2138 0.2055 0.0252  0.0028  -0.0033 295 TYR A OH  
2503 N N   . TYR A 296 ? 0.2106 0.2220 0.2156 0.0117  -0.0097 0.0024  296 TYR A N   
2504 C CA  . TYR A 296 ? 0.2115 0.2269 0.2204 0.0103  -0.0122 0.0035  296 TYR A CA  
2505 C C   . TYR A 296 ? 0.2122 0.2301 0.2215 0.0129  -0.0133 0.0040  296 TYR A C   
2506 O O   . TYR A 296 ? 0.2065 0.2287 0.2171 0.0143  -0.0129 0.0045  296 TYR A O   
2507 C CB  . TYR A 296 ? 0.2032 0.2247 0.2166 0.0080  -0.0127 0.0044  296 TYR A CB  
2508 C CG  . TYR A 296 ? 0.1593 0.1789 0.1725 0.0055  -0.0115 0.0040  296 TYR A CG  
2509 C CD1 . TYR A 296 ? 0.1996 0.2149 0.2117 0.0036  -0.0120 0.0034  296 TYR A CD1 
2510 C CD2 . TYR A 296 ? 0.1514 0.1737 0.1655 0.0050  -0.0099 0.0040  296 TYR A CD2 
2511 C CE1 . TYR A 296 ? 0.2556 0.2691 0.2676 0.0013  -0.0110 0.0030  296 TYR A CE1 
2512 C CE2 . TYR A 296 ? 0.1899 0.2106 0.2040 0.0026  -0.0089 0.0036  296 TYR A CE2 
2513 C CZ  . TYR A 296 ? 0.1855 0.2017 0.1984 0.0008  -0.0094 0.0031  296 TYR A CZ  
2514 O OH  . TYR A 296 ? 0.2210 0.2355 0.2338 -0.0015 -0.0085 0.0028  296 TYR A OH  
2515 N N   . PHE A 297 ? 0.1988 0.2137 0.2069 0.0134  -0.0147 0.0039  297 PHE A N   
2516 C CA  . PHE A 297 ? 0.1839 0.2011 0.1925 0.0156  -0.0160 0.0044  297 PHE A CA  
2517 C C   . PHE A 297 ? 0.1508 0.1748 0.1644 0.0143  -0.0180 0.0059  297 PHE A C   
2518 O O   . PHE A 297 ? 0.1705 0.1950 0.1861 0.0120  -0.0198 0.0063  297 PHE A O   
2519 C CB  . PHE A 297 ? 0.1665 0.1784 0.1723 0.0165  -0.0169 0.0039  297 PHE A CB  
2520 C CG  . PHE A 297 ? 0.1610 0.1749 0.1672 0.0188  -0.0182 0.0044  297 PHE A CG  
2521 C CD1 . PHE A 297 ? 0.2258 0.2391 0.2296 0.0219  -0.0169 0.0041  297 PHE A CD1 
2522 C CD2 . PHE A 297 ? 0.1942 0.2106 0.2030 0.0179  -0.0207 0.0054  297 PHE A CD2 
2523 C CE1 . PHE A 297 ? 0.1755 0.1908 0.1797 0.0240  -0.0181 0.0047  297 PHE A CE1 
2524 C CE2 . PHE A 297 ? 0.2091 0.2275 0.2183 0.0199  -0.0220 0.0059  297 PHE A CE2 
2525 C CZ  . PHE A 297 ? 0.1443 0.1622 0.1513 0.0230  -0.0207 0.0056  297 PHE A CZ  
2526 N N   . ARG A 298 ? 0.1853 0.2147 0.2009 0.0156  -0.0178 0.0067  298 ARG A N   
2527 C CA  . ARG A 298 ? 0.1457 0.1822 0.1662 0.0145  -0.0196 0.0082  298 ARG A CA  
2528 C C   . ARG A 298 ? 0.2383 0.2771 0.2619 0.0111  -0.0204 0.0086  298 ARG A C   
2529 O O   . ARG A 298 ? 0.2128 0.2557 0.2401 0.0095  -0.0225 0.0097  298 ARG A O   
2530 C CB  . ARG A 298 ? 0.1502 0.1875 0.1714 0.0154  -0.0219 0.0088  298 ARG A CB  
2531 C CG  . ARG A 298 ? 0.1391 0.1755 0.1578 0.0190  -0.0212 0.0086  298 ARG A CG  
2532 C CD  . ARG A 298 ? 0.1609 0.1980 0.1802 0.0200  -0.0234 0.0092  298 ARG A CD  
2533 N NE  . ARG A 298 ? 0.2006 0.2358 0.2170 0.0234  -0.0225 0.0087  298 ARG A NE  
2534 C CZ  . ARG A 298 ? 0.2140 0.2479 0.2293 0.0249  -0.0238 0.0089  298 ARG A CZ  
2535 N NH1 . ARG A 298 ? 0.2077 0.2419 0.2246 0.0235  -0.0261 0.0094  298 ARG A NH1 
2536 N NH2 . ARG A 298 ? 0.1761 0.2082 0.1887 0.0280  -0.0228 0.0084  298 ARG A NH2 
2537 N N   . GLU A 299 ? 0.2380 0.2742 0.2603 0.0098  -0.0186 0.0078  299 GLU A N   
2538 C CA  . GLU A 299 ? 0.2641 0.3019 0.2889 0.0066  -0.0189 0.0081  299 GLU A CA  
2539 C C   . GLU A 299 ? 0.3023 0.3386 0.3283 0.0045  -0.0210 0.0083  299 GLU A C   
2540 O O   . GLU A 299 ? 0.2740 0.3130 0.3030 0.0017  -0.0219 0.0090  299 GLU A O   
2541 C CB  . GLU A 299 ? 0.2806 0.3259 0.3098 0.0057  -0.0192 0.0093  299 GLU A CB  
2542 C CG  . GLU A 299 ? 0.2215 0.2682 0.2499 0.0072  -0.0169 0.0091  299 GLU A CG  
2543 C CD  . GLU A 299 ? 0.3333 0.3780 0.3609 0.0053  -0.0152 0.0084  299 GLU A CD  
2544 O OE1 . GLU A 299 ? 0.4145 0.4622 0.4430 0.0056  -0.0138 0.0086  299 GLU A OE1 
2545 O OE2 . GLU A 299 ? 0.3272 0.3673 0.3533 0.0036  -0.0153 0.0077  299 GLU A OE2 
2546 N N   . LEU A 300 ? 0.1757 0.2073 0.1989 0.0056  -0.0216 0.0078  300 LEU A N   
2547 C CA  . LEU A 300 ? 0.2394 0.2695 0.2635 0.0039  -0.0237 0.0080  300 LEU A CA  
2548 C C   . LEU A 300 ? 0.2015 0.2241 0.2217 0.0035  -0.0230 0.0067  300 LEU A C   
2549 O O   . LEU A 300 ? 0.2262 0.2476 0.2474 0.0011  -0.0241 0.0068  300 LEU A O   
2550 C CB  . LEU A 300 ? 0.2693 0.3015 0.2943 0.0053  -0.0257 0.0088  300 LEU A CB  
2551 C CG  . LEU A 300 ? 0.3213 0.3613 0.3510 0.0048  -0.0271 0.0103  300 LEU A CG  
2552 C CD1 . LEU A 300 ? 0.3314 0.3734 0.3617 0.0067  -0.0288 0.0110  300 LEU A CD1 
2553 C CD2 . LEU A 300 ? 0.2654 0.3084 0.2989 0.0014  -0.0286 0.0110  300 LEU A CD2 
2554 N N   . ILE A 301 ? 0.1760 0.1937 0.1919 0.0056  -0.0211 0.0056  301 ILE A N   
2555 C CA  . ILE A 301 ? 0.1260 0.1367 0.1383 0.0052  -0.0204 0.0045  301 ILE A CA  
2556 C C   . ILE A 301 ? 0.1279 0.1351 0.1367 0.0065  -0.0177 0.0034  301 ILE A C   
2557 O O   . ILE A 301 ? 0.2257 0.2341 0.2335 0.0088  -0.0166 0.0033  301 ILE A O   
2558 C CB  . ILE A 301 ? 0.2368 0.2440 0.2470 0.0067  -0.0217 0.0042  301 ILE A CB  
2559 C CG1 . ILE A 301 ? 0.2167 0.2168 0.2234 0.0060  -0.0212 0.0031  301 ILE A CG1 
2560 C CG2 . ILE A 301 ? 0.2637 0.2707 0.2718 0.0100  -0.0211 0.0040  301 ILE A CG2 
2561 C CD1 . ILE A 301 ? 0.2088 0.2050 0.2131 0.0076  -0.0224 0.0028  301 ILE A CD1 
2562 N N   . SER A 302 ? 0.1805 0.1835 0.1875 0.0049  -0.0167 0.0026  302 SER A N   
2563 C CA  . SER A 302 ? 0.1706 0.1700 0.1744 0.0057  -0.0141 0.0016  302 SER A CA  
2564 C C   . SER A 302 ? 0.2064 0.1997 0.2055 0.0081  -0.0133 0.0005  302 SER A C   
2565 O O   . SER A 302 ? 0.1748 0.1647 0.1727 0.0080  -0.0145 0.0003  302 SER A O   
2566 C CB  . SER A 302 ? 0.2472 0.2448 0.2511 0.0030  -0.0133 0.0012  302 SER A CB  
2567 O OG  . SER A 302 ? 0.2276 0.2308 0.2356 0.0009  -0.0137 0.0022  302 SER A OG  
2568 N N   . VAL A 303 ? 0.1383 0.1301 0.1347 0.0102  -0.0114 -0.0001 303 VAL A N   
2569 C CA  . VAL A 303 ? 0.1390 0.1252 0.1308 0.0127  -0.0105 -0.0011 303 VAL A CA  
2570 C C   . VAL A 303 ? 0.1998 0.1825 0.1884 0.0132  -0.0079 -0.0021 303 VAL A C   
2571 O O   . VAL A 303 ? 0.1977 0.1834 0.1871 0.0136  -0.0067 -0.0019 303 VAL A O   
2572 C CB  . VAL A 303 ? 0.1955 0.1841 0.1872 0.0157  -0.0109 -0.0007 303 VAL A CB  
2573 C CG1 . VAL A 303 ? 0.2146 0.1971 0.2014 0.0182  -0.0099 -0.0018 303 VAL A CG1 
2574 C CG2 . VAL A 303 ? 0.1523 0.1448 0.1473 0.0153  -0.0135 0.0003  303 VAL A CG2 
2575 N N   . PHE A 304 ? 0.1788 0.1550 0.1637 0.0132  -0.0071 -0.0031 304 PHE A N   
2576 C CA  . PHE A 304 ? 0.1886 0.1605 0.1695 0.0142  -0.0047 -0.0041 304 PHE A CA  
2577 C C   . PHE A 304 ? 0.1980 0.1657 0.1750 0.0172  -0.0043 -0.0049 304 PHE A C   
2578 O O   . PHE A 304 ? 0.1653 0.1312 0.1417 0.0178  -0.0057 -0.0049 304 PHE A O   
2579 C CB  . PHE A 304 ? 0.1436 0.1111 0.1231 0.0119  -0.0040 -0.0047 304 PHE A CB  
2580 C CG  . PHE A 304 ? 0.1955 0.1667 0.1785 0.0090  -0.0040 -0.0042 304 PHE A CG  
2581 C CD1 . PHE A 304 ? 0.2659 0.2382 0.2486 0.0087  -0.0021 -0.0043 304 PHE A CD1 
2582 C CD2 . PHE A 304 ? 0.1959 0.1692 0.1820 0.0066  -0.0058 -0.0035 304 PHE A CD2 
2583 C CE1 . PHE A 304 ? 0.2440 0.2196 0.2298 0.0060  -0.0021 -0.0038 304 PHE A CE1 
2584 C CE2 . PHE A 304 ? 0.1906 0.1672 0.1798 0.0039  -0.0058 -0.0029 304 PHE A CE2 
2585 C CZ  . PHE A 304 ? 0.2279 0.2057 0.2170 0.0036  -0.0039 -0.0031 304 PHE A CZ  
2586 N N   . PHE A 305 ? 0.1892 0.1552 0.1634 0.0191  -0.0023 -0.0055 305 PHE A N   
2587 C CA  . PHE A 305 ? 0.1835 0.1452 0.1536 0.0219  -0.0015 -0.0063 305 PHE A CA  
2588 C C   . PHE A 305 ? 0.1904 0.1455 0.1563 0.0217  0.0003  -0.0074 305 PHE A C   
2589 O O   . PHE A 305 ? 0.2099 0.1649 0.1753 0.0209  0.0019  -0.0077 305 PHE A O   
2590 C CB  . PHE A 305 ? 0.1559 0.1206 0.1258 0.0245  -0.0007 -0.0061 305 PHE A CB  
2591 C CG  . PHE A 305 ? 0.1941 0.1651 0.1680 0.0249  -0.0024 -0.0049 305 PHE A CG  
2592 C CD1 . PHE A 305 ? 0.2369 0.2077 0.2104 0.0269  -0.0038 -0.0047 305 PHE A CD1 
2593 C CD2 . PHE A 305 ? 0.1530 0.1301 0.1312 0.0232  -0.0029 -0.0039 305 PHE A CD2 
2594 C CE1 . PHE A 305 ? 0.2583 0.2350 0.2356 0.0272  -0.0055 -0.0036 305 PHE A CE1 
2595 C CE2 . PHE A 305 ? 0.1950 0.1779 0.1769 0.0236  -0.0046 -0.0028 305 PHE A CE2 
2596 C CZ  . PHE A 305 ? 0.2509 0.2337 0.2324 0.0255  -0.0059 -0.0026 305 PHE A CZ  
2597 N N   . ARG A 306 ? 0.1581 0.1079 0.1211 0.0223  -0.0001 -0.0081 306 ARG A N   
2598 C CA  . ARG A 306 ? 0.2496 0.1930 0.2085 0.0220  0.0014  -0.0092 306 ARG A CA  
2599 C C   . ARG A 306 ? 0.2906 0.2319 0.2461 0.0242  0.0036  -0.0099 306 ARG A C   
2600 O O   . ARG A 306 ? 0.2310 0.1742 0.1861 0.0267  0.0037  -0.0098 306 ARG A O   
2601 C CB  . ARG A 306 ? 0.3271 0.2654 0.2835 0.0225  0.0005  -0.0097 306 ARG A CB  
2602 C CG  . ARG A 306 ? 0.2745 0.2105 0.2279 0.0257  0.0007  -0.0102 306 ARG A CG  
2603 C CD  . ARG A 306 ? 0.3161 0.2460 0.2662 0.0262  0.0003  -0.0109 306 ARG A CD  
2604 N NE  . ARG A 306 ? 0.3079 0.2353 0.2549 0.0293  0.0007  -0.0114 306 ARG A NE  
2605 C CZ  . ARG A 306 ? 0.3366 0.2582 0.2797 0.0305  0.0010  -0.0123 306 ARG A CZ  
2606 N NH1 . ARG A 306 ? 0.2741 0.1914 0.2157 0.0288  0.0010  -0.0127 306 ARG A NH1 
2607 N NH2 . ARG A 306 ? 0.2601 0.1801 0.2007 0.0334  0.0014  -0.0126 306 ARG A NH2 
2608 N N   . ASP A 307 ? 0.2327 0.1704 0.1858 0.0233  0.0053  -0.0106 307 ASP A N   
2609 C CA  . ASP A 307 ? 0.2758 0.2103 0.2250 0.0252  0.0074  -0.0114 307 ASP A CA  
2610 C C   . ASP A 307 ? 0.2853 0.2139 0.2302 0.0272  0.0075  -0.0122 307 ASP A C   
2611 O O   . ASP A 307 ? 0.2734 0.1971 0.2161 0.0262  0.0077  -0.0128 307 ASP A O   
2612 C CB  . ASP A 307 ? 0.2788 0.2111 0.2267 0.0233  0.0091  -0.0118 307 ASP A CB  
2613 C CG  . ASP A 307 ? 0.2652 0.1947 0.2094 0.0252  0.0113  -0.0126 307 ASP A CG  
2614 O OD1 . ASP A 307 ? 0.2639 0.1889 0.2042 0.0274  0.0118  -0.0133 307 ASP A OD1 
2615 O OD2 . ASP A 307 ? 0.3403 0.2720 0.2852 0.0245  0.0126  -0.0125 307 ASP A OD2 
2616 N N   . LYS A 308 ? 0.2591 0.1884 0.2031 0.0301  0.0074  -0.0123 308 LYS A N   
2617 C CA  . LYS A 308 ? 0.2974 0.2218 0.2378 0.0321  0.0071  -0.0129 308 LYS A CA  
2618 C C   . LYS A 308 ? 0.2338 0.1516 0.1693 0.0326  0.0090  -0.0141 308 LYS A C   
2619 O O   . LYS A 308 ? 0.2223 0.1352 0.1553 0.0326  0.0087  -0.0147 308 LYS A O   
2620 C CB  . LYS A 308 ? 0.2789 0.2057 0.2193 0.0351  0.0068  -0.0127 308 LYS A CB  
2621 C CG  . LYS A 308 ? 0.3422 0.2641 0.2789 0.0374  0.0066  -0.0134 308 LYS A CG  
2622 C CD  . LYS A 308 ? 0.3263 0.2509 0.2632 0.0404  0.0063  -0.0131 308 LYS A CD  
2623 C CE  . LYS A 308 ? 0.4410 0.3623 0.3756 0.0423  0.0054  -0.0134 308 LYS A CE  
2624 N NZ  . LYS A 308 ? 0.3863 0.3005 0.3168 0.0421  0.0060  -0.0145 308 LYS A NZ  
2625 N N   . THR A 309 ? 0.2750 0.1925 0.2090 0.0331  0.0109  -0.0144 309 THR A N   
2626 C CA  . THR A 309 ? 0.2851 0.1961 0.2141 0.0339  0.0127  -0.0155 309 THR A CA  
2627 C C   . THR A 309 ? 0.2496 0.1572 0.1779 0.0311  0.0129  -0.0158 309 THR A C   
2628 O O   . THR A 309 ? 0.2923 0.1941 0.2171 0.0315  0.0133  -0.0166 309 THR A O   
2629 C CB  . THR A 309 ? 0.3588 0.2699 0.2858 0.0353  0.0147  -0.0159 309 THR A CB  
2630 O OG1 . THR A 309 ? 0.5779 0.4897 0.5059 0.0329  0.0157  -0.0158 309 THR A OG1 
2631 C CG2 . THR A 309 ? 0.2101 0.1266 0.1393 0.0371  0.0144  -0.0152 309 THR A CG2 
2632 N N   . LEU A 310 ? 0.2432 0.1543 0.1750 0.0284  0.0125  -0.0152 310 LEU A N   
2633 C CA  . LEU A 310 ? 0.2158 0.1237 0.1472 0.0258  0.0127  -0.0154 310 LEU A CA  
2634 C C   . LEU A 310 ? 0.2715 0.1773 0.2031 0.0253  0.0110  -0.0154 310 LEU A C   
2635 O O   . LEU A 310 ? 0.2659 0.1664 0.1946 0.0246  0.0114  -0.0160 310 LEU A O   
2636 C CB  . LEU A 310 ? 0.2299 0.1423 0.1651 0.0231  0.0126  -0.0147 310 LEU A CB  
2637 C CG  . LEU A 310 ? 0.2663 0.1797 0.2009 0.0229  0.0146  -0.0149 310 LEU A CG  
2638 C CD1 . LEU A 310 ? 0.3203 0.2385 0.2592 0.0201  0.0142  -0.0141 310 LEU A CD1 
2639 C CD2 . LEU A 310 ? 0.2845 0.1914 0.2144 0.0228  0.0164  -0.0158 310 LEU A CD2 
2640 N N   . SER A 311 ? 0.2101 0.1199 0.1448 0.0256  0.0091  -0.0147 311 SER A N   
2641 C CA  . SER A 311 ? 0.2779 0.1858 0.2127 0.0253  0.0074  -0.0146 311 SER A CA  
2642 C C   . SER A 311 ? 0.3217 0.2238 0.2519 0.0276  0.0078  -0.0155 311 SER A C   
2643 O O   . SER A 311 ? 0.2434 0.1412 0.1720 0.0269  0.0074  -0.0159 311 SER A O   
2644 C CB  . SER A 311 ? 0.2369 0.1503 0.1758 0.0255  0.0054  -0.0137 311 SER A CB  
2645 O OG  . SER A 311 ? 0.1891 0.1078 0.1323 0.0232  0.0048  -0.0128 311 SER A OG  
2646 N N   . ASP A 312 ? 0.2556 0.1575 0.1838 0.0303  0.0087  -0.0158 312 ASP A N   
2647 C CA  . ASP A 312 ? 0.2956 0.1924 0.2196 0.0327  0.0090  -0.0167 312 ASP A CA  
2648 C C   . ASP A 312 ? 0.2845 0.1752 0.2042 0.0324  0.0108  -0.0176 312 ASP A C   
2649 O O   . ASP A 312 ? 0.2921 0.1777 0.2086 0.0333  0.0108  -0.0183 312 ASP A O   
2650 C CB  . ASP A 312 ? 0.2966 0.1951 0.2198 0.0358  0.0095  -0.0167 312 ASP A CB  
2651 C CG  . ASP A 312 ? 0.3255 0.2282 0.2516 0.0368  0.0075  -0.0159 312 ASP A CG  
2652 O OD1 . ASP A 312 ? 0.2994 0.2029 0.2276 0.0354  0.0058  -0.0155 312 ASP A OD1 
2653 O OD2 . ASP A 312 ? 0.3712 0.2765 0.2974 0.0390  0.0077  -0.0157 312 ASP A OD2 
2654 N N   . LEU A 313 ? 0.2594 0.1505 0.1790 0.0313  0.0123  -0.0177 313 LEU A N   
2655 C CA  . LEU A 313 ? 0.2611 0.1466 0.1768 0.0308  0.0140  -0.0185 313 LEU A CA  
2656 C C   . LEU A 313 ? 0.2467 0.1287 0.1620 0.0288  0.0133  -0.0187 313 LEU A C   
2657 O O   . LEU A 313 ? 0.3007 0.1774 0.2124 0.0293  0.0138  -0.0193 313 LEU A O   
2658 C CB  . LEU A 313 ? 0.2869 0.1741 0.2032 0.0295  0.0156  -0.0184 313 LEU A CB  
2659 C CG  . LEU A 313 ? 0.2930 0.1815 0.2079 0.0319  0.0169  -0.0186 313 LEU A CG  
2660 C CD1 . LEU A 313 ? 0.3765 0.2680 0.2930 0.0305  0.0181  -0.0183 313 LEU A CD1 
2661 C CD2 . LEU A 313 ? 0.3301 0.2126 0.2396 0.0340  0.0183  -0.0196 313 LEU A CD2 
2662 N N   . ILE A 314 ? 0.2672 0.1525 0.1864 0.0264  0.0120  -0.0179 314 ILE A N   
2663 C CA  . ILE A 314 ? 0.2040 0.0863 0.1229 0.0245  0.0112  -0.0180 314 ILE A CA  
2664 C C   . ILE A 314 ? 0.2758 0.1558 0.1936 0.0261  0.0098  -0.0182 314 ILE A C   
2665 O O   . ILE A 314 ? 0.3048 0.1810 0.2205 0.0257  0.0098  -0.0185 314 ILE A O   
2666 C CB  . ILE A 314 ? 0.2438 0.1304 0.1673 0.0216  0.0101  -0.0172 314 ILE A CB  
2667 C CG1 . ILE A 314 ? 0.2505 0.1388 0.1749 0.0200  0.0116  -0.0171 314 ILE A CG1 
2668 C CG2 . ILE A 314 ? 0.2154 0.0991 0.1389 0.0199  0.0091  -0.0172 314 ILE A CG2 
2669 C CD1 . ILE A 314 ? 0.2095 0.1025 0.1385 0.0172  0.0106  -0.0162 314 ILE A CD1 
2670 N N   . GLY A 315 ? 0.3165 0.2004 0.2365 0.0274  0.0085  -0.0177 315 GLY A N   
2671 C CA  . GLY A 315 ? 0.3002 0.1827 0.2198 0.0285  0.0069  -0.0177 315 GLY A CA  
2672 C C   . GLY A 315 ? 0.3487 0.2262 0.2637 0.0312  0.0077  -0.0186 315 GLY A C   
2673 O O   . GLY A 315 ? 0.3869 0.2617 0.3008 0.0315  0.0068  -0.0188 315 GLY A O   
2674 N N   . PHE A 316 ? 0.3556 0.2323 0.2683 0.0329  0.0093  -0.0190 316 PHE A N   
2675 C CA  . PHE A 316 ? 0.3803 0.2556 0.2906 0.0349  0.0098  -0.0192 316 PHE A CA  
2676 C C   . PHE A 316 ? 0.3717 0.2472 0.2809 0.0342  0.0115  -0.0191 316 PHE A C   
2677 O O   . PHE A 316 ? 0.4131 0.2883 0.3211 0.0347  0.0116  -0.0189 316 PHE A O   
2678 C CB  . PHE A 316 ? 0.3564 0.2325 0.2660 0.0382  0.0095  -0.0195 316 PHE A CB  
2679 C CG  . PHE A 316 ? 0.3872 0.2674 0.3005 0.0381  0.0073  -0.0187 316 PHE A CG  
2680 C CD1 . PHE A 316 ? 0.4378 0.3154 0.3499 0.0390  0.0060  -0.0189 316 PHE A CD1 
2681 C CD2 . PHE A 316 ? 0.3486 0.2352 0.2663 0.0370  0.0065  -0.0178 316 PHE A CD2 
2682 C CE1 . PHE A 316 ? 0.4870 0.3683 0.4024 0.0388  0.0039  -0.0181 316 PHE A CE1 
2683 C CE2 . PHE A 316 ? 0.3578 0.2481 0.2789 0.0368  0.0044  -0.0170 316 PHE A CE2 
2684 C CZ  . PHE A 316 ? 0.4374 0.3251 0.3573 0.0377  0.0031  -0.0172 316 PHE A CZ  
2685 N N   . SER A 317 ? 0.3348 0.2108 0.2441 0.0331  0.0128  -0.0192 317 SER A N   
2686 C CA  . SER A 317 ? 0.3340 0.2101 0.2419 0.0329  0.0144  -0.0191 317 SER A CA  
2687 C C   . SER A 317 ? 0.3507 0.2270 0.2594 0.0300  0.0148  -0.0186 317 SER A C   
2688 O O   . SER A 317 ? 0.3874 0.2635 0.2952 0.0297  0.0151  -0.0183 317 SER A O   
2689 C CB  . SER A 317 ? 0.4152 0.2920 0.3225 0.0340  0.0157  -0.0195 317 SER A CB  
2690 O OG  . SER A 317 ? 0.5841 0.4610 0.4903 0.0332  0.0172  -0.0193 317 SER A OG  
2691 N N   . TYR A 318 ? 0.3221 0.1987 0.2325 0.0278  0.0147  -0.0185 318 TYR A N   
2692 C CA  . TYR A 318 ? 0.2653 0.1424 0.1764 0.0252  0.0153  -0.0181 318 TYR A CA  
2693 C C   . TYR A 318 ? 0.2698 0.1469 0.1815 0.0239  0.0145  -0.0176 318 TYR A C   
2694 O O   . TYR A 318 ? 0.2824 0.1601 0.1943 0.0222  0.0151  -0.0171 318 TYR A O   
2695 C CB  . TYR A 318 ? 0.2847 0.1623 0.1976 0.0231  0.0153  -0.0181 318 TYR A CB  
2696 C CG  . TYR A 318 ? 0.3205 0.1983 0.2328 0.0237  0.0166  -0.0185 318 TYR A CG  
2697 C CD1 . TYR A 318 ? 0.3407 0.2185 0.2511 0.0251  0.0180  -0.0187 318 TYR A CD1 
2698 C CD2 . TYR A 318 ? 0.3549 0.2329 0.2685 0.0228  0.0164  -0.0187 318 TYR A CD2 
2699 C CE1 . TYR A 318 ? 0.3530 0.2311 0.2629 0.0257  0.0192  -0.0191 318 TYR A CE1 
2700 C CE2 . TYR A 318 ? 0.3514 0.2297 0.2644 0.0234  0.0177  -0.0192 318 TYR A CE2 
2701 C CZ  . TYR A 318 ? 0.3792 0.2577 0.2904 0.0249  0.0191  -0.0193 318 TYR A CZ  
2702 O OH  . TYR A 318 ? 0.3203 0.2015 0.2324 0.0250  0.0202  -0.0193 318 TYR A OH  
2703 N N   . HIS A 319 ? 0.2821 0.1589 0.1941 0.0247  0.0132  -0.0176 319 HIS A N   
2704 C CA  . HIS A 319 ? 0.3720 0.2490 0.2845 0.0237  0.0125  -0.0171 319 HIS A CA  
2705 C C   . HIS A 319 ? 0.4267 0.3036 0.3376 0.0240  0.0135  -0.0168 319 HIS A C   
2706 O O   . HIS A 319 ? 0.4053 0.2827 0.3167 0.0225  0.0135  -0.0163 319 HIS A O   
2707 C CB  . HIS A 319 ? 0.3574 0.2339 0.2699 0.0251  0.0111  -0.0172 319 HIS A CB  
2708 C CG  . HIS A 319 ? 0.3378 0.2135 0.2482 0.0276  0.0113  -0.0174 319 HIS A CG  
2709 N ND1 . HIS A 319 ? 0.3753 0.2506 0.2847 0.0299  0.0114  -0.0179 319 HIS A ND1 
2710 C CD2 . HIS A 319 ? 0.3477 0.2231 0.2569 0.0282  0.0114  -0.0172 319 HIS A CD2 
2711 C CE1 . HIS A 319 ? 0.4201 0.2949 0.3278 0.0318  0.0116  -0.0180 319 HIS A CE1 
2712 N NE2 . HIS A 319 ? 0.3866 0.2614 0.2941 0.0307  0.0116  -0.0176 319 HIS A NE2 
2713 N N   . ALA A 320 ? 0.3931 0.2694 0.3021 0.0259  0.0143  -0.0171 320 ALA A N   
2714 C CA  . ALA A 320 ? 0.6010 0.4769 0.5082 0.0264  0.0152  -0.0169 320 ALA A CA  
2715 C C   . ALA A 320 ? 0.6702 0.5465 0.5771 0.0253  0.0166  -0.0167 320 ALA A C   
2716 O O   . ALA A 320 ? 0.6582 0.5340 0.5635 0.0257  0.0173  -0.0165 320 ALA A O   
2717 C CB  . ALA A 320 ? 0.5219 0.3971 0.4273 0.0292  0.0153  -0.0173 320 ALA A CB  
2718 N N   . TRP A 321 ? 0.5364 0.4133 0.4446 0.0238  0.0169  -0.0168 321 TRP A N   
2719 C CA  . TRP A 321 ? 0.4994 0.3766 0.4073 0.0225  0.0181  -0.0165 321 TRP A CA  
2720 C C   . TRP A 321 ? 0.4951 0.3732 0.4046 0.0199  0.0179  -0.0160 321 TRP A C   
2721 O O   . TRP A 321 ? 0.5149 0.3936 0.4261 0.0190  0.0168  -0.0158 321 TRP A O   
2722 C CB  . TRP A 321 ? 0.4433 0.3208 0.3516 0.0227  0.0188  -0.0170 321 TRP A CB  
2723 C CG  . TRP A 321 ? 0.3840 0.2610 0.2910 0.0252  0.0191  -0.0176 321 TRP A CG  
2724 C CD1 . TRP A 321 ? 0.3458 0.2224 0.2522 0.0273  0.0183  -0.0179 321 TRP A CD1 
2725 C CD2 . TRP A 321 ? 0.4498 0.3270 0.3560 0.0260  0.0203  -0.0180 321 TRP A CD2 
2726 N NE1 . TRP A 321 ? 0.3749 0.2515 0.2803 0.0295  0.0189  -0.0184 321 TRP A NE1 
2727 C CE2 . TRP A 321 ? 0.4095 0.2865 0.3147 0.0288  0.0202  -0.0185 321 TRP A CE2 
2728 C CE3 . TRP A 321 ? 0.4786 0.3563 0.3848 0.0248  0.0216  -0.0179 321 TRP A CE3 
2729 C CZ2 . TRP A 321 ? 0.4818 0.3593 0.3861 0.0303  0.0213  -0.0189 321 TRP A CZ2 
2730 C CZ3 . TRP A 321 ? 0.4406 0.3185 0.3459 0.0262  0.0227  -0.0184 321 TRP A CZ3 
2731 C CH2 . TRP A 321 ? 0.4418 0.3197 0.3461 0.0290  0.0225  -0.0188 321 TRP A CH2 
2732 N N   . ASN A 322 ? 0.4546 0.3329 0.3636 0.0188  0.0189  -0.0156 322 ASN A N   
2733 C CA  . ASN A 322 ? 0.4409 0.3203 0.3515 0.0164  0.0190  -0.0151 322 ASN A CA  
2734 C C   . ASN A 322 ? 0.4533 0.3333 0.3656 0.0153  0.0189  -0.0154 322 ASN A C   
2735 O O   . ASN A 322 ? 0.4228 0.3024 0.3345 0.0163  0.0195  -0.0159 322 ASN A O   
2736 C CB  . ASN A 322 ? 0.6010 0.4804 0.5104 0.0156  0.0201  -0.0146 322 ASN A CB  
2737 C CG  . ASN A 322 ? 0.7519 0.6326 0.6629 0.0132  0.0202  -0.0140 322 ASN A CG  
2738 O OD1 . ASN A 322 ? 0.8435 0.7247 0.7551 0.0121  0.0209  -0.0140 322 ASN A OD1 
2739 N ND2 . ASN A 322 ? 0.7636 0.6447 0.6751 0.0125  0.0195  -0.0136 322 ASN A ND2 
2740 N N   . ALA A 323 ? 0.4054 0.3176 0.2973 0.0098  -0.0008 -0.0143 323 ALA A N   
2741 C CA  . ALA A 323 ? 0.4292 0.3446 0.3217 0.0093  -0.0010 -0.0147 323 ALA A CA  
2742 C C   . ALA A 323 ? 0.4766 0.3926 0.3687 0.0071  -0.0002 -0.0162 323 ALA A C   
2743 O O   . ALA A 323 ? 0.4104 0.3277 0.3034 0.0072  0.0000  -0.0175 323 ALA A O   
2744 C CB  . ALA A 323 ? 0.3704 0.2881 0.2623 0.0089  -0.0017 -0.0128 323 ALA A CB  
2745 N N   . GLU A 324 ? 0.4118 0.3269 0.3026 0.0052  0.0002  -0.0160 324 GLU A N   
2746 C CA  . GLU A 324 ? 0.4237 0.3394 0.3142 0.0031  0.0009  -0.0173 324 GLU A CA  
2747 C C   . GLU A 324 ? 0.4281 0.3422 0.3193 0.0036  0.0015  -0.0194 324 GLU A C   
2748 O O   . GLU A 324 ? 0.4038 0.3194 0.2954 0.0028  0.0019  -0.0208 324 GLU A O   
2749 C CB  . GLU A 324 ? 0.5398 0.4544 0.4288 0.0011  0.0013  -0.0167 324 GLU A CB  
2750 C CG  . GLU A 324 ? 0.6550 0.5700 0.5434 -0.0012 0.0020  -0.0181 324 GLU A CG  
2751 C CD  . GLU A 324 ? 0.7857 0.7040 0.6739 -0.0026 0.0019  -0.0179 324 GLU A CD  
2752 O OE1 . GLU A 324 ? 0.7908 0.7111 0.6792 -0.0021 0.0012  -0.0165 324 GLU A OE1 
2753 O OE2 . GLU A 324 ? 0.8604 0.7794 0.7484 -0.0044 0.0025  -0.0191 324 GLU A OE2 
2754 N N   . ASP A 325 ? 0.4306 0.3418 0.3220 0.0049  0.0017  -0.0197 325 ASP A N   
2755 C CA  . ASP A 325 ? 0.4375 0.3471 0.3296 0.0055  0.0022  -0.0217 325 ASP A CA  
2756 C C   . ASP A 325 ? 0.3360 0.2471 0.2296 0.0071  0.0020  -0.0225 325 ASP A C   
2757 O O   . ASP A 325 ? 0.3361 0.2476 0.2303 0.0068  0.0025  -0.0242 325 ASP A O   
2758 C CB  . ASP A 325 ? 0.4447 0.3509 0.3368 0.0067  0.0024  -0.0217 325 ASP A CB  
2759 C CG  . ASP A 325 ? 0.6303 0.5346 0.5210 0.0049  0.0028  -0.0216 325 ASP A CG  
2760 O OD1 . ASP A 325 ? 0.6948 0.6005 0.5847 0.0027  0.0031  -0.0216 325 ASP A OD1 
2761 O OD2 . ASP A 325 ? 0.6284 0.5300 0.5190 0.0057  0.0029  -0.0215 325 ASP A OD2 
2762 N N   . ALA A 326 ? 0.3533 0.2653 0.2475 0.0088  0.0012  -0.0212 326 ALA A N   
2763 C CA  . ALA A 326 ? 0.3248 0.2382 0.2203 0.0105  0.0009  -0.0219 326 ALA A CA  
2764 C C   . ALA A 326 ? 0.3317 0.2481 0.2274 0.0091  0.0011  -0.0225 326 ALA A C   
2765 O O   . ALA A 326 ? 0.3300 0.2471 0.2268 0.0096  0.0013  -0.0240 326 ALA A O   
2766 C CB  . ALA A 326 ? 0.2732 0.1871 0.1692 0.0124  0.0000  -0.0202 326 ALA A CB  
2767 N N   . VAL A 327 ? 0.3689 0.2873 0.2638 0.0075  0.0009  -0.0214 327 VAL A N   
2768 C CA  . VAL A 327 ? 0.3439 0.2653 0.2390 0.0063  0.0010  -0.0218 327 VAL A CA  
2769 C C   . VAL A 327 ? 0.3219 0.2429 0.2168 0.0046  0.0018  -0.0237 327 VAL A C   
2770 O O   . VAL A 327 ? 0.2834 0.2059 0.1791 0.0045  0.0021  -0.0250 327 VAL A O   
2771 C CB  . VAL A 327 ? 0.3771 0.3005 0.2712 0.0049  0.0006  -0.0201 327 VAL A CB  
2772 C CG1 . VAL A 327 ? 0.3619 0.2881 0.2559 0.0031  0.0008  -0.0208 327 VAL A CG1 
2773 C CG2 . VAL A 327 ? 0.3904 0.3148 0.2848 0.0066  -0.0004 -0.0184 327 VAL A CG2 
2774 N N   . ARG A 328 ? 0.2620 0.1808 0.1559 0.0034  0.0024  -0.0239 328 ARG A N   
2775 C CA  . ARG A 328 ? 0.3136 0.2317 0.2073 0.0020  0.0032  -0.0257 328 ARG A CA  
2776 C C   . ARG A 328 ? 0.3766 0.2935 0.2715 0.0034  0.0035  -0.0275 328 ARG A C   
2777 O O   . ARG A 328 ? 0.3419 0.2598 0.2372 0.0027  0.0040  -0.0290 328 ARG A O   
2778 C CB  . ARG A 328 ? 0.4595 0.3752 0.3519 0.0007  0.0036  -0.0255 328 ARG A CB  
2779 C CG  . ARG A 328 ? 0.5936 0.5072 0.4861 0.0001  0.0045  -0.0274 328 ARG A CG  
2780 C CD  . ARG A 328 ? 0.6923 0.6032 0.5836 -0.0008 0.0048  -0.0270 328 ARG A CD  
2781 N NE  . ARG A 328 ? 0.7346 0.6429 0.6262 0.0011  0.0045  -0.0266 328 ARG A NE  
2782 C CZ  . ARG A 328 ? 0.7986 0.7047 0.6908 0.0022  0.0049  -0.0279 328 ARG A CZ  
2783 N NH1 . ARG A 328 ? 0.8703 0.7763 0.7628 0.0015  0.0055  -0.0298 328 ARG A NH1 
2784 N NH2 . ARG A 328 ? 0.7765 0.6803 0.6689 0.0040  0.0046  -0.0274 328 ARG A NH2 
2785 N N   . ASP A 329 ? 0.3717 0.2867 0.2672 0.0055  0.0032  -0.0273 329 ASP A N   
2786 C CA  . ASP A 329 ? 0.3972 0.3112 0.2940 0.0071  0.0035  -0.0288 329 ASP A CA  
2787 C C   . ASP A 329 ? 0.3746 0.2913 0.2725 0.0078  0.0032  -0.0293 329 ASP A C   
2788 O O   . ASP A 329 ? 0.3798 0.2968 0.2784 0.0078  0.0037  -0.0310 329 ASP A O   
2789 C CB  . ASP A 329 ? 0.2845 0.1960 0.1816 0.0094  0.0031  -0.0283 329 ASP A CB  
2790 C CG  . ASP A 329 ? 0.3797 0.2900 0.2781 0.0110  0.0033  -0.0299 329 ASP A CG  
2791 O OD1 . ASP A 329 ? 0.4386 0.3470 0.3369 0.0106  0.0040  -0.0313 329 ASP A OD1 
2792 O OD2 . ASP A 329 ? 0.4081 0.3194 0.3075 0.0128  0.0028  -0.0297 329 ASP A OD2 
2793 N N   . PHE A 330 ? 0.2781 0.1968 0.1761 0.0084  0.0025  -0.0278 330 PHE A N   
2794 C CA  . PHE A 330 ? 0.2739 0.1952 0.1730 0.0092  0.0021  -0.0281 330 PHE A CA  
2795 C C   . PHE A 330 ? 0.2972 0.2207 0.1961 0.0072  0.0026  -0.0291 330 PHE A C   
2796 O O   . PHE A 330 ? 0.2969 0.2213 0.1968 0.0075  0.0029  -0.0305 330 PHE A O   
2797 C CB  . PHE A 330 ? 0.2540 0.1770 0.1531 0.0100  0.0012  -0.0261 330 PHE A CB  
2798 C CG  . PHE A 330 ? 0.2960 0.2213 0.1963 0.0113  0.0008  -0.0262 330 PHE A CG  
2799 C CD1 . PHE A 330 ? 0.3611 0.2855 0.2626 0.0138  0.0004  -0.0264 330 PHE A CD1 
2800 C CD2 . PHE A 330 ? 0.2907 0.2192 0.1911 0.0102  0.0006  -0.0260 330 PHE A CD2 
2801 C CE1 . PHE A 330 ? 0.3259 0.2525 0.2287 0.0150  0.0000  -0.0265 330 PHE A CE1 
2802 C CE2 . PHE A 330 ? 0.3052 0.2358 0.2067 0.0113  0.0002  -0.0261 330 PHE A CE2 
2803 C CZ  . PHE A 330 ? 0.2685 0.1982 0.1712 0.0137  -0.0001 -0.0264 330 PHE A CZ  
2804 N N   . ILE A 331 ? 0.2809 0.2053 0.1786 0.0051  0.0027  -0.0283 331 ILE A N   
2805 C CA  . ILE A 331 ? 0.3156 0.2421 0.2130 0.0031  0.0031  -0.0292 331 ILE A CA  
2806 C C   . ILE A 331 ? 0.3536 0.2787 0.2512 0.0024  0.0040  -0.0312 331 ILE A C   
2807 O O   . ILE A 331 ? 0.3679 0.2945 0.2659 0.0016  0.0044  -0.0325 331 ILE A O   
2808 C CB  . ILE A 331 ? 0.3411 0.2687 0.2372 0.0010  0.0031  -0.0279 331 ILE A CB  
2809 C CG1 . ILE A 331 ? 0.3689 0.2981 0.2649 0.0017  0.0022  -0.0259 331 ILE A CG1 
2810 C CG2 . ILE A 331 ? 0.4477 0.3775 0.3435 -0.0012 0.0036  -0.0288 331 ILE A CG2 
2811 C CD1 . ILE A 331 ? 0.3757 0.3081 0.2723 0.0018  0.0018  -0.0257 331 ILE A CD1 
2812 N N   . GLY A 332 ? 0.3884 0.3105 0.2856 0.0026  0.0044  -0.0316 332 GLY A N   
2813 C CA  . GLY A 332 ? 0.3110 0.2315 0.2084 0.0020  0.0052  -0.0336 332 GLY A CA  
2814 C C   . GLY A 332 ? 0.3501 0.2708 0.2489 0.0036  0.0053  -0.0350 332 GLY A C   
2815 O O   . GLY A 332 ? 0.3817 0.3029 0.2808 0.0028  0.0058  -0.0366 332 GLY A O   
2816 N N   . ARG A 333 ? 0.3064 0.2266 0.2061 0.0059  0.0047  -0.0344 333 ARG A N   
2817 C CA  . ARG A 333 ? 0.3646 0.2852 0.2658 0.0075  0.0047  -0.0357 333 ARG A CA  
2818 C C   . ARG A 333 ? 0.3606 0.2844 0.2623 0.0070  0.0046  -0.0361 333 ARG A C   
2819 O O   . ARG A 333 ? 0.3019 0.2261 0.2045 0.0072  0.0050  -0.0377 333 ARG A O   
2820 C CB  . ARG A 333 ? 0.3502 0.2696 0.2521 0.0101  0.0041  -0.0349 333 ARG A CB  
2821 C CG  . ARG A 333 ? 0.3369 0.2530 0.2384 0.0108  0.0042  -0.0347 333 ARG A CG  
2822 C CD  . ARG A 333 ? 0.3640 0.2793 0.2662 0.0132  0.0035  -0.0336 333 ARG A CD  
2823 N NE  . ARG A 333 ? 0.3451 0.2571 0.2468 0.0140  0.0036  -0.0334 333 ARG A NE  
2824 C CZ  . ARG A 333 ? 0.3538 0.2636 0.2562 0.0154  0.0038  -0.0346 333 ARG A CZ  
2825 N NH1 . ARG A 333 ? 0.3149 0.2253 0.2185 0.0162  0.0040  -0.0361 333 ARG A NH1 
2826 N NH2 . ARG A 333 ? 0.4091 0.3160 0.3110 0.0159  0.0039  -0.0343 333 ARG A NH2 
2827 N N   . LEU A 334 ? 0.3015 0.2276 0.2028 0.0063  0.0041  -0.0346 334 LEU A N   
2828 C CA  . LEU A 334 ? 0.2588 0.1881 0.1605 0.0056  0.0040  -0.0348 334 LEU A CA  
2829 C C   . LEU A 334 ? 0.2890 0.2189 0.1903 0.0035  0.0048  -0.0362 334 LEU A C   
2830 O O   . LEU A 334 ? 0.3257 0.2572 0.2278 0.0033  0.0050  -0.0374 334 LEU A O   
2831 C CB  . LEU A 334 ? 0.2189 0.1504 0.1202 0.0051  0.0033  -0.0329 334 LEU A CB  
2832 C CG  . LEU A 334 ? 0.2261 0.1577 0.1279 0.0073  0.0025  -0.0315 334 LEU A CG  
2833 C CD1 . LEU A 334 ? 0.2192 0.1530 0.1203 0.0066  0.0019  -0.0296 334 LEU A CD1 
2834 C CD2 . LEU A 334 ? 0.2434 0.1758 0.1468 0.0092  0.0023  -0.0324 334 LEU A CD2 
2835 N N   . LYS A 335 ? 0.2737 0.2023 0.1737 0.0018  0.0052  -0.0361 335 LYS A N   
2836 C CA  . LYS A 335 ? 0.4057 0.3346 0.3053 -0.0003 0.0060  -0.0375 335 LYS A CA  
2837 C C   . LYS A 335 ? 0.3945 0.3220 0.2949 0.0004  0.0066  -0.0395 335 LYS A C   
2838 O O   . LYS A 335 ? 0.3638 0.2927 0.2646 -0.0006 0.0071  -0.0409 335 LYS A O   
2839 C CB  . LYS A 335 ? 0.3185 0.2457 0.2166 -0.0019 0.0063  -0.0370 335 LYS A CB  
2840 C CG  . LYS A 335 ? 0.5142 0.4417 0.4117 -0.0041 0.0071  -0.0383 335 LYS A CG  
2841 C CD  . LYS A 335 ? 0.5449 0.4708 0.4409 -0.0058 0.0074  -0.0377 335 LYS A CD  
2842 C CE  . LYS A 335 ? 0.5902 0.5127 0.4860 -0.0053 0.0079  -0.0386 335 LYS A CE  
2843 N NZ  . LYS A 335 ? 0.5830 0.5052 0.4787 -0.0068 0.0087  -0.0405 335 LYS A NZ  
2844 N N   . LYS A 336 ? 0.3876 0.3124 0.2884 0.0020  0.0066  -0.0398 336 LYS A N   
2845 C CA  . LYS A 336 ? 0.4514 0.3749 0.3531 0.0028  0.0071  -0.0418 336 LYS A CA  
2846 C C   . LYS A 336 ? 0.4529 0.3784 0.3559 0.0039  0.0070  -0.0425 336 LYS A C   
2847 O O   . LYS A 336 ? 0.4744 0.4006 0.3779 0.0033  0.0075  -0.0442 336 LYS A O   
2848 C CB  . LYS A 336 ? 0.4871 0.4074 0.3890 0.0046  0.0071  -0.0417 336 LYS A CB  
2849 C CG  . LYS A 336 ? 0.6131 0.5307 0.5140 0.0034  0.0077  -0.0424 336 LYS A CG  
2850 C CD  . LYS A 336 ? 0.6747 0.5907 0.5746 0.0034  0.0074  -0.0407 336 LYS A CD  
2851 C CE  . LYS A 336 ? 0.7826 0.6966 0.6831 0.0059  0.0069  -0.0402 336 LYS A CE  
2852 N NZ  . LYS A 336 ? 0.8125 0.7252 0.7121 0.0059  0.0065  -0.0384 336 LYS A NZ  
2853 N N   . ILE A 337 ? 0.4320 0.3587 0.3358 0.0055  0.0062  -0.0414 337 ILE A N   
2854 C CA  . ILE A 337 ? 0.3307 0.2597 0.2357 0.0064  0.0060  -0.0419 337 ILE A CA  
2855 C C   . ILE A 337 ? 0.3891 0.3207 0.2937 0.0044  0.0063  -0.0424 337 ILE A C   
2856 O O   . ILE A 337 ? 0.3855 0.3180 0.2909 0.0043  0.0067  -0.0439 337 ILE A O   
2857 C CB  . ILE A 337 ? 0.3077 0.2379 0.2131 0.0080  0.0050  -0.0402 337 ILE A CB  
2858 C CG1 . ILE A 337 ? 0.3346 0.2622 0.2403 0.0101  0.0047  -0.0396 337 ILE A CG1 
2859 C CG2 . ILE A 337 ? 0.3051 0.2377 0.2119 0.0089  0.0048  -0.0408 337 ILE A CG2 
2860 C CD1 . ILE A 337 ? 0.3911 0.3198 0.2972 0.0116  0.0037  -0.0378 337 ILE A CD1 
2861 N N   . HIS A 338 ? 0.3124 0.2452 0.2160 0.0027  0.0061  -0.0411 338 HIS A N   
2862 C CA  . HIS A 338 ? 0.3064 0.2419 0.2096 0.0008  0.0064  -0.0414 338 HIS A CA  
2863 C C   . HIS A 338 ? 0.3895 0.3245 0.2926 -0.0006 0.0073  -0.0433 338 HIS A C   
2864 O O   . HIS A 338 ? 0.3346 0.2715 0.2381 -0.0012 0.0075  -0.0443 338 HIS A O   
2865 C CB  . HIS A 338 ? 0.3427 0.2791 0.2446 -0.0007 0.0061  -0.0397 338 HIS A CB  
2866 C CG  . HIS A 338 ? 0.4275 0.3665 0.3288 -0.0028 0.0063  -0.0398 338 HIS A CG  
2867 N ND1 . HIS A 338 ? 0.4935 0.4323 0.3939 -0.0050 0.0069  -0.0404 338 HIS A ND1 
2868 C CD2 . HIS A 338 ? 0.4680 0.4101 0.3699 -0.0030 0.0059  -0.0394 338 HIS A CD2 
2869 C CE1 . HIS A 338 ? 0.4261 0.3676 0.3262 -0.0065 0.0069  -0.0403 338 HIS A CE1 
2870 N NE2 . HIS A 338 ? 0.4963 0.4399 0.3973 -0.0053 0.0063  -0.0397 338 HIS A NE2 
2871 N N   . GLU A 339 ? 0.4053 0.3375 0.3077 -0.0010 0.0078  -0.0439 339 GLU A N   
2872 C CA  . GLU A 339 ? 0.4764 0.4080 0.3787 -0.0024 0.0086  -0.0457 339 GLU A CA  
2873 C C   . GLU A 339 ? 0.4859 0.4164 0.3893 -0.0009 0.0089  -0.0474 339 GLU A C   
2874 O O   . GLU A 339 ? 0.4407 0.3709 0.3442 -0.0019 0.0097  -0.0491 339 GLU A O   
2875 C CB  . GLU A 339 ? 0.4540 0.3831 0.3549 -0.0036 0.0090  -0.0456 339 GLU A CB  
2876 C CG  . GLU A 339 ? 0.5888 0.5192 0.4885 -0.0057 0.0090  -0.0445 339 GLU A CG  
2877 C CD  . GLU A 339 ? 0.7050 0.6328 0.6034 -0.0063 0.0091  -0.0438 339 GLU A CD  
2878 O OE1 . GLU A 339 ? 0.6572 0.5823 0.5559 -0.0051 0.0093  -0.0443 339 GLU A OE1 
2879 O OE2 . GLU A 339 ? 0.7961 0.7248 0.6935 -0.0078 0.0090  -0.0426 339 GLU A OE2 
2880 N N   . SER A 340 ? 0.5173 0.4473 0.4218 0.0014  0.0085  -0.0471 340 SER A N   
2881 C CA  . SER A 340 ? 0.4504 0.3791 0.3561 0.0029  0.0087  -0.0487 340 SER A CA  
2882 C C   . SER A 340 ? 0.4494 0.3805 0.3563 0.0034  0.0087  -0.0497 340 SER A C   
2883 O O   . SER A 340 ? 0.4557 0.3860 0.3636 0.0043  0.0091  -0.0512 340 SER A O   
2884 C CB  . SER A 340 ? 0.4834 0.4102 0.3897 0.0053  0.0082  -0.0480 340 SER A CB  
2885 O OG  . SER A 340 ? 0.5247 0.4533 0.4318 0.0067  0.0075  -0.0470 340 SER A OG  
2886 N N   . VAL A 341 ? 0.3857 0.3197 0.2926 0.0027  0.0084  -0.0488 341 VAL A N   
2887 C CA  . VAL A 341 ? 0.3382 0.2746 0.2462 0.0033  0.0083  -0.0495 341 VAL A CA  
2888 C C   . VAL A 341 ? 0.4010 0.3400 0.3085 0.0010  0.0085  -0.0496 341 VAL A C   
2889 O O   . VAL A 341 ? 0.3977 0.3370 0.3039 -0.0006 0.0085  -0.0486 341 VAL A O   
2890 C CB  . VAL A 341 ? 0.3914 0.3290 0.3003 0.0052  0.0074  -0.0482 341 VAL A CB  
2891 C CG1 . VAL A 341 ? 0.3964 0.3315 0.3059 0.0074  0.0071  -0.0481 341 VAL A CG1 
2892 C CG2 . VAL A 341 ? 0.3926 0.3317 0.3006 0.0044  0.0068  -0.0462 341 VAL A CG2 
2893 N N   . ASP A 342 ? 0.4424 0.3832 0.3507 0.0010  0.0088  -0.0508 342 ASP A N   
2894 C CA  . ASP A 342 ? 0.4922 0.4355 0.4001 -0.0010 0.0090  -0.0511 342 ASP A CA  
2895 C C   . ASP A 342 ? 0.4256 0.3719 0.3339 -0.0008 0.0084  -0.0499 342 ASP A C   
2896 O O   . ASP A 342 ? 0.5049 0.4535 0.4128 -0.0025 0.0085  -0.0500 342 ASP A O   
2897 C CB  . ASP A 342 ? 0.6406 0.5842 0.5491 -0.0015 0.0098  -0.0532 342 ASP A CB  
2898 C CG  . ASP A 342 ? 0.8626 0.8038 0.7703 -0.0027 0.0105  -0.0544 342 ASP A CG  
2899 O OD1 . ASP A 342 ? 0.9270 0.8680 0.8334 -0.0045 0.0107  -0.0538 342 ASP A OD1 
2900 O OD2 . ASP A 342 ? 0.9403 0.8798 0.8487 -0.0018 0.0110  -0.0558 342 ASP A OD2 
2901 N N   . PHE A 343 ? 0.2619 0.2083 0.1709 0.0011  0.0076  -0.0488 343 PHE A N   
2902 C CA  . PHE A 343 ? 0.2791 0.2281 0.1884 0.0015  0.0069  -0.0476 343 PHE A CA  
2903 C C   . PHE A 343 ? 0.2210 0.1697 0.1295 0.0017  0.0063  -0.0455 343 PHE A C   
2904 O O   . PHE A 343 ? 0.2995 0.2459 0.2071 0.0014  0.0064  -0.0451 343 PHE A O   
2905 C CB  . PHE A 343 ? 0.3024 0.2520 0.2134 0.0038  0.0066  -0.0481 343 PHE A CB  
2906 C CG  . PHE A 343 ? 0.3417 0.2886 0.2532 0.0059  0.0064  -0.0480 343 PHE A CG  
2907 C CD1 . PHE A 343 ? 0.3257 0.2703 0.2376 0.0064  0.0070  -0.0496 343 PHE A CD1 
2908 C CD2 . PHE A 343 ? 0.2624 0.2091 0.1740 0.0074  0.0055  -0.0464 343 PHE A CD2 
2909 C CE1 . PHE A 343 ? 0.3320 0.2741 0.2443 0.0083  0.0068  -0.0495 343 PHE A CE1 
2910 C CE2 . PHE A 343 ? 0.2780 0.2223 0.1902 0.0093  0.0053  -0.0463 343 PHE A CE2 
2911 C CZ  . PHE A 343 ? 0.3496 0.2915 0.2620 0.0098  0.0060  -0.0479 343 PHE A CZ  
2912 N N   . GLN A 344 ? 0.2248 0.1757 0.1335 0.0021  0.0056  -0.0442 344 GLN A N   
2913 C CA  . GLN A 344 ? 0.2126 0.1633 0.1206 0.0024  0.0049  -0.0422 344 GLN A CA  
2914 C C   . GLN A 344 ? 0.2216 0.1709 0.1305 0.0049  0.0043  -0.0416 344 GLN A C   
2915 O O   . GLN A 344 ? 0.2108 0.1617 0.1208 0.0063  0.0038  -0.0414 344 GLN A O   
2916 C CB  . GLN A 344 ? 0.2284 0.1821 0.1360 0.0014  0.0044  -0.0410 344 GLN A CB  
2917 C CG  . GLN A 344 ? 0.3059 0.2612 0.2127 -0.0011 0.0050  -0.0416 344 GLN A CG  
2918 C CD  . GLN A 344 ? 0.3045 0.2626 0.2108 -0.0021 0.0045  -0.0402 344 GLN A CD  
2919 O OE1 . GLN A 344 ? 0.3107 0.2690 0.2158 -0.0037 0.0045  -0.0393 344 GLN A OE1 
2920 N NE2 . GLN A 344 ? 0.2459 0.2063 0.1533 -0.0012 0.0041  -0.0400 344 GLN A NE2 
2921 N N   . PRO A 345 ? 0.2164 0.1628 0.1249 0.0057  0.0044  -0.0414 345 PRO A N   
2922 C CA  . PRO A 345 ? 0.2471 0.1922 0.1565 0.0082  0.0039  -0.0410 345 PRO A CA  
2923 C C   . PRO A 345 ? 0.2625 0.2087 0.1719 0.0090  0.0029  -0.0390 345 PRO A C   
2924 O O   . PRO A 345 ? 0.2449 0.1919 0.1532 0.0078  0.0027  -0.0376 345 PRO A O   
2925 C CB  . PRO A 345 ? 0.3032 0.2449 0.2120 0.0083  0.0042  -0.0413 345 PRO A CB  
2926 C CG  . PRO A 345 ? 0.2899 0.2317 0.1972 0.0059  0.0045  -0.0407 345 PRO A CG  
2927 C CD  . PRO A 345 ? 0.2319 0.1764 0.1391 0.0042  0.0048  -0.0413 345 PRO A CD  
2928 N N   . VAL A 346 ? 0.2699 0.2160 0.1804 0.0113  0.0024  -0.0387 346 VAL A N   
2929 C CA  . VAL A 346 ? 0.2049 0.1517 0.1154 0.0125  0.0015  -0.0368 346 VAL A CA  
2930 C C   . VAL A 346 ? 0.2827 0.2266 0.1932 0.0141  0.0013  -0.0364 346 VAL A C   
2931 O O   . VAL A 346 ? 0.2440 0.1864 0.1556 0.0156  0.0015  -0.0375 346 VAL A O   
2932 C CB  . VAL A 346 ? 0.2292 0.1784 0.1410 0.0138  0.0010  -0.0367 346 VAL A CB  
2933 C CG1 . VAL A 346 ? 0.2413 0.1913 0.1531 0.0150  0.0000  -0.0347 346 VAL A CG1 
2934 C CG2 . VAL A 346 ? 0.2727 0.2248 0.1846 0.0121  0.0012  -0.0374 346 VAL A CG2 
2935 N N   . VAL A 347 ? 0.1667 0.1098 0.0762 0.0138  0.0010  -0.0348 347 VAL A N   
2936 C CA  . VAL A 347 ? 0.1931 0.1334 0.1025 0.0151  0.0008  -0.0343 347 VAL A CA  
2937 C C   . VAL A 347 ? 0.2794 0.2203 0.1890 0.0167  -0.0001 -0.0325 347 VAL A C   
2938 O O   . VAL A 347 ? 0.2155 0.1575 0.1241 0.0157  -0.0005 -0.0310 347 VAL A O   
2939 C CB  . VAL A 347 ? 0.2147 0.1531 0.1225 0.0135  0.0013  -0.0341 347 VAL A CB  
2940 C CG1 . VAL A 347 ? 0.3121 0.2475 0.2199 0.0149  0.0012  -0.0336 347 VAL A CG1 
2941 C CG2 . VAL A 347 ? 0.2213 0.1594 0.1290 0.0118  0.0022  -0.0359 347 VAL A CG2 
2942 N N   . PHE A 348 ? 0.2250 0.1652 0.1357 0.0190  -0.0005 -0.0326 348 PHE A N   
2943 C CA  . PHE A 348 ? 0.1872 0.1278 0.0983 0.0207  -0.0014 -0.0310 348 PHE A CA  
2944 C C   . PHE A 348 ? 0.2901 0.2278 0.2006 0.0216  -0.0015 -0.0302 348 PHE A C   
2945 O O   . PHE A 348 ? 0.2424 0.1777 0.1532 0.0224  -0.0011 -0.0312 348 PHE A O   
2946 C CB  . PHE A 348 ? 0.1630 0.1044 0.0756 0.0228  -0.0017 -0.0315 348 PHE A CB  
2947 C CG  . PHE A 348 ? 0.2469 0.1917 0.1600 0.0225  -0.0022 -0.0310 348 PHE A CG  
2948 C CD1 . PHE A 348 ? 0.1802 0.1269 0.0932 0.0207  -0.0017 -0.0320 348 PHE A CD1 
2949 C CD2 . PHE A 348 ? 0.2457 0.1916 0.1592 0.0240  -0.0031 -0.0296 348 PHE A CD2 
2950 C CE1 . PHE A 348 ? 0.2007 0.1505 0.1142 0.0205  -0.0021 -0.0315 348 PHE A CE1 
2951 C CE2 . PHE A 348 ? 0.2110 0.1600 0.1250 0.0238  -0.0035 -0.0292 348 PHE A CE2 
2952 C CZ  . PHE A 348 ? 0.1718 0.1228 0.0858 0.0220  -0.0030 -0.0301 348 PHE A CZ  
2953 N N   . VAL A 349 ? 0.2096 0.1476 0.1192 0.0213  -0.0020 -0.0283 349 VAL A N   
2954 C CA  . VAL A 349 ? 0.1676 0.1031 0.0765 0.0221  -0.0022 -0.0273 349 VAL A CA  
2955 C C   . VAL A 349 ? 0.2054 0.1417 0.1150 0.0241  -0.0032 -0.0258 349 VAL A C   
2956 O O   . VAL A 349 ? 0.2304 0.1688 0.1396 0.0237  -0.0037 -0.0244 349 VAL A O   
2957 C CB  . VAL A 349 ? 0.1841 0.1192 0.0914 0.0201  -0.0021 -0.0263 349 VAL A CB  
2958 C CG1 . VAL A 349 ? 0.1966 0.1294 0.1034 0.0211  -0.0024 -0.0250 349 VAL A CG1 
2959 C CG2 . VAL A 349 ? 0.2493 0.1837 0.1560 0.0181  -0.0011 -0.0278 349 VAL A CG2 
2960 N N   . VAL A 350 ? 0.2073 0.1420 0.1179 0.0264  -0.0034 -0.0262 350 VAL A N   
2961 C CA  . VAL A 350 ? 0.2305 0.1661 0.1419 0.0285  -0.0043 -0.0251 350 VAL A CA  
2962 C C   . VAL A 350 ? 0.2316 0.1643 0.1430 0.0301  -0.0045 -0.0245 350 VAL A C   
2963 O O   . VAL A 350 ? 0.2240 0.1544 0.1357 0.0308  -0.0040 -0.0257 350 VAL A O   
2964 C CB  . VAL A 350 ? 0.2384 0.1754 0.1514 0.0298  -0.0043 -0.0262 350 VAL A CB  
2965 C CG1 . VAL A 350 ? 0.2018 0.1398 0.1155 0.0318  -0.0053 -0.0250 350 VAL A CG1 
2966 C CG2 . VAL A 350 ? 0.1620 0.1014 0.0750 0.0280  -0.0040 -0.0271 350 VAL A CG2 
2967 N N   . LEU A 351 ? 0.2153 0.1482 0.1262 0.0308  -0.0052 -0.0226 351 LEU A N   
2968 C CA  . LEU A 351 ? 0.2081 0.1385 0.1190 0.0325  -0.0055 -0.0219 351 LEU A CA  
2969 C C   . LEU A 351 ? 0.1675 0.0991 0.0783 0.0335  -0.0064 -0.0198 351 LEU A C   
2970 O O   . LEU A 351 ? 0.2026 0.1368 0.1132 0.0327  -0.0068 -0.0190 351 LEU A O   
2971 C CB  . LEU A 351 ? 0.1920 0.1198 0.1016 0.0313  -0.0049 -0.0219 351 LEU A CB  
2972 C CG  . LEU A 351 ? 0.1974 0.1260 0.1055 0.0291  -0.0049 -0.0207 351 LEU A CG  
2973 C CD1 . LEU A 351 ? 0.1964 0.1224 0.1035 0.0290  -0.0048 -0.0199 351 LEU A CD1 
2974 C CD2 . LEU A 351 ? 0.1762 0.1060 0.0839 0.0268  -0.0042 -0.0219 351 LEU A CD2 
2975 N N   . ASP A 352 ? 0.1934 0.1229 0.1043 0.0353  -0.0068 -0.0191 352 ASP A N   
2976 C CA  . ASP A 352 ? 0.1916 0.1219 0.1022 0.0362  -0.0077 -0.0171 352 ASP A CA  
2977 C C   . ASP A 352 ? 0.2423 0.1734 0.1515 0.0341  -0.0076 -0.0158 352 ASP A C   
2978 O O   . ASP A 352 ? 0.2572 0.1869 0.1654 0.0326  -0.0070 -0.0162 352 ASP A O   
2979 C CB  . ASP A 352 ? 0.1857 0.1133 0.0964 0.0381  -0.0079 -0.0164 352 ASP A CB  
2980 C CG  . ASP A 352 ? 0.3489 0.2758 0.2610 0.0404  -0.0081 -0.0174 352 ASP A CG  
2981 O OD1 . ASP A 352 ? 0.2379 0.1666 0.1511 0.0406  -0.0080 -0.0184 352 ASP A OD1 
2982 O OD2 . ASP A 352 ? 0.3010 0.2256 0.2133 0.0421  -0.0083 -0.0170 352 ASP A OD2 
2983 N N   . GLY A 353 ? 0.1788 0.1124 0.0879 0.0340  -0.0083 -0.0144 353 GLY A N   
2984 C CA  . GLY A 353 ? 0.2030 0.1378 0.1107 0.0319  -0.0083 -0.0133 353 GLY A CA  
2985 C C   . GLY A 353 ? 0.2396 0.1732 0.1463 0.0321  -0.0087 -0.0114 353 GLY A C   
2986 O O   . GLY A 353 ? 0.2285 0.1629 0.1341 0.0304  -0.0087 -0.0105 353 GLY A O   
2987 N N   . GLU A 354 ? 0.1917 0.1236 0.0989 0.0343  -0.0091 -0.0109 354 GLU A N   
2988 C CA  . GLU A 354 ? 0.1906 0.1217 0.0970 0.0348  -0.0097 -0.0090 354 GLU A CA  
2989 C C   . GLU A 354 ? 0.2470 0.1747 0.1532 0.0358  -0.0095 -0.0091 354 GLU A C   
2990 O O   . GLU A 354 ? 0.2359 0.1626 0.1412 0.0359  -0.0098 -0.0076 354 GLU A O   
2991 C CB  . GLU A 354 ? 0.1971 0.1299 0.1042 0.0365  -0.0106 -0.0077 354 GLU A CB  
2992 C CG  . GLU A 354 ? 0.2007 0.1323 0.1090 0.0392  -0.0110 -0.0080 354 GLU A CG  
2993 C CD  . GLU A 354 ? 0.2733 0.2059 0.1830 0.0399  -0.0108 -0.0097 354 GLU A CD  
2994 O OE1 . GLU A 354 ? 0.2249 0.1593 0.1356 0.0411  -0.0114 -0.0094 354 GLU A OE1 
2995 O OE2 . GLU A 354 ? 0.2136 0.1451 0.1235 0.0392  -0.0100 -0.0114 354 GLU A OE2 
2996 N N   . ASN A 355 ? 0.2164 0.1422 0.1233 0.0365  -0.0089 -0.0107 355 ASN A N   
2997 C CA  . ASN A 355 ? 0.2757 0.1984 0.1826 0.0379  -0.0089 -0.0107 355 ASN A CA  
2998 C C   . ASN A 355 ? 0.2392 0.1595 0.1449 0.0364  -0.0082 -0.0112 355 ASN A C   
2999 O O   . ASN A 355 ? 0.2810 0.1989 0.1864 0.0372  -0.0082 -0.0106 355 ASN A O   
3000 C CB  . ASN A 355 ? 0.2961 0.2180 0.2044 0.0399  -0.0088 -0.0121 355 ASN A CB  
3001 C CG  . ASN A 355 ? 0.2911 0.2146 0.2004 0.0419  -0.0097 -0.0113 355 ASN A CG  
3002 O OD1 . ASN A 355 ? 0.2303 0.1543 0.1393 0.0425  -0.0104 -0.0096 355 ASN A OD1 
3003 N ND2 . ASN A 355 ? 0.2719 0.1964 0.1825 0.0428  -0.0097 -0.0126 355 ASN A ND2 
3004 N N   . CYS A 356 ? 0.2303 0.1513 0.1356 0.0343  -0.0075 -0.0122 356 CYS A N   
3005 C CA  . CYS A 356 ? 0.2071 0.1257 0.1114 0.0329  -0.0068 -0.0128 356 CYS A CA  
3006 C C   . CYS A 356 ? 0.2103 0.1288 0.1131 0.0314  -0.0068 -0.0112 356 CYS A C   
3007 O O   . CYS A 356 ? 0.2830 0.1991 0.1851 0.0309  -0.0064 -0.0113 356 CYS A O   
3008 C CB  . CYS A 356 ? 0.2008 0.1199 0.1052 0.0313  -0.0060 -0.0147 356 CYS A CB  
3009 S SG  . CYS A 356 ? 0.2442 0.1670 0.1484 0.0292  -0.0059 -0.0146 356 CYS A SG  
3010 N N   . TRP A 357 ? 0.2214 0.1424 0.1238 0.0307  -0.0073 -0.0099 357 TRP A N   
3011 C CA  . TRP A 357 ? 0.2456 0.1668 0.1466 0.0288  -0.0073 -0.0087 357 TRP A CA  
3012 C C   . TRP A 357 ? 0.2719 0.1910 0.1722 0.0296  -0.0076 -0.0073 357 TRP A C   
3013 O O   . TRP A 357 ? 0.2938 0.2118 0.1929 0.0281  -0.0073 -0.0067 357 TRP A O   
3014 C CB  . TRP A 357 ? 0.2580 0.1825 0.1588 0.0280  -0.0078 -0.0076 357 TRP A CB  
3015 C CG  . TRP A 357 ? 0.2386 0.1653 0.1402 0.0274  -0.0076 -0.0089 357 TRP A CG  
3016 C CD1 . TRP A 357 ? 0.2287 0.1578 0.1314 0.0285  -0.0081 -0.0088 357 TRP A CD1 
3017 C CD2 . TRP A 357 ? 0.2324 0.1592 0.1339 0.0257  -0.0068 -0.0106 357 TRP A CD2 
3018 N NE1 . TRP A 357 ? 0.2211 0.1516 0.1242 0.0276  -0.0077 -0.0103 357 TRP A NE1 
3019 C CE2 . TRP A 357 ? 0.2344 0.1636 0.1369 0.0258  -0.0068 -0.0114 357 TRP A CE2 
3020 C CE3 . TRP A 357 ? 0.2320 0.1571 0.1327 0.0241  -0.0060 -0.0115 357 TRP A CE3 
3021 C CZ2 . TRP A 357 ? 0.2749 0.2048 0.1775 0.0244  -0.0062 -0.0131 357 TRP A CZ2 
3022 C CZ3 . TRP A 357 ? 0.1881 0.1138 0.0889 0.0227  -0.0053 -0.0131 357 TRP A CZ3 
3023 C CH2 . TRP A 357 ? 0.2500 0.1782 0.1518 0.0228  -0.0054 -0.0139 357 TRP A CH2 
3024 N N   . GLU A 358 ? 0.2719 0.1903 0.1730 0.0320  -0.0082 -0.0066 358 GLU A N   
3025 C CA  . GLU A 358 ? 0.3022 0.2186 0.2027 0.0329  -0.0085 -0.0052 358 GLU A CA  
3026 C C   . GLU A 358 ? 0.2278 0.1409 0.1277 0.0325  -0.0078 -0.0060 358 GLU A C   
3027 O O   . GLU A 358 ? 0.2825 0.1939 0.1816 0.0327  -0.0080 -0.0048 358 GLU A O   
3028 C CB  . GLU A 358 ? 0.3375 0.2537 0.2390 0.0355  -0.0092 -0.0045 358 GLU A CB  
3029 C CG  . GLU A 358 ? 0.2441 0.1589 0.1467 0.0372  -0.0090 -0.0062 358 GLU A CG  
3030 C CD  . GLU A 358 ? 0.3072 0.2232 0.2111 0.0395  -0.0098 -0.0057 358 GLU A CD  
3031 O OE1 . GLU A 358 ? 0.3366 0.2507 0.2410 0.0415  -0.0100 -0.0056 358 GLU A OE1 
3032 O OE2 . GLU A 358 ? 0.3389 0.2577 0.2432 0.0393  -0.0101 -0.0055 358 GLU A OE2 
3033 N N   . TYR A 359 ? 0.2291 0.1414 0.1294 0.0320  -0.0071 -0.0079 359 TYR A N   
3034 C CA  . TYR A 359 ? 0.2822 0.1914 0.1820 0.0315  -0.0064 -0.0088 359 TYR A CA  
3035 C C   . TYR A 359 ? 0.3085 0.2178 0.2071 0.0288  -0.0058 -0.0091 359 TYR A C   
3036 O O   . TYR A 359 ? 0.3449 0.2518 0.2430 0.0282  -0.0052 -0.0098 359 TYR A O   
3037 C CB  . TYR A 359 ? 0.3016 0.2096 0.2025 0.0326  -0.0060 -0.0107 359 TYR A CB  
3038 C CG  . TYR A 359 ? 0.2986 0.2060 0.2006 0.0354  -0.0066 -0.0105 359 TYR A CG  
3039 C CD1 . TYR A 359 ? 0.3301 0.2349 0.2320 0.0369  -0.0068 -0.0099 359 TYR A CD1 
3040 C CD2 . TYR A 359 ? 0.2866 0.1962 0.1899 0.0365  -0.0070 -0.0109 359 TYR A CD2 
3041 C CE1 . TYR A 359 ? 0.3882 0.2925 0.2912 0.0394  -0.0073 -0.0097 359 TYR A CE1 
3042 C CE2 . TYR A 359 ? 0.3412 0.2503 0.2455 0.0390  -0.0075 -0.0107 359 TYR A CE2 
3043 C CZ  . TYR A 359 ? 0.3276 0.2340 0.2318 0.0404  -0.0077 -0.0101 359 TYR A CZ  
3044 O OH  . TYR A 359 ? 0.3579 0.2638 0.2631 0.0429  -0.0082 -0.0100 359 TYR A OH  
3045 N N   . TYR A 360 ? 0.2856 0.1976 0.1839 0.0272  -0.0059 -0.0088 360 TYR A N   
3046 C CA  . TYR A 360 ? 0.2812 0.1936 0.1784 0.0246  -0.0053 -0.0091 360 TYR A CA  
3047 C C   . TYR A 360 ? 0.2846 0.1968 0.1805 0.0238  -0.0056 -0.0072 360 TYR A C   
3048 O O   . TYR A 360 ? 0.3475 0.2608 0.2435 0.0247  -0.0063 -0.0056 360 TYR A O   
3049 C CB  . TYR A 360 ? 0.2930 0.2085 0.1903 0.0233  -0.0053 -0.0095 360 TYR A CB  
3050 C CG  . TYR A 360 ? 0.2843 0.2004 0.1826 0.0232  -0.0047 -0.0116 360 TYR A CG  
3051 C CD1 . TYR A 360 ? 0.2713 0.1874 0.1709 0.0252  -0.0050 -0.0124 360 TYR A CD1 
3052 C CD2 . TYR A 360 ? 0.2468 0.1634 0.1445 0.0210  -0.0040 -0.0126 360 TYR A CD2 
3053 C CE1 . TYR A 360 ? 0.2303 0.1469 0.1307 0.0250  -0.0045 -0.0142 360 TYR A CE1 
3054 C CE2 . TYR A 360 ? 0.2557 0.1729 0.1542 0.0208  -0.0036 -0.0145 360 TYR A CE2 
3055 C CZ  . TYR A 360 ? 0.2277 0.1450 0.1276 0.0228  -0.0038 -0.0153 360 TYR A CZ  
3056 O OH  . TYR A 360 ? 0.2281 0.1460 0.1288 0.0225  -0.0033 -0.0171 360 TYR A OH  
3057 N N   . GLU A 361 ? 0.2422 0.2675 0.1984 -0.0141 -0.0173 -0.0277 361 GLU A N   
3058 C CA  . GLU A 361 ? 0.2661 0.2930 0.2223 -0.0148 -0.0179 -0.0284 361 GLU A CA  
3059 C C   . GLU A 361 ? 0.2604 0.2893 0.2175 -0.0142 -0.0188 -0.0279 361 GLU A C   
3060 O O   . GLU A 361 ? 0.2684 0.2977 0.2253 -0.0136 -0.0189 -0.0275 361 GLU A O   
3061 C CB  . GLU A 361 ? 0.3780 0.4051 0.3327 -0.0157 -0.0177 -0.0293 361 GLU A CB  
3062 C CG  . GLU A 361 ? 0.5662 0.5914 0.5200 -0.0163 -0.0168 -0.0297 361 GLU A CG  
3063 C CD  . GLU A 361 ? 0.7224 0.7472 0.6767 -0.0168 -0.0168 -0.0301 361 GLU A CD  
3064 O OE1 . GLU A 361 ? 0.8437 0.8700 0.7987 -0.0171 -0.0174 -0.0304 361 GLU A OE1 
3065 O OE2 . GLU A 361 ? 0.6985 0.7216 0.6526 -0.0170 -0.0161 -0.0302 361 GLU A OE2 
3066 N N   . GLU A 362 ? 0.2291 0.2593 0.1871 -0.0143 -0.0194 -0.0281 362 GLU A N   
3067 C CA  . GLU A 362 ? 0.3338 0.3659 0.2928 -0.0138 -0.0203 -0.0277 362 GLU A CA  
3068 C C   . GLU A 362 ? 0.3580 0.3899 0.3178 -0.0127 -0.0204 -0.0267 362 GLU A C   
3069 O O   . GLU A 362 ? 0.2430 0.2761 0.2028 -0.0122 -0.0209 -0.0264 362 GLU A O   
3070 C CB  . GLU A 362 ? 0.4298 0.4636 0.3878 -0.0143 -0.0207 -0.0283 362 GLU A CB  
3071 C CG  . GLU A 362 ? 0.6184 0.6542 0.5773 -0.0137 -0.0216 -0.0280 362 GLU A CG  
3072 C CD  . GLU A 362 ? 0.7306 0.7681 0.6887 -0.0143 -0.0221 -0.0286 362 GLU A CD  
3073 O OE1 . GLU A 362 ? 0.7361 0.7739 0.6937 -0.0152 -0.0221 -0.0294 362 GLU A OE1 
3074 O OE2 . GLU A 362 ? 0.7425 0.7810 0.7004 -0.0139 -0.0225 -0.0283 362 GLU A OE2 
3075 N N   . ASN A 363 ? 0.2680 0.2984 0.2284 -0.0122 -0.0199 -0.0261 363 ASN A N   
3076 C CA  . ASN A 363 ? 0.2540 0.2842 0.2155 -0.0112 -0.0201 -0.0251 363 ASN A CA  
3077 C C   . ASN A 363 ? 0.1863 0.2166 0.1470 -0.0107 -0.0200 -0.0247 363 ASN A C   
3078 O O   . ASN A 363 ? 0.2090 0.2400 0.1705 -0.0099 -0.0204 -0.0240 363 ASN A O   
3079 C CB  . ASN A 363 ? 0.3070 0.3388 0.2698 -0.0107 -0.0210 -0.0248 363 ASN A CB  
3080 C CG  . ASN A 363 ? 0.1895 0.2210 0.1536 -0.0097 -0.0212 -0.0237 363 ASN A CG  
3081 O OD1 . ASN A 363 ? 0.1843 0.2142 0.1487 -0.0093 -0.0206 -0.0233 363 ASN A OD1 
3082 N ND2 . ASN A 363 ? 0.2276 0.2607 0.1925 -0.0091 -0.0219 -0.0233 363 ASN A ND2 
3083 N N   . GLY A 364 ? 0.2023 0.2318 0.1615 -0.0112 -0.0194 -0.0252 364 GLY A N   
3084 C CA  . GLY A 364 ? 0.2011 0.2306 0.1595 -0.0108 -0.0192 -0.0249 364 GLY A CA  
3085 C C   . GLY A 364 ? 0.2214 0.2528 0.1795 -0.0108 -0.0199 -0.0251 364 GLY A C   
3086 O O   . GLY A 364 ? 0.1883 0.2197 0.1458 -0.0104 -0.0198 -0.0248 364 GLY A O   
3087 N N   . ILE A 365 ? 0.2328 0.2657 0.1912 -0.0112 -0.0205 -0.0255 365 ILE A N   
3088 C CA  . ILE A 365 ? 0.2256 0.2605 0.1839 -0.0111 -0.0212 -0.0256 365 ILE A CA  
3089 C C   . ILE A 365 ? 0.2372 0.2722 0.1937 -0.0117 -0.0210 -0.0263 365 ILE A C   
3090 O O   . ILE A 365 ? 0.2807 0.3164 0.2368 -0.0113 -0.0211 -0.0261 365 ILE A O   
3091 C CB  . ILE A 365 ? 0.2754 0.3120 0.2346 -0.0113 -0.0220 -0.0259 365 ILE A CB  
3092 C CG1 . ILE A 365 ? 0.2653 0.3020 0.2262 -0.0105 -0.0224 -0.0250 365 ILE A CG1 
3093 C CG2 . ILE A 365 ? 0.1957 0.2343 0.1545 -0.0114 -0.0227 -0.0261 365 ILE A CG2 
3094 C CD1 . ILE A 365 ? 0.2710 0.3088 0.2329 -0.0107 -0.0230 -0.0253 365 ILE A CD1 
3095 N N   . PRO A 366 ? 0.2197 0.2540 0.1753 -0.0126 -0.0205 -0.0271 366 PRO A N   
3096 C CA  . PRO A 366 ? 0.3334 0.3676 0.2873 -0.0132 -0.0202 -0.0278 366 PRO A CA  
3097 C C   . PRO A 366 ? 0.2681 0.3011 0.2213 -0.0126 -0.0197 -0.0272 366 PRO A C   
3098 O O   . PRO A 366 ? 0.2467 0.2803 0.1990 -0.0125 -0.0198 -0.0273 366 PRO A O   
3099 C CB  . PRO A 366 ? 0.2901 0.3233 0.2434 -0.0142 -0.0198 -0.0286 366 PRO A CB  
3100 C CG  . PRO A 366 ? 0.2439 0.2778 0.1984 -0.0143 -0.0202 -0.0287 366 PRO A CG  
3101 C CD  . PRO A 366 ? 0.1970 0.2310 0.1530 -0.0133 -0.0205 -0.0277 366 PRO A CD  
3102 N N   . PHE A 367 ? 0.2304 0.2616 0.1840 -0.0122 -0.0191 -0.0267 367 PHE A N   
3103 C CA  . PHE A 367 ? 0.2519 0.2819 0.2049 -0.0117 -0.0185 -0.0262 367 PHE A CA  
3104 C C   . PHE A 367 ? 0.2256 0.2568 0.1791 -0.0108 -0.0190 -0.0254 367 PHE A C   
3105 O O   . PHE A 367 ? 0.2063 0.2376 0.1587 -0.0106 -0.0189 -0.0254 367 PHE A O   
3106 C CB  . PHE A 367 ? 0.2488 0.2768 0.2023 -0.0114 -0.0179 -0.0257 367 PHE A CB  
3107 C CG  . PHE A 367 ? 0.2205 0.2474 0.1737 -0.0107 -0.0173 -0.0251 367 PHE A CG  
3108 C CD1 . PHE A 367 ? 0.2853 0.3111 0.2369 -0.0111 -0.0167 -0.0254 367 PHE A CD1 
3109 C CD2 . PHE A 367 ? 0.1931 0.2198 0.1474 -0.0098 -0.0174 -0.0240 367 PHE A CD2 
3110 C CE1 . PHE A 367 ? 0.2206 0.2453 0.1717 -0.0105 -0.0161 -0.0248 367 PHE A CE1 
3111 C CE2 . PHE A 367 ? 0.2119 0.2374 0.1658 -0.0091 -0.0168 -0.0234 367 PHE A CE2 
3112 C CZ  . PHE A 367 ? 0.2411 0.2656 0.1934 -0.0095 -0.0162 -0.0238 367 PHE A CZ  
3113 N N   . LEU A 368 ? 0.1872 0.2190 0.1422 -0.0101 -0.0195 -0.0247 368 LEU A N   
3114 C CA  . LEU A 368 ? 0.2111 0.2438 0.1667 -0.0092 -0.0199 -0.0239 368 LEU A CA  
3115 C C   . LEU A 368 ? 0.1871 0.2217 0.1422 -0.0093 -0.0205 -0.0243 368 LEU A C   
3116 O O   . LEU A 368 ? 0.2414 0.2764 0.1960 -0.0088 -0.0205 -0.0239 368 LEU A O   
3117 C CB  . LEU A 368 ? 0.1525 0.1855 0.1099 -0.0085 -0.0203 -0.0232 368 LEU A CB  
3118 C CG  . LEU A 368 ? 0.1482 0.1794 0.1064 -0.0080 -0.0197 -0.0225 368 LEU A CG  
3119 C CD1 . LEU A 368 ? 0.1606 0.1922 0.1205 -0.0074 -0.0203 -0.0218 368 LEU A CD1 
3120 C CD2 . LEU A 368 ? 0.2068 0.2369 0.1644 -0.0075 -0.0191 -0.0220 368 LEU A CD2 
3121 N N   . GLU A 369 ? 0.2161 0.2520 0.1711 -0.0100 -0.0210 -0.0250 369 GLU A N   
3122 C CA  . GLU A 369 ? 0.1416 0.1793 0.0960 -0.0102 -0.0215 -0.0254 369 GLU A CA  
3123 C C   . GLU A 369 ? 0.2385 0.2757 0.1912 -0.0105 -0.0210 -0.0259 369 GLU A C   
3124 O O   . GLU A 369 ? 0.2601 0.2981 0.2122 -0.0102 -0.0213 -0.0257 369 GLU A O   
3125 C CB  . GLU A 369 ? 0.2247 0.2637 0.1794 -0.0109 -0.0221 -0.0261 369 GLU A CB  
3126 C CG  . GLU A 369 ? 0.1925 0.2327 0.1490 -0.0104 -0.0228 -0.0256 369 GLU A CG  
3127 C CD  . GLU A 369 ? 0.2698 0.3114 0.2266 -0.0111 -0.0234 -0.0263 369 GLU A CD  
3128 O OE1 . GLU A 369 ? 0.3028 0.3445 0.2585 -0.0119 -0.0233 -0.0272 369 GLU A OE1 
3129 O OE2 . GLU A 369 ? 0.2722 0.3148 0.2302 -0.0107 -0.0240 -0.0259 369 GLU A OE2 
3130 N N   . LYS A 370 ? 0.2168 0.2524 0.1685 -0.0112 -0.0204 -0.0264 370 LYS A N   
3131 C CA  . LYS A 370 ? 0.1916 0.2266 0.1417 -0.0115 -0.0199 -0.0269 370 LYS A CA  
3132 C C   . LYS A 370 ? 0.2712 0.3052 0.2210 -0.0107 -0.0194 -0.0261 370 LYS A C   
3133 O O   . LYS A 370 ? 0.2706 0.3050 0.2194 -0.0105 -0.0194 -0.0261 370 LYS A O   
3134 C CB  . LYS A 370 ? 0.2736 0.3072 0.2229 -0.0124 -0.0193 -0.0276 370 LYS A CB  
3135 C CG  . LYS A 370 ? 0.4940 0.5286 0.4429 -0.0134 -0.0197 -0.0286 370 LYS A CG  
3136 C CD  . LYS A 370 ? 0.6063 0.6398 0.5538 -0.0143 -0.0191 -0.0295 370 LYS A CD  
3137 C CE  . LYS A 370 ? 0.6676 0.7014 0.6152 -0.0153 -0.0192 -0.0303 370 LYS A CE  
3138 N NZ  . LYS A 370 ? 0.7146 0.7504 0.6621 -0.0157 -0.0200 -0.0309 370 LYS A NZ  
3139 N N   . LEU A 371 ? 0.2583 0.2910 0.2090 -0.0101 -0.0191 -0.0253 371 LEU A N   
3140 C CA  . LEU A 371 ? 0.2258 0.2576 0.1764 -0.0093 -0.0186 -0.0245 371 LEU A CA  
3141 C C   . LEU A 371 ? 0.2577 0.2910 0.2088 -0.0085 -0.0192 -0.0239 371 LEU A C   
3142 O O   . LEU A 371 ? 0.2749 0.3083 0.2251 -0.0082 -0.0190 -0.0237 371 LEU A O   
3143 C CB  . LEU A 371 ? 0.2293 0.2597 0.1812 -0.0088 -0.0183 -0.0238 371 LEU A CB  
3144 C CG  . LEU A 371 ? 0.1785 0.2080 0.1306 -0.0078 -0.0179 -0.0228 371 LEU A CG  
3145 C CD1 . LEU A 371 ? 0.1896 0.2177 0.1400 -0.0080 -0.0171 -0.0230 371 LEU A CD1 
3146 C CD2 . LEU A 371 ? 0.1858 0.2141 0.1393 -0.0073 -0.0177 -0.0220 371 LEU A CD2 
3147 N N   . TYR A 372 ? 0.2177 0.2523 0.1702 -0.0082 -0.0199 -0.0235 372 TYR A N   
3148 C CA  . TYR A 372 ? 0.1661 0.2022 0.1192 -0.0074 -0.0205 -0.0229 372 TYR A CA  
3149 C C   . TYR A 372 ? 0.2400 0.2775 0.1919 -0.0077 -0.0208 -0.0235 372 TYR A C   
3150 O O   . TYR A 372 ? 0.1471 0.1850 0.0986 -0.0071 -0.0209 -0.0230 372 TYR A O   
3151 C CB  . TYR A 372 ? 0.2290 0.2662 0.1838 -0.0071 -0.0212 -0.0225 372 TYR A CB  
3152 C CG  . TYR A 372 ? 0.2538 0.2898 0.2099 -0.0065 -0.0210 -0.0217 372 TYR A CG  
3153 C CD1 . TYR A 372 ? 0.1318 0.1660 0.0877 -0.0061 -0.0202 -0.0212 372 TYR A CD1 
3154 C CD2 . TYR A 372 ? 0.2202 0.2568 0.1778 -0.0064 -0.0215 -0.0215 372 TYR A CD2 
3155 C CE1 . TYR A 372 ? 0.1370 0.1700 0.0941 -0.0056 -0.0200 -0.0205 372 TYR A CE1 
3156 C CE2 . TYR A 372 ? 0.1916 0.2272 0.1505 -0.0058 -0.0213 -0.0208 372 TYR A CE2 
3157 C CZ  . TYR A 372 ? 0.2384 0.2722 0.1970 -0.0054 -0.0206 -0.0203 372 TYR A CZ  
3158 O OH  . TYR A 372 ? 0.1408 0.1735 0.1007 -0.0049 -0.0204 -0.0196 372 TYR A OH  
3159 N N   . SER A 373 ? 0.2414 0.2797 0.1928 -0.0086 -0.0211 -0.0244 373 SER A N   
3160 C CA  . SER A 373 ? 0.2641 0.3038 0.2143 -0.0089 -0.0214 -0.0250 373 SER A CA  
3161 C C   . SER A 373 ? 0.2933 0.3319 0.2419 -0.0090 -0.0208 -0.0252 373 SER A C   
3162 O O   . SER A 373 ? 0.2556 0.2950 0.2034 -0.0088 -0.0210 -0.0252 373 SER A O   
3163 C CB  . SER A 373 ? 0.3263 0.3670 0.2763 -0.0099 -0.0219 -0.0260 373 SER A CB  
3164 O OG  . SER A 373 ? 0.3697 0.4090 0.3190 -0.0107 -0.0213 -0.0267 373 SER A OG  
3165 N N   . THR A 374 ? 0.1929 0.2296 0.1409 -0.0093 -0.0200 -0.0254 374 THR A N   
3166 C CA  . THR A 374 ? 0.2170 0.2525 0.1635 -0.0094 -0.0193 -0.0255 374 THR A CA  
3167 C C   . THR A 374 ? 0.3002 0.3352 0.2468 -0.0083 -0.0191 -0.0245 374 THR A C   
3168 O O   . THR A 374 ? 0.3184 0.3535 0.2638 -0.0082 -0.0189 -0.0246 374 THR A O   
3169 C CB  . THR A 374 ? 0.2309 0.2645 0.1768 -0.0100 -0.0186 -0.0260 374 THR A CB  
3170 O OG1 . THR A 374 ? 0.2359 0.2700 0.1815 -0.0110 -0.0188 -0.0269 374 THR A OG1 
3171 C CG2 . THR A 374 ? 0.3180 0.3504 0.2623 -0.0101 -0.0179 -0.0262 374 THR A CG2 
3172 N N   . LEU A 375 ? 0.2697 0.3042 0.2177 -0.0076 -0.0190 -0.0237 375 LEU A N   
3173 C CA  . LEU A 375 ? 0.2675 0.3017 0.2158 -0.0066 -0.0189 -0.0226 375 LEU A CA  
3174 C C   . LEU A 375 ? 0.2619 0.2980 0.2102 -0.0062 -0.0195 -0.0224 375 LEU A C   
3175 O O   . LEU A 375 ? 0.3221 0.3581 0.2699 -0.0056 -0.0193 -0.0220 375 LEU A O   
3176 C CB  . LEU A 375 ? 0.2299 0.2634 0.1799 -0.0060 -0.0188 -0.0217 375 LEU A CB  
3177 C CG  . LEU A 375 ? 0.2741 0.3055 0.2241 -0.0062 -0.0181 -0.0217 375 LEU A CG  
3178 C CD1 . LEU A 375 ? 0.2201 0.2511 0.1719 -0.0056 -0.0182 -0.0209 375 LEU A CD1 
3179 C CD2 . LEU A 375 ? 0.2728 0.3027 0.2217 -0.0058 -0.0173 -0.0214 375 LEU A CD2 
3180 N N   . GLU A 376 ? 0.2996 0.3374 0.2486 -0.0064 -0.0203 -0.0227 376 GLU A N   
3181 C CA  . GLU A 376 ? 0.3310 0.3707 0.2801 -0.0060 -0.0210 -0.0226 376 GLU A CA  
3182 C C   . GLU A 376 ? 0.3602 0.4003 0.3077 -0.0063 -0.0209 -0.0231 376 GLU A C   
3183 O O   . GLU A 376 ? 0.3460 0.3870 0.2933 -0.0057 -0.0211 -0.0227 376 GLU A O   
3184 C CB  . GLU A 376 ? 0.3892 0.4306 0.3393 -0.0064 -0.0218 -0.0230 376 GLU A CB  
3185 C CG  . GLU A 376 ? 0.4555 0.4984 0.4069 -0.0057 -0.0225 -0.0223 376 GLU A CG  
3186 C CD  . GLU A 376 ? 0.4062 0.4500 0.3588 -0.0060 -0.0231 -0.0225 376 GLU A CD  
3187 O OE1 . GLU A 376 ? 0.5484 0.5922 0.5025 -0.0054 -0.0234 -0.0217 376 GLU A OE1 
3188 O OE2 . GLU A 376 ? 0.5025 0.5469 0.4546 -0.0069 -0.0234 -0.0234 376 GLU A OE2 
3189 N N   . LYS A 377 ? 0.2735 0.3129 0.2197 -0.0072 -0.0205 -0.0240 377 LYS A N   
3190 C CA  . LYS A 377 ? 0.2648 0.3046 0.2093 -0.0075 -0.0204 -0.0246 377 LYS A CA  
3191 C C   . LYS A 377 ? 0.3022 0.3405 0.2456 -0.0071 -0.0196 -0.0243 377 LYS A C   
3192 O O   . LYS A 377 ? 0.3661 0.4048 0.3082 -0.0071 -0.0196 -0.0246 377 LYS A O   
3193 C CB  . LYS A 377 ? 0.3249 0.3647 0.2685 -0.0087 -0.0204 -0.0258 377 LYS A CB  
3194 C CG  . LYS A 377 ? 0.3117 0.3529 0.2563 -0.0091 -0.0212 -0.0262 377 LYS A CG  
3195 C CD  . LYS A 377 ? 0.4601 0.5016 0.4038 -0.0102 -0.0212 -0.0274 377 LYS A CD  
3196 C CE  . LYS A 377 ? 0.6131 0.6556 0.5580 -0.0107 -0.0218 -0.0277 377 LYS A CE  
3197 N NZ  . LYS A 377 ? 0.7017 0.7459 0.6478 -0.0101 -0.0226 -0.0271 377 LYS A NZ  
3198 N N   . GLU A 378 ? 0.2530 0.2895 0.1968 -0.0067 -0.0190 -0.0237 378 GLU A N   
3199 C CA  . GLU A 378 ? 0.2734 0.3085 0.2161 -0.0064 -0.0182 -0.0234 378 GLU A CA  
3200 C C   . GLU A 378 ? 0.3409 0.3767 0.2840 -0.0053 -0.0184 -0.0225 378 GLU A C   
3201 O O   . GLU A 378 ? 0.3500 0.3860 0.2945 -0.0046 -0.0186 -0.0216 378 GLU A O   
3202 C CB  . GLU A 378 ? 0.3011 0.3342 0.2441 -0.0063 -0.0175 -0.0231 378 GLU A CB  
3203 C CG  . GLU A 378 ? 0.2958 0.3281 0.2387 -0.0073 -0.0173 -0.0239 378 GLU A CG  
3204 C CD  . GLU A 378 ? 0.4248 0.4568 0.3659 -0.0082 -0.0171 -0.0250 378 GLU A CD  
3205 O OE1 . GLU A 378 ? 0.4373 0.4691 0.3771 -0.0080 -0.0168 -0.0250 378 GLU A OE1 
3206 O OE2 . GLU A 378 ? 0.5475 0.5794 0.4885 -0.0090 -0.0172 -0.0258 378 GLU A OE2 
3207 N N   . GLU A 379 ? 0.3071 0.3434 0.2488 -0.0052 -0.0184 -0.0227 379 GLU A N   
3208 C CA  . GLU A 379 ? 0.2227 0.2597 0.1646 -0.0042 -0.0185 -0.0219 379 GLU A CA  
3209 C C   . GLU A 379 ? 0.2667 0.3021 0.2090 -0.0035 -0.0178 -0.0209 379 GLU A C   
3210 O O   . GLU A 379 ? 0.2835 0.3193 0.2266 -0.0025 -0.0180 -0.0200 379 GLU A O   
3211 C CB  . GLU A 379 ? 0.2633 0.3010 0.2035 -0.0043 -0.0185 -0.0224 379 GLU A CB  
3212 C CG  . GLU A 379 ? 0.3342 0.3739 0.2743 -0.0048 -0.0193 -0.0231 379 GLU A CG  
3213 C CD  . GLU A 379 ? 0.4391 0.4793 0.3774 -0.0048 -0.0193 -0.0235 379 GLU A CD  
3214 O OE1 . GLU A 379 ? 0.5129 0.5520 0.4503 -0.0045 -0.0187 -0.0233 379 GLU A OE1 
3215 O OE2 . GLU A 379 ? 0.4067 0.4485 0.3447 -0.0052 -0.0200 -0.0241 379 GLU A OE2 
3216 N N   . TRP A 380 ? 0.2408 0.2743 0.1825 -0.0038 -0.0171 -0.0211 380 TRP A N   
3217 C CA  . TRP A 380 ? 0.2108 0.2427 0.1525 -0.0031 -0.0164 -0.0203 380 TRP A CA  
3218 C C   . TRP A 380 ? 0.2400 0.2711 0.1834 -0.0028 -0.0163 -0.0196 380 TRP A C   
3219 O O   . TRP A 380 ? 0.2749 0.3045 0.2185 -0.0022 -0.0157 -0.0189 380 TRP A O   
3220 C CB  . TRP A 380 ? 0.1944 0.2247 0.1345 -0.0035 -0.0155 -0.0208 380 TRP A CB  
3221 C CG  . TRP A 380 ? 0.2489 0.2785 0.1886 -0.0046 -0.0154 -0.0218 380 TRP A CG  
3222 C CD1 . TRP A 380 ? 0.2961 0.3266 0.2350 -0.0055 -0.0158 -0.0228 380 TRP A CD1 
3223 C CD2 . TRP A 380 ? 0.2772 0.3052 0.2174 -0.0049 -0.0149 -0.0217 380 TRP A CD2 
3224 N NE1 . TRP A 380 ? 0.3174 0.3469 0.2563 -0.0063 -0.0156 -0.0235 380 TRP A NE1 
3225 C CE2 . TRP A 380 ? 0.3161 0.3440 0.2557 -0.0059 -0.0150 -0.0228 380 TRP A CE2 
3226 C CE3 . TRP A 380 ? 0.3208 0.3474 0.2619 -0.0043 -0.0144 -0.0209 380 TRP A CE3 
3227 C CZ2 . TRP A 380 ? 0.3689 0.3955 0.3089 -0.0064 -0.0146 -0.0230 380 TRP A CZ2 
3228 C CZ3 . TRP A 380 ? 0.2970 0.3221 0.2383 -0.0048 -0.0140 -0.0211 380 TRP A CZ3 
3229 C CH2 . TRP A 380 ? 0.3638 0.3890 0.3046 -0.0059 -0.0141 -0.0222 380 TRP A CH2 
3230 N N   . ILE A 381 ? 0.2048 0.2367 0.1493 -0.0031 -0.0168 -0.0198 381 ILE A N   
3231 C CA  . ILE A 381 ? 0.2495 0.2810 0.1958 -0.0028 -0.0169 -0.0192 381 ILE A CA  
3232 C C   . ILE A 381 ? 0.2891 0.3222 0.2368 -0.0022 -0.0177 -0.0186 381 ILE A C   
3233 O O   . ILE A 381 ? 0.3054 0.3402 0.2530 -0.0025 -0.0184 -0.0191 381 ILE A O   
3234 C CB  . ILE A 381 ? 0.2117 0.2426 0.1582 -0.0037 -0.0169 -0.0199 381 ILE A CB  
3235 C CG1 . ILE A 381 ? 0.2263 0.2555 0.1715 -0.0043 -0.0161 -0.0205 381 ILE A CG1 
3236 C CG2 . ILE A 381 ? 0.2493 0.2798 0.1977 -0.0033 -0.0170 -0.0192 381 ILE A CG2 
3237 C CD1 . ILE A 381 ? 0.2831 0.3117 0.2285 -0.0052 -0.0160 -0.0212 381 ILE A CD1 
3238 N N   . GLU A 382 ? 0.1956 0.2283 0.1446 -0.0013 -0.0176 -0.0175 382 GLU A N   
3239 C CA  . GLU A 382 ? 0.1381 0.1723 0.0887 -0.0007 -0.0184 -0.0169 382 GLU A CA  
3240 C C   . GLU A 382 ? 0.1370 0.1703 0.0892 -0.0005 -0.0183 -0.0163 382 GLU A C   
3241 O O   . GLU A 382 ? 0.1678 0.1996 0.1203 0.0000  -0.0177 -0.0157 382 GLU A O   
3242 C CB  . GLU A 382 ? 0.1796 0.2143 0.1303 0.0002  -0.0184 -0.0160 382 GLU A CB  
3243 C CG  . GLU A 382 ? 0.3007 0.3368 0.2530 0.0009  -0.0191 -0.0153 382 GLU A CG  
3244 C CD  . GLU A 382 ? 0.4268 0.4637 0.3790 0.0018  -0.0192 -0.0145 382 GLU A CD  
3245 O OE1 . GLU A 382 ? 0.5150 0.5527 0.4686 0.0025  -0.0197 -0.0138 382 GLU A OE1 
3246 O OE2 . GLU A 382 ? 0.4515 0.4880 0.4022 0.0018  -0.0188 -0.0147 382 GLU A OE2 
3247 N N   . THR A 383 ? 0.1838 0.2181 0.1371 -0.0008 -0.0190 -0.0166 383 THR A N   
3248 C CA  . THR A 383 ? 0.1678 0.2015 0.1227 -0.0005 -0.0190 -0.0160 383 THR A CA  
3249 C C   . THR A 383 ? 0.1860 0.2204 0.1422 0.0005  -0.0195 -0.0150 383 THR A C   
3250 O O   . THR A 383 ? 0.2593 0.2953 0.2156 0.0008  -0.0200 -0.0148 383 THR A O   
3251 C CB  . THR A 383 ? 0.1931 0.2274 0.1486 -0.0013 -0.0195 -0.0167 383 THR A CB  
3252 O OG1 . THR A 383 ? 0.1702 0.2066 0.1257 -0.0014 -0.0204 -0.0171 383 THR A OG1 
3253 C CG2 . THR A 383 ? 0.1945 0.2278 0.1486 -0.0023 -0.0190 -0.0177 383 THR A CG2 
3254 N N   . LEU A 384 ? 0.1512 0.1845 0.1087 0.0010  -0.0192 -0.0141 384 LEU A N   
3255 C CA  . LEU A 384 ? 0.1789 0.2126 0.1377 0.0021  -0.0195 -0.0130 384 LEU A CA  
3256 C C   . LEU A 384 ? 0.1675 0.2012 0.1282 0.0023  -0.0199 -0.0126 384 LEU A C   
3257 O O   . LEU A 384 ? 0.1839 0.2165 0.1448 0.0019  -0.0196 -0.0129 384 LEU A O   
3258 C CB  . LEU A 384 ? 0.1833 0.2156 0.1419 0.0027  -0.0188 -0.0123 384 LEU A CB  
3259 C CG  . LEU A 384 ? 0.1607 0.1928 0.1175 0.0027  -0.0183 -0.0125 384 LEU A CG  
3260 C CD1 . LEU A 384 ? 0.1336 0.1642 0.0905 0.0034  -0.0176 -0.0116 384 LEU A CD1 
3261 C CD2 . LEU A 384 ? 0.1333 0.1674 0.0898 0.0029  -0.0189 -0.0125 384 LEU A CD2 
3262 N N   . THR A 385 ? 0.1877 0.2226 0.1497 0.0030  -0.0205 -0.0119 385 THR A N   
3263 C CA  . THR A 385 ? 0.2268 0.2613 0.1905 0.0035  -0.0208 -0.0113 385 THR A CA  
3264 C C   . THR A 385 ? 0.1264 0.1591 0.0905 0.0041  -0.0201 -0.0104 385 THR A C   
3265 O O   . THR A 385 ? 0.1401 0.1722 0.1033 0.0044  -0.0196 -0.0101 385 THR A O   
3266 C CB  . THR A 385 ? 0.1707 0.2070 0.1358 0.0041  -0.0217 -0.0107 385 THR A CB  
3267 O OG1 . THR A 385 ? 0.1993 0.2357 0.1642 0.0049  -0.0216 -0.0099 385 THR A OG1 
3268 C CG2 . THR A 385 ? 0.2349 0.2730 0.1995 0.0035  -0.0224 -0.0115 385 THR A CG2 
3269 N N   . LEU A 386 ? 0.1251 0.1572 0.0907 0.0044  -0.0202 -0.0099 386 LEU A N   
3270 C CA  . LEU A 386 ? 0.1661 0.1965 0.1323 0.0051  -0.0196 -0.0090 386 LEU A CA  
3271 C C   . LEU A 386 ? 0.2162 0.2472 0.1828 0.0060  -0.0197 -0.0080 386 LEU A C   
3272 O O   . LEU A 386 ? 0.2447 0.2747 0.2110 0.0065  -0.0191 -0.0074 386 LEU A O   
3273 C CB  . LEU A 386 ? 0.1295 0.1592 0.0973 0.0053  -0.0198 -0.0086 386 LEU A CB  
3274 C CG  . LEU A 386 ? 0.1740 0.2030 0.1416 0.0045  -0.0197 -0.0094 386 LEU A CG  
3275 C CD1 . LEU A 386 ? 0.1516 0.1799 0.1209 0.0048  -0.0198 -0.0089 386 LEU A CD1 
3276 C CD2 . LEU A 386 ? 0.1542 0.1816 0.1202 0.0039  -0.0187 -0.0100 386 LEU A CD2 
3277 N N   . GLU A 387 ? 0.1904 0.2233 0.1578 0.0064  -0.0206 -0.0078 387 GLU A N   
3278 C CA  . GLU A 387 ? 0.2009 0.2345 0.1686 0.0072  -0.0207 -0.0070 387 GLU A CA  
3279 C C   . GLU A 387 ? 0.2045 0.2381 0.1705 0.0071  -0.0202 -0.0072 387 GLU A C   
3280 O O   . GLU A 387 ? 0.2316 0.2646 0.1975 0.0078  -0.0198 -0.0065 387 GLU A O   
3281 C CB  . GLU A 387 ? 0.3384 0.3740 0.3071 0.0075  -0.0217 -0.0068 387 GLU A CB  
3282 C CG  . GLU A 387 ? 0.4368 0.4734 0.4059 0.0084  -0.0219 -0.0060 387 GLU A CG  
3283 C CD  . GLU A 387 ? 0.6435 0.6821 0.6134 0.0086  -0.0229 -0.0059 387 GLU A CD  
3284 O OE1 . GLU A 387 ? 0.7013 0.7408 0.6713 0.0093  -0.0231 -0.0053 387 GLU A OE1 
3285 O OE2 . GLU A 387 ? 0.7129 0.7522 0.6832 0.0082  -0.0234 -0.0065 387 GLU A OE2 
3286 N N   . GLU A 388 ? 0.2223 0.2565 0.1869 0.0063  -0.0203 -0.0083 388 GLU A N   
3287 C CA  . GLU A 388 ? 0.2268 0.2611 0.1897 0.0062  -0.0198 -0.0085 388 GLU A CA  
3288 C C   . GLU A 388 ? 0.2273 0.2595 0.1893 0.0061  -0.0188 -0.0085 388 GLU A C   
3289 O O   . GLU A 388 ? 0.2420 0.2739 0.2032 0.0065  -0.0184 -0.0081 388 GLU A O   
3290 C CB  . GLU A 388 ? 0.1923 0.2276 0.1539 0.0053  -0.0201 -0.0097 388 GLU A CB  
3291 C CG  . GLU A 388 ? 0.2592 0.2967 0.2215 0.0054  -0.0211 -0.0098 388 GLU A CG  
3292 C CD  . GLU A 388 ? 0.2966 0.3351 0.2579 0.0044  -0.0214 -0.0110 388 GLU A CD  
3293 O OE1 . GLU A 388 ? 0.2320 0.2695 0.1926 0.0036  -0.0210 -0.0117 388 GLU A OE1 
3294 O OE2 . GLU A 388 ? 0.4002 0.4404 0.3614 0.0044  -0.0221 -0.0112 388 GLU A OE2 
3295 N N   . ALA A 389 ? 0.1951 0.2259 0.1571 0.0056  -0.0185 -0.0088 389 ALA A N   
3296 C CA  . ALA A 389 ? 0.1593 0.1881 0.1207 0.0056  -0.0175 -0.0087 389 ALA A CA  
3297 C C   . ALA A 389 ? 0.2158 0.2438 0.1782 0.0066  -0.0172 -0.0074 389 ALA A C   
3298 O O   . ALA A 389 ? 0.2384 0.2654 0.1999 0.0069  -0.0166 -0.0071 389 ALA A O   
3299 C CB  . ALA A 389 ? 0.1691 0.1967 0.1306 0.0049  -0.0173 -0.0092 389 ALA A CB  
3300 N N   . MET A 390 ? 0.1811 0.2096 0.1453 0.0072  -0.0178 -0.0068 390 MET A N   
3301 C CA  . MET A 390 ? 0.2956 0.3233 0.2609 0.0081  -0.0175 -0.0056 390 MET A CA  
3302 C C   . MET A 390 ? 0.2862 0.3147 0.2511 0.0088  -0.0175 -0.0050 390 MET A C   
3303 O O   . MET A 390 ? 0.2651 0.2925 0.2301 0.0094  -0.0169 -0.0042 390 MET A O   
3304 C CB  . MET A 390 ? 0.3222 0.3505 0.2896 0.0086  -0.0182 -0.0050 390 MET A CB  
3305 C CG  . MET A 390 ? 0.3675 0.3951 0.3361 0.0096  -0.0181 -0.0037 390 MET A CG  
3306 S SD  . MET A 390 ? 0.4261 0.4544 0.3971 0.0100  -0.0189 -0.0032 390 MET A SD  
3307 C CE  . MET A 390 ? 0.4259 0.4566 0.3972 0.0103  -0.0199 -0.0031 390 MET A CE  
3308 N N   . ARG A 391 ? 0.2289 0.2591 0.1933 0.0087  -0.0180 -0.0053 391 ARG A N   
3309 C CA  . ARG A 391 ? 0.3027 0.3338 0.2669 0.0094  -0.0181 -0.0047 391 ARG A CA  
3310 C C   . ARG A 391 ? 0.2984 0.3296 0.2606 0.0090  -0.0177 -0.0053 391 ARG A C   
3311 O O   . ARG A 391 ? 0.2839 0.3158 0.2457 0.0096  -0.0177 -0.0049 391 ARG A O   
3312 C CB  . ARG A 391 ? 0.4109 0.4439 0.3761 0.0097  -0.0191 -0.0045 391 ARG A CB  
3313 C CG  . ARG A 391 ? 0.6321 0.6666 0.5965 0.0089  -0.0196 -0.0056 391 ARG A CG  
3314 C CD  . ARG A 391 ? 0.7790 0.8155 0.7437 0.0093  -0.0203 -0.0054 391 ARG A CD  
3315 N NE  . ARG A 391 ? 0.8148 0.8525 0.7781 0.0086  -0.0206 -0.0064 391 ARG A NE  
3316 C CZ  . ARG A 391 ? 0.7794 0.8173 0.7411 0.0085  -0.0203 -0.0067 391 ARG A CZ  
3317 N NH1 . ARG A 391 ? 0.7364 0.7734 0.6976 0.0091  -0.0197 -0.0061 391 ARG A NH1 
3318 N NH2 . ARG A 391 ? 0.7227 0.7617 0.6832 0.0078  -0.0206 -0.0077 391 ARG A NH2 
3319 N N   . LYS A 392 ? 0.2119 0.2425 0.1727 0.0081  -0.0174 -0.0064 392 LYS A N   
3320 C CA  . LYS A 392 ? 0.2728 0.3037 0.2317 0.0077  -0.0171 -0.0070 392 LYS A CA  
3321 C C   . LYS A 392 ? 0.1850 0.2148 0.1432 0.0083  -0.0163 -0.0064 392 LYS A C   
3322 O O   . LYS A 392 ? 0.2843 0.3124 0.2427 0.0085  -0.0157 -0.0059 392 LYS A O   
3323 C CB  . LYS A 392 ? 0.3415 0.3717 0.2991 0.0066  -0.0168 -0.0082 392 LYS A CB  
3324 C CG  . LYS A 392 ? 0.4121 0.4428 0.3678 0.0062  -0.0166 -0.0090 392 LYS A CG  
3325 C CD  . LYS A 392 ? 0.5330 0.5646 0.4881 0.0052  -0.0171 -0.0102 392 LYS A CD  
3326 C CE  . LYS A 392 ? 0.5096 0.5434 0.4650 0.0053  -0.0180 -0.0103 392 LYS A CE  
3327 N NZ  . LYS A 392 ? 0.4866 0.5211 0.4409 0.0056  -0.0179 -0.0102 392 LYS A NZ  
3328 N N   . GLU A 393 ? 0.2738 0.3045 0.2311 0.0086  -0.0164 -0.0063 393 GLU A N   
3329 C CA  . GLU A 393 ? 0.3835 0.4134 0.3401 0.0093  -0.0157 -0.0056 393 GLU A CA  
3330 C C   . GLU A 393 ? 0.3296 0.3583 0.2843 0.0088  -0.0149 -0.0062 393 GLU A C   
3331 O O   . GLU A 393 ? 0.4332 0.4605 0.3876 0.0092  -0.0142 -0.0057 393 GLU A O   
3332 C CB  . GLU A 393 ? 0.3814 0.4129 0.3381 0.0100  -0.0162 -0.0051 393 GLU A CB  
3333 C CG  . GLU A 393 ? 0.5920 0.6237 0.5505 0.0110  -0.0164 -0.0038 393 GLU A CG  
3334 C CD  . GLU A 393 ? 0.7686 0.8024 0.7276 0.0115  -0.0171 -0.0035 393 GLU A CD  
3335 O OE1 . GLU A 393 ? 0.8049 0.8394 0.7656 0.0120  -0.0177 -0.0029 393 GLU A OE1 
3336 O OE2 . GLU A 393 ? 0.8182 0.8528 0.7758 0.0114  -0.0171 -0.0039 393 GLU A OE2 
3337 N N   . ASP A 394 ? 0.2603 0.2896 0.2137 0.0080  -0.0151 -0.0074 394 ASP A N   
3338 C CA  . ASP A 394 ? 0.2769 0.3051 0.2283 0.0075  -0.0144 -0.0080 394 ASP A CA  
3339 C C   . ASP A 394 ? 0.3015 0.3281 0.2527 0.0068  -0.0139 -0.0086 394 ASP A C   
3340 O O   . ASP A 394 ? 0.3338 0.3602 0.2837 0.0059  -0.0138 -0.0096 394 ASP A O   
3341 C CB  . ASP A 394 ? 0.3519 0.3815 0.3019 0.0070  -0.0148 -0.0089 394 ASP A CB  
3342 C CG  . ASP A 394 ? 0.5686 0.5996 0.5193 0.0063  -0.0156 -0.0096 394 ASP A CG  
3343 O OD1 . ASP A 394 ? 0.5626 0.5937 0.5149 0.0065  -0.0159 -0.0092 394 ASP A OD1 
3344 O OD2 . ASP A 394 ? 0.6020 0.6339 0.5515 0.0057  -0.0159 -0.0106 394 ASP A OD2 
3345 N N   . VAL A 395 ? 0.1895 0.2148 0.1418 0.0071  -0.0135 -0.0078 395 VAL A N   
3346 C CA  . VAL A 395 ? 0.2084 0.2320 0.1605 0.0066  -0.0130 -0.0082 395 VAL A CA  
3347 C C   . VAL A 395 ? 0.2578 0.2796 0.2099 0.0072  -0.0121 -0.0074 395 VAL A C   
3348 O O   . VAL A 395 ? 0.2807 0.3027 0.2332 0.0081  -0.0121 -0.0064 395 VAL A O   
3349 C CB  . VAL A 395 ? 0.2402 0.2638 0.1939 0.0063  -0.0135 -0.0083 395 VAL A CB  
3350 C CG1 . VAL A 395 ? 0.3350 0.3603 0.2886 0.0056  -0.0143 -0.0092 395 VAL A CG1 
3351 C CG2 . VAL A 395 ? 0.2781 0.3019 0.2337 0.0072  -0.0137 -0.0071 395 VAL A CG2 
3352 N N   . LYS A 396 ? 0.2646 0.2848 0.2161 0.0067  -0.0115 -0.0078 396 LYS A N   
3353 C CA  . LYS A 396 ? 0.2005 0.2188 0.1519 0.0072  -0.0107 -0.0070 396 LYS A CA  
3354 C C   . LYS A 396 ? 0.2442 0.2619 0.1976 0.0076  -0.0107 -0.0063 396 LYS A C   
3355 O O   . LYS A 396 ? 0.1963 0.2141 0.1504 0.0071  -0.0111 -0.0067 396 LYS A O   
3356 C CB  . LYS A 396 ? 0.1860 0.2029 0.1358 0.0065  -0.0099 -0.0078 396 LYS A CB  
3357 C CG  . LYS A 396 ? 0.1709 0.1860 0.1204 0.0070  -0.0090 -0.0071 396 LYS A CG  
3358 C CD  . LYS A 396 ? 0.3025 0.3162 0.2501 0.0064  -0.0083 -0.0079 396 LYS A CD  
3359 C CE  . LYS A 396 ? 0.3782 0.3899 0.3256 0.0068  -0.0073 -0.0072 396 LYS A CE  
3360 N NZ  . LYS A 396 ? 0.2742 0.2847 0.2196 0.0062  -0.0066 -0.0080 396 LYS A NZ  
3361 N N   . THR A 397 ? 0.1887 0.2204 0.2012 0.0103  0.0003  0.0002  397 THR A N   
3362 C CA  . THR A 397 ? 0.1605 0.1939 0.1726 0.0105  -0.0016 0.0008  397 THR A CA  
3363 C C   . THR A 397 ? 0.1583 0.1932 0.1737 0.0112  -0.0021 0.0016  397 THR A C   
3364 O O   . THR A 397 ? 0.2233 0.2582 0.2415 0.0112  -0.0011 0.0014  397 THR A O   
3365 C CB  . THR A 397 ? 0.1959 0.2301 0.2066 0.0095  -0.0027 -0.0005 397 THR A CB  
3366 O OG1 . THR A 397 ? 0.1914 0.2263 0.2046 0.0090  -0.0023 -0.0015 397 THR A OG1 
3367 C CG2 . THR A 397 ? 0.1834 0.2160 0.1909 0.0088  -0.0021 -0.0015 397 THR A CG2 
3368 N N   . GLU A 398 ? 0.1920 0.2283 0.2071 0.0117  -0.0038 0.0026  398 GLU A N   
3369 C CA  . GLU A 398 ? 0.2247 0.2626 0.2428 0.0124  -0.0044 0.0034  398 GLU A CA  
3370 C C   . GLU A 398 ? 0.2703 0.3099 0.2874 0.0124  -0.0065 0.0038  398 GLU A C   
3371 O O   . GLU A 398 ? 0.1882 0.2275 0.2024 0.0124  -0.0073 0.0040  398 GLU A O   
3372 C CB  . GLU A 398 ? 0.2938 0.3312 0.3131 0.0135  -0.0038 0.0050  398 GLU A CB  
3373 C CG  . GLU A 398 ? 0.2972 0.3363 0.3192 0.0143  -0.0047 0.0061  398 GLU A CG  
3374 C CD  . GLU A 398 ? 0.4009 0.4394 0.4244 0.0154  -0.0038 0.0076  398 GLU A CD  
3375 O OE1 . GLU A 398 ? 0.3743 0.4110 0.3969 0.0155  -0.0024 0.0076  398 GLU A OE1 
3376 O OE2 . GLU A 398 ? 0.4068 0.4466 0.4323 0.0162  -0.0046 0.0087  398 GLU A OE2 
3377 N N   . VAL A 399 ? 0.2183 0.2596 0.2379 0.0125  -0.0074 0.0037  399 VAL A N   
3378 C CA  . VAL A 399 ? 0.2135 0.2565 0.2325 0.0126  -0.0093 0.0042  399 VAL A CA  
3379 C C   . VAL A 399 ? 0.2081 0.2518 0.2282 0.0137  -0.0099 0.0059  399 VAL A C   
3380 O O   . VAL A 399 ? 0.2143 0.2580 0.2371 0.0143  -0.0091 0.0066  399 VAL A O   
3381 C CB  . VAL A 399 ? 0.2738 0.3184 0.2948 0.0119  -0.0101 0.0032  399 VAL A CB  
3382 C CG1 . VAL A 399 ? 0.2924 0.3388 0.3129 0.0121  -0.0121 0.0038  399 VAL A CG1 
3383 C CG2 . VAL A 399 ? 0.3415 0.3854 0.3612 0.0108  -0.0096 0.0015  399 VAL A CG2 
3384 N N   . ILE A 400 ? 0.1572 0.2016 0.1754 0.0141  -0.0114 0.0067  400 ILE A N   
3385 C CA  . ILE A 400 ? 0.2483 0.2935 0.2674 0.0151  -0.0122 0.0084  400 ILE A CA  
3386 C C   . ILE A 400 ? 0.2261 0.2732 0.2452 0.0151  -0.0142 0.0086  400 ILE A C   
3387 O O   . ILE A 400 ? 0.2351 0.2825 0.2519 0.0144  -0.0151 0.0078  400 ILE A O   
3388 C CB  . ILE A 400 ? 0.2683 0.3122 0.2849 0.0157  -0.0119 0.0094  400 ILE A CB  
3389 C CG1 . ILE A 400 ? 0.4104 0.4552 0.4277 0.0168  -0.0128 0.0111  400 ILE A CG1 
3390 C CG2 . ILE A 400 ? 0.3302 0.3735 0.3431 0.0151  -0.0126 0.0087  400 ILE A CG2 
3391 C CD1 . ILE A 400 ? 0.4429 0.4864 0.4577 0.0173  -0.0126 0.0121  400 ILE A CD1 
3392 N N   . GLU A 401 ? 0.1890 0.2376 0.2108 0.0158  -0.0148 0.0097  401 GLU A N   
3393 C CA  . GLU A 401 ? 0.2610 0.3116 0.2833 0.0158  -0.0166 0.0098  401 GLU A CA  
3394 C C   . GLU A 401 ? 0.2577 0.3090 0.2786 0.0166  -0.0180 0.0113  401 GLU A C   
3395 O O   . GLU A 401 ? 0.2566 0.3093 0.2769 0.0164  -0.0197 0.0113  401 GLU A O   
3396 C CB  . GLU A 401 ? 0.2662 0.3181 0.2923 0.0160  -0.0166 0.0100  401 GLU A CB  
3397 C CG  . GLU A 401 ? 0.3193 0.3711 0.3467 0.0151  -0.0158 0.0084  401 GLU A CG  
3398 C CD  . GLU A 401 ? 0.4989 0.5511 0.5241 0.0141  -0.0167 0.0071  401 GLU A CD  
3399 O OE1 . GLU A 401 ? 0.5725 0.6260 0.5968 0.0141  -0.0184 0.0074  401 GLU A OE1 
3400 O OE2 . GLU A 401 ? 0.5811 0.6322 0.6055 0.0132  -0.0158 0.0057  401 GLU A OE2 
3401 N N   . SER A 402 ? 0.2463 0.2966 0.2669 0.0174  -0.0174 0.0125  402 SER A N   
3402 C CA  . SER A 402 ? 0.3206 0.3715 0.3399 0.0181  -0.0187 0.0140  402 SER A CA  
3403 C C   . SER A 402 ? 0.3191 0.3685 0.3372 0.0188  -0.0177 0.0149  402 SER A C   
3404 O O   . SER A 402 ? 0.2901 0.3381 0.3092 0.0189  -0.0161 0.0148  402 SER A O   
3405 C CB  . SER A 402 ? 0.3585 0.4113 0.3808 0.0188  -0.0197 0.0150  402 SER A CB  
3406 O OG  . SER A 402 ? 0.5156 0.5679 0.5395 0.0198  -0.0189 0.0164  402 SER A OG  
3407 N N   . VAL A 403 ? 0.2324 0.2818 0.2482 0.0192  -0.0188 0.0158  403 VAL A N   
3408 C CA  . VAL A 403 ? 0.2714 0.3195 0.2860 0.0199  -0.0180 0.0169  403 VAL A CA  
3409 C C   . VAL A 403 ? 0.1615 0.2107 0.1766 0.0209  -0.0192 0.0186  403 VAL A C   
3410 O O   . VAL A 403 ? 0.2022 0.2531 0.2174 0.0209  -0.0209 0.0189  403 VAL A O   
3411 C CB  . VAL A 403 ? 0.2392 0.2858 0.2499 0.0194  -0.0179 0.0164  403 VAL A CB  
3412 C CG1 . VAL A 403 ? 0.2335 0.2790 0.2438 0.0185  -0.0166 0.0147  403 VAL A CG1 
3413 C CG2 . VAL A 403 ? 0.2486 0.2963 0.2569 0.0192  -0.0198 0.0164  403 VAL A CG2 
3414 N N   . LYS A 404 ? 0.2238 0.2722 0.2394 0.0217  -0.0184 0.0199  404 LYS A N   
3415 C CA  . LYS A 404 ? 0.2356 0.2847 0.2510 0.0227  -0.0195 0.0215  404 LYS A CA  
3416 C C   . LYS A 404 ? 0.1801 0.2285 0.1917 0.0225  -0.0201 0.0217  404 LYS A C   
3417 O O   . LYS A 404 ? 0.2137 0.2604 0.2233 0.0223  -0.0190 0.0213  404 LYS A O   
3418 C CB  . LYS A 404 ? 0.3369 0.3852 0.3542 0.0236  -0.0183 0.0227  404 LYS A CB  
3419 C CG  . LYS A 404 ? 0.4765 0.5255 0.4977 0.0239  -0.0177 0.0229  404 LYS A CG  
3420 C CD  . LYS A 404 ? 0.5145 0.5643 0.5375 0.0250  -0.0181 0.0246  404 LYS A CD  
3421 C CE  . LYS A 404 ? 0.5720 0.6230 0.5988 0.0253  -0.0181 0.0248  404 LYS A CE  
3422 N NZ  . LYS A 404 ? 0.5699 0.6226 0.5972 0.0246  -0.0193 0.0238  404 LYS A NZ  
3423 N N   . ALA A 405 ? 0.2161 0.2658 0.2265 0.0227  -0.0219 0.0222  405 ALA A N   
3424 C CA  . ALA A 405 ? 0.1621 0.2113 0.1688 0.0225  -0.0226 0.0223  405 ALA A CA  
3425 C C   . ALA A 405 ? 0.1336 0.1815 0.1393 0.0232  -0.0218 0.0235  405 ALA A C   
3426 O O   . ALA A 405 ? 0.2048 0.2528 0.2124 0.0241  -0.0216 0.0248  405 ALA A O   
3427 C CB  . ALA A 405 ? 0.1382 0.1891 0.1441 0.0226  -0.0247 0.0229  405 ALA A CB  
3428 N N   . GLY A 406 ? 0.1886 0.2351 0.1911 0.0229  -0.0214 0.0230  406 GLY A N   
3429 C CA  . GLY A 406 ? 0.1690 0.2141 0.1703 0.0236  -0.0206 0.0241  406 GLY A CA  
3430 C C   . GLY A 406 ? 0.1985 0.2423 0.1961 0.0230  -0.0204 0.0235  406 GLY A C   
3431 O O   . GLY A 406 ? 0.2055 0.2494 0.2012 0.0222  -0.0210 0.0223  406 GLY A O   
3432 N N   . THR A 407 ? 0.1415 0.1838 0.1380 0.0235  -0.0194 0.0242  407 THR A N   
3433 C CA  . THR A 407 ? 0.1868 0.2276 0.1799 0.0232  -0.0189 0.0238  407 THR A CA  
3434 C C   . THR A 407 ? 0.1947 0.2336 0.1884 0.0234  -0.0169 0.0239  407 THR A C   
3435 O O   . THR A 407 ? 0.2531 0.2920 0.2496 0.0239  -0.0161 0.0244  407 THR A O   
3436 C CB  . THR A 407 ? 0.1363 0.1772 0.1267 0.0236  -0.0200 0.0249  407 THR A CB  
3437 O OG1 . THR A 407 ? 0.1966 0.2369 0.1879 0.0246  -0.0194 0.0264  407 THR A OG1 
3438 C CG2 . THR A 407 ? 0.1462 0.1890 0.1366 0.0237  -0.0221 0.0253  407 THR A CG2 
3439 N N   . TRP A 408 ? 0.1773 0.2146 0.1682 0.0231  -0.0162 0.0234  408 TRP A N   
3440 C CA  . TRP A 408 ? 0.2047 0.2403 0.1960 0.0233  -0.0143 0.0236  408 TRP A CA  
3441 C C   . TRP A 408 ? 0.2758 0.3110 0.2672 0.0244  -0.0142 0.0253  408 TRP A C   
3442 O O   . TRP A 408 ? 0.2619 0.2956 0.2535 0.0247  -0.0127 0.0256  408 TRP A O   
3443 C CB  . TRP A 408 ? 0.2352 0.2691 0.2237 0.0226  -0.0134 0.0224  408 TRP A CB  
3444 C CG  . TRP A 408 ? 0.2424 0.2761 0.2272 0.0225  -0.0143 0.0226  408 TRP A CG  
3445 C CD1 . TRP A 408 ? 0.2755 0.3101 0.2591 0.0230  -0.0158 0.0237  408 TRP A CD1 
3446 C CD2 . TRP A 408 ? 0.1846 0.2169 0.1665 0.0217  -0.0138 0.0215  408 TRP A CD2 
3447 N NE1 . TRP A 408 ? 0.2746 0.3085 0.2546 0.0226  -0.0162 0.0234  408 TRP A NE1 
3448 C CE2 . TRP A 408 ? 0.2284 0.2609 0.2073 0.0219  -0.0149 0.0221  408 TRP A CE2 
3449 C CE3 . TRP A 408 ? 0.2513 0.2822 0.2326 0.0210  -0.0124 0.0201  408 TRP A CE3 
3450 C CZ2 . TRP A 408 ? 0.2863 0.3178 0.2618 0.0213  -0.0148 0.0213  408 TRP A CZ2 
3451 C CZ3 . TRP A 408 ? 0.2687 0.2985 0.2467 0.0204  -0.0122 0.0194  408 TRP A CZ3 
3452 C CH2 . TRP A 408 ? 0.2539 0.2840 0.2291 0.0206  -0.0134 0.0199  408 TRP A CH2 
3453 N N   . PHE A 409 ? 0.2070 0.2435 0.1984 0.0250  -0.0157 0.0266  409 PHE A N   
3454 C CA  . PHE A 409 ? 0.2264 0.2628 0.2185 0.0261  -0.0156 0.0283  409 PHE A CA  
3455 C C   . PHE A 409 ? 0.2495 0.2872 0.2455 0.0266  -0.0157 0.0289  409 PHE A C   
3456 O O   . PHE A 409 ? 0.2303 0.2696 0.2272 0.0267  -0.0171 0.0293  409 PHE A O   
3457 C CB  . PHE A 409 ? 0.3043 0.3413 0.2940 0.0264  -0.0170 0.0293  409 PHE A CB  
3458 C CG  . PHE A 409 ? 0.4131 0.4485 0.3992 0.0262  -0.0166 0.0291  409 PHE A CG  
3459 C CD1 . PHE A 409 ? 0.3987 0.4327 0.3845 0.0268  -0.0154 0.0300  409 PHE A CD1 
3460 C CD2 . PHE A 409 ? 0.4404 0.4758 0.4237 0.0254  -0.0173 0.0280  409 PHE A CD2 
3461 C CE1 . PHE A 409 ? 0.4362 0.4687 0.4187 0.0265  -0.0149 0.0298  409 PHE A CE1 
3462 C CE2 . PHE A 409 ? 0.4800 0.5139 0.4600 0.0252  -0.0168 0.0278  409 PHE A CE2 
3463 C CZ  . PHE A 409 ? 0.4920 0.5246 0.4717 0.0257  -0.0156 0.0287  409 PHE A CZ  
3464 N N   . ASP A 410 ? 0.2829 0.3196 0.2811 0.0269  -0.0141 0.0290  410 ASP A N   
3465 C CA  . ASP A 410 ? 0.2440 0.2816 0.2460 0.0274  -0.0139 0.0296  410 ASP A CA  
3466 C C   . ASP A 410 ? 0.3294 0.3686 0.3333 0.0269  -0.0148 0.0288  410 ASP A C   
3467 O O   . ASP A 410 ? 0.3878 0.4282 0.3945 0.0274  -0.0151 0.0294  410 ASP A O   
3468 C CB  . ASP A 410 ? 0.3413 0.3797 0.3441 0.0285  -0.0147 0.0315  410 ASP A CB  
3469 C CG  . ASP A 410 ? 0.5370 0.5739 0.5379 0.0290  -0.0140 0.0324  410 ASP A CG  
3470 O OD1 . ASP A 410 ? 0.5502 0.5854 0.5511 0.0289  -0.0123 0.0321  410 ASP A OD1 
3471 O OD2 . ASP A 410 ? 0.6123 0.6495 0.6114 0.0295  -0.0151 0.0335  410 ASP A OD2 
3472 N N   . GLY A 411 ? 0.2608 0.3001 0.2631 0.0260  -0.0151 0.0273  411 GLY A N   
3473 C CA  . GLY A 411 ? 0.2160 0.2568 0.2199 0.0255  -0.0159 0.0264  411 GLY A CA  
3474 C C   . GLY A 411 ? 0.2370 0.2798 0.2413 0.0258  -0.0178 0.0273  411 GLY A C   
3475 O O   . GLY A 411 ? 0.2994 0.3435 0.3059 0.0257  -0.0184 0.0269  411 GLY A O   
3476 N N   . ASN A 412 ? 0.2197 0.2626 0.2219 0.0263  -0.0188 0.0284  412 ASN A N   
3477 C CA  . ASN A 412 ? 0.2143 0.2591 0.2169 0.0266  -0.0206 0.0292  412 ASN A CA  
3478 C C   . ASN A 412 ? 0.1472 0.1920 0.1462 0.0265  -0.0218 0.0295  412 ASN A C   
3479 O O   . ASN A 412 ? 0.2190 0.2623 0.2153 0.0261  -0.0212 0.0289  412 ASN A O   
3480 C CB  . ASN A 412 ? 0.2914 0.3369 0.2967 0.0277  -0.0207 0.0309  412 ASN A CB  
3481 C CG  . ASN A 412 ? 0.3706 0.4148 0.3748 0.0285  -0.0200 0.0321  412 ASN A CG  
3482 O OD1 . ASN A 412 ? 0.2710 0.3147 0.2722 0.0285  -0.0206 0.0325  412 ASN A OD1 
3483 N ND2 . ASN A 412 ? 0.3552 0.3989 0.3619 0.0291  -0.0189 0.0329  412 ASN A ND2 
3484 N N   . PHE A 413 ? 0.1463 0.1927 0.1453 0.0268  -0.0235 0.0303  413 PHE A N   
3485 C CA  . PHE A 413 ? 0.1796 0.2262 0.1752 0.0267  -0.0248 0.0305  413 PHE A CA  
3486 C C   . PHE A 413 ? 0.2147 0.2613 0.2094 0.0276  -0.0254 0.0322  413 PHE A C   
3487 O O   . PHE A 413 ? 0.1872 0.2343 0.1794 0.0276  -0.0267 0.0326  413 PHE A O   
3488 C CB  . PHE A 413 ? 0.2104 0.2589 0.2062 0.0262  -0.0266 0.0300  413 PHE A CB  
3489 C CG  . PHE A 413 ? 0.1913 0.2399 0.1875 0.0252  -0.0262 0.0282  413 PHE A CG  
3490 C CD1 . PHE A 413 ? 0.1854 0.2332 0.1785 0.0244  -0.0263 0.0270  413 PHE A CD1 
3491 C CD2 . PHE A 413 ? 0.1916 0.2408 0.1911 0.0251  -0.0258 0.0278  413 PHE A CD2 
3492 C CE1 . PHE A 413 ? 0.1917 0.2396 0.1851 0.0235  -0.0260 0.0253  413 PHE A CE1 
3493 C CE2 . PHE A 413 ? 0.2044 0.2536 0.2041 0.0242  -0.0255 0.0261  413 PHE A CE2 
3494 C CZ  . PHE A 413 ? 0.2124 0.2609 0.2091 0.0234  -0.0256 0.0249  413 PHE A CZ  
3495 N N   . LEU A 414 ? 0.2528 0.2987 0.2491 0.0284  -0.0243 0.0333  414 LEU A N   
3496 C CA  . LEU A 414 ? 0.2764 0.3226 0.2723 0.0293  -0.0249 0.0350  414 LEU A CA  
3497 C C   . LEU A 414 ? 0.2609 0.3059 0.2531 0.0293  -0.0249 0.0353  414 LEU A C   
3498 O O   . LEU A 414 ? 0.2472 0.2926 0.2385 0.0299  -0.0258 0.0366  414 LEU A O   
3499 C CB  . LEU A 414 ? 0.2572 0.3029 0.2559 0.0301  -0.0237 0.0361  414 LEU A CB  
3500 C CG  . LEU A 414 ? 0.2904 0.3375 0.2929 0.0304  -0.0239 0.0362  414 LEU A CG  
3501 C CD1 . LEU A 414 ? 0.2548 0.3014 0.2600 0.0313  -0.0229 0.0374  414 LEU A CD1 
3502 C CD2 . LEU A 414 ? 0.2304 0.2794 0.2331 0.0305  -0.0259 0.0368  414 LEU A CD2 
3503 N N   . LYS A 415 ? 0.1860 0.2296 0.1760 0.0285  -0.0240 0.0340  415 LYS A N   
3504 C CA  . LYS A 415 ? 0.2292 0.2718 0.2157 0.0285  -0.0242 0.0342  415 LYS A CA  
3505 C C   . LYS A 415 ? 0.2205 0.2642 0.2045 0.0281  -0.0260 0.0340  415 LYS A C   
3506 O O   . LYS A 415 ? 0.2242 0.2673 0.2053 0.0282  -0.0264 0.0344  415 LYS A O   
3507 C CB  . LYS A 415 ? 0.2978 0.3385 0.2826 0.0278  -0.0227 0.0329  415 LYS A CB  
3508 C CG  . LYS A 415 ? 0.3933 0.4326 0.3799 0.0282  -0.0208 0.0332  415 LYS A CG  
3509 C CD  . LYS A 415 ? 0.4912 0.5303 0.4780 0.0293  -0.0208 0.0350  415 LYS A CD  
3510 C CE  . LYS A 415 ? 0.5511 0.5891 0.5345 0.0293  -0.0208 0.0354  415 LYS A CE  
3511 N NZ  . LYS A 415 ? 0.6142 0.6517 0.5980 0.0303  -0.0204 0.0371  415 LYS A NZ  
3512 N N   . TRP A 416 ? 0.1760 0.2212 0.1611 0.0277  -0.0271 0.0334  416 TRP A N   
3513 C CA  . TRP A 416 ? 0.1976 0.2439 0.1804 0.0273  -0.0288 0.0331  416 TRP A CA  
3514 C C   . TRP A 416 ? 0.1730 0.2214 0.1575 0.0277  -0.0305 0.0340  416 TRP A C   
3515 O O   . TRP A 416 ? 0.1998 0.2492 0.1825 0.0275  -0.0320 0.0340  416 TRP A O   
3516 C CB  . TRP A 416 ? 0.1472 0.1933 0.1290 0.0262  -0.0287 0.0312  416 TRP A CB  
3517 C CG  . TRP A 416 ? 0.2193 0.2634 0.1995 0.0257  -0.0271 0.0302  416 TRP A CG  
3518 C CD1 . TRP A 416 ? 0.2234 0.2665 0.2001 0.0254  -0.0270 0.0298  416 TRP A CD1 
3519 C CD2 . TRP A 416 ? 0.2099 0.2529 0.1919 0.0256  -0.0253 0.0296  416 TRP A CD2 
3520 N NE1 . TRP A 416 ? 0.2314 0.2728 0.2077 0.0250  -0.0254 0.0290  416 TRP A NE1 
3521 C CE2 . TRP A 416 ? 0.2090 0.2502 0.1885 0.0251  -0.0243 0.0288  416 TRP A CE2 
3522 C CE3 . TRP A 416 ? 0.1500 0.1933 0.1356 0.0258  -0.0245 0.0296  416 TRP A CE3 
3523 C CZ2 . TRP A 416 ? 0.1797 0.2195 0.1601 0.0248  -0.0224 0.0280  416 TRP A CZ2 
3524 C CZ3 . TRP A 416 ? 0.1558 0.1976 0.1423 0.0255  -0.0227 0.0288  416 TRP A CZ3 
3525 C CH2 . TRP A 416 ? 0.2177 0.2578 0.2016 0.0251  -0.0217 0.0280  416 TRP A CH2 
3526 N N   . ILE A 417 ? 0.1698 0.2189 0.1577 0.0283  -0.0302 0.0348  417 ILE A N   
3527 C CA  . ILE A 417 ? 0.1962 0.2473 0.1859 0.0287  -0.0317 0.0356  417 ILE A CA  
3528 C C   . ILE A 417 ? 0.2303 0.2815 0.2231 0.0296  -0.0311 0.0369  417 ILE A C   
3529 O O   . ILE A 417 ? 0.2049 0.2549 0.1990 0.0298  -0.0295 0.0368  417 ILE A O   
3530 C CB  . ILE A 417 ? 0.2410 0.2932 0.2318 0.0279  -0.0323 0.0343  417 ILE A CB  
3531 C CG1 . ILE A 417 ? 0.1809 0.2352 0.1725 0.0281  -0.0343 0.0350  417 ILE A CG1 
3532 C CG2 . ILE A 417 ? 0.2078 0.2597 0.2017 0.0278  -0.0310 0.0336  417 ILE A CG2 
3533 C CD1 . ILE A 417 ? 0.2502 0.3055 0.2414 0.0272  -0.0352 0.0336  417 ILE A CD1 
3534 N N   . GLY A 418 ? 0.3115 0.3643 0.3056 0.0302  -0.0324 0.0382  418 GLY A N   
3535 C CA  . GLY A 418 ? 0.3345 0.3878 0.3320 0.0310  -0.0320 0.0394  418 GLY A CA  
3536 C C   . GLY A 418 ? 0.4659 0.5191 0.4631 0.0320  -0.0323 0.0412  418 GLY A C   
3537 O O   . GLY A 418 ? 0.5593 0.6133 0.5593 0.0327  -0.0324 0.0423  418 GLY A O   
3538 N N   . ASN A 419 ? 0.4681 0.5205 0.4622 0.0321  -0.0325 0.0416  419 ASN A N   
3539 C CA  . ASN A 419 ? 0.4221 0.4746 0.4158 0.0330  -0.0330 0.0433  419 ASN A CA  
3540 C C   . ASN A 419 ? 0.4250 0.4786 0.4162 0.0329  -0.0348 0.0437  419 ASN A C   
3541 O O   . ASN A 419 ? 0.3934 0.4476 0.3831 0.0321  -0.0356 0.0426  419 ASN A O   
3542 C CB  . ASN A 419 ? 0.3252 0.3758 0.3176 0.0333  -0.0315 0.0437  419 ASN A CB  
3543 C CG  . ASN A 419 ? 0.3855 0.4349 0.3740 0.0327  -0.0314 0.0429  419 ASN A CG  
3544 O OD1 . ASN A 419 ? 0.3782 0.4283 0.3645 0.0322  -0.0326 0.0425  419 ASN A OD1 
3545 N ND2 . ASN A 419 ? 0.3947 0.4422 0.3823 0.0328  -0.0298 0.0428  419 ASN A ND2 
3546 N N   . LYS A 420 ? 0.3493 0.4032 0.3400 0.0336  -0.0355 0.0454  420 LYS A N   
3547 C CA  . LYS A 420 ? 0.2799 0.3352 0.2689 0.0337  -0.0374 0.0460  420 LYS A CA  
3548 C C   . LYS A 420 ? 0.2606 0.3152 0.2456 0.0330  -0.0378 0.0450  420 LYS A C   
3549 O O   . LYS A 420 ? 0.3060 0.3617 0.2898 0.0324  -0.0391 0.0444  420 LYS A O   
3550 C CB  . LYS A 420 ? 0.2984 0.3540 0.2877 0.0347  -0.0379 0.0479  420 LYS A CB  
3551 C CG  . LYS A 420 ? 0.3480 0.4049 0.3352 0.0347  -0.0398 0.0486  420 LYS A CG  
3552 C CD  . LYS A 420 ? 0.5542 0.6131 0.5440 0.0353  -0.0411 0.0497  420 LYS A CD  
3553 C CE  . LYS A 420 ? 0.6088 0.6684 0.5971 0.0359  -0.0424 0.0513  420 LYS A CE  
3554 N NZ  . LYS A 420 ? 0.6807 0.7423 0.6712 0.0363  -0.0438 0.0523  420 LYS A NZ  
3555 N N   . GLU A 421 ? 0.3188 0.3716 0.3018 0.0330  -0.0366 0.0449  421 GLU A N   
3556 C CA  . GLU A 421 ? 0.3900 0.4422 0.3692 0.0323  -0.0369 0.0441  421 GLU A CA  
3557 C C   . GLU A 421 ? 0.3724 0.4243 0.3510 0.0313  -0.0367 0.0422  421 GLU A C   
3558 O O   . GLU A 421 ? 0.3055 0.3580 0.2819 0.0307  -0.0379 0.0415  421 GLU A O   
3559 C CB  . GLU A 421 ? 0.4672 0.5174 0.4446 0.0326  -0.0356 0.0445  421 GLU A CB  
3560 C CG  . GLU A 421 ? 0.6663 0.7167 0.6441 0.0336  -0.0359 0.0464  421 GLU A CG  
3561 C CD  . GLU A 421 ? 0.8318 0.8819 0.8130 0.0343  -0.0348 0.0473  421 GLU A CD  
3562 O OE1 . GLU A 421 ? 0.8913 0.9408 0.8725 0.0351  -0.0343 0.0486  421 GLU A OE1 
3563 O OE2 . GLU A 421 ? 0.8524 0.9030 0.8363 0.0342  -0.0344 0.0466  421 GLU A OE2 
3564 N N   . LYS A 422 ? 0.3144 0.3656 0.2950 0.0311  -0.0353 0.0413  422 LYS A N   
3565 C CA  . LYS A 422 ? 0.2988 0.3499 0.2790 0.0301  -0.0350 0.0395  422 LYS A CA  
3566 C C   . LYS A 422 ? 0.3654 0.4183 0.3467 0.0298  -0.0366 0.0391  422 LYS A C   
3567 O O   . LYS A 422 ? 0.3300 0.3833 0.3096 0.0290  -0.0373 0.0379  422 LYS A O   
3568 C CB  . LYS A 422 ? 0.3095 0.3594 0.2919 0.0299  -0.0332 0.0387  422 LYS A CB  
3569 C CG  . LYS A 422 ? 0.2847 0.3325 0.2652 0.0299  -0.0316 0.0385  422 LYS A CG  
3570 C CD  . LYS A 422 ? 0.2795 0.3263 0.2625 0.0300  -0.0298 0.0381  422 LYS A CD  
3571 C CE  . LYS A 422 ? 0.3076 0.3524 0.2893 0.0302  -0.0283 0.0384  422 LYS A CE  
3572 N NZ  . LYS A 422 ? 0.3111 0.3549 0.2890 0.0296  -0.0283 0.0375  422 LYS A NZ  
3573 N N   . ASN A 423 ? 0.2636 0.3179 0.2478 0.0304  -0.0371 0.0402  423 ASN A N   
3574 C CA  . ASN A 423 ? 0.2620 0.3182 0.2474 0.0301  -0.0386 0.0399  423 ASN A CA  
3575 C C   . ASN A 423 ? 0.2659 0.3229 0.2484 0.0299  -0.0404 0.0402  423 ASN A C   
3576 O O   . ASN A 423 ? 0.2823 0.3404 0.2643 0.0293  -0.0414 0.0393  423 ASN A O   
3577 C CB  . ASN A 423 ? 0.2784 0.3358 0.2673 0.0309  -0.0389 0.0412  423 ASN A CB  
3578 C CG  . ASN A 423 ? 0.3539 0.4109 0.3460 0.0309  -0.0375 0.0406  423 ASN A CG  
3579 O OD1 . ASN A 423 ? 0.2797 0.3357 0.2714 0.0302  -0.0365 0.0391  423 ASN A OD1 
3580 N ND2 . ASN A 423 ? 0.3125 0.3704 0.3078 0.0316  -0.0375 0.0417  423 ASN A ND2 
3581 N N   . GLU A 424 ? 0.3398 0.3963 0.3203 0.0305  -0.0406 0.0413  424 GLU A N   
3582 C CA  . GLU A 424 ? 0.3412 0.3985 0.3189 0.0303  -0.0423 0.0416  424 GLU A CA  
3583 C C   . GLU A 424 ? 0.3232 0.3798 0.2979 0.0293  -0.0423 0.0400  424 GLU A C   
3584 O O   . GLU A 424 ? 0.2805 0.3382 0.2537 0.0289  -0.0438 0.0396  424 GLU A O   
3585 C CB  . GLU A 424 ? 0.4937 0.5506 0.4698 0.0310  -0.0424 0.0431  424 GLU A CB  
3586 C CG  . GLU A 424 ? 0.6079 0.6650 0.5804 0.0308  -0.0438 0.0432  424 GLU A CG  
3587 C CD  . GLU A 424 ? 0.7644 0.8236 0.7374 0.0308  -0.0457 0.0437  424 GLU A CD  
3588 O OE1 . GLU A 424 ? 0.7914 0.8516 0.7658 0.0304  -0.0463 0.0428  424 GLU A OE1 
3589 O OE2 . GLU A 424 ? 0.8447 0.9045 0.8166 0.0314  -0.0468 0.0450  424 GLU A OE2 
3590 N N   . TYR A 425 ? 0.3272 0.3822 0.3010 0.0290  -0.0408 0.0390  425 TYR A N   
3591 C CA  . TYR A 425 ? 0.2727 0.3269 0.2439 0.0280  -0.0407 0.0374  425 TYR A CA  
3592 C C   . TYR A 425 ? 0.2445 0.2999 0.2171 0.0273  -0.0413 0.0362  425 TYR A C   
3593 O O   . TYR A 425 ? 0.2806 0.3366 0.2513 0.0267  -0.0424 0.0353  425 TYR A O   
3594 C CB  . TYR A 425 ? 0.2777 0.3299 0.2481 0.0277  -0.0388 0.0366  425 TYR A CB  
3595 C CG  . TYR A 425 ? 0.2672 0.3182 0.2344 0.0278  -0.0386 0.0369  425 TYR A CG  
3596 C CD1 . TYR A 425 ? 0.2393 0.2908 0.2050 0.0284  -0.0396 0.0383  425 TYR A CD1 
3597 C CD2 . TYR A 425 ? 0.2785 0.3278 0.2438 0.0273  -0.0373 0.0358  425 TYR A CD2 
3598 C CE1 . TYR A 425 ? 0.2161 0.2664 0.1787 0.0285  -0.0394 0.0386  425 TYR A CE1 
3599 C CE2 . TYR A 425 ? 0.3032 0.3512 0.2653 0.0274  -0.0370 0.0361  425 TYR A CE2 
3600 C CZ  . TYR A 425 ? 0.3060 0.3546 0.2669 0.0280  -0.0381 0.0375  425 TYR A CZ  
3601 O OH  . TYR A 425 ? 0.3212 0.3687 0.2790 0.0281  -0.0379 0.0379  425 TYR A OH  
3602 N N   . TRP A 426 ? 0.2300 0.2857 0.2060 0.0274  -0.0406 0.0361  426 TRP A N   
3603 C CA  . TRP A 426 ? 0.2482 0.3051 0.2258 0.0268  -0.0412 0.0350  426 TRP A CA  
3604 C C   . TRP A 426 ? 0.2120 0.2709 0.1897 0.0269  -0.0432 0.0356  426 TRP A C   
3605 O O   . TRP A 426 ? 0.2794 0.3390 0.2562 0.0262  -0.0442 0.0345  426 TRP A O   
3606 C CB  . TRP A 426 ? 0.2655 0.3224 0.2469 0.0270  -0.0400 0.0349  426 TRP A CB  
3607 C CG  . TRP A 426 ? 0.2339 0.2890 0.2152 0.0267  -0.0381 0.0339  426 TRP A CG  
3608 C CD1 . TRP A 426 ? 0.1875 0.2412 0.1695 0.0272  -0.0366 0.0345  426 TRP A CD1 
3609 C CD2 . TRP A 426 ? 0.2600 0.3145 0.2407 0.0257  -0.0375 0.0320  426 TRP A CD2 
3610 N NE1 . TRP A 426 ? 0.2600 0.3122 0.2417 0.0266  -0.0351 0.0331  426 TRP A NE1 
3611 C CE2 . TRP A 426 ? 0.1645 0.2172 0.1454 0.0257  -0.0356 0.0316  426 TRP A CE2 
3612 C CE3 . TRP A 426 ? 0.1499 0.2051 0.1297 0.0248  -0.0384 0.0307  426 TRP A CE3 
3613 C CZ2 . TRP A 426 ? 0.2791 0.3308 0.2595 0.0248  -0.0346 0.0300  426 TRP A CZ2 
3614 C CZ3 . TRP A 426 ? 0.2552 0.3095 0.2346 0.0240  -0.0374 0.0291  426 TRP A CZ3 
3615 C CH2 . TRP A 426 ? 0.2058 0.2583 0.1854 0.0240  -0.0355 0.0287  426 TRP A CH2 
3616 N N   . LYS A 427 ? 0.2182 0.2778 0.1967 0.0278  -0.0439 0.0373  427 LYS A N   
3617 C CA  . LYS A 427 ? 0.2503 0.3118 0.2287 0.0279  -0.0458 0.0379  427 LYS A CA  
3618 C C   . LYS A 427 ? 0.2620 0.3235 0.2367 0.0274  -0.0469 0.0374  427 LYS A C   
3619 O O   . LYS A 427 ? 0.2474 0.3100 0.2215 0.0269  -0.0483 0.0368  427 LYS A O   
3620 C CB  . LYS A 427 ? 0.3351 0.3972 0.3147 0.0290  -0.0463 0.0399  427 LYS A CB  
3621 C CG  . LYS A 427 ? 0.5162 0.5789 0.4998 0.0295  -0.0458 0.0406  427 LYS A CG  
3622 C CD  . LYS A 427 ? 0.5746 0.6375 0.5591 0.0306  -0.0459 0.0425  427 LYS A CD  
3623 C CE  . LYS A 427 ? 0.6271 0.6905 0.6156 0.0312  -0.0452 0.0431  427 LYS A CE  
3624 N NZ  . LYS A 427 ? 0.7133 0.7763 0.7026 0.0322  -0.0448 0.0448  427 LYS A NZ  
3625 N N   . ILE A 428 ? 0.2913 0.3514 0.2632 0.0274  -0.0464 0.0376  428 ILE A N   
3626 C CA  . ILE A 428 ? 0.3122 0.3720 0.2803 0.0269  -0.0472 0.0369  428 ILE A CA  
3627 C C   . ILE A 428 ? 0.3085 0.3682 0.2760 0.0258  -0.0471 0.0350  428 ILE A C   
3628 O O   . ILE A 428 ? 0.2710 0.3316 0.2370 0.0253  -0.0485 0.0344  428 ILE A O   
3629 C CB  . ILE A 428 ? 0.3131 0.3712 0.2786 0.0271  -0.0463 0.0373  428 ILE A CB  
3630 C CG1 . ILE A 428 ? 0.3072 0.3658 0.2727 0.0281  -0.0469 0.0392  428 ILE A CG1 
3631 C CG2 . ILE A 428 ? 0.3032 0.3608 0.2651 0.0264  -0.0467 0.0362  428 ILE A CG2 
3632 C CD1 . ILE A 428 ? 0.3221 0.3790 0.2866 0.0286  -0.0456 0.0399  428 ILE A CD1 
3633 N N   . LEU A 429 ? 0.2750 0.3335 0.2435 0.0255  -0.0455 0.0340  429 LEU A N   
3634 C CA  . LEU A 429 ? 0.2405 0.2988 0.2086 0.0245  -0.0453 0.0322  429 LEU A CA  
3635 C C   . LEU A 429 ? 0.2473 0.3074 0.2171 0.0242  -0.0466 0.0318  429 LEU A C   
3636 O O   . LEU A 429 ? 0.2499 0.3105 0.2181 0.0235  -0.0475 0.0307  429 LEU A O   
3637 C CB  . LEU A 429 ? 0.2330 0.2899 0.2026 0.0243  -0.0433 0.0314  429 LEU A CB  
3638 C CG  . LEU A 429 ? 0.3210 0.3775 0.2901 0.0233  -0.0429 0.0294  429 LEU A CG  
3639 C CD1 . LEU A 429 ? 0.3601 0.4157 0.3253 0.0227  -0.0431 0.0286  429 LEU A CD1 
3640 C CD2 . LEU A 429 ? 0.2909 0.3461 0.2619 0.0232  -0.0409 0.0288  429 LEU A CD2 
3641 N N   . ILE A 430 ? 0.2634 0.3246 0.2366 0.0248  -0.0467 0.0327  430 ILE A N   
3642 C CA  . ILE A 430 ? 0.3456 0.4086 0.3207 0.0245  -0.0479 0.0323  430 ILE A CA  
3643 C C   . ILE A 430 ? 0.3243 0.3885 0.2974 0.0244  -0.0499 0.0327  430 ILE A C   
3644 O O   . ILE A 430 ? 0.2809 0.3460 0.2535 0.0237  -0.0508 0.0317  430 ILE A O   
3645 C CB  . ILE A 430 ? 0.2895 0.3533 0.2685 0.0252  -0.0476 0.0334  430 ILE A CB  
3646 C CG1 . ILE A 430 ? 0.2819 0.3446 0.2631 0.0251  -0.0457 0.0327  430 ILE A CG1 
3647 C CG2 . ILE A 430 ? 0.2068 0.2726 0.1875 0.0251  -0.0492 0.0335  430 ILE A CG2 
3648 C CD1 . ILE A 430 ? 0.2833 0.3460 0.2674 0.0260  -0.0450 0.0340  430 ILE A CD1 
3649 N N   . GLU A 431 ? 0.3284 0.3928 0.3004 0.0251  -0.0505 0.0342  431 GLU A N   
3650 C CA  . GLU A 431 ? 0.3292 0.3948 0.2992 0.0250  -0.0524 0.0346  431 GLU A CA  
3651 C C   . GLU A 431 ? 0.2864 0.3513 0.2528 0.0242  -0.0527 0.0333  431 GLU A C   
3652 O O   . GLU A 431 ? 0.3425 0.4086 0.3078 0.0237  -0.0542 0.0328  431 GLU A O   
3653 C CB  . GLU A 431 ? 0.3757 0.4415 0.3452 0.0259  -0.0529 0.0365  431 GLU A CB  
3654 C CG  . GLU A 431 ? 0.4764 0.5431 0.4494 0.0268  -0.0528 0.0378  431 GLU A CG  
3655 C CD  . GLU A 431 ? 0.5949 0.6636 0.5700 0.0267  -0.0542 0.0379  431 GLU A CD  
3656 O OE1 . GLU A 431 ? 0.5869 0.6565 0.5603 0.0262  -0.0557 0.0374  431 GLU A OE1 
3657 O OE2 . GLU A 431 ? 0.6461 0.7155 0.6246 0.0271  -0.0539 0.0384  431 GLU A OE2 
3658 N N   . ALA A 432 ? 0.3170 0.3802 0.2817 0.0240  -0.0514 0.0328  432 ALA A N   
3659 C CA  . ALA A 432 ? 0.2872 0.3496 0.2484 0.0232  -0.0516 0.0315  432 ALA A CA  
3660 C C   . ALA A 432 ? 0.3801 0.4428 0.3418 0.0223  -0.0517 0.0298  432 ALA A C   
3661 O O   . ALA A 432 ? 0.4007 0.4637 0.3600 0.0216  -0.0527 0.0289  432 ALA A O   
3662 C CB  . ALA A 432 ? 0.3147 0.3751 0.2741 0.0233  -0.0501 0.0313  432 ALA A CB  
3663 N N   . LYS A 433 ? 0.3572 0.4198 0.3218 0.0222  -0.0506 0.0293  433 LYS A N   
3664 C CA  . LYS A 433 ? 0.2839 0.3468 0.2492 0.0213  -0.0506 0.0277  433 LYS A CA  
3665 C C   . LYS A 433 ? 0.3549 0.4197 0.3205 0.0211  -0.0525 0.0276  433 LYS A C   
3666 O O   . LYS A 433 ? 0.4400 0.5051 0.4045 0.0202  -0.0530 0.0263  433 LYS A O   
3667 C CB  . LYS A 433 ? 0.3112 0.3738 0.2800 0.0214  -0.0492 0.0274  433 LYS A CB  
3668 C CG  . LYS A 433 ? 0.3248 0.3878 0.2947 0.0206  -0.0491 0.0258  433 LYS A CG  
3669 C CD  . LYS A 433 ? 0.3709 0.4326 0.3382 0.0197  -0.0485 0.0242  433 LYS A CD  
3670 C CE  . LYS A 433 ? 0.3222 0.3843 0.2907 0.0188  -0.0485 0.0227  433 LYS A CE  
3671 N NZ  . LYS A 433 ? 0.3560 0.4172 0.3216 0.0179  -0.0483 0.0211  433 LYS A NZ  
3672 N N   . LYS A 434 ? 0.3982 0.4643 0.3652 0.0218  -0.0536 0.0291  434 LYS A N   
3673 C CA  . LYS A 434 ? 0.4649 0.5329 0.4324 0.0216  -0.0554 0.0291  434 LYS A CA  
3674 C C   . LYS A 434 ? 0.4251 0.4933 0.3892 0.0210  -0.0567 0.0285  434 LYS A C   
3675 O O   . LYS A 434 ? 0.4805 0.5499 0.4445 0.0204  -0.0578 0.0278  434 LYS A O   
3676 C CB  . LYS A 434 ? 0.4526 0.5220 0.4221 0.0225  -0.0562 0.0309  434 LYS A CB  
3677 C CG  . LYS A 434 ? 0.4397 0.5095 0.4131 0.0229  -0.0554 0.0314  434 LYS A CG  
3678 C CD  . LYS A 434 ? 0.4634 0.5342 0.4383 0.0239  -0.0561 0.0333  434 LYS A CD  
3679 C CE  . LYS A 434 ? 0.4917 0.5627 0.4705 0.0245  -0.0551 0.0338  434 LYS A CE  
3680 N NZ  . LYS A 434 ? 0.5076 0.5792 0.4876 0.0255  -0.0555 0.0358  434 LYS A NZ  
3681 N N   . LYS A 435 ? 0.4257 0.4929 0.3868 0.0212  -0.0565 0.0289  435 LYS A N   
3682 C CA  . LYS A 435 ? 0.4321 0.4993 0.3896 0.0206  -0.0576 0.0283  435 LYS A CA  
3683 C C   . LYS A 435 ? 0.4186 0.4840 0.3735 0.0201  -0.0565 0.0272  435 LYS A C   
3684 O O   . LYS A 435 ? 0.4263 0.4913 0.3780 0.0199  -0.0571 0.0271  435 LYS A O   
3685 C CB  . LYS A 435 ? 0.4960 0.5639 0.4521 0.0213  -0.0589 0.0298  435 LYS A CB  
3686 C CG  . LYS A 435 ? 0.5547 0.6215 0.5103 0.0221  -0.0580 0.0311  435 LYS A CG  
3687 C CD  . LYS A 435 ? 0.5989 0.6666 0.5533 0.0227  -0.0593 0.0326  435 LYS A CD  
3688 C CE  . LYS A 435 ? 0.6191 0.6885 0.5767 0.0233  -0.0601 0.0339  435 LYS A CE  
3689 N NZ  . LYS A 435 ? 0.6262 0.6949 0.5866 0.0240  -0.0587 0.0346  435 LYS A NZ  
3690 N N   . ALA A 436 ? 0.4164 0.4375 0.2949 0.0028  -0.0265 -0.0223 436 ALA A N   
3691 C CA  . ALA A 436 ? 0.3886 0.4075 0.2665 0.0032  -0.0265 -0.0223 436 ALA A CA  
3692 C C   . ALA A 436 ? 0.4462 0.4629 0.3226 0.0021  -0.0250 -0.0236 436 ALA A C   
3693 O O   . ALA A 436 ? 0.5290 0.5441 0.4048 0.0012  -0.0242 -0.0248 436 ALA A O   
3694 C CB  . ALA A 436 ? 0.3229 0.3393 0.2013 0.0040  -0.0274 -0.0226 436 ALA A CB  
3695 N N   . LYS A 437 ? 0.4449 0.4613 0.3207 0.0023  -0.0246 -0.0232 437 LYS A N   
3696 C CA  . LYS A 437 ? 0.5049 0.5192 0.3793 0.0013  -0.0232 -0.0242 437 LYS A CA  
3697 C C   . LYS A 437 ? 0.4968 0.5080 0.3706 0.0015  -0.0231 -0.0246 437 LYS A C   
3698 O O   . LYS A 437 ? 0.5517 0.5606 0.4243 0.0006  -0.0219 -0.0256 437 LYS A O   
3699 C CB  . LYS A 437 ? 0.5897 0.6065 0.4638 0.0012  -0.0227 -0.0235 437 LYS A CB  
3700 C CG  . LYS A 437 ? 0.7563 0.7730 0.6303 0.0020  -0.0229 -0.0226 437 LYS A CG  
3701 C CD  . LYS A 437 ? 0.8586 0.8783 0.7327 0.0022  -0.0227 -0.0215 437 LYS A CD  
3702 C CE  . LYS A 437 ? 0.9303 0.9497 0.8043 0.0030  -0.0231 -0.0206 437 LYS A CE  
3703 N NZ  . LYS A 437 ? 0.9781 0.9979 0.8512 0.0026  -0.0221 -0.0205 437 LYS A NZ  
3704 N N   . ASN A 438 ? 0.4521 0.4631 0.3266 0.0027  -0.0242 -0.0238 438 ASN A N   
3705 C CA  . ASN A 438 ? 0.4140 0.4222 0.2880 0.0031  -0.0241 -0.0240 438 ASN A CA  
3706 C C   . ASN A 438 ? 0.3742 0.3812 0.2492 0.0044  -0.0255 -0.0235 438 ASN A C   
3707 O O   . ASN A 438 ? 0.3723 0.3807 0.2483 0.0051  -0.0266 -0.0230 438 ASN A O   
3708 C CB  . ASN A 438 ? 0.4124 0.4219 0.2859 0.0034  -0.0238 -0.0231 438 ASN A CB  
3709 C CG  . ASN A 438 ? 0.5125 0.5243 0.3871 0.0049  -0.0252 -0.0214 438 ASN A CG  
3710 O OD1 . ASN A 438 ? 0.6896 0.6995 0.5653 0.0058  -0.0259 -0.0206 438 ASN A OD1 
3711 N ND2 . ASN A 438 ? 0.5686 0.5841 0.4438 0.0049  -0.0254 -0.0204 438 ASN A ND2 
3712 N N   . ASP A 439 ? 0.4606 0.4647 0.3352 0.0050  -0.0256 -0.0237 439 ASP A N   
3713 C CA  . ASP A 439 ? 0.4055 0.4073 0.2808 0.0062  -0.0269 -0.0234 439 ASP A CA  
3714 C C   . ASP A 439 ? 0.3965 0.3995 0.2748 0.0071  -0.0279 -0.0212 439 ASP A C   
3715 O O   . ASP A 439 ? 0.4001 0.4011 0.2801 0.0078  -0.0287 -0.0206 439 ASP A O   
3716 C CB  . ASP A 439 ? 0.4048 0.4027 0.2794 0.0062  -0.0264 -0.0242 439 ASP A CB  
3717 C CG  . ASP A 439 ? 0.5263 0.5225 0.4008 0.0048  -0.0251 -0.0258 439 ASP A CG  
3718 O OD1 . ASP A 439 ? 0.4988 0.4962 0.3736 0.0041  -0.0249 -0.0264 439 ASP A OD1 
3719 O OD2 . ASP A 439 ? 0.5695 0.5632 0.4436 0.0045  -0.0244 -0.0266 439 ASP A OD2 
3720 N N   . TYR A 440 ? 0.3699 0.3762 0.2489 0.0071  -0.0278 -0.0199 440 TYR A N   
3721 C CA  . TYR A 440 ? 0.3541 0.3618 0.2360 0.0079  -0.0288 -0.0178 440 TYR A CA  
3722 C C   . TYR A 440 ? 0.3391 0.3479 0.2226 0.0082  -0.0297 -0.0175 440 TYR A C   
3723 O O   . TYR A 440 ? 0.2882 0.2972 0.1743 0.0090  -0.0307 -0.0159 440 TYR A O   
3724 C CB  . TYR A 440 ? 0.3042 0.3153 0.1865 0.0079  -0.0284 -0.0165 440 TYR A CB  
3725 C CG  . TYR A 440 ? 0.3617 0.3716 0.2442 0.0082  -0.0281 -0.0157 440 TYR A CG  
3726 C CD1 . TYR A 440 ? 0.4457 0.4544 0.3306 0.0091  -0.0290 -0.0141 440 TYR A CD1 
3727 C CD2 . TYR A 440 ? 0.4348 0.4448 0.3150 0.0076  -0.0270 -0.0165 440 TYR A CD2 
3728 C CE1 . TYR A 440 ? 0.5072 0.5148 0.3924 0.0094  -0.0287 -0.0133 440 TYR A CE1 
3729 C CE2 . TYR A 440 ? 0.4333 0.4422 0.3137 0.0079  -0.0268 -0.0158 440 TYR A CE2 
3730 C CZ  . TYR A 440 ? 0.5283 0.5361 0.4112 0.0088  -0.0276 -0.0142 440 TYR A CZ  
3731 O OH  . TYR A 440 ? 0.5843 0.5910 0.4674 0.0091  -0.0273 -0.0134 440 TYR A OH  
3732 N N   . ILE A 441 ? 0.2640 0.2732 0.1459 0.0075  -0.0294 -0.0190 441 ILE A N   
3733 C CA  . ILE A 441 ? 0.2816 0.2912 0.1649 0.0078  -0.0303 -0.0189 441 ILE A CA  
3734 C C   . ILE A 441 ? 0.3535 0.3595 0.2379 0.0085  -0.0310 -0.0190 441 ILE A C   
3735 O O   . ILE A 441 ? 0.2958 0.3019 0.1823 0.0091  -0.0320 -0.0181 441 ILE A O   
3736 C CB  . ILE A 441 ? 0.2878 0.2984 0.1691 0.0069  -0.0298 -0.0206 441 ILE A CB  
3737 C CG1 . ILE A 441 ? 0.2530 0.2651 0.1359 0.0072  -0.0307 -0.0201 441 ILE A CG1 
3738 C CG2 . ILE A 441 ? 0.2944 0.3018 0.1733 0.0065  -0.0291 -0.0226 441 ILE A CG2 
3739 C CD1 . ILE A 441 ? 0.2729 0.2888 0.1575 0.0075  -0.0311 -0.0183 441 ILE A CD1 
3740 N N   . LEU A 442 ? 0.3288 0.3316 0.2117 0.0084  -0.0305 -0.0201 442 LEU A N   
3741 C CA  . LEU A 442 ? 0.3154 0.3148 0.1994 0.0090  -0.0312 -0.0202 442 LEU A CA  
3742 C C   . LEU A 442 ? 0.2756 0.2749 0.1624 0.0100  -0.0320 -0.0182 442 LEU A C   
3743 O O   . LEU A 442 ? 0.2649 0.2628 0.1536 0.0107  -0.0330 -0.0176 442 LEU A O   
3744 C CB  . LEU A 442 ? 0.2792 0.2753 0.1608 0.0087  -0.0303 -0.0218 442 LEU A CB  
3745 C CG  . LEU A 442 ? 0.2894 0.2853 0.1682 0.0077  -0.0294 -0.0239 442 LEU A CG  
3746 C CD1 . LEU A 442 ? 0.3159 0.3085 0.1929 0.0074  -0.0286 -0.0253 442 LEU A CD1 
3747 C CD2 . LEU A 442 ? 0.2482 0.2442 0.1274 0.0077  -0.0300 -0.0246 442 LEU A CD2 
3748 N N   . VAL A 443 ? 0.2827 0.2832 0.1696 0.0100  -0.0316 -0.0171 443 VAL A N   
3749 C CA  . VAL A 443 ? 0.2860 0.2866 0.1757 0.0109  -0.0324 -0.0152 443 VAL A CA  
3750 C C   . VAL A 443 ? 0.3096 0.3124 0.2019 0.0114  -0.0334 -0.0137 443 VAL A C   
3751 O O   . VAL A 443 ? 0.2839 0.2856 0.1786 0.0123  -0.0344 -0.0126 443 VAL A O   
3752 C CB  . VAL A 443 ? 0.3521 0.3543 0.2414 0.0107  -0.0317 -0.0143 443 VAL A CB  
3753 C CG1 . VAL A 443 ? 0.2576 0.2600 0.1497 0.0117  -0.0324 -0.0122 443 VAL A CG1 
3754 C CG2 . VAL A 443 ? 0.3483 0.3482 0.2350 0.0102  -0.0306 -0.0157 443 VAL A CG2 
3755 N N   . ALA A 444 ? 0.2772 0.2832 0.1690 0.0109  -0.0332 -0.0138 444 ALA A N   
3756 C CA  . ALA A 444 ? 0.2552 0.2636 0.1494 0.0114  -0.0341 -0.0124 444 ALA A CA  
3757 C C   . ALA A 444 ? 0.2618 0.2687 0.1569 0.0117  -0.0350 -0.0130 444 ALA A C   
3758 O O   . ALA A 444 ? 0.2006 0.2089 0.0980 0.0122  -0.0359 -0.0117 444 ALA A O   
3759 C CB  . ALA A 444 ? 0.2718 0.2839 0.1650 0.0107  -0.0337 -0.0124 444 ALA A CB  
3760 N N   . GLU A 445 ? 0.2282 0.2323 0.1215 0.0114  -0.0347 -0.0148 445 GLU A N   
3761 C CA  . GLU A 445 ? 0.2418 0.2442 0.1359 0.0117  -0.0355 -0.0153 445 GLU A CA  
3762 C C   . GLU A 445 ? 0.3003 0.2998 0.1964 0.0127  -0.0363 -0.0146 445 GLU A C   
3763 O O   . GLU A 445 ? 0.2442 0.2423 0.1413 0.0131  -0.0371 -0.0149 445 GLU A O   
3764 C CB  . GLU A 445 ? 0.3027 0.3034 0.1940 0.0110  -0.0348 -0.0176 445 GLU A CB  
3765 C CG  . GLU A 445 ? 0.2950 0.2986 0.1846 0.0101  -0.0341 -0.0183 445 GLU A CG  
3766 C CD  . GLU A 445 ? 0.3718 0.3740 0.2583 0.0093  -0.0331 -0.0205 445 GLU A CD  
3767 O OE1 . GLU A 445 ? 0.3521 0.3509 0.2378 0.0094  -0.0329 -0.0214 445 GLU A OE1 
3768 O OE2 . GLU A 445 ? 0.3474 0.3518 0.2323 0.0085  -0.0325 -0.0213 445 GLU A OE2 
3769 N N   . GLY A 446 ? 0.2242 0.2232 0.1211 0.0130  -0.0363 -0.0136 446 GLY A N   
3770 C CA  . GLY A 446 ? 0.2167 0.2131 0.1156 0.0139  -0.0371 -0.0128 446 GLY A CA  
3771 C C   . GLY A 446 ? 0.2624 0.2598 0.1644 0.0147  -0.0383 -0.0114 446 GLY A C   
3772 O O   . GLY A 446 ? 0.2749 0.2756 0.1781 0.0147  -0.0385 -0.0102 446 GLY A O   
3773 N N   . SER A 447 ? 0.2258 0.2206 0.1293 0.0154  -0.0392 -0.0114 447 SER A N   
3774 C CA  . SER A 447 ? 0.1767 0.1722 0.0831 0.0161  -0.0404 -0.0103 447 SER A CA  
3775 C C   . SER A 447 ? 0.2578 0.2552 0.1669 0.0167  -0.0409 -0.0080 447 SER A C   
3776 O O   . SER A 447 ? 0.2143 0.2139 0.1256 0.0171  -0.0416 -0.0068 447 SER A O   
3777 C CB  . SER A 447 ? 0.1973 0.1893 0.1045 0.0168  -0.0412 -0.0109 447 SER A CB  
3778 O OG  . SER A 447 ? 0.2370 0.2267 0.1451 0.0173  -0.0413 -0.0104 447 SER A OG  
3779 N N   . ASP A 448 ? 0.2333 0.2301 0.1424 0.0169  -0.0405 -0.0074 448 ASP A N   
3780 C CA  . ASP A 448 ? 0.2175 0.2156 0.1294 0.0175  -0.0410 -0.0052 448 ASP A CA  
3781 C C   . ASP A 448 ? 0.2142 0.2165 0.1270 0.0173  -0.0410 -0.0040 448 ASP A C   
3782 O O   . ASP A 448 ? 0.2493 0.2530 0.1649 0.0180  -0.0418 -0.0022 448 ASP A O   
3783 C CB  . ASP A 448 ? 0.2064 0.2033 0.1177 0.0175  -0.0404 -0.0050 448 ASP A CB  
3784 C CG  . ASP A 448 ? 0.2631 0.2560 0.1731 0.0176  -0.0403 -0.0064 448 ASP A CG  
3785 O OD1 . ASP A 448 ? 0.2193 0.2112 0.1265 0.0169  -0.0395 -0.0082 448 ASP A OD1 
3786 O OD2 . ASP A 448 ? 0.2364 0.2274 0.1485 0.0184  -0.0410 -0.0057 448 ASP A OD2 
3787 N N   . TRP A 449 ? 0.1727 0.1769 0.0831 0.0165  -0.0400 -0.0048 449 TRP A N   
3788 C CA  . TRP A 449 ? 0.2048 0.2129 0.1157 0.0163  -0.0399 -0.0036 449 TRP A CA  
3789 C C   . TRP A 449 ? 0.2600 0.2696 0.1730 0.0166  -0.0409 -0.0030 449 TRP A C   
3790 O O   . TRP A 449 ? 0.2317 0.2440 0.1468 0.0170  -0.0413 -0.0013 449 TRP A O   
3791 C CB  . TRP A 449 ? 0.2616 0.2714 0.1695 0.0153  -0.0388 -0.0049 449 TRP A CB  
3792 C CG  . TRP A 449 ? 0.2714 0.2793 0.1770 0.0148  -0.0378 -0.0059 449 TRP A CG  
3793 C CD1 . TRP A 449 ? 0.2199 0.2260 0.1225 0.0141  -0.0371 -0.0080 449 TRP A CD1 
3794 C CD2 . TRP A 449 ? 0.1742 0.1815 0.0802 0.0151  -0.0375 -0.0050 449 TRP A CD2 
3795 N NE1 . TRP A 449 ? 0.2127 0.2172 0.1138 0.0139  -0.0363 -0.0084 449 TRP A NE1 
3796 C CE2 . TRP A 449 ? 0.1852 0.1904 0.0883 0.0145  -0.0366 -0.0066 449 TRP A CE2 
3797 C CE3 . TRP A 449 ? 0.1973 0.2057 0.1058 0.0158  -0.0380 -0.0029 449 TRP A CE3 
3798 C CZ2 . TRP A 449 ? 0.1755 0.1798 0.0783 0.0146  -0.0361 -0.0062 449 TRP A CZ2 
3799 C CZ3 . TRP A 449 ? 0.2303 0.2377 0.1383 0.0159  -0.0374 -0.0025 449 TRP A CZ3 
3800 C CH2 . TRP A 449 ? 0.1887 0.1940 0.0939 0.0153  -0.0365 -0.0042 449 TRP A CH2 
3801 N N   . PHE A 450 ? 0.2481 0.2559 0.1604 0.0165  -0.0412 -0.0044 450 PHE A N   
3802 C CA  . PHE A 450 ? 0.2709 0.2800 0.1849 0.0168  -0.0421 -0.0040 450 PHE A CA  
3803 C C   . PHE A 450 ? 0.2996 0.3075 0.2169 0.0179  -0.0433 -0.0026 450 PHE A C   
3804 O O   . PHE A 450 ? 0.2987 0.3084 0.2182 0.0182  -0.0441 -0.0016 450 PHE A O   
3805 C CB  . PHE A 450 ? 0.2423 0.2501 0.1542 0.0163  -0.0420 -0.0060 450 PHE A CB  
3806 C CG  . PHE A 450 ? 0.2822 0.2911 0.1908 0.0152  -0.0408 -0.0074 450 PHE A CG  
3807 C CD1 . PHE A 450 ? 0.2077 0.2200 0.1158 0.0148  -0.0405 -0.0073 450 PHE A CD1 
3808 C CD2 . PHE A 450 ? 0.3242 0.3309 0.2304 0.0148  -0.0399 -0.0088 450 PHE A CD2 
3809 C CE1 . PHE A 450 ? 0.1894 0.2028 0.0946 0.0138  -0.0394 -0.0086 450 PHE A CE1 
3810 C CE2 . PHE A 450 ? 0.2883 0.2961 0.1916 0.0138  -0.0388 -0.0101 450 PHE A CE2 
3811 C CZ  . PHE A 450 ? 0.2549 0.2660 0.1577 0.0133  -0.0386 -0.0100 450 PHE A CZ  
3812 N N   . TRP A 451 ? 0.2480 0.2530 0.1659 0.0183  -0.0435 -0.0026 451 TRP A N   
3813 C CA  . TRP A 451 ? 0.2881 0.2919 0.2092 0.0193  -0.0446 -0.0013 451 TRP A CA  
3814 C C   . TRP A 451 ? 0.3642 0.3709 0.2878 0.0197  -0.0448 0.0010  451 TRP A C   
3815 O O   . TRP A 451 ? 0.2874 0.2950 0.2138 0.0204  -0.0458 0.0023  451 TRP A O   
3816 C CB  . TRP A 451 ? 0.2353 0.2355 0.1562 0.0197  -0.0446 -0.0018 451 TRP A CB  
3817 C CG  . TRP A 451 ? 0.3900 0.3889 0.3142 0.0207  -0.0456 -0.0004 451 TRP A CG  
3818 C CD1 . TRP A 451 ? 0.4156 0.4153 0.3420 0.0212  -0.0458 0.0014  451 TRP A CD1 
3819 C CD2 . TRP A 451 ? 0.4301 0.4268 0.3559 0.0214  -0.0467 -0.0007 451 TRP A CD2 
3820 N NE1 . TRP A 451 ? 0.4076 0.4056 0.3368 0.0221  -0.0469 0.0022  451 TRP A NE1 
3821 C CE2 . TRP A 451 ? 0.4783 0.4745 0.4073 0.0222  -0.0475 0.0009  451 TRP A CE2 
3822 C CE3 . TRP A 451 ? 0.3474 0.3424 0.2723 0.0213  -0.0470 -0.0022 451 TRP A CE3 
3823 C CZ2 . TRP A 451 ? 0.4678 0.4620 0.3991 0.0231  -0.0486 0.0011  451 TRP A CZ2 
3824 C CZ3 . TRP A 451 ? 0.4083 0.4013 0.3354 0.0221  -0.0481 -0.0021 451 TRP A CZ3 
3825 C CH2 . TRP A 451 ? 0.4701 0.4626 0.4003 0.0230  -0.0489 -0.0004 451 TRP A CH2 
3826 N N   . TRP A 452 ? 0.2900 0.2980 0.2126 0.0194  -0.0440 0.0015  452 TRP A N   
3827 C CA  . TRP A 452 ? 0.2825 0.2929 0.2075 0.0199  -0.0442 0.0037  452 TRP A CA  
3828 C C   . TRP A 452 ? 0.3380 0.3523 0.2634 0.0196  -0.0442 0.0045  452 TRP A C   
3829 O O   . TRP A 452 ? 0.3538 0.3701 0.2819 0.0202  -0.0447 0.0065  452 TRP A O   
3830 C CB  . TRP A 452 ? 0.3106 0.3209 0.2343 0.0197  -0.0433 0.0040  452 TRP A CB  
3831 C CG  . TRP A 452 ? 0.3473 0.3540 0.2711 0.0200  -0.0434 0.0034  452 TRP A CG  
3832 C CD1 . TRP A 452 ? 0.3539 0.3582 0.2748 0.0195  -0.0426 0.0018  452 TRP A CD1 
3833 C CD2 . TRP A 452 ? 0.4353 0.4401 0.3619 0.0209  -0.0443 0.0045  452 TRP A CD2 
3834 N NE1 . TRP A 452 ? 0.4064 0.4076 0.3283 0.0200  -0.0429 0.0018  452 TRP A NE1 
3835 C CE2 . TRP A 452 ? 0.4248 0.4263 0.3502 0.0209  -0.0440 0.0035  452 TRP A CE2 
3836 C CE3 . TRP A 452 ? 0.5105 0.5162 0.4407 0.0218  -0.0453 0.0063  452 TRP A CE3 
3837 C CZ2 . TRP A 452 ? 0.5280 0.5269 0.4555 0.0218  -0.0447 0.0041  452 TRP A CZ2 
3838 C CZ3 . TRP A 452 ? 0.5267 0.5299 0.4591 0.0226  -0.0461 0.0069  452 TRP A CZ3 
3839 C CH2 . TRP A 452 ? 0.5664 0.5663 0.4974 0.0226  -0.0458 0.0058  452 TRP A CH2 
3840 N N   . GLN A 453 ? 0.3460 0.3615 0.2689 0.0188  -0.0436 0.0031  453 GLN A N   
3841 C CA  . GLN A 453 ? 0.4284 0.4476 0.3515 0.0186  -0.0435 0.0038  453 GLN A CA  
3842 C C   . GLN A 453 ? 0.4569 0.4770 0.3831 0.0192  -0.0447 0.0050  453 GLN A C   
3843 O O   . GLN A 453 ? 0.4220 0.4399 0.3486 0.0195  -0.0454 0.0042  453 GLN A O   
3844 C CB  . GLN A 453 ? 0.3911 0.4109 0.3110 0.0176  -0.0428 0.0019  453 GLN A CB  
3845 C CG  . GLN A 453 ? 0.4440 0.4675 0.3642 0.0173  -0.0428 0.0024  453 GLN A CG  
3846 C CD  . GLN A 453 ? 0.4788 0.5057 0.3988 0.0171  -0.0422 0.0037  453 GLN A CD  
3847 O OE1 . GLN A 453 ? 0.4165 0.4434 0.3374 0.0175  -0.0420 0.0048  453 GLN A OE1 
3848 N NE2 . GLN A 453 ? 0.4356 0.4655 0.3546 0.0166  -0.0419 0.0035  453 GLN A NE2 
3849 N N   . GLY A 454 ? 0.5382 0.5612 0.4665 0.0196  -0.0449 0.0069  454 GLY A N   
3850 C CA  . GLY A 454 ? 0.6805 0.7046 0.6117 0.0203  -0.0460 0.0082  454 GLY A CA  
3851 C C   . GLY A 454 ? 0.8099 0.8331 0.7445 0.0212  -0.0468 0.0100  454 GLY A C   
3852 O O   . GLY A 454 ? 0.8736 0.8987 0.8109 0.0218  -0.0475 0.0116  454 GLY A O   
3853 N N   . GLU A 455 ? 0.8245 0.8447 0.7590 0.0215  -0.0468 0.0097  455 GLU A N   
3854 C CA  . GLU A 455 ? 0.8345 0.8534 0.7722 0.0224  -0.0476 0.0112  455 GLU A CA  
3855 C C   . GLU A 455 ? 0.8368 0.8581 0.7758 0.0227  -0.0472 0.0131  455 GLU A C   
3856 O O   . GLU A 455 ? 0.8370 0.8576 0.7746 0.0224  -0.0465 0.0130  455 GLU A O   
3857 C CB  . GLU A 455 ? 0.7850 0.7999 0.7221 0.0226  -0.0476 0.0100  455 GLU A CB  
3858 C CG  . GLU A 455 ? 0.7873 0.7999 0.7225 0.0222  -0.0478 0.0079  455 GLU A CG  
3859 C CD  . GLU A 455 ? 0.8160 0.8286 0.7533 0.0227  -0.0489 0.0081  455 GLU A CD  
3860 O OE1 . GLU A 455 ? 0.8538 0.8668 0.7944 0.0235  -0.0497 0.0098  455 GLU A OE1 
3861 O OE2 . GLU A 455 ? 0.8234 0.8356 0.7591 0.0223  -0.0488 0.0066  455 GLU A OE2 
3862 N N   . GLU A 456 ? 0.8775 0.9014 0.8191 0.0231  -0.0478 0.0149  456 GLU A N   
3863 C CA  . GLU A 456 ? 0.8724 0.8991 0.8149 0.0233  -0.0473 0.0167  456 GLU A CA  
3864 C C   . GLU A 456 ? 0.8501 0.8755 0.7948 0.0240  -0.0476 0.0182  456 GLU A C   
3865 O O   . GLU A 456 ? 0.7864 0.8136 0.7313 0.0240  -0.0470 0.0193  456 GLU A O   
3866 C CB  . GLU A 456 ? 0.8796 0.9099 0.8240 0.0235  -0.0477 0.0182  456 GLU A CB  
3867 C CG  . GLU A 456 ? 0.9235 0.9554 0.8659 0.0228  -0.0475 0.0169  456 GLU A CG  
3868 C CD  . GLU A 456 ? 0.9505 0.9844 0.8897 0.0220  -0.0463 0.0162  456 GLU A CD  
3869 O OE1 . GLU A 456 ? 0.9589 0.9927 0.8973 0.0219  -0.0456 0.0165  456 GLU A OE1 
3870 O OE2 . GLU A 456 ? 0.9363 0.9721 0.8740 0.0214  -0.0461 0.0153  456 GLU A OE2 
3871 N N   . LYS A 457 ? 0.8662 0.8887 0.8128 0.0246  -0.0484 0.0181  457 LYS A N   
3872 C CA  . LYS A 457 ? 0.8725 0.8935 0.8212 0.0253  -0.0487 0.0193  457 LYS A CA  
3873 C C   . LYS A 457 ? 0.8932 0.9106 0.8400 0.0251  -0.0483 0.0178  457 LYS A C   
3874 O O   . LYS A 457 ? 0.9354 0.9514 0.8835 0.0256  -0.0484 0.0186  457 LYS A O   
3875 C CB  . LYS A 457 ? 0.8699 0.8904 0.8225 0.0262  -0.0499 0.0207  457 LYS A CB  
3876 C CG  . LYS A 457 ? 0.8375 0.8574 0.7929 0.0270  -0.0502 0.0224  457 LYS A CG  
3877 C CD  . LYS A 457 ? 0.7717 0.7890 0.7300 0.0278  -0.0514 0.0227  457 LYS A CD  
3878 C CE  . LYS A 457 ? 0.6669 0.6814 0.6259 0.0282  -0.0515 0.0228  457 LYS A CE  
3879 N NZ  . LYS A 457 ? 0.6514 0.6637 0.6136 0.0290  -0.0527 0.0232  457 LYS A NZ  
3880 N N   . ALA A 458 ? 0.8526 0.8685 0.7963 0.0244  -0.0479 0.0156  458 ALA A N   
3881 C CA  . ALA A 458 ? 0.8189 0.8316 0.7606 0.0242  -0.0474 0.0142  458 ALA A CA  
3882 C C   . ALA A 458 ? 0.8120 0.8254 0.7525 0.0239  -0.0464 0.0147  458 ALA A C   
3883 O O   . ALA A 458 ? 0.7896 0.8062 0.7294 0.0236  -0.0458 0.0154  458 ALA A O   
3884 C CB  . ALA A 458 ? 0.7864 0.7978 0.7249 0.0234  -0.0470 0.0118  458 ALA A CB  
3885 N N   . PRO A 459 ? 0.7641 0.7748 0.7043 0.0241  -0.0463 0.0143  459 PRO A N   
3886 C CA  . PRO A 459 ? 0.6916 0.7029 0.6311 0.0240  -0.0455 0.0151  459 PRO A CA  
3887 C C   . PRO A 459 ? 0.5254 0.5377 0.4611 0.0230  -0.0442 0.0138  459 PRO A C   
3888 O O   . PRO A 459 ? 0.5034 0.5138 0.4366 0.0224  -0.0439 0.0118  459 PRO A O   
3889 C CB  . PRO A 459 ? 0.7232 0.7310 0.6634 0.0244  -0.0457 0.0149  459 PRO A CB  
3890 C CG  . PRO A 459 ? 0.7396 0.7445 0.6788 0.0243  -0.0462 0.0130  459 PRO A CG  
3891 C CD  . PRO A 459 ? 0.7797 0.7866 0.7203 0.0244  -0.0469 0.0133  459 PRO A CD  
3892 N N   . PHE A 460 ? 0.3077 0.3231 0.2432 0.0228  -0.0436 0.0150  460 PHE A N   
3893 C CA  . PHE A 460 ? 0.2418 0.2584 0.1740 0.0219  -0.0424 0.0139  460 PHE A CA  
3894 C C   . PHE A 460 ? 0.3232 0.3406 0.2529 0.0212  -0.0421 0.0123  460 PHE A C   
3895 O O   . PHE A 460 ? 0.3229 0.3398 0.2494 0.0204  -0.0412 0.0107  460 PHE A O   
3896 C CB  . PHE A 460 ? 0.3131 0.3267 0.2434 0.0217  -0.0418 0.0128  460 PHE A CB  
3897 C CG  . PHE A 460 ? 0.4026 0.4152 0.3351 0.0224  -0.0420 0.0144  460 PHE A CG  
3898 C CD1 . PHE A 460 ? 0.4104 0.4255 0.3439 0.0226  -0.0417 0.0162  460 PHE A CD1 
3899 C CD2 . PHE A 460 ? 0.5330 0.5421 0.4666 0.0229  -0.0426 0.0140  460 PHE A CD2 
3900 C CE1 . PHE A 460 ? 0.5003 0.5145 0.4359 0.0233  -0.0419 0.0176  460 PHE A CE1 
3901 C CE2 . PHE A 460 ? 0.5524 0.5605 0.4880 0.0236  -0.0428 0.0154  460 PHE A CE2 
3902 C CZ  . PHE A 460 ? 0.5320 0.5427 0.4687 0.0238  -0.0425 0.0172  460 PHE A CZ  
3903 N N   . VAL A 461 ? 0.3621 0.3808 0.2933 0.0214  -0.0429 0.0126  461 VAL A N   
3904 C CA  . VAL A 461 ? 0.4241 0.4437 0.3532 0.0207  -0.0426 0.0111  461 VAL A CA  
3905 C C   . VAL A 461 ? 0.4079 0.4303 0.3345 0.0199  -0.0415 0.0108  461 VAL A C   
3906 O O   . VAL A 461 ? 0.3924 0.4147 0.3162 0.0191  -0.0409 0.0090  461 VAL A O   
3907 C CB  . VAL A 461 ? 0.4335 0.4545 0.3649 0.0211  -0.0436 0.0118  461 VAL A CB  
3908 C CG1 . VAL A 461 ? 0.5086 0.5264 0.4414 0.0216  -0.0445 0.0113  461 VAL A CG1 
3909 C CG2 . VAL A 461 ? 0.4662 0.4902 0.4004 0.0216  -0.0439 0.0142  461 VAL A CG2 
3910 N N   . GLU A 462 ? 0.2840 0.3090 0.2116 0.0201  -0.0413 0.0125  462 GLU A N   
3911 C CA  . GLU A 462 ? 0.3901 0.4178 0.3154 0.0194  -0.0402 0.0122  462 GLU A CA  
3912 C C   . GLU A 462 ? 0.2742 0.3001 0.1963 0.0188  -0.0393 0.0105  462 GLU A C   
3913 O O   . GLU A 462 ? 0.3037 0.3310 0.2231 0.0180  -0.0384 0.0094  462 GLU A O   
3914 C CB  . GLU A 462 ? 0.4816 0.5123 0.4086 0.0199  -0.0401 0.0144  462 GLU A CB  
3915 C CG  . GLU A 462 ? 0.5800 0.6121 0.5106 0.0207  -0.0411 0.0163  462 GLU A CG  
3916 C CD  . GLU A 462 ? 0.7073 0.7435 0.6389 0.0209  -0.0409 0.0181  462 GLU A CD  
3917 O OE1 . GLU A 462 ? 0.7503 0.7875 0.6812 0.0208  -0.0402 0.0188  462 GLU A OE1 
3918 O OE2 . GLU A 462 ? 0.7139 0.7523 0.6470 0.0211  -0.0414 0.0189  462 GLU A OE2 
3919 N N   . VAL A 463 ? 0.2459 0.2686 0.1682 0.0191  -0.0393 0.0104  463 VAL A N   
3920 C CA  . VAL A 463 ? 0.2255 0.2462 0.1449 0.0185  -0.0384 0.0088  463 VAL A CA  
3921 C C   . VAL A 463 ? 0.2978 0.3166 0.2148 0.0178  -0.0382 0.0064  463 VAL A C   
3922 O O   . VAL A 463 ? 0.2700 0.2891 0.1840 0.0170  -0.0373 0.0050  463 VAL A O   
3923 C CB  . VAL A 463 ? 0.2775 0.2953 0.1980 0.0190  -0.0386 0.0093  463 VAL A CB  
3924 C CG1 . VAL A 463 ? 0.3033 0.3188 0.2207 0.0184  -0.0376 0.0076  463 VAL A CG1 
3925 C CG2 . VAL A 463 ? 0.2504 0.2701 0.1732 0.0196  -0.0386 0.0116  463 VAL A CG2 
3926 N N   . PHE A 464 ? 0.2060 0.2229 0.1243 0.0182  -0.0391 0.0061  464 PHE A N   
3927 C CA  . PHE A 464 ? 0.2677 0.2831 0.1840 0.0176  -0.0390 0.0040  464 PHE A CA  
3928 C C   . PHE A 464 ? 0.2344 0.2528 0.1491 0.0169  -0.0386 0.0034  464 PHE A C   
3929 O O   . PHE A 464 ? 0.2825 0.3004 0.1943 0.0161  -0.0379 0.0015  464 PHE A O   
3930 C CB  . PHE A 464 ? 0.2508 0.2641 0.1691 0.0182  -0.0402 0.0040  464 PHE A CB  
3931 C CG  . PHE A 464 ? 0.2189 0.2286 0.1380 0.0187  -0.0405 0.0038  464 PHE A CG  
3932 C CD1 . PHE A 464 ? 0.3324 0.3390 0.2492 0.0184  -0.0401 0.0019  464 PHE A CD1 
3933 C CD2 . PHE A 464 ? 0.2877 0.2971 0.2097 0.0196  -0.0411 0.0057  464 PHE A CD2 
3934 C CE1 . PHE A 464 ? 0.3514 0.3546 0.2689 0.0189  -0.0404 0.0017  464 PHE A CE1 
3935 C CE2 . PHE A 464 ? 0.3301 0.3361 0.2528 0.0201  -0.0414 0.0055  464 PHE A CE2 
3936 C CZ  . PHE A 464 ? 0.3317 0.3347 0.2522 0.0197  -0.0411 0.0035  464 PHE A CZ  
3937 N N   . ASP A 465 ? 0.2703 0.2919 0.1868 0.0172  -0.0390 0.0049  465 ASP A N   
3938 C CA  . ASP A 465 ? 0.2660 0.2907 0.1812 0.0166  -0.0386 0.0045  465 ASP A CA  
3939 C C   . ASP A 465 ? 0.2460 0.2720 0.1584 0.0158  -0.0374 0.0038  465 ASP A C   
3940 O O   . ASP A 465 ? 0.2825 0.3090 0.1922 0.0150  -0.0367 0.0022  465 ASP A O   
3941 C CB  . ASP A 465 ? 0.2539 0.2818 0.1717 0.0171  -0.0392 0.0065  465 ASP A CB  
3942 C CG  . ASP A 465 ? 0.3154 0.3468 0.2319 0.0165  -0.0388 0.0061  465 ASP A CG  
3943 O OD1 . ASP A 465 ? 0.2668 0.2979 0.1821 0.0161  -0.0389 0.0048  465 ASP A OD1 
3944 O OD2 . ASP A 465 ? 0.2546 0.2889 0.1711 0.0165  -0.0384 0.0073  465 ASP A OD2 
3945 N N   . LYS A 466 ? 0.2267 0.2532 0.1396 0.0161  -0.0370 0.0050  466 LYS A N   
3946 C CA  . LYS A 466 ? 0.2693 0.2968 0.1796 0.0155  -0.0359 0.0044  466 LYS A CA  
3947 C C   . LYS A 466 ? 0.2887 0.3134 0.1961 0.0148  -0.0352 0.0021  466 LYS A C   
3948 O O   . LYS A 466 ? 0.2790 0.3047 0.1837 0.0140  -0.0343 0.0008  466 LYS A O   
3949 C CB  . LYS A 466 ? 0.2746 0.3026 0.1861 0.0160  -0.0357 0.0061  466 LYS A CB  
3950 C CG  . LYS A 466 ? 0.2480 0.2764 0.1568 0.0153  -0.0345 0.0053  466 LYS A CG  
3951 C CD  . LYS A 466 ? 0.3869 0.4168 0.2971 0.0158  -0.0343 0.0072  466 LYS A CD  
3952 C CE  . LYS A 466 ? 0.5428 0.5728 0.4502 0.0152  -0.0332 0.0064  466 LYS A CE  
3953 N NZ  . LYS A 466 ? 0.6034 0.6363 0.5118 0.0156  -0.0328 0.0082  466 LYS A NZ  
3954 N N   . LEU A 467 ? 0.2423 0.2633 0.1501 0.0151  -0.0355 0.0017  467 LEU A N   
3955 C CA  . LEU A 467 ? 0.1961 0.2143 0.1012 0.0145  -0.0349 -0.0004 467 LEU A CA  
3956 C C   . LEU A 467 ? 0.2347 0.2529 0.1380 0.0138  -0.0348 -0.0022 467 LEU A C   
3957 O O   . LEU A 467 ? 0.2714 0.2896 0.1718 0.0130  -0.0338 -0.0038 467 LEU A O   
3958 C CB  . LEU A 467 ? 0.2013 0.2156 0.1075 0.0151  -0.0354 -0.0005 467 LEU A CB  
3959 C CG  . LEU A 467 ? 0.2073 0.2208 0.1146 0.0156  -0.0353 0.0008  467 LEU A CG  
3960 C CD1 . LEU A 467 ? 0.2106 0.2208 0.1199 0.0164  -0.0362 0.0012  467 LEU A CD1 
3961 C CD2 . LEU A 467 ? 0.2580 0.2708 0.1624 0.0149  -0.0341 -0.0004 467 LEU A CD2 
3962 N N   . PHE A 468 ? 0.2230 0.2414 0.1279 0.0142  -0.0357 -0.0020 468 PHE A N   
3963 C CA  . PHE A 468 ? 0.2549 0.2731 0.1581 0.0136  -0.0356 -0.0037 468 PHE A CA  
3964 C C   . PHE A 468 ? 0.2969 0.3184 0.1982 0.0128  -0.0348 -0.0042 468 PHE A C   
3965 O O   . PHE A 468 ? 0.2485 0.2695 0.1471 0.0120  -0.0341 -0.0060 468 PHE A O   
3966 C CB  . PHE A 468 ? 0.2324 0.2508 0.1380 0.0141  -0.0367 -0.0031 468 PHE A CB  
3967 C CG  . PHE A 468 ? 0.2900 0.3091 0.1942 0.0135  -0.0367 -0.0045 468 PHE A CG  
3968 C CD1 . PHE A 468 ? 0.2989 0.3152 0.2013 0.0132  -0.0365 -0.0064 468 PHE A CD1 
3969 C CD2 . PHE A 468 ? 0.2884 0.3111 0.1932 0.0134  -0.0368 -0.0038 468 PHE A CD2 
3970 C CE1 . PHE A 468 ? 0.3094 0.3263 0.2106 0.0126  -0.0365 -0.0077 468 PHE A CE1 
3971 C CE2 . PHE A 468 ? 0.3431 0.3665 0.2466 0.0128  -0.0368 -0.0052 468 PHE A CE2 
3972 C CZ  . PHE A 468 ? 0.2943 0.3148 0.1960 0.0125  -0.0366 -0.0071 468 PHE A CZ  
3973 N N   . ARG A 469 ? 0.2176 0.2425 0.1203 0.0130  -0.0349 -0.0025 469 ARG A N   
3974 C CA  . ARG A 469 ? 0.2576 0.2859 0.1587 0.0124  -0.0342 -0.0029 469 ARG A CA  
3975 C C   . ARG A 469 ? 0.3412 0.3694 0.2396 0.0117  -0.0331 -0.0038 469 ARG A C   
3976 O O   . ARG A 469 ? 0.3011 0.3306 0.1972 0.0109  -0.0324 -0.0052 469 ARG A O   
3977 C CB  . ARG A 469 ? 0.3213 0.3531 0.2247 0.0129  -0.0347 -0.0008 469 ARG A CB  
3978 C CG  . ARG A 469 ? 0.3031 0.3355 0.2088 0.0134  -0.0358 -0.0001 469 ARG A CG  
3979 C CD  . ARG A 469 ? 0.3141 0.3498 0.2222 0.0139  -0.0362 0.0021  469 ARG A CD  
3980 N NE  . ARG A 469 ? 0.3056 0.3419 0.2160 0.0144  -0.0373 0.0028  469 ARG A NE  
3981 C CZ  . ARG A 469 ? 0.3164 0.3546 0.2263 0.0140  -0.0374 0.0023  469 ARG A CZ  
3982 N NH1 . ARG A 469 ? 0.2597 0.2994 0.1669 0.0132  -0.0366 0.0009  469 ARG A NH1 
3983 N NH2 . ARG A 469 ? 0.3536 0.3922 0.2657 0.0145  -0.0384 0.0030  469 ARG A NH2 
3984 N N   . SER A 470 ? 0.2806 0.3073 0.1793 0.0120  -0.0329 -0.0032 470 SER A N   
3985 C CA  . SER A 470 ? 0.2536 0.2798 0.1498 0.0114  -0.0317 -0.0042 470 SER A CA  
3986 C C   . SER A 470 ? 0.3143 0.3379 0.2078 0.0107  -0.0312 -0.0066 470 SER A C   
3987 O O   . SER A 470 ? 0.2638 0.2882 0.1547 0.0099  -0.0303 -0.0079 470 SER A O   
3988 C CB  . SER A 470 ? 0.3187 0.3434 0.2159 0.0120  -0.0317 -0.0030 470 SER A CB  
3989 O OG  . SER A 470 ? 0.3753 0.4025 0.2750 0.0127  -0.0322 -0.0008 470 SER A OG  
3990 N N   . PHE A 471 ? 0.3074 0.3278 0.2015 0.0110  -0.0318 -0.0072 471 PHE A N   
3991 C CA  . PHE A 471 ? 0.2998 0.3176 0.1915 0.0104  -0.0313 -0.0094 471 PHE A CA  
3992 C C   . PHE A 471 ? 0.3133 0.3330 0.2036 0.0097  -0.0311 -0.0106 471 PHE A C   
3993 O O   . PHE A 471 ? 0.3260 0.3453 0.2136 0.0088  -0.0302 -0.0124 471 PHE A O   
3994 C CB  . PHE A 471 ? 0.2232 0.2374 0.1160 0.0109  -0.0320 -0.0097 471 PHE A CB  
3995 C CG  . PHE A 471 ? 0.2262 0.2382 0.1202 0.0115  -0.0322 -0.0087 471 PHE A CG  
3996 C CD1 . PHE A 471 ? 0.2473 0.2588 0.1397 0.0112  -0.0313 -0.0090 471 PHE A CD1 
3997 C CD2 . PHE A 471 ? 0.3045 0.3152 0.2013 0.0124  -0.0332 -0.0075 471 PHE A CD2 
3998 C CE1 . PHE A 471 ? 0.2781 0.2876 0.1716 0.0118  -0.0314 -0.0081 471 PHE A CE1 
3999 C CE2 . PHE A 471 ? 0.2459 0.2546 0.1438 0.0130  -0.0334 -0.0066 471 PHE A CE2 
4000 C CZ  . PHE A 471 ? 0.3138 0.3219 0.2101 0.0127  -0.0325 -0.0069 471 PHE A CZ  
4001 N N   . VAL A 472 ? 0.2621 0.2839 0.1543 0.0100  -0.0319 -0.0097 472 VAL A N   
4002 C CA  . VAL A 472 ? 0.2667 0.2904 0.1577 0.0094  -0.0317 -0.0107 472 VAL A CA  
4003 C C   . VAL A 472 ? 0.2817 0.3083 0.1707 0.0087  -0.0307 -0.0111 472 VAL A C   
4004 O O   . VAL A 472 ? 0.2976 0.3245 0.1843 0.0078  -0.0301 -0.0128 472 VAL A O   
4005 C CB  . VAL A 472 ? 0.2973 0.3230 0.1909 0.0099  -0.0328 -0.0093 472 VAL A CB  
4006 C CG1 . VAL A 472 ? 0.3689 0.3975 0.2615 0.0093  -0.0326 -0.0100 472 VAL A CG1 
4007 C CG2 . VAL A 472 ? 0.2637 0.2864 0.1588 0.0105  -0.0337 -0.0095 472 VAL A CG2 
4008 N N   . ARG A 473 ? 0.3674 0.3962 0.2574 0.0090  -0.0306 -0.0095 473 ARG A N   
4009 C CA  . ARG A 473 ? 0.3731 0.4047 0.2614 0.0084  -0.0297 -0.0097 473 ARG A CA  
4010 C C   . ARG A 473 ? 0.3794 0.4090 0.2649 0.0077  -0.0287 -0.0114 473 ARG A C   
4011 O O   . ARG A 473 ? 0.3717 0.4023 0.2549 0.0069  -0.0279 -0.0129 473 ARG A O   
4012 C CB  . ARG A 473 ? 0.3082 0.3424 0.1983 0.0090  -0.0299 -0.0076 473 ARG A CB  
4013 C CG  . ARG A 473 ? 0.4357 0.4727 0.3240 0.0084  -0.0290 -0.0077 473 ARG A CG  
4014 C CD  . ARG A 473 ? 0.5455 0.5855 0.4359 0.0091  -0.0292 -0.0054 473 ARG A CD  
4015 N NE  . ARG A 473 ? 0.6792 0.7227 0.5681 0.0086  -0.0285 -0.0055 473 ARG A NE  
4016 C CZ  . ARG A 473 ? 0.7976 0.8443 0.6869 0.0085  -0.0288 -0.0051 473 ARG A CZ  
4017 N NH1 . ARG A 473 ? 0.8276 0.8746 0.7187 0.0089  -0.0297 -0.0046 473 ARG A NH1 
4018 N NH2 . ARG A 473 ? 0.8397 0.8895 0.7275 0.0081  -0.0281 -0.0053 473 ARG A NH2 
4019 N N   . ARG A 474 ? 0.3524 0.3791 0.2382 0.0081  -0.0287 -0.0112 474 ARG A N   
4020 C CA  . ARG A 474 ? 0.3329 0.3575 0.2162 0.0075  -0.0277 -0.0127 474 ARG A CA  
4021 C C   . ARG A 474 ? 0.4357 0.4586 0.3168 0.0067  -0.0273 -0.0150 474 ARG A C   
4022 O O   . ARG A 474 ? 0.4316 0.4543 0.3102 0.0060  -0.0263 -0.0165 474 ARG A O   
4023 C CB  . ARG A 474 ? 0.4198 0.4413 0.3040 0.0081  -0.0279 -0.0121 474 ARG A CB  
4024 C CG  . ARG A 474 ? 0.4974 0.5168 0.3792 0.0076  -0.0269 -0.0133 474 ARG A CG  
4025 C CD  . ARG A 474 ? 0.6540 0.6762 0.5345 0.0071  -0.0260 -0.0132 474 ARG A CD  
4026 N NE  . ARG A 474 ? 0.7896 0.8100 0.6675 0.0065  -0.0250 -0.0148 474 ARG A NE  
4027 C CZ  . ARG A 474 ? 0.8659 0.8858 0.7432 0.0065  -0.0244 -0.0143 474 ARG A CZ  
4028 N NH1 . ARG A 474 ? 0.8280 0.8491 0.7073 0.0073  -0.0248 -0.0123 474 ARG A NH1 
4029 N NH2 . ARG A 474 ? 0.9363 0.9545 0.8112 0.0059  -0.0235 -0.0159 474 ARG A NH2 
4030 N N   . ALA A 475 ? 0.3750 0.3967 0.2571 0.0070  -0.0280 -0.0153 475 ALA A N   
4031 C CA  . ALA A 475 ? 0.3204 0.3402 0.2006 0.0063  -0.0277 -0.0174 475 ALA A CA  
4032 C C   . ALA A 475 ? 0.4544 0.4767 0.3326 0.0055  -0.0271 -0.0186 475 ALA A C   
4033 O O   . ALA A 475 ? 0.4359 0.4561 0.3132 0.0046  -0.0264 -0.0202 475 ALA A O   
4034 C CB  . ALA A 475 ? 0.3038 0.3221 0.1857 0.0068  -0.0288 -0.0172 475 ALA A CB  
4035 N N   . GLN A 476 ? 0.4321 0.4582 0.3108 0.0054  -0.0270 -0.0176 476 GLN A N   
4036 C CA  . GLN A 476 ? 0.4697 0.4971 0.3481 0.0043  -0.0262 -0.0183 476 GLN A CA  
4037 C C   . GLN A 476 ? 0.5255 0.5541 0.4031 0.0036  -0.0250 -0.0184 476 GLN A C   
4038 O O   . GLN A 476 ? 0.6010 0.6310 0.4785 0.0028  -0.0243 -0.0188 476 GLN A O   
4039 C CB  . GLN A 476 ? 0.4503 0.4812 0.3303 0.0047  -0.0270 -0.0172 476 GLN A CB  
4040 C CG  . GLN A 476 ? 0.4855 0.5156 0.3664 0.0053  -0.0282 -0.0172 476 GLN A CG  
4041 C CD  . GLN A 476 ? 0.5257 0.5587 0.4089 0.0060  -0.0292 -0.0154 476 GLN A CD  
4042 O OE1 . GLN A 476 ? 0.5064 0.5422 0.3896 0.0058  -0.0292 -0.0154 476 GLN A OE1 
4043 N NE2 . GLN A 476 ? 0.4840 0.5162 0.3695 0.0069  -0.0299 -0.0136 476 GLN A NE2 
4044 N N   . GLU A 477 ? 0.5517 0.5797 0.4287 0.0038  -0.0246 -0.0180 477 GLU A N   
4045 C CA  . GLU A 477 ? 0.7003 0.7302 0.5768 0.0034  -0.0238 -0.0176 477 GLU A CA  
4046 C C   . GLU A 477 ? 0.7971 0.8246 0.6721 0.0028  -0.0226 -0.0186 477 GLU A C   
4047 O O   . GLU A 477 ? 0.8359 0.8610 0.7100 0.0018  -0.0217 -0.0201 477 GLU A O   
4048 C CB  . GLU A 477 ? 0.6899 0.7228 0.5675 0.0045  -0.0245 -0.0156 477 GLU A CB  
4049 C CG  . GLU A 477 ? 0.6928 0.7241 0.5699 0.0051  -0.0246 -0.0151 477 GLU A CG  
4050 C CD  . GLU A 477 ? 0.6566 0.6901 0.5356 0.0060  -0.0252 -0.0129 477 GLU A CD  
4051 O OE1 . GLU A 477 ? 0.6049 0.6414 0.4853 0.0063  -0.0257 -0.0117 477 GLU A OE1 
4052 O OE2 . GLU A 477 ? 0.7739 0.8057 0.6532 0.0064  -0.0251 -0.0122 477 GLU A OE2 
4053 N N   . MET B 1   ? 0.8198 0.8339 0.8247 -0.0265 -0.0120 -0.0194 1   MET B N   
4054 C CA  . MET B 1   ? 0.7819 0.7949 0.7879 -0.0259 -0.0125 -0.0186 1   MET B CA  
4055 C C   . MET B 1   ? 0.6585 0.6719 0.6652 -0.0259 -0.0121 -0.0176 1   MET B C   
4056 O O   . MET B 1   ? 0.6103 0.6236 0.6184 -0.0261 -0.0112 -0.0179 1   MET B O   
4057 C CB  . MET B 1   ? 0.8785 0.8906 0.8858 -0.0258 -0.0122 -0.0195 1   MET B CB  
4058 C CG  . MET B 1   ? 0.9894 1.0005 0.9978 -0.0253 -0.0126 -0.0188 1   MET B CG  
4059 S SD  . MET B 1   ? 1.1061 1.1168 1.1137 -0.0245 -0.0141 -0.0178 1   MET B SD  
4060 C CE  . MET B 1   ? 1.0676 1.0770 1.0764 -0.0241 -0.0145 -0.0180 1   MET B CE  
4061 N N   . LYS B 2   ? 0.5253 0.5390 0.5311 -0.0257 -0.0126 -0.0165 2   LYS B N   
4062 C CA  . LYS B 2   ? 0.4112 0.4253 0.4176 -0.0257 -0.0123 -0.0155 2   LYS B CA  
4063 C C   . LYS B 2   ? 0.3355 0.3487 0.3431 -0.0251 -0.0126 -0.0149 2   LYS B C   
4064 O O   . LYS B 2   ? 0.3678 0.3804 0.3750 -0.0244 -0.0135 -0.0144 2   LYS B O   
4065 C CB  . LYS B 2   ? 0.4293 0.4441 0.4341 -0.0257 -0.0127 -0.0145 2   LYS B CB  
4066 C CG  . LYS B 2   ? 0.4796 0.4949 0.4849 -0.0258 -0.0124 -0.0134 2   LYS B CG  
4067 C CD  . LYS B 2   ? 0.5181 0.5340 0.5220 -0.0257 -0.0130 -0.0123 2   LYS B CD  
4068 C CE  . LYS B 2   ? 0.4875 0.5025 0.4908 -0.0249 -0.0140 -0.0119 2   LYS B CE  
4069 N NZ  . LYS B 2   ? 0.4470 0.4625 0.4490 -0.0249 -0.0145 -0.0109 2   LYS B NZ  
4070 N N   . LYS B 3   ? 0.2746 0.2875 0.2836 -0.0252 -0.0119 -0.0150 3   LYS B N   
4071 C CA  . LYS B 3   ? 0.1799 0.1922 0.1902 -0.0247 -0.0121 -0.0144 3   LYS B CA  
4072 C C   . LYS B 3   ? 0.1814 0.1941 0.1919 -0.0245 -0.0120 -0.0133 3   LYS B C   
4073 O O   . LYS B 3   ? 0.1573 0.1709 0.1673 -0.0250 -0.0115 -0.0129 3   LYS B O   
4074 C CB  . LYS B 3   ? 0.2180 0.2298 0.2299 -0.0249 -0.0113 -0.0152 3   LYS B CB  
4075 C CG  . LYS B 3   ? 0.2892 0.3004 0.3009 -0.0251 -0.0112 -0.0163 3   LYS B CG  
4076 C CD  . LYS B 3   ? 0.4019 0.4126 0.4128 -0.0245 -0.0124 -0.0162 3   LYS B CD  
4077 C CE  . LYS B 3   ? 0.4976 0.5075 0.5093 -0.0245 -0.0124 -0.0170 3   LYS B CE  
4078 N NZ  . LYS B 3   ? 0.5031 0.5130 0.5157 -0.0250 -0.0113 -0.0179 3   LYS B NZ  
4079 N N   . LEU B 4   ? 0.1745 0.1866 0.1856 -0.0239 -0.0125 -0.0127 4   LEU B N   
4080 C CA  . LEU B 4   ? 0.0933 0.1057 0.1050 -0.0237 -0.0122 -0.0117 4   LEU B CA  
4081 C C   . LEU B 4   ? 0.1305 0.1424 0.1440 -0.0238 -0.0116 -0.0119 4   LEU B C   
4082 O O   . LEU B 4   ? 0.2050 0.2162 0.2191 -0.0235 -0.0118 -0.0124 4   LEU B O   
4083 C CB  . LEU B 4   ? 0.1480 0.1602 0.1593 -0.0229 -0.0131 -0.0111 4   LEU B CB  
4084 C CG  . LEU B 4   ? 0.1488 0.1612 0.1605 -0.0226 -0.0130 -0.0101 4   LEU B CG  
4085 C CD1 . LEU B 4   ? 0.1821 0.1946 0.1925 -0.0220 -0.0137 -0.0095 4   LEU B CD1 
4086 C CD2 . LEU B 4   ? 0.1818 0.1937 0.1950 -0.0222 -0.0129 -0.0102 4   LEU B CD2 
4087 N N   . PHE B 5   ? 0.1380 0.1504 0.1522 -0.0242 -0.0107 -0.0116 5   PHE B N   
4088 C CA  . PHE B 5   ? 0.1624 0.1745 0.1783 -0.0243 -0.0099 -0.0117 5   PHE B CA  
4089 C C   . PHE B 5   ? 0.1933 0.2054 0.2099 -0.0238 -0.0102 -0.0107 5   PHE B C   
4090 O O   . PHE B 5   ? 0.1579 0.1706 0.1740 -0.0237 -0.0102 -0.0099 5   PHE B O   
4091 C CB  . PHE B 5   ? 0.1528 0.1655 0.1695 -0.0250 -0.0087 -0.0121 5   PHE B CB  
4092 C CG  . PHE B 5   ? 0.1779 0.1906 0.1943 -0.0254 -0.0083 -0.0133 5   PHE B CG  
4093 C CD1 . PHE B 5   ? 0.2615 0.2734 0.2782 -0.0254 -0.0083 -0.0142 5   PHE B CD1 
4094 C CD2 . PHE B 5   ? 0.1540 0.1676 0.1696 -0.0259 -0.0079 -0.0135 5   PHE B CD2 
4095 C CE1 . PHE B 5   ? 0.2279 0.2398 0.2442 -0.0257 -0.0080 -0.0155 5   PHE B CE1 
4096 C CE2 . PHE B 5   ? 0.1830 0.1967 0.1983 -0.0263 -0.0075 -0.0148 5   PHE B CE2 
4097 C CZ  . PHE B 5   ? 0.1697 0.1825 0.1854 -0.0262 -0.0075 -0.0158 5   PHE B CZ  
4098 N N   . LEU B 6   ? 0.1592 0.1706 0.1767 -0.0235 -0.0104 -0.0108 6   LEU B N   
4099 C CA  . LEU B 6   ? 0.1346 0.1461 0.1527 -0.0229 -0.0107 -0.0100 6   LEU B CA  
4100 C C   . LEU B 6   ? 0.1857 0.1970 0.2055 -0.0232 -0.0098 -0.0099 6   LEU B C   
4101 O O   . LEU B 6   ? 0.1603 0.1710 0.1807 -0.0235 -0.0093 -0.0105 6   LEU B O   
4102 C CB  . LEU B 6   ? 0.1385 0.1495 0.1562 -0.0222 -0.0117 -0.0102 6   LEU B CB  
4103 C CG  . LEU B 6   ? 0.1270 0.1380 0.1452 -0.0215 -0.0120 -0.0097 6   LEU B CG  
4104 C CD1 . LEU B 6   ? 0.1017 0.1134 0.1190 -0.0212 -0.0121 -0.0089 6   LEU B CD1 
4105 C CD2 . LEU B 6   ? 0.1570 0.1675 0.1750 -0.0209 -0.0128 -0.0102 6   LEU B CD2 
4106 N N   . VAL B 7   ? 0.1276 0.1394 0.1479 -0.0231 -0.0094 -0.0090 7   VAL B N   
4107 C CA  . VAL B 7   ? 0.1385 0.1503 0.1604 -0.0234 -0.0084 -0.0088 7   VAL B CA  
4108 C C   . VAL B 7   ? 0.1615 0.1734 0.1839 -0.0228 -0.0088 -0.0080 7   VAL B C   
4109 O O   . VAL B 7   ? 0.1472 0.1599 0.1692 -0.0226 -0.0089 -0.0072 7   VAL B O   
4110 C CB  . VAL B 7   ? 0.1499 0.1623 0.1724 -0.0239 -0.0074 -0.0086 7   VAL B CB  
4111 C CG1 . VAL B 7   ? 0.1333 0.1454 0.1576 -0.0241 -0.0061 -0.0086 7   VAL B CG1 
4112 C CG2 . VAL B 7   ? 0.1701 0.1826 0.1918 -0.0243 -0.0071 -0.0095 7   VAL B CG2 
4113 N N   . PHE B 8   ? 0.1084 0.1199 0.1316 -0.0227 -0.0089 -0.0081 8   PHE B N   
4114 C CA  . PHE B 8   ? 0.0429 0.0547 0.0668 -0.0222 -0.0090 -0.0075 8   PHE B CA  
4115 C C   . PHE B 8   ? 0.0999 0.1119 0.1252 -0.0226 -0.0079 -0.0069 8   PHE B C   
4116 O O   . PHE B 8   ? 0.1185 0.1301 0.1447 -0.0231 -0.0070 -0.0073 8   PHE B O   
4117 C CB  . PHE B 8   ? 0.0953 0.1065 0.1194 -0.0219 -0.0097 -0.0078 8   PHE B CB  
4118 C CG  . PHE B 8   ? 0.0934 0.1045 0.1164 -0.0212 -0.0107 -0.0083 8   PHE B CG  
4119 C CD1 . PHE B 8   ? 0.1258 0.1376 0.1482 -0.0205 -0.0111 -0.0083 8   PHE B CD1 
4120 C CD2 . PHE B 8   ? 0.1220 0.1325 0.1442 -0.0214 -0.0112 -0.0089 8   PHE B CD2 
4121 C CE1 . PHE B 8   ? 0.0888 0.1006 0.1100 -0.0199 -0.0119 -0.0088 8   PHE B CE1 
4122 C CE2 . PHE B 8   ? 0.1478 0.1583 0.1690 -0.0207 -0.0121 -0.0094 8   PHE B CE2 
4123 C CZ  . PHE B 8   ? 0.0845 0.0956 0.1052 -0.0200 -0.0123 -0.0094 8   PHE B CZ  
4124 N N   . TRP B 9   ? 0.0877 0.1004 0.1133 -0.0224 -0.0077 -0.0061 9   TRP B N   
4125 C CA  . TRP B 9   ? 0.1727 0.1858 0.1998 -0.0227 -0.0066 -0.0054 9   TRP B CA  
4126 C C   . TRP B 9   ? 0.0919 0.1055 0.1192 -0.0222 -0.0069 -0.0048 9   TRP B C   
4127 O O   . TRP B 9   ? 0.0791 0.0932 0.1053 -0.0218 -0.0074 -0.0040 9   TRP B O   
4128 C CB  . TRP B 9   ? 0.1410 0.1545 0.1680 -0.0229 -0.0059 -0.0049 9   TRP B CB  
4129 C CG  . TRP B 9   ? 0.1070 0.1201 0.1354 -0.0224 -0.0044 -0.0043 9   TRP B CG  
4130 C CD1 . TRP B 9   ? 0.1432 0.1559 0.1731 -0.0221 -0.0037 -0.0042 9   TRP B CD1 
4131 C CD2 . TRP B 9   ? 0.1084 0.1214 0.1368 -0.0220 -0.0036 -0.0038 9   TRP B CD2 
4132 N NE1 . TRP B 9   ? 0.1012 0.1135 0.1320 -0.0216 -0.0024 -0.0035 9   TRP B NE1 
4133 C CE2 . TRP B 9   ? 0.0677 0.0802 0.0977 -0.0215 -0.0023 -0.0033 9   TRP B CE2 
4134 C CE3 . TRP B 9   ? 0.1566 0.1701 0.1840 -0.0220 -0.0037 -0.0037 9   TRP B CE3 
4135 C CZ2 . TRP B 9   ? 0.1463 0.1587 0.1768 -0.0210 -0.0013 -0.0027 9   TRP B CZ2 
4136 C CZ3 . TRP B 9   ? 0.0831 0.0964 0.1110 -0.0215 -0.0027 -0.0031 9   TRP B CZ3 
4137 C CH2 . TRP B 9   ? 0.1009 0.1137 0.1304 -0.0210 -0.0015 -0.0027 9   TRP B CH2 
4138 N N   . TRP B 10  ? 0.0613 0.0746 0.0898 -0.0222 -0.0067 -0.0049 10  TRP B N   
4139 C CA  . TRP B 10  ? 0.0477 0.0617 0.0761 -0.0218 -0.0068 -0.0045 10  TRP B CA  
4140 C C   . TRP B 10  ? 0.0547 0.0689 0.0847 -0.0217 -0.0060 -0.0032 10  TRP B C   
4141 O O   . TRP B 10  ? 0.1282 0.1418 0.1596 -0.0217 -0.0048 -0.0034 10  TRP B O   
4142 C CB  . TRP B 10  ? 0.0337 0.0475 0.0616 -0.0220 -0.0069 -0.0052 10  TRP B CB  
4143 C CG  . TRP B 10  ? 0.1036 0.1164 0.1314 -0.0212 -0.0081 -0.0059 10  TRP B CG  
4144 C CD1 . TRP B 10  ? 0.1407 0.1528 0.1673 -0.0221 -0.0084 -0.0060 10  TRP B CD1 
4145 C CD2 . TRP B 10  ? 0.0631 0.0766 0.0893 -0.0207 -0.0088 -0.0067 10  TRP B CD2 
4146 N NE1 . TRP B 10  ? 0.1064 0.1179 0.1321 -0.0214 -0.0096 -0.0065 10  TRP B NE1 
4147 C CE2 . TRP B 10  ? 0.0679 0.0805 0.0938 -0.0204 -0.0096 -0.0073 10  TRP B CE2 
4148 C CE3 . TRP B 10  ? 0.0884 0.1025 0.1134 -0.0203 -0.0094 -0.0060 10  TRP B CE3 
4149 C CZ2 . TRP B 10  ? 0.0610 0.0738 0.0853 -0.0199 -0.0103 -0.0079 10  TRP B CZ2 
4150 C CZ3 . TRP B 10  ? 0.1456 0.1597 0.1691 -0.0197 -0.0103 -0.0064 10  TRP B CZ3 
4151 C CH2 . TRP B 10  ? 0.1088 0.1224 0.1321 -0.0196 -0.0107 -0.0075 10  TRP B CH2 
4152 N N   . HIS B 11  ? 0.0897 0.1045 0.1191 -0.0211 -0.0063 -0.0021 11  HIS B N   
4153 C CA  . HIS B 11  ? 0.0712 0.0861 0.1013 -0.0204 -0.0053 -0.0010 11  HIS B CA  
4154 C C   . HIS B 11  ? 0.0727 0.0879 0.1035 -0.0200 -0.0053 -0.0005 11  HIS B C   
4155 O O   . HIS B 11  ? 0.0650 0.0809 0.0951 -0.0199 -0.0064 -0.0004 11  HIS B O   
4156 C CB  . HIS B 11  ? 0.1102 0.1255 0.1392 -0.0200 -0.0057 0.0000  11  HIS B CB  
4157 C CG  . HIS B 11  ? 0.0870 0.1027 0.1165 -0.0192 -0.0050 0.0013  11  HIS B CG  
4158 N ND1 . HIS B 11  ? 0.0687 0.0839 0.0994 -0.0188 -0.0036 0.0017  11  HIS B ND1 
4159 C CD2 . HIS B 11  ? 0.0367 0.0531 0.0656 -0.0187 -0.0056 0.0022  11  HIS B CD2 
4160 C CE1 . HIS B 11  ? 0.0979 0.1136 0.1288 -0.0181 -0.0033 0.0029  11  HIS B CE1 
4161 N NE2 . HIS B 11  ? 0.0405 0.0569 0.0702 -0.0180 -0.0046 0.0032  11  HIS B NE2 
4162 N N   . MET B 12  ? 0.0690 0.0838 0.1013 -0.0198 -0.0040 -0.0002 12  MET B N   
4163 C CA  . MET B 12  ? 0.0800 0.0953 0.1132 -0.0195 -0.0038 0.0002  12  MET B CA  
4164 C C   . MET B 12  ? 0.0649 0.0804 0.0986 -0.0187 -0.0029 0.0016  12  MET B C   
4165 O O   . MET B 12  ? 0.0873 0.1020 0.1218 -0.0186 -0.0017 0.0019  12  MET B O   
4166 C CB  . MET B 12  ? 0.0752 0.0899 0.1098 -0.0200 -0.0031 -0.0006 12  MET B CB  
4167 C CG  . MET B 12  ? 0.0514 0.0659 0.0858 -0.0208 -0.0038 -0.0020 12  MET B CG  
4168 S SD  . MET B 12  ? 0.0907 0.1059 0.1233 -0.0208 -0.0056 -0.0025 12  MET B SD  
4169 C CE  . MET B 12  ? 0.1302 0.1448 0.1620 -0.0214 -0.0058 -0.0040 12  MET B CE  
4170 N N   . HIS B 13  ? 0.0601 0.0763 0.0933 -0.0182 -0.0034 0.0023  13  HIS B N   
4171 C CA  . HIS B 13  ? 0.0777 0.0943 0.1113 -0.0174 -0.0027 0.0037  13  HIS B CA  
4172 C C   . HIS B 13  ? 0.0793 0.0967 0.1126 -0.0169 -0.0031 0.0043  13  HIS B C   
4173 O O   . HIS B 13  ? 0.0799 0.0979 0.1123 -0.0170 -0.0044 0.0039  13  HIS B O   
4174 C CB  . HIS B 13  ? 0.0661 0.0827 0.0985 -0.0171 -0.0029 0.0043  13  HIS B CB  
4175 C CG  . HIS B 13  ? 0.0910 0.1081 0.1235 -0.0162 -0.0024 0.0056  13  HIS B CG  
4176 N ND1 . HIS B 13  ? 0.0713 0.0880 0.1051 -0.0158 -0.0010 0.0064  13  HIS B ND1 
4177 C CD2 . HIS B 13  ? 0.0823 0.1002 0.1138 -0.0157 -0.0031 0.0064  13  HIS B CD2 
4178 C CE1 . HIS B 13  ? 0.0559 0.0732 0.0894 -0.0150 -0.0009 0.0076  13  HIS B CE1 
4179 N NE2 . HIS B 13  ? 0.1037 0.1218 0.1358 -0.0149 -0.0022 0.0076  13  HIS B NE2 
4180 N N   . GLN B 14  ? 0.0657 0.0834 0.1000 -0.0163 -0.0021 0.0053  14  GLN B N   
4181 C CA  . GLN B 14  ? 0.0820 0.1007 0.1160 -0.0156 -0.0024 0.0061  14  GLN B CA  
4182 C C   . GLN B 14  ? 0.1314 0.1500 0.1658 -0.0149 -0.0014 0.0075  14  GLN B C   
4183 O O   . GLN B 14  ? 0.0651 0.0830 0.1007 -0.0149 -0.0001 0.0077  14  GLN B O   
4184 C CB  . GLN B 14  ? 0.0429 0.0620 0.0778 -0.0157 -0.0023 0.0059  14  GLN B CB  
4185 C CG  . GLN B 14  ? 0.0624 0.0816 0.0969 -0.0164 -0.0033 0.0046  14  GLN B CG  
4186 C CD  . GLN B 14  ? 0.1050 0.1250 0.1380 -0.0161 -0.0049 0.0044  14  GLN B CD  
4187 O OE1 . GLN B 14  ? 0.1737 0.1944 0.2061 -0.0154 -0.0051 0.0053  14  GLN B OE1 
4188 N NE2 . GLN B 14  ? 0.1459 0.1658 0.1784 -0.0167 -0.0059 0.0033  14  GLN B NE2 
4189 N N   . PRO B 15  ? 0.1136 0.1330 0.1470 -0.0142 -0.0019 0.0083  15  PRO B N   
4190 C CA  . PRO B 15  ? 0.0695 0.0891 0.1034 -0.0134 -0.0009 0.0097  15  PRO B CA  
4191 C C   . PRO B 15  ? 0.1429 0.1627 0.1780 -0.0132 0.0000  0.0102  15  PRO B C   
4192 O O   . PRO B 15  ? 0.1190 0.1390 0.1544 -0.0135 -0.0002 0.0095  15  PRO B O   
4193 C CB  . PRO B 15  ? 0.0972 0.1178 0.1297 -0.0128 -0.0019 0.0103  15  PRO B CB  
4194 C CG  . PRO B 15  ? 0.0819 0.1031 0.1138 -0.0131 -0.0032 0.0095  15  PRO B CG  
4195 C CD  . PRO B 15  ? 0.0443 0.0647 0.0765 -0.0140 -0.0033 0.0082  15  PRO B CD  
4196 N N   . LEU B 16  ? 0.1137 0.1335 0.1494 -0.0126 0.0011  0.0114  16  LEU B N   
4197 C CA  . LEU B 16  ? 0.1102 0.1301 0.1471 -0.0124 0.0021  0.0119  16  LEU B CA  
4198 C C   . LEU B 16  ? 0.1145 0.1357 0.1508 -0.0118 0.0016  0.0124  16  LEU B C   
4199 O O   . LEU B 16  ? 0.1020 0.1240 0.1376 -0.0111 0.0013  0.0133  16  LEU B O   
4200 C CB  . LEU B 16  ? 0.0705 0.0897 0.1081 -0.0119 0.0035  0.0131  16  LEU B CB  
4201 C CG  . LEU B 16  ? 0.0763 0.0954 0.1152 -0.0117 0.0046  0.0138  16  LEU B CG  
4202 C CD1 . LEU B 16  ? 0.0801 0.0985 0.1203 -0.0127 0.0050  0.0127  16  LEU B CD1 
4203 C CD2 . LEU B 16  ? 0.1388 0.1574 0.1785 -0.0112 0.0059  0.0151  16  LEU B CD2 
4204 N N   . TYR B 17  ? 0.0860 0.1076 0.1227 -0.0122 0.0013  0.0117  17  TYR B N   
4205 C CA  . TYR B 17  ? 0.0807 0.1036 0.1169 -0.0117 0.0008  0.0120  17  TYR B CA  
4206 C C   . TYR B 17  ? 0.1386 0.1620 0.1758 -0.0112 0.0019  0.0131  17  TYR B C   
4207 O O   . TYR B 17  ? 0.1083 0.1330 0.1451 -0.0107 0.0016  0.0135  17  TYR B O   
4208 C CB  . TYR B 17  ? 0.0723 0.0956 0.1085 -0.0123 -0.0001 0.0107  17  TYR B CB  
4209 C CG  . TYR B 17  ? 0.0845 0.1076 0.1195 -0.0127 -0.0015 0.0096  17  TYR B CG  
4210 C CD1 . TYR B 17  ? 0.0615 0.0852 0.0951 -0.0122 -0.0026 0.0099  17  TYR B CD1 
4211 C CD2 . TYR B 17  ? 0.1149 0.1371 0.1502 -0.0136 -0.0017 0.0084  17  TYR B CD2 
4212 C CE1 . TYR B 17  ? 0.0704 0.0938 0.1029 -0.0126 -0.0039 0.0090  17  TYR B CE1 
4213 C CE2 . TYR B 17  ? 0.0859 0.1080 0.1201 -0.0140 -0.0030 0.0076  17  TYR B CE2 
4214 C CZ  . TYR B 17  ? 0.0973 0.1199 0.1301 -0.0135 -0.0040 0.0079  17  TYR B CZ  
4215 O OH  . TYR B 17  ? 0.1109 0.1333 0.1426 -0.0139 -0.0053 0.0071  17  TYR B OH  
4216 N N   . ARG B 18  ? 0.0314 0.0538 0.0698 -0.0114 0.0033  0.0137  18  ARG B N   
4217 C CA  . ARG B 18  ? 0.0504 0.0731 0.0899 -0.0110 0.0045  0.0147  18  ARG B CA  
4218 C C   . ARG B 18  ? 0.0824 0.1056 0.1213 -0.0100 0.0048  0.0162  18  ARG B C   
4219 O O   . ARG B 18  ? 0.1312 0.1536 0.1700 -0.0098 0.0053  0.0167  18  ARG B O   
4220 C CB  . ARG B 18  ? 0.0855 0.1067 0.1265 -0.0116 0.0058  0.0147  18  ARG B CB  
4221 C CG  . ARG B 18  ? 0.1566 0.1779 0.1989 -0.0115 0.0071  0.0157  18  ARG B CG  
4222 C CD  . ARG B 18  ? 0.2085 0.2282 0.2523 -0.0120 0.0083  0.0157  18  ARG B CD  
4223 N NE  . ARG B 18  ? 0.2636 0.2832 0.3088 -0.0121 0.0096  0.0166  18  ARG B NE  
4224 C CZ  . ARG B 18  ? 0.3233 0.3430 0.3688 -0.0114 0.0105  0.0181  18  ARG B CZ  
4225 N NH1 . ARG B 18  ? 0.3045 0.3243 0.3490 -0.0106 0.0103  0.0189  18  ARG B NH1 
4226 N NH2 . ARG B 18  ? 0.3877 0.4074 0.4345 -0.0115 0.0116  0.0189  18  ARG B NH2 
4227 N N   . GLU B 19  ? 0.0728 0.0974 0.1112 -0.0094 0.0046  0.0168  19  GLU B N   
4228 C CA  . GLU B 19  ? 0.0763 0.1015 0.1140 -0.0084 0.0048  0.0182  19  GLU B CA  
4229 C C   . GLU B 19  ? 0.1414 0.1659 0.1804 -0.0082 0.0064  0.0194  19  GLU B C   
4230 O O   . GLU B 19  ? 0.1606 0.1849 0.2008 -0.0086 0.0073  0.0195  19  GLU B O   
4231 C CB  . GLU B 19  ? 0.1461 0.1731 0.1832 -0.0078 0.0043  0.0184  19  GLU B CB  
4232 C CG  . GLU B 19  ? 0.2942 0.3221 0.3299 -0.0068 0.0036  0.0192  19  GLU B CG  
4233 C CD  . GLU B 19  ? 0.3443 0.3726 0.3803 -0.0061 0.0047  0.0208  19  GLU B CD  
4234 O OE1 . GLU B 19  ? 0.3099 0.3379 0.3472 -0.0063 0.0060  0.0213  19  GLU B OE1 
4235 O OE2 . GLU B 19  ? 0.4418 0.4707 0.4768 -0.0052 0.0044  0.0215  19  GLU B OE2 
4236 N N   . PRO B 20  ? 0.1285 0.1525 0.1672 -0.0077 0.0068  0.0203  20  PRO B N   
4237 C CA  . PRO B 20  ? 0.1672 0.1900 0.2072 -0.0077 0.0083  0.0212  20  PRO B CA  
4238 C C   . PRO B 20  ? 0.2490 0.2726 0.2896 -0.0071 0.0092  0.0226  20  PRO B C   
4239 O O   . PRO B 20  ? 0.3234 0.3460 0.3652 -0.0073 0.0105  0.0232  20  PRO B O   
4240 C CB  . PRO B 20  ? 0.1350 0.1573 0.1745 -0.0072 0.0082  0.0217  20  PRO B CB  
4241 C CG  . PRO B 20  ? 0.1862 0.2099 0.2241 -0.0066 0.0070  0.0217  20  PRO B CG  
4242 C CD  . PRO B 20  ? 0.1274 0.1518 0.1648 -0.0071 0.0059  0.0205  20  PRO B CD  
4243 N N   . TYR B 21  ? 0.1417 0.1668 0.1813 -0.0065 0.0087  0.0230  21  TYR B N   
4244 C CA  . TYR B 21  ? 0.1861 0.2121 0.2262 -0.0059 0.0096  0.0244  21  TYR B CA  
4245 C C   . TYR B 21  ? 0.2053 0.2319 0.2462 -0.0064 0.0099  0.0240  21  TYR B C   
4246 O O   . TYR B 21  ? 0.2666 0.2928 0.3086 -0.0065 0.0112  0.0249  21  TYR B O   
4247 C CB  . TYR B 21  ? 0.1748 0.2023 0.2134 -0.0048 0.0089  0.0251  21  TYR B CB  
4248 C CG  . TYR B 21  ? 0.2836 0.3107 0.3217 -0.0042 0.0089  0.0259  21  TYR B CG  
4249 C CD1 . TYR B 21  ? 0.3005 0.3272 0.3390 -0.0036 0.0100  0.0274  21  TYR B CD1 
4250 C CD2 . TYR B 21  ? 0.2329 0.2598 0.2699 -0.0042 0.0077  0.0251  21  TYR B CD2 
4251 C CE1 . TYR B 21  ? 0.2510 0.2774 0.2891 -0.0030 0.0100  0.0280  21  TYR B CE1 
4252 C CE2 . TYR B 21  ? 0.2394 0.2661 0.2760 -0.0037 0.0077  0.0257  21  TYR B CE2 
4253 C CZ  . TYR B 21  ? 0.2604 0.2868 0.2975 -0.0030 0.0088  0.0272  21  TYR B CZ  
4254 O OH  . TYR B 21  ? 0.2376 0.2637 0.2743 -0.0025 0.0088  0.0278  21  TYR B OH  
4255 N N   . THR B 22  ? 0.1752 0.2024 0.2155 -0.0068 0.0089  0.0227  22  THR B N   
4256 C CA  . THR B 22  ? 0.2071 0.2350 0.2482 -0.0073 0.0091  0.0222  22  THR B CA  
4257 C C   . THR B 22  ? 0.2545 0.2811 0.2969 -0.0085 0.0094  0.0211  22  THR B C   
4258 O O   . THR B 22  ? 0.1959 0.2227 0.2395 -0.0090 0.0100  0.0209  22  THR B O   
4259 C CB  . THR B 22  ? 0.2341 0.2636 0.2741 -0.0071 0.0078  0.0214  22  THR B CB  
4260 O OG1 . THR B 22  ? 0.1820 0.2110 0.2212 -0.0075 0.0066  0.0200  22  THR B OG1 
4261 C CG2 . THR B 22  ? 0.2304 0.2613 0.2691 -0.0059 0.0075  0.0224  22  THR B CG2 
4262 N N   . GLY B 23  ? 0.2105 0.2358 0.2528 -0.0089 0.0090  0.0203  23  GLY B N   
4263 C CA  . GLY B 23  ? 0.1682 0.1924 0.2114 -0.0100 0.0090  0.0190  23  GLY B CA  
4264 C C   . GLY B 23  ? 0.2086 0.2335 0.2513 -0.0104 0.0078  0.0176  23  GLY B C   
4265 O O   . GLY B 23  ? 0.2720 0.2962 0.3156 -0.0113 0.0078  0.0165  23  GLY B O   
4266 N N   . GLU B 24  ? 0.1175 0.1438 0.1589 -0.0098 0.0068  0.0175  24  GLU B N   
4267 C CA  . GLU B 24  ? 0.0814 0.1085 0.1223 -0.0102 0.0056  0.0161  24  GLU B CA  
4268 C C   . GLU B 24  ? 0.1269 0.1534 0.1669 -0.0105 0.0044  0.0150  24  GLU B C   
4269 O O   . GLU B 24  ? 0.1048 0.1311 0.1437 -0.0100 0.0039  0.0154  24  GLU B O   
4270 C CB  . GLU B 24  ? 0.1298 0.1588 0.1697 -0.0094 0.0050  0.0165  24  GLU B CB  
4271 C CG  . GLU B 24  ? 0.1731 0.2031 0.2141 -0.0092 0.0061  0.0174  24  GLU B CG  
4272 C CD  . GLU B 24  ? 0.2986 0.3304 0.3385 -0.0083 0.0056  0.0179  24  GLU B CD  
4273 O OE1 . GLU B 24  ? 0.4526 0.4855 0.4932 -0.0081 0.0064  0.0185  24  GLU B OE1 
4274 O OE2 . GLU B 24  ? 0.3191 0.3513 0.3575 -0.0077 0.0045  0.0177  24  GLU B OE2 
4275 N N   . TYR B 25  ? 0.0731 0.0992 0.1134 -0.0113 0.0039  0.0136  25  TYR B N   
4276 C CA  . TYR B 25  ? 0.0789 0.1046 0.1182 -0.0116 0.0026  0.0125  25  TYR B CA  
4277 C C   . TYR B 25  ? 0.1194 0.1464 0.1572 -0.0111 0.0012  0.0122  25  TYR B C   
4278 O O   . TYR B 25  ? 0.1098 0.1378 0.1479 -0.0112 0.0008  0.0117  25  TYR B O   
4279 C CB  . TYR B 25  ? 0.1302 0.1550 0.1703 -0.0127 0.0025  0.0112  25  TYR B CB  
4280 C CG  . TYR B 25  ? 0.1104 0.1337 0.1515 -0.0132 0.0034  0.0112  25  TYR B CG  
4281 C CD1 . TYR B 25  ? 0.1089 0.1316 0.1514 -0.0133 0.0049  0.0120  25  TYR B CD1 
4282 C CD2 . TYR B 25  ? 0.0705 0.0927 0.1110 -0.0137 0.0028  0.0104  25  TYR B CD2 
4283 C CE1 . TYR B 25  ? 0.1477 0.1689 0.1911 -0.0138 0.0058  0.0120  25  TYR B CE1 
4284 C CE2 . TYR B 25  ? 0.1078 0.1286 0.1492 -0.0141 0.0037  0.0103  25  TYR B CE2 
4285 C CZ  . TYR B 25  ? 0.1450 0.1652 0.1878 -0.0141 0.0051  0.0111  25  TYR B CZ  
4286 O OH  . TYR B 25  ? 0.1267 0.1454 0.1703 -0.0146 0.0059  0.0109  25  TYR B OH  
4287 N N   . LEU B 26  ? 0.1088 0.1360 0.1453 -0.0105 0.0004  0.0126  26  LEU B N   
4288 C CA  . LEU B 26  ? 0.1500 0.1785 0.1852 -0.0099 -0.0007 0.0125  26  LEU B CA  
4289 C C   . LEU B 26  ? 0.1795 0.2080 0.2139 -0.0103 -0.0023 0.0111  26  LEU B C   
4290 O O   . LEU B 26  ? 0.1129 0.1425 0.1464 -0.0098 -0.0033 0.0108  26  LEU B O   
4291 C CB  . LEU B 26  ? 0.1194 0.1481 0.1536 -0.0091 -0.0010 0.0135  26  LEU B CB  
4292 C CG  . LEU B 26  ? 0.1849 0.2139 0.2197 -0.0084 0.0004  0.0150  26  LEU B CG  
4293 C CD1 . LEU B 26  ? 0.2225 0.2517 0.2562 -0.0076 0.0001  0.0160  26  LEU B CD1 
4294 C CD2 . LEU B 26  ? 0.1601 0.1904 0.1953 -0.0081 0.0009  0.0154  26  LEU B CD2 
4295 N N   . LEU B 27  ? 0.0808 0.1081 0.1154 -0.0111 -0.0025 0.0102  27  LEU B N   
4296 C CA  . LEU B 27  ? 0.0991 0.1263 0.1331 -0.0116 -0.0038 0.0089  27  LEU B CA  
4297 C C   . LEU B 27  ? 0.1618 0.1882 0.1970 -0.0126 -0.0033 0.0080  27  LEU B C   
4298 O O   . LEU B 27  ? 0.1490 0.1745 0.1853 -0.0129 -0.0020 0.0084  27  LEU B O   
4299 C CB  . LEU B 27  ? 0.0888 0.1154 0.1215 -0.0117 -0.0049 0.0087  27  LEU B CB  
4300 C CG  . LEU B 27  ? 0.2086 0.2360 0.2400 -0.0108 -0.0056 0.0094  27  LEU B CG  
4301 C CD1 . LEU B 27  ? 0.1949 0.2215 0.2253 -0.0110 -0.0063 0.0093  27  LEU B CD1 
4302 C CD2 . LEU B 27  ? 0.2236 0.2521 0.2543 -0.0104 -0.0068 0.0089  27  LEU B CD2 
4303 N N   . PRO B 28  ? 0.1303 0.1570 0.1654 -0.0130 -0.0042 0.0068  28  PRO B N   
4304 C CA  . PRO B 28  ? 0.1089 0.1350 0.1453 -0.0139 -0.0038 0.0059  28  PRO B CA  
4305 C C   . PRO B 28  ? 0.0314 0.0563 0.0674 -0.0146 -0.0044 0.0049  28  PRO B C   
4306 O O   . PRO B 28  ? 0.0532 0.0776 0.0899 -0.0154 -0.0043 0.0040  28  PRO B O   
4307 C CB  . PRO B 28  ? 0.1390 0.1662 0.1754 -0.0139 -0.0045 0.0051  28  PRO B CB  
4308 C CG  . PRO B 28  ? 0.0875 0.1153 0.1223 -0.0133 -0.0060 0.0050  28  PRO B CG  
4309 C CD  . PRO B 28  ? 0.1117 0.1394 0.1458 -0.0126 -0.0056 0.0063  28  PRO B CD  
4310 N N   . TRP B 29  ? 0.1037 0.1280 0.1385 -0.0145 -0.0049 0.0052  29  TRP B N   
4311 C CA  . TRP B 29  ? 0.0976 0.1210 0.1318 -0.0151 -0.0056 0.0043  29  TRP B CA  
4312 C C   . TRP B 29  ? 0.1308 0.1530 0.1660 -0.0159 -0.0046 0.0039  29  TRP B C   
4313 O O   . TRP B 29  ? 0.1020 0.1237 0.1371 -0.0166 -0.0052 0.0028  29  TRP B O   
4314 C CB  . TRP B 29  ? 0.1051 0.1284 0.1379 -0.0148 -0.0063 0.0048  29  TRP B CB  
4315 C CG  . TRP B 29  ? 0.1088 0.1330 0.1404 -0.0141 -0.0076 0.0050  29  TRP B CG  
4316 C CD1 . TRP B 29  ? 0.1843 0.2090 0.2151 -0.0134 -0.0077 0.0060  29  TRP B CD1 
4317 C CD2 . TRP B 29  ? 0.1682 0.1930 0.1991 -0.0142 -0.0090 0.0041  29  TRP B CD2 
4318 N NE1 . TRP B 29  ? 0.1980 0.2235 0.2277 -0.0130 -0.0091 0.0057  29  TRP B NE1 
4319 C CE2 . TRP B 29  ? 0.1775 0.2030 0.2072 -0.0135 -0.0099 0.0046  29  TRP B CE2 
4320 C CE3 . TRP B 29  ? 0.1841 0.2087 0.2151 -0.0148 -0.0096 0.0028  29  TRP B CE3 
4321 C CZ2 . TRP B 29  ? 0.1823 0.2084 0.2111 -0.0133 -0.0114 0.0039  29  TRP B CZ2 
4322 C CZ3 . TRP B 29  ? 0.2437 0.2690 0.2739 -0.0146 -0.0111 0.0022  29  TRP B CZ3 
4323 C CH2 . TRP B 29  ? 0.1898 0.2157 0.2188 -0.0139 -0.0120 0.0028  29  TRP B CH2 
4324 N N   . THR B 30  ? 0.0947 0.1166 0.1310 -0.0157 -0.0032 0.0048  30  THR B N   
4325 C CA  . THR B 30  ? 0.0414 0.0622 0.0790 -0.0164 -0.0022 0.0043  30  THR B CA  
4326 C C   . THR B 30  ? 0.0926 0.1136 0.1313 -0.0170 -0.0021 0.0034  30  THR B C   
4327 O O   . THR B 30  ? 0.0756 0.0959 0.1147 -0.0178 -0.0022 0.0023  30  THR B O   
4328 C CB  . THR B 30  ? 0.1096 0.1298 0.1481 -0.0161 -0.0007 0.0055  30  THR B CB  
4329 O OG1 . THR B 30  ? 0.1150 0.1350 0.1524 -0.0156 -0.0009 0.0062  30  THR B OG1 
4330 C CG2 . THR B 30  ? 0.0802 0.0992 0.1200 -0.0168 0.0003  0.0050  30  THR B CG2 
4331 N N   . PHE B 31  ? 0.0655 0.0875 0.1048 -0.0167 -0.0018 0.0038  31  PHE B N   
4332 C CA  . PHE B 31  ? 0.0298 0.0521 0.0702 -0.0173 -0.0018 0.0029  31  PHE B CA  
4333 C C   . PHE B 31  ? 0.0480 0.0705 0.0876 -0.0177 -0.0033 0.0015  31  PHE B C   
4334 O O   . PHE B 31  ? 0.0525 0.0745 0.0928 -0.0185 -0.0033 0.0005  31  PHE B O   
4335 C CB  . PHE B 31  ? 0.0531 0.0767 0.0940 -0.0168 -0.0015 0.0035  31  PHE B CB  
4336 C CG  . PHE B 31  ? 0.1158 0.1401 0.1577 -0.0173 -0.0016 0.0026  31  PHE B CG  
4337 C CD1 . PHE B 31  ? 0.1102 0.1340 0.1539 -0.0179 -0.0005 0.0024  31  PHE B CD1 
4338 C CD2 . PHE B 31  ? 0.1067 0.1320 0.1479 -0.0171 -0.0029 0.0018  31  PHE B CD2 
4339 C CE1 . PHE B 31  ? 0.1119 0.1364 0.1567 -0.0184 -0.0006 0.0016  31  PHE B CE1 
4340 C CE2 . PHE B 31  ? 0.1289 0.1549 0.1711 -0.0176 -0.0030 0.0009  31  PHE B CE2 
4341 C CZ  . PHE B 31  ? 0.1059 0.1315 0.1499 -0.0183 -0.0019 0.0008  31  PHE B CZ  
4342 N N   . PHE B 32  ? 0.0311 0.0542 0.0691 -0.0172 -0.0045 0.0016  32  PHE B N   
4343 C CA  . PHE B 32  ? 0.0754 0.0987 0.1126 -0.0175 -0.0060 0.0003  32  PHE B CA  
4344 C C   . PHE B 32  ? 0.0933 0.1154 0.1301 -0.0182 -0.0064 -0.0004 32  PHE B C   
4345 O O   . PHE B 32  ? 0.0764 0.0984 0.1132 -0.0188 -0.0070 -0.0016 32  PHE B O   
4346 C CB  . PHE B 32  ? 0.0675 0.0917 0.1033 -0.0168 -0.0073 0.0006  32  PHE B CB  
4347 C CG  . PHE B 32  ? 0.0754 0.1010 0.1116 -0.0163 -0.0073 0.0007  32  PHE B CG  
4348 C CD1 . PHE B 32  ? 0.0970 0.1231 0.1344 -0.0167 -0.0072 0.0000  32  PHE B CD1 
4349 C CD2 . PHE B 32  ? 0.1179 0.1444 0.1533 -0.0154 -0.0076 0.0016  32  PHE B CD2 
4350 C CE1 . PHE B 32  ? 0.0595 0.0870 0.0973 -0.0162 -0.0072 0.0001  32  PHE B CE1 
4351 C CE2 . PHE B 32  ? 0.1188 0.1467 0.1546 -0.0149 -0.0076 0.0017  32  PHE B CE2 
4352 C CZ  . PHE B 32  ? 0.0685 0.0969 0.1054 -0.0153 -0.0074 0.0010  32  PHE B CZ  
4353 N N   . HIS B 33  ? 0.0366 0.0580 0.0728 -0.0181 -0.0060 0.0002  33  HIS B N   
4354 C CA  . HIS B 33  ? 0.0509 0.0712 0.0866 -0.0187 -0.0063 -0.0005 33  HIS B CA  
4355 C C   . HIS B 33  ? 0.0689 0.0884 0.1062 -0.0194 -0.0051 -0.0011 33  HIS B C   
4356 O O   . HIS B 33  ? 0.0633 0.0820 0.1000 -0.0199 -0.0054 -0.0021 33  HIS B O   
4357 C CB  . HIS B 33  ? 0.0289 0.0488 0.0636 -0.0184 -0.0063 0.0002  33  HIS B CB  
4358 C CG  . HIS B 33  ? 0.0632 0.0836 0.0962 -0.0180 -0.0078 0.0003  33  HIS B CG  
4359 N ND1 . HIS B 33  ? 0.0807 0.1009 0.1124 -0.0182 -0.0090 -0.0008 33  HIS B ND1 
4360 C CD2 . HIS B 33  ? 0.0912 0.1123 0.1234 -0.0172 -0.0081 0.0013  33  HIS B CD2 
4361 C CE1 . HIS B 33  ? 0.0898 0.1103 0.1199 -0.0176 -0.0100 -0.0005 33  HIS B CE1 
4362 N NE2 . HIS B 33  ? 0.1130 0.1343 0.1438 -0.0172 -0.0097 0.0008  33  HIS B NE2 
4363 N N   . ALA B 34  ? 0.0648 0.0843 0.1035 -0.0193 -0.0038 -0.0004 34  ALA B N   
4364 C CA  . ALA B 34  ? 0.1004 0.1191 0.1406 -0.0199 -0.0028 -0.0010 34  ALA B CA  
4365 C C   . ALA B 34  ? 0.1024 0.1213 0.1424 -0.0203 -0.0034 -0.0022 34  ALA B C   
4366 O O   . ALA B 34  ? 0.1394 0.1574 0.1787 -0.0208 -0.0035 -0.0031 34  ALA B O   
4367 C CB  . ALA B 34  ? 0.0586 0.0773 0.1003 -0.0197 -0.0013 0.0001  34  ALA B CB  
4368 N N   . VAL B 35  ? 0.0840 0.1042 0.1243 -0.0201 -0.0039 -0.0021 35  VAL B N   
4369 C CA  . VAL B 35  ? 0.0508 0.0712 0.0907 -0.0204 -0.0044 -0.0032 35  VAL B CA  
4370 C C   . VAL B 35  ? 0.1350 0.1551 0.1726 -0.0204 -0.0057 -0.0041 35  VAL B C   
4371 O O   . VAL B 35  ? 0.0992 0.1189 0.1362 -0.0207 -0.0061 -0.0049 35  VAL B O   
4372 C CB  . VAL B 35  ? 0.0557 0.0776 0.0967 -0.0201 -0.0044 -0.0029 35  VAL B CB  
4373 C CG1 . VAL B 35  ? 0.0305 0.0527 0.0736 -0.0200 -0.0029 -0.0018 35  VAL B CG1 
4374 C CG2 . VAL B 35  ? 0.0924 0.1154 0.1323 -0.0195 -0.0056 -0.0027 35  VAL B CG2 
4375 N N   . LYS B 36  ? 0.0637 0.0839 0.1000 -0.0200 -0.0065 -0.0039 36  LYS B N   
4376 C CA  . LYS B 36  ? 0.0959 0.1157 0.1297 -0.0200 -0.0078 -0.0047 36  LYS B CA  
4377 C C   . LYS B 36  ? 0.1459 0.1645 0.1786 -0.0204 -0.0077 -0.0050 36  LYS B C   
4378 O O   . LYS B 36  ? 0.1143 0.1324 0.1455 -0.0206 -0.0084 -0.0056 36  LYS B O   
4379 C CB  . LYS B 36  ? 0.0732 0.0938 0.1060 -0.0193 -0.0087 -0.0044 36  LYS B CB  
4380 C CG  . LYS B 36  ? 0.0896 0.1100 0.1199 -0.0190 -0.0098 -0.0053 36  LYS B CG  
4381 C CD  . LYS B 36  ? 0.1232 0.1443 0.1527 -0.0181 -0.0106 -0.0051 36  LYS B CD  
4382 C CE  . LYS B 36  ? 0.1462 0.1667 0.1750 -0.0178 -0.0109 -0.0045 36  LYS B CE  
4383 N NZ  . LYS B 36  ? 0.0737 0.0931 0.1011 -0.0180 -0.0110 -0.0052 36  LYS B NZ  
4384 N N   . ASP B 37  ? 0.0851 0.1032 0.1186 -0.0204 -0.0070 -0.0044 37  ASP B N   
4385 C CA  . ASP B 37  ? 0.1073 0.1246 0.1397 -0.0207 -0.0071 -0.0046 37  ASP B CA  
4386 C C   . ASP B 37  ? 0.1544 0.1706 0.1880 -0.0211 -0.0060 -0.0045 37  ASP B C   
4387 O O   . ASP B 37  ? 0.0923 0.1077 0.1252 -0.0214 -0.0061 -0.0050 37  ASP B O   
4388 C CB  . ASP B 37  ? 0.1142 0.1317 0.1457 -0.0202 -0.0076 -0.0041 37  ASP B CB  
4389 C CG  . ASP B 37  ? 0.1364 0.1546 0.1667 -0.0195 -0.0087 -0.0043 37  ASP B CG  
4390 O OD1 . ASP B 37  ? 0.1041 0.1223 0.1329 -0.0195 -0.0094 -0.0052 37  ASP B OD1 
4391 O OD2 . ASP B 37  ? 0.0787 0.0976 0.1096 -0.0191 -0.0088 -0.0033 37  ASP B OD2 
4392 N N   . TYR B 38  ? 0.0927 0.1091 0.1284 -0.0210 -0.0049 -0.0037 38  TYR B N   
4393 C CA  . TYR B 38  ? 0.0885 0.1039 0.1252 -0.0212 -0.0037 -0.0035 38  TYR B CA  
4394 C C   . TYR B 38  ? 0.0613 0.0758 0.0984 -0.0216 -0.0032 -0.0044 38  TYR B C   
4395 O O   . TYR B 38  ? 0.1047 0.1182 0.1419 -0.0219 -0.0027 -0.0047 38  TYR B O   
4396 C CB  . TYR B 38  ? 0.0932 0.1089 0.1318 -0.0209 -0.0026 -0.0023 38  TYR B CB  
4397 C CG  . TYR B 38  ? 0.1359 0.1522 0.1738 -0.0203 -0.0031 -0.0013 38  TYR B CG  
4398 C CD1 . TYR B 38  ? 0.1139 0.1301 0.1502 -0.0203 -0.0040 -0.0015 38  TYR B CD1 
4399 C CD2 . TYR B 38  ? 0.0551 0.0720 0.0933 -0.0196 -0.0026 -0.0001 38  TYR B CD2 
4400 C CE1 . TYR B 38  ? 0.1245 0.1412 0.1596 -0.0196 -0.0045 -0.0005 38  TYR B CE1 
4401 C CE2 . TYR B 38  ? 0.1204 0.1378 0.1573 -0.0189 -0.0030 0.0009  38  TYR B CE2 
4402 C CZ  . TYR B 38  ? 0.0842 0.1016 0.1197 -0.0189 -0.0040 0.0006  38  TYR B CZ  
4403 O OH  . TYR B 38  ? 0.1048 0.1226 0.1391 -0.0183 -0.0045 0.0016  38  TYR B OH  
4404 N N   . TYR B 39  ? 0.0703 0.0852 0.1077 -0.0217 -0.0034 -0.0048 39  TYR B N   
4405 C CA  . TYR B 39  ? 0.1159 0.1299 0.1533 -0.0221 -0.0032 -0.0057 39  TYR B CA  
4406 C C   . TYR B 39  ? 0.1011 0.1148 0.1365 -0.0223 -0.0045 -0.0065 39  TYR B C   
4407 O O   . TYR B 39  ? 0.0746 0.0874 0.1095 -0.0225 -0.0045 -0.0071 39  TYR B O   
4408 C CB  . TYR B 39  ? 0.0396 0.0541 0.0783 -0.0222 -0.0028 -0.0057 39  TYR B CB  
4409 C CG  . TYR B 39  ? 0.0722 0.0860 0.1110 -0.0226 -0.0028 -0.0066 39  TYR B CG  
4410 C CD1 . TYR B 39  ? 0.1197 0.1325 0.1597 -0.0229 -0.0018 -0.0068 39  TYR B CD1 
4411 C CD2 . TYR B 39  ? 0.1397 0.1538 0.1773 -0.0227 -0.0039 -0.0073 39  TYR B CD2 
4412 C CE1 . TYR B 39  ? 0.1363 0.1485 0.1764 -0.0232 -0.0018 -0.0077 39  TYR B CE1 
4413 C CE2 . TYR B 39  ? 0.1222 0.1357 0.1600 -0.0230 -0.0039 -0.0081 39  TYR B CE2 
4414 C CZ  . TYR B 39  ? 0.1284 0.1410 0.1674 -0.0233 -0.0028 -0.0083 39  TYR B CZ  
4415 O OH  . TYR B 39  ? 0.1643 0.1763 0.2035 -0.0236 -0.0028 -0.0091 39  TYR B OH  
4416 N N   . ASP B 40  ? 0.0736 0.0882 0.1077 -0.0220 -0.0056 -0.0064 40  ASP B N   
4417 C CA  . ASP B 40  ? 0.0579 0.0722 0.0901 -0.0221 -0.0068 -0.0071 40  ASP B CA  
4418 C C   . ASP B 40  ? 0.1110 0.1246 0.1417 -0.0222 -0.0073 -0.0072 40  ASP B C   
4419 O O   . ASP B 40  ? 0.1114 0.1243 0.1410 -0.0223 -0.0079 -0.0077 40  ASP B O   
4420 C CB  . ASP B 40  ? 0.1053 0.1205 0.1366 -0.0218 -0.0078 -0.0069 40  ASP B CB  
4421 C CG  . ASP B 40  ? 0.1314 0.1472 0.1638 -0.0218 -0.0075 -0.0072 40  ASP B CG  
4422 O OD1 . ASP B 40  ? 0.1499 0.1652 0.1822 -0.0220 -0.0077 -0.0078 40  ASP B OD1 
4423 O OD2 . ASP B 40  ? 0.1523 0.1691 0.1860 -0.0216 -0.0071 -0.0067 40  ASP B OD2 
4424 N N   . MET B 41  ? 0.0607 0.0745 0.0914 -0.0220 -0.0071 -0.0066 41  MET B N   
4425 C CA  . MET B 41  ? 0.0831 0.0963 0.1124 -0.0222 -0.0076 -0.0067 41  MET B CA  
4426 C C   . MET B 41  ? 0.0978 0.1100 0.1276 -0.0225 -0.0070 -0.0073 41  MET B C   
4427 O O   . MET B 41  ? 0.0995 0.1112 0.1281 -0.0226 -0.0077 -0.0078 41  MET B O   
4428 C CB  . MET B 41  ? 0.0518 0.0655 0.0811 -0.0220 -0.0074 -0.0060 41  MET B CB  
4429 C CG  . MET B 41  ? 0.0336 0.0484 0.0615 -0.0216 -0.0081 -0.0058 41  MET B CG  
4430 S SD  . MET B 41  ? 0.0879 0.1024 0.1126 -0.0213 -0.0091 -0.0065 41  MET B SD  
4431 C CE  . MET B 41  ? 0.0565 0.0710 0.0819 -0.0209 -0.0084 -0.0072 41  MET B CE  
4432 N N   . PRO B 42  ? 0.1371 0.1489 0.1687 -0.0226 -0.0057 -0.0073 42  PRO B N   
4433 C CA  . PRO B 42  ? 0.1113 0.1222 0.1435 -0.0229 -0.0051 -0.0081 42  PRO B CA  
4434 C C   . PRO B 42  ? 0.1149 0.1255 0.1468 -0.0231 -0.0055 -0.0088 42  PRO B C   
4435 O O   . PRO B 42  ? 0.1285 0.1385 0.1599 -0.0233 -0.0057 -0.0096 42  PRO B O   
4436 C CB  . PRO B 42  ? 0.1043 0.1149 0.1385 -0.0229 -0.0036 -0.0078 42  PRO B CB  
4437 C CG  . PRO B 42  ? 0.1127 0.1241 0.1477 -0.0227 -0.0034 -0.0069 42  PRO B CG  
4438 C CD  . PRO B 42  ? 0.1320 0.1442 0.1653 -0.0224 -0.0046 -0.0066 42  PRO B CD  
4439 N N   . ALA B 43  ? 0.1134 0.1246 0.1457 -0.0230 -0.0057 -0.0087 43  ALA B N   
4440 C CA  . ALA B 43  ? 0.1313 0.1423 0.1636 -0.0231 -0.0060 -0.0094 43  ALA B CA  
4441 C C   . ALA B 43  ? 0.1687 0.1795 0.1990 -0.0231 -0.0072 -0.0098 43  ALA B C   
4442 O O   . ALA B 43  ? 0.1071 0.1176 0.1373 -0.0232 -0.0074 -0.0105 43  ALA B O   
4443 C CB  . ALA B 43  ? 0.1201 0.1320 0.1532 -0.0230 -0.0059 -0.0091 43  ALA B CB  
4444 N N   . TYR B 44  ? 0.1074 0.1184 0.1361 -0.0229 -0.0081 -0.0094 44  TYR B N   
4445 C CA  . TYR B 44  ? 0.0692 0.0797 0.0961 -0.0228 -0.0092 -0.0097 44  TYR B CA  
4446 C C   . TYR B 44  ? 0.1284 0.1381 0.1554 -0.0231 -0.0089 -0.0105 44  TYR B C   
4447 O O   . TYR B 44  ? 0.1364 0.1457 0.1623 -0.0232 -0.0096 -0.0110 44  TYR B O   
4448 C CB  . TYR B 44  ? 0.1150 0.1256 0.1403 -0.0226 -0.0101 -0.0091 44  TYR B CB  
4449 C CG  . TYR B 44  ? 0.0935 0.1047 0.1179 -0.0223 -0.0109 -0.0085 44  TYR B CG  
4450 C CD1 . TYR B 44  ? 0.0690 0.0810 0.0940 -0.0221 -0.0105 -0.0079 44  TYR B CD1 
4451 C CD2 . TYR B 44  ? 0.1127 0.1236 0.1354 -0.0219 -0.0119 -0.0085 44  TYR B CD2 
4452 C CE1 . TYR B 44  ? 0.0720 0.0846 0.0959 -0.0216 -0.0110 -0.0075 44  TYR B CE1 
4453 C CE2 . TYR B 44  ? 0.1294 0.1408 0.1509 -0.0214 -0.0124 -0.0080 44  TYR B CE2 
4454 C CZ  . TYR B 44  ? 0.0991 0.1115 0.1213 -0.0213 -0.0119 -0.0075 44  TYR B CZ  
4455 O OH  . TYR B 44  ? 0.1539 0.1670 0.1748 -0.0209 -0.0121 -0.0073 44  TYR B OH  
4456 N N   . LEU B 45  ? 0.1050 0.1144 0.1332 -0.0233 -0.0078 -0.0107 45  LEU B N   
4457 C CA  . LEU B 45  ? 0.1617 0.1703 0.1901 -0.0236 -0.0074 -0.0115 45  LEU B CA  
4458 C C   . LEU B 45  ? 0.1554 0.1638 0.1846 -0.0238 -0.0071 -0.0123 45  LEU B C   
4459 O O   . LEU B 45  ? 0.1590 0.1667 0.1881 -0.0240 -0.0070 -0.0131 45  LEU B O   
4460 C CB  . LEU B 45  ? 0.1127 0.1211 0.1424 -0.0237 -0.0062 -0.0114 45  LEU B CB  
4461 C CG  . LEU B 45  ? 0.1740 0.1827 0.2030 -0.0236 -0.0064 -0.0108 45  LEU B CG  
4462 C CD1 . LEU B 45  ? 0.1151 0.1237 0.1456 -0.0236 -0.0051 -0.0106 45  LEU B CD1 
4463 C CD2 . LEU B 45  ? 0.1637 0.1721 0.1911 -0.0236 -0.0072 -0.0112 45  LEU B CD2 
4464 N N   . LYS B 46  ? 0.1348 0.1436 0.1648 -0.0238 -0.0070 -0.0121 46  LYS B N   
4465 C CA  . LYS B 46  ? 0.1801 0.1887 0.2107 -0.0240 -0.0069 -0.0128 46  LYS B CA  
4466 C C   . LYS B 46  ? 0.2339 0.2424 0.2628 -0.0239 -0.0081 -0.0131 46  LYS B C   
4467 O O   . LYS B 46  ? 0.2436 0.2517 0.2727 -0.0241 -0.0081 -0.0139 46  LYS B O   
4468 C CB  . LYS B 46  ? 0.2255 0.2348 0.2574 -0.0239 -0.0066 -0.0124 46  LYS B CB  
4469 C CG  . LYS B 46  ? 0.3253 0.3344 0.3591 -0.0241 -0.0052 -0.0121 46  LYS B CG  
4470 C CD  . LYS B 46  ? 0.4446 0.4540 0.4799 -0.0242 -0.0048 -0.0122 46  LYS B CD  
4471 C CE  . LYS B 46  ? 0.4225 0.4325 0.4592 -0.0241 -0.0040 -0.0113 46  LYS B CE  
4472 N NZ  . LYS B 46  ? 0.5263 0.5363 0.5647 -0.0243 -0.0033 -0.0114 46  LYS B NZ  
4473 N N   . ASP B 47  ? 0.1908 0.1996 0.2181 -0.0236 -0.0091 -0.0126 47  ASP B N   
4474 C CA  . ASP B 47  ? 0.2348 0.2436 0.2606 -0.0235 -0.0103 -0.0127 47  ASP B CA  
4475 C C   . ASP B 47  ? 0.2410 0.2492 0.2651 -0.0234 -0.0110 -0.0128 47  ASP B C   
4476 O O   . ASP B 47  ? 0.2062 0.2142 0.2291 -0.0234 -0.0119 -0.0130 47  ASP B O   
4477 C CB  . ASP B 47  ? 0.2415 0.2509 0.2666 -0.0232 -0.0110 -0.0120 47  ASP B CB  
4478 C CG  . ASP B 47  ? 0.3962 0.4063 0.4229 -0.0232 -0.0104 -0.0121 47  ASP B CG  
4479 O OD1 . ASP B 47  ? 0.2362 0.2461 0.2641 -0.0235 -0.0098 -0.0127 47  ASP B OD1 
4480 O OD2 . ASP B 47  ? 0.4977 0.5084 0.5245 -0.0230 -0.0105 -0.0115 47  ASP B OD2 
4481 N N   . PHE B 48  ? 0.1894 0.1975 0.2134 -0.0234 -0.0107 -0.0125 48  PHE B N   
4482 C CA  . PHE B 48  ? 0.1634 0.1711 0.1859 -0.0233 -0.0115 -0.0124 48  PHE B CA  
4483 C C   . PHE B 48  ? 0.2134 0.2209 0.2366 -0.0235 -0.0106 -0.0130 48  PHE B C   
4484 O O   . PHE B 48  ? 0.2102 0.2178 0.2347 -0.0236 -0.0096 -0.0129 48  PHE B O   
4485 C CB  . PHE B 48  ? 0.1398 0.1477 0.1614 -0.0229 -0.0122 -0.0114 48  PHE B CB  
4486 C CG  . PHE B 48  ? 0.2257 0.2339 0.2465 -0.0226 -0.0130 -0.0109 48  PHE B CG  
4487 C CD1 . PHE B 48  ? 0.2035 0.2113 0.2228 -0.0223 -0.0139 -0.0109 48  PHE B CD1 
4488 C CD2 . PHE B 48  ? 0.1710 0.1799 0.1926 -0.0226 -0.0127 -0.0104 48  PHE B CD2 
4489 C CE1 . PHE B 48  ? 0.2307 0.2386 0.2491 -0.0219 -0.0145 -0.0104 48  PHE B CE1 
4490 C CE2 . PHE B 48  ? 0.1799 0.1891 0.2007 -0.0222 -0.0132 -0.0101 48  PHE B CE2 
4491 C CZ  . PHE B 48  ? 0.2239 0.2326 0.2430 -0.0218 -0.0141 -0.0101 48  PHE B CZ  
4492 N N   . GLU B 49  ? 0.1883 0.1953 0.2107 -0.0236 -0.0110 -0.0137 49  GLU B N   
4493 C CA  . GLU B 49  ? 0.2741 0.2808 0.2970 -0.0239 -0.0101 -0.0144 49  GLU B CA  
4494 C C   . GLU B 49  ? 0.2603 0.2672 0.2825 -0.0238 -0.0103 -0.0140 49  GLU B C   
4495 O O   . GLU B 49  ? 0.2418 0.2485 0.2629 -0.0237 -0.0108 -0.0143 49  GLU B O   
4496 C CB  . GLU B 49  ? 0.3324 0.3387 0.3549 -0.0241 -0.0104 -0.0154 49  GLU B CB  
4497 C CG  . GLU B 49  ? 0.5097 0.5157 0.5336 -0.0244 -0.0092 -0.0164 49  GLU B CG  
4498 C CD  . GLU B 49  ? 0.6437 0.6497 0.6694 -0.0245 -0.0083 -0.0164 49  GLU B CD  
4499 O OE1 . GLU B 49  ? 0.6774 0.6836 0.7031 -0.0245 -0.0087 -0.0161 49  GLU B OE1 
4500 O OE2 . GLU B 49  ? 0.6742 0.6799 0.7012 -0.0247 -0.0072 -0.0167 49  GLU B OE2 
4501 N N   . ILE B 50  ? 0.1481 0.1554 0.1710 -0.0237 -0.0099 -0.0132 50  ILE B N   
4502 C CA  . ILE B 50  ? 0.1377 0.1453 0.1602 -0.0236 -0.0099 -0.0128 50  ILE B CA  
4503 C C   . ILE B 50  ? 0.1422 0.1500 0.1663 -0.0238 -0.0086 -0.0126 50  ILE B C   
4504 O O   . ILE B 50  ? 0.1624 0.1700 0.1878 -0.0239 -0.0079 -0.0128 50  ILE B O   
4505 C CB  . ILE B 50  ? 0.2629 0.2708 0.2844 -0.0231 -0.0110 -0.0118 50  ILE B CB  
4506 C CG1 . ILE B 50  ? 0.2683 0.2764 0.2905 -0.0230 -0.0109 -0.0111 50  ILE B CG1 
4507 C CG2 . ILE B 50  ? 0.2439 0.2513 0.2640 -0.0228 -0.0123 -0.0119 50  ILE B CG2 
4508 C CD1 . ILE B 50  ? 0.2644 0.2728 0.2861 -0.0225 -0.0118 -0.0102 50  ILE B CD1 
4509 N N   . LYS B 51  ? 0.1271 0.1352 0.1511 -0.0238 -0.0083 -0.0124 51  LYS B N   
4510 C CA  . LYS B 51  ? 0.1304 0.1387 0.1558 -0.0239 -0.0072 -0.0121 51  LYS B CA  
4511 C C   . LYS B 51  ? 0.1152 0.1241 0.1405 -0.0236 -0.0075 -0.0109 51  LYS B C   
4512 O O   . LYS B 51  ? 0.1448 0.1539 0.1688 -0.0234 -0.0086 -0.0105 51  LYS B O   
4513 C CB  . LYS B 51  ? 0.1431 0.1514 0.1686 -0.0242 -0.0065 -0.0126 51  LYS B CB  
4514 C CG  . LYS B 51  ? 0.2225 0.2302 0.2479 -0.0244 -0.0062 -0.0138 51  LYS B CG  
4515 C CD  . LYS B 51  ? 0.1977 0.2048 0.2248 -0.0245 -0.0053 -0.0143 51  LYS B CD  
4516 C CE  . LYS B 51  ? 0.3176 0.3241 0.3449 -0.0248 -0.0048 -0.0156 51  LYS B CE  
4517 N NZ  . LYS B 51  ? 0.4287 0.4353 0.4543 -0.0248 -0.0058 -0.0162 51  LYS B NZ  
4518 N N   . LEU B 52  ? 0.0715 0.0805 0.0981 -0.0236 -0.0067 -0.0105 52  LEU B N   
4519 C CA  . LEU B 52  ? 0.0772 0.0868 0.1040 -0.0234 -0.0069 -0.0094 52  LEU B CA  
4520 C C   . LEU B 52  ? 0.1331 0.1428 0.1616 -0.0234 -0.0055 -0.0091 52  LEU B C   
4521 O O   . LEU B 52  ? 0.1093 0.1185 0.1392 -0.0235 -0.0045 -0.0094 52  LEU B O   
4522 C CB  . LEU B 52  ? 0.1572 0.1671 0.1838 -0.0231 -0.0075 -0.0090 52  LEU B CB  
4523 C CG  . LEU B 52  ? 0.1082 0.1178 0.1332 -0.0229 -0.0089 -0.0091 52  LEU B CG  
4524 C CD1 . LEU B 52  ? 0.1334 0.1434 0.1586 -0.0228 -0.0093 -0.0088 52  LEU B CD1 
4525 C CD2 . LEU B 52  ? 0.1230 0.1328 0.1469 -0.0225 -0.0100 -0.0087 52  LEU B CD2 
4526 N N   . ASN B 53  ? 0.1075 0.1179 0.1361 -0.0234 -0.0054 -0.0084 53  ASN B N   
4527 C CA  . ASN B 53  ? 0.0721 0.0826 0.1024 -0.0233 -0.0041 -0.0079 53  ASN B CA  
4528 C C   . ASN B 53  ? 0.0728 0.0839 0.1036 -0.0230 -0.0041 -0.0068 53  ASN B C   
4529 O O   . ASN B 53  ? 0.1050 0.1166 0.1345 -0.0229 -0.0052 -0.0064 53  ASN B O   
4530 C CB  . ASN B 53  ? 0.0876 0.0982 0.1177 -0.0235 -0.0037 -0.0079 53  ASN B CB  
4531 C CG  . ASN B 53  ? 0.1014 0.1115 0.1307 -0.0238 -0.0038 -0.0091 53  ASN B CG  
4532 O OD1 . ASN B 53  ? 0.1408 0.1503 0.1712 -0.0239 -0.0029 -0.0098 53  ASN B OD1 
4533 N ND2 . ASN B 53  ? 0.0711 0.0816 0.0986 -0.0238 -0.0050 -0.0092 53  ASN B ND2 
4534 N N   . PHE B 54  ? 0.0544 0.0654 0.0871 -0.0229 -0.0029 -0.0064 54  PHE B N   
4535 C CA  . PHE B 54  ? 0.0537 0.0652 0.0872 -0.0225 -0.0027 -0.0053 54  PHE B CA  
4536 C C   . PHE B 54  ? 0.1282 0.1396 0.1624 -0.0219 -0.0017 -0.0042 54  PHE B C   
4537 O O   . PHE B 54  ? 0.1048 0.1155 0.1398 -0.0219 -0.0006 -0.0044 54  PHE B O   
4538 C CB  . PHE B 54  ? 0.0902 0.1014 0.1246 -0.0225 -0.0024 -0.0055 54  PHE B CB  
4539 C CG  . PHE B 54  ? 0.1035 0.1147 0.1364 -0.0226 -0.0035 -0.0062 54  PHE B CG  
4540 C CD1 . PHE B 54  ? 0.0725 0.0829 0.1050 -0.0229 -0.0036 -0.0072 54  PHE B CD1 
4541 C CD2 . PHE B 54  ? 0.1114 0.1234 0.1434 -0.0224 -0.0045 -0.0058 54  PHE B CD2 
4542 C CE1 . PHE B 54  ? 0.0892 0.0996 0.1205 -0.0230 -0.0046 -0.0078 54  PHE B CE1 
4543 C CE2 . PHE B 54  ? 0.1251 0.1370 0.1558 -0.0225 -0.0055 -0.0064 54  PHE B CE2 
4544 C CZ  . PHE B 54  ? 0.1324 0.1434 0.1627 -0.0228 -0.0056 -0.0073 54  PHE B CZ  
4545 N N   . ASN B 55  ? 0.0863 0.0984 0.1200 -0.0213 -0.0020 -0.0031 55  ASN B N   
4546 C CA  . ASN B 55  ? 0.0914 0.1035 0.1256 -0.0206 -0.0010 -0.0018 55  ASN B CA  
4547 C C   . ASN B 55  ? 0.1188 0.1311 0.1539 -0.0202 -0.0007 -0.0011 55  ASN B C   
4548 O O   . ASN B 55  ? 0.1211 0.1341 0.1557 -0.0203 -0.0017 -0.0010 55  ASN B O   
4549 C CB  . ASN B 55  ? 0.0615 0.0742 0.0942 -0.0202 -0.0016 -0.0009 55  ASN B CB  
4550 C CG  . ASN B 55  ? 0.0967 0.1095 0.1301 -0.0194 -0.0006 0.0003  55  ASN B CG  
4551 O OD1 . ASN B 55  ? 0.0867 0.0988 0.1207 -0.0193 0.0004  0.0002  55  ASN B OD1 
4552 N ND2 . ASN B 55  ? 0.0561 0.0695 0.0891 -0.0189 -0.0009 0.0014  55  ASN B ND2 
4553 N N   . LEU B 56  ? 0.0995 0.1111 0.1360 -0.0199 0.0006  -0.0005 56  LEU B N   
4554 C CA  . LEU B 56  ? 0.0988 0.1107 0.1363 -0.0195 0.0010  0.0004  56  LEU B CA  
4555 C C   . LEU B 56  ? 0.0637 0.0756 0.1013 -0.0187 0.0018  0.0018  56  LEU B C   
4556 O O   . LEU B 56  ? 0.1288 0.1399 0.1672 -0.0185 0.0028  0.0019  56  LEU B O   
4557 C CB  . LEU B 56  ? 0.1090 0.1202 0.1482 -0.0199 0.0019  -0.0002 56  LEU B CB  
4558 C CG  . LEU B 56  ? 0.1240 0.1351 0.1632 -0.0208 0.0012  -0.0016 56  LEU B CG  
4559 C CD1 . LEU B 56  ? 0.1764 0.1865 0.2174 -0.0212 0.0022  -0.0021 56  LEU B CD1 
4560 C CD2 . LEU B 56  ? 0.1577 0.1698 0.1964 -0.0208 0.0002  -0.0016 56  LEU B CD2 
4561 N N   . THR B 57  ? 0.0612 0.0740 0.0981 -0.0181 0.0014  0.0028  57  THR B N   
4562 C CA  . THR B 57  ? 0.0770 0.0899 0.1143 -0.0173 0.0022  0.0041  57  THR B CA  
4563 C C   . THR B 57  ? 0.0444 0.0567 0.0833 -0.0171 0.0034  0.0047  57  THR B C   
4564 O O   . THR B 57  ? 0.0762 0.0885 0.1158 -0.0174 0.0034  0.0044  57  THR B O   
4565 C CB  . THR B 57  ? 0.1054 0.1195 0.1415 -0.0167 0.0014  0.0051  57  THR B CB  
4566 O OG1 . THR B 57  ? 0.1111 0.1258 0.1474 -0.0167 0.0010  0.0053  57  THR B OG1 
4567 C CG2 . THR B 57  ? 0.0712 0.0857 0.1057 -0.0170 0.0001  0.0045  57  THR B CG2 
4568 N N   . PRO B 58  ? 0.0426 0.0544 0.0821 -0.0165 0.0045  0.0056  58  PRO B N   
4569 C CA  . PRO B 58  ? 0.0471 0.0582 0.0882 -0.0164 0.0057  0.0062  58  PRO B CA  
4570 C C   . PRO B 58  ? 0.1121 0.1242 0.1533 -0.0160 0.0056  0.0071  58  PRO B C   
4571 O O   . PRO B 58  ? 0.1132 0.1250 0.1556 -0.0162 0.0062  0.0072  58  PRO B O   
4572 C CB  . PRO B 58  ? 0.0721 0.0827 0.1137 -0.0157 0.0066  0.0070  58  PRO B CB  
4573 C CG  . PRO B 58  ? 0.0944 0.1048 0.1350 -0.0160 0.0062  0.0062  58  PRO B CG  
4574 C CD  . PRO B 58  ? 0.0357 0.0473 0.0748 -0.0162 0.0047  0.0058  58  PRO B CD  
4575 N N   . VAL B 59  ? 0.0807 0.0939 0.1207 -0.0154 0.0048  0.0078  59  VAL B N   
4576 C CA  . VAL B 59  ? 0.0672 0.0814 0.1072 -0.0150 0.0046  0.0087  59  VAL B CA  
4577 C C   . VAL B 59  ? 0.0935 0.1081 0.1334 -0.0156 0.0039  0.0077  59  VAL B C   
4578 O O   . VAL B 59  ? 0.0801 0.0953 0.1206 -0.0155 0.0041  0.0082  59  VAL B O   
4579 C CB  . VAL B 59  ? 0.0867 0.1019 0.1253 -0.0142 0.0040  0.0096  59  VAL B CB  
4580 C CG1 . VAL B 59  ? 0.0936 0.1092 0.1307 -0.0145 0.0026  0.0088  59  VAL B CG1 
4581 C CG2 . VAL B 59  ? 0.1012 0.1174 0.1397 -0.0137 0.0038  0.0105  59  VAL B CG2 
4582 N N   . LEU B 60  ? 0.0505 0.0650 0.0897 -0.0162 0.0030  0.0065  60  LEU B N   
4583 C CA  . LEU B 60  ? 0.0513 0.0662 0.0907 -0.0168 0.0024  0.0055  60  LEU B CA  
4584 C C   . LEU B 60  ? 0.0997 0.1137 0.1408 -0.0173 0.0034  0.0051  60  LEU B C   
4585 O O   . LEU B 60  ? 0.0901 0.1045 0.1320 -0.0175 0.0035  0.0051  60  LEU B O   
4586 C CB  . LEU B 60  ? 0.1159 0.1308 0.1542 -0.0174 0.0011  0.0043  60  LEU B CB  
4587 C CG  . LEU B 60  ? 0.0846 0.0997 0.1232 -0.0181 0.0005  0.0031  60  LEU B CG  
4588 C CD1 . LEU B 60  ? 0.0705 0.0867 0.1090 -0.0177 0.0001  0.0036  60  LEU B CD1 
4589 C CD2 . LEU B 60  ? 0.0894 0.1045 0.1268 -0.0187 -0.0007 0.0020  60  LEU B CD2 
4590 N N   . ILE B 61  ? 0.0762 0.0890 0.1180 -0.0176 0.0042  0.0048  61  ILE B N   
4591 C CA  . ILE B 61  ? 0.0896 0.1014 0.1331 -0.0181 0.0052  0.0043  61  ILE B CA  
4592 C C   . ILE B 61  ? 0.0503 0.0623 0.0949 -0.0177 0.0061  0.0055  61  ILE B C   
4593 O O   . ILE B 61  ? 0.0950 0.1070 0.1407 -0.0182 0.0064  0.0052  61  ILE B O   
4594 C CB  . ILE B 61  ? 0.0974 0.1080 0.1414 -0.0183 0.0059  0.0039  61  ILE B CB  
4595 C CG1 . ILE B 61  ? 0.0831 0.0936 0.1260 -0.0188 0.0049  0.0026  61  ILE B CG1 
4596 C CG2 . ILE B 61  ? 0.1555 0.1649 0.2014 -0.0188 0.0070  0.0036  61  ILE B CG2 
4597 C CD1 . ILE B 61  ? 0.1227 0.1320 0.1660 -0.0190 0.0056  0.0021  61  ILE B CD1 
4598 N N   . ASP B 62  ? 0.0953 0.1076 0.1398 -0.0169 0.0066  0.0069  62  ASP B N   
4599 C CA  . ASP B 62  ? 0.0868 0.0993 0.1322 -0.0165 0.0075  0.0081  62  ASP B CA  
4600 C C   . ASP B 62  ? 0.1286 0.1423 0.1739 -0.0166 0.0070  0.0081  62  ASP B C   
4601 O O   . ASP B 62  ? 0.0994 0.1131 0.1460 -0.0168 0.0077  0.0084  62  ASP B O   
4602 C CB  . ASP B 62  ? 0.1078 0.1206 0.1526 -0.0155 0.0078  0.0096  62  ASP B CB  
4603 C CG  . ASP B 62  ? 0.2016 0.2131 0.2469 -0.0153 0.0087  0.0099  62  ASP B CG  
4604 O OD1 . ASP B 62  ? 0.1709 0.1812 0.2174 -0.0158 0.0094  0.0093  62  ASP B OD1 
4605 O OD2 . ASP B 62  ? 0.1491 0.1609 0.1935 -0.0146 0.0086  0.0107  62  ASP B OD2 
4606 N N   . GLN B 63  ? 0.1066 0.1214 0.1504 -0.0164 0.0057  0.0078  63  GLN B N   
4607 C CA  . GLN B 63  ? 0.0952 0.1113 0.1388 -0.0164 0.0051  0.0078  63  GLN B CA  
4608 C C   . GLN B 63  ? 0.0829 0.0989 0.1275 -0.0173 0.0049  0.0065  63  GLN B C   
4609 O O   . GLN B 63  ? 0.1035 0.1201 0.1490 -0.0174 0.0053  0.0067  63  GLN B O   
4610 C CB  . GLN B 63  ? 0.0685 0.0857 0.1103 -0.0160 0.0037  0.0077  63  GLN B CB  
4611 C CG  . GLN B 63  ? 0.0441 0.0615 0.0851 -0.0151 0.0038  0.0089  63  GLN B CG  
4612 C CD  . GLN B 63  ? 0.1501 0.1685 0.1894 -0.0148 0.0024  0.0087  63  GLN B CD  
4613 O OE1 . GLN B 63  ? 0.1243 0.1437 0.1631 -0.0146 0.0017  0.0087  63  GLN B OE1 
4614 N NE2 . GLN B 63  ? 0.0928 0.1107 0.1311 -0.0148 0.0019  0.0085  63  GLN B NE2 
4615 N N   . ILE B 64  ? 0.0700 0.0852 0.1144 -0.0179 0.0045  0.0052  64  ILE B N   
4616 C CA  . ILE B 64  ? 0.0677 0.0827 0.1130 -0.0188 0.0043  0.0040  64  ILE B CA  
4617 C C   . ILE B 64  ? 0.1047 0.1191 0.1520 -0.0191 0.0057  0.0044  64  ILE B C   
4618 O O   . ILE B 64  ? 0.1083 0.1232 0.1566 -0.0195 0.0058  0.0041  64  ILE B O   
4619 C CB  . ILE B 64  ? 0.1326 0.1468 0.1774 -0.0194 0.0038  0.0027  64  ILE B CB  
4620 C CG1 . ILE B 64  ? 0.0593 0.0743 0.1022 -0.0192 0.0023  0.0023  64  ILE B CG1 
4621 C CG2 . ILE B 64  ? 0.1770 0.1908 0.2230 -0.0203 0.0038  0.0014  64  ILE B CG2 
4622 C CD1 . ILE B 64  ? 0.0821 0.0963 0.1243 -0.0197 0.0017  0.0012  64  ILE B CD1 
4623 N N   . GLN B 65  ? 0.1388 0.1521 0.1867 -0.0189 0.0068  0.0051  65  GLN B N   
4624 C CA  . GLN B 65  ? 0.1236 0.1360 0.1734 -0.0192 0.0081  0.0055  65  GLN B CA  
4625 C C   . GLN B 65  ? 0.1454 0.1589 0.1958 -0.0188 0.0086  0.0067  65  GLN B C   
4626 O O   . GLN B 65  ? 0.1442 0.1576 0.1955 -0.0192 0.0091  0.0065  65  GLN B O   
4627 C CB  . GLN B 65  ? 0.1668 0.1778 0.2170 -0.0189 0.0091  0.0062  65  GLN B CB  
4628 C CG  . GLN B 65  ? 0.1325 0.1423 0.1824 -0.0193 0.0089  0.0049  65  GLN B CG  
4629 C CD  . GLN B 65  ? 0.2120 0.2205 0.2625 -0.0190 0.0099  0.0055  65  GLN B CD  
4630 O OE1 . GLN B 65  ? 0.1926 0.2013 0.2424 -0.0182 0.0100  0.0066  65  GLN B OE1 
4631 N NE2 . GLN B 65  ? 0.2878 0.2948 0.3390 -0.0193 0.0105  0.0049  65  GLN B NE2 
4632 N N   . GLU B 66  ? 0.0970 0.1114 0.1462 -0.0179 0.0083  0.0078  66  GLU B N   
4633 C CA  . GLU B 66  ? 0.1018 0.1174 0.1514 -0.0175 0.0087  0.0089  66  GLU B CA  
4634 C C   . GLU B 66  ? 0.0863 0.1032 0.1360 -0.0179 0.0080  0.0081  66  GLU B C   
4635 O O   . GLU B 66  ? 0.1406 0.1580 0.1914 -0.0181 0.0087  0.0085  66  GLU B O   
4636 C CB  . GLU B 66  ? 0.1010 0.1175 0.1492 -0.0164 0.0084  0.0101  66  GLU B CB  
4637 C CG  . GLU B 66  ? 0.2876 0.3049 0.3362 -0.0159 0.0092  0.0115  66  GLU B CG  
4638 C CD  . GLU B 66  ? 0.3225 0.3404 0.3700 -0.0148 0.0092  0.0128  66  GLU B CD  
4639 O OE1 . GLU B 66  ? 0.1699 0.1874 0.2163 -0.0145 0.0087  0.0127  66  GLU B OE1 
4640 O OE2 . GLU B 66  ? 0.3818 0.4006 0.4295 -0.0143 0.0097  0.0140  66  GLU B OE2 
4641 N N   . TYR B 67  ? 0.0852 0.1026 0.1337 -0.0180 0.0067  0.0070  67  TYR B N   
4642 C CA  . TYR B 67  ? 0.1287 0.1473 0.1774 -0.0184 0.0060  0.0061  67  TYR B CA  
4643 C C   . TYR B 67  ? 0.1742 0.1921 0.2246 -0.0194 0.0065  0.0052  67  TYR B C   
4644 O O   . TYR B 67  ? 0.1470 0.1657 0.1983 -0.0197 0.0068  0.0051  67  TYR B O   
4645 C CB  . TYR B 67  ? 0.1115 0.1306 0.1585 -0.0184 0.0044  0.0050  67  TYR B CB  
4646 C CG  . TYR B 67  ? 0.0815 0.1018 0.1270 -0.0175 0.0036  0.0057  67  TYR B CG  
4647 C CD1 . TYR B 67  ? 0.0850 0.1069 0.1303 -0.0172 0.0031  0.0058  67  TYR B CD1 
4648 C CD2 . TYR B 67  ? 0.1613 0.1813 0.2054 -0.0169 0.0033  0.0063  67  TYR B CD2 
4649 C CE1 . TYR B 67  ? 0.0998 0.1227 0.1436 -0.0164 0.0023  0.0064  67  TYR B CE1 
4650 C CE2 . TYR B 67  ? 0.1282 0.1492 0.1709 -0.0161 0.0025  0.0069  67  TYR B CE2 
4651 C CZ  . TYR B 67  ? 0.0943 0.1168 0.1368 -0.0158 0.0020  0.0069  67  TYR B CZ  
4652 O OH  . TYR B 67  ? 0.0859 0.1095 0.1271 -0.0150 0.0012  0.0074  67  TYR B OH  
4653 N N   . ALA B 68  ? 0.1349 0.1512 0.1853 -0.0198 0.0067  0.0044  68  ALA B N   
4654 C CA  . ALA B 68  ? 0.1571 0.1725 0.2079 -0.0205 0.0069  0.0034  68  ALA B CA  
4655 C C   . ALA B 68  ? 0.1396 0.1546 0.1918 -0.0205 0.0083  0.0042  68  ALA B C   
4656 O O   . ALA B 68  ? 0.1789 0.1938 0.2317 -0.0210 0.0084  0.0036  68  ALA B O   
4657 C CB  . ALA B 68  ? 0.1620 0.1758 0.2123 -0.0208 0.0068  0.0024  68  ALA B CB  
4658 N N   . GLN B 69  ? 0.1180 0.1327 0.1705 -0.0200 0.0092  0.0057  69  GLN B N   
4659 C CA  . GLN B 69  ? 0.1739 0.1882 0.2276 -0.0199 0.0104  0.0068  69  GLN B CA  
4660 C C   . GLN B 69  ? 0.2401 0.2561 0.2941 -0.0196 0.0106  0.0076  69  GLN B C   
4661 O O   . GLN B 69  ? 0.3648 0.3807 0.4196 -0.0195 0.0116  0.0086  69  GLN B O   
4662 C CB  . GLN B 69  ? 0.1952 0.2083 0.2489 -0.0193 0.0113  0.0080  69  GLN B CB  
4663 C CG  . GLN B 69  ? 0.2062 0.2175 0.2598 -0.0196 0.0114  0.0071  69  GLN B CG  
4664 C CD  . GLN B 69  ? 0.3785 0.3889 0.4321 -0.0190 0.0120  0.0082  69  GLN B CD  
4665 O OE1 . GLN B 69  ? 0.5389 0.5499 0.5926 -0.0183 0.0125  0.0097  69  GLN B OE1 
4666 N NE2 . GLN B 69  ? 0.3735 0.3825 0.4270 -0.0191 0.0120  0.0074  69  GLN B NE2 
4667 N N   . GLY B 70  ? 0.2259 0.2436 0.2793 -0.0195 0.0096  0.0073  70  GLY B N   
4668 C CA  . GLY B 70  ? 0.2183 0.2379 0.2721 -0.0192 0.0097  0.0081  70  GLY B CA  
4669 C C   . GLY B 70  ? 0.2610 0.2812 0.3148 -0.0183 0.0103  0.0099  70  GLY B C   
4670 O O   . GLY B 70  ? 0.2696 0.2913 0.3237 -0.0180 0.0107  0.0108  70  GLY B O   
4671 N N   . LYS B 71  ? 0.2188 0.2380 0.2719 -0.0179 0.0104  0.0105  71  LYS B N   
4672 C CA  . LYS B 71  ? 0.2604 0.2799 0.3128 -0.0169 0.0110  0.0121  71  LYS B CA  
4673 C C   . LYS B 71  ? 0.3781 0.3987 0.4285 -0.0160 0.0099  0.0123  71  LYS B C   
4674 O O   . LYS B 71  ? 0.3956 0.4167 0.4454 -0.0152 0.0102  0.0136  71  LYS B O   
4675 C CB  . LYS B 71  ? 0.3502 0.3678 0.4030 -0.0168 0.0118  0.0127  71  LYS B CB  
4676 C CG  . LYS B 71  ? 0.4407 0.4567 0.4946 -0.0173 0.0129  0.0126  71  LYS B CG  
4677 C CD  . LYS B 71  ? 0.4691 0.4834 0.5230 -0.0170 0.0135  0.0131  71  LYS B CD  
4678 C CE  . LYS B 71  ? 0.5195 0.5320 0.5744 -0.0175 0.0143  0.0127  71  LYS B CE  
4679 N NZ  . LYS B 71  ? 0.5683 0.5790 0.6233 -0.0173 0.0148  0.0129  71  LYS B NZ  
4680 N N   . ALA B 72  ? 0.1783 0.1993 0.2277 -0.0162 0.0085  0.0110  72  ALA B N   
4681 C CA  . ALA B 72  ? 0.1113 0.1332 0.1588 -0.0154 0.0074  0.0111  72  ALA B CA  
4682 C C   . ALA B 72  ? 0.2465 0.2703 0.2936 -0.0149 0.0071  0.0115  72  ALA B C   
4683 O O   . ALA B 72  ? 0.2929 0.3175 0.3406 -0.0154 0.0068  0.0107  72  ALA B O   
4684 C CB  . ALA B 72  ? 0.1427 0.1644 0.1892 -0.0158 0.0061  0.0096  72  ALA B CB  
4685 N N   . LYS B 73  ? 0.1172 0.1418 0.1634 -0.0140 0.0072  0.0127  73  LYS B N   
4686 C CA  . LYS B 73  ? 0.1238 0.1503 0.1694 -0.0133 0.0068  0.0131  73  LYS B CA  
4687 C C   . LYS B 73  ? 0.2004 0.2275 0.2442 -0.0129 0.0052  0.0124  73  LYS B C   
4688 O O   . LYS B 73  ? 0.2247 0.2520 0.2673 -0.0121 0.0048  0.0131  73  LYS B O   
4689 C CB  . LYS B 73  ? 0.2178 0.2448 0.2635 -0.0126 0.0078  0.0148  73  LYS B CB  
4690 C CG  . LYS B 73  ? 0.3455 0.3716 0.3929 -0.0130 0.0094  0.0157  73  LYS B CG  
4691 C CD  . LYS B 73  ? 0.5372 0.5631 0.5844 -0.0121 0.0102  0.0174  73  LYS B CD  
4692 C CE  . LYS B 73  ? 0.5886 0.6128 0.6373 -0.0126 0.0116  0.0181  73  LYS B CE  
4693 N NZ  . LYS B 73  ? 0.5776 0.6000 0.6265 -0.0132 0.0114  0.0170  73  LYS B NZ  
4694 N N   . ASP B 74  ? 0.1151 0.1426 0.1587 -0.0134 0.0042  0.0110  74  ASP B N   
4695 C CA  . ASP B 74  ? 0.0621 0.0899 0.1041 -0.0131 0.0026  0.0102  74  ASP B CA  
4696 C C   . ASP B 74  ? 0.1285 0.1582 0.1699 -0.0125 0.0019  0.0102  74  ASP B C   
4697 O O   . ASP B 74  ? 0.1357 0.1662 0.1778 -0.0128 0.0019  0.0096  74  ASP B O   
4698 C CB  . ASP B 74  ? 0.0780 0.1050 0.1203 -0.0140 0.0019  0.0086  74  ASP B CB  
4699 C CG  . ASP B 74  ? 0.1104 0.1375 0.1510 -0.0139 0.0002  0.0077  74  ASP B CG  
4700 O OD1 . ASP B 74  ? 0.1500 0.1784 0.1896 -0.0133 -0.0007 0.0078  74  ASP B OD1 
4701 O OD2 . ASP B 74  ? 0.1447 0.1707 0.1851 -0.0145 -0.0003 0.0069  74  ASP B OD2 
4702 N N   . VAL B 75  ? 0.1612 0.1915 0.2011 -0.0116 0.0013  0.0109  75  VAL B N   
4703 C CA  . VAL B 75  ? 0.1451 0.1772 0.1844 -0.0108 0.0009  0.0111  75  VAL B CA  
4704 C C   . VAL B 75  ? 0.1097 0.1424 0.1485 -0.0110 -0.0006 0.0096  75  VAL B C   
4705 O O   . VAL B 75  ? 0.1395 0.1736 0.1786 -0.0108 -0.0007 0.0094  75  VAL B O   
4706 C CB  . VAL B 75  ? 0.2130 0.2456 0.2510 -0.0098 0.0006  0.0121  75  VAL B CB  
4707 C CG1 . VAL B 75  ? 0.2579 0.2900 0.2965 -0.0095 0.0020  0.0136  75  VAL B CG1 
4708 C CG2 . VAL B 75  ? 0.2321 0.2639 0.2687 -0.0097 -0.0007 0.0116  75  VAL B CG2 
4709 N N   . PHE B 76  ? 0.1608 0.1926 0.1988 -0.0113 -0.0017 0.0087  76  PHE B N   
4710 C CA  . PHE B 76  ? 0.1582 0.1905 0.1957 -0.0115 -0.0031 0.0074  76  PHE B CA  
4711 C C   . PHE B 76  ? 0.1721 0.2046 0.2111 -0.0123 -0.0026 0.0065  76  PHE B C   
4712 O O   . PHE B 76  ? 0.1642 0.1978 0.2034 -0.0123 -0.0032 0.0058  76  PHE B O   
4713 C CB  . PHE B 76  ? 0.1498 0.1811 0.1861 -0.0118 -0.0043 0.0066  76  PHE B CB  
4714 C CG  . PHE B 76  ? 0.3107 0.3426 0.3463 -0.0118 -0.0059 0.0053  76  PHE B CG  
4715 C CD1 . PHE B 76  ? 0.3614 0.3944 0.3959 -0.0110 -0.0069 0.0054  76  PHE B CD1 
4716 C CD2 . PHE B 76  ? 0.2846 0.3159 0.3208 -0.0127 -0.0063 0.0041  76  PHE B CD2 
4717 C CE1 . PHE B 76  ? 0.3485 0.3819 0.3824 -0.0110 -0.0084 0.0042  76  PHE B CE1 
4718 C CE2 . PHE B 76  ? 0.3389 0.3707 0.3745 -0.0127 -0.0077 0.0030  76  PHE B CE2 
4719 C CZ  . PHE B 76  ? 0.3548 0.3877 0.3892 -0.0118 -0.0088 0.0030  76  PHE B CZ  
4720 N N   . LEU B 77  ? 0.1253 0.1565 0.1655 -0.0131 -0.0017 0.0065  77  LEU B N   
4721 C CA  . LEU B 77  ? 0.1764 0.2076 0.2181 -0.0140 -0.0012 0.0057  77  LEU B CA  
4722 C C   . LEU B 77  ? 0.1694 0.2021 0.2122 -0.0137 -0.0003 0.0062  77  LEU B C   
4723 O O   . LEU B 77  ? 0.1192 0.1527 0.1628 -0.0141 -0.0005 0.0054  77  LEU B O   
4724 C CB  . LEU B 77  ? 0.1705 0.2000 0.2132 -0.0148 -0.0002 0.0057  77  LEU B CB  
4725 C CG  . LEU B 77  ? 0.2124 0.2416 0.2565 -0.0158 -0.0001 0.0046  77  LEU B CG  
4726 C CD1 . LEU B 77  ? 0.1833 0.2128 0.2266 -0.0160 -0.0017 0.0031  77  LEU B CD1 
4727 C CD2 . LEU B 77  ? 0.1655 0.1929 0.2104 -0.0165 0.0008  0.0046  77  LEU B CD2 
4728 N N   . GLU B 78  ? 0.1622 0.1954 0.2050 -0.0131 0.0006  0.0076  78  GLU B N   
4729 C CA  . GLU B 78  ? 0.1825 0.2172 0.2261 -0.0127 0.0014  0.0083  78  GLU B CA  
4730 C C   . GLU B 78  ? 0.1609 0.1973 0.2037 -0.0122 0.0003  0.0076  78  GLU B C   
4731 O O   . GLU B 78  ? 0.2263 0.2640 0.2701 -0.0123 0.0005  0.0073  78  GLU B O   
4732 C CB  . GLU B 78  ? 0.2323 0.2672 0.2758 -0.0121 0.0025  0.0100  78  GLU B CB  
4733 C CG  . GLU B 78  ? 0.4865 0.5227 0.5312 -0.0119 0.0038  0.0109  78  GLU B CG  
4734 C CD  . GLU B 78  ? 0.6203 0.6560 0.6669 -0.0130 0.0047  0.0105  78  GLU B CD  
4735 O OE1 . GLU B 78  ? 0.6841 0.7181 0.7313 -0.0137 0.0049  0.0101  78  GLU B OE1 
4736 O OE2 . GLU B 78  ? 0.6475 0.6846 0.6951 -0.0130 0.0052  0.0106  78  GLU B OE2 
4737 N N   . ALA B 79  ? 0.1250 0.1615 0.1661 -0.0116 -0.0011 0.0073  79  ALA B N   
4738 C CA  . ALA B 79  ? 0.1407 0.1787 0.1810 -0.0110 -0.0023 0.0065  79  ALA B CA  
4739 C C   . ALA B 79  ? 0.2469 0.2849 0.2877 -0.0117 -0.0031 0.0050  79  ALA B C   
4740 O O   . ALA B 79  ? 0.2028 0.2423 0.2438 -0.0114 -0.0036 0.0043  79  ALA B O   
4741 C CB  . ALA B 79  ? 0.1847 0.2225 0.2230 -0.0103 -0.0037 0.0065  79  ALA B CB  
4742 N N   . ILE B 80  ? 0.1308 0.1672 0.1719 -0.0126 -0.0033 0.0043  80  ILE B N   
4743 C CA  . ILE B 80  ? 0.1450 0.1814 0.1868 -0.0133 -0.0040 0.0029  80  ILE B CA  
4744 C C   . ILE B 80  ? 0.1492 0.1864 0.1930 -0.0139 -0.0028 0.0028  80  ILE B C   
4745 O O   . ILE B 80  ? 0.1781 0.2163 0.2224 -0.0140 -0.0032 0.0019  80  ILE B O   
4746 C CB  . ILE B 80  ? 0.0948 0.1294 0.1363 -0.0141 -0.0044 0.0022  80  ILE B CB  
4747 C CG1 . ILE B 80  ? 0.1500 0.1841 0.1895 -0.0136 -0.0059 0.0019  80  ILE B CG1 
4748 C CG2 . ILE B 80  ? 0.0811 0.1154 0.1237 -0.0150 -0.0047 0.0009  80  ILE B CG2 
4749 C CD1 . ILE B 80  ? 0.1616 0.1940 0.2008 -0.0143 -0.0064 0.0013  80  ILE B CD1 
4750 N N   . ARG B 81  ? 0.0829 0.1194 0.1277 -0.0142 -0.0012 0.0039  81  ARG B N   
4751 C CA  . ARG B 81  ? 0.1615 0.1984 0.2084 -0.0149 0.0000  0.0038  81  ARG B CA  
4752 C C   . ARG B 81  ? 0.1389 0.1780 0.1865 -0.0144 0.0004  0.0042  81  ARG B C   
4753 O O   . ARG B 81  ? 0.1562 0.1961 0.2051 -0.0150 0.0007  0.0036  81  ARG B O   
4754 C CB  . ARG B 81  ? 0.1542 0.1898 0.2020 -0.0154 0.0015  0.0049  81  ARG B CB  
4755 C CG  . ARG B 81  ? 0.3318 0.3674 0.3818 -0.0163 0.0026  0.0048  81  ARG B CG  
4756 C CD  . ARG B 81  ? 0.4292 0.4635 0.4801 -0.0165 0.0042  0.0061  81  ARG B CD  
4757 N NE  . ARG B 81  ? 0.4759 0.5081 0.5265 -0.0170 0.0041  0.0058  81  ARG B NE  
4758 C CZ  . ARG B 81  ? 0.6118 0.6429 0.6635 -0.0180 0.0042  0.0048  81  ARG B CZ  
4759 N NH1 . ARG B 81  ? 0.5672 0.5990 0.6203 -0.0187 0.0044  0.0041  81  ARG B NH1 
4760 N NH2 . ARG B 81  ? 0.6506 0.6799 0.7018 -0.0183 0.0041  0.0046  81  ARG B NH2 
4761 N N   . LYS B 82  ? 0.1098 0.1498 0.1563 -0.0134 0.0005  0.0052  82  LYS B N   
4762 C CA  . LYS B 82  ? 0.1603 0.2024 0.2074 -0.0129 0.0012  0.0058  82  LYS B CA  
4763 C C   . LYS B 82  ? 0.1539 0.1976 0.2012 -0.0129 0.0001  0.0045  82  LYS B C   
4764 O O   . LYS B 82  ? 0.1166 0.1599 0.1628 -0.0127 -0.0014 0.0033  82  LYS B O   
4765 C CB  . LYS B 82  ? 0.1947 0.2376 0.2404 -0.0118 0.0011  0.0069  82  LYS B CB  
4766 C CG  . LYS B 82  ? 0.3417 0.3838 0.3876 -0.0116 0.0025  0.0085  82  LYS B CG  
4767 C CD  . LYS B 82  ? 0.3397 0.3827 0.3839 -0.0104 0.0021  0.0094  82  LYS B CD  
4768 C CE  . LYS B 82  ? 0.3184 0.3604 0.3624 -0.0101 0.0031  0.0109  82  LYS B CE  
4769 N NZ  . LYS B 82  ? 0.3410 0.3843 0.3837 -0.0089 0.0030  0.0118  82  LYS B NZ  
4770 N N   . ASP B 83  ? 0.1589 0.2043 0.2074 -0.0129 0.0009  0.0047  83  ASP B N   
4771 C CA  . ASP B 83  ? 0.1799 0.2272 0.2283 -0.0124 0.0000  0.0037  83  ASP B CA  
4772 C C   . ASP B 83  ? 0.1457 0.1938 0.1922 -0.0112 -0.0010 0.0038  83  ASP B C   
4773 O O   . ASP B 83  ? 0.1186 0.1667 0.1643 -0.0105 -0.0004 0.0051  83  ASP B O   
4774 C CB  . ASP B 83  ? 0.1780 0.2272 0.2280 -0.0126 0.0012  0.0041  83  ASP B CB  
4775 C CG  . ASP B 83  ? 0.2333 0.2845 0.2836 -0.0123 0.0003  0.0029  83  ASP B CG  
4776 O OD1 . ASP B 83  ? 0.1921 0.2447 0.2412 -0.0112 -0.0005 0.0027  83  ASP B OD1 
4777 O OD2 . ASP B 83  ? 0.2689 0.3204 0.3207 -0.0131 0.0004  0.0020  83  ASP B OD2 
4778 N N   . PRO B 84  ? 0.1371 0.1857 0.1826 -0.0108 -0.0026 0.0026  84  PRO B N   
4779 C CA  . PRO B 84  ? 0.1143 0.1635 0.1579 -0.0096 -0.0037 0.0027  84  PRO B CA  
4780 C C   . PRO B 84  ? 0.1667 0.2179 0.2102 -0.0087 -0.0029 0.0036  84  PRO B C   
4781 O O   . PRO B 84  ? 0.1007 0.1521 0.1428 -0.0078 -0.0033 0.0042  84  PRO B O   
4782 C CB  . PRO B 84  ? 0.1663 0.2158 0.2093 -0.0095 -0.0054 0.0010  84  PRO B CB  
4783 C CG  . PRO B 84  ? 0.1402 0.1883 0.1843 -0.0107 -0.0055 0.0002  84  PRO B CG  
4784 C CD  . PRO B 84  ? 0.2159 0.2642 0.2619 -0.0114 -0.0037 0.0010  84  PRO B CD  
4785 N N   . ASP B 85  ? 0.1436 0.1964 0.1887 -0.0089 -0.0019 0.0038  85  ASP B N   
4786 C CA  . ASP B 85  ? 0.1328 0.1876 0.1779 -0.0081 -0.0010 0.0048  85  ASP B CA  
4787 C C   . ASP B 85  ? 0.1444 0.1984 0.1891 -0.0079 0.0001  0.0065  85  ASP B C   
4788 O O   . ASP B 85  ? 0.1665 0.2218 0.2104 -0.0069 0.0005  0.0074  85  ASP B O   
4789 C CB  . ASP B 85  ? 0.1968 0.2533 0.2438 -0.0085 0.0001  0.0048  85  ASP B CB  
4790 C CG  . ASP B 85  ? 0.3250 0.3829 0.3723 -0.0084 -0.0010 0.0032  85  ASP B CG  
4791 O OD1 . ASP B 85  ? 0.3044 0.3623 0.3502 -0.0077 -0.0026 0.0023  85  ASP B OD1 
4792 O OD2 . ASP B 85  ? 0.3709 0.4299 0.4199 -0.0091 -0.0003 0.0029  85  ASP B OD2 
4793 N N   . ASP B 86  ? 0.1268 0.1787 0.1719 -0.0087 0.0007  0.0070  86  ASP B N   
4794 C CA  . ASP B 86  ? 0.0940 0.1449 0.1389 -0.0086 0.0019  0.0086  86  ASP B CA  
4795 C C   . ASP B 86  ? 0.1517 0.2012 0.1949 -0.0081 0.0009  0.0087  86  ASP B C   
4796 O O   . ASP B 86  ? 0.1652 0.2139 0.2081 -0.0080 0.0017  0.0100  86  ASP B O   
4797 C CB  . ASP B 86  ? 0.1030 0.1527 0.1497 -0.0098 0.0032  0.0091  86  ASP B CB  
4798 C CG  . ASP B 86  ? 0.2980 0.3492 0.3465 -0.0102 0.0044  0.0094  86  ASP B CG  
4799 O OD1 . ASP B 86  ? 0.3490 0.4024 0.3973 -0.0094 0.0047  0.0097  86  ASP B OD1 
4800 O OD2 . ASP B 86  ? 0.3533 0.4037 0.4035 -0.0113 0.0052  0.0092  86  ASP B OD2 
4801 N N   . LEU B 87  ? 0.1075 0.1566 0.1495 -0.0079 -0.0008 0.0075  87  LEU B N   
4802 C CA  . LEU B 87  ? 0.1114 0.1592 0.1518 -0.0075 -0.0017 0.0076  87  LEU B CA  
4803 C C   . LEU B 87  ? 0.1653 0.2141 0.2044 -0.0063 -0.0017 0.0086  87  LEU B C   
4804 O O   . LEU B 87  ? 0.1085 0.1593 0.1472 -0.0055 -0.0020 0.0084  87  LEU B O   
4805 C CB  . LEU B 87  ? 0.0924 0.1397 0.1319 -0.0075 -0.0036 0.0060  87  LEU B CB  
4806 C CG  . LEU B 87  ? 0.1402 0.1859 0.1804 -0.0087 -0.0038 0.0051  87  LEU B CG  
4807 C CD1 . LEU B 87  ? 0.1260 0.1716 0.1653 -0.0086 -0.0056 0.0036  87  LEU B CD1 
4808 C CD2 . LEU B 87  ? 0.0880 0.1316 0.1280 -0.0091 -0.0033 0.0058  87  LEU B CD2 
4809 N N   . GLU B 88  ? 0.0947 0.1423 0.1330 -0.0061 -0.0015 0.0096  88  GLU B N   
4810 C CA  . GLU B 88  ? 0.1453 0.1937 0.1821 -0.0050 -0.0018 0.0103  88  GLU B CA  
4811 C C   . GLU B 88  ? 0.1680 0.2162 0.2033 -0.0045 -0.0038 0.0092  88  GLU B C   
4812 O O   . GLU B 88  ? 0.1509 0.1978 0.1860 -0.0051 -0.0047 0.0082  88  GLU B O   
4813 C CB  . GLU B 88  ? 0.1357 0.1827 0.1723 -0.0050 -0.0009 0.0117  88  GLU B CB  
4814 C CG  . GLU B 88  ? 0.1528 0.1997 0.1910 -0.0055 0.0009  0.0128  88  GLU B CG  
4815 C CD  . GLU B 88  ? 0.2618 0.3068 0.3001 -0.0059 0.0017  0.0139  88  GLU B CD  
4816 O OE1 . GLU B 88  ? 0.3188 0.3635 0.3584 -0.0063 0.0032  0.0148  88  GLU B OE1 
4817 O OE2 . GLU B 88  ? 0.2678 0.3117 0.3050 -0.0057 0.0008  0.0137  88  GLU B OE2 
4818 N N   . LYS B 89  ? 0.1156 0.1651 0.1496 -0.0034 -0.0043 0.0094  89  LYS B N   
4819 C CA  . LYS B 89  ? 0.1777 0.2271 0.2102 -0.0028 -0.0062 0.0085  89  LYS B CA  
4820 C C   . LYS B 89  ? 0.2389 0.2861 0.2707 -0.0033 -0.0067 0.0086  89  LYS B C   
4821 O O   . LYS B 89  ? 0.2120 0.2583 0.2431 -0.0035 -0.0082 0.0075  89  LYS B O   
4822 C CB  . LYS B 89  ? 0.2209 0.2718 0.2521 -0.0015 -0.0065 0.0090  89  LYS B CB  
4823 C CG  . LYS B 89  ? 0.3755 0.4264 0.4051 -0.0009 -0.0084 0.0081  89  LYS B CG  
4824 C CD  . LYS B 89  ? 0.5138 0.5659 0.5435 -0.0006 -0.0094 0.0066  89  LYS B CD  
4825 C CE  . LYS B 89  ? 0.5952 0.6483 0.6233 0.0006  -0.0108 0.0062  89  LYS B CE  
4826 N NZ  . LYS B 89  ? 0.6196 0.6748 0.6476 0.0016  -0.0099 0.0071  89  LYS B NZ  
4827 N N   . GLU B 90  ? 0.1467 0.1931 0.1787 -0.0034 -0.0056 0.0099  90  GLU B N   
4828 C CA  . GLU B 90  ? 0.2400 0.2845 0.2715 -0.0038 -0.0060 0.0100  90  GLU B CA  
4829 C C   . GLU B 90  ? 0.2281 0.2712 0.2604 -0.0050 -0.0061 0.0091  90  GLU B C   
4830 O O   . GLU B 90  ? 0.1981 0.2398 0.2298 -0.0054 -0.0070 0.0086  90  GLU B O   
4831 C CB  . GLU B 90  ? 0.2494 0.2934 0.2811 -0.0037 -0.0046 0.0116  90  GLU B CB  
4832 C CG  . GLU B 90  ? 0.4038 0.4489 0.4344 -0.0026 -0.0046 0.0126  90  GLU B CG  
4833 C CD  . GLU B 90  ? 0.4851 0.5295 0.5160 -0.0026 -0.0033 0.0142  90  GLU B CD  
4834 O OE1 . GLU B 90  ? 0.4942 0.5371 0.5261 -0.0034 -0.0025 0.0143  90  GLU B OE1 
4835 O OE2 . GLU B 90  ? 0.4646 0.5100 0.4949 -0.0017 -0.0029 0.0152  90  GLU B OE2 
4836 N N   . GLU B 91  ? 0.1472 0.1905 0.1810 -0.0056 -0.0051 0.0089  91  GLU B N   
4837 C CA  . GLU B 91  ? 0.1464 0.1885 0.1812 -0.0067 -0.0052 0.0080  91  GLU B CA  
4838 C C   . GLU B 91  ? 0.0677 0.1099 0.1019 -0.0068 -0.0068 0.0065  91  GLU B C   
4839 O O   . GLU B 91  ? 0.1509 0.1917 0.1849 -0.0075 -0.0076 0.0057  91  GLU B O   
4840 C CB  . GLU B 91  ? 0.0986 0.1408 0.1351 -0.0074 -0.0037 0.0083  91  GLU B CB  
4841 C CG  . GLU B 91  ? 0.0847 0.1262 0.1219 -0.0075 -0.0021 0.0098  91  GLU B CG  
4842 C CD  . GLU B 91  ? 0.2397 0.2817 0.2788 -0.0081 -0.0005 0.0102  91  GLU B CD  
4843 O OE1 . GLU B 91  ? 0.1615 0.2051 0.2011 -0.0078 -0.0003 0.0101  91  GLU B OE1 
4844 O OE2 . GLU B 91  ? 0.1901 0.2306 0.2302 -0.0089 0.0004  0.0106  91  GLU B OE2 
4845 N N   . VAL B 92  ? 0.1481 0.1920 0.1820 -0.0061 -0.0075 0.0060  92  VAL B N   
4846 C CA  . VAL B 92  ? 0.1242 0.1681 0.1574 -0.0061 -0.0091 0.0046  92  VAL B CA  
4847 C C   . VAL B 92  ? 0.1867 0.2296 0.2183 -0.0058 -0.0106 0.0044  92  VAL B C   
4848 O O   . VAL B 92  ? 0.1648 0.2067 0.1960 -0.0063 -0.0117 0.0034  92  VAL B O   
4849 C CB  . VAL B 92  ? 0.0995 0.1456 0.1327 -0.0053 -0.0095 0.0041  92  VAL B CB  
4850 C CG1 . VAL B 92  ? 0.1324 0.1785 0.1650 -0.0052 -0.0113 0.0026  92  VAL B CG1 
4851 C CG2 . VAL B 92  ? 0.1269 0.1741 0.1618 -0.0056 -0.0080 0.0044  92  VAL B CG2 
4852 N N   . GLU B 93  ? 0.1681 0.2111 0.1987 -0.0051 -0.0105 0.0054  93  GLU B N   
4853 C CA  . GLU B 93  ? 0.2176 0.2596 0.2468 -0.0049 -0.0118 0.0053  93  GLU B CA  
4854 C C   . GLU B 93  ? 0.2161 0.2562 0.2455 -0.0059 -0.0117 0.0053  93  GLU B C   
4855 O O   . GLU B 93  ? 0.2328 0.2719 0.2613 -0.0061 -0.0130 0.0045  93  GLU B O   
4856 C CB  . GLU B 93  ? 0.2264 0.2689 0.2546 -0.0040 -0.0115 0.0065  93  GLU B CB  
4857 C CG  . GLU B 93  ? 0.3271 0.3714 0.3547 -0.0029 -0.0121 0.0063  93  GLU B CG  
4858 C CD  . GLU B 93  ? 0.4056 0.4508 0.4326 -0.0020 -0.0114 0.0076  93  GLU B CD  
4859 O OE1 . GLU B 93  ? 0.4659 0.5103 0.4932 -0.0023 -0.0104 0.0087  93  GLU B OE1 
4860 O OE2 . GLU B 93  ? 0.4117 0.4583 0.4380 -0.0010 -0.0120 0.0075  93  GLU B OE2 
4861 N N   . LYS B 94  ? 0.1735 0.2130 0.2039 -0.0064 -0.0101 0.0061  94  LYS B N   
4862 C CA  . LYS B 94  ? 0.1911 0.2288 0.2217 -0.0073 -0.0099 0.0061  94  LYS B CA  
4863 C C   . LYS B 94  ? 0.1993 0.2364 0.2303 -0.0081 -0.0106 0.0048  94  LYS B C   
4864 O O   . LYS B 94  ? 0.1672 0.2030 0.1976 -0.0086 -0.0114 0.0043  94  LYS B O   
4865 C CB  . LYS B 94  ? 0.2343 0.2716 0.2661 -0.0076 -0.0080 0.0072  94  LYS B CB  
4866 C CG  . LYS B 94  ? 0.4580 0.4957 0.4893 -0.0068 -0.0074 0.0086  94  LYS B CG  
4867 C CD  . LYS B 94  ? 0.5774 0.6147 0.6071 -0.0064 -0.0086 0.0087  94  LYS B CD  
4868 C CE  . LYS B 94  ? 0.6080 0.6462 0.6370 -0.0054 -0.0083 0.0098  94  LYS B CE  
4869 N NZ  . LYS B 94  ? 0.6031 0.6413 0.6306 -0.0048 -0.0098 0.0097  94  LYS B NZ  
4870 N N   . LEU B 95  ? 0.1589 0.1969 0.1910 -0.0083 -0.0103 0.0042  95  LEU B N   
4871 C CA  . LEU B 95  ? 0.1070 0.1445 0.1396 -0.0091 -0.0109 0.0029  95  LEU B CA  
4872 C C   . LEU B 95  ? 0.1108 0.1481 0.1420 -0.0088 -0.0129 0.0019  95  LEU B C   
4873 O O   . LEU B 95  ? 0.1382 0.1744 0.1691 -0.0095 -0.0137 0.0012  95  LEU B O   
4874 C CB  . LEU B 95  ? 0.1293 0.1681 0.1631 -0.0091 -0.0104 0.0024  95  LEU B CB  
4875 C CG  . LEU B 95  ? 0.2657 0.3044 0.3012 -0.0097 -0.0085 0.0030  95  LEU B CG  
4876 C CD1 . LEU B 95  ? 0.3069 0.3474 0.3435 -0.0095 -0.0081 0.0028  95  LEU B CD1 
4877 C CD2 . LEU B 95  ? 0.3033 0.3405 0.3396 -0.0109 -0.0083 0.0024  95  LEU B CD2 
4878 N N   . ILE B 96  ? 0.1330 0.1714 0.1632 -0.0078 -0.0137 0.0020  96  ILE B N   
4879 C CA  . ILE B 96  ? 0.1988 0.2371 0.2277 -0.0075 -0.0156 0.0011  96  ILE B CA  
4880 C C   . ILE B 96  ? 0.1575 0.1941 0.1852 -0.0077 -0.0162 0.0013  96  ILE B C   
4881 O O   . ILE B 96  ? 0.1809 0.2154 0.2073 -0.0077 -0.0168 0.0002  96  ILE B O   
4882 C CB  . ILE B 96  ? 0.1925 0.2323 0.2208 -0.0064 -0.0162 0.0010  96  ILE B CB  
4883 C CG1 . ILE B 96  ? 0.1790 0.2203 0.2084 -0.0063 -0.0159 0.0004  96  ILE B CG1 
4884 C CG2 . ILE B 96  ? 0.2054 0.2429 0.2313 -0.0056 -0.0175 0.0000  96  ILE B CG2 
4885 C CD1 . ILE B 96  ? 0.2954 0.3386 0.3245 -0.0051 -0.0159 0.0006  96  ILE B CD1 
4886 N N   . GLU B 97  ? 0.1739 0.2105 0.2014 -0.0074 -0.0155 0.0026  97  GLU B N   
4887 C CA  . GLU B 97  ? 0.2675 0.3028 0.2939 -0.0076 -0.0160 0.0029  97  GLU B CA  
4888 C C   . GLU B 97  ? 0.2466 0.2804 0.2735 -0.0087 -0.0157 0.0027  97  GLU B C   
4889 O O   . GLU B 97  ? 0.2005 0.2323 0.2257 -0.0087 -0.0163 0.0019  97  GLU B O   
4890 C CB  . GLU B 97  ? 0.2237 0.2594 0.2500 -0.0071 -0.0152 0.0043  97  GLU B CB  
4891 C CG  . GLU B 97  ? 0.4240 0.4611 0.4496 -0.0059 -0.0154 0.0047  97  GLU B CG  
4892 C CD  . GLU B 97  ? 0.6462 0.6824 0.6698 -0.0051 -0.0168 0.0038  97  GLU B CD  
4893 O OE1 . GLU B 97  ? 0.6508 0.6865 0.6739 -0.0048 -0.0175 0.0025  97  GLU B OE1 
4894 O OE2 . GLU B 97  ? 0.7237 0.7591 0.7461 -0.0046 -0.0170 0.0042  97  GLU B OE2 
4895 N N   . PHE B 98  ? 0.1908 0.2246 0.2191 -0.0093 -0.0143 0.0029  98  PHE B N   
4896 C CA  . PHE B 98  ? 0.1309 0.1633 0.1597 -0.0103 -0.0140 0.0025  98  PHE B CA  
4897 C C   . PHE B 98  ? 0.1767 0.2084 0.2048 -0.0106 -0.0152 0.0010  98  PHE B C   
4898 O O   . PHE B 98  ? 0.1657 0.1957 0.1928 -0.0109 -0.0154 0.0005  98  PHE B O   
4899 C CB  . PHE B 98  ? 0.1184 0.1509 0.1488 -0.0108 -0.0123 0.0027  98  PHE B CB  
4900 C CG  . PHE B 98  ? 0.2165 0.2475 0.2474 -0.0117 -0.0118 0.0026  98  PHE B CG  
4901 C CD1 . PHE B 98  ? 0.2210 0.2511 0.2515 -0.0118 -0.0112 0.0034  98  PHE B CD1 
4902 C CD2 . PHE B 98  ? 0.1856 0.2163 0.2174 -0.0125 -0.0118 0.0015  98  PHE B CD2 
4903 C CE1 . PHE B 98  ? 0.1974 0.2262 0.2284 -0.0126 -0.0107 0.0032  98  PHE B CE1 
4904 C CE2 . PHE B 98  ? 0.1631 0.1924 0.1952 -0.0134 -0.0113 0.0013  98  PHE B CE2 
4905 C CZ  . PHE B 98  ? 0.1868 0.2152 0.2185 -0.0134 -0.0108 0.0021  98  PHE B CZ  
4906 N N   . THR B 99  ? 0.2050 0.2376 0.2332 -0.0101 -0.0156 0.0002  99  THR B N   
4907 C CA  . THR B 99  ? 0.1202 0.1516 0.1472 -0.0100 -0.0163 -0.0014 99  THR B CA  
4908 C C   . THR B 99  ? 0.1813 0.2111 0.2058 -0.0092 -0.0170 -0.0020 99  THR B C   
4909 O O   . THR B 99  ? 0.1457 0.1742 0.1691 -0.0094 -0.0172 -0.0028 99  THR B O   
4910 C CB  . THR B 99  ? 0.1676 0.2003 0.1953 -0.0096 -0.0165 -0.0021 99  THR B CB  
4911 O OG1 . THR B 99  ? 0.1740 0.2083 0.2042 -0.0104 -0.0155 -0.0014 99  THR B OG1 
4912 C CG2 . THR B 99  ? 0.1056 0.1375 0.1322 -0.0094 -0.0170 -0.0037 99  THR B CG2 
4913 N N   . LYS B 100 ? 0.1660 0.1962 0.1896 -0.0084 -0.0174 -0.0015 100 LYS B N   
4914 C CA  . LYS B 100 ? 0.1963 0.2252 0.2177 -0.0076 -0.0180 -0.0020 100 LYS B CA  
4915 C C   . LYS B 100 ? 0.1961 0.2235 0.2168 -0.0081 -0.0178 -0.0015 100 LYS B C   
4916 O O   . LYS B 100 ? 0.2666 0.2928 0.2857 -0.0079 -0.0180 -0.0021 100 LYS B O   
4917 C CB  . LYS B 100 ? 0.2782 0.3077 0.2989 -0.0066 -0.0184 -0.0016 100 LYS B CB  
4918 C CG  . LYS B 100 ? 0.3745 0.4053 0.3956 -0.0059 -0.0187 -0.0022 100 LYS B CG  
4919 C CD  . LYS B 100 ? 0.4815 0.5123 0.5013 -0.0046 -0.0192 -0.0022 100 LYS B CD  
4920 C CE  . LYS B 100 ? 0.6004 0.6320 0.6208 -0.0045 -0.0190 -0.0007 100 LYS B CE  
4921 N NZ  . LYS B 100 ? 0.6517 0.6824 0.6715 -0.0049 -0.0187 0.0001  100 LYS B NZ  
4922 N N   . LEU B 101 ? 0.1259 0.1538 0.1479 -0.0088 -0.0172 -0.0003 101 LEU B N   
4923 C CA  . LEU B 101 ? 0.1763 0.2029 0.1978 -0.0093 -0.0170 0.0001  101 LEU B CA  
4924 C C   . LEU B 101 ? 0.2714 0.2969 0.2927 -0.0100 -0.0169 -0.0008 101 LEU B C   
4925 O O   . LEU B 101 ? 0.2396 0.2638 0.2596 -0.0100 -0.0170 -0.0010 101 LEU B O   
4926 C CB  . LEU B 101 ? 0.2684 0.2960 0.2916 -0.0100 -0.0163 0.0015  101 LEU B CB  
4927 C CG  . LEU B 101 ? 0.3690 0.3954 0.3921 -0.0107 -0.0160 0.0019  101 LEU B CG  
4928 C CD1 . LEU B 101 ? 0.3587 0.3843 0.3801 -0.0101 -0.0164 0.0022  101 LEU B CD1 
4929 C CD2 . LEU B 101 ? 0.4093 0.4366 0.4345 -0.0115 -0.0150 0.0030  101 LEU B CD2 
4930 N N   . ASN B 102 ? 0.1683 0.1943 0.1908 -0.0104 -0.0166 -0.0014 102 ASN B N   
4931 C CA  . ASN B 102 ? 0.1467 0.1717 0.1691 -0.0111 -0.0164 -0.0022 102 ASN B CA  
4932 C C   . ASN B 102 ? 0.1598 0.1846 0.1810 -0.0106 -0.0168 -0.0035 102 ASN B C   
4933 O O   . ASN B 102 ? 0.1524 0.1765 0.1733 -0.0111 -0.0166 -0.0043 102 ASN B O   
4934 C CB  . ASN B 102 ? 0.1450 0.1708 0.1696 -0.0120 -0.0156 -0.0020 102 ASN B CB  
4935 C CG  . ASN B 102 ? 0.3037 0.3297 0.3296 -0.0126 -0.0149 -0.0008 102 ASN B CG  
4936 O OD1 . ASN B 102 ? 0.2152 0.2400 0.2405 -0.0130 -0.0147 -0.0007 102 ASN B OD1 
4937 N ND2 . ASN B 102 ? 0.2430 0.2704 0.2706 -0.0127 -0.0144 0.0003  102 ASN B ND2 
4938 N N   . TYR B 103 ? 0.1824 0.1789 0.2471 -0.0018 0.0187  -0.0076 103 TYR B N   
4939 C CA  . TYR B 103 ? 0.2480 0.2441 0.3147 -0.0015 0.0187  -0.0064 103 TYR B CA  
4940 C C   . TYR B 103 ? 0.2933 0.2885 0.3625 -0.0016 0.0198  -0.0060 103 TYR B C   
4941 O O   . TYR B 103 ? 0.1874 0.1817 0.2590 -0.0016 0.0197  -0.0050 103 TYR B O   
4942 C CB  . TYR B 103 ? 0.3275 0.3240 0.3938 -0.0014 0.0187  -0.0057 103 TYR B CB  
4943 C CG  . TYR B 103 ? 0.3387 0.3351 0.4084 -0.0011 0.0191  -0.0044 103 TYR B CG  
4944 C CD1 . TYR B 103 ? 0.4144 0.4114 0.4858 -0.0009 0.0184  -0.0039 103 TYR B CD1 
4945 C CD2 . TYR B 103 ? 0.3494 0.3449 0.4209 -0.0010 0.0202  -0.0037 103 TYR B CD2 
4946 C CE1 . TYR B 103 ? 0.3888 0.3856 0.4636 -0.0006 0.0188  -0.0024 103 TYR B CE1 
4947 C CE2 . TYR B 103 ? 0.3608 0.3560 0.4357 -0.0006 0.0206  -0.0022 103 TYR B CE2 
4948 C CZ  . TYR B 103 ? 0.4175 0.4134 0.4941 -0.0005 0.0199  -0.0015 103 TYR B CZ  
4949 O OH  . TYR B 103 ? 0.4643 0.4598 0.5442 -0.0001 0.0204  0.0002  103 TYR B OH  
4950 N N   . GLU B 104 ? 0.2377 0.2319 0.3043 -0.0020 0.0203  -0.0065 104 GLU B N   
4951 C CA  . GLU B 104 ? 0.2622 0.2537 0.3267 -0.0024 0.0201  -0.0057 104 GLU B CA  
4952 C C   . GLU B 104 ? 0.2524 0.2421 0.3145 -0.0035 0.0194  -0.0060 104 GLU B C   
4953 O O   . GLU B 104 ? 0.2531 0.2408 0.3145 -0.0040 0.0194  -0.0054 104 GLU B O   
4954 C CB  . GLU B 104 ? 0.2933 0.2846 0.3574 -0.0024 0.0214  -0.0062 104 GLU B CB  
4955 C CG  . GLU B 104 ? 0.3749 0.3673 0.4411 -0.0018 0.0221  -0.0056 104 GLU B CG  
4956 C CD  . GLU B 104 ? 0.4274 0.4183 0.4938 -0.0014 0.0216  -0.0041 104 GLU B CD  
4957 O OE1 . GLU B 104 ? 0.5685 0.5604 0.6367 -0.0010 0.0219  -0.0035 104 GLU B OE1 
4958 O OE2 . GLU B 104 ? 0.4905 0.4795 0.5572 -0.0014 0.0215  -0.0035 104 GLU B OE2 
4959 N N   . LYS B 105 ? 0.1991 0.1898 0.2605 -0.0039 0.0188  -0.0068 105 LYS B N   
4960 C CA  . LYS B 105 ? 0.1860 0.1752 0.2447 -0.0053 0.0180  -0.0069 105 LYS B CA  
4961 C C   . LYS B 105 ? 0.2091 0.1977 0.2693 -0.0062 0.0173  -0.0057 105 LYS B C   
4962 O O   . LYS B 105 ? 0.1766 0.1666 0.2404 -0.0056 0.0173  -0.0052 105 LYS B O   
4963 C CB  . LYS B 105 ? 0.1185 0.1092 0.1771 -0.0055 0.0181  -0.0082 105 LYS B CB  
4964 C CG  . LYS B 105 ? 0.1957 0.1873 0.2547 -0.0048 0.0196  -0.0096 105 LYS B CG  
4965 C CD  . LYS B 105 ? 0.1548 0.1480 0.2141 -0.0047 0.0198  -0.0108 105 LYS B CD  
4966 C CE  . LYS B 105 ? 0.2008 0.1956 0.2613 -0.0040 0.0213  -0.0118 105 LYS B CE  
4967 N NZ  . LYS B 105 ? 0.1956 0.1914 0.2553 -0.0040 0.0212  -0.0127 105 LYS B NZ  
4968 N N   . PRO B 106 ? 0.2044 0.1914 0.2629 -0.0076 0.0170  -0.0052 106 PRO B N   
4969 C CA  . PRO B 106 ? 0.1741 0.1613 0.2349 -0.0087 0.0165  -0.0038 106 PRO B CA  
4970 C C   . PRO B 106 ? 0.1439 0.1332 0.2055 -0.0095 0.0155  -0.0037 106 PRO B C   
4971 O O   . PRO B 106 ? 0.1576 0.1482 0.2226 -0.0098 0.0152  -0.0023 106 PRO B O   
4972 C CB  . PRO B 106 ? 0.2063 0.1917 0.2639 -0.0103 0.0162  -0.0037 106 PRO B CB  
4973 C CG  . PRO B 106 ? 0.2017 0.1855 0.2570 -0.0094 0.0169  -0.0045 106 PRO B CG  
4974 C CD  . PRO B 106 ? 0.1665 0.1517 0.2213 -0.0081 0.0171  -0.0056 106 PRO B CD  
4975 N N   . ILE B 107 ? 0.1492 0.1392 0.2079 -0.0098 0.0150  -0.0050 107 ILE B N   
4976 C CA  . ILE B 107 ? 0.1431 0.1352 0.2025 -0.0106 0.0141  -0.0048 107 ILE B CA  
4977 C C   . ILE B 107 ? 0.1249 0.1183 0.1879 -0.0089 0.0143  -0.0047 107 ILE B C   
4978 O O   . ILE B 107 ? 0.1608 0.1561 0.2248 -0.0094 0.0136  -0.0043 107 ILE B O   
4979 C CB  . ILE B 107 ? 0.0507 0.0429 0.1058 -0.0113 0.0134  -0.0060 107 ILE B CB  
4980 C CG1 . ILE B 107 ? 0.0596 0.0515 0.1150 -0.0094 0.0145  -0.0075 107 ILE B CG1 
4981 C CG2 . ILE B 107 ? 0.1213 0.1124 0.1729 -0.0132 0.0129  -0.0058 107 ILE B CG2 
4982 C CD1 . ILE B 107 ? 0.0860 0.0786 0.1405 -0.0096 0.0147  -0.0088 107 ILE B CD1 
4983 N N   . TYR B 108 ? 0.1235 0.1164 0.1885 -0.0070 0.0154  -0.0049 108 TYR B N   
4984 C CA  . TYR B 108 ? 0.1542 0.1483 0.2230 -0.0054 0.0157  -0.0047 108 TYR B CA  
4985 C C   . TYR B 108 ? 0.1889 0.1830 0.2622 -0.0048 0.0162  -0.0029 108 TYR B C   
4986 O O   . TYR B 108 ? 0.1789 0.1738 0.2555 -0.0032 0.0167  -0.0026 108 TYR B O   
4987 C CB  . TYR B 108 ? 0.1387 0.1330 0.2070 -0.0038 0.0166  -0.0059 108 TYR B CB  
4988 C CG  . TYR B 108 ? 0.1717 0.1670 0.2378 -0.0036 0.0161  -0.0071 108 TYR B CG  
4989 C CD1 . TYR B 108 ? 0.1158 0.1107 0.1785 -0.0045 0.0159  -0.0080 108 TYR B CD1 
4990 C CD2 . TYR B 108 ? 0.1801 0.1766 0.2484 -0.0024 0.0161  -0.0073 108 TYR B CD2 
4991 C CE1 . TYR B 108 ? 0.1607 0.1566 0.2236 -0.0041 0.0161  -0.0092 108 TYR B CE1 
4992 C CE2 . TYR B 108 ? 0.1295 0.1267 0.1962 -0.0021 0.0158  -0.0083 108 TYR B CE2 
4993 C CZ  . TYR B 108 ? 0.1670 0.1640 0.2319 -0.0029 0.0161  -0.0094 108 TYR B CZ  
4994 O OH  . TYR B 108 ? 0.1587 0.1565 0.2234 -0.0025 0.0162  -0.0105 108 TYR B OH  
4995 N N   . ARG B 109 ? 0.1157 0.1091 0.1892 -0.0060 0.0160  -0.0016 109 ARG B N   
4996 C CA  . ARG B 109 ? 0.2279 0.2213 0.3056 -0.0053 0.0166  0.0004  109 ARG B CA  
4997 C C   . ARG B 109 ? 0.1869 0.1833 0.2682 -0.0057 0.0157  0.0022  109 ARG B C   
4998 O O   . ARG B 109 ? 0.2384 0.2366 0.3204 -0.0072 0.0150  0.0038  109 ARG B O   
4999 C CB  . ARG B 109 ? 0.3996 0.3912 0.4761 -0.0063 0.0168  0.0013  109 ARG B CB  
5000 C CG  . ARG B 109 ? 0.5994 0.5886 0.6716 -0.0062 0.0174  -0.0003 109 ARG B CG  
5001 C CD  . ARG B 109 ? 0.6921 0.6794 0.7649 -0.0050 0.0185  0.0004  109 ARG B CD  
5002 N NE  . ARG B 109 ? 0.6450 0.6306 0.7170 -0.0062 0.0183  0.0017  109 ARG B NE  
5003 C CZ  . ARG B 109 ? 0.5986 0.5821 0.6665 -0.0070 0.0184  0.0009  109 ARG B CZ  
5004 N NH1 . ARG B 109 ? 0.5445 0.5277 0.6090 -0.0068 0.0185  -0.0011 109 ARG B NH1 
5005 N NH2 . ARG B 109 ? 0.6255 0.6075 0.6929 -0.0080 0.0183  0.0022  109 ARG B NH2 
5006 N N   . PHE B 110 ? 0.1151 0.1125 0.1983 -0.0043 0.0157  0.0019  110 PHE B N   
5007 C CA  . PHE B 110 ? 0.1297 0.1305 0.2163 -0.0043 0.0149  0.0036  110 PHE B CA  
5008 C C   . PHE B 110 ? 0.1532 0.1536 0.2438 -0.0021 0.0159  0.0047  110 PHE B C   
5009 O O   . PHE B 110 ? 0.1831 0.1810 0.2734 -0.0005 0.0168  0.0033  110 PHE B O   
5010 C CB  . PHE B 110 ? 0.1578 0.1599 0.2423 -0.0046 0.0139  0.0023  110 PHE B CB  
5011 C CG  . PHE B 110 ? 0.1483 0.1510 0.2288 -0.0067 0.0130  0.0013  110 PHE B CG  
5012 C CD1 . PHE B 110 ? 0.1007 0.1069 0.1814 -0.0084 0.0118  0.0026  110 PHE B CD1 
5013 C CD2 . PHE B 110 ? 0.2379 0.2383 0.3143 -0.0069 0.0132  -0.0009 110 PHE B CD2 
5014 C CE1 . PHE B 110 ? 0.1465 0.1531 0.2233 -0.0104 0.0111  0.0016  110 PHE B CE1 
5015 C CE2 . PHE B 110 ? 0.2697 0.2706 0.3422 -0.0087 0.0124  -0.0017 110 PHE B CE2 
5016 C CZ  . PHE B 110 ? 0.2125 0.2161 0.2851 -0.0105 0.0114  -0.0005 110 PHE B CZ  
5017 N N   . GLU B 111 ? 0.2117 0.2152 0.3059 -0.0017 0.0157  0.0074  111 GLU B N   
5018 C CA  . GLU B 111 ? 0.2720 0.2758 0.3690 0.0008  0.0165  0.0087  111 GLU B CA  
5019 C C   . GLU B 111 ? 0.1855 0.1882 0.2808 0.0013  0.0161  0.0075  111 GLU B C   
5020 O O   . GLU B 111 ? 0.2252 0.2253 0.3196 0.0020  0.0168  0.0072  111 GLU B O   
5021 C CB  . GLU B 111 ? 0.3645 0.3732 0.4641 0.0020  0.0157  0.0116  111 GLU B CB  
5022 C CG  . GLU B 111 ? 0.4982 0.5056 0.5983 0.0049  0.0164  0.0130  111 GLU B CG  
5023 C CD  . GLU B 111 ? 0.7610 0.7631 0.8596 0.0052  0.0178  0.0122  111 GLU B CD  
5024 O OE1 . GLU B 111 ? 0.8520 0.8522 0.9481 0.0035  0.0177  0.0120  111 GLU B OE1 
5025 O OE2 . GLU B 111 ? 0.7918 0.7910 0.8876 0.0059  0.0185  0.0116  111 GLU B OE2 
5026 N N   . ARG B 112 ? 0.1869 0.1918 0.2808 0.0003  0.0148  0.0068  112 ARG B N   
5027 C CA  . ARG B 112 ? 0.1894 0.1938 0.2817 0.0007  0.0143  0.0058  112 ARG B CA  
5028 C C   . ARG B 112 ? 0.1582 0.1573 0.2483 0.0005  0.0151  0.0035  112 ARG B C   
5029 O O   . ARG B 112 ? 0.2117 0.2093 0.3007 0.0005  0.0152  0.0031  112 ARG B O   
5030 C CB  . ARG B 112 ? 0.1661 0.1740 0.2571 -0.0004 0.0129  0.0056  112 ARG B CB  
5031 C CG  . ARG B 112 ? 0.2223 0.2300 0.3116 -0.0001 0.0123  0.0046  112 ARG B CG  
5032 C CD  . ARG B 112 ? 0.2018 0.2101 0.2921 0.0013  0.0124  0.0059  112 ARG B CD  
5033 N NE  . ARG B 112 ? 0.1947 0.2045 0.2835 0.0013  0.0116  0.0054  112 ARG B NE  
5034 C CZ  . ARG B 112 ? 0.2803 0.2906 0.3690 0.0023  0.0116  0.0060  112 ARG B CZ  
5035 N NH1 . ARG B 112 ? 0.1899 0.1994 0.2795 0.0035  0.0123  0.0071  112 ARG B NH1 
5036 N NH2 . ARG B 112 ? 0.1947 0.2064 0.2820 0.0022  0.0108  0.0055  112 ARG B NH2 
5037 N N   . ILE B 113 ? 0.1685 0.1658 0.2572 0.0003  0.0156  0.0019  113 ILE B N   
5038 C CA  . ILE B 113 ? 0.1832 0.1797 0.2664 0.0003  0.0158  -0.0002 113 ILE B CA  
5039 C C   . ILE B 113 ? 0.2463 0.2421 0.3284 -0.0005 0.0165  0.0006  113 ILE B C   
5040 O O   . ILE B 113 ? 0.2242 0.2214 0.3041 -0.0009 0.0166  -0.0001 113 ILE B O   
5041 C CB  . ILE B 113 ? 0.2117 0.2086 0.2933 0.0000  0.0161  -0.0017 113 ILE B CB  
5042 C CG1 . ILE B 113 ? 0.1801 0.1774 0.2616 -0.0005 0.0154  -0.0027 113 ILE B CG1 
5043 C CG2 . ILE B 113 ? 0.2554 0.2527 0.3325 -0.0001 0.0165  -0.0031 113 ILE B CG2 
5044 C CD1 . ILE B 113 ? 0.2224 0.2197 0.3001 -0.0016 0.0154  -0.0040 113 ILE B CD1 
5045 N N   . ARG B 114 ? 0.2160 0.2127 0.3018 -0.0002 0.0175  0.0021  114 ARG B N   
5046 C CA  . ARG B 114 ? 0.2199 0.2163 0.3061 0.0003  0.0186  0.0028  114 ARG B CA  
5047 C C   . ARG B 114 ? 0.2243 0.2207 0.3113 0.0006  0.0184  0.0037  114 ARG B C   
5048 O O   . ARG B 114 ? 0.2702 0.2664 0.3553 0.0006  0.0189  0.0033  114 ARG B O   
5049 C CB  . ARG B 114 ? 0.2454 0.2416 0.3353 0.0009  0.0196  0.0047  114 ARG B CB  
5050 C CG  . ARG B 114 ? 0.5280 0.5239 0.6168 0.0007  0.0202  0.0036  114 ARG B CG  
5051 C CD  . ARG B 114 ? 0.6481 0.6423 0.7376 0.0017  0.0206  0.0054  114 ARG B CD  
5052 N NE  . ARG B 114 ? 0.6760 0.6704 0.7686 0.0019  0.0200  0.0069  114 ARG B NE  
5053 C CZ  . ARG B 114 ? 0.6325 0.6261 0.7237 0.0006  0.0195  0.0061  114 ARG B CZ  
5054 N NH1 . ARG B 114 ? 0.5841 0.5769 0.6712 -0.0001 0.0197  0.0036  114 ARG B NH1 
5055 N NH2 . ARG B 114 ? 0.5996 0.5941 0.6923 -0.0008 0.0187  0.0080  114 ARG B NH2 
5056 N N   . GLU B 115 ? 0.2459 0.2429 0.3357 0.0011  0.0177  0.0051  115 GLU B N   
5057 C CA  . GLU B 115 ? 0.2022 0.2003 0.2908 0.0022  0.0172  0.0056  115 GLU B CA  
5058 C C   . GLU B 115 ? 0.2971 0.2941 0.3839 0.0007  0.0170  0.0040  115 GLU B C   
5059 O O   . GLU B 115 ? 0.3130 0.3099 0.3982 0.0010  0.0171  0.0038  115 GLU B O   
5060 C CB  . GLU B 115 ? 0.2296 0.2308 0.3198 0.0036  0.0160  0.0071  115 GLU B CB  
5061 C CG  . GLU B 115 ? 0.2526 0.2561 0.3450 0.0050  0.0159  0.0091  115 GLU B CG  
5062 C CD  . GLU B 115 ? 0.4173 0.4252 0.5112 0.0055  0.0146  0.0104  115 GLU B CD  
5063 O OE1 . GLU B 115 ? 0.3665 0.3756 0.4596 0.0050  0.0138  0.0097  115 GLU B OE1 
5064 O OE2 . GLU B 115 ? 0.4350 0.4456 0.5310 0.0063  0.0143  0.0123  115 GLU B OE2 
5065 N N   . LEU B 116 ? 0.1998 0.1967 0.2843 0.0002  0.0160  0.0025  116 LEU B N   
5066 C CA  . LEU B 116 ? 0.2180 0.2147 0.2985 -0.0003 0.0152  0.0008  116 LEU B CA  
5067 C C   . LEU B 116 ? 0.3438 0.3404 0.4204 -0.0008 0.0156  -0.0002 116 LEU B C   
5068 O O   . LEU B 116 ? 0.2889 0.2856 0.3635 -0.0009 0.0153  -0.0006 116 LEU B O   
5069 C CB  . LEU B 116 ? 0.2210 0.2173 0.2995 -0.0004 0.0143  -0.0004 116 LEU B CB  
5070 C CG  . LEU B 116 ? 0.3315 0.3286 0.4121 -0.0001 0.0135  -0.0002 116 LEU B CG  
5071 C CD1 . LEU B 116 ? 0.3059 0.3044 0.3907 0.0004  0.0136  0.0018  116 LEU B CD1 
5072 C CD2 . LEU B 116 ? 0.2288 0.2264 0.3111 -0.0001 0.0133  -0.0005 116 LEU B CD2 
5073 N N   . MET B 117 ? 0.3457 0.3426 0.4216 -0.0010 0.0162  -0.0005 117 MET B N   
5074 C CA  . MET B 117 ? 0.2862 0.2834 0.3590 -0.0012 0.0166  -0.0014 117 MET B CA  
5075 C C   . MET B 117 ? 0.3674 0.3640 0.4414 -0.0007 0.0175  -0.0005 117 MET B C   
5076 O O   . MET B 117 ? 0.4276 0.4242 0.4992 -0.0009 0.0177  -0.0010 117 MET B O   
5077 C CB  . MET B 117 ? 0.2800 0.2776 0.3517 -0.0012 0.0170  -0.0021 117 MET B CB  
5078 C CG  . MET B 117 ? 0.2849 0.2837 0.3549 -0.0012 0.0162  -0.0032 117 MET B CG  
5079 S SD  . MET B 117 ? 0.4124 0.4121 0.4775 -0.0014 0.0153  -0.0043 117 MET B SD  
5080 C CE  . MET B 117 ? 0.4199 0.4200 0.4857 -0.0018 0.0143  -0.0040 117 MET B CE  
5081 N N   . ASN B 118 ? 0.3635 0.3597 0.4413 -0.0002 0.0180  0.0010  118 ASN B N   
5082 C CA  . ASN B 118 ? 0.4600 0.4558 0.5394 0.0004  0.0189  0.0021  118 ASN B CA  
5083 C C   . ASN B 118 ? 0.4767 0.4727 0.5567 0.0006  0.0185  0.0025  118 ASN B C   
5084 O O   . ASN B 118 ? 0.5179 0.5136 0.5965 0.0019  0.0187  0.0031  118 ASN B O   
5085 C CB  . ASN B 118 ? 0.5055 0.5009 0.5868 0.0018  0.0194  0.0036  118 ASN B CB  
5086 C CG  . ASN B 118 ? 0.5341 0.5288 0.6147 0.0017  0.0203  0.0033  118 ASN B CG  
5087 O OD1 . ASN B 118 ? 0.5906 0.5849 0.6689 0.0014  0.0207  0.0026  118 ASN B OD1 
5088 N ND2 . ASN B 118 ? 0.5996 0.5942 0.6818 0.0021  0.0204  0.0040  118 ASN B ND2 
5089 N N   . LYS B 119 ? 0.4573 0.4537 0.5365 0.0003  0.0174  0.0019  119 LYS B N   
5090 C CA  . LYS B 119 ? 0.4270 0.4236 0.5067 0.0004  0.0170  0.0023  119 LYS B CA  
5091 C C   . LYS B 119 ? 0.4540 0.4504 0.5300 -0.0001 0.0166  0.0009  119 LYS B C   
5092 O O   . LYS B 119 ? 0.4187 0.4152 0.4916 -0.0007 0.0162  -0.0004 119 LYS B O   
5093 C CB  . LYS B 119 ? 0.4233 0.4204 0.5044 0.0006  0.0161  0.0025  119 LYS B CB  
5094 C CG  . LYS B 119 ? 0.5525 0.5514 0.6335 0.0023  0.0155  0.0035  119 LYS B CG  
5095 C CD  . LYS B 119 ? 0.5974 0.5965 0.6777 0.0018  0.0145  0.0028  119 LYS B CD  
5096 C CE  . LYS B 119 ? 0.6170 0.6185 0.6973 0.0034  0.0139  0.0037  119 LYS B CE  
5097 N NZ  . LYS B 119 ? 0.6028 0.6046 0.6821 0.0028  0.0131  0.0029  119 LYS B NZ  
5098 N N   . GLU B 120 ? 0.5160 0.5124 0.5934 0.0001  0.0171  0.0013  120 GLU B N   
5099 C CA  . GLU B 120 ? 0.5482 0.5445 0.6232 -0.0004 0.0170  0.0002  120 GLU B CA  
5100 C C   . GLU B 120 ? 0.5206 0.5172 0.5927 -0.0010 0.0157  -0.0009 120 GLU B C   
5101 O O   . GLU B 120 ? 0.5563 0.5531 0.6254 -0.0016 0.0153  -0.0019 120 GLU B O   
5102 C CB  . GLU B 120 ? 0.5625 0.5586 0.6398 -0.0001 0.0177  0.0010  120 GLU B CB  
5103 C CG  . GLU B 120 ? 0.6483 0.6440 0.7277 0.0004  0.0192  0.0021  120 GLU B CG  
5104 C CD  . GLU B 120 ? 0.7169 0.7126 0.7968 0.0016  0.0195  0.0029  120 GLU B CD  
5105 O OE1 . GLU B 120 ? 0.7354 0.7319 0.8151 0.0034  0.0189  0.0038  120 GLU B OE1 
5106 O OE2 . GLU B 120 ? 0.6727 0.6680 0.7530 0.0009  0.0202  0.0025  120 GLU B OE2 
5107 N N   . LYS B 121 ? 0.5374 0.5341 0.6105 -0.0008 0.0151  -0.0007 121 LYS B N   
5108 C CA  . LYS B 121 ? 0.5335 0.5303 0.6039 -0.0012 0.0139  -0.0017 121 LYS B CA  
5109 C C   . LYS B 121 ? 0.4398 0.4367 0.5121 -0.0008 0.0134  -0.0012 121 LYS B C   
5110 O O   . LYS B 121 ? 0.4605 0.4578 0.5365 -0.0003 0.0138  0.0001  121 LYS B O   
5111 C CB  . LYS B 121 ? 0.5992 0.5960 0.6689 -0.0014 0.0137  -0.0021 121 LYS B CB  
5112 C CG  . LYS B 121 ? 0.6855 0.6823 0.7538 -0.0018 0.0142  -0.0024 121 LYS B CG  
5113 C CD  . LYS B 121 ? 0.7344 0.7316 0.7987 -0.0025 0.0135  -0.0035 121 LYS B CD  
5114 C CE  . LYS B 121 ? 0.7573 0.7547 0.8203 -0.0026 0.0136  -0.0037 121 LYS B CE  
5115 N NZ  . LYS B 121 ? 0.7444 0.7426 0.8051 -0.0031 0.0137  -0.0042 121 LYS B NZ  
5116 N N   . LEU B 122 ? 0.3220 0.3188 0.3918 -0.0011 0.0125  -0.0021 122 LEU B N   
5117 C CA  . LEU B 122 ? 0.2531 0.2502 0.3245 -0.0008 0.0121  -0.0018 122 LEU B CA  
5118 C C   . LEU B 122 ? 0.2031 0.2005 0.2754 -0.0006 0.0115  -0.0020 122 LEU B C   
5119 O O   . LEU B 122 ? 0.2453 0.2423 0.3147 -0.0009 0.0110  -0.0030 122 LEU B O   
5120 C CB  . LEU B 122 ? 0.3238 0.3205 0.3924 -0.0010 0.0117  -0.0027 122 LEU B CB  
5121 C CG  . LEU B 122 ? 0.2891 0.2855 0.3572 -0.0013 0.0123  -0.0026 122 LEU B CG  
5122 C CD1 . LEU B 122 ? 0.2329 0.2287 0.2976 -0.0015 0.0119  -0.0037 122 LEU B CD1 
5123 C CD2 . LEU B 122 ? 0.2473 0.2440 0.3205 -0.0008 0.0131  -0.0013 122 LEU B CD2 
5124 N N   . ASN B 123 ? 0.2650 0.2632 0.3414 -0.0002 0.0114  -0.0009 123 ASN B N   
5125 C CA  . ASN B 123 ? 0.2526 0.2519 0.3295 0.0001  0.0107  -0.0010 123 ASN B CA  
5126 C C   . ASN B 123 ? 0.2583 0.2581 0.3343 -0.0001 0.0101  -0.0017 123 ASN B C   
5127 O O   . ASN B 123 ? 0.1698 0.1684 0.2448 -0.0003 0.0102  -0.0023 123 ASN B O   
5128 C CB  . ASN B 123 ? 0.1956 0.1992 0.2736 0.0014  0.0104  0.0007  123 ASN B CB  
5129 C CG  . ASN B 123 ? 0.2656 0.2723 0.3443 0.0023  0.0102  0.0019  123 ASN B CG  
5130 O OD1 . ASN B 123 ? 0.1852 0.1924 0.2644 0.0019  0.0100  0.0018  123 ASN B OD1 
5131 N ND2 . ASN B 123 ? 0.3179 0.3261 0.3977 0.0035  0.0106  0.0032  123 ASN B ND2 
5132 N N   . ARG B 124 ? 0.1927 0.1952 0.2686 0.0002  0.0093  -0.0016 124 ARG B N   
5133 C CA  . ARG B 124 ? 0.1590 0.1624 0.2341 -0.0002 0.0088  -0.0024 124 ARG B CA  
5134 C C   . ARG B 124 ? 0.1326 0.1391 0.2078 -0.0002 0.0085  -0.0014 124 ARG B C   
5135 O O   . ARG B 124 ? 0.1577 0.1635 0.2321 -0.0007 0.0085  -0.0022 124 ARG B O   
5136 C CB  . ARG B 124 ? 0.1811 0.1871 0.2561 -0.0002 0.0080  -0.0023 124 ARG B CB  
5137 C CG  . ARG B 124 ? 0.2378 0.2450 0.3116 -0.0008 0.0075  -0.0030 124 ARG B CG  
5138 C CD  . ARG B 124 ? 0.2651 0.2750 0.3388 -0.0010 0.0068  -0.0029 124 ARG B CD  
5139 N NE  . ARG B 124 ? 0.2673 0.2787 0.3400 -0.0018 0.0063  -0.0034 124 ARG B NE  
5140 C CZ  . ARG B 124 ? 0.1977 0.2131 0.2704 -0.0024 0.0057  -0.0024 124 ARG B CZ  
5141 N NH1 . ARG B 124 ? 0.2455 0.2640 0.3194 -0.0021 0.0055  -0.0009 124 ARG B NH1 
5142 N NH2 . ARG B 124 ? 0.2463 0.2629 0.3179 -0.0034 0.0054  -0.0029 124 ARG B NH2 
5143 N N   . GLU B 125 ? 0.1051 0.1153 0.1818 0.0003  0.0083  0.0002  125 GLU B N   
5144 C CA  . GLU B 125 ? 0.1725 0.1854 0.2510 0.0002  0.0081  0.0012  125 GLU B CA  
5145 C C   . GLU B 125 ? 0.1631 0.1727 0.2425 0.0001  0.0090  0.0009  125 GLU B C   
5146 O O   . GLU B 125 ? 0.1342 0.1444 0.2138 -0.0005 0.0089  0.0008  125 GLU B O   
5147 C CB  . GLU B 125 ? 0.2818 0.2987 0.3625 0.0011  0.0078  0.0031  125 GLU B CB  
5148 C CG  . GLU B 125 ? 0.4303 0.4516 0.5105 0.0009  0.0068  0.0036  125 GLU B CG  
5149 C CD  . GLU B 125 ? 0.5809 0.6061 0.6632 0.0020  0.0064  0.0054  125 GLU B CD  
5150 O OE1 . GLU B 125 ? 0.5949 0.6202 0.6792 0.0029  0.0069  0.0066  125 GLU B OE1 
5151 O OE2 . GLU B 125 ? 0.6336 0.6618 0.7154 0.0022  0.0057  0.0057  125 GLU B OE2 
5152 N N   . GLU B 126 ? 0.1537 0.1599 0.2332 0.0005  0.0098  0.0007  126 GLU B N   
5153 C CA  . GLU B 126 ? 0.1421 0.1451 0.2223 0.0003  0.0108  0.0003  126 GLU B CA  
5154 C C   . GLU B 126 ? 0.1404 0.1400 0.2185 -0.0003 0.0109  -0.0017 126 GLU B C   
5155 O O   . GLU B 126 ? 0.1399 0.1384 0.2183 -0.0003 0.0113  -0.0021 126 GLU B O   
5156 C CB  . GLU B 126 ? 0.1568 0.1577 0.2374 0.0005  0.0116  0.0007  126 GLU B CB  
5157 C CG  . GLU B 126 ? 0.1377 0.1419 0.2203 0.0018  0.0117  0.0027  126 GLU B CG  
5158 C CD  . GLU B 126 ? 0.2033 0.2068 0.2854 0.0023  0.0122  0.0030  126 GLU B CD  
5159 O OE1 . GLU B 126 ? 0.2956 0.2965 0.3759 0.0014  0.0124  0.0018  126 GLU B OE1 
5160 O OE2 . GLU B 126 ? 0.2981 0.3037 0.3813 0.0036  0.0124  0.0045  126 GLU B OE2 
5161 N N   . LEU B 127 ? 0.1453 0.1439 0.2206 -0.0004 0.0105  -0.0029 127 LEU B N   
5162 C CA  . LEU B 127 ? 0.1479 0.1461 0.2188 -0.0005 0.0103  -0.0044 127 LEU B CA  
5163 C C   . LEU B 127 ? 0.0986 0.0975 0.1712 -0.0007 0.0101  -0.0048 127 LEU B C   
5164 O O   . LEU B 127 ? 0.1241 0.1229 0.1949 -0.0008 0.0103  -0.0057 127 LEU B O   
5165 C CB  . LEU B 127 ? 0.1591 0.1568 0.2267 -0.0006 0.0099  -0.0053 127 LEU B CB  
5166 C CG  . LEU B 127 ? 0.2693 0.2661 0.3341 -0.0007 0.0101  -0.0052 127 LEU B CG  
5167 C CD1 . LEU B 127 ? 0.2401 0.2368 0.3037 -0.0008 0.0097  -0.0056 127 LEU B CD1 
5168 C CD2 . LEU B 127 ? 0.2996 0.2956 0.3602 -0.0006 0.0102  -0.0058 127 LEU B CD2 
5169 N N   . LEU B 128 ? 0.0561 0.0591 0.1290 -0.0013 0.0092  -0.0037 128 LEU B N   
5170 C CA  . LEU B 128 ? 0.1274 0.1338 0.1996 -0.0024 0.0086  -0.0035 128 LEU B CA  
5171 C C   . LEU B 128 ? 0.1369 0.1436 0.2106 -0.0028 0.0089  -0.0029 128 LEU B C   
5172 O O   . LEU B 128 ? 0.1615 0.1686 0.2335 -0.0037 0.0088  -0.0035 128 LEU B O   
5173 C CB  . LEU B 128 ? 0.0776 0.0884 0.1504 -0.0029 0.0076  -0.0022 128 LEU B CB  
5174 C CG  . LEU B 128 ? 0.1408 0.1523 0.2122 -0.0034 0.0071  -0.0030 128 LEU B CG  
5175 C CD1 . LEU B 128 ? 0.2944 0.3103 0.3666 -0.0037 0.0062  -0.0017 128 LEU B CD1 
5176 C CD2 . LEU B 128 ? 0.1518 0.1634 0.2216 -0.0045 0.0070  -0.0038 128 LEU B CD2 
5177 N N   . ASP B 129 ? 0.0472 0.0540 0.1239 -0.0022 0.0094  -0.0017 129 ASP B N   
5178 C CA  . ASP B 129 ? 0.1073 0.1142 0.1855 -0.0025 0.0098  -0.0011 129 ASP B CA  
5179 C C   . ASP B 129 ? 0.1284 0.1314 0.2053 -0.0021 0.0108  -0.0028 129 ASP B C   
5180 O O   . ASP B 129 ? 0.1064 0.1097 0.1824 -0.0029 0.0109  -0.0030 129 ASP B O   
5181 C CB  . ASP B 129 ? 0.0964 0.1042 0.1781 -0.0016 0.0102  0.0006  129 ASP B CB  
5182 C CG  . ASP B 129 ? 0.2123 0.2253 0.2956 -0.0018 0.0093  0.0025  129 ASP B CG  
5183 O OD1 . ASP B 129 ? 0.2346 0.2503 0.3164 -0.0028 0.0083  0.0023  129 ASP B OD1 
5184 O OD2 . ASP B 129 ? 0.2313 0.2458 0.3171 -0.0008 0.0094  0.0042  129 ASP B OD2 
5185 N N   . LEU B 130 ? 0.1141 0.1135 0.1904 -0.0009 0.0114  -0.0039 130 LEU B N   
5186 C CA  . LEU B 130 ? 0.1069 0.1049 0.1798 -0.0006 0.0120  -0.0051 130 LEU B CA  
5187 C C   . LEU B 130 ? 0.1128 0.1113 0.1834 -0.0009 0.0118  -0.0064 130 LEU B C   
5188 O O   . LEU B 130 ? 0.1146 0.1131 0.1842 -0.0011 0.0123  -0.0070 130 LEU B O   
5189 C CB  . LEU B 130 ? 0.0927 0.0900 0.1616 -0.0004 0.0119  -0.0053 130 LEU B CB  
5190 C CG  . LEU B 130 ? 0.1276 0.1248 0.1927 -0.0001 0.0122  -0.0060 130 LEU B CG  
5191 C CD1 . LEU B 130 ? 0.1510 0.1482 0.2182 0.0001  0.0131  -0.0055 130 LEU B CD1 
5192 C CD2 . LEU B 130 ? 0.1899 0.1867 0.2510 0.0003  0.0119  -0.0061 130 LEU B CD2 
5193 N N   . GLN B 131 ? 0.1371 0.1359 0.2068 -0.0011 0.0112  -0.0069 131 GLN B N   
5194 C CA  . GLN B 131 ? 0.0687 0.0682 0.1372 -0.0016 0.0112  -0.0081 131 GLN B CA  
5195 C C   . GLN B 131 ? 0.0949 0.0966 0.1622 -0.0036 0.0105  -0.0072 131 GLN B C   
5196 O O   . GLN B 131 ? 0.0992 0.1006 0.1652 -0.0041 0.0109  -0.0080 131 GLN B O   
5197 C CB  . GLN B 131 ? 0.0812 0.0812 0.1494 -0.0017 0.0106  -0.0084 131 GLN B CB  
5198 C CG  . GLN B 131 ? 0.1105 0.1096 0.1766 -0.0011 0.0105  -0.0086 131 GLN B CG  
5199 C CD  . GLN B 131 ? 0.1058 0.1052 0.1725 -0.0011 0.0100  -0.0089 131 GLN B CD  
5200 O OE1 . GLN B 131 ? 0.1482 0.1491 0.2170 -0.0017 0.0094  -0.0080 131 GLN B OE1 
5201 N NE2 . GLN B 131 ? 0.1071 0.1063 0.1708 -0.0010 0.0099  -0.0096 131 GLN B NE2 
5202 N N   . THR B 132 ? 0.0611 0.0654 0.1288 -0.0047 0.0096  -0.0055 132 THR B N   
5203 C CA  . THR B 132 ? 0.0649 0.0717 0.1317 -0.0067 0.0089  -0.0048 132 THR B CA  
5204 C C   . THR B 132 ? 0.0958 0.1016 0.1634 -0.0070 0.0095  -0.0045 132 THR B C   
5205 O O   . THR B 132 ? 0.1378 0.1440 0.2032 -0.0086 0.0092  -0.0046 132 THR B O   
5206 C CB  . THR B 132 ? 0.1030 0.1136 0.1719 -0.0074 0.0081  -0.0032 132 THR B CB  
5207 O OG1 . THR B 132 ? 0.0874 0.0987 0.1555 -0.0070 0.0076  -0.0034 132 THR B OG1 
5208 C CG2 . THR B 132 ? 0.1434 0.1566 0.2110 -0.0095 0.0073  -0.0026 132 THR B CG2 
5209 N N   . LEU B 133 ? 0.1249 0.1294 0.1956 -0.0057 0.0103  -0.0042 133 LEU B N   
5210 C CA  . LEU B 133 ? 0.0995 0.1028 0.1709 -0.0059 0.0110  -0.0039 133 LEU B CA  
5211 C C   . LEU B 133 ? 0.1254 0.1265 0.1937 -0.0056 0.0117  -0.0055 133 LEU B C   
5212 O O   . LEU B 133 ? 0.0772 0.0778 0.1441 -0.0066 0.0118  -0.0055 133 LEU B O   
5213 C CB  . LEU B 133 ? 0.1227 0.1252 0.1982 -0.0044 0.0118  -0.0029 133 LEU B CB  
5214 C CG  . LEU B 133 ? 0.0995 0.1052 0.1783 -0.0049 0.0112  -0.0007 133 LEU B CG  
5215 C CD1 . LEU B 133 ? 0.0793 0.0841 0.1617 -0.0031 0.0119  0.0004  133 LEU B CD1 
5216 C CD2 . LEU B 133 ? 0.1477 0.1555 0.2268 -0.0066 0.0107  0.0004  133 LEU B CD2 
5217 N N   . ASN B 134 ? 0.1288 0.1287 0.1959 -0.0042 0.0121  -0.0068 134 ASN B N   
5218 C CA  . ASN B 134 ? 0.1383 0.1372 0.2036 -0.0038 0.0129  -0.0082 134 ASN B CA  
5219 C C   . ASN B 134 ? 0.1977 0.1972 0.2608 -0.0055 0.0123  -0.0086 134 ASN B C   
5220 O O   . ASN B 134 ? 0.1327 0.1316 0.1944 -0.0061 0.0127  -0.0091 134 ASN B O   
5221 C CB  . ASN B 134 ? 0.0348 0.0334 0.1012 -0.0019 0.0137  -0.0096 134 ASN B CB  
5222 C CG  . ASN B 134 ? 0.1502 0.1485 0.2148 -0.0015 0.0139  -0.0090 134 ASN B CG  
5223 O OD1 . ASN B 134 ? 0.1342 0.1326 0.1977 -0.0016 0.0146  -0.0094 134 ASN B OD1 
5224 N ND2 . ASN B 134 ? 0.1138 0.1121 0.1783 -0.0010 0.0134  -0.0080 134 ASN B ND2 
5225 N N   . LEU B 135 ? 0.0894 0.0903 0.1521 -0.0064 0.0114  -0.0082 135 LEU B N   
5226 C CA  . LEU B 135 ? 0.1323 0.1341 0.1930 -0.0082 0.0108  -0.0083 135 LEU B CA  
5227 C C   . LEU B 135 ? 0.1176 0.1200 0.1770 -0.0101 0.0102  -0.0072 135 LEU B C   
5228 O O   . LEU B 135 ? 0.1091 0.1108 0.1667 -0.0111 0.0104  -0.0077 135 LEU B O   
5229 C CB  . LEU B 135 ? 0.1686 0.1723 0.2294 -0.0088 0.0098  -0.0079 135 LEU B CB  
5230 C CG  . LEU B 135 ? 0.2913 0.2949 0.3515 -0.0084 0.0099  -0.0091 135 LEU B CG  
5231 C CD1 . LEU B 135 ? 0.2107 0.2170 0.2703 -0.0101 0.0087  -0.0082 135 LEU B CD1 
5232 C CD2 . LEU B 135 ? 0.1070 0.1093 0.1658 -0.0083 0.0108  -0.0106 135 LEU B CD2 
5233 N N   . LEU B 136 ? 0.0787 0.0827 0.1392 -0.0106 0.0096  -0.0056 136 LEU B N   
5234 C CA  . LEU B 136 ? 0.0383 0.0433 0.0985 -0.0125 0.0091  -0.0044 136 LEU B CA  
5235 C C   . LEU B 136 ? 0.1230 0.1256 0.1827 -0.0124 0.0099  -0.0047 136 LEU B C   
5236 O O   . LEU B 136 ? 0.1133 0.1161 0.1718 -0.0140 0.0096  -0.0042 136 LEU B O   
5237 C CB  . LEU B 136 ? 0.0488 0.0565 0.1133 -0.0125 0.0088  -0.0029 136 LEU B CB  
5238 C CG  . LEU B 136 ? 0.0789 0.0899 0.1433 -0.0133 0.0078  -0.0024 136 LEU B CG  
5239 C CD1 . LEU B 136 ? 0.1346 0.1485 0.2034 -0.0126 0.0076  -0.0009 136 LEU B CD1 
5240 C CD2 . LEU B 136 ? 0.1230 0.1357 0.1845 -0.0157 0.0070  -0.0022 136 LEU B CD2 
5241 N N   . ALA B 137 ? 0.1056 0.1062 0.1662 -0.0104 0.0109  -0.0055 137 ALA B N   
5242 C CA  . ALA B 137 ? 0.1535 0.1520 0.2133 -0.0102 0.0117  -0.0058 137 ALA B CA  
5243 C C   . ALA B 137 ? 0.0868 0.0844 0.1433 -0.0113 0.0117  -0.0067 137 ALA B C   
5244 O O   . ALA B 137 ? 0.1048 0.1011 0.1599 -0.0121 0.0118  -0.0065 137 ALA B O   
5245 C CB  . ALA B 137 ? 0.0902 0.0874 0.1515 -0.0079 0.0128  -0.0065 137 ALA B CB  
5246 N N   . TRP B 138 ? 0.1161 0.1142 0.1721 -0.0112 0.0117  -0.0078 138 TRP B N   
5247 C CA  . TRP B 138 ? 0.1715 0.1688 0.2253 -0.0120 0.0120  -0.0088 138 TRP B CA  
5248 C C   . TRP B 138 ? 0.0929 0.0915 0.1450 -0.0143 0.0108  -0.0081 138 TRP B C   
5249 O O   . TRP B 138 ? 0.1057 0.1040 0.1562 -0.0149 0.0110  -0.0089 138 TRP B O   
5250 C CB  . TRP B 138 ? 0.1466 0.1438 0.2011 -0.0104 0.0130  -0.0104 138 TRP B CB  
5251 C CG  . TRP B 138 ? 0.0987 0.0953 0.1550 -0.0084 0.0142  -0.0110 138 TRP B CG  
5252 C CD1 . TRP B 138 ? 0.1173 0.1144 0.1759 -0.0068 0.0144  -0.0109 138 TRP B CD1 
5253 C CD2 . TRP B 138 ? 0.1191 0.1149 0.1751 -0.0077 0.0154  -0.0118 138 TRP B CD2 
5254 N NE1 . TRP B 138 ? 0.1406 0.1375 0.2006 -0.0053 0.0157  -0.0115 138 TRP B NE1 
5255 C CE2 . TRP B 138 ? 0.1381 0.1343 0.1965 -0.0059 0.0163  -0.0120 138 TRP B CE2 
5256 C CE3 . TRP B 138 ? 0.1082 0.1030 0.1622 -0.0086 0.0158  -0.0123 138 TRP B CE3 
5257 C CZ2 . TRP B 138 ? 0.1608 0.1570 0.2197 -0.0051 0.0177  -0.0126 138 TRP B CZ2 
5258 C CZ3 . TRP B 138 ? 0.1099 0.1044 0.1644 -0.0077 0.0171  -0.0129 138 TRP B CZ3 
5259 C CH2 . TRP B 138 ? 0.1621 0.1574 0.2190 -0.0060 0.0180  -0.0131 138 TRP B CH2 
5260 N N   . CYS B 139 ? 0.0722 0.0725 0.1246 -0.0155 0.0098  -0.0065 139 CYS B N   
5261 C CA  . CYS B 139 ? 0.0970 0.0991 0.1479 -0.0178 0.0087  -0.0057 139 CYS B CA  
5262 C C   . CYS B 139 ? 0.1041 0.1049 0.1527 -0.0193 0.0086  -0.0057 139 CYS B C   
5263 O O   . CYS B 139 ? 0.0936 0.0931 0.1420 -0.0193 0.0089  -0.0052 139 CYS B O   
5264 C CB  . CYS B 139 ? 0.1023 0.1072 0.1544 -0.0188 0.0078  -0.0039 139 CYS B CB  
5265 S SG  . CYS B 139 ? 0.1154 0.1238 0.1662 -0.0213 0.0064  -0.0030 139 CYS B SG  
5266 N N   . GLY B 140 ? 0.0976 0.0988 0.1445 -0.0205 0.0083  -0.0061 140 GLY B N   
5267 C CA  . GLY B 140 ? 0.0885 0.0885 0.1332 -0.0219 0.0081  -0.0061 140 GLY B CA  
5268 C C   . GLY B 140 ? 0.1215 0.1234 0.1655 -0.0243 0.0069  -0.0043 140 GLY B C   
5269 O O   . GLY B 140 ? 0.1068 0.1115 0.1519 -0.0249 0.0062  -0.0031 140 GLY B O   
5270 N N   . ARG B 141 ? 0.0984 0.0991 0.1405 -0.0255 0.0068  -0.0041 141 ARG B N   
5271 C CA  . ARG B 141 ? 0.1475 0.1497 0.1887 -0.0278 0.0057  -0.0024 141 ARG B CA  
5272 C C   . ARG B 141 ? 0.1421 0.1479 0.1835 -0.0294 0.0045  -0.0014 141 ARG B C   
5273 O O   . ARG B 141 ? 0.0954 0.1040 0.1373 -0.0307 0.0039  0.0000  141 ARG B O   
5274 C CB  . ARG B 141 ? 0.1348 0.1349 0.1740 -0.0288 0.0057  -0.0026 141 ARG B CB  
5275 C CG  . ARG B 141 ? 0.1457 0.1474 0.1840 -0.0312 0.0044  -0.0008 141 ARG B CG  
5276 C CD  . ARG B 141 ? 0.1617 0.1609 0.1983 -0.0318 0.0045  -0.0011 141 ARG B CD  
5277 N NE  . ARG B 141 ? 0.1961 0.1968 0.2323 -0.0340 0.0031  0.0007  141 ARG B NE  
5278 C CZ  . ARG B 141 ? 0.2087 0.2103 0.2450 -0.0350 0.0022  0.0010  141 ARG B CZ  
5279 N NH1 . ARG B 141 ? 0.1177 0.1189 0.1538 -0.0342 0.0027  -0.0005 141 ARG B NH1 
5280 N NH2 . ARG B 141 ? 0.2418 0.2448 0.2788 -0.0360 0.0012  0.0027  141 ARG B NH2 
5281 N N   . THR B 142 ? 0.0898 0.0956 0.1307 -0.0293 0.0044  -0.0023 142 THR B N   
5282 C CA  . THR B 142 ? 0.1267 0.1356 0.1676 -0.0308 0.0033  -0.0013 142 THR B CA  
5283 C C   . THR B 142 ? 0.1442 0.1562 0.1868 -0.0305 0.0031  -0.0006 142 THR B C   
5284 O O   . THR B 142 ? 0.1581 0.1735 0.2009 -0.0320 0.0023  0.0008  142 THR B O   
5285 C CB  . THR B 142 ? 0.1220 0.1301 0.1623 -0.0304 0.0035  -0.0025 142 THR B CB  
5286 O OG1 . THR B 142 ? 0.1147 0.1203 0.1536 -0.0307 0.0038  -0.0033 142 THR B OG1 
5287 C CG2 . THR B 142 ? 0.1350 0.1462 0.1758 -0.0317 0.0022  -0.0015 142 THR B CG2 
5288 N N   . LEU B 143 ? 0.1418 0.1528 0.1858 -0.0283 0.0040  -0.0018 143 LEU B N   
5289 C CA  . LEU B 143 ? 0.1292 0.1430 0.1752 -0.0277 0.0038  -0.0013 143 LEU B CA  
5290 C C   . LEU B 143 ? 0.1587 0.1735 0.2065 -0.0274 0.0041  -0.0005 143 LEU B C   
5291 O O   . LEU B 143 ? 0.1797 0.1977 0.2306 -0.0271 0.0041  0.0000  143 LEU B O   
5292 C CB  . LEU B 143 ? 0.0823 0.0944 0.1293 -0.0254 0.0046  -0.0027 143 LEU B CB  
5293 C CG  . LEU B 143 ? 0.0961 0.1083 0.1420 -0.0258 0.0044  -0.0035 143 LEU B CG  
5294 C CD1 . LEU B 143 ? 0.1064 0.1174 0.1535 -0.0236 0.0052  -0.0049 143 LEU B CD1 
5295 C CD2 . LEU B 143 ? 0.1775 0.1935 0.2233 -0.0276 0.0031  -0.0022 143 LEU B CD2 
5296 N N   . ARG B 144 ? 0.1468 0.1589 0.1948 -0.0270 0.0048  -0.0007 144 ARG B N   
5297 C CA  . ARG B 144 ? 0.0847 0.0977 0.1368 -0.0265 0.0054  0.0001  144 ARG B CA  
5298 C C   . ARG B 144 ? 0.1727 0.1895 0.2263 -0.0284 0.0048  0.0014  144 ARG B C   
5299 O O   . ARG B 144 ? 0.1774 0.1969 0.2352 -0.0277 0.0049  0.0025  144 ARG B O   
5300 C CB  . ARG B 144 ? 0.1195 0.1288 0.1709 -0.0260 0.0062  -0.0002 144 ARG B CB  
5301 C CG  . ARG B 144 ? 0.1579 0.1643 0.2102 -0.0235 0.0072  -0.0012 144 ARG B CG  
5302 C CD  . ARG B 144 ? 0.1915 0.1944 0.2424 -0.0232 0.0078  -0.0016 144 ARG B CD  
5303 N NE  . ARG B 144 ? 0.2287 0.2291 0.2802 -0.0209 0.0088  -0.0026 144 ARG B NE  
5304 C CZ  . ARG B 144 ? 0.1924 0.1922 0.2474 -0.0194 0.0096  -0.0022 144 ARG B CZ  
5305 N NH1 . ARG B 144 ? 0.2825 0.2843 0.3411 -0.0199 0.0096  -0.0006 144 ARG B NH1 
5306 N NH2 . ARG B 144 ? 0.2490 0.2467 0.3042 -0.0173 0.0105  -0.0031 144 ARG B NH2 
5307 N N   . LYS B 145 ? 0.1347 0.1521 0.1849 -0.0307 0.0041  0.0014  145 LYS B N   
5308 C CA  . LYS B 145 ? 0.2222 0.2436 0.2735 -0.0326 0.0037  0.0022  145 LYS B CA  
5309 C C   . LYS B 145 ? 0.2068 0.2321 0.2590 -0.0326 0.0032  0.0022  145 LYS B C   
5310 O O   . LYS B 145 ? 0.2007 0.2296 0.2567 -0.0323 0.0031  0.0029  145 LYS B O   
5311 C CB  . LYS B 145 ? 0.2181 0.2387 0.2652 -0.0351 0.0031  0.0023  145 LYS B CB  
5312 C CG  . LYS B 145 ? 0.4038 0.4210 0.4503 -0.0353 0.0036  0.0025  145 LYS B CG  
5313 C CD  . LYS B 145 ? 0.5029 0.5177 0.5452 -0.0363 0.0025  0.0028  145 LYS B CD  
5314 C CE  . LYS B 145 ? 0.4512 0.4641 0.4932 -0.0372 0.0029  0.0032  145 LYS B CE  
5315 N NZ  . LYS B 145 ? 0.3214 0.3307 0.3640 -0.0359 0.0039  0.0026  145 LYS B NZ  
5316 N N   . ASP B 146 ? 0.2270 0.2514 0.2761 -0.0325 0.0027  0.0016  146 ASP B N   
5317 C CA  . ASP B 146 ? 0.2059 0.2338 0.2552 -0.0327 0.0022  0.0015  146 ASP B CA  
5318 C C   . ASP B 146 ? 0.2556 0.2851 0.3091 -0.0304 0.0025  0.0016  146 ASP B C   
5319 O O   . ASP B 146 ? 0.2859 0.3194 0.3415 -0.0305 0.0023  0.0018  146 ASP B O   
5320 C CB  . ASP B 146 ? 0.2327 0.2585 0.2778 -0.0323 0.0013  0.0015  146 ASP B CB  
5321 C CG  . ASP B 146 ? 0.2798 0.3037 0.3226 -0.0334 0.0005  0.0021  146 ASP B CG  
5322 O OD1 . ASP B 146 ? 0.3485 0.3733 0.3900 -0.0345 0.0002  0.0028  146 ASP B OD1 
5323 O OD2 . ASP B 146 ? 0.3834 0.4051 0.4264 -0.0330 0.0002  0.0017  146 ASP B OD2 
5324 N N   . LEU B 147 ? 0.1724 0.1988 0.2271 -0.0283 0.0031  0.0014  147 LEU B N   
5325 C CA  . LEU B 147 ? 0.1480 0.1754 0.2064 -0.0260 0.0033  0.0017  147 LEU B CA  
5326 C C   . LEU B 147 ? 0.1454 0.1732 0.2084 -0.0249 0.0037  0.0029  147 LEU B C   
5327 O O   . LEU B 147 ? 0.1815 0.2083 0.2471 -0.0227 0.0041  0.0031  147 LEU B O   
5328 C CB  . LEU B 147 ? 0.1705 0.1942 0.2274 -0.0243 0.0038  0.0005  147 LEU B CB  
5329 C CG  . LEU B 147 ? 0.2182 0.2405 0.2706 -0.0249 0.0034  -0.0003 147 LEU B CG  
5330 C CD1 . LEU B 147 ? 0.1868 0.2052 0.2396 -0.0227 0.0042  -0.0016 147 LEU B CD1 
5331 C CD2 . LEU B 147 ? 0.3628 0.3887 0.4154 -0.0255 0.0027  0.0000  147 LEU B CD2 
5332 N N   . LYS B 148 ? 0.1079 0.1370 0.1718 -0.0262 0.0035  0.0040  148 LYS B N   
5333 C CA  . LYS B 148 ? 0.1608 0.1896 0.2285 -0.0252 0.0038  0.0056  148 LYS B CA  
5334 C C   . LYS B 148 ? 0.2188 0.2504 0.2913 -0.0231 0.0035  0.0072  148 LYS B C   
5335 O O   . LYS B 148 ? 0.2469 0.2769 0.3222 -0.0213 0.0041  0.0080  148 LYS B O   
5336 C CB  . LYS B 148 ? 0.2499 0.2803 0.3177 -0.0271 0.0033  0.0068  148 LYS B CB  
5337 C CG  . LYS B 148 ? 0.4322 0.4612 0.5027 -0.0265 0.0037  0.0084  148 LYS B CG  
5338 C CD  . LYS B 148 ? 0.5802 0.6091 0.6489 -0.0288 0.0035  0.0090  148 LYS B CD  
5339 C CE  . LYS B 148 ? 0.6087 0.6424 0.6776 -0.0302 0.0022  0.0101  148 LYS B CE  
5340 N NZ  . LYS B 148 ? 0.6207 0.6590 0.6940 -0.0286 0.0013  0.0127  148 LYS B NZ  
5341 N N   . ASP B 149 ? 0.2163 0.2520 0.2897 -0.0231 0.0026  0.0078  149 ASP B N   
5342 C CA  . ASP B 149 ? 0.2963 0.3351 0.3739 -0.0211 0.0022  0.0097  149 ASP B CA  
5343 C C   . ASP B 149 ? 0.2257 0.2623 0.3037 -0.0190 0.0029  0.0086  149 ASP B C   
5344 O O   . ASP B 149 ? 0.2420 0.2791 0.3234 -0.0169 0.0031  0.0098  149 ASP B O   
5345 C CB  . ASP B 149 ? 0.3610 0.4047 0.4388 -0.0218 0.0009  0.0105  149 ASP B CB  
5346 C CG  . ASP B 149 ? 0.4649 0.5108 0.5423 -0.0237 0.0002  0.0118  149 ASP B CG  
5347 O OD1 . ASP B 149 ? 0.3675 0.4134 0.4468 -0.0236 0.0001  0.0137  149 ASP B OD1 
5348 O OD2 . ASP B 149 ? 0.5817 0.6291 0.6567 -0.0254 -0.0003 0.0108  149 ASP B OD2 
5349 N N   . LEU B 150 ? 0.2113 0.2457 0.2856 -0.0195 0.0032  0.0063  150 LEU B N   
5350 C CA  . LEU B 150 ? 0.2025 0.2343 0.2767 -0.0177 0.0038  0.0052  150 LEU B CA  
5351 C C   . LEU B 150 ? 0.2185 0.2462 0.2937 -0.0165 0.0049  0.0049  150 LEU B C   
5352 O O   . LEU B 150 ? 0.1874 0.2140 0.2650 -0.0144 0.0054  0.0052  150 LEU B O   
5353 C CB  . LEU B 150 ? 0.2704 0.3007 0.3401 -0.0186 0.0037  0.0033  150 LEU B CB  
5354 C CG  . LEU B 150 ? 0.3439 0.3746 0.4130 -0.0175 0.0036  0.0026  150 LEU B CG  
5355 C CD1 . LEU B 150 ? 0.3171 0.3521 0.3895 -0.0166 0.0030  0.0040  150 LEU B CD1 
5356 C CD2 . LEU B 150 ? 0.2721 0.3027 0.3368 -0.0191 0.0032  0.0014  150 LEU B CD2 
5357 N N   . LEU B 151 ? 0.1918 0.2170 0.2650 -0.0178 0.0053  0.0044  151 LEU B N   
5358 C CA  . LEU B 151 ? 0.2219 0.2431 0.2958 -0.0167 0.0064  0.0041  151 LEU B CA  
5359 C C   . LEU B 151 ? 0.2735 0.2961 0.3522 -0.0155 0.0066  0.0063  151 LEU B C   
5360 O O   . LEU B 151 ? 0.2892 0.3094 0.3698 -0.0137 0.0076  0.0062  151 LEU B O   
5361 C CB  . LEU B 151 ? 0.2701 0.2888 0.3405 -0.0185 0.0066  0.0032  151 LEU B CB  
5362 C CG  . LEU B 151 ? 0.4649 0.4786 0.5335 -0.0176 0.0077  0.0018  151 LEU B CG  
5363 C CD1 . LEU B 151 ? 0.5149 0.5266 0.5785 -0.0193 0.0076  0.0005  151 LEU B CD1 
5364 C CD2 . LEU B 151 ? 0.4412 0.4537 0.5130 -0.0168 0.0085  0.0030  151 LEU B CD2 
5365 N N   . ASN B 152 ? 0.3575 0.3842 0.4382 -0.0163 0.0058  0.0083  152 ASN B N   
5366 C CA  . ASN B 152 ? 0.3843 0.4132 0.4696 -0.0149 0.0058  0.0109  152 ASN B CA  
5367 C C   . ASN B 152 ? 0.3303 0.3609 0.4187 -0.0124 0.0059  0.0118  152 ASN B C   
5368 O O   . ASN B 152 ? 0.3826 0.4138 0.4744 -0.0107 0.0063  0.0135  152 ASN B O   
5369 C CB  . ASN B 152 ? 0.5062 0.5395 0.5926 -0.0163 0.0046  0.0132  152 ASN B CB  
5370 C CG  . ASN B 152 ? 0.6089 0.6404 0.6928 -0.0186 0.0047  0.0129  152 ASN B CG  
5371 O OD1 . ASN B 152 ? 0.6042 0.6310 0.6861 -0.0189 0.0057  0.0114  152 ASN B OD1 
5372 N ND2 . ASN B 152 ? 0.6651 0.7001 0.7486 -0.0203 0.0035  0.0143  152 ASN B ND2 
5373 N N   . LYS B 153 ? 0.2992 0.3308 0.3862 -0.0122 0.0054  0.0106  153 LYS B N   
5374 C CA  . LYS B 153 ? 0.3078 0.3403 0.3968 -0.0099 0.0055  0.0111  153 LYS B CA  
5375 C C   . LYS B 153 ? 0.3279 0.3564 0.4182 -0.0081 0.0069  0.0105  153 LYS B C   
5376 O O   . LYS B 153 ? 0.2960 0.3252 0.3892 -0.0060 0.0072  0.0120  153 LYS B O   
5377 C CB  . LYS B 153 ? 0.3243 0.3570 0.4107 -0.0101 0.0050  0.0094  153 LYS B CB  
5378 C CG  . LYS B 153 ? 0.3250 0.3622 0.4108 -0.0112 0.0037  0.0100  153 LYS B CG  
5379 C CD  . LYS B 153 ? 0.2812 0.3177 0.3638 -0.0117 0.0035  0.0080  153 LYS B CD  
5380 C CE  . LYS B 153 ? 0.1928 0.2269 0.2758 -0.0097 0.0042  0.0073  153 LYS B CE  
5381 N NZ  . LYS B 153 ? 0.2435 0.2805 0.3290 -0.0078 0.0038  0.0088  153 LYS B NZ  
5382 N N   . GLY B 154 ? 0.2737 0.2977 0.3613 -0.0087 0.0077  0.0083  154 GLY B N   
5383 C CA  . GLY B 154 ? 0.3021 0.3217 0.3901 -0.0072 0.0090  0.0074  154 GLY B CA  
5384 C C   . GLY B 154 ? 0.2343 0.2532 0.3231 -0.0052 0.0093  0.0070  154 GLY B C   
5385 O O   . GLY B 154 ? 0.1956 0.2109 0.2848 -0.0040 0.0104  0.0063  154 GLY B O   
5386 N N   . ARG B 155 ? 0.1722 0.1943 0.2609 -0.0051 0.0083  0.0074  155 ARG B N   
5387 C CA  . ARG B 155 ? 0.1957 0.2172 0.2848 -0.0033 0.0085  0.0073  155 ARG B CA  
5388 C C   . ARG B 155 ? 0.1583 0.1833 0.2463 -0.0037 0.0073  0.0073  155 ARG B C   
5389 O O   . ARG B 155 ? 0.2563 0.2845 0.3437 -0.0052 0.0064  0.0078  155 ARG B O   
5390 C CB  . ARG B 155 ? 0.3035 0.3257 0.3957 -0.0013 0.0090  0.0092  155 ARG B CB  
5391 C CG  . ARG B 155 ? 0.3013 0.3284 0.3958 -0.0012 0.0082  0.0117  155 ARG B CG  
5392 C CD  . ARG B 155 ? 0.3911 0.4180 0.4883 0.0007  0.0089  0.0136  155 ARG B CD  
5393 N NE  . ARG B 155 ? 0.3424 0.3660 0.4391 0.0025  0.0098  0.0129  155 ARG B NE  
5394 C CZ  . ARG B 155 ? 0.3312 0.3513 0.4283 0.0035  0.0111  0.0128  155 ARG B CZ  
5395 N NH1 . ARG B 155 ? 0.3654 0.3846 0.4639 0.0032  0.0117  0.0133  155 ARG B NH1 
5396 N NH2 . ARG B 155 ? 0.4882 0.5055 0.5841 0.0047  0.0118  0.0121  155 ARG B NH2 
5397 N N   . ASN B 156 ? 0.1431 0.1673 0.2305 -0.0025 0.0074  0.0068  156 ASN B N   
5398 C CA  . ASN B 156 ? 0.1978 0.2252 0.2844 -0.0026 0.0064  0.0070  156 ASN B CA  
5399 C C   . ASN B 156 ? 0.2245 0.2527 0.3082 -0.0045 0.0057  0.0057  156 ASN B C   
5400 O O   . ASN B 156 ? 0.1895 0.2217 0.2730 -0.0053 0.0047  0.0064  156 ASN B O   
5401 C CB  . ASN B 156 ? 0.2652 0.2974 0.3542 -0.0019 0.0057  0.0093  156 ASN B CB  
5402 C CG  . ASN B 156 ? 0.3526 0.3842 0.4441 0.0001  0.0063  0.0109  156 ASN B CG  
5403 O OD1 . ASN B 156 ? 0.4274 0.4613 0.5210 0.0005  0.0061  0.0128  156 ASN B OD1 
5404 N ND2 . ASN B 156 ? 0.2893 0.3177 0.3803 0.0013  0.0071  0.0101  156 ASN B ND2 
5405 N N   . TYR B 157 ? 0.1133 0.1377 0.1946 -0.0050 0.0062  0.0039  157 TYR B N   
5406 C CA  . TYR B 157 ? 0.0683 0.0929 0.1462 -0.0067 0.0057  0.0026  157 TYR B CA  
5407 C C   . TYR B 157 ? 0.1026 0.1276 0.1788 -0.0063 0.0053  0.0019  157 TYR B C   
5408 O O   . TYR B 157 ? 0.1451 0.1680 0.2215 -0.0050 0.0058  0.0015  157 TYR B O   
5409 C CB  . TYR B 157 ? 0.0993 0.1197 0.1751 -0.0072 0.0064  0.0010  157 TYR B CB  
5410 C CG  . TYR B 157 ? 0.0746 0.0950 0.1514 -0.0080 0.0067  0.0016  157 TYR B CG  
5411 C CD1 . TYR B 157 ? 0.1297 0.1527 0.2053 -0.0099 0.0059  0.0020  157 TYR B CD1 
5412 C CD2 . TYR B 157 ? 0.0941 0.1118 0.1729 -0.0070 0.0076  0.0018  157 TYR B CD2 
5413 C CE1 . TYR B 157 ? 0.1742 0.1970 0.2505 -0.0109 0.0061  0.0026  157 TYR B CE1 
5414 C CE2 . TYR B 157 ? 0.1311 0.1486 0.2106 -0.0078 0.0079  0.0024  157 TYR B CE2 
5415 C CZ  . TYR B 157 ? 0.2186 0.2387 0.2969 -0.0098 0.0071  0.0028  157 TYR B CZ  
5416 O OH  . TYR B 157 ? 0.1762 0.1960 0.2550 -0.0107 0.0073  0.0035  157 TYR B OH  
5417 N N   . THR B 158 ? 0.0958 0.1233 0.1699 -0.0077 0.0045  0.0017  158 THR B N   
5418 C CA  . THR B 158 ? 0.0910 0.1189 0.1629 -0.0076 0.0042  0.0009  158 THR B CA  
5419 C C   . THR B 158 ? 0.1307 0.1553 0.2000 -0.0083 0.0044  -0.0006 158 THR B C   
5420 O O   . THR B 158 ? 0.0684 0.0919 0.1365 -0.0093 0.0046  -0.0011 158 THR B O   
5421 C CB  . THR B 158 ? 0.0916 0.1244 0.1635 -0.0084 0.0032  0.0018  158 THR B CB  
5422 O OG1 . THR B 158 ? 0.0747 0.1090 0.1452 -0.0103 0.0028  0.0017  158 THR B OG1 
5423 C CG2 . THR B 158 ? 0.1097 0.1456 0.1853 -0.0074 0.0030  0.0035  158 THR B CG2 
5424 N N   . GLN B 159 ? 0.0861 0.1092 0.1552 -0.0077 0.0045  -0.0015 159 GLN B N   
5425 C CA  . GLN B 159 ? 0.1921 0.2124 0.2596 -0.0080 0.0048  -0.0031 159 GLN B CA  
5426 C C   . GLN B 159 ? 0.1725 0.1950 0.2384 -0.0099 0.0042  -0.0030 159 GLN B C   
5427 O O   . GLN B 159 ? 0.1244 0.1448 0.1888 -0.0104 0.0045  -0.0040 159 GLN B O   
5428 C CB  . GLN B 159 ? 0.1197 0.1389 0.1874 -0.0072 0.0048  -0.0038 159 GLN B CB  
5429 C CG  . GLN B 159 ? 0.1375 0.1542 0.2036 -0.0073 0.0051  -0.0054 159 GLN B CG  
5430 C CD  . GLN B 159 ? 0.1446 0.1569 0.2103 -0.0062 0.0061  -0.0068 159 GLN B CD  
5431 O OE1 . GLN B 159 ? 0.1378 0.1482 0.2046 -0.0052 0.0066  -0.0067 159 GLN B OE1 
5432 N NE2 . GLN B 159 ? 0.1680 0.1787 0.2323 -0.0064 0.0065  -0.0081 159 GLN B NE2 
5433 N N   . GLU B 160 ? 0.0541 0.0811 0.1203 -0.0108 0.0034  -0.0018 160 GLU B N   
5434 C CA  . GLU B 160 ? 0.1050 0.1343 0.1697 -0.0127 0.0028  -0.0016 160 GLU B CA  
5435 C C   . GLU B 160 ? 0.0846 0.1134 0.1485 -0.0138 0.0030  -0.0014 160 GLU B C   
5436 O O   . GLU B 160 ? 0.1089 0.1367 0.1710 -0.0150 0.0030  -0.0020 160 GLU B O   
5437 C CB  . GLU B 160 ? 0.1272 0.1615 0.1925 -0.0134 0.0020  -0.0005 160 GLU B CB  
5438 C CG  . GLU B 160 ? 0.2142 0.2509 0.2778 -0.0155 0.0014  -0.0004 160 GLU B CG  
5439 C CD  . GLU B 160 ? 0.3356 0.3704 0.3976 -0.0159 0.0014  -0.0015 160 GLU B CD  
5440 O OE1 . GLU B 160 ? 0.4713 0.5065 0.5315 -0.0175 0.0012  -0.0016 160 GLU B OE1 
5441 O OE2 . GLU B 160 ? 0.4164 0.4493 0.4789 -0.0145 0.0017  -0.0021 160 GLU B OE2 
5442 N N   . GLU B 161 ? 0.0815 0.1111 0.1467 -0.0133 0.0031  -0.0005 161 GLU B N   
5443 C CA  . GLU B 161 ? 0.0565 0.0853 0.1210 -0.0143 0.0033  -0.0004 161 GLU B CA  
5444 C C   . GLU B 161 ? 0.0734 0.0973 0.1367 -0.0138 0.0041  -0.0018 161 GLU B C   
5445 O O   . GLU B 161 ? 0.0722 0.0952 0.1338 -0.0151 0.0042  -0.0021 161 GLU B O   
5446 C CB  . GLU B 161 ? 0.0417 0.0716 0.1094 -0.0134 0.0035  0.0008  161 GLU B CB  
5447 C CG  . GLU B 161 ? 0.0752 0.1103 0.1450 -0.0139 0.0027  0.0022  161 GLU B CG  
5448 C CD  . GLU B 161 ? 0.1679 0.2042 0.2419 -0.0123 0.0028  0.0037  161 GLU B CD  
5449 O OE1 . GLU B 161 ? 0.1000 0.1333 0.1754 -0.0108 0.0035  0.0036  161 GLU B OE1 
5450 O OE2 . GLU B 161 ? 0.2855 0.3259 0.3614 -0.0124 0.0021  0.0050  161 GLU B OE2 
5451 N N   . LYS B 162 ? 0.0787 0.0995 0.1428 -0.0120 0.0048  -0.0026 162 LYS B N   
5452 C CA  . LYS B 162 ? 0.0404 0.0569 0.1036 -0.0113 0.0057  -0.0041 162 LYS B CA  
5453 C C   . LYS B 162 ? 0.1248 0.1406 0.1860 -0.0121 0.0056  -0.0052 162 LYS B C   
5454 O O   . LYS B 162 ? 0.0958 0.1098 0.1557 -0.0126 0.0061  -0.0060 162 LYS B O   
5455 C CB  . LYS B 162 ? 0.0283 0.0421 0.0928 -0.0092 0.0064  -0.0049 162 LYS B CB  
5456 C CG  . LYS B 162 ? 0.0804 0.0901 0.1442 -0.0081 0.0074  -0.0066 162 LYS B CG  
5457 C CD  . LYS B 162 ? 0.1138 0.1211 0.1791 -0.0061 0.0081  -0.0072 162 LYS B CD  
5458 C CE  . LYS B 162 ? 0.1494 0.1573 0.2148 -0.0058 0.0077  -0.0074 162 LYS B CE  
5459 N NZ  . LYS B 162 ? 0.1123 0.1172 0.1786 -0.0039 0.0083  -0.0084 162 LYS B NZ  
5460 N N   . GLU B 163 ? 0.0845 0.1019 0.1457 -0.0123 0.0051  -0.0053 163 GLU B N   
5461 C CA  . GLU B 163 ? 0.1177 0.1347 0.1772 -0.0130 0.0051  -0.0062 163 GLU B CA  
5462 C C   . GLU B 163 ? 0.1065 0.1253 0.1644 -0.0152 0.0046  -0.0056 163 GLU B C   
5463 O O   . GLU B 163 ? 0.1311 0.1485 0.1873 -0.0158 0.0048  -0.0064 163 GLU B O   
5464 C CB  . GLU B 163 ? 0.1658 0.1842 0.2256 -0.0128 0.0047  -0.0062 163 GLU B CB  
5465 C CG  . GLU B 163 ? 0.1569 0.1727 0.2178 -0.0108 0.0053  -0.0072 163 GLU B CG  
5466 C CD  . GLU B 163 ? 0.3006 0.3178 0.3617 -0.0106 0.0049  -0.0072 163 GLU B CD  
5467 O OE1 . GLU B 163 ? 0.3662 0.3862 0.4265 -0.0120 0.0041  -0.0066 163 GLU B OE1 
5468 O OE2 . GLU B 163 ? 0.2272 0.2425 0.2892 -0.0091 0.0052  -0.0078 163 GLU B OE2 
5469 N N   . TYR B 164 ? 0.1313 0.1534 0.1896 -0.0163 0.0038  -0.0040 164 TYR B N   
5470 C CA  . TYR B 164 ? 0.1601 0.1840 0.2169 -0.0185 0.0033  -0.0034 164 TYR B CA  
5471 C C   . TYR B 164 ? 0.1843 0.2053 0.2400 -0.0187 0.0039  -0.0039 164 TYR B C   
5472 O O   . TYR B 164 ? 0.1039 0.1241 0.1577 -0.0199 0.0038  -0.0043 164 TYR B O   
5473 C CB  . TYR B 164 ? 0.2148 0.2430 0.2726 -0.0194 0.0026  -0.0018 164 TYR B CB  
5474 C CG  . TYR B 164 ? 0.1611 0.1916 0.2174 -0.0217 0.0020  -0.0011 164 TYR B CG  
5475 C CD1 . TYR B 164 ? 0.2890 0.3215 0.3438 -0.0233 0.0014  -0.0010 164 TYR B CD1 
5476 C CD2 . TYR B 164 ? 0.2076 0.2382 0.2637 -0.0224 0.0021  -0.0005 164 TYR B CD2 
5477 C CE1 . TYR B 164 ? 0.3592 0.3937 0.4125 -0.0255 0.0008  -0.0004 164 TYR B CE1 
5478 C CE2 . TYR B 164 ? 0.2101 0.2429 0.2647 -0.0247 0.0016  0.0000  164 TYR B CE2 
5479 C CZ  . TYR B 164 ? 0.3538 0.3885 0.4070 -0.0262 0.0010  0.0000  164 TYR B CZ  
5480 O OH  . TYR B 164 ? 0.3532 0.3897 0.4046 -0.0284 0.0006  0.0004  164 TYR B OH  
5481 N N   . VAL B 165 ? 0.0996 0.1190 0.1565 -0.0175 0.0044  -0.0039 165 VAL B N   
5482 C CA  . VAL B 165 ? 0.0920 0.1086 0.1480 -0.0175 0.0051  -0.0044 165 VAL B CA  
5483 C C   . VAL B 165 ? 0.0901 0.1035 0.1448 -0.0168 0.0058  -0.0062 165 VAL B C   
5484 O O   . VAL B 165 ? 0.1007 0.1130 0.1538 -0.0177 0.0060  -0.0066 165 VAL B O   
5485 C CB  . VAL B 165 ? 0.0838 0.0989 0.1415 -0.0160 0.0057  -0.0042 165 VAL B CB  
5486 C CG1 . VAL B 165 ? 0.0341 0.0460 0.0908 -0.0157 0.0065  -0.0051 165 VAL B CG1 
5487 C CG2 . VAL B 165 ? 0.0750 0.0934 0.1339 -0.0167 0.0051  -0.0025 165 VAL B CG2 
5488 N N   . LEU B 166 ? 0.0951 0.1074 0.1508 -0.0150 0.0063  -0.0072 166 LEU B N   
5489 C CA  . LEU B 166 ? 0.0406 0.0505 0.0953 -0.0141 0.0072  -0.0089 166 LEU B CA  
5490 C C   . LEU B 166 ? 0.1337 0.1445 0.1865 -0.0157 0.0068  -0.0091 166 LEU B C   
5491 O O   . LEU B 166 ? 0.0981 0.1072 0.1496 -0.0157 0.0075  -0.0101 166 LEU B O   
5492 C CB  . LEU B 166 ? 0.0470 0.0562 0.1031 -0.0123 0.0076  -0.0097 166 LEU B CB  
5493 C CG  . LEU B 166 ? 0.1361 0.1431 0.1937 -0.0103 0.0085  -0.0103 166 LEU B CG  
5494 C CD1 . LEU B 166 ? 0.2470 0.2538 0.3059 -0.0088 0.0086  -0.0108 166 LEU B CD1 
5495 C CD2 . LEU B 166 ? 0.1793 0.1842 0.2364 -0.0094 0.0097  -0.0116 166 LEU B CD2 
5496 N N   . ASN B 167 ? 0.0776 0.0911 0.1304 -0.0170 0.0058  -0.0081 167 ASN B N   
5497 C CA  . ASN B 167 ? 0.0853 0.0998 0.1363 -0.0185 0.0054  -0.0081 167 ASN B CA  
5498 C C   . ASN B 167 ? 0.1182 0.1326 0.1677 -0.0201 0.0051  -0.0076 167 ASN B C   
5499 O O   . ASN B 167 ? 0.1372 0.1503 0.1851 -0.0207 0.0054  -0.0084 167 ASN B O   
5500 C CB  . ASN B 167 ? 0.1761 0.1939 0.2274 -0.0195 0.0043  -0.0070 167 ASN B CB  
5501 C CG  . ASN B 167 ? 0.4256 0.4431 0.4775 -0.0183 0.0045  -0.0078 167 ASN B CG  
5502 O OD1 . ASN B 167 ? 0.4811 0.4961 0.5329 -0.0169 0.0054  -0.0093 167 ASN B OD1 
5503 N ND2 . ASN B 167 ? 0.4255 0.4460 0.4783 -0.0187 0.0037  -0.0068 167 ASN B ND2 
5504 N N   . LYS B 168 ? 0.1012 0.1167 0.1511 -0.0210 0.0046  -0.0063 168 LYS B N   
5505 C CA  . LYS B 168 ? 0.0940 0.1091 0.1424 -0.0225 0.0044  -0.0058 168 LYS B CA  
5506 C C   . LYS B 168 ? 0.1282 0.1399 0.1759 -0.0215 0.0056  -0.0073 168 LYS B C   
5507 O O   . LYS B 168 ? 0.0966 0.1073 0.1426 -0.0224 0.0057  -0.0076 168 LYS B O   
5508 C CB  . LYS B 168 ? 0.1312 0.1482 0.1804 -0.0233 0.0039  -0.0043 168 LYS B CB  
5509 C CG  . LYS B 168 ? 0.1707 0.1920 0.2205 -0.0247 0.0028  -0.0028 168 LYS B CG  
5510 C CD  . LYS B 168 ? 0.2499 0.2729 0.2981 -0.0267 0.0019  -0.0022 168 LYS B CD  
5511 C CE  . LYS B 168 ? 0.4777 0.5004 0.5245 -0.0284 0.0015  -0.0015 168 LYS B CE  
5512 N NZ  . LYS B 168 ? 0.5475 0.5712 0.5932 -0.0300 0.0005  -0.0007 168 LYS B NZ  
5513 N N   . TYR B 169 ? 0.0798 0.0897 0.1288 -0.0195 0.0065  -0.0081 169 TYR B N   
5514 C CA  . TYR B 169 ? 0.0694 0.0764 0.1180 -0.0183 0.0077  -0.0094 169 TYR B CA  
5515 C C   . TYR B 169 ? 0.0903 0.0965 0.1377 -0.0181 0.0083  -0.0108 169 TYR B C   
5516 O O   . TYR B 169 ? 0.0935 0.0983 0.1395 -0.0184 0.0089  -0.0115 169 TYR B O   
5517 C CB  . TYR B 169 ? 0.0658 0.0715 0.1162 -0.0161 0.0086  -0.0101 169 TYR B CB  
5518 C CG  . TYR B 169 ? 0.0365 0.0419 0.0878 -0.0159 0.0085  -0.0091 169 TYR B CG  
5519 C CD1 . TYR B 169 ? 0.0976 0.1048 0.1485 -0.0178 0.0075  -0.0076 169 TYR B CD1 
5520 C CD2 . TYR B 169 ? 0.0670 0.0708 0.1198 -0.0140 0.0094  -0.0098 169 TYR B CD2 
5521 C CE1 . TYR B 169 ? 0.0825 0.0895 0.1343 -0.0176 0.0075  -0.0067 169 TYR B CE1 
5522 C CE2 . TYR B 169 ? 0.0728 0.0763 0.1265 -0.0138 0.0094  -0.0089 169 TYR B CE2 
5523 C CZ  . TYR B 169 ? 0.1243 0.1294 0.1776 -0.0156 0.0084  -0.0073 169 TYR B CZ  
5524 O OH  . TYR B 169 ? 0.1032 0.1080 0.1574 -0.0154 0.0085  -0.0064 169 TYR B OH  
5525 N N   . PHE B 170 ? 0.0991 0.1060 0.1469 -0.0175 0.0083  -0.0113 170 PHE B N   
5526 C CA  . PHE B 170 ? 0.1066 0.1128 0.1534 -0.0172 0.0090  -0.0126 170 PHE B CA  
5527 C C   . PHE B 170 ? 0.1162 0.1231 0.1611 -0.0193 0.0084  -0.0121 170 PHE B C   
5528 O O   . PHE B 170 ? 0.1025 0.1084 0.1462 -0.0193 0.0091  -0.0132 170 PHE B O   
5529 C CB  . PHE B 170 ? 0.0784 0.0851 0.1261 -0.0161 0.0091  -0.0132 170 PHE B CB  
5530 C CG  . PHE B 170 ? 0.1973 0.2025 0.2465 -0.0137 0.0103  -0.0144 170 PHE B CG  
5531 C CD1 . PHE B 170 ? 0.1732 0.1772 0.2221 -0.0126 0.0116  -0.0158 170 PHE B CD1 
5532 C CD2 . PHE B 170 ? 0.1885 0.1937 0.2395 -0.0126 0.0102  -0.0139 170 PHE B CD2 
5533 C CE1 . PHE B 170 ? 0.1856 0.1888 0.2361 -0.0105 0.0128  -0.0168 170 PHE B CE1 
5534 C CE2 . PHE B 170 ? 0.1606 0.1645 0.2131 -0.0104 0.0113  -0.0149 170 PHE B CE2 
5535 C CZ  . PHE B 170 ? 0.2554 0.2584 0.3076 -0.0094 0.0125  -0.0164 170 PHE B CZ  
5536 N N   . GLU B 171 ? 0.1036 0.1126 0.1483 -0.0210 0.0070  -0.0106 171 GLU B N   
5537 C CA  . GLU B 171 ? 0.1102 0.1199 0.1533 -0.0230 0.0064  -0.0100 171 GLU B CA  
5538 C C   . GLU B 171 ? 0.1903 0.1982 0.2322 -0.0233 0.0069  -0.0104 171 GLU B C   
5539 O O   . GLU B 171 ? 0.0999 0.1071 0.1404 -0.0240 0.0072  -0.0109 171 GLU B O   
5540 C CB  . GLU B 171 ? 0.2464 0.2589 0.2898 -0.0247 0.0048  -0.0080 171 GLU B CB  
5541 C CG  . GLU B 171 ? 0.3634 0.3782 0.4078 -0.0246 0.0042  -0.0075 171 GLU B CG  
5542 C CD  . GLU B 171 ? 0.4622 0.4803 0.5071 -0.0264 0.0027  -0.0055 171 GLU B CD  
5543 O OE1 . GLU B 171 ? 0.3860 0.4047 0.4307 -0.0275 0.0021  -0.0043 171 GLU B OE1 
5544 O OE2 . GLU B 171 ? 0.4689 0.4892 0.5144 -0.0265 0.0021  -0.0049 171 GLU B OE2 
5545 N N   . ILE B 172 ? 0.1086 0.1155 0.1512 -0.0228 0.0071  -0.0101 172 ILE B N   
5546 C CA  . ILE B 172 ? 0.0711 0.0763 0.1127 -0.0230 0.0077  -0.0104 172 ILE B CA  
5547 C C   . ILE B 172 ? 0.0685 0.0718 0.1094 -0.0217 0.0092  -0.0122 172 ILE B C   
5548 O O   . ILE B 172 ? 0.0976 0.0999 0.1371 -0.0224 0.0096  -0.0127 172 ILE B O   
5549 C CB  . ILE B 172 ? 0.1135 0.1182 0.1561 -0.0225 0.0077  -0.0097 172 ILE B CB  
5550 C CG1 . ILE B 172 ? 0.1005 0.1073 0.1433 -0.0242 0.0063  -0.0077 172 ILE B CG1 
5551 C CG2 . ILE B 172 ? 0.1487 0.1511 0.1904 -0.0222 0.0086  -0.0104 172 ILE B CG2 
5552 C CD1 . ILE B 172 ? 0.1871 0.1942 0.2284 -0.0263 0.0055  -0.0069 172 ILE B CD1 
5553 N N   . ILE B 173 ? 0.0762 0.0792 0.1185 -0.0198 0.0101  -0.0132 173 ILE B N   
5554 C CA  . ILE B 173 ? 0.0887 0.0903 0.1306 -0.0185 0.0116  -0.0149 173 ILE B CA  
5555 C C   . ILE B 173 ? 0.1527 0.1547 0.1932 -0.0194 0.0117  -0.0154 173 ILE B C   
5556 O O   . ILE B 173 ? 0.1146 0.1157 0.1540 -0.0195 0.0126  -0.0163 173 ILE B O   
5557 C CB  . ILE B 173 ? 0.0835 0.0851 0.1274 -0.0163 0.0124  -0.0157 173 ILE B CB  
5558 C CG1 . ILE B 173 ? 0.1117 0.1127 0.1570 -0.0154 0.0125  -0.0152 173 ILE B CG1 
5559 C CG2 . ILE B 173 ? 0.1255 0.1264 0.1693 -0.0151 0.0139  -0.0172 173 ILE B CG2 
5560 C CD1 . ILE B 173 ? 0.1663 0.1673 0.2138 -0.0132 0.0132  -0.0159 173 ILE B CD1 
5561 N N   . LYS B 174 ? 0.0758 0.0794 0.1164 -0.0202 0.0107  -0.0149 174 LYS B N   
5562 C CA  . LYS B 174 ? 0.0655 0.0695 0.1047 -0.0210 0.0108  -0.0154 174 LYS B CA  
5563 C C   . LYS B 174 ? 0.1181 0.1219 0.1556 -0.0228 0.0104  -0.0149 174 LYS B C   
5564 O O   . LYS B 174 ? 0.1386 0.1422 0.1748 -0.0232 0.0110  -0.0157 174 LYS B O   
5565 C CB  . LYS B 174 ? 0.1772 0.1830 0.2169 -0.0215 0.0097  -0.0147 174 LYS B CB  
5566 C CG  . LYS B 174 ? 0.1991 0.2050 0.2403 -0.0197 0.0102  -0.0153 174 LYS B CG  
5567 C CD  . LYS B 174 ? 0.3168 0.3246 0.3584 -0.0204 0.0091  -0.0145 174 LYS B CD  
5568 C CE  . LYS B 174 ? 0.4624 0.4701 0.5054 -0.0186 0.0096  -0.0153 174 LYS B CE  
5569 N NZ  . LYS B 174 ? 0.5141 0.5237 0.5577 -0.0192 0.0084  -0.0142 174 LYS B NZ  
5570 N N   . LYS B 175 ? 0.0634 0.0672 0.1008 -0.0238 0.0096  -0.0137 175 LYS B N   
5571 C CA  . LYS B 175 ? 0.1222 0.1258 0.1580 -0.0255 0.0092  -0.0133 175 LYS B CA  
5572 C C   . LYS B 175 ? 0.2188 0.2205 0.2538 -0.0251 0.0103  -0.0142 175 LYS B C   
5573 O O   . LYS B 175 ? 0.1139 0.1151 0.1475 -0.0263 0.0102  -0.0139 175 LYS B O   
5574 C CB  . LYS B 175 ? 0.1781 0.1830 0.2143 -0.0270 0.0076  -0.0114 175 LYS B CB  
5575 C CG  . LYS B 175 ? 0.3004 0.3077 0.3374 -0.0279 0.0063  -0.0102 175 LYS B CG  
5576 C CD  . LYS B 175 ? 0.3176 0.3263 0.3552 -0.0294 0.0048  -0.0083 175 LYS B CD  
5577 C CE  . LYS B 175 ? 0.4923 0.5039 0.5313 -0.0299 0.0035  -0.0068 175 LYS B CE  
5578 N NZ  . LYS B 175 ? 0.6051 0.6177 0.6437 -0.0305 0.0033  -0.0071 175 LYS B NZ  
5579 N N   . THR B 176 ? 0.1493 0.1499 0.1851 -0.0233 0.0115  -0.0151 176 THR B N   
5580 C CA  . THR B 176 ? 0.1255 0.1245 0.1609 -0.0228 0.0124  -0.0156 176 THR B CA  
5581 C C   . THR B 176 ? 0.1918 0.1900 0.2256 -0.0231 0.0135  -0.0167 176 THR B C   
5582 O O   . THR B 176 ? 0.1633 0.1607 0.1958 -0.0241 0.0135  -0.0165 176 THR B O   
5583 C CB  . THR B 176 ? 0.1265 0.1250 0.1636 -0.0208 0.0134  -0.0162 176 THR B CB  
5584 O OG1 . THR B 176 ? 0.1130 0.1120 0.1513 -0.0207 0.0124  -0.0151 176 THR B OG1 
5585 C CG2 . THR B 176 ? 0.1260 0.1230 0.1626 -0.0202 0.0145  -0.0168 176 THR B CG2 
5586 N N   . LEU B 177 ? 0.1717 0.1702 0.2057 -0.0221 0.0146  -0.0179 177 LEU B N   
5587 C CA  . LEU B 177 ? 0.1490 0.1468 0.1815 -0.0224 0.0157  -0.0189 177 LEU B CA  
5588 C C   . LEU B 177 ? 0.1428 0.1408 0.1735 -0.0244 0.0149  -0.0184 177 LEU B C   
5589 O O   . LEU B 177 ? 0.1918 0.1890 0.2211 -0.0251 0.0156  -0.0188 177 LEU B O   
5590 C CB  . LEU B 177 ? 0.1461 0.1444 0.1792 -0.0211 0.0169  -0.0202 177 LEU B CB  
5591 C CG  . LEU B 177 ? 0.1547 0.1529 0.1897 -0.0191 0.0180  -0.0208 177 LEU B CG  
5592 C CD1 . LEU B 177 ? 0.1989 0.1977 0.2344 -0.0179 0.0192  -0.0220 177 LEU B CD1 
5593 C CD2 . LEU B 177 ? 0.1868 0.1839 0.2217 -0.0187 0.0189  -0.0210 177 LEU B CD2 
5594 N N   . SER B 178 ? 0.1279 0.1272 0.1588 -0.0254 0.0135  -0.0174 178 SER B N   
5595 C CA  . SER B 178 ? 0.1611 0.1609 0.1905 -0.0273 0.0126  -0.0168 178 SER B CA  
5596 C C   . SER B 178 ? 0.1340 0.1330 0.1627 -0.0284 0.0121  -0.0160 178 SER B C   
5597 O O   . SER B 178 ? 0.1339 0.1327 0.1611 -0.0297 0.0122  -0.0161 178 SER B O   
5598 C CB  . SER B 178 ? 0.1952 0.1968 0.2254 -0.0281 0.0112  -0.0157 178 SER B CB  
5599 O OG  . SER B 178 ? 0.2786 0.2809 0.3089 -0.0276 0.0116  -0.0165 178 SER B OG  
5600 N N   . ILE B 179 ? 0.1513 0.1501 0.1811 -0.0280 0.0116  -0.0152 179 ILE B N   
5601 C CA  . ILE B 179 ? 0.1021 0.1002 0.1312 -0.0291 0.0110  -0.0143 179 ILE B CA  
5602 C C   . ILE B 179 ? 0.2017 0.1980 0.2294 -0.0288 0.0124  -0.0155 179 ILE B C   
5603 O O   . ILE B 179 ? 0.1511 0.1468 0.1775 -0.0300 0.0122  -0.0152 179 ILE B O   
5604 C CB  . ILE B 179 ? 0.1791 0.1775 0.2097 -0.0290 0.0100  -0.0130 179 ILE B CB  
5605 C CG1 . ILE B 179 ? 0.2291 0.2272 0.2591 -0.0305 0.0091  -0.0119 179 ILE B CG1 
5606 C CG2 . ILE B 179 ? 0.1376 0.1347 0.1690 -0.0272 0.0110  -0.0137 179 ILE B CG2 
5607 C CD1 . ILE B 179 ? 0.1946 0.1938 0.2261 -0.0309 0.0076  -0.0101 179 ILE B CD1 
5608 N N   . TYR B 180 ? 0.1287 0.1244 0.1569 -0.0271 0.0139  -0.0167 180 TYR B N   
5609 C CA  . TYR B 180 ? 0.1740 0.1683 0.2011 -0.0268 0.0153  -0.0178 180 TYR B CA  
5610 C C   . TYR B 180 ? 0.1648 0.1592 0.1901 -0.0279 0.0158  -0.0185 180 TYR B C   
5611 O O   . TYR B 180 ? 0.1805 0.1739 0.2043 -0.0286 0.0163  -0.0187 180 TYR B O   
5612 C CB  . TYR B 180 ? 0.1759 0.1700 0.2042 -0.0248 0.0168  -0.0189 180 TYR B CB  
5613 C CG  . TYR B 180 ? 0.1310 0.1246 0.1607 -0.0238 0.0166  -0.0184 180 TYR B CG  
5614 C CD1 . TYR B 180 ? 0.1731 0.1654 0.2021 -0.0240 0.0169  -0.0182 180 TYR B CD1 
5615 C CD2 . TYR B 180 ? 0.1350 0.1293 0.1665 -0.0227 0.0162  -0.0181 180 TYR B CD2 
5616 C CE1 . TYR B 180 ? 0.1679 0.1597 0.1982 -0.0231 0.0168  -0.0177 180 TYR B CE1 
5617 C CE2 . TYR B 180 ? 0.0838 0.0777 0.1165 -0.0218 0.0161  -0.0176 180 TYR B CE2 
5618 C CZ  . TYR B 180 ? 0.1104 0.1030 0.1425 -0.0220 0.0164  -0.0175 180 TYR B CZ  
5619 O OH  . TYR B 180 ? 0.0540 0.0463 0.0875 -0.0211 0.0164  -0.0170 180 TYR B OH  
5620 N N   . ARG B 181 ? 0.1197 0.1152 0.1451 -0.0280 0.0157  -0.0187 181 ARG B N   
5621 C CA  . ARG B 181 ? 0.1568 0.1524 0.1804 -0.0290 0.0162  -0.0193 181 ARG B CA  
5622 C C   . ARG B 181 ? 0.1634 0.1591 0.1859 -0.0310 0.0150  -0.0184 181 ARG B C   
5623 O O   . ARG B 181 ? 0.1623 0.1574 0.1829 -0.0319 0.0156  -0.0188 181 ARG B O   
5624 C CB  . ARG B 181 ? 0.1530 0.1498 0.1770 -0.0288 0.0163  -0.0198 181 ARG B CB  
5625 C CG  . ARG B 181 ? 0.1723 0.1690 0.1973 -0.0270 0.0177  -0.0210 181 ARG B CG  
5626 C CD  . ARG B 181 ? 0.2021 0.1998 0.2272 -0.0268 0.0179  -0.0215 181 ARG B CD  
5627 N NE  . ARG B 181 ? 0.2692 0.2680 0.2957 -0.0265 0.0167  -0.0207 181 ARG B NE  
5628 C CZ  . ARG B 181 ? 0.2953 0.2945 0.3235 -0.0250 0.0170  -0.0210 181 ARG B CZ  
5629 N NH1 . ARG B 181 ? 0.2925 0.2912 0.3213 -0.0235 0.0185  -0.0221 181 ARG B NH1 
5630 N NH2 . ARG B 181 ? 0.3635 0.3636 0.3928 -0.0249 0.0158  -0.0202 181 ARG B NH2 
5631 N N   . GLU B 182 ? 0.1674 0.1640 0.1909 -0.0315 0.0134  -0.0170 182 GLU B N   
5632 C CA  . GLU B 182 ? 0.1260 0.1231 0.1487 -0.0333 0.0123  -0.0159 182 GLU B CA  
5633 C C   . GLU B 182 ? 0.2224 0.2181 0.2441 -0.0339 0.0124  -0.0158 182 GLU B C   
5634 O O   . GLU B 182 ? 0.2131 0.2086 0.2332 -0.0352 0.0125  -0.0159 182 GLU B O   
5635 C CB  . GLU B 182 ? 0.2498 0.2486 0.2743 -0.0337 0.0105  -0.0144 182 GLU B CB  
5636 C CG  . GLU B 182 ? 0.4059 0.4056 0.4299 -0.0356 0.0094  -0.0134 182 GLU B CG  
5637 C CD  . GLU B 182 ? 0.4828 0.4845 0.5088 -0.0360 0.0078  -0.0118 182 GLU B CD  
5638 O OE1 . GLU B 182 ? 0.4050 0.4070 0.4327 -0.0349 0.0074  -0.0112 182 GLU B OE1 
5639 O OE2 . GLU B 182 ? 0.5009 0.5039 0.5268 -0.0374 0.0070  -0.0110 182 GLU B OE2 
5640 N N   . ILE B 183 ? 0.1374 0.1322 0.1601 -0.0329 0.0125  -0.0155 183 ILE B N   
5641 C CA  . ILE B 183 ? 0.1351 0.1285 0.1568 -0.0334 0.0126  -0.0153 183 ILE B CA  
5642 C C   . ILE B 183 ? 0.1310 0.1231 0.1509 -0.0333 0.0143  -0.0167 183 ILE B C   
5643 O O   . ILE B 183 ? 0.2072 0.1985 0.2257 -0.0343 0.0144  -0.0167 183 ILE B O   
5644 C CB  . ILE B 183 ? 0.1476 0.1403 0.1708 -0.0324 0.0124  -0.0147 183 ILE B CB  
5645 C CG1 . ILE B 183 ? 0.2496 0.2417 0.2735 -0.0305 0.0137  -0.0159 183 ILE B CG1 
5646 C CG2 . ILE B 183 ? 0.2281 0.2222 0.2530 -0.0327 0.0107  -0.0132 183 ILE B CG2 
5647 C CD1 . ILE B 183 ? 0.2649 0.2553 0.2879 -0.0298 0.0151  -0.0167 183 ILE B CD1 
5648 N N   . LYS B 184 ? 0.2043 0.1964 0.2244 -0.0321 0.0155  -0.0180 184 LYS B N   
5649 C CA  . LYS B 184 ? 0.1881 0.1793 0.2066 -0.0320 0.0172  -0.0193 184 LYS B CA  
5650 C C   . LYS B 184 ? 0.2860 0.2776 0.3026 -0.0336 0.0171  -0.0195 184 LYS B C   
5651 O O   . LYS B 184 ? 0.2419 0.2325 0.2568 -0.0344 0.0177  -0.0198 184 LYS B O   
5652 C CB  . LYS B 184 ? 0.1905 0.1821 0.2101 -0.0303 0.0185  -0.0204 184 LYS B CB  
5653 C CG  . LYS B 184 ? 0.2220 0.2129 0.2405 -0.0299 0.0203  -0.0217 184 LYS B CG  
5654 C CD  . LYS B 184 ? 0.2196 0.2112 0.2395 -0.0283 0.0214  -0.0226 184 LYS B CD  
5655 C CE  . LYS B 184 ? 0.1936 0.1848 0.2128 -0.0279 0.0233  -0.0238 184 LYS B CE  
5656 N NZ  . LYS B 184 ? 0.3686 0.3593 0.3855 -0.0294 0.0235  -0.0240 184 LYS B NZ  
5657 N N   . GLU B 185 ? 0.2000 0.1930 0.2170 -0.0340 0.0165  -0.0192 185 GLU B N   
5658 C CA  . GLU B 185 ? 0.2515 0.2450 0.2668 -0.0355 0.0164  -0.0194 185 GLU B CA  
5659 C C   . GLU B 185 ? 0.2251 0.2185 0.2393 -0.0372 0.0155  -0.0185 185 GLU B C   
5660 O O   . GLU B 185 ? 0.2442 0.2374 0.2564 -0.0384 0.0159  -0.0189 185 GLU B O   
5661 C CB  . GLU B 185 ? 0.2556 0.2508 0.2717 -0.0356 0.0158  -0.0192 185 GLU B CB  
5662 C CG  . GLU B 185 ? 0.3398 0.3355 0.3541 -0.0367 0.0162  -0.0198 185 GLU B CG  
5663 C CD  . GLU B 185 ? 0.3669 0.3642 0.3823 -0.0365 0.0156  -0.0196 185 GLU B CD  
5664 O OE1 . GLU B 185 ? 0.4099 0.4073 0.4268 -0.0350 0.0158  -0.0198 185 GLU B OE1 
5665 O OE2 . GLU B 185 ? 0.4101 0.4085 0.4247 -0.0378 0.0149  -0.0192 185 GLU B OE2 
5666 N N   . GLU B 186 ? 0.1577 0.1515 0.1733 -0.0373 0.0141  -0.0172 186 GLU B N   
5667 C CA  . GLU B 186 ? 0.2238 0.2178 0.2388 -0.0388 0.0131  -0.0162 186 GLU B CA  
5668 C C   . GLU B 186 ? 0.2796 0.2717 0.2934 -0.0389 0.0137  -0.0164 186 GLU B C   
5669 O O   . GLU B 186 ? 0.2388 0.2309 0.2520 -0.0401 0.0130  -0.0157 186 GLU B O   
5670 C CB  . GLU B 186 ? 0.1986 0.1938 0.2158 -0.0388 0.0114  -0.0146 186 GLU B CB  
5671 C CG  . GLU B 186 ? 0.1645 0.1617 0.1828 -0.0390 0.0106  -0.0142 186 GLU B CG  
5672 C CD  . GLU B 186 ? 0.2673 0.2660 0.2880 -0.0391 0.0090  -0.0126 186 GLU B CD  
5673 O OE1 . GLU B 186 ? 0.3147 0.3127 0.3366 -0.0384 0.0087  -0.0119 186 GLU B OE1 
5674 O OE2 . GLU B 186 ? 0.3052 0.3059 0.3266 -0.0398 0.0082  -0.0119 186 GLU B OE2 
5675 N N   . GLY B 187 ? 0.2569 0.2478 0.2706 -0.0376 0.0150  -0.0174 187 GLY B N   
5676 C CA  . GLY B 187 ? 0.1936 0.1828 0.2062 -0.0377 0.0157  -0.0177 187 GLY B CA  
5677 C C   . GLY B 187 ? 0.2318 0.2204 0.2457 -0.0374 0.0147  -0.0166 187 GLY B C   
5678 O O   . GLY B 187 ? 0.2027 0.1900 0.2156 -0.0378 0.0150  -0.0165 187 GLY B O   
5679 N N   . LYS B 188 ? 0.1121 0.1017 0.1281 -0.0367 0.0137  -0.0157 188 LYS B N   
5680 C CA  . LYS B 188 ? 0.1279 0.1170 0.1452 -0.0364 0.0129  -0.0147 188 LYS B CA  
5681 C C   . LYS B 188 ? 0.1631 0.1509 0.1810 -0.0347 0.0140  -0.0154 188 LYS B C   
5682 O O   . LYS B 188 ? 0.1661 0.1531 0.1846 -0.0344 0.0136  -0.0147 188 LYS B O   
5683 C CB  . LYS B 188 ? 0.1971 0.1879 0.2166 -0.0364 0.0113  -0.0133 188 LYS B CB  
5684 C CG  . LYS B 188 ? 0.2308 0.2232 0.2502 -0.0381 0.0102  -0.0124 188 LYS B CG  
5685 C CD  . LYS B 188 ? 0.2811 0.2755 0.3027 -0.0380 0.0090  -0.0113 188 LYS B CD  
5686 C CE  . LYS B 188 ? 0.2837 0.2799 0.3057 -0.0396 0.0078  -0.0102 188 LYS B CE  
5687 N NZ  . LYS B 188 ? 0.4468 0.4433 0.4704 -0.0399 0.0068  -0.0087 188 LYS B NZ  
5688 N N   . GLY B 189 ? 0.1703 0.1580 0.1879 -0.0336 0.0154  -0.0167 189 GLY B N   
5689 C CA  . GLY B 189 ? 0.2239 0.2106 0.2421 -0.0320 0.0165  -0.0174 189 GLY B CA  
5690 C C   . GLY B 189 ? 0.2365 0.2235 0.2545 -0.0311 0.0182  -0.0189 189 GLY B C   
5691 O O   . GLY B 189 ? 0.1988 0.1868 0.2166 -0.0314 0.0182  -0.0192 189 GLY B O   
5692 N N   . SER B 190 ? 0.1276 0.1137 0.1455 -0.0300 0.0196  -0.0197 190 SER B N   
5693 C CA  . SER B 190 ? 0.1297 0.1162 0.1479 -0.0289 0.0212  -0.0210 190 SER B CA  
5694 C C   . SER B 190 ? 0.1438 0.1311 0.1644 -0.0272 0.0214  -0.0210 190 SER B C   
5695 O O   . SER B 190 ? 0.1462 0.1332 0.1678 -0.0266 0.0207  -0.0203 190 SER B O   
5696 C CB  . SER B 190 ? 0.1252 0.1107 0.1423 -0.0286 0.0228  -0.0218 190 SER B CB  
5697 O OG  . SER B 190 ? 0.1641 0.1488 0.1791 -0.0302 0.0227  -0.0218 190 SER B OG  
5698 N N   . VAL B 191 ? 0.1486 0.1368 0.1698 -0.0263 0.0223  -0.0219 191 VAL B N   
5699 C CA  . VAL B 191 ? 0.1700 0.1591 0.1935 -0.0246 0.0227  -0.0221 191 VAL B CA  
5700 C C   . VAL B 191 ? 0.1938 0.1830 0.2177 -0.0234 0.0247  -0.0233 191 VAL B C   
5701 O O   . VAL B 191 ? 0.1874 0.1769 0.2103 -0.0238 0.0255  -0.0240 191 VAL B O   
5702 C CB  . VAL B 191 ? 0.1367 0.1270 0.1610 -0.0244 0.0219  -0.0219 191 VAL B CB  
5703 C CG1 . VAL B 191 ? 0.0550 0.0461 0.0818 -0.0226 0.0223  -0.0220 191 VAL B CG1 
5704 C CG2 . VAL B 191 ? 0.1120 0.1023 0.1358 -0.0258 0.0200  -0.0207 191 VAL B CG2 
5705 N N   . SER B 192 ? 0.1599 0.1492 0.1853 -0.0221 0.0253  -0.0233 192 SER B N   
5706 C CA  . SER B 192 ? 0.1255 0.1153 0.1518 -0.0209 0.0271  -0.0243 192 SER B CA  
5707 C C   . SER B 192 ? 0.1294 0.1206 0.1581 -0.0193 0.0275  -0.0245 192 SER B C   
5708 O O   . SER B 192 ? 0.1009 0.0925 0.1305 -0.0191 0.0263  -0.0239 192 SER B O   
5709 C CB  . SER B 192 ? 0.0560 0.0449 0.0822 -0.0206 0.0278  -0.0242 192 SER B CB  
5710 O OG  . SER B 192 ? 0.1366 0.1255 0.1643 -0.0198 0.0272  -0.0236 192 SER B OG  
5711 N N   . THR B 193 ? 0.1130 0.1051 0.1429 -0.0182 0.0290  -0.0253 193 THR B N   
5712 C CA  . THR B 193 ? 0.1238 0.1173 0.1563 -0.0166 0.0295  -0.0254 193 THR B CA  
5713 C C   . THR B 193 ? 0.1076 0.1015 0.1412 -0.0156 0.0310  -0.0258 193 THR B C   
5714 O O   . THR B 193 ? 0.0780 0.0711 0.1105 -0.0162 0.0316  -0.0259 193 THR B O   
5715 C CB  . THR B 193 ? 0.1237 0.1184 0.1568 -0.0162 0.0298  -0.0260 193 THR B CB  
5716 O OG1 . THR B 193 ? 0.1454 0.1413 0.1809 -0.0147 0.0298  -0.0259 193 THR B OG1 
5717 C CG2 . THR B 193 ? 0.1125 0.1076 0.1451 -0.0162 0.0312  -0.0267 193 THR B CG2 
5718 N N   . SER B 194 ? 0.1158 0.1106 0.1509 -0.0143 0.0302  -0.0251 194 SER B N   
5719 C CA  . SER B 194 ? 0.1302 0.1251 0.1655 -0.0134 0.0298  -0.0243 194 SER B CA  
5720 C C   . SER B 194 ? 0.1412 0.1369 0.1763 -0.0127 0.0290  -0.0237 194 SER B C   
5721 O O   . SER B 194 ? 0.0836 0.0799 0.1190 -0.0125 0.0285  -0.0238 194 SER B O   
5722 C CB  . SER B 194 ? 0.1014 0.0964 0.1380 -0.0126 0.0292  -0.0236 194 SER B CB  
5723 O OG  . SER B 194 ? 0.1049 0.0991 0.1416 -0.0133 0.0301  -0.0240 194 SER B OG  
5724 N N   . PRO B 195 ? 0.0917 0.0678 0.1254 -0.0116 0.0061  -0.0064 195 PRO B N   
5725 C CA  . PRO B 195 ? 0.1499 0.1269 0.1860 -0.0109 0.0062  -0.0064 195 PRO B CA  
5726 C C   . PRO B 195 ? 0.1578 0.1355 0.1940 -0.0104 0.0054  -0.0058 195 PRO B C   
5727 O O   . PRO B 195 ? 0.1229 0.1010 0.1576 -0.0105 0.0047  -0.0053 195 PRO B O   
5728 C CB  . PRO B 195 ? 0.2121 0.1903 0.2490 -0.0107 0.0064  -0.0061 195 PRO B CB  
5729 C CG  . PRO B 195 ? 0.2735 0.2511 0.3089 -0.0113 0.0068  -0.0064 195 PRO B CG  
5730 C CD  . PRO B 195 ? 0.1340 0.1105 0.1672 -0.0119 0.0064  -0.0064 195 PRO B CD  
5731 N N   . TYR B 196 ? 0.0675 0.0454 0.1056 -0.0100 0.0055  -0.0059 196 TYR B N   
5732 C CA  . TYR B 196 ? 0.0978 0.0756 0.1357 -0.0098 0.0048  -0.0057 196 TYR B CA  
5733 C C   . TYR B 196 ? 0.1323 0.1112 0.1694 -0.0095 0.0039  -0.0049 196 TYR B C   
5734 O O   . TYR B 196 ? 0.1166 0.0950 0.1521 -0.0098 0.0034  -0.0047 196 TYR B O   
5735 C CB  . TYR B 196 ? 0.0848 0.0629 0.1250 -0.0092 0.0051  -0.0059 196 TYR B CB  
5736 C CG  . TYR B 196 ? 0.0933 0.0706 0.1334 -0.0092 0.0047  -0.0059 196 TYR B CG  
5737 C CD1 . TYR B 196 ? 0.1034 0.0816 0.1432 -0.0089 0.0038  -0.0053 196 TYR B CD1 
5738 C CD2 . TYR B 196 ? 0.0910 0.0667 0.1311 -0.0095 0.0051  -0.0065 196 TYR B CD2 
5739 C CE1 . TYR B 196 ? 0.1413 0.1189 0.1810 -0.0089 0.0034  -0.0053 196 TYR B CE1 
5740 C CE2 . TYR B 196 ? 0.0833 0.0582 0.1232 -0.0094 0.0047  -0.0065 196 TYR B CE2 
5741 C CZ  . TYR B 196 ? 0.1314 0.1073 0.1711 -0.0091 0.0039  -0.0059 196 TYR B CZ  
5742 O OH  . TYR B 196 ? 0.1695 0.1447 0.2091 -0.0091 0.0035  -0.0060 196 TYR B OH  
5743 N N   . TYR B 197 ? 0.0970 0.0775 0.1353 -0.0090 0.0037  -0.0044 197 TYR B N   
5744 C CA  . TYR B 197 ? 0.1466 0.1282 0.1842 -0.0087 0.0027  -0.0037 197 TYR B CA  
5745 C C   . TYR B 197 ? 0.1204 0.1022 0.1563 -0.0091 0.0025  -0.0034 197 TYR B C   
5746 O O   . TYR B 197 ? 0.0752 0.0582 0.1110 -0.0087 0.0018  -0.0027 197 TYR B O   
5747 C CB  . TYR B 197 ? 0.1343 0.1175 0.1742 -0.0079 0.0024  -0.0033 197 TYR B CB  
5748 C CG  . TYR B 197 ? 0.1081 0.0911 0.1494 -0.0076 0.0025  -0.0036 197 TYR B CG  
5749 C CD1 . TYR B 197 ? 0.1114 0.0942 0.1520 -0.0076 0.0018  -0.0034 197 TYR B CD1 
5750 C CD2 . TYR B 197 ? 0.1350 0.1178 0.1782 -0.0075 0.0032  -0.0040 197 TYR B CD2 
5751 C CE1 . TYR B 197 ? 0.0978 0.0802 0.1395 -0.0074 0.0019  -0.0036 197 TYR B CE1 
5752 C CE2 . TYR B 197 ? 0.1520 0.1345 0.1964 -0.0073 0.0032  -0.0043 197 TYR B CE2 
5753 C CZ  . TYR B 197 ? 0.1563 0.1386 0.1999 -0.0073 0.0025  -0.0040 197 TYR B CZ  
5754 O OH  . TYR B 197 ? 0.1660 0.1478 0.2106 -0.0071 0.0025  -0.0043 197 TYR B OH  
5755 N N   . HIS B 198 ? 0.0841 0.0649 0.1187 -0.0097 0.0030  -0.0037 198 HIS B N   
5756 C CA  . HIS B 198 ? 0.1298 0.1106 0.1625 -0.0102 0.0028  -0.0034 198 HIS B CA  
5757 C C   . HIS B 198 ? 0.1454 0.1276 0.1792 -0.0098 0.0027  -0.0030 198 HIS B C   
5758 O O   . HIS B 198 ? 0.1047 0.0874 0.1374 -0.0098 0.0020  -0.0024 198 HIS B O   
5759 C CB  . HIS B 198 ? 0.1206 0.1013 0.1513 -0.0104 0.0020  -0.0030 198 HIS B CB  
5760 C CG  . HIS B 198 ? 0.0578 0.0380 0.0861 -0.0111 0.0018  -0.0028 198 HIS B CG  
5761 N ND1 . HIS B 198 ? 0.0848 0.0658 0.1122 -0.0111 0.0012  -0.0022 198 HIS B ND1 
5762 C CD2 . HIS B 198 ? 0.0768 0.0558 0.1033 -0.0119 0.0020  -0.0031 198 HIS B CD2 
5763 C CE1 . HIS B 198 ? 0.0941 0.0744 0.1193 -0.0119 0.0012  -0.0021 198 HIS B CE1 
5764 N NE2 . HIS B 198 ? 0.1127 0.0918 0.1373 -0.0123 0.0016  -0.0027 198 HIS B NE2 
5765 N N   . PRO B 199 ? 0.1553 0.1378 0.1910 -0.0095 0.0033  -0.0033 199 PRO B N   
5766 C CA  . PRO B 199 ? 0.1246 0.1082 0.1612 -0.0092 0.0032  -0.0029 199 PRO B CA  
5767 C C   . PRO B 199 ? 0.1405 0.1237 0.1757 -0.0098 0.0034  -0.0030 199 PRO B C   
5768 O O   . PRO B 199 ? 0.1632 0.1453 0.1970 -0.0105 0.0039  -0.0034 199 PRO B O   
5769 C CB  . PRO B 199 ? 0.1284 0.1125 0.1677 -0.0087 0.0039  -0.0033 199 PRO B CB  
5770 C CG  . PRO B 199 ? 0.0784 0.0611 0.1174 -0.0091 0.0047  -0.0041 199 PRO B CG  
5771 C CD  . PRO B 199 ? 0.0949 0.0768 0.1322 -0.0094 0.0042  -0.0040 199 PRO B CD  
5772 N N   . LEU B 200 ? 0.1891 0.1733 0.2247 -0.0096 0.0032  -0.0025 200 LEU B N   
5773 C CA  . LEU B 200 ? 0.1090 0.0930 0.1437 -0.0102 0.0035  -0.0026 200 LEU B CA  
5774 C C   . LEU B 200 ? 0.1283 0.1122 0.1650 -0.0100 0.0045  -0.0031 200 LEU B C   
5775 O O   . LEU B 200 ? 0.1109 0.0958 0.1492 -0.0095 0.0045  -0.0029 200 LEU B O   
5776 C CB  . LEU B 200 ? 0.1211 0.1059 0.1551 -0.0102 0.0028  -0.0018 200 LEU B CB  
5777 C CG  . LEU B 200 ? 0.1199 0.1047 0.1518 -0.0104 0.0018  -0.0013 200 LEU B CG  
5778 C CD1 . LEU B 200 ? 0.1580 0.1437 0.1896 -0.0102 0.0011  -0.0005 200 LEU B CD1 
5779 C CD2 . LEU B 200 ? 0.1918 0.1754 0.2211 -0.0114 0.0019  -0.0015 200 LEU B CD2 
5780 N N   . ILE B 201 ? 0.1641 0.1470 0.2007 -0.0104 0.0052  -0.0039 201 ILE B N   
5781 C CA  . ILE B 201 ? 0.0986 0.0814 0.1371 -0.0102 0.0063  -0.0045 201 ILE B CA  
5782 C C   . ILE B 201 ? 0.0782 0.0616 0.1171 -0.0103 0.0065  -0.0044 201 ILE B C   
5783 O O   . ILE B 201 ? 0.1056 0.0897 0.1467 -0.0098 0.0070  -0.0045 201 ILE B O   
5784 C CB  . ILE B 201 ? 0.0870 0.0684 0.1248 -0.0107 0.0070  -0.0053 201 ILE B CB  
5785 C CG1 . ILE B 201 ? 0.0921 0.0729 0.1298 -0.0106 0.0068  -0.0055 201 ILE B CG1 
5786 C CG2 . ILE B 201 ? 0.0546 0.0359 0.0941 -0.0107 0.0080  -0.0060 201 ILE B CG2 
5787 C CD1 . ILE B 201 ? 0.0925 0.0737 0.1326 -0.0099 0.0071  -0.0056 201 ILE B CD1 
5788 N N   . PRO B 202 ? 0.1362 0.1194 0.1732 -0.0109 0.0062  -0.0041 202 PRO B N   
5789 C CA  . PRO B 202 ? 0.1193 0.1030 0.1568 -0.0111 0.0064  -0.0039 202 PRO B CA  
5790 C C   . PRO B 202 ? 0.1616 0.1466 0.2005 -0.0104 0.0060  -0.0033 202 PRO B C   
5791 O O   . PRO B 202 ? 0.0915 0.0770 0.1319 -0.0102 0.0064  -0.0033 202 PRO B O   
5792 C CB  . PRO B 202 ? 0.1012 0.0845 0.1360 -0.0120 0.0060  -0.0036 202 PRO B CB  
5793 C CG  . PRO B 202 ? 0.1285 0.1109 0.1620 -0.0124 0.0060  -0.0040 202 PRO B CG  
5794 C CD  . PRO B 202 ? 0.1100 0.0925 0.1444 -0.0117 0.0058  -0.0040 202 PRO B CD  
5795 N N   . ILE B 203 ? 0.0786 0.0640 0.1171 -0.0101 0.0050  -0.0027 203 ILE B N   
5796 C CA  . ILE B 203 ? 0.0923 0.0789 0.1321 -0.0094 0.0045  -0.0021 203 ILE B CA  
5797 C C   . ILE B 203 ? 0.1250 0.1121 0.1677 -0.0085 0.0051  -0.0024 203 ILE B C   
5798 O O   . ILE B 203 ? 0.1063 0.0942 0.1507 -0.0081 0.0052  -0.0022 203 ILE B O   
5799 C CB  . ILE B 203 ? 0.1163 0.1033 0.1549 -0.0092 0.0034  -0.0014 203 ILE B CB  
5800 C CG1 . ILE B 203 ? 0.1509 0.1376 0.1869 -0.0101 0.0028  -0.0009 203 ILE B CG1 
5801 C CG2 . ILE B 203 ? 0.0913 0.0796 0.1318 -0.0083 0.0029  -0.0008 203 ILE B CG2 
5802 C CD1 . ILE B 203 ? 0.2434 0.2306 0.2782 -0.0099 0.0017  -0.0001 203 ILE B CD1 
5803 N N   . LEU B 204 ? 0.1145 0.1012 0.1577 -0.0084 0.0054  -0.0029 204 LEU B N   
5804 C CA  . LEU B 204 ? 0.0709 0.0580 0.1166 -0.0077 0.0059  -0.0033 204 LEU B CA  
5805 C C   . LEU B 204 ? 0.1805 0.1674 0.2276 -0.0077 0.0070  -0.0038 204 LEU B C   
5806 O O   . LEU B 204 ? 0.1406 0.1284 0.1901 -0.0071 0.0073  -0.0038 204 LEU B O   
5807 C CB  . LEU B 204 ? 0.0515 0.0378 0.0971 -0.0078 0.0061  -0.0037 204 LEU B CB  
5808 C CG  . LEU B 204 ? 0.1103 0.0968 0.1549 -0.0076 0.0052  -0.0033 204 LEU B CG  
5809 C CD1 . LEU B 204 ? 0.0888 0.0745 0.1338 -0.0076 0.0055  -0.0038 204 LEU B CD1 
5810 C CD2 . LEU B 204 ? 0.1922 0.1801 0.2380 -0.0069 0.0044  -0.0026 204 LEU B CD2 
5811 N N   . LEU B 205 ? 0.0723 0.0583 0.1182 -0.0084 0.0075  -0.0042 205 LEU B N   
5812 C CA  . LEU B 205 ? 0.0959 0.0818 0.1430 -0.0085 0.0086  -0.0048 205 LEU B CA  
5813 C C   . LEU B 205 ? 0.1508 0.1374 0.1983 -0.0084 0.0084  -0.0042 205 LEU B C   
5814 O O   . LEU B 205 ? 0.0984 0.0855 0.1479 -0.0080 0.0091  -0.0044 205 LEU B O   
5815 C CB  . LEU B 205 ? 0.0658 0.0504 0.1114 -0.0093 0.0092  -0.0054 205 LEU B CB  
5816 C CG  . LEU B 205 ? 0.1093 0.0929 0.1547 -0.0094 0.0095  -0.0060 205 LEU B CG  
5817 C CD1 . LEU B 205 ? 0.1270 0.1095 0.1707 -0.0102 0.0100  -0.0066 205 LEU B CD1 
5818 C CD2 . LEU B 205 ? 0.1985 0.1822 0.2463 -0.0089 0.0103  -0.0065 205 LEU B CD2 
5819 N N   . ASN B 206 ? 0.0901 0.0769 0.1358 -0.0087 0.0075  -0.0036 206 ASN B N   
5820 C CA  . ASN B 206 ? 0.1055 0.0929 0.1512 -0.0089 0.0073  -0.0031 206 ASN B CA  
5821 C C   . ASN B 206 ? 0.0729 0.0606 0.1167 -0.0092 0.0061  -0.0022 206 ASN B C   
5822 O O   . ASN B 206 ? 0.1387 0.1258 0.1801 -0.0100 0.0058  -0.0021 206 ASN B O   
5823 C CB  . ASN B 206 ? 0.1995 0.1862 0.2443 -0.0096 0.0081  -0.0036 206 ASN B CB  
5824 C CG  . ASN B 206 ? 0.1978 0.1850 0.2423 -0.0100 0.0078  -0.0030 206 ASN B CG  
5825 O OD1 . ASN B 206 ? 0.1915 0.1796 0.2370 -0.0095 0.0073  -0.0023 206 ASN B OD1 
5826 N ND2 . ASN B 206 ? 0.1726 0.1592 0.2153 -0.0110 0.0079  -0.0031 206 ASN B ND2 
5827 N N   . PRO B 207 ? 0.1217 0.1104 0.1665 -0.0085 0.0054  -0.0016 207 PRO B N   
5828 C CA  . PRO B 207 ? 0.0625 0.0514 0.1054 -0.0087 0.0042  -0.0007 207 PRO B CA  
5829 C C   . PRO B 207 ? 0.1642 0.1530 0.2054 -0.0096 0.0039  -0.0002 207 PRO B C   
5830 O O   . PRO B 207 ? 0.0982 0.0869 0.1372 -0.0101 0.0031  0.0003  207 PRO B O   
5831 C CB  . PRO B 207 ? 0.1144 0.1045 0.1593 -0.0077 0.0037  -0.0002 207 PRO B CB  
5832 C CG  . PRO B 207 ? 0.0885 0.0787 0.1357 -0.0070 0.0045  -0.0008 207 PRO B CG  
5833 C CD  . PRO B 207 ? 0.0986 0.0880 0.1460 -0.0075 0.0056  -0.0016 207 PRO B CD  
5834 N N   . ASN B 208 ? 0.1142 0.1031 0.1563 -0.0097 0.0045  -0.0004 208 ASN B N   
5835 C CA  . ASN B 208 ? 0.0952 0.0841 0.1357 -0.0107 0.0042  0.0001  208 ASN B CA  
5836 C C   . ASN B 208 ? 0.0856 0.0736 0.1236 -0.0118 0.0043  -0.0002 208 ASN B C   
5837 O O   . ASN B 208 ? 0.1333 0.1213 0.1696 -0.0127 0.0039  0.0003  208 ASN B O   
5838 C CB  . ASN B 208 ? 0.1602 0.1494 0.2025 -0.0106 0.0050  0.0000  208 ASN B CB  
5839 C CG  . ASN B 208 ? 0.1592 0.1493 0.2038 -0.0096 0.0048  0.0004  208 ASN B CG  
5840 O OD1 . ASN B 208 ? 0.1960 0.1866 0.2406 -0.0091 0.0039  0.0010  208 ASN B OD1 
5841 N ND2 . ASN B 208 ? 0.2717 0.2620 0.3183 -0.0093 0.0056  0.0001  208 ASN B ND2 
5842 N N   . CYS B 209 ? 0.1180 0.1053 0.1558 -0.0117 0.0048  -0.0009 209 CYS B N   
5843 C CA  . CYS B 209 ? 0.0872 0.0736 0.1227 -0.0128 0.0048  -0.0011 209 CYS B CA  
5844 C C   . CYS B 209 ? 0.1051 0.0916 0.1381 -0.0134 0.0038  -0.0004 209 CYS B C   
5845 O O   . CYS B 209 ? 0.0963 0.0823 0.1271 -0.0145 0.0036  -0.0004 209 CYS B O   
5846 C CB  . CYS B 209 ? 0.1676 0.1533 0.2035 -0.0126 0.0056  -0.0021 209 CYS B CB  
5847 S SG  . CYS B 209 ? 0.1762 0.1617 0.2114 -0.0121 0.0049  -0.0020 209 CYS B SG  
5848 N N   . VAL B 210 ? 0.0827 0.0698 0.1159 -0.0128 0.0030  0.0002  210 VAL B N   
5849 C CA  . VAL B 210 ? 0.0906 0.0778 0.1215 -0.0134 0.0020  0.0008  210 VAL B CA  
5850 C C   . VAL B 210 ? 0.0829 0.0704 0.1124 -0.0144 0.0018  0.0014  210 VAL B C   
5851 O O   . VAL B 210 ? 0.1459 0.1332 0.1730 -0.0153 0.0013  0.0017  210 VAL B O   
5852 C CB  . VAL B 210 ? 0.2008 0.1886 0.2324 -0.0125 0.0013  0.0013  210 VAL B CB  
5853 C CG1 . VAL B 210 ? 0.1653 0.1529 0.1982 -0.0116 0.0016  0.0008  210 VAL B CG1 
5854 C CG2 . VAL B 210 ? 0.1755 0.1643 0.2089 -0.0119 0.0011  0.0019  210 VAL B CG2 
5855 N N   . TYR B 211 ? 0.1437 0.1316 0.1746 -0.0144 0.0021  0.0015  211 TYR B N   
5856 C CA  . TYR B 211 ? 0.1410 0.1294 0.1707 -0.0154 0.0018  0.0020  211 TYR B CA  
5857 C C   . TYR B 211 ? 0.2395 0.2274 0.2676 -0.0167 0.0022  0.0017  211 TYR B C   
5858 O O   . TYR B 211 ? 0.2077 0.1961 0.2344 -0.0178 0.0020  0.0022  211 TYR B O   
5859 C CB  . TYR B 211 ? 0.0969 0.0860 0.1288 -0.0149 0.0020  0.0023  211 TYR B CB  
5860 C CG  . TYR B 211 ? 0.1397 0.1294 0.1731 -0.0137 0.0015  0.0028  211 TYR B CG  
5861 C CD1 . TYR B 211 ? 0.1526 0.1428 0.1849 -0.0137 0.0005  0.0035  211 TYR B CD1 
5862 C CD2 . TYR B 211 ? 0.1657 0.1556 0.2018 -0.0125 0.0019  0.0024  211 TYR B CD2 
5863 C CE1 . TYR B 211 ? 0.1882 0.1790 0.2219 -0.0126 -0.0001 0.0040  211 TYR B CE1 
5864 C CE2 . TYR B 211 ? 0.2311 0.2218 0.2688 -0.0114 0.0014  0.0029  211 TYR B CE2 
5865 C CZ  . TYR B 211 ? 0.3197 0.3107 0.3561 -0.0115 0.0003  0.0037  211 TYR B CZ  
5866 O OH  . TYR B 211 ? 0.5739 0.5657 0.6117 -0.0104 -0.0003 0.0042  211 TYR B OH  
5867 N N   . GLU B 212 ? 0.1855 0.1725 0.2136 -0.0166 0.0028  0.0009  212 GLU B N   
5868 C CA  . GLU B 212 ? 0.2720 0.2587 0.2986 -0.0179 0.0030  0.0007  212 GLU B CA  
5869 C C   . GLU B 212 ? 0.2714 0.2579 0.2950 -0.0189 0.0023  0.0012  212 GLU B C   
5870 O O   . GLU B 212 ? 0.2803 0.2669 0.3023 -0.0202 0.0022  0.0013  212 GLU B O   
5871 C CB  . GLU B 212 ? 0.1900 0.1758 0.2175 -0.0174 0.0038  -0.0003 212 GLU B CB  
5872 C CG  . GLU B 212 ? 0.1372 0.1232 0.1676 -0.0164 0.0048  -0.0009 212 GLU B CG  
5873 C CD  . GLU B 212 ? 0.1818 0.1669 0.2131 -0.0161 0.0058  -0.0019 212 GLU B CD  
5874 O OE1 . GLU B 212 ? 0.2517 0.2362 0.2814 -0.0167 0.0058  -0.0022 212 GLU B OE1 
5875 O OE2 . GLU B 212 ? 0.3133 0.2985 0.3469 -0.0151 0.0065  -0.0025 212 GLU B OE2 
5876 N N   . THR B 213 ? 0.2258 0.2122 0.2488 -0.0184 0.0018  0.0013  213 THR B N   
5877 C CA  . THR B 213 ? 0.1908 0.1771 0.2111 -0.0193 0.0013  0.0016  213 THR B CA  
5878 C C   . THR B 213 ? 0.2175 0.2046 0.2375 -0.0190 0.0008  0.0022  213 THR B C   
5879 O O   . THR B 213 ? 0.2410 0.2283 0.2592 -0.0198 0.0008  0.0023  213 THR B O   
5880 C CB  . THR B 213 ? 0.2255 0.2108 0.2451 -0.0189 0.0012  0.0013  213 THR B CB  
5881 O OG1 . THR B 213 ? 0.2045 0.1900 0.2260 -0.0175 0.0012  0.0012  213 THR B OG1 
5882 C CG2 . THR B 213 ? 0.1722 0.1568 0.1919 -0.0192 0.0017  0.0007  213 THR B CG2 
5883 N N   . THR B 214 ? 0.2141 0.2017 0.2361 -0.0178 0.0005  0.0025  214 THR B N   
5884 C CA  . THR B 214 ? 0.1562 0.1446 0.1782 -0.0173 -0.0002 0.0032  214 THR B CA  
5885 C C   . THR B 214 ? 0.1804 0.1697 0.2044 -0.0168 -0.0003 0.0037  214 THR B C   
5886 O O   . THR B 214 ? 0.1891 0.1786 0.2150 -0.0157 -0.0005 0.0038  214 THR B O   
5887 C CB  . THR B 214 ? 0.1200 0.1083 0.1424 -0.0162 -0.0007 0.0033  214 THR B CB  
5888 O OG1 . THR B 214 ? 0.1574 0.1455 0.1818 -0.0152 -0.0005 0.0030  214 THR B OG1 
5889 C CG2 . THR B 214 ? 0.1305 0.1181 0.1509 -0.0168 -0.0006 0.0029  214 THR B CG2 
5890 N N   . PRO B 215 ? 0.1829 0.1727 0.2064 -0.0177 -0.0002 0.0039  215 PRO B N   
5891 C CA  . PRO B 215 ? 0.2164 0.2069 0.2417 -0.0174 -0.0002 0.0044  215 PRO B CA  
5892 C C   . PRO B 215 ? 0.2004 0.1918 0.2269 -0.0164 -0.0012 0.0052  215 PRO B C   
5893 O O   . PRO B 215 ? 0.2407 0.2326 0.2689 -0.0158 -0.0012 0.0055  215 PRO B O   
5894 C CB  . PRO B 215 ? 0.2597 0.2508 0.2840 -0.0188 0.0001  0.0045  215 PRO B CB  
5895 C CG  . PRO B 215 ? 0.2848 0.2752 0.3072 -0.0198 0.0006  0.0038  215 PRO B CG  
5896 C CD  . PRO B 215 ? 0.2062 0.1959 0.2279 -0.0192 0.0003  0.0036  215 PRO B CD  
5897 N N   . ASN B 216 ? 0.2515 0.2431 0.2768 -0.0162 -0.0020 0.0057  216 ASN B N   
5898 C CA  . ASN B 216 ? 0.2924 0.2849 0.3186 -0.0153 -0.0031 0.0067  216 ASN B CA  
5899 C C   . ASN B 216 ? 0.3369 0.3293 0.3642 -0.0140 -0.0035 0.0066  216 ASN B C   
5900 O O   . ASN B 216 ? 0.3062 0.2994 0.3343 -0.0133 -0.0044 0.0074  216 ASN B O   
5901 C CB  . ASN B 216 ? 0.4077 0.4008 0.4322 -0.0158 -0.0039 0.0074  216 ASN B CB  
5902 C CG  . ASN B 216 ? 0.4556 0.4492 0.4795 -0.0169 -0.0037 0.0076  216 ASN B CG  
5903 O OD1 . ASN B 216 ? 0.4944 0.4884 0.5193 -0.0172 -0.0032 0.0077  216 ASN B OD1 
5904 N ND2 . ASN B 216 ? 0.4687 0.4625 0.4911 -0.0175 -0.0039 0.0078  216 ASN B ND2 
5905 N N   . VAL B 217 ? 0.2744 0.2660 0.3018 -0.0138 -0.0028 0.0058  217 VAL B N   
5906 C CA  . VAL B 217 ? 0.1971 0.1887 0.2257 -0.0127 -0.0032 0.0057  217 VAL B CA  
5907 C C   . VAL B 217 ? 0.2095 0.2017 0.2405 -0.0117 -0.0033 0.0060  217 VAL B C   
5908 O O   . VAL B 217 ? 0.2342 0.2264 0.2663 -0.0118 -0.0027 0.0058  217 VAL B O   
5909 C CB  . VAL B 217 ? 0.2192 0.2098 0.2474 -0.0127 -0.0024 0.0048  217 VAL B CB  
5910 C CG1 . VAL B 217 ? 0.2482 0.2384 0.2779 -0.0127 -0.0014 0.0041  217 VAL B CG1 
5911 C CG2 . VAL B 217 ? 0.2507 0.2414 0.2794 -0.0118 -0.0029 0.0048  217 VAL B CG2 
5912 N N   . LYS B 218 ? 0.2151 0.2079 0.2470 -0.0106 -0.0041 0.0064  218 LYS B N   
5913 C CA  . LYS B 218 ? 0.1476 0.1410 0.1821 -0.0096 -0.0042 0.0066  218 LYS B CA  
5914 C C   . LYS B 218 ? 0.1180 0.1111 0.1538 -0.0088 -0.0037 0.0058  218 LYS B C   
5915 O O   . LYS B 218 ? 0.1518 0.1447 0.1867 -0.0087 -0.0039 0.0057  218 LYS B O   
5916 C CB  . LYS B 218 ? 0.2150 0.2093 0.2498 -0.0089 -0.0055 0.0076  218 LYS B CB  
5917 C CG  . LYS B 218 ? 0.3139 0.3087 0.3473 -0.0096 -0.0062 0.0085  218 LYS B CG  
5918 C CD  . LYS B 218 ? 0.4787 0.4744 0.5124 -0.0089 -0.0075 0.0095  218 LYS B CD  
5919 C CE  . LYS B 218 ? 0.5984 0.5944 0.6302 -0.0096 -0.0084 0.0104  218 LYS B CE  
5920 N NZ  . LYS B 218 ? 0.6590 0.6559 0.6910 -0.0089 -0.0098 0.0115  218 LYS B NZ  
5921 N N   . ILE B 219 ? 0.1413 0.1344 0.1792 -0.0084 -0.0029 0.0053  219 ILE B N   
5922 C CA  . ILE B 219 ? 0.1500 0.1431 0.1895 -0.0076 -0.0024 0.0047  219 ILE B CA  
5923 C C   . ILE B 219 ? 0.1345 0.1286 0.1768 -0.0065 -0.0025 0.0049  219 ILE B C   
5924 O O   . ILE B 219 ? 0.1423 0.1368 0.1852 -0.0065 -0.0027 0.0054  219 ILE B O   
5925 C CB  . ILE B 219 ? 0.1732 0.1654 0.2127 -0.0081 -0.0012 0.0037  219 ILE B CB  
5926 C CG1 . ILE B 219 ? 0.2126 0.2049 0.2537 -0.0081 -0.0004 0.0035  219 ILE B CG1 
5927 C CG2 . ILE B 219 ? 0.1697 0.1610 0.2064 -0.0092 -0.0011 0.0035  219 ILE B CG2 
5928 C CD1 . ILE B 219 ? 0.2220 0.2134 0.2634 -0.0084 0.0008  0.0025  219 ILE B CD1 
5929 N N   . PRO B 220 ? 0.1917 0.1862 0.2355 -0.0057 -0.0025 0.0046  220 PRO B N   
5930 C CA  . PRO B 220 ? 0.1751 0.1705 0.2216 -0.0047 -0.0025 0.0048  220 PRO B CA  
5931 C C   . PRO B 220 ? 0.1157 0.1110 0.1640 -0.0046 -0.0014 0.0042  220 PRO B C   
5932 O O   . PRO B 220 ? 0.1293 0.1237 0.1769 -0.0053 -0.0005 0.0037  220 PRO B O   
5933 C CB  . PRO B 220 ? 0.2086 0.2044 0.2560 -0.0040 -0.0026 0.0045  220 PRO B CB  
5934 C CG  . PRO B 220 ? 0.1978 0.1927 0.2433 -0.0047 -0.0024 0.0040  220 PRO B CG  
5935 C CD  . PRO B 220 ? 0.2638 0.2579 0.3067 -0.0057 -0.0026 0.0043  220 PRO B CD  
5936 N N   . ASP B 221 ? 0.1129 0.1091 0.1638 -0.0037 -0.0014 0.0044  221 ASP B N   
5937 C CA  . ASP B 221 ? 0.1282 0.1245 0.1812 -0.0035 -0.0003 0.0040  221 ASP B CA  
5938 C C   . ASP B 221 ? 0.1240 0.1201 0.1782 -0.0032 0.0006  0.0030  221 ASP B C   
5939 O O   . ASP B 221 ? 0.1334 0.1302 0.1891 -0.0025 0.0004  0.0029  221 ASP B O   
5940 C CB  . ASP B 221 ? 0.1106 0.1080 0.1658 -0.0026 -0.0008 0.0046  221 ASP B CB  
5941 C CG  . ASP B 221 ? 0.1843 0.1818 0.2416 -0.0024 0.0003  0.0042  221 ASP B CG  
5942 O OD1 . ASP B 221 ? 0.1855 0.1822 0.2420 -0.0030 0.0010  0.0039  221 ASP B OD1 
5943 O OD2 . ASP B 221 ? 0.2295 0.2279 0.2892 -0.0015 0.0003  0.0043  221 ASP B OD2 
5944 N N   . PHE B 222 ? 0.0944 0.0895 0.1478 -0.0039 0.0016  0.0023  222 PHE B N   
5945 C CA  . PHE B 222 ? 0.1605 0.1552 0.2149 -0.0038 0.0025  0.0014  222 PHE B CA  
5946 C C   . PHE B 222 ? 0.1642 0.1595 0.2215 -0.0032 0.0033  0.0010  222 PHE B C   
5947 O O   . PHE B 222 ? 0.1586 0.1534 0.2164 -0.0034 0.0043  0.0005  222 PHE B O   
5948 C CB  . PHE B 222 ? 0.1119 0.1053 0.1643 -0.0047 0.0031  0.0007  222 PHE B CB  
5949 C CG  . PHE B 222 ? 0.1605 0.1534 0.2104 -0.0052 0.0024  0.0008  222 PHE B CG  
5950 C CD1 . PHE B 222 ? 0.1297 0.1226 0.1776 -0.0056 0.0015  0.0015  222 PHE B CD1 
5951 C CD2 . PHE B 222 ? 0.1255 0.1180 0.1753 -0.0052 0.0026  0.0003  222 PHE B CD2 
5952 C CE1 . PHE B 222 ? 0.1114 0.1038 0.1571 -0.0060 0.0009  0.0017  222 PHE B CE1 
5953 C CE2 . PHE B 222 ? 0.1531 0.1451 0.2007 -0.0056 0.0020  0.0004  222 PHE B CE2 
5954 C CZ  . PHE B 222 ? 0.1051 0.0971 0.1507 -0.0060 0.0012  0.0011  222 PHE B CZ  
5955 N N   . ALA B 223 ? 0.1586 0.1550 0.2178 -0.0023 0.0029  0.0014  223 ALA B N   
5956 C CA  . ALA B 223 ? 0.2077 0.2049 0.2698 -0.0017 0.0036  0.0012  223 ALA B CA  
5957 C C   . ALA B 223 ? 0.2034 0.2003 0.2668 -0.0017 0.0045  0.0004  223 ALA B C   
5958 O O   . ALA B 223 ? 0.2678 0.2654 0.3337 -0.0012 0.0051  0.0002  223 ALA B O   
5959 C CB  . ALA B 223 ? 0.1706 0.1691 0.2342 -0.0009 0.0027  0.0020  223 ALA B CB  
5960 N N   . VAL B 224 ? 0.1050 0.1010 0.1669 -0.0022 0.0047  -0.0001 224 VAL B N   
5961 C CA  . VAL B 224 ? 0.1662 0.1618 0.2290 -0.0023 0.0055  -0.0010 224 VAL B CA  
5962 C C   . VAL B 224 ? 0.1430 0.1372 0.2039 -0.0031 0.0062  -0.0016 224 VAL B C   
5963 O O   . VAL B 224 ? 0.1589 0.1525 0.2175 -0.0036 0.0057  -0.0014 224 VAL B O   
5964 C CB  . VAL B 224 ? 0.1845 0.1804 0.2475 -0.0020 0.0049  -0.0009 224 VAL B CB  
5965 C CG1 . VAL B 224 ? 0.2412 0.2370 0.3059 -0.0020 0.0058  -0.0016 224 VAL B CG1 
5966 C CG2 . VAL B 224 ? 0.3890 0.3863 0.4528 -0.0014 0.0039  -0.0001 224 VAL B CG2 
5967 N N   . SER B 225 ? 0.1171 0.1106 0.1789 -0.0033 0.0072  -0.0024 225 SER B N   
5968 C CA  . SER B 225 ? 0.1649 0.1570 0.2249 -0.0040 0.0079  -0.0030 225 SER B CA  
5969 C C   . SER B 225 ? 0.1521 0.1435 0.2109 -0.0043 0.0075  -0.0033 225 SER B C   
5970 O O   . SER B 225 ? 0.1048 0.0965 0.1649 -0.0040 0.0075  -0.0034 225 SER B O   
5971 C CB  . SER B 225 ? 0.1614 0.1531 0.2230 -0.0041 0.0091  -0.0037 225 SER B CB  
5972 O OG  . SER B 225 ? 0.1741 0.1643 0.2340 -0.0049 0.0097  -0.0044 225 SER B OG  
5973 N N   . PHE B 226 ? 0.1221 0.1126 0.1784 -0.0050 0.0073  -0.0033 226 PHE B N   
5974 C CA  . PHE B 226 ? 0.1303 0.1198 0.1851 -0.0054 0.0071  -0.0036 226 PHE B CA  
5975 C C   . PHE B 226 ? 0.1229 0.1110 0.1769 -0.0060 0.0080  -0.0045 226 PHE B C   
5976 O O   . PHE B 226 ? 0.1141 0.1012 0.1663 -0.0065 0.0079  -0.0047 226 PHE B O   
5977 C CB  . PHE B 226 ? 0.0721 0.0616 0.1246 -0.0056 0.0061  -0.0031 226 PHE B CB  
5978 C CG  . PHE B 226 ? 0.1233 0.1140 0.1763 -0.0050 0.0051  -0.0023 226 PHE B CG  
5979 C CD1 . PHE B 226 ? 0.0596 0.0506 0.1132 -0.0047 0.0047  -0.0023 226 PHE B CD1 
5980 C CD2 . PHE B 226 ? 0.1343 0.1258 0.1872 -0.0048 0.0045  -0.0016 226 PHE B CD2 
5981 C CE1 . PHE B 226 ? 0.1200 0.1122 0.1742 -0.0041 0.0037  -0.0016 226 PHE B CE1 
5982 C CE2 . PHE B 226 ? 0.1794 0.1721 0.2329 -0.0042 0.0035  -0.0009 226 PHE B CE2 
5983 C CZ  . PHE B 226 ? 0.1750 0.1680 0.2291 -0.0038 0.0031  -0.0009 226 PHE B CZ  
5984 N N   . ARG B 227 ? 0.1442 0.1321 0.1993 -0.0061 0.0090  -0.0049 227 ARG B N   
5985 C CA  . ARG B 227 ? 0.0726 0.0592 0.1267 -0.0067 0.0098  -0.0056 227 ARG B CA  
5986 C C   . ARG B 227 ? 0.1464 0.1320 0.2009 -0.0068 0.0102  -0.0062 227 ARG B C   
5987 O O   . ARG B 227 ? 0.1193 0.1035 0.1722 -0.0074 0.0103  -0.0067 227 ARG B O   
5988 C CB  . ARG B 227 ? 0.1399 0.1265 0.1951 -0.0067 0.0107  -0.0059 227 ARG B CB  
5989 C CG  . ARG B 227 ? 0.2423 0.2297 0.2970 -0.0067 0.0104  -0.0054 227 ARG B CG  
5990 C CD  . ARG B 227 ? 0.1774 0.1648 0.2333 -0.0067 0.0113  -0.0057 227 ARG B CD  
5991 N NE  . ARG B 227 ? 0.1749 0.1611 0.2303 -0.0073 0.0123  -0.0066 227 ARG B NE  
5992 C CZ  . ARG B 227 ? 0.2884 0.2738 0.3417 -0.0080 0.0123  -0.0068 227 ARG B CZ  
5993 N NH1 . ARG B 227 ? 0.1736 0.1594 0.2253 -0.0083 0.0115  -0.0062 227 ARG B NH1 
5994 N NH2 . ARG B 227 ? 0.3346 0.3189 0.3876 -0.0084 0.0132  -0.0076 227 ARG B NH2 
5995 N N   . GLU B 228 ? 0.1470 0.1330 0.2035 -0.0063 0.0103  -0.0062 228 GLU B N   
5996 C CA  . GLU B 228 ? 0.1315 0.1164 0.1881 -0.0065 0.0105  -0.0067 228 GLU B CA  
5997 C C   . GLU B 228 ? 0.1308 0.1153 0.1858 -0.0067 0.0097  -0.0065 228 GLU B C   
5998 O O   . GLU B 228 ? 0.1160 0.0991 0.1700 -0.0071 0.0098  -0.0069 228 GLU B O   
5999 C CB  . GLU B 228 ? 0.1893 0.1746 0.2483 -0.0060 0.0108  -0.0067 228 GLU B CB  
6000 C CG  . GLU B 228 ? 0.3694 0.3534 0.4284 -0.0062 0.0108  -0.0071 228 GLU B CG  
6001 C CD  . GLU B 228 ? 0.6182 0.6019 0.6792 -0.0059 0.0114  -0.0074 228 GLU B CD  
6002 O OE1 . GLU B 228 ? 0.6542 0.6395 0.7172 -0.0054 0.0115  -0.0070 228 GLU B OE1 
6003 O OE2 . GLU B 228 ? 0.6811 0.6631 0.7418 -0.0063 0.0119  -0.0080 228 GLU B OE2 
6004 N N   . ASP B 229 ? 0.0878 0.0735 0.1425 -0.0063 0.0087  -0.0058 229 ASP B N   
6005 C CA  . ASP B 229 ? 0.0818 0.0672 0.1348 -0.0065 0.0079  -0.0055 229 ASP B CA  
6006 C C   . ASP B 229 ? 0.1401 0.1243 0.1906 -0.0072 0.0080  -0.0057 229 ASP B C   
6007 O O   . ASP B 229 ? 0.1733 0.1565 0.2225 -0.0075 0.0077  -0.0059 229 ASP B O   
6008 C CB  . ASP B 229 ? 0.0962 0.0831 0.1493 -0.0060 0.0069  -0.0047 229 ASP B CB  
6009 C CG  . ASP B 229 ? 0.1387 0.1267 0.1940 -0.0053 0.0066  -0.0044 229 ASP B CG  
6010 O OD1 . ASP B 229 ? 0.1617 0.1491 0.2183 -0.0053 0.0072  -0.0049 229 ASP B OD1 
6011 O OD2 . ASP B 229 ? 0.1373 0.1265 0.1929 -0.0049 0.0058  -0.0037 229 ASP B OD2 
6012 N N   . ALA B 230 ? 0.0823 0.0666 0.1321 -0.0075 0.0082  -0.0057 230 ALA B N   
6013 C CA  . ALA B 230 ? 0.0437 0.0268 0.0911 -0.0082 0.0083  -0.0060 230 ALA B CA  
6014 C C   . ALA B 230 ? 0.1125 0.0940 0.1597 -0.0086 0.0091  -0.0068 230 ALA B C   
6015 O O   . ALA B 230 ? 0.1506 0.1311 0.1961 -0.0091 0.0088  -0.0070 230 ALA B O   
6016 C CB  . ALA B 230 ? 0.0434 0.0268 0.0905 -0.0084 0.0087  -0.0060 230 ALA B CB  
6017 N N   . SER B 231 ? 0.1297 0.1110 0.1787 -0.0084 0.0099  -0.0073 231 SER B N   
6018 C CA  . SER B 231 ? 0.1096 0.0892 0.1585 -0.0088 0.0105  -0.0081 231 SER B CA  
6019 C C   . SER B 231 ? 0.1128 0.0917 0.1613 -0.0088 0.0100  -0.0081 231 SER B C   
6020 O O   . SER B 231 ? 0.1300 0.1073 0.1770 -0.0092 0.0101  -0.0085 231 SER B O   
6021 C CB  . SER B 231 ? 0.1986 0.1782 0.2496 -0.0085 0.0114  -0.0085 231 SER B CB  
6022 O OG  . SER B 231 ? 0.4014 0.3806 0.4523 -0.0088 0.0122  -0.0090 231 SER B OG  
6023 N N   . LYS B 232 ? 0.1153 0.0953 0.1651 -0.0082 0.0095  -0.0076 232 LYS B N   
6024 C CA  . LYS B 232 ? 0.1216 0.1010 0.1712 -0.0082 0.0090  -0.0075 232 LYS B CA  
6025 C C   . LYS B 232 ? 0.1609 0.1398 0.2082 -0.0085 0.0083  -0.0073 232 LYS B C   
6026 O O   . LYS B 232 ? 0.0891 0.0667 0.1355 -0.0088 0.0082  -0.0076 232 LYS B O   
6027 C CB  . LYS B 232 ? 0.2208 0.2017 0.2723 -0.0075 0.0085  -0.0070 232 LYS B CB  
6028 C CG  . LYS B 232 ? 0.4128 0.3934 0.4663 -0.0072 0.0090  -0.0074 232 LYS B CG  
6029 C CD  . LYS B 232 ? 0.4569 0.4391 0.5122 -0.0066 0.0085  -0.0068 232 LYS B CD  
6030 C CE  . LYS B 232 ? 0.4811 0.4630 0.5358 -0.0065 0.0077  -0.0066 232 LYS B CE  
6031 N NZ  . LYS B 232 ? 0.5646 0.5447 0.6193 -0.0068 0.0080  -0.0071 232 LYS B NZ  
6032 N N   . HIS B 233 ? 0.1216 0.1015 0.1679 -0.0085 0.0077  -0.0068 233 HIS B N   
6033 C CA  . HIS B 233 ? 0.1120 0.0914 0.1560 -0.0089 0.0071  -0.0065 233 HIS B CA  
6034 C C   . HIS B 233 ? 0.1290 0.1067 0.1715 -0.0096 0.0076  -0.0072 233 HIS B C   
6035 O O   . HIS B 233 ? 0.1050 0.0815 0.1461 -0.0099 0.0073  -0.0073 233 HIS B O   
6036 C CB  . HIS B 233 ? 0.1139 0.0944 0.1569 -0.0089 0.0066  -0.0060 233 HIS B CB  
6037 C CG  . HIS B 233 ? 0.0738 0.0559 0.1177 -0.0083 0.0059  -0.0052 233 HIS B CG  
6038 N ND1 . HIS B 233 ? 0.1230 0.1053 0.1659 -0.0082 0.0050  -0.0048 233 HIS B ND1 
6039 C CD2 . HIS B 233 ? 0.0829 0.0664 0.1284 -0.0077 0.0058  -0.0049 233 HIS B CD2 
6040 C CE1 . HIS B 233 ? 0.1035 0.0874 0.1476 -0.0076 0.0044  -0.0042 233 HIS B CE1 
6041 N NE2 . HIS B 233 ? 0.0734 0.0579 0.1190 -0.0073 0.0049  -0.0042 233 HIS B NE2 
6042 N N   . VAL B 234 ? 0.1146 0.0919 0.1573 -0.0099 0.0084  -0.0076 234 VAL B N   
6043 C CA  . VAL B 234 ? 0.1007 0.0763 0.1419 -0.0105 0.0088  -0.0083 234 VAL B CA  
6044 C C   . VAL B 234 ? 0.1586 0.1326 0.2002 -0.0105 0.0091  -0.0088 234 VAL B C   
6045 O O   . VAL B 234 ? 0.1373 0.1099 0.1774 -0.0110 0.0089  -0.0091 234 VAL B O   
6046 C CB  . VAL B 234 ? 0.1304 0.1061 0.1718 -0.0107 0.0096  -0.0086 234 VAL B CB  
6047 C CG1 . VAL B 234 ? 0.1555 0.1294 0.1955 -0.0114 0.0101  -0.0093 234 VAL B CG1 
6048 C CG2 . VAL B 234 ? 0.1342 0.1112 0.1748 -0.0108 0.0092  -0.0080 234 VAL B CG2 
6049 N N   . GLU B 235 ? 0.0809 0.0551 0.1245 -0.0101 0.0095  -0.0090 235 GLU B N   
6050 C CA  . GLU B 235 ? 0.1882 0.1607 0.2322 -0.0102 0.0098  -0.0096 235 GLU B CA  
6051 C C   . GLU B 235 ? 0.1792 0.1512 0.2225 -0.0101 0.0090  -0.0093 235 GLU B C   
6052 O O   . GLU B 235 ? 0.1525 0.1227 0.1947 -0.0105 0.0090  -0.0098 235 GLU B O   
6053 C CB  . GLU B 235 ? 0.2808 0.2538 0.3272 -0.0097 0.0103  -0.0098 235 GLU B CB  
6054 C CG  . GLU B 235 ? 0.4222 0.3932 0.4690 -0.0098 0.0108  -0.0105 235 GLU B CG  
6055 C CD  . GLU B 235 ? 0.5018 0.4707 0.5469 -0.0104 0.0111  -0.0112 235 GLU B CD  
6056 O OE1 . GLU B 235 ? 0.4122 0.3813 0.4571 -0.0106 0.0117  -0.0114 235 GLU B OE1 
6057 O OE2 . GLU B 235 ? 0.6135 0.5807 0.6573 -0.0106 0.0108  -0.0114 235 GLU B OE2 
6058 N N   . LEU B 236 ? 0.1028 0.0764 0.1468 -0.0097 0.0084  -0.0086 236 LEU B N   
6059 C CA  . LEU B 236 ? 0.1023 0.0756 0.1457 -0.0097 0.0076  -0.0084 236 LEU B CA  
6060 C C   . LEU B 236 ? 0.1051 0.0775 0.1459 -0.0102 0.0072  -0.0083 236 LEU B C   
6061 O O   . LEU B 236 ? 0.1257 0.0968 0.1656 -0.0104 0.0069  -0.0084 236 LEU B O   
6062 C CB  . LEU B 236 ? 0.1175 0.0927 0.1620 -0.0091 0.0070  -0.0076 236 LEU B CB  
6063 C CG  . LEU B 236 ? 0.1740 0.1501 0.2210 -0.0085 0.0073  -0.0076 236 LEU B CG  
6064 C CD1 . LEU B 236 ? 0.2312 0.2095 0.2793 -0.0079 0.0067  -0.0069 236 LEU B CD1 
6065 C CD2 . LEU B 236 ? 0.1963 0.1711 0.2438 -0.0085 0.0073  -0.0080 236 LEU B CD2 
6066 N N   . ALA B 237 ? 0.0902 0.0632 0.1300 -0.0104 0.0072  -0.0081 237 ALA B N   
6067 C CA  . ALA B 237 ? 0.1315 0.1036 0.1690 -0.0110 0.0069  -0.0081 237 ALA B CA  
6068 C C   . ALA B 237 ? 0.1760 0.1460 0.2125 -0.0115 0.0074  -0.0089 237 ALA B C   
6069 O O   . ALA B 237 ? 0.1276 0.0964 0.1626 -0.0118 0.0070  -0.0089 237 ALA B O   
6070 C CB  . ALA B 237 ? 0.1306 0.1037 0.1670 -0.0112 0.0068  -0.0078 237 ALA B CB  
6071 N N   . LYS B 238 ? 0.1348 0.1042 0.1722 -0.0116 0.0082  -0.0094 238 LYS B N   
6072 C CA  . LYS B 238 ? 0.1451 0.1123 0.1817 -0.0120 0.0086  -0.0102 238 LYS B CA  
6073 C C   . LYS B 238 ? 0.1694 0.1353 0.2062 -0.0119 0.0083  -0.0104 238 LYS B C   
6074 O O   . LYS B 238 ? 0.1691 0.1331 0.2044 -0.0123 0.0082  -0.0108 238 LYS B O   
6075 C CB  . LYS B 238 ? 0.1534 0.1204 0.1913 -0.0120 0.0095  -0.0108 238 LYS B CB  
6076 C CG  . LYS B 238 ? 0.2061 0.1740 0.2436 -0.0122 0.0099  -0.0108 238 LYS B CG  
6077 C CD  . LYS B 238 ? 0.2424 0.2101 0.2812 -0.0121 0.0108  -0.0114 238 LYS B CD  
6078 C CE  . LYS B 238 ? 0.3717 0.3371 0.4098 -0.0125 0.0113  -0.0123 238 LYS B CE  
6079 N NZ  . LYS B 238 ? 0.2997 0.2649 0.3394 -0.0123 0.0122  -0.0128 238 LYS B NZ  
6080 N N   . GLU B 239 ? 0.1467 0.1134 0.1851 -0.0113 0.0081  -0.0101 239 GLU B N   
6081 C CA  . GLU B 239 ? 0.1721 0.1375 0.2106 -0.0112 0.0078  -0.0103 239 GLU B CA  
6082 C C   . GLU B 239 ? 0.1976 0.1629 0.2347 -0.0114 0.0070  -0.0098 239 GLU B C   
6083 O O   . GLU B 239 ? 0.2068 0.1703 0.2428 -0.0116 0.0068  -0.0101 239 GLU B O   
6084 C CB  . GLU B 239 ? 0.2471 0.2136 0.2879 -0.0106 0.0079  -0.0101 239 GLU B CB  
6085 C CG  . GLU B 239 ? 0.4472 0.4131 0.4894 -0.0105 0.0087  -0.0106 239 GLU B CG  
6086 C CD  . GLU B 239 ? 0.7059 0.6691 0.7470 -0.0109 0.0090  -0.0115 239 GLU B CD  
6087 O OE1 . GLU B 239 ? 0.7621 0.7237 0.8028 -0.0109 0.0087  -0.0117 239 GLU B OE1 
6088 O OE2 . GLU B 239 ? 0.7577 0.7202 0.7982 -0.0112 0.0096  -0.0119 239 GLU B OE2 
6089 N N   . LYS B 240 ? 0.1452 0.1124 0.1820 -0.0112 0.0065  -0.0091 240 LYS B N   
6090 C CA  . LYS B 240 ? 0.1062 0.0733 0.1416 -0.0113 0.0057  -0.0087 240 LYS B CA  
6091 C C   . LYS B 240 ? 0.1589 0.1245 0.1921 -0.0120 0.0057  -0.0090 240 LYS B C   
6092 O O   . LYS B 240 ? 0.1645 0.1287 0.1965 -0.0122 0.0053  -0.0090 240 LYS B O   
6093 C CB  . LYS B 240 ? 0.1025 0.0718 0.1380 -0.0110 0.0052  -0.0079 240 LYS B CB  
6094 C CG  . LYS B 240 ? 0.0894 0.0587 0.1235 -0.0111 0.0043  -0.0074 240 LYS B CG  
6095 C CD  . LYS B 240 ? 0.0965 0.0659 0.1318 -0.0107 0.0040  -0.0073 240 LYS B CD  
6096 C CE  . LYS B 240 ? 0.1933 0.1620 0.2269 -0.0109 0.0033  -0.0070 240 LYS B CE  
6097 N NZ  . LYS B 240 ? 0.2355 0.2046 0.2703 -0.0104 0.0028  -0.0068 240 LYS B NZ  
6098 N N   . TYR B 241 ? 0.1082 0.0738 0.1407 -0.0123 0.0061  -0.0092 241 TYR B N   
6099 C CA  . TYR B 241 ? 0.1555 0.1197 0.1860 -0.0129 0.0061  -0.0095 241 TYR B CA  
6100 C C   . TYR B 241 ? 0.1922 0.1539 0.2224 -0.0132 0.0063  -0.0102 241 TYR B C   
6101 O O   . TYR B 241 ? 0.1811 0.1414 0.2097 -0.0135 0.0060  -0.0103 241 TYR B O   
6102 C CB  . TYR B 241 ? 0.1707 0.1354 0.2010 -0.0132 0.0066  -0.0096 241 TYR B CB  
6103 C CG  . TYR B 241 ? 0.1582 0.1217 0.1865 -0.0139 0.0066  -0.0099 241 TYR B CG  
6104 C CD1 . TYR B 241 ? 0.1662 0.1279 0.1941 -0.0142 0.0071  -0.0106 241 TYR B CD1 
6105 C CD2 . TYR B 241 ? 0.1426 0.1069 0.1694 -0.0141 0.0061  -0.0093 241 TYR B CD2 
6106 C CE1 . TYR B 241 ? 0.1550 0.1157 0.1812 -0.0148 0.0071  -0.0109 241 TYR B CE1 
6107 C CE2 . TYR B 241 ? 0.1620 0.1254 0.1871 -0.0147 0.0061  -0.0095 241 TYR B CE2 
6108 C CZ  . TYR B 241 ? 0.1139 0.0755 0.1388 -0.0150 0.0066  -0.0103 241 TYR B CZ  
6109 O OH  . TYR B 241 ? 0.1537 0.1144 0.1770 -0.0156 0.0066  -0.0106 241 TYR B OH  
6110 N N   . PHE B 242 ? 0.1933 0.1546 0.2251 -0.0129 0.0069  -0.0107 242 PHE B N   
6111 C CA  . PHE B 242 ? 0.2276 0.1865 0.2591 -0.0130 0.0071  -0.0114 242 PHE B CA  
6112 C C   . PHE B 242 ? 0.2389 0.1969 0.2700 -0.0129 0.0065  -0.0113 242 PHE B C   
6113 O O   . PHE B 242 ? 0.2267 0.1825 0.2565 -0.0133 0.0063  -0.0117 242 PHE B O   
6114 C CB  . PHE B 242 ? 0.2530 0.2118 0.2864 -0.0127 0.0078  -0.0119 242 PHE B CB  
6115 C CG  . PHE B 242 ? 0.2916 0.2479 0.3249 -0.0127 0.0081  -0.0126 242 PHE B CG  
6116 C CD1 . PHE B 242 ? 0.3398 0.2942 0.3720 -0.0131 0.0084  -0.0134 242 PHE B CD1 
6117 C CD2 . PHE B 242 ? 0.3306 0.2865 0.3651 -0.0123 0.0079  -0.0126 242 PHE B CD2 
6118 C CE1 . PHE B 242 ? 0.3738 0.3257 0.4059 -0.0130 0.0085  -0.0141 242 PHE B CE1 
6119 C CE2 . PHE B 242 ? 0.4631 0.4165 0.4974 -0.0122 0.0081  -0.0133 242 PHE B CE2 
6120 C CZ  . PHE B 242 ? 0.3646 0.3159 0.3976 -0.0126 0.0084  -0.0141 242 PHE B CZ  
6121 N N   . GLU B 243 ? 0.2421 0.2016 0.2743 -0.0125 0.0061  -0.0107 243 GLU B N   
6122 C CA  . GLU B 243 ? 0.3083 0.2672 0.3400 -0.0124 0.0054  -0.0104 243 GLU B CA  
6123 C C   . GLU B 243 ? 0.3305 0.2888 0.3601 -0.0128 0.0049  -0.0102 243 GLU B C   
6124 O O   . GLU B 243 ? 0.3500 0.3065 0.3787 -0.0130 0.0046  -0.0104 243 GLU B O   
6125 C CB  . GLU B 243 ? 0.3666 0.3277 0.4000 -0.0118 0.0051  -0.0097 243 GLU B CB  
6126 C CG  . GLU B 243 ? 0.5355 0.4964 0.5688 -0.0117 0.0045  -0.0095 243 GLU B CG  
6127 C CD  . GLU B 243 ? 0.5876 0.5509 0.6217 -0.0112 0.0039  -0.0087 243 GLU B CD  
6128 O OE1 . GLU B 243 ? 0.5703 0.5353 0.6060 -0.0108 0.0041  -0.0084 243 GLU B OE1 
6129 O OE2 . GLU B 243 ? 0.6195 0.5828 0.6526 -0.0113 0.0033  -0.0083 243 GLU B OE2 
6130 N N   . ILE B 244 ? 0.1533 0.1128 0.1820 -0.0130 0.0047  -0.0098 244 ILE B N   
6131 C CA  . ILE B 244 ? 0.1598 0.1189 0.1865 -0.0134 0.0042  -0.0095 244 ILE B CA  
6132 C C   . ILE B 244 ? 0.2279 0.1850 0.2531 -0.0140 0.0044  -0.0101 244 ILE B C   
6133 O O   . ILE B 244 ? 0.2504 0.2060 0.2742 -0.0143 0.0040  -0.0101 244 ILE B O   
6134 C CB  . ILE B 244 ? 0.1480 0.1091 0.1742 -0.0134 0.0039  -0.0088 244 ILE B CB  
6135 C CG1 . ILE B 244 ? 0.1828 0.1460 0.2106 -0.0128 0.0037  -0.0082 244 ILE B CG1 
6136 C CG2 . ILE B 244 ? 0.1963 0.1569 0.2203 -0.0139 0.0033  -0.0085 244 ILE B CG2 
6137 C CD1 . ILE B 244 ? 0.2080 0.1708 0.2361 -0.0126 0.0032  -0.0080 244 ILE B CD1 
6138 N N   . PHE B 245 ? 0.2102 0.1672 0.2356 -0.0142 0.0050  -0.0105 245 PHE B N   
6139 C CA  . PHE B 245 ? 0.2379 0.1934 0.2619 -0.0147 0.0052  -0.0110 245 PHE B CA  
6140 C C   . PHE B 245 ? 0.2000 0.1535 0.2244 -0.0148 0.0057  -0.0119 245 PHE B C   
6141 O O   . PHE B 245 ? 0.2505 0.2024 0.2737 -0.0152 0.0058  -0.0124 245 PHE B O   
6142 C CB  . PHE B 245 ? 0.1992 0.1560 0.2229 -0.0150 0.0055  -0.0108 245 PHE B CB  
6143 C CG  . PHE B 245 ? 0.2294 0.1878 0.2521 -0.0150 0.0049  -0.0100 245 PHE B CG  
6144 C CD1 . PHE B 245 ? 0.2168 0.1745 0.2377 -0.0154 0.0043  -0.0097 245 PHE B CD1 
6145 C CD2 . PHE B 245 ? 0.2069 0.1675 0.2307 -0.0146 0.0049  -0.0094 245 PHE B CD2 
6146 C CE1 . PHE B 245 ? 0.2837 0.2429 0.3037 -0.0154 0.0037  -0.0089 245 PHE B CE1 
6147 C CE2 . PHE B 245 ? 0.2174 0.1792 0.2402 -0.0146 0.0043  -0.0087 245 PHE B CE2 
6148 C CZ  . PHE B 245 ? 0.2020 0.1631 0.2229 -0.0150 0.0037  -0.0084 245 PHE B CZ  
6149 N N   . GLY B 246 ? 0.2132 0.1665 0.2392 -0.0143 0.0061  -0.0121 246 GLY B N   
6150 C CA  . GLY B 246 ? 0.2429 0.1940 0.2691 -0.0143 0.0065  -0.0130 246 GLY B CA  
6151 C C   . GLY B 246 ? 0.3077 0.2588 0.3346 -0.0144 0.0073  -0.0136 246 GLY B C   
6152 O O   . GLY B 246 ? 0.2332 0.1825 0.2604 -0.0143 0.0077  -0.0143 246 GLY B O   
6153 N N   . GLU B 247 ? 0.3431 0.2961 0.3702 -0.0145 0.0075  -0.0132 247 GLU B N   
6154 C CA  . GLU B 247 ? 0.3253 0.2786 0.3533 -0.0145 0.0084  -0.0137 247 GLU B CA  
6155 C C   . GLU B 247 ? 0.3368 0.2928 0.3660 -0.0142 0.0086  -0.0131 247 GLU B C   
6156 O O   . GLU B 247 ? 0.2362 0.1937 0.2653 -0.0141 0.0080  -0.0123 247 GLU B O   
6157 C CB  . GLU B 247 ? 0.3476 0.3001 0.3740 -0.0151 0.0086  -0.0141 247 GLU B CB  
6158 C CG  . GLU B 247 ? 0.5378 0.4913 0.5628 -0.0154 0.0080  -0.0135 247 GLU B CG  
6159 C CD  . GLU B 247 ? 0.6977 0.6508 0.7216 -0.0160 0.0083  -0.0139 247 GLU B CD  
6160 O OE1 . GLU B 247 ? 0.7687 0.7199 0.7923 -0.0161 0.0087  -0.0147 247 GLU B OE1 
6161 O OE2 . GLU B 247 ? 0.6980 0.6525 0.7212 -0.0162 0.0081  -0.0134 247 GLU B OE2 
6162 N N   . HIS B 248 ? 0.2165 0.1729 0.2469 -0.0141 0.0093  -0.0135 248 HIS B N   
6163 C CA  . HIS B 248 ? 0.2347 0.1935 0.2662 -0.0139 0.0095  -0.0130 248 HIS B CA  
6164 C C   . HIS B 248 ? 0.2233 0.1831 0.2535 -0.0143 0.0094  -0.0127 248 HIS B C   
6165 O O   . HIS B 248 ? 0.2286 0.1873 0.2576 -0.0148 0.0096  -0.0131 248 HIS B O   
6166 C CB  . HIS B 248 ? 0.2965 0.2554 0.3296 -0.0136 0.0103  -0.0134 248 HIS B CB  
6167 C CG  . HIS B 248 ? 0.4582 0.4165 0.4927 -0.0131 0.0103  -0.0135 248 HIS B CG  
6168 N ND1 . HIS B 248 ? 0.5238 0.4798 0.5583 -0.0131 0.0106  -0.0143 248 HIS B ND1 
6169 C CD2 . HIS B 248 ? 0.4956 0.4553 0.5315 -0.0126 0.0101  -0.0130 248 HIS B CD2 
6170 C CE1 . HIS B 248 ? 0.4937 0.4496 0.5295 -0.0126 0.0105  -0.0142 248 HIS B CE1 
6171 N NE2 . HIS B 248 ? 0.5115 0.4698 0.5483 -0.0123 0.0102  -0.0134 248 HIS B NE2 
6172 N N   . PRO B 249 ? 0.1264 0.0883 0.1569 -0.0141 0.0091  -0.0119 249 PRO B N   
6173 C CA  . PRO B 249 ? 0.1462 0.1090 0.1754 -0.0146 0.0090  -0.0116 249 PRO B CA  
6174 C C   . PRO B 249 ? 0.2193 0.1825 0.2490 -0.0147 0.0099  -0.0121 249 PRO B C   
6175 O O   . PRO B 249 ? 0.2403 0.2041 0.2717 -0.0144 0.0104  -0.0122 249 PRO B O   
6176 C CB  . PRO B 249 ? 0.0662 0.0310 0.0957 -0.0142 0.0084  -0.0107 249 PRO B CB  
6177 C CG  . PRO B 249 ? 0.1616 0.1271 0.1931 -0.0136 0.0086  -0.0106 249 PRO B CG  
6178 C CD  . PRO B 249 ? 0.1290 0.0926 0.1610 -0.0136 0.0089  -0.0113 249 PRO B CD  
6179 N N   . VAL B 250 ? 0.1796 0.1426 0.2080 -0.0153 0.0100  -0.0123 250 VAL B N   
6180 C CA  . VAL B 250 ? 0.2357 0.1991 0.2643 -0.0155 0.0107  -0.0126 250 VAL B CA  
6181 C C   . VAL B 250 ? 0.1522 0.1174 0.1801 -0.0157 0.0104  -0.0120 250 VAL B C   
6182 O O   . VAL B 250 ? 0.1665 0.1323 0.1946 -0.0158 0.0110  -0.0122 250 VAL B O   
6183 C CB  . VAL B 250 ? 0.3360 0.2978 0.3638 -0.0160 0.0112  -0.0135 250 VAL B CB  
6184 C CG1 . VAL B 250 ? 0.3180 0.2779 0.3465 -0.0158 0.0115  -0.0142 250 VAL B CG1 
6185 C CG2 . VAL B 250 ? 0.2553 0.2164 0.2811 -0.0165 0.0107  -0.0133 250 VAL B CG2 
6186 N N   . TYR B 251 ? 0.1725 0.1381 0.1993 -0.0157 0.0096  -0.0112 251 TYR B N   
6187 C CA  . TYR B 251 ? 0.1760 0.1430 0.2018 -0.0158 0.0091  -0.0105 251 TYR B CA  
6188 C C   . TYR B 251 ? 0.1602 0.1285 0.1868 -0.0153 0.0085  -0.0098 251 TYR B C   
6189 O O   . TYR B 251 ? 0.1240 0.0919 0.1509 -0.0150 0.0081  -0.0096 251 TYR B O   
6190 C CB  . TYR B 251 ? 0.2594 0.2259 0.2831 -0.0164 0.0086  -0.0103 251 TYR B CB  
6191 C CG  . TYR B 251 ? 0.2518 0.2169 0.2750 -0.0169 0.0091  -0.0111 251 TYR B CG  
6192 C CD1 . TYR B 251 ? 0.2369 0.2021 0.2605 -0.0171 0.0099  -0.0117 251 TYR B CD1 
6193 C CD2 . TYR B 251 ? 0.3196 0.2833 0.3419 -0.0170 0.0088  -0.0113 251 TYR B CD2 
6194 C CE1 . TYR B 251 ? 0.3264 0.2902 0.3494 -0.0176 0.0104  -0.0125 251 TYR B CE1 
6195 C CE2 . TYR B 251 ? 0.2733 0.2355 0.2950 -0.0175 0.0092  -0.0121 251 TYR B CE2 
6196 C CZ  . TYR B 251 ? 0.3545 0.3168 0.3766 -0.0177 0.0101  -0.0127 251 TYR B CZ  
6197 O OH  . TYR B 251 ? 0.3856 0.3465 0.4071 -0.0181 0.0106  -0.0135 251 TYR B OH  
6198 N N   . MET B 252 ? 0.1554 0.1252 0.1823 -0.0152 0.0084  -0.0093 252 MET B N   
6199 C CA  . MET B 252 ? 0.1393 0.1103 0.1665 -0.0147 0.0077  -0.0085 252 MET B CA  
6200 C C   . MET B 252 ? 0.1261 0.0981 0.1519 -0.0150 0.0071  -0.0078 252 MET B C   
6201 O O   . MET B 252 ? 0.1115 0.0837 0.1368 -0.0154 0.0075  -0.0080 252 MET B O   
6202 C CB  . MET B 252 ? 0.1521 0.1240 0.1816 -0.0141 0.0082  -0.0086 252 MET B CB  
6203 C CG  . MET B 252 ? 0.2048 0.1759 0.2356 -0.0137 0.0085  -0.0090 252 MET B CG  
6204 S SD  . MET B 252 ? 0.2188 0.1913 0.2521 -0.0129 0.0085  -0.0087 252 MET B SD  
6205 C CE  . MET B 252 ? 0.1931 0.1643 0.2274 -0.0126 0.0086  -0.0092 252 MET B CE  
6206 N N   . TRP B 253 ? 0.0945 0.0670 0.1197 -0.0148 0.0063  -0.0071 253 TRP B N   
6207 C CA  . TRP B 253 ? 0.0537 0.0271 0.0777 -0.0149 0.0056  -0.0064 253 TRP B CA  
6208 C C   . TRP B 253 ? 0.0985 0.0733 0.1240 -0.0143 0.0056  -0.0060 253 TRP B C   
6209 O O   . TRP B 253 ? 0.1062 0.0813 0.1328 -0.0137 0.0053  -0.0058 253 TRP B O   
6210 C CB  . TRP B 253 ? 0.0588 0.0321 0.0811 -0.0151 0.0047  -0.0058 253 TRP B CB  
6211 C CG  . TRP B 253 ? 0.0910 0.0652 0.1121 -0.0151 0.0039  -0.0050 253 TRP B CG  
6212 C CD1 . TRP B 253 ? 0.0662 0.0413 0.0875 -0.0147 0.0033  -0.0044 253 TRP B CD1 
6213 C CD2 . TRP B 253 ? 0.0902 0.0647 0.1101 -0.0157 0.0038  -0.0048 253 TRP B CD2 
6214 N NE1 . TRP B 253 ? 0.1145 0.0903 0.1345 -0.0150 0.0027  -0.0038 253 TRP B NE1 
6215 C CE2 . TRP B 253 ? 0.1568 0.1322 0.1759 -0.0156 0.0030  -0.0040 253 TRP B CE2 
6216 C CE3 . TRP B 253 ? 0.0904 0.0646 0.1098 -0.0163 0.0042  -0.0051 253 TRP B CE3 
6217 C CZ2 . TRP B 253 ? 0.0959 0.0717 0.1137 -0.0162 0.0025  -0.0035 253 TRP B CZ2 
6218 C CZ3 . TRP B 253 ? 0.1061 0.0808 0.1243 -0.0168 0.0038  -0.0046 253 TRP B CZ3 
6219 C CH2 . TRP B 253 ? 0.0818 0.0572 0.0991 -0.0167 0.0029  -0.0038 253 TRP B CH2 
6220 N N   . PRO B 254 ? 0.1147 0.0902 0.1405 -0.0144 0.0058  -0.0059 254 PRO B N   
6221 C CA  . PRO B 254 ? 0.0634 0.0401 0.0905 -0.0139 0.0056  -0.0055 254 PRO B CA  
6222 C C   . PRO B 254 ? 0.0806 0.0580 0.1067 -0.0137 0.0046  -0.0047 254 PRO B C   
6223 O O   . PRO B 254 ? 0.0847 0.0620 0.1087 -0.0143 0.0041  -0.0043 254 PRO B O   
6224 C CB  . PRO B 254 ? 0.0898 0.0669 0.1171 -0.0142 0.0061  -0.0057 254 PRO B CB  
6225 C CG  . PRO B 254 ? 0.1531 0.1296 0.1785 -0.0150 0.0060  -0.0058 254 PRO B CG  
6226 C CD  . PRO B 254 ? 0.0796 0.0549 0.1043 -0.0151 0.0061  -0.0061 254 PRO B CD  
6227 N N   . PRO B 255 ? 0.0962 0.0744 0.1236 -0.0130 0.0043  -0.0044 255 PRO B N   
6228 C CA  . PRO B 255 ? 0.0683 0.0471 0.0946 -0.0129 0.0034  -0.0036 255 PRO B CA  
6229 C C   . PRO B 255 ? 0.1085 0.0879 0.1335 -0.0133 0.0030  -0.0031 255 PRO B C   
6230 O O   . PRO B 255 ? 0.1003 0.0803 0.1263 -0.0132 0.0033  -0.0031 255 PRO B O   
6231 C CB  . PRO B 255 ? 0.0597 0.0395 0.0883 -0.0120 0.0033  -0.0035 255 PRO B CB  
6232 C CG  . PRO B 255 ? 0.1024 0.0815 0.1325 -0.0118 0.0040  -0.0042 255 PRO B CG  
6233 C CD  . PRO B 255 ? 0.0991 0.0774 0.1288 -0.0124 0.0048  -0.0048 255 PRO B CD  
6234 N N   . GLU B 256 ? 0.0767 0.0559 0.0996 -0.0137 0.0023  -0.0026 256 GLU B N   
6235 C CA  . GLU B 256 ? 0.1054 0.0849 0.1265 -0.0142 0.0018  -0.0021 256 GLU B CA  
6236 C C   . GLU B 256 ? 0.1035 0.0826 0.1241 -0.0150 0.0022  -0.0024 256 GLU B C   
6237 O O   . GLU B 256 ? 0.1178 0.0974 0.1378 -0.0153 0.0020  -0.0020 256 GLU B O   
6238 C CB  . GLU B 256 ? 0.1130 0.0938 0.1352 -0.0137 0.0014  -0.0016 256 GLU B CB  
6239 C CG  . GLU B 256 ? 0.1556 0.1371 0.1788 -0.0128 0.0009  -0.0013 256 GLU B CG  
6240 C CD  . GLU B 256 ? 0.1844 0.1656 0.2056 -0.0131 0.0003  -0.0010 256 GLU B CD  
6241 O OE1 . GLU B 256 ? 0.1886 0.1700 0.2105 -0.0125 0.0000  -0.0009 256 GLU B OE1 
6242 O OE2 . GLU B 256 ? 0.1906 0.1714 0.2096 -0.0138 0.0001  -0.0008 256 GLU B OE2 
6243 N N   . ALA B 257 ? 0.0636 0.0418 0.0844 -0.0152 0.0028  -0.0030 257 ALA B N   
6244 C CA  . ALA B 257 ? 0.1559 0.1339 0.1767 -0.0158 0.0033  -0.0034 257 ALA B CA  
6245 C C   . ALA B 257 ? 0.1533 0.1320 0.1757 -0.0155 0.0038  -0.0035 257 ALA B C   
6246 O O   . ALA B 257 ? 0.1204 0.0991 0.1425 -0.0160 0.0041  -0.0036 257 ALA B O   
6247 C CB  . ALA B 257 ? 0.0996 0.0773 0.1180 -0.0167 0.0027  -0.0029 257 ALA B CB  
6248 N N   . SER B 258 ? 0.1448 0.1241 0.1690 -0.0147 0.0039  -0.0035 258 SER B N   
6249 C CA  . SER B 258 ? 0.1199 0.1001 0.1456 -0.0144 0.0042  -0.0034 258 SER B CA  
6250 C C   . SER B 258 ? 0.0620 0.0420 0.0894 -0.0143 0.0053  -0.0042 258 SER B C   
6251 O O   . SER B 258 ? 0.1165 0.0961 0.1452 -0.0139 0.0058  -0.0047 258 SER B O   
6252 C CB  . SER B 258 ? 0.1731 0.1543 0.2003 -0.0135 0.0039  -0.0030 258 SER B CB  
6253 O OG  . SER B 258 ? 0.2234 0.2053 0.2517 -0.0133 0.0040  -0.0028 258 SER B OG  
6254 N N   . VAL B 259 ? 0.1042 0.0843 0.1315 -0.0148 0.0056  -0.0042 259 VAL B N   
6255 C CA  . VAL B 259 ? 0.0729 0.0529 0.1018 -0.0147 0.0067  -0.0050 259 VAL B CA  
6256 C C   . VAL B 259 ? 0.1148 0.0956 0.1445 -0.0146 0.0068  -0.0047 259 VAL B C   
6257 O O   . VAL B 259 ? 0.0707 0.0521 0.0995 -0.0149 0.0060  -0.0040 259 VAL B O   
6258 C CB  . VAL B 259 ? 0.1484 0.1275 0.1762 -0.0154 0.0072  -0.0056 259 VAL B CB  
6259 C CG1 . VAL B 259 ? 0.1720 0.1501 0.1990 -0.0154 0.0072  -0.0059 259 VAL B CG1 
6260 C CG2 . VAL B 259 ? 0.1430 0.1224 0.1688 -0.0163 0.0066  -0.0051 259 VAL B CG2 
6261 N N   . SER B 260 ? 0.1007 0.0815 0.1323 -0.0144 0.0078  -0.0054 260 SER B N   
6262 C CA  . SER B 260 ? 0.0909 0.0725 0.1236 -0.0144 0.0081  -0.0053 260 SER B CA  
6263 C C   . SER B 260 ? 0.0858 0.0669 0.1198 -0.0143 0.0093  -0.0063 260 SER B C   
6264 O O   . SER B 260 ? 0.1055 0.0859 0.1399 -0.0141 0.0098  -0.0069 260 SER B O   
6265 C CB  . SER B 260 ? 0.0928 0.0752 0.1271 -0.0135 0.0078  -0.0048 260 SER B CB  
6266 O OG  . SER B 260 ? 0.1179 0.1003 0.1542 -0.0127 0.0083  -0.0053 260 SER B OG  
6267 N N   . ASN B 261 ? 0.0821 0.0637 0.1169 -0.0145 0.0098  -0.0064 261 ASN B N   
6268 C CA  . ASN B 261 ? 0.1638 0.1450 0.2001 -0.0144 0.0110  -0.0073 261 ASN B CA  
6269 C C   . ASN B 261 ? 0.1536 0.1347 0.1920 -0.0135 0.0116  -0.0077 261 ASN B C   
6270 O O   . ASN B 261 ? 0.1324 0.1127 0.1713 -0.0134 0.0123  -0.0085 261 ASN B O   
6271 C CB  . ASN B 261 ? 0.1819 0.1637 0.2189 -0.0146 0.0114  -0.0072 261 ASN B CB  
6272 C CG  . ASN B 261 ? 0.2039 0.1858 0.2390 -0.0156 0.0110  -0.0070 261 ASN B CG  
6273 O OD1 . ASN B 261 ? 0.1659 0.1472 0.1993 -0.0162 0.0109  -0.0072 261 ASN B OD1 
6274 N ND2 . ASN B 261 ? 0.1341 0.1168 0.1692 -0.0160 0.0108  -0.0064 261 ASN B ND2 
6275 N N   . GLU B 262 ? 0.1415 0.1234 0.1811 -0.0128 0.0111  -0.0071 262 GLU B N   
6276 C CA  . GLU B 262 ? 0.1320 0.1138 0.1736 -0.0120 0.0116  -0.0075 262 GLU B CA  
6277 C C   . GLU B 262 ? 0.1487 0.1298 0.1897 -0.0119 0.0113  -0.0077 262 GLU B C   
6278 O O   . GLU B 262 ? 0.1218 0.1023 0.1640 -0.0116 0.0119  -0.0083 262 GLU B O   
6279 C CB  . GLU B 262 ? 0.0972 0.0801 0.1404 -0.0113 0.0111  -0.0068 262 GLU B CB  
6280 C CG  . GLU B 262 ? 0.1672 0.1508 0.2115 -0.0112 0.0115  -0.0067 262 GLU B CG  
6281 C CD  . GLU B 262 ? 0.2927 0.2773 0.3387 -0.0104 0.0112  -0.0061 262 GLU B CD  
6282 O OE1 . GLU B 262 ? 0.3182 0.3034 0.3646 -0.0105 0.0111  -0.0057 262 GLU B OE1 
6283 O OE2 . GLU B 262 ? 0.2452 0.2301 0.2922 -0.0098 0.0109  -0.0060 262 GLU B OE2 
6284 N N   . ALA B 263 ? 0.1009 0.0819 0.1400 -0.0122 0.0104  -0.0071 263 ALA B N   
6285 C CA  . ALA B 263 ? 0.0892 0.0695 0.1275 -0.0122 0.0101  -0.0073 263 ALA B CA  
6286 C C   . ALA B 263 ? 0.1290 0.1080 0.1666 -0.0128 0.0108  -0.0081 263 ALA B C   
6287 O O   . ALA B 263 ? 0.1020 0.0802 0.1400 -0.0126 0.0111  -0.0085 263 ALA B O   
6288 C CB  . ALA B 263 ? 0.0729 0.0533 0.1091 -0.0125 0.0089  -0.0065 263 ALA B CB  
6289 N N   . LEU B 264 ? 0.1350 0.1138 0.1713 -0.0134 0.0110  -0.0083 264 LEU B N   
6290 C CA  . LEU B 264 ? 0.1241 0.1018 0.1597 -0.0139 0.0117  -0.0091 264 LEU B CA  
6291 C C   . LEU B 264 ? 0.1371 0.1142 0.1746 -0.0136 0.0127  -0.0099 264 LEU B C   
6292 O O   . LEU B 264 ? 0.1429 0.1188 0.1803 -0.0138 0.0131  -0.0105 264 LEU B O   
6293 C CB  . LEU B 264 ? 0.1430 0.1207 0.1771 -0.0147 0.0117  -0.0091 264 LEU B CB  
6294 C CG  . LEU B 264 ? 0.1515 0.1293 0.1833 -0.0152 0.0107  -0.0084 264 LEU B CG  
6295 C CD1 . LEU B 264 ? 0.1641 0.1423 0.1948 -0.0160 0.0106  -0.0083 264 LEU B CD1 
6296 C CD2 . LEU B 264 ? 0.2153 0.1921 0.2458 -0.0155 0.0104  -0.0086 264 LEU B CD2 
6297 N N   . GLU B 265 ? 0.1623 0.1402 0.2016 -0.0132 0.0132  -0.0099 265 GLU B N   
6298 C CA  . GLU B 265 ? 0.1634 0.1409 0.2047 -0.0129 0.0141  -0.0106 265 GLU B CA  
6299 C C   . GLU B 265 ? 0.1925 0.1695 0.2346 -0.0124 0.0139  -0.0106 265 GLU B C   
6300 O O   . GLU B 265 ? 0.1216 0.0974 0.1642 -0.0124 0.0145  -0.0113 265 GLU B O   
6301 C CB  . GLU B 265 ? 0.1870 0.1655 0.2300 -0.0125 0.0145  -0.0105 265 GLU B CB  
6302 C CG  . GLU B 265 ? 0.2182 0.1970 0.2605 -0.0130 0.0149  -0.0106 265 GLU B CG  
6303 C CD  . GLU B 265 ? 0.4533 0.4313 0.4961 -0.0133 0.0160  -0.0116 265 GLU B CD  
6304 O OE1 . GLU B 265 ? 0.4570 0.4354 0.4993 -0.0138 0.0163  -0.0118 265 GLU B OE1 
6305 O OE2 . GLU B 265 ? 0.4893 0.4665 0.5331 -0.0130 0.0165  -0.0122 265 GLU B OE2 
6306 N N   . LEU B 266 ? 0.1507 0.1285 0.1931 -0.0119 0.0131  -0.0099 266 LEU B N   
6307 C CA  . LEU B 266 ? 0.1011 0.0784 0.1442 -0.0115 0.0129  -0.0099 266 LEU B CA  
6308 C C   . LEU B 266 ? 0.0774 0.0533 0.1190 -0.0120 0.0127  -0.0102 266 LEU B C   
6309 O O   . LEU B 266 ? 0.1310 0.1058 0.1732 -0.0119 0.0130  -0.0107 266 LEU B O   
6310 C CB  . LEU B 266 ? 0.1080 0.0866 0.1516 -0.0110 0.0120  -0.0090 266 LEU B CB  
6311 C CG  . LEU B 266 ? 0.1533 0.1316 0.1975 -0.0106 0.0116  -0.0089 266 LEU B CG  
6312 C CD1 . LEU B 266 ? 0.1140 0.0920 0.1603 -0.0102 0.0123  -0.0094 266 LEU B CD1 
6313 C CD2 . LEU B 266 ? 0.1352 0.1147 0.1793 -0.0102 0.0106  -0.0080 266 LEU B CD2 
6314 N N   . TYR B 267 ? 0.1084 0.0842 0.1479 -0.0125 0.0122  -0.0100 267 TYR B N   
6315 C CA  . TYR B 267 ? 0.1545 0.1289 0.1923 -0.0129 0.0120  -0.0103 267 TYR B CA  
6316 C C   . TYR B 267 ? 0.2410 0.2140 0.2790 -0.0132 0.0129  -0.0112 267 TYR B C   
6317 O O   . TYR B 267 ? 0.1195 0.0912 0.1573 -0.0133 0.0130  -0.0117 267 TYR B O   
6318 C CB  . TYR B 267 ? 0.1493 0.1239 0.1849 -0.0134 0.0113  -0.0098 267 TYR B CB  
6319 C CG  . TYR B 267 ? 0.1216 0.0970 0.1566 -0.0132 0.0103  -0.0089 267 TYR B CG  
6320 C CD1 . TYR B 267 ? 0.1221 0.0971 0.1571 -0.0129 0.0098  -0.0088 267 TYR B CD1 
6321 C CD2 . TYR B 267 ? 0.1645 0.1411 0.1990 -0.0132 0.0098  -0.0083 267 TYR B CD2 
6322 C CE1 . TYR B 267 ? 0.1591 0.1349 0.1935 -0.0127 0.0088  -0.0080 267 TYR B CE1 
6323 C CE2 . TYR B 267 ? 0.1559 0.1332 0.1897 -0.0130 0.0088  -0.0074 267 TYR B CE2 
6324 C CZ  . TYR B 267 ? 0.1543 0.1312 0.1882 -0.0127 0.0084  -0.0073 267 TYR B CZ  
6325 O OH  . TYR B 267 ? 0.1291 0.1067 0.1624 -0.0124 0.0074  -0.0066 267 TYR B OH  
6326 N N   . TYR B 268 ? 0.1735 0.1469 0.2118 -0.0134 0.0136  -0.0116 268 TYR B N   
6327 C CA  . TYR B 268 ? 0.1320 0.1041 0.1706 -0.0137 0.0145  -0.0126 268 TYR B CA  
6328 C C   . TYR B 268 ? 0.0984 0.0697 0.1387 -0.0132 0.0149  -0.0130 268 TYR B C   
6329 O O   . TYR B 268 ? 0.1314 0.1010 0.1714 -0.0134 0.0152  -0.0136 268 TYR B O   
6330 C CB  . TYR B 268 ? 0.1416 0.1145 0.1805 -0.0140 0.0151  -0.0128 268 TYR B CB  
6331 C CG  . TYR B 268 ? 0.1490 0.1208 0.1887 -0.0140 0.0162  -0.0138 268 TYR B CG  
6332 C CD1 . TYR B 268 ? 0.2068 0.1770 0.2453 -0.0145 0.0165  -0.0145 268 TYR B CD1 
6333 C CD2 . TYR B 268 ? 0.1855 0.1578 0.2272 -0.0136 0.0168  -0.0139 268 TYR B CD2 
6334 C CE1 . TYR B 268 ? 0.2450 0.2141 0.2842 -0.0146 0.0173  -0.0155 268 TYR B CE1 
6335 C CE2 . TYR B 268 ? 0.1840 0.1551 0.2264 -0.0136 0.0177  -0.0149 268 TYR B CE2 
6336 C CZ  . TYR B 268 ? 0.2983 0.2678 0.3394 -0.0141 0.0179  -0.0156 268 TYR B CZ  
6337 O OH  . TYR B 268 ? 0.4139 0.3821 0.4556 -0.0141 0.0187  -0.0166 268 TYR B OH  
6338 N N   . GLU B 269 ? 0.1345 0.1070 0.1766 -0.0127 0.0150  -0.0126 269 GLU B N   
6339 C CA  . GLU B 269 ? 0.1705 0.1423 0.2143 -0.0122 0.0154  -0.0130 269 GLU B CA  
6340 C C   . GLU B 269 ? 0.2172 0.1878 0.2606 -0.0121 0.0148  -0.0129 269 GLU B C   
6341 O O   . GLU B 269 ? 0.2023 0.1715 0.2463 -0.0120 0.0151  -0.0134 269 GLU B O   
6342 C CB  . GLU B 269 ? 0.1993 0.1727 0.2451 -0.0116 0.0155  -0.0125 269 GLU B CB  
6343 C CG  . GLU B 269 ? 0.3446 0.3187 0.3913 -0.0116 0.0163  -0.0127 269 GLU B CG  
6344 C CD  . GLU B 269 ? 0.5239 0.4999 0.5719 -0.0112 0.0161  -0.0120 269 GLU B CD  
6345 O OE1 . GLU B 269 ? 0.5794 0.5562 0.6281 -0.0107 0.0154  -0.0114 269 GLU B OE1 
6346 O OE2 . GLU B 269 ? 0.5896 0.5664 0.6379 -0.0112 0.0165  -0.0120 269 GLU B OE2 
6347 N N   . LYS B 270 ? 0.2155 0.1866 0.2578 -0.0122 0.0140  -0.0123 270 LYS B N   
6348 C CA  . LYS B 270 ? 0.1220 0.0921 0.1638 -0.0121 0.0134  -0.0122 270 LYS B CA  
6349 C C   . LYS B 270 ? 0.1280 0.0964 0.1678 -0.0127 0.0133  -0.0127 270 LYS B C   
6350 O O   . LYS B 270 ? 0.1984 0.1659 0.2374 -0.0127 0.0127  -0.0126 270 LYS B O   
6351 C CB  . LYS B 270 ? 0.1233 0.0949 0.1650 -0.0118 0.0125  -0.0113 270 LYS B CB  
6352 C CG  . LYS B 270 ? 0.1448 0.1181 0.1884 -0.0112 0.0124  -0.0108 270 LYS B CG  
6353 C CD  . LYS B 270 ? 0.2950 0.2678 0.3404 -0.0107 0.0127  -0.0110 270 LYS B CD  
6354 C CE  . LYS B 270 ? 0.3941 0.3683 0.4416 -0.0102 0.0129  -0.0107 270 LYS B CE  
6355 N NZ  . LYS B 270 ? 0.4942 0.4676 0.5433 -0.0099 0.0135  -0.0112 270 LYS B NZ  
6356 N N   . GLY B 271 ? 0.1568 0.1246 0.1959 -0.0131 0.0138  -0.0133 271 GLY B N   
6357 C CA  . GLY B 271 ? 0.1968 0.1628 0.2342 -0.0137 0.0138  -0.0138 271 GLY B CA  
6358 C C   . GLY B 271 ? 0.1915 0.1577 0.2269 -0.0141 0.0132  -0.0134 271 GLY B C   
6359 O O   . GLY B 271 ? 0.1893 0.1541 0.2234 -0.0145 0.0130  -0.0137 271 GLY B O   
6360 N N   . ILE B 272 ? 0.1621 0.1301 0.1973 -0.0141 0.0128  -0.0127 272 ILE B N   
6361 C CA  . ILE B 272 ? 0.1030 0.0712 0.1363 -0.0145 0.0122  -0.0123 272 ILE B CA  
6362 C C   . ILE B 272 ? 0.1987 0.1668 0.2311 -0.0151 0.0128  -0.0128 272 ILE B C   
6363 O O   . ILE B 272 ? 0.1777 0.1466 0.2110 -0.0151 0.0134  -0.0129 272 ILE B O   
6364 C CB  . ILE B 272 ? 0.1432 0.1131 0.1764 -0.0143 0.0115  -0.0113 272 ILE B CB  
6365 C CG1 . ILE B 272 ? 0.1865 0.1567 0.2208 -0.0137 0.0110  -0.0109 272 ILE B CG1 
6366 C CG2 . ILE B 272 ? 0.1492 0.1193 0.1802 -0.0148 0.0108  -0.0108 272 ILE B CG2 
6367 C CD1 . ILE B 272 ? 0.2247 0.1934 0.2582 -0.0138 0.0107  -0.0111 272 ILE B CD1 
6368 N N   . ASN B 273 ? 0.1281 0.0950 0.1588 -0.0156 0.0126  -0.0130 273 ASN B N   
6369 C CA  . ASN B 273 ? 0.2061 0.1728 0.2360 -0.0162 0.0132  -0.0135 273 ASN B CA  
6370 C C   . ASN B 273 ? 0.1676 0.1354 0.1960 -0.0166 0.0128  -0.0129 273 ASN B C   
6371 O O   . ASN B 273 ? 0.1865 0.1548 0.2147 -0.0170 0.0133  -0.0132 273 ASN B O   
6372 C CB  . ASN B 273 ? 0.3850 0.3498 0.4139 -0.0166 0.0133  -0.0142 273 ASN B CB  
6373 C CG  . ASN B 273 ? 0.4738 0.4371 0.5038 -0.0164 0.0139  -0.0151 273 ASN B CG  
6374 O OD1 . ASN B 273 ? 0.5769 0.5408 0.6085 -0.0160 0.0145  -0.0153 273 ASN B OD1 
6375 N ND2 . ASN B 273 ? 0.4982 0.4596 0.5275 -0.0165 0.0138  -0.0156 273 ASN B ND2 
6376 N N   . MET B 274 ? 0.1457 0.1140 0.1732 -0.0166 0.0118  -0.0121 274 MET B N   
6377 C CA  . MET B 274 ? 0.1092 0.0784 0.1353 -0.0170 0.0113  -0.0115 274 MET B CA  
6378 C C   . MET B 274 ? 0.1886 0.1588 0.2145 -0.0166 0.0103  -0.0105 274 MET B C   
6379 O O   . MET B 274 ? 0.1561 0.1258 0.1822 -0.0162 0.0099  -0.0104 274 MET B O   
6380 C CB  . MET B 274 ? 0.1640 0.1323 0.1882 -0.0176 0.0111  -0.0117 274 MET B CB  
6381 C CG  . MET B 274 ? 0.2093 0.1786 0.2320 -0.0180 0.0106  -0.0111 274 MET B CG  
6382 S SD  . MET B 274 ? 0.3883 0.3578 0.4097 -0.0179 0.0093  -0.0101 274 MET B SD  
6383 C CE  . MET B 274 ? 0.3636 0.3316 0.3836 -0.0183 0.0092  -0.0105 274 MET B CE  
6384 N N   . LEU B 275 ? 0.1155 0.0869 0.1408 -0.0167 0.0100  -0.0099 275 LEU B N   
6385 C CA  . LEU B 275 ? 0.2033 0.1754 0.2279 -0.0165 0.0089  -0.0090 275 LEU B CA  
6386 C C   . LEU B 275 ? 0.1979 0.1706 0.2208 -0.0171 0.0084  -0.0085 275 LEU B C   
6387 O O   . LEU B 275 ? 0.1837 0.1562 0.2061 -0.0176 0.0089  -0.0089 275 LEU B O   
6388 C CB  . LEU B 275 ? 0.1912 0.1644 0.2174 -0.0159 0.0088  -0.0086 275 LEU B CB  
6389 C CG  . LEU B 275 ? 0.2561 0.2301 0.2835 -0.0158 0.0095  -0.0088 275 LEU B CG  
6390 C CD1 . LEU B 275 ? 0.3380 0.3129 0.3642 -0.0163 0.0090  -0.0082 275 LEU B CD1 
6391 C CD2 . LEU B 275 ? 0.2512 0.2259 0.2808 -0.0151 0.0097  -0.0088 275 LEU B CD2 
6392 N N   . ALA B 276 ? 0.1220 0.0952 0.1439 -0.0170 0.0074  -0.0076 276 ALA B N   
6393 C CA  . ALA B 276 ? 0.2025 0.1763 0.2228 -0.0176 0.0068  -0.0070 276 ALA B CA  
6394 C C   . ALA B 276 ? 0.1428 0.1176 0.1633 -0.0173 0.0061  -0.0062 276 ALA B C   
6395 O O   . ALA B 276 ? 0.1516 0.1267 0.1731 -0.0167 0.0059  -0.0060 276 ALA B O   
6396 C CB  . ALA B 276 ? 0.1223 0.0955 0.1408 -0.0179 0.0060  -0.0067 276 ALA B CB  
6397 N N   . THR B 277 ? 0.1223 0.0977 0.1417 -0.0178 0.0056  -0.0057 277 THR B N   
6398 C CA  . THR B 277 ? 0.1220 0.0984 0.1412 -0.0177 0.0048  -0.0048 277 THR B CA  
6399 C C   . THR B 277 ? 0.1400 0.1166 0.1572 -0.0184 0.0040  -0.0042 277 THR B C   
6400 O O   . THR B 277 ? 0.2093 0.1854 0.2255 -0.0188 0.0038  -0.0043 277 THR B O   
6401 C CB  . THR B 277 ? 0.1713 0.1484 0.1922 -0.0174 0.0054  -0.0050 277 THR B CB  
6402 O OG1 . THR B 277 ? 0.1744 0.1524 0.1950 -0.0173 0.0046  -0.0042 277 THR B OG1 
6403 C CG2 . THR B 277 ? 0.1587 0.1359 0.1797 -0.0179 0.0061  -0.0055 277 THR B CG2 
6404 N N   . ASP B 278 ? 0.1079 0.0853 0.1246 -0.0186 0.0033  -0.0034 278 ASP B N   
6405 C CA  . ASP B 278 ? 0.1373 0.1151 0.1523 -0.0192 0.0022  -0.0025 278 ASP B CA  
6406 C C   . ASP B 278 ? 0.1782 0.1564 0.1931 -0.0199 0.0023  -0.0025 278 ASP B C   
6407 O O   . ASP B 278 ? 0.1343 0.1129 0.1502 -0.0199 0.0029  -0.0028 278 ASP B O   
6408 C CB  . ASP B 278 ? 0.1592 0.1374 0.1734 -0.0191 0.0013  -0.0017 278 ASP B CB  
6409 C CG  . ASP B 278 ? 0.1548 0.1332 0.1671 -0.0198 0.0001  -0.0007 278 ASP B CG  
6410 O OD1 . ASP B 278 ? 0.1869 0.1649 0.1986 -0.0198 -0.0003 -0.0007 278 ASP B OD1 
6411 O OD2 . ASP B 278 ? 0.2139 0.1932 0.2255 -0.0200 -0.0005 -0.0001 278 ASP B OD2 
6412 N N   . GLU B 279 ? 0.2000 0.1785 0.2139 -0.0204 0.0016  -0.0020 279 GLU B N   
6413 C CA  . GLU B 279 ? 0.2346 0.2137 0.2487 -0.0210 0.0018  -0.0020 279 GLU B CA  
6414 C C   . GLU B 279 ? 0.1744 0.1544 0.1885 -0.0213 0.0010  -0.0011 279 GLU B C   
6415 O O   . GLU B 279 ? 0.2379 0.2186 0.2526 -0.0217 0.0013  -0.0011 279 GLU B O   
6416 C CB  . GLU B 279 ? 0.3119 0.2910 0.3253 -0.0213 0.0016  -0.0020 279 GLU B CB  
6417 C CG  . GLU B 279 ? 0.3289 0.3088 0.3422 -0.0213 0.0004  -0.0009 279 GLU B CG  
6418 C CD  . GLU B 279 ? 0.3994 0.3796 0.4124 -0.0216 0.0008  -0.0013 279 GLU B CD  
6419 O OE1 . GLU B 279 ? 0.4229 0.4034 0.4357 -0.0221 0.0014  -0.0016 279 GLU B OE1 
6420 O OE2 . GLU B 279 ? 0.2700 0.2499 0.2826 -0.0213 0.0005  -0.0012 279 GLU B OE2 
6421 N N   . VAL B 280 ? 0.1622 0.1424 0.1758 -0.0211 0.0001  -0.0003 280 VAL B N   
6422 C CA  . VAL B 280 ? 0.1832 0.1644 0.1966 -0.0213 -0.0003 0.0004  280 VAL B CA  
6423 C C   . VAL B 280 ? 0.1809 0.1620 0.1956 -0.0213 0.0007  -0.0003 280 VAL B C   
6424 O O   . VAL B 280 ? 0.1813 0.1632 0.1964 -0.0218 0.0007  0.0000  280 VAL B O   
6425 C CB  . VAL B 280 ? 0.2429 0.2244 0.2548 -0.0208 -0.0009 0.0009  280 VAL B CB  
6426 C CG1 . VAL B 280 ? 0.2359 0.2181 0.2472 -0.0211 -0.0008 0.0012  280 VAL B CG1 
6427 C CG2 . VAL B 280 ? 0.2463 0.2284 0.2574 -0.0205 -0.0021 0.0017  280 VAL B CG2 
6428 N N   . ILE B 281 ? 0.1429 0.1233 0.1586 -0.0205 0.0018  -0.0012 281 ILE B N   
6429 C CA  . ILE B 281 ? 0.1504 0.1310 0.1679 -0.0201 0.0029  -0.0019 281 ILE B CA  
6430 C C   . ILE B 281 ? 0.1386 0.1193 0.1565 -0.0207 0.0035  -0.0024 281 ILE B C   
6431 O O   . ILE B 281 ? 0.1655 0.1468 0.1843 -0.0209 0.0039  -0.0025 281 ILE B O   
6432 C CB  . ILE B 281 ? 0.1946 0.1746 0.2135 -0.0192 0.0037  -0.0028 281 ILE B CB  
6433 C CG1 . ILE B 281 ? 0.2839 0.2640 0.3027 -0.0186 0.0031  -0.0023 281 ILE B CG1 
6434 C CG2 . ILE B 281 ? 0.2296 0.2097 0.2506 -0.0188 0.0049  -0.0035 281 ILE B CG2 
6435 C CD1 . ILE B 281 ? 0.3150 0.2958 0.3335 -0.0186 0.0025  -0.0015 281 ILE B CD1 
6436 N N   . LEU B 282 ? 0.1121 0.0923 0.1294 -0.0210 0.0037  -0.0028 282 LEU B N   
6437 C CA  . LEU B 282 ? 0.1207 0.1011 0.1382 -0.0215 0.0045  -0.0034 282 LEU B CA  
6438 C C   . LEU B 282 ? 0.1799 0.1614 0.1970 -0.0223 0.0037  -0.0025 282 LEU B C   
6439 O O   . LEU B 282 ? 0.2133 0.1953 0.2310 -0.0227 0.0042  -0.0027 282 LEU B O   
6440 C CB  . LEU B 282 ? 0.1894 0.1691 0.2062 -0.0216 0.0048  -0.0040 282 LEU B CB  
6441 C CG  . LEU B 282 ? 0.1992 0.1790 0.2159 -0.0222 0.0057  -0.0048 282 LEU B CG  
6442 C CD1 . LEU B 282 ? 0.1729 0.1523 0.1910 -0.0219 0.0070  -0.0058 282 LEU B CD1 
6443 C CD2 . LEU B 282 ? 0.2004 0.1795 0.2161 -0.0224 0.0059  -0.0052 282 LEU B CD2 
6444 N N   . LYS B 283 ? 0.1499 0.1318 0.1660 -0.0225 0.0024  -0.0015 283 LYS B N   
6445 C CA  . LYS B 283 ? 0.1769 0.1601 0.1933 -0.0231 0.0016  -0.0005 283 LYS B CA  
6446 C C   . LYS B 283 ? 0.1697 0.1535 0.1866 -0.0233 0.0014  0.0000  283 LYS B C   
6447 O O   . LYS B 283 ? 0.1639 0.1487 0.1814 -0.0239 0.0013  0.0004  283 LYS B O   
6448 C CB  . LYS B 283 ? 0.1939 0.1775 0.2101 -0.0230 0.0003  0.0005  283 LYS B CB  
6449 C CG  . LYS B 283 ? 0.4042 0.3878 0.4201 -0.0230 0.0006  0.0001  283 LYS B CG  
6450 C CD  . LYS B 283 ? 0.4253 0.4094 0.4415 -0.0223 0.0000  0.0007  283 LYS B CD  
6451 C CE  . LYS B 283 ? 0.5987 0.5830 0.6142 -0.0227 0.0006  0.0002  283 LYS B CE  
6452 N NZ  . LYS B 283 ? 0.6297 0.6137 0.6447 -0.0221 0.0004  0.0002  283 LYS B NZ  
6453 N N   . ASN B 284 ? 0.1750 0.1583 0.1918 -0.0228 0.0014  0.0000  284 ASN B N   
6454 C CA  . ASN B 284 ? 0.1674 0.1514 0.1847 -0.0229 0.0015  0.0003  284 ASN B CA  
6455 C C   . ASN B 284 ? 0.2178 0.2018 0.2366 -0.0228 0.0028  -0.0007 284 ASN B C   
6456 O O   . ASN B 284 ? 0.2098 0.1945 0.2292 -0.0230 0.0028  -0.0003 284 ASN B O   
6457 C CB  . ASN B 284 ? 0.1284 0.1119 0.1453 -0.0222 0.0014  0.0003  284 ASN B CB  
6458 C CG  . ASN B 284 ? 0.2268 0.2106 0.2418 -0.0224 0.0003  0.0012  284 ASN B CG  
6459 O OD1 . ASN B 284 ? 0.2576 0.2424 0.2716 -0.0226 -0.0006 0.0020  284 ASN B OD1 
6460 N ND2 . ASN B 284 ? 0.2118 0.1951 0.2264 -0.0218 0.0005  0.0010  284 ASN B ND2 
6461 N N   . SER B 285 ? 0.2013 0.1844 0.2206 -0.0224 0.0039  -0.0018 285 SER B N   
6462 C CA  . SER B 285 ? 0.1605 0.1436 0.1815 -0.0221 0.0052  -0.0029 285 SER B CA  
6463 C C   . SER B 285 ? 0.1964 0.1798 0.2174 -0.0229 0.0058  -0.0034 285 SER B C   
6464 O O   . SER B 285 ? 0.3106 0.2944 0.3327 -0.0229 0.0066  -0.0038 285 SER B O   
6465 C CB  . SER B 285 ? 0.1664 0.1483 0.1881 -0.0212 0.0062  -0.0040 285 SER B CB  
6466 O OG  . SER B 285 ? 0.1944 0.1761 0.2164 -0.0204 0.0058  -0.0036 285 SER B OG  
6467 N N   . VAL B 286 ? 0.1651 0.1484 0.1849 -0.0234 0.0055  -0.0033 286 VAL B N   
6468 C CA  . VAL B 286 ? 0.2315 0.2152 0.2512 -0.0240 0.0063  -0.0039 286 VAL B CA  
6469 C C   . VAL B 286 ? 0.2689 0.2536 0.2877 -0.0248 0.0052  -0.0029 286 VAL B C   
6470 O O   . VAL B 286 ? 0.2197 0.2044 0.2378 -0.0247 0.0041  -0.0020 286 VAL B O   
6471 C CB  . VAL B 286 ? 0.2809 0.2635 0.3004 -0.0237 0.0074  -0.0053 286 VAL B CB  
6472 C CG1 . VAL B 286 ? 0.3076 0.2892 0.3284 -0.0228 0.0082  -0.0061 286 VAL B CG1 
6473 C CG2 . VAL B 286 ? 0.3190 0.3011 0.3371 -0.0238 0.0068  -0.0050 286 VAL B CG2 
6474 N N   . GLU B 287 ? 0.3147 0.3002 0.3335 -0.0256 0.0057  -0.0032 287 GLU B N   
6475 C CA  . GLU B 287 ? 0.2321 0.2187 0.2503 -0.0263 0.0049  -0.0024 287 GLU B CA  
6476 C C   . GLU B 287 ? 0.2350 0.2209 0.2519 -0.0262 0.0051  -0.0029 287 GLU B C   
6477 O O   . GLU B 287 ? 0.2805 0.2665 0.2969 -0.0260 0.0042  -0.0021 287 GLU B O   
6478 C CB  . GLU B 287 ? 0.3006 0.2885 0.3194 -0.0271 0.0054  -0.0025 287 GLU B CB  
6479 C CG  . GLU B 287 ? 0.2159 0.2050 0.2361 -0.0273 0.0051  -0.0017 287 GLU B CG  
6480 C CD  . GLU B 287 ? 0.4734 0.4641 0.4942 -0.0282 0.0056  -0.0018 287 GLU B CD  
6481 O OE1 . GLU B 287 ? 0.5284 0.5195 0.5484 -0.0288 0.0060  -0.0022 287 GLU B OE1 
6482 O OE2 . GLU B 287 ? 0.5497 0.5413 0.5718 -0.0284 0.0056  -0.0013 287 GLU B OE2 
6483 N N   . ARG B 288 ? 0.2291 0.2142 0.2454 -0.0263 0.0062  -0.0041 288 ARG B N   
6484 C CA  . ARG B 288 ? 0.2926 0.2771 0.3076 -0.0264 0.0065  -0.0046 288 ARG B CA  
6485 C C   . ARG B 288 ? 0.2223 0.2053 0.2372 -0.0256 0.0065  -0.0050 288 ARG B C   
6486 O O   . ARG B 288 ? 0.3501 0.3322 0.3652 -0.0253 0.0076  -0.0061 288 ARG B O   
6487 C CB  . ARG B 288 ? 0.3151 0.2998 0.3296 -0.0271 0.0076  -0.0057 288 ARG B CB  
6488 C CG  . ARG B 288 ? 0.3100 0.2963 0.3242 -0.0280 0.0073  -0.0052 288 ARG B CG  
6489 C CD  . ARG B 288 ? 0.3826 0.3691 0.3963 -0.0287 0.0085  -0.0063 288 ARG B CD  
6490 N NE  . ARG B 288 ? 0.4561 0.4427 0.4713 -0.0286 0.0092  -0.0069 288 ARG B NE  
6491 C CZ  . ARG B 288 ? 0.5586 0.5441 0.5741 -0.0284 0.0104  -0.0082 288 ARG B CZ  
6492 N NH1 . ARG B 288 ? 0.5907 0.5751 0.6052 -0.0282 0.0109  -0.0090 288 ARG B NH1 
6493 N NH2 . ARG B 288 ? 0.6800 0.6657 0.6969 -0.0283 0.0111  -0.0088 288 ARG B NH2 
6494 N N   . ALA B 289 ? 0.3115 0.2944 0.3261 -0.0251 0.0055  -0.0041 289 ALA B N   
6495 C CA  . ALA B 289 ? 0.2981 0.2800 0.3128 -0.0243 0.0053  -0.0042 289 ALA B CA  
6496 C C   . ALA B 289 ? 0.2149 0.1960 0.2285 -0.0242 0.0053  -0.0045 289 ALA B C   
6497 O O   . ALA B 289 ? 0.3048 0.2858 0.3179 -0.0239 0.0044  -0.0037 289 ALA B O   
6498 C CB  . ALA B 289 ? 0.3051 0.2874 0.3203 -0.0239 0.0041  -0.0030 289 ALA B CB  
6499 N N   . SER B 290 ? 0.1979 0.1784 0.2111 -0.0245 0.0064  -0.0055 290 SER B N   
6500 C CA  . SER B 290 ? 0.1673 0.1470 0.1794 -0.0244 0.0065  -0.0059 290 SER B CA  
6501 C C   . SER B 290 ? 0.1259 0.1045 0.1386 -0.0236 0.0066  -0.0062 290 SER B C   
6502 O O   . SER B 290 ? 0.1603 0.1383 0.1738 -0.0234 0.0076  -0.0070 290 SER B O   
6503 C CB  . SER B 290 ? 0.1876 0.1671 0.1988 -0.0250 0.0075  -0.0068 290 SER B CB  
6504 O OG  . SER B 290 ? 0.1695 0.1483 0.1797 -0.0249 0.0075  -0.0070 290 SER B OG  
6505 N N   . PRO B 291 ? 0.1494 0.1277 0.1616 -0.0232 0.0058  -0.0056 291 PRO B N   
6506 C CA  . PRO B 291 ? 0.1704 0.1476 0.1830 -0.0226 0.0059  -0.0059 291 PRO B CA  
6507 C C   . PRO B 291 ? 0.1564 0.1326 0.1685 -0.0227 0.0067  -0.0068 291 PRO B C   
6508 O O   . PRO B 291 ? 0.1600 0.1354 0.1723 -0.0222 0.0067  -0.0070 291 PRO B O   
6509 C CB  . PRO B 291 ? 0.1604 0.1378 0.1726 -0.0222 0.0046  -0.0048 291 PRO B CB  
6510 C CG  . PRO B 291 ? 0.1906 0.1688 0.2018 -0.0227 0.0042  -0.0044 291 PRO B CG  
6511 C CD  . PRO B 291 ? 0.1940 0.1728 0.2053 -0.0233 0.0048  -0.0047 291 PRO B CD  
6512 N N   . TYR B 292 ? 0.1868 0.1631 0.1981 -0.0233 0.0074  -0.0074 292 TYR B N   
6513 C CA  . TYR B 292 ? 0.1839 0.1592 0.1945 -0.0234 0.0081  -0.0081 292 TYR B CA  
6514 C C   . TYR B 292 ? 0.1564 0.1311 0.1679 -0.0235 0.0093  -0.0093 292 TYR B C   
6515 O O   . TYR B 292 ? 0.1804 0.1542 0.1914 -0.0237 0.0100  -0.0100 292 TYR B O   
6516 C CB  . TYR B 292 ? 0.1699 0.1456 0.1790 -0.0241 0.0080  -0.0081 292 TYR B CB  
6517 C CG  . TYR B 292 ? 0.1630 0.1394 0.1713 -0.0240 0.0069  -0.0070 292 TYR B CG  
6518 C CD1 . TYR B 292 ? 0.2163 0.1922 0.2247 -0.0234 0.0061  -0.0064 292 TYR B CD1 
6519 C CD2 . TYR B 292 ? 0.2605 0.2379 0.2680 -0.0245 0.0065  -0.0065 292 TYR B CD2 
6520 C CE1 . TYR B 292 ? 0.2108 0.1874 0.2188 -0.0232 0.0050  -0.0055 292 TYR B CE1 
6521 C CE2 . TYR B 292 ? 0.2129 0.1909 0.2198 -0.0243 0.0055  -0.0056 292 TYR B CE2 
6522 C CZ  . TYR B 292 ? 0.2122 0.1898 0.2195 -0.0236 0.0048  -0.0051 292 TYR B CZ  
6523 O OH  . TYR B 292 ? 0.2981 0.2763 0.3049 -0.0234 0.0039  -0.0043 292 TYR B OH  
6524 N N   . LEU B 293 ? 0.1547 0.1297 0.1675 -0.0233 0.0097  -0.0095 293 LEU B N   
6525 C CA  . LEU B 293 ? 0.1427 0.1172 0.1566 -0.0232 0.0109  -0.0105 293 LEU B CA  
6526 C C   . LEU B 293 ? 0.1728 0.1465 0.1881 -0.0224 0.0109  -0.0106 293 LEU B C   
6527 O O   . LEU B 293 ? 0.1686 0.1427 0.1842 -0.0219 0.0100  -0.0098 293 LEU B O   
6528 C CB  . LEU B 293 ? 0.1702 0.1456 0.1849 -0.0235 0.0114  -0.0108 293 LEU B CB  
6529 C CG  . LEU B 293 ? 0.2401 0.2162 0.2538 -0.0244 0.0118  -0.0111 293 LEU B CG  
6530 C CD1 . LEU B 293 ? 0.2428 0.2195 0.2550 -0.0248 0.0108  -0.0102 293 LEU B CD1 
6531 C CD2 . LEU B 293 ? 0.2551 0.2322 0.2699 -0.0245 0.0121  -0.0112 293 LEU B CD2 
6532 N N   . ARG B 294 ? 0.1554 0.1283 0.1715 -0.0223 0.0119  -0.0116 294 ARG B N   
6533 C CA  . ARG B 294 ? 0.1459 0.1183 0.1637 -0.0216 0.0121  -0.0119 294 ARG B CA  
6534 C C   . ARG B 294 ? 0.2199 0.1931 0.2391 -0.0215 0.0127  -0.0121 294 ARG B C   
6535 O O   . ARG B 294 ? 0.2011 0.1745 0.2203 -0.0219 0.0134  -0.0127 294 ARG B O   
6536 C CB  . ARG B 294 ? 0.1413 0.1123 0.1594 -0.0215 0.0129  -0.0128 294 ARG B CB  
6537 C CG  . ARG B 294 ? 0.1925 0.1628 0.2123 -0.0208 0.0131  -0.0131 294 ARG B CG  
6538 C CD  . ARG B 294 ? 0.1868 0.1556 0.2067 -0.0207 0.0134  -0.0138 294 ARG B CD  
6539 N NE  . ARG B 294 ? 0.2118 0.1800 0.2315 -0.0212 0.0144  -0.0148 294 ARG B NE  
6540 C CZ  . ARG B 294 ? 0.2341 0.2015 0.2527 -0.0217 0.0145  -0.0152 294 ARG B CZ  
6541 N NH1 . ARG B 294 ? 0.2147 0.1816 0.2321 -0.0217 0.0138  -0.0147 294 ARG B NH1 
6542 N NH2 . ARG B 294 ? 0.2446 0.2116 0.2632 -0.0221 0.0154  -0.0162 294 ARG B NH2 
6543 N N   . TYR B 295 ? 0.1622 0.1358 0.1824 -0.0209 0.0122  -0.0115 295 TYR B N   
6544 C CA  . TYR B 295 ? 0.1275 0.1018 0.1490 -0.0207 0.0127  -0.0116 295 TYR B CA  
6545 C C   . TYR B 295 ? 0.1744 0.1481 0.1978 -0.0200 0.0134  -0.0123 295 TYR B C   
6546 O O   . TYR B 295 ? 0.1908 0.1638 0.2145 -0.0196 0.0132  -0.0123 295 TYR B O   
6547 C CB  . TYR B 295 ? 0.1360 0.1115 0.1575 -0.0206 0.0117  -0.0105 295 TYR B CB  
6548 C CG  . TYR B 295 ? 0.1556 0.1318 0.1755 -0.0213 0.0110  -0.0099 295 TYR B CG  
6549 C CD1 . TYR B 295 ? 0.1805 0.1564 0.1987 -0.0215 0.0102  -0.0093 295 TYR B CD1 
6550 C CD2 . TYR B 295 ? 0.1638 0.1409 0.1838 -0.0218 0.0112  -0.0098 295 TYR B CD2 
6551 C CE1 . TYR B 295 ? 0.1751 0.1518 0.1920 -0.0222 0.0096  -0.0087 295 TYR B CE1 
6552 C CE2 . TYR B 295 ? 0.1824 0.1602 0.2009 -0.0225 0.0105  -0.0092 295 TYR B CE2 
6553 C CZ  . TYR B 295 ? 0.1716 0.1492 0.1887 -0.0227 0.0097  -0.0087 295 TYR B CZ  
6554 O OH  . TYR B 295 ? 0.1802 0.1587 0.1961 -0.0234 0.0091  -0.0080 295 TYR B OH  
6555 N N   . TYR B 296 ? 0.1552 0.1293 0.1798 -0.0200 0.0143  -0.0128 296 TYR B N   
6556 C CA  . TYR B 296 ? 0.1535 0.1271 0.1801 -0.0194 0.0150  -0.0134 296 TYR B CA  
6557 C C   . TYR B 296 ? 0.1872 0.1620 0.2151 -0.0190 0.0149  -0.0130 296 TYR B C   
6558 O O   . TYR B 296 ? 0.1909 0.1664 0.2190 -0.0194 0.0153  -0.0131 296 TYR B O   
6559 C CB  . TYR B 296 ? 0.1645 0.1374 0.1915 -0.0197 0.0162  -0.0147 296 TYR B CB  
6560 C CG  . TYR B 296 ? 0.2550 0.2267 0.2807 -0.0201 0.0163  -0.0152 296 TYR B CG  
6561 C CD1 . TYR B 296 ? 0.2454 0.2160 0.2708 -0.0198 0.0159  -0.0151 296 TYR B CD1 
6562 C CD2 . TYR B 296 ? 0.3046 0.2764 0.3293 -0.0209 0.0167  -0.0157 296 TYR B CD2 
6563 C CE1 . TYR B 296 ? 0.2369 0.2065 0.2612 -0.0202 0.0159  -0.0155 296 TYR B CE1 
6564 C CE2 . TYR B 296 ? 0.1837 0.1545 0.2072 -0.0213 0.0168  -0.0162 296 TYR B CE2 
6565 C CZ  . TYR B 296 ? 0.2531 0.2227 0.2764 -0.0209 0.0164  -0.0161 296 TYR B CZ  
6566 O OH  . TYR B 296 ? 0.2457 0.2142 0.2678 -0.0213 0.0165  -0.0165 296 TYR B OH  
6567 N N   . PHE B 297 ? 0.1735 0.1483 0.2023 -0.0183 0.0145  -0.0124 297 PHE B N   
6568 C CA  . PHE B 297 ? 0.1228 0.0987 0.1530 -0.0179 0.0144  -0.0120 297 PHE B CA  
6569 C C   . PHE B 297 ? 0.1480 0.1236 0.1801 -0.0176 0.0155  -0.0129 297 PHE B C   
6570 O O   . PHE B 297 ? 0.1202 0.0951 0.1535 -0.0170 0.0159  -0.0133 297 PHE B O   
6571 C CB  . PHE B 297 ? 0.1829 0.1590 0.2134 -0.0173 0.0135  -0.0112 297 PHE B CB  
6572 C CG  . PHE B 297 ? 0.1231 0.1002 0.1550 -0.0168 0.0134  -0.0107 297 PHE B CG  
6573 C CD1 . PHE B 297 ? 0.1597 0.1378 0.1909 -0.0172 0.0128  -0.0099 297 PHE B CD1 
6574 C CD2 . PHE B 297 ? 0.1482 0.1253 0.1822 -0.0161 0.0140  -0.0110 297 PHE B CD2 
6575 C CE1 . PHE B 297 ? 0.1673 0.1463 0.1998 -0.0167 0.0127  -0.0095 297 PHE B CE1 
6576 C CE2 . PHE B 297 ? 0.1785 0.1565 0.2139 -0.0156 0.0139  -0.0105 297 PHE B CE2 
6577 C CZ  . PHE B 297 ? 0.1636 0.1426 0.1983 -0.0159 0.0133  -0.0098 297 PHE B CZ  
6578 N N   . ARG B 298 ? 0.1724 0.1487 0.2049 -0.0179 0.0161  -0.0131 298 ARG B N   
6579 C CA  . ARG B 298 ? 0.2030 0.1791 0.2374 -0.0176 0.0172  -0.0139 298 ARG B CA  
6580 C C   . ARG B 298 ? 0.1687 0.1435 0.2035 -0.0175 0.0180  -0.0150 298 ARG B C   
6581 O O   . ARG B 298 ? 0.1587 0.1330 0.1950 -0.0171 0.0187  -0.0156 298 ARG B O   
6582 C CB  . ARG B 298 ? 0.2148 0.1915 0.2510 -0.0167 0.0171  -0.0135 298 ARG B CB  
6583 C CG  . ARG B 298 ? 0.1317 0.1097 0.1678 -0.0168 0.0164  -0.0125 298 ARG B CG  
6584 C CD  . ARG B 298 ? 0.2728 0.2514 0.3108 -0.0160 0.0163  -0.0120 298 ARG B CD  
6585 N NE  . ARG B 298 ? 0.2805 0.2602 0.3179 -0.0162 0.0154  -0.0110 298 ARG B NE  
6586 C CZ  . ARG B 298 ? 0.2724 0.2529 0.3110 -0.0156 0.0149  -0.0103 298 ARG B CZ  
6587 N NH1 . ARG B 298 ? 0.3341 0.3144 0.3745 -0.0147 0.0153  -0.0105 298 ARG B NH1 
6588 N NH2 . ARG B 298 ? 0.2783 0.2596 0.3160 -0.0159 0.0140  -0.0093 298 ARG B NH2 
6589 N N   . GLU B 299 ? 0.1759 0.1499 0.2090 -0.0180 0.0178  -0.0152 299 GLU B N   
6590 C CA  . GLU B 299 ? 0.1799 0.1524 0.2129 -0.0181 0.0183  -0.0161 299 GLU B CA  
6591 C C   . GLU B 299 ? 0.2606 0.2321 0.2947 -0.0174 0.0181  -0.0160 299 GLU B C   
6592 O O   . GLU B 299 ? 0.2231 0.1933 0.2576 -0.0172 0.0186  -0.0168 299 GLU B O   
6593 C CB  . GLU B 299 ? 0.2947 0.2667 0.3285 -0.0183 0.0194  -0.0172 299 GLU B CB  
6594 C CG  . GLU B 299 ? 0.2874 0.2605 0.3205 -0.0190 0.0197  -0.0174 299 GLU B CG  
6595 C CD  . GLU B 299 ? 0.3709 0.3436 0.4020 -0.0198 0.0196  -0.0177 299 GLU B CD  
6596 O OE1 . GLU B 299 ? 0.4694 0.4426 0.5001 -0.0204 0.0201  -0.0182 299 GLU B OE1 
6597 O OE2 . GLU B 299 ? 0.3428 0.3147 0.3729 -0.0197 0.0190  -0.0174 299 GLU B OE2 
6598 N N   . LEU B 300 ? 0.2162 0.1886 0.2507 -0.0169 0.0174  -0.0151 300 LEU B N   
6599 C CA  . LEU B 300 ? 0.1854 0.1570 0.2208 -0.0162 0.0171  -0.0150 300 LEU B CA  
6600 C C   . LEU B 300 ? 0.2399 0.2109 0.2740 -0.0163 0.0163  -0.0145 300 LEU B C   
6601 O O   . LEU B 300 ? 0.2407 0.2105 0.2751 -0.0161 0.0162  -0.0148 300 LEU B O   
6602 C CB  . LEU B 300 ? 0.2405 0.2134 0.2774 -0.0156 0.0169  -0.0143 300 LEU B CB  
6603 C CG  . LEU B 300 ? 0.2105 0.1842 0.2491 -0.0154 0.0177  -0.0146 300 LEU B CG  
6604 C CD1 . LEU B 300 ? 0.1789 0.1538 0.2188 -0.0148 0.0173  -0.0137 300 LEU B CD1 
6605 C CD2 . LEU B 300 ? 0.2636 0.2360 0.3033 -0.0152 0.0186  -0.0156 300 LEU B CD2 
6606 N N   . ILE B 301 ? 0.1578 0.1296 0.1904 -0.0166 0.0155  -0.0139 301 ILE B N   
6607 C CA  . ILE B 301 ? 0.1110 0.0824 0.1424 -0.0166 0.0146  -0.0133 301 ILE B CA  
6608 C C   . ILE B 301 ? 0.1536 0.1254 0.1830 -0.0173 0.0141  -0.0129 301 ILE B C   
6609 O O   . ILE B 301 ? 0.1921 0.1649 0.2212 -0.0176 0.0141  -0.0127 301 ILE B O   
6610 C CB  . ILE B 301 ? 0.1181 0.0903 0.1504 -0.0160 0.0140  -0.0125 301 ILE B CB  
6611 C CG1 . ILE B 301 ? 0.1419 0.1137 0.1730 -0.0159 0.0130  -0.0119 301 ILE B CG1 
6612 C CG2 . ILE B 301 ? 0.2042 0.1780 0.2367 -0.0159 0.0137  -0.0118 301 ILE B CG2 
6613 C CD1 . ILE B 301 ? 0.1918 0.1644 0.2239 -0.0153 0.0124  -0.0112 301 ILE B CD1 
6614 N N   . SER B 302 ? 0.1497 0.1206 0.1777 -0.0176 0.0137  -0.0129 302 SER B N   
6615 C CA  . SER B 302 ? 0.1665 0.1376 0.1925 -0.0182 0.0132  -0.0126 302 SER B CA  
6616 C C   . SER B 302 ? 0.1495 0.1214 0.1747 -0.0180 0.0121  -0.0115 302 SER B C   
6617 O O   . SER B 302 ? 0.1281 0.1000 0.1538 -0.0175 0.0116  -0.0110 302 SER B O   
6618 C CB  . SER B 302 ? 0.2726 0.2424 0.2974 -0.0185 0.0132  -0.0130 302 SER B CB  
6619 O OG  . SER B 302 ? 0.2573 0.2261 0.2826 -0.0188 0.0142  -0.0141 302 SER B OG  
6620 N N   . VAL B 303 ? 0.1884 0.1612 0.2125 -0.0185 0.0117  -0.0110 303 VAL B N   
6621 C CA  . VAL B 303 ? 0.1635 0.1370 0.1866 -0.0184 0.0106  -0.0099 303 VAL B CA  
6622 C C   . VAL B 303 ? 0.2085 0.1820 0.2296 -0.0191 0.0100  -0.0096 303 VAL B C   
6623 O O   . VAL B 303 ? 0.1714 0.1451 0.1919 -0.0197 0.0104  -0.0099 303 VAL B O   
6624 C CB  . VAL B 303 ? 0.1485 0.1232 0.1724 -0.0183 0.0104  -0.0094 303 VAL B CB  
6625 C CG1 . VAL B 303 ? 0.1523 0.1277 0.1752 -0.0183 0.0092  -0.0083 303 VAL B CG1 
6626 C CG2 . VAL B 303 ? 0.1266 0.1015 0.1527 -0.0176 0.0111  -0.0098 303 VAL B CG2 
6627 N N   . PHE B 304 ? 0.1055 0.0788 0.1256 -0.0190 0.0091  -0.0090 304 PHE B N   
6628 C CA  . PHE B 304 ? 0.0997 0.0732 0.1179 -0.0196 0.0084  -0.0084 304 PHE B CA  
6629 C C   . PHE B 304 ? 0.1348 0.1092 0.1526 -0.0195 0.0072  -0.0073 304 PHE B C   
6630 O O   . PHE B 304 ? 0.1261 0.1006 0.1445 -0.0189 0.0069  -0.0069 304 PHE B O   
6631 C CB  . PHE B 304 ? 0.1081 0.0806 0.1253 -0.0197 0.0081  -0.0085 304 PHE B CB  
6632 C CG  . PHE B 304 ? 0.1381 0.1097 0.1552 -0.0200 0.0090  -0.0095 304 PHE B CG  
6633 C CD1 . PHE B 304 ? 0.1157 0.0875 0.1316 -0.0207 0.0092  -0.0096 304 PHE B CD1 
6634 C CD2 . PHE B 304 ? 0.1404 0.1109 0.1585 -0.0198 0.0097  -0.0102 304 PHE B CD2 
6635 C CE1 . PHE B 304 ? 0.1933 0.1643 0.2091 -0.0211 0.0101  -0.0105 304 PHE B CE1 
6636 C CE2 . PHE B 304 ? 0.2155 0.1851 0.2333 -0.0201 0.0105  -0.0111 304 PHE B CE2 
6637 C CZ  . PHE B 304 ? 0.1498 0.1197 0.1665 -0.0208 0.0107  -0.0113 304 PHE B CZ  
6638 N N   . PHE B 305 ? 0.0911 0.0661 0.1077 -0.0200 0.0067  -0.0068 305 PHE B N   
6639 C CA  . PHE B 305 ? 0.1342 0.1101 0.1502 -0.0201 0.0055  -0.0057 305 PHE B CA  
6640 C C   . PHE B 305 ? 0.1007 0.0762 0.1151 -0.0203 0.0047  -0.0052 305 PHE B C   
6641 O O   . PHE B 305 ? 0.1410 0.1164 0.1547 -0.0207 0.0049  -0.0055 305 PHE B O   
6642 C CB  . PHE B 305 ? 0.1450 0.1217 0.1609 -0.0206 0.0055  -0.0054 305 PHE B CB  
6643 C CG  . PHE B 305 ? 0.1591 0.1361 0.1766 -0.0203 0.0063  -0.0059 305 PHE B CG  
6644 C CD1 . PHE B 305 ? 0.1589 0.1357 0.1772 -0.0205 0.0076  -0.0069 305 PHE B CD1 
6645 C CD2 . PHE B 305 ? 0.1651 0.1427 0.1833 -0.0199 0.0059  -0.0054 305 PHE B CD2 
6646 C CE1 . PHE B 305 ? 0.1506 0.1276 0.1704 -0.0202 0.0083  -0.0074 305 PHE B CE1 
6647 C CE2 . PHE B 305 ? 0.1245 0.1025 0.1444 -0.0196 0.0067  -0.0058 305 PHE B CE2 
6648 C CZ  . PHE B 305 ? 0.1589 0.1365 0.1796 -0.0198 0.0079  -0.0068 305 PHE B CZ  
6649 N N   . ARG B 306 ? 0.0953 0.0708 0.1094 -0.0199 0.0038  -0.0045 306 ARG B N   
6650 C CA  . ARG B 306 ? 0.0746 0.0499 0.0876 -0.0200 0.0030  -0.0041 306 ARG B CA  
6651 C C   . ARG B 306 ? 0.1499 0.1260 0.1621 -0.0205 0.0023  -0.0034 306 ARG B C   
6652 O O   . ARG B 306 ? 0.1765 0.1534 0.1889 -0.0206 0.0020  -0.0029 306 ARG B O   
6653 C CB  . ARG B 306 ? 0.1099 0.0850 0.1226 -0.0195 0.0021  -0.0035 306 ARG B CB  
6654 C CG  . ARG B 306 ? 0.1331 0.1091 0.1455 -0.0195 0.0012  -0.0025 306 ARG B CG  
6655 C CD  . ARG B 306 ? 0.1927 0.1686 0.2044 -0.0192 0.0004  -0.0020 306 ARG B CD  
6656 N NE  . ARG B 306 ? 0.1965 0.1731 0.2075 -0.0193 -0.0005 -0.0011 306 ARG B NE  
6657 C CZ  . ARG B 306 ? 0.1396 0.1167 0.1493 -0.0190 -0.0011 -0.0005 306 ARG B CZ  
6658 N NH1 . ARG B 306 ? 0.1048 0.0814 0.1138 -0.0187 -0.0013 -0.0005 306 ARG B NH1 
6659 N NH2 . ARG B 306 ? 0.1366 0.1147 0.1453 -0.0190 -0.0015 0.0001  306 ARG B NH2 
6660 N N   . ASP B 307 ? 0.0794 0.0554 0.0909 -0.0206 0.0021  -0.0034 307 ASP B N   
6661 C CA  . ASP B 307 ? 0.1334 0.1103 0.1445 -0.0209 0.0015  -0.0027 307 ASP B CA  
6662 C C   . ASP B 307 ? 0.1358 0.1133 0.1473 -0.0204 0.0002  -0.0017 307 ASP B C   
6663 O O   . ASP B 307 ? 0.1373 0.1145 0.1486 -0.0200 -0.0003 -0.0015 307 ASP B O   
6664 C CB  . ASP B 307 ? 0.1474 0.1240 0.1575 -0.0211 0.0019  -0.0031 307 ASP B CB  
6665 C CG  . ASP B 307 ? 0.1972 0.1748 0.2068 -0.0214 0.0017  -0.0028 307 ASP B CG  
6666 O OD1 . ASP B 307 ? 0.1484 0.1269 0.1585 -0.0210 0.0009  -0.0020 307 ASP B OD1 
6667 O OD2 . ASP B 307 ? 0.2609 0.2385 0.2695 -0.0220 0.0024  -0.0033 307 ASP B OD2 
6668 N N   . LYS B 308 ? 0.1143 0.0928 0.1264 -0.0204 -0.0003 -0.0011 308 LYS B N   
6669 C CA  . LYS B 308 ? 0.1732 0.1526 0.1857 -0.0196 -0.0013 -0.0002 308 LYS B CA  
6670 C C   . LYS B 308 ? 0.1587 0.1390 0.1719 -0.0190 -0.0013 -0.0001 308 LYS B C   
6671 O O   . LYS B 308 ? 0.1689 0.1496 0.1826 -0.0182 -0.0016 0.0001  308 LYS B O   
6672 C CB  . LYS B 308 ? 0.1700 0.1504 0.1830 -0.0195 -0.0015 0.0003  308 LYS B CB  
6673 C CG  . LYS B 308 ? 0.1772 0.1589 0.1913 -0.0184 -0.0023 0.0010  308 LYS B CG  
6674 C CD  . LYS B 308 ? 0.2940 0.2770 0.3096 -0.0183 -0.0022 0.0013  308 LYS B CD  
6675 C CE  . LYS B 308 ? 0.2594 0.2441 0.2784 -0.0167 -0.0005 0.0005  308 LYS B CE  
6676 N NZ  . LYS B 308 ? 0.1721 0.1560 0.1887 -0.0166 0.0027  -0.0016 308 LYS B NZ  
6677 N N   . THR B 309 ? 0.1607 0.1412 0.1735 -0.0196 -0.0006 -0.0005 309 THR B N   
6678 C CA  . THR B 309 ? 0.1184 0.0993 0.1304 -0.0195 -0.0003 -0.0005 309 THR B CA  
6679 C C   . THR B 309 ? 0.0930 0.0732 0.1044 -0.0193 -0.0004 -0.0008 309 THR B C   
6680 O O   . THR B 309 ? 0.1526 0.1331 0.1637 -0.0189 -0.0004 -0.0007 309 THR B O   
6681 C CB  . THR B 309 ? 0.2829 0.2642 0.2928 -0.0202 0.0001  -0.0007 309 THR B CB  
6682 O OG1 . THR B 309 ? 0.5349 0.5154 0.5433 -0.0208 0.0005  -0.0011 309 THR B OG1 
6683 C CG2 . THR B 309 ? 0.1504 0.1323 0.1609 -0.0206 0.0002  -0.0006 309 THR B CG2 
6684 N N   . LEU B 310 ? 0.1288 0.1079 0.1395 -0.0198 -0.0002 -0.0012 310 LEU B N   
6685 C CA  . LEU B 310 ? 0.0935 0.0719 0.1037 -0.0196 -0.0002 -0.0014 310 LEU B CA  
6686 C C   . LEU B 310 ? 0.0844 0.0626 0.0958 -0.0188 -0.0009 -0.0011 310 LEU B C   
6687 O O   . LEU B 310 ? 0.1424 0.1208 0.1538 -0.0184 -0.0010 -0.0011 310 LEU B O   
6688 C CB  . LEU B 310 ? 0.1397 0.1169 0.1489 -0.0202 0.0004  -0.0021 310 LEU B CB  
6689 C CG  . LEU B 310 ? 0.1706 0.1480 0.1781 -0.0209 0.0011  -0.0025 310 LEU B CG  
6690 C CD1 . LEU B 310 ? 0.1725 0.1487 0.1795 -0.0213 0.0019  -0.0033 310 LEU B CD1 
6691 C CD2 . LEU B 310 ? 0.2019 0.1796 0.2078 -0.0209 0.0010  -0.0023 310 LEU B CD2 
6692 N N   . SER B 311 ? 0.0807 0.0587 0.0924 -0.0187 -0.0013 -0.0008 311 SER B N   
6693 C CA  . SER B 311 ? 0.1208 0.0985 0.1322 -0.0182 -0.0020 -0.0005 311 SER B CA  
6694 C C   . SER B 311 ? 0.1775 0.1570 0.1907 -0.0171 -0.0024 0.0000  311 SER B C   
6695 O O   . SER B 311 ? 0.1347 0.1144 0.1485 -0.0164 -0.0026 0.0001  311 SER B O   
6696 C CB  . SER B 311 ? 0.0983 0.0751 0.1087 -0.0187 -0.0019 -0.0006 311 SER B CB  
6697 O OG  . SER B 311 ? 0.1322 0.1078 0.1428 -0.0193 -0.0009 -0.0015 311 SER B OG  
6698 N N   . ASP B 312 ? 0.1532 0.1340 0.1677 -0.0168 -0.0016 -0.0001 312 ASP B N   
6699 C CA  . ASP B 312 ? 0.1742 0.1560 0.1889 -0.0163 0.0000  -0.0008 312 ASP B CA  
6700 C C   . ASP B 312 ? 0.1458 0.1272 0.1582 -0.0168 0.0000  -0.0008 312 ASP B C   
6701 O O   . ASP B 312 ? 0.1469 0.1283 0.1580 -0.0167 0.0001  -0.0007 312 ASP B O   
6702 C CB  . ASP B 312 ? 0.1866 0.1690 0.2007 -0.0167 0.0004  -0.0007 312 ASP B CB  
6703 C CG  . ASP B 312 ? 0.2541 0.2371 0.2700 -0.0162 0.0009  -0.0010 312 ASP B CG  
6704 O OD1 . ASP B 312 ? 0.2069 0.1897 0.2235 -0.0156 0.0020  -0.0018 312 ASP B OD1 
6705 O OD2 . ASP B 312 ? 0.2848 0.2681 0.3004 -0.0165 0.0011  -0.0009 312 ASP B OD2 
6706 N N   . LEU B 313 ? 0.1363 0.1171 0.1477 -0.0175 -0.0003 -0.0007 313 LEU B N   
6707 C CA  . LEU B 313 ? 0.1224 0.1029 0.1313 -0.0178 -0.0005 -0.0005 313 LEU B CA  
6708 C C   . LEU B 313 ? 0.0864 0.0665 0.0958 -0.0173 -0.0005 -0.0007 313 LEU B C   
6709 O O   . LEU B 313 ? 0.1064 0.0867 0.1139 -0.0171 -0.0009 -0.0004 313 LEU B O   
6710 C CB  . LEU B 313 ? 0.1283 0.1083 0.1355 -0.0185 -0.0005 -0.0006 313 LEU B CB  
6711 C CG  . LEU B 313 ? 0.2037 0.1842 0.2091 -0.0191 -0.0006 -0.0003 313 LEU B CG  
6712 C CD1 . LEU B 313 ? 0.1466 0.1267 0.1509 -0.0198 -0.0003 -0.0007 313 LEU B CD1 
6713 C CD2 . LEU B 313 ? 0.1612 0.1424 0.1640 -0.0191 -0.0013 0.0003  313 LEU B CD2 
6714 N N   . ILE B 314 ? 0.0914 0.0711 0.1026 -0.0169 -0.0005 -0.0010 314 ILE B N   
6715 C CA  . ILE B 314 ? 0.0961 0.0756 0.1078 -0.0164 -0.0004 -0.0012 314 ILE B CA  
6716 C C   . ILE B 314 ? 0.1603 0.1404 0.1722 -0.0158 0.0002  -0.0014 314 ILE B C   
6717 O O   . ILE B 314 ? 0.1371 0.1170 0.1475 -0.0158 0.0002  -0.0013 314 ILE B O   
6718 C CB  . ILE B 314 ? 0.1154 0.0941 0.1281 -0.0164 -0.0012 -0.0011 314 ILE B CB  
6719 C CG1 . ILE B 314 ? 0.1149 0.0925 0.1260 -0.0174 -0.0011 -0.0013 314 ILE B CG1 
6720 C CG2 . ILE B 314 ? 0.1314 0.1099 0.1448 -0.0158 -0.0013 -0.0012 314 ILE B CG2 
6721 C CD1 . ILE B 314 ? 0.1335 0.1095 0.1442 -0.0179 -0.0014 -0.0015 314 ILE B CD1 
6722 N N   . GLY B 315 ? 0.1162 0.0968 0.1294 -0.0155 0.0008  -0.0016 315 GLY B N   
6723 C CA  . GLY B 315 ? 0.1329 0.1130 0.1436 -0.0157 0.0019  -0.0021 315 GLY B CA  
6724 C C   . GLY B 315 ? 0.2236 0.2041 0.2332 -0.0158 0.0007  -0.0012 315 GLY B C   
6725 O O   . GLY B 315 ? 0.1675 0.1478 0.1763 -0.0157 0.0002  -0.0008 315 GLY B O   
6726 N N   . PHE B 316 ? 0.1363 0.1173 0.1458 -0.0161 0.0000  -0.0006 316 PHE B N   
6727 C CA  . PHE B 316 ? 0.1805 0.1623 0.1884 -0.0159 -0.0013 0.0003  316 PHE B CA  
6728 C C   . PHE B 316 ? 0.1652 0.1473 0.1710 -0.0160 -0.0024 0.0011  316 PHE B C   
6729 O O   . PHE B 316 ? 0.2457 0.2283 0.2499 -0.0157 -0.0036 0.0020  316 PHE B O   
6730 C CB  . PHE B 316 ? 0.1580 0.1402 0.1664 -0.0161 -0.0011 0.0004  316 PHE B CB  
6731 C CG  . PHE B 316 ? 0.2270 0.2088 0.2363 -0.0161 -0.0003 -0.0001 316 PHE B CG  
6732 C CD1 . PHE B 316 ? 0.2963 0.2783 0.3053 -0.0156 -0.0010 0.0003  316 PHE B CD1 
6733 C CD2 . PHE B 316 ? 0.2887 0.2703 0.2986 -0.0163 0.0009  -0.0008 316 PHE B CD2 
6734 C CE1 . PHE B 316 ? 0.2467 0.2282 0.2559 -0.0156 -0.0006 0.0001  316 PHE B CE1 
6735 C CE2 . PHE B 316 ? 0.3212 0.3021 0.3299 -0.0166 0.0012  -0.0010 316 PHE B CE2 
6736 C CZ  . PHE B 316 ? 0.2792 0.2600 0.2879 -0.0162 0.0003  -0.0005 316 PHE B CZ  
6737 N N   . SER B 317 ? 0.1865 0.1682 0.1920 -0.0165 -0.0021 0.0008  317 SER B N   
6738 C CA  . SER B 317 ? 0.1756 0.1576 0.1785 -0.0168 -0.0030 0.0015  317 SER B CA  
6739 C C   . SER B 317 ? 0.2183 0.1998 0.2197 -0.0168 -0.0034 0.0016  317 SER B C   
6740 O O   . SER B 317 ? 0.1827 0.1646 0.1821 -0.0166 -0.0045 0.0024  317 SER B O   
6741 C CB  . SER B 317 ? 0.1993 0.1811 0.2018 -0.0175 -0.0026 0.0013  317 SER B CB  
6742 O OG  . SER B 317 ? 0.2428 0.2251 0.2465 -0.0176 -0.0024 0.0013  317 SER B OG  
6743 N N   . TYR B 318 ? 0.1296 0.1104 0.1322 -0.0169 -0.0026 0.0009  318 TYR B N   
6744 C CA  . TYR B 318 ? 0.1073 0.0877 0.1082 -0.0170 -0.0029 0.0011  318 TYR B CA  
6745 C C   . TYR B 318 ? 0.1199 0.1004 0.1201 -0.0165 -0.0037 0.0015  318 TYR B C   
6746 O O   . TYR B 318 ? 0.1444 0.1246 0.1427 -0.0166 -0.0042 0.0018  318 TYR B O   
6747 C CB  . TYR B 318 ? 0.1122 0.0917 0.1145 -0.0173 -0.0021 0.0003  318 TYR B CB  
6748 C CG  . TYR B 318 ? 0.1496 0.1289 0.1517 -0.0179 -0.0017 0.0000  318 TYR B CG  
6749 C CD1 . TYR B 318 ? 0.2034 0.1831 0.2032 -0.0184 -0.0021 0.0005  318 TYR B CD1 
6750 C CD2 . TYR B 318 ? 0.1839 0.1626 0.1880 -0.0181 -0.0010 -0.0006 318 TYR B CD2 
6751 C CE1 . TYR B 318 ? 0.1649 0.1445 0.1644 -0.0190 -0.0016 0.0002  318 TYR B CE1 
6752 C CE2 . TYR B 318 ? 0.1441 0.1226 0.1477 -0.0187 -0.0007 -0.0008 318 TYR B CE2 
6753 C CZ  . TYR B 318 ? 0.2043 0.1832 0.2057 -0.0192 -0.0009 -0.0005 318 TYR B CZ  
6754 O OH  . TYR B 318 ? 0.1705 0.1492 0.1714 -0.0198 -0.0005 -0.0008 318 TYR B OH  
6755 N N   . HIS B 319 ? 0.1895 0.1704 0.1909 -0.0160 -0.0038 0.0016  319 HIS B N   
6756 C CA  . HIS B 319 ? 0.1967 0.1778 0.1972 -0.0154 -0.0047 0.0021  319 HIS B CA  
6757 C C   . HIS B 319 ? 0.2326 0.2143 0.2304 -0.0155 -0.0060 0.0031  319 HIS B C   
6758 O O   . HIS B 319 ? 0.2365 0.2182 0.2331 -0.0152 -0.0068 0.0035  319 HIS B O   
6759 C CB  . HIS B 319 ? 0.1468 0.1284 0.1487 -0.0149 -0.0049 0.0022  319 HIS B CB  
6760 C CG  . HIS B 319 ? 0.1345 0.1169 0.1358 -0.0147 -0.0057 0.0029  319 HIS B CG  
6761 N ND1 . HIS B 319 ? 0.2015 0.1847 0.2014 -0.0143 -0.0071 0.0039  319 HIS B ND1 
6762 C CD2 . HIS B 319 ? 0.1676 0.1503 0.1698 -0.0149 -0.0053 0.0028  319 HIS B CD2 
6763 C CE1 . HIS B 319 ? 0.1473 0.1311 0.1471 -0.0142 -0.0076 0.0044  319 HIS B CE1 
6764 N NE2 . HIS B 319 ? 0.2317 0.2153 0.2329 -0.0146 -0.0065 0.0037  319 HIS B NE2 
6765 N N   . ALA B 320 ? 0.2145 0.1966 0.2114 -0.0157 -0.0063 0.0034  320 ALA B N   
6766 C CA  . ALA B 320 ? 0.2085 0.1912 0.2030 -0.0158 -0.0076 0.0043  320 ALA B CA  
6767 C C   . ALA B 320 ? 0.2029 0.1850 0.1953 -0.0164 -0.0075 0.0043  320 ALA B C   
6768 O O   . ALA B 320 ? 0.3149 0.2975 0.3051 -0.0166 -0.0084 0.0050  320 ALA B O   
6769 C CB  . ALA B 320 ? 0.2338 0.2172 0.2281 -0.0159 -0.0080 0.0048  320 ALA B CB  
6770 N N   . TRP B 321 ? 0.1999 0.1813 0.1930 -0.0168 -0.0064 0.0035  321 TRP B N   
6771 C CA  . TRP B 321 ? 0.2624 0.2433 0.2537 -0.0174 -0.0063 0.0034  321 TRP B CA  
6772 C C   . TRP B 321 ? 0.2678 0.2482 0.2587 -0.0172 -0.0063 0.0033  321 TRP B C   
6773 O O   . TRP B 321 ? 0.2715 0.2516 0.2641 -0.0168 -0.0060 0.0030  321 TRP B O   
6774 C CB  . TRP B 321 ? 0.1364 0.1168 0.1288 -0.0179 -0.0051 0.0026  321 TRP B CB  
6775 C CG  . TRP B 321 ? 0.1652 0.1460 0.1580 -0.0182 -0.0049 0.0027  321 TRP B CG  
6776 C CD1 . TRP B 321 ? 0.1998 0.1813 0.1939 -0.0178 -0.0051 0.0029  321 TRP B CD1 
6777 C CD2 . TRP B 321 ? 0.1825 0.1632 0.1746 -0.0189 -0.0045 0.0024  321 TRP B CD2 
6778 N NE1 . TRP B 321 ? 0.2767 0.2584 0.2708 -0.0183 -0.0049 0.0028  321 TRP B NE1 
6779 C CE2 . TRP B 321 ? 0.2171 0.1984 0.2100 -0.0190 -0.0045 0.0025  321 TRP B CE2 
6780 C CE3 . TRP B 321 ? 0.2708 0.2510 0.2615 -0.0195 -0.0041 0.0021  321 TRP B CE3 
6781 C CZ2 . TRP B 321 ? 0.3148 0.2962 0.3073 -0.0196 -0.0041 0.0024  321 TRP B CZ2 
6782 C CZ3 . TRP B 321 ? 0.2650 0.2453 0.2552 -0.0202 -0.0037 0.0020  321 TRP B CZ3 
6783 C CH2 . TRP B 321 ? 0.2263 0.2072 0.2174 -0.0202 -0.0037 0.0021  321 TRP B CH2 
6784 N N   . ASN B 322 ? 0.2252 0.2053 0.2138 -0.0177 -0.0066 0.0035  322 ASN B N   
6785 C CA  . ASN B 322 ? 0.2456 0.2249 0.2338 -0.0177 -0.0063 0.0032  322 ASN B CA  
6786 C C   . ASN B 322 ? 0.2237 0.2022 0.2137 -0.0180 -0.0050 0.0023  322 ASN B C   
6787 O O   . ASN B 322 ? 0.2015 0.1800 0.1921 -0.0184 -0.0044 0.0019  322 ASN B O   
6788 C CB  . ASN B 322 ? 0.3202 0.2995 0.3054 -0.0182 -0.0069 0.0037  322 ASN B CB  
6789 C CG  . ASN B 322 ? 0.4833 0.4617 0.4678 -0.0185 -0.0063 0.0032  322 ASN B CG  
6790 O OD1 . ASN B 322 ? 0.5004 0.4783 0.4852 -0.0191 -0.0055 0.0026  322 ASN B OD1 
6791 N ND2 . ASN B 322 ? 0.5490 0.5272 0.5324 -0.0183 -0.0069 0.0035  322 ASN B ND2 
6792 N N   . ALA B 323 ? 0.1882 0.1887 0.2015 -0.0069 0.0044  0.0331  323 ALA B N   
6793 C CA  . ALA B 323 ? 0.2102 0.2129 0.2217 -0.0078 0.0030  0.0307  323 ALA B CA  
6794 C C   . ALA B 323 ? 0.2733 0.2780 0.2809 -0.0081 0.0018  0.0315  323 ALA B C   
6795 O O   . ALA B 323 ? 0.1929 0.1981 0.1974 -0.0091 0.0019  0.0297  323 ALA B O   
6796 C CB  . ALA B 323 ? 0.2260 0.2305 0.2405 -0.0075 0.0013  0.0298  323 ALA B CB  
6797 N N   . GLU B 324 ? 0.1960 0.2018 0.2036 -0.0074 0.0006  0.0340  324 GLU B N   
6798 C CA  . GLU B 324 ? 0.1854 0.1934 0.1896 -0.0078 -0.0007 0.0347  324 GLU B CA  
6799 C C   . GLU B 324 ? 0.2333 0.2398 0.2337 -0.0083 0.0008  0.0350  324 GLU B C   
6800 O O   . GLU B 324 ? 0.1895 0.1974 0.1865 -0.0092 0.0004  0.0338  324 GLU B O   
6801 C CB  . GLU B 324 ? 0.2752 0.2848 0.2805 -0.0068 -0.0023 0.0375  324 GLU B CB  
6802 C CG  . GLU B 324 ? 0.4960 0.5083 0.4976 -0.0074 -0.0040 0.0376  324 GLU B CG  
6803 C CD  . GLU B 324 ? 0.7370 0.7509 0.7369 -0.0085 -0.0047 0.0346  324 GLU B CD  
6804 O OE1 . GLU B 324 ? 0.8102 0.8253 0.8126 -0.0085 -0.0058 0.0331  324 GLU B OE1 
6805 O OE2 . GLU B 324 ? 0.8220 0.8356 0.8183 -0.0094 -0.0040 0.0335  324 GLU B OE2 
6806 N N   . ASP B 325 ? 0.2198 0.2237 0.2210 -0.0079 0.0027  0.0365  325 ASP B N   
6807 C CA  . ASP B 325 ? 0.2500 0.2524 0.2480 -0.0084 0.0044  0.0368  325 ASP B CA  
6808 C C   . ASP B 325 ? 0.2135 0.2153 0.2096 -0.0095 0.0053  0.0338  325 ASP B C   
6809 O O   . ASP B 325 ? 0.1726 0.1748 0.1650 -0.0103 0.0056  0.0333  325 ASP B O   
6810 C CB  . ASP B 325 ? 0.3361 0.3354 0.3357 -0.0077 0.0063  0.0387  325 ASP B CB  
6811 C CG  . ASP B 325 ? 0.4486 0.4482 0.4493 -0.0066 0.0055  0.0420  325 ASP B CG  
6812 O OD1 . ASP B 325 ? 0.4986 0.5006 0.4978 -0.0065 0.0037  0.0430  325 ASP B OD1 
6813 O OD2 . ASP B 325 ? 0.4869 0.4843 0.4901 -0.0058 0.0068  0.0435  325 ASP B OD2 
6814 N N   . ALA B 326 ? 0.1609 0.1620 0.1596 -0.0096 0.0059  0.0318  326 ALA B N   
6815 C CA  . ALA B 326 ? 0.1142 0.1149 0.1114 -0.0106 0.0068  0.0289  326 ALA B CA  
6816 C C   . ALA B 326 ? 0.1910 0.1944 0.1856 -0.0114 0.0051  0.0272  326 ALA B C   
6817 O O   . ALA B 326 ? 0.1566 0.1600 0.1481 -0.0123 0.0057  0.0257  326 ALA B O   
6818 C CB  . ALA B 326 ? 0.1550 0.1545 0.1558 -0.0105 0.0075  0.0272  326 ALA B CB  
6819 N N   . VAL B 327 ? 0.1680 0.1738 0.1638 -0.0111 0.0029  0.0274  327 VAL B N   
6820 C CA  . VAL B 327 ? 0.2027 0.2111 0.1960 -0.0118 0.0013  0.0259  327 VAL B CA  
6821 C C   . VAL B 327 ? 0.1500 0.1593 0.1392 -0.0122 0.0011  0.0272  327 VAL B C   
6822 O O   . VAL B 327 ? 0.1717 0.1819 0.1578 -0.0131 0.0011  0.0255  327 VAL B O   
6823 C CB  . VAL B 327 ? 0.1924 0.2032 0.1878 -0.0114 -0.0010 0.0260  327 VAL B CB  
6824 C CG1 . VAL B 327 ? 0.2181 0.2319 0.2106 -0.0121 -0.0029 0.0251  327 VAL B CG1 
6825 C CG2 . VAL B 327 ? 0.1683 0.1784 0.1672 -0.0114 -0.0008 0.0239  327 VAL B CG2 
6826 N N   . ARG B 328 ? 0.2282 0.2373 0.2175 -0.0114 0.0009  0.0302  328 ARG B N   
6827 C CA  . ARG B 328 ? 0.2335 0.2432 0.2190 -0.0117 0.0008  0.0317  328 ARG B CA  
6828 C C   . ARG B 328 ? 0.2631 0.2710 0.2459 -0.0125 0.0029  0.0306  328 ARG B C   
6829 O O   . ARG B 328 ? 0.1973 0.2062 0.1763 -0.0132 0.0026  0.0302  328 ARG B O   
6830 C CB  . ARG B 328 ? 0.1862 0.1952 0.1726 -0.0107 0.0008  0.0351  328 ARG B CB  
6831 C CG  . ARG B 328 ? 0.3057 0.3171 0.2938 -0.0100 -0.0015 0.0366  328 ARG B CG  
6832 C CD  . ARG B 328 ? 0.4407 0.4511 0.4305 -0.0088 -0.0013 0.0400  328 ARG B CD  
6833 N NE  . ARG B 328 ? 0.4248 0.4376 0.4158 -0.0082 -0.0035 0.0414  328 ARG B NE  
6834 C CZ  . ARG B 328 ? 0.5086 0.5210 0.5029 -0.0071 -0.0039 0.0435  328 ARG B CZ  
6835 N NH1 . ARG B 328 ? 0.4871 0.4967 0.4837 -0.0064 -0.0020 0.0444  328 ARG B NH1 
6836 N NH2 . ARG B 328 ? 0.4296 0.4446 0.4249 -0.0065 -0.0060 0.0448  328 ARG B NH2 
6837 N N   . ASP B 329 ? 0.2306 0.2357 0.2152 -0.0123 0.0049  0.0304  329 ASP B N   
6838 C CA  . ASP B 329 ? 0.2075 0.2108 0.1897 -0.0130 0.0069  0.0294  329 ASP B CA  
6839 C C   . ASP B 329 ? 0.2174 0.2218 0.1978 -0.0140 0.0067  0.0262  329 ASP B C   
6840 O O   . ASP B 329 ? 0.2641 0.2689 0.2409 -0.0148 0.0072  0.0255  329 ASP B O   
6841 C CB  . ASP B 329 ? 0.1325 0.1328 0.1175 -0.0126 0.0090  0.0295  329 ASP B CB  
6842 C CG  . ASP B 329 ? 0.2876 0.2860 0.2703 -0.0134 0.0111  0.0285  329 ASP B CG  
6843 O OD1 . ASP B 329 ? 0.3583 0.3558 0.3387 -0.0134 0.0120  0.0303  329 ASP B OD1 
6844 O OD2 . ASP B 329 ? 0.2511 0.2490 0.2341 -0.0139 0.0120  0.0260  329 ASP B OD2 
6845 N N   . PHE B 330 ? 0.1149 0.1200 0.0977 -0.0140 0.0060  0.0242  330 PHE B N   
6846 C CA  . PHE B 330 ? 0.1237 0.1298 0.1053 -0.0149 0.0058  0.0211  330 PHE B CA  
6847 C C   . PHE B 330 ? 0.2327 0.2416 0.2109 -0.0155 0.0041  0.0207  330 PHE B C   
6848 O O   . PHE B 330 ? 0.2287 0.2379 0.2039 -0.0164 0.0046  0.0191  330 PHE B O   
6849 C CB  . PHE B 330 ? 0.1291 0.1354 0.1142 -0.0147 0.0051  0.0195  330 PHE B CB  
6850 C CG  . PHE B 330 ? 0.1560 0.1627 0.1405 -0.0155 0.0054  0.0162  330 PHE B CG  
6851 C CD1 . PHE B 330 ? 0.2088 0.2133 0.1939 -0.0158 0.0074  0.0148  330 PHE B CD1 
6852 C CD2 . PHE B 330 ? 0.1628 0.1719 0.1464 -0.0160 0.0036  0.0146  330 PHE B CD2 
6853 C CE1 . PHE B 330 ? 0.2257 0.2305 0.2103 -0.0165 0.0077  0.0119  330 PHE B CE1 
6854 C CE2 . PHE B 330 ? 0.2075 0.2168 0.1906 -0.0167 0.0039  0.0116  330 PHE B CE2 
6855 C CZ  . PHE B 330 ? 0.2564 0.2635 0.2400 -0.0169 0.0059  0.0103  330 PHE B CZ  
6856 N N   . ILE B 331 ? 0.2256 0.2364 0.2043 -0.0151 0.0021  0.0221  331 ILE B N   
6857 C CA  . ILE B 331 ? 0.2314 0.2450 0.2070 -0.0157 0.0005  0.0219  331 ILE B CA  
6858 C C   . ILE B 331 ? 0.2019 0.2151 0.1737 -0.0161 0.0013  0.0231  331 ILE B C   
6859 O O   . ILE B 331 ? 0.2501 0.2647 0.2186 -0.0169 0.0010  0.0218  331 ILE B O   
6860 C CB  . ILE B 331 ? 0.2316 0.2473 0.2088 -0.0150 -0.0017 0.0235  331 ILE B CB  
6861 C CG1 . ILE B 331 ? 0.2503 0.2664 0.2310 -0.0148 -0.0026 0.0219  331 ILE B CG1 
6862 C CG2 . ILE B 331 ? 0.1967 0.2152 0.1704 -0.0156 -0.0035 0.0235  331 ILE B CG2 
6863 C CD1 . ILE B 331 ? 0.2294 0.2470 0.2090 -0.0157 -0.0033 0.0188  331 ILE B CD1 
6864 N N   . GLY B 332 ? 0.2055 0.2169 0.1777 -0.0155 0.0024  0.0256  332 GLY B N   
6865 C CA  . GLY B 332 ? 0.1790 0.1900 0.1476 -0.0158 0.0032  0.0270  332 GLY B CA  
6866 C C   . GLY B 332 ? 0.2227 0.2326 0.1891 -0.0167 0.0050  0.0249  332 GLY B C   
6867 O O   . GLY B 332 ? 0.1887 0.1992 0.1513 -0.0174 0.0051  0.0249  332 GLY B O   
6868 N N   . ARG B 333 ? 0.1654 0.1735 0.1338 -0.0168 0.0063  0.0231  333 ARG B N   
6869 C CA  . ARG B 333 ? 0.2163 0.2235 0.1828 -0.0176 0.0079  0.0210  333 ARG B CA  
6870 C C   . ARG B 333 ? 0.2190 0.2284 0.1834 -0.0185 0.0068  0.0184  333 ARG B C   
6871 O O   . ARG B 333 ? 0.1959 0.2055 0.1571 -0.0193 0.0075  0.0173  333 ARG B O   
6872 C CB  . ARG B 333 ? 0.2025 0.2072 0.1720 -0.0174 0.0096  0.0199  333 ARG B CB  
6873 C CG  . ARG B 333 ? 0.1827 0.1849 0.1537 -0.0168 0.0112  0.0222  333 ARG B CG  
6874 C CD  . ARG B 333 ? 0.2256 0.2257 0.2000 -0.0165 0.0125  0.0211  333 ARG B CD  
6875 N NE  . ARG B 333 ? 0.2009 0.1985 0.1768 -0.0159 0.0141  0.0232  333 ARG B NE  
6876 C CZ  . ARG B 333 ? 0.2690 0.2646 0.2435 -0.0163 0.0162  0.0234  333 ARG B CZ  
6877 N NH1 . ARG B 333 ? 0.2476 0.2435 0.2191 -0.0172 0.0169  0.0217  333 ARG B NH1 
6878 N NH2 . ARG B 333 ? 0.3015 0.2948 0.2775 -0.0157 0.0175  0.0254  333 ARG B NH2 
6879 N N   . LEU B 334 ? 0.1802 0.1913 0.1465 -0.0183 0.0051  0.0174  334 LEU B N   
6880 C CA  . LEU B 334 ? 0.1777 0.1910 0.1420 -0.0191 0.0039  0.0151  334 LEU B CA  
6881 C C   . LEU B 334 ? 0.1887 0.2040 0.1492 -0.0195 0.0029  0.0161  334 LEU B C   
6882 O O   . LEU B 334 ? 0.1837 0.2000 0.1411 -0.0204 0.0029  0.0144  334 LEU B O   
6883 C CB  . LEU B 334 ? 0.1215 0.1363 0.0886 -0.0188 0.0021  0.0141  334 LEU B CB  
6884 C CG  . LEU B 334 ? 0.1404 0.1535 0.1112 -0.0185 0.0030  0.0126  334 LEU B CG  
6885 C CD1 . LEU B 334 ? 0.2226 0.2372 0.1961 -0.0181 0.0012  0.0120  334 LEU B CD1 
6886 C CD2 . LEU B 334 ? 0.1534 0.1657 0.1230 -0.0192 0.0044  0.0098  334 LEU B CD2 
6887 N N   . LYS B 335 ? 0.1574 0.1732 0.1181 -0.0189 0.0019  0.0190  335 LYS B N   
6888 C CA  . LYS B 335 ? 0.2742 0.2919 0.2313 -0.0194 0.0010  0.0202  335 LYS B CA  
6889 C C   . LYS B 335 ? 0.2836 0.3001 0.2372 -0.0200 0.0027  0.0201  335 LYS B C   
6890 O O   . LYS B 335 ? 0.2601 0.2782 0.2103 -0.0208 0.0022  0.0194  335 LYS B O   
6891 C CB  . LYS B 335 ? 0.2554 0.2734 0.2134 -0.0185 0.0000  0.0235  335 LYS B CB  
6892 C CG  . LYS B 335 ? 0.4732 0.4938 0.4279 -0.0189 -0.0016 0.0246  335 LYS B CG  
6893 C CD  . LYS B 335 ? 0.5373 0.5582 0.4930 -0.0180 -0.0026 0.0280  335 LYS B CD  
6894 C CE  . LYS B 335 ? 0.5915 0.6145 0.5435 -0.0184 -0.0038 0.0294  335 LYS B CE  
6895 N NZ  . LYS B 335 ? 0.6263 0.6485 0.5780 -0.0177 -0.0036 0.0329  335 LYS B NZ  
6896 N N   . LYS B 336 ? 0.2930 0.3068 0.2477 -0.0197 0.0048  0.0207  336 LYS B N   
6897 C CA  . LYS B 336 ? 0.2604 0.2731 0.2120 -0.0204 0.0065  0.0207  336 LYS B CA  
6898 C C   . LYS B 336 ? 0.2532 0.2663 0.2030 -0.0214 0.0071  0.0175  336 LYS B C   
6899 O O   . LYS B 336 ? 0.3014 0.3153 0.2476 -0.0221 0.0074  0.0170  336 LYS B O   
6900 C CB  . LYS B 336 ? 0.3217 0.3312 0.2749 -0.0199 0.0086  0.0220  336 LYS B CB  
6901 C CG  . LYS B 336 ? 0.3905 0.3993 0.3440 -0.0192 0.0085  0.0255  336 LYS B CG  
6902 C CD  . LYS B 336 ? 0.5554 0.5611 0.5107 -0.0187 0.0106  0.0266  336 LYS B CD  
6903 C CE  . LYS B 336 ? 0.6551 0.6600 0.6108 -0.0179 0.0105  0.0301  336 LYS B CE  
6904 N NZ  . LYS B 336 ? 0.6580 0.6600 0.6169 -0.0172 0.0120  0.0312  336 LYS B NZ  
6905 N N   . ILE B 337 ? 0.2350 0.2476 0.1874 -0.0213 0.0073  0.0153  337 ILE B N   
6906 C CA  . ILE B 337 ? 0.2063 0.2195 0.1574 -0.0221 0.0077  0.0122  337 ILE B CA  
6907 C C   . ILE B 337 ? 0.2707 0.2868 0.2191 -0.0227 0.0059  0.0112  337 ILE B C   
6908 O O   . ILE B 337 ? 0.2823 0.2992 0.2275 -0.0236 0.0063  0.0098  337 ILE B O   
6909 C CB  . ILE B 337 ? 0.2136 0.2260 0.1682 -0.0218 0.0079  0.0102  337 ILE B CB  
6910 C CG1 . ILE B 337 ? 0.2163 0.2259 0.1734 -0.0213 0.0098  0.0109  337 ILE B CG1 
6911 C CG2 . ILE B 337 ? 0.1935 0.2067 0.1467 -0.0226 0.0081  0.0069  337 ILE B CG2 
6912 C CD1 . ILE B 337 ? 0.2146 0.2233 0.1756 -0.0209 0.0099  0.0095  337 ILE B CD1 
6913 N N   . HIS B 338 ? 0.2019 0.2197 0.1516 -0.0223 0.0039  0.0120  338 HIS B N   
6914 C CA  . HIS B 338 ? 0.2340 0.2547 0.1815 -0.0229 0.0020  0.0113  338 HIS B CA  
6915 C C   . HIS B 338 ? 0.2312 0.2527 0.1744 -0.0235 0.0021  0.0124  338 HIS B C   
6916 O O   . HIS B 338 ? 0.2823 0.3055 0.2225 -0.0243 0.0017  0.0107  338 HIS B O   
6917 C CB  . HIS B 338 ? 0.1599 0.1820 0.1096 -0.0222 -0.0001 0.0127  338 HIS B CB  
6918 C CG  . HIS B 338 ? 0.2444 0.2696 0.1921 -0.0227 -0.0021 0.0121  338 HIS B CG  
6919 N ND1 . HIS B 338 ? 0.3434 0.3702 0.2900 -0.0225 -0.0036 0.0144  338 HIS B ND1 
6920 C CD2 . HIS B 338 ? 0.3167 0.3435 0.2633 -0.0234 -0.0030 0.0094  338 HIS B CD2 
6921 C CE1 . HIS B 338 ? 0.3449 0.3743 0.2897 -0.0231 -0.0053 0.0132  338 HIS B CE1 
6922 N NE2 . HIS B 338 ? 0.3227 0.3521 0.2675 -0.0237 -0.0049 0.0101  338 HIS B NE2 
6923 N N   . GLU B 339 ? 0.2553 0.2757 0.1981 -0.0230 0.0027  0.0152  339 GLU B N   
6924 C CA  . GLU B 339 ? 0.3287 0.3498 0.2676 -0.0236 0.0029  0.0165  339 GLU B CA  
6925 C C   . GLU B 339 ? 0.3373 0.3569 0.2738 -0.0243 0.0050  0.0155  339 GLU B C   
6926 O O   . GLU B 339 ? 0.3349 0.3554 0.2677 -0.0249 0.0051  0.0160  339 GLU B O   
6927 C CB  . GLU B 339 ? 0.2642 0.2846 0.2035 -0.0228 0.0026  0.0201  339 GLU B CB  
6928 C CG  . GLU B 339 ? 0.3555 0.3775 0.2970 -0.0221 0.0005  0.0215  339 GLU B CG  
6929 C CD  . GLU B 339 ? 0.5354 0.5561 0.4785 -0.0211 0.0007  0.0249  339 GLU B CD  
6930 O OE1 . GLU B 339 ? 0.5789 0.5971 0.5220 -0.0209 0.0026  0.0258  339 GLU B OE1 
6931 O OE2 . GLU B 339 ? 0.6231 0.6452 0.5672 -0.0205 -0.0010 0.0266  339 GLU B OE2 
6932 N N   . SER B 340 ? 0.2606 0.2782 0.1990 -0.0242 0.0066  0.0140  340 SER B N   
6933 C CA  . SER B 340 ? 0.2865 0.3025 0.2231 -0.0247 0.0088  0.0134  340 SER B CA  
6934 C C   . SER B 340 ? 0.3128 0.3300 0.2468 -0.0257 0.0090  0.0104  340 SER B C   
6935 O O   . SER B 340 ? 0.3120 0.3283 0.2438 -0.0263 0.0107  0.0099  340 SER B O   
6936 C CB  . SER B 340 ? 0.3722 0.3855 0.3119 -0.0242 0.0105  0.0130  340 SER B CB  
6937 O OG  . SER B 340 ? 0.3510 0.3645 0.2924 -0.0244 0.0105  0.0102  340 SER B OG  
6938 N N   . VAL B 341 ? 0.3038 0.3230 0.2380 -0.0259 0.0075  0.0085  341 VAL B N   
6939 C CA  . VAL B 341 ? 0.3396 0.3599 0.2715 -0.0268 0.0077  0.0056  341 VAL B CA  
6940 C C   . VAL B 341 ? 0.3253 0.3485 0.2558 -0.0272 0.0054  0.0050  341 VAL B C   
6941 O O   . VAL B 341 ? 0.2950 0.3192 0.2272 -0.0267 0.0038  0.0063  341 VAL B O   
6942 C CB  . VAL B 341 ? 0.3482 0.3675 0.2827 -0.0267 0.0085  0.0030  341 VAL B CB  
6943 C CG1 . VAL B 341 ? 0.3019 0.3184 0.2379 -0.0265 0.0107  0.0035  341 VAL B CG1 
6944 C CG2 . VAL B 341 ? 0.3416 0.3615 0.2796 -0.0261 0.0070  0.0026  341 VAL B CG2 
6945 N N   . ASP B 342 ? 0.2835 0.3083 0.2109 -0.0281 0.0054  0.0032  342 ASP B N   
6946 C CA  . ASP B 342 ? 0.3611 0.3886 0.2867 -0.0286 0.0035  0.0024  342 ASP B CA  
6947 C C   . ASP B 342 ? 0.3584 0.3868 0.2852 -0.0288 0.0028  -0.0007 342 ASP B C   
6948 O O   . ASP B 342 ? 0.4382 0.4689 0.3636 -0.0293 0.0012  -0.0017 342 ASP B O   
6949 C CB  . ASP B 342 ? 0.4936 0.5224 0.4146 -0.0295 0.0036  0.0025  342 ASP B CB  
6950 C CG  . ASP B 342 ? 0.6538 0.6811 0.5739 -0.0298 0.0057  0.0009  342 ASP B CG  
6951 O OD1 . ASP B 342 ? 0.7313 0.7568 0.6535 -0.0296 0.0071  -0.0002 342 ASP B OD1 
6952 O OD2 . ASP B 342 ? 0.7107 0.7383 0.6293 -0.0298 0.0058  0.0007  342 ASP B OD2 
6953 N N   . PHE B 343 ? 0.3105 0.3372 0.2398 -0.0285 0.0041  -0.0022 343 PHE B N   
6954 C CA  . PHE B 343 ? 0.2093 0.2365 0.1404 -0.0286 0.0034  -0.0049 343 PHE B CA  
6955 C C   . PHE B 343 ? 0.2617 0.2882 0.1970 -0.0277 0.0026  -0.0039 343 PHE B C   
6956 O O   . PHE B 343 ? 0.2257 0.2514 0.1623 -0.0270 0.0025  -0.0013 343 PHE B O   
6957 C CB  . PHE B 343 ? 0.2225 0.2485 0.1537 -0.0289 0.0051  -0.0074 343 PHE B CB  
6958 C CG  . PHE B 343 ? 0.2157 0.2389 0.1487 -0.0284 0.0070  -0.0066 343 PHE B CG  
6959 C CD1 . PHE B 343 ? 0.3336 0.3559 0.2646 -0.0286 0.0086  -0.0054 343 PHE B CD1 
6960 C CD2 . PHE B 343 ? 0.2075 0.2293 0.1444 -0.0277 0.0074  -0.0072 343 PHE B CD2 
6961 C CE1 . PHE B 343 ? 0.2274 0.2472 0.1601 -0.0282 0.0104  -0.0047 343 PHE B CE1 
6962 C CE2 . PHE B 343 ? 0.2000 0.2194 0.1387 -0.0273 0.0092  -0.0064 343 PHE B CE2 
6963 C CZ  . PHE B 343 ? 0.2982 0.3165 0.2347 -0.0276 0.0107  -0.0052 343 PHE B CZ  
6964 N N   . GLN B 344 ? 0.1684 0.1952 0.1057 -0.0276 0.0020  -0.0061 344 GLN B N   
6965 C CA  . GLN B 344 ? 0.1560 0.1823 0.0973 -0.0268 0.0011  -0.0054 344 GLN B CA  
6966 C C   . GLN B 344 ? 0.1605 0.1842 0.1047 -0.0263 0.0029  -0.0061 344 GLN B C   
6967 O O   . GLN B 344 ? 0.1943 0.2176 0.1391 -0.0265 0.0034  -0.0086 344 GLN B O   
6968 C CB  . GLN B 344 ? 0.1296 0.1577 0.0716 -0.0270 -0.0007 -0.0073 344 GLN B CB  
6969 C CG  . GLN B 344 ? 0.2073 0.2382 0.1467 -0.0275 -0.0025 -0.0066 344 GLN B CG  
6970 C CD  . GLN B 344 ? 0.2353 0.2680 0.1757 -0.0277 -0.0044 -0.0084 344 GLN B CD  
6971 O OE1 . GLN B 344 ? 0.3498 0.3839 0.2911 -0.0274 -0.0061 -0.0070 344 GLN B OE1 
6972 N NE2 . GLN B 344 ? 0.3014 0.3341 0.2417 -0.0282 -0.0040 -0.0113 344 GLN B NE2 
6973 N N   . PRO B 345 ? 0.1762 0.1981 0.1221 -0.0256 0.0037  -0.0038 345 PRO B N   
6974 C CA  . PRO B 345 ? 0.2042 0.2236 0.1526 -0.0252 0.0055  -0.0043 345 PRO B CA  
6975 C C   . PRO B 345 ? 0.1817 0.2008 0.1340 -0.0247 0.0048  -0.0054 345 PRO B C   
6976 O O   . PRO B 345 ? 0.1496 0.1699 0.1033 -0.0244 0.0031  -0.0046 345 PRO B O   
6977 C CB  . PRO B 345 ? 0.1695 0.1873 0.1185 -0.0247 0.0064  -0.0013 345 PRO B CB  
6978 C CG  . PRO B 345 ? 0.1642 0.1836 0.1130 -0.0244 0.0045  0.0008  345 PRO B CG  
6979 C CD  . PRO B 345 ? 0.1571 0.1791 0.1030 -0.0251 0.0030  -0.0006 345 PRO B CD  
6980 N N   . VAL B 346 ? 0.1695 0.1869 0.1234 -0.0247 0.0062  -0.0071 346 VAL B N   
6981 C CA  . VAL B 346 ? 0.1221 0.1388 0.0799 -0.0242 0.0059  -0.0080 346 VAL B CA  
6982 C C   . VAL B 346 ? 0.1865 0.2007 0.1467 -0.0235 0.0074  -0.0064 346 VAL B C   
6983 O O   . VAL B 346 ? 0.1803 0.1929 0.1398 -0.0237 0.0093  -0.0067 346 VAL B O   
6984 C CB  . VAL B 346 ? 0.1579 0.1746 0.1158 -0.0246 0.0063  -0.0112 346 VAL B CB  
6985 C CG1 . VAL B 346 ? 0.2069 0.2231 0.1688 -0.0241 0.0057  -0.0120 346 VAL B CG1 
6986 C CG2 . VAL B 346 ? 0.1301 0.1491 0.0850 -0.0253 0.0050  -0.0127 346 VAL B CG2 
6987 N N   . VAL B 347 ? 0.1003 0.1141 0.0634 -0.0228 0.0066  -0.0048 347 VAL B N   
6988 C CA  . VAL B 347 ? 0.1090 0.1206 0.0746 -0.0221 0.0078  -0.0029 347 VAL B CA  
6989 C C   . VAL B 347 ? 0.1420 0.1527 0.1115 -0.0217 0.0078  -0.0040 347 VAL B C   
6990 O O   . VAL B 347 ? 0.1576 0.1692 0.1292 -0.0213 0.0063  -0.0037 347 VAL B O   
6991 C CB  . VAL B 347 ? 0.1648 0.1768 0.1306 -0.0216 0.0070  0.0002  347 VAL B CB  
6992 C CG1 . VAL B 347 ? 0.1710 0.1806 0.1392 -0.0209 0.0084  0.0020  347 VAL B CG1 
6993 C CG2 . VAL B 347 ? 0.1367 0.1499 0.0984 -0.0221 0.0068  0.0012  347 VAL B CG2 
6994 N N   . PHE B 348 ? 0.1296 0.1384 0.1000 -0.0218 0.0096  -0.0053 348 PHE B N   
6995 C CA  . PHE B 348 ? 0.1900 0.1978 0.1641 -0.0214 0.0098  -0.0064 348 PHE B CA  
6996 C C   . PHE B 348 ? 0.1078 0.1137 0.0847 -0.0207 0.0107  -0.0043 348 PHE B C   
6997 O O   . PHE B 348 ? 0.1313 0.1356 0.1074 -0.0207 0.0123  -0.0032 348 PHE B O   
6998 C CB  . PHE B 348 ? 0.1478 0.1547 0.1218 -0.0218 0.0111  -0.0090 348 PHE B CB  
6999 C CG  . PHE B 348 ? 0.1896 0.1981 0.1632 -0.0222 0.0100  -0.0116 348 PHE B CG  
7000 C CD1 . PHE B 348 ? 0.1123 0.1227 0.0826 -0.0228 0.0090  -0.0124 348 PHE B CD1 
7001 C CD2 . PHE B 348 ? 0.1873 0.1952 0.1637 -0.0221 0.0100  -0.0134 348 PHE B CD2 
7002 C CE1 . PHE B 348 ? 0.1249 0.1367 0.0949 -0.0232 0.0080  -0.0149 348 PHE B CE1 
7003 C CE2 . PHE B 348 ? 0.1645 0.1736 0.1406 -0.0225 0.0091  -0.0158 348 PHE B CE2 
7004 C CZ  . PHE B 348 ? 0.1256 0.1367 0.0984 -0.0230 0.0080  -0.0166 348 PHE B CZ  
7005 N N   . VAL B 349 ? 0.1316 0.1375 0.1116 -0.0201 0.0096  -0.0037 349 VAL B N   
7006 C CA  . VAL B 349 ? 0.1226 0.1268 0.1057 -0.0194 0.0104  -0.0018 349 VAL B CA  
7007 C C   . VAL B 349 ? 0.1545 0.1577 0.1408 -0.0192 0.0108  -0.0036 349 VAL B C   
7008 O O   . VAL B 349 ? 0.1092 0.1134 0.0971 -0.0191 0.0093  -0.0045 349 VAL B O   
7009 C CB  . VAL B 349 ? 0.1080 0.1131 0.0922 -0.0187 0.0088  0.0005  349 VAL B CB  
7010 C CG1 . VAL B 349 ? 0.1331 0.1363 0.1205 -0.0180 0.0096  0.0023  349 VAL B CG1 
7011 C CG2 . VAL B 349 ? 0.1730 0.1794 0.1539 -0.0189 0.0082  0.0021  349 VAL B CG2 
7012 N N   . VAL B 350 ? 0.1056 0.1068 0.0925 -0.0193 0.0127  -0.0042 350 VAL B N   
7013 C CA  . VAL B 350 ? 0.0905 0.0907 0.0798 -0.0193 0.0133  -0.0062 350 VAL B CA  
7014 C C   . VAL B 350 ? 0.1112 0.1091 0.1033 -0.0189 0.0148  -0.0050 350 VAL B C   
7015 O O   . VAL B 350 ? 0.1417 0.1383 0.1327 -0.0190 0.0164  -0.0040 350 VAL B O   
7016 C CB  . VAL B 350 ? 0.1313 0.1315 0.1187 -0.0200 0.0143  -0.0087 350 VAL B CB  
7017 C CG1 . VAL B 350 ? 0.0792 0.0785 0.0693 -0.0200 0.0146  -0.0107 350 VAL B CG1 
7018 C CG2 . VAL B 350 ? 0.1157 0.1180 0.0998 -0.0206 0.0130  -0.0099 350 VAL B CG2 
7019 N N   . LEU B 351 ? 0.1249 0.1224 0.1205 -0.0184 0.0143  -0.0050 351 LEU B N   
7020 C CA  . LEU B 351 ? 0.1186 0.1139 0.1170 -0.0180 0.0158  -0.0039 351 LEU B CA  
7021 C C   . LEU B 351 ? 0.1438 0.1389 0.1458 -0.0176 0.0151  -0.0049 351 LEU B C   
7022 O O   . LEU B 351 ? 0.0765 0.0732 0.0788 -0.0177 0.0135  -0.0061 351 LEU B O   
7023 C CB  . LEU B 351 ? 0.1094 0.1043 0.1080 -0.0174 0.0157  -0.0009 351 LEU B CB  
7024 C CG  . LEU B 351 ? 0.1241 0.1205 0.1236 -0.0169 0.0137  0.0005  351 LEU B CG  
7025 C CD1 . LEU B 351 ? 0.1528 0.1480 0.1545 -0.0161 0.0141  0.0031  351 LEU B CD1 
7026 C CD2 . LEU B 351 ? 0.1430 0.1415 0.1391 -0.0172 0.0124  0.0008  351 LEU B CD2 
7027 N N   . ASP B 352 ? 0.0967 0.0899 0.1014 -0.0173 0.0165  -0.0044 352 ASP B N   
7028 C CA  . ASP B 352 ? 0.1487 0.1415 0.1570 -0.0170 0.0159  -0.0049 352 ASP B CA  
7029 C C   . ASP B 352 ? 0.1633 0.1577 0.1729 -0.0165 0.0139  -0.0036 352 ASP B C   
7030 O O   . ASP B 352 ? 0.1001 0.0947 0.1091 -0.0161 0.0136  -0.0013 352 ASP B O   
7031 C CB  . ASP B 352 ? 0.1397 0.1302 0.1507 -0.0166 0.0176  -0.0040 352 ASP B CB  
7032 C CG  . ASP B 352 ? 0.1843 0.1733 0.1945 -0.0172 0.0196  -0.0053 352 ASP B CG  
7033 O OD1 . ASP B 352 ? 0.1689 0.1587 0.1768 -0.0177 0.0197  -0.0071 352 ASP B OD1 
7034 O OD2 . ASP B 352 ? 0.2033 0.1906 0.2153 -0.0168 0.0209  -0.0046 352 ASP B OD2 
7035 N N   . GLY B 353 ? 0.0876 0.0831 0.0988 -0.0165 0.0125  -0.0050 353 GLY B N   
7036 C CA  . GLY B 353 ? 0.1208 0.1179 0.1331 -0.0161 0.0105  -0.0041 353 GLY B CA  
7037 C C   . GLY B 353 ? 0.1169 0.1133 0.1331 -0.0154 0.0103  -0.0028 353 GLY B C   
7038 O O   . GLY B 353 ? 0.1360 0.1338 0.1534 -0.0150 0.0087  -0.0019 353 GLY B O   
7039 N N   . GLU B 354 ? 0.0915 0.0857 0.1098 -0.0152 0.0120  -0.0027 354 GLU B N   
7040 C CA  . GLU B 354 ? 0.0674 0.0609 0.0895 -0.0146 0.0119  -0.0018 354 GLU B CA  
7041 C C   . GLU B 354 ? 0.1624 0.1539 0.1859 -0.0142 0.0136  0.0001  354 GLU B C   
7042 O O   . GLU B 354 ? 0.0993 0.0902 0.1258 -0.0136 0.0135  0.0013  354 GLU B O   
7043 C CB  . GLU B 354 ? 0.0437 0.0369 0.0682 -0.0149 0.0119  -0.0040 354 GLU B CB  
7044 C CG  . GLU B 354 ? 0.0609 0.0519 0.0860 -0.0151 0.0140  -0.0050 354 GLU B CG  
7045 C CD  . GLU B 354 ? 0.0928 0.0839 0.1147 -0.0159 0.0147  -0.0068 354 GLU B CD  
7046 O OE1 . GLU B 354 ? 0.0947 0.0859 0.1168 -0.0161 0.0147  -0.0090 354 GLU B OE1 
7047 O OE2 . GLU B 354 ? 0.1136 0.1048 0.1327 -0.0160 0.0152  -0.0060 354 GLU B OE2 
7048 N N   . ASN B 355 ? 0.1100 0.1002 0.1313 -0.0145 0.0152  0.0004  355 ASN B N   
7049 C CA  . ASN B 355 ? 0.1759 0.1639 0.1987 -0.0142 0.0171  0.0017  355 ASN B CA  
7050 C C   . ASN B 355 ? 0.1452 0.1329 0.1675 -0.0136 0.0172  0.0045  355 ASN B C   
7051 O O   . ASN B 355 ? 0.1588 0.1448 0.1831 -0.0132 0.0184  0.0059  355 ASN B O   
7052 C CB  . ASN B 355 ? 0.1698 0.1564 0.1908 -0.0147 0.0190  0.0004  355 ASN B CB  
7053 C CG  . ASN B 355 ? 0.1600 0.1471 0.1810 -0.0140 0.0182  -0.0020 355 ASN B CG  
7054 O OD1 . ASN B 355 ? 0.2185 0.2060 0.2417 -0.0131 0.0172  -0.0022 355 ASN B OD1 
7055 N ND2 . ASN B 355 ? 0.1895 0.1768 0.2081 -0.0143 0.0186  -0.0037 355 ASN B ND2 
7056 N N   . CYS B 356 ? 0.1513 0.1406 0.1710 -0.0136 0.0160  0.0054  356 CYS B N   
7057 C CA  . CYS B 356 ? 0.1453 0.1342 0.1644 -0.0131 0.0162  0.0081  356 CYS B CA  
7058 C C   . CYS B 356 ? 0.1764 0.1661 0.1980 -0.0123 0.0148  0.0099  356 CYS B C   
7059 O O   . CYS B 356 ? 0.1252 0.1140 0.1475 -0.0117 0.0154  0.0122  356 CYS B O   
7060 C CB  . CYS B 356 ? 0.1000 0.0900 0.1150 -0.0135 0.0158  0.0086  356 CYS B CB  
7061 S SG  . CYS B 356 ? 0.1400 0.1332 0.1533 -0.0137 0.0132  0.0074  356 CYS B SG  
7062 N N   . TRP B 357 ? 0.1396 0.1310 0.1627 -0.0122 0.0131  0.0090  357 TRP B N   
7063 C CA  . TRP B 357 ? 0.1164 0.1091 0.1412 -0.0114 0.0114  0.0108  357 TRP B CA  
7064 C C   . TRP B 357 ? 0.0906 0.0817 0.1191 -0.0107 0.0122  0.0123  357 TRP B C   
7065 O O   . TRP B 357 ? 0.1222 0.1138 0.1518 -0.0100 0.0114  0.0144  357 TRP B O   
7066 C CB  . TRP B 357 ? 0.0580 0.0529 0.0834 -0.0116 0.0094  0.0092  357 TRP B CB  
7067 C CG  . TRP B 357 ? 0.1113 0.1075 0.1332 -0.0124 0.0088  0.0075  357 TRP B CG  
7068 C CD1 . TRP B 357 ? 0.0818 0.0783 0.1032 -0.0131 0.0088  0.0048  357 TRP B CD1 
7069 C CD2 . TRP B 357 ? 0.1033 0.1007 0.1216 -0.0126 0.0083  0.0083  357 TRP B CD2 
7070 N NE1 . TRP B 357 ? 0.0815 0.0794 0.0994 -0.0137 0.0082  0.0039  357 TRP B NE1 
7071 C CE2 . TRP B 357 ? 0.0925 0.0909 0.1083 -0.0135 0.0080  0.0060  357 TRP B CE2 
7072 C CE3 . TRP B 357 ? 0.1135 0.1112 0.1304 -0.0122 0.0081  0.0108  357 TRP B CE3 
7073 C CZ2 . TRP B 357 ? 0.1437 0.1434 0.1558 -0.0139 0.0075  0.0060  357 TRP B CZ2 
7074 C CZ3 . TRP B 357 ? 0.1069 0.1058 0.1199 -0.0127 0.0076  0.0109  357 TRP B CZ3 
7075 C CH2 . TRP B 357 ? 0.1405 0.1405 0.1512 -0.0135 0.0073  0.0085  357 TRP B CH2 
7076 N N   . GLU B 358 ? 0.0934 0.0827 0.1240 -0.0109 0.0137  0.0111  358 GLU B N   
7077 C CA  . GLU B 358 ? 0.1393 0.1271 0.1734 -0.0102 0.0145  0.0124  358 GLU B CA  
7078 C C   . GLU B 358 ? 0.0867 0.0730 0.1204 -0.0097 0.0157  0.0150  358 GLU B C   
7079 O O   . GLU B 358 ? 0.1451 0.1306 0.1816 -0.0089 0.0160  0.0166  358 GLU B O   
7080 C CB  . GLU B 358 ? 0.0950 0.0812 0.1303 -0.0103 0.0158  0.0105  358 GLU B CB  
7081 C CG  . GLU B 358 ? 0.0945 0.0798 0.1262 -0.0103 0.0170  0.0092  358 GLU B CG  
7082 C CD  . GLU B 358 ? 0.1894 0.1751 0.2202 -0.0100 0.0168  0.0063  358 GLU B CD  
7083 O OE1 . GLU B 358 ? 0.2252 0.2106 0.2549 -0.0089 0.0171  0.0056  358 GLU B OE1 
7084 O OE2 . GLU B 358 ? 0.1718 0.1583 0.2032 -0.0108 0.0161  0.0049  358 GLU B OE2 
7085 N N   . TYR B 359 ? 0.1223 0.1084 0.1525 -0.0100 0.0163  0.0154  359 TYR B N   
7086 C CA  . TYR B 359 ? 0.1813 0.1660 0.2107 -0.0096 0.0175  0.0178  359 TYR B CA  
7087 C C   . TYR B 359 ? 0.1630 0.1494 0.1911 -0.0091 0.0159  0.0199  359 TYR B C   
7088 O O   . TYR B 359 ? 0.1641 0.1495 0.1919 -0.0086 0.0165  0.0222  359 TYR B O   
7089 C CB  . TYR B 359 ? 0.1770 0.1603 0.2033 -0.0103 0.0193  0.0172  359 TYR B CB  
7090 C CG  . TYR B 359 ? 0.1256 0.1083 0.1516 -0.0100 0.0197  0.0144  359 TYR B CG  
7091 C CD1 . TYR B 359 ? 0.1174 0.0997 0.1438 -0.0088 0.0197  0.0139  359 TYR B CD1 
7092 C CD2 . TYR B 359 ? 0.2092 0.1924 0.2341 -0.0109 0.0197  0.0120  359 TYR B CD2 
7093 C CE1 . TYR B 359 ? 0.1326 0.1150 0.1584 -0.0083 0.0197  0.0115  359 TYR B CE1 
7094 C CE2 . TYR B 359 ? 0.2383 0.2214 0.2625 -0.0103 0.0197  0.0096  359 TYR B CE2 
7095 C CZ  . TYR B 359 ? 0.2927 0.2756 0.3175 -0.0090 0.0196  0.0094  359 TYR B CZ  
7096 O OH  . TYR B 359 ? 0.2851 0.2682 0.3092 -0.0083 0.0196  0.0073  359 TYR B OH  
7097 N N   . TYR B 360 ? 0.1430 0.1320 0.1703 -0.0092 0.0138  0.0192  360 TYR B N   
7098 C CA  . TYR B 360 ? 0.1613 0.1522 0.1876 -0.0087 0.0120  0.0211  360 TYR B CA  
7099 C C   . TYR B 360 ? 0.1539 0.1454 0.1839 -0.0078 0.0109  0.0224  360 TYR B C   
7100 O O   . TYR B 360 ? 0.1855 0.1769 0.2184 -0.0077 0.0108  0.0212  360 TYR B O   
7101 C CB  . TYR B 360 ? 0.1774 0.1708 0.2013 -0.0092 0.0102  0.0196  360 TYR B CB  
7102 C CG  . TYR B 360 ? 0.1611 0.1548 0.1808 -0.0101 0.0106  0.0187  360 TYR B CG  
7103 C CD1 . TYR B 360 ? 0.1339 0.1263 0.1525 -0.0108 0.0122  0.0167  360 TYR B CD1 
7104 C CD2 . TYR B 360 ? 0.1773 0.1728 0.1941 -0.0101 0.0093  0.0198  360 TYR B CD2 
7105 C CE1 . TYR B 360 ? 0.1477 0.1404 0.1624 -0.0116 0.0125  0.0158  360 TYR B CE1 
7106 C CE2 . TYR B 360 ? 0.1521 0.1480 0.1651 -0.0109 0.0096  0.0189  360 TYR B CE2 
7107 C CZ  . TYR B 360 ? 0.0922 0.0867 0.1041 -0.0116 0.0112  0.0169  360 TYR B CZ  
7108 O OH  . TYR B 360 ? 0.1150 0.1100 0.1231 -0.0123 0.0114  0.0160  360 TYR B OH  
7109 N N   . GLU B 361 ? 0.1884 0.1806 0.2182 -0.0070 0.0101  0.0249  361 GLU B N   
7110 C CA  . GLU B 361 ? 0.1787 0.1720 0.2118 -0.0062 0.0087  0.0262  361 GLU B CA  
7111 C C   . GLU B 361 ? 0.1905 0.1863 0.2241 -0.0065 0.0067  0.0245  361 GLU B C   
7112 O O   . GLU B 361 ? 0.1679 0.1655 0.1987 -0.0071 0.0056  0.0234  361 GLU B O   
7113 C CB  . GLU B 361 ? 0.2503 0.2443 0.2826 -0.0054 0.0080  0.0291  361 GLU B CB  
7114 C CG  . GLU B 361 ? 0.4893 0.4807 0.5212 -0.0050 0.0100  0.0310  361 GLU B CG  
7115 C CD  . GLU B 361 ? 0.6451 0.6343 0.6808 -0.0045 0.0115  0.0315  361 GLU B CD  
7116 O OE1 . GLU B 361 ? 0.6620 0.6487 0.6975 -0.0047 0.0136  0.0312  361 GLU B OE1 
7117 O OE2 . GLU B 361 ? 0.7198 0.7098 0.7587 -0.0038 0.0105  0.0321  361 GLU B OE2 
7118 N N   . GLU B 362 ? 0.1798 0.1758 0.2172 -0.0061 0.0062  0.0242  362 GLU B N   
7119 C CA  . GLU B 362 ? 0.1732 0.1714 0.2117 -0.0063 0.0043  0.0226  362 GLU B CA  
7120 C C   . GLU B 362 ? 0.1314 0.1300 0.1675 -0.0074 0.0043  0.0198  362 GLU B C   
7121 O O   . GLU B 362 ? 0.1854 0.1863 0.2200 -0.0078 0.0026  0.0188  362 GLU B O   
7122 C CB  . GLU B 362 ? 0.2172 0.2181 0.2553 -0.0058 0.0021  0.0242  362 GLU B CB  
7123 C CG  . GLU B 362 ? 0.3027 0.3030 0.3426 -0.0047 0.0023  0.0272  362 GLU B CG  
7124 C CD  . GLU B 362 ? 0.5067 0.5097 0.5476 -0.0041 0.0000  0.0286  362 GLU B CD  
7125 O OE1 . GLU B 362 ? 0.5007 0.5062 0.5399 -0.0046 -0.0017 0.0277  362 GLU B OE1 
7126 O OE2 . GLU B 362 ? 0.6186 0.6214 0.6622 -0.0031 0.0000  0.0307  362 GLU B OE2 
7127 N N   . ASN B 363 ? 0.0738 0.0702 0.1093 -0.0079 0.0063  0.0186  363 ASN B N   
7128 C CA  . ASN B 363 ? 0.0823 0.0789 0.1163 -0.0088 0.0065  0.0157  363 ASN B CA  
7129 C C   . ASN B 363 ? 0.1994 0.1975 0.2292 -0.0094 0.0056  0.0152  363 ASN B C   
7130 O O   . ASN B 363 ? 0.1743 0.1736 0.2029 -0.0101 0.0048  0.0129  363 ASN B O   
7131 C CB  . ASN B 363 ? 0.1144 0.1120 0.1510 -0.0090 0.0054  0.0140  363 ASN B CB  
7132 C CG  . ASN B 363 ? 0.1794 0.1765 0.2151 -0.0099 0.0060  0.0111  363 ASN B CG  
7133 O OD1 . ASN B 363 ? 0.1675 0.1626 0.2021 -0.0102 0.0078  0.0105  363 ASN B OD1 
7134 N ND2 . ASN B 363 ? 0.1633 0.1620 0.1994 -0.0102 0.0045  0.0093  363 ASN B ND2 
7135 N N   . GLY B 364 ? 0.1518 0.1500 0.1794 -0.0092 0.0058  0.0171  364 GLY B N   
7136 C CA  . GLY B 364 ? 0.1066 0.1063 0.1302 -0.0098 0.0050  0.0168  364 GLY B CA  
7137 C C   . GLY B 364 ? 0.1501 0.1528 0.1731 -0.0098 0.0026  0.0166  364 GLY B C   
7138 O O   . GLY B 364 ? 0.1512 0.1553 0.1709 -0.0104 0.0018  0.0161  364 GLY B O   
7139 N N   . ILE B 365 ? 0.0746 0.0784 0.1007 -0.0093 0.0013  0.0171  365 ILE B N   
7140 C CA  . ILE B 365 ? 0.1259 0.1326 0.1515 -0.0094 -0.0011 0.0167  365 ILE B CA  
7141 C C   . ILE B 365 ? 0.1808 0.1890 0.2042 -0.0091 -0.0022 0.0190  365 ILE B C   
7142 O O   . ILE B 365 ? 0.1379 0.1481 0.1585 -0.0097 -0.0034 0.0183  365 ILE B O   
7143 C CB  . ILE B 365 ? 0.1733 0.1807 0.2029 -0.0090 -0.0021 0.0166  365 ILE B CB  
7144 C CG1 . ILE B 365 ? 0.1310 0.1371 0.1622 -0.0095 -0.0012 0.0140  365 ILE B CG1 
7145 C CG2 . ILE B 365 ? 0.1645 0.1750 0.1937 -0.0090 -0.0046 0.0166  365 ILE B CG2 
7146 C CD1 . ILE B 365 ? 0.1678 0.1735 0.2033 -0.0089 -0.0014 0.0142  365 ILE B CD1 
7147 N N   . PRO B 366 ? 0.2002 0.2075 0.2246 -0.0082 -0.0017 0.0217  366 PRO B N   
7148 C CA  . PRO B 366 ? 0.1825 0.1913 0.2045 -0.0080 -0.0026 0.0238  366 PRO B CA  
7149 C C   . PRO B 366 ? 0.1538 0.1624 0.1714 -0.0088 -0.0020 0.0231  366 PRO B C   
7150 O O   . PRO B 366 ? 0.1187 0.1294 0.1336 -0.0091 -0.0034 0.0234  366 PRO B O   
7151 C CB  . PRO B 366 ? 0.1771 0.1842 0.2010 -0.0070 -0.0016 0.0266  366 PRO B CB  
7152 C CG  . PRO B 366 ? 0.1443 0.1502 0.1724 -0.0065 -0.0011 0.0261  366 PRO B CG  
7153 C CD  . PRO B 366 ? 0.1434 0.1487 0.1714 -0.0074 -0.0005 0.0230  366 PRO B CD  
7154 N N   . PHE B 367 ? 0.1297 0.1359 0.1465 -0.0092 0.0001  0.0221  367 PHE B N   
7155 C CA  . PHE B 367 ? 0.1410 0.1471 0.1538 -0.0100 0.0008  0.0213  367 PHE B CA  
7156 C C   . PHE B 367 ? 0.1512 0.1593 0.1619 -0.0109 -0.0005 0.0189  367 PHE B C   
7157 O O   . PHE B 367 ? 0.1455 0.1552 0.1530 -0.0113 -0.0014 0.0191  367 PHE B O   
7158 C CB  . PHE B 367 ? 0.1910 0.1942 0.2036 -0.0102 0.0033  0.0206  367 PHE B CB  
7159 C CG  . PHE B 367 ? 0.1920 0.1951 0.2005 -0.0111 0.0040  0.0196  367 PHE B CG  
7160 C CD1 . PHE B 367 ? 0.1333 0.1364 0.1389 -0.0110 0.0042  0.0215  367 PHE B CD1 
7161 C CD2 . PHE B 367 ? 0.1345 0.1374 0.1420 -0.0119 0.0045  0.0167  367 PHE B CD2 
7162 C CE1 . PHE B 367 ? 0.1744 0.1776 0.1763 -0.0119 0.0049  0.0205  367 PHE B CE1 
7163 C CE2 . PHE B 367 ? 0.1374 0.1404 0.1412 -0.0127 0.0052  0.0157  367 PHE B CE2 
7164 C CZ  . PHE B 367 ? 0.1653 0.1684 0.1663 -0.0127 0.0054  0.0176  367 PHE B CZ  
7165 N N   . LEU B 368 ? 0.0968 0.1049 0.1093 -0.0112 -0.0006 0.0165  368 LEU B N   
7166 C CA  . LEU B 368 ? 0.0723 0.0822 0.0828 -0.0121 -0.0016 0.0140  368 LEU B CA  
7167 C C   . LEU B 368 ? 0.0742 0.0871 0.0842 -0.0121 -0.0041 0.0146  368 LEU B C   
7168 O O   . LEU B 368 ? 0.0866 0.1012 0.0936 -0.0127 -0.0050 0.0136  368 LEU B O   
7169 C CB  . LEU B 368 ? 0.0690 0.0780 0.0815 -0.0124 -0.0012 0.0114  368 LEU B CB  
7170 C CG  . LEU B 368 ? 0.0922 0.0988 0.1039 -0.0128 0.0011  0.0102  368 LEU B CG  
7171 C CD1 . LEU B 368 ? 0.1577 0.1636 0.1713 -0.0132 0.0015  0.0076  368 LEU B CD1 
7172 C CD2 . LEU B 368 ? 0.1399 0.1468 0.1473 -0.0135 0.0016  0.0097  368 LEU B CD2 
7173 N N   . GLU B 369 ? 0.1244 0.1380 0.1374 -0.0113 -0.0051 0.0160  369 GLU B N   
7174 C CA  . GLU B 369 ? 0.1434 0.1600 0.1560 -0.0113 -0.0075 0.0166  369 GLU B CA  
7175 C C   . GLU B 369 ? 0.2089 0.2266 0.2182 -0.0113 -0.0080 0.0184  369 GLU B C   
7176 O O   . GLU B 369 ? 0.1238 0.1438 0.1307 -0.0118 -0.0095 0.0178  369 GLU B O   
7177 C CB  . GLU B 369 ? 0.0788 0.0958 0.0954 -0.0104 -0.0084 0.0180  369 GLU B CB  
7178 C CG  . GLU B 369 ? 0.1169 0.1337 0.1365 -0.0106 -0.0085 0.0157  369 GLU B CG  
7179 C CD  . GLU B 369 ? 0.2474 0.2648 0.2710 -0.0098 -0.0094 0.0169  369 GLU B CD  
7180 O OE1 . GLU B 369 ? 0.2144 0.2319 0.2388 -0.0090 -0.0096 0.0196  369 GLU B OE1 
7181 O OE2 . GLU B 369 ? 0.2025 0.2201 0.2283 -0.0100 -0.0099 0.0152  369 GLU B OE2 
7182 N N   . LYS B 370 ? 0.1170 0.1331 0.1260 -0.0107 -0.0068 0.0207  370 LYS B N   
7183 C CA  . LYS B 370 ? 0.1610 0.1780 0.1667 -0.0107 -0.0072 0.0225  370 LYS B CA  
7184 C C   . LYS B 370 ? 0.1650 0.1820 0.1667 -0.0118 -0.0066 0.0208  370 LYS B C   
7185 O O   . LYS B 370 ? 0.1358 0.1548 0.1345 -0.0122 -0.0077 0.0211  370 LYS B O   
7186 C CB  . LYS B 370 ? 0.1941 0.2093 0.2006 -0.0099 -0.0059 0.0253  370 LYS B CB  
7187 C CG  . LYS B 370 ? 0.3202 0.3357 0.3302 -0.0088 -0.0068 0.0275  370 LYS B CG  
7188 C CD  . LYS B 370 ? 0.3746 0.3878 0.3855 -0.0080 -0.0052 0.0300  370 LYS B CD  
7189 C CE  . LYS B 370 ? 0.3810 0.3940 0.3960 -0.0069 -0.0056 0.0317  370 LYS B CE  
7190 N NZ  . LYS B 370 ? 0.3473 0.3634 0.3628 -0.0065 -0.0080 0.0330  370 LYS B NZ  
7191 N N   . LEU B 371 ? 0.1870 0.2019 0.1887 -0.0122 -0.0047 0.0190  371 LEU B N   
7192 C CA  . LEU B 371 ? 0.1007 0.1155 0.0986 -0.0131 -0.0040 0.0173  371 LEU B CA  
7193 C C   . LEU B 371 ? 0.1450 0.1622 0.1415 -0.0139 -0.0056 0.0151  371 LEU B C   
7194 O O   . LEU B 371 ? 0.1802 0.1989 0.1732 -0.0145 -0.0063 0.0148  371 LEU B O   
7195 C CB  . LEU B 371 ? 0.0811 0.0932 0.0796 -0.0134 -0.0018 0.0158  371 LEU B CB  
7196 C CG  . LEU B 371 ? 0.1318 0.1437 0.1268 -0.0143 -0.0009 0.0138  371 LEU B CG  
7197 C CD1 . LEU B 371 ? 0.1526 0.1646 0.1442 -0.0145 -0.0004 0.0155  371 LEU B CD1 
7198 C CD2 . LEU B 371 ? 0.1195 0.1290 0.1156 -0.0146 0.0011  0.0120  371 LEU B CD2 
7199 N N   . TYR B 372 ? 0.1251 0.1428 0.1243 -0.0139 -0.0064 0.0135  372 TYR B N   
7200 C CA  . TYR B 372 ? 0.1295 0.1493 0.1274 -0.0147 -0.0078 0.0112  372 TYR B CA  
7201 C C   . TYR B 372 ? 0.2261 0.2489 0.2229 -0.0147 -0.0100 0.0124  372 TYR B C   
7202 O O   . TYR B 372 ? 0.2033 0.2279 0.1972 -0.0155 -0.0110 0.0111  372 TYR B O   
7203 C CB  . TYR B 372 ? 0.0956 0.1151 0.0968 -0.0147 -0.0080 0.0092  372 TYR B CB  
7204 C CG  . TYR B 372 ? 0.0884 0.1053 0.0903 -0.0149 -0.0059 0.0075  372 TYR B CG  
7205 C CD1 . TYR B 372 ? 0.1892 0.2048 0.1882 -0.0154 -0.0043 0.0069  372 TYR B CD1 
7206 C CD2 . TYR B 372 ? 0.0908 0.1066 0.0961 -0.0147 -0.0056 0.0064  372 TYR B CD2 
7207 C CE1 . TYR B 372 ? 0.1611 0.1745 0.1609 -0.0156 -0.0025 0.0053  372 TYR B CE1 
7208 C CE2 . TYR B 372 ? 0.1261 0.1397 0.1321 -0.0149 -0.0038 0.0048  372 TYR B CE2 
7209 C CZ  . TYR B 372 ? 0.1429 0.1554 0.1461 -0.0154 -0.0023 0.0042  372 TYR B CZ  
7210 O OH  . TYR B 372 ? 0.1135 0.1239 0.1175 -0.0156 -0.0006 0.0026  372 TYR B OH  
7211 N N   . SER B 373 ? 0.1763 0.1996 0.1752 -0.0138 -0.0109 0.0148  373 SER B N   
7212 C CA  . SER B 373 ? 0.1600 0.1861 0.1579 -0.0138 -0.0130 0.0161  373 SER B CA  
7213 C C   . SER B 373 ? 0.1973 0.2240 0.1912 -0.0141 -0.0129 0.0174  373 SER B C   
7214 O O   . SER B 373 ? 0.2329 0.2622 0.2246 -0.0145 -0.0145 0.0174  373 SER B O   
7215 C CB  . SER B 373 ? 0.3009 0.3274 0.3021 -0.0127 -0.0138 0.0185  373 SER B CB  
7216 O OG  . SER B 373 ? 0.4425 0.4667 0.4447 -0.0120 -0.0122 0.0206  373 SER B OG  
7217 N N   . THR B 374 ? 0.1769 0.2015 0.1700 -0.0138 -0.0111 0.0186  374 THR B N   
7218 C CA  . THR B 374 ? 0.2252 0.2501 0.2144 -0.0141 -0.0109 0.0198  374 THR B CA  
7219 C C   . THR B 374 ? 0.3105 0.3360 0.2963 -0.0153 -0.0107 0.0172  374 THR B C   
7220 O O   . THR B 374 ? 0.2863 0.3140 0.2691 -0.0158 -0.0118 0.0172  374 THR B O   
7221 C CB  . THR B 374 ? 0.2393 0.2615 0.2286 -0.0136 -0.0089 0.0217  374 THR B CB  
7222 O OG1 . THR B 374 ? 0.2209 0.2426 0.2135 -0.0125 -0.0091 0.0240  374 THR B OG1 
7223 C CG2 . THR B 374 ? 0.2842 0.3069 0.2696 -0.0139 -0.0087 0.0231  374 THR B CG2 
7224 N N   . LEU B 375 ? 0.2700 0.2938 0.2563 -0.0157 -0.0092 0.0149  375 LEU B N   
7225 C CA  . LEU B 375 ? 0.2031 0.2273 0.1864 -0.0167 -0.0089 0.0123  375 LEU B CA  
7226 C C   . LEU B 375 ? 0.3014 0.3284 0.2839 -0.0173 -0.0110 0.0108  375 LEU B C   
7227 O O   . LEU B 375 ? 0.2961 0.3246 0.2752 -0.0181 -0.0115 0.0098  375 LEU B O   
7228 C CB  . LEU B 375 ? 0.1333 0.1552 0.1181 -0.0169 -0.0072 0.0101  375 LEU B CB  
7229 C CG  . LEU B 375 ? 0.1428 0.1620 0.1276 -0.0166 -0.0049 0.0109  375 LEU B CG  
7230 C CD1 . LEU B 375 ? 0.1369 0.1540 0.1234 -0.0168 -0.0034 0.0086  375 LEU B CD1 
7231 C CD2 . LEU B 375 ? 0.2296 0.2489 0.2101 -0.0172 -0.0042 0.0111  375 LEU B CD2 
7232 N N   . GLU B 376 ? 0.3463 0.3742 0.3320 -0.0169 -0.0122 0.0106  376 GLU B N   
7233 C CA  . GLU B 376 ? 0.3032 0.3336 0.2886 -0.0174 -0.0142 0.0091  376 GLU B CA  
7234 C C   . GLU B 376 ? 0.4085 0.4416 0.3908 -0.0178 -0.0158 0.0102  376 GLU B C   
7235 O O   . GLU B 376 ? 0.3624 0.3975 0.3429 -0.0186 -0.0170 0.0085  376 GLU B O   
7236 C CB  . GLU B 376 ? 0.3226 0.3534 0.3123 -0.0168 -0.0152 0.0096  376 GLU B CB  
7237 C CG  . GLU B 376 ? 0.4121 0.4453 0.4024 -0.0172 -0.0172 0.0082  376 GLU B CG  
7238 C CD  . GLU B 376 ? 0.4014 0.4344 0.3961 -0.0164 -0.0178 0.0088  376 GLU B CD  
7239 O OE1 . GLU B 376 ? 0.4301 0.4633 0.4264 -0.0156 -0.0181 0.0115  376 GLU B OE1 
7240 O OE2 . GLU B 376 ? 0.4842 0.5169 0.4808 -0.0167 -0.0178 0.0067  376 GLU B OE2 
7241 N N   . LYS B 377 ? 0.3685 0.4016 0.3502 -0.0172 -0.0157 0.0131  377 LYS B N   
7242 C CA  . LYS B 377 ? 0.3745 0.4102 0.3537 -0.0175 -0.0173 0.0146  377 LYS B CA  
7243 C C   . LYS B 377 ? 0.4147 0.4501 0.3899 -0.0179 -0.0164 0.0153  377 LYS B C   
7244 O O   . LYS B 377 ? 0.3804 0.4178 0.3530 -0.0182 -0.0177 0.0164  377 LYS B O   
7245 C CB  . LYS B 377 ? 0.4848 0.5212 0.4663 -0.0164 -0.0184 0.0176  377 LYS B CB  
7246 C CG  . LYS B 377 ? 0.4644 0.5016 0.4498 -0.0160 -0.0196 0.0171  377 LYS B CG  
7247 C CD  . LYS B 377 ? 0.5596 0.5961 0.5483 -0.0148 -0.0196 0.0199  377 LYS B CD  
7248 C CE  . LYS B 377 ? 0.5901 0.6266 0.5830 -0.0144 -0.0201 0.0191  377 LYS B CE  
7249 N NZ  . LYS B 377 ? 0.6157 0.6509 0.6118 -0.0132 -0.0197 0.0217  377 LYS B NZ  
7250 N N   . GLU B 378 ? 0.3056 0.3383 0.2801 -0.0180 -0.0143 0.0147  378 GLU B N   
7251 C CA  . GLU B 378 ? 0.3552 0.3875 0.3257 -0.0185 -0.0133 0.0150  378 GLU B CA  
7252 C C   . GLU B 378 ? 0.3532 0.3871 0.3207 -0.0196 -0.0138 0.0123  378 GLU B C   
7253 O O   . GLU B 378 ? 0.4176 0.4505 0.3854 -0.0201 -0.0129 0.0097  378 GLU B O   
7254 C CB  . GLU B 378 ? 0.4385 0.4676 0.4095 -0.0182 -0.0108 0.0150  378 GLU B CB  
7255 C CG  . GLU B 378 ? 0.4760 0.5034 0.4494 -0.0172 -0.0101 0.0179  378 GLU B CG  
7256 C CD  . GLU B 378 ? 0.6408 0.6686 0.6116 -0.0170 -0.0101 0.0205  378 GLU B CD  
7257 O OE1 . GLU B 378 ? 0.7128 0.7423 0.6800 -0.0178 -0.0107 0.0202  378 GLU B OE1 
7258 O OE2 . GLU B 378 ? 0.7056 0.7318 0.6778 -0.0162 -0.0093 0.0230  378 GLU B OE2 
7259 N N   . GLU B 379 ? 0.3798 0.4162 0.3444 -0.0201 -0.0152 0.0130  379 GLU B N   
7260 C CA  . GLU B 379 ? 0.3561 0.3943 0.3180 -0.0212 -0.0159 0.0104  379 GLU B CA  
7261 C C   . GLU B 379 ? 0.3487 0.3853 0.3077 -0.0219 -0.0141 0.0088  379 GLU B C   
7262 O O   . GLU B 379 ? 0.3350 0.3724 0.2927 -0.0227 -0.0141 0.0061  379 GLU B O   
7263 C CB  . GLU B 379 ? 0.4671 0.5083 0.4265 -0.0216 -0.0178 0.0116  379 GLU B CB  
7264 C CG  . GLU B 379 ? 0.6258 0.6690 0.5876 -0.0213 -0.0199 0.0122  379 GLU B CG  
7265 C CD  . GLU B 379 ? 0.7961 0.8416 0.7565 -0.0211 -0.0215 0.0148  379 GLU B CD  
7266 O OE1 . GLU B 379 ? 0.8358 0.8826 0.7925 -0.0218 -0.0218 0.0150  379 GLU B OE1 
7267 O OE2 . GLU B 379 ? 0.8251 0.8711 0.7883 -0.0203 -0.0225 0.0168  379 GLU B OE2 
7268 N N   . TRP B 380 ? 0.2478 0.2825 0.2061 -0.0216 -0.0124 0.0104  380 TRP B N   
7269 C CA  . TRP B 380 ? 0.2540 0.2874 0.2096 -0.0222 -0.0107 0.0090  380 TRP B CA  
7270 C C   . TRP B 380 ? 0.2031 0.2340 0.1610 -0.0220 -0.0089 0.0073  380 TRP B C   
7271 O O   . TRP B 380 ? 0.2358 0.2655 0.1918 -0.0226 -0.0073 0.0059  380 TRP B O   
7272 C CB  . TRP B 380 ? 0.2848 0.3175 0.2382 -0.0221 -0.0098 0.0115  380 TRP B CB  
7273 C CG  . TRP B 380 ? 0.2917 0.3226 0.2478 -0.0210 -0.0092 0.0142  380 TRP B CG  
7274 C CD1 . TRP B 380 ? 0.3355 0.3674 0.2930 -0.0203 -0.0105 0.0167  380 TRP B CD1 
7275 C CD2 . TRP B 380 ? 0.3132 0.3411 0.2708 -0.0205 -0.0070 0.0146  380 TRP B CD2 
7276 N NE1 . TRP B 380 ? 0.2460 0.2756 0.2060 -0.0193 -0.0093 0.0186  380 TRP B NE1 
7277 C CE2 . TRP B 380 ? 0.2559 0.2830 0.2159 -0.0195 -0.0072 0.0174  380 TRP B CE2 
7278 C CE3 . TRP B 380 ? 0.2162 0.2419 0.1733 -0.0209 -0.0050 0.0128  380 TRP B CE3 
7279 C CZ2 . TRP B 380 ? 0.2605 0.2848 0.2225 -0.0189 -0.0054 0.0185  380 TRP B CZ2 
7280 C CZ3 . TRP B 380 ? 0.2278 0.2508 0.1869 -0.0203 -0.0032 0.0140  380 TRP B CZ3 
7281 C CH2 . TRP B 380 ? 0.2255 0.2478 0.1870 -0.0193 -0.0034 0.0167  380 TRP B CH2 
7282 N N   . ILE B 381 ? 0.1986 0.2286 0.1605 -0.0213 -0.0090 0.0073  381 ILE B N   
7283 C CA  . ILE B 381 ? 0.2310 0.2587 0.1951 -0.0212 -0.0075 0.0056  381 ILE B CA  
7284 C C   . ILE B 381 ? 0.2546 0.2835 0.2201 -0.0216 -0.0086 0.0029  381 ILE B C   
7285 O O   . ILE B 381 ? 0.2602 0.2908 0.2271 -0.0214 -0.0104 0.0033  381 ILE B O   
7286 C CB  . ILE B 381 ? 0.2296 0.2553 0.1975 -0.0202 -0.0067 0.0074  381 ILE B CB  
7287 C CG1 . ILE B 381 ? 0.2145 0.2388 0.1811 -0.0198 -0.0055 0.0101  381 ILE B CG1 
7288 C CG2 . ILE B 381 ? 0.2051 0.2285 0.1752 -0.0201 -0.0051 0.0055  381 ILE B CG2 
7289 C CD1 . ILE B 381 ? 0.2445 0.2670 0.2145 -0.0187 -0.0049 0.0122  381 ILE B CD1 
7290 N N   . GLU B 382 ? 0.1693 0.1973 0.1343 -0.0221 -0.0075 0.0003  382 GLU B N   
7291 C CA  . GLU B 382 ? 0.1922 0.2208 0.1588 -0.0224 -0.0083 -0.0023 382 GLU B CA  
7292 C C   . GLU B 382 ? 0.1936 0.2196 0.1627 -0.0221 -0.0066 -0.0036 382 GLU B C   
7293 O O   . GLU B 382 ? 0.1819 0.2066 0.1495 -0.0224 -0.0049 -0.0047 382 GLU B O   
7294 C CB  . GLU B 382 ? 0.2101 0.2404 0.1734 -0.0234 -0.0089 -0.0046 382 GLU B CB  
7295 C CG  . GLU B 382 ? 0.2836 0.3146 0.2483 -0.0237 -0.0096 -0.0074 382 GLU B CG  
7296 C CD  . GLU B 382 ? 0.4741 0.5068 0.4354 -0.0248 -0.0101 -0.0096 382 GLU B CD  
7297 O OE1 . GLU B 382 ? 0.5178 0.5519 0.4759 -0.0252 -0.0106 -0.0086 382 GLU B OE1 
7298 O OE2 . GLU B 382 ? 0.5291 0.5616 0.4908 -0.0251 -0.0099 -0.0123 382 GLU B OE2 
7299 N N   . THR B 383 ? 0.2197 0.2451 0.1925 -0.0215 -0.0070 -0.0034 383 THR B N   
7300 C CA  . THR B 383 ? 0.1416 0.1649 0.1169 -0.0213 -0.0055 -0.0049 383 THR B CA  
7301 C C   . THR B 383 ? 0.2314 0.2552 0.2061 -0.0220 -0.0058 -0.0082 383 THR B C   
7302 O O   . THR B 383 ? 0.2221 0.2480 0.1961 -0.0224 -0.0074 -0.0092 383 THR B O   
7303 C CB  . THR B 383 ? 0.1590 0.1815 0.1386 -0.0204 -0.0059 -0.0038 383 THR B CB  
7304 O OG1 . THR B 383 ? 0.1703 0.1948 0.1510 -0.0205 -0.0080 -0.0040 383 THR B OG1 
7305 C CG2 . THR B 383 ? 0.2403 0.2617 0.2207 -0.0197 -0.0053 -0.0006 383 THR B CG2 
7306 N N   . LEU B 384 ? 0.1477 0.1696 0.1228 -0.0221 -0.0041 -0.0098 384 LEU B N   
7307 C CA  . LEU B 384 ? 0.1398 0.1620 0.1142 -0.0227 -0.0039 -0.0129 384 LEU B CA  
7308 C C   . LEU B 384 ? 0.1508 0.1711 0.1284 -0.0224 -0.0031 -0.0142 384 LEU B C   
7309 O O   . LEU B 384 ? 0.1303 0.1487 0.1099 -0.0219 -0.0018 -0.0131 384 LEU B O   
7310 C CB  . LEU B 384 ? 0.1496 0.1714 0.1205 -0.0233 -0.0026 -0.0139 384 LEU B CB  
7311 C CG  . LEU B 384 ? 0.2280 0.2514 0.1950 -0.0238 -0.0031 -0.0129 384 LEU B CG  
7312 C CD1 . LEU B 384 ? 0.1561 0.1790 0.1201 -0.0243 -0.0016 -0.0142 384 LEU B CD1 
7313 C CD2 . LEU B 384 ? 0.1969 0.2230 0.1629 -0.0242 -0.0052 -0.0137 384 LEU B CD2 
7314 N N   . THR B 385 ? 0.1364 0.1574 0.1145 -0.0228 -0.0037 -0.0167 385 THR B N   
7315 C CA  . THR B 385 ? 0.1116 0.1309 0.0922 -0.0227 -0.0027 -0.0184 385 THR B CA  
7316 C C   . THR B 385 ? 0.1395 0.1575 0.1180 -0.0230 -0.0008 -0.0197 385 THR B C   
7317 O O   . THR B 385 ? 0.1802 0.1990 0.1553 -0.0235 -0.0006 -0.0197 385 THR B O   
7318 C CB  . THR B 385 ? 0.1309 0.1512 0.1125 -0.0230 -0.0039 -0.0207 385 THR B CB  
7319 O OG1 . THR B 385 ? 0.1932 0.2147 0.1714 -0.0238 -0.0042 -0.0226 385 THR B OG1 
7320 C CG2 . THR B 385 ? 0.1434 0.1653 0.1266 -0.0228 -0.0060 -0.0196 385 THR B CG2 
7321 N N   . LEU B 386 ? 0.1028 0.1189 0.0833 -0.0228 0.0005  -0.0209 386 LEU B N   
7322 C CA  . LEU B 386 ? 0.1348 0.1498 0.1136 -0.0231 0.0023  -0.0223 386 LEU B CA  
7323 C C   . LEU B 386 ? 0.1581 0.1745 0.1341 -0.0239 0.0017  -0.0246 386 LEU B C   
7324 O O   . LEU B 386 ? 0.1918 0.2084 0.1649 -0.0243 0.0026  -0.0251 386 LEU B O   
7325 C CB  . LEU B 386 ? 0.0855 0.0984 0.0671 -0.0229 0.0035  -0.0234 386 LEU B CB  
7326 C CG  . LEU B 386 ? 0.1679 0.1792 0.1525 -0.0222 0.0043  -0.0214 386 LEU B CG  
7327 C CD1 . LEU B 386 ? 0.1607 0.1700 0.1477 -0.0220 0.0056  -0.0227 386 LEU B CD1 
7328 C CD2 . LEU B 386 ? 0.1667 0.1774 0.1496 -0.0220 0.0054  -0.0192 386 LEU B CD2 
7329 N N   . GLU B 387 ? 0.1923 0.2099 0.1693 -0.0241 0.0002  -0.0261 387 GLU B N   
7330 C CA  . GLU B 387 ? 0.2002 0.2192 0.1746 -0.0248 -0.0004 -0.0283 387 GLU B CA  
7331 C C   . GLU B 387 ? 0.1789 0.1998 0.1498 -0.0252 -0.0011 -0.0274 387 GLU B C   
7332 O O   . GLU B 387 ? 0.2816 0.3026 0.2502 -0.0253 -0.0004 -0.0282 387 GLU B O   
7333 C CB  . GLU B 387 ? 0.2123 0.2319 0.1890 -0.0244 -0.0018 -0.0293 387 GLU B CB  
7334 C CG  . GLU B 387 ? 0.3959 0.4153 0.3724 -0.0236 -0.0018 -0.0300 387 GLU B CG  
7335 C CD  . GLU B 387 ? 0.4812 0.5012 0.4596 -0.0232 -0.0033 -0.0305 387 GLU B CD  
7336 O OE1 . GLU B 387 ? 0.5662 0.5864 0.5467 -0.0234 -0.0041 -0.0304 387 GLU B OE1 
7337 O OE2 . GLU B 387 ? 0.5668 0.5870 0.5446 -0.0228 -0.0036 -0.0310 387 GLU B OE2 
7338 N N   . GLU B 388 ? 0.2021 0.2240 0.1732 -0.0250 -0.0023 -0.0251 388 GLU B N   
7339 C CA  . GLU B 388 ? 0.1933 0.2169 0.1610 -0.0254 -0.0030 -0.0241 388 GLU B CA  
7340 C C   . GLU B 388 ? 0.2474 0.2701 0.2129 -0.0254 -0.0013 -0.0231 388 GLU B C   
7341 O O   . GLU B 388 ? 0.2261 0.2499 0.1882 -0.0260 -0.0012 -0.0236 388 GLU B O   
7342 C CB  . GLU B 388 ? 0.2100 0.2348 0.1787 -0.0250 -0.0045 -0.0217 388 GLU B CB  
7343 C CG  . GLU B 388 ? 0.1794 0.2058 0.1496 -0.0252 -0.0064 -0.0228 388 GLU B CG  
7344 C CD  . GLU B 388 ? 0.3083 0.3357 0.2801 -0.0247 -0.0079 -0.0204 388 GLU B CD  
7345 O OE1 . GLU B 388 ? 0.1949 0.2211 0.1683 -0.0241 -0.0073 -0.0182 388 GLU B OE1 
7346 O OE2 . GLU B 388 ? 0.4669 0.4963 0.4384 -0.0251 -0.0097 -0.0209 388 GLU B OE2 
7347 N N   . ALA B 389 ? 0.1830 0.2037 0.1504 -0.0248 0.0001  -0.0218 389 ALA B N   
7348 C CA  . ALA B 389 ? 0.2117 0.2313 0.1772 -0.0249 0.0018  -0.0209 389 ALA B CA  
7349 C C   . ALA B 389 ? 0.2568 0.2761 0.2205 -0.0254 0.0030  -0.0235 389 ALA B C   
7350 O O   . ALA B 389 ? 0.2536 0.2731 0.2142 -0.0258 0.0039  -0.0234 389 ALA B O   
7351 C CB  . ALA B 389 ? 0.1845 0.2018 0.1525 -0.0242 0.0031  -0.0192 389 ALA B CB  
7352 N N   . MET B 390 ? 0.2400 0.2587 0.2054 -0.0254 0.0031  -0.0257 390 MET B N   
7353 C CA  . MET B 390 ? 0.3036 0.3214 0.2694 -0.0249 0.0043  -0.0269 390 MET B CA  
7354 C C   . MET B 390 ? 0.3172 0.3364 0.2815 -0.0248 0.0035  -0.0272 390 MET B C   
7355 O O   . MET B 390 ? 0.2775 0.2962 0.2412 -0.0244 0.0044  -0.0272 390 MET B O   
7356 C CB  . MET B 390 ? 0.2300 0.2464 0.1998 -0.0240 0.0045  -0.0278 390 MET B CB  
7357 C CG  . MET B 390 ? 0.4556 0.4710 0.4268 -0.0230 0.0054  -0.0281 390 MET B CG  
7358 S SD  . MET B 390 ? 0.4960 0.5100 0.4717 -0.0219 0.0057  -0.0286 390 MET B SD  
7359 C CE  . MET B 390 ? 0.3959 0.4111 0.3720 -0.0217 0.0037  -0.0295 390 MET B CE  
7360 N N   . ARG B 391 ? 0.2676 0.2885 0.2311 -0.0251 0.0017  -0.0275 391 ARG B N   
7361 C CA  . ARG B 391 ? 0.3306 0.3527 0.2931 -0.0249 0.0009  -0.0280 391 ARG B CA  
7362 C C   . ARG B 391 ? 0.3320 0.3560 0.2908 -0.0258 0.0000  -0.0271 391 ARG B C   
7363 O O   . ARG B 391 ? 0.2938 0.3187 0.2513 -0.0257 -0.0006 -0.0274 391 ARG B O   
7364 C CB  . ARG B 391 ? 0.3830 0.4055 0.3475 -0.0246 -0.0005 -0.0289 391 ARG B CB  
7365 C CG  . ARG B 391 ? 0.5392 0.5598 0.5072 -0.0237 0.0002  -0.0296 391 ARG B CG  
7366 C CD  . ARG B 391 ? 0.6565 0.6774 0.6260 -0.0232 -0.0010 -0.0305 391 ARG B CD  
7367 N NE  . ARG B 391 ? 0.7892 0.8084 0.7620 -0.0223 -0.0005 -0.0310 391 ARG B NE  
7368 C CZ  . ARG B 391 ? 0.8491 0.8670 0.8232 -0.0214 0.0006  -0.0312 391 ARG B CZ  
7369 N NH1 . ARG B 391 ? 0.9131 0.9310 0.8855 -0.0214 0.0013  -0.0311 391 ARG B NH1 
7370 N NH2 . ARG B 391 ? 0.7531 0.7696 0.7300 -0.0206 0.0009  -0.0313 391 ARG B NH2 
7371 N N   . LYS B 392 ? 0.2234 0.2480 0.1803 -0.0265 -0.0001 -0.0258 392 LYS B N   
7372 C CA  . LYS B 392 ? 0.3747 0.4013 0.3282 -0.0272 -0.0010 -0.0245 392 LYS B CA  
7373 C C   . LYS B 392 ? 0.3673 0.3937 0.3189 -0.0271 -0.0001 -0.0244 392 LYS B C   
7374 O O   . LYS B 392 ? 0.2434 0.2682 0.1949 -0.0268 0.0016  -0.0242 392 LYS B O   
7375 C CB  . LYS B 392 ? 0.3772 0.4031 0.3309 -0.0271 -0.0007 -0.0219 392 LYS B CB  
7376 C CG  . LYS B 392 ? 0.4524 0.4799 0.4039 -0.0272 -0.0018 -0.0197 392 LYS B CG  
7377 C CD  . LYS B 392 ? 0.5039 0.5314 0.4581 -0.0265 -0.0029 -0.0174 392 LYS B CD  
7378 C CE  . LYS B 392 ? 0.4790 0.5083 0.4345 -0.0266 -0.0049 -0.0183 392 LYS B CE  
7379 N NZ  . LYS B 392 ? 0.5664 0.5982 0.5188 -0.0272 -0.0064 -0.0180 392 LYS B NZ  
7380 N N   . GLU B 393 ? 0.2832 0.3112 0.2332 -0.0272 -0.0012 -0.0245 393 GLU B N   
7381 C CA  . GLU B 393 ? 0.3467 0.3747 0.2951 -0.0270 -0.0005 -0.0246 393 GLU B CA  
7382 C C   . GLU B 393 ? 0.3091 0.3377 0.2543 -0.0276 -0.0001 -0.0228 393 GLU B C   
7383 O O   . GLU B 393 ? 0.3428 0.3702 0.2873 -0.0274 0.0013  -0.0226 393 GLU B O   
7384 C CB  . GLU B 393 ? 0.4271 0.4563 0.3751 -0.0270 -0.0018 -0.0255 393 GLU B CB  
7385 C CG  . GLU B 393 ? 0.5576 0.5860 0.5086 -0.0263 -0.0019 -0.0272 393 GLU B CG  
7386 C CD  . GLU B 393 ? 0.6906 0.7198 0.6410 -0.0262 -0.0028 -0.0281 393 GLU B CD  
7387 O OE1 . GLU B 393 ? 0.7099 0.7408 0.6577 -0.0267 -0.0036 -0.0275 393 GLU B OE1 
7388 O OE2 . GLU B 393 ? 0.7069 0.7351 0.6594 -0.0255 -0.0026 -0.0293 393 GLU B OE2 
7389 N N   . ASP B 394 ? 0.2670 0.2972 0.2103 -0.0283 -0.0014 -0.0213 394 ASP B N   
7390 C CA  . ASP B 394 ? 0.2525 0.2834 0.1925 -0.0287 -0.0012 -0.0194 394 ASP B CA  
7391 C C   . ASP B 394 ? 0.3530 0.3826 0.2926 -0.0288 0.0002  -0.0179 394 ASP B C   
7392 O O   . ASP B 394 ? 0.3238 0.3535 0.2630 -0.0287 -0.0002 -0.0153 394 ASP B O   
7393 C CB  . ASP B 394 ? 0.2963 0.3298 0.2345 -0.0293 -0.0033 -0.0181 394 ASP B CB  
7394 C CG  . ASP B 394 ? 0.4353 0.4693 0.3761 -0.0291 -0.0047 -0.0180 394 ASP B CG  
7395 O OD1 . ASP B 394 ? 0.5321 0.5646 0.4756 -0.0288 -0.0040 -0.0194 394 ASP B OD1 
7396 O OD2 . ASP B 394 ? 0.4423 0.4778 0.3833 -0.0290 -0.0063 -0.0164 394 ASP B OD2 
7397 N N   . VAL B 395 ? 0.2599 0.2872 0.2013 -0.0284 0.0020  -0.0188 395 VAL B N   
7398 C CA  . VAL B 395 ? 0.2677 0.2933 0.2088 -0.0284 0.0036  -0.0175 395 VAL B CA  
7399 C C   . VAL B 395 ? 0.2421 0.2663 0.1834 -0.0279 0.0053  -0.0179 395 VAL B C   
7400 O O   . VAL B 395 ? 0.3055 0.3298 0.2476 -0.0276 0.0052  -0.0193 395 VAL B O   
7401 C CB  . VAL B 395 ? 0.2669 0.2907 0.2122 -0.0276 0.0041  -0.0177 395 VAL B CB  
7402 C CG1 . VAL B 395 ? 0.3053 0.3299 0.2531 -0.0272 0.0023  -0.0165 395 VAL B CG1 
7403 C CG2 . VAL B 395 ? 0.2974 0.3205 0.2445 -0.0275 0.0047  -0.0204 395 VAL B CG2 
7404 N N   . LYS B 396 ? 0.2435 0.2662 0.1841 -0.0280 0.0068  -0.0165 396 LYS B N   
7405 C CA  . LYS B 396 ? 0.1793 0.2006 0.1204 -0.0275 0.0084  -0.0167 396 LYS B CA  
7406 C C   . LYS B 396 ? 0.2471 0.2664 0.1916 -0.0269 0.0096  -0.0179 396 LYS B C   
7407 O O   . LYS B 396 ? 0.1785 0.1970 0.1243 -0.0270 0.0099  -0.0178 396 LYS B O   
7408 C CB  . LYS B 396 ? 0.2761 0.2968 0.2150 -0.0278 0.0094  -0.0144 396 LYS B CB  
7409 C CG  . LYS B 396 ? 0.4280 0.4504 0.3637 -0.0282 0.0084  -0.0133 396 LYS B CG  
7410 C CD  . LYS B 396 ? 0.4875 0.5091 0.4223 -0.0279 0.0095  -0.0128 396 LYS B CD  
7411 C CE  . LYS B 396 ? 0.5254 0.5487 0.4571 -0.0283 0.0085  -0.0116 396 LYS B CE  
7412 N NZ  . LYS B 396 ? 0.5084 0.5331 0.4399 -0.0283 0.0075  -0.0133 396 LYS B NZ  
7413 N N   . THR B 397 ? 0.1614 0.1902 0.2291 0.0052  0.0093  0.0180  397 THR B N   
7414 C CA  . THR B 397 ? 0.2113 0.2415 0.2791 0.0051  0.0093  0.0171  397 THR B CA  
7415 C C   . THR B 397 ? 0.2819 0.3127 0.3503 0.0041  0.0093  0.0173  397 THR B C   
7416 O O   . THR B 397 ? 0.2297 0.2603 0.2984 0.0035  0.0094  0.0182  397 THR B O   
7417 C CB  . THR B 397 ? 0.2292 0.2611 0.2963 0.0057  0.0097  0.0171  397 THR B CB  
7418 O OG1 . THR B 397 ? 0.2275 0.2606 0.2945 0.0053  0.0100  0.0180  397 THR B OG1 
7419 C CG2 . THR B 397 ? 0.2039 0.2353 0.2704 0.0067  0.0098  0.0171  397 THR B CG2 
7420 N N   . GLU B 398 ? 0.1948 0.2264 0.2635 0.0039  0.0093  0.0164  398 GLU B N   
7421 C CA  . GLU B 398 ? 0.1625 0.1947 0.2318 0.0030  0.0092  0.0165  398 GLU B CA  
7422 C C   . GLU B 398 ? 0.2048 0.2385 0.2741 0.0030  0.0093  0.0156  398 GLU B C   
7423 O O   . GLU B 398 ? 0.1714 0.2051 0.2406 0.0036  0.0092  0.0147  398 GLU B O   
7424 C CB  . GLU B 398 ? 0.1733 0.2039 0.2434 0.0023  0.0088  0.0163  398 GLU B CB  
7425 C CG  . GLU B 398 ? 0.2563 0.2875 0.3271 0.0014  0.0087  0.0161  398 GLU B CG  
7426 C CD  . GLU B 398 ? 0.4058 0.4353 0.4773 0.0008  0.0083  0.0160  398 GLU B CD  
7427 O OE1 . GLU B 398 ? 0.4690 0.4968 0.5405 0.0010  0.0081  0.0162  398 GLU B OE1 
7428 O OE2 . GLU B 398 ? 0.4620 0.4918 0.5341 0.0001  0.0082  0.0156  398 GLU B OE2 
7429 N N   . VAL B 399 ? 0.1805 0.2156 0.2500 0.0024  0.0095  0.0159  399 VAL B N   
7430 C CA  . VAL B 399 ? 0.1693 0.2059 0.2389 0.0023  0.0095  0.0152  399 VAL B CA  
7431 C C   . VAL B 399 ? 0.2202 0.2563 0.2906 0.0016  0.0092  0.0146  399 VAL B C   
7432 O O   . VAL B 399 ? 0.2357 0.2711 0.3065 0.0008  0.0091  0.0151  399 VAL B O   
7433 C CB  . VAL B 399 ? 0.2222 0.2607 0.2917 0.0021  0.0099  0.0158  399 VAL B CB  
7434 C CG1 . VAL B 399 ? 0.2500 0.2900 0.3197 0.0019  0.0099  0.0151  399 VAL B CG1 
7435 C CG2 . VAL B 399 ? 0.1881 0.2272 0.2569 0.0029  0.0102  0.0163  399 VAL B CG2 
7436 N N   . ILE B 400 ? 0.2393 0.2758 0.3098 0.0017  0.0090  0.0135  400 ILE B N   
7437 C CA  . ILE B 400 ? 0.2040 0.2402 0.2751 0.0010  0.0087  0.0129  400 ILE B CA  
7438 C C   . ILE B 400 ? 0.1554 0.1934 0.2265 0.0009  0.0088  0.0123  400 ILE B C   
7439 O O   . ILE B 400 ? 0.1423 0.1813 0.2129 0.0016  0.0090  0.0120  400 ILE B O   
7440 C CB  . ILE B 400 ? 0.2581 0.2926 0.3294 0.0012  0.0084  0.0121  400 ILE B CB  
7441 C CG1 . ILE B 400 ? 0.3053 0.3400 0.3761 0.0022  0.0084  0.0114  400 ILE B CG1 
7442 C CG2 . ILE B 400 ? 0.3515 0.3841 0.4231 0.0010  0.0082  0.0127  400 ILE B CG2 
7443 C CD1 . ILE B 400 ? 0.4365 0.4695 0.5074 0.0025  0.0080  0.0106  400 ILE B CD1 
7444 N N   . GLU B 401 ? 0.1542 0.1927 0.2260 0.0000  0.0088  0.0122  401 GLU B N   
7445 C CA  . GLU B 401 ? 0.1641 0.2044 0.2359 -0.0002 0.0089  0.0118  401 GLU B CA  
7446 C C   . GLU B 401 ? 0.1595 0.1998 0.2317 -0.0004 0.0086  0.0107  401 GLU B C   
7447 O O   . GLU B 401 ? 0.1287 0.1704 0.2008 -0.0004 0.0086  0.0102  401 GLU B O   
7448 C CB  . GLU B 401 ? 0.2143 0.2554 0.2865 -0.0011 0.0090  0.0126  401 GLU B CB  
7449 C CG  . GLU B 401 ? 0.3356 0.3771 0.4075 -0.0009 0.0093  0.0137  401 GLU B CG  
7450 C CD  . GLU B 401 ? 0.4243 0.4672 0.4956 -0.0002 0.0097  0.0138  401 GLU B CD  
7451 O OE1 . GLU B 401 ? 0.4630 0.5058 0.5338 0.0002  0.0099  0.0146  401 GLU B OE1 
7452 O OE2 . GLU B 401 ? 0.4255 0.4697 0.4967 0.0000  0.0097  0.0132  401 GLU B OE2 
7453 N N   . SER B 402 ? 0.1260 0.1646 0.1985 -0.0005 0.0082  0.0102  402 SER B N   
7454 C CA  . SER B 402 ? 0.1402 0.1788 0.2131 -0.0008 0.0079  0.0091  402 SER B CA  
7455 C C   . SER B 402 ? 0.1698 0.2065 0.2429 -0.0006 0.0076  0.0085  402 SER B C   
7456 O O   . SER B 402 ? 0.1543 0.1895 0.2275 -0.0006 0.0075  0.0090  402 SER B O   
7457 C CB  . SER B 402 ? 0.1965 0.2354 0.2700 -0.0019 0.0079  0.0092  402 SER B CB  
7458 O OG  . SER B 402 ? 0.2228 0.2620 0.2967 -0.0022 0.0076  0.0081  402 SER B OG  
7459 N N   . VAL B 403 ? 0.1229 0.1596 0.1960 -0.0003 0.0074  0.0074  403 VAL B N   
7460 C CA  . VAL B 403 ? 0.1003 0.1353 0.1737 -0.0002 0.0071  0.0067  403 VAL B CA  
7461 C C   . VAL B 403 ? 0.1294 0.1644 0.2033 -0.0008 0.0068  0.0057  403 VAL B C   
7462 O O   . VAL B 403 ? 0.1262 0.1628 0.2001 -0.0011 0.0069  0.0053  403 VAL B O   
7463 C CB  . VAL B 403 ? 0.1201 0.1547 0.1929 0.0008  0.0071  0.0062  403 VAL B CB  
7464 C CG1 . VAL B 403 ? 0.1730 0.2075 0.2452 0.0014  0.0074  0.0072  403 VAL B CG1 
7465 C CG2 . VAL B 403 ? 0.1166 0.1529 0.1890 0.0011  0.0072  0.0054  403 VAL B CG2 
7466 N N   . LYS B 404 ? 0.1434 0.1768 0.2179 -0.0011 0.0065  0.0052  404 LYS B N   
7467 C CA  . LYS B 404 ? 0.1246 0.1578 0.1996 -0.0016 0.0062  0.0042  404 LYS B CA  
7468 C C   . LYS B 404 ? 0.1076 0.1406 0.1823 -0.0009 0.0061  0.0031  404 LYS B C   
7469 O O   . LYS B 404 ? 0.1304 0.1622 0.2051 -0.0003 0.0060  0.0030  404 LYS B O   
7470 C CB  . LYS B 404 ? 0.1074 0.1388 0.1832 -0.0022 0.0059  0.0042  404 LYS B CB  
7471 C CG  . LYS B 404 ? 0.2730 0.3043 0.3495 -0.0028 0.0056  0.0031  404 LYS B CG  
7472 C CD  . LYS B 404 ? 0.4802 0.5103 0.5575 -0.0037 0.0054  0.0035  404 LYS B CD  
7473 C CE  . LYS B 404 ? 0.5263 0.5576 0.6036 -0.0044 0.0056  0.0044  404 LYS B CE  
7474 N NZ  . LYS B 404 ? 0.5479 0.5783 0.6261 -0.0053 0.0054  0.0046  404 LYS B NZ  
7475 N N   . ALA B 405 ? 0.1343 0.1689 0.2090 -0.0009 0.0061  0.0023  405 ALA B N   
7476 C CA  . ALA B 405 ? 0.0721 0.1068 0.1463 -0.0002 0.0060  0.0013  405 ALA B CA  
7477 C C   . ALA B 405 ? 0.0722 0.1051 0.1469 -0.0002 0.0057  0.0005  405 ALA B C   
7478 O O   . ALA B 405 ? 0.1188 0.1508 0.1943 -0.0009 0.0055  0.0002  405 ALA B O   
7479 C CB  . ALA B 405 ? 0.0604 0.0969 0.1346 -0.0005 0.0060  0.0005  405 ALA B CB  
7480 N N   . GLY B 406 ? 0.0524 0.0847 0.1267 0.0007  0.0057  0.0000  406 GLY B N   
7481 C CA  . GLY B 406 ? 0.0617 0.0923 0.1364 0.0008  0.0054  -0.0008 406 GLY B CA  
7482 C C   . GLY B 406 ? 0.1399 0.1702 0.2141 0.0018  0.0054  -0.0012 406 GLY B C   
7483 O O   . GLY B 406 ? 0.0867 0.1183 0.1602 0.0024  0.0056  -0.0010 406 GLY B O   
7484 N N   . THR B 407 ? 0.0938 0.1224 0.1683 0.0020  0.0052  -0.0018 407 THR B N   
7485 C CA  . THR B 407 ? 0.1227 0.1507 0.1969 0.0030  0.0051  -0.0022 407 THR B CA  
7486 C C   . THR B 407 ? 0.1218 0.1476 0.1964 0.0031  0.0050  -0.0018 407 THR B C   
7487 O O   . THR B 407 ? 0.0961 0.1209 0.1712 0.0025  0.0049  -0.0014 407 THR B O   
7488 C CB  . THR B 407 ? 0.0400 0.0682 0.1143 0.0031  0.0049  -0.0037 407 THR B CB  
7489 O OG1 . THR B 407 ? 0.0816 0.1082 0.1568 0.0026  0.0046  -0.0044 407 THR B OG1 
7490 C CG2 . THR B 407 ? 0.0751 0.1053 0.1492 0.0027  0.0050  -0.0042 407 THR B CG2 
7491 N N   . TRP B 408 ? 0.0712 0.0962 0.1454 0.0040  0.0050  -0.0021 408 TRP B N   
7492 C CA  . TRP B 408 ? 0.0958 0.1187 0.1704 0.0041  0.0048  -0.0017 408 TRP B CA  
7493 C C   . TRP B 408 ? 0.0987 0.1203 0.1742 0.0038  0.0045  -0.0028 408 TRP B C   
7494 O O   . TRP B 408 ? 0.1611 0.1809 0.2371 0.0039  0.0043  -0.0026 408 TRP B O   
7495 C CB  . TRP B 408 ? 0.0415 0.0640 0.1155 0.0052  0.0049  -0.0015 408 TRP B CB  
7496 C CG  . TRP B 408 ? 0.1644 0.1873 0.2379 0.0059  0.0049  -0.0026 408 TRP B CG  
7497 C CD1 . TRP B 408 ? 0.1559 0.1795 0.2296 0.0057  0.0048  -0.0039 408 TRP B CD1 
7498 C CD2 . TRP B 408 ? 0.0401 0.0629 0.1130 0.0068  0.0050  -0.0025 408 TRP B CD2 
7499 N NE1 . TRP B 408 ? 0.1139 0.1379 0.1872 0.0065  0.0048  -0.0046 408 TRP B NE1 
7500 C CE2 . TRP B 408 ? 0.1253 0.1487 0.1980 0.0072  0.0049  -0.0038 408 TRP B CE2 
7501 C CE3 . TRP B 408 ? 0.0555 0.0776 0.1279 0.0074  0.0052  -0.0015 408 TRP B CE3 
7502 C CZ2 . TRP B 408 ? 0.1927 0.2160 0.2648 0.0081  0.0050  -0.0040 408 TRP B CZ2 
7503 C CZ3 . TRP B 408 ? 0.1198 0.1419 0.1917 0.0083  0.0052  -0.0018 408 TRP B CZ3 
7504 C CH2 . TRP B 408 ? 0.1352 0.1579 0.2069 0.0087  0.0051  -0.0030 408 TRP B CH2 
7505 N N   . PHE B 409 ? 0.0887 0.1111 0.1644 0.0034  0.0044  -0.0038 409 PHE B N   
7506 C CA  . PHE B 409 ? 0.1153 0.1366 0.1920 0.0029  0.0040  -0.0048 409 PHE B CA  
7507 C C   . PHE B 409 ? 0.1829 0.2042 0.2602 0.0019  0.0040  -0.0044 409 PHE B C   
7508 O O   . PHE B 409 ? 0.1689 0.1916 0.2462 0.0013  0.0040  -0.0047 409 PHE B O   
7509 C CB  . PHE B 409 ? 0.1654 0.1875 0.2421 0.0031  0.0039  -0.0063 409 PHE B CB  
7510 C CG  . PHE B 409 ? 0.3302 0.3514 0.4066 0.0040  0.0039  -0.0069 409 PHE B CG  
7511 C CD1 . PHE B 409 ? 0.2793 0.2986 0.3564 0.0041  0.0036  -0.0072 409 PHE B CD1 
7512 C CD2 . PHE B 409 ? 0.2206 0.2430 0.2961 0.0047  0.0041  -0.0070 409 PHE B CD2 
7513 C CE1 . PHE B 409 ? 0.3065 0.3250 0.3834 0.0049  0.0036  -0.0077 409 PHE B CE1 
7514 C CE2 . PHE B 409 ? 0.3209 0.3426 0.3962 0.0055  0.0040  -0.0075 409 PHE B CE2 
7515 C CZ  . PHE B 409 ? 0.3655 0.3851 0.4414 0.0056  0.0038  -0.0079 409 PHE B CZ  
7516 N N   . ASP B 410 ? 0.1997 0.2194 0.2775 0.0016  0.0038  -0.0036 410 ASP B N   
7517 C CA  . ASP B 410 ? 0.2177 0.2372 0.2963 0.0006  0.0037  -0.0031 410 ASP B CA  
7518 C C   . ASP B 410 ? 0.1825 0.2037 0.2606 0.0002  0.0040  -0.0022 410 ASP B C   
7519 O O   . ASP B 410 ? 0.1554 0.1768 0.2340 -0.0007 0.0040  -0.0020 410 ASP B O   
7520 C CB  . ASP B 410 ? 0.2271 0.2462 0.3065 0.0000  0.0035  -0.0043 410 ASP B CB  
7521 C CG  . ASP B 410 ? 0.4185 0.4359 0.4984 0.0003  0.0032  -0.0052 410 ASP B CG  
7522 O OD1 . ASP B 410 ? 0.3683 0.3841 0.4486 0.0006  0.0031  -0.0047 410 ASP B OD1 
7523 O OD2 . ASP B 410 ? 0.4817 0.4996 0.5617 0.0004  0.0031  -0.0065 410 ASP B OD2 
7524 N N   . GLY B 411 ? 0.1040 0.1264 0.1812 0.0008  0.0043  -0.0017 411 GLY B N   
7525 C CA  . GLY B 411 ? 0.0995 0.1235 0.1763 0.0004  0.0046  -0.0009 411 GLY B CA  
7526 C C   . GLY B 411 ? 0.1230 0.1486 0.1997 -0.0001 0.0046  -0.0017 411 GLY B C   
7527 O O   . GLY B 411 ? 0.1166 0.1435 0.1933 -0.0006 0.0048  -0.0010 411 GLY B O   
7528 N N   . ASN B 412 ? 0.1004 0.1262 0.1773 0.0001  0.0044  -0.0030 412 ASN B N   
7529 C CA  . ASN B 412 ? 0.1117 0.1391 0.1887 -0.0005 0.0044  -0.0037 412 ASN B CA  
7530 C C   . ASN B 412 ? 0.0671 0.0953 0.1437 0.0001  0.0044  -0.0049 412 ASN B C   
7531 O O   . ASN B 412 ? 0.1217 0.1493 0.1979 0.0009  0.0044  -0.0050 412 ASN B O   
7532 C CB  . ASN B 412 ? 0.1918 0.2184 0.2698 -0.0014 0.0041  -0.0041 412 ASN B CB  
7533 C CG  . ASN B 412 ? 0.1883 0.2132 0.2669 -0.0013 0.0038  -0.0052 412 ASN B CG  
7534 O OD1 . ASN B 412 ? 0.1689 0.1940 0.2472 -0.0008 0.0038  -0.0062 412 ASN B OD1 
7535 N ND2 . ASN B 412 ? 0.1717 0.1951 0.2511 -0.0019 0.0036  -0.0050 412 ASN B ND2 
7536 N N   . PHE B 413 ? 0.0627 0.0922 0.1394 -0.0004 0.0043  -0.0057 413 PHE B N   
7537 C CA  . PHE B 413 ? 0.0875 0.1182 0.1638 0.0001  0.0044  -0.0067 413 PHE B CA  
7538 C C   . PHE B 413 ? 0.1395 0.1696 0.2163 -0.0001 0.0041  -0.0081 413 PHE B C   
7539 O O   . PHE B 413 ? 0.0893 0.1205 0.1657 0.0001  0.0040  -0.0091 413 PHE B O   
7540 C CB  . PHE B 413 ? 0.0929 0.1258 0.1686 -0.0001 0.0045  -0.0065 413 PHE B CB  
7541 C CG  . PHE B 413 ? 0.1301 0.1639 0.2052 0.0003  0.0049  -0.0052 413 PHE B CG  
7542 C CD1 . PHE B 413 ? 0.1084 0.1428 0.1828 0.0012  0.0050  -0.0051 413 PHE B CD1 
7543 C CD2 . PHE B 413 ? 0.1149 0.1487 0.1902 -0.0003 0.0050  -0.0041 413 PHE B CD2 
7544 C CE1 . PHE B 413 ? 0.1015 0.1366 0.1753 0.0015  0.0053  -0.0040 413 PHE B CE1 
7545 C CE2 . PHE B 413 ? 0.0590 0.0937 0.1338 0.0000  0.0053  -0.0030 413 PHE B CE2 
7546 C CZ  . PHE B 413 ? 0.0855 0.1208 0.1595 0.0009  0.0054  -0.0029 413 PHE B CZ  
7547 N N   . LEU B 414 ? 0.0724 0.1009 0.1501 -0.0006 0.0038  -0.0084 414 LEU B N   
7548 C CA  . LEU B 414 ? 0.0676 0.0956 0.1458 -0.0009 0.0035  -0.0098 414 LEU B CA  
7549 C C   . LEU B 414 ? 0.1446 0.1722 0.2226 -0.0001 0.0035  -0.0108 414 LEU B C   
7550 O O   . LEU B 414 ? 0.1003 0.1281 0.1787 -0.0004 0.0033  -0.0121 414 LEU B O   
7551 C CB  . LEU B 414 ? 0.1295 0.1557 0.2087 -0.0015 0.0033  -0.0097 414 LEU B CB  
7552 C CG  . LEU B 414 ? 0.1156 0.1422 0.1952 -0.0024 0.0033  -0.0089 414 LEU B CG  
7553 C CD1 . LEU B 414 ? 0.1459 0.1706 0.2265 -0.0030 0.0031  -0.0089 414 LEU B CD1 
7554 C CD2 . LEU B 414 ? 0.1482 0.1767 0.2277 -0.0030 0.0034  -0.0095 414 LEU B CD2 
7555 N N   . LYS B 415 ? 0.0780 0.1051 0.1554 0.0008  0.0036  -0.0103 415 LYS B N   
7556 C CA  . LYS B 415 ? 0.1222 0.1492 0.1994 0.0015  0.0035  -0.0113 415 LYS B CA  
7557 C C   . LYS B 415 ? 0.1738 0.2029 0.2504 0.0017  0.0036  -0.0120 415 LYS B C   
7558 O O   . LYS B 415 ? 0.0863 0.1153 0.1627 0.0022  0.0036  -0.0130 415 LYS B O   
7559 C CB  . LYS B 415 ? 0.1234 0.1493 0.2002 0.0024  0.0036  -0.0106 415 LYS B CB  
7560 C CG  . LYS B 415 ? 0.1818 0.2055 0.2593 0.0023  0.0035  -0.0103 415 LYS B CG  
7561 C CD  . LYS B 415 ? 0.3386 0.3611 0.4167 0.0024  0.0032  -0.0116 415 LYS B CD  
7562 C CE  . LYS B 415 ? 0.4484 0.4686 0.5272 0.0025  0.0030  -0.0113 415 LYS B CE  
7563 N NZ  . LYS B 415 ? 0.4283 0.4474 0.5080 0.0024  0.0027  -0.0127 415 LYS B NZ  
7564 N N   . TRP B 416 ? 0.0518 0.0826 0.1280 0.0014  0.0038  -0.0114 416 TRP B N   
7565 C CA  . TRP B 416 ? 0.0789 0.1117 0.1544 0.0016  0.0039  -0.0119 416 TRP B CA  
7566 C C   . TRP B 416 ? 0.0691 0.1035 0.1449 0.0007  0.0039  -0.0123 416 TRP B C   
7567 O O   . TRP B 416 ? 0.0527 0.0888 0.1280 0.0008  0.0039  -0.0128 416 TRP B O   
7568 C CB  . TRP B 416 ? 0.1000 0.1338 0.1747 0.0022  0.0042  -0.0108 416 TRP B CB  
7569 C CG  . TRP B 416 ? 0.0658 0.0982 0.1401 0.0031  0.0043  -0.0103 416 TRP B CG  
7570 C CD1 . TRP B 416 ? 0.0396 0.0720 0.1135 0.0039  0.0043  -0.0109 416 TRP B CD1 
7571 C CD2 . TRP B 416 ? 0.0840 0.1149 0.1585 0.0031  0.0043  -0.0093 416 TRP B CD2 
7572 N NE1 . TRP B 416 ? 0.0389 0.0698 0.1126 0.0045  0.0043  -0.0102 416 TRP B NE1 
7573 C CE2 . TRP B 416 ? 0.0712 0.1012 0.1454 0.0041  0.0044  -0.0092 416 TRP B CE2 
7574 C CE3 . TRP B 416 ? 0.0872 0.1174 0.1622 0.0025  0.0043  -0.0084 416 TRP B CE3 
7575 C CZ2 . TRP B 416 ? 0.0584 0.0867 0.1326 0.0044  0.0044  -0.0083 416 TRP B CZ2 
7576 C CZ3 . TRP B 416 ? 0.0709 0.0996 0.1460 0.0028  0.0044  -0.0074 416 TRP B CZ3 
7577 C CH2 . TRP B 416 ? 0.0664 0.0942 0.1410 0.0037  0.0044  -0.0074 416 TRP B CH2 
7578 N N   . ILE B 417 ? 0.0686 0.1024 0.1450 -0.0001 0.0038  -0.0120 417 ILE B N   
7579 C CA  . ILE B 417 ? 0.0794 0.1146 0.1560 -0.0010 0.0038  -0.0123 417 ILE B CA  
7580 C C   . ILE B 417 ? 0.1797 0.2136 0.2573 -0.0018 0.0035  -0.0124 417 ILE B C   
7581 O O   . ILE B 417 ? 0.1050 0.1371 0.1829 -0.0017 0.0035  -0.0119 417 ILE B O   
7582 C CB  . ILE B 417 ? 0.1137 0.1505 0.1899 -0.0011 0.0040  -0.0111 417 ILE B CB  
7583 C CG1 . ILE B 417 ? 0.0543 0.0930 0.1305 -0.0018 0.0040  -0.0115 417 ILE B CG1 
7584 C CG2 . ILE B 417 ? 0.1432 0.1789 0.2196 -0.0014 0.0041  -0.0098 417 ILE B CG2 
7585 C CD1 . ILE B 417 ? 0.0618 0.1024 0.1374 -0.0017 0.0042  -0.0107 417 ILE B CD1 
7586 N N   . GLY B 418 ? 0.1626 0.1974 0.2406 -0.0026 0.0034  -0.0132 418 GLY B N   
7587 C CA  . GLY B 418 ? 0.1332 0.1670 0.2120 -0.0035 0.0032  -0.0132 418 GLY B CA  
7588 C C   . GLY B 418 ? 0.2310 0.2641 0.3105 -0.0039 0.0030  -0.0146 418 GLY B C   
7589 O O   . GLY B 418 ? 0.3727 0.4055 0.4530 -0.0047 0.0028  -0.0147 418 GLY B O   
7590 N N   . ASN B 419 ? 0.1936 0.2266 0.2730 -0.0033 0.0029  -0.0157 419 ASN B N   
7591 C CA  . ASN B 419 ? 0.2435 0.2760 0.3236 -0.0037 0.0026  -0.0171 419 ASN B CA  
7592 C C   . ASN B 419 ? 0.2836 0.3181 0.3632 -0.0037 0.0026  -0.0181 419 ASN B C   
7593 O O   . ASN B 419 ? 0.2093 0.2453 0.2881 -0.0033 0.0028  -0.0177 419 ASN B O   
7594 C CB  . ASN B 419 ? 0.3107 0.3412 0.3912 -0.0032 0.0024  -0.0177 419 ASN B CB  
7595 C CG  . ASN B 419 ? 0.2778 0.3084 0.3576 -0.0022 0.0025  -0.0180 419 ASN B CG  
7596 O OD1 . ASN B 419 ? 0.2585 0.2909 0.3376 -0.0019 0.0027  -0.0183 419 ASN B OD1 
7597 N ND2 . ASN B 419 ? 0.3357 0.3645 0.4157 -0.0016 0.0025  -0.0181 419 ASN B ND2 
7598 N N   . LYS B 420 ? 0.2079 0.2424 0.2880 -0.0042 0.0024  -0.0195 420 LYS B N   
7599 C CA  . LYS B 420 ? 0.2208 0.2574 0.3006 -0.0044 0.0024  -0.0204 420 LYS B CA  
7600 C C   . LYS B 420 ? 0.2299 0.2671 0.3089 -0.0034 0.0025  -0.0207 420 LYS B C   
7601 O O   . LYS B 420 ? 0.2217 0.2609 0.3000 -0.0033 0.0027  -0.0205 420 LYS B O   
7602 C CB  . LYS B 420 ? 0.2930 0.3293 0.3735 -0.0050 0.0021  -0.0219 420 LYS B CB  
7603 C CG  . LYS B 420 ? 0.4687 0.5049 0.5499 -0.0061 0.0020  -0.0217 420 LYS B CG  
7604 C CD  . LYS B 420 ? 0.5401 0.5769 0.6218 -0.0067 0.0018  -0.0232 420 LYS B CD  
7605 C CE  . LYS B 420 ? 0.6197 0.6564 0.7021 -0.0078 0.0017  -0.0230 420 LYS B CE  
7606 N NZ  . LYS B 420 ? 0.6434 0.6813 0.7261 -0.0085 0.0016  -0.0243 420 LYS B NZ  
7607 N N   . GLU B 421 ? 0.1569 0.1926 0.2359 -0.0027 0.0025  -0.0210 421 GLU B N   
7608 C CA  . GLU B 421 ? 0.1424 0.1788 0.2208 -0.0019 0.0026  -0.0214 421 GLU B CA  
7609 C C   . GLU B 421 ? 0.1295 0.1667 0.2070 -0.0013 0.0028  -0.0201 421 GLU B C   
7610 O O   . GLU B 421 ? 0.1549 0.1937 0.2317 -0.0009 0.0029  -0.0202 421 GLU B O   
7611 C CB  . GLU B 421 ? 0.3724 0.4067 0.4511 -0.0013 0.0024  -0.0221 421 GLU B CB  
7612 C CG  . GLU B 421 ? 0.6093 0.6443 0.6878 -0.0009 0.0024  -0.0235 421 GLU B CG  
7613 C CD  . GLU B 421 ? 0.8077 0.8436 0.8867 -0.0017 0.0022  -0.0248 421 GLU B CD  
7614 O OE1 . GLU B 421 ? 0.8863 0.9211 0.9662 -0.0023 0.0020  -0.0252 421 GLU B OE1 
7615 O OE2 . GLU B 421 ? 0.8967 0.9346 0.9752 -0.0018 0.0022  -0.0253 421 GLU B OE2 
7616 N N   . LYS B 422 ? 0.1364 0.1724 0.2140 -0.0011 0.0029  -0.0189 422 LYS B N   
7617 C CA  . LYS B 422 ? 0.0698 0.1066 0.1466 -0.0006 0.0032  -0.0176 422 LYS B CA  
7618 C C   . LYS B 422 ? 0.0861 0.1250 0.1626 -0.0011 0.0033  -0.0171 422 LYS B C   
7619 O O   . LYS B 422 ? 0.1502 0.1905 0.2258 -0.0007 0.0035  -0.0167 422 LYS B O   
7620 C CB  . LYS B 422 ? 0.1010 0.1361 0.1780 -0.0004 0.0033  -0.0164 422 LYS B CB  
7621 C CG  . LYS B 422 ? 0.0708 0.1040 0.1478 0.0003  0.0032  -0.0167 422 LYS B CG  
7622 C CD  . LYS B 422 ? 0.0441 0.0755 0.1214 0.0004  0.0032  -0.0156 422 LYS B CD  
7623 C CE  . LYS B 422 ? 0.1693 0.1989 0.2468 0.0011  0.0031  -0.0159 422 LYS B CE  
7624 N NZ  . LYS B 422 ? 0.3673 0.3949 0.4456 0.0008  0.0030  -0.0154 422 LYS B NZ  
7625 N N   . ASN B 423 ? 0.0974 0.1365 0.1744 -0.0021 0.0032  -0.0172 423 ASN B N   
7626 C CA  . ASN B 423 ? 0.1181 0.1593 0.1949 -0.0026 0.0033  -0.0167 423 ASN B CA  
7627 C C   . ASN B 423 ? 0.1220 0.1650 0.1983 -0.0025 0.0033  -0.0177 423 ASN B C   
7628 O O   . ASN B 423 ? 0.0940 0.1389 0.1699 -0.0026 0.0034  -0.0172 423 ASN B O   
7629 C CB  . ASN B 423 ? 0.1178 0.1588 0.1953 -0.0036 0.0032  -0.0167 423 ASN B CB  
7630 C CG  . ASN B 423 ? 0.1145 0.1542 0.1923 -0.0038 0.0033  -0.0154 423 ASN B CG  
7631 O OD1 . ASN B 423 ? 0.1190 0.1579 0.1964 -0.0031 0.0034  -0.0146 423 ASN B OD1 
7632 N ND2 . ASN B 423 ? 0.1684 0.2080 0.2468 -0.0047 0.0032  -0.0153 423 ASN B ND2 
7633 N N   . GLU B 424 ? 0.0997 0.1423 0.1762 -0.0024 0.0031  -0.0190 424 GLU B N   
7634 C CA  . GLU B 424 ? 0.1727 0.2172 0.2488 -0.0023 0.0031  -0.0199 424 GLU B CA  
7635 C C   . GLU B 424 ? 0.1515 0.1968 0.2267 -0.0014 0.0032  -0.0194 424 GLU B C   
7636 O O   . GLU B 424 ? 0.1020 0.1493 0.1768 -0.0014 0.0033  -0.0194 424 GLU B O   
7637 C CB  . GLU B 424 ? 0.1744 0.2182 0.2509 -0.0023 0.0028  -0.0215 424 GLU B CB  
7638 C CG  . GLU B 424 ? 0.3031 0.3486 0.3791 -0.0021 0.0028  -0.0225 424 GLU B CG  
7639 C CD  . GLU B 424 ? 0.4549 0.5025 0.5309 -0.0029 0.0028  -0.0227 424 GLU B CD  
7640 O OE1 . GLU B 424 ? 0.5043 0.5519 0.5808 -0.0037 0.0027  -0.0224 424 GLU B OE1 
7641 O OE2 . GLU B 424 ? 0.4019 0.4512 0.4773 -0.0027 0.0028  -0.0231 424 GLU B OE2 
7642 N N   . TYR B 425 ? 0.1345 0.1784 0.2096 -0.0006 0.0033  -0.0189 425 TYR B N   
7643 C CA  . TYR B 425 ? 0.0818 0.1265 0.1560 0.0002  0.0035  -0.0183 425 TYR B CA  
7644 C C   . TYR B 425 ? 0.1098 0.1558 0.1837 0.0001  0.0037  -0.0170 425 TYR B C   
7645 O O   . TYR B 425 ? 0.0520 0.0996 0.1252 0.0004  0.0038  -0.0168 425 TYR B O   
7646 C CB  . TYR B 425 ? 0.1217 0.1644 0.1958 0.0011  0.0036  -0.0179 425 TYR B CB  
7647 C CG  . TYR B 425 ? 0.0640 0.1062 0.1380 0.0017  0.0035  -0.0190 425 TYR B CG  
7648 C CD1 . TYR B 425 ? 0.1582 0.2007 0.2325 0.0013  0.0033  -0.0204 425 TYR B CD1 
7649 C CD2 . TYR B 425 ? 0.0812 0.1225 0.1547 0.0026  0.0036  -0.0186 425 TYR B CD2 
7650 C CE1 . TYR B 425 ? 0.0937 0.1358 0.1679 0.0019  0.0032  -0.0215 425 TYR B CE1 
7651 C CE2 . TYR B 425 ? 0.1442 0.1850 0.2176 0.0032  0.0035  -0.0196 425 TYR B CE2 
7652 C CZ  . TYR B 425 ? 0.1798 0.2209 0.2535 0.0028  0.0033  -0.0210 425 TYR B CZ  
7653 O OH  . TYR B 425 ? 0.1440 0.1847 0.2177 0.0034  0.0032  -0.0220 425 TYR B OH  
7654 N N   . TRP B 426 ? 0.0623 0.1075 0.1366 -0.0003 0.0038  -0.0161 426 TRP B N   
7655 C CA  . TRP B 426 ? 0.0532 0.0997 0.1272 -0.0005 0.0040  -0.0149 426 TRP B CA  
7656 C C   . TRP B 426 ? 0.0370 0.0856 0.1109 -0.0011 0.0039  -0.0153 426 TRP B C   
7657 O O   . TRP B 426 ? 0.0803 0.1305 0.1537 -0.0009 0.0040  -0.0147 426 TRP B O   
7658 C CB  . TRP B 426 ? 0.0733 0.1186 0.1477 -0.0009 0.0040  -0.0139 426 TRP B CB  
7659 C CG  . TRP B 426 ? 0.0668 0.1104 0.1411 -0.0003 0.0041  -0.0131 426 TRP B CG  
7660 C CD1 . TRP B 426 ? 0.0807 0.1222 0.1554 -0.0002 0.0040  -0.0133 426 TRP B CD1 
7661 C CD2 . TRP B 426 ? 0.0759 0.1197 0.1495 0.0004  0.0044  -0.0120 426 TRP B CD2 
7662 N NE1 . TRP B 426 ? 0.0997 0.1401 0.1741 0.0004  0.0042  -0.0124 426 TRP B NE1 
7663 C CE2 . TRP B 426 ? 0.1011 0.1430 0.1748 0.0008  0.0044  -0.0116 426 TRP B CE2 
7664 C CE3 . TRP B 426 ? 0.0741 0.1197 0.1472 0.0007  0.0046  -0.0114 426 TRP B CE3 
7665 C CZ2 . TRP B 426 ? 0.1482 0.1898 0.2214 0.0016  0.0046  -0.0106 426 TRP B CZ2 
7666 C CZ3 . TRP B 426 ? 0.0753 0.1206 0.1479 0.0014  0.0048  -0.0104 426 TRP B CZ3 
7667 C CH2 . TRP B 426 ? 0.0899 0.1332 0.1625 0.0018  0.0048  -0.0100 426 TRP B CH2 
7668 N N   . LYS B 427 ? 0.0528 0.1015 0.1273 -0.0018 0.0037  -0.0163 427 LYS B N   
7669 C CA  . LYS B 427 ? 0.0987 0.1494 0.1731 -0.0024 0.0036  -0.0168 427 LYS B CA  
7670 C C   . LYS B 427 ? 0.0976 0.1498 0.1714 -0.0019 0.0036  -0.0173 427 LYS B C   
7671 O O   . LYS B 427 ? 0.0708 0.1251 0.1444 -0.0020 0.0037  -0.0170 427 LYS B O   
7672 C CB  . LYS B 427 ? 0.2514 0.3017 0.3265 -0.0032 0.0034  -0.0180 427 LYS B CB  
7673 C CG  . LYS B 427 ? 0.4863 0.5386 0.5614 -0.0039 0.0033  -0.0183 427 LYS B CG  
7674 C CD  . LYS B 427 ? 0.6245 0.6764 0.7004 -0.0049 0.0032  -0.0183 427 LYS B CD  
7675 C CE  . LYS B 427 ? 0.6629 0.7149 0.7387 -0.0051 0.0034  -0.0168 427 LYS B CE  
7676 N NZ  . LYS B 427 ? 0.5306 0.5825 0.6071 -0.0060 0.0033  -0.0165 427 LYS B NZ  
7677 N N   . ILE B 428 ? 0.0699 0.1213 0.1435 -0.0012 0.0036  -0.0180 428 ILE B N   
7678 C CA  . ILE B 428 ? 0.1324 0.1851 0.2053 -0.0007 0.0036  -0.0185 428 ILE B CA  
7679 C C   . ILE B 428 ? 0.0859 0.1395 0.1583 0.0000  0.0038  -0.0173 428 ILE B C   
7680 O O   . ILE B 428 ? 0.1103 0.1658 0.1823 0.0000  0.0038  -0.0172 428 ILE B O   
7681 C CB  . ILE B 428 ? 0.0796 0.1311 0.1525 -0.0001 0.0035  -0.0195 428 ILE B CB  
7682 C CG1 . ILE B 428 ? 0.1757 0.2270 0.2492 -0.0007 0.0032  -0.0209 428 ILE B CG1 
7683 C CG2 . ILE B 428 ? 0.1215 0.1740 0.1937 0.0007  0.0035  -0.0196 428 ILE B CG2 
7684 C CD1 . ILE B 428 ? 0.2035 0.2533 0.2770 -0.0001 0.0032  -0.0218 428 ILE B CD1 
7685 N N   . LEU B 429 ? 0.0727 0.1248 0.1450 0.0004  0.0039  -0.0163 429 LEU B N   
7686 C CA  . LEU B 429 ? 0.1120 0.1647 0.1837 0.0010  0.0042  -0.0151 429 LEU B CA  
7687 C C   . LEU B 429 ? 0.1003 0.1548 0.1721 0.0005  0.0042  -0.0144 429 LEU B C   
7688 O O   . LEU B 429 ? 0.1055 0.1615 0.1769 0.0008  0.0043  -0.0139 429 LEU B O   
7689 C CB  . LEU B 429 ? 0.0792 0.1299 0.1510 0.0014  0.0043  -0.0143 429 LEU B CB  
7690 C CG  . LEU B 429 ? 0.0891 0.1403 0.1604 0.0021  0.0045  -0.0131 429 LEU B CG  
7691 C CD1 . LEU B 429 ? 0.1561 0.2077 0.2267 0.0030  0.0046  -0.0135 429 LEU B CD1 
7692 C CD2 . LEU B 429 ? 0.1170 0.1664 0.1884 0.0023  0.0047  -0.0121 429 LEU B CD2 
7693 N N   . ILE B 430 ? 0.0865 0.1407 0.1589 -0.0004 0.0042  -0.0142 430 ILE B N   
7694 C CA  . ILE B 430 ? 0.0886 0.1444 0.1611 -0.0009 0.0043  -0.0135 430 ILE B CA  
7695 C C   . ILE B 430 ? 0.0924 0.1504 0.1647 -0.0011 0.0042  -0.0141 430 ILE B C   
7696 O O   . ILE B 430 ? 0.0769 0.1359 0.1481 -0.0010 0.0042  -0.0132 430 ILE B O   
7697 C CB  . ILE B 430 ? 0.1445 0.1996 0.2177 -0.0018 0.0042  -0.0133 430 ILE B CB  
7698 C CG1 . ILE B 430 ? 0.1036 0.1569 0.1769 -0.0016 0.0044  -0.0123 430 ILE B CG1 
7699 C CG2 . ILE B 430 ? 0.1555 0.2125 0.2288 -0.0025 0.0043  -0.0129 430 ILE B CG2 
7700 C CD1 . ILE B 430 ? 0.0894 0.1412 0.1634 -0.0023 0.0043  -0.0125 430 ILE B CD1 
7701 N N   . GLU B 431 ? 0.1290 0.1871 0.2014 -0.0014 0.0040  -0.0153 431 GLU B N   
7702 C CA  . GLU B 431 ? 0.1282 0.1882 0.2002 -0.0017 0.0038  -0.0159 431 GLU B CA  
7703 C C   . GLU B 431 ? 0.2144 0.2743 0.2844 -0.0008 0.0038  -0.0154 431 GLU B C   
7704 O O   . GLU B 431 ? 0.1475 0.2083 0.2161 -0.0009 0.0037  -0.0147 431 GLU B O   
7705 C CB  . GLU B 431 ? 0.1991 0.2591 0.2717 -0.0023 0.0036  -0.0173 431 GLU B CB  
7706 C CG  . GLU B 431 ? 0.3293 0.3910 0.4012 -0.0026 0.0034  -0.0179 431 GLU B CG  
7707 C CD  . GLU B 431 ? 0.5243 0.5871 0.5954 -0.0032 0.0034  -0.0168 431 GLU B CD  
7708 O OE1 . GLU B 431 ? 0.5315 0.5949 0.6009 -0.0030 0.0033  -0.0163 431 GLU B OE1 
7709 O OE2 . GLU B 431 ? 0.4531 0.5159 0.5252 -0.0038 0.0035  -0.0165 431 GLU B OE2 
7710 N N   . ALA B 432 ? 0.1573 0.2162 0.2274 0.0000  0.0039  -0.0157 432 ALA B N   
7711 C CA  . ALA B 432 ? 0.1094 0.1682 0.1776 0.0008  0.0039  -0.0152 432 ALA B CA  
7712 C C   . ALA B 432 ? 0.2003 0.2589 0.2672 0.0012  0.0040  -0.0136 432 ALA B C   
7713 O O   . ALA B 432 ? 0.1050 0.1639 0.1702 0.0015  0.0040  -0.0129 432 ALA B O   
7714 C CB  . ALA B 432 ? 0.1353 0.1929 0.2039 0.0015  0.0039  -0.0159 432 ALA B CB  
7715 N N   . LYS B 433 ? 0.0884 0.1466 0.1563 0.0010  0.0042  -0.0128 433 LYS B N   
7716 C CA  . LYS B 433 ? 0.1354 0.1935 0.2021 0.0014  0.0044  -0.0113 433 LYS B CA  
7717 C C   . LYS B 433 ? 0.1524 0.2117 0.2180 0.0009  0.0043  -0.0106 433 LYS B C   
7718 O O   . LYS B 433 ? 0.1430 0.2023 0.2071 0.0013  0.0043  -0.0095 433 LYS B O   
7719 C CB  . LYS B 433 ? 0.1312 0.1886 0.1991 0.0013  0.0046  -0.0107 433 LYS B CB  
7720 C CG  . LYS B 433 ? 0.1046 0.1621 0.1715 0.0014  0.0048  -0.0092 433 LYS B CG  
7721 C CD  . LYS B 433 ? 0.1327 0.1895 0.1980 0.0024  0.0048  -0.0085 433 LYS B CD  
7722 C CE  . LYS B 433 ? 0.0927 0.1496 0.1571 0.0026  0.0050  -0.0070 433 LYS B CE  
7723 N NZ  . LYS B 433 ? 0.1483 0.2046 0.2108 0.0035  0.0050  -0.0062 433 LYS B NZ  
7724 N N   . LYS B 434 ? 0.1751 0.2353 0.2415 0.0000  0.0041  -0.0113 434 LYS B N   
7725 C CA  . LYS B 434 ? 0.2629 0.3243 0.3284 -0.0004 0.0040  -0.0107 434 LYS B CA  
7726 C C   . LYS B 434 ? 0.2308 0.2923 0.2946 0.0000  0.0039  -0.0105 434 LYS B C   
7727 O O   . LYS B 434 ? 0.3651 0.4272 0.4279 0.0000  0.0038  -0.0096 434 LYS B O   
7728 C CB  . LYS B 434 ? 0.1574 0.2197 0.2241 -0.0014 0.0039  -0.0116 434 LYS B CB  
7729 C CG  . LYS B 434 ? 0.1961 0.2581 0.2644 -0.0020 0.0040  -0.0116 434 LYS B CG  
7730 C CD  . LYS B 434 ? 0.3212 0.3842 0.3904 -0.0030 0.0038  -0.0125 434 LYS B CD  
7731 C CE  . LYS B 434 ? 0.3359 0.3985 0.4069 -0.0037 0.0039  -0.0128 434 LYS B CE  
7732 N NZ  . LYS B 434 ? 0.4121 0.4755 0.4840 -0.0046 0.0037  -0.0138 434 LYS B NZ  
7733 N N   . LYS B 435 ? 0.1937 0.2549 0.2574 0.0005  0.0038  -0.0114 435 LYS B N   
7734 C CA  . LYS B 435 ? 0.2174 0.2788 0.2796 0.0008  0.0036  -0.0114 435 LYS B CA  
7735 C C   . LYS B 435 ? 0.3161 0.3764 0.3773 0.0018  0.0037  -0.0111 435 LYS B C   
7736 O O   . LYS B 435 ? 0.2031 0.2633 0.2631 0.0021  0.0036  -0.0112 435 LYS B O   
7737 C CB  . LYS B 435 ? 0.3261 0.3880 0.3886 0.0004  0.0034  -0.0129 435 LYS B CB  
7738 C CG  . LYS B 435 ? 0.4237 0.4864 0.4877 -0.0005 0.0034  -0.0137 435 LYS B CG  
7739 C CD  . LYS B 435 ? 0.5232 0.5867 0.5871 -0.0010 0.0031  -0.0149 435 LYS B CD  
7740 C CE  . LYS B 435 ? 0.5992 0.6634 0.6646 -0.0019 0.0031  -0.0158 435 LYS B CE  
7741 N NZ  . LYS B 435 ? 0.6401 0.7055 0.7050 -0.0026 0.0028  -0.0161 435 LYS B NZ  
7742 N N   . ALA B 436 ? 0.1862 0.2069 0.2277 0.0010  0.0016  0.0299  436 ALA B N   
7743 C CA  . ALA B 436 ? 0.2115 0.2315 0.2539 0.0010  0.0017  0.0297  436 ALA B CA  
7744 C C   . ALA B 436 ? 0.2564 0.2761 0.2980 0.0013  0.0022  0.0297  436 ALA B C   
7745 O O   . ALA B 436 ? 0.3078 0.3270 0.3480 0.0013  0.0023  0.0294  436 ALA B O   
7746 C CB  . ALA B 436 ? 0.2007 0.2189 0.2431 0.0007  0.0014  0.0285  436 ALA B CB  
7747 N N   . LYS B 437 ? 0.1918 0.2120 0.2344 0.0015  0.0024  0.0302  437 LYS B N   
7748 C CA  . LYS B 437 ? 0.2372 0.2574 0.2794 0.0017  0.0028  0.0304  437 LYS B CA  
7749 C C   . LYS B 437 ? 0.3133 0.3323 0.3561 0.0017  0.0029  0.0298  437 LYS B C   
7750 O O   . LYS B 437 ? 0.3217 0.3405 0.3641 0.0019  0.0032  0.0298  437 LYS B O   
7751 C CB  . LYS B 437 ? 0.2771 0.2993 0.3199 0.0021  0.0031  0.0317  437 LYS B CB  
7752 C CG  . LYS B 437 ? 0.3199 0.3431 0.3618 0.0022  0.0031  0.0322  437 LYS B CG  
7753 C CD  . LYS B 437 ? 0.4765 0.5018 0.5191 0.0023  0.0030  0.0333  437 LYS B CD  
7754 C CE  . LYS B 437 ? 0.4555 0.4817 0.4972 0.0023  0.0029  0.0336  437 LYS B CE  
7755 N NZ  . LYS B 437 ? 0.3636 0.3907 0.4058 0.0021  0.0026  0.0335  437 LYS B NZ  
7756 N N   . ASN B 438 ? 0.2255 0.2439 0.2693 0.0015  0.0026  0.0293  438 ASN B N   
7757 C CA  . ASN B 438 ? 0.2403 0.2577 0.2848 0.0015  0.0026  0.0287  438 ASN B CA  
7758 C C   . ASN B 438 ? 0.2784 0.2947 0.3234 0.0011  0.0022  0.0278  438 ASN B C   
7759 O O   . ASN B 438 ? 0.1976 0.2139 0.2425 0.0009  0.0018  0.0276  438 ASN B O   
7760 C CB  . ASN B 438 ? 0.2586 0.2772 0.3046 0.0018  0.0029  0.0297  438 ASN B CB  
7761 C CG  . ASN B 438 ? 0.2173 0.2376 0.2639 0.0021  0.0024  0.0289  438 ASN B CG  
7762 O OD1 . ASN B 438 ? 0.2002 0.2201 0.2470 0.0020  0.0018  0.0274  438 ASN B OD1 
7763 N ND2 . ASN B 438 ? 0.1811 0.2035 0.2275 0.0024  0.0024  0.0290  438 ASN B ND2 
7764 N N   . ASP B 439 ? 0.1794 0.1947 0.2249 0.0011  0.0022  0.0271  439 ASP B N   
7765 C CA  . ASP B 439 ? 0.2285 0.2425 0.2743 0.0007  0.0017  0.0260  439 ASP B CA  
7766 C C   . ASP B 439 ? 0.1817 0.1959 0.2292 0.0007  0.0012  0.0260  439 ASP B C   
7767 O O   . ASP B 439 ? 0.1439 0.1572 0.1918 0.0005  0.0007  0.0249  439 ASP B O   
7768 C CB  . ASP B 439 ? 0.2477 0.2606 0.2934 0.0007  0.0018  0.0252  439 ASP B CB  
7769 C CG  . ASP B 439 ? 0.3770 0.3891 0.4207 0.0005  0.0021  0.0246  439 ASP B CG  
7770 O OD1 . ASP B 439 ? 0.3398 0.3521 0.3823 0.0005  0.0021  0.0247  439 ASP B OD1 
7771 O OD2 . ASP B 439 ? 0.3747 0.3860 0.4181 0.0005  0.0022  0.0240  439 ASP B OD2 
7772 N N   . TYR B 440 ? 0.1694 0.1857 0.2168 0.0014  0.0010  0.0256  440 TYR B N   
7773 C CA  . TYR B 440 ? 0.1455 0.1629 0.1930 0.0019  0.0000  0.0238  440 TYR B CA  
7774 C C   . TYR B 440 ? 0.1304 0.1473 0.1774 0.0017  -0.0004 0.0235  440 TYR B C   
7775 O O   . TYR B 440 ? 0.1166 0.1336 0.1635 0.0020  -0.0013 0.0220  440 TYR B O   
7776 C CB  . TYR B 440 ? 0.1330 0.1529 0.1806 0.0026  -0.0001 0.0232  440 TYR B CB  
7777 C CG  . TYR B 440 ? 0.1865 0.2071 0.2349 0.0031  -0.0002 0.0223  440 TYR B CG  
7778 C CD1 . TYR B 440 ? 0.2056 0.2259 0.2542 0.0034  -0.0009 0.0205  440 TYR B CD1 
7779 C CD2 . TYR B 440 ? 0.2101 0.2313 0.2587 0.0031  0.0005  0.0231  440 TYR B CD2 
7780 C CE1 . TYR B 440 ? 0.2595 0.2805 0.3088 0.0038  -0.0010 0.0196  440 TYR B CE1 
7781 C CE2 . TYR B 440 ? 0.1544 0.1763 0.2037 0.0035  0.0005  0.0222  440 TYR B CE2 
7782 C CZ  . TYR B 440 ? 0.3328 0.3545 0.3825 0.0038  -0.0003 0.0205  440 TYR B CZ  
7783 O OH  . TYR B 440 ? 0.3765 0.3988 0.4268 0.0042  -0.0003 0.0196  440 TYR B OH  
7784 N N   . ILE B 441 ? 0.1294 0.1457 0.1758 0.0011  0.0001  0.0250  441 ILE B N   
7785 C CA  . ILE B 441 ? 0.0434 0.0591 0.0895 0.0007  -0.0003 0.0248  441 ILE B CA  
7786 C C   . ILE B 441 ? 0.0746 0.0884 0.1211 0.0003  -0.0007 0.0241  441 ILE B C   
7787 O O   . ILE B 441 ? 0.1449 0.1583 0.1911 0.0003  -0.0014 0.0230  441 ILE B O   
7788 C CB  . ILE B 441 ? 0.0718 0.0874 0.1173 0.0002  0.0004  0.0266  441 ILE B CB  
7789 C CG1 . ILE B 441 ? 0.0877 0.1032 0.1327 0.0000  -0.0001 0.0263  441 ILE B CG1 
7790 C CG2 . ILE B 441 ? 0.1688 0.1832 0.2127 0.0001  0.0007  0.0257  441 ILE B CG2 
7791 C CD1 . ILE B 441 ? 0.1947 0.2121 0.2393 0.0007  -0.0007 0.0254  441 ILE B CD1 
7792 N N   . LEU B 442 ? 0.0675 0.0802 0.1144 -0.0001 -0.0002 0.0244  442 LEU B N   
7793 C CA  . LEU B 442 ? 0.1015 0.1127 0.1484 -0.0004 -0.0007 0.0231  442 LEU B CA  
7794 C C   . LEU B 442 ? 0.1297 0.1409 0.1773 0.0001  -0.0015 0.0217  442 LEU B C   
7795 O O   . LEU B 442 ? 0.0923 0.1024 0.1398 -0.0001 -0.0022 0.0207  442 LEU B O   
7796 C CB  . LEU B 442 ? 0.0896 0.1003 0.1356 -0.0004 -0.0002 0.0226  442 LEU B CB  
7797 C CG  . LEU B 442 ? 0.1169 0.1278 0.1611 -0.0003 0.0004  0.0228  442 LEU B CG  
7798 C CD1 . LEU B 442 ? 0.1881 0.1984 0.2316 -0.0004 0.0008  0.0223  442 LEU B CD1 
7799 C CD2 . LEU B 442 ? 0.0321 0.0427 0.0751 -0.0006 0.0002  0.0224  442 LEU B CD2 
7800 N N   . VAL B 443 ? 0.0976 0.1100 0.1453 0.0009  -0.0016 0.0212  443 VAL B N   
7801 C CA  . VAL B 443 ? 0.0721 0.0849 0.1199 0.0016  -0.0025 0.0194  443 VAL B CA  
7802 C C   . VAL B 443 ? 0.0947 0.1079 0.1419 0.0019  -0.0034 0.0185  443 VAL B C   
7803 O O   . VAL B 443 ? 0.0660 0.0784 0.1131 0.0021  -0.0042 0.0172  443 VAL B O   
7804 C CB  . VAL B 443 ? 0.1009 0.1155 0.1490 0.0023  -0.0024 0.0191  443 VAL B CB  
7805 C CG1 . VAL B 443 ? 0.0498 0.0650 0.0980 0.0031  -0.0033 0.0172  443 VAL B CG1 
7806 C CG2 . VAL B 443 ? 0.0814 0.0956 0.1301 0.0020  -0.0015 0.0201  443 VAL B CG2 
7807 N N   . ALA B 444 ? 0.1196 0.1341 0.1663 0.0020  -0.0032 0.0192  444 ALA B N   
7808 C CA  . ALA B 444 ? 0.0887 0.1038 0.1348 0.0024  -0.0040 0.0184  444 ALA B CA  
7809 C C   . ALA B 444 ? 0.1443 0.1575 0.1900 0.0017  -0.0043 0.0184  444 ALA B C   
7810 O O   . ALA B 444 ? 0.1165 0.1298 0.1617 0.0020  -0.0051 0.0175  444 ALA B O   
7811 C CB  . ALA B 444 ? 0.0618 0.0788 0.1076 0.0025  -0.0036 0.0192  444 ALA B CB  
7812 N N   . GLU B 445 ? 0.1050 0.1168 0.1510 0.0009  -0.0037 0.0194  445 GLU B N   
7813 C CA  . GLU B 445 ? 0.0903 0.1005 0.1362 0.0002  -0.0041 0.0193  445 GLU B CA  
7814 C C   . GLU B 445 ? 0.0571 0.0660 0.1032 0.0002  -0.0048 0.0179  445 GLU B C   
7815 O O   . GLU B 445 ? 0.0792 0.0868 0.1252 -0.0004 -0.0053 0.0175  445 GLU B O   
7816 C CB  . GLU B 445 ? 0.1240 0.1337 0.1704 -0.0009 -0.0031 0.0208  445 GLU B CB  
7817 C CG  . GLU B 445 ? 0.1247 0.1355 0.1707 -0.0010 -0.0023 0.0223  445 GLU B CG  
7818 C CD  . GLU B 445 ? 0.1558 0.1667 0.2002 -0.0010 -0.0015 0.0224  445 GLU B CD  
7819 O OE1 . GLU B 445 ? 0.0823 0.0924 0.1263 -0.0011 -0.0014 0.0216  445 GLU B OE1 
7820 O OE2 . GLU B 445 ? 0.1596 0.1714 0.2032 -0.0009 -0.0010 0.0232  445 GLU B OE2 
7821 N N   . GLY B 446 ? 0.0814 0.0905 0.1278 0.0008  -0.0051 0.0170  446 GLY B N   
7822 C CA  . GLY B 446 ? 0.0787 0.0865 0.1252 0.0009  -0.0059 0.0156  446 GLY B CA  
7823 C C   . GLY B 446 ? 0.0841 0.0914 0.1299 0.0012  -0.0069 0.0145  446 GLY B C   
7824 O O   . GLY B 446 ? 0.0954 0.1039 0.1406 0.0018  -0.0072 0.0144  446 GLY B O   
7825 N N   . SER B 447 ? 0.0490 0.0546 0.0947 0.0007  -0.0075 0.0137  447 SER B N   
7826 C CA  . SER B 447 ? 0.0620 0.0669 0.1070 0.0009  -0.0086 0.0127  447 SER B CA  
7827 C C   . SER B 447 ? 0.1168 0.1224 0.1614 0.0020  -0.0093 0.0115  447 SER B C   
7828 O O   . SER B 447 ? 0.0591 0.0648 0.1029 0.0023  -0.0100 0.0109  447 SER B O   
7829 C CB  . SER B 447 ? 0.0803 0.0835 0.1255 0.0002  -0.0091 0.0121  447 SER B CB  
7830 O OG  . SER B 447 ? 0.1465 0.1490 0.1921 0.0004  -0.0094 0.0111  447 SER B OG  
7831 N N   . ASP B 448 ? 0.1070 0.1132 0.1521 0.0025  -0.0092 0.0110  448 ASP B N   
7832 C CA  . ASP B 448 ? 0.1023 0.1092 0.1471 0.0034  -0.0099 0.0097  448 ASP B CA  
7833 C C   . ASP B 448 ? 0.0918 0.1006 0.1361 0.0041  -0.0100 0.0097  448 ASP B C   
7834 O O   . ASP B 448 ? 0.0701 0.0791 0.1139 0.0046  -0.0109 0.0086  448 ASP B O   
7835 C CB  . ASP B 448 ? 0.1346 0.1419 0.1801 0.0037  -0.0096 0.0093  448 ASP B CB  
7836 C CG  . ASP B 448 ? 0.1133 0.1189 0.1593 0.0030  -0.0094 0.0094  448 ASP B CG  
7837 O OD1 . ASP B 448 ? 0.0658 0.0712 0.1123 0.0023  -0.0086 0.0106  448 ASP B OD1 
7838 O OD2 . ASP B 448 ? 0.1286 0.1330 0.1747 0.0030  -0.0101 0.0083  448 ASP B OD2 
7839 N N   . TRP B 449 ? 0.1160 0.1263 0.1604 0.0041  -0.0093 0.0108  449 TRP B N   
7840 C CA  . TRP B 449 ? 0.1225 0.1350 0.1666 0.0047  -0.0094 0.0107  449 TRP B CA  
7841 C C   . TRP B 449 ? 0.1468 0.1586 0.1900 0.0046  -0.0101 0.0104  449 TRP B C   
7842 O O   . TRP B 449 ? 0.1115 0.1246 0.1544 0.0053  -0.0107 0.0096  449 TRP B O   
7843 C CB  . TRP B 449 ? 0.0778 0.0919 0.1222 0.0045  -0.0084 0.0121  449 TRP B CB  
7844 C CG  . TRP B 449 ? 0.1259 0.1400 0.1711 0.0043  -0.0077 0.0126  449 TRP B CG  
7845 C CD1 . TRP B 449 ? 0.1079 0.1212 0.1535 0.0035  -0.0068 0.0140  449 TRP B CD1 
7846 C CD2 . TRP B 449 ? 0.0978 0.1128 0.1436 0.0049  -0.0077 0.0118  449 TRP B CD2 
7847 N NE1 . TRP B 449 ? 0.1182 0.1317 0.1644 0.0036  -0.0063 0.0141  449 TRP B NE1 
7848 C CE2 . TRP B 449 ? 0.0546 0.0691 0.1010 0.0044  -0.0068 0.0128  449 TRP B CE2 
7849 C CE3 . TRP B 449 ? 0.1165 0.1326 0.1623 0.0057  -0.0083 0.0104  449 TRP B CE3 
7850 C CZ2 . TRP B 449 ? 0.0766 0.0917 0.1236 0.0048  -0.0066 0.0123  449 TRP B CZ2 
7851 C CZ3 . TRP B 449 ? 0.0879 0.1046 0.1343 0.0060  -0.0081 0.0100  449 TRP B CZ3 
7852 C CH2 . TRP B 449 ? 0.1120 0.1283 0.1590 0.0056  -0.0073 0.0109  449 TRP B CH2 
7853 N N   . PHE B 450 ? 0.0812 0.0912 0.1241 0.0038  -0.0101 0.0110  450 PHE B N   
7854 C CA  . PHE B 450 ? 0.1017 0.1111 0.1439 0.0037  -0.0107 0.0109  450 PHE B CA  
7855 C C   . PHE B 450 ? 0.1120 0.1197 0.1537 0.0038  -0.0117 0.0095  450 PHE B C   
7856 O O   . PHE B 450 ? 0.1374 0.1450 0.1784 0.0040  -0.0124 0.0090  450 PHE B O   
7857 C CB  . PHE B 450 ? 0.0972 0.1053 0.1393 0.0027  -0.0102 0.0121  450 PHE B CB  
7858 C CG  . PHE B 450 ? 0.0920 0.1014 0.1346 0.0024  -0.0091 0.0135  450 PHE B CG  
7859 C CD1 . PHE B 450 ? 0.1121 0.1230 0.1543 0.0025  -0.0088 0.0142  450 PHE B CD1 
7860 C CD2 . PHE B 450 ? 0.1407 0.1500 0.1841 0.0021  -0.0083 0.0142  450 PHE B CD2 
7861 C CE1 . PHE B 450 ? 0.1079 0.1199 0.1505 0.0022  -0.0078 0.0156  450 PHE B CE1 
7862 C CE2 . PHE B 450 ? 0.0938 0.1043 0.1376 0.0018  -0.0073 0.0156  450 PHE B CE2 
7863 C CZ  . PHE B 450 ? 0.1075 0.1193 0.1509 0.0019  -0.0070 0.0163  450 PHE B CZ  
7864 N N   . TRP B 451 ? 0.1193 0.1259 0.1615 0.0037  -0.0118 0.0089  451 TRP B N   
7865 C CA  . TRP B 451 ? 0.1502 0.1552 0.1920 0.0038  -0.0129 0.0075  451 TRP B CA  
7866 C C   . TRP B 451 ? 0.1508 0.1572 0.1924 0.0048  -0.0134 0.0065  451 TRP B C   
7867 O O   . TRP B 451 ? 0.1644 0.1701 0.2053 0.0049  -0.0143 0.0056  451 TRP B O   
7868 C CB  . TRP B 451 ? 0.1230 0.1267 0.1655 0.0035  -0.0128 0.0071  451 TRP B CB  
7869 C CG  . TRP B 451 ? 0.2335 0.2358 0.2758 0.0036  -0.0138 0.0056  451 TRP B CG  
7870 C CD1 . TRP B 451 ? 0.2047 0.2076 0.2471 0.0043  -0.0142 0.0045  451 TRP B CD1 
7871 C CD2 . TRP B 451 ? 0.1696 0.1696 0.2115 0.0029  -0.0146 0.0050  451 TRP B CD2 
7872 N NE1 . TRP B 451 ? 0.2898 0.2908 0.3319 0.0041  -0.0151 0.0033  451 TRP B NE1 
7873 C CE2 . TRP B 451 ? 0.2743 0.2736 0.3161 0.0033  -0.0154 0.0035  451 TRP B CE2 
7874 C CE3 . TRP B 451 ? 0.0890 0.0878 0.1308 0.0020  -0.0146 0.0054  451 TRP B CE3 
7875 C CZ2 . TRP B 451 ? 0.2952 0.2925 0.3367 0.0027  -0.0164 0.0025  451 TRP B CZ2 
7876 C CZ3 . TRP B 451 ? 0.2369 0.2340 0.2785 0.0014  -0.0156 0.0044  451 TRP B CZ3 
7877 C CH2 . TRP B 451 ? 0.3360 0.3323 0.3775 0.0018  -0.0164 0.0030  451 TRP B CH2 
7878 N N   . TRP B 452 ? 0.1177 0.1262 0.1598 0.0054  -0.0129 0.0065  452 TRP B N   
7879 C CA  . TRP B 452 ? 0.2166 0.2267 0.2586 0.0062  -0.0134 0.0055  452 TRP B CA  
7880 C C   . TRP B 452 ? 0.2872 0.2994 0.3288 0.0066  -0.0135 0.0058  452 TRP B C   
7881 O O   . TRP B 452 ? 0.2353 0.2485 0.2766 0.0071  -0.0140 0.0049  452 TRP B O   
7882 C CB  . TRP B 452 ? 0.1671 0.1788 0.2099 0.0067  -0.0129 0.0054  452 TRP B CB  
7883 C CG  . TRP B 452 ? 0.2216 0.2315 0.2649 0.0064  -0.0129 0.0049  452 TRP B CG  
7884 C CD1 . TRP B 452 ? 0.2870 0.2966 0.3310 0.0060  -0.0122 0.0057  452 TRP B CD1 
7885 C CD2 . TRP B 452 ? 0.2841 0.2922 0.3273 0.0064  -0.0138 0.0036  452 TRP B CD2 
7886 N NE1 . TRP B 452 ? 0.2536 0.2615 0.2979 0.0058  -0.0125 0.0049  452 TRP B NE1 
7887 C CE2 . TRP B 452 ? 0.2641 0.2710 0.3079 0.0060  -0.0135 0.0036  452 TRP B CE2 
7888 C CE3 . TRP B 452 ? 0.2831 0.2904 0.3257 0.0066  -0.0148 0.0024  452 TRP B CE3 
7889 C CZ2 . TRP B 452 ? 0.3752 0.3803 0.4190 0.0059  -0.0142 0.0025  452 TRP B CZ2 
7890 C CZ3 . TRP B 452 ? 0.3481 0.3535 0.3908 0.0065  -0.0155 0.0013  452 TRP B CZ3 
7891 C CH2 . TRP B 452 ? 0.4466 0.4509 0.4899 0.0061  -0.0152 0.0013  452 TRP B CH2 
7892 N N   . GLN B 453 ? 0.2564 0.2691 0.2979 0.0062  -0.0129 0.0070  453 GLN B N   
7893 C CA  . GLN B 453 ? 0.2528 0.2677 0.2940 0.0065  -0.0129 0.0072  453 GLN B CA  
7894 C C   . GLN B 453 ? 0.2846 0.2985 0.3248 0.0066  -0.0138 0.0066  453 GLN B C   
7895 O O   . GLN B 453 ? 0.2398 0.2512 0.2796 0.0061  -0.0142 0.0065  453 GLN B O   
7896 C CB  . GLN B 453 ? 0.1130 0.1282 0.1541 0.0060  -0.0121 0.0087  453 GLN B CB  
7897 C CG  . GLN B 453 ? 0.2298 0.2467 0.2704 0.0061  -0.0121 0.0090  453 GLN B CG  
7898 C CD  . GLN B 453 ? 0.2775 0.2975 0.3184 0.0069  -0.0121 0.0085  453 GLN B CD  
7899 O OE1 . GLN B 453 ? 0.2960 0.3170 0.3374 0.0074  -0.0122 0.0077  453 GLN B OE1 
7900 N NE2 . GLN B 453 ? 0.2168 0.2384 0.2575 0.0068  -0.0119 0.0090  453 GLN B NE2 
7901 N N   . GLY B 454 ? 0.4773 0.4934 0.5174 0.0072  -0.0141 0.0060  454 GLY B N   
7902 C CA  . GLY B 454 ? 0.6209 0.6364 0.6602 0.0072  -0.0150 0.0054  454 GLY B CA  
7903 C C   . GLY B 454 ? 0.7611 0.7750 0.8003 0.0074  -0.0158 0.0040  454 GLY B C   
7904 O O   . GLY B 454 ? 0.8614 0.8745 0.8999 0.0074  -0.0166 0.0034  454 GLY B O   
7905 N N   . GLU B 455 ? 0.7329 0.7461 0.7727 0.0075  -0.0157 0.0036  455 GLU B N   
7906 C CA  . GLU B 455 ? 0.7566 0.7677 0.7963 0.0075  -0.0166 0.0023  455 GLU B CA  
7907 C C   . GLU B 455 ? 0.7356 0.7484 0.7753 0.0082  -0.0170 0.0013  455 GLU B C   
7908 O O   . GLU B 455 ? 0.6846 0.7000 0.7250 0.0086  -0.0165 0.0014  455 GLU B O   
7909 C CB  . GLU B 455 ? 0.7972 0.8067 0.8374 0.0073  -0.0164 0.0021  455 GLU B CB  
7910 C CG  . GLU B 455 ? 0.8138 0.8215 0.8540 0.0065  -0.0159 0.0031  455 GLU B CG  
7911 C CD  . GLU B 455 ? 0.8044 0.8099 0.8437 0.0059  -0.0166 0.0030  455 GLU B CD  
7912 O OE1 . GLU B 455 ? 0.8067 0.8116 0.8454 0.0061  -0.0174 0.0021  455 GLU B OE1 
7913 O OE2 . GLU B 455 ? 0.8016 0.8062 0.8408 0.0053  -0.0162 0.0040  455 GLU B OE2 
7914 N N   . GLU B 456 ? 0.8582 0.8695 0.8974 0.0082  -0.0180 0.0002  456 GLU B N   
7915 C CA  . GLU B 456 ? 0.9056 0.9182 0.9448 0.0087  -0.0186 -0.0008 456 GLU B CA  
7916 C C   . GLU B 456 ? 0.8303 0.8439 0.8703 0.0091  -0.0184 -0.0015 456 GLU B C   
7917 O O   . GLU B 456 ? 0.7956 0.8071 0.8356 0.0091  -0.0189 -0.0026 456 GLU B O   
7918 C CB  . GLU B 456 ? 0.9504 0.9604 0.9888 0.0085  -0.0197 -0.0020 456 GLU B CB  
7919 C CG  . GLU B 456 ? 0.9692 0.9783 1.0067 0.0081  -0.0198 -0.0013 456 GLU B CG  
7920 C CD  . GLU B 456 ? 0.9818 0.9897 1.0184 0.0081  -0.0208 -0.0023 456 GLU B CD  
7921 O OE1 . GLU B 456 ? 0.9716 0.9814 1.0079 0.0083  -0.0208 -0.0020 456 GLU B OE1 
7922 O OE2 . GLU B 456 ? 0.9873 0.9923 1.0235 0.0079  -0.0216 -0.0033 456 GLU B OE2 
7923 N N   . LYS B 457 ? 0.8016 0.8184 0.8423 0.0094  -0.0176 -0.0008 457 LYS B N   
7924 C CA  . LYS B 457 ? 0.7864 0.8048 0.8280 0.0097  -0.0170 -0.0008 457 LYS B CA  
7925 C C   . LYS B 457 ? 0.7767 0.7927 0.8186 0.0096  -0.0172 -0.0015 457 LYS B C   
7926 O O   . LYS B 457 ? 0.7550 0.7714 0.7974 0.0099  -0.0174 -0.0025 457 LYS B O   
7927 C CB  . LYS B 457 ? 0.7510 0.7720 0.7929 0.0102  -0.0171 -0.0013 457 LYS B CB  
7928 C CG  . LYS B 457 ? 0.7725 0.7965 0.8144 0.0103  -0.0167 -0.0004 457 LYS B CG  
7929 C CD  . LYS B 457 ? 0.7840 0.8110 0.8264 0.0107  -0.0166 -0.0007 457 LYS B CD  
7930 C CE  . LYS B 457 ? 0.7889 0.8173 0.8323 0.0109  -0.0160 -0.0006 457 LYS B CE  
7931 N NZ  . LYS B 457 ? 0.8057 0.8341 0.8495 0.0112  -0.0165 -0.0019 457 LYS B NZ  
7932 N N   . ALA B 458 ? 0.7466 0.7603 0.7883 0.0091  -0.0171 -0.0010 458 ALA B N   
7933 C CA  . ALA B 458 ? 0.6710 0.6824 0.7129 0.0088  -0.0171 -0.0014 458 ALA B CA  
7934 C C   . ALA B 458 ? 0.6374 0.6507 0.6803 0.0092  -0.0164 -0.0012 458 ALA B C   
7935 O O   . ALA B 458 ? 0.6441 0.6603 0.6874 0.0094  -0.0157 -0.0004 458 ALA B O   
7936 C CB  . ALA B 458 ? 0.5892 0.5988 0.6309 0.0081  -0.0168 -0.0004 458 ALA B CB  
7937 N N   . PRO B 459 ? 0.6028 0.6146 0.6461 0.0091  -0.0165 -0.0019 459 PRO B N   
7938 C CA  . PRO B 459 ? 0.5172 0.5308 0.5613 0.0095  -0.0160 -0.0021 459 PRO B CA  
7939 C C   . PRO B 459 ? 0.3431 0.3591 0.3877 0.0096  -0.0149 -0.0007 459 PRO B C   
7940 O O   . PRO B 459 ? 0.3244 0.3395 0.3691 0.0091  -0.0144 0.0003  459 PRO B O   
7941 C CB  . PRO B 459 ? 0.5467 0.5578 0.5911 0.0092  -0.0163 -0.0028 459 PRO B CB  
7942 C CG  . PRO B 459 ? 0.6118 0.6201 0.6555 0.0085  -0.0167 -0.0026 459 PRO B CG  
7943 C CD  . PRO B 459 ? 0.5948 0.6032 0.6377 0.0085  -0.0171 -0.0025 459 PRO B CD  
7944 N N   . PHE B 460 ? 0.2945 0.3136 0.3396 0.0101  -0.0146 -0.0006 460 PHE B N   
7945 C CA  . PHE B 460 ? 0.2845 0.3061 0.3300 0.0102  -0.0136 0.0006  460 PHE B CA  
7946 C C   . PHE B 460 ? 0.3016 0.3234 0.3467 0.0099  -0.0131 0.0018  460 PHE B C   
7947 O O   . PHE B 460 ? 0.1973 0.2200 0.2428 0.0097  -0.0123 0.0027  460 PHE B O   
7948 C CB  . PHE B 460 ? 0.2834 0.3046 0.3297 0.0101  -0.0130 0.0007  460 PHE B CB  
7949 C CG  . PHE B 460 ? 0.2601 0.2813 0.3069 0.0105  -0.0134 -0.0005 460 PHE B CG  
7950 C CD1 . PHE B 460 ? 0.3089 0.3330 0.3561 0.0110  -0.0133 -0.0008 460 PHE B CD1 
7951 C CD2 . PHE B 460 ? 0.3171 0.3355 0.3638 0.0102  -0.0139 -0.0014 460 PHE B CD2 
7952 C CE1 . PHE B 460 ? 0.3641 0.3881 0.4117 0.0113  -0.0136 -0.0019 460 PHE B CE1 
7953 C CE2 . PHE B 460 ? 0.3323 0.3507 0.3795 0.0106  -0.0143 -0.0026 460 PHE B CE2 
7954 C CZ  . PHE B 460 ? 0.3581 0.3792 0.4057 0.0111  -0.0141 -0.0028 460 PHE B CZ  
7955 N N   . VAL B 461 ? 0.2155 0.2365 0.2599 0.0097  -0.0137 0.0017  461 VAL B N   
7956 C CA  . VAL B 461 ? 0.2651 0.2861 0.3091 0.0093  -0.0133 0.0028  461 VAL B CA  
7957 C C   . VAL B 461 ? 0.2565 0.2808 0.3008 0.0096  -0.0125 0.0036  461 VAL B C   
7958 O O   . VAL B 461 ? 0.1663 0.1906 0.2105 0.0092  -0.0120 0.0046  461 VAL B O   
7959 C CB  . VAL B 461 ? 0.3658 0.3855 0.4088 0.0092  -0.0141 0.0025  461 VAL B CB  
7960 C CG1 . VAL B 461 ? 0.3566 0.3783 0.3996 0.0096  -0.0145 0.0018  461 VAL B CG1 
7961 C CG2 . VAL B 461 ? 0.2929 0.3123 0.3355 0.0087  -0.0137 0.0037  461 VAL B CG2 
7962 N N   . GLU B 462 ? 0.1253 0.1522 0.1699 0.0101  -0.0125 0.0031  462 GLU B N   
7963 C CA  . GLU B 462 ? 0.1841 0.2141 0.2290 0.0103  -0.0118 0.0037  462 GLU B CA  
7964 C C   . GLU B 462 ? 0.1879 0.2182 0.2335 0.0102  -0.0110 0.0042  462 GLU B C   
7965 O O   . GLU B 462 ? 0.1586 0.1903 0.2044 0.0100  -0.0104 0.0048  462 GLU B O   
7966 C CB  . GLU B 462 ? 0.3049 0.3379 0.3500 0.0108  -0.0120 0.0031  462 GLU B CB  
7967 C CG  . GLU B 462 ? 0.4829 0.5151 0.5275 0.0108  -0.0129 0.0025  462 GLU B CG  
7968 C CD  . GLU B 462 ? 0.6045 0.6397 0.6492 0.0112  -0.0130 0.0022  462 GLU B CD  
7969 O OE1 . GLU B 462 ? 0.6333 0.6715 0.6785 0.0114  -0.0124 0.0025  462 GLU B OE1 
7970 O OE2 . GLU B 462 ? 0.6879 0.7223 0.7323 0.0112  -0.0138 0.0016  462 GLU B OE2 
7971 N N   . VAL B 463 ? 0.1459 0.1745 0.1918 0.0101  -0.0110 0.0039  463 VAL B N   
7972 C CA  . VAL B 463 ? 0.0685 0.0971 0.1151 0.0099  -0.0103 0.0044  463 VAL B CA  
7973 C C   . VAL B 463 ? 0.1026 0.1291 0.1491 0.0092  -0.0099 0.0055  463 VAL B C   
7974 O O   . VAL B 463 ? 0.1481 0.1752 0.1949 0.0089  -0.0091 0.0064  463 VAL B O   
7975 C CB  . VAL B 463 ? 0.1778 0.2054 0.2249 0.0101  -0.0104 0.0037  463 VAL B CB  
7976 C CG1 . VAL B 463 ? 0.1290 0.1565 0.1768 0.0098  -0.0096 0.0044  463 VAL B CG1 
7977 C CG2 . VAL B 463 ? 0.1221 0.1520 0.1695 0.0107  -0.0107 0.0028  463 VAL B CG2 
7978 N N   . PHE B 464 ? 0.0900 0.1137 0.1358 0.0089  -0.0104 0.0055  464 PHE B N   
7979 C CA  . PHE B 464 ? 0.0981 0.1199 0.1437 0.0082  -0.0100 0.0066  464 PHE B CA  
7980 C C   . PHE B 464 ? 0.1074 0.1307 0.1528 0.0080  -0.0097 0.0075  464 PHE B C   
7981 O O   . PHE B 464 ? 0.1247 0.1475 0.1703 0.0075  -0.0090 0.0087  464 PHE B O   
7982 C CB  . PHE B 464 ? 0.1173 0.1363 0.1624 0.0078  -0.0108 0.0063  464 PHE B CB  
7983 C CG  . PHE B 464 ? 0.1178 0.1347 0.1631 0.0077  -0.0110 0.0057  464 PHE B CG  
7984 C CD1 . PHE B 464 ? 0.1431 0.1599 0.1885 0.0081  -0.0117 0.0044  464 PHE B CD1 
7985 C CD2 . PHE B 464 ? 0.1959 0.2107 0.2414 0.0070  -0.0106 0.0064  464 PHE B CD2 
7986 C CE1 . PHE B 464 ? 0.1639 0.1787 0.2095 0.0080  -0.0119 0.0037  464 PHE B CE1 
7987 C CE2 . PHE B 464 ? 0.2371 0.2502 0.2830 0.0069  -0.0108 0.0058  464 PHE B CE2 
7988 C CZ  . PHE B 464 ? 0.1612 0.1742 0.2071 0.0073  -0.0115 0.0044  464 PHE B CZ  
7989 N N   . ASP B 465 ? 0.1376 0.1627 0.1827 0.0084  -0.0101 0.0069  465 ASP B N   
7990 C CA  . ASP B 465 ? 0.1405 0.1671 0.1854 0.0083  -0.0099 0.0076  465 ASP B CA  
7991 C C   . ASP B 465 ? 0.0925 0.1211 0.1381 0.0083  -0.0090 0.0081  465 ASP B C   
7992 O O   . ASP B 465 ? 0.1256 0.1543 0.1713 0.0078  -0.0084 0.0093  465 ASP B O   
7993 C CB  . ASP B 465 ? 0.0993 0.1273 0.1436 0.0088  -0.0106 0.0067  465 ASP B CB  
7994 C CG  . ASP B 465 ? 0.1946 0.2244 0.2388 0.0087  -0.0103 0.0073  465 ASP B CG  
7995 O OD1 . ASP B 465 ? 0.1575 0.1859 0.2012 0.0081  -0.0102 0.0082  465 ASP B OD1 
7996 O OD2 . ASP B 465 ? 0.2041 0.2366 0.2487 0.0090  -0.0102 0.0068  465 ASP B OD2 
7997 N N   . LYS B 466 ? 0.0673 0.0977 0.1135 0.0088  -0.0090 0.0073  466 LYS B N   
7998 C CA  . LYS B 466 ? 0.0781 0.1103 0.1250 0.0087  -0.0082 0.0077  466 LYS B CA  
7999 C C   . LYS B 466 ? 0.0796 0.1100 0.1269 0.0081  -0.0075 0.0090  466 LYS B C   
8000 O O   . LYS B 466 ? 0.1484 0.1794 0.1960 0.0077  -0.0067 0.0102  466 LYS B O   
8001 C CB  . LYS B 466 ? 0.1373 0.1716 0.1847 0.0094  -0.0084 0.0066  466 LYS B CB  
8002 C CG  . LYS B 466 ? 0.1263 0.1621 0.1747 0.0093  -0.0076 0.0070  466 LYS B CG  
8003 C CD  . LYS B 466 ? 0.2537 0.2916 0.3025 0.0099  -0.0078 0.0057  466 LYS B CD  
8004 C CE  . LYS B 466 ? 0.3294 0.3698 0.3791 0.0099  -0.0072 0.0057  466 LYS B CE  
8005 N NZ  . LYS B 466 ? 0.5012 0.5411 0.5516 0.0096  -0.0064 0.0065  466 LYS B NZ  
8006 N N   . LEU B 467 ? 0.1131 0.1412 0.1603 0.0080  -0.0076 0.0089  467 LEU B N   
8007 C CA  . LEU B 467 ? 0.0428 0.0691 0.0903 0.0074  -0.0069 0.0101  467 LEU B CA  
8008 C C   . LEU B 467 ? 0.0786 0.1037 0.1257 0.0066  -0.0065 0.0116  467 LEU B C   
8009 O O   . LEU B 467 ? 0.0547 0.0800 0.1021 0.0062  -0.0056 0.0129  467 LEU B O   
8010 C CB  . LEU B 467 ? 0.0223 0.0463 0.0699 0.0073  -0.0072 0.0096  467 LEU B CB  
8011 C CG  . LEU B 467 ? 0.0846 0.1094 0.1327 0.0078  -0.0074 0.0086  467 LEU B CG  
8012 C CD1 . LEU B 467 ? 0.0480 0.0704 0.0960 0.0078  -0.0079 0.0079  467 LEU B CD1 
8013 C CD2 . LEU B 467 ? 0.0327 0.0582 0.0815 0.0076  -0.0065 0.0094  467 LEU B CD2 
8014 N N   . PHE B 468 ? 0.1115 0.1353 0.1579 0.0065  -0.0070 0.0114  468 PHE B N   
8015 C CA  . PHE B 468 ? 0.0776 0.1002 0.1236 0.0058  -0.0066 0.0128  468 PHE B CA  
8016 C C   . PHE B 468 ? 0.0849 0.1095 0.1309 0.0057  -0.0061 0.0137  468 PHE B C   
8017 O O   . PHE B 468 ? 0.1098 0.1340 0.1559 0.0051  -0.0053 0.0152  468 PHE B O   
8018 C CB  . PHE B 468 ? 0.0220 0.0434 0.0673 0.0058  -0.0074 0.0123  468 PHE B CB  
8019 C CG  . PHE B 468 ? 0.0902 0.1108 0.1349 0.0051  -0.0071 0.0136  468 PHE B CG  
8020 C CD1 . PHE B 468 ? 0.0693 0.0878 0.1141 0.0044  -0.0066 0.0147  468 PHE B CD1 
8021 C CD2 . PHE B 468 ? 0.0959 0.1180 0.1402 0.0053  -0.0073 0.0137  468 PHE B CD2 
8022 C CE1 . PHE B 468 ? 0.0722 0.0901 0.1165 0.0037  -0.0063 0.0159  468 PHE B CE1 
8023 C CE2 . PHE B 468 ? 0.0885 0.1099 0.1324 0.0047  -0.0070 0.0149  468 PHE B CE2 
8024 C CZ  . PHE B 468 ? 0.1347 0.1541 0.1786 0.0039  -0.0065 0.0160  468 PHE B CZ  
8025 N N   . ARG B 469 ? 0.0564 0.0834 0.1025 0.0063  -0.0065 0.0128  469 ARG B N   
8026 C CA  . ARG B 469 ? 0.1436 0.1725 0.1897 0.0061  -0.0059 0.0136  469 ARG B CA  
8027 C C   . ARG B 469 ? 0.1148 0.1447 0.1616 0.0060  -0.0050 0.0144  469 ARG B C   
8028 O O   . ARG B 469 ? 0.1373 0.1677 0.1840 0.0056  -0.0043 0.0158  469 ARG B O   
8029 C CB  . ARG B 469 ? 0.1168 0.1478 0.1629 0.0067  -0.0066 0.0124  469 ARG B CB  
8030 C CG  . ARG B 469 ? 0.0565 0.0866 0.1017 0.0067  -0.0074 0.0120  469 ARG B CG  
8031 C CD  . ARG B 469 ? 0.1186 0.1507 0.1636 0.0073  -0.0081 0.0107  469 ARG B CD  
8032 N NE  . ARG B 469 ? 0.1509 0.1821 0.1951 0.0074  -0.0089 0.0102  469 ARG B NE  
8033 C CZ  . ARG B 469 ? 0.1399 0.1712 0.1836 0.0071  -0.0089 0.0108  469 ARG B CZ  
8034 N NH1 . ARG B 469 ? 0.1153 0.1475 0.1592 0.0067  -0.0082 0.0120  469 ARG B NH1 
8035 N NH2 . ARG B 469 ? 0.1957 0.2260 0.2386 0.0072  -0.0097 0.0103  469 ARG B NH2 
8036 N N   . SER B 470 ? 0.0739 0.1041 0.1213 0.0063  -0.0051 0.0136  470 SER B N   
8037 C CA  . SER B 470 ? 0.1008 0.1317 0.1488 0.0062  -0.0042 0.0144  470 SER B CA  
8038 C C   . SER B 470 ? 0.0985 0.1273 0.1463 0.0055  -0.0035 0.0162  470 SER B C   
8039 O O   . SER B 470 ? 0.0897 0.1190 0.1376 0.0052  -0.0026 0.0175  470 SER B O   
8040 C CB  . SER B 470 ? 0.1811 0.2126 0.2297 0.0067  -0.0045 0.0131  470 SER B CB  
8041 O OG  . SER B 470 ? 0.2780 0.3117 0.3268 0.0073  -0.0051 0.0116  470 SER B OG  
8042 N N   . PHE B 471 ? 0.1025 0.1289 0.1501 0.0052  -0.0037 0.0162  471 PHE B N   
8043 C CA  . PHE B 471 ? 0.1029 0.1273 0.1504 0.0045  -0.0030 0.0178  471 PHE B CA  
8044 C C   . PHE B 471 ? 0.1046 0.1289 0.1514 0.0041  -0.0026 0.0192  471 PHE B C   
8045 O O   . PHE B 471 ? 0.1400 0.1639 0.1868 0.0036  -0.0017 0.0208  471 PHE B O   
8046 C CB  . PHE B 471 ? 0.0356 0.0575 0.0830 0.0043  -0.0034 0.0174  471 PHE B CB  
8047 C CG  . PHE B 471 ? 0.1624 0.1840 0.2103 0.0047  -0.0038 0.0161  471 PHE B CG  
8048 C CD1 . PHE B 471 ? 0.1266 0.1489 0.1752 0.0048  -0.0032 0.0163  471 PHE B CD1 
8049 C CD2 . PHE B 471 ? 0.1104 0.1309 0.1581 0.0049  -0.0046 0.0148  471 PHE B CD2 
8050 C CE1 . PHE B 471 ? 0.1284 0.1504 0.1774 0.0052  -0.0036 0.0151  471 PHE B CE1 
8051 C CE2 . PHE B 471 ? 0.1081 0.1283 0.1563 0.0053  -0.0050 0.0137  471 PHE B CE2 
8052 C CZ  . PHE B 471 ? 0.1663 0.1873 0.2151 0.0054  -0.0044 0.0138  471 PHE B CZ  
8053 N N   . VAL B 472 ? 0.0888 0.1137 0.1352 0.0042  -0.0031 0.0187  472 VAL B N   
8054 C CA  . VAL B 472 ? 0.1240 0.1490 0.1698 0.0037  -0.0028 0.0200  472 VAL B CA  
8055 C C   . VAL B 472 ? 0.1044 0.1314 0.1502 0.0038  -0.0021 0.0209  472 VAL B C   
8056 O O   . VAL B 472 ? 0.1439 0.1705 0.1894 0.0033  -0.0014 0.0226  472 VAL B O   
8057 C CB  . VAL B 472 ? 0.1185 0.1437 0.1638 0.0039  -0.0036 0.0191  472 VAL B CB  
8058 C CG1 . VAL B 472 ? 0.2014 0.2274 0.2461 0.0036  -0.0033 0.0202  472 VAL B CG1 
8059 C CG2 . VAL B 472 ? 0.1657 0.1884 0.2107 0.0036  -0.0041 0.0187  472 VAL B CG2 
8060 N N   . ARG B 473 ? 0.1143 0.1434 0.1606 0.0043  -0.0023 0.0198  473 ARG B N   
8061 C CA  . ARG B 473 ? 0.1587 0.1898 0.2051 0.0044  -0.0017 0.0206  473 ARG B CA  
8062 C C   . ARG B 473 ? 0.1904 0.2208 0.2370 0.0041  -0.0009 0.0219  473 ARG B C   
8063 O O   . ARG B 473 ? 0.1599 0.1905 0.2061 0.0038  -0.0002 0.0235  473 ARG B O   
8064 C CB  . ARG B 473 ? 0.1900 0.2234 0.2369 0.0050  -0.0022 0.0190  473 ARG B CB  
8065 C CG  . ARG B 473 ? 0.2429 0.2787 0.2901 0.0050  -0.0016 0.0195  473 ARG B CG  
8066 C CD  . ARG B 473 ? 0.4260 0.4637 0.4740 0.0056  -0.0019 0.0179  473 ARG B CD  
8067 N NE  . ARG B 473 ? 0.6025 0.6404 0.6507 0.0061  -0.0029 0.0159  473 ARG B NE  
8068 C CZ  . ARG B 473 ? 0.6982 0.7368 0.7472 0.0066  -0.0034 0.0144  473 ARG B CZ  
8069 N NH1 . ARG B 473 ? 0.7877 0.8266 0.8372 0.0066  -0.0029 0.0145  473 ARG B NH1 
8070 N NH2 . ARG B 473 ? 0.6908 0.7295 0.7397 0.0071  -0.0043 0.0127  473 ARG B NH2 
8071 N N   . ARG B 474 ? 0.1525 0.1819 0.1997 0.0042  -0.0010 0.0213  474 ARG B N   
8072 C CA  . ARG B 474 ? 0.1966 0.2254 0.2440 0.0040  -0.0002 0.0223  474 ARG B CA  
8073 C C   . ARG B 474 ? 0.1838 0.2105 0.2306 0.0034  0.0004  0.0242  474 ARG B C   
8074 O O   . ARG B 474 ? 0.1424 0.1690 0.1892 0.0033  0.0011  0.0256  474 ARG B O   
8075 C CB  . ARG B 474 ? 0.1907 0.2189 0.2389 0.0043  -0.0005 0.0211  474 ARG B CB  
8076 C CG  . ARG B 474 ? 0.2249 0.2524 0.2734 0.0042  0.0002  0.0220  474 ARG B CG  
8077 C CD  . ARG B 474 ? 0.3170 0.3466 0.3658 0.0044  0.0006  0.0224  474 ARG B CD  
8078 N NE  . ARG B 474 ? 0.4312 0.4600 0.4803 0.0042  0.0013  0.0233  474 ARG B NE  
8079 C CZ  . ARG B 474 ? 0.5507 0.5786 0.5994 0.0039  0.0020  0.0251  474 ARG B CZ  
8080 N NH1 . ARG B 474 ? 0.5428 0.5706 0.5907 0.0036  0.0021  0.0263  474 ARG B NH1 
8081 N NH2 . ARG B 474 ? 0.5865 0.6136 0.6355 0.0038  0.0024  0.0258  474 ARG B NH2 
8082 N N   . ALA B 475 ? 0.1448 0.1698 0.1913 0.0031  0.0001  0.0242  475 ALA B N   
8083 C CA  . ALA B 475 ? 0.1509 0.1740 0.1970 0.0025  0.0006  0.0258  475 ALA B CA  
8084 C C   . ALA B 475 ? 0.1889 0.2127 0.2342 0.0023  0.0011  0.0275  475 ALA B C   
8085 O O   . ALA B 475 ? 0.1893 0.2116 0.2342 0.0019  0.0017  0.0291  475 ALA B O   
8086 C CB  . ALA B 475 ? 0.1583 0.1796 0.2041 0.0021  0.0001  0.0253  475 ALA B CB  
8087 N N   . GLN B 476 ? 0.1407 0.1667 0.1859 0.0026  0.0009  0.0271  476 GLN B N   
8088 C CA  . GLN B 476 ? 0.1455 0.1723 0.1900 0.0025  0.0014  0.0286  476 GLN B CA  
8089 C C   . GLN B 476 ? 0.3185 0.3467 0.3631 0.0028  0.0019  0.0293  476 GLN B C   
8090 O O   . GLN B 476 ? 0.3355 0.3649 0.3795 0.0028  0.0021  0.0303  476 GLN B O   
8091 C CB  . GLN B 476 ? 0.1720 0.2002 0.2161 0.0026  0.0009  0.0278  476 GLN B CB  
8092 C CG  . GLN B 476 ? 0.1654 0.1919 0.2093 0.0023  0.0003  0.0273  476 GLN B CG  
8093 C CD  . GLN B 476 ? 0.2905 0.3184 0.3342 0.0025  -0.0003 0.0262  476 GLN B CD  
8094 O OE1 . GLN B 476 ? 0.3307 0.3590 0.3737 0.0023  -0.0002 0.0271  476 GLN B OE1 
8095 N NE2 . GLN B 476 ? 0.1812 0.2096 0.2253 0.0030  -0.0011 0.0243  476 GLN B NE2 
8096 N N   . GLU B 477 ? 0.2873 0.3156 0.3326 0.0030  0.0020  0.0288  477 GLU B N   
8097 C CA  . GLU B 477 ? 0.2596 0.2891 0.3051 0.0032  0.0025  0.0295  477 GLU B CA  
8098 C C   . GLU B 477 ? 0.4339 0.4615 0.4794 0.0031  0.0030  0.0306  477 GLU B C   
8099 O O   . GLU B 477 ? 0.4795 0.5075 0.5250 0.0032  0.0034  0.0319  477 GLU B O   
8100 C CB  . GLU B 477 ? 0.3743 0.4059 0.4206 0.0036  0.0022  0.0278  477 GLU B CB  
8101 C CG  . GLU B 477 ? 0.4745 0.5080 0.5208 0.0038  0.0017  0.0266  477 GLU B CG  
8102 C CD  . GLU B 477 ? 0.5802 0.6153 0.6274 0.0042  0.0012  0.0246  477 GLU B CD  
8103 O OE1 . GLU B 477 ? 0.5765 0.6112 0.6243 0.0044  0.0013  0.0242  477 GLU B OE1 
8104 O OE2 . GLU B 477 ? 0.5451 0.5819 0.5924 0.0045  0.0007  0.0235  477 GLU B OE2 
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